File: 1sui.cif

package info (click to toggle)
freesasa 2.1.2-6
links: PTS, VCS
area: main
in suites: forky, sid
size: 13,740 kB
sloc: ansic: 11,281; cpp: 1,342; sh: 397; perl: 169; makefile: 119; yacc: 87; lex: 54
file content (10211 lines) | stat: -rw-r--r-- 807,244 bytes
parent folder | download | duplicates (3)
data_1SUI
# 
_entry.id   1SUI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.286 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1SUI         
RCSB  RCSB022000   
WWPDB D_1000022000 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          1SUS 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1SUI 
_pdbx_database_status.recvd_initial_deposition_date   2004-03-26 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Ferrer, J.-L.' 1 
'Zubieta, C.'   2 
'Dixon, R.A.'   3 
'Noel, J.P.'    4 
# 
_citation.id                        primary 
_citation.title                     'Crystal Structures of Alfalfa Caffeoyl Coenzyme A 3-O-Methyltransferase' 
_citation.journal_abbrev            'Plant Physiol.' 
_citation.journal_volume            137 
_citation.page_first                1009 
_citation.page_last                 1017 
_citation.year                      2005 
_citation.journal_id_ASTM           PLPHAY 
_citation.country                   US 
_citation.journal_id_ISSN           0032-0889 
_citation.journal_id_CSD            0765 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   15734921 
_citation.pdbx_database_id_DOI      10.1104/pp.104.048751 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Ferrer, J.-L.' 1 
primary 'Zubieta, C.'   2 
primary 'Dixon, R.A.'   3 
primary 'Noel, J.P.'    4 
# 
_cell.entry_id           1SUI 
_cell.length_a           60.854 
_cell.length_b           136.486 
_cell.length_c           332.778 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              32 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1SUI 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Caffeoyl-CoA O-methyltransferase' 28036.178 4  2.1.1.104 ? ? ? 
2 non-polymer syn 'CALCIUM ION'                      40.078    4  ?         ? ? ? 
3 non-polymer syn S-ADENOSYL-L-HOMOCYSTEINE          384.411   4  ?         ? ? ? 
4 non-polymer syn 'FERULOYL COENZYME A'              959.702   1  ?         ? ? ? 
5 water       nat water                              18.015    66 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Trans-caffeoyl-CoA 3-O-methyltransferase, CCoAMT, CCoAOMT' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MATNEDQKQTESGRHQEVGHKSLLQSDALYQYILETSVFPREHEAMKELREVTAKHPWNIMTTSADEGQFLSMLLKLINA
KNTMEIGVYTGYSLLATALAIPEDGKILAMDINKENYELGLPVIKKAGVDHKIDFREGPALPVLDEMIKDEKNHGSYDFI
FVDADKDNYLNYHKRLIDLVKVGGVIGYDNTLWNGSVVAPPDAPLRKYVRYYRDFVLELNKALAVDPRIEICMLPVGDGI
TICRRIK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MATNEDQKQTESGRHQEVGHKSLLQSDALYQYILETSVFPREHEAMKELREVTAKHPWNIMTTSADEGQFLSMLLKLINA
KNTMEIGVYTGYSLLATALAIPEDGKILAMDINKENYELGLPVIKKAGVDHKIDFREGPALPVLDEMIKDEKNHGSYDFI
FVDADKDNYLNYHKRLIDLVKVGGVIGYDNTLWNGSVVAPPDAPLRKYVRYYRDFVLELNKALAVDPRIEICMLPVGDGI
TICRRIK
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   THR n 
1 4   ASN n 
1 5   GLU n 
1 6   ASP n 
1 7   GLN n 
1 8   LYS n 
1 9   GLN n 
1 10  THR n 
1 11  GLU n 
1 12  SER n 
1 13  GLY n 
1 14  ARG n 
1 15  HIS n 
1 16  GLN n 
1 17  GLU n 
1 18  VAL n 
1 19  GLY n 
1 20  HIS n 
1 21  LYS n 
1 22  SER n 
1 23  LEU n 
1 24  LEU n 
1 25  GLN n 
1 26  SER n 
1 27  ASP n 
1 28  ALA n 
1 29  LEU n 
1 30  TYR n 
1 31  GLN n 
1 32  TYR n 
1 33  ILE n 
1 34  LEU n 
1 35  GLU n 
1 36  THR n 
1 37  SER n 
1 38  VAL n 
1 39  PHE n 
1 40  PRO n 
1 41  ARG n 
1 42  GLU n 
1 43  HIS n 
1 44  GLU n 
1 45  ALA n 
1 46  MET n 
1 47  LYS n 
1 48  GLU n 
1 49  LEU n 
1 50  ARG n 
1 51  GLU n 
1 52  VAL n 
1 53  THR n 
1 54  ALA n 
1 55  LYS n 
1 56  HIS n 
1 57  PRO n 
1 58  TRP n 
1 59  ASN n 
1 60  ILE n 
1 61  MET n 
1 62  THR n 
1 63  THR n 
1 64  SER n 
1 65  ALA n 
1 66  ASP n 
1 67  GLU n 
1 68  GLY n 
1 69  GLN n 
1 70  PHE n 
1 71  LEU n 
1 72  SER n 
1 73  MET n 
1 74  LEU n 
1 75  LEU n 
1 76  LYS n 
1 77  LEU n 
1 78  ILE n 
1 79  ASN n 
1 80  ALA n 
1 81  LYS n 
1 82  ASN n 
1 83  THR n 
1 84  MET n 
1 85  GLU n 
1 86  ILE n 
1 87  GLY n 
1 88  VAL n 
1 89  TYR n 
1 90  THR n 
1 91  GLY n 
1 92  TYR n 
1 93  SER n 
1 94  LEU n 
1 95  LEU n 
1 96  ALA n 
1 97  THR n 
1 98  ALA n 
1 99  LEU n 
1 100 ALA n 
1 101 ILE n 
1 102 PRO n 
1 103 GLU n 
1 104 ASP n 
1 105 GLY n 
1 106 LYS n 
1 107 ILE n 
1 108 LEU n 
1 109 ALA n 
1 110 MET n 
1 111 ASP n 
1 112 ILE n 
1 113 ASN n 
1 114 LYS n 
1 115 GLU n 
1 116 ASN n 
1 117 TYR n 
1 118 GLU n 
1 119 LEU n 
1 120 GLY n 
1 121 LEU n 
1 122 PRO n 
1 123 VAL n 
1 124 ILE n 
1 125 LYS n 
1 126 LYS n 
1 127 ALA n 
1 128 GLY n 
1 129 VAL n 
1 130 ASP n 
1 131 HIS n 
1 132 LYS n 
1 133 ILE n 
1 134 ASP n 
1 135 PHE n 
1 136 ARG n 
1 137 GLU n 
1 138 GLY n 
1 139 PRO n 
1 140 ALA n 
1 141 LEU n 
1 142 PRO n 
1 143 VAL n 
1 144 LEU n 
1 145 ASP n 
1 146 GLU n 
1 147 MET n 
1 148 ILE n 
1 149 LYS n 
1 150 ASP n 
1 151 GLU n 
1 152 LYS n 
1 153 ASN n 
1 154 HIS n 
1 155 GLY n 
1 156 SER n 
1 157 TYR n 
1 158 ASP n 
1 159 PHE n 
1 160 ILE n 
1 161 PHE n 
1 162 VAL n 
1 163 ASP n 
1 164 ALA n 
1 165 ASP n 
1 166 LYS n 
1 167 ASP n 
1 168 ASN n 
1 169 TYR n 
1 170 LEU n 
1 171 ASN n 
1 172 TYR n 
1 173 HIS n 
1 174 LYS n 
1 175 ARG n 
1 176 LEU n 
1 177 ILE n 
1 178 ASP n 
1 179 LEU n 
1 180 VAL n 
1 181 LYS n 
1 182 VAL n 
1 183 GLY n 
1 184 GLY n 
1 185 VAL n 
1 186 ILE n 
1 187 GLY n 
1 188 TYR n 
1 189 ASP n 
1 190 ASN n 
1 191 THR n 
1 192 LEU n 
1 193 TRP n 
1 194 ASN n 
1 195 GLY n 
1 196 SER n 
1 197 VAL n 
1 198 VAL n 
1 199 ALA n 
1 200 PRO n 
1 201 PRO n 
1 202 ASP n 
1 203 ALA n 
1 204 PRO n 
1 205 LEU n 
1 206 ARG n 
1 207 LYS n 
1 208 TYR n 
1 209 VAL n 
1 210 ARG n 
1 211 TYR n 
1 212 TYR n 
1 213 ARG n 
1 214 ASP n 
1 215 PHE n 
1 216 VAL n 
1 217 LEU n 
1 218 GLU n 
1 219 LEU n 
1 220 ASN n 
1 221 LYS n 
1 222 ALA n 
1 223 LEU n 
1 224 ALA n 
1 225 VAL n 
1 226 ASP n 
1 227 PRO n 
1 228 ARG n 
1 229 ILE n 
1 230 GLU n 
1 231 ILE n 
1 232 CYS n 
1 233 MET n 
1 234 LEU n 
1 235 PRO n 
1 236 VAL n 
1 237 GLY n 
1 238 ASP n 
1 239 GLY n 
1 240 ILE n 
1 241 THR n 
1 242 ILE n 
1 243 CYS n 
1 244 ARG n 
1 245 ARG n 
1 246 ILE n 
1 247 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     Medicago 
_entity_src_gen.pdbx_gene_src_gene                 CCOMT 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Medicago sativa' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3879 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     Escherichia 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   'Escherichia coli' 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       PET15B 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAMT_MEDSA 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MATNEDQKQTESGRHQEVGHKSLLQSDALYQYILETSVFPREHEAMKELREVTAKHPWNIMTTSADEGQFLSMLLKLINA
KNTMEIGVYTGYSLLATALAIPEDGKILAMDINKENYELGLPVIKKAGVDHKIDFREGPALPVLDEMIKDEKNHGSYDFI
FVDADKDNYLNYHKRLIDLVKVGGVIGYDNTLWNGSVVAPPDAPLRKYVRYYRDFVLELNKALAVDPRIEICMLPVGDGI
TICRRIK
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_accession          Q40313 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 1SUI A 1 ? 247 ? Q40313 1 ? 247 ? 1 247 
2 1 1SUI B 1 ? 247 ? Q40313 1 ? 247 ? 1 247 
3 1 1SUI C 1 ? 247 ? Q40313 1 ? 247 ? 1 247 
4 1 1SUI D 1 ? 247 ? Q40313 1 ? 247 ? 1 247 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                   ? 'C3 H7 N O2'          89.093  
ARG 'L-peptide linking' y ARGININE                  ? 'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE                ? 'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'           ? 'C4 H7 N O4'          133.103 
CA  non-polymer         . 'CALCIUM ION'             ? 'Ca 2'                40.078  
CYS 'L-peptide linking' y CYSTEINE                  ? 'C3 H7 N O2 S'        121.158 
FRE non-polymer         . 'FERULOYL COENZYME A'     ? 'C31 H44 N7 O20 P3 S' 959.702 
GLN 'L-peptide linking' y GLUTAMINE                 ? 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'           ? 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE                   ? 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE                 ? 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                     ? 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE                ? 'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                   ? 'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                    ? 'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                ? 'C5 H11 N O2 S'       149.211 
PHE 'L-peptide linking' y PHENYLALANINE             ? 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                   ? 'C5 H9 N O2'          115.130 
SAH 'L-peptide linking' n S-ADENOSYL-L-HOMOCYSTEINE ? 'C14 H20 N6 O5 S'     384.411 
SER 'L-peptide linking' y SERINE                    ? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE                 ? 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                ? 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE                  ? 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE                    ? 'C5 H11 N O2'         117.146 
# 
_exptl.entry_id          1SUI 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.08 
_exptl_crystal.density_percent_sol   60.08 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            288 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              8.50 
_exptl_crystal_grow.pdbx_details    
'PEG 8000, TAPS, calcium acetate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 288K, pH 8.50' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100.0 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   2001-04-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'SI (111)' 
_diffrn_radiation.pdbx_diffrn_protocol             MAD 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
loop_
_diffrn_radiation_wavelength.id 
_diffrn_radiation_wavelength.wavelength 
_diffrn_radiation_wavelength.wt 
1 0.97966 1.0 
2 0.97927 1.0 
3 0.97549 1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE BM30A' 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   BM30A 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        '0.97966, 0.97927, 0.97549' 
# 
_reflns.entry_id                     1SUI 
_reflns.observed_criterion_sigma_I   -3.000 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             25.000 
_reflns.d_resolution_high            2.700 
_reflns.number_obs                   34905 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         85.7 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.063 
_reflns.pdbx_netI_over_sigmaI        22.3000 
_reflns.B_iso_Wilson_estimate        84.70 
_reflns.pdbx_redundancy              2.340 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             2.70 
_reflns_shell.d_res_low              2.78 
_reflns_shell.percent_possible_all   49.5 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.315 
_reflns_shell.meanI_over_sigI_obs    1.000 
_reflns_shell.pdbx_redundancy        1.54 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1SUI 
_refine.ls_number_reflns_obs                     34736 
_refine.ls_number_reflns_all                     34736 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             25.00 
_refine.ls_d_res_high                            2.70 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          0.235 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.235 
_refine.ls_R_factor_R_free                       0.285 
_refine.ls_R_factor_R_free_error                 0.007 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  1761 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               84.00 
_refine.aniso_B[1][1]                            3.51000 
_refine.aniso_B[2][2]                            -17.65000 
_refine.aniso_B[3][3]                            14.14000 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          MAD 
_refine.pdbx_isotropic_thermal_model             ANISOTROPIC 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        1SUI 
_refine_analyze.Luzzati_coordinate_error_obs    0.44 
_refine_analyze.Luzzati_sigma_a_obs             0.57 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.54 
_refine_analyze.Luzzati_sigma_a_free            0.65 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        7210 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         170 
_refine_hist.number_atoms_solvent             66 
_refine_hist.number_atoms_total               7446 
_refine_hist.d_res_high                       2.70 
_refine_hist.d_res_low                        25.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_bond_d                0.008 ? ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_na             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_prot           ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d               ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_na            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_prot          ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg             1.70  ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_na          ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_prot        ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d      22.20 ? ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_na   ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_prot ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d      1.27  ? ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_na   ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_prot ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_scbond_it             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_scangle_it            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.d_res_high                       2.70 
_refine_ls_shell.d_res_low                        2.73 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.R_factor_R_work                  0.46 
_refine_ls_shell.percent_reflns_obs               ? 
_refine_ls_shell.R_factor_R_free                  0.55 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             23 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  1SUI 
_struct.title                     'Alfalfa caffeoyl coenzyme A 3-O-methyltransferase' 
_struct.pdbx_descriptor           'Caffeoyl-CoA O-methyltransferase (E.C.2.1.1.104)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1SUI 
_struct_keywords.pdbx_keywords   TRANSFERASE 
_struct_keywords.text            'ROSSMANN FOLD, PROTEIN-COFACTOR-SUBSTRATE COMPLEX, TRANSFERASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 2 ? 
I N N 3 ? 
J N N 2 ? 
K N N 3 ? 
L N N 2 ? 
M N N 3 ? 
N N N 5 ? 
O N N 5 ? 
P N N 5 ? 
Q N N 5 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  ALA A 28  ? VAL A 38  ? ALA A 28  VAL A 38  1 ? 11 
HELX_P HELX_P2  2  GLU A 44  ? LYS A 55  ? GLU A 44  LYS A 55  1 ? 12 
HELX_P HELX_P3  3  TRP A 58  ? THR A 62  ? TRP A 58  THR A 62  5 ? 5  
HELX_P HELX_P4  4  SER A 64  ? ILE A 78  ? SER A 64  ILE A 78  1 ? 15 
HELX_P HELX_P5  5  VAL A 88  ? THR A 90  ? VAL A 88  THR A 90  5 ? 3  
HELX_P HELX_P6  6  GLY A 91  ? ILE A 101 ? GLY A 91  ILE A 101 1 ? 11 
HELX_P HELX_P7  7  LYS A 114 ? ALA A 127 ? LYS A 114 ALA A 127 1 ? 14 
HELX_P HELX_P8  8  VAL A 129 ? HIS A 131 ? VAL A 129 HIS A 131 5 ? 3  
HELX_P HELX_P9  9  PRO A 139 ? ASP A 150 ? PRO A 139 ASP A 150 1 ? 12 
HELX_P HELX_P10 10 GLU A 151 ? HIS A 154 ? GLU A 151 HIS A 154 5 ? 4  
HELX_P HELX_P11 11 ASN A 168 ? VAL A 180 ? ASN A 168 VAL A 180 1 ? 13 
HELX_P HELX_P12 12 LEU A 192 ? ALA A 199 ? LEU A 192 ALA A 199 5 ? 8  
HELX_P HELX_P13 13 ARG A 206 ? VAL A 225 ? ARG A 206 VAL A 225 1 ? 20 
HELX_P HELX_P14 14 SER B 26  ? VAL B 38  ? SER B 26  VAL B 38  1 ? 13 
HELX_P HELX_P15 15 HIS B 43  ? LYS B 55  ? HIS B 43  LYS B 55  1 ? 13 
HELX_P HELX_P16 16 SER B 64  ? ASN B 79  ? SER B 64  ASN B 79  1 ? 16 
HELX_P HELX_P17 17 VAL B 88  ? THR B 90  ? VAL B 88  THR B 90  5 ? 3  
HELX_P HELX_P18 18 GLY B 91  ? ILE B 101 ? GLY B 91  ILE B 101 1 ? 11 
HELX_P HELX_P19 19 ASN B 113 ? ALA B 127 ? ASN B 113 ALA B 127 1 ? 15 
HELX_P HELX_P20 20 VAL B 129 ? HIS B 131 ? VAL B 129 HIS B 131 5 ? 3  
HELX_P HELX_P21 21 PRO B 139 ? ILE B 148 ? PRO B 139 ILE B 148 1 ? 10 
HELX_P HELX_P22 22 ASN B 168 ? LEU B 179 ? ASN B 168 LEU B 179 1 ? 12 
HELX_P HELX_P23 23 ARG B 206 ? ASP B 226 ? ARG B 206 ASP B 226 1 ? 21 
HELX_P HELX_P24 24 ALA C 28  ? SER C 37  ? ALA C 28  SER C 37  1 ? 10 
HELX_P HELX_P25 25 ALA C 45  ? THR C 53  ? ALA C 45  THR C 53  1 ? 9  
HELX_P HELX_P26 26 ALA C 65  ? ILE C 78  ? ALA C 65  ILE C 78  1 ? 14 
HELX_P HELX_P27 27 GLY C 91  ? ILE C 101 ? GLY C 91  ILE C 101 1 ? 11 
HELX_P HELX_P28 28 GLY C 120 ? ALA C 127 ? GLY C 120 ALA C 127 1 ? 8  
HELX_P HELX_P29 29 VAL C 129 ? ILE C 133 ? VAL C 129 ILE C 133 5 ? 5  
HELX_P HELX_P30 30 ALA C 140 ? ASP C 150 ? ALA C 140 ASP C 150 1 ? 11 
HELX_P HELX_P31 31 ASN C 168 ? VAL C 180 ? ASN C 168 VAL C 180 1 ? 13 
HELX_P HELX_P32 32 ARG C 206 ? ASP C 226 ? ARG C 206 ASP C 226 1 ? 21 
HELX_P HELX_P33 33 ALA D 28  ? THR D 36  ? ALA D 28  THR D 36  1 ? 9  
HELX_P HELX_P34 34 GLU D 44  ? THR D 53  ? GLU D 44  THR D 53  1 ? 10 
HELX_P HELX_P35 35 TRP D 58  ? THR D 62  ? TRP D 58  THR D 62  5 ? 5  
HELX_P HELX_P36 36 SER D 64  ? LEU D 77  ? SER D 64  LEU D 77  1 ? 14 
HELX_P HELX_P37 37 VAL D 88  ? THR D 90  ? VAL D 88  THR D 90  5 ? 3  
HELX_P HELX_P38 38 GLY D 91  ? ILE D 101 ? GLY D 91  ILE D 101 1 ? 11 
HELX_P HELX_P39 39 ASN D 113 ? GLU D 118 ? ASN D 113 GLU D 118 1 ? 6  
HELX_P HELX_P40 40 LEU D 121 ? LYS D 126 ? LEU D 121 LYS D 126 1 ? 6  
HELX_P HELX_P41 41 LEU D 141 ? ASP D 145 ? LEU D 141 ASP D 145 5 ? 5  
HELX_P HELX_P42 42 ASN D 168 ? ARG D 175 ? ASN D 168 ARG D 175 1 ? 8  
HELX_P HELX_P43 43 LEU D 176 ? LYS D 181 ? LEU D 176 LYS D 181 1 ? 6  
HELX_P HELX_P44 44 ARG D 206 ? ALA D 224 ? ARG D 206 ALA D 224 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
metalc1  metalc ? ? E CA . CA ? ? ? 1_555 A ASP 163 OD2 ? ? A CA 305 A ASP 163 1_555 ? ? ? ? ? ? ? 2.895 ? 
metalc2  metalc ? ? E CA . CA ? ? ? 1_555 A ASP 163 OD1 ? ? A CA 305 A ASP 163 1_555 ? ? ? ? ? ? ? 2.740 ? 
metalc3  metalc ? ? E CA . CA ? ? ? 1_555 A ASP 189 OD2 ? ? A CA 305 A ASP 189 1_555 ? ? ? ? ? ? ? 2.266 ? 
metalc4  metalc ? ? E CA . CA ? ? ? 1_555 A ASN 190 OD1 ? ? A CA 305 A ASN 190 1_555 ? ? ? ? ? ? ? 2.610 ? 
metalc5  metalc ? ? E CA . CA ? ? ? 1_555 A ASN 190 ND2 ? ? A CA 305 A ASN 190 1_555 ? ? ? ? ? ? ? 3.221 ? 
metalc6  metalc ? ? H CA . CA ? ? ? 1_555 B ASN 190 OD1 ? ? B CA 306 B ASN 190 1_555 ? ? ? ? ? ? ? 2.480 ? 
metalc7  metalc ? ? H CA . CA ? ? ? 1_555 O HOH .   O   ? ? B CA 306 B HOH 311 1_555 ? ? ? ? ? ? ? 2.458 ? 
metalc8  metalc ? ? H CA . CA ? ? ? 1_555 B ASP 163 OD1 ? ? B CA 306 B ASP 163 1_555 ? ? ? ? ? ? ? 2.524 ? 
metalc9  metalc ? ? H CA . CA ? ? ? 1_555 B ASP 163 OD2 ? ? B CA 306 B ASP 163 1_555 ? ? ? ? ? ? ? 2.685 ? 
metalc10 metalc ? ? H CA . CA ? ? ? 1_555 B ASP 189 OD2 ? ? B CA 306 B ASP 189 1_555 ? ? ? ? ? ? ? 3.228 ? 
metalc11 metalc ? ? J CA . CA ? ? ? 1_555 C ASP 189 OD1 ? ? C CA 307 C ASP 189 1_555 ? ? ? ? ? ? ? 3.218 ? 
metalc12 metalc ? ? J CA . CA ? ? ? 1_555 C ASP 163 OD1 ? ? C CA 307 C ASP 163 1_555 ? ? ? ? ? ? ? 2.870 ? 
metalc13 metalc ? ? J CA . CA ? ? ? 1_555 C ASN 190 OD1 ? ? C CA 307 C ASN 190 1_555 ? ? ? ? ? ? ? 2.430 ? 
metalc14 metalc ? ? J CA . CA ? ? ? 1_555 C ASN 190 ND2 ? ? C CA 307 C ASN 190 1_555 ? ? ? ? ? ? ? 3.191 ? 
metalc15 metalc ? ? J CA . CA ? ? ? 1_555 C ASP 163 OD2 ? ? C CA 307 C ASP 163 1_555 ? ? ? ? ? ? ? 2.779 ? 
metalc16 metalc ? ? L CA . CA ? ? ? 1_555 D ASP 163 OD1 ? ? D CA 308 D ASP 163 1_555 ? ? ? ? ? ? ? 3.324 ? 
metalc17 metalc ? ? L CA . CA ? ? ? 1_555 D ASP 163 OD2 ? ? D CA 308 D ASP 163 1_555 ? ? ? ? ? ? ? 2.904 ? 
metalc18 metalc ? ? L CA . CA ? ? ? 1_555 D ASP 189 OD2 ? ? D CA 308 D ASP 189 1_555 ? ? ? ? ? ? ? 2.308 ? 
metalc19 metalc ? ? L CA . CA ? ? ? 1_555 D ASN 190 OD1 ? ? D CA 308 D ASN 190 1_555 ? ? ? ? ? ? ? 3.267 ? 
metalc20 metalc ? ? L CA . CA ? ? ? 1_555 M SAH .   OXT ? ? D CA 308 D SAH 304 1_555 ? ? ? ? ? ? ? 3.324 ? 
metalc21 metalc ? ? L CA . CA ? ? ? 1_555 D ASN 190 ND2 ? ? D CA 308 D ASN 190 1_555 ? ? ? ? ? ? ? 3.327 ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 7 ? 
B ? 7 ? 
C ? 6 ? 
D ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? parallel      
A 2 3 ? parallel      
A 3 4 ? parallel      
A 4 5 ? parallel      
A 5 6 ? anti-parallel 
A 6 7 ? anti-parallel 
B 1 2 ? parallel      
B 2 3 ? parallel      
B 3 4 ? parallel      
B 4 5 ? parallel      
B 5 6 ? anti-parallel 
B 6 7 ? anti-parallel 
C 1 2 ? parallel      
C 2 3 ? parallel      
C 3 4 ? parallel      
C 4 5 ? anti-parallel 
C 5 6 ? anti-parallel 
D 1 2 ? parallel      
D 2 3 ? parallel      
D 3 4 ? parallel      
D 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ILE A 133 ? GLU A 137 ? ILE A 133 GLU A 137 
A 2 LYS A 106 ? ASP A 111 ? LYS A 106 ASP A 111 
A 3 ASN A 82  ? ILE A 86  ? ASN A 82  ILE A 86  
A 4 PHE A 159 ? VAL A 162 ? PHE A 159 VAL A 162 
A 5 ILE A 186 ? ASP A 189 ? ILE A 186 ASP A 189 
A 6 ILE A 240 ? CYS A 243 ? ILE A 240 CYS A 243 
A 7 CYS A 232 ? LEU A 234 ? CYS A 232 LEU A 234 
B 1 ILE B 133 ? GLU B 137 ? ILE B 133 GLU B 137 
B 2 LYS B 106 ? ASP B 111 ? LYS B 106 ASP B 111 
B 3 ASN B 82  ? ILE B 86  ? ASN B 82  ILE B 86  
B 4 TYR B 157 ? VAL B 162 ? TYR B 157 VAL B 162 
B 5 VAL B 180 ? ASP B 189 ? VAL B 180 ASP B 189 
B 6 ILE B 240 ? ARG B 244 ? ILE B 240 ARG B 244 
B 7 CYS B 232 ? LEU B 234 ? CYS B 232 LEU B 234 
C 1 ILE C 107 ? ASP C 111 ? ILE C 107 ASP C 111 
C 2 THR C 83  ? ILE C 86  ? THR C 83  ILE C 86  
C 3 PHE C 159 ? VAL C 162 ? PHE C 159 VAL C 162 
C 4 ILE C 186 ? ASP C 189 ? ILE C 186 ASP C 189 
C 5 ILE C 240 ? CYS C 243 ? ILE C 240 CYS C 243 
C 6 CYS C 232 ? LEU C 234 ? CYS C 232 LEU C 234 
D 1 ALA D 109 ? MET D 110 ? ALA D 109 MET D 110 
D 2 THR D 83  ? ILE D 86  ? THR D 83  ILE D 86  
D 3 PHE D 159 ? VAL D 162 ? PHE D 159 VAL D 162 
D 4 VAL D 185 ? ASP D 189 ? VAL D 185 ASP D 189 
D 5 ILE D 240 ? CYS D 243 ? ILE D 240 CYS D 243 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O ARG A 136 ? O ARG A 136 N ALA A 109 ? N ALA A 109 
A 2 3 O LYS A 106 ? O LYS A 106 N THR A 83  ? N THR A 83  
A 3 4 N ILE A 86  ? N ILE A 86  O PHE A 161 ? O PHE A 161 
A 4 5 N VAL A 162 ? N VAL A 162 O GLY A 187 ? O GLY A 187 
A 5 6 N ILE A 186 ? N ILE A 186 O CYS A 243 ? O CYS A 243 
A 6 7 O ILE A 242 ? O ILE A 242 N CYS A 232 ? N CYS A 232 
B 1 2 O ASP B 134 ? O ASP B 134 N ILE B 107 ? N ILE B 107 
B 2 3 O MET B 110 ? O MET B 110 N GLU B 85  ? N GLU B 85  
B 3 4 N MET B 84  ? N MET B 84  O PHE B 161 ? O PHE B 161 
B 4 5 N VAL B 162 ? N VAL B 162 O GLY B 187 ? O GLY B 187 
B 5 6 N TYR B 188 ? N TYR B 188 O THR B 241 ? O THR B 241 
B 6 7 O ILE B 240 ? O ILE B 240 N LEU B 234 ? N LEU B 234 
C 1 2 O LEU C 108 ? O LEU C 108 N THR C 83  ? N THR C 83  
C 2 3 N ILE C 86  ? N ILE C 86  O PHE C 161 ? O PHE C 161 
C 3 4 N ILE C 160 ? N ILE C 160 O GLY C 187 ? O GLY C 187 
C 4 5 N ILE C 186 ? N ILE C 186 O CYS C 243 ? O CYS C 243 
C 5 6 O ILE C 242 ? O ILE C 242 N CYS C 232 ? N CYS C 232 
D 1 2 O MET D 110 ? O MET D 110 N GLU D 85  ? N GLU D 85  
D 2 3 N MET D 84  ? N MET D 84  O PHE D 161 ? O PHE D 161 
D 3 4 N VAL D 162 ? N VAL D 162 O ASP D 189 ? O ASP D 189 
D 4 5 N TYR D 188 ? N TYR D 188 O THR D 241 ? O THR D 241 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE CA A 305'  
AC2 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CA B 306'  
AC3 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CA C 307'  
AC4 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CA D 308'  
AC5 Software ? ? ? ? 21 'BINDING SITE FOR RESIDUE SAH A 301' 
AC6 Software ? ? ? ? 14 'BINDING SITE FOR RESIDUE SAH B 302' 
AC7 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE SAH C 303' 
AC8 Software ? ? ? ? 15 'BINDING SITE FOR RESIDUE SAH D 304' 
AC9 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE FRE A 306' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 3  ASP A 163 ? ASP A 163 . ? 1_555 ? 
2  AC1 3  ASP A 189 ? ASP A 189 . ? 1_555 ? 
3  AC1 3  ASN A 190 ? ASN A 190 . ? 1_555 ? 
4  AC2 4  ASP B 163 ? ASP B 163 . ? 1_555 ? 
5  AC2 4  ASP B 189 ? ASP B 189 . ? 1_555 ? 
6  AC2 4  ASN B 190 ? ASN B 190 . ? 1_555 ? 
7  AC2 4  HOH O .   ? HOH B 311 . ? 1_555 ? 
8  AC3 4  ASP C 163 ? ASP C 163 . ? 1_555 ? 
9  AC3 4  ASP C 189 ? ASP C 189 . ? 1_555 ? 
10 AC3 4  ASN C 190 ? ASN C 190 . ? 1_555 ? 
11 AC3 4  SAH K .   ? SAH C 303 . ? 1_555 ? 
12 AC4 4  ASP D 163 ? ASP D 163 . ? 1_555 ? 
13 AC4 4  ASP D 189 ? ASP D 189 . ? 1_555 ? 
14 AC4 4  ASN D 190 ? ASN D 190 . ? 1_555 ? 
15 AC4 4  SAH M .   ? SAH D 304 . ? 1_555 ? 
16 AC5 21 MET A 61  ? MET A 61  . ? 1_555 ? 
17 AC5 21 THR A 62  ? THR A 62  . ? 1_555 ? 
18 AC5 21 THR A 63  ? THR A 63  . ? 1_555 ? 
19 AC5 21 GLU A 85  ? GLU A 85  . ? 1_555 ? 
20 AC5 21 GLY A 87  ? GLY A 87  . ? 1_555 ? 
21 AC5 21 VAL A 88  ? VAL A 88  . ? 1_555 ? 
22 AC5 21 TYR A 89  ? TYR A 89  . ? 1_555 ? 
23 AC5 21 SER A 93  ? SER A 93  . ? 1_555 ? 
24 AC5 21 ASP A 111 ? ASP A 111 . ? 1_555 ? 
25 AC5 21 ILE A 112 ? ILE A 112 . ? 1_555 ? 
26 AC5 21 GLY A 138 ? GLY A 138 . ? 1_555 ? 
27 AC5 21 PRO A 139 ? PRO A 139 . ? 1_555 ? 
28 AC5 21 ALA A 140 ? ALA A 140 . ? 1_555 ? 
29 AC5 21 ASP A 163 ? ASP A 163 . ? 1_555 ? 
30 AC5 21 ALA A 164 ? ALA A 164 . ? 1_555 ? 
31 AC5 21 ASP A 165 ? ASP A 165 . ? 1_555 ? 
32 AC5 21 TYR A 172 ? TYR A 172 . ? 1_555 ? 
33 AC5 21 FRE G .   ? FRE A 306 . ? 1_555 ? 
34 AC5 21 HOH N .   ? HOH A 307 . ? 1_555 ? 
35 AC5 21 HOH N .   ? HOH A 308 . ? 1_555 ? 
36 AC5 21 HOH N .   ? HOH A 310 . ? 1_555 ? 
37 AC6 14 MET B 61  ? MET B 61  . ? 1_555 ? 
38 AC6 14 THR B 62  ? THR B 62  . ? 1_555 ? 
39 AC6 14 GLU B 67  ? GLU B 67  . ? 1_555 ? 
40 AC6 14 GLY B 87  ? GLY B 87  . ? 1_555 ? 
41 AC6 14 VAL B 88  ? VAL B 88  . ? 1_555 ? 
42 AC6 14 TYR B 89  ? TYR B 89  . ? 1_555 ? 
43 AC6 14 SER B 93  ? SER B 93  . ? 1_555 ? 
44 AC6 14 ASP B 111 ? ASP B 111 . ? 1_555 ? 
45 AC6 14 ILE B 112 ? ILE B 112 . ? 1_555 ? 
46 AC6 14 ASP B 163 ? ASP B 163 . ? 1_555 ? 
47 AC6 14 ASP B 165 ? ASP B 165 . ? 1_555 ? 
48 AC6 14 TYR B 172 ? TYR B 172 . ? 1_555 ? 
49 AC6 14 ASP B 189 ? ASP B 189 . ? 1_555 ? 
50 AC6 14 HOH O .   ? HOH B 308 . ? 1_555 ? 
51 AC7 12 ILE C 60  ? ILE C 60  . ? 1_555 ? 
52 AC7 12 MET C 61  ? MET C 61  . ? 1_555 ? 
53 AC7 12 GLU C 67  ? GLU C 67  . ? 1_555 ? 
54 AC7 12 GLY C 87  ? GLY C 87  . ? 1_555 ? 
55 AC7 12 VAL C 88  ? VAL C 88  . ? 1_555 ? 
56 AC7 12 TYR C 89  ? TYR C 89  . ? 1_555 ? 
57 AC7 12 SER C 93  ? SER C 93  . ? 1_555 ? 
58 AC7 12 ILE C 112 ? ILE C 112 . ? 1_555 ? 
59 AC7 12 ASP C 163 ? ASP C 163 . ? 1_555 ? 
60 AC7 12 ASP C 165 ? ASP C 165 . ? 1_555 ? 
61 AC7 12 CA  J .   ? CA  C 307 . ? 1_555 ? 
62 AC7 12 LYS D 207 ? LYS D 207 . ? 3_555 ? 
63 AC8 15 PRO C 57  ? PRO C 57  . ? 3_555 ? 
64 AC8 15 MET D 61  ? MET D 61  . ? 1_555 ? 
65 AC8 15 THR D 63  ? THR D 63  . ? 1_555 ? 
66 AC8 15 GLY D 87  ? GLY D 87  . ? 1_555 ? 
67 AC8 15 VAL D 88  ? VAL D 88  . ? 1_555 ? 
68 AC8 15 TYR D 89  ? TYR D 89  . ? 1_555 ? 
69 AC8 15 SER D 93  ? SER D 93  . ? 1_555 ? 
70 AC8 15 ASP D 111 ? ASP D 111 . ? 1_555 ? 
71 AC8 15 ILE D 112 ? ILE D 112 . ? 1_555 ? 
72 AC8 15 ASN D 113 ? ASN D 113 . ? 1_555 ? 
73 AC8 15 ASP D 163 ? ASP D 163 . ? 1_555 ? 
74 AC8 15 ALA D 164 ? ALA D 164 . ? 1_555 ? 
75 AC8 15 ASP D 165 ? ASP D 165 . ? 1_555 ? 
76 AC8 15 TYR D 172 ? TYR D 172 . ? 1_555 ? 
77 AC8 15 CA  L .   ? CA  D 308 . ? 1_555 ? 
78 AC9 12 LYS A 21  ? LYS A 21  . ? 1_555 ? 
79 AC9 12 ILE A 60  ? ILE A 60  . ? 1_555 ? 
80 AC9 12 ASP A 163 ? ASP A 163 . ? 1_555 ? 
81 AC9 12 LYS A 166 ? LYS A 166 . ? 1_555 ? 
82 AC9 12 ASN A 190 ? ASN A 190 . ? 1_555 ? 
83 AC9 12 TRP A 193 ? TRP A 193 . ? 1_555 ? 
84 AC9 12 ASN A 194 ? ASN A 194 . ? 1_555 ? 
85 AC9 12 PRO A 204 ? PRO A 204 . ? 1_555 ? 
86 AC9 12 ARG A 206 ? ARG A 206 . ? 1_555 ? 
87 AC9 12 SAH F .   ? SAH A 301 . ? 1_555 ? 
88 AC9 12 HOH N .   ? HOH A 308 . ? 1_555 ? 
89 AC9 12 TRP B 58  ? TRP B 58  . ? 8_555 ? 
# 
_database_PDB_matrix.entry_id          1SUI 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    1SUI 
_atom_sites.fract_transf_matrix[1][1]   0.016433 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007327 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.003005 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CA 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . LYS A 1 21  ? 32.783  44.353  36.405  1.00 97.33  ? 21  LYS A N     1 
ATOM   2    C  CA    . LYS A 1 21  ? 31.664  44.809  37.284  1.00 97.42  ? 21  LYS A CA    1 
ATOM   3    C  C     . LYS A 1 21  ? 30.300  44.273  36.814  1.00 97.20  ? 21  LYS A C     1 
ATOM   4    O  O     . LYS A 1 21  ? 30.232  43.363  35.971  1.00 98.03  ? 21  LYS A O     1 
ATOM   5    C  CB    . LYS A 1 21  ? 31.637  46.344  37.343  1.00 97.16  ? 21  LYS A CB    1 
ATOM   6    C  CG    . LYS A 1 21  ? 32.917  46.949  37.896  1.00 97.34  ? 21  LYS A CG    1 
ATOM   7    C  CD    . LYS A 1 21  ? 32.760  48.417  38.256  1.00 97.96  ? 21  LYS A CD    1 
ATOM   8    C  CE    . LYS A 1 21  ? 34.051  48.952  38.871  1.00 98.33  ? 21  LYS A CE    1 
ATOM   9    N  NZ    . LYS A 1 21  ? 33.889  50.300  39.481  1.00 97.49  ? 21  LYS A NZ    1 
ATOM   10   N  N     . SER A 1 22  ? 29.223  44.836  37.370  1.00 95.26  ? 22  SER A N     1 
ATOM   11   C  CA    . SER A 1 22  ? 27.851  44.441  37.032  1.00 91.68  ? 22  SER A CA    1 
ATOM   12   C  C     . SER A 1 22  ? 26.881  45.602  37.240  1.00 88.96  ? 22  SER A C     1 
ATOM   13   O  O     . SER A 1 22  ? 27.284  46.691  37.648  1.00 88.47  ? 22  SER A O     1 
ATOM   14   C  CB    . SER A 1 22  ? 27.419  43.241  37.885  1.00 91.77  ? 22  SER A CB    1 
ATOM   15   O  OG    . SER A 1 22  ? 27.771  43.431  39.247  1.00 91.42  ? 22  SER A OG    1 
ATOM   16   N  N     . LEU A 1 23  ? 25.605  45.364  36.954  1.00 85.81  ? 23  LEU A N     1 
ATOM   17   C  CA    . LEU A 1 23  ? 24.576  46.394  37.102  1.00 83.05  ? 23  LEU A CA    1 
ATOM   18   C  C     . LEU A 1 23  ? 23.921  46.401  38.478  1.00 80.88  ? 23  LEU A C     1 
ATOM   19   O  O     . LEU A 1 23  ? 22.944  47.116  38.710  1.00 79.39  ? 23  LEU A O     1 
ATOM   20   C  CB    . LEU A 1 23  ? 23.476  46.202  36.058  1.00 83.61  ? 23  LEU A CB    1 
ATOM   21   C  CG    . LEU A 1 23  ? 23.797  46.407  34.587  1.00 83.03  ? 23  LEU A CG    1 
ATOM   22   C  CD1   . LEU A 1 23  ? 22.502  46.343  33.799  1.00 83.17  ? 23  LEU A CD1   1 
ATOM   23   C  CD2   . LEU A 1 23  ? 24.471  47.749  34.396  1.00 83.74  ? 23  LEU A CD2   1 
ATOM   24   N  N     . LEU A 1 24  ? 24.450  45.597  39.387  1.00 79.15  ? 24  LEU A N     1 
ATOM   25   C  CA    . LEU A 1 24  ? 23.891  45.519  40.721  1.00 77.55  ? 24  LEU A CA    1 
ATOM   26   C  C     . LEU A 1 24  ? 24.594  46.480  41.676  1.00 79.01  ? 24  LEU A C     1 
ATOM   27   O  O     . LEU A 1 24  ? 25.504  47.210  41.283  1.00 79.59  ? 24  LEU A O     1 
ATOM   28   C  CB    . LEU A 1 24  ? 23.963  44.073  41.220  1.00 73.47  ? 24  LEU A CB    1 
ATOM   29   C  CG    . LEU A 1 24  ? 23.103  43.102  40.405  1.00 68.70  ? 24  LEU A CG    1 
ATOM   30   C  CD1   . LEU A 1 24  ? 23.291  41.689  40.877  1.00 66.94  ? 24  LEU A CD1   1 
ATOM   31   C  CD2   . LEU A 1 24  ? 21.663  43.496  40.536  1.00 68.66  ? 24  LEU A CD2   1 
ATOM   32   N  N     . GLN A 1 25  ? 24.160  46.483  42.929  1.00 80.66  ? 25  GLN A N     1 
ATOM   33   C  CA    . GLN A 1 25  ? 24.720  47.374  43.936  1.00 81.80  ? 25  GLN A CA    1 
ATOM   34   C  C     . GLN A 1 25  ? 26.120  47.004  44.419  1.00 82.33  ? 25  GLN A C     1 
ATOM   35   O  O     . GLN A 1 25  ? 26.887  47.873  44.817  1.00 83.10  ? 25  GLN A O     1 
ATOM   36   C  CB    . GLN A 1 25  ? 23.770  47.444  45.134  1.00 82.73  ? 25  GLN A CB    1 
ATOM   37   C  CG    . GLN A 1 25  ? 23.573  46.117  45.862  1.00 83.80  ? 25  GLN A CG    1 
ATOM   38   C  CD    . GLN A 1 25  ? 22.416  46.155  46.854  1.00 84.47  ? 25  GLN A CD    1 
ATOM   39   O  OE1   . GLN A 1 25  ? 22.156  45.177  47.559  1.00 84.51  ? 25  GLN A OE1   1 
ATOM   40   N  NE2   . GLN A 1 25  ? 21.711  47.285  46.905  1.00 84.05  ? 25  GLN A NE2   1 
ATOM   41   N  N     . SER A 1 26  ? 26.462  45.723  44.384  1.00 82.34  ? 26  SER A N     1 
ATOM   42   C  CA    . SER A 1 26  ? 27.771  45.300  44.855  1.00 82.75  ? 26  SER A CA    1 
ATOM   43   C  C     . SER A 1 26  ? 28.295  44.113  44.069  1.00 82.92  ? 26  SER A C     1 
ATOM   44   O  O     . SER A 1 26  ? 27.518  43.315  43.547  1.00 82.66  ? 26  SER A O     1 
ATOM   45   C  CB    . SER A 1 26  ? 27.682  44.921  46.331  1.00 84.01  ? 26  SER A CB    1 
ATOM   46   O  OG    . SER A 1 26  ? 26.745  43.871  46.523  1.00 84.96  ? 26  SER A OG    1 
ATOM   47   N  N     . ASP A 1 27  ? 29.615  43.987  43.997  1.00 82.99  ? 27  ASP A N     1 
ATOM   48   C  CA    . ASP A 1 27  ? 30.208  42.874  43.275  1.00 83.79  ? 27  ASP A CA    1 
ATOM   49   C  C     . ASP A 1 27  ? 30.027  41.581  44.059  1.00 83.31  ? 27  ASP A C     1 
ATOM   50   O  O     . ASP A 1 27  ? 30.193  40.486  43.509  1.00 84.11  ? 27  ASP A O     1 
ATOM   51   C  CB    . ASP A 1 27  ? 31.698  43.117  43.023  1.00 85.69  ? 27  ASP A CB    1 
ATOM   52   C  CG    . ASP A 1 27  ? 31.952  44.339  42.164  1.00 88.59  ? 27  ASP A CG    1 
ATOM   53   O  OD1   . ASP A 1 27  ? 31.350  44.433  41.069  1.00 90.40  ? 27  ASP A OD1   1 
ATOM   54   O  OD2   . ASP A 1 27  ? 32.755  45.206  42.580  1.00 90.52  ? 27  ASP A OD2   1 
ATOM   55   N  N     . ALA A 1 28  ? 29.683  41.698  45.338  1.00 80.69  ? 28  ALA A N     1 
ATOM   56   C  CA    . ALA A 1 28  ? 29.499  40.508  46.148  1.00 78.66  ? 28  ALA A CA    1 
ATOM   57   C  C     . ALA A 1 28  ? 28.084  39.957  46.044  1.00 77.57  ? 28  ALA A C     1 
ATOM   58   O  O     . ALA A 1 28  ? 27.881  38.751  46.181  1.00 77.76  ? 28  ALA A O     1 
ATOM   59   C  CB    . ALA A 1 28  ? 29.844  40.797  47.578  1.00 77.87  ? 28  ALA A CB    1 
ATOM   60   N  N     . LEU A 1 29  ? 27.107  40.827  45.797  1.00 75.75  ? 29  LEU A N     1 
ATOM   61   C  CA    . LEU A 1 29  ? 25.721  40.375  45.673  1.00 75.25  ? 29  LEU A CA    1 
ATOM   62   C  C     . LEU A 1 29  ? 25.632  39.585  44.383  1.00 75.47  ? 29  LEU A C     1 
ATOM   63   O  O     . LEU A 1 29  ? 25.050  38.496  44.330  1.00 74.30  ? 29  LEU A O     1 
ATOM   64   C  CB    . LEU A 1 29  ? 24.757  41.563  45.594  1.00 74.12  ? 29  LEU A CB    1 
ATOM   65   C  CG    . LEU A 1 29  ? 23.257  41.333  45.852  1.00 73.13  ? 29  LEU A CG    1 
ATOM   66   C  CD1   . LEU A 1 29  ? 22.504  42.521  45.306  1.00 72.81  ? 29  LEU A CD1   1 
ATOM   67   C  CD2   . LEU A 1 29  ? 22.741  40.069  45.194  1.00 73.79  ? 29  LEU A CD2   1 
ATOM   68   N  N     . TYR A 1 30  ? 26.215  40.160  43.337  1.00 76.17  ? 30  TYR A N     1 
ATOM   69   C  CA    . TYR A 1 30  ? 26.226  39.535  42.029  1.00 77.16  ? 30  TYR A CA    1 
ATOM   70   C  C     . TYR A 1 30  ? 26.909  38.175  42.129  1.00 77.68  ? 30  TYR A C     1 
ATOM   71   O  O     . TYR A 1 30  ? 26.380  37.154  41.663  1.00 78.55  ? 30  TYR A O     1 
ATOM   72   C  CB    . TYR A 1 30  ? 26.964  40.421  41.027  1.00 77.72  ? 30  TYR A CB    1 
ATOM   73   C  CG    . TYR A 1 30  ? 27.060  39.796  39.663  1.00 79.24  ? 30  TYR A CG    1 
ATOM   74   C  CD1   . TYR A 1 30  ? 25.908  39.435  38.962  1.00 80.37  ? 30  TYR A CD1   1 
ATOM   75   C  CD2   . TYR A 1 30  ? 28.296  39.509  39.097  1.00 79.30  ? 30  TYR A CD2   1 
ATOM   76   C  CE1   . TYR A 1 30  ? 25.986  38.796  37.735  1.00 81.25  ? 30  TYR A CE1   1 
ATOM   77   C  CE2   . TYR A 1 30  ? 28.386  38.874  37.870  1.00 80.67  ? 30  TYR A CE2   1 
ATOM   78   C  CZ    . TYR A 1 30  ? 27.229  38.517  37.196  1.00 81.46  ? 30  TYR A CZ    1 
ATOM   79   O  OH    . TYR A 1 30  ? 27.315  37.870  35.986  1.00 83.57  ? 30  TYR A OH    1 
ATOM   80   N  N     . GLN A 1 31  ? 28.083  38.164  42.749  1.00 76.58  ? 31  GLN A N     1 
ATOM   81   C  CA    . GLN A 1 31  ? 28.819  36.925  42.916  1.00 75.38  ? 31  GLN A CA    1 
ATOM   82   C  C     . GLN A 1 31  ? 27.964  35.872  43.617  1.00 73.64  ? 31  GLN A C     1 
ATOM   83   O  O     . GLN A 1 31  ? 27.977  34.697  43.235  1.00 72.85  ? 31  GLN A O     1 
ATOM   84   C  CB    . GLN A 1 31  ? 30.101  37.187  43.701  1.00 77.36  ? 31  GLN A CB    1 
ATOM   85   C  CG    . GLN A 1 31  ? 31.291  37.583  42.830  1.00 79.73  ? 31  GLN A CG    1 
ATOM   86   C  CD    . GLN A 1 31  ? 31.743  36.449  41.927  1.00 82.01  ? 31  GLN A CD    1 
ATOM   87   O  OE1   . GLN A 1 31  ? 31.133  36.184  40.890  1.00 83.61  ? 31  GLN A OE1   1 
ATOM   88   N  NE2   . GLN A 1 31  ? 32.810  35.758  42.328  1.00 83.08  ? 31  GLN A NE2   1 
ATOM   89   N  N     . TYR A 1 32  ? 27.212  36.302  44.629  1.00 72.08  ? 32  TYR A N     1 
ATOM   90   C  CA    . TYR A 1 32  ? 26.339  35.401  45.382  1.00 70.80  ? 32  TYR A CA    1 
ATOM   91   C  C     . TYR A 1 32  ? 25.390  34.661  44.450  1.00 69.04  ? 32  TYR A C     1 
ATOM   92   O  O     . TYR A 1 32  ? 25.152  33.468  44.624  1.00 68.57  ? 32  TYR A O     1 
ATOM   93   C  CB    . TYR A 1 32  ? 25.526  36.181  46.434  1.00 71.83  ? 32  TYR A CB    1 
ATOM   94   C  CG    . TYR A 1 32  ? 24.435  35.370  47.119  1.00 71.29  ? 32  TYR A CG    1 
ATOM   95   C  CD1   . TYR A 1 32  ? 24.748  34.294  47.951  1.00 71.53  ? 32  TYR A CD1   1 
ATOM   96   C  CD2   . TYR A 1 32  ? 23.089  35.651  46.892  1.00 70.97  ? 32  TYR A CD2   1 
ATOM   97   C  CE1   . TYR A 1 32  ? 23.745  33.516  48.531  1.00 71.68  ? 32  TYR A CE1   1 
ATOM   98   C  CE2   . TYR A 1 32  ? 22.081  34.881  47.465  1.00 71.62  ? 32  TYR A CE2   1 
ATOM   99   C  CZ    . TYR A 1 32  ? 22.414  33.816  48.279  1.00 72.10  ? 32  TYR A CZ    1 
ATOM   100  O  OH    . TYR A 1 32  ? 21.413  33.041  48.820  1.00 73.15  ? 32  TYR A OH    1 
ATOM   101  N  N     . ILE A 1 33  ? 24.855  35.370  43.459  1.00 67.71  ? 33  ILE A N     1 
ATOM   102  C  CA    . ILE A 1 33  ? 23.925  34.767  42.510  1.00 66.49  ? 33  ILE A CA    1 
ATOM   103  C  C     . ILE A 1 33  ? 24.626  33.705  41.680  1.00 67.14  ? 33  ILE A C     1 
ATOM   104  O  O     . ILE A 1 33  ? 24.086  32.620  41.434  1.00 66.45  ? 33  ILE A O     1 
ATOM   105  C  CB    . ILE A 1 33  ? 23.336  35.830  41.576  1.00 64.19  ? 33  ILE A CB    1 
ATOM   106  C  CG1   . ILE A 1 33  ? 22.665  36.922  42.409  1.00 64.03  ? 33  ILE A CG1   1 
ATOM   107  C  CG2   . ILE A 1 33  ? 22.326  35.197  40.651  1.00 63.81  ? 33  ILE A CG2   1 
ATOM   108  C  CD1   . ILE A 1 33  ? 22.010  38.017  41.613  1.00 61.59  ? 33  ILE A CD1   1 
ATOM   109  N  N     . LEU A 1 34  ? 25.847  34.030  41.269  1.00 67.86  ? 34  LEU A N     1 
ATOM   110  C  CA    . LEU A 1 34  ? 26.670  33.142  40.459  1.00 68.16  ? 34  LEU A CA    1 
ATOM   111  C  C     . LEU A 1 34  ? 27.097  31.904  41.220  1.00 68.59  ? 34  LEU A C     1 
ATOM   112  O  O     . LEU A 1 34  ? 26.920  30.773  40.754  1.00 67.15  ? 34  LEU A O     1 
ATOM   113  C  CB    . LEU A 1 34  ? 27.911  33.888  39.998  1.00 67.53  ? 34  LEU A CB    1 
ATOM   114  C  CG    . LEU A 1 34  ? 27.579  35.146  39.213  1.00 68.26  ? 34  LEU A CG    1 
ATOM   115  C  CD1   . LEU A 1 34  ? 28.812  36.009  39.092  1.00 68.15  ? 34  LEU A CD1   1 
ATOM   116  C  CD2   . LEU A 1 34  ? 27.027  34.755  37.853  1.00 67.89  ? 34  LEU A CD2   1 
ATOM   117  N  N     . GLU A 1 35  ? 27.673  32.131  42.394  1.00 70.07  ? 35  GLU A N     1 
ATOM   118  C  CA    . GLU A 1 35  ? 28.151  31.037  43.220  1.00 72.53  ? 35  GLU A CA    1 
ATOM   119  C  C     . GLU A 1 35  ? 27.059  30.107  43.744  1.00 72.28  ? 35  GLU A C     1 
ATOM   120  O  O     . GLU A 1 35  ? 27.314  28.926  43.978  1.00 72.82  ? 35  GLU A O     1 
ATOM   121  C  CB    . GLU A 1 35  ? 28.980  31.582  44.394  1.00 74.10  ? 35  GLU A CB    1 
ATOM   122  C  CG    . GLU A 1 35  ? 30.410  32.046  44.023  1.00 77.76  ? 35  GLU A CG    1 
ATOM   123  C  CD    . GLU A 1 35  ? 31.274  30.937  43.395  1.00 79.60  ? 35  GLU A CD    1 
ATOM   124  O  OE1   . GLU A 1 35  ? 31.167  29.767  43.831  1.00 81.32  ? 35  GLU A OE1   1 
ATOM   125  O  OE2   . GLU A 1 35  ? 32.074  31.233  42.475  1.00 79.77  ? 35  GLU A OE2   1 
ATOM   126  N  N     . THR A 1 36  ? 25.840  30.610  43.900  1.00 72.02  ? 36  THR A N     1 
ATOM   127  C  CA    . THR A 1 36  ? 24.788  29.763  44.436  1.00 72.08  ? 36  THR A CA    1 
ATOM   128  C  C     . THR A 1 36  ? 23.778  29.211  43.451  1.00 71.48  ? 36  THR A C     1 
ATOM   129  O  O     . THR A 1 36  ? 23.353  28.069  43.591  1.00 72.75  ? 36  THR A O     1 
ATOM   130  C  CB    . THR A 1 36  ? 24.001  30.477  45.570  1.00 73.02  ? 36  THR A CB    1 
ATOM   131  O  OG1   . THR A 1 36  ? 23.210  31.537  45.017  1.00 73.81  ? 36  THR A OG1   1 
ATOM   132  C  CG2   . THR A 1 36  ? 24.968  31.048  46.623  1.00 73.31  ? 36  THR A CG2   1 
ATOM   133  N  N     . SER A 1 37  ? 23.382  29.987  42.453  1.00 70.65  ? 37  SER A N     1 
ATOM   134  C  CA    . SER A 1 37  ? 22.378  29.473  41.534  1.00 69.75  ? 37  SER A CA    1 
ATOM   135  C  C     . SER A 1 37  ? 22.781  29.390  40.083  1.00 69.05  ? 37  SER A C     1 
ATOM   136  O  O     . SER A 1 37  ? 21.952  29.066  39.236  1.00 68.47  ? 37  SER A O     1 
ATOM   137  C  CB    . SER A 1 37  ? 21.117  30.300  41.645  1.00 70.26  ? 37  SER A CB    1 
ATOM   138  O  OG    . SER A 1 37  ? 21.432  31.648  41.382  1.00 74.24  ? 37  SER A OG    1 
ATOM   139  N  N     . VAL A 1 38  ? 24.043  29.679  39.783  1.00 68.99  ? 38  VAL A N     1 
ATOM   140  C  CA    . VAL A 1 38  ? 24.500  29.594  38.399  1.00 68.07  ? 38  VAL A CA    1 
ATOM   141  C  C     . VAL A 1 38  ? 25.608  28.560  38.180  1.00 66.94  ? 38  VAL A C     1 
ATOM   142  O  O     . VAL A 1 38  ? 25.379  27.532  37.547  1.00 66.00  ? 38  VAL A O     1 
ATOM   143  C  CB    . VAL A 1 38  ? 24.987  30.970  37.862  1.00 68.40  ? 38  VAL A CB    1 
ATOM   144  C  CG1   . VAL A 1 38  ? 25.329  30.855  36.385  1.00 66.22  ? 38  VAL A CG1   1 
ATOM   145  C  CG2   . VAL A 1 38  ? 23.912  32.037  38.077  1.00 66.81  ? 38  VAL A CG2   1 
ATOM   146  N  N     . PHE A 1 39  ? 26.796  28.812  38.715  1.00 66.81  ? 39  PHE A N     1 
ATOM   147  C  CA    . PHE A 1 39  ? 27.905  27.888  38.500  1.00 68.32  ? 39  PHE A CA    1 
ATOM   148  C  C     . PHE A 1 39  ? 27.612  26.408  38.774  1.00 70.61  ? 39  PHE A C     1 
ATOM   149  O  O     . PHE A 1 39  ? 27.881  25.547  37.931  1.00 70.10  ? 39  PHE A O     1 
ATOM   150  C  CB    . PHE A 1 39  ? 29.136  28.354  39.280  1.00 65.35  ? 39  PHE A CB    1 
ATOM   151  C  CG    . PHE A 1 39  ? 29.624  29.710  38.870  1.00 63.20  ? 39  PHE A CG    1 
ATOM   152  C  CD1   . PHE A 1 39  ? 29.632  30.083  37.529  1.00 62.78  ? 39  PHE A CD1   1 
ATOM   153  C  CD2   . PHE A 1 39  ? 30.068  30.619  39.816  1.00 62.53  ? 39  PHE A CD2   1 
ATOM   154  C  CE1   . PHE A 1 39  ? 30.072  31.348  37.135  1.00 62.66  ? 39  PHE A CE1   1 
ATOM   155  C  CE2   . PHE A 1 39  ? 30.514  31.893  39.435  1.00 63.56  ? 39  PHE A CE2   1 
ATOM   156  C  CZ    . PHE A 1 39  ? 30.514  32.257  38.091  1.00 62.52  ? 39  PHE A CZ    1 
ATOM   157  N  N     . PRO A 1 40  ? 27.071  26.087  39.959  1.00 73.25  ? 40  PRO A N     1 
ATOM   158  C  CA    . PRO A 1 40  ? 26.771  24.681  40.253  1.00 74.89  ? 40  PRO A CA    1 
ATOM   159  C  C     . PRO A 1 40  ? 25.688  24.229  39.288  1.00 77.18  ? 40  PRO A C     1 
ATOM   160  O  O     . PRO A 1 40  ? 24.606  24.820  39.248  1.00 78.63  ? 40  PRO A O     1 
ATOM   161  C  CB    . PRO A 1 40  ? 26.264  24.736  41.685  1.00 74.68  ? 40  PRO A CB    1 
ATOM   162  C  CG    . PRO A 1 40  ? 26.991  25.938  42.251  1.00 74.19  ? 40  PRO A CG    1 
ATOM   163  C  CD    . PRO A 1 40  ? 26.854  26.931  41.146  1.00 73.38  ? 40  PRO A CD    1 
ATOM   164  N  N     . ARG A 1 41  ? 25.961  23.191  38.509  1.00 79.16  ? 41  ARG A N     1 
ATOM   165  C  CA    . ARG A 1 41  ? 24.976  22.712  37.527  1.00 81.15  ? 41  ARG A CA    1 
ATOM   166  C  C     . ARG A 1 41  ? 24.899  23.694  36.363  1.00 80.78  ? 41  ARG A C     1 
ATOM   167  O  O     . ARG A 1 41  ? 23.920  24.433  36.243  1.00 81.52  ? 41  ARG A O     1 
ATOM   168  C  CB    . ARG A 1 41  ? 23.562  22.622  38.123  1.00 83.33  ? 41  ARG A CB    1 
ATOM   169  C  CG    . ARG A 1 41  ? 23.448  22.016  39.515  1.00 84.85  ? 41  ARG A CG    1 
ATOM   170  C  CD    . ARG A 1 41  ? 22.036  22.193  40.055  1.00 85.05  ? 41  ARG A CD    1 
ATOM   171  N  NE    . ARG A 1 41  ? 21.051  21.450  39.275  1.00 86.40  ? 41  ARG A NE    1 
ATOM   172  C  CZ    . ARG A 1 41  ? 19.732  21.595  39.393  1.00 87.99  ? 41  ARG A CZ    1 
ATOM   173  N  NH1   . ARG A 1 41  ? 19.218  22.464  40.263  1.00 87.35  ? 41  ARG A NH1   1 
ATOM   174  N  NH2   . ARG A 1 41  ? 18.919  20.864  38.640  1.00 89.24  ? 41  ARG A NH2   1 
ATOM   175  N  N     . GLU A 1 42  ? 25.930  23.720  35.526  1.00 80.02  ? 42  GLU A N     1 
ATOM   176  C  CA    . GLU A 1 42  ? 25.934  24.597  34.365  1.00 79.09  ? 42  GLU A CA    1 
ATOM   177  C  C     . GLU A 1 42  ? 26.687  23.883  33.256  1.00 77.83  ? 42  GLU A C     1 
ATOM   178  O  O     . GLU A 1 42  ? 27.759  24.281  32.795  1.00 78.64  ? 42  GLU A O     1 
ATOM   179  C  CB    . GLU A 1 42  ? 26.581  25.947  34.686  1.00 79.48  ? 42  GLU A CB    1 
ATOM   180  C  CG    . GLU A 1 42  ? 28.075  25.915  34.754  1.00 81.58  ? 42  GLU A CG    1 
ATOM   181  C  CD    . GLU A 1 42  ? 28.676  27.289  34.568  1.00 82.01  ? 42  GLU A CD    1 
ATOM   182  O  OE1   . GLU A 1 42  ? 28.219  28.029  33.663  1.00 81.43  ? 42  GLU A OE1   1 
ATOM   183  O  OE2   . GLU A 1 42  ? 29.612  27.615  35.325  1.00 82.19  ? 42  GLU A OE2   1 
ATOM   184  N  N     . HIS A 1 43  ? 26.095  22.786  32.841  1.00 75.06  ? 43  HIS A N     1 
ATOM   185  C  CA    . HIS A 1 43  ? 26.644  21.962  31.790  1.00 72.49  ? 43  HIS A CA    1 
ATOM   186  C  C     . HIS A 1 43  ? 28.140  21.577  31.805  1.00 72.22  ? 43  HIS A C     1 
ATOM   187  O  O     . HIS A 1 43  ? 28.470  20.381  31.869  1.00 72.20  ? 43  HIS A O     1 
ATOM   188  C  CB    . HIS A 1 43  ? 26.289  22.545  30.430  1.00 67.45  ? 43  HIS A CB    1 
ATOM   189  C  CG    . HIS A 1 43  ? 26.224  21.499  29.374  1.00 64.23  ? 43  HIS A CG    1 
ATOM   190  N  ND1   . HIS A 1 43  ? 27.358  20.929  28.838  1.00 62.12  ? 43  HIS A ND1   1 
ATOM   191  C  CD2   . HIS A 1 43  ? 25.181  20.765  28.920  1.00 63.28  ? 43  HIS A CD2   1 
ATOM   192  C  CE1   . HIS A 1 43  ? 27.017  19.882  28.110  1.00 62.83  ? 43  HIS A CE1   1 
ATOM   193  N  NE2   . HIS A 1 43  ? 25.701  19.758  28.146  1.00 62.79  ? 43  HIS A NE2   1 
ATOM   194  N  N     . GLU A 1 44  ? 29.024  22.570  31.711  1.00 70.05  ? 44  GLU A N     1 
ATOM   195  C  CA    . GLU A 1 44  ? 30.475  22.381  31.718  1.00 68.82  ? 44  GLU A CA    1 
ATOM   196  C  C     . GLU A 1 44  ? 31.008  23.034  30.468  1.00 66.28  ? 44  GLU A C     1 
ATOM   197  O  O     . GLU A 1 44  ? 31.992  23.766  30.521  1.00 65.76  ? 44  GLU A O     1 
ATOM   198  C  CB    . GLU A 1 44  ? 30.885  20.901  31.709  1.00 72.02  ? 44  GLU A CB    1 
ATOM   199  C  CG    . GLU A 1 44  ? 30.782  20.224  30.340  1.00 77.87  ? 44  GLU A CG    1 
ATOM   200  C  CD    . GLU A 1 44  ? 31.385  18.822  30.322  1.00 81.07  ? 44  GLU A CD    1 
ATOM   201  O  OE1   . GLU A 1 44  ? 30.837  17.932  31.016  1.00 82.78  ? 44  GLU A OE1   1 
ATOM   202  O  OE2   . GLU A 1 44  ? 32.405  18.613  29.617  1.00 82.42  ? 44  GLU A OE2   1 
ATOM   203  N  N     . ALA A 1 45  ? 30.340  22.766  29.345  1.00 63.07  ? 45  ALA A N     1 
ATOM   204  C  CA    . ALA A 1 45  ? 30.717  23.348  28.065  1.00 60.16  ? 45  ALA A CA    1 
ATOM   205  C  C     . ALA A 1 45  ? 30.815  24.856  28.240  1.00 58.80  ? 45  ALA A C     1 
ATOM   206  O  O     . ALA A 1 45  ? 31.704  25.502  27.693  1.00 57.88  ? 45  ALA A O     1 
ATOM   207  C  CB    . ALA A 1 45  ? 29.682  23.015  27.024  1.00 59.10  ? 45  ALA A CB    1 
ATOM   208  N  N     . MET A 1 46  ? 29.885  25.406  29.010  1.00 58.35  ? 46  MET A N     1 
ATOM   209  C  CA    . MET A 1 46  ? 29.864  26.830  29.292  1.00 58.64  ? 46  MET A CA    1 
ATOM   210  C  C     . MET A 1 46  ? 31.116  27.146  30.097  1.00 59.22  ? 46  MET A C     1 
ATOM   211  O  O     . MET A 1 46  ? 31.778  28.146  29.872  1.00 59.34  ? 46  MET A O     1 
ATOM   212  C  CB    . MET A 1 46  ? 28.639  27.194  30.124  1.00 58.18  ? 46  MET A CB    1 
ATOM   213  C  CG    . MET A 1 46  ? 27.348  26.558  29.679  1.00 59.00  ? 46  MET A CG    1 
ATOM   214  S  SD    . MET A 1 46  ? 26.877  27.045  28.030  1.00 61.09  ? 46  MET A SD    1 
ATOM   215  C  CE    . MET A 1 46  ? 26.741  28.740  28.223  1.00 61.66  ? 46  MET A CE    1 
ATOM   216  N  N     . LYS A 1 47  ? 31.438  26.278  31.043  1.00 61.24  ? 47  LYS A N     1 
ATOM   217  C  CA    . LYS A 1 47  ? 32.609  26.475  31.877  1.00 63.54  ? 47  LYS A CA    1 
ATOM   218  C  C     . LYS A 1 47  ? 33.837  26.523  30.971  1.00 63.74  ? 47  LYS A C     1 
ATOM   219  O  O     . LYS A 1 47  ? 34.662  27.429  31.073  1.00 63.78  ? 47  LYS A O     1 
ATOM   220  C  CB    . LYS A 1 47  ? 32.723  25.319  32.874  1.00 67.03  ? 47  LYS A CB    1 
ATOM   221  C  CG    . LYS A 1 47  ? 33.485  25.630  34.164  1.00 71.05  ? 47  LYS A CG    1 
ATOM   222  C  CD    . LYS A 1 47  ? 33.294  24.499  35.206  1.00 74.71  ? 47  LYS A CD    1 
ATOM   223  C  CE    . LYS A 1 47  ? 31.814  24.309  35.647  1.00 76.84  ? 47  LYS A CE    1 
ATOM   224  N  NZ    . LYS A 1 47  ? 31.262  25.421  36.504  1.00 77.29  ? 47  LYS A NZ    1 
ATOM   225  N  N     . GLU A 1 48  ? 33.948  25.547  30.077  1.00 62.80  ? 48  GLU A N     1 
ATOM   226  C  CA    . GLU A 1 48  ? 35.075  25.487  29.164  1.00 62.37  ? 48  GLU A CA    1 
ATOM   227  C  C     . GLU A 1 48  ? 35.133  26.746  28.342  1.00 61.52  ? 48  GLU A C     1 
ATOM   228  O  O     . GLU A 1 48  ? 36.043  27.555  28.486  1.00 61.39  ? 48  GLU A O     1 
ATOM   229  C  CB    . GLU A 1 48  ? 34.938  24.313  28.199  1.00 65.13  ? 48  GLU A CB    1 
ATOM   230  C  CG    . GLU A 1 48  ? 35.091  22.941  28.807  1.00 69.74  ? 48  GLU A CG    1 
ATOM   231  C  CD    . GLU A 1 48  ? 34.862  21.840  27.785  1.00 73.23  ? 48  GLU A CD    1 
ATOM   232  O  OE1   . GLU A 1 48  ? 35.568  21.835  26.745  1.00 74.53  ? 48  GLU A OE1   1 
ATOM   233  O  OE2   . GLU A 1 48  ? 33.977  20.983  28.024  1.00 74.75  ? 48  GLU A OE2   1 
ATOM   234  N  N     . LEU A 1 49  ? 34.145  26.891  27.464  1.00 60.79  ? 49  LEU A N     1 
ATOM   235  C  CA    . LEU A 1 49  ? 34.058  28.032  26.564  1.00 59.02  ? 49  LEU A CA    1 
ATOM   236  C  C     . LEU A 1 49  ? 34.344  29.355  27.266  1.00 58.88  ? 49  LEU A C     1 
ATOM   237  O  O     . LEU A 1 49  ? 34.962  30.253  26.693  1.00 58.47  ? 49  LEU A O     1 
ATOM   238  C  CB    . LEU A 1 49  ? 32.686  28.067  25.894  1.00 56.50  ? 49  LEU A CB    1 
ATOM   239  C  CG    . LEU A 1 49  ? 32.551  29.157  24.835  1.00 56.78  ? 49  LEU A CG    1 
ATOM   240  C  CD1   . LEU A 1 49  ? 33.699  29.072  23.853  1.00 56.85  ? 49  LEU A CD1   1 
ATOM   241  C  CD2   . LEU A 1 49  ? 31.234  29.005  24.119  1.00 56.81  ? 49  LEU A CD2   1 
ATOM   242  N  N     . ARG A 1 50  ? 33.909  29.467  28.512  1.00 58.27  ? 50  ARG A N     1 
ATOM   243  C  CA    . ARG A 1 50  ? 34.132  30.681  29.274  1.00 58.97  ? 50  ARG A CA    1 
ATOM   244  C  C     . ARG A 1 50  ? 35.612  30.830  29.616  1.00 59.30  ? 50  ARG A C     1 
ATOM   245  O  O     . ARG A 1 50  ? 36.079  31.931  29.877  1.00 60.01  ? 50  ARG A O     1 
ATOM   246  C  CB    . ARG A 1 50  ? 33.280  30.656  30.547  1.00 59.14  ? 50  ARG A CB    1 
ATOM   247  C  CG    . ARG A 1 50  ? 33.308  31.928  31.365  1.00 60.84  ? 50  ARG A CG    1 
ATOM   248  C  CD    . ARG A 1 50  ? 32.097  32.029  32.288  1.00 63.24  ? 50  ARG A CD    1 
ATOM   249  N  NE    . ARG A 1 50  ? 31.975  30.881  33.181  1.00 66.02  ? 50  ARG A NE    1 
ATOM   250  C  CZ    . ARG A 1 50  ? 30.967  30.008  33.156  1.00 68.32  ? 50  ARG A CZ    1 
ATOM   251  N  NH1   . ARG A 1 50  ? 29.971  30.142  32.283  1.00 67.66  ? 50  ARG A NH1   1 
ATOM   252  N  NH2   . ARG A 1 50  ? 30.961  28.981  33.998  1.00 68.08  ? 50  ARG A NH2   1 
ATOM   253  N  N     . GLU A 1 51  ? 36.342  29.717  29.598  1.00 60.69  ? 51  GLU A N     1 
ATOM   254  C  CA    . GLU A 1 51  ? 37.776  29.696  29.901  1.00 61.83  ? 51  GLU A CA    1 
ATOM   255  C  C     . GLU A 1 51  ? 38.592  30.044  28.669  1.00 60.82  ? 51  GLU A C     1 
ATOM   256  O  O     . GLU A 1 51  ? 39.583  30.784  28.741  1.00 61.19  ? 51  GLU A O     1 
ATOM   257  C  CB    . GLU A 1 51  ? 38.192  28.314  30.387  1.00 65.36  ? 51  GLU A CB    1 
ATOM   258  C  CG    . GLU A 1 51  ? 37.952  28.060  31.860  1.00 71.19  ? 51  GLU A CG    1 
ATOM   259  C  CD    . GLU A 1 51  ? 38.252  26.619  32.242  1.00 74.40  ? 51  GLU A CD    1 
ATOM   260  O  OE1   . GLU A 1 51  ? 39.193  26.028  31.653  1.00 75.16  ? 51  GLU A OE1   1 
ATOM   261  O  OE2   . GLU A 1 51  ? 37.552  26.085  33.136  1.00 76.03  ? 51  GLU A OE2   1 
ATOM   262  N  N     . VAL A 1 52  ? 38.178  29.474  27.543  1.00 58.60  ? 52  VAL A N     1 
ATOM   263  C  CA    . VAL A 1 52  ? 38.805  29.722  26.255  1.00 55.89  ? 52  VAL A CA    1 
ATOM   264  C  C     . VAL A 1 52  ? 38.735  31.228  25.982  1.00 56.44  ? 52  VAL A C     1 
ATOM   265  O  O     . VAL A 1 52  ? 39.743  31.873  25.713  1.00 57.06  ? 52  VAL A O     1 
ATOM   266  C  CB    . VAL A 1 52  ? 38.038  28.966  25.154  1.00 54.44  ? 52  VAL A CB    1 
ATOM   267  C  CG1   . VAL A 1 52  ? 38.369  29.516  23.788  1.00 53.55  ? 52  VAL A CG1   1 
ATOM   268  C  CG2   . VAL A 1 52  ? 38.355  27.500  25.240  1.00 52.52  ? 52  VAL A CG2   1 
ATOM   269  N  N     . THR A 1 53  ? 37.530  31.781  26.090  1.00 56.10  ? 53  THR A N     1 
ATOM   270  C  CA    . THR A 1 53  ? 37.287  33.193  25.837  1.00 55.56  ? 53  THR A CA    1 
ATOM   271  C  C     . THR A 1 53  ? 38.032  34.110  26.781  1.00 55.88  ? 53  THR A C     1 
ATOM   272  O  O     . THR A 1 53  ? 38.390  35.221  26.407  1.00 56.03  ? 53  THR A O     1 
ATOM   273  C  CB    . THR A 1 53  ? 35.764  33.510  25.906  1.00 55.36  ? 53  THR A CB    1 
ATOM   274  O  OG1   . THR A 1 53  ? 35.066  32.662  24.992  1.00 53.00  ? 53  THR A OG1   1 
ATOM   275  C  CG2   . THR A 1 53  ? 35.474  34.954  25.516  1.00 53.73  ? 53  THR A CG2   1 
ATOM   276  N  N     . ALA A 1 54  ? 38.289  33.653  27.999  1.00 57.04  ? 54  ALA A N     1 
ATOM   277  C  CA    . ALA A 1 54  ? 38.987  34.500  28.966  1.00 59.06  ? 54  ALA A CA    1 
ATOM   278  C  C     . ALA A 1 54  ? 40.384  34.934  28.541  1.00 60.34  ? 54  ALA A C     1 
ATOM   279  O  O     . ALA A 1 54  ? 40.885  35.944  29.022  1.00 59.80  ? 54  ALA A O     1 
ATOM   280  C  CB    . ALA A 1 54  ? 39.054  33.812  30.311  1.00 58.55  ? 54  ALA A CB    1 
ATOM   281  N  N     . LYS A 1 55  ? 41.008  34.175  27.643  1.00 63.09  ? 55  LYS A N     1 
ATOM   282  C  CA    . LYS A 1 55  ? 42.354  34.491  27.168  1.00 66.14  ? 55  LYS A CA    1 
ATOM   283  C  C     . LYS A 1 55  ? 42.353  35.460  25.974  1.00 67.04  ? 55  LYS A C     1 
ATOM   284  O  O     . LYS A 1 55  ? 43.393  36.026  25.605  1.00 67.11  ? 55  LYS A O     1 
ATOM   285  C  CB    . LYS A 1 55  ? 43.085  33.194  26.793  1.00 68.43  ? 55  LYS A CB    1 
ATOM   286  C  CG    . LYS A 1 55  ? 44.567  33.379  26.397  1.00 73.68  ? 55  LYS A CG    1 
ATOM   287  C  CD    . LYS A 1 55  ? 44.746  33.811  24.929  1.00 75.44  ? 55  LYS A CD    1 
ATOM   288  C  CE    . LYS A 1 55  ? 46.217  33.922  24.540  1.00 76.43  ? 55  LYS A CE    1 
ATOM   289  N  NZ    . LYS A 1 55  ? 46.406  33.946  23.053  1.00 77.20  ? 55  LYS A NZ    1 
ATOM   290  N  N     . HIS A 1 56  ? 41.174  35.653  25.391  1.00 67.71  ? 56  HIS A N     1 
ATOM   291  C  CA    . HIS A 1 56  ? 40.992  36.526  24.237  1.00 67.74  ? 56  HIS A CA    1 
ATOM   292  C  C     . HIS A 1 56  ? 40.913  37.989  24.674  1.00 68.06  ? 56  HIS A C     1 
ATOM   293  O  O     . HIS A 1 56  ? 40.281  38.316  25.681  1.00 68.07  ? 56  HIS A O     1 
ATOM   294  C  CB    . HIS A 1 56  ? 39.718  36.106  23.502  1.00 67.99  ? 56  HIS A CB    1 
ATOM   295  C  CG    . HIS A 1 56  ? 39.615  36.629  22.105  1.00 68.80  ? 56  HIS A CG    1 
ATOM   296  N  ND1   . HIS A 1 56  ? 39.262  37.931  21.818  1.00 68.46  ? 56  HIS A ND1   1 
ATOM   297  C  CD2   . HIS A 1 56  ? 39.788  36.013  20.911  1.00 68.22  ? 56  HIS A CD2   1 
ATOM   298  C  CE1   . HIS A 1 56  ? 39.217  38.093  20.508  1.00 68.91  ? 56  HIS A CE1   1 
ATOM   299  N  NE2   . HIS A 1 56  ? 39.531  36.945  19.934  1.00 68.42  ? 56  HIS A NE2   1 
ATOM   300  N  N     . PRO A 1 57  ? 41.550  38.891  23.910  1.00 68.58  ? 57  PRO A N     1 
ATOM   301  C  CA    . PRO A 1 57  ? 41.597  40.338  24.166  1.00 68.54  ? 57  PRO A CA    1 
ATOM   302  C  C     . PRO A 1 57  ? 40.260  41.025  24.445  1.00 68.59  ? 57  PRO A C     1 
ATOM   303  O  O     . PRO A 1 57  ? 40.121  41.731  25.441  1.00 69.18  ? 57  PRO A O     1 
ATOM   304  C  CB    . PRO A 1 57  ? 42.252  40.896  22.905  1.00 68.17  ? 57  PRO A CB    1 
ATOM   305  C  CG    . PRO A 1 57  ? 43.103  39.776  22.443  1.00 68.97  ? 57  PRO A CG    1 
ATOM   306  C  CD    . PRO A 1 57  ? 42.229  38.568  22.643  1.00 68.20  ? 57  PRO A CD    1 
ATOM   307  N  N     . TRP A 1 58  ? 39.284  40.831  23.561  1.00 68.58  ? 58  TRP A N     1 
ATOM   308  C  CA    . TRP A 1 58  ? 37.987  41.477  23.724  1.00 68.05  ? 58  TRP A CA    1 
ATOM   309  C  C     . TRP A 1 58  ? 37.001  40.685  24.551  1.00 66.28  ? 58  TRP A C     1 
ATOM   310  O  O     . TRP A 1 58  ? 35.792  40.827  24.389  1.00 65.04  ? 58  TRP A O     1 
ATOM   311  C  CB    . TRP A 1 58  ? 37.390  41.792  22.349  1.00 70.55  ? 58  TRP A CB    1 
ATOM   312  C  CG    . TRP A 1 58  ? 38.192  42.813  21.605  1.00 73.18  ? 58  TRP A CG    1 
ATOM   313  C  CD1   . TRP A 1 58  ? 38.383  44.129  21.951  1.00 74.21  ? 58  TRP A CD1   1 
ATOM   314  C  CD2   . TRP A 1 58  ? 38.993  42.585  20.448  1.00 74.40  ? 58  TRP A CD2   1 
ATOM   315  N  NE1   . TRP A 1 58  ? 39.264  44.728  21.081  1.00 74.91  ? 58  TRP A NE1   1 
ATOM   316  C  CE2   . TRP A 1 58  ? 39.656  43.803  20.149  1.00 75.49  ? 58  TRP A CE2   1 
ATOM   317  C  CE3   . TRP A 1 58  ? 39.219  41.469  19.633  1.00 75.65  ? 58  TRP A CE3   1 
ATOM   318  C  CZ2   . TRP A 1 58  ? 40.533  43.933  19.069  1.00 76.50  ? 58  TRP A CZ2   1 
ATOM   319  C  CZ3   . TRP A 1 58  ? 40.089  41.596  18.555  1.00 78.00  ? 58  TRP A CZ3   1 
ATOM   320  C  CH2   . TRP A 1 58  ? 40.737  42.823  18.283  1.00 78.15  ? 58  TRP A CH2   1 
ATOM   321  N  N     . ASN A 1 59  ? 37.520  39.871  25.461  1.00 64.96  ? 59  ASN A N     1 
ATOM   322  C  CA    . ASN A 1 59  ? 36.661  39.050  26.301  1.00 64.89  ? 59  ASN A CA    1 
ATOM   323  C  C     . ASN A 1 59  ? 35.582  39.844  27.056  1.00 63.57  ? 59  ASN A C     1 
ATOM   324  O  O     . ASN A 1 59  ? 34.625  39.262  27.571  1.00 63.86  ? 59  ASN A O     1 
ATOM   325  C  CB    . ASN A 1 59  ? 37.510  38.240  27.284  1.00 65.17  ? 59  ASN A CB    1 
ATOM   326  C  CG    . ASN A 1 59  ? 38.171  39.102  28.328  1.00 66.60  ? 59  ASN A CG    1 
ATOM   327  O  OD1   . ASN A 1 59  ? 37.513  39.603  29.240  1.00 67.20  ? 59  ASN A OD1   1 
ATOM   328  N  ND2   . ASN A 1 59  ? 39.481  39.288  28.201  1.00 67.08  ? 59  ASN A ND2   1 
ATOM   329  N  N     . ILE A 1 60  ? 35.715  41.165  27.107  1.00 60.99  ? 60  ILE A N     1 
ATOM   330  C  CA    . ILE A 1 60  ? 34.728  41.971  27.811  1.00 59.69  ? 60  ILE A CA    1 
ATOM   331  C  C     . ILE A 1 60  ? 33.334  41.870  27.201  1.00 59.29  ? 60  ILE A C     1 
ATOM   332  O  O     . ILE A 1 60  ? 32.334  42.176  27.859  1.00 59.74  ? 60  ILE A O     1 
ATOM   333  C  CB    . ILE A 1 60  ? 35.117  43.454  27.831  1.00 59.80  ? 60  ILE A CB    1 
ATOM   334  C  CG1   . ILE A 1 60  ? 34.091  44.241  28.644  1.00 60.55  ? 60  ILE A CG1   1 
ATOM   335  C  CG2   . ILE A 1 60  ? 35.176  44.002  26.412  1.00 58.79  ? 60  ILE A CG2   1 
ATOM   336  C  CD1   . ILE A 1 60  ? 34.346  45.723  28.660  1.00 61.05  ? 60  ILE A CD1   1 
ATOM   337  N  N     . MET A 1 61  ? 33.270  41.431  25.948  1.00 57.76  ? 61  MET A N     1 
ATOM   338  C  CA    . MET A 1 61  ? 32.001  41.327  25.242  1.00 55.35  ? 61  MET A CA    1 
ATOM   339  C  C     . MET A 1 61  ? 31.236  40.040  25.504  1.00 54.02  ? 61  MET A C     1 
ATOM   340  O  O     . MET A 1 61  ? 30.034  39.967  25.266  1.00 55.50  ? 61  MET A O     1 
ATOM   341  C  CB    . MET A 1 61  ? 32.238  41.475  23.744  1.00 54.74  ? 61  MET A CB    1 
ATOM   342  C  CG    . MET A 1 61  ? 32.959  42.752  23.366  1.00 55.55  ? 61  MET A CG    1 
ATOM   343  S  SD    . MET A 1 61  ? 33.113  43.004  21.579  1.00 58.21  ? 61  MET A SD    1 
ATOM   344  C  CE    . MET A 1 61  ? 33.462  41.276  21.001  1.00 57.38  ? 61  MET A CE    1 
ATOM   345  N  N     . THR A 1 62  ? 31.912  39.019  26.000  1.00 51.59  ? 62  THR A N     1 
ATOM   346  C  CA    . THR A 1 62  ? 31.216  37.767  26.245  1.00 51.36  ? 62  THR A CA    1 
ATOM   347  C  C     . THR A 1 62  ? 30.012  37.914  27.177  1.00 51.56  ? 62  THR A C     1 
ATOM   348  O  O     . THR A 1 62  ? 30.064  38.596  28.193  1.00 52.62  ? 62  THR A O     1 
ATOM   349  C  CB    . THR A 1 62  ? 32.157  36.715  26.842  1.00 50.85  ? 62  THR A CB    1 
ATOM   350  O  OG1   . THR A 1 62  ? 31.495  35.446  26.878  1.00 48.53  ? 62  THR A OG1   1 
ATOM   351  C  CG2   . THR A 1 62  ? 32.559  37.110  28.245  1.00 50.72  ? 62  THR A CG2   1 
ATOM   352  N  N     . THR A 1 63  ? 28.916  37.280  26.816  1.00 51.11  ? 63  THR A N     1 
ATOM   353  C  CA    . THR A 1 63  ? 27.733  37.315  27.646  1.00 52.89  ? 63  THR A CA    1 
ATOM   354  C  C     . THR A 1 63  ? 28.069  36.755  29.040  1.00 52.81  ? 63  THR A C     1 
ATOM   355  O  O     . THR A 1 63  ? 28.875  35.829  29.163  1.00 51.49  ? 63  THR A O     1 
ATOM   356  C  CB    . THR A 1 63  ? 26.615  36.481  26.974  1.00 54.57  ? 63  THR A CB    1 
ATOM   357  O  OG1   . THR A 1 63  ? 25.988  37.283  25.965  1.00 58.07  ? 63  THR A OG1   1 
ATOM   358  C  CG2   . THR A 1 63  ? 25.575  36.001  27.983  1.00 54.93  ? 63  THR A CG2   1 
ATOM   359  N  N     . SER A 1 64  ? 27.457  37.325  30.081  1.00 52.90  ? 64  SER A N     1 
ATOM   360  C  CA    . SER A 1 64  ? 27.683  36.875  31.458  1.00 53.51  ? 64  SER A CA    1 
ATOM   361  C  C     . SER A 1 64  ? 27.010  35.526  31.745  1.00 53.11  ? 64  SER A C     1 
ATOM   362  O  O     . SER A 1 64  ? 26.033  35.152  31.087  1.00 51.52  ? 64  SER A O     1 
ATOM   363  C  CB    . SER A 1 64  ? 27.163  37.917  32.450  1.00 55.22  ? 64  SER A CB    1 
ATOM   364  O  OG    . SER A 1 64  ? 25.761  38.100  32.305  1.00 59.32  ? 64  SER A OG    1 
ATOM   365  N  N     . ALA A 1 65  ? 27.538  34.809  32.736  1.00 52.46  ? 65  ALA A N     1 
ATOM   366  C  CA    . ALA A 1 65  ? 27.011  33.504  33.110  1.00 53.41  ? 65  ALA A CA    1 
ATOM   367  C  C     . ALA A 1 65  ? 25.544  33.546  33.564  1.00 54.20  ? 65  ALA A C     1 
ATOM   368  O  O     . ALA A 1 65  ? 24.770  32.628  33.263  1.00 54.00  ? 65  ALA A O     1 
ATOM   369  C  CB    . ALA A 1 65  ? 27.880  32.892  34.200  1.00 53.14  ? 65  ALA A CB    1 
ATOM   370  N  N     . ASP A 1 66  ? 25.156  34.598  34.283  1.00 53.60  ? 66  ASP A N     1 
ATOM   371  C  CA    . ASP A 1 66  ? 23.774  34.711  34.739  1.00 54.31  ? 66  ASP A CA    1 
ATOM   372  C  C     . ASP A 1 66  ? 22.817  35.011  33.585  1.00 53.97  ? 66  ASP A C     1 
ATOM   373  O  O     . ASP A 1 66  ? 21.651  34.618  33.611  1.00 53.04  ? 66  ASP A O     1 
ATOM   374  C  CB    . ASP A 1 66  ? 23.653  35.784  35.830  1.00 56.60  ? 66  ASP A CB    1 
ATOM   375  C  CG    . ASP A 1 66  ? 23.879  37.195  35.310  1.00 60.44  ? 66  ASP A CG    1 
ATOM   376  O  OD1   . ASP A 1 66  ? 24.896  37.422  34.613  1.00 61.91  ? 66  ASP A OD1   1 
ATOM   377  O  OD2   . ASP A 1 66  ? 23.041  38.082  35.617  1.00 62.04  ? 66  ASP A OD2   1 
ATOM   378  N  N     . GLU A 1 67  ? 23.310  35.708  32.567  1.00 55.28  ? 67  GLU A N     1 
ATOM   379  C  CA    . GLU A 1 67  ? 22.482  36.018  31.412  1.00 56.20  ? 67  GLU A CA    1 
ATOM   380  C  C     . GLU A 1 67  ? 22.370  34.798  30.494  1.00 55.00  ? 67  GLU A C     1 
ATOM   381  O  O     . GLU A 1 67  ? 21.395  34.644  29.762  1.00 53.99  ? 67  GLU A O     1 
ATOM   382  C  CB    . GLU A 1 67  ? 23.049  37.198  30.622  1.00 57.74  ? 67  GLU A CB    1 
ATOM   383  C  CG    . GLU A 1 67  ? 22.020  37.755  29.643  1.00 59.73  ? 67  GLU A CG    1 
ATOM   384  C  CD    . GLU A 1 67  ? 22.543  38.871  28.764  1.00 61.97  ? 67  GLU A CD    1 
ATOM   385  O  OE1   . GLU A 1 67  ? 23.379  39.692  29.223  1.00 61.83  ? 67  GLU A OE1   1 
ATOM   386  O  OE2   . GLU A 1 67  ? 22.083  38.928  27.603  1.00 63.69  ? 67  GLU A OE2   1 
ATOM   387  N  N     . GLY A 1 68  ? 23.381  33.942  30.517  1.00 54.03  ? 68  GLY A N     1 
ATOM   388  C  CA    . GLY A 1 68  ? 23.315  32.753  29.702  1.00 53.47  ? 68  GLY A CA    1 
ATOM   389  C  C     . GLY A 1 68  ? 22.235  31.909  30.333  1.00 54.36  ? 68  GLY A C     1 
ATOM   390  O  O     . GLY A 1 68  ? 21.438  31.278  29.644  1.00 55.19  ? 68  GLY A O     1 
ATOM   391  N  N     . GLN A 1 69  ? 22.209  31.917  31.666  1.00 55.52  ? 69  GLN A N     1 
ATOM   392  C  CA    . GLN A 1 69  ? 21.220  31.173  32.449  1.00 55.07  ? 69  GLN A CA    1 
ATOM   393  C  C     . GLN A 1 69  ? 19.796  31.672  32.171  1.00 54.43  ? 69  GLN A C     1 
ATOM   394  O  O     . GLN A 1 69  ? 18.870  30.877  31.991  1.00 53.91  ? 69  GLN A O     1 
ATOM   395  C  CB    . GLN A 1 69  ? 21.520  31.307  33.937  1.00 55.73  ? 69  GLN A CB    1 
ATOM   396  C  CG    . GLN A 1 69  ? 21.564  29.974  34.653  1.00 59.68  ? 69  GLN A CG    1 
ATOM   397  C  CD    . GLN A 1 69  ? 20.720  29.968  35.906  1.00 60.67  ? 69  GLN A CD    1 
ATOM   398  O  OE1   . GLN A 1 69  ? 20.719  30.931  36.666  1.00 62.52  ? 69  GLN A OE1   1 
ATOM   399  N  NE2   . GLN A 1 69  ? 20.006  28.875  36.135  1.00 61.73  ? 69  GLN A NE2   1 
ATOM   400  N  N     . PHE A 1 70  ? 19.618  32.988  32.144  1.00 53.51  ? 70  PHE A N     1 
ATOM   401  C  CA    . PHE A 1 70  ? 18.312  33.537  31.853  1.00 54.14  ? 70  PHE A CA    1 
ATOM   402  C  C     . PHE A 1 70  ? 17.851  33.135  30.447  1.00 54.97  ? 70  PHE A C     1 
ATOM   403  O  O     . PHE A 1 70  ? 16.689  32.779  30.252  1.00 56.95  ? 70  PHE A O     1 
ATOM   404  C  CB    . PHE A 1 70  ? 18.318  35.055  31.976  1.00 55.43  ? 70  PHE A CB    1 
ATOM   405  C  CG    . PHE A 1 70  ? 16.994  35.674  31.656  1.00 56.14  ? 70  PHE A CG    1 
ATOM   406  C  CD1   . PHE A 1 70  ? 15.853  35.287  32.350  1.00 55.05  ? 70  PHE A CD1   1 
ATOM   407  C  CD2   . PHE A 1 70  ? 16.871  36.591  30.621  1.00 55.43  ? 70  PHE A CD2   1 
ATOM   408  C  CE1   . PHE A 1 70  ? 14.612  35.800  32.011  1.00 55.77  ? 70  PHE A CE1   1 
ATOM   409  C  CE2   . PHE A 1 70  ? 15.628  37.110  30.275  1.00 54.92  ? 70  PHE A CE2   1 
ATOM   410  C  CZ    . PHE A 1 70  ? 14.502  36.716  30.966  1.00 55.48  ? 70  PHE A CZ    1 
ATOM   411  N  N     . LEU A 1 71  ? 18.747  33.193  29.464  1.00 54.48  ? 71  LEU A N     1 
ATOM   412  C  CA    . LEU A 1 71  ? 18.392  32.803  28.106  1.00 52.42  ? 71  LEU A CA    1 
ATOM   413  C  C     . LEU A 1 71  ? 17.962  31.340  28.082  1.00 52.66  ? 71  LEU A C     1 
ATOM   414  O  O     . LEU A 1 71  ? 16.954  30.981  27.458  1.00 51.47  ? 71  LEU A O     1 
ATOM   415  C  CB    . LEU A 1 71  ? 19.575  33.001  27.159  1.00 52.37  ? 71  LEU A CB    1 
ATOM   416  C  CG    . LEU A 1 71  ? 20.028  34.436  26.882  1.00 53.37  ? 71  LEU A CG    1 
ATOM   417  C  CD1   . LEU A 1 71  ? 21.097  34.416  25.794  1.00 54.13  ? 71  LEU A CD1   1 
ATOM   418  C  CD2   . LEU A 1 71  ? 18.850  35.288  26.441  1.00 52.33  ? 71  LEU A CD2   1 
ATOM   419  N  N     . SER A 1 72  ? 18.723  30.488  28.761  1.00 52.77  ? 72  SER A N     1 
ATOM   420  C  CA    . SER A 1 72  ? 18.371  29.072  28.799  1.00 54.83  ? 72  SER A CA    1 
ATOM   421  C  C     . SER A 1 72  ? 16.948  28.890  29.319  1.00 55.17  ? 72  SER A C     1 
ATOM   422  O  O     . SER A 1 72  ? 16.151  28.147  28.739  1.00 55.74  ? 72  SER A O     1 
ATOM   423  C  CB    . SER A 1 72  ? 19.348  28.295  29.678  1.00 54.81  ? 72  SER A CB    1 
ATOM   424  O  OG    . SER A 1 72  ? 20.599  28.153  29.031  1.00 56.37  ? 72  SER A OG    1 
ATOM   425  N  N     . MET A 1 73  ? 16.642  29.574  30.416  1.00 54.59  ? 73  MET A N     1 
ATOM   426  C  CA    . MET A 1 73  ? 15.322  29.509  31.018  1.00 54.35  ? 73  MET A CA    1 
ATOM   427  C  C     . MET A 1 73  ? 14.282  29.970  30.004  1.00 53.58  ? 73  MET A C     1 
ATOM   428  O  O     . MET A 1 73  ? 13.353  29.238  29.654  1.00 52.75  ? 73  MET A O     1 
ATOM   429  C  CB    . MET A 1 73  ? 15.273  30.413  32.252  1.00 56.29  ? 73  MET A CB    1 
ATOM   430  C  CG    . MET A 1 73  ? 13.946  30.408  32.996  1.00 59.42  ? 73  MET A CG    1 
ATOM   431  S  SD    . MET A 1 73  ? 13.564  28.774  33.686  1.00 64.83  ? 73  MET A SD    1 
ATOM   432  C  CE    . MET A 1 73  ? 14.587  28.799  35.164  1.00 62.85  ? 73  MET A CE    1 
ATOM   433  N  N     . LEU A 1 74  ? 14.460  31.197  29.532  1.00 52.17  ? 74  LEU A N     1 
ATOM   434  C  CA    . LEU A 1 74  ? 13.552  31.806  28.584  1.00 51.13  ? 74  LEU A CA    1 
ATOM   435  C  C     . LEU A 1 74  ? 13.304  30.909  27.367  1.00 51.19  ? 74  LEU A C     1 
ATOM   436  O  O     . LEU A 1 74  ? 12.151  30.716  26.959  1.00 50.11  ? 74  LEU A O     1 
ATOM   437  C  CB    . LEU A 1 74  ? 14.121  33.163  28.165  1.00 51.86  ? 74  LEU A CB    1 
ATOM   438  C  CG    . LEU A 1 74  ? 13.327  34.096  27.249  1.00 53.92  ? 74  LEU A CG    1 
ATOM   439  C  CD1   . LEU A 1 74  ? 12.048  34.553  27.924  1.00 56.04  ? 74  LEU A CD1   1 
ATOM   440  C  CD2   . LEU A 1 74  ? 14.188  35.305  26.921  1.00 56.19  ? 74  LEU A CD2   1 
ATOM   441  N  N     . LEU A 1 75  ? 14.377  30.352  26.803  1.00 49.51  ? 75  LEU A N     1 
ATOM   442  C  CA    . LEU A 1 75  ? 14.251  29.498  25.625  1.00 49.41  ? 75  LEU A CA    1 
ATOM   443  C  C     . LEU A 1 75  ? 13.414  28.260  25.922  1.00 50.35  ? 75  LEU A C     1 
ATOM   444  O  O     . LEU A 1 75  ? 12.573  27.856  25.117  1.00 49.74  ? 75  LEU A O     1 
ATOM   445  C  CB    . LEU A 1 75  ? 15.641  29.115  25.085  1.00 47.30  ? 75  LEU A CB    1 
ATOM   446  C  CG    . LEU A 1 75  ? 16.385  30.212  24.296  1.00 46.66  ? 75  LEU A CG    1 
ATOM   447  C  CD1   . LEU A 1 75  ? 17.850  29.836  24.091  1.00 44.08  ? 75  LEU A CD1   1 
ATOM   448  C  CD2   . LEU A 1 75  ? 15.693  30.446  22.960  1.00 42.15  ? 75  LEU A CD2   1 
ATOM   449  N  N     . LYS A 1 76  ? 13.640  27.661  27.086  1.00 52.19  ? 76  LYS A N     1 
ATOM   450  C  CA    . LYS A 1 76  ? 12.879  26.488  27.513  1.00 52.89  ? 76  LYS A CA    1 
ATOM   451  C  C     . LYS A 1 76  ? 11.396  26.826  27.708  1.00 52.94  ? 76  LYS A C     1 
ATOM   452  O  O     . LYS A 1 76  ? 10.529  26.122  27.203  1.00 53.53  ? 76  LYS A O     1 
ATOM   453  C  CB    . LYS A 1 76  ? 13.449  25.957  28.819  1.00 54.60  ? 76  LYS A CB    1 
ATOM   454  C  CG    . LYS A 1 76  ? 14.838  25.396  28.693  1.00 56.67  ? 76  LYS A CG    1 
ATOM   455  C  CD    . LYS A 1 76  ? 14.793  23.952  28.230  1.00 58.05  ? 76  LYS A CD    1 
ATOM   456  C  CE    . LYS A 1 76  ? 16.203  23.437  28.041  1.00 59.95  ? 76  LYS A CE    1 
ATOM   457  N  NZ    . LYS A 1 76  ? 17.072  23.879  29.176  1.00 60.66  ? 76  LYS A NZ    1 
ATOM   458  N  N     . LEU A 1 77  ? 11.107  27.904  28.434  1.00 52.91  ? 77  LEU A N     1 
ATOM   459  C  CA    . LEU A 1 77  ? 9.723   28.310  28.681  1.00 53.49  ? 77  LEU A CA    1 
ATOM   460  C  C     . LEU A 1 77  ? 8.909   28.636  27.422  1.00 54.64  ? 77  LEU A C     1 
ATOM   461  O  O     . LEU A 1 77  ? 7.694   28.486  27.422  1.00 55.23  ? 77  LEU A O     1 
ATOM   462  C  CB    . LEU A 1 77  ? 9.677   29.523  29.606  1.00 51.55  ? 77  LEU A CB    1 
ATOM   463  C  CG    . LEU A 1 77  ? 10.384  29.394  30.949  1.00 51.80  ? 77  LEU A CG    1 
ATOM   464  C  CD1   . LEU A 1 77  ? 10.430  30.743  31.622  1.00 49.29  ? 77  LEU A CD1   1 
ATOM   465  C  CD2   . LEU A 1 77  ? 9.668   28.382  31.819  1.00 52.69  ? 77  LEU A CD2   1 
ATOM   466  N  N     . ILE A 1 78  ? 9.547   29.087  26.348  1.00 54.80  ? 78  ILE A N     1 
ATOM   467  C  CA    . ILE A 1 78  ? 8.763   29.408  25.160  1.00 55.03  ? 78  ILE A CA    1 
ATOM   468  C  C     . ILE A 1 78  ? 8.860   28.322  24.108  1.00 55.21  ? 78  ILE A C     1 
ATOM   469  O  O     . ILE A 1 78  ? 8.355   28.465  22.995  1.00 55.53  ? 78  ILE A O     1 
ATOM   470  C  CB    . ILE A 1 78  ? 9.165   30.791  24.547  1.00 54.53  ? 78  ILE A CB    1 
ATOM   471  C  CG1   . ILE A 1 78  ? 10.584  30.741  23.975  1.00 54.45  ? 78  ILE A CG1   1 
ATOM   472  C  CG2   . ILE A 1 78  ? 9.070   31.871  25.613  1.00 54.23  ? 78  ILE A CG2   1 
ATOM   473  C  CD1   . ILE A 1 78  ? 11.044  32.036  23.346  1.00 53.29  ? 78  ILE A CD1   1 
ATOM   474  N  N     . ASN A 1 79  ? 9.504   27.225  24.473  1.00 56.43  ? 79  ASN A N     1 
ATOM   475  C  CA    . ASN A 1 79  ? 9.653   26.101  23.563  1.00 58.41  ? 79  ASN A CA    1 
ATOM   476  C  C     . ASN A 1 79  ? 10.204  26.492  22.204  1.00 58.12  ? 79  ASN A C     1 
ATOM   477  O  O     . ASN A 1 79  ? 9.808   25.933  21.180  1.00 58.01  ? 79  ASN A O     1 
ATOM   478  C  CB    . ASN A 1 79  ? 8.312   25.395  23.395  1.00 61.77  ? 79  ASN A CB    1 
ATOM   479  C  CG    . ASN A 1 79  ? 8.276   24.049  24.096  1.00 67.07  ? 79  ASN A CG    1 
ATOM   480  O  OD1   . ASN A 1 79  ? 8.651   23.015  23.514  1.00 68.22  ? 79  ASN A OD1   1 
ATOM   481  N  ND2   . ASN A 1 79  ? 7.844   24.054  25.364  1.00 68.25  ? 79  ASN A ND2   1 
ATOM   482  N  N     . ALA A 1 80  ? 11.142  27.436  22.207  1.00 58.16  ? 80  ALA A N     1 
ATOM   483  C  CA    . ALA A 1 80  ? 11.766  27.914  20.981  1.00 56.90  ? 80  ALA A CA    1 
ATOM   484  C  C     . ALA A 1 80  ? 12.513  26.790  20.293  1.00 55.43  ? 80  ALA A C     1 
ATOM   485  O  O     . ALA A 1 80  ? 13.263  26.045  20.924  1.00 55.37  ? 80  ALA A O     1 
ATOM   486  C  CB    . ALA A 1 80  ? 12.713  29.056  21.290  1.00 57.70  ? 80  ALA A CB    1 
ATOM   487  N  N     . LYS A 1 81  ? 12.291  26.674  18.993  1.00 54.38  ? 81  LYS A N     1 
ATOM   488  C  CA    . LYS A 1 81  ? 12.928  25.643  18.191  1.00 53.54  ? 81  LYS A CA    1 
ATOM   489  C  C     . LYS A 1 81  ? 13.792  26.283  17.112  1.00 52.29  ? 81  LYS A C     1 
ATOM   490  O  O     . LYS A 1 81  ? 14.935  25.878  16.895  1.00 51.39  ? 81  LYS A O     1 
ATOM   491  C  CB    . LYS A 1 81  ? 11.870  24.755  17.530  1.00 54.65  ? 81  LYS A CB    1 
ATOM   492  C  CG    . LYS A 1 81  ? 11.898  23.304  17.983  1.00 59.18  ? 81  LYS A CG    1 
ATOM   493  C  CD    . LYS A 1 81  ? 10.956  22.425  17.153  1.00 62.32  ? 81  LYS A CD    1 
ATOM   494  C  CE    . LYS A 1 81  ? 11.418  22.295  15.696  1.00 64.94  ? 81  LYS A CE    1 
ATOM   495  N  NZ    . LYS A 1 81  ? 10.400  21.634  14.795  1.00 66.14  ? 81  LYS A NZ    1 
ATOM   496  N  N     . ASN A 1 82  ? 13.242  27.298  16.454  1.00 50.56  ? 82  ASN A N     1 
ATOM   497  C  CA    . ASN A 1 82  ? 13.932  27.980  15.375  1.00 48.81  ? 82  ASN A CA    1 
ATOM   498  C  C     . ASN A 1 82  ? 14.357  29.377  15.790  1.00 48.21  ? 82  ASN A C     1 
ATOM   499  O  O     . ASN A 1 82  ? 13.516  30.245  15.983  1.00 49.75  ? 82  ASN A O     1 
ATOM   500  C  CB    . ASN A 1 82  ? 12.995  28.037  14.180  1.00 50.11  ? 82  ASN A CB    1 
ATOM   501  C  CG    . ASN A 1 82  ? 13.691  28.455  12.924  1.00 52.40  ? 82  ASN A CG    1 
ATOM   502  O  OD1   . ASN A 1 82  ? 14.777  27.956  12.606  1.00 53.56  ? 82  ASN A OD1   1 
ATOM   503  N  ND2   . ASN A 1 82  ? 13.069  29.372  12.181  1.00 53.72  ? 82  ASN A ND2   1 
ATOM   504  N  N     . THR A 1 83  ? 15.660  29.611  15.905  1.00 47.31  ? 83  THR A N     1 
ATOM   505  C  CA    . THR A 1 83  ? 16.142  30.921  16.340  1.00 45.78  ? 83  THR A CA    1 
ATOM   506  C  C     . THR A 1 83  ? 17.224  31.575  15.479  1.00 45.84  ? 83  THR A C     1 
ATOM   507  O  O     . THR A 1 83  ? 17.758  30.976  14.546  1.00 45.79  ? 83  THR A O     1 
ATOM   508  C  CB    . THR A 1 83  ? 16.686  30.844  17.772  1.00 45.70  ? 83  THR A CB    1 
ATOM   509  O  OG1   . THR A 1 83  ? 18.055  30.431  17.743  1.00 45.47  ? 83  THR A OG1   1 
ATOM   510  C  CG2   . THR A 1 83  ? 15.899  29.828  18.580  1.00 45.83  ? 83  THR A CG2   1 
ATOM   511  N  N     . MET A 1 84  ? 17.541  32.821  15.828  1.00 46.60  ? 84  MET A N     1 
ATOM   512  C  CA    . MET A 1 84  ? 18.542  33.624  15.131  1.00 46.02  ? 84  MET A CA    1 
ATOM   513  C  C     . MET A 1 84  ? 19.338  34.396  16.171  1.00 47.08  ? 84  MET A C     1 
ATOM   514  O  O     . MET A 1 84  ? 18.758  34.888  17.146  1.00 45.66  ? 84  MET A O     1 
ATOM   515  C  CB    . MET A 1 84  ? 17.861  34.642  14.212  1.00 44.00  ? 84  MET A CB    1 
ATOM   516  C  CG    . MET A 1 84  ? 18.816  35.422  13.334  1.00 42.73  ? 84  MET A CG    1 
ATOM   517  S  SD    . MET A 1 84  ? 18.051  36.865  12.556  1.00 43.99  ? 84  MET A SD    1 
ATOM   518  C  CE    . MET A 1 84  ? 16.836  36.117  11.474  1.00 41.46  ? 84  MET A CE    1 
ATOM   519  N  N     . GLU A 1 85  ? 20.652  34.497  15.955  1.00 47.80  ? 85  GLU A N     1 
ATOM   520  C  CA    . GLU A 1 85  ? 21.543  35.245  16.835  1.00 49.55  ? 85  GLU A CA    1 
ATOM   521  C  C     . GLU A 1 85  ? 22.414  36.214  16.029  1.00 48.88  ? 85  GLU A C     1 
ATOM   522  O  O     . GLU A 1 85  ? 23.078  35.808  15.078  1.00 49.59  ? 85  GLU A O     1 
ATOM   523  C  CB    . GLU A 1 85  ? 22.448  34.305  17.633  1.00 53.25  ? 85  GLU A CB    1 
ATOM   524  C  CG    . GLU A 1 85  ? 23.425  35.069  18.561  1.00 63.97  ? 85  GLU A CG    1 
ATOM   525  C  CD    . GLU A 1 85  ? 23.832  34.291  19.839  1.00 69.65  ? 85  GLU A CD    1 
ATOM   526  O  OE1   . GLU A 1 85  ? 22.928  33.734  20.529  1.00 69.94  ? 85  GLU A OE1   1 
ATOM   527  O  OE2   . GLU A 1 85  ? 25.054  34.260  20.155  1.00 70.83  ? 85  GLU A OE2   1 
ATOM   528  N  N     . ILE A 1 86  ? 22.403  37.494  16.395  1.00 47.00  ? 86  ILE A N     1 
ATOM   529  C  CA    . ILE A 1 86  ? 23.224  38.487  15.706  1.00 45.27  ? 86  ILE A CA    1 
ATOM   530  C  C     . ILE A 1 86  ? 24.294  38.961  16.683  1.00 45.46  ? 86  ILE A C     1 
ATOM   531  O  O     . ILE A 1 86  ? 23.993  39.622  17.681  1.00 45.22  ? 86  ILE A O     1 
ATOM   532  C  CB    . ILE A 1 86  ? 22.405  39.706  15.232  1.00 43.34  ? 86  ILE A CB    1 
ATOM   533  C  CG1   . ILE A 1 86  ? 21.275  39.256  14.314  1.00 42.12  ? 86  ILE A CG1   1 
ATOM   534  C  CG2   . ILE A 1 86  ? 23.302  40.659  14.459  1.00 41.55  ? 86  ILE A CG2   1 
ATOM   535  C  CD1   . ILE A 1 86  ? 20.416  40.395  13.821  1.00 41.27  ? 86  ILE A CD1   1 
ATOM   536  N  N     . GLY A 1 87  ? 25.544  38.636  16.364  1.00 45.02  ? 87  GLY A N     1 
ATOM   537  C  CA    . GLY A 1 87  ? 26.658  38.965  17.231  1.00 44.94  ? 87  GLY A CA    1 
ATOM   538  C  C     . GLY A 1 87  ? 26.958  37.653  17.943  1.00 47.10  ? 87  GLY A C     1 
ATOM   539  O  O     . GLY A 1 87  ? 26.313  37.320  18.943  1.00 47.17  ? 87  GLY A O     1 
ATOM   540  N  N     . VAL A 1 88  ? 27.917  36.889  17.422  1.00 46.90  ? 88  VAL A N     1 
ATOM   541  C  CA    . VAL A 1 88  ? 28.242  35.579  17.984  1.00 46.02  ? 88  VAL A CA    1 
ATOM   542  C  C     . VAL A 1 88  ? 29.453  35.548  18.884  1.00 47.48  ? 88  VAL A C     1 
ATOM   543  O  O     . VAL A 1 88  ? 29.403  34.960  19.961  1.00 47.77  ? 88  VAL A O     1 
ATOM   544  C  CB    . VAL A 1 88  ? 28.486  34.545  16.890  1.00 43.55  ? 88  VAL A CB    1 
ATOM   545  C  CG1   . VAL A 1 88  ? 28.781  33.212  17.521  1.00 42.68  ? 88  VAL A CG1   1 
ATOM   546  C  CG2   . VAL A 1 88  ? 27.290  34.463  15.968  1.00 43.63  ? 88  VAL A CG2   1 
ATOM   547  N  N     . TYR A 1 89  ? 30.544  36.136  18.401  1.00 50.28  ? 89  TYR A N     1 
ATOM   548  C  CA    . TYR A 1 89  ? 31.806  36.224  19.122  1.00 51.29  ? 89  TYR A CA    1 
ATOM   549  C  C     . TYR A 1 89  ? 32.095  35.036  20.002  1.00 53.45  ? 89  TYR A C     1 
ATOM   550  O  O     . TYR A 1 89  ? 31.375  34.806  20.979  1.00 59.17  ? 89  TYR A O     1 
ATOM   551  C  CB    . TYR A 1 89  ? 31.805  37.470  20.020  1.00 49.46  ? 89  TYR A CB    1 
ATOM   552  C  CG    . TYR A 1 89  ? 33.021  37.600  20.914  1.00 47.14  ? 89  TYR A CG    1 
ATOM   553  C  CD1   . TYR A 1 89  ? 34.277  37.844  20.374  1.00 50.91  ? 89  TYR A CD1   1 
ATOM   554  C  CD2   . TYR A 1 89  ? 32.919  37.494  22.290  1.00 46.69  ? 89  TYR A CD2   1 
ATOM   555  C  CE1   . TYR A 1 89  ? 35.412  37.986  21.183  1.00 50.44  ? 89  TYR A CE1   1 
ATOM   556  C  CE2   . TYR A 1 89  ? 34.043  37.633  23.115  1.00 47.70  ? 89  TYR A CE2   1 
ATOM   557  C  CZ    . TYR A 1 89  ? 35.287  37.882  22.547  1.00 49.93  ? 89  TYR A CZ    1 
ATOM   558  O  OH    . TYR A 1 89  ? 36.413  38.045  23.321  1.00 48.62  ? 89  TYR A OH    1 
ATOM   559  N  N     . THR A 1 90  ? 33.124  34.265  19.695  1.00 52.30  ? 90  THR A N     1 
ATOM   560  C  CA    . THR A 1 90  ? 33.467  33.163  20.599  1.00 50.49  ? 90  THR A CA    1 
ATOM   561  C  C     . THR A 1 90  ? 32.411  32.077  20.827  1.00 49.50  ? 90  THR A C     1 
ATOM   562  O  O     . THR A 1 90  ? 32.758  30.904  20.929  1.00 50.48  ? 90  THR A O     1 
ATOM   563  C  CB    . THR A 1 90  ? 33.892  33.739  21.940  1.00 49.30  ? 90  THR A CB    1 
ATOM   564  O  OG1   . THR A 1 90  ? 35.315  33.862  21.963  1.00 49.10  ? 90  THR A OG1   1 
ATOM   565  C  CG2   . THR A 1 90  ? 33.403  32.885  23.063  1.00 50.14  ? 90  THR A CG2   1 
ATOM   566  N  N     . GLY A 1 91  ? 31.147  32.461  20.974  1.00 48.61  ? 91  GLY A N     1 
ATOM   567  C  CA    . GLY A 1 91  ? 30.100  31.462  21.094  1.00 47.92  ? 91  GLY A CA    1 
ATOM   568  C  C     . GLY A 1 91  ? 29.280  31.241  22.343  1.00 47.37  ? 91  GLY A C     1 
ATOM   569  O  O     . GLY A 1 91  ? 28.442  30.341  22.346  1.00 47.30  ? 91  GLY A O     1 
ATOM   570  N  N     . TYR A 1 92  ? 29.474  32.041  23.383  1.00 46.94  ? 92  TYR A N     1 
ATOM   571  C  CA    . TYR A 1 92  ? 28.726  31.829  24.615  1.00 47.44  ? 92  TYR A CA    1 
ATOM   572  C  C     . TYR A 1 92  ? 27.185  31.823  24.538  1.00 46.99  ? 92  TYR A C     1 
ATOM   573  O  O     . TYR A 1 92  ? 26.551  30.887  25.027  1.00 46.16  ? 92  TYR A O     1 
ATOM   574  C  CB    . TYR A 1 92  ? 29.196  32.811  25.677  1.00 49.14  ? 92  TYR A CB    1 
ATOM   575  C  CG    . TYR A 1 92  ? 28.839  32.350  27.062  1.00 53.15  ? 92  TYR A CG    1 
ATOM   576  C  CD1   . TYR A 1 92  ? 27.561  32.555  27.575  1.00 54.35  ? 92  TYR A CD1   1 
ATOM   577  C  CD2   . TYR A 1 92  ? 29.764  31.667  27.853  1.00 53.10  ? 92  TYR A CD2   1 
ATOM   578  C  CE1   . TYR A 1 92  ? 27.212  32.094  28.842  1.00 55.15  ? 92  TYR A CE1   1 
ATOM   579  C  CE2   . TYR A 1 92  ? 29.421  31.205  29.120  1.00 53.36  ? 92  TYR A CE2   1 
ATOM   580  C  CZ    . TYR A 1 92  ? 28.144  31.422  29.609  1.00 53.84  ? 92  TYR A CZ    1 
ATOM   581  O  OH    . TYR A 1 92  ? 27.783  30.981  30.865  1.00 55.36  ? 92  TYR A OH    1 
ATOM   582  N  N     . SER A 1 93  ? 26.580  32.853  23.952  1.00 47.46  ? 93  SER A N     1 
ATOM   583  C  CA    . SER A 1 93  ? 25.117  32.909  23.817  1.00 47.47  ? 93  SER A CA    1 
ATOM   584  C  C     . SER A 1 93  ? 24.650  31.719  22.977  1.00 47.40  ? 93  SER A C     1 
ATOM   585  O  O     . SER A 1 93  ? 23.641  31.068  23.277  1.00 45.67  ? 93  SER A O     1 
ATOM   586  C  CB    . SER A 1 93  ? 24.679  34.177  23.080  1.00 47.57  ? 93  SER A CB    1 
ATOM   587  O  OG    . SER A 1 93  ? 25.336  35.319  23.572  1.00 53.68  ? 93  SER A OG    1 
ATOM   588  N  N     . LEU A 1 94  ? 25.393  31.478  21.899  1.00 47.26  ? 94  LEU A N     1 
ATOM   589  C  CA    . LEU A 1 94  ? 25.109  30.410  20.960  1.00 46.62  ? 94  LEU A CA    1 
ATOM   590  C  C     . LEU A 1 94  ? 25.081  29.070  21.650  1.00 46.93  ? 94  LEU A C     1 
ATOM   591  O  O     . LEU A 1 94  ? 24.099  28.334  21.554  1.00 48.25  ? 94  LEU A O     1 
ATOM   592  C  CB    . LEU A 1 94  ? 26.175  30.374  19.877  1.00 47.65  ? 94  LEU A CB    1 
ATOM   593  C  CG    . LEU A 1 94  ? 25.665  30.475  18.445  1.00 48.17  ? 94  LEU A CG    1 
ATOM   594  C  CD1   . LEU A 1 94  ? 26.720  29.922  17.509  1.00 47.04  ? 94  LEU A CD1   1 
ATOM   595  C  CD2   . LEU A 1 94  ? 24.356  29.717  18.308  1.00 47.63  ? 94  LEU A CD2   1 
ATOM   596  N  N     . LEU A 1 95  ? 26.176  28.754  22.335  1.00 45.55  ? 95  LEU A N     1 
ATOM   597  C  CA    . LEU A 1 95  ? 26.299  27.497  23.054  1.00 44.00  ? 95  LEU A CA    1 
ATOM   598  C  C     . LEU A 1 95  ? 25.102  27.332  23.971  1.00 44.81  ? 95  LEU A C     1 
ATOM   599  O  O     . LEU A 1 95  ? 24.441  26.294  23.963  1.00 45.92  ? 95  LEU A O     1 
ATOM   600  C  CB    . LEU A 1 95  ? 27.569  27.489  23.897  1.00 41.21  ? 95  LEU A CB    1 
ATOM   601  C  CG    . LEU A 1 95  ? 28.236  26.148  24.207  1.00 37.80  ? 95  LEU A CG    1 
ATOM   602  C  CD1   . LEU A 1 95  ? 28.793  26.252  25.595  1.00 35.94  ? 95  LEU A CD1   1 
ATOM   603  C  CD2   . LEU A 1 95  ? 27.280  24.987  24.094  1.00 35.58  ? 95  LEU A CD2   1 
ATOM   604  N  N     . ALA A 1 96  ? 24.825  28.362  24.764  1.00 44.58  ? 96  ALA A N     1 
ATOM   605  C  CA    . ALA A 1 96  ? 23.702  28.311  25.684  1.00 45.17  ? 96  ALA A CA    1 
ATOM   606  C  C     . ALA A 1 96  ? 22.404  28.014  24.940  1.00 45.99  ? 96  ALA A C     1 
ATOM   607  O  O     . ALA A 1 96  ? 21.620  27.167  25.366  1.00 48.41  ? 96  ALA A O     1 
ATOM   608  C  CB    . ALA A 1 96  ? 23.578  29.630  26.453  1.00 44.23  ? 96  ALA A CB    1 
ATOM   609  N  N     . THR A 1 97  ? 22.181  28.700  23.825  1.00 45.10  ? 97  THR A N     1 
ATOM   610  C  CA    . THR A 1 97  ? 20.966  28.500  23.061  1.00 43.93  ? 97  THR A CA    1 
ATOM   611  C  C     . THR A 1 97  ? 20.878  27.091  22.488  1.00 45.37  ? 97  THR A C     1 
ATOM   612  O  O     . THR A 1 97  ? 19.838  26.434  22.590  1.00 45.93  ? 97  THR A O     1 
ATOM   613  C  CB    . THR A 1 97  ? 20.888  29.493  21.912  1.00 42.43  ? 97  THR A CB    1 
ATOM   614  O  OG1   . THR A 1 97  ? 21.091  30.810  22.423  1.00 43.13  ? 97  THR A OG1   1 
ATOM   615  C  CG2   . THR A 1 97  ? 19.534  29.418  21.225  1.00 40.20  ? 97  THR A CG2   1 
ATOM   616  N  N     . ALA A 1 98  ? 21.966  26.626  21.882  1.00 45.41  ? 98  ALA A N     1 
ATOM   617  C  CA    . ALA A 1 98  ? 21.977  25.304  21.270  1.00 45.12  ? 98  ALA A CA    1 
ATOM   618  C  C     . ALA A 1 98  ? 21.743  24.190  22.291  1.00 46.06  ? 98  ALA A C     1 
ATOM   619  O  O     . ALA A 1 98  ? 21.132  23.169  21.976  1.00 46.70  ? 98  ALA A O     1 
ATOM   620  C  CB    . ALA A 1 98  ? 23.275  25.092  20.543  1.00 43.76  ? 98  ALA A CB    1 
ATOM   621  N  N     . LEU A 1 99  ? 22.218  24.384  23.514  1.00 45.45  ? 99  LEU A N     1 
ATOM   622  C  CA    . LEU A 1 99  ? 22.024  23.384  24.552  1.00 45.03  ? 99  LEU A CA    1 
ATOM   623  C  C     . LEU A 1 99  ? 20.606  23.448  25.108  1.00 46.74  ? 99  LEU A C     1 
ATOM   624  O  O     . LEU A 1 99  ? 20.133  22.492  25.721  1.00 50.05  ? 99  LEU A O     1 
ATOM   625  C  CB    . LEU A 1 99  ? 23.009  23.594  25.706  1.00 42.09  ? 99  LEU A CB    1 
ATOM   626  C  CG    . LEU A 1 99  ? 24.495  23.328  25.475  1.00 40.38  ? 99  LEU A CG    1 
ATOM   627  C  CD1   . LEU A 1 99  ? 25.316  23.889  26.626  1.00 37.30  ? 99  LEU A CD1   1 
ATOM   628  C  CD2   . LEU A 1 99  ? 24.715  21.845  25.313  1.00 37.38  ? 99  LEU A CD2   1 
ATOM   629  N  N     . ALA A 1 100 ? 19.917  24.565  24.908  1.00 46.58  ? 100 ALA A N     1 
ATOM   630  C  CA    . ALA A 1 100 ? 18.571  24.682  25.452  1.00 45.76  ? 100 ALA A CA    1 
ATOM   631  C  C     . ALA A 1 100 ? 17.466  24.256  24.500  1.00 46.01  ? 100 ALA A C     1 
ATOM   632  O  O     . ALA A 1 100 ? 16.447  23.738  24.939  1.00 46.80  ? 100 ALA A O     1 
ATOM   633  C  CB    . ALA A 1 100 ? 18.327  26.094  25.951  1.00 43.49  ? 100 ALA A CB    1 
ATOM   634  N  N     . ILE A 1 101 ? 17.648  24.456  23.201  1.00 47.01  ? 101 ILE A N     1 
ATOM   635  C  CA    . ILE A 1 101 ? 16.602  24.049  22.266  1.00 48.44  ? 101 ILE A CA    1 
ATOM   636  C  C     . ILE A 1 101 ? 16.674  22.537  22.030  1.00 49.19  ? 101 ILE A C     1 
ATOM   637  O  O     . ILE A 1 101 ? 17.674  21.896  22.360  1.00 49.60  ? 101 ILE A O     1 
ATOM   638  C  CB    . ILE A 1 101 ? 16.700  24.825  20.916  1.00 47.36  ? 101 ILE A CB    1 
ATOM   639  C  CG1   . ILE A 1 101 ? 18.108  24.716  20.329  1.00 48.33  ? 101 ILE A CG1   1 
ATOM   640  C  CG2   . ILE A 1 101 ? 16.361  26.290  21.141  1.00 48.06  ? 101 ILE A CG2   1 
ATOM   641  C  CD1   . ILE A 1 101 ? 18.282  25.439  19.004  1.00 45.69  ? 101 ILE A CD1   1 
ATOM   642  N  N     . PRO A 1 102 ? 15.594  21.940  21.498  1.00 49.51  ? 102 PRO A N     1 
ATOM   643  C  CA    . PRO A 1 102 ? 15.558  20.502  21.230  1.00 50.21  ? 102 PRO A CA    1 
ATOM   644  C  C     . PRO A 1 102 ? 16.594  20.015  20.221  1.00 51.97  ? 102 PRO A C     1 
ATOM   645  O  O     . PRO A 1 102 ? 17.236  20.813  19.535  1.00 51.37  ? 102 PRO A O     1 
ATOM   646  C  CB    . PRO A 1 102 ? 14.115  20.266  20.793  1.00 48.62  ? 102 PRO A CB    1 
ATOM   647  C  CG    . PRO A 1 102 ? 13.657  21.588  20.331  1.00 48.33  ? 102 PRO A CG    1 
ATOM   648  C  CD    . PRO A 1 102 ? 14.262  22.527  21.314  1.00 49.67  ? 102 PRO A CD    1 
ATOM   649  N  N     . GLU A 1 103 ? 16.744  18.695  20.141  1.00 54.78  ? 103 GLU A N     1 
ATOM   650  C  CA    . GLU A 1 103 ? 17.736  18.079  19.272  1.00 57.39  ? 103 GLU A CA    1 
ATOM   651  C  C     . GLU A 1 103 ? 17.647  18.457  17.799  1.00 58.06  ? 103 GLU A C     1 
ATOM   652  O  O     . GLU A 1 103 ? 18.646  18.370  17.067  1.00 56.85  ? 103 GLU A O     1 
ATOM   653  C  CB    . GLU A 1 103 ? 17.694  16.559  19.432  1.00 59.54  ? 103 GLU A CB    1 
ATOM   654  C  CG    . GLU A 1 103 ? 18.992  15.856  19.014  1.00 66.50  ? 103 GLU A CG    1 
ATOM   655  C  CD    . GLU A 1 103 ? 20.219  16.240  19.884  1.00 70.60  ? 103 GLU A CD    1 
ATOM   656  O  OE1   . GLU A 1 103 ? 20.611  17.432  19.913  1.00 71.47  ? 103 GLU A OE1   1 
ATOM   657  O  OE2   . GLU A 1 103 ? 20.801  15.341  20.537  1.00 72.53  ? 103 GLU A OE2   1 
ATOM   658  N  N     . ASP A 1 104 ? 16.461  18.886  17.373  1.00 58.95  ? 104 ASP A N     1 
ATOM   659  C  CA    . ASP A 1 104 ? 16.230  19.281  15.982  1.00 60.68  ? 104 ASP A CA    1 
ATOM   660  C  C     . ASP A 1 104 ? 16.076  20.796  15.836  1.00 59.98  ? 104 ASP A C     1 
ATOM   661  O  O     . ASP A 1 104 ? 15.500  21.288  14.858  1.00 58.82  ? 104 ASP A O     1 
ATOM   662  C  CB    . ASP A 1 104 ? 14.981  18.580  15.448  1.00 63.96  ? 104 ASP A CB    1 
ATOM   663  C  CG    . ASP A 1 104 ? 13.769  18.810  16.327  1.00 67.61  ? 104 ASP A CG    1 
ATOM   664  O  OD1   . ASP A 1 104 ? 13.928  18.737  17.567  1.00 68.39  ? 104 ASP A OD1   1 
ATOM   665  O  OD2   . ASP A 1 104 ? 12.665  19.054  15.785  1.00 69.69  ? 104 ASP A OD2   1 
ATOM   666  N  N     . GLY A 1 105 ? 16.594  21.521  16.824  1.00 59.39  ? 105 GLY A N     1 
ATOM   667  C  CA    . GLY A 1 105 ? 16.526  22.967  16.810  1.00 58.59  ? 105 GLY A CA    1 
ATOM   668  C  C     . GLY A 1 105 ? 17.541  23.566  15.857  1.00 57.86  ? 105 GLY A C     1 
ATOM   669  O  O     . GLY A 1 105 ? 18.591  22.968  15.592  1.00 58.57  ? 105 GLY A O     1 
ATOM   670  N  N     . LYS A 1 106 ? 17.230  24.753  15.345  1.00 56.07  ? 106 LYS A N     1 
ATOM   671  C  CA    . LYS A 1 106 ? 18.109  25.437  14.409  1.00 53.79  ? 106 LYS A CA    1 
ATOM   672  C  C     . LYS A 1 106 ? 18.365  26.876  14.805  1.00 50.89  ? 106 LYS A C     1 
ATOM   673  O  O     . LYS A 1 106 ? 17.481  27.577  15.289  1.00 49.72  ? 106 LYS A O     1 
ATOM   674  C  CB    . LYS A 1 106 ? 17.515  25.376  13.002  1.00 55.31  ? 106 LYS A CB    1 
ATOM   675  C  CG    . LYS A 1 106 ? 17.522  23.975  12.426  1.00 58.21  ? 106 LYS A CG    1 
ATOM   676  C  CD    . LYS A 1 106 ? 16.508  23.817  11.315  1.00 61.83  ? 106 LYS A CD    1 
ATOM   677  C  CE    . LYS A 1 106 ? 16.390  22.360  10.926  1.00 64.87  ? 106 LYS A CE    1 
ATOM   678  N  NZ    . LYS A 1 106 ? 16.274  21.498  12.146  1.00 68.12  ? 106 LYS A NZ    1 
ATOM   679  N  N     . ILE A 1 107 ? 19.594  27.306  14.576  1.00 48.56  ? 107 ILE A N     1 
ATOM   680  C  CA    . ILE A 1 107 ? 20.018  28.648  14.905  1.00 47.01  ? 107 ILE A CA    1 
ATOM   681  C  C     . ILE A 1 107 ? 20.747  29.286  13.735  1.00 47.05  ? 107 ILE A C     1 
ATOM   682  O  O     . ILE A 1 107 ? 21.714  28.717  13.227  1.00 47.15  ? 107 ILE A O     1 
ATOM   683  C  CB    . ILE A 1 107 ? 21.015  28.638  16.080  1.00 45.32  ? 107 ILE A CB    1 
ATOM   684  C  CG1   . ILE A 1 107 ? 20.491  27.767  17.210  1.00 43.65  ? 107 ILE A CG1   1 
ATOM   685  C  CG2   . ILE A 1 107 ? 21.267  30.056  16.558  1.00 43.38  ? 107 ILE A CG2   1 
ATOM   686  C  CD1   . ILE A 1 107 ? 21.509  27.518  18.285  1.00 43.08  ? 107 ILE A CD1   1 
ATOM   687  N  N     . LEU A 1 108 ? 20.291  30.461  13.310  1.00 47.30  ? 108 LEU A N     1 
ATOM   688  C  CA    . LEU A 1 108 ? 20.968  31.198  12.243  1.00 47.11  ? 108 LEU A CA    1 
ATOM   689  C  C     . LEU A 1 108 ? 21.875  32.202  12.976  1.00 46.29  ? 108 LEU A C     1 
ATOM   690  O  O     . LEU A 1 108 ? 21.382  33.184  13.535  1.00 46.69  ? 108 LEU A O     1 
ATOM   691  C  CB    . LEU A 1 108 ? 19.951  31.938  11.368  1.00 47.73  ? 108 LEU A CB    1 
ATOM   692  C  CG    . LEU A 1 108 ? 20.559  32.911  10.352  1.00 49.64  ? 108 LEU A CG    1 
ATOM   693  C  CD1   . LEU A 1 108 ? 21.469  32.151  9.410   1.00 49.53  ? 108 LEU A CD1   1 
ATOM   694  C  CD2   . LEU A 1 108 ? 19.467  33.616  9.582   1.00 50.52  ? 108 LEU A CD2   1 
ATOM   695  N  N     . ALA A 1 109 ? 23.185  31.950  12.982  1.00 44.49  ? 109 ALA A N     1 
ATOM   696  C  CA    . ALA A 1 109 ? 24.133  32.810  13.686  1.00 44.05  ? 109 ALA A CA    1 
ATOM   697  C  C     . ALA A 1 109 ? 24.957  33.696  12.761  1.00 45.25  ? 109 ALA A C     1 
ATOM   698  O  O     . ALA A 1 109 ? 25.663  33.198  11.888  1.00 46.24  ? 109 ALA A O     1 
ATOM   699  C  CB    . ALA A 1 109 ? 25.051  31.960  14.528  1.00 43.64  ? 109 ALA A CB    1 
ATOM   700  N  N     . MET A 1 110 ? 24.895  35.009  12.987  1.00 44.83  ? 110 MET A N     1 
ATOM   701  C  CA    . MET A 1 110 ? 25.597  35.986  12.162  1.00 43.87  ? 110 MET A CA    1 
ATOM   702  C  C     . MET A 1 110 ? 26.661  36.815  12.885  1.00 44.21  ? 110 MET A C     1 
ATOM   703  O  O     . MET A 1 110 ? 26.407  37.355  13.950  1.00 46.78  ? 110 MET A O     1 
ATOM   704  C  CB    . MET A 1 110 ? 24.571  36.938  11.547  1.00 44.59  ? 110 MET A CB    1 
ATOM   705  C  CG    . MET A 1 110 ? 23.673  36.306  10.494  1.00 48.02  ? 110 MET A CG    1 
ATOM   706  S  SD    . MET A 1 110 ? 22.341  37.415  9.909   1.00 51.98  ? 110 MET A SD    1 
ATOM   707  C  CE    . MET A 1 110 ? 20.864  36.495  10.464  1.00 52.35  ? 110 MET A CE    1 
ATOM   708  N  N     . ASP A 1 111 ? 27.854  36.922  12.312  1.00 43.76  ? 111 ASP A N     1 
ATOM   709  C  CA    . ASP A 1 111 ? 28.900  37.746  12.910  1.00 45.37  ? 111 ASP A CA    1 
ATOM   710  C  C     . ASP A 1 111 ? 29.937  38.170  11.859  1.00 47.10  ? 111 ASP A C     1 
ATOM   711  O  O     . ASP A 1 111 ? 30.295  37.393  10.989  1.00 48.36  ? 111 ASP A O     1 
ATOM   712  C  CB    . ASP A 1 111 ? 29.570  37.019  14.073  1.00 43.95  ? 111 ASP A CB    1 
ATOM   713  C  CG    . ASP A 1 111 ? 30.342  37.969  14.979  1.00 46.77  ? 111 ASP A CG    1 
ATOM   714  O  OD1   . ASP A 1 111 ? 31.375  38.513  14.533  1.00 47.16  ? 111 ASP A OD1   1 
ATOM   715  O  OD2   . ASP A 1 111 ? 29.910  38.194  16.135  1.00 46.74  ? 111 ASP A OD2   1 
ATOM   716  N  N     . ILE A 1 112 ? 30.406  39.410  11.929  1.00 48.68  ? 112 ILE A N     1 
ATOM   717  C  CA    . ILE A 1 112 ? 31.374  39.908  10.956  1.00 52.24  ? 112 ILE A CA    1 
ATOM   718  C  C     . ILE A 1 112 ? 32.777  39.323  11.049  1.00 55.03  ? 112 ILE A C     1 
ATOM   719  O  O     . ILE A 1 112 ? 33.503  39.267  10.055  1.00 55.11  ? 112 ILE A O     1 
ATOM   720  C  CB    . ILE A 1 112 ? 31.540  41.428  11.053  1.00 51.25  ? 112 ILE A CB    1 
ATOM   721  C  CG1   . ILE A 1 112 ? 31.866  41.808  12.492  1.00 51.69  ? 112 ILE A CG1   1 
ATOM   722  C  CG2   . ILE A 1 112 ? 30.312  42.125  10.523  1.00 50.30  ? 112 ILE A CG2   1 
ATOM   723  C  CD1   . ILE A 1 112 ? 32.095  43.276  12.701  1.00 52.74  ? 112 ILE A CD1   1 
ATOM   724  N  N     . ASN A 1 113 ? 33.170  38.891  12.238  1.00 58.85  ? 113 ASN A N     1 
ATOM   725  C  CA    . ASN A 1 113 ? 34.510  38.356  12.410  1.00 61.69  ? 113 ASN A CA    1 
ATOM   726  C  C     . ASN A 1 113 ? 34.697  36.917  11.905  1.00 63.85  ? 113 ASN A C     1 
ATOM   727  O  O     . ASN A 1 113 ? 35.151  36.720  10.766  1.00 66.43  ? 113 ASN A O     1 
ATOM   728  C  CB    . ASN A 1 113 ? 34.937  38.484  13.875  1.00 59.78  ? 113 ASN A CB    1 
ATOM   729  C  CG    . ASN A 1 113 ? 36.387  38.125  14.085  1.00 58.75  ? 113 ASN A CG    1 
ATOM   730  O  OD1   . ASN A 1 113 ? 36.750  36.951  14.069  1.00 59.65  ? 113 ASN A OD1   1 
ATOM   731  N  ND2   . ASN A 1 113 ? 37.226  39.129  14.270  1.00 55.15  ? 113 ASN A ND2   1 
ATOM   732  N  N     . LYS A 1 114 ? 34.362  35.934  12.744  1.00 62.79  ? 114 LYS A N     1 
ATOM   733  C  CA    . LYS A 1 114 ? 34.486  34.505  12.423  1.00 62.63  ? 114 LYS A CA    1 
ATOM   734  C  C     . LYS A 1 114 ? 35.747  33.800  12.934  1.00 61.57  ? 114 LYS A C     1 
ATOM   735  O  O     . LYS A 1 114 ? 35.716  32.597  13.170  1.00 60.39  ? 114 LYS A O     1 
ATOM   736  C  CB    . LYS A 1 114 ? 34.353  34.226  10.924  1.00 62.51  ? 114 LYS A CB    1 
ATOM   737  C  CG    . LYS A 1 114 ? 34.602  32.759  10.608  1.00 64.57  ? 114 LYS A CG    1 
ATOM   738  C  CD    . LYS A 1 114 ? 33.980  32.326  9.302   1.00 67.95  ? 114 LYS A CD    1 
ATOM   739  C  CE    . LYS A 1 114 ? 34.077  30.811  9.142   1.00 68.70  ? 114 LYS A CE    1 
ATOM   740  N  NZ    . LYS A 1 114 ? 33.309  30.317  7.962   1.00 69.19  ? 114 LYS A NZ    1 
ATOM   741  N  N     . GLU A 1 115 ? 36.866  34.502  13.075  1.00 60.98  ? 115 GLU A N     1 
ATOM   742  C  CA    . GLU A 1 115 ? 38.032  33.824  13.623  1.00 61.04  ? 115 GLU A CA    1 
ATOM   743  C  C     . GLU A 1 115 ? 37.560  33.548  15.045  1.00 59.45  ? 115 GLU A C     1 
ATOM   744  O  O     . GLU A 1 115 ? 37.632  32.414  15.527  1.00 59.44  ? 115 GLU A O     1 
ATOM   745  C  CB    . GLU A 1 115 ? 39.274  34.723  13.660  1.00 63.41  ? 115 GLU A CB    1 
ATOM   746  C  CG    . GLU A 1 115 ? 39.736  35.275  12.303  1.00 70.67  ? 115 GLU A CG    1 
ATOM   747  C  CD    . GLU A 1 115 ? 39.688  36.822  12.240  1.00 75.40  ? 115 GLU A CD    1 
ATOM   748  O  OE1   . GLU A 1 115 ? 40.269  37.494  13.139  1.00 74.89  ? 115 GLU A OE1   1 
ATOM   749  O  OE2   . GLU A 1 115 ? 39.068  37.365  11.287  1.00 77.69  ? 115 GLU A OE2   1 
ATOM   750  N  N     . ASN A 1 116 ? 37.034  34.592  15.689  1.00 56.55  ? 116 ASN A N     1 
ATOM   751  C  CA    . ASN A 1 116 ? 36.528  34.499  17.052  1.00 53.86  ? 116 ASN A CA    1 
ATOM   752  C  C     . ASN A 1 116 ? 35.563  33.332  17.226  1.00 53.32  ? 116 ASN A C     1 
ATOM   753  O  O     . ASN A 1 116 ? 35.703  32.546  18.156  1.00 54.30  ? 116 ASN A O     1 
ATOM   754  C  CB    . ASN A 1 116 ? 35.798  35.781  17.461  1.00 54.20  ? 116 ASN A CB    1 
ATOM   755  C  CG    . ASN A 1 116 ? 36.697  37.006  17.485  1.00 54.04  ? 116 ASN A CG    1 
ATOM   756  O  OD1   . ASN A 1 116 ? 37.899  36.914  17.743  1.00 55.75  ? 116 ASN A OD1   1 
ATOM   757  N  ND2   . ASN A 1 116 ? 36.103  38.173  17.242  1.00 51.13  ? 116 ASN A ND2   1 
ATOM   758  N  N     . TYR A 1 117 ? 34.576  33.222  16.343  1.00 51.74  ? 117 TYR A N     1 
ATOM   759  C  CA    . TYR A 1 117 ? 33.600  32.142  16.437  1.00 50.64  ? 117 TYR A CA    1 
ATOM   760  C  C     . TYR A 1 117 ? 34.223  30.751  16.431  1.00 51.50  ? 117 TYR A C     1 
ATOM   761  O  O     . TYR A 1 117 ? 33.751  29.851  17.115  1.00 52.24  ? 117 TYR A O     1 
ATOM   762  C  CB    . TYR A 1 117 ? 32.586  32.242  15.298  1.00 49.90  ? 117 TYR A CB    1 
ATOM   763  C  CG    . TYR A 1 117 ? 31.752  30.991  15.106  1.00 49.42  ? 117 TYR A CG    1 
ATOM   764  C  CD1   . TYR A 1 117 ? 30.969  30.475  16.142  1.00 49.32  ? 117 TYR A CD1   1 
ATOM   765  C  CD2   . TYR A 1 117 ? 31.776  30.299  13.901  1.00 48.98  ? 117 TYR A CD2   1 
ATOM   766  C  CE1   . TYR A 1 117 ? 30.239  29.294  15.972  1.00 47.99  ? 117 TYR A CE1   1 
ATOM   767  C  CE2   . TYR A 1 117 ? 31.052  29.124  13.727  1.00 48.15  ? 117 TYR A CE2   1 
ATOM   768  C  CZ    . TYR A 1 117 ? 30.293  28.628  14.762  1.00 47.34  ? 117 TYR A CZ    1 
ATOM   769  O  OH    . TYR A 1 117 ? 29.613  27.450  14.590  1.00 47.36  ? 117 TYR A OH    1 
ATOM   770  N  N     . GLU A 1 118 ? 35.284  30.567  15.663  1.00 52.62  ? 118 GLU A N     1 
ATOM   771  C  CA    . GLU A 1 118 ? 35.916  29.261  15.593  1.00 54.33  ? 118 GLU A CA    1 
ATOM   772  C  C     . GLU A 1 118 ? 36.759  28.983  16.819  1.00 53.45  ? 118 GLU A C     1 
ATOM   773  O  O     . GLU A 1 118 ? 37.172  27.851  17.063  1.00 52.56  ? 118 GLU A O     1 
ATOM   774  C  CB    . GLU A 1 118 ? 36.762  29.154  14.329  1.00 56.38  ? 118 GLU A CB    1 
ATOM   775  C  CG    . GLU A 1 118 ? 35.933  29.229  13.064  1.00 60.24  ? 118 GLU A CG    1 
ATOM   776  C  CD    . GLU A 1 118 ? 36.793  29.393  11.835  1.00 64.47  ? 118 GLU A CD    1 
ATOM   777  O  OE1   . GLU A 1 118 ? 37.970  29.818  11.997  1.00 65.65  ? 118 GLU A OE1   1 
ATOM   778  O  OE2   . GLU A 1 118 ? 36.291  29.111  10.718  1.00 65.58  ? 118 GLU A OE2   1 
ATOM   779  N  N     . LEU A 1 119 ? 37.005  30.024  17.594  1.00 53.35  ? 119 LEU A N     1 
ATOM   780  C  CA    . LEU A 1 119 ? 37.791  29.882  18.799  1.00 54.72  ? 119 LEU A CA    1 
ATOM   781  C  C     . LEU A 1 119 ? 37.008  29.007  19.767  1.00 55.99  ? 119 LEU A C     1 
ATOM   782  O  O     . LEU A 1 119 ? 37.592  28.242  20.536  1.00 57.50  ? 119 LEU A O     1 
ATOM   783  C  CB    . LEU A 1 119 ? 38.009  31.241  19.431  1.00 55.21  ? 119 LEU A CB    1 
ATOM   784  C  CG    . LEU A 1 119 ? 39.288  31.381  20.223  1.00 55.77  ? 119 LEU A CG    1 
ATOM   785  C  CD1   . LEU A 1 119 ? 40.434  31.262  19.231  1.00 56.18  ? 119 LEU A CD1   1 
ATOM   786  C  CD2   . LEU A 1 119 ? 39.313  32.725  20.955  1.00 55.65  ? 119 LEU A CD2   1 
ATOM   787  N  N     . GLY A 1 120 ? 35.681  29.127  19.719  1.00 55.69  ? 120 GLY A N     1 
ATOM   788  C  CA    . GLY A 1 120 ? 34.828  28.359  20.606  1.00 54.65  ? 120 GLY A CA    1 
ATOM   789  C  C     . GLY A 1 120 ? 34.116  27.185  19.965  1.00 54.26  ? 120 GLY A C     1 
ATOM   790  O  O     . GLY A 1 120 ? 33.531  26.346  20.661  1.00 54.03  ? 120 GLY A O     1 
ATOM   791  N  N     . LEU A 1 121 ? 34.158  27.116  18.640  1.00 53.45  ? 121 LEU A N     1 
ATOM   792  C  CA    . LEU A 1 121 ? 33.502  26.033  17.930  1.00 52.62  ? 121 LEU A CA    1 
ATOM   793  C  C     . LEU A 1 121 ? 33.957  24.667  18.424  1.00 53.61  ? 121 LEU A C     1 
ATOM   794  O  O     . LEU A 1 121 ? 33.162  23.728  18.489  1.00 54.58  ? 121 LEU A O     1 
ATOM   795  C  CB    . LEU A 1 121 ? 33.752  26.140  16.426  1.00 51.25  ? 121 LEU A CB    1 
ATOM   796  C  CG    . LEU A 1 121 ? 32.944  25.133  15.598  1.00 50.01  ? 121 LEU A CG    1 
ATOM   797  C  CD1   . LEU A 1 121 ? 31.464  25.243  15.913  1.00 47.69  ? 121 LEU A CD1   1 
ATOM   798  C  CD2   . LEU A 1 121 ? 33.182  25.387  14.136  1.00 48.64  ? 121 LEU A CD2   1 
ATOM   799  N  N     . PRO A 1 122 ? 35.246  24.525  18.776  1.00 53.89  ? 122 PRO A N     1 
ATOM   800  C  CA    . PRO A 1 122 ? 35.669  23.205  19.252  1.00 54.23  ? 122 PRO A CA    1 
ATOM   801  C  C     . PRO A 1 122 ? 34.803  22.732  20.431  1.00 54.47  ? 122 PRO A C     1 
ATOM   802  O  O     . PRO A 1 122 ? 34.437  21.552  20.527  1.00 55.17  ? 122 PRO A O     1 
ATOM   803  C  CB    . PRO A 1 122 ? 37.130  23.438  19.644  1.00 53.01  ? 122 PRO A CB    1 
ATOM   804  C  CG    . PRO A 1 122 ? 37.562  24.483  18.695  1.00 51.47  ? 122 PRO A CG    1 
ATOM   805  C  CD    . PRO A 1 122 ? 36.397  25.442  18.704  1.00 52.89  ? 122 PRO A CD    1 
ATOM   806  N  N     . VAL A 1 123 ? 34.471  23.669  21.313  1.00 52.76  ? 123 VAL A N     1 
ATOM   807  C  CA    . VAL A 1 123 ? 33.660  23.366  22.472  1.00 51.30  ? 123 VAL A CA    1 
ATOM   808  C  C     . VAL A 1 123 ? 32.242  22.986  22.060  1.00 51.35  ? 123 VAL A C     1 
ATOM   809  O  O     . VAL A 1 123 ? 31.709  21.970  22.490  1.00 52.16  ? 123 VAL A O     1 
ATOM   810  C  CB    . VAL A 1 123 ? 33.619  24.569  23.430  1.00 51.14  ? 123 VAL A CB    1 
ATOM   811  C  CG1   . VAL A 1 123 ? 32.803  24.226  24.669  1.00 50.28  ? 123 VAL A CG1   1 
ATOM   812  C  CG2   . VAL A 1 123 ? 35.041  24.970  23.810  1.00 49.78  ? 123 VAL A CG2   1 
ATOM   813  N  N     . ILE A 1 124 ? 31.628  23.791  21.213  1.00 51.17  ? 124 ILE A N     1 
ATOM   814  C  CA    . ILE A 1 124 ? 30.275  23.493  20.788  1.00 51.43  ? 124 ILE A CA    1 
ATOM   815  C  C     . ILE A 1 124 ? 30.205  22.095  20.169  1.00 52.71  ? 124 ILE A C     1 
ATOM   816  O  O     . ILE A 1 124 ? 29.215  21.366  20.360  1.00 51.99  ? 124 ILE A O     1 
ATOM   817  C  CB    . ILE A 1 124 ? 29.775  24.580  19.808  1.00 51.09  ? 124 ILE A CB    1 
ATOM   818  C  CG1   . ILE A 1 124 ? 29.655  25.914  20.558  1.00 51.34  ? 124 ILE A CG1   1 
ATOM   819  C  CG2   . ILE A 1 124 ? 28.444  24.185  19.199  1.00 48.74  ? 124 ILE A CG2   1 
ATOM   820  C  CD1   . ILE A 1 124 ? 29.360  27.113  19.667  1.00 52.39  ? 124 ILE A CD1   1 
ATOM   821  N  N     . LYS A 1 125 ? 31.261  21.715  19.449  1.00 53.76  ? 125 LYS A N     1 
ATOM   822  C  CA    . LYS A 1 125 ? 31.324  20.393  18.819  1.00 54.94  ? 125 LYS A CA    1 
ATOM   823  C  C     . LYS A 1 125 ? 31.516  19.309  19.885  1.00 55.28  ? 125 LYS A C     1 
ATOM   824  O  O     . LYS A 1 125 ? 30.951  18.210  19.794  1.00 54.73  ? 125 LYS A O     1 
ATOM   825  C  CB    . LYS A 1 125 ? 32.465  20.330  17.799  1.00 55.45  ? 125 LYS A CB    1 
ATOM   826  C  CG    . LYS A 1 125 ? 32.083  20.820  16.402  1.00 57.56  ? 125 LYS A CG    1 
ATOM   827  C  CD    . LYS A 1 125 ? 33.292  20.796  15.465  1.00 59.82  ? 125 LYS A CD    1 
ATOM   828  C  CE    . LYS A 1 125 ? 33.040  21.547  14.161  1.00 58.61  ? 125 LYS A CE    1 
ATOM   829  N  NZ    . LYS A 1 125 ? 34.320  21.888  13.450  1.00 57.75  ? 125 LYS A NZ    1 
ATOM   830  N  N     . LYS A 1 126 ? 32.314  19.627  20.899  1.00 54.15  ? 126 LYS A N     1 
ATOM   831  C  CA    . LYS A 1 126 ? 32.543  18.687  21.977  1.00 53.93  ? 126 LYS A CA    1 
ATOM   832  C  C     . LYS A 1 126 ? 31.246  18.504  22.777  1.00 53.64  ? 126 LYS A C     1 
ATOM   833  O  O     . LYS A 1 126 ? 31.014  17.451  23.373  1.00 54.27  ? 126 LYS A O     1 
ATOM   834  C  CB    . LYS A 1 126 ? 33.663  19.188  22.887  1.00 53.96  ? 126 LYS A CB    1 
ATOM   835  C  CG    . LYS A 1 126 ? 33.970  18.253  24.014  1.00 54.26  ? 126 LYS A CG    1 
ATOM   836  C  CD    . LYS A 1 126 ? 34.968  18.847  24.970  1.00 58.17  ? 126 LYS A CD    1 
ATOM   837  C  CE    . LYS A 1 126 ? 35.001  18.031  26.269  1.00 59.45  ? 126 LYS A CE    1 
ATOM   838  N  NZ    . LYS A 1 126 ? 35.958  18.589  27.275  1.00 62.75  ? 126 LYS A NZ    1 
ATOM   839  N  N     . ALA A 1 127 ? 30.401  19.529  22.795  1.00 52.74  ? 127 ALA A N     1 
ATOM   840  C  CA    . ALA A 1 127 ? 29.135  19.435  23.515  1.00 52.15  ? 127 ALA A CA    1 
ATOM   841  C  C     . ALA A 1 127 ? 28.123  18.762  22.600  1.00 51.23  ? 127 ALA A C     1 
ATOM   842  O  O     . ALA A 1 127 ? 26.952  18.592  22.961  1.00 49.80  ? 127 ALA A O     1 
ATOM   843  C  CB    . ALA A 1 127 ? 28.644  20.824  23.927  1.00 52.88  ? 127 ALA A CB    1 
ATOM   844  N  N     . GLY A 1 128 ? 28.600  18.392  21.413  1.00 50.20  ? 128 GLY A N     1 
ATOM   845  C  CA    . GLY A 1 128 ? 27.773  17.726  20.425  1.00 51.91  ? 128 GLY A CA    1 
ATOM   846  C  C     . GLY A 1 128 ? 26.535  18.477  19.971  1.00 53.39  ? 128 GLY A C     1 
ATOM   847  O  O     . GLY A 1 128 ? 25.522  17.865  19.626  1.00 52.99  ? 128 GLY A O     1 
ATOM   848  N  N     . VAL A 1 129 ? 26.609  19.803  19.928  1.00 54.62  ? 129 VAL A N     1 
ATOM   849  C  CA    . VAL A 1 129 ? 25.437  20.577  19.534  1.00 54.51  ? 129 VAL A CA    1 
ATOM   850  C  C     . VAL A 1 129 ? 25.696  21.541  18.360  1.00 55.08  ? 129 VAL A C     1 
ATOM   851  O  O     . VAL A 1 129 ? 24.835  22.351  17.980  1.00 54.66  ? 129 VAL A O     1 
ATOM   852  C  CB    . VAL A 1 129 ? 24.881  21.324  20.774  1.00 53.23  ? 129 VAL A CB    1 
ATOM   853  C  CG1   . VAL A 1 129 ? 25.790  22.493  21.146  1.00 51.51  ? 129 VAL A CG1   1 
ATOM   854  C  CG2   . VAL A 1 129 ? 23.449  21.731  20.528  1.00 52.87  ? 129 VAL A CG2   1 
ATOM   855  N  N     . ASP A 1 130 ? 26.881  21.421  17.773  1.00 54.40  ? 130 ASP A N     1 
ATOM   856  C  CA    . ASP A 1 130 ? 27.254  22.251  16.651  1.00 54.68  ? 130 ASP A CA    1 
ATOM   857  C  C     . ASP A 1 130 ? 26.373  21.988  15.432  1.00 53.97  ? 130 ASP A C     1 
ATOM   858  O  O     . ASP A 1 130 ? 26.343  22.790  14.507  1.00 55.94  ? 130 ASP A O     1 
ATOM   859  C  CB    . ASP A 1 130 ? 28.728  22.022  16.283  1.00 57.79  ? 130 ASP A CB    1 
ATOM   860  C  CG    . ASP A 1 130 ? 29.001  20.615  15.728  1.00 61.13  ? 130 ASP A CG    1 
ATOM   861  O  OD1   . ASP A 1 130 ? 28.868  19.626  16.485  1.00 62.67  ? 130 ASP A OD1   1 
ATOM   862  O  OD2   . ASP A 1 130 ? 29.360  20.499  14.532  1.00 61.92  ? 130 ASP A OD2   1 
ATOM   863  N  N     . HIS A 1 131 ? 25.648  20.877  15.419  1.00 52.46  ? 131 HIS A N     1 
ATOM   864  C  CA    . HIS A 1 131 ? 24.803  20.564  14.272  1.00 50.69  ? 131 HIS A CA    1 
ATOM   865  C  C     . HIS A 1 131 ? 23.582  21.463  14.144  1.00 50.94  ? 131 HIS A C     1 
ATOM   866  O  O     . HIS A 1 131 ? 22.932  21.472  13.106  1.00 52.01  ? 131 HIS A O     1 
ATOM   867  C  CB    . HIS A 1 131 ? 24.336  19.105  14.318  1.00 48.76  ? 131 HIS A CB    1 
ATOM   868  C  CG    . HIS A 1 131 ? 23.473  18.783  15.496  1.00 48.50  ? 131 HIS A CG    1 
ATOM   869  N  ND1   . HIS A 1 131 ? 23.973  18.663  16.778  1.00 49.57  ? 131 HIS A ND1   1 
ATOM   870  C  CD2   . HIS A 1 131 ? 22.136  18.593  15.595  1.00 48.61  ? 131 HIS A CD2   1 
ATOM   871  C  CE1   . HIS A 1 131 ? 22.981  18.418  17.616  1.00 49.20  ? 131 HIS A CE1   1 
ATOM   872  N  NE2   . HIS A 1 131 ? 21.854  18.371  16.924  1.00 49.84  ? 131 HIS A NE2   1 
ATOM   873  N  N     . LYS A 1 132 ? 23.261  22.220  15.185  1.00 50.98  ? 132 LYS A N     1 
ATOM   874  C  CA    . LYS A 1 132 ? 22.087  23.087  15.137  1.00 50.66  ? 132 LYS A CA    1 
ATOM   875  C  C     . LYS A 1 132 ? 22.421  24.467  14.615  1.00 51.49  ? 132 LYS A C     1 
ATOM   876  O  O     . LYS A 1 132 ? 21.530  25.236  14.271  1.00 53.46  ? 132 LYS A O     1 
ATOM   877  C  CB    . LYS A 1 132 ? 21.479  23.249  16.529  1.00 48.47  ? 132 LYS A CB    1 
ATOM   878  C  CG    . LYS A 1 132 ? 21.054  21.976  17.194  1.00 45.71  ? 132 LYS A CG    1 
ATOM   879  C  CD    . LYS A 1 132 ? 20.570  22.232  18.605  1.00 43.25  ? 132 LYS A CD    1 
ATOM   880  C  CE    . LYS A 1 132 ? 20.486  20.939  19.381  1.00 39.97  ? 132 LYS A CE    1 
ATOM   881  N  NZ    . LYS A 1 132 ? 19.903  21.172  20.704  1.00 35.34  ? 132 LYS A NZ    1 
ATOM   882  N  N     . ILE A 1 133 ? 23.710  24.772  14.562  1.00 51.22  ? 133 ILE A N     1 
ATOM   883  C  CA    . ILE A 1 133 ? 24.188  26.074  14.136  1.00 50.41  ? 133 ILE A CA    1 
ATOM   884  C  C     . ILE A 1 133 ? 24.453  26.238  12.644  1.00 50.43  ? 133 ILE A C     1 
ATOM   885  O  O     . ILE A 1 133 ? 25.101  25.408  12.032  1.00 50.87  ? 133 ILE A O     1 
ATOM   886  C  CB    . ILE A 1 133 ? 25.489  26.414  14.899  1.00 49.72  ? 133 ILE A CB    1 
ATOM   887  C  CG1   . ILE A 1 133 ? 25.223  26.361  16.407  1.00 48.55  ? 133 ILE A CG1   1 
ATOM   888  C  CG2   . ILE A 1 133 ? 26.027  27.775  14.464  1.00 47.56  ? 133 ILE A CG2   1 
ATOM   889  C  CD1   . ILE A 1 133 ? 26.479  26.408  17.259  1.00 47.34  ? 133 ILE A CD1   1 
ATOM   890  N  N     . ASP A 1 134 ? 23.931  27.321  12.075  1.00 51.94  ? 134 ASP A N     1 
ATOM   891  C  CA    . ASP A 1 134 ? 24.155  27.689  10.674  1.00 51.48  ? 134 ASP A CA    1 
ATOM   892  C  C     . ASP A 1 134 ? 24.867  29.046  10.764  1.00 50.40  ? 134 ASP A C     1 
ATOM   893  O  O     . ASP A 1 134 ? 24.224  30.105  10.823  1.00 49.59  ? 134 ASP A O     1 
ATOM   894  C  CB    . ASP A 1 134 ? 22.829  27.850  9.917   1.00 54.08  ? 134 ASP A CB    1 
ATOM   895  C  CG    . ASP A 1 134 ? 23.025  28.374  8.476   1.00 58.09  ? 134 ASP A CG    1 
ATOM   896  O  OD1   . ASP A 1 134 ? 24.193  28.505  8.027   1.00 59.42  ? 134 ASP A OD1   1 
ATOM   897  O  OD2   . ASP A 1 134 ? 22.010  28.655  7.791   1.00 59.13  ? 134 ASP A OD2   1 
ATOM   898  N  N     . PHE A 1 135 ? 26.193  29.022  10.806  1.00 48.18  ? 135 PHE A N     1 
ATOM   899  C  CA    . PHE A 1 135 ? 26.925  30.272  10.927  1.00 47.94  ? 135 PHE A CA    1 
ATOM   900  C  C     . PHE A 1 135 ? 27.110  30.941  9.584   1.00 47.88  ? 135 PHE A C     1 
ATOM   901  O  O     . PHE A 1 135 ? 27.364  30.282  8.589   1.00 48.46  ? 135 PHE A O     1 
ATOM   902  C  CB    . PHE A 1 135 ? 28.287  30.042  11.562  1.00 45.80  ? 135 PHE A CB    1 
ATOM   903  C  CG    . PHE A 1 135 ? 29.055  31.305  11.805  1.00 45.10  ? 135 PHE A CG    1 
ATOM   904  C  CD1   . PHE A 1 135 ? 28.811  32.074  12.933  1.00 43.83  ? 135 PHE A CD1   1 
ATOM   905  C  CD2   . PHE A 1 135 ? 30.057  31.698  10.929  1.00 46.04  ? 135 PHE A CD2   1 
ATOM   906  C  CE1   . PHE A 1 135 ? 29.555  33.208  13.200  1.00 44.02  ? 135 PHE A CE1   1 
ATOM   907  C  CE2   . PHE A 1 135 ? 30.816  32.839  11.180  1.00 46.40  ? 135 PHE A CE2   1 
ATOM   908  C  CZ    . PHE A 1 135 ? 30.567  33.597  12.321  1.00 46.22  ? 135 PHE A CZ    1 
ATOM   909  N  N     . ARG A 1 136 ? 26.984  32.259  9.570   1.00 48.68  ? 136 ARG A N     1 
ATOM   910  C  CA    . ARG A 1 136 ? 27.132  33.039  8.353   1.00 49.39  ? 136 ARG A CA    1 
ATOM   911  C  C     . ARG A 1 136 ? 28.051  34.214  8.638   1.00 50.36  ? 136 ARG A C     1 
ATOM   912  O  O     . ARG A 1 136 ? 27.709  35.092  9.432   1.00 51.15  ? 136 ARG A O     1 
ATOM   913  C  CB    . ARG A 1 136 ? 25.775  33.578  7.885   1.00 47.79  ? 136 ARG A CB    1 
ATOM   914  C  CG    . ARG A 1 136 ? 25.092  32.788  6.790   1.00 49.44  ? 136 ARG A CG    1 
ATOM   915  C  CD    . ARG A 1 136 ? 24.213  31.703  7.361   1.00 53.96  ? 136 ARG A CD    1 
ATOM   916  N  NE    . ARG A 1 136 ? 23.238  31.171  6.408   1.00 55.95  ? 136 ARG A NE    1 
ATOM   917  C  CZ    . ARG A 1 136 ? 22.482  31.912  5.598   1.00 58.41  ? 136 ARG A CZ    1 
ATOM   918  N  NH1   . ARG A 1 136 ? 22.575  33.238  5.586   1.00 59.35  ? 136 ARG A NH1   1 
ATOM   919  N  NH2   . ARG A 1 136 ? 21.590  31.324  4.820   1.00 62.18  ? 136 ARG A NH2   1 
ATOM   920  N  N     . GLU A 1 137 ? 29.214  34.252  8.000   1.00 51.11  ? 137 GLU A N     1 
ATOM   921  C  CA    . GLU A 1 137 ? 30.109  35.376  8.244   1.00 53.24  ? 137 GLU A CA    1 
ATOM   922  C  C     . GLU A 1 137 ? 29.662  36.610  7.486   1.00 53.55  ? 137 GLU A C     1 
ATOM   923  O  O     . GLU A 1 137 ? 29.253  36.516  6.330   1.00 53.66  ? 137 GLU A O     1 
ATOM   924  C  CB    . GLU A 1 137 ? 31.537  35.048  7.839   1.00 54.34  ? 137 GLU A CB    1 
ATOM   925  C  CG    . GLU A 1 137 ? 32.452  36.240  7.941   1.00 56.32  ? 137 GLU A CG    1 
ATOM   926  C  CD    . GLU A 1 137 ? 33.905  35.880  7.687   1.00 61.73  ? 137 GLU A CD    1 
ATOM   927  O  OE1   . GLU A 1 137 ? 34.168  35.074  6.756   1.00 62.91  ? 137 GLU A OE1   1 
ATOM   928  O  OE2   . GLU A 1 137 ? 34.783  36.415  8.412   1.00 61.63  ? 137 GLU A OE2   1 
ATOM   929  N  N     . GLY A 1 138 ? 29.724  37.763  8.151   1.00 53.94  ? 138 GLY A N     1 
ATOM   930  C  CA    . GLY A 1 138 ? 29.344  39.007  7.504   1.00 53.07  ? 138 GLY A CA    1 
ATOM   931  C  C     . GLY A 1 138 ? 28.333  39.883  8.215   1.00 51.87  ? 138 GLY A C     1 
ATOM   932  O  O     . GLY A 1 138 ? 27.651  39.444  9.144   1.00 53.33  ? 138 GLY A O     1 
ATOM   933  N  N     . PRO A 1 139 ? 28.211  41.141  7.779   1.00 50.01  ? 139 PRO A N     1 
ATOM   934  C  CA    . PRO A 1 139 ? 27.288  42.134  8.334   1.00 49.70  ? 139 PRO A CA    1 
ATOM   935  C  C     . PRO A 1 139 ? 25.867  41.577  8.338   1.00 48.95  ? 139 PRO A C     1 
ATOM   936  O  O     . PRO A 1 139 ? 25.429  40.962  7.361   1.00 48.26  ? 139 PRO A O     1 
ATOM   937  C  CB    . PRO A 1 139 ? 27.430  43.313  7.371   1.00 49.63  ? 139 PRO A CB    1 
ATOM   938  C  CG    . PRO A 1 139 ? 28.821  43.167  6.845   1.00 48.68  ? 139 PRO A CG    1 
ATOM   939  C  CD    . PRO A 1 139 ? 28.934  41.691  6.619   1.00 49.72  ? 139 PRO A CD    1 
ATOM   940  N  N     . ALA A 1 140 ? 25.136  41.822  9.418   1.00 48.17  ? 140 ALA A N     1 
ATOM   941  C  CA    . ALA A 1 140 ? 23.776  41.309  9.538   1.00 47.11  ? 140 ALA A CA    1 
ATOM   942  C  C     . ALA A 1 140 ? 22.688  41.944  8.658   1.00 46.37  ? 140 ALA A C     1 
ATOM   943  O  O     . ALA A 1 140 ? 21.887  41.214  8.067   1.00 45.36  ? 140 ALA A O     1 
ATOM   944  C  CB    . ALA A 1 140 ? 23.350  41.350  11.000  1.00 47.06  ? 140 ALA A CB    1 
ATOM   945  N  N     . LEU A 1 141 ? 22.660  43.281  8.567   1.00 46.31  ? 141 LEU A N     1 
ATOM   946  C  CA    . LEU A 1 141 ? 21.642  43.996  7.783   1.00 45.19  ? 141 LEU A CA    1 
ATOM   947  C  C     . LEU A 1 141 ? 21.403  43.456  6.384   1.00 46.49  ? 141 LEU A C     1 
ATOM   948  O  O     . LEU A 1 141 ? 20.263  43.193  6.009   1.00 47.69  ? 141 LEU A O     1 
ATOM   949  C  CB    . LEU A 1 141 ? 21.969  45.468  7.682   1.00 45.01  ? 141 LEU A CB    1 
ATOM   950  C  CG    . LEU A 1 141 ? 21.172  46.431  8.555   1.00 48.15  ? 141 LEU A CG    1 
ATOM   951  C  CD1   . LEU A 1 141 ? 21.403  47.834  7.986   1.00 48.02  ? 141 LEU A CD1   1 
ATOM   952  C  CD2   . LEU A 1 141 ? 19.670  46.096  8.571   1.00 46.91  ? 141 LEU A CD2   1 
ATOM   953  N  N     . PRO A 1 142 ? 22.470  43.308  5.578   1.00 46.41  ? 142 PRO A N     1 
ATOM   954  C  CA    . PRO A 1 142 ? 22.323  42.785  4.220   1.00 45.63  ? 142 PRO A CA    1 
ATOM   955  C  C     . PRO A 1 142 ? 21.475  41.512  4.221   1.00 45.77  ? 142 PRO A C     1 
ATOM   956  O  O     . PRO A 1 142 ? 20.446  41.416  3.547   1.00 44.20  ? 142 PRO A O     1 
ATOM   957  C  CB    . PRO A 1 142 ? 23.764  42.503  3.827   1.00 45.03  ? 142 PRO A CB    1 
ATOM   958  C  CG    . PRO A 1 142 ? 24.492  43.602  4.474   1.00 44.50  ? 142 PRO A CG    1 
ATOM   959  C  CD    . PRO A 1 142 ? 23.877  43.670  5.839   1.00 46.00  ? 142 PRO A CD    1 
ATOM   960  N  N     . VAL A 1 143 ? 21.935  40.536  5.000   1.00 47.10  ? 143 VAL A N     1 
ATOM   961  C  CA    . VAL A 1 143 ? 21.265  39.248  5.126   1.00 47.21  ? 143 VAL A CA    1 
ATOM   962  C  C     . VAL A 1 143 ? 19.820  39.434  5.539   1.00 47.44  ? 143 VAL A C     1 
ATOM   963  O  O     . VAL A 1 143 ? 18.930  38.785  4.999   1.00 48.10  ? 143 VAL A O     1 
ATOM   964  C  CB    . VAL A 1 143 ? 21.964  38.355  6.167   1.00 46.14  ? 143 VAL A CB    1 
ATOM   965  C  CG1   . VAL A 1 143 ? 21.276  36.997  6.239   1.00 44.39  ? 143 VAL A CG1   1 
ATOM   966  C  CG2   . VAL A 1 143 ? 23.429  38.205  5.811   1.00 44.13  ? 143 VAL A CG2   1 
ATOM   967  N  N     . LEU A 1 144 ? 19.594  40.318  6.503   1.00 47.35  ? 144 LEU A N     1 
ATOM   968  C  CA    . LEU A 1 144 ? 18.245  40.578  6.971   1.00 49.02  ? 144 LEU A CA    1 
ATOM   969  C  C     . LEU A 1 144 ? 17.394  41.065  5.813   1.00 51.74  ? 144 LEU A C     1 
ATOM   970  O  O     . LEU A 1 144 ? 16.333  40.507  5.525   1.00 51.49  ? 144 LEU A O     1 
ATOM   971  C  CB    . LEU A 1 144 ? 18.263  41.634  8.074   1.00 46.89  ? 144 LEU A CB    1 
ATOM   972  C  CG    . LEU A 1 144 ? 17.970  41.189  9.503   1.00 45.13  ? 144 LEU A CG    1 
ATOM   973  C  CD1   . LEU A 1 144 ? 17.789  39.678  9.549   1.00 46.07  ? 144 LEU A CD1   1 
ATOM   974  C  CD2   . LEU A 1 144 ? 19.094  41.627  10.404  1.00 43.06  ? 144 LEU A CD2   1 
ATOM   975  N  N     . ASP A 1 145 ? 17.868  42.114  5.150   1.00 55.20  ? 145 ASP A N     1 
ATOM   976  C  CA    . ASP A 1 145 ? 17.155  42.676  4.027   1.00 58.38  ? 145 ASP A CA    1 
ATOM   977  C  C     . ASP A 1 145 ? 16.808  41.626  2.984   1.00 61.99  ? 145 ASP A C     1 
ATOM   978  O  O     . ASP A 1 145 ? 15.744  41.680  2.365   1.00 64.16  ? 145 ASP A O     1 
ATOM   979  C  CB    . ASP A 1 145 ? 17.968  43.794  3.399   1.00 57.10  ? 145 ASP A CB    1 
ATOM   980  C  CG    . ASP A 1 145 ? 17.815  45.099  4.143   1.00 57.92  ? 145 ASP A CG    1 
ATOM   981  O  OD1   . ASP A 1 145 ? 16.743  45.297  4.755   1.00 57.91  ? 145 ASP A OD1   1 
ATOM   982  O  OD2   . ASP A 1 145 ? 18.750  45.932  4.106   1.00 57.17  ? 145 ASP A OD2   1 
ATOM   983  N  N     . GLU A 1 146 ? 17.691  40.656  2.794   1.00 64.65  ? 146 GLU A N     1 
ATOM   984  C  CA    . GLU A 1 146 ? 17.427  39.612  1.816   1.00 66.64  ? 146 GLU A CA    1 
ATOM   985  C  C     . GLU A 1 146 ? 16.299  38.684  2.273   1.00 65.16  ? 146 GLU A C     1 
ATOM   986  O  O     . GLU A 1 146 ? 15.421  38.334  1.487   1.00 63.34  ? 146 GLU A O     1 
ATOM   987  C  CB    . GLU A 1 146 ? 18.713  38.843  1.555   1.00 70.89  ? 146 GLU A CB    1 
ATOM   988  C  CG    . GLU A 1 146 ? 19.855  39.795  1.219   1.00 78.36  ? 146 GLU A CG    1 
ATOM   989  C  CD    . GLU A 1 146 ? 21.128  39.092  0.773   1.00 82.83  ? 146 GLU A CD    1 
ATOM   990  O  OE1   . GLU A 1 146 ? 21.085  38.396  -0.272  1.00 85.04  ? 146 GLU A OE1   1 
ATOM   991  O  OE2   . GLU A 1 146 ? 22.169  39.242  1.465   1.00 85.20  ? 146 GLU A OE2   1 
ATOM   992  N  N     . MET A 1 147 ? 16.307  38.310  3.548   1.00 65.08  ? 147 MET A N     1 
ATOM   993  C  CA    . MET A 1 147 ? 15.265  37.440  4.082   1.00 65.38  ? 147 MET A CA    1 
ATOM   994  C  C     . MET A 1 147 ? 13.902  38.104  3.964   1.00 66.10  ? 147 MET A C     1 
ATOM   995  O  O     . MET A 1 147 ? 12.904  37.453  3.664   1.00 65.80  ? 147 MET A O     1 
ATOM   996  C  CB    . MET A 1 147 ? 15.543  37.106  5.544   1.00 64.27  ? 147 MET A CB    1 
ATOM   997  C  CG    . MET A 1 147 ? 16.888  36.443  5.773   1.00 65.86  ? 147 MET A CG    1 
ATOM   998  S  SD    . MET A 1 147 ? 17.130  35.860  7.469   1.00 67.35  ? 147 MET A SD    1 
ATOM   999  C  CE    . MET A 1 147 ? 15.979  34.467  7.482   1.00 68.14  ? 147 MET A CE    1 
ATOM   1000 N  N     . ILE A 1 148 ? 13.865  39.408  4.194   1.00 67.43  ? 148 ILE A N     1 
ATOM   1001 C  CA    . ILE A 1 148 ? 12.615  40.147  4.120   1.00 69.70  ? 148 ILE A CA    1 
ATOM   1002 C  C     . ILE A 1 148 ? 11.902  40.008  2.776   1.00 72.01  ? 148 ILE A C     1 
ATOM   1003 O  O     . ILE A 1 148 ? 10.669  39.978  2.731   1.00 72.64  ? 148 ILE A O     1 
ATOM   1004 C  CB    . ILE A 1 148 ? 12.846  41.650  4.432   1.00 68.16  ? 148 ILE A CB    1 
ATOM   1005 C  CG1   . ILE A 1 148 ? 13.056  41.823  5.931   1.00 66.72  ? 148 ILE A CG1   1 
ATOM   1006 C  CG2   . ILE A 1 148 ? 11.655  42.494  3.980   1.00 66.95  ? 148 ILE A CG2   1 
ATOM   1007 C  CD1   . ILE A 1 148 ? 11.888  41.343  6.756   1.00 65.58  ? 148 ILE A CD1   1 
ATOM   1008 N  N     . LYS A 1 149 ? 12.670  39.916  1.690   1.00 74.27  ? 149 LYS A N     1 
ATOM   1009 C  CA    . LYS A 1 149 ? 12.096  39.801  0.347   1.00 76.05  ? 149 LYS A CA    1 
ATOM   1010 C  C     . LYS A 1 149 ? 11.239  38.553  0.148   1.00 77.78  ? 149 LYS A C     1 
ATOM   1011 O  O     . LYS A 1 149 ? 10.219  38.600  -0.534  1.00 77.72  ? 149 LYS A O     1 
ATOM   1012 C  CB    . LYS A 1 149 ? 13.202  39.837  -0.702  1.00 75.63  ? 149 LYS A CB    1 
ATOM   1013 C  CG    . LYS A 1 149 ? 14.014  41.124  -0.708  1.00 75.31  ? 149 LYS A CG    1 
ATOM   1014 C  CD    . LYS A 1 149 ? 15.131  41.027  -1.734  1.00 75.92  ? 149 LYS A CD    1 
ATOM   1015 C  CE    . LYS A 1 149 ? 16.078  42.205  -1.657  1.00 75.91  ? 149 LYS A CE    1 
ATOM   1016 N  NZ    . LYS A 1 149 ? 17.140  42.087  -2.695  1.00 76.66  ? 149 LYS A NZ    1 
ATOM   1017 N  N     . ASP A 1 150 ? 11.652  37.433  0.733   1.00 80.31  ? 150 ASP A N     1 
ATOM   1018 C  CA    . ASP A 1 150 ? 10.876  36.200  0.620   1.00 82.70  ? 150 ASP A CA    1 
ATOM   1019 C  C     . ASP A 1 150 ? 9.804   36.237  1.708   1.00 83.30  ? 150 ASP A C     1 
ATOM   1020 O  O     . ASP A 1 150 ? 10.119  36.272  2.896   1.00 83.03  ? 150 ASP A O     1 
ATOM   1021 C  CB    . ASP A 1 150 ? 11.776  34.979  0.818   1.00 84.66  ? 150 ASP A CB    1 
ATOM   1022 C  CG    . ASP A 1 150 ? 11.070  33.671  0.493   1.00 86.69  ? 150 ASP A CG    1 
ATOM   1023 O  OD1   . ASP A 1 150 ? 9.947   33.442  1.002   1.00 88.25  ? 150 ASP A OD1   1 
ATOM   1024 O  OD2   . ASP A 1 150 ? 11.646  32.868  -0.270  1.00 86.80  ? 150 ASP A OD2   1 
ATOM   1025 N  N     . GLU A 1 151 ? 8.541   36.231  1.296   1.00 84.60  ? 151 GLU A N     1 
ATOM   1026 C  CA    . GLU A 1 151 ? 7.422   36.295  2.232   1.00 85.60  ? 151 GLU A CA    1 
ATOM   1027 C  C     . GLU A 1 151 ? 7.335   35.096  3.175   1.00 83.60  ? 151 GLU A C     1 
ATOM   1028 O  O     . GLU A 1 151 ? 6.839   35.210  4.300   1.00 82.23  ? 151 GLU A O     1 
ATOM   1029 C  CB    . GLU A 1 151 ? 6.104   36.428  1.456   1.00 89.38  ? 151 GLU A CB    1 
ATOM   1030 N  N     . LYS A 1 152 ? 7.817   33.947  2.720   1.00 81.28  ? 152 LYS A N     1 
ATOM   1031 C  CA    . LYS A 1 152 ? 7.750   32.753  3.538   1.00 79.33  ? 152 LYS A CA    1 
ATOM   1032 C  C     . LYS A 1 152 ? 8.647   32.818  4.760   1.00 77.07  ? 152 LYS A C     1 
ATOM   1033 O  O     . LYS A 1 152 ? 8.498   32.015  5.676   1.00 77.37  ? 152 LYS A O     1 
ATOM   1034 C  CB    . LYS A 1 152 ? 8.071   31.517  2.691   1.00 81.44  ? 152 LYS A CB    1 
ATOM   1035 C  CG    . LYS A 1 152 ? 7.124   31.361  1.487   1.00 85.24  ? 152 LYS A CG    1 
ATOM   1036 C  CD    . LYS A 1 152 ? 6.832   29.892  1.119   1.00 86.44  ? 152 LYS A CD    1 
ATOM   1037 C  CE    . LYS A 1 152 ? 5.820   29.231  2.074   1.00 86.85  ? 152 LYS A CE    1 
ATOM   1038 N  NZ    . LYS A 1 152 ? 4.460   29.847  2.026   1.00 85.03  ? 152 LYS A NZ    1 
ATOM   1039 N  N     . ASN A 1 153 ? 9.571   33.775  4.780   1.00 74.36  ? 153 ASN A N     1 
ATOM   1040 C  CA    . ASN A 1 153 ? 10.482  33.942  5.912   1.00 71.81  ? 153 ASN A CA    1 
ATOM   1041 C  C     . ASN A 1 153 ? 9.826   34.722  7.052   1.00 69.30  ? 153 ASN A C     1 
ATOM   1042 O  O     . ASN A 1 153 ? 10.224  34.613  8.211   1.00 68.42  ? 153 ASN A O     1 
ATOM   1043 C  CB    . ASN A 1 153 ? 11.756  34.679  5.484   1.00 73.73  ? 153 ASN A CB    1 
ATOM   1044 C  CG    . ASN A 1 153 ? 12.712  33.802  4.703   1.00 74.21  ? 153 ASN A CG    1 
ATOM   1045 O  OD1   . ASN A 1 153 ? 13.055  32.700  5.132   1.00 75.27  ? 153 ASN A OD1   1 
ATOM   1046 N  ND2   . ASN A 1 153 ? 13.164  34.298  3.558   1.00 74.77  ? 153 ASN A ND2   1 
ATOM   1047 N  N     . HIS A 1 154 ? 8.821   35.517  6.719   1.00 66.93  ? 154 HIS A N     1 
ATOM   1048 C  CA    . HIS A 1 154 ? 8.134   36.306  7.726   1.00 64.16  ? 154 HIS A CA    1 
ATOM   1049 C  C     . HIS A 1 154 ? 7.557   35.413  8.803   1.00 62.11  ? 154 HIS A C     1 
ATOM   1050 O  O     . HIS A 1 154 ? 7.075   34.323  8.527   1.00 63.06  ? 154 HIS A O     1 
ATOM   1051 C  CB    . HIS A 1 154 ? 7.035   37.146  7.078   1.00 64.00  ? 154 HIS A CB    1 
ATOM   1052 C  CG    . HIS A 1 154 ? 7.558   38.187  6.140   1.00 64.30  ? 154 HIS A CG    1 
ATOM   1053 N  ND1   . HIS A 1 154 ? 6.904   39.377  5.910   1.00 64.67  ? 154 HIS A ND1   1 
ATOM   1054 C  CD2   . HIS A 1 154 ? 8.686   38.224  5.390   1.00 64.85  ? 154 HIS A CD2   1 
ATOM   1055 C  CE1   . HIS A 1 154 ? 7.609   40.105  5.060   1.00 66.37  ? 154 HIS A CE1   1 
ATOM   1056 N  NE2   . HIS A 1 154 ? 8.695   39.427  4.729   1.00 66.22  ? 154 HIS A NE2   1 
ATOM   1057 N  N     . GLY A 1 155 ? 7.625   35.879  10.038  1.00 59.70  ? 155 GLY A N     1 
ATOM   1058 C  CA    . GLY A 1 155 ? 7.115   35.105  11.149  1.00 56.98  ? 155 GLY A CA    1 
ATOM   1059 C  C     . GLY A 1 155 ? 7.617   33.671  11.246  1.00 55.56  ? 155 GLY A C     1 
ATOM   1060 O  O     . GLY A 1 155 ? 6.871   32.803  11.698  1.00 55.73  ? 155 GLY A O     1 
ATOM   1061 N  N     . SER A 1 156 ? 8.866   33.408  10.865  1.00 53.74  ? 156 SER A N     1 
ATOM   1062 C  CA    . SER A 1 156 ? 9.371   32.039  10.922  1.00 53.47  ? 156 SER A CA    1 
ATOM   1063 C  C     . SER A 1 156 ? 10.331  31.738  12.063  1.00 53.27  ? 156 SER A C     1 
ATOM   1064 O  O     . SER A 1 156 ? 10.858  30.621  12.152  1.00 53.04  ? 156 SER A O     1 
ATOM   1065 C  CB    . SER A 1 156 ? 10.052  31.667  9.605   1.00 53.62  ? 156 SER A CB    1 
ATOM   1066 O  OG    . SER A 1 156 ? 11.225  32.432  9.404   1.00 52.81  ? 156 SER A OG    1 
ATOM   1067 N  N     . TYR A 1 157 ? 10.565  32.726  12.925  1.00 52.46  ? 157 TYR A N     1 
ATOM   1068 C  CA    . TYR A 1 157 ? 11.476  32.560  14.055  1.00 50.64  ? 157 TYR A CA    1 
ATOM   1069 C  C     . TYR A 1 157 ? 10.750  32.659  15.373  1.00 50.72  ? 157 TYR A C     1 
ATOM   1070 O  O     . TYR A 1 157 ? 9.820   33.455  15.514  1.00 51.65  ? 157 TYR A O     1 
ATOM   1071 C  CB    . TYR A 1 157 ? 12.570  33.621  14.023  1.00 48.53  ? 157 TYR A CB    1 
ATOM   1072 C  CG    . TYR A 1 157 ? 13.541  33.449  12.887  1.00 48.85  ? 157 TYR A CG    1 
ATOM   1073 C  CD1   . TYR A 1 157 ? 13.292  33.995  11.634  1.00 49.14  ? 157 TYR A CD1   1 
ATOM   1074 C  CD2   . TYR A 1 157 ? 14.706  32.721  13.065  1.00 48.97  ? 157 TYR A CD2   1 
ATOM   1075 C  CE1   . TYR A 1 157 ? 14.187  33.815  10.600  1.00 50.56  ? 157 TYR A CE1   1 
ATOM   1076 C  CE2   . TYR A 1 157 ? 15.600  32.534  12.047  1.00 48.91  ? 157 TYR A CE2   1 
ATOM   1077 C  CZ    . TYR A 1 157 ? 15.344  33.079  10.819  1.00 51.42  ? 157 TYR A CZ    1 
ATOM   1078 O  OH    . TYR A 1 157 ? 16.271  32.888  9.822   1.00 54.37  ? 157 TYR A OH    1 
ATOM   1079 N  N     . ASP A 1 158 ? 11.181  31.855  16.341  1.00 50.13  ? 158 ASP A N     1 
ATOM   1080 C  CA    . ASP A 1 158 ? 10.569  31.861  17.661  1.00 49.21  ? 158 ASP A CA    1 
ATOM   1081 C  C     . ASP A 1 158 ? 11.315  32.809  18.556  1.00 47.45  ? 158 ASP A C     1 
ATOM   1082 O  O     . ASP A 1 158 ? 10.721  33.428  19.427  1.00 47.75  ? 158 ASP A O     1 
ATOM   1083 C  CB    . ASP A 1 158 ? 10.646  30.491  18.337  1.00 52.53  ? 158 ASP A CB    1 
ATOM   1084 C  CG    . ASP A 1 158 ? 10.117  29.381  17.484  1.00 54.89  ? 158 ASP A CG    1 
ATOM   1085 O  OD1   . ASP A 1 158 ? 9.043   29.563  16.863  1.00 56.26  ? 158 ASP A OD1   1 
ATOM   1086 O  OD2   . ASP A 1 158 ? 10.780  28.320  17.455  1.00 55.91  ? 158 ASP A OD2   1 
ATOM   1087 N  N     . PHE A 1 159 ? 12.626  32.896  18.352  1.00 45.80  ? 159 PHE A N     1 
ATOM   1088 C  CA    . PHE A 1 159 ? 13.488  33.731  19.185  1.00 45.39  ? 159 PHE A CA    1 
ATOM   1089 C  C     . PHE A 1 159 ? 14.621  34.389  18.378  1.00 45.76  ? 159 PHE A C     1 
ATOM   1090 O  O     . PHE A 1 159 ? 15.224  33.764  17.500  1.00 46.98  ? 159 PHE A O     1 
ATOM   1091 C  CB    . PHE A 1 159 ? 14.061  32.853  20.307  1.00 43.63  ? 159 PHE A CB    1 
ATOM   1092 C  CG    . PHE A 1 159 ? 14.954  33.577  21.258  1.00 42.18  ? 159 PHE A CG    1 
ATOM   1093 C  CD1   . PHE A 1 159 ? 14.443  34.526  22.121  1.00 41.28  ? 159 PHE A CD1   1 
ATOM   1094 C  CD2   . PHE A 1 159 ? 16.326  33.322  21.272  1.00 42.28  ? 159 PHE A CD2   1 
ATOM   1095 C  CE1   . PHE A 1 159 ? 15.285  35.221  22.993  1.00 41.88  ? 159 PHE A CE1   1 
ATOM   1096 C  CE2   . PHE A 1 159 ? 17.181  34.009  22.136  1.00 40.15  ? 159 PHE A CE2   1 
ATOM   1097 C  CZ    . PHE A 1 159 ? 16.661  34.959  22.996  1.00 41.86  ? 159 PHE A CZ    1 
ATOM   1098 N  N     . ILE A 1 160 ? 14.901  35.657  18.665  1.00 44.19  ? 160 ILE A N     1 
ATOM   1099 C  CA    . ILE A 1 160 ? 15.966  36.369  17.973  1.00 42.37  ? 160 ILE A CA    1 
ATOM   1100 C  C     . ILE A 1 160 ? 16.775  37.177  18.970  1.00 40.66  ? 160 ILE A C     1 
ATOM   1101 O  O     . ILE A 1 160 ? 16.265  38.099  19.596  1.00 41.87  ? 160 ILE A O     1 
ATOM   1102 C  CB    . ILE A 1 160 ? 15.406  37.327  16.893  1.00 41.87  ? 160 ILE A CB    1 
ATOM   1103 C  CG1   . ILE A 1 160 ? 14.695  36.519  15.810  1.00 43.48  ? 160 ILE A CG1   1 
ATOM   1104 C  CG2   . ILE A 1 160 ? 16.538  38.134  16.267  1.00 40.67  ? 160 ILE A CG2   1 
ATOM   1105 C  CD1   . ILE A 1 160 ? 14.027  37.358  14.700  1.00 43.33  ? 160 ILE A CD1   1 
ATOM   1106 N  N     . PHE A 1 161 ? 18.045  36.835  19.111  1.00 39.23  ? 161 PHE A N     1 
ATOM   1107 C  CA    . PHE A 1 161 ? 18.910  37.543  20.041  1.00 38.12  ? 161 PHE A CA    1 
ATOM   1108 C  C     . PHE A 1 161 ? 19.799  38.524  19.285  1.00 37.62  ? 161 PHE A C     1 
ATOM   1109 O  O     . PHE A 1 161 ? 20.494  38.147  18.353  1.00 37.90  ? 161 PHE A O     1 
ATOM   1110 C  CB    . PHE A 1 161 ? 19.769  36.545  20.803  1.00 37.16  ? 161 PHE A CB    1 
ATOM   1111 C  CG    . PHE A 1 161 ? 20.483  37.134  21.971  1.00 38.25  ? 161 PHE A CG    1 
ATOM   1112 C  CD1   . PHE A 1 161 ? 19.787  37.817  22.947  1.00 38.73  ? 161 PHE A CD1   1 
ATOM   1113 C  CD2   . PHE A 1 161 ? 21.850  36.954  22.131  1.00 39.76  ? 161 PHE A CD2   1 
ATOM   1114 C  CE1   . PHE A 1 161 ? 20.447  38.316  24.081  1.00 41.60  ? 161 PHE A CE1   1 
ATOM   1115 C  CE2   . PHE A 1 161 ? 22.517  37.446  23.261  1.00 41.11  ? 161 PHE A CE2   1 
ATOM   1116 C  CZ    . PHE A 1 161 ? 21.816  38.127  24.235  1.00 40.17  ? 161 PHE A CZ    1 
ATOM   1117 N  N     . VAL A 1 162 ? 19.771  39.785  19.694  1.00 37.08  ? 162 VAL A N     1 
ATOM   1118 C  CA    . VAL A 1 162 ? 20.568  40.820  19.062  1.00 37.02  ? 162 VAL A CA    1 
ATOM   1119 C  C     . VAL A 1 162 ? 21.585  41.332  20.073  1.00 38.07  ? 162 VAL A C     1 
ATOM   1120 O  O     . VAL A 1 162 ? 21.229  42.035  21.013  1.00 37.09  ? 162 VAL A O     1 
ATOM   1121 C  CB    . VAL A 1 162 ? 19.676  42.002  18.598  1.00 36.97  ? 162 VAL A CB    1 
ATOM   1122 C  CG1   . VAL A 1 162 ? 20.497  43.033  17.871  1.00 36.99  ? 162 VAL A CG1   1 
ATOM   1123 C  CG2   . VAL A 1 162 ? 18.587  41.502  17.704  1.00 37.01  ? 162 VAL A CG2   1 
ATOM   1124 N  N     . ASP A 1 163 ? 22.849  40.963  19.874  1.00 39.72  ? 163 ASP A N     1 
ATOM   1125 C  CA    . ASP A 1 163 ? 23.939  41.382  20.753  1.00 42.26  ? 163 ASP A CA    1 
ATOM   1126 C  C     . ASP A 1 163 ? 25.085  41.809  19.836  1.00 43.33  ? 163 ASP A C     1 
ATOM   1127 O  O     . ASP A 1 163 ? 26.194  41.316  19.957  1.00 43.97  ? 163 ASP A O     1 
ATOM   1128 C  CB    . ASP A 1 163 ? 24.376  40.206  21.658  1.00 41.50  ? 163 ASP A CB    1 
ATOM   1129 C  CG    . ASP A 1 163 ? 25.207  40.651  22.863  1.00 43.43  ? 163 ASP A CG    1 
ATOM   1130 O  OD1   . ASP A 1 163 ? 25.230  41.845  23.207  1.00 44.86  ? 163 ASP A OD1   1 
ATOM   1131 O  OD2   . ASP A 1 163 ? 25.833  39.794  23.505  1.00 47.62  ? 163 ASP A OD2   1 
ATOM   1132 N  N     . ALA A 1 164 ? 24.811  42.725  18.915  1.00 45.28  ? 164 ALA A N     1 
ATOM   1133 C  CA    . ALA A 1 164 ? 25.828  43.177  17.975  1.00 47.24  ? 164 ALA A CA    1 
ATOM   1134 C  C     . ALA A 1 164 ? 26.047  44.680  18.039  1.00 48.75  ? 164 ALA A C     1 
ATOM   1135 O  O     . ALA A 1 164 ? 26.116  45.243  19.117  1.00 49.53  ? 164 ALA A O     1 
ATOM   1136 C  CB    . ALA A 1 164 ? 25.436  42.767  16.568  1.00 46.31  ? 164 ALA A CB    1 
ATOM   1137 N  N     . ASP A 1 165 ? 26.153  45.317  16.875  1.00 51.17  ? 165 ASP A N     1 
ATOM   1138 C  CA    . ASP A 1 165 ? 26.370  46.759  16.748  1.00 52.78  ? 165 ASP A CA    1 
ATOM   1139 C  C     . ASP A 1 165 ? 25.925  47.654  17.889  1.00 55.39  ? 165 ASP A C     1 
ATOM   1140 O  O     . ASP A 1 165 ? 26.686  47.901  18.834  1.00 59.51  ? 165 ASP A O     1 
ATOM   1141 C  CB    . ASP A 1 165 ? 25.698  47.264  15.498  1.00 52.04  ? 165 ASP A CB    1 
ATOM   1142 C  CG    . ASP A 1 165 ? 26.096  46.481  14.291  1.00 51.88  ? 165 ASP A CG    1 
ATOM   1143 O  OD1   . ASP A 1 165 ? 25.628  45.330  14.186  1.00 50.23  ? 165 ASP A OD1   1 
ATOM   1144 O  OD2   . ASP A 1 165 ? 26.877  47.011  13.465  1.00 50.57  ? 165 ASP A OD2   1 
ATOM   1145 N  N     . LYS A 1 166 ? 24.702  48.165  17.774  1.00 54.93  ? 166 LYS A N     1 
ATOM   1146 C  CA    . LYS A 1 166 ? 24.103  49.070  18.771  1.00 54.91  ? 166 LYS A CA    1 
ATOM   1147 C  C     . LYS A 1 166 ? 23.569  50.232  17.957  1.00 54.42  ? 166 LYS A C     1 
ATOM   1148 O  O     . LYS A 1 166 ? 22.382  50.572  18.036  1.00 51.77  ? 166 LYS A O     1 
ATOM   1149 C  CB    . LYS A 1 166 ? 25.138  49.586  19.767  1.00 54.27  ? 166 LYS A CB    1 
ATOM   1150 C  CG    . LYS A 1 166 ? 24.668  49.574  21.193  1.00 56.65  ? 166 LYS A CG    1 
ATOM   1151 C  CD    . LYS A 1 166 ? 24.411  48.156  21.682  1.00 60.64  ? 166 LYS A CD    1 
ATOM   1152 C  CE    . LYS A 1 166 ? 25.701  47.346  21.861  1.00 63.17  ? 166 LYS A CE    1 
ATOM   1153 N  NZ    . LYS A 1 166 ? 25.460  45.953  22.402  1.00 63.33  ? 166 LYS A NZ    1 
ATOM   1154 N  N     . ASP A 1 167 ? 24.456  50.824  17.155  1.00 53.53  ? 167 ASP A N     1 
ATOM   1155 C  CA    . ASP A 1 167 ? 24.057  51.914  16.286  1.00 52.71  ? 167 ASP A CA    1 
ATOM   1156 C  C     . ASP A 1 167 ? 23.332  51.311  15.092  1.00 51.37  ? 167 ASP A C     1 
ATOM   1157 O  O     . ASP A 1 167 ? 23.098  51.983  14.092  1.00 51.12  ? 167 ASP A O     1 
ATOM   1158 C  CB    . ASP A 1 167 ? 25.264  52.750  15.847  1.00 53.18  ? 167 ASP A CB    1 
ATOM   1159 C  CG    . ASP A 1 167 ? 26.347  51.925  15.193  1.00 56.19  ? 167 ASP A CG    1 
ATOM   1160 O  OD1   . ASP A 1 167 ? 26.511  50.748  15.572  1.00 55.67  ? 167 ASP A OD1   1 
ATOM   1161 O  OD2   . ASP A 1 167 ? 27.051  52.464  14.312  1.00 57.18  ? 167 ASP A OD2   1 
ATOM   1162 N  N     . ASN A 1 168 ? 22.964  50.036  15.219  1.00 50.26  ? 168 ASN A N     1 
ATOM   1163 C  CA    . ASN A 1 168 ? 22.221  49.332  14.178  1.00 49.78  ? 168 ASN A CA    1 
ATOM   1164 C  C     . ASN A 1 168 ? 20.980  48.596  14.689  1.00 49.55  ? 168 ASN A C     1 
ATOM   1165 O  O     . ASN A 1 168 ? 20.275  47.964  13.904  1.00 49.79  ? 168 ASN A O     1 
ATOM   1166 C  CB    . ASN A 1 168 ? 23.108  48.324  13.460  1.00 49.55  ? 168 ASN A CB    1 
ATOM   1167 C  CG    . ASN A 1 168 ? 23.613  48.839  12.139  1.00 49.27  ? 168 ASN A CG    1 
ATOM   1168 O  OD1   . ASN A 1 168 ? 22.834  49.270  11.291  1.00 49.05  ? 168 ASN A OD1   1 
ATOM   1169 N  ND2   . ASN A 1 168 ? 24.926  48.795  11.950  1.00 49.87  ? 168 ASN A ND2   1 
ATOM   1170 N  N     . TYR A 1 169 ? 20.706  48.678  15.991  1.00 48.47  ? 169 TYR A N     1 
ATOM   1171 C  CA    . TYR A 1 169 ? 19.557  47.984  16.575  1.00 46.03  ? 169 TYR A CA    1 
ATOM   1172 C  C     . TYR A 1 169 ? 18.225  48.444  16.000  1.00 44.17  ? 169 TYR A C     1 
ATOM   1173 O  O     . TYR A 1 169 ? 17.383  47.633  15.648  1.00 43.37  ? 169 TYR A O     1 
ATOM   1174 C  CB    . TYR A 1 169 ? 19.563  48.154  18.098  1.00 47.56  ? 169 TYR A CB    1 
ATOM   1175 C  CG    . TYR A 1 169 ? 20.561  47.266  18.826  1.00 48.74  ? 169 TYR A CG    1 
ATOM   1176 C  CD1   . TYR A 1 169 ? 21.734  46.845  18.204  1.00 49.08  ? 169 TYR A CD1   1 
ATOM   1177 C  CD2   . TYR A 1 169 ? 20.346  46.875  20.149  1.00 49.07  ? 169 TYR A CD2   1 
ATOM   1178 C  CE1   . TYR A 1 169 ? 22.666  46.064  18.872  1.00 49.43  ? 169 TYR A CE1   1 
ATOM   1179 C  CE2   . TYR A 1 169 ? 21.278  46.096  20.826  1.00 49.20  ? 169 TYR A CE2   1 
ATOM   1180 C  CZ    . TYR A 1 169 ? 22.434  45.700  20.177  1.00 50.12  ? 169 TYR A CZ    1 
ATOM   1181 O  OH    . TYR A 1 169 ? 23.379  44.962  20.840  1.00 53.08  ? 169 TYR A OH    1 
ATOM   1182 N  N     . LEU A 1 170 ? 18.040  49.752  15.906  1.00 44.42  ? 170 LEU A N     1 
ATOM   1183 C  CA    . LEU A 1 170 ? 16.814  50.319  15.367  1.00 43.37  ? 170 LEU A CA    1 
ATOM   1184 C  C     . LEU A 1 170 ? 16.644  49.831  13.949  1.00 43.37  ? 170 LEU A C     1 
ATOM   1185 O  O     . LEU A 1 170 ? 15.535  49.569  13.509  1.00 42.36  ? 170 LEU A O     1 
ATOM   1186 C  CB    . LEU A 1 170 ? 16.897  51.841  15.371  1.00 45.95  ? 170 LEU A CB    1 
ATOM   1187 C  CG    . LEU A 1 170 ? 15.837  52.570  16.186  1.00 47.90  ? 170 LEU A CG    1 
ATOM   1188 C  CD1   . LEU A 1 170 ? 14.459  52.223  15.643  1.00 52.11  ? 170 LEU A CD1   1 
ATOM   1189 C  CD2   . LEU A 1 170 ? 15.939  52.165  17.639  1.00 49.62  ? 170 LEU A CD2   1 
ATOM   1190 N  N     . ASN A 1 171 ? 17.751  49.727  13.222  1.00 44.35  ? 171 ASN A N     1 
ATOM   1191 C  CA    . ASN A 1 171 ? 17.685  49.249  11.853  1.00 45.48  ? 171 ASN A CA    1 
ATOM   1192 C  C     . ASN A 1 171 ? 17.315  47.785  11.811  1.00 45.82  ? 171 ASN A C     1 
ATOM   1193 O  O     . ASN A 1 171 ? 16.523  47.381  10.964  1.00 47.37  ? 171 ASN A O     1 
ATOM   1194 C  CB    . ASN A 1 171 ? 19.004  49.461  11.119  1.00 46.31  ? 171 ASN A CB    1 
ATOM   1195 C  CG    . ASN A 1 171 ? 19.282  50.918  10.849  1.00 46.53  ? 171 ASN A CG    1 
ATOM   1196 O  OD1   . ASN A 1 171 ? 18.359  51.714  10.636  1.00 46.53  ? 171 ASN A OD1   1 
ATOM   1197 N  ND2   . ASN A 1 171 ? 20.558  51.279  10.843  1.00 48.04  ? 171 ASN A ND2   1 
ATOM   1198 N  N     . TYR A 1 172 ? 17.888  46.988  12.713  1.00 45.25  ? 172 TYR A N     1 
ATOM   1199 C  CA    . TYR A 1 172 ? 17.571  45.565  12.773  1.00 44.62  ? 172 TYR A CA    1 
ATOM   1200 C  C     . TYR A 1 172 ? 16.087  45.413  13.063  1.00 45.70  ? 172 TYR A C     1 
ATOM   1201 O  O     . TYR A 1 172 ? 15.373  44.683  12.366  1.00 45.19  ? 172 TYR A O     1 
ATOM   1202 C  CB    . TYR A 1 172 ? 18.372  44.878  13.875  1.00 43.54  ? 172 TYR A CB    1 
ATOM   1203 C  CG    . TYR A 1 172 ? 19.837  44.802  13.574  1.00 43.58  ? 172 TYR A CG    1 
ATOM   1204 C  CD1   . TYR A 1 172 ? 20.283  44.377  12.320  1.00 44.87  ? 172 TYR A CD1   1 
ATOM   1205 C  CD2   . TYR A 1 172 ? 20.784  45.155  14.528  1.00 43.87  ? 172 TYR A CD2   1 
ATOM   1206 C  CE1   . TYR A 1 172 ? 21.637  44.307  12.018  1.00 45.69  ? 172 TYR A CE1   1 
ATOM   1207 C  CE2   . TYR A 1 172 ? 22.151  45.094  14.239  1.00 46.39  ? 172 TYR A CE2   1 
ATOM   1208 C  CZ    . TYR A 1 172 ? 22.569  44.670  12.979  1.00 47.69  ? 172 TYR A CZ    1 
ATOM   1209 O  OH    . TYR A 1 172 ? 23.910  44.633  12.668  1.00 49.67  ? 172 TYR A OH    1 
ATOM   1210 N  N     . HIS A 1 173 ? 15.629  46.124  14.091  1.00 45.78  ? 173 HIS A N     1 
ATOM   1211 C  CA    . HIS A 1 173 ? 14.234  46.091  14.500  1.00 46.67  ? 173 HIS A CA    1 
ATOM   1212 C  C     . HIS A 1 173 ? 13.255  46.292  13.341  1.00 46.97  ? 173 HIS A C     1 
ATOM   1213 O  O     . HIS A 1 173 ? 12.236  45.612  13.268  1.00 46.96  ? 173 HIS A O     1 
ATOM   1214 C  CB    . HIS A 1 173 ? 13.981  47.144  15.576  1.00 46.68  ? 173 HIS A CB    1 
ATOM   1215 C  CG    . HIS A 1 173 ? 12.701  46.944  16.322  1.00 47.28  ? 173 HIS A CG    1 
ATOM   1216 N  ND1   . HIS A 1 173 ? 12.399  45.768  16.972  1.00 49.31  ? 173 HIS A ND1   1 
ATOM   1217 C  CD2   . HIS A 1 173 ? 11.645  47.766  16.519  1.00 47.12  ? 173 HIS A CD2   1 
ATOM   1218 C  CE1   . HIS A 1 173 ? 11.211  45.872  17.537  1.00 49.98  ? 173 HIS A CE1   1 
ATOM   1219 N  NE2   . HIS A 1 173 ? 10.732  47.075  17.276  1.00 49.86  ? 173 HIS A NE2   1 
ATOM   1220 N  N     . LYS A 1 174 ? 13.551  47.226  12.443  1.00 47.99  ? 174 LYS A N     1 
ATOM   1221 C  CA    . LYS A 1 174 ? 12.670  47.470  11.305  1.00 49.12  ? 174 LYS A CA    1 
ATOM   1222 C  C     . LYS A 1 174 ? 12.318  46.178  10.588  1.00 48.17  ? 174 LYS A C     1 
ATOM   1223 O  O     . LYS A 1 174 ? 11.157  45.974  10.233  1.00 48.40  ? 174 LYS A O     1 
ATOM   1224 C  CB    . LYS A 1 174 ? 13.304  48.462  10.326  1.00 50.72  ? 174 LYS A CB    1 
ATOM   1225 C  CG    . LYS A 1 174 ? 12.991  49.890  10.676  1.00 57.05  ? 174 LYS A CG    1 
ATOM   1226 C  CD    . LYS A 1 174 ? 13.963  50.894  10.045  1.00 62.65  ? 174 LYS A CD    1 
ATOM   1227 C  CE    . LYS A 1 174 ? 13.631  52.341  10.487  1.00 64.51  ? 174 LYS A CE    1 
ATOM   1228 N  NZ    . LYS A 1 174 ? 13.592  52.539  11.986  1.00 65.12  ? 174 LYS A NZ    1 
ATOM   1229 N  N     . ARG A 1 175 ? 13.307  45.310  10.377  1.00 47.28  ? 175 ARG A N     1 
ATOM   1230 C  CA    . ARG A 1 175 ? 13.043  44.043  9.707   1.00 48.39  ? 175 ARG A CA    1 
ATOM   1231 C  C     . ARG A 1 175 ? 12.917  42.856  10.643  1.00 47.73  ? 175 ARG A C     1 
ATOM   1232 O  O     . ARG A 1 175 ? 12.240  41.880  10.320  1.00 48.83  ? 175 ARG A O     1 
ATOM   1233 C  CB    . ARG A 1 175 ? 14.096  43.725  8.636   1.00 48.71  ? 175 ARG A CB    1 
ATOM   1234 C  CG    . ARG A 1 175 ? 15.427  44.389  8.808   1.00 50.75  ? 175 ARG A CG    1 
ATOM   1235 C  CD    . ARG A 1 175 ? 15.379  45.856  8.433   1.00 48.90  ? 175 ARG A CD    1 
ATOM   1236 N  NE    . ARG A 1 175 ? 16.216  46.149  7.276   1.00 48.78  ? 175 ARG A NE    1 
ATOM   1237 C  CZ    . ARG A 1 175 ? 16.839  47.309  7.080   1.00 48.21  ? 175 ARG A CZ    1 
ATOM   1238 N  NH1   . ARG A 1 175 ? 16.725  48.291  7.965   1.00 49.45  ? 175 ARG A NH1   1 
ATOM   1239 N  NH2   . ARG A 1 175 ? 17.581  47.491  6.001   1.00 46.88  ? 175 ARG A NH2   1 
ATOM   1240 N  N     . LEU A 1 176 ? 13.555  42.912  11.802  1.00 47.08  ? 176 LEU A N     1 
ATOM   1241 C  CA    . LEU A 1 176 ? 13.433  41.786  12.723  1.00 46.41  ? 176 LEU A CA    1 
ATOM   1242 C  C     . LEU A 1 176 ? 11.977  41.586  13.128  1.00 46.43  ? 176 LEU A C     1 
ATOM   1243 O  O     . LEU A 1 176 ? 11.550  40.460  13.297  1.00 46.05  ? 176 LEU A O     1 
ATOM   1244 C  CB    . LEU A 1 176 ? 14.297  42.001  13.966  1.00 43.89  ? 176 LEU A CB    1 
ATOM   1245 C  CG    . LEU A 1 176 ? 15.544  41.128  14.139  1.00 43.02  ? 176 LEU A CG    1 
ATOM   1246 C  CD1   . LEU A 1 176 ? 16.016  40.554  12.805  1.00 41.54  ? 176 LEU A CD1   1 
ATOM   1247 C  CD2   . LEU A 1 176 ? 16.633  41.962  14.797  1.00 41.03  ? 176 LEU A CD2   1 
ATOM   1248 N  N     . ILE A 1 177 ? 11.220  42.678  13.240  1.00 47.02  ? 177 ILE A N     1 
ATOM   1249 C  CA    . ILE A 1 177 ? 9.814   42.639  13.644  1.00 48.27  ? 177 ILE A CA    1 
ATOM   1250 C  C     . ILE A 1 177 ? 8.878   41.866  12.727  1.00 50.10  ? 177 ILE A C     1 
ATOM   1251 O  O     . ILE A 1 177 ? 7.809   41.440  13.164  1.00 49.91  ? 177 ILE A O     1 
ATOM   1252 C  CB    . ILE A 1 177 ? 9.220   44.047  13.771  1.00 48.95  ? 177 ILE A CB    1 
ATOM   1253 C  CG1   . ILE A 1 177 ? 7.922   43.981  14.569  1.00 48.66  ? 177 ILE A CG1   1 
ATOM   1254 C  CG2   . ILE A 1 177 ? 8.923   44.624  12.386  1.00 47.59  ? 177 ILE A CG2   1 
ATOM   1255 C  CD1   . ILE A 1 177 ? 8.128   43.526  15.982  1.00 49.19  ? 177 ILE A CD1   1 
ATOM   1256 N  N     . ASP A 1 178 ? 9.246   41.723  11.456  1.00 51.02  ? 178 ASP A N     1 
ATOM   1257 C  CA    . ASP A 1 178 ? 8.416   40.974  10.516  1.00 52.13  ? 178 ASP A CA    1 
ATOM   1258 C  C     . ASP A 1 178 ? 8.891   39.529  10.438  1.00 51.67  ? 178 ASP A C     1 
ATOM   1259 O  O     . ASP A 1 178 ? 8.158   38.647  9.991   1.00 52.14  ? 178 ASP A O     1 
ATOM   1260 C  CB    . ASP A 1 178 ? 8.442   41.610  9.116   1.00 54.64  ? 178 ASP A CB    1 
ATOM   1261 C  CG    . ASP A 1 178 ? 7.459   42.779  8.974   1.00 59.14  ? 178 ASP A CG    1 
ATOM   1262 O  OD1   . ASP A 1 178 ? 6.281   42.635  9.394   1.00 60.01  ? 178 ASP A OD1   1 
ATOM   1263 O  OD2   . ASP A 1 178 ? 7.857   43.839  8.427   1.00 59.69  ? 178 ASP A OD2   1 
ATOM   1264 N  N     . LEU A 1 179 ? 10.122  39.293  10.883  1.00 50.93  ? 179 LEU A N     1 
ATOM   1265 C  CA    . LEU A 1 179 ? 10.705  37.961  10.875  1.00 49.69  ? 179 LEU A CA    1 
ATOM   1266 C  C     . LEU A 1 179 ? 10.388  37.195  12.158  1.00 50.90  ? 179 LEU A C     1 
ATOM   1267 O  O     . LEU A 1 179 ? 10.418  35.969  12.175  1.00 51.11  ? 179 LEU A O     1 
ATOM   1268 C  CB    . LEU A 1 179 ? 12.212  38.060  10.700  1.00 47.84  ? 179 LEU A CB    1 
ATOM   1269 C  CG    . LEU A 1 179 ? 12.699  38.652  9.384   1.00 44.21  ? 179 LEU A CG    1 
ATOM   1270 C  CD1   . LEU A 1 179 ? 14.209  38.773  9.410   1.00 41.68  ? 179 LEU A CD1   1 
ATOM   1271 C  CD2   . LEU A 1 179 ? 12.267  37.765  8.244   1.00 44.26  ? 179 LEU A CD2   1 
ATOM   1272 N  N     . VAL A 1 180 ? 10.128  37.918  13.242  1.00 53.19  ? 180 VAL A N     1 
ATOM   1273 C  CA    . VAL A 1 180 ? 9.739   37.276  14.499  1.00 54.48  ? 180 VAL A CA    1 
ATOM   1274 C  C     . VAL A 1 180 ? 8.308   36.908  14.210  1.00 56.85  ? 180 VAL A C     1 
ATOM   1275 O  O     . VAL A 1 180 ? 7.591   37.689  13.590  1.00 60.64  ? 180 VAL A O     1 
ATOM   1276 C  CB    . VAL A 1 180 ? 9.559   38.242  15.682  1.00 53.85  ? 180 VAL A CB    1 
ATOM   1277 C  CG1   . VAL A 1 180 ? 10.036  37.589  16.927  1.00 54.52  ? 180 VAL A CG1   1 
ATOM   1278 C  CG2   . VAL A 1 180 ? 10.209  39.579  15.427  1.00 55.77  ? 180 VAL A CG2   1 
ATOM   1279 N  N     . LYS A 1 181 ? 7.846   35.763  14.661  1.00 56.77  ? 181 LYS A N     1 
ATOM   1280 C  CA    . LYS A 1 181 ? 6.446   35.486  14.426  1.00 57.57  ? 181 LYS A CA    1 
ATOM   1281 C  C     . LYS A 1 181 ? 5.718   36.003  15.670  1.00 56.82  ? 181 LYS A C     1 
ATOM   1282 O  O     . LYS A 1 181 ? 6.360   36.240  16.692  1.00 56.31  ? 181 LYS A O     1 
ATOM   1283 C  CB    . LYS A 1 181 ? 6.245   33.992  14.230  1.00 59.46  ? 181 LYS A CB    1 
ATOM   1284 C  CG    . LYS A 1 181 ? 5.860   33.230  15.461  1.00 60.78  ? 181 LYS A CG    1 
ATOM   1285 C  CD    . LYS A 1 181 ? 6.953   33.189  16.487  1.00 62.76  ? 181 LYS A CD    1 
ATOM   1286 C  CE    . LYS A 1 181 ? 6.744   31.987  17.396  1.00 63.82  ? 181 LYS A CE    1 
ATOM   1287 N  NZ    . LYS A 1 181 ? 6.846   30.725  16.604  1.00 64.35  ? 181 LYS A NZ    1 
ATOM   1288 N  N     . VAL A 1 182 ? 4.405   36.193  15.595  1.00 55.79  ? 182 VAL A N     1 
ATOM   1289 C  CA    . VAL A 1 182 ? 3.658   36.712  16.740  1.00 55.70  ? 182 VAL A CA    1 
ATOM   1290 C  C     . VAL A 1 182 ? 4.006   36.088  18.085  1.00 55.45  ? 182 VAL A C     1 
ATOM   1291 O  O     . VAL A 1 182 ? 3.951   36.768  19.110  1.00 54.07  ? 182 VAL A O     1 
ATOM   1292 C  CB    . VAL A 1 182 ? 2.182   36.570  16.521  1.00 57.44  ? 182 VAL A CB    1 
ATOM   1293 C  CG1   . VAL A 1 182 ? 1.704   37.635  15.535  1.00 55.69  ? 182 VAL A CG1   1 
ATOM   1294 C  CG2   . VAL A 1 182 ? 1.892   35.159  16.016  1.00 60.57  ? 182 VAL A CG2   1 
ATOM   1295 N  N     . GLY A 1 183 ? 4.339   34.796  18.096  1.00 56.03  ? 183 GLY A N     1 
ATOM   1296 C  CA    . GLY A 1 183 ? 4.747   34.159  19.349  1.00 53.81  ? 183 GLY A CA    1 
ATOM   1297 C  C     . GLY A 1 183 ? 5.643   35.184  20.017  1.00 50.68  ? 183 GLY A C     1 
ATOM   1298 O  O     . GLY A 1 183 ? 5.445   35.536  21.177  1.00 50.09  ? 183 GLY A O     1 
ATOM   1299 N  N     . GLY A 1 184 ? 6.640   35.649  19.266  1.00 48.29  ? 184 GLY A N     1 
ATOM   1300 C  CA    . GLY A 1 184 ? 7.489   36.721  19.744  1.00 47.76  ? 184 GLY A CA    1 
ATOM   1301 C  C     . GLY A 1 184 ? 8.866   36.519  20.307  1.00 46.49  ? 184 GLY A C     1 
ATOM   1302 O  O     . GLY A 1 184 ? 9.558   35.556  20.039  1.00 48.67  ? 184 GLY A O     1 
ATOM   1303 N  N     . VAL A 1 185 ? 9.258   37.492  21.103  1.00 46.50  ? 185 VAL A N     1 
ATOM   1304 C  CA    . VAL A 1 185 ? 10.555  37.518  21.757  1.00 45.70  ? 185 VAL A CA    1 
ATOM   1305 C  C     . VAL A 1 185 ? 11.748  37.793  20.846  1.00 44.99  ? 185 VAL A C     1 
ATOM   1306 O  O     . VAL A 1 185 ? 12.129  36.994  19.983  1.00 44.94  ? 185 VAL A O     1 
ATOM   1307 C  CB    . VAL A 1 185 ? 10.830  36.254  22.556  1.00 44.26  ? 185 VAL A CB    1 
ATOM   1308 C  CG1   . VAL A 1 185 ? 12.101  36.445  23.332  1.00 45.03  ? 185 VAL A CG1   1 
ATOM   1309 C  CG2   . VAL A 1 185 ? 9.696   35.984  23.513  1.00 43.58  ? 185 VAL A CG2   1 
ATOM   1310 N  N     . ILE A 1 186 ? 12.299  38.978  21.064  1.00 42.90  ? 186 ILE A N     1 
ATOM   1311 C  CA    . ILE A 1 186 ? 13.456  39.490  20.374  1.00 41.21  ? 186 ILE A CA    1 
ATOM   1312 C  C     . ILE A 1 186 ? 14.224  40.044  21.555  1.00 40.76  ? 186 ILE A C     1 
ATOM   1313 O  O     . ILE A 1 186 ? 13.662  40.777  22.364  1.00 40.59  ? 186 ILE A O     1 
ATOM   1314 C  CB    . ILE A 1 186 ? 13.086  40.662  19.436  1.00 40.40  ? 186 ILE A CB    1 
ATOM   1315 C  CG1   . ILE A 1 186 ? 12.256  40.153  18.272  1.00 39.01  ? 186 ILE A CG1   1 
ATOM   1316 C  CG2   . ILE A 1 186 ? 14.346  41.357  18.916  1.00 38.42  ? 186 ILE A CG2   1 
ATOM   1317 C  CD1   . ILE A 1 186 ? 11.922  41.233  17.313  1.00 38.77  ? 186 ILE A CD1   1 
ATOM   1318 N  N     . GLY A 1 187 ? 15.492  39.704  21.682  1.00 39.20  ? 187 GLY A N     1 
ATOM   1319 C  CA    . GLY A 1 187 ? 16.202  40.230  22.817  1.00 40.60  ? 187 GLY A CA    1 
ATOM   1320 C  C     . GLY A 1 187 ? 17.285  41.199  22.440  1.00 42.49  ? 187 GLY A C     1 
ATOM   1321 O  O     . GLY A 1 187 ? 18.173  40.850  21.671  1.00 43.39  ? 187 GLY A O     1 
ATOM   1322 N  N     . TYR A 1 188 ? 17.210  42.419  22.963  1.00 43.13  ? 188 TYR A N     1 
ATOM   1323 C  CA    . TYR A 1 188 ? 18.241  43.415  22.701  1.00 43.74  ? 188 TYR A CA    1 
ATOM   1324 C  C     . TYR A 1 188 ? 19.160  43.466  23.930  1.00 44.72  ? 188 TYR A C     1 
ATOM   1325 O  O     . TYR A 1 188 ? 18.717  43.704  25.062  1.00 45.70  ? 188 TYR A O     1 
ATOM   1326 C  CB    . TYR A 1 188 ? 17.610  44.774  22.419  1.00 43.99  ? 188 TYR A CB    1 
ATOM   1327 C  CG    . TYR A 1 188 ? 16.898  44.806  21.096  1.00 46.70  ? 188 TYR A CG    1 
ATOM   1328 C  CD1   . TYR A 1 188 ? 17.608  44.798  19.902  1.00 48.72  ? 188 TYR A CD1   1 
ATOM   1329 C  CD2   . TYR A 1 188 ? 15.507  44.772  21.032  1.00 48.32  ? 188 TYR A CD2   1 
ATOM   1330 C  CE1   . TYR A 1 188 ? 16.946  44.747  18.669  1.00 50.14  ? 188 TYR A CE1   1 
ATOM   1331 C  CE2   . TYR A 1 188 ? 14.834  44.723  19.808  1.00 48.73  ? 188 TYR A CE2   1 
ATOM   1332 C  CZ    . TYR A 1 188 ? 15.555  44.709  18.632  1.00 49.73  ? 188 TYR A CZ    1 
ATOM   1333 O  OH    . TYR A 1 188 ? 14.886  44.655  17.429  1.00 48.88  ? 188 TYR A OH    1 
ATOM   1334 N  N     . ASP A 1 189 ? 20.444  43.231  23.698  1.00 44.17  ? 189 ASP A N     1 
ATOM   1335 C  CA    . ASP A 1 189 ? 21.416  43.202  24.766  1.00 43.85  ? 189 ASP A CA    1 
ATOM   1336 C  C     . ASP A 1 189 ? 22.144  44.503  25.053  1.00 43.95  ? 189 ASP A C     1 
ATOM   1337 O  O     . ASP A 1 189 ? 22.360  45.325  24.164  1.00 43.17  ? 189 ASP A O     1 
ATOM   1338 C  CB    . ASP A 1 189 ? 22.428  42.107  24.468  1.00 46.25  ? 189 ASP A CB    1 
ATOM   1339 C  CG    . ASP A 1 189 ? 22.801  41.336  25.691  1.00 50.05  ? 189 ASP A CG    1 
ATOM   1340 O  OD1   . ASP A 1 189 ? 21.894  41.149  26.533  1.00 54.81  ? 189 ASP A OD1   1 
ATOM   1341 O  OD2   . ASP A 1 189 ? 23.973  40.911  25.820  1.00 52.68  ? 189 ASP A OD2   1 
ATOM   1342 N  N     . ASN A 1 190 ? 22.530  44.662  26.316  1.00 44.83  ? 190 ASN A N     1 
ATOM   1343 C  CA    . ASN A 1 190 ? 23.262  45.827  26.809  1.00 45.90  ? 190 ASN A CA    1 
ATOM   1344 C  C     . ASN A 1 190 ? 22.446  47.102  26.745  1.00 44.72  ? 190 ASN A C     1 
ATOM   1345 O  O     . ASN A 1 190 ? 22.971  48.192  26.559  1.00 44.17  ? 190 ASN A O     1 
ATOM   1346 C  CB    . ASN A 1 190 ? 24.578  46.004  26.045  1.00 49.14  ? 190 ASN A CB    1 
ATOM   1347 C  CG    . ASN A 1 190 ? 25.400  44.731  26.000  1.00 52.04  ? 190 ASN A CG    1 
ATOM   1348 O  OD1   . ASN A 1 190 ? 25.265  43.922  25.083  1.00 55.54  ? 190 ASN A OD1   1 
ATOM   1349 N  ND2   . ASN A 1 190 ? 26.248  44.540  27.001  1.00 55.18  ? 190 ASN A ND2   1 
ATOM   1350 N  N     . THR A 1 191 ? 21.149  46.929  26.927  1.00 44.76  ? 191 THR A N     1 
ATOM   1351 C  CA    . THR A 1 191 ? 20.163  47.989  26.915  1.00 46.06  ? 191 THR A CA    1 
ATOM   1352 C  C     . THR A 1 191 ? 20.351  49.057  28.022  1.00 47.87  ? 191 THR A C     1 
ATOM   1353 O  O     . THR A 1 191 ? 19.794  50.166  27.950  1.00 46.02  ? 191 THR A O     1 
ATOM   1354 C  CB    . THR A 1 191 ? 18.812  47.315  27.016  1.00 45.21  ? 191 THR A CB    1 
ATOM   1355 O  OG1   . THR A 1 191 ? 18.598  46.598  25.804  1.00 47.48  ? 191 THR A OG1   1 
ATOM   1356 C  CG2   . THR A 1 191 ? 17.700  48.299  27.228  1.00 49.86  ? 191 THR A CG2   1 
ATOM   1357 N  N     . LEU A 1 192 ? 21.135  48.719  29.044  1.00 49.50  ? 192 LEU A N     1 
ATOM   1358 C  CA    . LEU A 1 192 ? 21.394  49.644  30.138  1.00 50.43  ? 192 LEU A CA    1 
ATOM   1359 C  C     . LEU A 1 192 ? 22.820  50.144  30.012  1.00 51.34  ? 192 LEU A C     1 
ATOM   1360 O  O     . LEU A 1 192 ? 23.321  50.850  30.880  1.00 51.93  ? 192 LEU A O     1 
ATOM   1361 C  CB    . LEU A 1 192 ? 21.176  48.961  31.491  1.00 51.19  ? 192 LEU A CB    1 
ATOM   1362 C  CG    . LEU A 1 192 ? 19.720  48.576  31.803  1.00 51.59  ? 192 LEU A CG    1 
ATOM   1363 C  CD1   . LEU A 1 192 ? 19.626  48.050  33.238  1.00 52.17  ? 192 LEU A CD1   1 
ATOM   1364 C  CD2   . LEU A 1 192 ? 18.811  49.782  31.631  1.00 49.23  ? 192 LEU A CD2   1 
ATOM   1365 N  N     . TRP A 1 193 ? 23.453  49.745  28.911  1.00 52.48  ? 193 TRP A N     1 
ATOM   1366 C  CA    . TRP A 1 193 ? 24.812  50.137  28.520  1.00 51.92  ? 193 TRP A CA    1 
ATOM   1367 C  C     . TRP A 1 193 ? 25.778  50.526  29.652  1.00 52.24  ? 193 TRP A C     1 
ATOM   1368 O  O     . TRP A 1 193 ? 26.337  51.635  29.677  1.00 51.40  ? 193 TRP A O     1 
ATOM   1369 C  CB    . TRP A 1 193 ? 24.694  51.281  27.501  1.00 50.73  ? 193 TRP A CB    1 
ATOM   1370 C  CG    . TRP A 1 193 ? 25.922  51.557  26.712  1.00 49.63  ? 193 TRP A CG    1 
ATOM   1371 C  CD1   . TRP A 1 193 ? 26.517  52.763  26.527  1.00 49.06  ? 193 TRP A CD1   1 
ATOM   1372 C  CD2   . TRP A 1 193 ? 26.681  50.618  25.959  1.00 48.42  ? 193 TRP A CD2   1 
ATOM   1373 N  NE1   . TRP A 1 193 ? 27.604  52.636  25.700  1.00 48.30  ? 193 TRP A NE1   1 
ATOM   1374 C  CE2   . TRP A 1 193 ? 27.724  51.328  25.335  1.00 47.93  ? 193 TRP A CE2   1 
ATOM   1375 C  CE3   . TRP A 1 193 ? 26.575  49.246  25.744  1.00 49.98  ? 193 TRP A CE3   1 
ATOM   1376 C  CZ2   . TRP A 1 193 ? 28.650  50.721  24.517  1.00 49.89  ? 193 TRP A CZ2   1 
ATOM   1377 C  CZ3   . TRP A 1 193 ? 27.480  48.651  24.935  1.00 48.36  ? 193 TRP A CZ3   1 
ATOM   1378 C  CH2   . TRP A 1 193 ? 28.513  49.388  24.325  1.00 50.00  ? 193 TRP A CH2   1 
ATOM   1379 N  N     . ASN A 1 194 ? 25.980  49.608  30.587  1.00 52.64  ? 194 ASN A N     1 
ATOM   1380 C  CA    . ASN A 1 194 ? 26.890  49.854  31.694  1.00 53.56  ? 194 ASN A CA    1 
ATOM   1381 C  C     . ASN A 1 194 ? 26.409  51.042  32.503  1.00 53.92  ? 194 ASN A C     1 
ATOM   1382 O  O     . ASN A 1 194 ? 27.214  51.830  32.965  1.00 56.05  ? 194 ASN A O     1 
ATOM   1383 C  CB    . ASN A 1 194 ? 28.295  50.150  31.159  1.00 55.03  ? 194 ASN A CB    1 
ATOM   1384 C  CG    . ASN A 1 194 ? 29.372  50.065  32.240  1.00 58.39  ? 194 ASN A CG    1 
ATOM   1385 O  OD1   . ASN A 1 194 ? 29.183  50.530  33.358  1.00 60.94  ? 194 ASN A OD1   1 
ATOM   1386 N  ND2   . ASN A 1 194 ? 30.516  49.488  31.898  1.00 59.86  ? 194 ASN A ND2   1 
ATOM   1387 N  N     . GLY A 1 195 ? 25.100  51.186  32.665  1.00 54.15  ? 195 GLY A N     1 
ATOM   1388 C  CA    . GLY A 1 195 ? 24.576  52.306  33.427  1.00 53.23  ? 195 GLY A CA    1 
ATOM   1389 C  C     . GLY A 1 195 ? 24.850  53.681  32.835  1.00 54.03  ? 195 GLY A C     1 
ATOM   1390 O  O     . GLY A 1 195 ? 24.256  54.666  33.268  1.00 53.57  ? 195 GLY A O     1 
ATOM   1391 N  N     . SER A 1 196 ? 25.739  53.769  31.847  1.00 55.08  ? 196 SER A N     1 
ATOM   1392 C  CA    . SER A 1 196 ? 26.055  55.066  31.239  1.00 55.67  ? 196 SER A CA    1 
ATOM   1393 C  C     . SER A 1 196 ? 24.796  55.812  30.780  1.00 55.84  ? 196 SER A C     1 
ATOM   1394 O  O     . SER A 1 196 ? 24.861  56.983  30.431  1.00 55.70  ? 196 SER A O     1 
ATOM   1395 C  CB    . SER A 1 196 ? 27.035  54.900  30.055  1.00 54.68  ? 196 SER A CB    1 
ATOM   1396 O  OG    . SER A 1 196 ? 26.467  54.197  28.965  1.00 53.10  ? 196 SER A OG    1 
ATOM   1397 N  N     . VAL A 1 197 ? 23.654  55.134  30.799  1.00 56.54  ? 197 VAL A N     1 
ATOM   1398 C  CA    . VAL A 1 197 ? 22.400  55.744  30.386  1.00 58.07  ? 197 VAL A CA    1 
ATOM   1399 C  C     . VAL A 1 197 ? 21.858  56.789  31.370  1.00 59.98  ? 197 VAL A C     1 
ATOM   1400 O  O     . VAL A 1 197 ? 20.859  57.453  31.088  1.00 61.05  ? 197 VAL A O     1 
ATOM   1401 C  CB    . VAL A 1 197 ? 21.327  54.674  30.169  1.00 56.76  ? 197 VAL A CB    1 
ATOM   1402 C  CG1   . VAL A 1 197 ? 21.721  53.791  29.015  1.00 56.09  ? 197 VAL A CG1   1 
ATOM   1403 C  CG2   . VAL A 1 197 ? 21.163  53.854  31.414  1.00 55.68  ? 197 VAL A CG2   1 
ATOM   1404 N  N     . VAL A 1 198 ? 22.508  56.932  32.522  1.00 61.22  ? 198 VAL A N     1 
ATOM   1405 C  CA    . VAL A 1 198 ? 22.089  57.904  33.532  1.00 61.77  ? 198 VAL A CA    1 
ATOM   1406 C  C     . VAL A 1 198 ? 23.324  58.538  34.167  1.00 64.35  ? 198 VAL A C     1 
ATOM   1407 O  O     . VAL A 1 198 ? 23.235  59.154  35.224  1.00 64.95  ? 198 VAL A O     1 
ATOM   1408 C  CB    . VAL A 1 198 ? 21.252  57.240  34.661  1.00 60.84  ? 198 VAL A CB    1 
ATOM   1409 C  CG1   . VAL A 1 198 ? 19.959  56.675  34.103  1.00 59.94  ? 198 VAL A CG1   1 
ATOM   1410 C  CG2   . VAL A 1 198 ? 22.051  56.135  35.324  1.00 57.91  ? 198 VAL A CG2   1 
ATOM   1411 N  N     . ALA A 1 199 ? 24.471  58.383  33.509  1.00 67.71  ? 199 ALA A N     1 
ATOM   1412 C  CA    . ALA A 1 199 ? 25.741  58.917  33.997  1.00 70.97  ? 199 ALA A CA    1 
ATOM   1413 C  C     . ALA A 1 199 ? 25.775  60.439  34.012  1.00 74.17  ? 199 ALA A C     1 
ATOM   1414 O  O     . ALA A 1 199 ? 25.255  61.096  33.100  1.00 73.13  ? 199 ALA A O     1 
ATOM   1415 C  CB    . ALA A 1 199 ? 26.897  58.380  33.159  1.00 70.35  ? 199 ALA A CB    1 
ATOM   1416 N  N     . PRO A 1 200 ? 26.413  61.017  35.052  1.00 77.43  ? 200 PRO A N     1 
ATOM   1417 C  CA    . PRO A 1 200 ? 26.569  62.458  35.282  1.00 79.18  ? 200 PRO A CA    1 
ATOM   1418 C  C     . PRO A 1 200 ? 27.269  63.213  34.154  1.00 81.71  ? 200 PRO A C     1 
ATOM   1419 O  O     . PRO A 1 200 ? 28.398  62.890  33.772  1.00 81.36  ? 200 PRO A O     1 
ATOM   1420 C  CB    . PRO A 1 200 ? 27.344  62.511  36.593  1.00 78.34  ? 200 PRO A CB    1 
ATOM   1421 C  CG    . PRO A 1 200 ? 28.183  61.278  36.530  1.00 77.95  ? 200 PRO A CG    1 
ATOM   1422 C  CD    . PRO A 1 200 ? 27.190  60.253  36.048  1.00 77.58  ? 200 PRO A CD    1 
ATOM   1423 N  N     . PRO A 1 201 ? 26.591  64.237  33.608  1.00 84.44  ? 201 PRO A N     1 
ATOM   1424 C  CA    . PRO A 1 201 ? 27.078  65.091  32.516  1.00 85.99  ? 201 PRO A CA    1 
ATOM   1425 C  C     . PRO A 1 201 ? 28.357  65.821  32.906  1.00 87.48  ? 201 PRO A C     1 
ATOM   1426 O  O     . PRO A 1 201 ? 28.376  67.055  32.943  1.00 89.08  ? 201 PRO A O     1 
ATOM   1427 C  CB    . PRO A 1 201 ? 25.921  66.072  32.298  1.00 85.53  ? 201 PRO A CB    1 
ATOM   1428 C  CG    . PRO A 1 201 ? 24.715  65.302  32.759  1.00 85.86  ? 201 PRO A CG    1 
ATOM   1429 C  CD    . PRO A 1 201 ? 25.221  64.620  34.001  1.00 85.27  ? 201 PRO A CD    1 
ATOM   1430 N  N     . ASP A 1 202 ? 29.417  65.069  33.199  1.00 88.15  ? 202 ASP A N     1 
ATOM   1431 C  CA    . ASP A 1 202 ? 30.696  65.660  33.603  1.00 88.45  ? 202 ASP A CA    1 
ATOM   1432 C  C     . ASP A 1 202 ? 31.653  64.594  34.110  1.00 87.73  ? 202 ASP A C     1 
ATOM   1433 O  O     . ASP A 1 202 ? 32.716  64.913  34.646  1.00 87.28  ? 202 ASP A O     1 
ATOM   1434 C  CB    . ASP A 1 202 ? 30.489  66.717  34.709  1.00 90.66  ? 202 ASP A CB    1 
ATOM   1435 C  CG    . ASP A 1 202 ? 29.938  66.121  36.022  1.00 92.81  ? 202 ASP A CG    1 
ATOM   1436 O  OD1   . ASP A 1 202 ? 30.668  65.361  36.703  1.00 93.73  ? 202 ASP A OD1   1 
ATOM   1437 O  OD2   . ASP A 1 202 ? 28.773  66.420  36.377  1.00 92.78  ? 202 ASP A OD2   1 
ATOM   1438 N  N     . ALA A 1 203 ? 31.270  63.330  33.950  1.00 86.87  ? 203 ALA A N     1 
ATOM   1439 C  CA    . ALA A 1 203 ? 32.102  62.223  34.400  1.00 86.67  ? 203 ALA A CA    1 
ATOM   1440 C  C     . ALA A 1 203 ? 32.594  61.448  33.195  1.00 86.77  ? 203 ALA A C     1 
ATOM   1441 O  O     . ALA A 1 203 ? 32.161  60.324  32.967  1.00 87.71  ? 203 ALA A O     1 
ATOM   1442 C  CB    . ALA A 1 203 ? 31.301  61.314  35.305  1.00 86.25  ? 203 ALA A CB    1 
ATOM   1443 N  N     . PRO A 1 204 ? 33.527  62.030  32.416  1.00 86.75  ? 204 PRO A N     1 
ATOM   1444 C  CA    . PRO A 1 204 ? 34.053  61.357  31.224  1.00 85.28  ? 204 PRO A CA    1 
ATOM   1445 C  C     . PRO A 1 204 ? 34.130  59.829  31.312  1.00 82.92  ? 204 PRO A C     1 
ATOM   1446 O  O     . PRO A 1 204 ? 34.553  59.254  32.328  1.00 81.94  ? 204 PRO A O     1 
ATOM   1447 C  CB    . PRO A 1 204 ? 35.410  62.031  31.020  1.00 86.82  ? 204 PRO A CB    1 
ATOM   1448 C  CG    . PRO A 1 204 ? 35.107  63.455  31.408  1.00 87.03  ? 204 PRO A CG    1 
ATOM   1449 C  CD    . PRO A 1 204 ? 34.303  63.256  32.700  1.00 87.71  ? 204 PRO A CD    1 
ATOM   1450 N  N     . LEU A 1 205 ? 33.691  59.204  30.219  1.00 79.39  ? 205 LEU A N     1 
ATOM   1451 C  CA    . LEU A 1 205 ? 33.642  57.762  30.064  1.00 75.45  ? 205 LEU A CA    1 
ATOM   1452 C  C     . LEU A 1 205 ? 34.473  57.387  28.855  1.00 74.37  ? 205 LEU A C     1 
ATOM   1453 O  O     . LEU A 1 205 ? 34.878  58.259  28.093  1.00 73.62  ? 205 LEU A O     1 
ATOM   1454 C  CB    . LEU A 1 205 ? 32.189  57.324  29.854  1.00 73.09  ? 205 LEU A CB    1 
ATOM   1455 C  CG    . LEU A 1 205 ? 31.131  58.432  29.909  1.00 69.61  ? 205 LEU A CG    1 
ATOM   1456 C  CD1   . LEU A 1 205 ? 30.909  58.997  28.539  1.00 68.47  ? 205 LEU A CD1   1 
ATOM   1457 C  CD2   . LEU A 1 205 ? 29.836  57.888  30.434  1.00 68.42  ? 205 LEU A CD2   1 
ATOM   1458 N  N     . ARG A 1 206 ? 34.730  56.094  28.677  1.00 74.54  ? 206 ARG A N     1 
ATOM   1459 C  CA    . ARG A 1 206 ? 35.513  55.634  27.531  1.00 74.85  ? 206 ARG A CA    1 
ATOM   1460 C  C     . ARG A 1 206 ? 34.893  56.153  26.230  1.00 73.17  ? 206 ARG A C     1 
ATOM   1461 O  O     . ARG A 1 206 ? 33.675  56.292  26.108  1.00 73.22  ? 206 ARG A O     1 
ATOM   1462 C  CB    . ARG A 1 206 ? 35.579  54.100  27.484  1.00 77.97  ? 206 ARG A CB    1 
ATOM   1463 C  CG    . ARG A 1 206 ? 36.039  53.415  28.769  1.00 84.04  ? 206 ARG A CG    1 
ATOM   1464 C  CD    . ARG A 1 206 ? 37.190  54.161  29.440  1.00 89.11  ? 206 ARG A CD    1 
ATOM   1465 N  NE    . ARG A 1 206 ? 36.709  55.092  30.464  1.00 93.73  ? 206 ARG A NE    1 
ATOM   1466 C  CZ    . ARG A 1 206 ? 37.443  56.056  31.019  1.00 95.50  ? 206 ARG A CZ    1 
ATOM   1467 N  NH1   . ARG A 1 206 ? 38.710  56.231  30.644  1.00 95.96  ? 206 ARG A NH1   1 
ATOM   1468 N  NH2   . ARG A 1 206 ? 36.915  56.838  31.960  1.00 95.77  ? 206 ARG A NH2   1 
ATOM   1469 N  N     . LYS A 1 207 ? 35.739  56.433  25.253  1.00 70.82  ? 207 LYS A N     1 
ATOM   1470 C  CA    . LYS A 1 207 ? 35.272  56.944  23.980  1.00 68.51  ? 207 LYS A CA    1 
ATOM   1471 C  C     . LYS A 1 207 ? 34.165  56.113  23.317  1.00 66.92  ? 207 LYS A C     1 
ATOM   1472 O  O     . LYS A 1 207 ? 33.221  56.685  22.770  1.00 67.22  ? 207 LYS A O     1 
ATOM   1473 C  CB    . LYS A 1 207 ? 36.473  57.104  23.044  1.00 70.42  ? 207 LYS A CB    1 
ATOM   1474 C  CG    . LYS A 1 207 ? 36.168  57.653  21.661  1.00 72.22  ? 207 LYS A CG    1 
ATOM   1475 C  CD    . LYS A 1 207 ? 37.400  58.323  21.029  1.00 75.07  ? 207 LYS A CD    1 
ATOM   1476 C  CE    . LYS A 1 207 ? 38.659  57.427  20.995  1.00 76.70  ? 207 LYS A CE    1 
ATOM   1477 N  NZ    . LYS A 1 207 ? 39.471  57.409  22.265  1.00 76.47  ? 207 LYS A NZ    1 
ATOM   1478 N  N     . TYR A 1 208 ? 34.241  54.782  23.367  1.00 63.88  ? 208 TYR A N     1 
ATOM   1479 C  CA    . TYR A 1 208 ? 33.199  53.991  22.711  1.00 61.17  ? 208 TYR A CA    1 
ATOM   1480 C  C     . TYR A 1 208 ? 31.882  53.904  23.468  1.00 59.57  ? 208 TYR A C     1 
ATOM   1481 O  O     . TYR A 1 208 ? 30.827  53.849  22.847  1.00 59.34  ? 208 TYR A O     1 
ATOM   1482 C  CB    . TYR A 1 208 ? 33.687  52.580  22.366  1.00 61.64  ? 208 TYR A CB    1 
ATOM   1483 C  CG    . TYR A 1 208 ? 33.745  51.621  23.527  1.00 65.52  ? 208 TYR A CG    1 
ATOM   1484 C  CD1   . TYR A 1 208 ? 34.768  51.694  24.482  1.00 67.20  ? 208 TYR A CD1   1 
ATOM   1485 C  CD2   . TYR A 1 208 ? 32.780  50.622  23.674  1.00 67.81  ? 208 TYR A CD2   1 
ATOM   1486 C  CE1   . TYR A 1 208 ? 34.828  50.782  25.560  1.00 67.23  ? 208 TYR A CE1   1 
ATOM   1487 C  CE2   . TYR A 1 208 ? 32.828  49.708  24.749  1.00 67.92  ? 208 TYR A CE2   1 
ATOM   1488 C  CZ    . TYR A 1 208 ? 33.854  49.795  25.679  1.00 67.19  ? 208 TYR A CZ    1 
ATOM   1489 O  OH    . TYR A 1 208 ? 33.908  48.884  26.705  1.00 67.75  ? 208 TYR A OH    1 
ATOM   1490 N  N     . VAL A 1 209 ? 31.910  53.882  24.797  1.00 57.32  ? 209 VAL A N     1 
ATOM   1491 C  CA    . VAL A 1 209 ? 30.640  53.829  25.517  1.00 56.32  ? 209 VAL A CA    1 
ATOM   1492 C  C     . VAL A 1 209 ? 29.938  55.176  25.332  1.00 54.53  ? 209 VAL A C     1 
ATOM   1493 O  O     . VAL A 1 209 ? 28.710  55.254  25.261  1.00 53.28  ? 209 VAL A O     1 
ATOM   1494 C  CB    . VAL A 1 209 ? 30.820  53.537  27.026  1.00 55.62  ? 209 VAL A CB    1 
ATOM   1495 C  CG1   . VAL A 1 209 ? 31.990  54.297  27.565  1.00 57.84  ? 209 VAL A CG1   1 
ATOM   1496 C  CG2   . VAL A 1 209 ? 29.560  53.953  27.792  1.00 54.41  ? 209 VAL A CG2   1 
ATOM   1497 N  N     . ARG A 1 210 ? 30.733  56.234  25.253  1.00 53.34  ? 210 ARG A N     1 
ATOM   1498 C  CA    . ARG A 1 210 ? 30.205  57.574  25.041  1.00 53.24  ? 210 ARG A CA    1 
ATOM   1499 C  C     . ARG A 1 210 ? 29.508  57.638  23.680  1.00 53.17  ? 210 ARG A C     1 
ATOM   1500 O  O     . ARG A 1 210 ? 28.470  58.284  23.526  1.00 53.02  ? 210 ARG A O     1 
ATOM   1501 C  CB    . ARG A 1 210 ? 31.346  58.582  25.092  1.00 53.76  ? 210 ARG A CB    1 
ATOM   1502 C  CG    . ARG A 1 210 ? 30.961  59.991  24.697  1.00 54.70  ? 210 ARG A CG    1 
ATOM   1503 C  CD    . ARG A 1 210 ? 31.975  60.972  25.250  1.00 55.36  ? 210 ARG A CD    1 
ATOM   1504 N  NE    . ARG A 1 210 ? 31.297  61.950  26.089  1.00 56.68  ? 210 ARG A NE    1 
ATOM   1505 C  CZ    . ARG A 1 210 ? 31.786  62.418  27.226  1.00 58.38  ? 210 ARG A CZ    1 
ATOM   1506 N  NH1   . ARG A 1 210 ? 32.964  62.000  27.677  1.00 59.21  ? 210 ARG A NH1   1 
ATOM   1507 N  NH2   . ARG A 1 210 ? 31.094  63.313  27.910  1.00 62.31  ? 210 ARG A NH2   1 
ATOM   1508 N  N     . TYR A 1 211 ? 30.092  56.954  22.701  1.00 52.44  ? 211 TYR A N     1 
ATOM   1509 C  CA    . TYR A 1 211 ? 29.556  56.901  21.346  1.00 51.45  ? 211 TYR A CA    1 
ATOM   1510 C  C     . TYR A 1 211 ? 28.241  56.127  21.247  1.00 50.54  ? 211 TYR A C     1 
ATOM   1511 O  O     . TYR A 1 211 ? 27.250  56.660  20.772  1.00 51.36  ? 211 TYR A O     1 
ATOM   1512 C  CB    . TYR A 1 211 ? 30.577  56.254  20.408  1.00 51.79  ? 211 TYR A CB    1 
ATOM   1513 C  CG    . TYR A 1 211 ? 30.091  56.118  18.985  1.00 50.94  ? 211 TYR A CG    1 
ATOM   1514 C  CD1   . TYR A 1 211 ? 30.169  57.190  18.099  1.00 50.78  ? 211 TYR A CD1   1 
ATOM   1515 C  CD2   . TYR A 1 211 ? 29.510  54.931  18.539  1.00 50.14  ? 211 TYR A CD2   1 
ATOM   1516 C  CE1   . TYR A 1 211 ? 29.679  57.088  16.810  1.00 51.57  ? 211 TYR A CE1   1 
ATOM   1517 C  CE2   . TYR A 1 211 ? 29.018  54.817  17.253  1.00 51.25  ? 211 TYR A CE2   1 
ATOM   1518 C  CZ    . TYR A 1 211 ? 29.103  55.900  16.391  1.00 51.51  ? 211 TYR A CZ    1 
ATOM   1519 O  OH    . TYR A 1 211 ? 28.597  55.810  15.115  1.00 52.82  ? 211 TYR A OH    1 
ATOM   1520 N  N     . TYR A 1 212 ? 28.241  54.868  21.678  1.00 49.48  ? 212 TYR A N     1 
ATOM   1521 C  CA    . TYR A 1 212 ? 27.044  54.039  21.619  1.00 50.81  ? 212 TYR A CA    1 
ATOM   1522 C  C     . TYR A 1 212 ? 25.925  54.443  22.587  1.00 51.40  ? 212 TYR A C     1 
ATOM   1523 O  O     . TYR A 1 212 ? 24.793  53.976  22.463  1.00 51.20  ? 212 TYR A O     1 
ATOM   1524 C  CB    . TYR A 1 212 ? 27.404  52.573  21.862  1.00 52.31  ? 212 TYR A CB    1 
ATOM   1525 C  CG    . TYR A 1 212 ? 28.149  51.917  20.728  1.00 54.80  ? 212 TYR A CG    1 
ATOM   1526 C  CD1   . TYR A 1 212 ? 27.541  51.718  19.489  1.00 57.02  ? 212 TYR A CD1   1 
ATOM   1527 C  CD2   . TYR A 1 212 ? 29.466  51.513  20.882  1.00 56.26  ? 212 TYR A CD2   1 
ATOM   1528 C  CE1   . TYR A 1 212 ? 28.224  51.136  18.435  1.00 56.79  ? 212 TYR A CE1   1 
ATOM   1529 C  CE2   . TYR A 1 212 ? 30.164  50.933  19.830  1.00 57.16  ? 212 TYR A CE2   1 
ATOM   1530 C  CZ    . TYR A 1 212 ? 29.538  50.750  18.614  1.00 57.78  ? 212 TYR A CZ    1 
ATOM   1531 O  OH    . TYR A 1 212 ? 30.245  50.209  17.565  1.00 61.04  ? 212 TYR A OH    1 
ATOM   1532 N  N     . ARG A 1 213 ? 26.224  55.304  23.551  1.00 51.99  ? 213 ARG A N     1 
ATOM   1533 C  CA    . ARG A 1 213 ? 25.197  55.713  24.489  1.00 52.89  ? 213 ARG A CA    1 
ATOM   1534 C  C     . ARG A 1 213 ? 24.037  56.469  23.831  1.00 54.09  ? 213 ARG A C     1 
ATOM   1535 O  O     . ARG A 1 213 ? 22.866  56.263  24.191  1.00 55.07  ? 213 ARG A O     1 
ATOM   1536 C  CB    . ARG A 1 213 ? 25.784  56.575  25.590  1.00 52.66  ? 213 ARG A CB    1 
ATOM   1537 C  CG    . ARG A 1 213 ? 24.752  56.915  26.636  1.00 55.77  ? 213 ARG A CG    1 
ATOM   1538 C  CD    . ARG A 1 213 ? 25.347  57.726  27.752  1.00 59.00  ? 213 ARG A CD    1 
ATOM   1539 N  NE    . ARG A 1 213 ? 25.592  59.100  27.353  1.00 61.86  ? 213 ARG A NE    1 
ATOM   1540 C  CZ    . ARG A 1 213 ? 26.325  59.946  28.060  1.00 64.26  ? 213 ARG A CZ    1 
ATOM   1541 N  NH1   . ARG A 1 213 ? 26.881  59.546  29.198  1.00 65.58  ? 213 ARG A NH1   1 
ATOM   1542 N  NH2   . ARG A 1 213 ? 26.504  61.187  27.633  1.00 65.59  ? 213 ARG A NH2   1 
ATOM   1543 N  N     . ASP A 1 214 ? 24.349  57.349  22.881  1.00 52.55  ? 214 ASP A N     1 
ATOM   1544 C  CA    . ASP A 1 214 ? 23.299  58.106  22.211  1.00 51.69  ? 214 ASP A CA    1 
ATOM   1545 C  C     . ASP A 1 214 ? 22.381  57.112  21.500  1.00 51.05  ? 214 ASP A C     1 
ATOM   1546 O  O     . ASP A 1 214 ? 21.156  57.275  21.466  1.00 49.81  ? 214 ASP A O     1 
ATOM   1547 C  CB    . ASP A 1 214 ? 23.911  59.088  21.210  1.00 52.06  ? 214 ASP A CB    1 
ATOM   1548 C  CG    . ASP A 1 214 ? 25.032  59.913  21.816  1.00 53.48  ? 214 ASP A CG    1 
ATOM   1549 O  OD1   . ASP A 1 214 ? 24.908  60.319  22.989  1.00 55.57  ? 214 ASP A OD1   1 
ATOM   1550 O  OD2   . ASP A 1 214 ? 26.038  60.165  21.119  1.00 54.94  ? 214 ASP A OD2   1 
ATOM   1551 N  N     . PHE A 1 215 ? 22.989  56.065  20.947  1.00 49.66  ? 215 PHE A N     1 
ATOM   1552 C  CA    . PHE A 1 215 ? 22.243  55.027  20.250  1.00 48.02  ? 215 PHE A CA    1 
ATOM   1553 C  C     . PHE A 1 215 ? 21.347  54.199  21.155  1.00 47.21  ? 215 PHE A C     1 
ATOM   1554 O  O     . PHE A 1 215 ? 20.175  53.987  20.837  1.00 47.75  ? 215 PHE A O     1 
ATOM   1555 C  CB    . PHE A 1 215 ? 23.209  54.128  19.496  1.00 45.92  ? 215 PHE A CB    1 
ATOM   1556 C  CG    . PHE A 1 215 ? 23.755  54.776  18.292  1.00 44.52  ? 215 PHE A CG    1 
ATOM   1557 C  CD1   . PHE A 1 215 ? 22.905  55.093  17.238  1.00 43.10  ? 215 PHE A CD1   1 
ATOM   1558 C  CD2   . PHE A 1 215 ? 25.081  55.200  18.251  1.00 44.45  ? 215 PHE A CD2   1 
ATOM   1559 C  CE1   . PHE A 1 215 ? 23.356  55.838  16.162  1.00 42.46  ? 215 PHE A CE1   1 
ATOM   1560 C  CE2   . PHE A 1 215 ? 25.552  55.949  17.174  1.00 44.70  ? 215 PHE A CE2   1 
ATOM   1561 C  CZ    . PHE A 1 215 ? 24.683  56.273  16.125  1.00 43.60  ? 215 PHE A CZ    1 
ATOM   1562 N  N     . VAL A 1 216 ? 21.895  53.735  22.273  1.00 44.75  ? 216 VAL A N     1 
ATOM   1563 C  CA    . VAL A 1 216 ? 21.122  52.952  23.205  1.00 44.49  ? 216 VAL A CA    1 
ATOM   1564 C  C     . VAL A 1 216 ? 19.925  53.756  23.699  1.00 43.53  ? 216 VAL A C     1 
ATOM   1565 O  O     . VAL A 1 216 ? 18.788  53.302  23.581  1.00 42.54  ? 216 VAL A O     1 
ATOM   1566 C  CB    . VAL A 1 216 ? 21.989  52.499  24.387  1.00 45.52  ? 216 VAL A CB    1 
ATOM   1567 C  CG1   . VAL A 1 216 ? 21.149  51.735  25.405  1.00 44.60  ? 216 VAL A CG1   1 
ATOM   1568 C  CG2   . VAL A 1 216 ? 23.107  51.601  23.874  1.00 46.25  ? 216 VAL A CG2   1 
ATOM   1569 N  N     . LEU A 1 217 ? 20.165  54.949  24.237  1.00 44.21  ? 217 LEU A N     1 
ATOM   1570 C  CA    . LEU A 1 217 ? 19.060  55.789  24.719  1.00 45.99  ? 217 LEU A CA    1 
ATOM   1571 C  C     . LEU A 1 217 ? 17.969  55.903  23.644  1.00 48.05  ? 217 LEU A C     1 
ATOM   1572 O  O     . LEU A 1 217 ? 16.780  55.709  23.925  1.00 48.27  ? 217 LEU A O     1 
ATOM   1573 C  CB    . LEU A 1 217 ? 19.553  57.194  25.078  1.00 42.67  ? 217 LEU A CB    1 
ATOM   1574 C  CG    . LEU A 1 217 ? 20.643  57.373  26.128  1.00 41.64  ? 217 LEU A CG    1 
ATOM   1575 C  CD1   . LEU A 1 217 ? 20.719  58.839  26.502  1.00 40.20  ? 217 LEU A CD1   1 
ATOM   1576 C  CD2   . LEU A 1 217 ? 20.328  56.562  27.359  1.00 42.25  ? 217 LEU A CD2   1 
ATOM   1577 N  N     . GLU A 1 218 ? 18.399  56.222  22.420  1.00 50.90  ? 218 GLU A N     1 
ATOM   1578 C  CA    . GLU A 1 218 ? 17.525  56.357  21.247  1.00 53.10  ? 218 GLU A CA    1 
ATOM   1579 C  C     . GLU A 1 218 ? 16.727  55.063  21.040  1.00 52.25  ? 218 GLU A C     1 
ATOM   1580 O  O     . GLU A 1 218 ? 15.512  55.094  20.835  1.00 51.91  ? 218 GLU A O     1 
ATOM   1581 C  CB    . GLU A 1 218 ? 18.372  56.637  19.997  1.00 56.89  ? 218 GLU A CB    1 
ATOM   1582 C  CG    . GLU A 1 218 ? 17.561  56.743  18.702  1.00 65.78  ? 218 GLU A CG    1 
ATOM   1583 C  CD    . GLU A 1 218 ? 18.397  56.521  17.426  1.00 70.36  ? 218 GLU A CD    1 
ATOM   1584 O  OE1   . GLU A 1 218 ? 19.128  55.503  17.347  1.00 72.73  ? 218 GLU A OE1   1 
ATOM   1585 O  OE2   . GLU A 1 218 ? 18.305  57.357  16.495  1.00 73.34  ? 218 GLU A OE2   1 
ATOM   1586 N  N     . LEU A 1 219 ? 17.439  53.935  21.088  1.00 50.19  ? 219 LEU A N     1 
ATOM   1587 C  CA    . LEU A 1 219 ? 16.858  52.609  20.931  1.00 46.79  ? 219 LEU A CA    1 
ATOM   1588 C  C     . LEU A 1 219 ? 15.777  52.404  21.974  1.00 46.84  ? 219 LEU A C     1 
ATOM   1589 O  O     . LEU A 1 219 ? 14.644  52.070  21.642  1.00 47.34  ? 219 LEU A O     1 
ATOM   1590 C  CB    . LEU A 1 219 ? 17.950  51.535  21.105  1.00 45.73  ? 219 LEU A CB    1 
ATOM   1591 C  CG    . LEU A 1 219 ? 17.694  50.033  20.879  1.00 42.54  ? 219 LEU A CG    1 
ATOM   1592 C  CD1   . LEU A 1 219 ? 17.411  49.360  22.168  1.00 42.34  ? 219 LEU A CD1   1 
ATOM   1593 C  CD2   . LEU A 1 219 ? 16.543  49.820  19.921  1.00 42.07  ? 219 LEU A CD2   1 
ATOM   1594 N  N     . ASN A 1 220 ? 16.122  52.619  23.238  1.00 45.76  ? 220 ASN A N     1 
ATOM   1595 C  CA    . ASN A 1 220 ? 15.162  52.411  24.313  1.00 45.46  ? 220 ASN A CA    1 
ATOM   1596 C  C     . ASN A 1 220 ? 13.857  53.166  24.145  1.00 45.85  ? 220 ASN A C     1 
ATOM   1597 O  O     . ASN A 1 220 ? 12.779  52.583  24.296  1.00 44.15  ? 220 ASN A O     1 
ATOM   1598 C  CB    . ASN A 1 220 ? 15.806  52.725  25.663  1.00 44.48  ? 220 ASN A CB    1 
ATOM   1599 C  CG    . ASN A 1 220 ? 16.901  51.737  26.011  1.00 43.42  ? 220 ASN A CG    1 
ATOM   1600 O  OD1   . ASN A 1 220 ? 16.808  50.560  25.664  1.00 45.15  ? 220 ASN A OD1   1 
ATOM   1601 N  ND2   . ASN A 1 220 ? 17.931  52.199  26.703  1.00 41.94  ? 220 ASN A ND2   1 
ATOM   1602 N  N     . LYS A 1 221 ? 13.945  54.451  23.814  1.00 46.52  ? 221 LYS A N     1 
ATOM   1603 C  CA    . LYS A 1 221 ? 12.745  55.242  23.610  1.00 48.02  ? 221 LYS A CA    1 
ATOM   1604 C  C     . LYS A 1 221 ? 11.867  54.657  22.483  1.00 48.08  ? 221 LYS A C     1 
ATOM   1605 O  O     . LYS A 1 221 ? 10.659  54.452  22.648  1.00 48.29  ? 221 LYS A O     1 
ATOM   1606 C  CB    . LYS A 1 221 ? 13.119  56.693  23.300  1.00 50.71  ? 221 LYS A CB    1 
ATOM   1607 C  CG    . LYS A 1 221 ? 13.832  57.423  24.447  1.00 55.35  ? 221 LYS A CG    1 
ATOM   1608 C  CD    . LYS A 1 221 ? 13.828  58.959  24.232  1.00 59.68  ? 221 LYS A CD    1 
ATOM   1609 C  CE    . LYS A 1 221 ? 14.462  59.725  25.421  1.00 62.14  ? 221 LYS A CE    1 
ATOM   1610 N  NZ    . LYS A 1 221 ? 13.799  61.049  25.730  1.00 62.19  ? 221 LYS A NZ    1 
ATOM   1611 N  N     . ALA A 1 222 ? 12.468  54.367  21.339  1.00 47.60  ? 222 ALA A N     1 
ATOM   1612 C  CA    . ALA A 1 222 ? 11.693  53.812  20.239  1.00 47.28  ? 222 ALA A CA    1 
ATOM   1613 C  C     . ALA A 1 222 ? 10.993  52.540  20.685  1.00 46.94  ? 222 ALA A C     1 
ATOM   1614 O  O     . ALA A 1 222 ? 9.809   52.350  20.425  1.00 45.56  ? 222 ALA A O     1 
ATOM   1615 C  CB    . ALA A 1 222 ? 12.597  53.524  19.039  1.00 46.34  ? 222 ALA A CB    1 
ATOM   1616 N  N     . LEU A 1 223 ? 11.737  51.674  21.366  1.00 47.56  ? 223 LEU A N     1 
ATOM   1617 C  CA    . LEU A 1 223 ? 11.206  50.404  21.838  1.00 47.93  ? 223 LEU A CA    1 
ATOM   1618 C  C     . LEU A 1 223 ? 10.062  50.568  22.839  1.00 49.10  ? 223 LEU A C     1 
ATOM   1619 O  O     . LEU A 1 223 ? 9.040   49.882  22.744  1.00 49.21  ? 223 LEU A O     1 
ATOM   1620 C  CB    . LEU A 1 223 ? 12.333  49.587  22.456  1.00 46.48  ? 223 LEU A CB    1 
ATOM   1621 C  CG    . LEU A 1 223 ? 12.665  48.244  21.820  1.00 44.46  ? 223 LEU A CG    1 
ATOM   1622 C  CD1   . LEU A 1 223 ? 12.456  48.284  20.318  1.00 43.40  ? 223 LEU A CD1   1 
ATOM   1623 C  CD2   . LEU A 1 223 ? 14.097  47.906  22.181  1.00 43.24  ? 223 LEU A CD2   1 
ATOM   1624 N  N     . ALA A 1 224 ? 10.220  51.483  23.788  1.00 49.43  ? 224 ALA A N     1 
ATOM   1625 C  CA    . ALA A 1 224 ? 9.178   51.710  24.779  1.00 49.11  ? 224 ALA A CA    1 
ATOM   1626 C  C     . ALA A 1 224 ? 7.896   52.253  24.164  1.00 50.17  ? 224 ALA A C     1 
ATOM   1627 O  O     . ALA A 1 224 ? 6.846   52.200  24.791  1.00 52.35  ? 224 ALA A O     1 
ATOM   1628 C  CB    . ALA A 1 224 ? 9.669   52.662  25.816  1.00 48.25  ? 224 ALA A CB    1 
ATOM   1629 N  N     . VAL A 1 225 ? 7.981   52.759  22.937  1.00 50.06  ? 225 VAL A N     1 
ATOM   1630 C  CA    . VAL A 1 225 ? 6.836   53.349  22.248  1.00 49.24  ? 225 VAL A CA    1 
ATOM   1631 C  C     . VAL A 1 225 ? 6.336   52.564  21.025  1.00 48.92  ? 225 VAL A C     1 
ATOM   1632 O  O     . VAL A 1 225 ? 5.452   53.025  20.308  1.00 48.95  ? 225 VAL A O     1 
ATOM   1633 C  CB    . VAL A 1 225 ? 7.189   54.816  21.820  1.00 48.97  ? 225 VAL A CB    1 
ATOM   1634 C  CG1   . VAL A 1 225 ? 6.107   55.406  20.965  1.00 50.32  ? 225 VAL A CG1   1 
ATOM   1635 C  CG2   . VAL A 1 225 ? 7.370   55.684  23.044  1.00 48.36  ? 225 VAL A CG2   1 
ATOM   1636 N  N     . ASP A 1 226 ? 6.885   51.379  20.778  1.00 49.92  ? 226 ASP A N     1 
ATOM   1637 C  CA    . ASP A 1 226 ? 6.461   50.584  19.617  1.00 48.80  ? 226 ASP A CA    1 
ATOM   1638 C  C     . ASP A 1 226 ? 5.204   49.777  19.933  1.00 47.97  ? 226 ASP A C     1 
ATOM   1639 O  O     . ASP A 1 226 ? 5.219   48.868  20.762  1.00 45.82  ? 226 ASP A O     1 
ATOM   1640 C  CB    . ASP A 1 226 ? 7.585   49.641  19.155  1.00 48.72  ? 226 ASP A CB    1 
ATOM   1641 C  CG    . ASP A 1 226 ? 7.248   48.911  17.856  1.00 50.24  ? 226 ASP A CG    1 
ATOM   1642 O  OD1   . ASP A 1 226 ? 6.068   48.893  17.439  1.00 52.74  ? 226 ASP A OD1   1 
ATOM   1643 O  OD2   . ASP A 1 226 ? 8.167   48.334  17.246  1.00 50.23  ? 226 ASP A OD2   1 
ATOM   1644 N  N     . PRO A 1 227 ? 4.093   50.111  19.260  1.00 48.77  ? 227 PRO A N     1 
ATOM   1645 C  CA    . PRO A 1 227 ? 2.788   49.468  19.415  1.00 48.63  ? 227 PRO A CA    1 
ATOM   1646 C  C     . PRO A 1 227 ? 2.827   47.991  19.099  1.00 48.93  ? 227 PRO A C     1 
ATOM   1647 O  O     . PRO A 1 227 ? 2.043   47.223  19.646  1.00 50.11  ? 227 PRO A O     1 
ATOM   1648 C  CB    . PRO A 1 227 ? 1.913   50.218  18.420  1.00 48.78  ? 227 PRO A CB    1 
ATOM   1649 C  CG    . PRO A 1 227 ? 2.551   51.557  18.338  1.00 49.08  ? 227 PRO A CG    1 
ATOM   1650 C  CD    . PRO A 1 227 ? 4.008   51.213  18.285  1.00 48.79  ? 227 PRO A CD    1 
ATOM   1651 N  N     . ARG A 1 228 ? 3.739   47.590  18.221  1.00 48.80  ? 228 ARG A N     1 
ATOM   1652 C  CA    . ARG A 1 228 ? 3.823   46.192  17.830  1.00 50.44  ? 228 ARG A CA    1 
ATOM   1653 C  C     . ARG A 1 228 ? 4.471   45.218  18.819  1.00 50.85  ? 228 ARG A C     1 
ATOM   1654 O  O     . ARG A 1 228 ? 4.455   44.010  18.586  1.00 50.95  ? 228 ARG A O     1 
ATOM   1655 C  CB    . ARG A 1 228 ? 4.529   46.081  16.486  1.00 51.11  ? 228 ARG A CB    1 
ATOM   1656 C  CG    . ARG A 1 228 ? 3.933   46.963  15.434  1.00 52.05  ? 228 ARG A CG    1 
ATOM   1657 C  CD    . ARG A 1 228 ? 4.594   46.746  14.083  1.00 54.51  ? 228 ARG A CD    1 
ATOM   1658 N  NE    . ARG A 1 228 ? 4.362   45.404  13.549  1.00 54.63  ? 228 ARG A NE    1 
ATOM   1659 C  CZ    . ARG A 1 228 ? 4.781   45.001  12.353  1.00 54.30  ? 228 ARG A CZ    1 
ATOM   1660 N  NH1   . ARG A 1 228 ? 5.447   45.836  11.571  1.00 52.91  ? 228 ARG A NH1   1 
ATOM   1661 N  NH2   . ARG A 1 228 ? 4.549   43.760  11.946  1.00 56.15  ? 228 ARG A NH2   1 
ATOM   1662 N  N     . ILE A 1 229 ? 5.026   45.722  19.917  1.00 51.22  ? 229 ILE A N     1 
ATOM   1663 C  CA    . ILE A 1 229 ? 5.670   44.845  20.889  1.00 51.06  ? 229 ILE A CA    1 
ATOM   1664 C  C     . ILE A 1 229 ? 5.202   45.059  22.337  1.00 53.38  ? 229 ILE A C     1 
ATOM   1665 O  O     . ILE A 1 229 ? 4.440   45.980  22.621  1.00 52.95  ? 229 ILE A O     1 
ATOM   1666 C  CB    . ILE A 1 229 ? 7.211   44.988  20.814  1.00 48.36  ? 229 ILE A CB    1 
ATOM   1667 C  CG1   . ILE A 1 229 ? 7.610   46.442  21.047  1.00 46.23  ? 229 ILE A CG1   1 
ATOM   1668 C  CG2   . ILE A 1 229 ? 7.716   44.487  19.475  1.00 46.60  ? 229 ILE A CG2   1 
ATOM   1669 C  CD1   . ILE A 1 229 ? 9.071   46.710  20.855  1.00 44.92  ? 229 ILE A CD1   1 
ATOM   1670 N  N     . GLU A 1 230 ? 5.682   44.193  23.236  1.00 55.55  ? 230 GLU A N     1 
ATOM   1671 C  CA    . GLU A 1 230 ? 5.342   44.196  24.655  1.00 55.87  ? 230 GLU A CA    1 
ATOM   1672 C  C     . GLU A 1 230 ? 6.474   44.734  25.552  1.00 55.76  ? 230 GLU A C     1 
ATOM   1673 O  O     . GLU A 1 230 ? 6.233   45.549  26.439  1.00 56.76  ? 230 GLU A O     1 
ATOM   1674 C  CB    . GLU A 1 230 ? 5.004   42.769  25.061  1.00 60.53  ? 230 GLU A CB    1 
ATOM   1675 C  CG    . GLU A 1 230 ? 3.937   42.607  26.143  1.00 66.25  ? 230 GLU A CG    1 
ATOM   1676 C  CD    . GLU A 1 230 ? 2.570   43.026  25.661  1.00 67.57  ? 230 GLU A CD    1 
ATOM   1677 O  OE1   . GLU A 1 230 ? 2.405   44.230  25.396  1.00 68.77  ? 230 GLU A OE1   1 
ATOM   1678 O  OE2   . GLU A 1 230 ? 1.674   42.155  25.543  1.00 68.45  ? 230 GLU A OE2   1 
ATOM   1679 N  N     . ILE A 1 231 ? 7.696   44.253  25.341  1.00 54.40  ? 231 ILE A N     1 
ATOM   1680 C  CA    . ILE A 1 231 ? 8.898   44.684  26.098  1.00 54.38  ? 231 ILE A CA    1 
ATOM   1681 C  C     . ILE A 1 231 ? 8.983   44.612  27.632  1.00 53.78  ? 231 ILE A C     1 
ATOM   1682 O  O     . ILE A 1 231 ? 8.042   44.939  28.349  1.00 53.74  ? 231 ILE A O     1 
ATOM   1683 C  CB    . ILE A 1 231 ? 9.350   46.138  25.732  1.00 52.95  ? 231 ILE A CB    1 
ATOM   1684 C  CG1   . ILE A 1 231 ? 8.483   47.165  26.447  1.00 52.43  ? 231 ILE A CG1   1 
ATOM   1685 C  CG2   . ILE A 1 231 ? 9.274   46.355  24.231  1.00 54.84  ? 231 ILE A CG2   1 
ATOM   1686 C  CD1   . ILE A 1 231 ? 8.971   48.585  26.298  1.00 52.36  ? 231 ILE A CD1   1 
ATOM   1687 N  N     . CYS A 1 232 ? 10.160  44.199  28.106  1.00 53.23  ? 232 CYS A N     1 
ATOM   1688 C  CA    . CYS A 1 232 ? 10.487  44.092  29.524  1.00 52.72  ? 232 CYS A CA    1 
ATOM   1689 C  C     . CYS A 1 232 ? 11.998  44.317  29.631  1.00 52.05  ? 232 CYS A C     1 
ATOM   1690 O  O     . CYS A 1 232 ? 12.769  43.622  28.985  1.00 51.80  ? 232 CYS A O     1 
ATOM   1691 C  CB    . CYS A 1 232 ? 10.128  42.696  30.061  1.00 54.27  ? 232 CYS A CB    1 
ATOM   1692 S  SG    . CYS A 1 232 ? 10.500  42.411  31.850  1.00 54.40  ? 232 CYS A SG    1 
ATOM   1693 N  N     . MET A 1 233 ? 12.419  45.287  30.433  1.00 52.06  ? 233 MET A N     1 
ATOM   1694 C  CA    . MET A 1 233 ? 13.843  45.578  30.602  1.00 54.16  ? 233 MET A CA    1 
ATOM   1695 C  C     . MET A 1 233 ? 14.457  44.895  31.821  1.00 55.33  ? 233 MET A C     1 
ATOM   1696 O  O     . MET A 1 233 ? 14.421  45.456  32.915  1.00 58.18  ? 233 MET A O     1 
ATOM   1697 C  CB    . MET A 1 233 ? 14.063  47.080  30.765  1.00 54.90  ? 233 MET A CB    1 
ATOM   1698 C  CG    . MET A 1 233 ? 14.458  47.816  29.522  1.00 57.64  ? 233 MET A CG    1 
ATOM   1699 S  SD    . MET A 1 233 ? 14.942  49.512  29.923  1.00 65.06  ? 233 MET A SD    1 
ATOM   1700 C  CE    . MET A 1 233 ? 13.756  50.432  28.975  1.00 62.43  ? 233 MET A CE    1 
ATOM   1701 N  N     . LEU A 1 234 ? 15.034  43.710  31.659  1.00 54.30  ? 234 LEU A N     1 
ATOM   1702 C  CA    . LEU A 1 234 ? 15.638  43.027  32.801  1.00 52.52  ? 234 LEU A CA    1 
ATOM   1703 C  C     . LEU A 1 234 ? 17.050  43.483  33.084  1.00 52.29  ? 234 LEU A C     1 
ATOM   1704 O  O     . LEU A 1 234 ? 17.892  43.488  32.202  1.00 53.68  ? 234 LEU A O     1 
ATOM   1705 C  CB    . LEU A 1 234 ? 15.692  41.531  32.573  1.00 52.88  ? 234 LEU A CB    1 
ATOM   1706 C  CG    . LEU A 1 234 ? 14.428  40.715  32.713  1.00 54.24  ? 234 LEU A CG    1 
ATOM   1707 C  CD1   . LEU A 1 234 ? 14.876  39.308  33.050  1.00 55.39  ? 234 LEU A CD1   1 
ATOM   1708 C  CD2   . LEU A 1 234 ? 13.532  41.262  33.810  1.00 54.39  ? 234 LEU A CD2   1 
ATOM   1709 N  N     . PRO A 1 235 ? 17.344  43.854  34.326  1.00 51.80  ? 235 PRO A N     1 
ATOM   1710 C  CA    . PRO A 1 235 ? 18.715  44.282  34.576  1.00 52.80  ? 235 PRO A CA    1 
ATOM   1711 C  C     . PRO A 1 235 ? 19.736  43.149  34.751  1.00 53.85  ? 235 PRO A C     1 
ATOM   1712 O  O     . PRO A 1 235 ? 20.679  43.280  35.535  1.00 55.90  ? 235 PRO A O     1 
ATOM   1713 C  CB    . PRO A 1 235 ? 18.573  45.149  35.816  1.00 52.47  ? 235 PRO A CB    1 
ATOM   1714 C  CG    . PRO A 1 235 ? 17.451  44.489  36.531  1.00 52.69  ? 235 PRO A CG    1 
ATOM   1715 C  CD    . PRO A 1 235 ? 16.466  44.267  35.426  1.00 51.97  ? 235 PRO A CD    1 
ATOM   1716 N  N     . VAL A 1 236 ? 19.556  42.036  34.038  1.00 53.20  ? 236 VAL A N     1 
ATOM   1717 C  CA    . VAL A 1 236 ? 20.524  40.934  34.116  1.00 52.16  ? 236 VAL A CA    1 
ATOM   1718 C  C     . VAL A 1 236 ? 21.612  41.235  33.105  1.00 51.94  ? 236 VAL A C     1 
ATOM   1719 O  O     . VAL A 1 236 ? 21.329  41.790  32.053  1.00 51.41  ? 236 VAL A O     1 
ATOM   1720 C  CB    . VAL A 1 236 ? 19.931  39.591  33.717  1.00 51.36  ? 236 VAL A CB    1 
ATOM   1721 C  CG1   . VAL A 1 236 ? 19.114  39.027  34.841  1.00 52.62  ? 236 VAL A CG1   1 
ATOM   1722 C  CG2   . VAL A 1 236 ? 19.096  39.761  32.484  1.00 51.15  ? 236 VAL A CG2   1 
ATOM   1723 N  N     . GLY A 1 237 ? 22.848  40.858  33.415  1.00 52.09  ? 237 GLY A N     1 
ATOM   1724 C  CA    . GLY A 1 237 ? 23.950  41.120  32.504  1.00 51.41  ? 237 GLY A CA    1 
ATOM   1725 C  C     . GLY A 1 237 ? 24.118  42.614  32.355  1.00 51.33  ? 237 GLY A C     1 
ATOM   1726 O  O     . GLY A 1 237 ? 24.348  43.323  33.331  1.00 52.98  ? 237 GLY A O     1 
ATOM   1727 N  N     . ASP A 1 238 ? 24.000  43.112  31.137  1.00 50.72  ? 238 ASP A N     1 
ATOM   1728 C  CA    . ASP A 1 238 ? 24.122  44.535  30.929  1.00 49.90  ? 238 ASP A CA    1 
ATOM   1729 C  C     . ASP A 1 238 ? 22.738  45.037  30.553  1.00 49.37  ? 238 ASP A C     1 
ATOM   1730 O  O     . ASP A 1 238 ? 22.568  46.122  30.002  1.00 50.61  ? 238 ASP A O     1 
ATOM   1731 C  CB    . ASP A 1 238 ? 25.129  44.811  29.826  1.00 52.02  ? 238 ASP A CB    1 
ATOM   1732 C  CG    . ASP A 1 238 ? 25.534  46.252  29.782  1.00 55.03  ? 238 ASP A CG    1 
ATOM   1733 O  OD1   . ASP A 1 238 ? 25.610  46.842  30.883  1.00 55.33  ? 238 ASP A OD1   1 
ATOM   1734 O  OD2   . ASP A 1 238 ? 25.778  46.790  28.669  1.00 56.88  ? 238 ASP A OD2   1 
ATOM   1735 N  N     . GLY A 1 239 ? 21.744  44.227  30.887  1.00 48.10  ? 239 GLY A N     1 
ATOM   1736 C  CA    . GLY A 1 239 ? 20.372  44.558  30.587  1.00 46.87  ? 239 GLY A CA    1 
ATOM   1737 C  C     . GLY A 1 239 ? 19.963  43.937  29.266  1.00 46.90  ? 239 GLY A C     1 
ATOM   1738 O  O     . GLY A 1 239 ? 20.720  43.984  28.302  1.00 47.91  ? 239 GLY A O     1 
ATOM   1739 N  N     . ILE A 1 240 ? 18.789  43.321  29.231  1.00 45.26  ? 240 ILE A N     1 
ATOM   1740 C  CA    . ILE A 1 240 ? 18.271  42.735  28.009  1.00 46.28  ? 240 ILE A CA    1 
ATOM   1741 C  C     . ILE A 1 240 ? 16.900  43.328  27.945  1.00 45.79  ? 240 ILE A C     1 
ATOM   1742 O  O     . ILE A 1 240 ? 16.223  43.371  28.965  1.00 46.34  ? 240 ILE A O     1 
ATOM   1743 C  CB    . ILE A 1 240 ? 18.001  41.222  28.117  1.00 49.96  ? 240 ILE A CB    1 
ATOM   1744 C  CG1   . ILE A 1 240 ? 18.664  40.671  29.373  1.00 52.56  ? 240 ILE A CG1   1 
ATOM   1745 C  CG2   . ILE A 1 240 ? 18.431  40.492  26.824  1.00 47.55  ? 240 ILE A CG2   1 
ATOM   1746 C  CD1   . ILE A 1 240 ? 20.167  40.770  29.363  1.00 57.83  ? 240 ILE A CD1   1 
ATOM   1747 N  N     . THR A 1 241 ? 16.480  43.815  26.789  1.00 44.07  ? 241 THR A N     1 
ATOM   1748 C  CA    . THR A 1 241 ? 15.106  44.283  26.698  1.00 42.84  ? 241 THR A CA    1 
ATOM   1749 C  C     . THR A 1 241 ? 14.386  43.174  25.935  1.00 43.43  ? 241 THR A C     1 
ATOM   1750 O  O     . THR A 1 241 ? 14.654  42.961  24.756  1.00 43.82  ? 241 THR A O     1 
ATOM   1751 C  CB    . THR A 1 241 ? 14.977  45.605  25.948  1.00 41.42  ? 241 THR A CB    1 
ATOM   1752 O  OG1   . THR A 1 241 ? 15.418  46.675  26.789  1.00 41.27  ? 241 THR A OG1   1 
ATOM   1753 C  CG2   . THR A 1 241 ? 13.544  45.850  25.568  1.00 40.44  ? 241 THR A CG2   1 
ATOM   1754 N  N     . ILE A 1 242 ? 13.514  42.437  26.620  1.00 43.18  ? 242 ILE A N     1 
ATOM   1755 C  CA    . ILE A 1 242 ? 12.780  41.350  25.981  1.00 45.13  ? 242 ILE A CA    1 
ATOM   1756 C  C     . ILE A 1 242 ? 11.506  41.859  25.320  1.00 45.31  ? 242 ILE A C     1 
ATOM   1757 O  O     . ILE A 1 242 ? 10.623  42.382  25.980  1.00 45.58  ? 242 ILE A O     1 
ATOM   1758 C  CB    . ILE A 1 242 ? 12.428  40.222  26.991  1.00 45.73  ? 242 ILE A CB    1 
ATOM   1759 C  CG1   . ILE A 1 242 ? 13.611  39.273  27.155  1.00 46.09  ? 242 ILE A CG1   1 
ATOM   1760 C  CG2   . ILE A 1 242 ? 11.280  39.396  26.468  1.00 45.14  ? 242 ILE A CG2   1 
ATOM   1761 C  CD1   . ILE A 1 242 ? 14.866  39.962  27.602  1.00 51.61  ? 242 ILE A CD1   1 
ATOM   1762 N  N     . CYS A 1 243 ? 11.416  41.676  24.010  1.00 47.07  ? 243 CYS A N     1 
ATOM   1763 C  CA    . CYS A 1 243 ? 10.272  42.149  23.237  1.00 48.50  ? 243 CYS A CA    1 
ATOM   1764 C  C     . CYS A 1 243 ? 9.406   41.023  22.712  1.00 49.68  ? 243 CYS A C     1 
ATOM   1765 O  O     . CYS A 1 243 ? 9.881   40.139  22.011  1.00 46.89  ? 243 CYS A O     1 
ATOM   1766 C  CB    . CYS A 1 243 ? 10.758  42.985  22.048  1.00 46.89  ? 243 CYS A CB    1 
ATOM   1767 S  SG    . CYS A 1 243 ? 11.879  44.309  22.514  1.00 46.45  ? 243 CYS A SG    1 
ATOM   1768 N  N     . ARG A 1 244 ? 8.125   41.073  23.049  1.00 52.66  ? 244 ARG A N     1 
ATOM   1769 C  CA    . ARG A 1 244 ? 7.184   40.071  22.587  1.00 54.86  ? 244 ARG A CA    1 
ATOM   1770 C  C     . ARG A 1 244 ? 6.378   40.733  21.489  1.00 56.28  ? 244 ARG A C     1 
ATOM   1771 O  O     . ARG A 1 244 ? 5.768   41.786  21.692  1.00 55.09  ? 244 ARG A O     1 
ATOM   1772 C  CB    . ARG A 1 244 ? 6.266   39.635  23.724  1.00 56.13  ? 244 ARG A CB    1 
ATOM   1773 C  CG    . ARG A 1 244 ? 5.347   38.502  23.363  1.00 59.30  ? 244 ARG A CG    1 
ATOM   1774 C  CD    . ARG A 1 244 ? 4.529   38.034  24.559  1.00 63.86  ? 244 ARG A CD    1 
ATOM   1775 N  NE    . ARG A 1 244 ? 3.217   37.594  24.098  1.00 66.82  ? 244 ARG A NE    1 
ATOM   1776 C  CZ    . ARG A 1 244 ? 2.178   38.408  23.941  1.00 67.41  ? 244 ARG A CZ    1 
ATOM   1777 N  NH1   . ARG A 1 244 ? 2.293   39.704  24.233  1.00 66.57  ? 244 ARG A NH1   1 
ATOM   1778 N  NH2   . ARG A 1 244 ? 1.044   37.938  23.436  1.00 67.20  ? 244 ARG A NH2   1 
ATOM   1779 N  N     . ARG A 1 245 ? 6.397   40.135  20.308  1.00 57.75  ? 245 ARG A N     1 
ATOM   1780 C  CA    . ARG A 1 245 ? 5.648   40.711  19.211  1.00 59.98  ? 245 ARG A CA    1 
ATOM   1781 C  C     . ARG A 1 245 ? 4.170   40.418  19.393  1.00 62.51  ? 245 ARG A C     1 
ATOM   1782 O  O     . ARG A 1 245 ? 3.796   39.286  19.678  1.00 63.59  ? 245 ARG A O     1 
ATOM   1783 C  CB    . ARG A 1 245 ? 6.116   40.136  17.893  1.00 58.46  ? 245 ARG A CB    1 
ATOM   1784 C  CG    . ARG A 1 245 ? 5.447   40.789  16.740  1.00 56.48  ? 245 ARG A CG    1 
ATOM   1785 C  CD    . ARG A 1 245 ? 5.698   40.032  15.488  1.00 56.59  ? 245 ARG A CD    1 
ATOM   1786 N  NE    . ARG A 1 245 ? 4.833   40.547  14.444  1.00 57.57  ? 245 ARG A NE    1 
ATOM   1787 C  CZ    . ARG A 1 245 ? 4.767   40.043  13.224  1.00 56.86  ? 245 ARG A CZ    1 
ATOM   1788 N  NH1   . ARG A 1 245 ? 5.522   39.008  12.901  1.00 57.55  ? 245 ARG A NH1   1 
ATOM   1789 N  NH2   . ARG A 1 245 ? 3.948   40.579  12.334  1.00 56.18  ? 245 ARG A NH2   1 
ATOM   1790 N  N     . ILE A 1 246 ? 3.328   41.434  19.233  1.00 66.18  ? 246 ILE A N     1 
ATOM   1791 C  CA    . ILE A 1 246 ? 1.895   41.234  19.393  1.00 68.38  ? 246 ILE A CA    1 
ATOM   1792 C  C     . ILE A 1 246 ? 1.158   41.345  18.067  1.00 70.03  ? 246 ILE A C     1 
ATOM   1793 O  O     . ILE A 1 246 ? -0.005  40.956  17.968  1.00 70.82  ? 246 ILE A O     1 
ATOM   1794 C  CB    . ILE A 1 246 ? 1.308   42.199  20.448  1.00 68.04  ? 246 ILE A CB    1 
ATOM   1795 C  CG1   . ILE A 1 246 ? 1.513   43.646  20.027  1.00 68.28  ? 246 ILE A CG1   1 
ATOM   1796 C  CG2   . ILE A 1 246 ? 2.006   41.959  21.788  1.00 67.75  ? 246 ILE A CG2   1 
ATOM   1797 C  CD1   . ILE A 1 246 ? 1.074   44.657  21.073  1.00 67.90  ? 246 ILE A CD1   1 
ATOM   1798 N  N     . LYS A 1 247 ? 1.861   41.841  17.048  1.00 72.00  ? 247 LYS A N     1 
ATOM   1799 C  CA    . LYS A 1 247 ? 1.335   41.955  15.683  1.00 73.66  ? 247 LYS A CA    1 
ATOM   1800 C  C     . LYS A 1 247 ? 2.272   42.725  14.744  1.00 74.70  ? 247 LYS A C     1 
ATOM   1801 O  O     . LYS A 1 247 ? 3.150   43.479  15.236  1.00 74.51  ? 247 LYS A O     1 
ATOM   1802 C  CB    . LYS A 1 247 ? -0.066  42.591  15.681  1.00 73.36  ? 247 LYS A CB    1 
ATOM   1803 C  CG    . LYS A 1 247 ? -0.166  43.979  16.286  1.00 73.51  ? 247 LYS A CG    1 
ATOM   1804 C  CD    . LYS A 1 247 ? 0.120   45.062  15.259  1.00 75.13  ? 247 LYS A CD    1 
ATOM   1805 C  CE    . LYS A 1 247 ? -0.180  46.457  15.810  1.00 75.14  ? 247 LYS A CE    1 
ATOM   1806 N  NZ    . LYS A 1 247 ? -1.606  46.599  16.216  1.00 74.74  ? 247 LYS A NZ    1 
ATOM   1807 O  OXT   . LYS A 1 247 ? 2.114   42.558  13.512  1.00 75.67  ? 247 LYS A OXT   1 
ATOM   1808 N  N     . LYS B 1 21  ? -1.622  9.429   -4.770  1.00 74.28  ? 21  LYS B N     1 
ATOM   1809 C  CA    . LYS B 1 21  ? -1.506  7.957   -4.568  1.00 74.83  ? 21  LYS B CA    1 
ATOM   1810 C  C     . LYS B 1 21  ? -0.062  7.446   -4.673  1.00 73.71  ? 21  LYS B C     1 
ATOM   1811 O  O     . LYS B 1 21  ? 0.680   7.802   -5.593  1.00 75.20  ? 21  LYS B O     1 
ATOM   1812 C  CB    . LYS B 1 21  ? -2.379  7.226   -5.587  1.00 76.47  ? 21  LYS B CB    1 
ATOM   1813 C  CG    . LYS B 1 21  ? -2.213  5.719   -5.592  1.00 79.12  ? 21  LYS B CG    1 
ATOM   1814 C  CD    . LYS B 1 21  ? -3.186  5.071   -6.571  1.00 83.65  ? 21  LYS B CD    1 
ATOM   1815 C  CE    . LYS B 1 21  ? -4.645  5.404   -6.218  1.00 85.44  ? 21  LYS B CE    1 
ATOM   1816 N  NZ    . LYS B 1 21  ? -5.637  4.920   -7.230  1.00 85.63  ? 21  LYS B NZ    1 
ATOM   1817 N  N     . SER B 1 22  ? 0.325   6.609   -3.714  1.00 70.40  ? 22  SER B N     1 
ATOM   1818 C  CA    . SER B 1 22  ? 1.657   6.012   -3.674  1.00 65.04  ? 22  SER B CA    1 
ATOM   1819 C  C     . SER B 1 22  ? 1.451   4.515   -3.760  1.00 62.53  ? 22  SER B C     1 
ATOM   1820 O  O     . SER B 1 22  ? 0.341   4.055   -4.034  1.00 62.23  ? 22  SER B O     1 
ATOM   1821 C  CB    . SER B 1 22  ? 2.360   6.336   -2.360  1.00 64.83  ? 22  SER B CB    1 
ATOM   1822 O  OG    . SER B 1 22  ? 1.649   5.790   -1.262  1.00 61.54  ? 22  SER B OG    1 
ATOM   1823 N  N     . LEU B 1 23  ? 2.507   3.751   -3.516  1.00 59.03  ? 23  LEU B N     1 
ATOM   1824 C  CA    . LEU B 1 23  ? 2.390   2.301   -3.580  1.00 57.04  ? 23  LEU B CA    1 
ATOM   1825 C  C     . LEU B 1 23  ? 2.071   1.673   -2.229  1.00 55.51  ? 23  LEU B C     1 
ATOM   1826 O  O     . LEU B 1 23  ? 1.907   0.460   -2.131  1.00 56.51  ? 23  LEU B O     1 
ATOM   1827 C  CB    . LEU B 1 23  ? 3.681   1.682   -4.121  1.00 55.97  ? 23  LEU B CB    1 
ATOM   1828 C  CG    . LEU B 1 23  ? 4.090   2.104   -5.520  1.00 55.25  ? 23  LEU B CG    1 
ATOM   1829 C  CD1   . LEU B 1 23  ? 5.374   1.396   -5.912  1.00 54.64  ? 23  LEU B CD1   1 
ATOM   1830 C  CD2   . LEU B 1 23  ? 2.971   1.783   -6.471  1.00 53.13  ? 23  LEU B CD2   1 
ATOM   1831 N  N     . LEU B 1 24  ? 1.985   2.483   -1.184  1.00 53.13  ? 24  LEU B N     1 
ATOM   1832 C  CA    . LEU B 1 24  ? 1.708   1.942   0.135   1.00 52.27  ? 24  LEU B CA    1 
ATOM   1833 C  C     . LEU B 1 24  ? 0.197   1.810   0.331   1.00 52.95  ? 24  LEU B C     1 
ATOM   1834 O  O     . LEU B 1 24  ? -0.575  2.220   -0.524  1.00 53.18  ? 24  LEU B O     1 
ATOM   1835 C  CB    . LEU B 1 24  ? 2.313   2.854   1.195   1.00 51.20  ? 24  LEU B CB    1 
ATOM   1836 C  CG    . LEU B 1 24  ? 3.741   3.334   0.943   1.00 48.37  ? 24  LEU B CG    1 
ATOM   1837 C  CD1   . LEU B 1 24  ? 4.116   4.277   2.033   1.00 49.75  ? 24  LEU B CD1   1 
ATOM   1838 C  CD2   . LEU B 1 24  ? 4.701   2.183   0.900   1.00 48.67  ? 24  LEU B CD2   1 
ATOM   1839 N  N     . GLN B 1 25  ? -0.229  1.238   1.453   1.00 53.65  ? 25  GLN B N     1 
ATOM   1840 C  CA    . GLN B 1 25  ? -1.651  1.071   1.696   1.00 53.29  ? 25  GLN B CA    1 
ATOM   1841 C  C     . GLN B 1 25  ? -2.412  2.374   1.807   1.00 54.00  ? 25  GLN B C     1 
ATOM   1842 O  O     . GLN B 1 25  ? -3.603  2.404   1.529   1.00 56.32  ? 25  GLN B O     1 
ATOM   1843 C  CB    . GLN B 1 25  ? -1.919  0.255   2.964   1.00 52.17  ? 25  GLN B CB    1 
ATOM   1844 C  CG    . GLN B 1 25  ? -0.721  -0.106  3.805   1.00 51.34  ? 25  GLN B CG    1 
ATOM   1845 C  CD    . GLN B 1 25  ? -1.123  -0.457  5.232   1.00 51.83  ? 25  GLN B CD    1 
ATOM   1846 O  OE1   . GLN B 1 25  ? -1.449  0.426   6.027   1.00 52.89  ? 25  GLN B OE1   1 
ATOM   1847 N  NE2   . GLN B 1 25  ? -1.120  -1.745  5.557   1.00 50.29  ? 25  GLN B NE2   1 
ATOM   1848 N  N     . SER B 1 26  ? -1.747  3.452   2.200   1.00 53.69  ? 26  SER B N     1 
ATOM   1849 C  CA    . SER B 1 26  ? -2.452  4.719   2.352   1.00 54.85  ? 26  SER B CA    1 
ATOM   1850 C  C     . SER B 1 26  ? -1.575  5.960   2.256   1.00 55.98  ? 26  SER B C     1 
ATOM   1851 O  O     . SER B 1 26  ? -0.430  5.968   2.710   1.00 57.35  ? 26  SER B O     1 
ATOM   1852 C  CB    . SER B 1 26  ? -3.157  4.738   3.700   1.00 54.50  ? 26  SER B CB    1 
ATOM   1853 O  OG    . SER B 1 26  ? -2.207  4.801   4.751   1.00 57.49  ? 26  SER B OG    1 
ATOM   1854 N  N     . ASP B 1 27  ? -2.128  7.022   1.687   1.00 56.86  ? 27  ASP B N     1 
ATOM   1855 C  CA    . ASP B 1 27  ? -1.392  8.267   1.554   1.00 57.84  ? 27  ASP B CA    1 
ATOM   1856 C  C     . ASP B 1 27  ? -1.008  8.765   2.941   1.00 56.96  ? 27  ASP B C     1 
ATOM   1857 O  O     . ASP B 1 27  ? 0.011   9.437   3.112   1.00 57.43  ? 27  ASP B O     1 
ATOM   1858 C  CB    . ASP B 1 27  ? -2.250  9.315   0.846   1.00 61.66  ? 27  ASP B CB    1 
ATOM   1859 C  CG    . ASP B 1 27  ? -2.781  8.821   -0.479  1.00 65.59  ? 27  ASP B CG    1 
ATOM   1860 O  OD1   . ASP B 1 27  ? -1.960  8.309   -1.274  1.00 68.42  ? 27  ASP B OD1   1 
ATOM   1861 O  OD2   . ASP B 1 27  ? -4.005  8.941   -0.725  1.00 67.95  ? 27  ASP B OD2   1 
ATOM   1862 N  N     . ALA B 1 28  ? -1.825  8.434   3.934   1.00 54.96  ? 28  ALA B N     1 
ATOM   1863 C  CA    . ALA B 1 28  ? -1.537  8.862   5.284   1.00 53.15  ? 28  ALA B CA    1 
ATOM   1864 C  C     . ALA B 1 28  ? -0.246  8.186   5.728   1.00 52.32  ? 28  ALA B C     1 
ATOM   1865 O  O     . ALA B 1 28  ? 0.588   8.801   6.388   1.00 52.37  ? 28  ALA B O     1 
ATOM   1866 C  CB    . ALA B 1 28  ? -2.678  8.493   6.196   1.00 52.86  ? 28  ALA B CB    1 
ATOM   1867 N  N     . LEU B 1 29  ? -0.071  6.923   5.347   1.00 51.87  ? 29  LEU B N     1 
ATOM   1868 C  CA    . LEU B 1 29  ? 1.133   6.198   5.720   1.00 51.07  ? 29  LEU B CA    1 
ATOM   1869 C  C     . LEU B 1 29  ? 2.340   6.730   4.965   1.00 50.81  ? 29  LEU B C     1 
ATOM   1870 O  O     . LEU B 1 29  ? 3.407   6.915   5.533   1.00 51.93  ? 29  LEU B O     1 
ATOM   1871 C  CB    . LEU B 1 29  ? 0.984   4.704   5.444   1.00 51.21  ? 29  LEU B CB    1 
ATOM   1872 C  CG    . LEU B 1 29  ? 2.229   3.891   5.817   1.00 51.06  ? 29  LEU B CG    1 
ATOM   1873 C  CD1   . LEU B 1 29  ? 2.515   4.044   7.289   1.00 50.37  ? 29  LEU B CD1   1 
ATOM   1874 C  CD2   . LEU B 1 29  ? 2.019   2.447   5.472   1.00 50.46  ? 29  LEU B CD2   1 
ATOM   1875 N  N     . TYR B 1 30  ? 2.182   6.970   3.675   1.00 50.77  ? 30  TYR B N     1 
ATOM   1876 C  CA    . TYR B 1 30  ? 3.290   7.497   2.910   1.00 49.38  ? 30  TYR B CA    1 
ATOM   1877 C  C     . TYR B 1 30  ? 3.670   8.880   3.449   1.00 50.25  ? 30  TYR B C     1 
ATOM   1878 O  O     . TYR B 1 30  ? 4.856   9.190   3.553   1.00 50.94  ? 30  TYR B O     1 
ATOM   1879 C  CB    . TYR B 1 30  ? 2.913   7.555   1.436   1.00 49.18  ? 30  TYR B CB    1 
ATOM   1880 C  CG    . TYR B 1 30  ? 3.920   8.256   0.561   1.00 49.96  ? 30  TYR B CG    1 
ATOM   1881 C  CD1   . TYR B 1 30  ? 3.853   9.630   0.368   1.00 49.61  ? 30  TYR B CD1   1 
ATOM   1882 C  CD2   . TYR B 1 30  ? 4.920   7.546   -0.097  1.00 50.03  ? 30  TYR B CD2   1 
ATOM   1883 C  CE1   . TYR B 1 30  ? 4.741   10.282  -0.455  1.00 49.71  ? 30  TYR B CE1   1 
ATOM   1884 C  CE2   . TYR B 1 30  ? 5.821   8.195   -0.929  1.00 50.40  ? 30  TYR B CE2   1 
ATOM   1885 C  CZ    . TYR B 1 30  ? 5.720   9.568   -1.103  1.00 50.59  ? 30  TYR B CZ    1 
ATOM   1886 O  OH    . TYR B 1 30  ? 6.582   10.241  -1.940  1.00 51.47  ? 30  TYR B OH    1 
ATOM   1887 N  N     . GLN B 1 31  ? 2.671   9.699   3.800   1.00 49.86  ? 31  GLN B N     1 
ATOM   1888 C  CA    . GLN B 1 31  ? 2.914   11.043  4.351   1.00 48.30  ? 31  GLN B CA    1 
ATOM   1889 C  C     . GLN B 1 31  ? 3.676   10.949  5.657   1.00 48.21  ? 31  GLN B C     1 
ATOM   1890 O  O     . GLN B 1 31  ? 4.494   11.820  5.970   1.00 47.52  ? 31  GLN B O     1 
ATOM   1891 C  CB    . GLN B 1 31  ? 1.601   11.790  4.627   1.00 48.40  ? 31  GLN B CB    1 
ATOM   1892 C  CG    . GLN B 1 31  ? 1.038   12.548  3.433   1.00 50.30  ? 31  GLN B CG    1 
ATOM   1893 C  CD    . GLN B 1 31  ? 2.057   13.496  2.811   1.00 51.33  ? 31  GLN B CD    1 
ATOM   1894 O  OE1   . GLN B 1 31  ? 2.390   13.371  1.618   1.00 50.56  ? 31  GLN B OE1   1 
ATOM   1895 N  NE2   . GLN B 1 31  ? 2.565   14.449  3.615   1.00 47.06  ? 31  GLN B NE2   1 
ATOM   1896 N  N     . TYR B 1 32  ? 3.389   9.890   6.414   1.00 46.46  ? 32  TYR B N     1 
ATOM   1897 C  CA    . TYR B 1 32  ? 4.024   9.660   7.699   1.00 45.56  ? 32  TYR B CA    1 
ATOM   1898 C  C     . TYR B 1 32  ? 5.517   9.506   7.483   1.00 45.29  ? 32  TYR B C     1 
ATOM   1899 O  O     . TYR B 1 32  ? 6.311   10.099  8.216   1.00 45.93  ? 32  TYR B O     1 
ATOM   1900 C  CB    . TYR B 1 32  ? 3.446   8.404   8.365   1.00 45.04  ? 32  TYR B CB    1 
ATOM   1901 C  CG    . TYR B 1 32  ? 4.131   8.026   9.656   1.00 45.44  ? 32  TYR B CG    1 
ATOM   1902 C  CD1   . TYR B 1 32  ? 3.891   8.729   10.831  1.00 45.40  ? 32  TYR B CD1   1 
ATOM   1903 C  CD2   . TYR B 1 32  ? 5.060   6.995   9.691   1.00 46.51  ? 32  TYR B CD2   1 
ATOM   1904 C  CE1   . TYR B 1 32  ? 4.562   8.418   12.005  1.00 45.08  ? 32  TYR B CE1   1 
ATOM   1905 C  CE2   . TYR B 1 32  ? 5.742   6.677   10.864  1.00 46.84  ? 32  TYR B CE2   1 
ATOM   1906 C  CZ    . TYR B 1 32  ? 5.491   7.397   12.013  1.00 46.19  ? 32  TYR B CZ    1 
ATOM   1907 O  OH    . TYR B 1 32  ? 6.212   7.121   13.153  1.00 47.30  ? 32  TYR B OH    1 
ATOM   1908 N  N     . ILE B 1 33  ? 5.886   8.719   6.469   1.00 43.84  ? 33  ILE B N     1 
ATOM   1909 C  CA    . ILE B 1 33  ? 7.280   8.479   6.139   1.00 42.53  ? 33  ILE B CA    1 
ATOM   1910 C  C     . ILE B 1 33  ? 7.947   9.793   5.794   1.00 43.84  ? 33  ILE B C     1 
ATOM   1911 O  O     . ILE B 1 33  ? 8.962   10.148  6.387   1.00 45.67  ? 33  ILE B O     1 
ATOM   1912 C  CB    . ILE B 1 33  ? 7.422   7.550   4.942   1.00 41.10  ? 33  ILE B CB    1 
ATOM   1913 C  CG1   . ILE B 1 33  ? 6.907   6.166   5.298   1.00 41.77  ? 33  ILE B CG1   1 
ATOM   1914 C  CG2   . ILE B 1 33  ? 8.873   7.450   4.529   1.00 39.48  ? 33  ILE B CG2   1 
ATOM   1915 C  CD1   . ILE B 1 33  ? 6.992   5.196   4.137   1.00 40.42  ? 33  ILE B CD1   1 
ATOM   1916 N  N     . LEU B 1 34  ? 7.373   10.515  4.838   1.00 44.50  ? 34  LEU B N     1 
ATOM   1917 C  CA    . LEU B 1 34  ? 7.918   11.798  4.415   1.00 46.00  ? 34  LEU B CA    1 
ATOM   1918 C  C     . LEU B 1 34  ? 8.053   12.732  5.588   1.00 47.66  ? 34  LEU B C     1 
ATOM   1919 O  O     . LEU B 1 34  ? 9.126   13.269  5.844   1.00 47.22  ? 34  LEU B O     1 
ATOM   1920 C  CB    . LEU B 1 34  ? 7.014   12.465  3.385   1.00 45.40  ? 34  LEU B CB    1 
ATOM   1921 C  CG    . LEU B 1 34  ? 6.799   11.767  2.046   1.00 45.60  ? 34  LEU B CG    1 
ATOM   1922 C  CD1   . LEU B 1 34  ? 5.843   12.604  1.257   1.00 46.16  ? 34  LEU B CD1   1 
ATOM   1923 C  CD2   . LEU B 1 34  ? 8.099   11.581  1.287   1.00 43.94  ? 34  LEU B CD2   1 
ATOM   1924 N  N     . GLU B 1 35  ? 6.958   12.930  6.307   1.00 50.54  ? 35  GLU B N     1 
ATOM   1925 C  CA    . GLU B 1 35  ? 6.982   13.830  7.443   1.00 53.73  ? 35  GLU B CA    1 
ATOM   1926 C  C     . GLU B 1 35  ? 7.949   13.451  8.545   1.00 53.67  ? 35  GLU B C     1 
ATOM   1927 O  O     . GLU B 1 35  ? 8.593   14.327  9.116   1.00 54.27  ? 35  GLU B O     1 
ATOM   1928 C  CB    . GLU B 1 35  ? 5.578   13.998  8.029   1.00 57.59  ? 35  GLU B CB    1 
ATOM   1929 C  CG    . GLU B 1 35  ? 4.864   15.274  7.568   1.00 63.87  ? 35  GLU B CG    1 
ATOM   1930 C  CD    . GLU B 1 35  ? 3.375   15.056  7.277   1.00 68.66  ? 35  GLU B CD    1 
ATOM   1931 O  OE1   . GLU B 1 35  ? 2.641   14.564  8.180   1.00 70.06  ? 35  GLU B OE1   1 
ATOM   1932 O  OE2   . GLU B 1 35  ? 2.944   15.380  6.136   1.00 69.50  ? 35  GLU B OE2   1 
ATOM   1933 N  N     . THR B 1 36  ? 8.086   12.168  8.856   1.00 53.66  ? 36  THR B N     1 
ATOM   1934 C  CA    . THR B 1 36  ? 8.991   11.838  9.947   1.00 54.97  ? 36  THR B CA    1 
ATOM   1935 C  C     . THR B 1 36  ? 10.416  11.526  9.529   1.00 54.40  ? 36  THR B C     1 
ATOM   1936 O  O     . THR B 1 36  ? 11.331  11.653  10.341  1.00 55.06  ? 36  THR B O     1 
ATOM   1937 C  CB    . THR B 1 36  ? 8.490   10.645  10.819  1.00 55.35  ? 36  THR B CB    1 
ATOM   1938 O  OG1   . THR B 1 36  ? 8.868   9.416   10.202  1.00 58.38  ? 36  THR B OG1   1 
ATOM   1939 C  CG2   . THR B 1 36  ? 6.981   10.671  10.977  1.00 55.90  ? 36  THR B CG2   1 
ATOM   1940 N  N     . SER B 1 37  ? 10.630  11.134  8.279   1.00 53.10  ? 37  SER B N     1 
ATOM   1941 C  CA    . SER B 1 37  ? 11.988  10.795  7.889   1.00 52.33  ? 37  SER B CA    1 
ATOM   1942 C  C     . SER B 1 37  ? 12.664  11.595  6.783   1.00 51.34  ? 37  SER B C     1 
ATOM   1943 O  O     . SER B 1 37  ? 13.882  11.563  6.696   1.00 51.82  ? 37  SER B O     1 
ATOM   1944 C  CB    . SER B 1 37  ? 12.069  9.302   7.549   1.00 53.02  ? 37  SER B CB    1 
ATOM   1945 O  OG    . SER B 1 37  ? 11.560  9.016   6.254   1.00 54.42  ? 37  SER B OG    1 
ATOM   1946 N  N     . VAL B 1 38  ? 11.911  12.314  5.952   1.00 50.93  ? 38  VAL B N     1 
ATOM   1947 C  CA    . VAL B 1 38  ? 12.524  13.071  4.853   1.00 50.47  ? 38  VAL B CA    1 
ATOM   1948 C  C     . VAL B 1 38  ? 12.541  14.600  4.963   1.00 52.16  ? 38  VAL B C     1 
ATOM   1949 O  O     . VAL B 1 38  ? 13.598  15.228  4.867   1.00 51.26  ? 38  VAL B O     1 
ATOM   1950 C  CB    . VAL B 1 38  ? 11.855  12.765  3.521   1.00 48.85  ? 38  VAL B CB    1 
ATOM   1951 C  CG1   . VAL B 1 38  ? 12.776  13.191  2.410   1.00 49.50  ? 38  VAL B CG1   1 
ATOM   1952 C  CG2   . VAL B 1 38  ? 11.502  11.296  3.418   1.00 47.78  ? 38  VAL B CG2   1 
ATOM   1953 N  N     . PHE B 1 39  ? 11.364  15.195  5.139   1.00 52.98  ? 39  PHE B N     1 
ATOM   1954 C  CA    . PHE B 1 39  ? 11.253  16.641  5.224   1.00 52.48  ? 39  PHE B CA    1 
ATOM   1955 C  C     . PHE B 1 39  ? 12.162  17.226  6.288   1.00 54.71  ? 39  PHE B C     1 
ATOM   1956 O  O     . PHE B 1 39  ? 12.950  18.129  6.009   1.00 56.33  ? 39  PHE B O     1 
ATOM   1957 C  CB    . PHE B 1 39  ? 9.797   17.056  5.476   1.00 49.78  ? 39  PHE B CB    1 
ATOM   1958 C  CG    . PHE B 1 39  ? 8.869   16.729  4.334   1.00 47.78  ? 39  PHE B CG    1 
ATOM   1959 C  CD1   . PHE B 1 39  ? 9.367   16.545  3.043   1.00 43.59  ? 39  PHE B CD1   1 
ATOM   1960 C  CD2   . PHE B 1 39  ? 7.495   16.596  4.546   1.00 46.61  ? 39  PHE B CD2   1 
ATOM   1961 C  CE1   . PHE B 1 39  ? 8.519   16.229  1.982   1.00 42.28  ? 39  PHE B CE1   1 
ATOM   1962 C  CE2   . PHE B 1 39  ? 6.638   16.279  3.479   1.00 46.33  ? 39  PHE B CE2   1 
ATOM   1963 C  CZ    . PHE B 1 39  ? 7.157   16.095  2.194   1.00 42.71  ? 39  PHE B CZ    1 
ATOM   1964 N  N     . PRO B 1 40  ? 12.086  16.710  7.522   1.00 55.89  ? 40  PRO B N     1 
ATOM   1965 C  CA    . PRO B 1 40  ? 12.944  17.245  8.586   1.00 55.85  ? 40  PRO B CA    1 
ATOM   1966 C  C     . PRO B 1 40  ? 14.444  17.102  8.311   1.00 56.81  ? 40  PRO B C     1 
ATOM   1967 O  O     . PRO B 1 40  ? 15.250  17.889  8.796   1.00 57.51  ? 40  PRO B O     1 
ATOM   1968 C  CB    . PRO B 1 40  ? 12.510  16.442  9.802   1.00 55.23  ? 40  PRO B CB    1 
ATOM   1969 C  CG    . PRO B 1 40  ? 12.180  15.117  9.207   1.00 56.92  ? 40  PRO B CG    1 
ATOM   1970 C  CD    . PRO B 1 40  ? 11.387  15.492  7.970   1.00 54.86  ? 40  PRO B CD    1 
ATOM   1971 N  N     . ARG B 1 41  ? 14.808  16.110  7.510   1.00 57.74  ? 41  ARG B N     1 
ATOM   1972 C  CA    . ARG B 1 41  ? 16.203  15.840  7.203   1.00 58.41  ? 41  ARG B CA    1 
ATOM   1973 C  C     . ARG B 1 41  ? 16.733  16.341  5.853   1.00 58.10  ? 41  ARG B C     1 
ATOM   1974 O  O     . ARG B 1 41  ? 17.928  16.597  5.707   1.00 55.43  ? 41  ARG B O     1 
ATOM   1975 C  CB    . ARG B 1 41  ? 16.429  14.335  7.279   1.00 60.55  ? 41  ARG B CB    1 
ATOM   1976 C  CG    . ARG B 1 41  ? 16.276  13.722  8.655   1.00 62.97  ? 41  ARG B CG    1 
ATOM   1977 C  CD    . ARG B 1 41  ? 17.637  13.562  9.311   1.00 65.64  ? 41  ARG B CD    1 
ATOM   1978 N  NE    . ARG B 1 41  ? 17.630  12.534  10.349  1.00 66.12  ? 41  ARG B NE    1 
ATOM   1979 C  CZ    . ARG B 1 41  ? 18.700  12.177  11.049  1.00 65.92  ? 41  ARG B CZ    1 
ATOM   1980 N  NH1   . ARG B 1 41  ? 19.871  12.768  10.823  1.00 65.32  ? 41  ARG B NH1   1 
ATOM   1981 N  NH2   . ARG B 1 41  ? 18.598  11.224  11.965  1.00 65.18  ? 41  ARG B NH2   1 
ATOM   1982 N  N     . GLU B 1 42  ? 15.848  16.471  4.872   1.00 58.82  ? 42  GLU B N     1 
ATOM   1983 C  CA    . GLU B 1 42  ? 16.249  16.875  3.521   1.00 59.14  ? 42  GLU B CA    1 
ATOM   1984 C  C     . GLU B 1 42  ? 16.972  18.209  3.403   1.00 58.74  ? 42  GLU B C     1 
ATOM   1985 O  O     . GLU B 1 42  ? 16.778  19.116  4.206   1.00 58.86  ? 42  GLU B O     1 
ATOM   1986 C  CB    . GLU B 1 42  ? 15.035  16.889  2.591   1.00 58.77  ? 42  GLU B CB    1 
ATOM   1987 C  CG    . GLU B 1 42  ? 14.204  18.147  2.698   1.00 60.68  ? 42  GLU B CG    1 
ATOM   1988 C  CD    . GLU B 1 42  ? 13.026  18.136  1.755   1.00 61.70  ? 42  GLU B CD    1 
ATOM   1989 O  OE1   . GLU B 1 42  ? 13.202  17.675  0.607   1.00 60.72  ? 42  GLU B OE1   1 
ATOM   1990 O  OE2   . GLU B 1 42  ? 11.935  18.600  2.161   1.00 62.88  ? 42  GLU B OE2   1 
ATOM   1991 N  N     . HIS B 1 43  ? 17.800  18.303  2.373   1.00 57.78  ? 43  HIS B N     1 
ATOM   1992 C  CA    . HIS B 1 43  ? 18.573  19.496  2.074   1.00 58.67  ? 43  HIS B CA    1 
ATOM   1993 C  C     . HIS B 1 43  ? 17.674  20.596  1.474   1.00 60.13  ? 43  HIS B C     1 
ATOM   1994 O  O     . HIS B 1 43  ? 16.719  20.306  0.741   1.00 60.65  ? 43  HIS B O     1 
ATOM   1995 C  CB    . HIS B 1 43  ? 19.675  19.097  1.095   1.00 58.34  ? 43  HIS B CB    1 
ATOM   1996 C  CG    . HIS B 1 43  ? 20.669  20.177  0.802   1.00 57.48  ? 43  HIS B CG    1 
ATOM   1997 N  ND1   . HIS B 1 43  ? 22.010  19.911  0.617   1.00 56.74  ? 43  HIS B ND1   1 
ATOM   1998 C  CD2   . HIS B 1 43  ? 20.513  21.502  0.580   1.00 56.73  ? 43  HIS B CD2   1 
ATOM   1999 C  CE1   . HIS B 1 43  ? 22.636  21.026  0.292   1.00 56.65  ? 43  HIS B CE1   1 
ATOM   2000 N  NE2   . HIS B 1 43  ? 21.750  22.005  0.261   1.00 56.96  ? 43  HIS B NE2   1 
ATOM   2001 N  N     . GLU B 1 44  ? 17.981  21.854  1.787   1.00 60.75  ? 44  GLU B N     1 
ATOM   2002 C  CA    . GLU B 1 44  ? 17.209  22.994  1.288   1.00 60.31  ? 44  GLU B CA    1 
ATOM   2003 C  C     . GLU B 1 44  ? 17.038  22.932  -0.218  1.00 57.81  ? 44  GLU B C     1 
ATOM   2004 O  O     . GLU B 1 44  ? 15.917  23.015  -0.725  1.00 55.79  ? 44  GLU B O     1 
ATOM   2005 C  CB    . GLU B 1 44  ? 17.903  24.301  1.662   1.00 64.55  ? 44  GLU B CB    1 
ATOM   2006 C  CG    . GLU B 1 44  ? 18.114  24.459  3.161   1.00 73.15  ? 44  GLU B CG    1 
ATOM   2007 C  CD    . GLU B 1 44  ? 17.004  25.243  3.842   1.00 77.20  ? 44  GLU B CD    1 
ATOM   2008 O  OE1   . GLU B 1 44  ? 17.007  26.491  3.703   1.00 80.72  ? 44  GLU B OE1   1 
ATOM   2009 O  OE2   . GLU B 1 44  ? 16.136  24.620  4.507   1.00 78.26  ? 44  GLU B OE2   1 
ATOM   2010 N  N     . ALA B 1 45  ? 18.158  22.787  -0.923  1.00 55.75  ? 45  ALA B N     1 
ATOM   2011 C  CA    . ALA B 1 45  ? 18.151  22.716  -2.378  1.00 54.73  ? 45  ALA B CA    1 
ATOM   2012 C  C     . ALA B 1 45  ? 17.099  21.740  -2.872  1.00 54.62  ? 45  ALA B C     1 
ATOM   2013 O  O     . ALA B 1 45  ? 16.489  21.953  -3.910  1.00 56.28  ? 45  ALA B O     1 
ATOM   2014 C  CB    . ALA B 1 45  ? 19.512  22.296  -2.885  1.00 53.25  ? 45  ALA B CB    1 
ATOM   2015 N  N     . MET B 1 46  ? 16.877  20.670  -2.126  1.00 53.87  ? 46  MET B N     1 
ATOM   2016 C  CA    . MET B 1 46  ? 15.900  19.680  -2.535  1.00 53.51  ? 46  MET B CA    1 
ATOM   2017 C  C     . MET B 1 46  ? 14.492  20.230  -2.492  1.00 52.32  ? 46  MET B C     1 
ATOM   2018 O  O     . MET B 1 46  ? 13.679  19.923  -3.354  1.00 51.95  ? 46  MET B O     1 
ATOM   2019 C  CB    . MET B 1 46  ? 15.977  18.428  -1.649  1.00 54.36  ? 46  MET B CB    1 
ATOM   2020 C  CG    . MET B 1 46  ? 17.280  17.646  -1.742  1.00 54.48  ? 46  MET B CG    1 
ATOM   2021 S  SD    . MET B 1 46  ? 17.755  17.173  -3.418  1.00 55.70  ? 46  MET B SD    1 
ATOM   2022 C  CE    . MET B 1 46  ? 16.579  15.929  -3.791  1.00 57.67  ? 46  MET B CE    1 
ATOM   2023 N  N     . LYS B 1 47  ? 14.191  21.035  -1.486  1.00 52.42  ? 47  LYS B N     1 
ATOM   2024 C  CA    . LYS B 1 47  ? 12.848  21.576  -1.380  1.00 52.84  ? 47  LYS B CA    1 
ATOM   2025 C  C     . LYS B 1 47  ? 12.616  22.632  -2.459  1.00 52.56  ? 47  LYS B C     1 
ATOM   2026 O  O     . LYS B 1 47  ? 11.515  22.767  -2.977  1.00 51.21  ? 47  LYS B O     1 
ATOM   2027 C  CB    . LYS B 1 47  ? 12.631  22.161  0.007   1.00 53.74  ? 47  LYS B CB    1 
ATOM   2028 C  CG    . LYS B 1 47  ? 11.168  22.328  0.366   1.00 58.00  ? 47  LYS B CG    1 
ATOM   2029 C  CD    . LYS B 1 47  ? 10.985  22.964  1.759   1.00 60.63  ? 47  LYS B CD    1 
ATOM   2030 C  CE    . LYS B 1 47  ? 9.518   22.925  2.222   1.00 61.44  ? 47  LYS B CE    1 
ATOM   2031 N  NZ    . LYS B 1 47  ? 9.288   23.528  3.575   1.00 61.61  ? 47  LYS B NZ    1 
ATOM   2032 N  N     . GLU B 1 48  ? 13.671  23.366  -2.801  1.00 52.57  ? 48  GLU B N     1 
ATOM   2033 C  CA    . GLU B 1 48  ? 13.604  24.396  -3.829  1.00 52.56  ? 48  GLU B CA    1 
ATOM   2034 C  C     . GLU B 1 48  ? 13.295  23.793  -5.187  1.00 51.62  ? 48  GLU B C     1 
ATOM   2035 O  O     . GLU B 1 48  ? 12.458  24.306  -5.932  1.00 51.60  ? 48  GLU B O     1 
ATOM   2036 C  CB    . GLU B 1 48  ? 14.935  25.138  -3.946  1.00 55.34  ? 48  GLU B CB    1 
ATOM   2037 C  CG    . GLU B 1 48  ? 15.193  26.195  -2.896  1.00 59.87  ? 48  GLU B CG    1 
ATOM   2038 C  CD    . GLU B 1 48  ? 16.371  27.091  -3.263  1.00 63.60  ? 48  GLU B CD    1 
ATOM   2039 O  OE1   . GLU B 1 48  ? 16.284  27.760  -4.327  1.00 63.82  ? 48  GLU B OE1   1 
ATOM   2040 O  OE2   . GLU B 1 48  ? 17.375  27.119  -2.496  1.00 63.08  ? 48  GLU B OE2   1 
ATOM   2041 N  N     . LEU B 1 49  ? 14.003  22.719  -5.514  1.00 49.75  ? 49  LEU B N     1 
ATOM   2042 C  CA    . LEU B 1 49  ? 13.814  22.052  -6.788  1.00 49.05  ? 49  LEU B CA    1 
ATOM   2043 C  C     . LEU B 1 49  ? 12.462  21.356  -6.843  1.00 49.61  ? 49  LEU B C     1 
ATOM   2044 O  O     . LEU B 1 49  ? 11.911  21.151  -7.923  1.00 49.08  ? 49  LEU B O     1 
ATOM   2045 C  CB    . LEU B 1 49  ? 14.937  21.042  -7.038  1.00 48.63  ? 49  LEU B CB    1 
ATOM   2046 C  CG    . LEU B 1 49  ? 15.098  20.647  -8.509  1.00 49.86  ? 49  LEU B CG    1 
ATOM   2047 C  CD1   . LEU B 1 49  ? 15.404  21.898  -9.310  1.00 50.95  ? 49  LEU B CD1   1 
ATOM   2048 C  CD2   . LEU B 1 49  ? 16.211  19.644  -8.687  1.00 50.02  ? 49  LEU B CD2   1 
ATOM   2049 N  N     . ARG B 1 50  ? 11.914  20.984  -5.690  1.00 50.64  ? 50  ARG B N     1 
ATOM   2050 C  CA    . ARG B 1 50  ? 10.611  20.337  -5.709  1.00 51.63  ? 50  ARG B CA    1 
ATOM   2051 C  C     . ARG B 1 50  ? 9.593   21.386  -6.088  1.00 53.07  ? 50  ARG B C     1 
ATOM   2052 O  O     . ARG B 1 50  ? 8.772   21.160  -6.973  1.00 53.14  ? 50  ARG B O     1 
ATOM   2053 C  CB    . ARG B 1 50  ? 10.245  19.730  -4.357  1.00 49.27  ? 50  ARG B CB    1 
ATOM   2054 C  CG    . ARG B 1 50  ? 10.586  18.268  -4.240  1.00 49.79  ? 50  ARG B CG    1 
ATOM   2055 C  CD    . ARG B 1 50  ? 9.573   17.539  -3.382  1.00 49.46  ? 50  ARG B CD    1 
ATOM   2056 N  NE    . ARG B 1 50  ? 9.397   18.168  -2.079  1.00 49.80  ? 50  ARG B NE    1 
ATOM   2057 C  CZ    . ARG B 1 50  ? 10.310  18.153  -1.114  1.00 48.06  ? 50  ARG B CZ    1 
ATOM   2058 N  NH1   . ARG B 1 50  ? 11.465  17.527  -1.313  1.00 45.36  ? 50  ARG B NH1   1 
ATOM   2059 N  NH2   . ARG B 1 50  ? 10.071  18.782  0.033   1.00 45.39  ? 50  ARG B NH2   1 
ATOM   2060 N  N     . GLU B 1 51  ? 9.662   22.538  -5.425  1.00 55.06  ? 51  GLU B N     1 
ATOM   2061 C  CA    . GLU B 1 51  ? 8.745   23.633  -5.714  1.00 58.11  ? 51  GLU B CA    1 
ATOM   2062 C  C     . GLU B 1 51  ? 8.892   24.054  -7.176  1.00 57.26  ? 51  GLU B C     1 
ATOM   2063 O  O     . GLU B 1 51  ? 7.894   24.244  -7.875  1.00 57.35  ? 51  GLU B O     1 
ATOM   2064 C  CB    . GLU B 1 51  ? 9.012   24.815  -4.781  1.00 60.91  ? 51  GLU B CB    1 
ATOM   2065 C  CG    . GLU B 1 51  ? 8.954   24.410  -3.319  1.00 69.28  ? 51  GLU B CG    1 
ATOM   2066 C  CD    . GLU B 1 51  ? 9.037   25.587  -2.357  1.00 75.74  ? 51  GLU B CD    1 
ATOM   2067 O  OE1   . GLU B 1 51  ? 8.019   26.317  -2.237  1.00 79.14  ? 51  GLU B OE1   1 
ATOM   2068 O  OE2   . GLU B 1 51  ? 10.115  25.781  -1.724  1.00 78.44  ? 51  GLU B OE2   1 
ATOM   2069 N  N     . VAL B 1 52  ? 10.132  24.179  -7.644  1.00 55.46  ? 52  VAL B N     1 
ATOM   2070 C  CA    . VAL B 1 52  ? 10.365  24.552  -9.029  1.00 53.38  ? 52  VAL B CA    1 
ATOM   2071 C  C     . VAL B 1 52  ? 9.643   23.571  -9.930  1.00 52.92  ? 52  VAL B C     1 
ATOM   2072 O  O     . VAL B 1 52  ? 8.861   23.969  -10.788 1.00 52.91  ? 52  VAL B O     1 
ATOM   2073 C  CB    . VAL B 1 52  ? 11.856  24.544  -9.362  1.00 53.12  ? 52  VAL B CB    1 
ATOM   2074 C  CG1   . VAL B 1 52  ? 12.072  24.708  -10.865 1.00 52.98  ? 52  VAL B CG1   1 
ATOM   2075 C  CG2   . VAL B 1 52  ? 12.538  25.670  -8.611  1.00 54.33  ? 52  VAL B CG2   1 
ATOM   2076 N  N     . THR B 1 53  ? 9.894   22.285  -9.728  1.00 52.23  ? 53  THR B N     1 
ATOM   2077 C  CA    . THR B 1 53  ? 9.243   21.274  -10.538 1.00 52.15  ? 53  THR B CA    1 
ATOM   2078 C  C     . THR B 1 53  ? 7.722   21.344  -10.452 1.00 51.61  ? 53  THR B C     1 
ATOM   2079 O  O     . THR B 1 53  ? 7.031   20.972  -11.394 1.00 51.30  ? 53  THR B O     1 
ATOM   2080 C  CB    . THR B 1 53  ? 9.692   19.868  -10.134 1.00 53.24  ? 53  THR B CB    1 
ATOM   2081 O  OG1   . THR B 1 53  ? 11.075  19.702  -10.455 1.00 53.01  ? 53  THR B OG1   1 
ATOM   2082 C  CG2   . THR B 1 53  ? 8.898   18.821  -10.893 1.00 54.48  ? 53  THR B CG2   1 
ATOM   2083 N  N     . ALA B 1 54  ? 7.203   21.820  -9.325  1.00 52.28  ? 54  ALA B N     1 
ATOM   2084 C  CA    . ALA B 1 54  ? 5.758   21.938  -9.123  1.00 52.23  ? 54  ALA B CA    1 
ATOM   2085 C  C     . ALA B 1 54  ? 5.154   23.002  -10.031 1.00 53.16  ? 54  ALA B C     1 
ATOM   2086 O  O     . ALA B 1 54  ? 3.942   23.038  -10.228 1.00 53.58  ? 54  ALA B O     1 
ATOM   2087 C  CB    . ALA B 1 54  ? 5.459   22.273  -7.677  1.00 50.35  ? 54  ALA B CB    1 
ATOM   2088 N  N     . LYS B 1 55  ? 6.001   23.871  -10.571 1.00 53.65  ? 55  LYS B N     1 
ATOM   2089 C  CA    . LYS B 1 55  ? 5.552   24.922  -11.471 1.00 55.27  ? 55  LYS B CA    1 
ATOM   2090 C  C     . LYS B 1 55  ? 5.943   24.611  -12.906 1.00 56.36  ? 55  LYS B C     1 
ATOM   2091 O  O     . LYS B 1 55  ? 6.301   25.515  -13.640 1.00 57.05  ? 55  LYS B O     1 
ATOM   2092 C  CB    . LYS B 1 55  ? 6.186   26.256  -11.106 1.00 55.05  ? 55  LYS B CB    1 
ATOM   2093 C  CG    . LYS B 1 55  ? 5.993   26.677  -9.683  1.00 57.04  ? 55  LYS B CG    1 
ATOM   2094 C  CD    . LYS B 1 55  ? 6.657   28.008  -9.449  1.00 58.23  ? 55  LYS B CD    1 
ATOM   2095 C  CE    . LYS B 1 55  ? 6.598   28.368  -7.993  1.00 61.31  ? 55  LYS B CE    1 
ATOM   2096 N  NZ    . LYS B 1 55  ? 6.794   29.832  -7.825  1.00 66.16  ? 55  LYS B NZ    1 
ATOM   2097 N  N     . HIS B 1 56  ? 5.904   23.349  -13.307 1.00 58.07  ? 56  HIS B N     1 
ATOM   2098 C  CA    . HIS B 1 56  ? 6.268   23.009  -14.669 1.00 62.12  ? 56  HIS B CA    1 
ATOM   2099 C  C     . HIS B 1 56  ? 4.996   22.922  -15.469 1.00 66.19  ? 56  HIS B C     1 
ATOM   2100 O  O     . HIS B 1 56  ? 4.105   22.173  -15.114 1.00 67.37  ? 56  HIS B O     1 
ATOM   2101 C  CB    . HIS B 1 56  ? 6.995   21.679  -14.707 1.00 61.13  ? 56  HIS B CB    1 
ATOM   2102 C  CG    . HIS B 1 56  ? 7.545   21.323  -16.052 1.00 60.43  ? 56  HIS B CG    1 
ATOM   2103 N  ND1   . HIS B 1 56  ? 6.856   20.550  -16.960 1.00 60.30  ? 56  HIS B ND1   1 
ATOM   2104 C  CD2   . HIS B 1 56  ? 8.744   21.590  -16.621 1.00 59.88  ? 56  HIS B CD2   1 
ATOM   2105 C  CE1   . HIS B 1 56  ? 7.610   20.347  -18.024 1.00 59.75  ? 56  HIS B CE1   1 
ATOM   2106 N  NE2   . HIS B 1 56  ? 8.761   20.968  -17.844 1.00 59.92  ? 56  HIS B NE2   1 
ATOM   2107 N  N     . PRO B 1 57  ? 4.896   23.687  -16.568 1.00 70.41  ? 57  PRO B N     1 
ATOM   2108 C  CA    . PRO B 1 57  ? 3.708   23.698  -17.424 1.00 73.30  ? 57  PRO B CA    1 
ATOM   2109 C  C     . PRO B 1 57  ? 2.878   22.417  -17.412 1.00 76.14  ? 57  PRO B C     1 
ATOM   2110 O  O     . PRO B 1 57  ? 1.652   22.475  -17.322 1.00 76.41  ? 57  PRO B O     1 
ATOM   2111 C  CB    . PRO B 1 57  ? 4.288   24.035  -18.783 1.00 73.09  ? 57  PRO B CB    1 
ATOM   2112 C  CG    . PRO B 1 57  ? 5.306   25.074  -18.403 1.00 72.99  ? 57  PRO B CG    1 
ATOM   2113 C  CD    . PRO B 1 57  ? 5.993   24.446  -17.199 1.00 70.96  ? 57  PRO B CD    1 
ATOM   2114 N  N     . TRP B 1 58  ? 3.526   21.261  -17.498 1.00 78.87  ? 58  TRP B N     1 
ATOM   2115 C  CA    . TRP B 1 58  ? 2.767   20.018  -17.460 1.00 83.37  ? 58  TRP B CA    1 
ATOM   2116 C  C     . TRP B 1 58  ? 3.328   18.964  -16.509 1.00 85.40  ? 58  TRP B C     1 
ATOM   2117 O  O     . TRP B 1 58  ? 4.009   18.007  -16.899 1.00 84.93  ? 58  TRP B O     1 
ATOM   2118 C  CB    . TRP B 1 58  ? 2.582   19.442  -18.870 1.00 85.88  ? 58  TRP B CB    1 
ATOM   2119 C  CG    . TRP B 1 58  ? 3.719   19.664  -19.793 1.00 87.20  ? 58  TRP B CG    1 
ATOM   2120 C  CD1   . TRP B 1 58  ? 5.019   19.331  -19.577 1.00 89.10  ? 58  TRP B CD1   1 
ATOM   2121 C  CD2   . TRP B 1 58  ? 3.665   20.271  -21.090 1.00 86.71  ? 58  TRP B CD2   1 
ATOM   2122 N  NE1   . TRP B 1 58  ? 5.788   19.697  -20.660 1.00 90.72  ? 58  TRP B NE1   1 
ATOM   2123 C  CE2   . TRP B 1 58  ? 4.981   20.276  -21.604 1.00 88.00  ? 58  TRP B CE2   1 
ATOM   2124 C  CE3   . TRP B 1 58  ? 2.636   20.810  -21.866 1.00 84.94  ? 58  TRP B CE3   1 
ATOM   2125 C  CZ2   . TRP B 1 58  ? 5.296   20.801  -22.858 1.00 86.46  ? 58  TRP B CZ2   1 
ATOM   2126 C  CZ3   . TRP B 1 58  ? 2.951   21.331  -23.111 1.00 86.13  ? 58  TRP B CZ3   1 
ATOM   2127 C  CH2   . TRP B 1 58  ? 4.271   21.322  -23.594 1.00 86.02  ? 58  TRP B CH2   1 
ATOM   2128 N  N     . ASN B 1 59  ? 3.009   19.171  -15.239 1.00 88.14  ? 59  ASN B N     1 
ATOM   2129 C  CA    . ASN B 1 59  ? 3.420   18.301  -14.151 1.00 90.60  ? 59  ASN B CA    1 
ATOM   2130 C  C     . ASN B 1 59  ? 2.676   16.981  -14.289 1.00 90.91  ? 59  ASN B C     1 
ATOM   2131 O  O     . ASN B 1 59  ? 1.685   16.743  -13.590 1.00 92.01  ? 59  ASN B O     1 
ATOM   2132 C  CB    . ASN B 1 59  ? 3.075   18.961  -12.806 1.00 92.14  ? 59  ASN B CB    1 
ATOM   2133 C  CG    . ASN B 1 59  ? 2.123   20.159  -12.963 1.00 94.06  ? 59  ASN B CG    1 
ATOM   2134 O  OD1   . ASN B 1 59  ? 2.563   21.310  -13.078 1.00 93.02  ? 59  ASN B OD1   1 
ATOM   2135 N  ND2   . ASN B 1 59  ? 0.815   19.885  -12.985 1.00 95.14  ? 59  ASN B ND2   1 
ATOM   2136 N  N     . ILE B 1 60  ? 3.144   16.132  -15.199 1.00 90.52  ? 60  ILE B N     1 
ATOM   2137 C  CA    . ILE B 1 60  ? 2.508   14.838  -15.416 1.00 91.04  ? 60  ILE B CA    1 
ATOM   2138 C  C     . ILE B 1 60  ? 3.252   13.733  -14.682 1.00 92.16  ? 60  ILE B C     1 
ATOM   2139 O  O     . ILE B 1 60  ? 2.828   12.577  -14.699 1.00 92.29  ? 60  ILE B O     1 
ATOM   2140 C  CB    . ILE B 1 60  ? 2.476   14.452  -16.919 1.00 89.45  ? 60  ILE B CB    1 
ATOM   2141 C  CG1   . ILE B 1 60  ? 3.904   14.320  -17.451 1.00 88.80  ? 60  ILE B CG1   1 
ATOM   2142 C  CG2   . ILE B 1 60  ? 1.716   15.492  -17.709 1.00 89.86  ? 60  ILE B CG2   1 
ATOM   2143 C  CD1   . ILE B 1 60  ? 4.005   13.786  -18.853 1.00 87.52  ? 60  ILE B CD1   1 
ATOM   2144 N  N     . MET B 1 61  ? 4.350   14.084  -14.019 1.00 93.46  ? 61  MET B N     1 
ATOM   2145 C  CA    . MET B 1 61  ? 5.141   13.064  -13.350 1.00 94.81  ? 61  MET B CA    1 
ATOM   2146 C  C     . MET B 1 61  ? 6.031   13.563  -12.221 1.00 95.64  ? 61  MET B C     1 
ATOM   2147 O  O     . MET B 1 61  ? 5.668   14.444  -11.437 1.00 96.11  ? 61  MET B O     1 
ATOM   2148 C  CB    . MET B 1 61  ? 6.028   12.386  -14.392 1.00 95.06  ? 61  MET B CB    1 
ATOM   2149 C  CG    . MET B 1 61  ? 7.020   13.358  -15.034 1.00 94.77  ? 61  MET B CG    1 
ATOM   2150 S  SD    . MET B 1 61  ? 8.085   12.612  -16.281 1.00 96.25  ? 61  MET B SD    1 
ATOM   2151 C  CE    . MET B 1 61  ? 7.425   13.349  -17.783 1.00 95.08  ? 61  MET B CE    1 
ATOM   2152 N  N     . THR B 1 62  ? 7.208   12.941  -12.173 1.00 96.48  ? 62  THR B N     1 
ATOM   2153 C  CA    . THR B 1 62  ? 8.301   13.198  -11.229 1.00 96.10  ? 62  THR B CA    1 
ATOM   2154 C  C     . THR B 1 62  ? 8.038   13.436  -9.738  1.00 94.71  ? 62  THR B C     1 
ATOM   2155 O  O     . THR B 1 62  ? 6.902   13.425  -9.231  1.00 94.89  ? 62  THR B O     1 
ATOM   2156 C  CB    . THR B 1 62  ? 9.190   14.389  -11.711 1.00 96.64  ? 62  THR B CB    1 
ATOM   2157 O  OG1   . THR B 1 62  ? 10.446  14.383  -11.008 1.00 94.69  ? 62  THR B OG1   1 
ATOM   2158 C  CG2   . THR B 1 62  ? 8.478   15.720  -11.441 1.00 96.34  ? 62  THR B CG2   1 
ATOM   2159 N  N     . THR B 1 63  ? 9.171   13.642  -9.073  1.00 91.50  ? 63  THR B N     1 
ATOM   2160 C  CA    . THR B 1 63  ? 9.303   13.926  -7.664  1.00 85.66  ? 63  THR B CA    1 
ATOM   2161 C  C     . THR B 1 63  ? 8.535   13.087  -6.663  1.00 82.43  ? 63  THR B C     1 
ATOM   2162 O  O     . THR B 1 63  ? 7.325   13.218  -6.495  1.00 82.01  ? 63  THR B O     1 
ATOM   2163 C  CB    . THR B 1 63  ? 9.027   15.400  -7.404  1.00 84.55  ? 63  THR B CB    1 
ATOM   2164 O  OG1   . THR B 1 63  ? 9.685   16.179  -8.409  1.00 82.79  ? 63  THR B OG1   1 
ATOM   2165 C  CG2   . THR B 1 63  ? 9.576   15.799  -6.054  1.00 83.24  ? 63  THR B CG2   1 
ATOM   2166 N  N     . SER B 1 64  ? 9.283   12.204  -6.019  1.00 78.59  ? 64  SER B N     1 
ATOM   2167 C  CA    . SER B 1 64  ? 8.789   11.354  -4.958  1.00 74.73  ? 64  SER B CA    1 
ATOM   2168 C  C     . SER B 1 64  ? 9.783   11.833  -3.922  1.00 72.59  ? 64  SER B C     1 
ATOM   2169 O  O     . SER B 1 64  ? 10.966  11.508  -4.010  1.00 72.17  ? 64  SER B O     1 
ATOM   2170 C  CB    . SER B 1 64  ? 9.033   9.883   -5.268  1.00 73.85  ? 64  SER B CB    1 
ATOM   2171 O  OG    . SER B 1 64  ? 8.485   9.532   -6.524  1.00 74.66  ? 64  SER B OG    1 
ATOM   2172 N  N     . ALA B 1 65  ? 9.327   12.652  -2.983  1.00 69.55  ? 65  ALA B N     1 
ATOM   2173 C  CA    . ALA B 1 65  ? 10.224  13.177  -1.967  1.00 68.38  ? 65  ALA B CA    1 
ATOM   2174 C  C     . ALA B 1 65  ? 11.130  12.079  -1.412  1.00 67.79  ? 65  ALA B C     1 
ATOM   2175 O  O     . ALA B 1 65  ? 12.318  12.300  -1.184  1.00 67.85  ? 65  ALA B O     1 
ATOM   2176 C  CB    . ALA B 1 65  ? 9.418   13.816  -0.851  1.00 67.93  ? 65  ALA B CB    1 
ATOM   2177 N  N     . ASP B 1 66  ? 10.562  10.889  -1.238  1.00 66.93  ? 66  ASP B N     1 
ATOM   2178 C  CA    . ASP B 1 66  ? 11.272  9.737   -0.697  1.00 66.14  ? 66  ASP B CA    1 
ATOM   2179 C  C     . ASP B 1 66  ? 12.374  9.115   -1.570  1.00 66.00  ? 66  ASP B C     1 
ATOM   2180 O  O     . ASP B 1 66  ? 13.234  8.406   -1.052  1.00 66.74  ? 66  ASP B O     1 
ATOM   2181 C  CB    . ASP B 1 66  ? 10.251  8.661   -0.286  1.00 65.38  ? 66  ASP B CB    1 
ATOM   2182 C  CG    . ASP B 1 66  ? 9.430   8.131   -1.466  1.00 66.25  ? 66  ASP B CG    1 
ATOM   2183 O  OD1   . ASP B 1 66  ? 8.960   8.940   -2.298  1.00 66.21  ? 66  ASP B OD1   1 
ATOM   2184 O  OD2   . ASP B 1 66  ? 9.239   6.897   -1.555  1.00 65.92  ? 66  ASP B OD2   1 
ATOM   2185 N  N     . GLU B 1 67  ? 12.367  9.371   -2.875  1.00 65.65  ? 67  GLU B N     1 
ATOM   2186 C  CA    . GLU B 1 67  ? 13.391  8.800   -3.751  1.00 65.66  ? 67  GLU B CA    1 
ATOM   2187 C  C     . GLU B 1 67  ? 14.767  9.423   -3.573  1.00 63.37  ? 67  GLU B C     1 
ATOM   2188 O  O     . GLU B 1 67  ? 15.777  8.807   -3.895  1.00 62.13  ? 67  GLU B O     1 
ATOM   2189 C  CB    . GLU B 1 67  ? 12.973  8.900   -5.227  1.00 69.47  ? 67  GLU B CB    1 
ATOM   2190 C  CG    . GLU B 1 67  ? 12.278  7.624   -5.761  1.00 76.20  ? 67  GLU B CG    1 
ATOM   2191 C  CD    . GLU B 1 67  ? 11.903  7.690   -7.255  1.00 80.86  ? 67  GLU B CD    1 
ATOM   2192 O  OE1   . GLU B 1 67  ? 12.718  8.213   -8.055  1.00 83.42  ? 67  GLU B OE1   1 
ATOM   2193 O  OE2   . GLU B 1 67  ? 10.802  7.203   -7.635  1.00 81.94  ? 67  GLU B OE2   1 
ATOM   2194 N  N     . GLY B 1 68  ? 14.805  10.640  -3.047  1.00 62.17  ? 68  GLY B N     1 
ATOM   2195 C  CA    . GLY B 1 68  ? 16.074  11.320  -2.851  1.00 60.84  ? 68  GLY B CA    1 
ATOM   2196 C  C     . GLY B 1 68  ? 16.774  10.855  -1.596  1.00 60.01  ? 68  GLY B C     1 
ATOM   2197 O  O     . GLY B 1 68  ? 17.996  10.709  -1.563  1.00 59.08  ? 68  GLY B O     1 
ATOM   2198 N  N     . GLN B 1 69  ? 15.981  10.638  -0.554  1.00 59.32  ? 69  GLN B N     1 
ATOM   2199 C  CA    . GLN B 1 69  ? 16.486  10.170  0.720   1.00 58.70  ? 69  GLN B CA    1 
ATOM   2200 C  C     . GLN B 1 69  ? 17.088  8.791   0.436   1.00 57.54  ? 69  GLN B C     1 
ATOM   2201 O  O     . GLN B 1 69  ? 18.177  8.461   0.912   1.00 57.95  ? 69  GLN B O     1 
ATOM   2202 C  CB    . GLN B 1 69  ? 15.324  10.073  1.716   1.00 61.00  ? 69  GLN B CB    1 
ATOM   2203 C  CG    . GLN B 1 69  ? 15.701  9.691   3.140   1.00 66.29  ? 69  GLN B CG    1 
ATOM   2204 C  CD    . GLN B 1 69  ? 14.476  9.366   4.027   1.00 70.56  ? 69  GLN B CD    1 
ATOM   2205 O  OE1   . GLN B 1 69  ? 13.891  8.263   3.982   1.00 71.02  ? 69  GLN B OE1   1 
ATOM   2206 N  NE2   . GLN B 1 69  ? 14.089  10.337  4.833   1.00 72.02  ? 69  GLN B NE2   1 
ATOM   2207 N  N     . PHE B 1 70  ? 16.393  7.995   -0.369  1.00 55.06  ? 70  PHE B N     1 
ATOM   2208 C  CA    . PHE B 1 70  ? 16.886  6.673   -0.690  1.00 53.24  ? 70  PHE B CA    1 
ATOM   2209 C  C     . PHE B 1 70  ? 18.179  6.704   -1.496  1.00 53.63  ? 70  PHE B C     1 
ATOM   2210 O  O     . PHE B 1 70  ? 19.184  6.138   -1.056  1.00 53.82  ? 70  PHE B O     1 
ATOM   2211 C  CB    . PHE B 1 70  ? 15.848  5.871   -1.457  1.00 53.26  ? 70  PHE B CB    1 
ATOM   2212 C  CG    . PHE B 1 70  ? 16.303  4.478   -1.791  1.00 53.69  ? 70  PHE B CG    1 
ATOM   2213 C  CD1   . PHE B 1 70  ? 16.494  3.537   -0.783  1.00 53.40  ? 70  PHE B CD1   1 
ATOM   2214 C  CD2   . PHE B 1 70  ? 16.626  4.133   -3.098  1.00 53.85  ? 70  PHE B CD2   1 
ATOM   2215 C  CE1   . PHE B 1 70  ? 17.004  2.284   -1.069  1.00 53.04  ? 70  PHE B CE1   1 
ATOM   2216 C  CE2   . PHE B 1 70  ? 17.139  2.876   -3.394  1.00 53.91  ? 70  PHE B CE2   1 
ATOM   2217 C  CZ    . PHE B 1 70  ? 17.329  1.952   -2.379  1.00 52.94  ? 70  PHE B CZ    1 
ATOM   2218 N  N     . LEU B 1 71  ? 18.155  7.344   -2.672  1.00 52.97  ? 71  LEU B N     1 
ATOM   2219 C  CA    . LEU B 1 71  ? 19.347  7.438   -3.533  1.00 51.81  ? 71  LEU B CA    1 
ATOM   2220 C  C     . LEU B 1 71  ? 20.533  8.038   -2.790  1.00 51.14  ? 71  LEU B C     1 
ATOM   2221 O  O     . LEU B 1 71  ? 21.680  7.654   -3.010  1.00 49.53  ? 71  LEU B O     1 
ATOM   2222 C  CB    . LEU B 1 71  ? 19.065  8.278   -4.772  1.00 52.59  ? 71  LEU B CB    1 
ATOM   2223 C  CG    . LEU B 1 71  ? 18.156  7.646   -5.828  1.00 54.77  ? 71  LEU B CG    1 
ATOM   2224 C  CD1   . LEU B 1 71  ? 18.124  8.538   -7.080  1.00 54.10  ? 71  LEU B CD1   1 
ATOM   2225 C  CD2   . LEU B 1 71  ? 18.664  6.255   -6.169  1.00 53.96  ? 71  LEU B CD2   1 
ATOM   2226 N  N     . SER B 1 72  ? 20.244  8.995   -1.919  1.00 50.67  ? 72  SER B N     1 
ATOM   2227 C  CA    . SER B 1 72  ? 21.263  9.634   -1.108  1.00 50.03  ? 72  SER B CA    1 
ATOM   2228 C  C     . SER B 1 72  ? 21.955  8.546   -0.287  1.00 49.27  ? 72  SER B C     1 
ATOM   2229 O  O     . SER B 1 72  ? 23.165  8.343   -0.387  1.00 48.06  ? 72  SER B O     1 
ATOM   2230 C  CB    . SER B 1 72  ? 20.599  10.657  -0.187  1.00 50.01  ? 72  SER B CB    1 
ATOM   2231 O  OG    . SER B 1 72  ? 21.460  11.049  0.864   1.00 53.20  ? 72  SER B OG    1 
ATOM   2232 N  N     . MET B 1 73  ? 21.169  7.847   0.525   1.00 48.89  ? 73  MET B N     1 
ATOM   2233 C  CA    . MET B 1 73  ? 21.678  6.766   1.363   1.00 48.12  ? 73  MET B CA    1 
ATOM   2234 C  C     . MET B 1 73  ? 22.490  5.776   0.531   1.00 47.05  ? 73  MET B C     1 
ATOM   2235 O  O     . MET B 1 73  ? 23.666  5.559   0.785   1.00 47.15  ? 73  MET B O     1 
ATOM   2236 C  CB    . MET B 1 73  ? 20.508  6.032   2.023   1.00 48.66  ? 73  MET B CB    1 
ATOM   2237 C  CG    . MET B 1 73  ? 20.903  4.971   3.031   1.00 49.25  ? 73  MET B CG    1 
ATOM   2238 S  SD    . MET B 1 73  ? 21.704  5.667   4.480   1.00 53.88  ? 73  MET B SD    1 
ATOM   2239 C  CE    . MET B 1 73  ? 20.330  5.898   5.614   1.00 49.72  ? 73  MET B CE    1 
ATOM   2240 N  N     . LEU B 1 74  ? 21.854  5.189   -0.473  1.00 45.81  ? 74  LEU B N     1 
ATOM   2241 C  CA    . LEU B 1 74  ? 22.502  4.201   -1.329  1.00 45.28  ? 74  LEU B CA    1 
ATOM   2242 C  C     . LEU B 1 74  ? 23.874  4.647   -1.808  1.00 45.42  ? 74  LEU B C     1 
ATOM   2243 O  O     . LEU B 1 74  ? 24.850  3.901   -1.665  1.00 46.19  ? 74  LEU B O     1 
ATOM   2244 C  CB    . LEU B 1 74  ? 21.624  3.912   -2.540  1.00 45.67  ? 74  LEU B CB    1 
ATOM   2245 C  CG    . LEU B 1 74  ? 21.647  2.565   -3.263  1.00 46.48  ? 74  LEU B CG    1 
ATOM   2246 C  CD1   . LEU B 1 74  ? 21.137  2.844   -4.672  1.00 47.76  ? 74  LEU B CD1   1 
ATOM   2247 C  CD2   . LEU B 1 74  ? 23.023  1.940   -3.328  1.00 46.34  ? 74  LEU B CD2   1 
ATOM   2248 N  N     . LEU B 1 75  ? 23.943  5.853   -2.385  1.00 44.94  ? 75  LEU B N     1 
ATOM   2249 C  CA    . LEU B 1 75  ? 25.197  6.423   -2.910  1.00 42.67  ? 75  LEU B CA    1 
ATOM   2250 C  C     . LEU B 1 75  ? 26.261  6.572   -1.826  1.00 43.05  ? 75  LEU B C     1 
ATOM   2251 O  O     . LEU B 1 75  ? 27.414  6.188   -2.026  1.00 42.75  ? 75  LEU B O     1 
ATOM   2252 C  CB    . LEU B 1 75  ? 24.943  7.784   -3.562  1.00 38.36  ? 75  LEU B CB    1 
ATOM   2253 C  CG    . LEU B 1 75  ? 24.084  7.739   -4.817  1.00 37.68  ? 75  LEU B CG    1 
ATOM   2254 C  CD1   . LEU B 1 75  ? 23.720  9.159   -5.267  1.00 38.40  ? 75  LEU B CD1   1 
ATOM   2255 C  CD2   . LEU B 1 75  ? 24.840  6.995   -5.902  1.00 38.26  ? 75  LEU B CD2   1 
ATOM   2256 N  N     . LYS B 1 76  ? 25.882  7.138   -0.685  1.00 43.33  ? 76  LYS B N     1 
ATOM   2257 C  CA    . LYS B 1 76  ? 26.829  7.288   0.401   1.00 45.66  ? 76  LYS B CA    1 
ATOM   2258 C  C     . LYS B 1 76  ? 27.349  5.892   0.759   1.00 48.07  ? 76  LYS B C     1 
ATOM   2259 O  O     . LYS B 1 76  ? 28.566  5.696   0.897   1.00 50.57  ? 76  LYS B O     1 
ATOM   2260 C  CB    . LYS B 1 76  ? 26.165  7.920   1.625   1.00 46.14  ? 76  LYS B CB    1 
ATOM   2261 C  CG    . LYS B 1 76  ? 25.726  9.373   1.459   1.00 47.05  ? 76  LYS B CG    1 
ATOM   2262 C  CD    . LYS B 1 76  ? 26.900  10.322  1.485   1.00 50.51  ? 76  LYS B CD    1 
ATOM   2263 C  CE    . LYS B 1 76  ? 26.450  11.769  1.345   1.00 54.46  ? 76  LYS B CE    1 
ATOM   2264 N  NZ    . LYS B 1 76  ? 25.531  12.181  2.461   1.00 58.54  ? 76  LYS B NZ    1 
ATOM   2265 N  N     . LEU B 1 77  ? 26.443  4.918   0.881   1.00 47.20  ? 77  LEU B N     1 
ATOM   2266 C  CA    . LEU B 1 77  ? 26.845  3.551   1.232   1.00 47.89  ? 77  LEU B CA    1 
ATOM   2267 C  C     . LEU B 1 77  ? 27.777  2.836   0.254   1.00 49.58  ? 77  LEU B C     1 
ATOM   2268 O  O     . LEU B 1 77  ? 28.668  2.099   0.681   1.00 51.65  ? 77  LEU B O     1 
ATOM   2269 C  CB    . LEU B 1 77  ? 25.626  2.658   1.480   1.00 44.36  ? 77  LEU B CB    1 
ATOM   2270 C  CG    . LEU B 1 77  ? 24.850  2.889   2.772   1.00 41.07  ? 77  LEU B CG    1 
ATOM   2271 C  CD1   . LEU B 1 77  ? 23.702  1.898   2.889   1.00 39.34  ? 77  LEU B CD1   1 
ATOM   2272 C  CD2   . LEU B 1 77  ? 25.789  2.772   3.929   1.00 38.43  ? 77  LEU B CD2   1 
ATOM   2273 N  N     . ILE B 1 78  ? 27.579  3.022   -1.044  1.00 50.07  ? 78  ILE B N     1 
ATOM   2274 C  CA    . ILE B 1 78  ? 28.447  2.363   -2.007  1.00 51.61  ? 78  ILE B CA    1 
ATOM   2275 C  C     . ILE B 1 78  ? 29.642  3.226   -2.388  1.00 53.73  ? 78  ILE B C     1 
ATOM   2276 O  O     . ILE B 1 78  ? 30.434  2.854   -3.251  1.00 54.04  ? 78  ILE B O     1 
ATOM   2277 C  CB    . ILE B 1 78  ? 27.690  2.030   -3.284  1.00 51.53  ? 78  ILE B CB    1 
ATOM   2278 C  CG1   . ILE B 1 78  ? 27.077  3.303   -3.864  1.00 51.13  ? 78  ILE B CG1   1 
ATOM   2279 C  CG2   . ILE B 1 78  ? 26.635  0.989   -2.997  1.00 51.75  ? 78  ILE B CG2   1 
ATOM   2280 C  CD1   . ILE B 1 78  ? 26.317  3.065   -5.146  1.00 51.80  ? 78  ILE B CD1   1 
ATOM   2281 N  N     . ASN B 1 79  ? 29.768  4.385   -1.753  1.00 56.08  ? 79  ASN B N     1 
ATOM   2282 C  CA    . ASN B 1 79  ? 30.860  5.296   -2.055  1.00 58.00  ? 79  ASN B CA    1 
ATOM   2283 C  C     . ASN B 1 79  ? 30.995  5.580   -3.542  1.00 58.38  ? 79  ASN B C     1 
ATOM   2284 O  O     . ASN B 1 79  ? 32.090  5.501   -4.096  1.00 59.16  ? 79  ASN B O     1 
ATOM   2285 C  CB    . ASN B 1 79  ? 32.175  4.736   -1.542  1.00 62.10  ? 79  ASN B CB    1 
ATOM   2286 C  CG    . ASN B 1 79  ? 32.263  4.770   -0.042  1.00 67.24  ? 79  ASN B CG    1 
ATOM   2287 O  OD1   . ASN B 1 79  ? 32.076  5.828   0.573   1.00 70.92  ? 79  ASN B OD1   1 
ATOM   2288 N  ND2   . ASN B 1 79  ? 32.553  3.616   0.568   1.00 68.29  ? 79  ASN B ND2   1 
ATOM   2289 N  N     . ALA B 1 80  ? 29.886  5.917   -4.188  1.00 57.89  ? 80  ALA B N     1 
ATOM   2290 C  CA    . ALA B 1 80  ? 29.911  6.221   -5.608  1.00 56.74  ? 80  ALA B CA    1 
ATOM   2291 C  C     . ALA B 1 80  ? 30.650  7.545   -5.847  1.00 56.78  ? 80  ALA B C     1 
ATOM   2292 O  O     . ALA B 1 80  ? 30.466  8.520   -5.111  1.00 56.46  ? 80  ALA B O     1 
ATOM   2293 C  CB    . ALA B 1 80  ? 28.495  6.302   -6.133  1.00 57.34  ? 80  ALA B CB    1 
ATOM   2294 N  N     . LYS B 1 81  ? 31.485  7.564   -6.883  1.00 55.96  ? 81  LYS B N     1 
ATOM   2295 C  CA    . LYS B 1 81  ? 32.276  8.735   -7.235  1.00 54.39  ? 81  LYS B CA    1 
ATOM   2296 C  C     . LYS B 1 81  ? 32.048  9.151   -8.675  1.00 52.63  ? 81  LYS B C     1 
ATOM   2297 O  O     . LYS B 1 81  ? 32.072  10.327  -8.999  1.00 52.07  ? 81  LYS B O     1 
ATOM   2298 C  CB    . LYS B 1 81  ? 33.767  8.442   -7.064  1.00 57.48  ? 81  LYS B CB    1 
ATOM   2299 C  CG    . LYS B 1 81  ? 34.353  8.766   -5.708  1.00 61.30  ? 81  LYS B CG    1 
ATOM   2300 C  CD    . LYS B 1 81  ? 35.866  8.943   -5.838  1.00 65.54  ? 81  LYS B CD    1 
ATOM   2301 C  CE    . LYS B 1 81  ? 36.523  9.365   -4.521  1.00 67.78  ? 81  LYS B CE    1 
ATOM   2302 N  NZ    . LYS B 1 81  ? 36.480  8.289   -3.478  1.00 68.59  ? 81  LYS B NZ    1 
ATOM   2303 N  N     . ASN B 1 82  ? 31.854  8.184   -9.552  1.00 51.48  ? 82  ASN B N     1 
ATOM   2304 C  CA    . ASN B 1 82  ? 31.648  8.501   -10.950 1.00 52.15  ? 82  ASN B CA    1 
ATOM   2305 C  C     . ASN B 1 82  ? 30.349  7.860   -11.444 1.00 52.33  ? 82  ASN B C     1 
ATOM   2306 O  O     . ASN B 1 82  ? 30.302  6.672   -11.761 1.00 53.10  ? 82  ASN B O     1 
ATOM   2307 C  CB    . ASN B 1 82  ? 32.859  8.022   -11.753 1.00 52.48  ? 82  ASN B CB    1 
ATOM   2308 C  CG    . ASN B 1 82  ? 32.755  8.362   -13.225 1.00 55.66  ? 82  ASN B CG    1 
ATOM   2309 O  OD1   . ASN B 1 82  ? 32.381  9.492   -13.595 1.00 56.28  ? 82  ASN B OD1   1 
ATOM   2310 N  ND2   . ASN B 1 82  ? 33.090  7.391   -14.083 1.00 54.08  ? 82  ASN B ND2   1 
ATOM   2311 N  N     . THR B 1 83  ? 29.294  8.663   -11.522 1.00 51.83  ? 83  THR B N     1 
ATOM   2312 C  CA    . THR B 1 83  ? 27.991  8.160   -11.928 1.00 51.78  ? 83  THR B CA    1 
ATOM   2313 C  C     . THR B 1 83  ? 27.526  8.566   -13.321 1.00 51.53  ? 83  THR B C     1 
ATOM   2314 O  O     . THR B 1 83  ? 28.255  9.211   -14.076 1.00 52.50  ? 83  THR B O     1 
ATOM   2315 C  CB    . THR B 1 83  ? 26.931  8.598   -10.924 1.00 51.87  ? 83  THR B CB    1 
ATOM   2316 O  OG1   . THR B 1 83  ? 26.696  10.000  -11.070 1.00 52.69  ? 83  THR B OG1   1 
ATOM   2317 C  CG2   . THR B 1 83  ? 27.416  8.339   -9.505  1.00 51.22  ? 83  THR B CG2   1 
ATOM   2318 N  N     . MET B 1 84  ? 26.305  8.151   -13.652 1.00 51.26  ? 84  MET B N     1 
ATOM   2319 C  CA    . MET B 1 84  ? 25.668  8.445   -14.939 1.00 51.84  ? 84  MET B CA    1 
ATOM   2320 C  C     . MET B 1 84  ? 24.176  8.485   -14.649 1.00 52.08  ? 84  MET B C     1 
ATOM   2321 O  O     . MET B 1 84  ? 23.713  7.874   -13.686 1.00 53.03  ? 84  MET B O     1 
ATOM   2322 C  CB    . MET B 1 84  ? 25.951  7.347   -15.973 1.00 51.53  ? 84  MET B CB    1 
ATOM   2323 C  CG    . MET B 1 84  ? 25.470  7.684   -17.379 1.00 52.95  ? 84  MET B CG    1 
ATOM   2324 S  SD    . MET B 1 84  ? 25.305  6.266   -18.531 1.00 56.31  ? 84  MET B SD    1 
ATOM   2325 C  CE    . MET B 1 84  ? 26.965  5.829   -18.735 1.00 54.34  ? 84  MET B CE    1 
ATOM   2326 N  N     . GLU B 1 85  ? 23.423  9.216   -15.457 1.00 50.99  ? 85  GLU B N     1 
ATOM   2327 C  CA    . GLU B 1 85  ? 21.998  9.296   -15.235 1.00 50.59  ? 85  GLU B CA    1 
ATOM   2328 C  C     . GLU B 1 85  ? 21.264  9.522   -16.527 1.00 50.56  ? 85  GLU B C     1 
ATOM   2329 O  O     . GLU B 1 85  ? 21.407  10.577  -17.138 1.00 51.90  ? 85  GLU B O     1 
ATOM   2330 C  CB    . GLU B 1 85  ? 21.659  10.428  -14.273 1.00 51.14  ? 85  GLU B CB    1 
ATOM   2331 C  CG    . GLU B 1 85  ? 20.161  10.675  -14.215 1.00 57.97  ? 85  GLU B CG    1 
ATOM   2332 C  CD    . GLU B 1 85  ? 19.681  11.256  -12.891 1.00 61.13  ? 85  GLU B CD    1 
ATOM   2333 O  OE1   . GLU B 1 85  ? 20.159  10.778  -11.836 1.00 61.53  ? 85  GLU B OE1   1 
ATOM   2334 O  OE2   . GLU B 1 85  ? 18.811  12.172  -12.910 1.00 63.46  ? 85  GLU B OE2   1 
ATOM   2335 N  N     . ILE B 1 86  ? 20.479  8.537   -16.946 1.00 49.24  ? 86  ILE B N     1 
ATOM   2336 C  CA    . ILE B 1 86  ? 19.708  8.659   -18.172 1.00 49.36  ? 86  ILE B CA    1 
ATOM   2337 C  C     . ILE B 1 86  ? 18.286  9.071   -17.770 1.00 51.37  ? 86  ILE B C     1 
ATOM   2338 O  O     . ILE B 1 86  ? 17.572  8.313   -17.124 1.00 52.72  ? 86  ILE B O     1 
ATOM   2339 C  CB    . ILE B 1 86  ? 19.717  7.332   -18.931 1.00 47.90  ? 86  ILE B CB    1 
ATOM   2340 C  CG1   . ILE B 1 86  ? 21.167  6.942   -19.223 1.00 46.05  ? 86  ILE B CG1   1 
ATOM   2341 C  CG2   . ILE B 1 86  ? 18.923  7.450   -20.225 1.00 45.83  ? 86  ILE B CG2   1 
ATOM   2342 C  CD1   . ILE B 1 86  ? 21.318  5.560   -19.749 1.00 44.86  ? 86  ILE B CD1   1 
ATOM   2343 N  N     . GLY B 1 87  ? 17.896  10.287  -18.147 1.00 51.81  ? 87  GLY B N     1 
ATOM   2344 C  CA    . GLY B 1 87  ? 16.598  10.816  -17.785 1.00 51.55  ? 87  GLY B CA    1 
ATOM   2345 C  C     . GLY B 1 87  ? 16.826  11.806  -16.653 1.00 53.51  ? 87  GLY B C     1 
ATOM   2346 O  O     . GLY B 1 87  ? 16.786  11.438  -15.477 1.00 55.56  ? 87  GLY B O     1 
ATOM   2347 N  N     . VAL B 1 88  ? 17.061  13.069  -16.997 1.00 53.50  ? 88  VAL B N     1 
ATOM   2348 C  CA    . VAL B 1 88  ? 17.342  14.097  -16.000 1.00 52.46  ? 88  VAL B CA    1 
ATOM   2349 C  C     . VAL B 1 88  ? 16.118  14.886  -15.552 1.00 52.91  ? 88  VAL B C     1 
ATOM   2350 O  O     . VAL B 1 88  ? 15.803  14.893  -14.372 1.00 53.70  ? 88  VAL B O     1 
ATOM   2351 C  CB    . VAL B 1 88  ? 18.431  15.081  -16.517 1.00 51.50  ? 88  VAL B CB    1 
ATOM   2352 C  CG1   . VAL B 1 88  ? 18.788  16.079  -15.437 1.00 50.78  ? 88  VAL B CG1   1 
ATOM   2353 C  CG2   . VAL B 1 88  ? 19.668  14.313  -16.947 1.00 49.44  ? 88  VAL B CG2   1 
ATOM   2354 N  N     . TYR B 1 89  ? 15.454  15.567  -16.483 1.00 54.03  ? 89  TYR B N     1 
ATOM   2355 C  CA    . TYR B 1 89  ? 14.248  16.353  -16.192 1.00 54.54  ? 89  TYR B CA    1 
ATOM   2356 C  C     . TYR B 1 89  ? 14.296  17.205  -14.943 1.00 54.92  ? 89  TYR B C     1 
ATOM   2357 O  O     . TYR B 1 89  ? 14.095  16.689  -13.850 1.00 60.02  ? 89  TYR B O     1 
ATOM   2358 C  CB    . TYR B 1 89  ? 13.037  15.434  -16.031 1.00 53.34  ? 89  TYR B CB    1 
ATOM   2359 C  CG    . TYR B 1 89  ? 11.739  16.169  -15.738 1.00 54.12  ? 89  TYR B CG    1 
ATOM   2360 C  CD1   . TYR B 1 89  ? 11.017  16.779  -16.766 1.00 55.52  ? 89  TYR B CD1   1 
ATOM   2361 C  CD2   . TYR B 1 89  ? 11.227  16.252  -14.443 1.00 52.99  ? 89  TYR B CD2   1 
ATOM   2362 C  CE1   . TYR B 1 89  ? 9.816   17.448  -16.515 1.00 55.84  ? 89  TYR B CE1   1 
ATOM   2363 C  CE2   . TYR B 1 89  ? 10.025  16.920  -14.179 1.00 53.93  ? 89  TYR B CE2   1 
ATOM   2364 C  CZ    . TYR B 1 89  ? 9.327   17.512  -15.224 1.00 55.88  ? 89  TYR B CZ    1 
ATOM   2365 O  OH    . TYR B 1 89  ? 8.135   18.153  -14.998 1.00 56.51  ? 89  TYR B OH    1 
ATOM   2366 N  N     . THR B 1 90  ? 14.520  18.498  -15.067 1.00 52.69  ? 90  THR B N     1 
ATOM   2367 C  CA    . THR B 1 90  ? 14.530  19.335  -13.866 1.00 51.25  ? 90  THR B CA    1 
ATOM   2368 C  C     . THR B 1 90  ? 15.677  19.035  -12.916 1.00 49.91  ? 90  THR B C     1 
ATOM   2369 O  O     . THR B 1 90  ? 16.146  19.922  -12.215 1.00 51.19  ? 90  THR B O     1 
ATOM   2370 C  CB    . THR B 1 90  ? 13.220  19.194  -13.065 1.00 50.88  ? 90  THR B CB    1 
ATOM   2371 O  OG1   . THR B 1 90  ? 12.119  19.659  -13.847 1.00 51.18  ? 90  THR B OG1   1 
ATOM   2372 C  CG2   . THR B 1 90  ? 13.295  20.023  -11.803 1.00 53.87  ? 90  THR B CG2   1 
ATOM   2373 N  N     . GLY B 1 91  ? 16.092  17.778  -12.862 1.00 49.78  ? 91  GLY B N     1 
ATOM   2374 C  CA    . GLY B 1 91  ? 17.210  17.386  -12.019 1.00 49.55  ? 91  GLY B CA    1 
ATOM   2375 C  C     . GLY B 1 91  ? 17.018  17.085  -10.546 1.00 48.51  ? 91  GLY B C     1 
ATOM   2376 O  O     . GLY B 1 91  ? 17.904  17.379  -9.768  1.00 46.93  ? 91  GLY B O     1 
ATOM   2377 N  N     . TYR B 1 92  ? 15.899  16.485  -10.153 1.00 50.30  ? 92  TYR B N     1 
ATOM   2378 C  CA    . TYR B 1 92  ? 15.679  16.169  -8.741  1.00 50.66  ? 92  TYR B CA    1 
ATOM   2379 C  C     . TYR B 1 92  ? 16.593  15.054  -8.241  1.00 51.02  ? 92  TYR B C     1 
ATOM   2380 O  O     . TYR B 1 92  ? 17.234  15.196  -7.197  1.00 51.30  ? 92  TYR B O     1 
ATOM   2381 C  CB    . TYR B 1 92  ? 14.234  15.769  -8.489  1.00 50.34  ? 92  TYR B CB    1 
ATOM   2382 C  CG    . TYR B 1 92  ? 13.891  15.667  -7.023  1.00 52.78  ? 92  TYR B CG    1 
ATOM   2383 C  CD1   . TYR B 1 92  ? 13.989  16.780  -6.181  1.00 54.03  ? 92  TYR B CD1   1 
ATOM   2384 C  CD2   . TYR B 1 92  ? 13.439  14.468  -6.475  1.00 53.89  ? 92  TYR B CD2   1 
ATOM   2385 C  CE1   . TYR B 1 92  ? 13.636  16.699  -4.824  1.00 55.18  ? 92  TYR B CE1   1 
ATOM   2386 C  CE2   . TYR B 1 92  ? 13.087  14.374  -5.123  1.00 55.56  ? 92  TYR B CE2   1 
ATOM   2387 C  CZ    . TYR B 1 92  ? 13.185  15.491  -4.304  1.00 55.93  ? 92  TYR B CZ    1 
ATOM   2388 O  OH    . TYR B 1 92  ? 12.815  15.394  -2.976  1.00 56.17  ? 92  TYR B OH    1 
ATOM   2389 N  N     . SER B 1 93  ? 16.650  13.943  -8.968  1.00 50.75  ? 93  SER B N     1 
ATOM   2390 C  CA    . SER B 1 93  ? 17.518  12.850  -8.555  1.00 51.88  ? 93  SER B CA    1 
ATOM   2391 C  C     . SER B 1 93  ? 18.971  13.188  -8.919  1.00 51.78  ? 93  SER B C     1 
ATOM   2392 O  O     . SER B 1 93  ? 19.915  12.572  -8.414  1.00 52.39  ? 93  SER B O     1 
ATOM   2393 C  CB    . SER B 1 93  ? 17.086  11.528  -9.208  1.00 52.31  ? 93  SER B CB    1 
ATOM   2394 O  OG    . SER B 1 93  ? 17.350  11.513  -10.595 1.00 55.58  ? 93  SER B OG    1 
ATOM   2395 N  N     . LEU B 1 94  ? 19.142  14.170  -9.800  1.00 50.98  ? 94  LEU B N     1 
ATOM   2396 C  CA    . LEU B 1 94  ? 20.472  14.615  -10.196 1.00 49.24  ? 94  LEU B CA    1 
ATOM   2397 C  C     . LEU B 1 94  ? 21.039  15.425  -9.026  1.00 47.94  ? 94  LEU B C     1 
ATOM   2398 O  O     . LEU B 1 94  ? 22.180  15.242  -8.614  1.00 48.83  ? 94  LEU B O     1 
ATOM   2399 C  CB    . LEU B 1 94  ? 20.387  15.519  -11.428 1.00 49.76  ? 94  LEU B CB    1 
ATOM   2400 C  CG    . LEU B 1 94  ? 21.512  15.456  -12.468 1.00 48.90  ? 94  LEU B CG    1 
ATOM   2401 C  CD1   . LEU B 1 94  ? 21.636  16.804  -13.112 1.00 47.05  ? 94  LEU B CD1   1 
ATOM   2402 C  CD2   . LEU B 1 94  ? 22.820  15.064  -11.828 1.00 50.18  ? 94  LEU B CD2   1 
ATOM   2403 N  N     . LEU B 1 95  ? 20.222  16.327  -8.504  1.00 45.55  ? 95  LEU B N     1 
ATOM   2404 C  CA    . LEU B 1 95  ? 20.607  17.172  -7.399  1.00 44.50  ? 95  LEU B CA    1 
ATOM   2405 C  C     . LEU B 1 95  ? 20.970  16.269  -6.236  1.00 46.73  ? 95  LEU B C     1 
ATOM   2406 O  O     . LEU B 1 95  ? 21.967  16.484  -5.552  1.00 48.48  ? 95  LEU B O     1 
ATOM   2407 C  CB    . LEU B 1 95  ? 19.433  18.045  -6.992  1.00 42.80  ? 95  LEU B CB    1 
ATOM   2408 C  CG    . LEU B 1 95  ? 19.686  19.438  -6.434  1.00 42.48  ? 95  LEU B CG    1 
ATOM   2409 C  CD1   . LEU B 1 95  ? 18.574  19.772  -5.463  1.00 42.43  ? 95  LEU B CD1   1 
ATOM   2410 C  CD2   . LEU B 1 95  ? 21.015  19.514  -5.742  1.00 43.31  ? 95  LEU B CD2   1 
ATOM   2411 N  N     . ALA B 1 96  ? 20.150  15.246  -6.018  1.00 46.87  ? 96  ALA B N     1 
ATOM   2412 C  CA    . ALA B 1 96  ? 20.372  14.311  -4.922  1.00 46.07  ? 96  ALA B CA    1 
ATOM   2413 C  C     . ALA B 1 96  ? 21.685  13.559  -5.079  1.00 44.74  ? 96  ALA B C     1 
ATOM   2414 O  O     . ALA B 1 96  ? 22.406  13.331  -4.110  1.00 43.30  ? 96  ALA B O     1 
ATOM   2415 C  CB    . ALA B 1 96  ? 19.205  13.327  -4.841  1.00 48.05  ? 96  ALA B CB    1 
ATOM   2416 N  N     . THR B 1 97  ? 21.986  13.164  -6.308  1.00 44.08  ? 97  THR B N     1 
ATOM   2417 C  CA    . THR B 1 97  ? 23.214  12.447  -6.576  1.00 44.80  ? 97  THR B CA    1 
ATOM   2418 C  C     . THR B 1 97  ? 24.385  13.407  -6.381  1.00 44.59  ? 97  THR B C     1 
ATOM   2419 O  O     . THR B 1 97  ? 25.367  13.044  -5.744  1.00 44.96  ? 97  THR B O     1 
ATOM   2420 C  CB    . THR B 1 97  ? 23.225  11.860  -8.023  1.00 45.48  ? 97  THR B CB    1 
ATOM   2421 O  OG1   . THR B 1 97  ? 22.145  10.922  -8.175  1.00 43.88  ? 97  THR B OG1   1 
ATOM   2422 C  CG2   . THR B 1 97  ? 24.560  11.155  -8.319  1.00 45.00  ? 97  THR B CG2   1 
ATOM   2423 N  N     . ALA B 1 98  ? 24.269  14.631  -6.904  1.00 44.33  ? 98  ALA B N     1 
ATOM   2424 C  CA    . ALA B 1 98  ? 25.327  15.643  -6.789  1.00 43.62  ? 98  ALA B CA    1 
ATOM   2425 C  C     . ALA B 1 98  ? 25.569  16.113  -5.354  1.00 44.25  ? 98  ALA B C     1 
ATOM   2426 O  O     . ALA B 1 98  ? 26.696  16.401  -4.961  1.00 43.55  ? 98  ALA B O     1 
ATOM   2427 C  CB    . ALA B 1 98  ? 25.005  16.816  -7.653  1.00 42.55  ? 98  ALA B CB    1 
ATOM   2428 N  N     . LEU B 1 99  ? 24.512  16.213  -4.567  1.00 45.84  ? 99  LEU B N     1 
ATOM   2429 C  CA    . LEU B 1 99  ? 24.675  16.614  -3.179  1.00 48.24  ? 99  LEU B CA    1 
ATOM   2430 C  C     . LEU B 1 99  ? 25.240  15.432  -2.369  1.00 51.17  ? 99  LEU B C     1 
ATOM   2431 O  O     . LEU B 1 99  ? 25.714  15.608  -1.238  1.00 52.97  ? 99  LEU B O     1 
ATOM   2432 C  CB    . LEU B 1 99  ? 23.324  17.031  -2.579  1.00 45.88  ? 99  LEU B CB    1 
ATOM   2433 C  CG    . LEU B 1 99  ? 22.742  18.391  -2.972  1.00 46.37  ? 99  LEU B CG    1 
ATOM   2434 C  CD1   . LEU B 1 99  ? 21.356  18.574  -2.365  1.00 45.02  ? 99  LEU B CD1   1 
ATOM   2435 C  CD2   . LEU B 1 99  ? 23.668  19.481  -2.501  1.00 44.32  ? 99  LEU B CD2   1 
ATOM   2436 N  N     . ALA B 1 100 ? 25.211  14.234  -2.953  1.00 52.11  ? 100 ALA B N     1 
ATOM   2437 C  CA    . ALA B 1 100 ? 25.653  13.041  -2.238  1.00 51.96  ? 100 ALA B CA    1 
ATOM   2438 C  C     . ALA B 1 100 ? 27.060  12.531  -2.481  1.00 52.11  ? 100 ALA B C     1 
ATOM   2439 O  O     . ALA B 1 100 ? 27.746  12.165  -1.525  1.00 53.29  ? 100 ALA B O     1 
ATOM   2440 C  CB    . ALA B 1 100 ? 24.661  11.915  -2.479  1.00 52.55  ? 100 ALA B CB    1 
ATOM   2441 N  N     . ILE B 1 101 ? 27.485  12.476  -3.741  1.00 51.22  ? 101 ILE B N     1 
ATOM   2442 C  CA    . ILE B 1 101 ? 28.812  11.982  -4.055  1.00 51.09  ? 101 ILE B CA    1 
ATOM   2443 C  C     . ILE B 1 101 ? 29.841  13.012  -3.653  1.00 55.44  ? 101 ILE B C     1 
ATOM   2444 O  O     . ILE B 1 101 ? 29.511  14.184  -3.451  1.00 56.13  ? 101 ILE B O     1 
ATOM   2445 C  CB    . ILE B 1 101 ? 28.967  11.657  -5.552  1.00 48.78  ? 101 ILE B CB    1 
ATOM   2446 C  CG1   . ILE B 1 101 ? 28.952  12.936  -6.384  1.00 47.67  ? 101 ILE B CG1   1 
ATOM   2447 C  CG2   . ILE B 1 101 ? 27.843  10.742  -5.991  1.00 48.22  ? 101 ILE B CG2   1 
ATOM   2448 C  CD1   . ILE B 1 101 ? 28.886  12.680  -7.880  1.00 44.73  ? 101 ILE B CD1   1 
ATOM   2449 N  N     . PRO B 1 102 ? 31.108  12.582  -3.510  1.00 59.17  ? 102 PRO B N     1 
ATOM   2450 C  CA    . PRO B 1 102 ? 32.211  13.471  -3.121  1.00 60.96  ? 102 PRO B CA    1 
ATOM   2451 C  C     . PRO B 1 102 ? 32.469  14.632  -4.092  1.00 62.16  ? 102 PRO B C     1 
ATOM   2452 O  O     . PRO B 1 102 ? 32.016  14.619  -5.248  1.00 60.36  ? 102 PRO B O     1 
ATOM   2453 C  CB    . PRO B 1 102 ? 33.400  12.512  -2.989  1.00 60.70  ? 102 PRO B CB    1 
ATOM   2454 C  CG    . PRO B 1 102 ? 33.065  11.408  -3.946  1.00 59.79  ? 102 PRO B CG    1 
ATOM   2455 C  CD    . PRO B 1 102 ? 31.594  11.201  -3.698  1.00 59.79  ? 102 PRO B CD    1 
ATOM   2456 N  N     . GLU B 1 103 ? 33.196  15.634  -3.602  1.00 64.18  ? 103 GLU B N     1 
ATOM   2457 C  CA    . GLU B 1 103 ? 33.497  16.816  -4.394  1.00 66.26  ? 103 GLU B CA    1 
ATOM   2458 C  C     . GLU B 1 103 ? 34.124  16.488  -5.728  1.00 66.64  ? 103 GLU B C     1 
ATOM   2459 O  O     . GLU B 1 103 ? 33.767  17.092  -6.741  1.00 66.95  ? 103 GLU B O     1 
ATOM   2460 C  CB    . GLU B 1 103 ? 34.399  17.770  -3.616  1.00 67.75  ? 103 GLU B CB    1 
ATOM   2461 C  CG    . GLU B 1 103 ? 33.665  18.989  -3.083  1.00 74.91  ? 103 GLU B CG    1 
ATOM   2462 C  CD    . GLU B 1 103 ? 32.389  18.632  -2.295  1.00 80.18  ? 103 GLU B CD    1 
ATOM   2463 O  OE1   . GLU B 1 103 ? 32.502  17.917  -1.265  1.00 82.08  ? 103 GLU B OE1   1 
ATOM   2464 O  OE2   . GLU B 1 103 ? 31.275  19.068  -2.705  1.00 80.95  ? 103 GLU B OE2   1 
ATOM   2465 N  N     . ASP B 1 104 ? 35.046  15.528  -5.736  1.00 65.91  ? 104 ASP B N     1 
ATOM   2466 C  CA    . ASP B 1 104 ? 35.713  15.149  -6.973  1.00 65.46  ? 104 ASP B CA    1 
ATOM   2467 C  C     . ASP B 1 104 ? 34.889  14.161  -7.788  1.00 62.56  ? 104 ASP B C     1 
ATOM   2468 O  O     . ASP B 1 104 ? 35.404  13.541  -8.715  1.00 60.93  ? 104 ASP B O     1 
ATOM   2469 C  CB    . ASP B 1 104 ? 37.111  14.577  -6.678  1.00 70.77  ? 104 ASP B CB    1 
ATOM   2470 C  CG    . ASP B 1 104 ? 37.079  13.359  -5.751  1.00 75.99  ? 104 ASP B CG    1 
ATOM   2471 O  OD1   . ASP B 1 104 ? 36.547  13.484  -4.617  1.00 77.63  ? 104 ASP B OD1   1 
ATOM   2472 O  OD2   . ASP B 1 104 ? 37.597  12.282  -6.157  1.00 77.62  ? 104 ASP B OD2   1 
ATOM   2473 N  N     . GLY B 1 105 ? 33.607  14.039  -7.434  1.00 60.75  ? 105 GLY B N     1 
ATOM   2474 C  CA    . GLY B 1 105 ? 32.692  13.139  -8.127  1.00 57.18  ? 105 GLY B CA    1 
ATOM   2475 C  C     . GLY B 1 105 ? 32.247  13.659  -9.481  1.00 55.06  ? 105 GLY B C     1 
ATOM   2476 O  O     . GLY B 1 105 ? 32.255  14.855  -9.725  1.00 55.52  ? 105 GLY B O     1 
ATOM   2477 N  N     . LYS B 1 106 ? 31.851  12.768  -10.373 1.00 54.78  ? 106 LYS B N     1 
ATOM   2478 C  CA    . LYS B 1 106 ? 31.441  13.201  -11.704 1.00 55.88  ? 106 LYS B CA    1 
ATOM   2479 C  C     . LYS B 1 106 ? 30.224  12.432  -12.195 1.00 53.57  ? 106 LYS B C     1 
ATOM   2480 O  O     . LYS B 1 106 ? 30.186  11.206  -12.116 1.00 54.65  ? 106 LYS B O     1 
ATOM   2481 C  CB    . LYS B 1 106 ? 32.615  13.055  -12.702 1.00 58.89  ? 106 LYS B CB    1 
ATOM   2482 C  CG    . LYS B 1 106 ? 33.809  14.015  -12.460 1.00 62.36  ? 106 LYS B CG    1 
ATOM   2483 C  CD    . LYS B 1 106 ? 33.352  15.496  -12.492 1.00 67.37  ? 106 LYS B CD    1 
ATOM   2484 C  CE    . LYS B 1 106 ? 34.505  16.527  -12.465 1.00 68.39  ? 106 LYS B CE    1 
ATOM   2485 N  NZ    . LYS B 1 106 ? 34.075  17.898  -12.941 1.00 66.69  ? 106 LYS B NZ    1 
ATOM   2486 N  N     . ILE B 1 107 ? 29.241  13.168  -12.710 1.00 50.33  ? 107 ILE B N     1 
ATOM   2487 C  CA    . ILE B 1 107 ? 27.998  12.591  -13.198 1.00 48.02  ? 107 ILE B CA    1 
ATOM   2488 C  C     . ILE B 1 107 ? 27.680  12.928  -14.647 1.00 48.59  ? 107 ILE B C     1 
ATOM   2489 O  O     . ILE B 1 107 ? 27.475  14.093  -14.987 1.00 49.48  ? 107 ILE B O     1 
ATOM   2490 C  CB    . ILE B 1 107 ? 26.815  13.095  -12.388 1.00 47.11  ? 107 ILE B CB    1 
ATOM   2491 C  CG1   . ILE B 1 107 ? 27.111  12.985  -10.895 1.00 46.56  ? 107 ILE B CG1   1 
ATOM   2492 C  CG2   . ILE B 1 107 ? 25.576  12.327  -12.786 1.00 47.08  ? 107 ILE B CG2   1 
ATOM   2493 C  CD1   . ILE B 1 107 ? 26.126  13.723  -10.028 1.00 44.65  ? 107 ILE B CD1   1 
ATOM   2494 N  N     . LEU B 1 108 ? 27.620  11.915  -15.500 1.00 48.89  ? 108 LEU B N     1 
ATOM   2495 C  CA    . LEU B 1 108 ? 27.282  12.134  -16.899 1.00 49.54  ? 108 LEU B CA    1 
ATOM   2496 C  C     . LEU B 1 108 ? 25.758  12.146  -16.996 1.00 51.37  ? 108 LEU B C     1 
ATOM   2497 O  O     . LEU B 1 108 ? 25.111  11.098  -16.940 1.00 51.95  ? 108 LEU B O     1 
ATOM   2498 C  CB    . LEU B 1 108 ? 27.850  11.015  -17.762 1.00 49.83  ? 108 LEU B CB    1 
ATOM   2499 C  CG    . LEU B 1 108 ? 27.276  10.922  -19.169 1.00 51.02  ? 108 LEU B CG    1 
ATOM   2500 C  CD1   . LEU B 1 108 ? 27.488  12.255  -19.882 1.00 52.57  ? 108 LEU B CD1   1 
ATOM   2501 C  CD2   . LEU B 1 108 ? 27.931  9.780   -19.919 1.00 50.63  ? 108 LEU B CD2   1 
ATOM   2502 N  N     . ALA B 1 109 ? 25.189  13.340  -17.132 1.00 52.93  ? 109 ALA B N     1 
ATOM   2503 C  CA    . ALA B 1 109 ? 23.747  13.505  -17.211 1.00 53.27  ? 109 ALA B CA    1 
ATOM   2504 C  C     . ALA B 1 109 ? 23.258  13.506  -18.629 1.00 55.22  ? 109 ALA B C     1 
ATOM   2505 O  O     . ALA B 1 109 ? 23.732  14.278  -19.449 1.00 56.73  ? 109 ALA B O     1 
ATOM   2506 C  CB    . ALA B 1 109 ? 23.350  14.790  -16.552 1.00 53.06  ? 109 ALA B CB    1 
ATOM   2507 N  N     . MET B 1 110 ? 22.299  12.642  -18.924 1.00 57.58  ? 110 MET B N     1 
ATOM   2508 C  CA    . MET B 1 110 ? 21.741  12.589  -20.267 1.00 59.90  ? 110 MET B CA    1 
ATOM   2509 C  C     . MET B 1 110 ? 20.226  12.696  -20.253 1.00 60.32  ? 110 MET B C     1 
ATOM   2510 O  O     . MET B 1 110 ? 19.544  11.966  -19.542 1.00 60.12  ? 110 MET B O     1 
ATOM   2511 C  CB    . MET B 1 110 ? 22.137  11.297  -20.987 1.00 61.14  ? 110 MET B CB    1 
ATOM   2512 C  CG    . MET B 1 110 ? 23.566  11.247  -21.465 1.00 62.21  ? 110 MET B CG    1 
ATOM   2513 S  SD    . MET B 1 110 ? 23.900  9.645   -22.238 1.00 68.57  ? 110 MET B SD    1 
ATOM   2514 C  CE    . MET B 1 110 ? 24.919  8.838   -20.973 1.00 65.70  ? 110 MET B CE    1 
ATOM   2515 N  N     . ASP B 1 111 ? 19.714  13.640  -21.033 1.00 61.53  ? 111 ASP B N     1 
ATOM   2516 C  CA    . ASP B 1 111 ? 18.285  13.836  -21.174 1.00 61.84  ? 111 ASP B CA    1 
ATOM   2517 C  C     . ASP B 1 111 ? 18.019  14.349  -22.574 1.00 61.88  ? 111 ASP B C     1 
ATOM   2518 O  O     . ASP B 1 111 ? 18.932  14.799  -23.260 1.00 60.79  ? 111 ASP B O     1 
ATOM   2519 C  CB    . ASP B 1 111 ? 17.740  14.818  -20.153 1.00 63.37  ? 111 ASP B CB    1 
ATOM   2520 C  CG    . ASP B 1 111 ? 16.233  14.746  -20.057 1.00 65.75  ? 111 ASP B CG    1 
ATOM   2521 O  OD1   . ASP B 1 111 ? 15.556  15.089  -21.051 1.00 66.25  ? 111 ASP B OD1   1 
ATOM   2522 O  OD2   . ASP B 1 111 ? 15.723  14.326  -18.994 1.00 67.99  ? 111 ASP B OD2   1 
ATOM   2523 N  N     . ILE B 1 112 ? 16.765  14.276  -22.996 1.00 62.73  ? 112 ILE B N     1 
ATOM   2524 C  CA    . ILE B 1 112 ? 16.387  14.703  -24.331 1.00 63.92  ? 112 ILE B CA    1 
ATOM   2525 C  C     . ILE B 1 112 ? 15.909  16.149  -24.392 1.00 65.75  ? 112 ILE B C     1 
ATOM   2526 O  O     . ILE B 1 112 ? 15.812  16.726  -25.473 1.00 66.54  ? 112 ILE B O     1 
ATOM   2527 C  CB    . ILE B 1 112 ? 15.286  13.773  -24.888 1.00 62.38  ? 112 ILE B CB    1 
ATOM   2528 C  CG1   . ILE B 1 112 ? 15.617  13.395  -26.320 1.00 63.08  ? 112 ILE B CG1   1 
ATOM   2529 C  CG2   . ILE B 1 112 ? 13.928  14.421  -24.798 1.00 62.75  ? 112 ILE B CG2   1 
ATOM   2530 C  CD1   . ILE B 1 112 ? 16.818  12.485  -26.417 1.00 63.39  ? 112 ILE B CD1   1 
ATOM   2531 N  N     . ASN B 1 113 ? 15.648  16.741  -23.231 1.00 67.28  ? 113 ASN B N     1 
ATOM   2532 C  CA    . ASN B 1 113 ? 15.132  18.105  -23.168 1.00 68.97  ? 113 ASN B CA    1 
ATOM   2533 C  C     . ASN B 1 113 ? 15.942  19.045  -22.253 1.00 68.50  ? 113 ASN B C     1 
ATOM   2534 O  O     . ASN B 1 113 ? 15.698  19.097  -21.053 1.00 68.34  ? 113 ASN B O     1 
ATOM   2535 C  CB    . ASN B 1 113 ? 13.677  18.025  -22.695 1.00 70.99  ? 113 ASN B CB    1 
ATOM   2536 C  CG    . ASN B 1 113 ? 12.930  19.324  -22.864 1.00 73.14  ? 113 ASN B CG    1 
ATOM   2537 O  OD1   . ASN B 1 113 ? 13.457  20.404  -22.573 1.00 73.93  ? 113 ASN B OD1   1 
ATOM   2538 N  ND2   . ASN B 1 113 ? 11.681  19.229  -23.320 1.00 73.03  ? 113 ASN B ND2   1 
ATOM   2539 N  N     . LYS B 1 114 ? 16.883  19.797  -22.825 1.00 68.85  ? 114 LYS B N     1 
ATOM   2540 C  CA    . LYS B 1 114 ? 17.728  20.726  -22.057 1.00 69.47  ? 114 LYS B CA    1 
ATOM   2541 C  C     . LYS B 1 114 ? 16.930  21.812  -21.341 1.00 68.20  ? 114 LYS B C     1 
ATOM   2542 O  O     . LYS B 1 114 ? 17.427  22.462  -20.428 1.00 65.75  ? 114 LYS B O     1 
ATOM   2543 C  CB    . LYS B 1 114 ? 18.746  21.416  -22.976 1.00 72.51  ? 114 LYS B CB    1 
ATOM   2544 C  CG    . LYS B 1 114 ? 18.077  22.324  -24.014 1.00 77.45  ? 114 LYS B CG    1 
ATOM   2545 C  CD    . LYS B 1 114 ? 19.033  23.280  -24.733 1.00 79.42  ? 114 LYS B CD    1 
ATOM   2546 C  CE    . LYS B 1 114 ? 18.249  24.155  -25.722 1.00 81.31  ? 114 LYS B CE    1 
ATOM   2547 N  NZ    . LYS B 1 114 ? 19.075  25.192  -26.408 1.00 82.22  ? 114 LYS B NZ    1 
ATOM   2548 N  N     . GLU B 1 115 ? 15.694  22.011  -21.769 1.00 69.04  ? 115 GLU B N     1 
ATOM   2549 C  CA    . GLU B 1 115 ? 14.849  23.038  -21.184 1.00 70.15  ? 115 GLU B CA    1 
ATOM   2550 C  C     . GLU B 1 115 ? 14.497  22.722  -19.753 1.00 67.74  ? 115 GLU B C     1 
ATOM   2551 O  O     . GLU B 1 115 ? 14.624  23.564  -18.865 1.00 68.49  ? 115 GLU B O     1 
ATOM   2552 C  CB    . GLU B 1 115 ? 13.559  23.174  -21.984 1.00 75.19  ? 115 GLU B CB    1 
ATOM   2553 C  CG    . GLU B 1 115 ? 13.761  23.430  -23.469 1.00 81.35  ? 115 GLU B CG    1 
ATOM   2554 C  CD    . GLU B 1 115 ? 12.457  23.317  -24.242 1.00 85.51  ? 115 GLU B CD    1 
ATOM   2555 O  OE1   . GLU B 1 115 ? 11.504  24.081  -23.932 1.00 86.05  ? 115 GLU B OE1   1 
ATOM   2556 O  OE2   . GLU B 1 115 ? 12.393  22.455  -25.156 1.00 87.99  ? 115 GLU B OE2   1 
ATOM   2557 N  N     . ASN B 1 116 ? 14.025  21.501  -19.546 1.00 65.18  ? 116 ASN B N     1 
ATOM   2558 C  CA    . ASN B 1 116 ? 13.630  21.029  -18.225 1.00 61.51  ? 116 ASN B CA    1 
ATOM   2559 C  C     . ASN B 1 116 ? 14.795  21.103  -17.246 1.00 59.06  ? 116 ASN B C     1 
ATOM   2560 O  O     . ASN B 1 116 ? 14.644  21.567  -16.118 1.00 57.74  ? 116 ASN B O     1 
ATOM   2561 C  CB    . ASN B 1 116 ? 13.116  19.596  -18.339 1.00 61.94  ? 116 ASN B CB    1 
ATOM   2562 C  CG    . ASN B 1 116 ? 11.808  19.505  -19.111 1.00 61.01  ? 116 ASN B CG    1 
ATOM   2563 O  OD1   . ASN B 1 116 ? 11.479  18.461  -19.675 1.00 62.03  ? 116 ASN B OD1   1 
ATOM   2564 N  ND2   . ASN B 1 116 ? 11.049  20.595  -19.123 1.00 60.55  ? 116 ASN B ND2   1 
ATOM   2565 N  N     . TYR B 1 117 ? 15.960  20.650  -17.686 1.00 56.79  ? 117 TYR B N     1 
ATOM   2566 C  CA    . TYR B 1 117 ? 17.144  20.681  -16.848 1.00 55.63  ? 117 TYR B CA    1 
ATOM   2567 C  C     . TYR B 1 117 ? 17.489  22.114  -16.462 1.00 54.84  ? 117 TYR B C     1 
ATOM   2568 O  O     . TYR B 1 117 ? 17.859  22.388  -15.324 1.00 53.68  ? 117 TYR B O     1 
ATOM   2569 C  CB    . TYR B 1 117 ? 18.309  20.029  -17.595 1.00 55.72  ? 117 TYR B CB    1 
ATOM   2570 C  CG    . TYR B 1 117 ? 19.673  20.283  -17.006 1.00 57.30  ? 117 TYR B CG    1 
ATOM   2571 C  CD1   . TYR B 1 117 ? 19.986  19.898  -15.703 1.00 59.29  ? 117 TYR B CD1   1 
ATOM   2572 C  CD2   . TYR B 1 117 ? 20.666  20.890  -17.763 1.00 57.94  ? 117 TYR B CD2   1 
ATOM   2573 C  CE1   . TYR B 1 117 ? 21.263  20.112  -15.177 1.00 59.03  ? 117 TYR B CE1   1 
ATOM   2574 C  CE2   . TYR B 1 117 ? 21.935  21.106  -17.249 1.00 58.65  ? 117 TYR B CE2   1 
ATOM   2575 C  CZ    . TYR B 1 117 ? 22.223  20.715  -15.965 1.00 59.44  ? 117 TYR B CZ    1 
ATOM   2576 O  OH    . TYR B 1 117 ? 23.487  20.925  -15.488 1.00 63.70  ? 117 TYR B OH    1 
ATOM   2577 N  N     . GLU B 1 118 ? 17.355  23.028  -17.418 1.00 56.30  ? 118 GLU B N     1 
ATOM   2578 C  CA    . GLU B 1 118 ? 17.669  24.433  -17.190 1.00 56.76  ? 118 GLU B CA    1 
ATOM   2579 C  C     . GLU B 1 118 ? 16.641  25.131  -16.341 1.00 54.71  ? 118 GLU B C     1 
ATOM   2580 O  O     . GLU B 1 118 ? 16.856  26.244  -15.885 1.00 53.46  ? 118 GLU B O     1 
ATOM   2581 C  CB    . GLU B 1 118 ? 17.830  25.163  -18.515 1.00 60.62  ? 118 GLU B CB    1 
ATOM   2582 C  CG    . GLU B 1 118 ? 19.117  24.807  -19.220 1.00 67.82  ? 118 GLU B CG    1 
ATOM   2583 C  CD    . GLU B 1 118 ? 19.263  25.523  -20.543 1.00 72.29  ? 118 GLU B CD    1 
ATOM   2584 O  OE1   . GLU B 1 118 ? 19.130  26.771  -20.560 1.00 73.58  ? 118 GLU B OE1   1 
ATOM   2585 O  OE2   . GLU B 1 118 ? 19.512  24.834  -21.563 1.00 75.08  ? 118 GLU B OE2   1 
ATOM   2586 N  N     . LEU B 1 119 ? 15.515  24.471  -16.135 1.00 54.30  ? 119 LEU B N     1 
ATOM   2587 C  CA    . LEU B 1 119 ? 14.459  25.017  -15.297 1.00 54.91  ? 119 LEU B CA    1 
ATOM   2588 C  C     . LEU B 1 119 ? 14.878  24.809  -13.832 1.00 54.59  ? 119 LEU B C     1 
ATOM   2589 O  O     . LEU B 1 119 ? 14.521  25.596  -12.945 1.00 54.32  ? 119 LEU B O     1 
ATOM   2590 C  CB    . LEU B 1 119 ? 13.148  24.283  -15.589 1.00 55.63  ? 119 LEU B CB    1 
ATOM   2591 C  CG    . LEU B 1 119 ? 11.866  24.758  -14.920 1.00 55.83  ? 119 LEU B CG    1 
ATOM   2592 C  CD1   . LEU B 1 119 ? 11.621  26.229  -15.217 1.00 57.96  ? 119 LEU B CD1   1 
ATOM   2593 C  CD2   . LEU B 1 119 ? 10.723  23.921  -15.449 1.00 56.05  ? 119 LEU B CD2   1 
ATOM   2594 N  N     . GLY B 1 120 ? 15.647  23.742  -13.601 1.00 53.19  ? 120 GLY B N     1 
ATOM   2595 C  CA    . GLY B 1 120 ? 16.121  23.432  -12.270 1.00 52.27  ? 120 GLY B CA    1 
ATOM   2596 C  C     . GLY B 1 120 ? 17.565  23.842  -12.047 1.00 52.61  ? 120 GLY B C     1 
ATOM   2597 O  O     . GLY B 1 120 ? 17.958  24.115  -10.906 1.00 52.11  ? 120 GLY B O     1 
ATOM   2598 N  N     . LEU B 1 121 ? 18.348  23.906  -13.128 1.00 51.78  ? 121 LEU B N     1 
ATOM   2599 C  CA    . LEU B 1 121 ? 19.760  24.267  -13.045 1.00 50.97  ? 121 LEU B CA    1 
ATOM   2600 C  C     . LEU B 1 121 ? 20.087  25.437  -12.115 1.00 52.16  ? 121 LEU B C     1 
ATOM   2601 O  O     . LEU B 1 121 ? 21.141  25.452  -11.479 1.00 52.40  ? 121 LEU B O     1 
ATOM   2602 C  CB    . LEU B 1 121 ? 20.333  24.542  -14.433 1.00 49.86  ? 121 LEU B CB    1 
ATOM   2603 C  CG    . LEU B 1 121 ? 21.851  24.787  -14.391 1.00 49.85  ? 121 LEU B CG    1 
ATOM   2604 C  CD1   . LEU B 1 121 ? 22.502  23.671  -13.606 1.00 49.57  ? 121 LEU B CD1   1 
ATOM   2605 C  CD2   . LEU B 1 121 ? 22.448  24.857  -15.794 1.00 48.48  ? 121 LEU B CD2   1 
ATOM   2606 N  N     . PRO B 1 122 ? 19.220  26.457  -12.048 1.00 52.70  ? 122 PRO B N     1 
ATOM   2607 C  CA    . PRO B 1 122 ? 19.617  27.515  -11.118 1.00 52.78  ? 122 PRO B CA    1 
ATOM   2608 C  C     . PRO B 1 122 ? 19.707  26.985  -9.681  1.00 52.09  ? 122 PRO B C     1 
ATOM   2609 O  O     . PRO B 1 122 ? 20.447  27.511  -8.854  1.00 51.41  ? 122 PRO B O     1 
ATOM   2610 C  CB    . PRO B 1 122 ? 18.524  28.588  -11.305 1.00 51.93  ? 122 PRO B CB    1 
ATOM   2611 C  CG    . PRO B 1 122 ? 17.411  27.888  -12.029 1.00 52.44  ? 122 PRO B CG    1 
ATOM   2612 C  CD    . PRO B 1 122 ? 18.137  26.920  -12.930 1.00 52.76  ? 122 PRO B CD    1 
ATOM   2613 N  N     . VAL B 1 123 ? 18.959  25.931  -9.388  1.00 52.22  ? 123 VAL B N     1 
ATOM   2614 C  CA    . VAL B 1 123 ? 18.995  25.358  -8.045  1.00 53.04  ? 123 VAL B CA    1 
ATOM   2615 C  C     . VAL B 1 123 ? 20.328  24.633  -7.807  1.00 52.94  ? 123 VAL B C     1 
ATOM   2616 O  O     . VAL B 1 123 ? 21.013  24.859  -6.802  1.00 51.68  ? 123 VAL B O     1 
ATOM   2617 C  CB    . VAL B 1 123 ? 17.823  24.389  -7.834  1.00 51.74  ? 123 VAL B CB    1 
ATOM   2618 C  CG1   . VAL B 1 123 ? 17.919  23.755  -6.465  1.00 52.16  ? 123 VAL B CG1   1 
ATOM   2619 C  CG2   . VAL B 1 123 ? 16.509  25.143  -7.964  1.00 50.51  ? 123 VAL B CG2   1 
ATOM   2620 N  N     . ILE B 1 124 ? 20.689  23.769  -8.746  1.00 53.74  ? 124 ILE B N     1 
ATOM   2621 C  CA    . ILE B 1 124 ? 21.936  23.029  -8.680  1.00 54.53  ? 124 ILE B CA    1 
ATOM   2622 C  C     . ILE B 1 124 ? 23.121  24.001  -8.582  1.00 56.21  ? 124 ILE B C     1 
ATOM   2623 O  O     . ILE B 1 124 ? 24.012  23.805  -7.758  1.00 57.28  ? 124 ILE B O     1 
ATOM   2624 C  CB    . ILE B 1 124 ? 22.069  22.135  -9.913  1.00 53.77  ? 124 ILE B CB    1 
ATOM   2625 C  CG1   . ILE B 1 124 ? 20.815  21.263  -10.021 1.00 53.49  ? 124 ILE B CG1   1 
ATOM   2626 C  CG2   . ILE B 1 124 ? 23.334  21.287  -9.824  1.00 54.20  ? 124 ILE B CG2   1 
ATOM   2627 C  CD1   . ILE B 1 124 ? 20.819  20.301  -11.186 1.00 54.30  ? 124 ILE B CD1   1 
ATOM   2628 N  N     . LYS B 1 125 ? 23.132  25.052  -9.405  1.00 57.93  ? 125 LYS B N     1 
ATOM   2629 C  CA    . LYS B 1 125 ? 24.212  26.050  -9.363  1.00 58.88  ? 125 LYS B CA    1 
ATOM   2630 C  C     . LYS B 1 125 ? 24.348  26.664  -7.978  1.00 59.30  ? 125 LYS B C     1 
ATOM   2631 O  O     . LYS B 1 125 ? 25.455  26.873  -7.484  1.00 59.48  ? 125 LYS B O     1 
ATOM   2632 C  CB    . LYS B 1 125 ? 23.967  27.171  -10.378 1.00 58.58  ? 125 LYS B CB    1 
ATOM   2633 C  CG    . LYS B 1 125 ? 24.641  26.943  -11.717 1.00 59.40  ? 125 LYS B CG    1 
ATOM   2634 C  CD    . LYS B 1 125 ? 24.223  27.976  -12.750 1.00 59.48  ? 125 LYS B CD    1 
ATOM   2635 C  CE    . LYS B 1 125 ? 24.886  27.692  -14.097 1.00 61.29  ? 125 LYS B CE    1 
ATOM   2636 N  NZ    . LYS B 1 125 ? 24.270  28.427  -15.245 1.00 61.87  ? 125 LYS B NZ    1 
ATOM   2637 N  N     . LYS B 1 126 ? 23.210  26.954  -7.360  1.00 60.95  ? 126 LYS B N     1 
ATOM   2638 C  CA    . LYS B 1 126 ? 23.172  27.544  -6.027  1.00 62.30  ? 126 LYS B CA    1 
ATOM   2639 C  C     . LYS B 1 126 ? 23.725  26.553  -4.988  1.00 62.64  ? 126 LYS B C     1 
ATOM   2640 O  O     . LYS B 1 126 ? 24.565  26.921  -4.167  1.00 63.50  ? 126 LYS B O     1 
ATOM   2641 C  CB    . LYS B 1 126 ? 21.732  27.944  -5.692  1.00 63.14  ? 126 LYS B CB    1 
ATOM   2642 C  CG    . LYS B 1 126 ? 21.555  28.686  -4.384  1.00 65.52  ? 126 LYS B CG    1 
ATOM   2643 C  CD    . LYS B 1 126 ? 20.068  28.802  -4.042  1.00 68.29  ? 126 LYS B CD    1 
ATOM   2644 C  CE    . LYS B 1 126 ? 19.843  29.300  -2.613  1.00 70.36  ? 126 LYS B CE    1 
ATOM   2645 N  NZ    . LYS B 1 126 ? 18.396  29.330  -2.223  1.00 69.82  ? 126 LYS B NZ    1 
ATOM   2646 N  N     . ALA B 1 127 ? 23.270  25.301  -5.026  1.00 61.73  ? 127 ALA B N     1 
ATOM   2647 C  CA    . ALA B 1 127 ? 23.766  24.293  -4.087  1.00 60.80  ? 127 ALA B CA    1 
ATOM   2648 C  C     . ALA B 1 127 ? 25.264  24.083  -4.319  1.00 60.88  ? 127 ALA B C     1 
ATOM   2649 O  O     . ALA B 1 127 ? 25.918  23.306  -3.624  1.00 61.33  ? 127 ALA B O     1 
ATOM   2650 C  CB    . ALA B 1 127 ? 23.031  22.996  -4.280  1.00 59.64  ? 127 ALA B CB    1 
ATOM   2651 N  N     . GLY B 1 128 ? 25.793  24.777  -5.321  1.00 60.55  ? 128 GLY B N     1 
ATOM   2652 C  CA    . GLY B 1 128 ? 27.208  24.704  -5.639  1.00 59.65  ? 128 GLY B CA    1 
ATOM   2653 C  C     . GLY B 1 128 ? 27.744  23.369  -6.102  1.00 59.26  ? 128 GLY B C     1 
ATOM   2654 O  O     . GLY B 1 128 ? 28.914  23.073  -5.870  1.00 60.04  ? 128 GLY B O     1 
ATOM   2655 N  N     . VAL B 1 129 ? 26.922  22.573  -6.779  1.00 58.29  ? 129 VAL B N     1 
ATOM   2656 C  CA    . VAL B 1 129 ? 27.379  21.268  -7.234  1.00 57.26  ? 129 VAL B CA    1 
ATOM   2657 C  C     . VAL B 1 129 ? 27.276  21.039  -8.735  1.00 56.56  ? 129 VAL B C     1 
ATOM   2658 O  O     . VAL B 1 129 ? 27.489  19.933  -9.201  1.00 55.92  ? 129 VAL B O     1 
ATOM   2659 C  CB    . VAL B 1 129 ? 26.627  20.139  -6.502  1.00 57.30  ? 129 VAL B CB    1 
ATOM   2660 C  CG1   . VAL B 1 129 ? 26.812  20.291  -4.998  1.00 55.07  ? 129 VAL B CG1   1 
ATOM   2661 C  CG2   . VAL B 1 129 ? 25.144  20.180  -6.860  1.00 57.73  ? 129 VAL B CG2   1 
ATOM   2662 N  N     . ASP B 1 130 ? 26.976  22.080  -9.497  1.00 56.82  ? 130 ASP B N     1 
ATOM   2663 C  CA    . ASP B 1 130 ? 26.882  21.914  -10.940 1.00 58.74  ? 130 ASP B CA    1 
ATOM   2664 C  C     . ASP B 1 130 ? 28.228  21.621  -11.619 1.00 59.31  ? 130 ASP B C     1 
ATOM   2665 O  O     . ASP B 1 130 ? 28.261  21.148  -12.762 1.00 59.38  ? 130 ASP B O     1 
ATOM   2666 C  CB    . ASP B 1 130 ? 26.251  23.145  -11.592 1.00 61.02  ? 130 ASP B CB    1 
ATOM   2667 C  CG    . ASP B 1 130 ? 27.073  24.402  -11.393 1.00 63.77  ? 130 ASP B CG    1 
ATOM   2668 O  OD1   . ASP B 1 130 ? 27.047  24.957  -10.266 1.00 64.01  ? 130 ASP B OD1   1 
ATOM   2669 O  OD2   . ASP B 1 130 ? 27.747  24.828  -12.366 1.00 64.32  ? 130 ASP B OD2   1 
ATOM   2670 N  N     . HIS B 1 131 ? 29.338  21.893  -10.940 1.00 58.67  ? 131 HIS B N     1 
ATOM   2671 C  CA    . HIS B 1 131 ? 30.626  21.612  -11.556 1.00 59.10  ? 131 HIS B CA    1 
ATOM   2672 C  C     . HIS B 1 131 ? 30.793  20.105  -11.752 1.00 58.99  ? 131 HIS B C     1 
ATOM   2673 O  O     . HIS B 1 131 ? 31.508  19.660  -12.661 1.00 59.38  ? 131 HIS B O     1 
ATOM   2674 C  CB    . HIS B 1 131 ? 31.782  22.160  -10.710 1.00 60.16  ? 131 HIS B CB    1 
ATOM   2675 C  CG    . HIS B 1 131 ? 31.859  21.585  -9.332  1.00 61.03  ? 131 HIS B CG    1 
ATOM   2676 N  ND1   . HIS B 1 131 ? 31.057  22.018  -8.298  1.00 62.51  ? 131 HIS B ND1   1 
ATOM   2677 C  CD2   . HIS B 1 131 ? 32.648  20.615  -8.814  1.00 60.97  ? 131 HIS B CD2   1 
ATOM   2678 C  CE1   . HIS B 1 131 ? 31.350  21.340  -7.202  1.00 62.42  ? 131 HIS B CE1   1 
ATOM   2679 N  NE2   . HIS B 1 131 ? 32.313  20.482  -7.488  1.00 61.96  ? 131 HIS B NE2   1 
ATOM   2680 N  N     . LYS B 1 132 ? 30.118  19.329  -10.902 1.00 56.96  ? 132 LYS B N     1 
ATOM   2681 C  CA    . LYS B 1 132 ? 30.175  17.865  -10.948 1.00 54.02  ? 132 LYS B CA    1 
ATOM   2682 C  C     . LYS B 1 132 ? 29.475  17.263  -12.160 1.00 53.12  ? 132 LYS B C     1 
ATOM   2683 O  O     . LYS B 1 132 ? 29.799  16.157  -12.581 1.00 52.62  ? 132 LYS B O     1 
ATOM   2684 C  CB    . LYS B 1 132 ? 29.522  17.274  -9.693  1.00 51.12  ? 132 LYS B CB    1 
ATOM   2685 C  CG    . LYS B 1 132 ? 30.164  17.702  -8.384  1.00 49.89  ? 132 LYS B CG    1 
ATOM   2686 C  CD    . LYS B 1 132 ? 29.497  17.069  -7.176  1.00 46.89  ? 132 LYS B CD    1 
ATOM   2687 C  CE    . LYS B 1 132 ? 30.313  17.319  -5.925  1.00 47.94  ? 132 LYS B CE    1 
ATOM   2688 N  NZ    . LYS B 1 132 ? 29.698  16.799  -4.666  1.00 48.38  ? 132 LYS B NZ    1 
ATOM   2689 N  N     . ILE B 1 133 ? 28.538  18.012  -12.733 1.00 52.44  ? 133 ILE B N     1 
ATOM   2690 C  CA    . ILE B 1 133 ? 27.714  17.526  -13.836 1.00 51.61  ? 133 ILE B CA    1 
ATOM   2691 C  C     . ILE B 1 133 ? 28.168  17.737  -15.278 1.00 52.90  ? 133 ILE B C     1 
ATOM   2692 O  O     . ILE B 1 133 ? 28.629  18.802  -15.639 1.00 54.91  ? 133 ILE B O     1 
ATOM   2693 C  CB    . ILE B 1 133 ? 26.282  18.109  -13.681 1.00 49.17  ? 133 ILE B CB    1 
ATOM   2694 C  CG1   . ILE B 1 133 ? 25.765  17.818  -12.268 1.00 43.40  ? 133 ILE B CG1   1 
ATOM   2695 C  CG2   . ILE B 1 133 ? 25.352  17.530  -14.744 1.00 47.73  ? 133 ILE B CG2   1 
ATOM   2696 C  CD1   . ILE B 1 133 ? 24.542  18.568  -11.906 1.00 42.06  ? 133 ILE B CD1   1 
ATOM   2697 N  N     . ASP B 1 134 ? 28.044  16.703  -16.101 1.00 55.27  ? 134 ASP B N     1 
ATOM   2698 C  CA    . ASP B 1 134 ? 28.382  16.808  -17.516 1.00 57.29  ? 134 ASP B CA    1 
ATOM   2699 C  C     . ASP B 1 134 ? 27.072  16.510  -18.228 1.00 58.39  ? 134 ASP B C     1 
ATOM   2700 O  O     . ASP B 1 134 ? 26.767  15.345  -18.499 1.00 59.30  ? 134 ASP B O     1 
ATOM   2701 C  CB    . ASP B 1 134 ? 29.459  15.789  -17.934 1.00 58.23  ? 134 ASP B CB    1 
ATOM   2702 C  CG    . ASP B 1 134 ? 29.642  15.695  -19.480 1.00 62.00  ? 134 ASP B CG    1 
ATOM   2703 O  OD1   . ASP B 1 134 ? 29.265  16.645  -20.216 1.00 62.30  ? 134 ASP B OD1   1 
ATOM   2704 O  OD2   . ASP B 1 134 ? 30.181  14.667  -19.966 1.00 61.70  ? 134 ASP B OD2   1 
ATOM   2705 N  N     . PHE B 1 135 ? 26.293  17.558  -18.509 1.00 58.73  ? 135 PHE B N     1 
ATOM   2706 C  CA    . PHE B 1 135 ? 25.006  17.395  -19.177 1.00 59.33  ? 135 PHE B CA    1 
ATOM   2707 C  C     . PHE B 1 135 ? 25.126  17.223  -20.680 1.00 60.56  ? 135 PHE B C     1 
ATOM   2708 O  O     . PHE B 1 135 ? 26.049  17.729  -21.307 1.00 62.06  ? 135 PHE B O     1 
ATOM   2709 C  CB    . PHE B 1 135 ? 24.087  18.582  -18.886 1.00 58.37  ? 135 PHE B CB    1 
ATOM   2710 C  CG    . PHE B 1 135 ? 22.678  18.400  -19.411 1.00 58.72  ? 135 PHE B CG    1 
ATOM   2711 C  CD1   . PHE B 1 135 ? 22.371  18.660  -20.746 1.00 57.74  ? 135 PHE B CD1   1 
ATOM   2712 C  CD2   . PHE B 1 135 ? 21.665  17.932  -18.574 1.00 57.19  ? 135 PHE B CD2   1 
ATOM   2713 C  CE1   . PHE B 1 135 ? 21.080  18.455  -21.235 1.00 57.31  ? 135 PHE B CE1   1 
ATOM   2714 C  CE2   . PHE B 1 135 ? 20.376  17.728  -19.059 1.00 55.21  ? 135 PHE B CE2   1 
ATOM   2715 C  CZ    . PHE B 1 135 ? 20.083  17.988  -20.387 1.00 55.25  ? 135 PHE B CZ    1 
ATOM   2716 N  N     . ARG B 1 136 ? 24.185  16.498  -21.263 1.00 61.11  ? 136 ARG B N     1 
ATOM   2717 C  CA    . ARG B 1 136 ? 24.212  16.295  -22.693 1.00 62.83  ? 136 ARG B CA    1 
ATOM   2718 C  C     . ARG B 1 136 ? 22.828  16.053  -23.264 1.00 64.50  ? 136 ARG B C     1 
ATOM   2719 O  O     . ARG B 1 136 ? 22.286  14.946  -23.150 1.00 65.10  ? 136 ARG B O     1 
ATOM   2720 C  CB    . ARG B 1 136 ? 25.117  15.116  -23.064 1.00 61.86  ? 136 ARG B CB    1 
ATOM   2721 C  CG    . ARG B 1 136 ? 26.588  15.298  -22.747 1.00 61.72  ? 136 ARG B CG    1 
ATOM   2722 C  CD    . ARG B 1 136 ? 27.412  14.303  -23.543 1.00 61.88  ? 136 ARG B CD    1 
ATOM   2723 N  NE    . ARG B 1 136 ? 28.658  13.966  -22.867 1.00 63.28  ? 136 ARG B NE    1 
ATOM   2724 C  CZ    . ARG B 1 136 ? 29.489  13.015  -23.277 1.00 63.96  ? 136 ARG B CZ    1 
ATOM   2725 N  NH1   . ARG B 1 136 ? 29.213  12.311  -24.368 1.00 63.80  ? 136 ARG B NH1   1 
ATOM   2726 N  NH2   . ARG B 1 136 ? 30.579  12.740  -22.574 1.00 65.13  ? 136 ARG B NH2   1 
ATOM   2727 N  N     . GLU B 1 137 ? 22.263  17.084  -23.887 1.00 65.07  ? 137 GLU B N     1 
ATOM   2728 C  CA    . GLU B 1 137 ? 20.955  16.951  -24.500 1.00 67.33  ? 137 GLU B CA    1 
ATOM   2729 C  C     . GLU B 1 137 ? 21.071  15.996  -25.682 1.00 67.52  ? 137 GLU B C     1 
ATOM   2730 O  O     . GLU B 1 137 ? 22.070  16.001  -26.404 1.00 67.96  ? 137 GLU B O     1 
ATOM   2731 C  CB    . GLU B 1 137 ? 20.434  18.307  -24.984 1.00 68.88  ? 137 GLU B CB    1 
ATOM   2732 C  CG    . GLU B 1 137 ? 19.061  18.226  -25.650 1.00 71.46  ? 137 GLU B CG    1 
ATOM   2733 C  CD    . GLU B 1 137 ? 18.631  19.540  -26.286 1.00 75.50  ? 137 GLU B CD    1 
ATOM   2734 O  OE1   . GLU B 1 137 ? 19.441  20.142  -27.043 1.00 76.94  ? 137 GLU B OE1   1 
ATOM   2735 O  OE2   . GLU B 1 137 ? 17.478  19.964  -26.039 1.00 76.06  ? 137 GLU B OE2   1 
ATOM   2736 N  N     . GLY B 1 138 ? 20.049  15.167  -25.868 1.00 67.83  ? 138 GLY B N     1 
ATOM   2737 C  CA    . GLY B 1 138 ? 20.054  14.224  -26.972 1.00 68.22  ? 138 GLY B CA    1 
ATOM   2738 C  C     . GLY B 1 138 ? 19.946  12.771  -26.551 1.00 67.81  ? 138 GLY B C     1 
ATOM   2739 O  O     . GLY B 1 138 ? 20.333  12.419  -25.436 1.00 67.60  ? 138 GLY B O     1 
ATOM   2740 N  N     . PRO B 1 139 ? 19.433  11.899  -27.434 1.00 67.42  ? 139 PRO B N     1 
ATOM   2741 C  CA    . PRO B 1 139 ? 19.260  10.464  -27.189 1.00 67.34  ? 139 PRO B CA    1 
ATOM   2742 C  C     . PRO B 1 139 ? 20.500  9.844   -26.561 1.00 67.57  ? 139 PRO B C     1 
ATOM   2743 O  O     . PRO B 1 139 ? 21.634  10.149  -26.958 1.00 67.54  ? 139 PRO B O     1 
ATOM   2744 C  CB    . PRO B 1 139 ? 18.986  9.914   -28.580 1.00 66.98  ? 139 PRO B CB    1 
ATOM   2745 C  CG    . PRO B 1 139 ? 18.241  11.032  -29.218 1.00 67.29  ? 139 PRO B CG    1 
ATOM   2746 C  CD    . PRO B 1 139 ? 19.060  12.233  -28.818 1.00 66.62  ? 139 PRO B CD    1 
ATOM   2747 N  N     . ALA B 1 140 ? 20.276  8.964   -25.588 1.00 67.13  ? 140 ALA B N     1 
ATOM   2748 C  CA    . ALA B 1 140 ? 21.369  8.312   -24.879 1.00 66.29  ? 140 ALA B CA    1 
ATOM   2749 C  C     . ALA B 1 140 ? 21.839  7.036   -25.557 1.00 65.64  ? 140 ALA B C     1 
ATOM   2750 O  O     . ALA B 1 140 ? 23.024  6.699   -25.516 1.00 64.35  ? 140 ALA B O     1 
ATOM   2751 C  CB    . ALA B 1 140 ? 20.943  8.015   -23.454 1.00 66.57  ? 140 ALA B CB    1 
ATOM   2752 N  N     . LEU B 1 141 ? 20.906  6.336   -26.189 1.00 65.71  ? 141 LEU B N     1 
ATOM   2753 C  CA    . LEU B 1 141 ? 21.224  5.089   -26.859 1.00 66.30  ? 141 LEU B CA    1 
ATOM   2754 C  C     . LEU B 1 141 ? 22.480  5.174   -27.758 1.00 67.21  ? 141 LEU B C     1 
ATOM   2755 O  O     . LEU B 1 141 ? 23.305  4.251   -27.764 1.00 66.64  ? 141 LEU B O     1 
ATOM   2756 C  CB    . LEU B 1 141 ? 20.001  4.622   -27.642 1.00 65.42  ? 141 LEU B CB    1 
ATOM   2757 C  CG    . LEU B 1 141 ? 19.885  3.106   -27.782 1.00 66.12  ? 141 LEU B CG    1 
ATOM   2758 C  CD1   . LEU B 1 141 ? 20.284  2.431   -26.477 1.00 66.54  ? 141 LEU B CD1   1 
ATOM   2759 C  CD2   . LEU B 1 141 ? 18.459  2.746   -28.172 1.00 66.74  ? 141 LEU B CD2   1 
ATOM   2760 N  N     . PRO B 1 142 ? 22.645  6.279   -28.523 1.00 67.57  ? 142 PRO B N     1 
ATOM   2761 C  CA    . PRO B 1 142 ? 23.816  6.443   -29.397 1.00 66.57  ? 142 PRO B CA    1 
ATOM   2762 C  C     . PRO B 1 142 ? 25.067  6.704   -28.560 1.00 66.04  ? 142 PRO B C     1 
ATOM   2763 O  O     . PRO B 1 142 ? 26.075  6.007   -28.688 1.00 66.52  ? 142 PRO B O     1 
ATOM   2764 C  CB    . PRO B 1 142 ? 23.462  7.666   -30.242 1.00 65.49  ? 142 PRO B CB    1 
ATOM   2765 C  CG    . PRO B 1 142 ? 21.982  7.675   -30.245 1.00 67.17  ? 142 PRO B CG    1 
ATOM   2766 C  CD    . PRO B 1 142 ? 21.650  7.327   -28.815 1.00 68.08  ? 142 PRO B CD    1 
ATOM   2767 N  N     . VAL B 1 143 ? 24.986  7.726   -27.712 1.00 64.61  ? 143 VAL B N     1 
ATOM   2768 C  CA    . VAL B 1 143 ? 26.090  8.103   -26.841 1.00 64.26  ? 143 VAL B CA    1 
ATOM   2769 C  C     . VAL B 1 143 ? 26.562  6.880   -26.082 1.00 64.80  ? 143 VAL B C     1 
ATOM   2770 O  O     . VAL B 1 143 ? 27.737  6.742   -25.756 1.00 64.02  ? 143 VAL B O     1 
ATOM   2771 C  CB    . VAL B 1 143 ? 25.654  9.159   -25.805 1.00 63.66  ? 143 VAL B CB    1 
ATOM   2772 C  CG1   . VAL B 1 143 ? 26.847  9.575   -24.947 1.00 62.19  ? 143 VAL B CG1   1 
ATOM   2773 C  CG2   . VAL B 1 143 ? 25.035  10.352  -26.507 1.00 63.28  ? 143 VAL B CG2   1 
ATOM   2774 N  N     . LEU B 1 144 ? 25.615  5.997   -25.798 1.00 65.95  ? 144 LEU B N     1 
ATOM   2775 C  CA    . LEU B 1 144 ? 25.887  4.767   -25.069 1.00 66.91  ? 144 LEU B CA    1 
ATOM   2776 C  C     . LEU B 1 144 ? 26.633  3.769   -25.963 1.00 67.92  ? 144 LEU B C     1 
ATOM   2777 O  O     . LEU B 1 144 ? 27.639  3.190   -25.547 1.00 65.99  ? 144 LEU B O     1 
ATOM   2778 C  CB    . LEU B 1 144 ? 24.556  4.178   -24.574 1.00 65.72  ? 144 LEU B CB    1 
ATOM   2779 C  CG    . LEU B 1 144 ? 24.301  3.874   -23.090 1.00 61.99  ? 144 LEU B CG    1 
ATOM   2780 C  CD1   . LEU B 1 144 ? 24.908  4.917   -22.164 1.00 60.25  ? 144 LEU B CD1   1 
ATOM   2781 C  CD2   . LEU B 1 144 ? 22.801  3.797   -22.908 1.00 60.27  ? 144 LEU B CD2   1 
ATOM   2782 N  N     . ASP B 1 145 ? 26.144  3.577   -27.188 1.00 70.16  ? 145 ASP B N     1 
ATOM   2783 C  CA    . ASP B 1 145 ? 26.791  2.659   -28.121 1.00 73.62  ? 145 ASP B CA    1 
ATOM   2784 C  C     . ASP B 1 145 ? 28.240  3.071   -28.391 1.00 75.61  ? 145 ASP B C     1 
ATOM   2785 O  O     . ASP B 1 145 ? 29.142  2.234   -28.380 1.00 75.30  ? 145 ASP B O     1 
ATOM   2786 C  CB    . ASP B 1 145 ? 26.019  2.581   -29.449 1.00 73.71  ? 145 ASP B CB    1 
ATOM   2787 C  CG    . ASP B 1 145 ? 24.905  1.526   -29.432 1.00 74.94  ? 145 ASP B CG    1 
ATOM   2788 O  OD1   . ASP B 1 145 ? 25.127  0.397   -28.930 1.00 74.63  ? 145 ASP B OD1   1 
ATOM   2789 O  OD2   . ASP B 1 145 ? 23.805  1.821   -29.942 1.00 75.16  ? 145 ASP B OD2   1 
ATOM   2790 N  N     . GLU B 1 146 ? 28.461  4.357   -28.641 1.00 78.56  ? 146 GLU B N     1 
ATOM   2791 C  CA    . GLU B 1 146 ? 29.811  4.851   -28.893 1.00 81.41  ? 146 GLU B CA    1 
ATOM   2792 C  C     . GLU B 1 146 ? 30.691  4.543   -27.697 1.00 81.78  ? 146 GLU B C     1 
ATOM   2793 O  O     . GLU B 1 146 ? 31.674  3.820   -27.803 1.00 82.28  ? 146 GLU B O     1 
ATOM   2794 C  CB    . GLU B 1 146 ? 29.799  6.361   -29.130 1.00 83.86  ? 146 GLU B CB    1 
ATOM   2795 C  CG    . GLU B 1 146 ? 29.661  6.766   -30.588 1.00 88.45  ? 146 GLU B CG    1 
ATOM   2796 C  CD    . GLU B 1 146 ? 30.869  6.355   -31.414 1.00 91.41  ? 146 GLU B CD    1 
ATOM   2797 O  OE1   . GLU B 1 146 ? 32.004  6.589   -30.941 1.00 92.05  ? 146 GLU B OE1   1 
ATOM   2798 O  OE2   . GLU B 1 146 ? 30.688  5.811   -32.532 1.00 93.22  ? 146 GLU B OE2   1 
ATOM   2799 N  N     . MET B 1 147 ? 30.320  5.099   -26.554 1.00 82.94  ? 147 MET B N     1 
ATOM   2800 C  CA    . MET B 1 147 ? 31.052  4.913   -25.306 1.00 83.19  ? 147 MET B CA    1 
ATOM   2801 C  C     . MET B 1 147 ? 31.494  3.465   -25.109 1.00 83.50  ? 147 MET B C     1 
ATOM   2802 O  O     . MET B 1 147 ? 32.554  3.205   -24.542 1.00 82.76  ? 147 MET B O     1 
ATOM   2803 C  CB    . MET B 1 147 ? 30.161  5.331   -24.135 1.00 82.68  ? 147 MET B CB    1 
ATOM   2804 C  CG    . MET B 1 147 ? 30.888  5.963   -22.977 1.00 82.81  ? 147 MET B CG    1 
ATOM   2805 S  SD    . MET B 1 147 ? 29.742  6.379   -21.646 1.00 83.90  ? 147 MET B SD    1 
ATOM   2806 C  CE    . MET B 1 147 ? 28.754  7.693   -22.425 1.00 83.79  ? 147 MET B CE    1 
ATOM   2807 N  N     . ILE B 1 148 ? 30.677  2.533   -25.597 1.00 84.88  ? 148 ILE B N     1 
ATOM   2808 C  CA    . ILE B 1 148 ? 30.935  1.098   -25.455 1.00 86.19  ? 148 ILE B CA    1 
ATOM   2809 C  C     . ILE B 1 148 ? 31.992  0.520   -26.408 1.00 87.21  ? 148 ILE B C     1 
ATOM   2810 O  O     . ILE B 1 148 ? 32.375  -0.648  -26.286 1.00 86.83  ? 148 ILE B O     1 
ATOM   2811 C  CB    . ILE B 1 148 ? 29.600  0.301   -25.607 1.00 86.56  ? 148 ILE B CB    1 
ATOM   2812 C  CG1   . ILE B 1 148 ? 29.556  -0.835  -24.588 1.00 86.68  ? 148 ILE B CG1   1 
ATOM   2813 C  CG2   . ILE B 1 148 ? 29.453  -0.252  -27.032 1.00 86.24  ? 148 ILE B CG2   1 
ATOM   2814 C  CD1   . ILE B 1 148 ? 28.268  -1.631  -24.630 1.00 87.83  ? 148 ILE B CD1   1 
ATOM   2815 N  N     . LYS B 1 149 ? 32.465  1.335   -27.350 1.00 88.23  ? 149 LYS B N     1 
ATOM   2816 C  CA    . LYS B 1 149 ? 33.470  0.893   -28.311 1.00 87.93  ? 149 LYS B CA    1 
ATOM   2817 C  C     . LYS B 1 149 ? 34.800  0.635   -27.626 1.00 88.90  ? 149 LYS B C     1 
ATOM   2818 O  O     . LYS B 1 149 ? 35.414  -0.400  -27.848 1.00 89.74  ? 149 LYS B O     1 
ATOM   2819 C  CB    . LYS B 1 149 ? 33.683  1.940   -29.408 1.00 87.25  ? 149 LYS B CB    1 
ATOM   2820 C  CG    . LYS B 1 149 ? 32.465  2.253   -30.263 1.00 87.14  ? 149 LYS B CG    1 
ATOM   2821 C  CD    . LYS B 1 149 ? 32.019  1.065   -31.095 1.00 87.20  ? 149 LYS B CD    1 
ATOM   2822 C  CE    . LYS B 1 149 ? 30.871  1.447   -32.022 1.00 86.83  ? 149 LYS B CE    1 
ATOM   2823 N  NZ    . LYS B 1 149 ? 31.238  2.571   -32.932 1.00 87.20  ? 149 LYS B NZ    1 
ATOM   2824 N  N     . ASP B 1 150 ? 35.242  1.572   -26.791 1.00 90.06  ? 150 ASP B N     1 
ATOM   2825 C  CA    . ASP B 1 150 ? 36.526  1.429   -26.102 1.00 91.66  ? 150 ASP B CA    1 
ATOM   2826 C  C     . ASP B 1 150 ? 36.447  0.766   -24.723 1.00 91.57  ? 150 ASP B C     1 
ATOM   2827 O  O     . ASP B 1 150 ? 36.001  1.378   -23.751 1.00 91.37  ? 150 ASP B O     1 
ATOM   2828 C  CB    . ASP B 1 150 ? 37.207  2.800   -25.991 1.00 93.64  ? 150 ASP B CB    1 
ATOM   2829 C  CG    . ASP B 1 150 ? 38.534  2.744   -25.240 1.00 96.21  ? 150 ASP B CG    1 
ATOM   2830 O  OD1   . ASP B 1 150 ? 39.202  1.683   -25.285 1.00 96.45  ? 150 ASP B OD1   1 
ATOM   2831 O  OD2   . ASP B 1 150 ? 38.913  3.767   -24.617 1.00 96.55  ? 150 ASP B OD2   1 
ATOM   2832 N  N     . GLU B 1 151 ? 36.901  -0.484  -24.650 1.00 91.68  ? 151 GLU B N     1 
ATOM   2833 C  CA    . GLU B 1 151 ? 36.890  -1.257  -23.408 1.00 91.90  ? 151 GLU B CA    1 
ATOM   2834 C  C     . GLU B 1 151 ? 37.515  -0.558  -22.197 1.00 89.42  ? 151 GLU B C     1 
ATOM   2835 O  O     . GLU B 1 151 ? 37.622  -1.144  -21.118 1.00 88.35  ? 151 GLU B O     1 
ATOM   2836 C  CB    . GLU B 1 151 ? 37.565  -2.624  -23.624 1.00 96.03  ? 151 GLU B CB    1 
ATOM   2837 N  N     . LYS B 1 152 ? 37.946  0.684   -22.379 1.00 87.22  ? 152 LYS B N     1 
ATOM   2838 C  CA    . LYS B 1 152 ? 38.518  1.443   -21.277 1.00 85.82  ? 152 LYS B CA    1 
ATOM   2839 C  C     . LYS B 1 152 ? 37.339  2.073   -20.531 1.00 84.00  ? 152 LYS B C     1 
ATOM   2840 O  O     . LYS B 1 152 ? 37.453  2.513   -19.378 1.00 82.64  ? 152 LYS B O     1 
ATOM   2841 C  CB    . LYS B 1 152 ? 39.463  2.530   -21.795 1.00 86.88  ? 152 LYS B CB    1 
ATOM   2842 C  CG    . LYS B 1 152 ? 40.753  2.009   -22.418 1.00 88.03  ? 152 LYS B CG    1 
ATOM   2843 C  CD    . LYS B 1 152 ? 41.713  3.162   -22.698 1.00 89.14  ? 152 LYS B CD    1 
ATOM   2844 C  CE    . LYS B 1 152 ? 43.007  2.700   -23.355 1.00 88.76  ? 152 LYS B CE    1 
ATOM   2845 N  NZ    . LYS B 1 152 ? 43.930  3.855   -23.529 1.00 89.50  ? 152 LYS B NZ    1 
ATOM   2846 N  N     . ASN B 1 153 ? 36.198  2.104   -21.213 1.00 81.61  ? 153 ASN B N     1 
ATOM   2847 C  CA    . ASN B 1 153 ? 34.979  2.645   -20.635 1.00 79.00  ? 153 ASN B CA    1 
ATOM   2848 C  C     . ASN B 1 153 ? 34.109  1.534   -20.047 1.00 77.17  ? 153 ASN B C     1 
ATOM   2849 O  O     . ASN B 1 153 ? 33.073  1.809   -19.449 1.00 77.35  ? 153 ASN B O     1 
ATOM   2850 C  CB    . ASN B 1 153 ? 34.196  3.436   -21.684 1.00 77.81  ? 153 ASN B CB    1 
ATOM   2851 C  CG    . ASN B 1 153 ? 34.874  4.735   -22.046 1.00 77.32  ? 153 ASN B CG    1 
ATOM   2852 O  OD1   . ASN B 1 153 ? 35.126  5.589   -21.184 1.00 76.15  ? 153 ASN B OD1   1 
ATOM   2853 N  ND2   . ASN B 1 153 ? 35.181  4.896   -23.322 1.00 77.33  ? 153 ASN B ND2   1 
ATOM   2854 N  N     . HIS B 1 154 ? 34.533  0.282   -20.218 1.00 74.36  ? 154 HIS B N     1 
ATOM   2855 C  CA    . HIS B 1 154 ? 33.796  -0.853  -19.676 1.00 70.78  ? 154 HIS B CA    1 
ATOM   2856 C  C     . HIS B 1 154 ? 34.092  -0.993  -18.192 1.00 69.62  ? 154 HIS B C     1 
ATOM   2857 O  O     . HIS B 1 154 ? 35.252  -1.012  -17.776 1.00 69.44  ? 154 HIS B O     1 
ATOM   2858 C  CB    . HIS B 1 154 ? 34.176  -2.143  -20.395 1.00 69.68  ? 154 HIS B CB    1 
ATOM   2859 C  CG    . HIS B 1 154 ? 33.726  -2.188  -21.820 1.00 70.53  ? 154 HIS B CG    1 
ATOM   2860 N  ND1   . HIS B 1 154 ? 33.262  -3.340  -22.417 1.00 69.69  ? 154 HIS B ND1   1 
ATOM   2861 C  CD2   . HIS B 1 154 ? 33.664  -1.221  -22.767 1.00 70.30  ? 154 HIS B CD2   1 
ATOM   2862 C  CE1   . HIS B 1 154 ? 32.931  -3.081  -23.669 1.00 70.17  ? 154 HIS B CE1   1 
ATOM   2863 N  NE2   . HIS B 1 154 ? 33.166  -1.803  -23.907 1.00 70.43  ? 154 HIS B NE2   1 
ATOM   2864 N  N     . GLY B 1 155 ? 33.030  -1.077  -17.398 1.00 67.31  ? 155 GLY B N     1 
ATOM   2865 C  CA    . GLY B 1 155 ? 33.186  -1.210  -15.968 1.00 63.91  ? 155 GLY B CA    1 
ATOM   2866 C  C     . GLY B 1 155 ? 33.765  0.041   -15.351 1.00 61.88  ? 155 GLY B C     1 
ATOM   2867 O  O     . GLY B 1 155 ? 34.491  -0.034  -14.361 1.00 61.87  ? 155 GLY B O     1 
ATOM   2868 N  N     . SER B 1 156 ? 33.432  1.195   -15.920 1.00 60.04  ? 156 SER B N     1 
ATOM   2869 C  CA    . SER B 1 156 ? 33.947  2.467   -15.415 1.00 59.10  ? 156 SER B CA    1 
ATOM   2870 C  C     . SER B 1 156 ? 32.990  3.306   -14.550 1.00 58.36  ? 156 SER B C     1 
ATOM   2871 O  O     . SER B 1 156 ? 33.409  4.308   -13.971 1.00 59.75  ? 156 SER B O     1 
ATOM   2872 C  CB    . SER B 1 156 ? 34.433  3.316   -16.584 1.00 58.33  ? 156 SER B CB    1 
ATOM   2873 O  OG    . SER B 1 156 ? 33.387  3.530   -17.509 1.00 56.88  ? 156 SER B OG    1 
ATOM   2874 N  N     . TYR B 1 157 ? 31.721  2.911   -14.461 1.00 56.54  ? 157 TYR B N     1 
ATOM   2875 C  CA    . TYR B 1 157 ? 30.747  3.647   -13.654 1.00 54.58  ? 157 TYR B CA    1 
ATOM   2876 C  C     . TYR B 1 157 ? 30.457  2.977   -12.326 1.00 52.95  ? 157 TYR B C     1 
ATOM   2877 O  O     . TYR B 1 157 ? 30.343  1.755   -12.251 1.00 54.35  ? 157 TYR B O     1 
ATOM   2878 C  CB    . TYR B 1 157 ? 29.448  3.814   -14.436 1.00 55.62  ? 157 TYR B CB    1 
ATOM   2879 C  CG    . TYR B 1 157 ? 29.601  4.796   -15.563 1.00 57.26  ? 157 TYR B CG    1 
ATOM   2880 C  CD1   . TYR B 1 157 ? 29.612  6.176   -15.316 1.00 56.65  ? 157 TYR B CD1   1 
ATOM   2881 C  CD2   . TYR B 1 157 ? 29.817  4.353   -16.868 1.00 57.30  ? 157 TYR B CD2   1 
ATOM   2882 C  CE1   . TYR B 1 157 ? 29.843  7.092   -16.345 1.00 57.06  ? 157 TYR B CE1   1 
ATOM   2883 C  CE2   . TYR B 1 157 ? 30.050  5.254   -17.902 1.00 58.79  ? 157 TYR B CE2   1 
ATOM   2884 C  CZ    . TYR B 1 157 ? 30.063  6.620   -17.635 1.00 58.82  ? 157 TYR B CZ    1 
ATOM   2885 O  OH    . TYR B 1 157 ? 30.311  7.490   -18.669 1.00 59.93  ? 157 TYR B OH    1 
ATOM   2886 N  N     . ASP B 1 158 ? 30.340  3.768   -11.273 1.00 50.54  ? 158 ASP B N     1 
ATOM   2887 C  CA    . ASP B 1 158 ? 30.046  3.200   -9.972  1.00 51.64  ? 158 ASP B CA    1 
ATOM   2888 C  C     . ASP B 1 158 ? 28.547  3.042   -9.786  1.00 50.92  ? 158 ASP B C     1 
ATOM   2889 O  O     . ASP B 1 158 ? 28.091  2.159   -9.076  1.00 51.13  ? 158 ASP B O     1 
ATOM   2890 C  CB    . ASP B 1 158 ? 30.559  4.099   -8.848  1.00 55.42  ? 158 ASP B CB    1 
ATOM   2891 C  CG    . ASP B 1 158 ? 32.081  4.192   -8.800  1.00 59.73  ? 158 ASP B CG    1 
ATOM   2892 O  OD1   . ASP B 1 158 ? 32.768  3.201   -9.160  1.00 61.85  ? 158 ASP B OD1   1 
ATOM   2893 O  OD2   . ASP B 1 158 ? 32.588  5.259   -8.372  1.00 60.48  ? 158 ASP B OD2   1 
ATOM   2894 N  N     . PHE B 1 159 ? 27.788  3.901   -10.449 1.00 50.39  ? 159 PHE B N     1 
ATOM   2895 C  CA    . PHE B 1 159 ? 26.347  3.922   -10.314 1.00 49.29  ? 159 PHE B CA    1 
ATOM   2896 C  C     . PHE B 1 159 ? 25.713  4.569   -11.537 1.00 49.39  ? 159 PHE B C     1 
ATOM   2897 O  O     . PHE B 1 159 ? 26.118  5.645   -11.950 1.00 50.55  ? 159 PHE B O     1 
ATOM   2898 C  CB    . PHE B 1 159 ? 26.008  4.747   -9.075  1.00 50.51  ? 159 PHE B CB    1 
ATOM   2899 C  CG    . PHE B 1 159 ? 24.551  4.959   -8.862  1.00 52.88  ? 159 PHE B CG    1 
ATOM   2900 C  CD1   . PHE B 1 159 ? 23.771  3.975   -8.273  1.00 55.15  ? 159 PHE B CD1   1 
ATOM   2901 C  CD2   . PHE B 1 159 ? 23.949  6.143   -9.246  1.00 54.28  ? 159 PHE B CD2   1 
ATOM   2902 C  CE1   . PHE B 1 159 ? 22.399  4.171   -8.065  1.00 55.34  ? 159 PHE B CE1   1 
ATOM   2903 C  CE2   . PHE B 1 159 ? 22.582  6.346   -9.044  1.00 56.38  ? 159 PHE B CE2   1 
ATOM   2904 C  CZ    . PHE B 1 159 ? 21.808  5.356   -8.451  1.00 55.82  ? 159 PHE B CZ    1 
ATOM   2905 N  N     . ILE B 1 160 ? 24.712  3.916   -12.107 1.00 48.67  ? 160 ILE B N     1 
ATOM   2906 C  CA    . ILE B 1 160 ? 24.004  4.438   -13.262 1.00 48.34  ? 160 ILE B CA    1 
ATOM   2907 C  C     . ILE B 1 160 ? 22.541  4.398   -12.884 1.00 48.66  ? 160 ILE B C     1 
ATOM   2908 O  O     . ILE B 1 160 ? 22.048  3.364   -12.441 1.00 50.76  ? 160 ILE B O     1 
ATOM   2909 C  CB    . ILE B 1 160 ? 24.197  3.547   -14.493 1.00 49.27  ? 160 ILE B CB    1 
ATOM   2910 C  CG1   . ILE B 1 160 ? 25.682  3.477   -14.863 1.00 49.79  ? 160 ILE B CG1   1 
ATOM   2911 C  CG2   . ILE B 1 160 ? 23.336  4.062   -15.639 1.00 47.33  ? 160 ILE B CG2   1 
ATOM   2912 C  CD1   . ILE B 1 160 ? 25.973  2.572   -16.046 1.00 49.58  ? 160 ILE B CD1   1 
ATOM   2913 N  N     . PHE B 1 161 ? 21.840  5.510   -13.051 1.00 47.83  ? 161 PHE B N     1 
ATOM   2914 C  CA    . PHE B 1 161 ? 20.432  5.557   -12.690 1.00 46.96  ? 161 PHE B CA    1 
ATOM   2915 C  C     . PHE B 1 161 ? 19.566  5.894   -13.878 1.00 45.38  ? 161 PHE B C     1 
ATOM   2916 O  O     . PHE B 1 161 ? 19.683  6.968   -14.441 1.00 46.90  ? 161 PHE B O     1 
ATOM   2917 C  CB    . PHE B 1 161 ? 20.203  6.582   -11.592 1.00 46.61  ? 161 PHE B CB    1 
ATOM   2918 C  CG    . PHE B 1 161 ? 18.813  6.581   -11.060 1.00 47.74  ? 161 PHE B CG    1 
ATOM   2919 C  CD1   . PHE B 1 161 ? 18.268  5.427   -10.522 1.00 48.67  ? 161 PHE B CD1   1 
ATOM   2920 C  CD2   . PHE B 1 161 ? 18.052  7.737   -11.064 1.00 48.81  ? 161 PHE B CD2   1 
ATOM   2921 C  CE1   . PHE B 1 161 ? 16.980  5.424   -9.987  1.00 49.15  ? 161 PHE B CE1   1 
ATOM   2922 C  CE2   . PHE B 1 161 ? 16.764  7.744   -10.532 1.00 49.63  ? 161 PHE B CE2   1 
ATOM   2923 C  CZ    . PHE B 1 161 ? 16.229  6.583   -9.991  1.00 49.14  ? 161 PHE B CZ    1 
ATOM   2924 N  N     . VAL B 1 162 ? 18.677  4.983   -14.240 1.00 44.06  ? 162 VAL B N     1 
ATOM   2925 C  CA    . VAL B 1 162 ? 17.816  5.189   -15.391 1.00 43.73  ? 162 VAL B CA    1 
ATOM   2926 C  C     . VAL B 1 162 ? 16.387  5.530   -15.039 1.00 44.18  ? 162 VAL B C     1 
ATOM   2927 O  O     . VAL B 1 162 ? 15.733  4.803   -14.303 1.00 44.24  ? 162 VAL B O     1 
ATOM   2928 C  CB    . VAL B 1 162 ? 17.804  3.944   -16.263 1.00 43.07  ? 162 VAL B CB    1 
ATOM   2929 C  CG1   . VAL B 1 162 ? 16.935  4.154   -17.489 1.00 42.11  ? 162 VAL B CG1   1 
ATOM   2930 C  CG2   . VAL B 1 162 ? 19.208  3.611   -16.658 1.00 44.07  ? 162 VAL B CG2   1 
ATOM   2931 N  N     . ASP B 1 163 ? 15.908  6.641   -15.585 1.00 45.66  ? 163 ASP B N     1 
ATOM   2932 C  CA    . ASP B 1 163 ? 14.545  7.100   -15.368 1.00 49.14  ? 163 ASP B CA    1 
ATOM   2933 C  C     . ASP B 1 163 ? 14.102  7.865   -16.590 1.00 51.32  ? 163 ASP B C     1 
ATOM   2934 O  O     . ASP B 1 163 ? 13.826  9.059   -16.531 1.00 52.22  ? 163 ASP B O     1 
ATOM   2935 C  CB    . ASP B 1 163 ? 14.452  8.018   -14.156 1.00 49.64  ? 163 ASP B CB    1 
ATOM   2936 C  CG    . ASP B 1 163 ? 13.033  8.481   -13.896 1.00 50.51  ? 163 ASP B CG    1 
ATOM   2937 O  OD1   . ASP B 1 163 ? 12.093  7.923   -14.512 1.00 52.53  ? 163 ASP B OD1   1 
ATOM   2938 O  OD2   . ASP B 1 163 ? 12.849  9.395   -13.070 1.00 52.39  ? 163 ASP B OD2   1 
ATOM   2939 N  N     . ALA B 1 164 ? 14.030  7.167   -17.707 1.00 54.19  ? 164 ALA B N     1 
ATOM   2940 C  CA    . ALA B 1 164 ? 13.653  7.796   -18.944 1.00 56.64  ? 164 ALA B CA    1 
ATOM   2941 C  C     . ALA B 1 164 ? 12.344  7.262   -19.461 1.00 59.08  ? 164 ALA B C     1 
ATOM   2942 O  O     . ALA B 1 164 ? 11.428  6.965   -18.703 1.00 59.07  ? 164 ALA B O     1 
ATOM   2943 C  CB    . ALA B 1 164 ? 14.744  7.587   -19.980 1.00 55.91  ? 164 ALA B CB    1 
ATOM   2944 N  N     . ASP B 1 165 ? 12.285  7.172   -20.781 1.00 63.57  ? 165 ASP B N     1 
ATOM   2945 C  CA    . ASP B 1 165 ? 11.134  6.698   -21.534 1.00 67.37  ? 165 ASP B CA    1 
ATOM   2946 C  C     . ASP B 1 165 ? 10.408  5.530   -20.882 1.00 67.42  ? 165 ASP B C     1 
ATOM   2947 O  O     . ASP B 1 165 ? 9.333   5.725   -20.301 1.00 69.31  ? 165 ASP B O     1 
ATOM   2948 C  CB    . ASP B 1 165 ? 11.623  6.321   -22.923 1.00 71.21  ? 165 ASP B CB    1 
ATOM   2949 C  CG    . ASP B 1 165 ? 13.027  5.739   -22.884 1.00 75.96  ? 165 ASP B CG    1 
ATOM   2950 O  OD1   . ASP B 1 165 ? 13.157  4.566   -22.446 1.00 77.72  ? 165 ASP B OD1   1 
ATOM   2951 O  OD2   . ASP B 1 165 ? 13.990  6.460   -23.258 1.00 74.92  ? 165 ASP B OD2   1 
ATOM   2952 N  N     . LYS B 1 166 ? 10.994  4.335   -20.977 1.00 65.26  ? 166 LYS B N     1 
ATOM   2953 C  CA    . LYS B 1 166 ? 10.424  3.112   -20.410 1.00 65.05  ? 166 LYS B CA    1 
ATOM   2954 C  C     . LYS B 1 166 ? 10.495  2.053   -21.485 1.00 65.69  ? 166 LYS B C     1 
ATOM   2955 O  O     . LYS B 1 166 ? 10.887  0.917   -21.234 1.00 66.70  ? 166 LYS B O     1 
ATOM   2956 C  CB    . LYS B 1 166 ? 8.955   3.287   -20.039 1.00 64.47  ? 166 LYS B CB    1 
ATOM   2957 C  CG    . LYS B 1 166 ? 8.534   2.536   -18.816 1.00 65.47  ? 166 LYS B CG    1 
ATOM   2958 C  CD    . LYS B 1 166 ? 9.162   3.154   -17.579 1.00 67.37  ? 166 LYS B CD    1 
ATOM   2959 C  CE    . LYS B 1 166 ? 8.678   4.584   -17.343 1.00 67.73  ? 166 LYS B CE    1 
ATOM   2960 N  NZ    . LYS B 1 166 ? 9.479   5.268   -16.281 1.00 66.70  ? 166 LYS B NZ    1 
ATOM   2961 N  N     . ASP B 1 167 ? 10.099  2.440   -22.692 1.00 65.61  ? 167 ASP B N     1 
ATOM   2962 C  CA    . ASP B 1 167 ? 10.098  1.537   -23.825 1.00 65.01  ? 167 ASP B CA    1 
ATOM   2963 C  C     . ASP B 1 167 ? 11.517  1.207   -24.258 1.00 63.75  ? 167 ASP B C     1 
ATOM   2964 O  O     . ASP B 1 167 ? 11.743  0.276   -25.034 1.00 63.72  ? 167 ASP B O     1 
ATOM   2965 C  CB    . ASP B 1 167 ? 9.280   2.142   -24.979 1.00 67.37  ? 167 ASP B CB    1 
ATOM   2966 C  CG    . ASP B 1 167 ? 9.556   3.633   -25.196 1.00 69.59  ? 167 ASP B CG    1 
ATOM   2967 O  OD1   . ASP B 1 167 ? 9.577   4.401   -24.211 1.00 70.07  ? 167 ASP B OD1   1 
ATOM   2968 O  OD2   . ASP B 1 167 ? 9.733   4.046   -26.365 1.00 71.61  ? 167 ASP B OD2   1 
ATOM   2969 N  N     . ASN B 1 168 ? 12.475  1.953   -23.722 1.00 61.70  ? 168 ASN B N     1 
ATOM   2970 C  CA    . ASN B 1 168 ? 13.877  1.737   -24.051 1.00 61.52  ? 168 ASN B CA    1 
ATOM   2971 C  C     . ASN B 1 168 ? 14.713  1.218   -22.877 1.00 61.32  ? 168 ASN B C     1 
ATOM   2972 O  O     . ASN B 1 168 ? 15.937  1.121   -22.987 1.00 61.36  ? 168 ASN B O     1 
ATOM   2973 C  CB    . ASN B 1 168 ? 14.491  3.039   -24.572 1.00 62.52  ? 168 ASN B CB    1 
ATOM   2974 C  CG    . ASN B 1 168 ? 14.138  3.317   -26.026 1.00 63.30  ? 168 ASN B CG    1 
ATOM   2975 O  OD1   . ASN B 1 168 ? 14.685  2.690   -26.940 1.00 63.89  ? 168 ASN B OD1   1 
ATOM   2976 N  ND2   . ASN B 1 168 ? 13.220  4.254   -26.248 1.00 61.61  ? 168 ASN B ND2   1 
ATOM   2977 N  N     . TYR B 1 169 ? 14.060  0.885   -21.763 1.00 60.31  ? 169 TYR B N     1 
ATOM   2978 C  CA    . TYR B 1 169 ? 14.764  0.390   -20.578 1.00 58.64  ? 169 TYR B CA    1 
ATOM   2979 C  C     . TYR B 1 169 ? 15.586  -0.854  -20.876 1.00 59.73  ? 169 TYR B C     1 
ATOM   2980 O  O     . TYR B 1 169 ? 16.754  -0.934  -20.503 1.00 59.81  ? 169 TYR B O     1 
ATOM   2981 C  CB    . TYR B 1 169 ? 13.771  0.091   -19.452 1.00 57.06  ? 169 TYR B CB    1 
ATOM   2982 C  CG    . TYR B 1 169 ? 13.517  1.246   -18.506 1.00 55.27  ? 169 TYR B CG    1 
ATOM   2983 C  CD1   . TYR B 1 169 ? 13.709  2.560   -18.912 1.00 54.27  ? 169 TYR B CD1   1 
ATOM   2984 C  CD2   . TYR B 1 169 ? 13.058  1.021   -17.210 1.00 54.95  ? 169 TYR B CD2   1 
ATOM   2985 C  CE1   . TYR B 1 169 ? 13.452  3.618   -18.055 1.00 54.51  ? 169 TYR B CE1   1 
ATOM   2986 C  CE2   . TYR B 1 169 ? 12.796  2.082   -16.339 1.00 54.59  ? 169 TYR B CE2   1 
ATOM   2987 C  CZ    . TYR B 1 169 ? 12.997  3.376   -16.771 1.00 55.00  ? 169 TYR B CZ    1 
ATOM   2988 O  OH    . TYR B 1 169 ? 12.753  4.436   -15.924 1.00 56.70  ? 169 TYR B OH    1 
ATOM   2989 N  N     . LEU B 1 170 ? 14.978  -1.826  -21.549 1.00 60.70  ? 170 LEU B N     1 
ATOM   2990 C  CA    . LEU B 1 170 ? 15.679  -3.053  -21.889 1.00 61.49  ? 170 LEU B CA    1 
ATOM   2991 C  C     . LEU B 1 170 ? 16.910  -2.751  -22.749 1.00 61.93  ? 170 LEU B C     1 
ATOM   2992 O  O     . LEU B 1 170 ? 17.967  -3.372  -22.578 1.00 61.54  ? 170 LEU B O     1 
ATOM   2993 C  CB    . LEU B 1 170 ? 14.745  -4.002  -22.644 1.00 63.61  ? 170 LEU B CB    1 
ATOM   2994 C  CG    . LEU B 1 170 ? 14.478  -5.388  -22.033 1.00 65.68  ? 170 LEU B CG    1 
ATOM   2995 C  CD1   . LEU B 1 170 ? 15.808  -6.057  -21.697 1.00 66.51  ? 170 LEU B CD1   1 
ATOM   2996 C  CD2   . LEU B 1 170 ? 13.616  -5.264  -20.783 1.00 65.36  ? 170 LEU B CD2   1 
ATOM   2997 N  N     . ASN B 1 171 ? 16.772  -1.793  -23.668 1.00 61.83  ? 171 ASN B N     1 
ATOM   2998 C  CA    . ASN B 1 171 ? 17.873  -1.414  -24.557 1.00 60.89  ? 171 ASN B CA    1 
ATOM   2999 C  C     . ASN B 1 171 ? 19.038  -0.810  -23.804 1.00 59.57  ? 171 ASN B C     1 
ATOM   3000 O  O     . ASN B 1 171 ? 20.180  -1.226  -23.999 1.00 61.03  ? 171 ASN B O     1 
ATOM   3001 C  CB    . ASN B 1 171 ? 17.428  -0.403  -25.612 1.00 62.18  ? 171 ASN B CB    1 
ATOM   3002 C  CG    . ASN B 1 171 ? 16.308  -0.916  -26.477 1.00 63.12  ? 171 ASN B CG    1 
ATOM   3003 O  OD1   . ASN B 1 171 ? 16.349  -2.043  -26.966 1.00 64.08  ? 171 ASN B OD1   1 
ATOM   3004 N  ND2   . ASN B 1 171 ? 15.297  -0.081  -26.685 1.00 64.00  ? 171 ASN B ND2   1 
ATOM   3005 N  N     . TYR B 1 172 ? 18.766  0.177   -22.959 1.00 55.27  ? 172 TYR B N     1 
ATOM   3006 C  CA    . TYR B 1 172 ? 19.845  0.797   -22.214 1.00 53.53  ? 172 TYR B CA    1 
ATOM   3007 C  C     . TYR B 1 172 ? 20.607  -0.279  -21.461 1.00 52.28  ? 172 TYR B C     1 
ATOM   3008 O  O     . TYR B 1 172 ? 21.842  -0.255  -21.387 1.00 49.49  ? 172 TYR B O     1 
ATOM   3009 C  CB    . TYR B 1 172 ? 19.304  1.822   -21.214 1.00 54.46  ? 172 TYR B CB    1 
ATOM   3010 C  CG    . TYR B 1 172 ? 18.553  2.985   -21.832 1.00 55.59  ? 172 TYR B CG    1 
ATOM   3011 C  CD1   . TYR B 1 172 ? 19.082  3.689   -22.919 1.00 55.91  ? 172 TYR B CD1   1 
ATOM   3012 C  CD2   . TYR B 1 172 ? 17.326  3.408   -21.308 1.00 55.94  ? 172 TYR B CD2   1 
ATOM   3013 C  CE1   . TYR B 1 172 ? 18.410  4.785   -23.470 1.00 55.96  ? 172 TYR B CE1   1 
ATOM   3014 C  CE2   . TYR B 1 172 ? 16.650  4.503   -21.846 1.00 56.41  ? 172 TYR B CE2   1 
ATOM   3015 C  CZ    . TYR B 1 172 ? 17.200  5.186   -22.928 1.00 57.32  ? 172 TYR B CZ    1 
ATOM   3016 O  OH    . TYR B 1 172 ? 16.555  6.279   -23.453 1.00 57.26  ? 172 TYR B OH    1 
ATOM   3017 N  N     . HIS B 1 173 ? 19.852  -1.242  -20.931 1.00 52.41  ? 173 HIS B N     1 
ATOM   3018 C  CA    . HIS B 1 173 ? 20.422  -2.325  -20.140 1.00 51.84  ? 173 HIS B CA    1 
ATOM   3019 C  C     . HIS B 1 173 ? 21.482  -3.137  -20.865 1.00 52.68  ? 173 HIS B C     1 
ATOM   3020 O  O     . HIS B 1 173 ? 22.510  -3.484  -20.267 1.00 51.37  ? 173 HIS B O     1 
ATOM   3021 C  CB    . HIS B 1 173 ? 19.325  -3.252  -19.610 1.00 49.37  ? 173 HIS B CB    1 
ATOM   3022 C  CG    . HIS B 1 173 ? 19.823  -4.239  -18.597 1.00 48.14  ? 173 HIS B CG    1 
ATOM   3023 N  ND1   . HIS B 1 173 ? 20.388  -3.852  -17.400 1.00 46.46  ? 173 HIS B ND1   1 
ATOM   3024 C  CD2   . HIS B 1 173 ? 19.927  -5.589  -18.642 1.00 46.47  ? 173 HIS B CD2   1 
ATOM   3025 C  CE1   . HIS B 1 173 ? 20.826  -4.920  -16.757 1.00 46.47  ? 173 HIS B CE1   1 
ATOM   3026 N  NE2   . HIS B 1 173 ? 20.559  -5.987  -17.490 1.00 46.01  ? 173 HIS B NE2   1 
ATOM   3027 N  N     . LYS B 1 174 ? 21.239  -3.438  -22.142 1.00 54.67  ? 174 LYS B N     1 
ATOM   3028 C  CA    . LYS B 1 174 ? 22.199  -4.199  -22.945 1.00 57.11  ? 174 LYS B CA    1 
ATOM   3029 C  C     . LYS B 1 174 ? 23.576  -3.535  -22.917 1.00 57.16  ? 174 LYS B C     1 
ATOM   3030 O  O     . LYS B 1 174 ? 24.600  -4.223  -22.978 1.00 57.14  ? 174 LYS B O     1 
ATOM   3031 C  CB    . LYS B 1 174 ? 21.735  -4.317  -24.403 1.00 59.98  ? 174 LYS B CB    1 
ATOM   3032 C  CG    . LYS B 1 174 ? 20.330  -4.864  -24.574 1.00 67.44  ? 174 LYS B CG    1 
ATOM   3033 C  CD    . LYS B 1 174 ? 20.105  -6.096  -23.682 1.00 73.75  ? 174 LYS B CD    1 
ATOM   3034 C  CE    . LYS B 1 174 ? 18.634  -6.557  -23.670 1.00 76.82  ? 174 LYS B CE    1 
ATOM   3035 N  NZ    . LYS B 1 174 ? 18.331  -7.563  -22.591 1.00 76.73  ? 174 LYS B NZ    1 
ATOM   3036 N  N     . ARG B 1 175 ? 23.600  -2.204  -22.817 1.00 56.21  ? 175 ARG B N     1 
ATOM   3037 C  CA    . ARG B 1 175 ? 24.861  -1.471  -22.790 1.00 56.13  ? 175 ARG B CA    1 
ATOM   3038 C  C     . ARG B 1 175 ? 25.322  -1.229  -21.342 1.00 56.13  ? 175 ARG B C     1 
ATOM   3039 O  O     . ARG B 1 175 ? 26.424  -1.610  -20.940 1.00 54.99  ? 175 ARG B O     1 
ATOM   3040 C  CB    . ARG B 1 175 ? 24.715  -0.117  -23.501 1.00 56.35  ? 175 ARG B CB    1 
ATOM   3041 C  CG    . ARG B 1 175 ? 23.631  -0.014  -24.598 1.00 58.37  ? 175 ARG B CG    1 
ATOM   3042 C  CD    . ARG B 1 175 ? 24.090  -0.542  -25.947 1.00 59.55  ? 175 ARG B CD    1 
ATOM   3043 N  NE    . ARG B 1 175 ? 23.220  -0.170  -27.070 1.00 61.24  ? 175 ARG B NE    1 
ATOM   3044 C  CZ    . ARG B 1 175 ? 21.929  -0.481  -27.168 1.00 63.06  ? 175 ARG B CZ    1 
ATOM   3045 N  NH1   . ARG B 1 175 ? 21.337  -1.165  -26.203 1.00 64.87  ? 175 ARG B NH1   1 
ATOM   3046 N  NH2   . ARG B 1 175 ? 21.229  -0.138  -28.245 1.00 63.09  ? 175 ARG B NH2   1 
ATOM   3047 N  N     . LEU B 1 176 ? 24.456  -0.593  -20.564 1.00 56.07  ? 176 LEU B N     1 
ATOM   3048 C  CA    . LEU B 1 176 ? 24.743  -0.258  -19.179 1.00 56.10  ? 176 LEU B CA    1 
ATOM   3049 C  C     . LEU B 1 176 ? 25.417  -1.348  -18.354 1.00 56.92  ? 176 LEU B C     1 
ATOM   3050 O  O     . LEU B 1 176 ? 26.218  -1.048  -17.465 1.00 56.71  ? 176 LEU B O     1 
ATOM   3051 C  CB    . LEU B 1 176 ? 23.445  0.182   -18.498 1.00 56.02  ? 176 LEU B CB    1 
ATOM   3052 C  CG    . LEU B 1 176 ? 23.155  1.681   -18.338 1.00 55.86  ? 176 LEU B CG    1 
ATOM   3053 C  CD1   . LEU B 1 176 ? 23.894  2.510   -19.379 1.00 54.15  ? 176 LEU B CD1   1 
ATOM   3054 C  CD2   . LEU B 1 176 ? 21.655  1.891   -18.435 1.00 55.12  ? 176 LEU B CD2   1 
ATOM   3055 N  N     . ILE B 1 177 ? 25.093  -2.609  -18.639 1.00 57.81  ? 177 ILE B N     1 
ATOM   3056 C  CA    . ILE B 1 177 ? 25.669  -3.736  -17.903 1.00 57.86  ? 177 ILE B CA    1 
ATOM   3057 C  C     . ILE B 1 177 ? 27.192  -3.837  -18.112 1.00 59.57  ? 177 ILE B C     1 
ATOM   3058 O  O     . ILE B 1 177 ? 27.928  -4.260  -17.206 1.00 59.60  ? 177 ILE B O     1 
ATOM   3059 C  CB    . ILE B 1 177 ? 24.997  -5.068  -18.322 1.00 57.12  ? 177 ILE B CB    1 
ATOM   3060 C  CG1   . ILE B 1 177 ? 24.858  -6.005  -17.102 1.00 56.21  ? 177 ILE B CG1   1 
ATOM   3061 C  CG2   . ILE B 1 177 ? 25.755  -5.694  -19.478 1.00 55.18  ? 177 ILE B CG2   1 
ATOM   3062 C  CD1   . ILE B 1 177 ? 26.055  -6.070  -16.156 1.00 53.55  ? 177 ILE B CD1   1 
ATOM   3063 N  N     . ASP B 1 178 ? 27.659  -3.461  -19.307 1.00 59.89  ? 178 ASP B N     1 
ATOM   3064 C  CA    . ASP B 1 178 ? 29.091  -3.486  -19.607 1.00 59.04  ? 178 ASP B CA    1 
ATOM   3065 C  C     . ASP B 1 178 ? 29.795  -2.284  -19.003 1.00 57.20  ? 178 ASP B C     1 
ATOM   3066 O  O     . ASP B 1 178 ? 30.946  -2.383  -18.583 1.00 56.02  ? 178 ASP B O     1 
ATOM   3067 C  CB    . ASP B 1 178 ? 29.344  -3.462  -21.111 1.00 61.61  ? 178 ASP B CB    1 
ATOM   3068 C  CG    . ASP B 1 178 ? 29.028  -4.775  -21.779 1.00 64.84  ? 178 ASP B CG    1 
ATOM   3069 O  OD1   . ASP B 1 178 ? 29.484  -5.834  -21.271 1.00 64.10  ? 178 ASP B OD1   1 
ATOM   3070 O  OD2   . ASP B 1 178 ? 28.334  -4.736  -22.827 1.00 67.46  ? 178 ASP B OD2   1 
ATOM   3071 N  N     . LEU B 1 179 ? 29.099  -1.147  -18.983 1.00 55.67  ? 179 LEU B N     1 
ATOM   3072 C  CA    . LEU B 1 179 ? 29.663  0.085   -18.457 1.00 53.51  ? 179 LEU B CA    1 
ATOM   3073 C  C     . LEU B 1 179 ? 29.743  0.123   -16.943 1.00 53.26  ? 179 LEU B C     1 
ATOM   3074 O  O     . LEU B 1 179 ? 30.549  0.877   -16.396 1.00 53.20  ? 179 LEU B O     1 
ATOM   3075 C  CB    . LEU B 1 179 ? 28.886  1.314   -18.960 1.00 52.59  ? 179 LEU B CB    1 
ATOM   3076 C  CG    . LEU B 1 179 ? 28.977  1.822   -20.413 1.00 52.49  ? 179 LEU B CG    1 
ATOM   3077 C  CD1   . LEU B 1 179 ? 30.373  1.586   -20.990 1.00 49.94  ? 179 LEU B CD1   1 
ATOM   3078 C  CD2   . LEU B 1 179 ? 27.944  1.119   -21.259 1.00 53.22  ? 179 LEU B CD2   1 
ATOM   3079 N  N     . VAL B 1 180 ? 28.921  -0.672  -16.257 1.00 52.37  ? 180 VAL B N     1 
ATOM   3080 C  CA    . VAL B 1 180 ? 28.970  -0.679  -14.794 1.00 51.98  ? 180 VAL B CA    1 
ATOM   3081 C  C     . VAL B 1 180 ? 30.059  -1.593  -14.291 1.00 51.45  ? 180 VAL B C     1 
ATOM   3082 O  O     . VAL B 1 180 ? 30.205  -2.725  -14.747 1.00 50.61  ? 180 VAL B O     1 
ATOM   3083 C  CB    . VAL B 1 180 ? 27.657  -1.148  -14.145 1.00 52.28  ? 180 VAL B CB    1 
ATOM   3084 C  CG1   . VAL B 1 180 ? 26.708  -0.006  -14.052 1.00 54.26  ? 180 VAL B CG1   1 
ATOM   3085 C  CG2   . VAL B 1 180 ? 27.050  -2.282  -14.942 1.00 51.68  ? 180 VAL B CG2   1 
ATOM   3086 N  N     . LYS B 1 181 ? 30.834  -1.111  -13.340 1.00 51.12  ? 181 LYS B N     1 
ATOM   3087 C  CA    . LYS B 1 181 ? 31.886  -1.958  -12.815 1.00 53.23  ? 181 LYS B CA    1 
ATOM   3088 C  C     . LYS B 1 181 ? 31.195  -3.145  -12.139 1.00 51.71  ? 181 LYS B C     1 
ATOM   3089 O  O     . LYS B 1 181 ? 30.051  -3.019  -11.710 1.00 52.79  ? 181 LYS B O     1 
ATOM   3090 C  CB    . LYS B 1 181 ? 32.730  -1.174  -11.795 1.00 54.18  ? 181 LYS B CB    1 
ATOM   3091 C  CG    . LYS B 1 181 ? 32.036  -0.936  -10.467 1.00 56.85  ? 181 LYS B CG    1 
ATOM   3092 C  CD    . LYS B 1 181 ? 32.903  -0.143  -9.518  1.00 58.47  ? 181 LYS B CD    1 
ATOM   3093 C  CE    . LYS B 1 181 ? 32.237  -0.014  -8.159  1.00 60.19  ? 181 LYS B CE    1 
ATOM   3094 N  NZ    . LYS B 1 181 ? 33.095  0.755   -7.205  1.00 63.95  ? 181 LYS B NZ    1 
ATOM   3095 N  N     . VAL B 1 182 ? 31.860  -4.296  -12.069 1.00 49.88  ? 182 VAL B N     1 
ATOM   3096 C  CA    . VAL B 1 182 ? 31.277  -5.442  -11.372 1.00 48.65  ? 182 VAL B CA    1 
ATOM   3097 C  C     . VAL B 1 182 ? 31.129  -5.001  -9.905  1.00 47.14  ? 182 VAL B C     1 
ATOM   3098 O  O     . VAL B 1 182 ? 32.085  -4.534  -9.285  1.00 45.07  ? 182 VAL B O     1 
ATOM   3099 C  CB    . VAL B 1 182 ? 32.195  -6.694  -11.438 1.00 49.39  ? 182 VAL B CB    1 
ATOM   3100 C  CG1   . VAL B 1 182 ? 31.719  -7.733  -10.443 1.00 49.10  ? 182 VAL B CG1   1 
ATOM   3101 C  CG2   . VAL B 1 182 ? 32.185  -7.289  -12.852 1.00 48.51  ? 182 VAL B CG2   1 
ATOM   3102 N  N     . GLY B 1 183 ? 29.926  -5.132  -9.361  1.00 45.93  ? 183 GLY B N     1 
ATOM   3103 C  CA    . GLY B 1 183 ? 29.696  -4.707  -7.992  1.00 45.21  ? 183 GLY B CA    1 
ATOM   3104 C  C     . GLY B 1 183 ? 29.004  -3.364  -8.017  1.00 44.71  ? 183 GLY B C     1 
ATOM   3105 O  O     . GLY B 1 183 ? 28.417  -2.921  -7.023  1.00 43.19  ? 183 GLY B O     1 
ATOM   3106 N  N     . GLY B 1 184 ? 29.089  -2.709  -9.173  1.00 44.69  ? 184 GLY B N     1 
ATOM   3107 C  CA    . GLY B 1 184 ? 28.445  -1.425  -9.338  1.00 45.93  ? 184 GLY B CA    1 
ATOM   3108 C  C     . GLY B 1 184 ? 26.947  -1.652  -9.411  1.00 46.96  ? 184 GLY B C     1 
ATOM   3109 O  O     . GLY B 1 184 ? 26.504  -2.773  -9.679  1.00 47.26  ? 184 GLY B O     1 
ATOM   3110 N  N     . VAL B 1 185 ? 26.156  -0.613  -9.163  1.00 46.42  ? 185 VAL B N     1 
ATOM   3111 C  CA    . VAL B 1 185 ? 24.711  -0.767  -9.231  1.00 46.04  ? 185 VAL B CA    1 
ATOM   3112 C  C     . VAL B 1 185 ? 24.041  0.104   -10.268 1.00 46.30  ? 185 VAL B C     1 
ATOM   3113 O  O     . VAL B 1 185 ? 24.383  1.268   -10.426 1.00 47.83  ? 185 VAL B O     1 
ATOM   3114 C  CB    . VAL B 1 185 ? 24.025  -0.496  -7.866  1.00 45.58  ? 185 VAL B CB    1 
ATOM   3115 C  CG1   . VAL B 1 185 ? 24.965  0.187   -6.926  1.00 45.26  ? 185 VAL B CG1   1 
ATOM   3116 C  CG2   . VAL B 1 185 ? 22.781  0.355   -8.068  1.00 42.96  ? 185 VAL B CG2   1 
ATOM   3117 N  N     . ILE B 1 186 ? 23.086  -0.486  -10.976 1.00 46.27  ? 186 ILE B N     1 
ATOM   3118 C  CA    . ILE B 1 186 ? 22.290  0.221   -11.976 1.00 44.72  ? 186 ILE B CA    1 
ATOM   3119 C  C     . ILE B 1 186 ? 20.889  0.277   -11.363 1.00 46.22  ? 186 ILE B C     1 
ATOM   3120 O  O     . ILE B 1 186 ? 20.420  -0.718  -10.810 1.00 47.12  ? 186 ILE B O     1 
ATOM   3121 C  CB    . ILE B 1 186 ? 22.181  -0.568  -13.270 1.00 41.21  ? 186 ILE B CB    1 
ATOM   3122 C  CG1   . ILE B 1 186 ? 23.564  -0.763  -13.879 1.00 40.66  ? 186 ILE B CG1   1 
ATOM   3123 C  CG2   . ILE B 1 186 ? 21.240  0.136   -14.213 1.00 39.48  ? 186 ILE B CG2   1 
ATOM   3124 C  CD1   . ILE B 1 186 ? 23.579  -1.697  -15.092 1.00 37.64  ? 186 ILE B CD1   1 
ATOM   3125 N  N     . GLY B 1 187 ? 20.222  1.423   -11.432 1.00 45.81  ? 187 GLY B N     1 
ATOM   3126 C  CA    . GLY B 1 187 ? 18.889  1.491   -10.871 1.00 44.64  ? 187 GLY B CA    1 
ATOM   3127 C  C     . GLY B 1 187 ? 17.840  1.935   -11.864 1.00 44.78  ? 187 GLY B C     1 
ATOM   3128 O  O     . GLY B 1 187 ? 17.989  2.973   -12.492 1.00 45.83  ? 187 GLY B O     1 
ATOM   3129 N  N     . TYR B 1 188 ? 16.783  1.149   -12.022 1.00 45.44  ? 188 TYR B N     1 
ATOM   3130 C  CA    . TYR B 1 188 ? 15.684  1.515   -12.922 1.00 46.39  ? 188 TYR B CA    1 
ATOM   3131 C  C     . TYR B 1 188 ? 14.489  2.059   -12.112 1.00 47.64  ? 188 TYR B C     1 
ATOM   3132 O  O     . TYR B 1 188 ? 14.037  1.427   -11.149 1.00 49.29  ? 188 TYR B O     1 
ATOM   3133 C  CB    . TYR B 1 188 ? 15.261  0.306   -13.753 1.00 45.25  ? 188 TYR B CB    1 
ATOM   3134 C  CG    . TYR B 1 188 ? 16.372  -0.200  -14.638 1.00 45.29  ? 188 TYR B CG    1 
ATOM   3135 C  CD1   . TYR B 1 188 ? 17.316  -1.094  -14.154 1.00 45.83  ? 188 TYR B CD1   1 
ATOM   3136 C  CD2   . TYR B 1 188 ? 16.514  0.263   -15.939 1.00 44.19  ? 188 TYR B CD2   1 
ATOM   3137 C  CE1   . TYR B 1 188 ? 18.367  -1.509  -14.934 1.00 45.57  ? 188 TYR B CE1   1 
ATOM   3138 C  CE2   . TYR B 1 188 ? 17.559  -0.142  -16.727 1.00 44.45  ? 188 TYR B CE2   1 
ATOM   3139 C  CZ    . TYR B 1 188 ? 18.489  -1.031  -16.222 1.00 46.59  ? 188 TYR B CZ    1 
ATOM   3140 O  OH    . TYR B 1 188 ? 19.546  -1.447  -17.014 1.00 48.37  ? 188 TYR B OH    1 
ATOM   3141 N  N     . ASP B 1 189 ? 13.981  3.228   -12.508 1.00 47.89  ? 189 ASP B N     1 
ATOM   3142 C  CA    . ASP B 1 189 ? 12.860  3.883   -11.812 1.00 48.15  ? 189 ASP B CA    1 
ATOM   3143 C  C     . ASP B 1 189 ? 11.486  3.544   -12.416 1.00 47.97  ? 189 ASP B C     1 
ATOM   3144 O  O     . ASP B 1 189 ? 11.374  3.232   -13.613 1.00 47.10  ? 189 ASP B O     1 
ATOM   3145 C  CB    . ASP B 1 189 ? 13.086  5.418   -11.819 1.00 47.70  ? 189 ASP B CB    1 
ATOM   3146 C  CG    . ASP B 1 189 ? 12.208  6.178   -10.797 1.00 49.17  ? 189 ASP B CG    1 
ATOM   3147 O  OD1   . ASP B 1 189 ? 11.592  5.559   -9.897  1.00 50.60  ? 189 ASP B OD1   1 
ATOM   3148 O  OD2   . ASP B 1 189 ? 12.146  7.422   -10.880 1.00 48.68  ? 189 ASP B OD2   1 
ATOM   3149 N  N     . ASN B 1 190 ? 10.456  3.598   -11.567 1.00 48.10  ? 190 ASN B N     1 
ATOM   3150 C  CA    . ASN B 1 190 ? 9.056   3.351   -11.951 1.00 48.85  ? 190 ASN B CA    1 
ATOM   3151 C  C     . ASN B 1 190 ? 8.775   1.917   -12.378 1.00 48.29  ? 190 ASN B C     1 
ATOM   3152 O  O     . ASN B 1 190 ? 8.011   1.709   -13.315 1.00 49.01  ? 190 ASN B O     1 
ATOM   3153 C  CB    . ASN B 1 190 ? 8.613   4.274   -13.114 1.00 49.69  ? 190 ASN B CB    1 
ATOM   3154 C  CG    . ASN B 1 190 ? 8.680   5.772   -12.770 1.00 51.16  ? 190 ASN B CG    1 
ATOM   3155 O  OD1   . ASN B 1 190 ? 9.741   6.398   -12.843 1.00 52.01  ? 190 ASN B OD1   1 
ATOM   3156 N  ND2   . ASN B 1 190 ? 7.540   6.346   -12.406 1.00 50.44  ? 190 ASN B ND2   1 
ATOM   3157 N  N     . THR B 1 191 ? 9.353   0.928   -11.699 1.00 47.04  ? 191 THR B N     1 
ATOM   3158 C  CA    . THR B 1 191 ? 9.142   -0.460  -12.113 1.00 44.33  ? 191 THR B CA    1 
ATOM   3159 C  C     . THR B 1 191 ? 7.940   -1.181  -11.545 1.00 42.91  ? 191 THR B C     1 
ATOM   3160 O  O     . THR B 1 191 ? 7.766   -2.370  -11.769 1.00 40.60  ? 191 THR B O     1 
ATOM   3161 C  CB    . THR B 1 191 ? 10.392  -1.316  -11.877 1.00 44.78  ? 191 THR B CB    1 
ATOM   3162 O  OG1   . THR B 1 191 ? 10.777  -1.252  -10.499 1.00 45.54  ? 191 THR B OG1   1 
ATOM   3163 C  CG2   . THR B 1 191 ? 11.528  -0.822  -12.757 1.00 44.88  ? 191 THR B CG2   1 
ATOM   3164 N  N     . LEU B 1 192 ? 7.115   -0.471  -10.792 1.00 43.52  ? 192 LEU B N     1 
ATOM   3165 C  CA    . LEU B 1 192 ? 5.899   -1.076  -10.291 1.00 44.11  ? 192 LEU B CA    1 
ATOM   3166 C  C     . LEU B 1 192 ? 4.762   -0.384  -11.028 1.00 45.54  ? 192 LEU B C     1 
ATOM   3167 O  O     . LEU B 1 192 ? 3.609   -0.755  -10.903 1.00 45.22  ? 192 LEU B O     1 
ATOM   3168 C  CB    . LEU B 1 192 ? 5.795   -0.942  -8.771  1.00 43.56  ? 192 LEU B CB    1 
ATOM   3169 C  CG    . LEU B 1 192 ? 6.660   -2.017  -8.081  1.00 43.11  ? 192 LEU B CG    1 
ATOM   3170 C  CD1   . LEU B 1 192 ? 6.529   -1.934  -6.586  1.00 41.41  ? 192 LEU B CD1   1 
ATOM   3171 C  CD2   . LEU B 1 192 ? 6.236   -3.393  -8.560  1.00 41.70  ? 192 LEU B CD2   1 
ATOM   3172 N  N     . TRP B 1 193 ? 5.128   0.615   -11.828 1.00 49.31  ? 193 TRP B N     1 
ATOM   3173 C  CA    . TRP B 1 193 ? 4.204   1.374   -12.678 1.00 52.25  ? 193 TRP B CA    1 
ATOM   3174 C  C     . TRP B 1 193 ? 2.828   1.555   -12.062 1.00 54.91  ? 193 TRP B C     1 
ATOM   3175 O  O     . TRP B 1 193 ? 1.809   1.389   -12.737 1.00 54.56  ? 193 TRP B O     1 
ATOM   3176 C  CB    . TRP B 1 193 ? 4.074   0.653   -14.022 1.00 51.69  ? 193 TRP B CB    1 
ATOM   3177 C  CG    . TRP B 1 193 ? 3.481   1.469   -15.117 1.00 51.43  ? 193 TRP B CG    1 
ATOM   3178 C  CD1   . TRP B 1 193 ? 2.424   1.129   -15.916 1.00 51.46  ? 193 TRP B CD1   1 
ATOM   3179 C  CD2   . TRP B 1 193 ? 3.904   2.768   -15.543 1.00 51.29  ? 193 TRP B CD2   1 
ATOM   3180 N  NE1   . TRP B 1 193 ? 2.161   2.137   -16.809 1.00 50.07  ? 193 TRP B NE1   1 
ATOM   3181 C  CE2   . TRP B 1 193 ? 3.053   3.157   -16.603 1.00 50.60  ? 193 TRP B CE2   1 
ATOM   3182 C  CE3   . TRP B 1 193 ? 4.918   3.643   -15.133 1.00 50.83  ? 193 TRP B CE3   1 
ATOM   3183 C  CZ2   . TRP B 1 193 ? 3.185   4.381   -17.253 1.00 48.92  ? 193 TRP B CZ2   1 
ATOM   3184 C  CZ3   . TRP B 1 193 ? 5.048   4.855   -15.781 1.00 50.65  ? 193 TRP B CZ3   1 
ATOM   3185 C  CH2   . TRP B 1 193 ? 4.186   5.214   -16.829 1.00 50.46  ? 193 TRP B CH2   1 
ATOM   3186 N  N     . ASN B 1 194 ? 2.812   1.900   -10.779 1.00 58.89  ? 194 ASN B N     1 
ATOM   3187 C  CA    . ASN B 1 194 ? 1.579   2.086   -10.019 1.00 62.49  ? 194 ASN B CA    1 
ATOM   3188 C  C     . ASN B 1 194 ? 0.819   0.760   -9.872  1.00 62.90  ? 194 ASN B C     1 
ATOM   3189 O  O     . ASN B 1 194 ? 0.743   0.192   -8.788  1.00 63.00  ? 194 ASN B O     1 
ATOM   3190 C  CB    . ASN B 1 194 ? 0.680   3.115   -10.697 1.00 66.55  ? 194 ASN B CB    1 
ATOM   3191 C  CG    . ASN B 1 194 ? -0.205  3.840   -9.705  1.00 72.32  ? 194 ASN B CG    1 
ATOM   3192 O  OD1   . ASN B 1 194 ? -0.648  3.259   -8.703  1.00 74.42  ? 194 ASN B OD1   1 
ATOM   3193 N  ND2   . ASN B 1 194 ? -0.474  5.119   -9.976  1.00 75.32  ? 194 ASN B ND2   1 
ATOM   3194 N  N     . GLY B 1 195 ? 0.262   0.274   -10.976 1.00 64.00  ? 195 GLY B N     1 
ATOM   3195 C  CA    . GLY B 1 195 ? -0.475  -0.974  -10.961 1.00 61.68  ? 195 GLY B CA    1 
ATOM   3196 C  C     . GLY B 1 195 ? -0.148  -1.736  -12.222 1.00 62.16  ? 195 GLY B C     1 
ATOM   3197 O  O     . GLY B 1 195 ? -0.315  -1.241  -13.353 1.00 60.37  ? 195 GLY B O     1 
ATOM   3198 N  N     . SER B 1 196 ? 0.350   -2.947  -11.994 1.00 62.68  ? 196 SER B N     1 
ATOM   3199 C  CA    . SER B 1 196 ? 0.760   -3.886  -13.035 1.00 61.17  ? 196 SER B CA    1 
ATOM   3200 C  C     . SER B 1 196 ? 0.318   -5.273  -12.566 1.00 61.81  ? 196 SER B C     1 
ATOM   3201 O  O     . SER B 1 196 ? 0.898   -6.289  -12.942 1.00 61.11  ? 196 SER B O     1 
ATOM   3202 C  CB    . SER B 1 196 ? 2.287   -3.856  -13.210 1.00 58.24  ? 196 SER B CB    1 
ATOM   3203 O  OG    . SER B 1 196 ? 2.943   -4.238  -12.017 1.00 53.40  ? 196 SER B OG    1 
ATOM   3204 N  N     . VAL B 1 197 ? -0.683  -5.282  -11.693 1.00 62.33  ? 197 VAL B N     1 
ATOM   3205 C  CA    . VAL B 1 197 ? -1.278  -6.499  -11.164 1.00 64.08  ? 197 VAL B CA    1 
ATOM   3206 C  C     . VAL B 1 197 ? -2.759  -6.179  -11.120 1.00 67.57  ? 197 VAL B C     1 
ATOM   3207 O  O     . VAL B 1 197 ? -3.507  -6.683  -10.284 1.00 67.79  ? 197 VAL B O     1 
ATOM   3208 C  CB    . VAL B 1 197 ? -0.800  -6.855  -9.727  1.00 61.39  ? 197 VAL B CB    1 
ATOM   3209 C  CG1   . VAL B 1 197 ? 0.610   -7.366  -9.757  1.00 60.39  ? 197 VAL B CG1   1 
ATOM   3210 C  CG2   . VAL B 1 197 ? -0.915  -5.668  -8.827  1.00 59.67  ? 197 VAL B CG2   1 
ATOM   3211 N  N     . VAL B 1 198 ? -3.173  -5.315  -12.033 1.00 71.82  ? 198 VAL B N     1 
ATOM   3212 C  CA    . VAL B 1 198 ? -4.563  -4.910  -12.111 1.00 76.95  ? 198 VAL B CA    1 
ATOM   3213 C  C     . VAL B 1 198 ? -5.390  -5.951  -12.833 1.00 79.70  ? 198 VAL B C     1 
ATOM   3214 O  O     . VAL B 1 198 ? -4.955  -6.523  -13.837 1.00 79.72  ? 198 VAL B O     1 
ATOM   3215 C  CB    . VAL B 1 198 ? -4.716  -3.558  -12.839 1.00 78.38  ? 198 VAL B CB    1 
ATOM   3216 C  CG1   . VAL B 1 198 ? -3.725  -3.470  -14.005 1.00 79.40  ? 198 VAL B CG1   1 
ATOM   3217 C  CG2   . VAL B 1 198 ? -6.151  -3.404  -13.341 1.00 79.28  ? 198 VAL B CG2   1 
ATOM   3218 N  N     . ALA B 1 199 ? -6.588  -6.189  -12.312 1.00 83.15  ? 199 ALA B N     1 
ATOM   3219 C  CA    . ALA B 1 199 ? -7.484  -7.162  -12.903 1.00 86.08  ? 199 ALA B CA    1 
ATOM   3220 C  C     . ALA B 1 199 ? -7.598  -6.898  -14.397 1.00 88.81  ? 199 ALA B C     1 
ATOM   3221 O  O     . ALA B 1 199 ? -7.793  -5.759  -14.825 1.00 88.47  ? 199 ALA B O     1 
ATOM   3222 C  CB    . ALA B 1 199 ? -8.849  -7.076  -12.248 1.00 85.83  ? 199 ALA B CB    1 
ATOM   3223 N  N     . PRO B 1 200 ? -7.436  -7.949  -15.213 1.00 91.85  ? 200 PRO B N     1 
ATOM   3224 C  CA    . PRO B 1 200 ? -7.530  -7.834  -16.671 1.00 94.29  ? 200 PRO B CA    1 
ATOM   3225 C  C     . PRO B 1 200 ? -8.884  -7.268  -17.095 1.00 96.70  ? 200 PRO B C     1 
ATOM   3226 O  O     . PRO B 1 200 ? -8.952  -6.356  -17.929 1.00 95.73  ? 200 PRO B O     1 
ATOM   3227 C  CB    . PRO B 1 200 ? -7.341  -9.271  -17.139 1.00 93.79  ? 200 PRO B CB    1 
ATOM   3228 C  CG    . PRO B 1 200 ? -6.386  -9.814  -16.123 1.00 94.13  ? 200 PRO B CG    1 
ATOM   3229 C  CD    . PRO B 1 200 ? -6.956  -9.287  -14.824 1.00 92.85  ? 200 PRO B CD    1 
ATOM   3230 N  N     . PRO B 1 201 ? -9.985  -7.795  -16.511 1.00 99.49  ? 201 PRO B N     1 
ATOM   3231 C  CA    . PRO B 1 201 ? -11.312 -7.293  -16.878 1.00 100.61 ? 201 PRO B CA    1 
ATOM   3232 C  C     . PRO B 1 201 ? -11.362 -5.808  -16.588 1.00 101.11 ? 201 PRO B C     1 
ATOM   3233 O  O     . PRO B 1 201 ? -11.942 -5.028  -17.347 1.00 101.63 ? 201 PRO B O     1 
ATOM   3234 C  CB    . PRO B 1 201 ? -12.246 -8.093  -15.969 1.00 100.71 ? 201 PRO B CB    1 
ATOM   3235 C  CG    . PRO B 1 201 ? -11.427 -8.245  -14.718 1.00 100.51 ? 201 PRO B CG    1 
ATOM   3236 C  CD    . PRO B 1 201 ? -10.081 -8.649  -15.307 1.00 100.61 ? 201 PRO B CD    1 
ATOM   3237 N  N     . ASP B 1 202 ? -10.736 -5.426  -15.481 1.00 101.25 ? 202 ASP B N     1 
ATOM   3238 C  CA    . ASP B 1 202 ? -10.706 -4.035  -15.086 1.00 101.55 ? 202 ASP B CA    1 
ATOM   3239 C  C     . ASP B 1 202 ? -10.300 -3.125  -16.234 1.00 100.78 ? 202 ASP B C     1 
ATOM   3240 O  O     . ASP B 1 202 ? -9.110  -2.868  -16.455 1.00 100.39 ? 202 ASP B O     1 
ATOM   3241 C  CB    . ASP B 1 202 ? -9.737  -3.813  -13.939 1.00 103.14 ? 202 ASP B CB    1 
ATOM   3242 C  CG    . ASP B 1 202 ? -9.470  -2.349  -13.712 1.00 105.51 ? 202 ASP B CG    1 
ATOM   3243 O  OD1   . ASP B 1 202 ? -10.373 -1.642  -13.209 1.00 107.09 ? 202 ASP B OD1   1 
ATOM   3244 O  OD2   . ASP B 1 202 ? -8.363  -1.897  -14.065 1.00 107.31 ? 202 ASP B OD2   1 
ATOM   3245 N  N     . ALA B 1 203 ? -11.298 -2.644  -16.968 1.00 99.52  ? 203 ALA B N     1 
ATOM   3246 C  CA    . ALA B 1 203 ? -11.045 -1.731  -18.073 1.00 97.33  ? 203 ALA B CA    1 
ATOM   3247 C  C     . ALA B 1 203 ? -10.354 -0.484  -17.489 1.00 94.47  ? 203 ALA B C     1 
ATOM   3248 O  O     . ALA B 1 203 ? -9.488  0.118   -18.139 1.00 95.35  ? 203 ALA B O     1 
ATOM   3249 C  CB    . ALA B 1 203 ? -12.369 -1.354  -18.764 1.00 97.35  ? 203 ALA B CB    1 
ATOM   3250 N  N     . PRO B 1 204 ? -10.727 -0.088  -16.250 1.00 90.03  ? 204 PRO B N     1 
ATOM   3251 C  CA    . PRO B 1 204 ? -10.112 1.082   -15.631 1.00 85.90  ? 204 PRO B CA    1 
ATOM   3252 C  C     . PRO B 1 204 ? -8.585  1.117   -15.708 1.00 81.77  ? 204 PRO B C     1 
ATOM   3253 O  O     . PRO B 1 204 ? -7.885  0.616   -14.835 1.00 82.38  ? 204 PRO B O     1 
ATOM   3254 C  CB    . PRO B 1 204 ? -10.637 1.015   -14.203 1.00 86.52  ? 204 PRO B CB    1 
ATOM   3255 C  CG    . PRO B 1 204 ? -12.030 0.567   -14.417 1.00 87.00  ? 204 PRO B CG    1 
ATOM   3256 C  CD    . PRO B 1 204 ? -11.860 -0.555  -15.424 1.00 89.03  ? 204 PRO B CD    1 
ATOM   3257 N  N     . LEU B 1 205 ? -8.090  1.710   -16.783 1.00 76.57  ? 205 LEU B N     1 
ATOM   3258 C  CA    . LEU B 1 205 ? -6.670  1.889   -17.026 1.00 71.17  ? 205 LEU B CA    1 
ATOM   3259 C  C     . LEU B 1 205 ? -6.577  2.799   -18.231 1.00 69.13  ? 205 LEU B C     1 
ATOM   3260 O  O     . LEU B 1 205 ? -6.805  2.372   -19.362 1.00 69.66  ? 205 LEU B O     1 
ATOM   3261 C  CB    . LEU B 1 205 ? -5.977  0.568   -17.326 1.00 69.62  ? 205 LEU B CB    1 
ATOM   3262 C  CG    . LEU B 1 205 ? -5.527  -0.258  -16.127 1.00 69.18  ? 205 LEU B CG    1 
ATOM   3263 C  CD1   . LEU B 1 205 ? -4.520  -1.286  -16.594 1.00 68.35  ? 205 LEU B CD1   1 
ATOM   3264 C  CD2   . LEU B 1 205 ? -4.909  0.642   -15.077 1.00 68.18  ? 205 LEU B CD2   1 
ATOM   3265 N  N     . ARG B 1 206 ? -6.279  4.068   -17.992 1.00 65.99  ? 206 ARG B N     1 
ATOM   3266 C  CA    . ARG B 1 206 ? -6.172  5.004   -19.095 1.00 62.55  ? 206 ARG B CA    1 
ATOM   3267 C  C     . ARG B 1 206 ? -5.212  4.403   -20.122 1.00 59.44  ? 206 ARG B C     1 
ATOM   3268 O  O     . ARG B 1 206 ? -4.214  3.772   -19.765 1.00 58.15  ? 206 ARG B O     1 
ATOM   3269 C  CB    . ARG B 1 206 ? -5.667  6.365   -18.596 1.00 63.57  ? 206 ARG B CB    1 
ATOM   3270 C  CG    . ARG B 1 206 ? -5.722  6.556   -17.085 1.00 65.40  ? 206 ARG B CG    1 
ATOM   3271 C  CD    . ARG B 1 206 ? -5.730  8.021   -16.719 1.00 66.13  ? 206 ARG B CD    1 
ATOM   3272 N  NE    . ARG B 1 206 ? -7.072  8.576   -16.877 1.00 70.67  ? 206 ARG B NE    1 
ATOM   3273 C  CZ    . ARG B 1 206 ? -7.962  8.686   -15.889 1.00 72.27  ? 206 ARG B CZ    1 
ATOM   3274 N  NH1   . ARG B 1 206 ? -7.644  8.281   -14.661 1.00 70.98  ? 206 ARG B NH1   1 
ATOM   3275 N  NH2   . ARG B 1 206 ? -9.174  9.195   -16.132 1.00 71.26  ? 206 ARG B NH2   1 
ATOM   3276 N  N     . LYS B 1 207 ? -5.526  4.579   -21.398 1.00 56.47  ? 207 LYS B N     1 
ATOM   3277 C  CA    . LYS B 1 207 ? -4.680  4.036   -22.443 1.00 54.17  ? 207 LYS B CA    1 
ATOM   3278 C  C     . LYS B 1 207 ? -3.199  4.321   -22.205 1.00 51.78  ? 207 LYS B C     1 
ATOM   3279 O  O     . LYS B 1 207 ? -2.342  3.545   -22.614 1.00 51.20  ? 207 LYS B O     1 
ATOM   3280 C  CB    . LYS B 1 207 ? -5.087  4.592   -23.815 1.00 56.54  ? 207 LYS B CB    1 
ATOM   3281 C  CG    . LYS B 1 207 ? -6.447  4.136   -24.334 1.00 58.82  ? 207 LYS B CG    1 
ATOM   3282 C  CD    . LYS B 1 207 ? -6.521  2.632   -24.566 1.00 61.26  ? 207 LYS B CD    1 
ATOM   3283 C  CE    . LYS B 1 207 ? -7.975  2.206   -24.830 1.00 63.90  ? 207 LYS B CE    1 
ATOM   3284 N  NZ    . LYS B 1 207 ? -8.148  0.725   -24.991 1.00 65.17  ? 207 LYS B NZ    1 
ATOM   3285 N  N     . TYR B 1 208 ? -2.890  5.432   -21.547 1.00 49.50  ? 208 TYR B N     1 
ATOM   3286 C  CA    . TYR B 1 208 ? -1.497  5.779   -21.302 1.00 46.26  ? 208 TYR B CA    1 
ATOM   3287 C  C     . TYR B 1 208 ? -0.762  4.848   -20.354 1.00 45.33  ? 208 TYR B C     1 
ATOM   3288 O  O     . TYR B 1 208 ? 0.378   4.476   -20.612 1.00 44.80  ? 208 TYR B O     1 
ATOM   3289 C  CB    . TYR B 1 208 ? -1.398  7.209   -20.788 1.00 46.14  ? 208 TYR B CB    1 
ATOM   3290 C  CG    . TYR B 1 208 ? -0.004  7.626   -20.366 1.00 47.60  ? 208 TYR B CG    1 
ATOM   3291 C  CD1   . TYR B 1 208 ? 0.485   7.322   -19.091 1.00 48.60  ? 208 TYR B CD1   1 
ATOM   3292 C  CD2   . TYR B 1 208 ? 0.830   8.322   -21.236 1.00 47.74  ? 208 TYR B CD2   1 
ATOM   3293 C  CE1   . TYR B 1 208 ? 1.758   7.697   -18.702 1.00 47.97  ? 208 TYR B CE1   1 
ATOM   3294 C  CE2   . TYR B 1 208 ? 2.113   8.700   -20.852 1.00 48.88  ? 208 TYR B CE2   1 
ATOM   3295 C  CZ    . TYR B 1 208 ? 2.565   8.382   -19.585 1.00 49.03  ? 208 TYR B CZ    1 
ATOM   3296 O  OH    . TYR B 1 208 ? 3.828   8.751   -19.196 1.00 52.43  ? 208 TYR B OH    1 
ATOM   3297 N  N     . VAL B 1 209 ? -1.392  4.461   -19.255 1.00 44.29  ? 209 VAL B N     1 
ATOM   3298 C  CA    . VAL B 1 209 ? -0.696  3.600   -18.330 1.00 44.30  ? 209 VAL B CA    1 
ATOM   3299 C  C     . VAL B 1 209 ? -0.662  2.194   -18.878 1.00 46.53  ? 209 VAL B C     1 
ATOM   3300 O  O     . VAL B 1 209 ? 0.327   1.476   -18.702 1.00 46.08  ? 209 VAL B O     1 
ATOM   3301 C  CB    . VAL B 1 209 ? -1.339  3.631   -16.914 1.00 43.70  ? 209 VAL B CB    1 
ATOM   3302 C  CG1   . VAL B 1 209 ? -2.257  4.844   -16.788 1.00 42.33  ? 209 VAL B CG1   1 
ATOM   3303 C  CG2   . VAL B 1 209 ? -2.060  2.352   -16.616 1.00 40.30  ? 209 VAL B CG2   1 
ATOM   3304 N  N     . ARG B 1 210 ? -1.736  1.797   -19.558 1.00 48.65  ? 210 ARG B N     1 
ATOM   3305 C  CA    . ARG B 1 210 ? -1.795  0.453   -20.120 1.00 51.27  ? 210 ARG B CA    1 
ATOM   3306 C  C     . ARG B 1 210 ? -0.722  0.291   -21.212 1.00 52.05  ? 210 ARG B C     1 
ATOM   3307 O  O     . ARG B 1 210 ? -0.066  -0.751  -21.316 1.00 53.11  ? 210 ARG B O     1 
ATOM   3308 C  CB    . ARG B 1 210 ? -3.203  0.175   -20.665 1.00 51.67  ? 210 ARG B CB    1 
ATOM   3309 C  CG    . ARG B 1 210 ? -3.330  -1.121  -21.461 1.00 56.61  ? 210 ARG B CG    1 
ATOM   3310 C  CD    . ARG B 1 210 ? -4.792  -1.492  -21.768 1.00 60.19  ? 210 ARG B CD    1 
ATOM   3311 N  NE    . ARG B 1 210 ? -5.318  -2.435  -20.779 1.00 64.11  ? 210 ARG B NE    1 
ATOM   3312 C  CZ    . ARG B 1 210 ? -6.422  -2.246  -20.057 1.00 65.44  ? 210 ARG B CZ    1 
ATOM   3313 N  NH1   . ARG B 1 210 ? -7.148  -1.141  -20.204 1.00 63.62  ? 210 ARG B NH1   1 
ATOM   3314 N  NH2   . ARG B 1 210 ? -6.787  -3.161  -19.162 1.00 67.15  ? 210 ARG B NH2   1 
ATOM   3315 N  N     . TYR B 1 211 ? -0.527  1.338   -21.997 1.00 51.89  ? 211 TYR B N     1 
ATOM   3316 C  CA    . TYR B 1 211 ? 0.448   1.334   -23.076 1.00 53.03  ? 211 TYR B CA    1 
ATOM   3317 C  C     . TYR B 1 211 ? 1.865   1.120   -22.577 1.00 54.13  ? 211 TYR B C     1 
ATOM   3318 O  O     . TYR B 1 211 ? 2.644   0.389   -23.181 1.00 55.37  ? 211 TYR B O     1 
ATOM   3319 C  CB    . TYR B 1 211 ? 0.385   2.662   -23.842 1.00 52.79  ? 211 TYR B CB    1 
ATOM   3320 C  CG    . TYR B 1 211 ? 1.520   2.871   -24.813 1.00 53.02  ? 211 TYR B CG    1 
ATOM   3321 C  CD1   . TYR B 1 211 ? 1.490   2.317   -26.098 1.00 54.03  ? 211 TYR B CD1   1 
ATOM   3322 C  CD2   . TYR B 1 211 ? 2.654   3.584   -24.434 1.00 54.70  ? 211 TYR B CD2   1 
ATOM   3323 C  CE1   . TYR B 1 211 ? 2.568   2.466   -26.978 1.00 54.82  ? 211 TYR B CE1   1 
ATOM   3324 C  CE2   . TYR B 1 211 ? 3.740   3.737   -25.305 1.00 56.02  ? 211 TYR B CE2   1 
ATOM   3325 C  CZ    . TYR B 1 211 ? 3.689   3.175   -26.568 1.00 55.69  ? 211 TYR B CZ    1 
ATOM   3326 O  OH    . TYR B 1 211 ? 4.774   3.306   -27.392 1.00 58.23  ? 211 TYR B OH    1 
ATOM   3327 N  N     . TYR B 1 212 ? 2.217   1.769   -21.482 1.00 55.17  ? 212 TYR B N     1 
ATOM   3328 C  CA    . TYR B 1 212 ? 3.567   1.630   -20.981 1.00 56.39  ? 212 TYR B CA    1 
ATOM   3329 C  C     . TYR B 1 212 ? 3.747   0.449   -20.054 1.00 56.78  ? 212 TYR B C     1 
ATOM   3330 O  O     . TYR B 1 212 ? 4.854   -0.034  -19.854 1.00 56.99  ? 212 TYR B O     1 
ATOM   3331 C  CB    . TYR B 1 212 ? 3.980   2.915   -20.291 1.00 57.10  ? 212 TYR B CB    1 
ATOM   3332 C  CG    . TYR B 1 212 ? 4.471   3.959   -21.255 1.00 59.36  ? 212 TYR B CG    1 
ATOM   3333 C  CD1   . TYR B 1 212 ? 5.698   3.810   -21.901 1.00 59.69  ? 212 TYR B CD1   1 
ATOM   3334 C  CD2   . TYR B 1 212 ? 3.716   5.102   -21.524 1.00 60.97  ? 212 TYR B CD2   1 
ATOM   3335 C  CE1   . TYR B 1 212 ? 6.166   4.775   -22.791 1.00 61.53  ? 212 TYR B CE1   1 
ATOM   3336 C  CE2   . TYR B 1 212 ? 4.177   6.078   -22.417 1.00 62.35  ? 212 TYR B CE2   1 
ATOM   3337 C  CZ    . TYR B 1 212 ? 5.402   5.902   -23.040 1.00 62.46  ? 212 TYR B CZ    1 
ATOM   3338 O  OH    . TYR B 1 212 ? 5.874   6.859   -23.899 1.00 65.93  ? 212 TYR B OH    1 
ATOM   3339 N  N     . ARG B 1 213 ? 2.644   -0.021  -19.498 1.00 57.50  ? 213 ARG B N     1 
ATOM   3340 C  CA    . ARG B 1 213 ? 2.666   -1.146  -18.585 1.00 57.32  ? 213 ARG B CA    1 
ATOM   3341 C  C     . ARG B 1 213 ? 3.310   -2.389  -19.193 1.00 57.30  ? 213 ARG B C     1 
ATOM   3342 O  O     . ARG B 1 213 ? 4.065   -3.101  -18.535 1.00 56.06  ? 213 ARG B O     1 
ATOM   3343 C  CB    . ARG B 1 213 ? 1.244   -1.463  -18.167 1.00 56.89  ? 213 ARG B CB    1 
ATOM   3344 C  CG    . ARG B 1 213 ? 1.119   -2.691  -17.343 1.00 57.13  ? 213 ARG B CG    1 
ATOM   3345 C  CD    . ARG B 1 213 ? -0.314  -3.046  -17.258 1.00 59.35  ? 213 ARG B CD    1 
ATOM   3346 N  NE    . ARG B 1 213 ? -0.492  -4.304  -16.570 1.00 64.49  ? 213 ARG B NE    1 
ATOM   3347 C  CZ    . ARG B 1 213 ? -1.621  -4.997  -16.597 1.00 66.59  ? 213 ARG B CZ    1 
ATOM   3348 N  NH1   . ARG B 1 213 ? -2.654  -4.516  -17.290 1.00 64.77  ? 213 ARG B NH1   1 
ATOM   3349 N  NH2   . ARG B 1 213 ? -1.705  -6.167  -15.946 1.00 65.11  ? 213 ARG B NH2   1 
ATOM   3350 N  N     . ASP B 1 214 ? 3.009   -2.645  -20.455 1.00 57.89  ? 214 ASP B N     1 
ATOM   3351 C  CA    . ASP B 1 214 ? 3.553   -3.812  -21.133 1.00 59.50  ? 214 ASP B CA    1 
ATOM   3352 C  C     . ASP B 1 214 ? 5.066   -3.861  -21.136 1.00 57.48  ? 214 ASP B C     1 
ATOM   3353 O  O     . ASP B 1 214 ? 5.657   -4.931  -20.977 1.00 57.66  ? 214 ASP B O     1 
ATOM   3354 C  CB    . ASP B 1 214 ? 3.034   -3.866  -22.565 1.00 64.42  ? 214 ASP B CB    1 
ATOM   3355 C  CG    . ASP B 1 214 ? 1.547   -4.116  -22.621 1.00 69.91  ? 214 ASP B CG    1 
ATOM   3356 O  OD1   . ASP B 1 214 ? 0.783   -3.333  -22.001 1.00 72.67  ? 214 ASP B OD1   1 
ATOM   3357 O  OD2   . ASP B 1 214 ? 1.145   -5.104  -23.275 1.00 74.21  ? 214 ASP B OD2   1 
ATOM   3358 N  N     . PHE B 1 215 ? 5.693   -2.709  -21.331 1.00 54.98  ? 215 PHE B N     1 
ATOM   3359 C  CA    . PHE B 1 215 ? 7.148   -2.641  -21.347 1.00 53.74  ? 215 PHE B CA    1 
ATOM   3360 C  C     . PHE B 1 215 ? 7.697   -2.908  -19.951 1.00 52.51  ? 215 PHE B C     1 
ATOM   3361 O  O     . PHE B 1 215 ? 8.671   -3.637  -19.774 1.00 52.70  ? 215 PHE B O     1 
ATOM   3362 C  CB    . PHE B 1 215 ? 7.600   -1.262  -21.818 1.00 52.25  ? 215 PHE B CB    1 
ATOM   3363 C  CG    . PHE B 1 215 ? 7.271   -0.983  -23.244 1.00 52.22  ? 215 PHE B CG    1 
ATOM   3364 C  CD1   . PHE B 1 215 ? 8.071   -1.492  -24.264 1.00 50.08  ? 215 PHE B CD1   1 
ATOM   3365 C  CD2   . PHE B 1 215 ? 6.136   -0.239  -23.579 1.00 52.88  ? 215 PHE B CD2   1 
ATOM   3366 C  CE1   . PHE B 1 215 ? 7.752   -1.270  -25.596 1.00 49.68  ? 215 PHE B CE1   1 
ATOM   3367 C  CE2   . PHE B 1 215 ? 5.806   -0.010  -24.919 1.00 52.08  ? 215 PHE B CE2   1 
ATOM   3368 C  CZ    . PHE B 1 215 ? 6.620   -0.531  -25.928 1.00 49.92  ? 215 PHE B CZ    1 
ATOM   3369 N  N     . VAL B 1 216 ? 7.049   -2.312  -18.960 1.00 51.28  ? 216 VAL B N     1 
ATOM   3370 C  CA    . VAL B 1 216 ? 7.467   -2.458  -17.582 1.00 49.42  ? 216 VAL B CA    1 
ATOM   3371 C  C     . VAL B 1 216 ? 7.428   -3.922  -17.158 1.00 49.29  ? 216 VAL B C     1 
ATOM   3372 O  O     . VAL B 1 216 ? 8.350   -4.409  -16.513 1.00 48.85  ? 216 VAL B O     1 
ATOM   3373 C  CB    . VAL B 1 216 ? 6.584   -1.587  -16.674 1.00 48.32  ? 216 VAL B CB    1 
ATOM   3374 C  CG1   . VAL B 1 216 ? 6.978   -1.772  -15.233 1.00 48.52  ? 216 VAL B CG1   1 
ATOM   3375 C  CG2   . VAL B 1 216 ? 6.737   -0.133  -17.071 1.00 45.64  ? 216 VAL B CG2   1 
ATOM   3376 N  N     . LEU B 1 217 ? 6.365   -4.624  -17.534 1.00 49.55  ? 217 LEU B N     1 
ATOM   3377 C  CA    . LEU B 1 217 ? 6.238   -6.037  -17.202 1.00 49.26  ? 217 LEU B CA    1 
ATOM   3378 C  C     . LEU B 1 217 ? 7.393   -6.805  -17.829 1.00 50.21  ? 217 LEU B C     1 
ATOM   3379 O  O     . LEU B 1 217 ? 8.002   -7.665  -17.189 1.00 49.81  ? 217 LEU B O     1 
ATOM   3380 C  CB    . LEU B 1 217 ? 4.911   -6.586  -17.719 1.00 46.88  ? 217 LEU B CB    1 
ATOM   3381 C  CG    . LEU B 1 217 ? 3.692   -6.099  -16.938 1.00 48.09  ? 217 LEU B CG    1 
ATOM   3382 C  CD1   . LEU B 1 217 ? 2.423   -6.529  -17.649 1.00 46.62  ? 217 LEU B CD1   1 
ATOM   3383 C  CD2   . LEU B 1 217 ? 3.743   -6.638  -15.507 1.00 45.99  ? 217 LEU B CD2   1 
ATOM   3384 N  N     . GLU B 1 218 ? 7.697   -6.484  -19.084 1.00 51.22  ? 218 GLU B N     1 
ATOM   3385 C  CA    . GLU B 1 218 ? 8.789   -7.146  -19.790 1.00 52.77  ? 218 GLU B CA    1 
ATOM   3386 C  C     . GLU B 1 218 ? 10.148  -6.816  -19.165 1.00 51.54  ? 218 GLU B C     1 
ATOM   3387 O  O     . GLU B 1 218 ? 10.989  -7.698  -18.980 1.00 51.23  ? 218 GLU B O     1 
ATOM   3388 C  CB    . GLU B 1 218 ? 8.780   -6.744  -21.262 1.00 55.15  ? 218 GLU B CB    1 
ATOM   3389 C  CG    . GLU B 1 218 ? 10.121  -6.928  -21.941 1.00 62.25  ? 218 GLU B CG    1 
ATOM   3390 C  CD    . GLU B 1 218 ? 10.209  -6.192  -23.269 1.00 67.39  ? 218 GLU B CD    1 
ATOM   3391 O  OE1   . GLU B 1 218 ? 9.579   -6.669  -24.243 1.00 70.33  ? 218 GLU B OE1   1 
ATOM   3392 O  OE2   . GLU B 1 218 ? 10.895  -5.135  -23.333 1.00 67.46  ? 218 GLU B OE2   1 
ATOM   3393 N  N     . LEU B 1 219 ? 10.362  -5.547  -18.841 1.00 49.69  ? 219 LEU B N     1 
ATOM   3394 C  CA    . LEU B 1 219 ? 11.615  -5.131  -18.235 1.00 47.81  ? 219 LEU B CA    1 
ATOM   3395 C  C     . LEU B 1 219 ? 11.849  -5.970  -16.977 1.00 46.81  ? 219 LEU B C     1 
ATOM   3396 O  O     . LEU B 1 219 ? 12.934  -6.521  -16.768 1.00 43.48  ? 219 LEU B O     1 
ATOM   3397 C  CB    . LEU B 1 219 ? 11.554  -3.633  -17.887 1.00 46.86  ? 219 LEU B CB    1 
ATOM   3398 C  CG    . LEU B 1 219 ? 12.795  -2.870  -17.375 1.00 48.54  ? 219 LEU B CG    1 
ATOM   3399 C  CD1   . LEU B 1 219 ? 12.734  -2.720  -15.869 1.00 47.10  ? 219 LEU B CD1   1 
ATOM   3400 C  CD2   . LEU B 1 219 ? 14.093  -3.563  -17.808 1.00 46.37  ? 219 LEU B CD2   1 
ATOM   3401 N  N     . ASN B 1 220 ? 10.807  -6.077  -16.159 1.00 46.66  ? 220 ASN B N     1 
ATOM   3402 C  CA    . ASN B 1 220 ? 10.879  -6.823  -14.917 1.00 48.24  ? 220 ASN B CA    1 
ATOM   3403 C  C     . ASN B 1 220 ? 11.266  -8.288  -15.118 1.00 50.40  ? 220 ASN B C     1 
ATOM   3404 O  O     . ASN B 1 220 ? 12.223  -8.759  -14.501 1.00 49.81  ? 220 ASN B O     1 
ATOM   3405 C  CB    . ASN B 1 220 ? 9.550   -6.720  -14.175 1.00 48.45  ? 220 ASN B CB    1 
ATOM   3406 C  CG    . ASN B 1 220 ? 9.235   -5.296  -13.735 1.00 49.94  ? 220 ASN B CG    1 
ATOM   3407 O  OD1   . ASN B 1 220 ? 10.045  -4.384  -13.911 1.00 48.90  ? 220 ASN B OD1   1 
ATOM   3408 N  ND2   . ASN B 1 220 ? 8.054   -5.101  -13.152 1.00 49.88  ? 220 ASN B ND2   1 
ATOM   3409 N  N     . LYS B 1 221 ? 10.531  -9.005  -15.973 1.00 51.90  ? 221 LYS B N     1 
ATOM   3410 C  CA    . LYS B 1 221 ? 10.825  -10.411 -16.245 1.00 53.05  ? 221 LYS B CA    1 
ATOM   3411 C  C     . LYS B 1 221 ? 12.271  -10.551 -16.659 1.00 52.96  ? 221 LYS B C     1 
ATOM   3412 O  O     . LYS B 1 221 ? 13.019  -11.336 -16.077 1.00 54.06  ? 221 LYS B O     1 
ATOM   3413 C  CB    . LYS B 1 221 ? 9.941   -10.948 -17.368 1.00 55.92  ? 221 LYS B CB    1 
ATOM   3414 C  CG    . LYS B 1 221 ? 8.535   -11.287 -16.937 1.00 61.63  ? 221 LYS B CG    1 
ATOM   3415 C  CD    . LYS B 1 221 ? 7.712   -11.840 -18.092 1.00 65.04  ? 221 LYS B CD    1 
ATOM   3416 C  CE    . LYS B 1 221 ? 6.376   -12.405 -17.591 1.00 68.74  ? 221 LYS B CE    1 
ATOM   3417 N  NZ    . LYS B 1 221 ? 6.540   -13.575 -16.645 1.00 69.56  ? 221 LYS B NZ    1 
ATOM   3418 N  N     . ALA B 1 222 ? 12.653  -9.778  -17.672 1.00 52.37  ? 222 ALA B N     1 
ATOM   3419 C  CA    . ALA B 1 222 ? 14.008  -9.779  -18.206 1.00 51.48  ? 222 ALA B CA    1 
ATOM   3420 C  C     . ALA B 1 222 ? 15.053  -9.645  -17.100 1.00 52.03  ? 222 ALA B C     1 
ATOM   3421 O  O     . ALA B 1 222 ? 15.972  -10.459 -16.986 1.00 52.24  ? 222 ALA B O     1 
ATOM   3422 C  CB    . ALA B 1 222 ? 14.161  -8.639  -19.208 1.00 49.90  ? 222 ALA B CB    1 
ATOM   3423 N  N     . LEU B 1 223 ? 14.899  -8.604  -16.291 1.00 51.60  ? 223 LEU B N     1 
ATOM   3424 C  CA    . LEU B 1 223 ? 15.809  -8.323  -15.198 1.00 51.19  ? 223 LEU B CA    1 
ATOM   3425 C  C     . LEU B 1 223 ? 15.833  -9.440  -14.164 1.00 51.45  ? 223 LEU B C     1 
ATOM   3426 O  O     . LEU B 1 223 ? 16.894  -9.804  -13.665 1.00 53.12  ? 223 LEU B O     1 
ATOM   3427 C  CB    . LEU B 1 223 ? 15.395  -7.011  -14.531 1.00 50.36  ? 223 LEU B CB    1 
ATOM   3428 C  CG    . LEU B 1 223 ? 16.315  -5.793  -14.538 1.00 47.83  ? 223 LEU B CG    1 
ATOM   3429 C  CD1   . LEU B 1 223 ? 17.191  -5.713  -15.773 1.00 44.81  ? 223 LEU B CD1   1 
ATOM   3430 C  CD2   . LEU B 1 223 ? 15.417  -4.597  -14.419 1.00 47.23  ? 223 LEU B CD2   1 
ATOM   3431 N  N     . ALA B 1 224 ? 14.663  -9.981  -13.846 1.00 51.46  ? 224 ALA B N     1 
ATOM   3432 C  CA    . ALA B 1 224 ? 14.547  -11.051 -12.856 1.00 50.91  ? 224 ALA B CA    1 
ATOM   3433 C  C     . ALA B 1 224 ? 15.309  -12.298 -13.256 1.00 50.54  ? 224 ALA B C     1 
ATOM   3434 O  O     . ALA B 1 224 ? 15.746  -13.068 -12.412 1.00 51.15  ? 224 ALA B O     1 
ATOM   3435 C  CB    . ALA B 1 224 ? 13.094  -11.400 -12.646 1.00 50.91  ? 224 ALA B CB    1 
ATOM   3436 N  N     . VAL B 1 225 ? 15.474  -12.488 -14.553 1.00 50.84  ? 225 VAL B N     1 
ATOM   3437 C  CA    . VAL B 1 225 ? 16.161  -13.658 -15.063 1.00 51.12  ? 225 VAL B CA    1 
ATOM   3438 C  C     . VAL B 1 225 ? 17.629  -13.424 -15.446 1.00 51.46  ? 225 VAL B C     1 
ATOM   3439 O  O     . VAL B 1 225 ? 18.363  -14.383 -15.682 1.00 51.76  ? 225 VAL B O     1 
ATOM   3440 C  CB    . VAL B 1 225 ? 15.377  -14.210 -16.278 1.00 51.02  ? 225 VAL B CB    1 
ATOM   3441 C  CG1   . VAL B 1 225 ? 16.186  -15.232 -17.007 1.00 53.22  ? 225 VAL B CG1   1 
ATOM   3442 C  CG2   . VAL B 1 225 ? 14.076  -14.843 -15.812 1.00 50.51  ? 225 VAL B CG2   1 
ATOM   3443 N  N     . ASP B 1 226 ? 18.070  -12.167 -15.479 1.00 51.53  ? 226 ASP B N     1 
ATOM   3444 C  CA    . ASP B 1 226 ? 19.445  -11.857 -15.875 1.00 52.33  ? 226 ASP B CA    1 
ATOM   3445 C  C     . ASP B 1 226 ? 20.526  -12.503 -15.013 1.00 52.31  ? 226 ASP B C     1 
ATOM   3446 O  O     . ASP B 1 226 ? 20.625  -12.247 -13.823 1.00 52.71  ? 226 ASP B O     1 
ATOM   3447 C  CB    . ASP B 1 226 ? 19.670  -10.343 -15.901 1.00 54.31  ? 226 ASP B CB    1 
ATOM   3448 C  CG    . ASP B 1 226 ? 20.907  -9.934  -16.727 1.00 56.46  ? 226 ASP B CG    1 
ATOM   3449 O  OD1   . ASP B 1 226 ? 21.998  -10.532 -16.553 1.00 55.37  ? 226 ASP B OD1   1 
ATOM   3450 O  OD2   . ASP B 1 226 ? 20.784  -8.992  -17.549 1.00 57.90  ? 226 ASP B OD2   1 
ATOM   3451 N  N     . PRO B 1 227 ? 21.377  -13.331 -15.627 1.00 52.97  ? 227 PRO B N     1 
ATOM   3452 C  CA    . PRO B 1 227 ? 22.474  -14.040 -14.964 1.00 53.70  ? 227 PRO B CA    1 
ATOM   3453 C  C     . PRO B 1 227 ? 23.531  -13.118 -14.369 1.00 54.92  ? 227 PRO B C     1 
ATOM   3454 O  O     . PRO B 1 227 ? 24.167  -13.446 -13.371 1.00 56.98  ? 227 PRO B O     1 
ATOM   3455 C  CB    . PRO B 1 227 ? 23.084  -14.867 -16.091 1.00 53.31  ? 227 PRO B CB    1 
ATOM   3456 C  CG    . PRO B 1 227 ? 21.984  -14.981 -17.094 1.00 52.65  ? 227 PRO B CG    1 
ATOM   3457 C  CD    . PRO B 1 227 ? 21.343  -13.650 -17.064 1.00 52.59  ? 227 PRO B CD    1 
ATOM   3458 N  N     . ARG B 1 228 ? 23.705  -11.962 -14.994 1.00 55.74  ? 228 ARG B N     1 
ATOM   3459 C  CA    . ARG B 1 228 ? 24.740  -11.012 -14.615 1.00 56.79  ? 228 ARG B CA    1 
ATOM   3460 C  C     . ARG B 1 228 ? 24.482  -10.057 -13.454 1.00 56.94  ? 228 ARG B C     1 
ATOM   3461 O  O     . ARG B 1 228 ? 25.393  -9.324  -13.034 1.00 55.45  ? 228 ARG B O     1 
ATOM   3462 C  CB    . ARG B 1 228 ? 25.128  -10.223 -15.869 1.00 57.75  ? 228 ARG B CB    1 
ATOM   3463 C  CG    . ARG B 1 228 ? 25.308  -11.131 -17.095 1.00 61.34  ? 228 ARG B CG    1 
ATOM   3464 C  CD    . ARG B 1 228 ? 25.788  -10.392 -18.338 1.00 63.85  ? 228 ARG B CD    1 
ATOM   3465 N  NE    . ARG B 1 228 ? 26.978  -9.595  -18.044 1.00 67.45  ? 228 ARG B NE    1 
ATOM   3466 C  CZ    . ARG B 1 228 ? 27.744  -9.007  -18.960 1.00 67.98  ? 228 ARG B CZ    1 
ATOM   3467 N  NH1   . ARG B 1 228 ? 27.456  -9.129  -20.252 1.00 69.11  ? 228 ARG B NH1   1 
ATOM   3468 N  NH2   . ARG B 1 228 ? 28.785  -8.276  -18.575 1.00 66.72  ? 228 ARG B NH2   1 
ATOM   3469 N  N     . ILE B 1 229 ? 23.272  -10.084 -12.904 1.00 56.86  ? 229 ILE B N     1 
ATOM   3470 C  CA    . ILE B 1 229 ? 22.938  -9.167  -11.822 1.00 57.20  ? 229 ILE B CA    1 
ATOM   3471 C  C     . ILE B 1 229 ? 22.229  -9.837  -10.658 1.00 57.92  ? 229 ILE B C     1 
ATOM   3472 O  O     . ILE B 1 229 ? 22.000  -11.046 -10.678 1.00 59.14  ? 229 ILE B O     1 
ATOM   3473 C  CB    . ILE B 1 229 ? 22.036  -8.044  -12.351 1.00 56.73  ? 229 ILE B CB    1 
ATOM   3474 C  CG1   . ILE B 1 229 ? 20.770  -8.656  -12.965 1.00 56.86  ? 229 ILE B CG1   1 
ATOM   3475 C  CG2   . ILE B 1 229 ? 22.785  -7.221  -13.384 1.00 55.29  ? 229 ILE B CG2   1 
ATOM   3476 C  CD1   . ILE B 1 229 ? 19.769  -7.646  -13.506 1.00 57.07  ? 229 ILE B CD1   1 
ATOM   3477 N  N     . GLU B 1 230 ? 21.870  -9.041  -9.650  1.00 57.61  ? 230 GLU B N     1 
ATOM   3478 C  CA    . GLU B 1 230 ? 21.165  -9.555  -8.483  1.00 58.03  ? 230 GLU B CA    1 
ATOM   3479 C  C     . GLU B 1 230 ? 19.708  -9.080  -8.381  1.00 56.80  ? 230 GLU B C     1 
ATOM   3480 O  O     . GLU B 1 230 ? 18.777  -9.888  -8.389  1.00 59.69  ? 230 GLU B O     1 
ATOM   3481 C  CB    . GLU B 1 230 ? 21.913  -9.186  -7.213  1.00 61.14  ? 230 GLU B CB    1 
ATOM   3482 C  CG    . GLU B 1 230 ? 23.122  -10.080 -6.919  1.00 65.64  ? 230 GLU B CG    1 
ATOM   3483 C  CD    . GLU B 1 230 ? 22.751  -11.538 -6.687  1.00 68.34  ? 230 GLU B CD    1 
ATOM   3484 O  OE1   . GLU B 1 230 ? 21.750  -11.812 -5.981  1.00 70.30  ? 230 GLU B OE1   1 
ATOM   3485 O  OE2   . GLU B 1 230 ? 23.472  -12.416 -7.200  1.00 69.79  ? 230 GLU B OE2   1 
ATOM   3486 N  N     . ILE B 1 231 ? 19.515  -7.776  -8.278  1.00 52.83  ? 231 ILE B N     1 
ATOM   3487 C  CA    . ILE B 1 231 ? 18.182  -7.156  -8.188  1.00 49.27  ? 231 ILE B CA    1 
ATOM   3488 C  C     . ILE B 1 231 ? 17.368  -7.275  -6.903  1.00 47.50  ? 231 ILE B C     1 
ATOM   3489 O  O     . ILE B 1 231 ? 17.251  -8.324  -6.272  1.00 46.58  ? 231 ILE B O     1 
ATOM   3490 C  CB    . ILE B 1 231 ? 17.231  -7.539  -9.369  1.00 45.71  ? 231 ILE B CB    1 
ATOM   3491 C  CG1   . ILE B 1 231 ? 16.404  -8.768  -9.021  1.00 44.68  ? 231 ILE B CG1   1 
ATOM   3492 C  CG2   . ILE B 1 231 ? 18.025  -7.729  -10.635 1.00 47.59  ? 231 ILE B CG2   1 
ATOM   3493 C  CD1   . ILE B 1 231 ? 15.310  -9.071  -10.019 1.00 43.17  ? 231 ILE B CD1   1 
ATOM   3494 N  N     . CYS B 1 232 ? 16.802  -6.135  -6.546  1.00 46.52  ? 232 CYS B N     1 
ATOM   3495 C  CA    . CYS B 1 232 ? 15.983  -5.983  -5.380  1.00 46.20  ? 232 CYS B CA    1 
ATOM   3496 C  C     . CYS B 1 232 ? 14.986  -4.893  -5.750  1.00 46.20  ? 232 CYS B C     1 
ATOM   3497 O  O     . CYS B 1 232 ? 15.385  -3.754  -5.988  1.00 45.17  ? 232 CYS B O     1 
ATOM   3498 C  CB    . CYS B 1 232 ? 16.856  -5.543  -4.218  1.00 46.12  ? 232 CYS B CB    1 
ATOM   3499 S  SG    . CYS B 1 232 ? 15.932  -5.022  -2.803  1.00 51.09  ? 232 CYS B SG    1 
ATOM   3500 N  N     . MET B 1 233 ? 13.700  -5.258  -5.833  1.00 47.03  ? 233 MET B N     1 
ATOM   3501 C  CA    . MET B 1 233 ? 12.626  -4.321  -6.174  1.00 46.11  ? 233 MET B CA    1 
ATOM   3502 C  C     . MET B 1 233 ? 12.134  -3.648  -4.917  1.00 46.15  ? 233 MET B C     1 
ATOM   3503 O  O     . MET B 1 233 ? 11.580  -4.288  -4.028  1.00 47.61  ? 233 MET B O     1 
ATOM   3504 C  CB    . MET B 1 233 ? 11.458  -5.041  -6.820  1.00 46.31  ? 233 MET B CB    1 
ATOM   3505 C  CG    . MET B 1 233 ? 11.784  -5.695  -8.125  1.00 50.13  ? 233 MET B CG    1 
ATOM   3506 S  SD    . MET B 1 233 ? 10.300  -6.448  -8.822  1.00 57.71  ? 233 MET B SD    1 
ATOM   3507 C  CE    . MET B 1 233 ? 9.509   -5.004  -9.561  1.00 53.53  ? 233 MET B CE    1 
ATOM   3508 N  N     . LEU B 1 234 ? 12.334  -2.345  -4.836  1.00 46.33  ? 234 LEU B N     1 
ATOM   3509 C  CA    . LEU B 1 234 ? 11.920  -1.616  -3.659  1.00 46.26  ? 234 LEU B CA    1 
ATOM   3510 C  C     . LEU B 1 234 ? 10.688  -0.784  -3.888  1.00 46.09  ? 234 LEU B C     1 
ATOM   3511 O  O     . LEU B 1 234 ? 10.588  -0.064  -4.870  1.00 46.59  ? 234 LEU B O     1 
ATOM   3512 C  CB    . LEU B 1 234 ? 13.038  -0.699  -3.200  1.00 46.64  ? 234 LEU B CB    1 
ATOM   3513 C  CG    . LEU B 1 234 ? 14.257  -1.415  -2.660  1.00 48.51  ? 234 LEU B CG    1 
ATOM   3514 C  CD1   . LEU B 1 234 ? 15.458  -0.521  -2.823  1.00 49.52  ? 234 LEU B CD1   1 
ATOM   3515 C  CD2   . LEU B 1 234 ? 14.029  -1.783  -1.202  1.00 49.43  ? 234 LEU B CD2   1 
ATOM   3516 N  N     . PRO B 1 235 ? 9.713   -0.897  -2.990  1.00 46.38  ? 235 PRO B N     1 
ATOM   3517 C  CA    . PRO B 1 235 ? 8.505   -0.100  -3.146  1.00 46.93  ? 235 PRO B CA    1 
ATOM   3518 C  C     . PRO B 1 235 ? 8.762   1.353   -2.678  1.00 46.26  ? 235 PRO B C     1 
ATOM   3519 O  O     . PRO B 1 235 ? 8.067   1.902   -1.827  1.00 47.08  ? 235 PRO B O     1 
ATOM   3520 C  CB    . PRO B 1 235 ? 7.488   -0.862  -2.297  1.00 46.82  ? 235 PRO B CB    1 
ATOM   3521 C  CG    . PRO B 1 235 ? 8.324   -1.465  -1.237  1.00 46.51  ? 235 PRO B CG    1 
ATOM   3522 C  CD    . PRO B 1 235 ? 9.491   -1.986  -2.030  1.00 46.88  ? 235 PRO B CD    1 
ATOM   3523 N  N     . VAL B 1 236 ? 9.797   1.962   -3.229  1.00 45.83  ? 236 VAL B N     1 
ATOM   3524 C  CA    . VAL B 1 236 ? 10.105  3.341   -2.905  1.00 46.77  ? 236 VAL B CA    1 
ATOM   3525 C  C     . VAL B 1 236 ? 9.636   4.187   -4.088  1.00 47.50  ? 236 VAL B C     1 
ATOM   3526 O  O     . VAL B 1 236 ? 9.872   3.828   -5.252  1.00 48.06  ? 236 VAL B O     1 
ATOM   3527 C  CB    . VAL B 1 236 ? 11.613  3.539   -2.680  1.00 45.95  ? 236 VAL B CB    1 
ATOM   3528 C  CG1   . VAL B 1 236 ? 12.066  4.892   -3.226  1.00 44.31  ? 236 VAL B CG1   1 
ATOM   3529 C  CG2   . VAL B 1 236 ? 11.906  3.453   -1.204  1.00 44.65  ? 236 VAL B CG2   1 
ATOM   3530 N  N     . GLY B 1 237 ? 8.976   5.306   -3.802  1.00 46.35  ? 237 GLY B N     1 
ATOM   3531 C  CA    . GLY B 1 237 ? 8.484   6.138   -4.889  1.00 45.62  ? 237 GLY B CA    1 
ATOM   3532 C  C     . GLY B 1 237 ? 7.522   5.314   -5.717  1.00 44.17  ? 237 GLY B C     1 
ATOM   3533 O  O     . GLY B 1 237 ? 6.591   4.730   -5.167  1.00 45.73  ? 237 GLY B O     1 
ATOM   3534 N  N     . ASP B 1 238 ? 7.727   5.243   -7.023  1.00 43.82  ? 238 ASP B N     1 
ATOM   3535 C  CA    . ASP B 1 238 ? 6.836   4.430   -7.840  1.00 45.28  ? 238 ASP B CA    1 
ATOM   3536 C  C     . ASP B 1 238 ? 7.502   3.096   -8.181  1.00 44.27  ? 238 ASP B C     1 
ATOM   3537 O  O     . ASP B 1 238 ? 7.211   2.471   -9.195  1.00 43.80  ? 238 ASP B O     1 
ATOM   3538 C  CB    . ASP B 1 238 ? 6.436   5.192   -9.107  1.00 49.31  ? 238 ASP B CB    1 
ATOM   3539 C  CG    . ASP B 1 238 ? 5.297   4.512   -9.874  1.00 53.90  ? 238 ASP B CG    1 
ATOM   3540 O  OD1   . ASP B 1 238 ? 4.312   4.081   -9.231  1.00 55.77  ? 238 ASP B OD1   1 
ATOM   3541 O  OD2   . ASP B 1 238 ? 5.381   4.419   -11.124 1.00 56.77  ? 238 ASP B OD2   1 
ATOM   3542 N  N     . GLY B 1 239 ? 8.404   2.658   -7.310  1.00 44.56  ? 239 GLY B N     1 
ATOM   3543 C  CA    . GLY B 1 239 ? 9.092   1.402   -7.534  1.00 43.27  ? 239 GLY B CA    1 
ATOM   3544 C  C     . GLY B 1 239 ? 10.458  1.557   -8.169  1.00 43.30  ? 239 GLY B C     1 
ATOM   3545 O  O     . GLY B 1 239 ? 10.586  2.039   -9.307  1.00 43.61  ? 239 GLY B O     1 
ATOM   3546 N  N     . ILE B 1 240 ? 11.488  1.151   -7.435  1.00 41.45  ? 240 ILE B N     1 
ATOM   3547 C  CA    . ILE B 1 240 ? 12.844  1.232   -7.943  1.00 41.82  ? 240 ILE B CA    1 
ATOM   3548 C  C     . ILE B 1 240 ? 13.502  -0.143  -7.864  1.00 43.61  ? 240 ILE B C     1 
ATOM   3549 O  O     . ILE B 1 240 ? 13.457  -0.806  -6.821  1.00 43.75  ? 240 ILE B O     1 
ATOM   3550 C  CB    . ILE B 1 240 ? 13.670  2.257   -7.141  1.00 40.95  ? 240 ILE B CB    1 
ATOM   3551 C  CG1   . ILE B 1 240 ? 12.985  3.619   -7.214  1.00 41.89  ? 240 ILE B CG1   1 
ATOM   3552 C  CG2   . ILE B 1 240 ? 15.080  2.360   -7.701  1.00 37.80  ? 240 ILE B CG2   1 
ATOM   3553 C  CD1   . ILE B 1 240 ? 13.572  4.647   -6.300  1.00 44.14  ? 240 ILE B CD1   1 
ATOM   3554 N  N     . THR B 1 241 ? 14.092  -0.584  -8.975  1.00 43.37  ? 241 THR B N     1 
ATOM   3555 C  CA    . THR B 1 241 ? 14.770  -1.875  -9.005  1.00 41.91  ? 241 THR B CA    1 
ATOM   3556 C  C     . THR B 1 241 ? 16.287  -1.682  -8.998  1.00 42.22  ? 241 THR B C     1 
ATOM   3557 O  O     . THR B 1 241 ? 16.881  -1.278  -9.992  1.00 42.34  ? 241 THR B O     1 
ATOM   3558 C  CB    . THR B 1 241 ? 14.376  -2.679  -10.250 1.00 41.56  ? 241 THR B CB    1 
ATOM   3559 O  OG1   . THR B 1 241 ? 12.985  -2.994  -10.187 1.00 42.22  ? 241 THR B OG1   1 
ATOM   3560 C  CG2   . THR B 1 241 ? 15.178  -3.971  -10.338 1.00 40.63  ? 241 THR B CG2   1 
ATOM   3561 N  N     . ILE B 1 242 ? 16.906  -1.958  -7.861  1.00 41.94  ? 242 ILE B N     1 
ATOM   3562 C  CA    . ILE B 1 242 ? 18.344  -1.840  -7.731  1.00 41.20  ? 242 ILE B CA    1 
ATOM   3563 C  C     . ILE B 1 242 ? 18.973  -3.094  -8.316  1.00 41.78  ? 242 ILE B C     1 
ATOM   3564 O  O     . ILE B 1 242 ? 18.545  -4.184  -7.997  1.00 40.66  ? 242 ILE B O     1 
ATOM   3565 C  CB    . ILE B 1 242 ? 18.738  -1.736  -6.261  1.00 40.44  ? 242 ILE B CB    1 
ATOM   3566 C  CG1   . ILE B 1 242 ? 18.215  -0.432  -5.681  1.00 40.84  ? 242 ILE B CG1   1 
ATOM   3567 C  CG2   . ILE B 1 242 ? 20.226  -1.825  -6.122  1.00 41.42  ? 242 ILE B CG2   1 
ATOM   3568 C  CD1   . ILE B 1 242 ? 18.678  0.778   -6.433  1.00 41.16  ? 242 ILE B CD1   1 
ATOM   3569 N  N     . CYS B 1 243 ? 19.980  -2.940  -9.168  1.00 43.95  ? 243 CYS B N     1 
ATOM   3570 C  CA    . CYS B 1 243 ? 20.662  -4.087  -9.777  1.00 45.86  ? 243 CYS B CA    1 
ATOM   3571 C  C     . CYS B 1 243 ? 22.139  -4.020  -9.451  1.00 48.51  ? 243 CYS B C     1 
ATOM   3572 O  O     . CYS B 1 243 ? 22.756  -2.975  -9.663  1.00 48.72  ? 243 CYS B O     1 
ATOM   3573 C  CB    . CYS B 1 243 ? 20.551  -4.057  -11.298 1.00 44.54  ? 243 CYS B CB    1 
ATOM   3574 S  SG    . CYS B 1 243 ? 18.907  -3.944  -11.965 1.00 46.37  ? 243 CYS B SG    1 
ATOM   3575 N  N     . ARG B 1 244 ? 22.705  -5.120  -8.946  1.00 51.27  ? 244 ARG B N     1 
ATOM   3576 C  CA    . ARG B 1 244 ? 24.141  -5.187  -8.629  1.00 52.11  ? 244 ARG B CA    1 
ATOM   3577 C  C     . ARG B 1 244 ? 24.770  -6.089  -9.677  1.00 53.49  ? 244 ARG B C     1 
ATOM   3578 O  O     . ARG B 1 244 ? 24.294  -7.202  -9.885  1.00 55.09  ? 244 ARG B O     1 
ATOM   3579 C  CB    . ARG B 1 244 ? 24.376  -5.790  -7.242  1.00 50.99  ? 244 ARG B CB    1 
ATOM   3580 C  CG    . ARG B 1 244 ? 25.835  -5.765  -6.818  1.00 52.26  ? 244 ARG B CG    1 
ATOM   3581 C  CD    . ARG B 1 244 ? 26.085  -6.360  -5.418  1.00 54.41  ? 244 ARG B CD    1 
ATOM   3582 N  NE    . ARG B 1 244 ? 26.180  -7.822  -5.409  1.00 55.03  ? 244 ARG B NE    1 
ATOM   3583 C  CZ    . ARG B 1 244 ? 25.209  -8.635  -4.998  1.00 55.67  ? 244 ARG B CZ    1 
ATOM   3584 N  NH1   . ARG B 1 244 ? 24.070  -8.123  -4.552  1.00 56.07  ? 244 ARG B NH1   1 
ATOM   3585 N  NH2   . ARG B 1 244 ? 25.359  -9.958  -5.053  1.00 55.47  ? 244 ARG B NH2   1 
ATOM   3586 N  N     . ARG B 1 245 ? 25.815  -5.620  -10.357 1.00 55.28  ? 245 ARG B N     1 
ATOM   3587 C  CA    . ARG B 1 245 ? 26.467  -6.441  -11.384 1.00 56.65  ? 245 ARG B CA    1 
ATOM   3588 C  C     . ARG B 1 245 ? 27.369  -7.519  -10.781 1.00 57.54  ? 245 ARG B C     1 
ATOM   3589 O  O     . ARG B 1 245 ? 28.287  -7.198  -10.023 1.00 56.69  ? 245 ARG B O     1 
ATOM   3590 C  CB    . ARG B 1 245 ? 27.313  -5.585  -12.304 1.00 56.98  ? 245 ARG B CB    1 
ATOM   3591 C  CG    . ARG B 1 245 ? 27.994  -6.429  -13.329 1.00 60.14  ? 245 ARG B CG    1 
ATOM   3592 C  CD    . ARG B 1 245 ? 28.987  -5.682  -14.171 1.00 63.15  ? 245 ARG B CD    1 
ATOM   3593 N  NE    . ARG B 1 245 ? 29.479  -6.558  -15.230 1.00 65.16  ? 245 ARG B NE    1 
ATOM   3594 C  CZ    . ARG B 1 245 ? 30.470  -6.260  -16.057 1.00 64.25  ? 245 ARG B CZ    1 
ATOM   3595 N  NH1   . ARG B 1 245 ? 31.092  -5.099  -15.960 1.00 63.97  ? 245 ARG B NH1   1 
ATOM   3596 N  NH2   . ARG B 1 245 ? 30.839  -7.135  -16.976 1.00 65.53  ? 245 ARG B NH2   1 
ATOM   3597 N  N     . ILE B 1 246 ? 27.132  -8.788  -11.126 1.00 58.20  ? 246 ILE B N     1 
ATOM   3598 C  CA    . ILE B 1 246 ? 27.951  -9.859  -10.557 1.00 59.76  ? 246 ILE B CA    1 
ATOM   3599 C  C     . ILE B 1 246 ? 29.075  -10.356 -11.453 1.00 61.40  ? 246 ILE B C     1 
ATOM   3600 O  O     . ILE B 1 246 ? 30.096  -10.813 -10.948 1.00 61.20  ? 246 ILE B O     1 
ATOM   3601 C  CB    . ILE B 1 246 ? 27.090  -11.071 -10.058 1.00 58.78  ? 246 ILE B CB    1 
ATOM   3602 C  CG1   . ILE B 1 246 ? 26.101  -11.528 -11.134 1.00 58.72  ? 246 ILE B CG1   1 
ATOM   3603 C  CG2   . ILE B 1 246 ? 26.355  -10.683 -8.785  1.00 56.85  ? 246 ILE B CG2   1 
ATOM   3604 C  CD1   . ILE B 1 246 ? 25.257  -12.737 -10.732 1.00 54.55  ? 246 ILE B CD1   1 
ATOM   3605 N  N     . LYS B 1 247 ? 28.896  -10.278 -12.769 1.00 63.62  ? 247 LYS B N     1 
ATOM   3606 C  CA    . LYS B 1 247 ? 29.952  -10.675 -13.701 1.00 67.02  ? 247 LYS B CA    1 
ATOM   3607 C  C     . LYS B 1 247 ? 29.722  -10.119 -15.099 1.00 68.94  ? 247 LYS B C     1 
ATOM   3608 O  O     . LYS B 1 247 ? 28.641  -9.537  -15.327 1.00 70.20  ? 247 LYS B O     1 
ATOM   3609 C  CB    . LYS B 1 247 ? 30.112  -12.199 -13.767 1.00 67.67  ? 247 LYS B CB    1 
ATOM   3610 C  CG    . LYS B 1 247 ? 28.859  -12.986 -14.108 1.00 71.06  ? 247 LYS B CG    1 
ATOM   3611 C  CD    . LYS B 1 247 ? 29.112  -14.482 -13.887 1.00 72.87  ? 247 LYS B CD    1 
ATOM   3612 C  CE    . LYS B 1 247 ? 27.819  -15.289 -13.720 1.00 74.00  ? 247 LYS B CE    1 
ATOM   3613 N  NZ    . LYS B 1 247 ? 27.064  -15.518 -14.993 1.00 74.33  ? 247 LYS B NZ    1 
ATOM   3614 O  OXT   . LYS B 1 247 ? 30.631  -10.262 -15.949 1.00 71.06  ? 247 LYS B OXT   1 
ATOM   3615 N  N     . LYS C 1 21  ? 15.526  52.982  47.455  1.00 88.65  ? 21  LYS C N     1 
ATOM   3616 C  CA    . LYS C 1 21  ? 16.730  52.248  46.978  1.00 88.98  ? 21  LYS C CA    1 
ATOM   3617 C  C     . LYS C 1 21  ? 16.386  50.817  46.557  1.00 89.04  ? 21  LYS C C     1 
ATOM   3618 O  O     . LYS C 1 21  ? 15.609  50.124  47.223  1.00 89.57  ? 21  LYS C O     1 
ATOM   3619 C  CB    . LYS C 1 21  ? 17.809  52.228  48.072  1.00 88.44  ? 21  LYS C CB    1 
ATOM   3620 C  CG    . LYS C 1 21  ? 19.071  51.442  47.702  1.00 89.14  ? 21  LYS C CG    1 
ATOM   3621 C  CD    . LYS C 1 21  ? 20.115  51.479  48.821  1.00 88.72  ? 21  LYS C CD    1 
ATOM   3622 C  CE    . LYS C 1 21  ? 21.238  50.455  48.613  1.00 88.52  ? 21  LYS C CE    1 
ATOM   3623 N  NZ    . LYS C 1 21  ? 22.137  50.729  47.451  1.00 86.58  ? 21  LYS C NZ    1 
ATOM   3624 N  N     . SER C 1 22  ? 16.968  50.391  45.438  1.00 87.94  ? 22  SER C N     1 
ATOM   3625 C  CA    . SER C 1 22  ? 16.753  49.048  44.910  1.00 85.66  ? 22  SER C CA    1 
ATOM   3626 C  C     . SER C 1 22  ? 18.054  48.267  45.007  1.00 83.87  ? 22  SER C C     1 
ATOM   3627 O  O     . SER C 1 22  ? 18.925  48.591  45.824  1.00 84.88  ? 22  SER C O     1 
ATOM   3628 C  CB    . SER C 1 22  ? 16.304  49.098  43.449  1.00 86.08  ? 22  SER C CB    1 
ATOM   3629 O  OG    . SER C 1 22  ? 17.344  49.590  42.623  1.00 85.54  ? 22  SER C OG    1 
ATOM   3630 N  N     . LEU C 1 23  ? 18.183  47.249  44.160  1.00 80.21  ? 23  LEU C N     1 
ATOM   3631 C  CA    . LEU C 1 23  ? 19.362  46.395  44.152  1.00 76.90  ? 23  LEU C CA    1 
ATOM   3632 C  C     . LEU C 1 23  ? 20.375  46.818  43.104  1.00 74.95  ? 23  LEU C C     1 
ATOM   3633 O  O     . LEU C 1 23  ? 21.521  46.379  43.131  1.00 74.33  ? 23  LEU C O     1 
ATOM   3634 C  CB    . LEU C 1 23  ? 18.944  44.941  43.908  1.00 76.94  ? 23  LEU C CB    1 
ATOM   3635 C  CG    . LEU C 1 23  ? 18.163  44.253  45.040  1.00 77.05  ? 23  LEU C CG    1 
ATOM   3636 C  CD1   . LEU C 1 23  ? 17.555  42.944  44.552  1.00 76.12  ? 23  LEU C CD1   1 
ATOM   3637 C  CD2   . LEU C 1 23  ? 19.091  44.014  46.225  1.00 76.12  ? 23  LEU C CD2   1 
ATOM   3638 N  N     . LEU C 1 24  ? 19.947  47.681  42.189  1.00 73.09  ? 24  LEU C N     1 
ATOM   3639 C  CA    . LEU C 1 24  ? 20.805  48.155  41.117  1.00 70.38  ? 24  LEU C CA    1 
ATOM   3640 C  C     . LEU C 1 24  ? 21.847  49.115  41.660  1.00 71.26  ? 24  LEU C C     1 
ATOM   3641 O  O     . LEU C 1 24  ? 21.799  49.490  42.828  1.00 70.88  ? 24  LEU C O     1 
ATOM   3642 C  CB    . LEU C 1 24  ? 19.962  48.835  40.045  1.00 66.63  ? 24  LEU C CB    1 
ATOM   3643 C  CG    . LEU C 1 24  ? 18.783  47.986  39.573  1.00 63.93  ? 24  LEU C CG    1 
ATOM   3644 C  CD1   . LEU C 1 24  ? 18.036  48.714  38.484  1.00 64.01  ? 24  LEU C CD1   1 
ATOM   3645 C  CD2   . LEU C 1 24  ? 19.273  46.651  39.079  1.00 63.12  ? 24  LEU C CD2   1 
ATOM   3646 N  N     . GLN C 1 25  ? 22.784  49.504  40.800  1.00 72.36  ? 25  GLN C N     1 
ATOM   3647 C  CA    . GLN C 1 25  ? 23.873  50.410  41.159  1.00 73.48  ? 25  GLN C CA    1 
ATOM   3648 C  C     . GLN C 1 25  ? 23.450  51.745  41.737  1.00 73.71  ? 25  GLN C C     1 
ATOM   3649 O  O     . GLN C 1 25  ? 23.989  52.192  42.745  1.00 73.99  ? 25  GLN C O     1 
ATOM   3650 C  CB    . GLN C 1 25  ? 24.724  50.736  39.944  1.00 74.38  ? 25  GLN C CB    1 
ATOM   3651 C  CG    . GLN C 1 25  ? 25.232  49.574  39.157  1.00 75.17  ? 25  GLN C CG    1 
ATOM   3652 C  CD    . GLN C 1 25  ? 26.118  50.047  38.032  1.00 75.23  ? 25  GLN C CD    1 
ATOM   3653 O  OE1   . GLN C 1 25  ? 25.792  51.022  37.343  1.00 74.15  ? 25  GLN C OE1   1 
ATOM   3654 N  NE2   . GLN C 1 25  ? 27.245  49.365  37.832  1.00 75.57  ? 25  GLN C NE2   1 
ATOM   3655 N  N     . SER C 1 26  ? 22.526  52.405  41.052  1.00 73.82  ? 26  SER C N     1 
ATOM   3656 C  CA    . SER C 1 26  ? 22.057  53.706  41.487  1.00 75.17  ? 26  SER C CA    1 
ATOM   3657 C  C     . SER C 1 26  ? 20.549  53.722  41.529  1.00 75.53  ? 26  SER C C     1 
ATOM   3658 O  O     . SER C 1 26  ? 19.895  52.758  41.144  1.00 75.61  ? 26  SER C O     1 
ATOM   3659 C  CB    . SER C 1 26  ? 22.521  54.798  40.518  1.00 75.64  ? 26  SER C CB    1 
ATOM   3660 O  OG    . SER C 1 26  ? 21.670  54.860  39.381  1.00 76.63  ? 26  SER C OG    1 
ATOM   3661 N  N     . ASP C 1 27  ? 20.003  54.839  41.987  1.00 75.82  ? 27  ASP C N     1 
ATOM   3662 C  CA    . ASP C 1 27  ? 18.568  54.997  42.056  1.00 76.22  ? 27  ASP C CA    1 
ATOM   3663 C  C     . ASP C 1 27  ? 18.082  55.506  40.708  1.00 75.38  ? 27  ASP C C     1 
ATOM   3664 O  O     . ASP C 1 27  ? 16.936  55.270  40.306  1.00 74.96  ? 27  ASP C O     1 
ATOM   3665 C  CB    . ASP C 1 27  ? 18.217  56.001  43.143  1.00 79.23  ? 27  ASP C CB    1 
ATOM   3666 C  CG    . ASP C 1 27  ? 17.473  55.370  44.282  1.00 81.19  ? 27  ASP C CG    1 
ATOM   3667 O  OD1   . ASP C 1 27  ? 16.317  54.927  44.066  1.00 81.50  ? 27  ASP C OD1   1 
ATOM   3668 O  OD2   . ASP C 1 27  ? 18.056  55.313  45.386  1.00 83.81  ? 27  ASP C OD2   1 
ATOM   3669 N  N     . ALA C 1 28  ? 18.974  56.217  40.022  1.00 73.36  ? 28  ALA C N     1 
ATOM   3670 C  CA    . ALA C 1 28  ? 18.672  56.783  38.720  1.00 70.69  ? 28  ALA C CA    1 
ATOM   3671 C  C     . ALA C 1 28  ? 18.582  55.658  37.711  1.00 68.80  ? 28  ALA C C     1 
ATOM   3672 O  O     . ALA C 1 28  ? 17.716  55.664  36.835  1.00 69.34  ? 28  ALA C O     1 
ATOM   3673 C  CB    . ALA C 1 28  ? 19.760  57.768  38.313  1.00 70.11  ? 28  ALA C CB    1 
ATOM   3674 N  N     . LEU C 1 29  ? 19.475  54.685  37.838  1.00 65.18  ? 29  LEU C N     1 
ATOM   3675 C  CA    . LEU C 1 29  ? 19.464  53.581  36.906  1.00 63.21  ? 29  LEU C CA    1 
ATOM   3676 C  C     . LEU C 1 29  ? 18.133  52.871  37.039  1.00 62.01  ? 29  LEU C C     1 
ATOM   3677 O  O     . LEU C 1 29  ? 17.506  52.504  36.049  1.00 61.52  ? 29  LEU C O     1 
ATOM   3678 C  CB    . LEU C 1 29  ? 20.621  52.630  37.197  1.00 61.90  ? 29  LEU C CB    1 
ATOM   3679 C  CG    . LEU C 1 29  ? 20.836  51.537  36.149  1.00 60.59  ? 29  LEU C CG    1 
ATOM   3680 C  CD1   . LEU C 1 29  ? 20.902  52.151  34.766  1.00 58.21  ? 29  LEU C CD1   1 
ATOM   3681 C  CD2   . LEU C 1 29  ? 22.107  50.777  36.466  1.00 59.27  ? 29  LEU C CD2   1 
ATOM   3682 N  N     . TYR C 1 30  ? 17.697  52.702  38.277  1.00 62.28  ? 30  TYR C N     1 
ATOM   3683 C  CA    . TYR C 1 30  ? 16.435  52.043  38.545  1.00 62.50  ? 30  TYR C CA    1 
ATOM   3684 C  C     . TYR C 1 30  ? 15.278  52.891  37.992  1.00 63.76  ? 30  TYR C C     1 
ATOM   3685 O  O     . TYR C 1 30  ? 14.316  52.373  37.411  1.00 64.74  ? 30  TYR C O     1 
ATOM   3686 C  CB    . TYR C 1 30  ? 16.284  51.825  40.048  1.00 62.46  ? 30  TYR C CB    1 
ATOM   3687 C  CG    . TYR C 1 30  ? 14.998  51.137  40.414  1.00 63.06  ? 30  TYR C CG    1 
ATOM   3688 C  CD1   . TYR C 1 30  ? 14.760  49.816  40.042  1.00 63.05  ? 30  TYR C CD1   1 
ATOM   3689 C  CD2   . TYR C 1 30  ? 13.982  51.833  41.062  1.00 62.42  ? 30  TYR C CD2   1 
ATOM   3690 C  CE1   . TYR C 1 30  ? 13.538  49.212  40.300  1.00 63.73  ? 30  TYR C CE1   1 
ATOM   3691 C  CE2   . TYR C 1 30  ? 12.766  51.240  41.321  1.00 62.51  ? 30  TYR C CE2   1 
ATOM   3692 C  CZ    . TYR C 1 30  ? 12.546  49.935  40.938  1.00 63.22  ? 30  TYR C CZ    1 
ATOM   3693 O  OH    . TYR C 1 30  ? 11.322  49.363  41.183  1.00 64.83  ? 30  TYR C OH    1 
ATOM   3694 N  N     . GLN C 1 31  ? 15.373  54.201  38.168  1.00 64.47  ? 31  GLN C N     1 
ATOM   3695 C  CA    . GLN C 1 31  ? 14.348  55.096  37.654  1.00 64.65  ? 31  GLN C CA    1 
ATOM   3696 C  C     . GLN C 1 31  ? 14.360  55.074  36.124  1.00 63.29  ? 31  GLN C C     1 
ATOM   3697 O  O     . GLN C 1 31  ? 13.304  55.034  35.488  1.00 63.07  ? 31  GLN C O     1 
ATOM   3698 C  CB    . GLN C 1 31  ? 14.588  56.518  38.167  1.00 67.76  ? 31  GLN C CB    1 
ATOM   3699 C  CG    . GLN C 1 31  ? 14.203  56.696  39.629  1.00 72.52  ? 31  GLN C CG    1 
ATOM   3700 C  CD    . GLN C 1 31  ? 12.698  56.554  39.859  1.00 74.57  ? 31  GLN C CD    1 
ATOM   3701 O  OE1   . GLN C 1 31  ? 12.262  56.053  40.903  1.00 75.78  ? 31  GLN C OE1   1 
ATOM   3702 N  NE2   . GLN C 1 31  ? 11.898  57.008  38.887  1.00 74.18  ? 31  GLN C NE2   1 
ATOM   3703 N  N     . TYR C 1 32  ? 15.555  55.090  35.538  1.00 60.44  ? 32  TYR C N     1 
ATOM   3704 C  CA    . TYR C 1 32  ? 15.679  55.059  34.089  1.00 57.84  ? 32  TYR C CA    1 
ATOM   3705 C  C     . TYR C 1 32  ? 14.899  53.868  33.559  1.00 56.53  ? 32  TYR C C     1 
ATOM   3706 O  O     . TYR C 1 32  ? 14.287  53.936  32.494  1.00 55.50  ? 32  TYR C O     1 
ATOM   3707 C  CB    . TYR C 1 32  ? 17.146  54.922  33.659  1.00 57.66  ? 32  TYR C CB    1 
ATOM   3708 C  CG    . TYR C 1 32  ? 17.298  54.864  32.156  1.00 56.90  ? 32  TYR C CG    1 
ATOM   3709 C  CD1   . TYR C 1 32  ? 17.196  56.016  31.392  1.00 56.17  ? 32  TYR C CD1   1 
ATOM   3710 C  CD2   . TYR C 1 32  ? 17.448  53.646  31.488  1.00 56.16  ? 32  TYR C CD2   1 
ATOM   3711 C  CE1   . TYR C 1 32  ? 17.228  55.966  30.007  1.00 56.17  ? 32  TYR C CE1   1 
ATOM   3712 C  CE2   . TYR C 1 32  ? 17.478  53.587  30.098  1.00 55.02  ? 32  TYR C CE2   1 
ATOM   3713 C  CZ    . TYR C 1 32  ? 17.364  54.754  29.365  1.00 55.02  ? 32  TYR C CZ    1 
ATOM   3714 O  OH    . TYR C 1 32  ? 17.348  54.735  27.991  1.00 53.51  ? 32  TYR C OH    1 
ATOM   3715 N  N     . ILE C 1 33  ? 14.927  52.770  34.306  1.00 55.62  ? 33  ILE C N     1 
ATOM   3716 C  CA    . ILE C 1 33  ? 14.216  51.583  33.879  1.00 55.47  ? 33  ILE C CA    1 
ATOM   3717 C  C     . ILE C 1 33  ? 12.715  51.807  33.943  1.00 57.04  ? 33  ILE C C     1 
ATOM   3718 O  O     . ILE C 1 33  ? 11.978  51.416  33.032  1.00 56.96  ? 33  ILE C O     1 
ATOM   3719 C  CB    . ILE C 1 33  ? 14.579  50.373  34.733  1.00 53.21  ? 33  ILE C CB    1 
ATOM   3720 C  CG1   . ILE C 1 33  ? 16.085  50.149  34.686  1.00 51.00  ? 33  ILE C CG1   1 
ATOM   3721 C  CG2   . ILE C 1 33  ? 13.856  49.135  34.203  1.00 53.08  ? 33  ILE C CG2   1 
ATOM   3722 C  CD1   . ILE C 1 33  ? 16.520  48.878  35.368  1.00 51.73  ? 33  ILE C CD1   1 
ATOM   3723 N  N     . LEU C 1 34  ? 12.269  52.449  35.018  1.00 58.83  ? 34  LEU C N     1 
ATOM   3724 C  CA    . LEU C 1 34  ? 10.848  52.726  35.210  1.00 60.70  ? 34  LEU C CA    1 
ATOM   3725 C  C     . LEU C 1 34  ? 10.331  53.862  34.334  1.00 61.11  ? 34  LEU C C     1 
ATOM   3726 O  O     . LEU C 1 34  ? 9.253   53.747  33.740  1.00 60.79  ? 34  LEU C O     1 
ATOM   3727 C  CB    . LEU C 1 34  ? 10.581  53.045  36.677  1.00 62.23  ? 34  LEU C CB    1 
ATOM   3728 C  CG    . LEU C 1 34  ? 10.863  51.886  37.632  1.00 63.50  ? 34  LEU C CG    1 
ATOM   3729 C  CD1   . LEU C 1 34  ? 10.772  52.385  39.051  1.00 63.72  ? 34  LEU C CD1   1 
ATOM   3730 C  CD2   . LEU C 1 34  ? 9.866   50.755  37.393  1.00 63.30  ? 34  LEU C CD2   1 
ATOM   3731 N  N     . GLU C 1 35  ? 11.098  54.949  34.252  1.00 61.08  ? 35  GLU C N     1 
ATOM   3732 C  CA    . GLU C 1 35  ? 10.718  56.107  33.444  1.00 61.87  ? 35  GLU C CA    1 
ATOM   3733 C  C     . GLU C 1 35  ? 10.510  55.732  31.982  1.00 60.33  ? 35  GLU C C     1 
ATOM   3734 O  O     . GLU C 1 35  ? 9.481   56.045  31.396  1.00 60.87  ? 35  GLU C O     1 
ATOM   3735 C  CB    . GLU C 1 35  ? 11.795  57.194  33.508  1.00 66.08  ? 35  GLU C CB    1 
ATOM   3736 C  CG    . GLU C 1 35  ? 12.285  57.545  34.905  1.00 73.34  ? 35  GLU C CG    1 
ATOM   3737 C  CD    . GLU C 1 35  ? 11.336  58.444  35.680  1.00 77.68  ? 35  GLU C CD    1 
ATOM   3738 O  OE1   . GLU C 1 35  ? 10.099  58.332  35.490  1.00 80.23  ? 35  GLU C OE1   1 
ATOM   3739 O  OE2   . GLU C 1 35  ? 11.837  59.253  36.497  1.00 79.20  ? 35  GLU C OE2   1 
ATOM   3740 N  N     . THR C 1 36  ? 11.489  55.052  31.398  1.00 58.74  ? 36  THR C N     1 
ATOM   3741 C  CA    . THR C 1 36  ? 11.412  54.682  29.994  1.00 57.83  ? 36  THR C CA    1 
ATOM   3742 C  C     . THR C 1 36  ? 10.647  53.398  29.664  1.00 58.80  ? 36  THR C C     1 
ATOM   3743 O  O     . THR C 1 36  ? 9.839   53.380  28.741  1.00 59.20  ? 36  THR C O     1 
ATOM   3744 C  CB    . THR C 1 36  ? 12.834  54.587  29.372  1.00 56.63  ? 36  THR C CB    1 
ATOM   3745 O  OG1   . THR C 1 36  ? 13.274  53.231  29.367  1.00 56.10  ? 36  THR C OG1   1 
ATOM   3746 C  CG2   . THR C 1 36  ? 13.830  55.412  30.174  1.00 55.95  ? 36  THR C CG2   1 
ATOM   3747 N  N     . SER C 1 37  ? 10.881  52.332  30.419  1.00 59.70  ? 37  SER C N     1 
ATOM   3748 C  CA    . SER C 1 37  ? 10.230  51.056  30.147  1.00 60.08  ? 37  SER C CA    1 
ATOM   3749 C  C     . SER C 1 37  ? 8.904   50.749  30.823  1.00 60.37  ? 37  SER C C     1 
ATOM   3750 O  O     . SER C 1 37  ? 8.019   50.152  30.208  1.00 59.49  ? 37  SER C O     1 
ATOM   3751 C  CB    . SER C 1 37  ? 11.179  49.923  30.491  1.00 61.63  ? 37  SER C CB    1 
ATOM   3752 O  OG    . SER C 1 37  ? 10.448  48.772  30.888  1.00 64.95  ? 37  SER C OG    1 
ATOM   3753 N  N     . VAL C 1 38  ? 8.775   51.132  32.090  1.00 61.09  ? 38  VAL C N     1 
ATOM   3754 C  CA    . VAL C 1 38  ? 7.568   50.830  32.860  1.00 61.84  ? 38  VAL C CA    1 
ATOM   3755 C  C     . VAL C 1 38  ? 6.377   51.803  32.813  1.00 62.27  ? 38  VAL C C     1 
ATOM   3756 O  O     . VAL C 1 38  ? 5.382   51.532  32.138  1.00 63.25  ? 38  VAL C O     1 
ATOM   3757 C  CB    . VAL C 1 38  ? 7.938   50.571  34.331  1.00 61.05  ? 38  VAL C CB    1 
ATOM   3758 C  CG1   . VAL C 1 38  ? 6.697   50.228  35.117  1.00 60.68  ? 38  VAL C CG1   1 
ATOM   3759 C  CG2   . VAL C 1 38  ? 8.949   49.442  34.413  1.00 58.14  ? 38  VAL C CG2   1 
ATOM   3760 N  N     . PHE C 1 39  ? 6.462   52.922  33.522  1.00 62.18  ? 39  PHE C N     1 
ATOM   3761 C  CA    . PHE C 1 39  ? 5.356   53.876  33.543  1.00 62.29  ? 39  PHE C CA    1 
ATOM   3762 C  C     . PHE C 1 39  ? 4.679   54.131  32.193  1.00 64.06  ? 39  PHE C C     1 
ATOM   3763 O  O     . PHE C 1 39  ? 3.453   54.165  32.116  1.00 64.51  ? 39  PHE C O     1 
ATOM   3764 C  CB    . PHE C 1 39  ? 5.807   55.219  34.119  1.00 59.36  ? 39  PHE C CB    1 
ATOM   3765 C  CG    . PHE C 1 39  ? 6.458   55.118  35.460  1.00 58.04  ? 39  PHE C CG    1 
ATOM   3766 C  CD1   . PHE C 1 39  ? 6.076   54.132  36.364  1.00 57.66  ? 39  PHE C CD1   1 
ATOM   3767 C  CD2   . PHE C 1 39  ? 7.465   56.013  35.822  1.00 58.12  ? 39  PHE C CD2   1 
ATOM   3768 C  CE1   . PHE C 1 39  ? 6.690   54.033  37.610  1.00 58.16  ? 39  PHE C CE1   1 
ATOM   3769 C  CE2   . PHE C 1 39  ? 8.089   55.931  37.059  1.00 57.62  ? 39  PHE C CE2   1 
ATOM   3770 C  CZ    . PHE C 1 39  ? 7.701   54.934  37.961  1.00 59.22  ? 39  PHE C CZ    1 
ATOM   3771 N  N     . PRO C 1 40  ? 5.463   54.315  31.113  1.00 65.61  ? 40  PRO C N     1 
ATOM   3772 C  CA    . PRO C 1 40  ? 4.871   54.572  29.797  1.00 66.32  ? 40  PRO C CA    1 
ATOM   3773 C  C     . PRO C 1 40  ? 3.798   53.575  29.381  1.00 67.90  ? 40  PRO C C     1 
ATOM   3774 O  O     . PRO C 1 40  ? 2.634   53.931  29.247  1.00 69.35  ? 40  PRO C O     1 
ATOM   3775 C  CB    . PRO C 1 40  ? 6.077   54.546  28.865  1.00 65.84  ? 40  PRO C CB    1 
ATOM   3776 C  CG    . PRO C 1 40  ? 7.172   55.062  29.718  1.00 65.26  ? 40  PRO C CG    1 
ATOM   3777 C  CD    . PRO C 1 40  ? 6.936   54.326  31.023  1.00 65.86  ? 40  PRO C CD    1 
ATOM   3778 N  N     . ARG C 1 41  ? 4.178   52.324  29.173  1.00 69.38  ? 41  ARG C N     1 
ATOM   3779 C  CA    . ARG C 1 41  ? 3.195   51.342  28.763  1.00 71.43  ? 41  ARG C CA    1 
ATOM   3780 C  C     . ARG C 1 41  ? 2.626   50.565  29.926  1.00 73.52  ? 41  ARG C C     1 
ATOM   3781 O  O     . ARG C 1 41  ? 1.968   49.537  29.745  1.00 72.92  ? 41  ARG C O     1 
ATOM   3782 C  CB    . ARG C 1 41  ? 3.783   50.396  27.721  1.00 70.41  ? 41  ARG C CB    1 
ATOM   3783 C  CG    . ARG C 1 41  ? 5.158   49.875  28.016  1.00 67.96  ? 41  ARG C CG    1 
ATOM   3784 C  CD    . ARG C 1 41  ? 5.851   49.673  26.687  1.00 68.05  ? 41  ARG C CD    1 
ATOM   3785 N  NE    . ARG C 1 41  ? 4.980   48.990  25.734  1.00 67.26  ? 41  ARG C NE    1 
ATOM   3786 C  CZ    . ARG C 1 41  ? 5.279   48.783  24.457  1.00 66.79  ? 41  ARG C CZ    1 
ATOM   3787 N  NH1   . ARG C 1 41  ? 6.433   49.205  23.963  1.00 67.46  ? 41  ARG C NH1   1 
ATOM   3788 N  NH2   . ARG C 1 41  ? 4.421   48.153  23.672  1.00 67.39  ? 41  ARG C NH2   1 
ATOM   3789 N  N     . GLU C 1 42  ? 2.869   51.075  31.126  1.00 76.44  ? 42  GLU C N     1 
ATOM   3790 C  CA    . GLU C 1 42  ? 2.351   50.437  32.321  1.00 79.42  ? 42  GLU C CA    1 
ATOM   3791 C  C     . GLU C 1 42  ? 0.856   50.246  32.146  1.00 81.78  ? 42  GLU C C     1 
ATOM   3792 O  O     . GLU C 1 42  ? 0.172   51.057  31.521  1.00 81.64  ? 42  GLU C O     1 
ATOM   3793 C  CB    . GLU C 1 42  ? 2.621   51.290  33.552  1.00 79.02  ? 42  GLU C CB    1 
ATOM   3794 C  CG    . GLU C 1 42  ? 2.074   50.696  34.819  1.00 79.22  ? 42  GLU C CG    1 
ATOM   3795 C  CD    . GLU C 1 42  ? 2.505   51.476  36.033  1.00 79.98  ? 42  GLU C CD    1 
ATOM   3796 O  OE1   . GLU C 1 42  ? 2.420   52.722  35.984  1.00 80.16  ? 42  GLU C OE1   1 
ATOM   3797 O  OE2   . GLU C 1 42  ? 2.922   50.846  37.032  1.00 80.69  ? 42  GLU C OE2   1 
ATOM   3798 N  N     . HIS C 1 43  ? 0.364   49.150  32.701  1.00 85.19  ? 43  HIS C N     1 
ATOM   3799 C  CA    . HIS C 1 43  ? -1.043  48.791  32.620  1.00 87.45  ? 43  HIS C CA    1 
ATOM   3800 C  C     . HIS C 1 43  ? -1.914  49.863  33.257  1.00 87.44  ? 43  HIS C C     1 
ATOM   3801 O  O     . HIS C 1 43  ? -1.425  50.756  33.949  1.00 87.06  ? 43  HIS C O     1 
ATOM   3802 C  CB    . HIS C 1 43  ? -1.244  47.454  33.333  1.00 90.38  ? 43  HIS C CB    1 
ATOM   3803 C  CG    . HIS C 1 43  ? -0.012  46.598  33.349  1.00 93.01  ? 43  HIS C CG    1 
ATOM   3804 N  ND1   . HIS C 1 43  ? 0.442   45.926  32.235  1.00 94.55  ? 43  HIS C ND1   1 
ATOM   3805 C  CD2   . HIS C 1 43  ? 0.900   46.368  34.325  1.00 93.85  ? 43  HIS C CD2   1 
ATOM   3806 C  CE1   . HIS C 1 43  ? 1.581   45.321  32.524  1.00 96.19  ? 43  HIS C CE1   1 
ATOM   3807 N  NE2   . HIS C 1 43  ? 1.881   45.574  33.786  1.00 95.18  ? 43  HIS C NE2   1 
ATOM   3808 N  N     . GLU C 1 44  ? -3.211  49.765  33.019  1.00 87.71  ? 44  GLU C N     1 
ATOM   3809 C  CA    . GLU C 1 44  ? -4.165  50.714  33.572  1.00 88.46  ? 44  GLU C CA    1 
ATOM   3810 C  C     . GLU C 1 44  ? -4.424  50.459  35.064  1.00 88.72  ? 44  GLU C C     1 
ATOM   3811 O  O     . GLU C 1 44  ? -4.739  49.330  35.473  1.00 88.26  ? 44  GLU C O     1 
ATOM   3812 C  CB    . GLU C 1 44  ? -5.488  50.607  32.815  1.00 88.55  ? 44  GLU C CB    1 
ATOM   3813 C  CG    . GLU C 1 44  ? -6.247  49.300  33.072  1.00 87.67  ? 44  GLU C CG    1 
ATOM   3814 C  CD    . GLU C 1 44  ? -5.495  48.075  32.593  1.00 87.26  ? 44  GLU C CD    1 
ATOM   3815 O  OE1   . GLU C 1 44  ? -4.363  47.843  33.058  1.00 86.70  ? 44  GLU C OE1   1 
ATOM   3816 O  OE2   . GLU C 1 44  ? -6.039  47.338  31.747  1.00 88.09  ? 44  GLU C OE2   1 
ATOM   3817 N  N     . ALA C 1 45  ? -4.284  51.504  35.875  1.00 88.11  ? 45  ALA C N     1 
ATOM   3818 C  CA    . ALA C 1 45  ? -4.551  51.378  37.301  1.00 88.37  ? 45  ALA C CA    1 
ATOM   3819 C  C     . ALA C 1 45  ? -3.448  50.749  38.135  1.00 87.94  ? 45  ALA C C     1 
ATOM   3820 O  O     . ALA C 1 45  ? -3.510  50.784  39.360  1.00 88.52  ? 45  ALA C O     1 
ATOM   3821 C  CB    . ALA C 1 45  ? -5.856  50.601  37.519  1.00 89.35  ? 45  ALA C CB    1 
ATOM   3822 N  N     . MET C 1 46  ? -2.457  50.142  37.497  1.00 86.83  ? 46  MET C N     1 
ATOM   3823 C  CA    . MET C 1 46  ? -1.368  49.561  38.264  1.00 84.84  ? 46  MET C CA    1 
ATOM   3824 C  C     . MET C 1 46  ? -0.826  50.705  39.108  1.00 85.04  ? 46  MET C C     1 
ATOM   3825 O  O     . MET C 1 46  ? -0.251  50.494  40.179  1.00 85.17  ? 46  MET C O     1 
ATOM   3826 C  CB    . MET C 1 46  ? -0.278  49.037  37.337  1.00 83.00  ? 46  MET C CB    1 
ATOM   3827 C  CG    . MET C 1 46  ? -0.642  47.764  36.619  1.00 80.69  ? 46  MET C CG    1 
ATOM   3828 S  SD    . MET C 1 46  ? -0.504  46.304  37.652  1.00 78.52  ? 46  MET C SD    1 
ATOM   3829 C  CE    . MET C 1 46  ? -2.039  45.515  37.304  1.00 78.56  ? 46  MET C CE    1 
ATOM   3830 N  N     . LYS C 1 47  ? -1.025  51.922  38.607  1.00 84.76  ? 47  LYS C N     1 
ATOM   3831 C  CA    . LYS C 1 47  ? -0.584  53.122  39.304  1.00 84.90  ? 47  LYS C CA    1 
ATOM   3832 C  C     . LYS C 1 47  ? -1.652  53.488  40.330  1.00 84.57  ? 47  LYS C C     1 
ATOM   3833 O  O     . LYS C 1 47  ? -1.355  54.123  41.339  1.00 84.66  ? 47  LYS C O     1 
ATOM   3834 C  CB    . LYS C 1 47  ? -0.382  54.280  38.321  1.00 84.82  ? 47  LYS C CB    1 
ATOM   3835 C  CG    . LYS C 1 47  ? 0.195   55.533  38.959  1.00 84.81  ? 47  LYS C CG    1 
ATOM   3836 C  CD    . LYS C 1 47  ? -0.015  56.758  38.079  1.00 86.19  ? 47  LYS C CD    1 
ATOM   3837 C  CE    . LYS C 1 47  ? 0.502   58.024  38.760  1.00 87.47  ? 47  LYS C CE    1 
ATOM   3838 N  NZ    . LYS C 1 47  ? -0.037  59.281  38.157  1.00 87.14  ? 47  LYS C NZ    1 
ATOM   3839 N  N     . GLU C 1 48  ? -2.897  53.101  40.054  1.00 84.24  ? 48  GLU C N     1 
ATOM   3840 C  CA    . GLU C 1 48  ? -4.003  53.356  40.976  1.00 84.14  ? 48  GLU C CA    1 
ATOM   3841 C  C     . GLU C 1 48  ? -3.743  52.482  42.194  1.00 83.56  ? 48  GLU C C     1 
ATOM   3842 O  O     . GLU C 1 48  ? -3.519  52.978  43.301  1.00 83.13  ? 48  GLU C O     1 
ATOM   3843 C  CB    . GLU C 1 48  ? -5.347  52.952  40.351  1.00 84.63  ? 48  GLU C CB    1 
ATOM   3844 C  CG    . GLU C 1 48  ? -6.090  54.060  39.603  1.00 86.55  ? 48  GLU C CG    1 
ATOM   3845 C  CD    . GLU C 1 48  ? -7.259  53.533  38.756  1.00 87.56  ? 48  GLU C CD    1 
ATOM   3846 O  OE1   . GLU C 1 48  ? -7.998  52.643  39.236  1.00 88.44  ? 48  GLU C OE1   1 
ATOM   3847 O  OE2   . GLU C 1 48  ? -7.446  54.014  37.614  1.00 86.81  ? 48  GLU C OE2   1 
ATOM   3848 N  N     . LEU C 1 49  ? -3.754  51.174  41.955  1.00 83.00  ? 49  LEU C N     1 
ATOM   3849 C  CA    . LEU C 1 49  ? -3.529  50.170  42.983  1.00 82.83  ? 49  LEU C CA    1 
ATOM   3850 C  C     . LEU C 1 49  ? -2.212  50.367  43.727  1.00 83.20  ? 49  LEU C C     1 
ATOM   3851 O  O     . LEU C 1 49  ? -2.054  49.908  44.861  1.00 83.72  ? 49  LEU C O     1 
ATOM   3852 C  CB    . LEU C 1 49  ? -3.569  48.772  42.356  1.00 81.97  ? 49  LEU C CB    1 
ATOM   3853 C  CG    . LEU C 1 49  ? -3.358  47.581  43.299  1.00 81.82  ? 49  LEU C CG    1 
ATOM   3854 C  CD1   . LEU C 1 49  ? -4.336  47.675  44.458  1.00 81.57  ? 49  LEU C CD1   1 
ATOM   3855 C  CD2   . LEU C 1 49  ? -3.537  46.272  42.542  1.00 80.36  ? 49  LEU C CD2   1 
ATOM   3856 N  N     . ARG C 1 50  ? -1.267  51.052  43.096  1.00 83.62  ? 50  ARG C N     1 
ATOM   3857 C  CA    . ARG C 1 50  ? 0.027   51.289  43.717  1.00 83.96  ? 50  ARG C CA    1 
ATOM   3858 C  C     . ARG C 1 50  ? -0.016  52.535  44.589  1.00 84.51  ? 50  ARG C C     1 
ATOM   3859 O  O     . ARG C 1 50  ? 0.760   52.660  45.535  1.00 83.86  ? 50  ARG C O     1 
ATOM   3860 C  CB    . ARG C 1 50  ? 1.112   51.405  42.636  1.00 83.50  ? 50  ARG C CB    1 
ATOM   3861 C  CG    . ARG C 1 50  ? 2.518   51.703  43.150  1.00 82.80  ? 50  ARG C CG    1 
ATOM   3862 C  CD    . ARG C 1 50  ? 3.571   51.082  42.244  1.00 82.05  ? 50  ARG C CD    1 
ATOM   3863 N  NE    . ARG C 1 50  ? 3.266   51.278  40.828  1.00 81.61  ? 50  ARG C NE    1 
ATOM   3864 C  CZ    . ARG C 1 50  ? 3.460   52.412  40.166  1.00 81.15  ? 50  ARG C CZ    1 
ATOM   3865 N  NH1   . ARG C 1 50  ? 3.973   53.472  40.781  1.00 81.36  ? 50  ARG C NH1   1 
ATOM   3866 N  NH2   . ARG C 1 50  ? 3.122   52.492  38.889  1.00 80.33  ? 50  ARG C NH2   1 
ATOM   3867 N  N     . GLU C 1 51  ? -0.926  53.454  44.269  1.00 86.22  ? 51  GLU C N     1 
ATOM   3868 C  CA    . GLU C 1 51  ? -1.074  54.682  45.048  1.00 88.47  ? 51  GLU C CA    1 
ATOM   3869 C  C     . GLU C 1 51  ? -2.061  54.421  46.181  1.00 88.82  ? 51  GLU C C     1 
ATOM   3870 O  O     . GLU C 1 51  ? -2.271  55.265  47.052  1.00 88.38  ? 51  GLU C O     1 
ATOM   3871 C  CB    . GLU C 1 51  ? -1.567  55.838  44.173  1.00 89.96  ? 51  GLU C CB    1 
ATOM   3872 C  CG    . GLU C 1 51  ? -0.578  56.258  43.093  1.00 93.29  ? 51  GLU C CG    1 
ATOM   3873 C  CD    . GLU C 1 51  ? -0.899  57.621  42.488  1.00 95.72  ? 51  GLU C CD    1 
ATOM   3874 O  OE1   . GLU C 1 51  ? -2.079  57.867  42.145  1.00 96.52  ? 51  GLU C OE1   1 
ATOM   3875 O  OE2   . GLU C 1 51  ? 0.038   58.444  42.348  1.00 96.29  ? 51  GLU C OE2   1 
ATOM   3876 N  N     . VAL C 1 52  ? -2.664  53.236  46.144  1.00 89.47  ? 52  VAL C N     1 
ATOM   3877 C  CA    . VAL C 1 52  ? -3.603  52.786  47.164  1.00 89.52  ? 52  VAL C CA    1 
ATOM   3878 C  C     . VAL C 1 52  ? -2.757  52.152  48.254  1.00 90.15  ? 52  VAL C C     1 
ATOM   3879 O  O     . VAL C 1 52  ? -2.956  52.404  49.439  1.00 90.57  ? 52  VAL C O     1 
ATOM   3880 C  CB    . VAL C 1 52  ? -4.556  51.709  46.613  1.00 89.39  ? 52  VAL C CB    1 
ATOM   3881 C  CG1   . VAL C 1 52  ? -5.291  51.032  47.751  1.00 88.87  ? 52  VAL C CG1   1 
ATOM   3882 C  CG2   . VAL C 1 52  ? -5.541  52.337  45.637  1.00 89.86  ? 52  VAL C CG2   1 
ATOM   3883 N  N     . THR C 1 53  ? -1.804  51.329  47.829  1.00 90.90  ? 53  THR C N     1 
ATOM   3884 C  CA    . THR C 1 53  ? -0.901  50.645  48.742  1.00 91.73  ? 53  THR C CA    1 
ATOM   3885 C  C     . THR C 1 53  ? -0.005  51.658  49.443  1.00 92.54  ? 53  THR C C     1 
ATOM   3886 O  O     . THR C 1 53  ? 0.694   51.328  50.395  1.00 92.32  ? 53  THR C O     1 
ATOM   3887 C  CB    . THR C 1 53  ? -0.023  49.633  47.988  1.00 91.56  ? 53  THR C CB    1 
ATOM   3888 O  OG1   . THR C 1 53  ? -0.858  48.786  47.192  1.00 90.67  ? 53  THR C OG1   1 
ATOM   3889 C  CG2   . THR C 1 53  ? 0.764   48.769  48.965  1.00 91.54  ? 53  THR C CG2   1 
ATOM   3890 N  N     . ALA C 1 54  ? -0.023  52.893  48.961  1.00 94.11  ? 54  ALA C N     1 
ATOM   3891 C  CA    . ALA C 1 54  ? 0.773   53.946  49.567  1.00 96.68  ? 54  ALA C CA    1 
ATOM   3892 C  C     . ALA C 1 54  ? -0.095  54.576  50.652  1.00 98.95  ? 54  ALA C C     1 
ATOM   3893 O  O     . ALA C 1 54  ? 0.392   55.291  51.533  1.00 98.73  ? 54  ALA C O     1 
ATOM   3894 C  CB    . ALA C 1 54  ? 1.163   54.982  48.520  1.00 96.19  ? 54  ALA C CB    1 
ATOM   3895 N  N     . LYS C 1 55  ? -1.394  54.296  50.573  1.00 101.64 ? 55  LYS C N     1 
ATOM   3896 C  CA    . LYS C 1 55  ? -2.357  54.800  51.544  1.00 104.68 ? 55  LYS C CA    1 
ATOM   3897 C  C     . LYS C 1 55  ? -2.516  53.821  52.716  1.00 107.07 ? 55  LYS C C     1 
ATOM   3898 O  O     . LYS C 1 55  ? -3.121  54.154  53.741  1.00 107.80 ? 55  LYS C O     1 
ATOM   3899 C  CB    . LYS C 1 55  ? -3.720  55.046  50.876  1.00 103.47 ? 55  LYS C CB    1 
ATOM   3900 C  CG    . LYS C 1 55  ? -3.926  56.478  50.396  1.00 102.45 ? 55  LYS C CG    1 
ATOM   3901 C  CD    . LYS C 1 55  ? -5.411  56.804  50.256  1.00 101.56 ? 55  LYS C CD    1 
ATOM   3902 C  CE    . LYS C 1 55  ? -5.656  58.311  50.174  1.00 100.24 ? 55  LYS C CE    1 
ATOM   3903 N  NZ    . LYS C 1 55  ? -7.108  58.649  50.237  1.00 98.63  ? 55  LYS C NZ    1 
ATOM   3904 N  N     . HIS C 1 56  ? -1.965  52.619  52.559  1.00 109.17 ? 56  HIS C N     1 
ATOM   3905 C  CA    . HIS C 1 56  ? -2.035  51.595  53.596  1.00 111.33 ? 56  HIS C CA    1 
ATOM   3906 C  C     . HIS C 1 56  ? -1.408  52.129  54.881  1.00 113.23 ? 56  HIS C C     1 
ATOM   3907 O  O     . HIS C 1 56  ? -0.336  52.739  54.858  1.00 113.36 ? 56  HIS C O     1 
ATOM   3908 C  CB    . HIS C 1 56  ? -1.308  50.334  53.128  1.00 111.42 ? 56  HIS C CB    1 
ATOM   3909 C  CG    . HIS C 1 56  ? -1.433  49.169  54.061  1.00 111.44 ? 56  HIS C CG    1 
ATOM   3910 N  ND1   . HIS C 1 56  ? -0.678  49.049  55.209  1.00 111.44 ? 56  HIS C ND1   1 
ATOM   3911 C  CD2   . HIS C 1 56  ? -2.201  48.055  53.997  1.00 110.97 ? 56  HIS C CD2   1 
ATOM   3912 C  CE1   . HIS C 1 56  ? -0.972  47.908  55.807  1.00 111.73 ? 56  HIS C CE1   1 
ATOM   3913 N  NE2   . HIS C 1 56  ? -1.893  47.286  55.093  1.00 111.00 ? 56  HIS C NE2   1 
ATOM   3914 N  N     . PRO C 1 57  ? -2.080  51.905  56.021  1.00 114.89 ? 57  PRO C N     1 
ATOM   3915 C  CA    . PRO C 1 57  ? -1.643  52.346  57.348  1.00 116.10 ? 57  PRO C CA    1 
ATOM   3916 C  C     . PRO C 1 57  ? -0.289  51.842  57.833  1.00 117.58 ? 57  PRO C C     1 
ATOM   3917 O  O     . PRO C 1 57  ? 0.412   52.553  58.547  1.00 117.37 ? 57  PRO C O     1 
ATOM   3918 C  CB    . PRO C 1 57  ? -2.784  51.885  58.249  1.00 115.89 ? 57  PRO C CB    1 
ATOM   3919 C  CG    . PRO C 1 57  ? -3.272  50.654  57.559  1.00 115.55 ? 57  PRO C CG    1 
ATOM   3920 C  CD    . PRO C 1 57  ? -3.316  51.111  56.127  1.00 115.23 ? 57  PRO C CD    1 
ATOM   3921 N  N     . TRP C 1 58  ? 0.088   50.627  57.456  1.00 119.77 ? 58  TRP C N     1 
ATOM   3922 C  CA    . TRP C 1 58  ? 1.364   50.100  57.915  1.00 122.66 ? 58  TRP C CA    1 
ATOM   3923 C  C     . TRP C 1 58  ? 2.566   50.381  57.016  1.00 124.31 ? 58  TRP C C     1 
ATOM   3924 O  O     . TRP C 1 58  ? 3.704   50.334  57.483  1.00 124.96 ? 58  TRP C O     1 
ATOM   3925 C  CB    . TRP C 1 58  ? 1.245   48.595  58.188  1.00 123.38 ? 58  TRP C CB    1 
ATOM   3926 C  CG    . TRP C 1 58  ? 0.638   48.285  59.541  1.00 124.43 ? 58  TRP C CG    1 
ATOM   3927 C  CD1   . TRP C 1 58  ? 1.100   48.699  60.759  1.00 124.56 ? 58  TRP C CD1   1 
ATOM   3928 C  CD2   . TRP C 1 58  ? -0.534  47.497  59.807  1.00 124.69 ? 58  TRP C CD2   1 
ATOM   3929 N  NE1   . TRP C 1 58  ? 0.293   48.221  61.764  1.00 124.45 ? 58  TRP C NE1   1 
ATOM   3930 C  CE2   . TRP C 1 58  ? -0.717  47.481  61.208  1.00 124.61 ? 58  TRP C CE2   1 
ATOM   3931 C  CE3   . TRP C 1 58  ? -1.446  46.804  59.000  1.00 124.86 ? 58  TRP C CE3   1 
ATOM   3932 C  CZ2   . TRP C 1 58  ? -1.775  46.797  61.819  1.00 124.41 ? 58  TRP C CZ2   1 
ATOM   3933 C  CZ3   . TRP C 1 58  ? -2.500  46.123  59.611  1.00 124.65 ? 58  TRP C CZ3   1 
ATOM   3934 C  CH2   . TRP C 1 58  ? -2.652  46.127  61.007  1.00 124.30 ? 58  TRP C CH2   1 
ATOM   3935 N  N     . ASN C 1 59  ? 2.323   50.692  55.743  1.00 126.09 ? 59  ASN C N     1 
ATOM   3936 C  CA    . ASN C 1 59  ? 3.405   50.967  54.786  1.00 127.55 ? 59  ASN C CA    1 
ATOM   3937 C  C     . ASN C 1 59  ? 4.329   49.759  54.710  1.00 127.98 ? 59  ASN C C     1 
ATOM   3938 O  O     . ASN C 1 59  ? 5.179   49.666  53.826  1.00 128.14 ? 59  ASN C O     1 
ATOM   3939 C  CB    . ASN C 1 59  ? 4.246   52.184  55.205  1.00 128.32 ? 59  ASN C CB    1 
ATOM   3940 C  CG    . ASN C 1 59  ? 3.427   53.456  55.349  1.00 129.04 ? 59  ASN C CG    1 
ATOM   3941 O  OD1   . ASN C 1 59  ? 2.584   53.772  54.505  1.00 129.15 ? 59  ASN C OD1   1 
ATOM   3942 N  ND2   . ASN C 1 59  ? 3.689   54.205  56.417  1.00 129.13 ? 59  ASN C ND2   1 
ATOM   3943 N  N     . ILE C 1 60  ? 4.148   48.853  55.666  1.00 128.39 ? 60  ILE C N     1 
ATOM   3944 C  CA    . ILE C 1 60  ? 4.917   47.627  55.804  1.00 128.90 ? 60  ILE C CA    1 
ATOM   3945 C  C     . ILE C 1 60  ? 6.166   47.508  54.926  1.00 128.50 ? 60  ILE C C     1 
ATOM   3946 O  O     . ILE C 1 60  ? 7.274   47.730  55.415  1.00 128.44 ? 60  ILE C O     1 
ATOM   3947 C  CB    . ILE C 1 60  ? 3.990   46.399  55.607  1.00 130.10 ? 60  ILE C CB    1 
ATOM   3948 C  CG1   . ILE C 1 60  ? 4.805   45.102  55.642  1.00 130.82 ? 60  ILE C CG1   1 
ATOM   3949 C  CG2   . ILE C 1 60  ? 3.171   46.571  54.344  1.00 130.44 ? 60  ILE C CG2   1 
ATOM   3950 C  CD1   . ILE C 1 60  ? 5.399   44.777  57.009  1.00 130.66 ? 60  ILE C CD1   1 
ATOM   3951 N  N     . MET C 1 61  ? 6.010   47.174  53.644  1.00 128.08 ? 61  MET C N     1 
ATOM   3952 C  CA    . MET C 1 61  ? 7.184   47.032  52.780  1.00 127.41 ? 61  MET C CA    1 
ATOM   3953 C  C     . MET C 1 61  ? 7.037   47.222  51.263  1.00 125.86 ? 61  MET C C     1 
ATOM   3954 O  O     . MET C 1 61  ? 6.012   47.690  50.756  1.00 125.22 ? 61  MET C O     1 
ATOM   3955 C  CB    . MET C 1 61  ? 7.856   45.679  53.050  1.00 128.83 ? 61  MET C CB    1 
ATOM   3956 C  CG    . MET C 1 61  ? 6.898   44.496  53.068  1.00 130.67 ? 61  MET C CG    1 
ATOM   3957 S  SD    . MET C 1 61  ? 5.959   44.307  51.538  1.00 132.84 ? 61  MET C SD    1 
ATOM   3958 C  CE    . MET C 1 61  ? 4.549   45.383  51.840  1.00 131.37 ? 61  MET C CE    1 
ATOM   3959 N  N     . THR C 1 62  ? 8.106   46.829  50.568  1.00 124.21 ? 62  THR C N     1 
ATOM   3960 C  CA    . THR C 1 62  ? 8.277   46.919  49.115  1.00 122.16 ? 62  THR C CA    1 
ATOM   3961 C  C     . THR C 1 62  ? 7.125   46.620  48.153  1.00 119.96 ? 62  THR C C     1 
ATOM   3962 O  O     . THR C 1 62  ? 6.521   45.544  48.171  1.00 119.99 ? 62  THR C O     1 
ATOM   3963 C  CB    . THR C 1 62  ? 9.480   46.046  48.663  1.00 122.81 ? 62  THR C CB    1 
ATOM   3964 O  OG1   . THR C 1 62  ? 9.181   44.658  48.877  1.00 123.18 ? 62  THR C OG1   1 
ATOM   3965 C  CG2   . THR C 1 62  ? 10.734  46.420  49.449  1.00 122.88 ? 62  THR C CG2   1 
ATOM   3966 N  N     . THR C 1 63  ? 6.859   47.591  47.287  1.00 117.09 ? 63  THR C N     1 
ATOM   3967 C  CA    . THR C 1 63  ? 5.833   47.483  46.259  1.00 114.54 ? 63  THR C CA    1 
ATOM   3968 C  C     . THR C 1 63  ? 6.512   47.971  44.965  1.00 111.96 ? 63  THR C C     1 
ATOM   3969 O  O     . THR C 1 63  ? 6.329   49.112  44.535  1.00 111.74 ? 63  THR C O     1 
ATOM   3970 C  CB    . THR C 1 63  ? 4.583   48.349  46.623  1.00 114.81 ? 63  THR C CB    1 
ATOM   3971 O  OG1   . THR C 1 63  ? 3.645   48.334  45.538  1.00 114.49 ? 63  THR C OG1   1 
ATOM   3972 C  CG2   . THR C 1 63  ? 4.985   49.782  46.941  1.00 115.01 ? 63  THR C CG2   1 
ATOM   3973 N  N     . SER C 1 64  ? 7.313   47.087  44.368  1.00 108.65 ? 64  SER C N     1 
ATOM   3974 C  CA    . SER C 1 64  ? 8.072   47.387  43.151  1.00 105.12 ? 64  SER C CA    1 
ATOM   3975 C  C     . SER C 1 64  ? 7.259   47.575  41.874  1.00 102.30 ? 64  SER C C     1 
ATOM   3976 O  O     . SER C 1 64  ? 6.411   46.749  41.528  1.00 101.83 ? 64  SER C O     1 
ATOM   3977 C  CB    . SER C 1 64  ? 9.132   46.306  42.915  1.00 105.50 ? 64  SER C CB    1 
ATOM   3978 O  OG    . SER C 1 64  ? 10.191  46.414  43.852  1.00 105.97 ? 64  SER C OG    1 
ATOM   3979 N  N     . ALA C 1 65  ? 7.559   48.660  41.165  1.00 98.51  ? 65  ALA C N     1 
ATOM   3980 C  CA    . ALA C 1 65  ? 6.875   49.005  39.928  1.00 94.82  ? 65  ALA C CA    1 
ATOM   3981 C  C     . ALA C 1 65  ? 7.226   48.102  38.751  1.00 92.11  ? 65  ALA C C     1 
ATOM   3982 O  O     . ALA C 1 65  ? 6.429   47.951  37.830  1.00 91.37  ? 65  ALA C O     1 
ATOM   3983 C  CB    . ALA C 1 65  ? 7.174   50.450  39.570  1.00 95.15  ? 65  ALA C CB    1 
ATOM   3984 N  N     . ASP C 1 66  ? 8.409   47.495  38.782  1.00 89.01  ? 66  ASP C N     1 
ATOM   3985 C  CA    . ASP C 1 66  ? 8.841   46.628  37.690  1.00 85.89  ? 66  ASP C CA    1 
ATOM   3986 C  C     . ASP C 1 66  ? 8.357   45.179  37.685  1.00 84.74  ? 66  ASP C C     1 
ATOM   3987 O  O     . ASP C 1 66  ? 8.427   44.514  36.653  1.00 84.44  ? 66  ASP C O     1 
ATOM   3988 C  CB    . ASP C 1 66  ? 10.373  46.654  37.565  1.00 84.44  ? 66  ASP C CB    1 
ATOM   3989 C  CG    . ASP C 1 66  ? 11.074  46.719  38.901  1.00 81.70  ? 66  ASP C CG    1 
ATOM   3990 O  OD1   . ASP C 1 66  ? 10.678  47.560  39.724  1.00 81.71  ? 66  ASP C OD1   1 
ATOM   3991 O  OD2   . ASP C 1 66  ? 12.030  45.950  39.119  1.00 79.64  ? 66  ASP C OD2   1 
ATOM   3992 N  N     . GLU C 1 67  ? 7.865   44.681  38.814  1.00 83.67  ? 67  GLU C N     1 
ATOM   3993 C  CA    . GLU C 1 67  ? 7.388   43.300  38.857  1.00 82.06  ? 67  GLU C CA    1 
ATOM   3994 C  C     . GLU C 1 67  ? 6.195   43.112  37.926  1.00 79.20  ? 67  GLU C C     1 
ATOM   3995 O  O     . GLU C 1 67  ? 6.021   42.049  37.332  1.00 78.25  ? 67  GLU C O     1 
ATOM   3996 C  CB    . GLU C 1 67  ? 6.994   42.904  40.283  1.00 84.36  ? 67  GLU C CB    1 
ATOM   3997 C  CG    . GLU C 1 67  ? 8.062   43.203  41.328  1.00 88.34  ? 67  GLU C CG    1 
ATOM   3998 C  CD    . GLU C 1 67  ? 7.707   42.664  42.709  1.00 90.55  ? 67  GLU C CD    1 
ATOM   3999 O  OE1   . GLU C 1 67  ? 6.523   42.776  43.107  1.00 91.03  ? 67  GLU C OE1   1 
ATOM   4000 O  OE2   . GLU C 1 67  ? 8.618   42.140  43.398  1.00 91.72  ? 67  GLU C OE2   1 
ATOM   4001 N  N     . GLY C 1 68  ? 5.380   44.152  37.794  1.00 76.82  ? 68  GLY C N     1 
ATOM   4002 C  CA    . GLY C 1 68  ? 4.207   44.070  36.941  1.00 75.01  ? 68  GLY C CA    1 
ATOM   4003 C  C     . GLY C 1 68  ? 4.526   43.769  35.492  1.00 73.74  ? 68  GLY C C     1 
ATOM   4004 O  O     . GLY C 1 68  ? 3.955   42.844  34.898  1.00 72.42  ? 68  GLY C O     1 
ATOM   4005 N  N     . GLN C 1 69  ? 5.436   44.562  34.925  1.00 72.59  ? 69  GLN C N     1 
ATOM   4006 C  CA    . GLN C 1 69  ? 5.868   44.407  33.538  1.00 70.43  ? 69  GLN C CA    1 
ATOM   4007 C  C     . GLN C 1 69  ? 6.522   43.034  33.370  1.00 66.70  ? 69  GLN C C     1 
ATOM   4008 O  O     . GLN C 1 69  ? 6.364   42.378  32.345  1.00 65.25  ? 69  GLN C O     1 
ATOM   4009 C  CB    . GLN C 1 69  ? 6.856   45.528  33.173  1.00 73.44  ? 69  GLN C CB    1 
ATOM   4010 C  CG    . GLN C 1 69  ? 7.209   45.611  31.680  1.00 77.93  ? 69  GLN C CG    1 
ATOM   4011 C  CD    . GLN C 1 69  ? 8.236   46.708  31.358  1.00 80.40  ? 69  GLN C CD    1 
ATOM   4012 O  OE1   . GLN C 1 69  ? 9.376   46.686  31.844  1.00 79.77  ? 69  GLN C OE1   1 
ATOM   4013 N  NE2   . GLN C 1 69  ? 7.830   47.670  30.529  1.00 81.23  ? 69  GLN C NE2   1 
ATOM   4014 N  N     . PHE C 1 70  ? 7.251   42.603  34.394  1.00 64.01  ? 70  PHE C N     1 
ATOM   4015 C  CA    . PHE C 1 70  ? 7.910   41.309  34.366  1.00 61.59  ? 70  PHE C CA    1 
ATOM   4016 C  C     . PHE C 1 70  ? 6.895   40.164  34.418  1.00 60.92  ? 70  PHE C C     1 
ATOM   4017 O  O     . PHE C 1 70  ? 6.874   39.301  33.539  1.00 60.88  ? 70  PHE C O     1 
ATOM   4018 C  CB    . PHE C 1 70  ? 8.880   41.170  35.536  1.00 60.72  ? 70  PHE C CB    1 
ATOM   4019 C  CG    . PHE C 1 70  ? 9.604   39.861  35.548  1.00 60.67  ? 70  PHE C CG    1 
ATOM   4020 C  CD1   . PHE C 1 70  ? 10.678  39.638  34.691  1.00 60.60  ? 70  PHE C CD1   1 
ATOM   4021 C  CD2   . PHE C 1 70  ? 9.158   38.816  36.347  1.00 60.94  ? 70  PHE C CD2   1 
ATOM   4022 C  CE1   . PHE C 1 70  ? 11.291  38.392  34.627  1.00 60.84  ? 70  PHE C CE1   1 
ATOM   4023 C  CE2   . PHE C 1 70  ? 9.767   37.561  36.288  1.00 61.08  ? 70  PHE C CE2   1 
ATOM   4024 C  CZ    . PHE C 1 70  ? 10.831  37.348  35.429  1.00 60.83  ? 70  PHE C CZ    1 
ATOM   4025 N  N     . LEU C 1 71  ? 6.062   40.144  35.454  1.00 60.00  ? 71  LEU C N     1 
ATOM   4026 C  CA    . LEU C 1 71  ? 5.057   39.095  35.575  1.00 59.24  ? 71  LEU C CA    1 
ATOM   4027 C  C     . LEU C 1 71  ? 4.222   39.024  34.306  1.00 57.85  ? 71  LEU C C     1 
ATOM   4028 O  O     . LEU C 1 71  ? 3.996   37.943  33.760  1.00 56.26  ? 71  LEU C O     1 
ATOM   4029 C  CB    . LEU C 1 71  ? 4.148   39.356  36.781  1.00 61.91  ? 71  LEU C CB    1 
ATOM   4030 C  CG    . LEU C 1 71  ? 4.503   38.637  38.086  1.00 62.87  ? 71  LEU C CG    1 
ATOM   4031 C  CD1   . LEU C 1 71  ? 4.403   37.151  37.850  1.00 64.33  ? 71  LEU C CD1   1 
ATOM   4032 C  CD2   . LEU C 1 71  ? 5.908   38.991  38.543  1.00 64.66  ? 71  LEU C CD2   1 
ATOM   4033 N  N     . SER C 1 72  ? 3.771   40.185  33.839  1.00 57.17  ? 72  SER C N     1 
ATOM   4034 C  CA    . SER C 1 72  ? 2.964   40.268  32.627  1.00 57.20  ? 72  SER C CA    1 
ATOM   4035 C  C     . SER C 1 72  ? 3.631   39.540  31.464  1.00 57.10  ? 72  SER C C     1 
ATOM   4036 O  O     . SER C 1 72  ? 3.024   38.666  30.831  1.00 57.79  ? 72  SER C O     1 
ATOM   4037 C  CB    . SER C 1 72  ? 2.739   41.728  32.244  1.00 58.28  ? 72  SER C CB    1 
ATOM   4038 O  OG    . SER C 1 72  ? 2.096   41.833  30.981  1.00 59.16  ? 72  SER C OG    1 
ATOM   4039 N  N     . MET C 1 73  ? 4.880   39.907  31.182  1.00 55.61  ? 73  MET C N     1 
ATOM   4040 C  CA    . MET C 1 73  ? 5.632   39.284  30.106  1.00 53.95  ? 73  MET C CA    1 
ATOM   4041 C  C     . MET C 1 73  ? 5.787   37.784  30.347  1.00 53.23  ? 73  MET C C     1 
ATOM   4042 O  O     . MET C 1 73  ? 5.512   36.981  29.464  1.00 51.87  ? 73  MET C O     1 
ATOM   4043 C  CB    . MET C 1 73  ? 7.018   39.925  29.988  1.00 56.34  ? 73  MET C CB    1 
ATOM   4044 C  CG    . MET C 1 73  ? 7.906   39.320  28.904  1.00 59.18  ? 73  MET C CG    1 
ATOM   4045 S  SD    . MET C 1 73  ? 7.669   40.062  27.260  1.00 65.61  ? 73  MET C SD    1 
ATOM   4046 C  CE    . MET C 1 73  ? 5.889   39.719  26.952  1.00 64.58  ? 73  MET C CE    1 
ATOM   4047 N  N     . LEU C 1 74  ? 6.213   37.397  31.545  1.00 52.44  ? 74  LEU C N     1 
ATOM   4048 C  CA    . LEU C 1 74  ? 6.410   35.983  31.818  1.00 53.28  ? 74  LEU C CA    1 
ATOM   4049 C  C     . LEU C 1 74  ? 5.148   35.155  31.595  1.00 54.86  ? 74  LEU C C     1 
ATOM   4050 O  O     . LEU C 1 74  ? 5.206   34.076  30.992  1.00 54.74  ? 74  LEU C O     1 
ATOM   4051 C  CB    . LEU C 1 74  ? 6.913   35.784  33.241  1.00 52.03  ? 74  LEU C CB    1 
ATOM   4052 C  CG    . LEU C 1 74  ? 7.757   34.534  33.496  1.00 51.39  ? 74  LEU C CG    1 
ATOM   4053 C  CD1   . LEU C 1 74  ? 8.061   34.459  34.973  1.00 52.42  ? 74  LEU C CD1   1 
ATOM   4054 C  CD2   . LEU C 1 74  ? 7.033   33.289  33.056  1.00 51.77  ? 74  LEU C CD2   1 
ATOM   4055 N  N     . LEU C 1 75  ? 4.008   35.660  32.067  1.00 56.43  ? 75  LEU C N     1 
ATOM   4056 C  CA    . LEU C 1 75  ? 2.738   34.941  31.929  1.00 56.83  ? 75  LEU C CA    1 
ATOM   4057 C  C     . LEU C 1 75  ? 2.271   34.793  30.492  1.00 57.05  ? 75  LEU C C     1 
ATOM   4058 O  O     . LEU C 1 75  ? 1.788   33.729  30.106  1.00 56.64  ? 75  LEU C O     1 
ATOM   4059 C  CB    . LEU C 1 75  ? 1.648   35.613  32.766  1.00 56.56  ? 75  LEU C CB    1 
ATOM   4060 C  CG    . LEU C 1 75  ? 1.864   35.386  34.259  1.00 56.97  ? 75  LEU C CG    1 
ATOM   4061 C  CD1   . LEU C 1 75  ? 1.094   36.405  35.065  1.00 56.46  ? 75  LEU C CD1   1 
ATOM   4062 C  CD2   . LEU C 1 75  ? 1.458   33.966  34.602  1.00 56.38  ? 75  LEU C CD2   1 
ATOM   4063 N  N     . LYS C 1 76  ? 2.401   35.852  29.699  1.00 57.50  ? 76  LYS C N     1 
ATOM   4064 C  CA    . LYS C 1 76  ? 1.991   35.762  28.309  1.00 58.53  ? 76  LYS C CA    1 
ATOM   4065 C  C     . LYS C 1 76  ? 2.958   34.828  27.586  1.00 58.49  ? 76  LYS C C     1 
ATOM   4066 O  O     . LYS C 1 76  ? 2.557   34.045  26.725  1.00 57.16  ? 76  LYS C O     1 
ATOM   4067 C  CB    . LYS C 1 76  ? 1.997   37.140  27.651  1.00 60.63  ? 76  LYS C CB    1 
ATOM   4068 C  CG    . LYS C 1 76  ? 1.050   38.136  28.281  1.00 62.52  ? 76  LYS C CG    1 
ATOM   4069 C  CD    . LYS C 1 76  ? 0.727   39.251  27.301  1.00 66.38  ? 76  LYS C CD    1 
ATOM   4070 C  CE    . LYS C 1 76  ? -0.340  40.178  27.849  1.00 69.54  ? 76  LYS C CE    1 
ATOM   4071 N  NZ    . LYS C 1 76  ? 0.098   40.803  29.135  1.00 72.51  ? 76  LYS C NZ    1 
ATOM   4072 N  N     . LEU C 1 77  ? 4.231   34.898  27.956  1.00 58.65  ? 77  LEU C N     1 
ATOM   4073 C  CA    . LEU C 1 77  ? 5.228   34.046  27.330  1.00 60.74  ? 77  LEU C CA    1 
ATOM   4074 C  C     . LEU C 1 77  ? 4.944   32.562  27.557  1.00 62.66  ? 77  LEU C C     1 
ATOM   4075 O  O     . LEU C 1 77  ? 4.937   31.777  26.604  1.00 63.59  ? 77  LEU C O     1 
ATOM   4076 C  CB    . LEU C 1 77  ? 6.632   34.377  27.847  1.00 59.80  ? 77  LEU C CB    1 
ATOM   4077 C  CG    . LEU C 1 77  ? 7.305   35.645  27.328  1.00 58.07  ? 77  LEU C CG    1 
ATOM   4078 C  CD1   . LEU C 1 77  ? 8.707   35.760  27.900  1.00 56.23  ? 77  LEU C CD1   1 
ATOM   4079 C  CD2   . LEU C 1 77  ? 7.339   35.598  25.819  1.00 57.25  ? 77  LEU C CD2   1 
ATOM   4080 N  N     . ILE C 1 78  ? 4.720   32.170  28.808  1.00 63.21  ? 78  ILE C N     1 
ATOM   4081 C  CA    . ILE C 1 78  ? 4.451   30.769  29.092  1.00 65.35  ? 78  ILE C CA    1 
ATOM   4082 C  C     . ILE C 1 78  ? 3.011   30.383  28.816  1.00 67.12  ? 78  ILE C C     1 
ATOM   4083 O  O     . ILE C 1 78  ? 2.626   29.248  29.060  1.00 68.08  ? 78  ILE C O     1 
ATOM   4084 C  CB    . ILE C 1 78  ? 4.767   30.406  30.555  1.00 65.44  ? 78  ILE C CB    1 
ATOM   4085 C  CG1   . ILE C 1 78  ? 3.966   31.306  31.499  1.00 65.41  ? 78  ILE C CG1   1 
ATOM   4086 C  CG2   . ILE C 1 78  ? 6.260   30.520  30.806  1.00 65.39  ? 78  ILE C CG2   1 
ATOM   4087 C  CD1   . ILE C 1 78  ? 4.167   31.004  32.972  1.00 64.46  ? 78  ILE C CD1   1 
ATOM   4088 N  N     . ASN C 1 79  ? 2.218   31.327  28.318  1.00 69.41  ? 79  ASN C N     1 
ATOM   4089 C  CA    . ASN C 1 79  ? 0.807   31.078  27.999  1.00 72.03  ? 79  ASN C CA    1 
ATOM   4090 C  C     . ASN C 1 79  ? 0.031   30.473  29.174  1.00 72.70  ? 79  ASN C C     1 
ATOM   4091 O  O     . ASN C 1 79  ? -0.641  29.451  29.028  1.00 72.53  ? 79  ASN C O     1 
ATOM   4092 C  CB    . ASN C 1 79  ? 0.703   30.146  26.788  1.00 73.96  ? 79  ASN C CB    1 
ATOM   4093 C  CG    . ASN C 1 79  ? -0.534  30.413  25.954  1.00 76.94  ? 79  ASN C CG    1 
ATOM   4094 O  OD1   . ASN C 1 79  ? -0.802  29.719  24.972  1.00 79.60  ? 79  ASN C OD1   1 
ATOM   4095 N  ND2   . ASN C 1 79  ? -1.292  31.431  26.335  1.00 78.12  ? 79  ASN C ND2   1 
ATOM   4096 N  N     . ALA C 1 80  ? 0.122   31.119  30.333  1.00 73.51  ? 80  ALA C N     1 
ATOM   4097 C  CA    . ALA C 1 80  ? -0.542  30.656  31.543  1.00 73.79  ? 80  ALA C CA    1 
ATOM   4098 C  C     . ALA C 1 80  ? -2.037  30.951  31.564  1.00 75.22  ? 80  ALA C C     1 
ATOM   4099 O  O     . ALA C 1 80  ? -2.465  32.075  31.298  1.00 75.29  ? 80  ALA C O     1 
ATOM   4100 C  CB    . ALA C 1 80  ? 0.122   31.280  32.763  1.00 71.90  ? 80  ALA C CB    1 
ATOM   4101 N  N     . LYS C 1 81  ? -2.825  29.930  31.894  1.00 77.03  ? 81  LYS C N     1 
ATOM   4102 C  CA    . LYS C 1 81  ? -4.275  30.060  31.979  1.00 78.23  ? 81  LYS C CA    1 
ATOM   4103 C  C     . LYS C 1 81  ? -4.744  29.705  33.392  1.00 78.51  ? 81  LYS C C     1 
ATOM   4104 O  O     . LYS C 1 81  ? -5.481  30.474  34.018  1.00 79.13  ? 81  LYS C O     1 
ATOM   4105 C  CB    . LYS C 1 81  ? -4.940  29.157  30.938  1.00 79.48  ? 81  LYS C CB    1 
ATOM   4106 C  CG    . LYS C 1 81  ? -4.468  29.471  29.524  1.00 81.74  ? 81  LYS C CG    1 
ATOM   4107 C  CD    . LYS C 1 81  ? -5.038  28.543  28.462  1.00 83.54  ? 81  LYS C CD    1 
ATOM   4108 C  CE    . LYS C 1 81  ? -4.503  28.934  27.079  1.00 85.53  ? 81  LYS C CE    1 
ATOM   4109 N  NZ    . LYS C 1 81  ? -5.145  28.179  25.952  1.00 87.76  ? 81  LYS C NZ    1 
ATOM   4110 N  N     . ASN C 1 82  ? -4.305  28.556  33.903  1.00 77.48  ? 82  ASN C N     1 
ATOM   4111 C  CA    . ASN C 1 82  ? -4.684  28.138  35.254  1.00 76.34  ? 82  ASN C CA    1 
ATOM   4112 C  C     . ASN C 1 82  ? -3.539  28.434  36.236  1.00 75.13  ? 82  ASN C C     1 
ATOM   4113 O  O     . ASN C 1 82  ? -2.596  27.652  36.371  1.00 73.76  ? 82  ASN C O     1 
ATOM   4114 C  CB    . ASN C 1 82  ? -5.050  26.640  35.255  1.00 76.01  ? 82  ASN C CB    1 
ATOM   4115 C  CG    . ASN C 1 82  ? -5.654  26.173  36.579  1.00 75.83  ? 82  ASN C CG    1 
ATOM   4116 O  OD1   . ASN C 1 82  ? -6.361  26.921  37.263  1.00 74.78  ? 82  ASN C OD1   1 
ATOM   4117 N  ND2   . ASN C 1 82  ? -5.386  24.923  36.935  1.00 75.75  ? 82  ASN C ND2   1 
ATOM   4118 N  N     . THR C 1 83  ? -3.627  29.574  36.917  1.00 74.48  ? 83  THR C N     1 
ATOM   4119 C  CA    . THR C 1 83  ? -2.591  29.976  37.867  1.00 74.12  ? 83  THR C CA    1 
ATOM   4120 C  C     . THR C 1 83  ? -3.044  29.975  39.323  1.00 75.04  ? 83  THR C C     1 
ATOM   4121 O  O     . THR C 1 83  ? -4.231  29.853  39.622  1.00 75.70  ? 83  THR C O     1 
ATOM   4122 C  CB    . THR C 1 83  ? -2.046  31.391  37.534  1.00 72.67  ? 83  THR C CB    1 
ATOM   4123 O  OG1   . THR C 1 83  ? -2.453  32.327  38.537  1.00 68.77  ? 83  THR C OG1   1 
ATOM   4124 C  CG2   . THR C 1 83  ? -2.572  31.851  36.199  1.00 72.75  ? 83  THR C CG2   1 
ATOM   4125 N  N     . MET C 1 84  ? -2.075  30.114  40.221  1.00 75.80  ? 84  MET C N     1 
ATOM   4126 C  CA    . MET C 1 84  ? -2.321  30.151  41.654  1.00 75.97  ? 84  MET C CA    1 
ATOM   4127 C  C     . MET C 1 84  ? -1.348  31.145  42.263  1.00 76.80  ? 84  MET C C     1 
ATOM   4128 O  O     . MET C 1 84  ? -0.166  31.145  41.925  1.00 76.10  ? 84  MET C O     1 
ATOM   4129 C  CB    . MET C 1 84  ? -2.081  28.778  42.279  1.00 76.60  ? 84  MET C CB    1 
ATOM   4130 C  CG    . MET C 1 84  ? -2.337  28.724  43.781  1.00 77.50  ? 84  MET C CG    1 
ATOM   4131 S  SD    . MET C 1 84  ? -1.570  27.299  44.596  1.00 80.68  ? 84  MET C SD    1 
ATOM   4132 C  CE    . MET C 1 84  ? -2.265  25.921  43.619  1.00 77.34  ? 84  MET C CE    1 
ATOM   4133 N  N     . GLU C 1 85  ? -1.851  31.990  43.157  1.00 78.54  ? 85  GLU C N     1 
ATOM   4134 C  CA    . GLU C 1 85  ? -1.028  32.989  43.835  1.00 79.80  ? 85  GLU C CA    1 
ATOM   4135 C  C     . GLU C 1 85  ? -1.165  32.821  45.331  1.00 80.28  ? 85  GLU C C     1 
ATOM   4136 O  O     . GLU C 1 85  ? -2.270  32.850  45.858  1.00 81.12  ? 85  GLU C O     1 
ATOM   4137 C  CB    . GLU C 1 85  ? -1.468  34.405  43.465  1.00 80.56  ? 85  GLU C CB    1 
ATOM   4138 C  CG    . GLU C 1 85  ? -0.847  35.470  44.347  1.00 82.01  ? 85  GLU C CG    1 
ATOM   4139 C  CD    . GLU C 1 85  ? -0.669  36.787  43.617  1.00 84.53  ? 85  GLU C CD    1 
ATOM   4140 O  OE1   . GLU C 1 85  ? -0.100  36.760  42.498  1.00 84.59  ? 85  GLU C OE1   1 
ATOM   4141 O  OE2   . GLU C 1 85  ? -1.083  37.845  44.155  1.00 84.92  ? 85  GLU C OE2   1 
ATOM   4142 N  N     . ILE C 1 86  ? -0.042  32.659  46.014  1.00 80.15  ? 86  ILE C N     1 
ATOM   4143 C  CA    . ILE C 1 86  ? -0.048  32.489  47.457  1.00 79.88  ? 86  ILE C CA    1 
ATOM   4144 C  C     . ILE C 1 86  ? 0.637   33.677  48.111  1.00 79.98  ? 86  ILE C C     1 
ATOM   4145 O  O     . ILE C 1 86  ? 1.861   33.769  48.134  1.00 80.13  ? 86  ILE C O     1 
ATOM   4146 C  CB    . ILE C 1 86  ? 0.678   31.185  47.845  1.00 80.75  ? 86  ILE C CB    1 
ATOM   4147 C  CG1   . ILE C 1 86  ? -0.174  29.987  47.417  1.00 80.60  ? 86  ILE C CG1   1 
ATOM   4148 C  CG2   . ILE C 1 86  ? 0.998   31.172  49.334  1.00 79.79  ? 86  ILE C CG2   1 
ATOM   4149 C  CD1   . ILE C 1 86  ? 0.515   28.649  47.575  1.00 81.15  ? 86  ILE C CD1   1 
ATOM   4150 N  N     . GLY C 1 87  ? -0.163  34.590  48.643  1.00 80.21  ? 87  GLY C N     1 
ATOM   4151 C  CA    . GLY C 1 87  ? 0.392   35.769  49.283  1.00 81.01  ? 87  GLY C CA    1 
ATOM   4152 C  C     . GLY C 1 87  ? -0.056  37.019  48.553  1.00 81.81  ? 87  GLY C C     1 
ATOM   4153 O  O     . GLY C 1 87  ? 0.655   37.518  47.678  1.00 82.83  ? 87  GLY C O     1 
ATOM   4154 N  N     . VAL C 1 88  ? -1.229  37.534  48.910  1.00 81.19  ? 88  VAL C N     1 
ATOM   4155 C  CA    . VAL C 1 88  ? -1.763  38.711  48.243  1.00 79.89  ? 88  VAL C CA    1 
ATOM   4156 C  C     . VAL C 1 88  ? -1.382  40.048  48.867  1.00 79.93  ? 88  VAL C C     1 
ATOM   4157 O  O     . VAL C 1 88  ? -0.287  40.539  48.635  1.00 79.67  ? 88  VAL C O     1 
ATOM   4158 C  CB    . VAL C 1 88  ? -3.289  38.609  48.120  1.00 79.22  ? 88  VAL C CB    1 
ATOM   4159 C  CG1   . VAL C 1 88  ? -3.825  39.801  47.352  1.00 79.79  ? 88  VAL C CG1   1 
ATOM   4160 C  CG2   . VAL C 1 88  ? -3.660  37.309  47.416  1.00 77.05  ? 88  VAL C CG2   1 
ATOM   4161 N  N     . TYR C 1 89  ? -2.270  40.635  49.662  1.00 81.17  ? 89  TYR C N     1 
ATOM   4162 C  CA    . TYR C 1 89  ? -2.005  41.939  50.276  1.00 82.17  ? 89  TYR C CA    1 
ATOM   4163 C  C     . TYR C 1 89  ? -2.202  42.982  49.195  1.00 83.28  ? 89  TYR C C     1 
ATOM   4164 O  O     . TYR C 1 89  ? -1.374  43.093  48.290  1.00 85.88  ? 89  TYR C O     1 
ATOM   4165 C  CB    . TYR C 1 89  ? -0.563  42.028  50.802  1.00 81.12  ? 89  TYR C CB    1 
ATOM   4166 C  CG    . TYR C 1 89  ? -0.129  43.415  51.264  1.00 81.03  ? 89  TYR C CG    1 
ATOM   4167 C  CD1   . TYR C 1 89  ? -0.055  44.487  50.373  1.00 80.64  ? 89  TYR C CD1   1 
ATOM   4168 C  CD2   . TYR C 1 89  ? 0.223   43.649  52.595  1.00 81.66  ? 89  TYR C CD2   1 
ATOM   4169 C  CE1   . TYR C 1 89  ? 0.357   45.750  50.791  1.00 80.50  ? 89  TYR C CE1   1 
ATOM   4170 C  CE2   . TYR C 1 89  ? 0.637   44.915  53.024  1.00 80.62  ? 89  TYR C CE2   1 
ATOM   4171 C  CZ    . TYR C 1 89  ? 0.701   45.955  52.117  1.00 80.22  ? 89  TYR C CZ    1 
ATOM   4172 O  OH    . TYR C 1 89  ? 1.111   47.198  52.536  1.00 79.25  ? 89  TYR C OH    1 
ATOM   4173 N  N     . THR C 1 90  ? -3.284  43.750  49.282  1.00 83.23  ? 90  THR C N     1 
ATOM   4174 C  CA    . THR C 1 90  ? -3.558  44.777  48.280  1.00 82.19  ? 90  THR C CA    1 
ATOM   4175 C  C     . THR C 1 90  ? -3.882  44.129  46.939  1.00 81.70  ? 90  THR C C     1 
ATOM   4176 O  O     . THR C 1 90  ? -4.898  44.436  46.323  1.00 81.30  ? 90  THR C O     1 
ATOM   4177 C  CB    . THR C 1 90  ? -2.354  45.698  48.107  1.00 82.00  ? 90  THR C CB    1 
ATOM   4178 O  OG1   . THR C 1 90  ? -2.210  46.515  49.273  1.00 82.73  ? 90  THR C OG1   1 
ATOM   4179 C  CG2   . THR C 1 90  ? -2.527  46.565  46.893  1.00 83.66  ? 90  THR C CG2   1 
ATOM   4180 N  N     . GLY C 1 91  ? -3.002  43.235  46.494  1.00 82.36  ? 91  GLY C N     1 
ATOM   4181 C  CA    . GLY C 1 91  ? -3.204  42.529  45.240  1.00 82.80  ? 91  GLY C CA    1 
ATOM   4182 C  C     . GLY C 1 91  ? -2.483  43.123  44.045  1.00 82.40  ? 91  GLY C C     1 
ATOM   4183 O  O     . GLY C 1 91  ? -3.022  43.124  42.935  1.00 81.63  ? 91  GLY C O     1 
ATOM   4184 N  N     . TYR C 1 92  ? -1.263  43.616  44.255  1.00 82.08  ? 92  TYR C N     1 
ATOM   4185 C  CA    . TYR C 1 92  ? -0.499  44.221  43.162  1.00 81.40  ? 92  TYR C CA    1 
ATOM   4186 C  C     . TYR C 1 92  ? 0.014   43.204  42.137  1.00 79.32  ? 92  TYR C C     1 
ATOM   4187 O  O     . TYR C 1 92  ? -0.095  43.419  40.930  1.00 77.34  ? 92  TYR C O     1 
ATOM   4188 C  CB    . TYR C 1 92  ? 0.667   45.036  43.721  1.00 83.06  ? 92  TYR C CB    1 
ATOM   4189 C  CG    . TYR C 1 92  ? 1.377   45.856  42.675  1.00 84.60  ? 92  TYR C CG    1 
ATOM   4190 C  CD1   . TYR C 1 92  ? 0.659   46.582  41.723  1.00 85.68  ? 92  TYR C CD1   1 
ATOM   4191 C  CD2   . TYR C 1 92  ? 2.765   45.927  42.646  1.00 85.63  ? 92  TYR C CD2   1 
ATOM   4192 C  CE1   . TYR C 1 92  ? 1.308   47.362  40.767  1.00 86.64  ? 92  TYR C CE1   1 
ATOM   4193 C  CE2   . TYR C 1 92  ? 3.425   46.704  41.697  1.00 87.31  ? 92  TYR C CE2   1 
ATOM   4194 C  CZ    . TYR C 1 92  ? 2.693   47.419  40.760  1.00 87.18  ? 92  TYR C CZ    1 
ATOM   4195 O  OH    . TYR C 1 92  ? 3.354   48.192  39.828  1.00 87.62  ? 92  TYR C OH    1 
ATOM   4196 N  N     . SER C 1 93  ? 0.578   42.101  42.619  1.00 78.02  ? 93  SER C N     1 
ATOM   4197 C  CA    . SER C 1 93  ? 1.068   41.063  41.723  1.00 75.89  ? 93  SER C CA    1 
ATOM   4198 C  C     . SER C 1 93  ? -0.137  40.264  41.249  1.00 73.99  ? 93  SER C C     1 
ATOM   4199 O  O     . SER C 1 93  ? -0.090  39.607  40.206  1.00 73.34  ? 93  SER C O     1 
ATOM   4200 C  CB    . SER C 1 93  ? 2.046   40.142  42.446  1.00 76.24  ? 93  SER C CB    1 
ATOM   4201 O  OG    . SER C 1 93  ? 1.404   39.447  43.499  1.00 80.31  ? 93  SER C OG    1 
ATOM   4202 N  N     . LEU C 1 94  ? -1.219  40.337  42.022  1.00 72.23  ? 94  LEU C N     1 
ATOM   4203 C  CA    . LEU C 1 94  ? -2.452  39.628  41.694  1.00 70.82  ? 94  LEU C CA    1 
ATOM   4204 C  C     . LEU C 1 94  ? -3.156  40.336  40.532  1.00 69.75  ? 94  LEU C C     1 
ATOM   4205 O  O     . LEU C 1 94  ? -3.682  39.684  39.623  1.00 67.89  ? 94  LEU C O     1 
ATOM   4206 C  CB    . LEU C 1 94  ? -3.365  39.562  42.936  1.00 71.22  ? 94  LEU C CB    1 
ATOM   4207 C  CG    . LEU C 1 94  ? -4.539  38.560  43.026  1.00 70.46  ? 94  LEU C CG    1 
ATOM   4208 C  CD1   . LEU C 1 94  ? -5.778  39.103  42.336  1.00 70.33  ? 94  LEU C CD1   1 
ATOM   4209 C  CD2   . LEU C 1 94  ? -4.123  37.218  42.434  1.00 69.87  ? 94  LEU C CD2   1 
ATOM   4210 N  N     . LEU C 1 95  ? -3.152  41.669  40.561  1.00 68.85  ? 95  LEU C N     1 
ATOM   4211 C  CA    . LEU C 1 95  ? -3.784  42.454  39.503  1.00 67.80  ? 95  LEU C CA    1 
ATOM   4212 C  C     . LEU C 1 95  ? -3.027  42.160  38.216  1.00 67.69  ? 95  LEU C C     1 
ATOM   4213 O  O     . LEU C 1 95  ? -3.624  41.864  37.173  1.00 66.71  ? 95  LEU C O     1 
ATOM   4214 C  CB    . LEU C 1 95  ? -3.698  43.956  39.805  1.00 66.78  ? 95  LEU C CB    1 
ATOM   4215 C  CG    . LEU C 1 95  ? -4.902  44.788  39.338  1.00 66.53  ? 95  LEU C CG    1 
ATOM   4216 C  CD1   . LEU C 1 95  ? -4.556  46.263  39.379  1.00 65.11  ? 95  LEU C CD1   1 
ATOM   4217 C  CD2   . LEU C 1 95  ? -5.314  44.379  37.937  1.00 65.17  ? 95  LEU C CD2   1 
ATOM   4218 N  N     . ALA C 1 96  ? -1.701  42.251  38.311  1.00 67.36  ? 96  ALA C N     1 
ATOM   4219 C  CA    . ALA C 1 96  ? -0.815  41.983  37.189  1.00 66.31  ? 96  ALA C CA    1 
ATOM   4220 C  C     . ALA C 1 96  ? -1.219  40.649  36.568  1.00 66.47  ? 96  ALA C C     1 
ATOM   4221 O  O     . ALA C 1 96  ? -1.648  40.600  35.415  1.00 67.22  ? 96  ALA C O     1 
ATOM   4222 C  CB    . ALA C 1 96  ? 0.645   41.931  37.670  1.00 64.72  ? 96  ALA C CB    1 
ATOM   4223 N  N     . THR C 1 97  ? -1.103  39.570  37.335  1.00 65.64  ? 97  THR C N     1 
ATOM   4224 C  CA    . THR C 1 97  ? -1.457  38.255  36.815  1.00 65.39  ? 97  THR C CA    1 
ATOM   4225 C  C     . THR C 1 97  ? -2.860  38.234  36.220  1.00 65.34  ? 97  THR C C     1 
ATOM   4226 O  O     . THR C 1 97  ? -3.087  37.628  35.180  1.00 65.09  ? 97  THR C O     1 
ATOM   4227 C  CB    . THR C 1 97  ? -1.376  37.179  37.904  1.00 65.56  ? 97  THR C CB    1 
ATOM   4228 O  OG1   . THR C 1 97  ? -0.120  37.283  38.588  1.00 64.85  ? 97  THR C OG1   1 
ATOM   4229 C  CG2   . THR C 1 97  ? -1.510  35.790  37.280  1.00 64.13  ? 97  THR C CG2   1 
ATOM   4230 N  N     . ALA C 1 98  ? -3.800  38.896  36.884  1.00 66.31  ? 98  ALA C N     1 
ATOM   4231 C  CA    . ALA C 1 98  ? -5.174  38.941  36.399  1.00 67.11  ? 98  ALA C CA    1 
ATOM   4232 C  C     . ALA C 1 98  ? -5.256  39.634  35.039  1.00 66.96  ? 98  ALA C C     1 
ATOM   4233 O  O     . ALA C 1 98  ? -5.896  39.121  34.122  1.00 66.40  ? 98  ALA C O     1 
ATOM   4234 C  CB    . ALA C 1 98  ? -6.063  39.651  37.411  1.00 68.12  ? 98  ALA C CB    1 
ATOM   4235 N  N     . LEU C 1 99  ? -4.614  40.795  34.910  1.00 66.60  ? 99  LEU C N     1 
ATOM   4236 C  CA    . LEU C 1 99  ? -4.607  41.532  33.642  1.00 67.71  ? 99  LEU C CA    1 
ATOM   4237 C  C     . LEU C 1 99  ? -3.793  40.842  32.556  1.00 69.68  ? 99  LEU C C     1 
ATOM   4238 O  O     . LEU C 1 99  ? -4.183  40.850  31.387  1.00 71.07  ? 99  LEU C O     1 
ATOM   4239 C  CB    . LEU C 1 99  ? -4.030  42.932  33.822  1.00 64.04  ? 99  LEU C CB    1 
ATOM   4240 C  CG    . LEU C 1 99  ? -4.992  44.004  34.296  1.00 62.55  ? 99  LEU C CG    1 
ATOM   4241 C  CD1   . LEU C 1 99  ? -4.219  45.273  34.550  1.00 61.18  ? 99  LEU C CD1   1 
ATOM   4242 C  CD2   . LEU C 1 99  ? -6.084  44.210  33.265  1.00 61.18  ? 99  LEU C CD2   1 
ATOM   4243 N  N     . ALA C 1 100 ? -2.662  40.256  32.947  1.00 71.59  ? 100 ALA C N     1 
ATOM   4244 C  CA    . ALA C 1 100 ? -1.764  39.585  32.011  1.00 73.30  ? 100 ALA C CA    1 
ATOM   4245 C  C     . ALA C 1 100 ? -2.325  38.292  31.415  1.00 74.64  ? 100 ALA C C     1 
ATOM   4246 O  O     . ALA C 1 100 ? -2.216  38.069  30.203  1.00 74.60  ? 100 ALA C O     1 
ATOM   4247 C  CB    . ALA C 1 100 ? -0.417  39.317  32.684  1.00 72.22  ? 100 ALA C CB    1 
ATOM   4248 N  N     . ILE C 1 101 ? -2.922  37.441  32.249  1.00 76.26  ? 101 ILE C N     1 
ATOM   4249 C  CA    . ILE C 1 101 ? -3.487  36.181  31.754  1.00 77.21  ? 101 ILE C CA    1 
ATOM   4250 C  C     . ILE C 1 101 ? -4.718  36.454  30.895  1.00 78.43  ? 101 ILE C C     1 
ATOM   4251 O  O     . ILE C 1 101 ? -5.199  37.586  30.820  1.00 77.36  ? 101 ILE C O     1 
ATOM   4252 C  CB    . ILE C 1 101 ? -3.903  35.238  32.899  1.00 76.65  ? 101 ILE C CB    1 
ATOM   4253 C  CG1   . ILE C 1 101 ? -5.013  35.885  33.723  1.00 76.80  ? 101 ILE C CG1   1 
ATOM   4254 C  CG2   . ILE C 1 101 ? -2.704  34.909  33.772  1.00 76.41  ? 101 ILE C CG2   1 
ATOM   4255 C  CD1   . ILE C 1 101 ? -5.680  34.933  34.666  1.00 77.07  ? 101 ILE C CD1   1 
ATOM   4256 N  N     . PRO C 1 102 ? -5.237  35.418  30.223  1.00 80.51  ? 102 PRO C N     1 
ATOM   4257 C  CA    . PRO C 1 102 ? -6.420  35.604  29.376  1.00 83.62  ? 102 PRO C CA    1 
ATOM   4258 C  C     . PRO C 1 102 ? -7.752  35.709  30.129  1.00 87.50  ? 102 PRO C C     1 
ATOM   4259 O  O     . PRO C 1 102 ? -7.851  35.324  31.299  1.00 88.05  ? 102 PRO C O     1 
ATOM   4260 C  CB    . PRO C 1 102 ? -6.362  34.399  28.438  1.00 81.68  ? 102 PRO C CB    1 
ATOM   4261 C  CG    . PRO C 1 102 ? -5.706  33.361  29.270  1.00 80.43  ? 102 PRO C CG    1 
ATOM   4262 C  CD    . PRO C 1 102 ? -4.605  34.113  29.964  1.00 79.88  ? 102 PRO C CD    1 
ATOM   4263 N  N     . GLU C 1 103 ? -8.765  36.248  29.444  1.00 91.76  ? 103 GLU C N     1 
ATOM   4264 C  CA    . GLU C 1 103 ? -10.114 36.423  29.999  1.00 94.78  ? 103 GLU C CA    1 
ATOM   4265 C  C     . GLU C 1 103 ? -10.689 35.058  30.345  1.00 95.36  ? 103 GLU C C     1 
ATOM   4266 O  O     . GLU C 1 103 ? -11.550 34.924  31.217  1.00 94.84  ? 103 GLU C O     1 
ATOM   4267 C  CB    . GLU C 1 103 ? -11.030 37.103  28.974  1.00 96.67  ? 103 GLU C CB    1 
ATOM   4268 C  CG    . GLU C 1 103 ? -11.737 38.356  29.480  1.00 100.86 ? 103 GLU C CG    1 
ATOM   4269 C  CD    . GLU C 1 103 ? -10.781 39.527  29.699  1.00 104.22 ? 103 GLU C CD    1 
ATOM   4270 O  OE1   . GLU C 1 103 ? -9.922  39.438  30.610  1.00 105.02 ? 103 GLU C OE1   1 
ATOM   4271 O  OE2   . GLU C 1 103 ? -10.888 40.536  28.954  1.00 105.55 ? 103 GLU C OE2   1 
ATOM   4272 N  N     . ASP C 1 104 ? -10.189 34.054  29.634  1.00 96.37  ? 104 ASP C N     1 
ATOM   4273 C  CA    . ASP C 1 104 ? -10.592 32.671  29.800  1.00 97.57  ? 104 ASP C CA    1 
ATOM   4274 C  C     . ASP C 1 104 ? -10.216 32.144  31.185  1.00 98.11  ? 104 ASP C C     1 
ATOM   4275 O  O     . ASP C 1 104 ? -10.942 32.344  32.157  1.00 98.73  ? 104 ASP C O     1 
ATOM   4276 C  CB    . ASP C 1 104 ? -9.911  31.828  28.725  1.00 98.81  ? 104 ASP C CB    1 
ATOM   4277 C  CG    . ASP C 1 104 ? -10.430 30.413  28.682  1.00 100.63 ? 104 ASP C CG    1 
ATOM   4278 O  OD1   . ASP C 1 104 ? -10.562 29.797  29.766  1.00 100.19 ? 104 ASP C OD1   1 
ATOM   4279 O  OD2   . ASP C 1 104 ? -10.696 29.919  27.560  1.00 101.69 ? 104 ASP C OD2   1 
ATOM   4280 N  N     . GLY C 1 105 ? -9.072  31.471  31.259  1.00 98.38  ? 105 GLY C N     1 
ATOM   4281 C  CA    . GLY C 1 105 ? -8.592  30.907  32.508  1.00 98.15  ? 105 GLY C CA    1 
ATOM   4282 C  C     . GLY C 1 105 ? -8.813  31.751  33.747  1.00 98.13  ? 105 GLY C C     1 
ATOM   4283 O  O     . GLY C 1 105 ? -9.107  32.942  33.667  1.00 97.76  ? 105 GLY C O     1 
ATOM   4284 N  N     . LYS C 1 106 ? -8.647  31.122  34.903  1.00 98.79  ? 106 LYS C N     1 
ATOM   4285 C  CA    . LYS C 1 106 ? -8.850  31.794  36.176  1.00 99.76  ? 106 LYS C CA    1 
ATOM   4286 C  C     . LYS C 1 106 ? -7.608  31.719  37.063  1.00 99.76  ? 106 LYS C C     1 
ATOM   4287 O  O     . LYS C 1 106 ? -6.713  30.900  36.835  1.00 99.22  ? 106 LYS C O     1 
ATOM   4288 C  CB    . LYS C 1 106 ? -10.043 31.154  36.891  1.00 101.26 ? 106 LYS C CB    1 
ATOM   4289 C  CG    . LYS C 1 106 ? -11.283 31.000  36.005  1.00 102.23 ? 106 LYS C CG    1 
ATOM   4290 C  CD    . LYS C 1 106 ? -12.224 29.927  36.543  1.00 103.30 ? 106 LYS C CD    1 
ATOM   4291 C  CE    . LYS C 1 106 ? -11.540 28.556  36.591  1.00 103.79 ? 106 LYS C CE    1 
ATOM   4292 N  NZ    . LYS C 1 106 ? -12.418 27.478  37.137  1.00 102.89 ? 106 LYS C NZ    1 
ATOM   4293 N  N     . ILE C 1 107 ? -7.570  32.578  38.078  1.00 99.91  ? 107 ILE C N     1 
ATOM   4294 C  CA    . ILE C 1 107 ? -6.453  32.635  39.012  1.00 100.60 ? 107 ILE C CA    1 
ATOM   4295 C  C     . ILE C 1 107 ? -6.863  32.206  40.405  1.00 101.58 ? 107 ILE C C     1 
ATOM   4296 O  O     . ILE C 1 107 ? -7.523  32.963  41.112  1.00 102.35 ? 107 ILE C O     1 
ATOM   4297 C  CB    . ILE C 1 107 ? -5.904  34.064  39.153  1.00 100.81 ? 107 ILE C CB    1 
ATOM   4298 C  CG1   . ILE C 1 107 ? -5.289  34.525  37.835  1.00 101.49 ? 107 ILE C CG1   1 
ATOM   4299 C  CG2   . ILE C 1 107 ? -4.879  34.118  40.279  1.00 100.48 ? 107 ILE C CG2   1 
ATOM   4300 C  CD1   . ILE C 1 107 ? -4.838  35.974  37.849  1.00 101.70 ? 107 ILE C CD1   1 
ATOM   4301 N  N     . LEU C 1 108 ? -6.476  31.000  40.804  1.00 102.34 ? 108 LEU C N     1 
ATOM   4302 C  CA    . LEU C 1 108 ? -6.782  30.518  42.147  1.00 102.65 ? 108 LEU C CA    1 
ATOM   4303 C  C     . LEU C 1 108 ? -5.924  31.421  43.038  1.00 102.71 ? 108 LEU C C     1 
ATOM   4304 O  O     . LEU C 1 108 ? -4.819  31.053  43.426  1.00 102.11 ? 108 LEU C O     1 
ATOM   4305 C  CB    . LEU C 1 108 ? -6.344  29.052  42.288  1.00 103.52 ? 108 LEU C CB    1 
ATOM   4306 C  CG    . LEU C 1 108 ? -6.887  28.105  43.373  1.00 103.70 ? 108 LEU C CG    1 
ATOM   4307 C  CD1   . LEU C 1 108 ? -6.673  28.681  44.772  1.00 102.88 ? 108 LEU C CD1   1 
ATOM   4308 C  CD2   . LEU C 1 108 ? -8.360  27.848  43.106  1.00 103.77 ? 108 LEU C CD2   1 
ATOM   4309 N  N     . ALA C 1 109 ? -6.426  32.616  43.333  1.00 103.57 ? 109 ALA C N     1 
ATOM   4310 C  CA    . ALA C 1 109 ? -5.688  33.576  44.149  1.00 105.12 ? 109 ALA C CA    1 
ATOM   4311 C  C     . ALA C 1 109 ? -5.588  33.120  45.585  1.00 106.17 ? 109 ALA C C     1 
ATOM   4312 O  O     . ALA C 1 109 ? -5.882  33.881  46.504  1.00 105.84 ? 109 ALA C O     1 
ATOM   4313 C  CB    . ALA C 1 109 ? -6.354  34.935  44.087  1.00 104.91 ? 109 ALA C CB    1 
ATOM   4314 N  N     . MET C 1 110 ? -5.154  31.876  45.758  1.00 108.26 ? 110 MET C N     1 
ATOM   4315 C  CA    . MET C 1 110 ? -5.007  31.251  47.070  1.00 110.39 ? 110 MET C CA    1 
ATOM   4316 C  C     . MET C 1 110 ? -5.424  32.163  48.197  1.00 111.41 ? 110 MET C C     1 
ATOM   4317 O  O     . MET C 1 110 ? -6.599  32.192  48.560  1.00 112.64 ? 110 MET C O     1 
ATOM   4318 C  CB    . MET C 1 110 ? -3.565  30.787  47.305  1.00 110.92 ? 110 MET C CB    1 
ATOM   4319 C  CG    . MET C 1 110 ? -3.363  29.967  48.583  1.00 108.51 ? 110 MET C CG    1 
ATOM   4320 S  SD    . MET C 1 110 ? -4.511  28.582  48.712  1.00 106.01 ? 110 MET C SD    1 
ATOM   4321 C  CE    . MET C 1 110 ? -4.295  27.772  47.122  1.00 106.42 ? 110 MET C CE    1 
ATOM   4322 N  N     . ASP C 1 111 ? -4.485  32.927  48.744  1.00 112.04 ? 111 ASP C N     1 
ATOM   4323 C  CA    . ASP C 1 111 ? -4.865  33.789  49.843  1.00 113.54 ? 111 ASP C CA    1 
ATOM   4324 C  C     . ASP C 1 111 ? -3.770  34.607  50.481  1.00 112.89 ? 111 ASP C C     1 
ATOM   4325 O  O     . ASP C 1 111 ? -2.684  34.807  49.938  1.00 112.81 ? 111 ASP C O     1 
ATOM   4326 C  CB    . ASP C 1 111 ? -5.468  32.944  50.952  1.00 116.58 ? 111 ASP C CB    1 
ATOM   4327 C  CG    . ASP C 1 111 ? -4.415  32.131  51.676  1.00 119.62 ? 111 ASP C CG    1 
ATOM   4328 O  OD1   . ASP C 1 111 ? -3.707  31.350  50.994  1.00 119.63 ? 111 ASP C OD1   1 
ATOM   4329 O  OD2   . ASP C 1 111 ? -4.289  32.286  52.916  1.00 121.43 ? 111 ASP C OD2   1 
ATOM   4330 N  N     . ILE C 1 112 ? -4.122  35.046  51.684  1.00 112.10 ? 112 ILE C N     1 
ATOM   4331 C  CA    . ILE C 1 112 ? -3.313  35.834  52.588  1.00 111.30 ? 112 ILE C CA    1 
ATOM   4332 C  C     . ILE C 1 112 ? -4.108  35.671  53.884  1.00 110.95 ? 112 ILE C C     1 
ATOM   4333 O  O     . ILE C 1 112 ? -5.123  34.972  53.901  1.00 109.41 ? 112 ILE C O     1 
ATOM   4334 C  CB    . ILE C 1 112 ? -3.245  37.329  52.139  1.00 111.11 ? 112 ILE C CB    1 
ATOM   4335 C  CG1   . ILE C 1 112 ? -2.561  38.177  53.221  1.00 110.85 ? 112 ILE C CG1   1 
ATOM   4336 C  CG2   . ILE C 1 112 ? -4.639  37.839  51.809  1.00 111.18 ? 112 ILE C CG2   1 
ATOM   4337 C  CD1   . ILE C 1 112 ? -2.260  39.606  52.819  1.00 110.42 ? 112 ILE C CD1   1 
ATOM   4338 N  N     . ASN C 1 113 ? -3.651  36.289  54.965  1.00 111.55 ? 113 ASN C N     1 
ATOM   4339 C  CA    . ASN C 1 113 ? -4.348  36.190  56.240  1.00 111.68 ? 113 ASN C CA    1 
ATOM   4340 C  C     . ASN C 1 113 ? -5.226  37.412  56.516  1.00 111.42 ? 113 ASN C C     1 
ATOM   4341 O  O     . ASN C 1 113 ? -6.391  37.270  56.902  1.00 111.73 ? 113 ASN C O     1 
ATOM   4342 C  CB    . ASN C 1 113 ? -3.334  35.985  57.373  1.00 112.21 ? 113 ASN C CB    1 
ATOM   4343 C  CG    . ASN C 1 113 ? -2.825  34.550  57.446  1.00 112.68 ? 113 ASN C CG    1 
ATOM   4344 O  OD1   . ASN C 1 113 ? -1.901  34.235  58.203  1.00 112.76 ? 113 ASN C OD1   1 
ATOM   4345 N  ND2   . ASN C 1 113 ? -3.437  33.670  56.661  1.00 113.18 ? 113 ASN C ND2   1 
ATOM   4346 N  N     . LYS C 1 114 ? -4.673  38.604  56.307  1.00 110.47 ? 114 LYS C N     1 
ATOM   4347 C  CA    . LYS C 1 114 ? -5.415  39.842  56.531  1.00 109.73 ? 114 LYS C CA    1 
ATOM   4348 C  C     . LYS C 1 114 ? -6.172  40.250  55.263  1.00 108.61 ? 114 LYS C C     1 
ATOM   4349 O  O     . LYS C 1 114 ? -5.918  39.714  54.187  1.00 108.04 ? 114 LYS C O     1 
ATOM   4350 C  CB    . LYS C 1 114 ? -4.450  40.957  56.963  1.00 109.85 ? 114 LYS C CB    1 
ATOM   4351 C  CG    . LYS C 1 114 ? -5.121  42.281  57.342  1.00 110.56 ? 114 LYS C CG    1 
ATOM   4352 C  CD    . LYS C 1 114 ? -6.165  42.099  58.445  1.00 111.10 ? 114 LYS C CD    1 
ATOM   4353 C  CE    . LYS C 1 114 ? -6.717  43.434  58.928  1.00 111.01 ? 114 LYS C CE    1 
ATOM   4354 N  NZ    . LYS C 1 114 ? -5.662  44.256  59.583  1.00 110.88 ? 114 LYS C NZ    1 
ATOM   4355 N  N     . GLU C 1 115 ? -7.110  41.185  55.393  1.00 107.83 ? 115 GLU C N     1 
ATOM   4356 C  CA    . GLU C 1 115 ? -7.872  41.641  54.240  1.00 107.03 ? 115 GLU C CA    1 
ATOM   4357 C  C     . GLU C 1 115 ? -7.443  42.984  53.694  1.00 106.68 ? 115 GLU C C     1 
ATOM   4358 O  O     . GLU C 1 115 ? -8.231  43.933  53.621  1.00 106.00 ? 115 GLU C O     1 
ATOM   4359 C  CB    . GLU C 1 115 ? -9.361  41.661  54.545  1.00 107.34 ? 115 GLU C CB    1 
ATOM   4360 C  CG    . GLU C 1 115 ? -9.950  40.275  54.565  1.00 108.45 ? 115 GLU C CG    1 
ATOM   4361 C  CD    . GLU C 1 115 ? -9.436  39.421  53.421  1.00 108.08 ? 115 GLU C CD    1 
ATOM   4362 O  OE1   . GLU C 1 115 ? -8.230  39.094  53.418  1.00 107.39 ? 115 GLU C OE1   1 
ATOM   4363 O  OE2   . GLU C 1 115 ? -10.237 39.081  52.525  1.00 108.84 ? 115 GLU C OE2   1 
ATOM   4364 N  N     . ASN C 1 116 ? -6.167  43.047  53.324  1.00 105.96 ? 116 ASN C N     1 
ATOM   4365 C  CA    . ASN C 1 116 ? -5.581  44.231  52.726  1.00 104.45 ? 116 ASN C CA    1 
ATOM   4366 C  C     . ASN C 1 116 ? -5.988  44.059  51.269  1.00 103.74 ? 116 ASN C C     1 
ATOM   4367 O  O     . ASN C 1 116 ? -5.921  44.984  50.459  1.00 103.86 ? 116 ASN C O     1 
ATOM   4368 C  CB    . ASN C 1 116 ? -4.065  44.185  52.869  1.00 104.33 ? 116 ASN C CB    1 
ATOM   4369 C  CG    . ASN C 1 116 ? -3.627  44.018  54.304  1.00 104.13 ? 116 ASN C CG    1 
ATOM   4370 O  OD1   . ASN C 1 116 ? -3.840  44.902  55.134  1.00 104.50 ? 116 ASN C OD1   1 
ATOM   4371 N  ND2   . ASN C 1 116 ? -3.017  42.876  54.611  1.00 103.97 ? 116 ASN C ND2   1 
ATOM   4372 N  N     . TYR C 1 117 ? -6.409  42.836  50.963  1.00 102.69 ? 117 TYR C N     1 
ATOM   4373 C  CA    . TYR C 1 117 ? -6.884  42.458  49.644  1.00 101.80 ? 117 TYR C CA    1 
ATOM   4374 C  C     . TYR C 1 117 ? -8.141  43.286  49.409  1.00 101.78 ? 117 TYR C C     1 
ATOM   4375 O  O     . TYR C 1 117 ? -8.465  43.667  48.286  1.00 101.58 ? 117 TYR C O     1 
ATOM   4376 C  CB    . TYR C 1 117 ? -7.213  40.968  49.647  1.00 100.87 ? 117 TYR C CB    1 
ATOM   4377 C  CG    . TYR C 1 117 ? -8.107  40.526  48.528  1.00 100.41 ? 117 TYR C CG    1 
ATOM   4378 C  CD1   . TYR C 1 117 ? -7.678  40.563  47.205  1.00 100.63 ? 117 TYR C CD1   1 
ATOM   4379 C  CD2   . TYR C 1 117 ? -9.387  40.058  48.793  1.00 100.88 ? 117 TYR C CD2   1 
ATOM   4380 C  CE1   . TYR C 1 117 ? -8.509  40.139  46.168  1.00 101.31 ? 117 TYR C CE1   1 
ATOM   4381 C  CE2   . TYR C 1 117 ? -10.225 39.632  47.770  1.00 101.75 ? 117 TYR C CE2   1 
ATOM   4382 C  CZ    . TYR C 1 117 ? -9.783  39.673  46.460  1.00 101.69 ? 117 TYR C CZ    1 
ATOM   4383 O  OH    . TYR C 1 117 ? -10.620 39.239  45.456  1.00 101.75 ? 117 TYR C OH    1 
ATOM   4384 N  N     . GLU C 1 118 ? -8.842  43.560  50.500  1.00 102.19 ? 118 GLU C N     1 
ATOM   4385 C  CA    . GLU C 1 118 ? -10.052 44.363  50.467  1.00 102.03 ? 118 GLU C CA    1 
ATOM   4386 C  C     . GLU C 1 118 ? -9.628  45.781  50.067  1.00 101.01 ? 118 GLU C C     1 
ATOM   4387 O  O     . GLU C 1 118 ? -10.248 46.419  49.216  1.00 101.09 ? 118 GLU C O     1 
ATOM   4388 C  CB    . GLU C 1 118 ? -10.690 44.376  51.863  1.00 103.68 ? 118 GLU C CB    1 
ATOM   4389 C  CG    . GLU C 1 118 ? -12.198 44.110  51.906  1.00 106.09 ? 118 GLU C CG    1 
ATOM   4390 C  CD    . GLU C 1 118 ? -12.580 42.725  51.394  1.00 107.26 ? 118 GLU C CD    1 
ATOM   4391 O  OE1   . GLU C 1 118 ? -11.916 41.742  51.789  1.00 108.36 ? 118 GLU C OE1   1 
ATOM   4392 O  OE2   . GLU C 1 118 ? -13.551 42.618  50.608  1.00 107.47 ? 118 GLU C OE2   1 
ATOM   4393 N  N     . LEU C 1 119 ? -8.550  46.251  50.687  1.00 99.52  ? 119 LEU C N     1 
ATOM   4394 C  CA    . LEU C 1 119 ? -8.002  47.583  50.447  1.00 97.89  ? 119 LEU C CA    1 
ATOM   4395 C  C     . LEU C 1 119 ? -7.721  47.848  48.971  1.00 97.45  ? 119 LEU C C     1 
ATOM   4396 O  O     . LEU C 1 119 ? -7.531  48.996  48.568  1.00 97.60  ? 119 LEU C O     1 
ATOM   4397 C  CB    . LEU C 1 119 ? -6.705  47.755  51.245  1.00 97.10  ? 119 LEU C CB    1 
ATOM   4398 C  CG    . LEU C 1 119 ? -6.343  49.127  51.825  1.00 96.63  ? 119 LEU C CG    1 
ATOM   4399 C  CD1   . LEU C 1 119 ? -5.045  49.006  52.616  1.00 96.43  ? 119 LEU C CD1   1 
ATOM   4400 C  CD2   . LEU C 1 119 ? -6.201  50.156  50.724  1.00 95.95  ? 119 LEU C CD2   1 
ATOM   4401 N  N     . GLY C 1 120 ? -7.694  46.796  48.160  1.00 96.63  ? 120 GLY C N     1 
ATOM   4402 C  CA    . GLY C 1 120 ? -7.411  46.992  46.751  1.00 95.49  ? 120 GLY C CA    1 
ATOM   4403 C  C     . GLY C 1 120 ? -8.360  46.321  45.783  1.00 94.47  ? 120 GLY C C     1 
ATOM   4404 O  O     . GLY C 1 120 ? -8.285  46.554  44.578  1.00 94.44  ? 120 GLY C O     1 
ATOM   4405 N  N     . LEU C 1 121 ? -9.265  45.499  46.300  1.00 93.74  ? 121 LEU C N     1 
ATOM   4406 C  CA    . LEU C 1 121 ? -10.213 44.799  45.445  1.00 93.36  ? 121 LEU C CA    1 
ATOM   4407 C  C     . LEU C 1 121 ? -11.075 45.706  44.556  1.00 92.23  ? 121 LEU C C     1 
ATOM   4408 O  O     . LEU C 1 121 ? -11.557 45.274  43.507  1.00 91.39  ? 121 LEU C O     1 
ATOM   4409 C  CB    . LEU C 1 121 ? -11.108 43.895  46.290  1.00 94.36  ? 121 LEU C CB    1 
ATOM   4410 C  CG    . LEU C 1 121 ? -12.104 43.058  45.486  1.00 96.01  ? 121 LEU C CG    1 
ATOM   4411 C  CD1   . LEU C 1 121 ? -11.381 42.303  44.376  1.00 96.69  ? 121 LEU C CD1   1 
ATOM   4412 C  CD2   . LEU C 1 121 ? -12.815 42.095  46.420  1.00 97.61  ? 121 LEU C CD2   1 
ATOM   4413 N  N     . PRO C 1 122 ? -11.291 46.970  44.963  1.00 91.64  ? 122 PRO C N     1 
ATOM   4414 C  CA    . PRO C 1 122 ? -12.109 47.843  44.116  1.00 91.10  ? 122 PRO C CA    1 
ATOM   4415 C  C     . PRO C 1 122 ? -11.475 48.125  42.752  1.00 90.75  ? 122 PRO C C     1 
ATOM   4416 O  O     . PRO C 1 122 ? -12.168 48.179  41.738  1.00 90.76  ? 122 PRO C O     1 
ATOM   4417 C  CB    . PRO C 1 122 ? -12.256 49.105  44.966  1.00 90.97  ? 122 PRO C CB    1 
ATOM   4418 C  CG    . PRO C 1 122 ? -11.011 49.105  45.803  1.00 90.26  ? 122 PRO C CG    1 
ATOM   4419 C  CD    . PRO C 1 122 ? -10.924 47.664  46.211  1.00 91.11  ? 122 PRO C CD    1 
ATOM   4420 N  N     . VAL C 1 123 ? -10.158 48.299  42.731  1.00 90.39  ? 123 VAL C N     1 
ATOM   4421 C  CA    . VAL C 1 123 ? -9.447  48.570  41.489  1.00 90.15  ? 123 VAL C CA    1 
ATOM   4422 C  C     . VAL C 1 123 ? -9.410  47.334  40.598  1.00 90.35  ? 123 VAL C C     1 
ATOM   4423 O  O     . VAL C 1 123 ? -9.602  47.432  39.387  1.00 89.55  ? 123 VAL C O     1 
ATOM   4424 C  CB    . VAL C 1 123 ? -8.003  49.012  41.754  1.00 90.06  ? 123 VAL C CB    1 
ATOM   4425 C  CG1   . VAL C 1 123 ? -7.357  49.459  40.457  1.00 89.45  ? 123 VAL C CG1   1 
ATOM   4426 C  CG2   . VAL C 1 123 ? -7.983  50.129  42.779  1.00 90.82  ? 123 VAL C CG2   1 
ATOM   4427 N  N     . ILE C 1 124 ? -9.152  46.175  41.201  1.00 90.92  ? 124 ILE C N     1 
ATOM   4428 C  CA    . ILE C 1 124 ? -9.104  44.916  40.459  1.00 91.70  ? 124 ILE C CA    1 
ATOM   4429 C  C     . ILE C 1 124 ? -10.503 44.606  39.942  1.00 92.55  ? 124 ILE C C     1 
ATOM   4430 O  O     . ILE C 1 124 ? -10.679 43.778  39.042  1.00 93.12  ? 124 ILE C O     1 
ATOM   4431 C  CB    . ILE C 1 124 ? -8.627  43.745  41.349  1.00 91.20  ? 124 ILE C CB    1 
ATOM   4432 C  CG1   . ILE C 1 124 ? -7.226  44.041  41.882  1.00 91.43  ? 124 ILE C CG1   1 
ATOM   4433 C  CG2   . ILE C 1 124 ? -8.626  42.445  40.556  1.00 90.20  ? 124 ILE C CG2   1 
ATOM   4434 C  CD1   . ILE C 1 124 ? -6.674  42.970  42.799  1.00 92.04  ? 124 ILE C CD1   1 
ATOM   4435 N  N     . LYS C 1 125 ? -11.492 45.276  40.532  1.00 92.85  ? 125 LYS C N     1 
ATOM   4436 C  CA    . LYS C 1 125 ? -12.889 45.118  40.146  1.00 92.56  ? 125 LYS C CA    1 
ATOM   4437 C  C     . LYS C 1 125 ? -13.199 46.189  39.101  1.00 91.55  ? 125 LYS C C     1 
ATOM   4438 O  O     . LYS C 1 125 ? -13.885 45.928  38.106  1.00 91.05  ? 125 LYS C O     1 
ATOM   4439 C  CB    . LYS C 1 125 ? -13.795 45.268  41.378  1.00 94.17  ? 125 LYS C CB    1 
ATOM   4440 C  CG    . LYS C 1 125 ? -15.283 45.435  41.073  1.00 96.35  ? 125 LYS C CG    1 
ATOM   4441 C  CD    . LYS C 1 125 ? -15.799 44.373  40.101  1.00 98.13  ? 125 LYS C CD    1 
ATOM   4442 C  CE    . LYS C 1 125 ? -17.182 44.741  39.552  1.00 98.31  ? 125 LYS C CE    1 
ATOM   4443 N  NZ    . LYS C 1 125 ? -17.627 43.797  38.488  1.00 97.81  ? 125 LYS C NZ    1 
ATOM   4444 N  N     . LYS C 1 126 ? -12.665 47.387  39.326  1.00 90.01  ? 126 LYS C N     1 
ATOM   4445 C  CA    . LYS C 1 126 ? -12.852 48.504  38.411  1.00 89.05  ? 126 LYS C CA    1 
ATOM   4446 C  C     . LYS C 1 126 ? -12.196 48.219  37.060  1.00 89.31  ? 126 LYS C C     1 
ATOM   4447 O  O     . LYS C 1 126 ? -12.616 48.749  36.034  1.00 89.18  ? 126 LYS C O     1 
ATOM   4448 C  CB    . LYS C 1 126 ? -12.253 49.772  39.002  1.00 88.21  ? 126 LYS C CB    1 
ATOM   4449 C  CG    . LYS C 1 126 ? -12.246 50.931  38.036  1.00 88.01  ? 126 LYS C CG    1 
ATOM   4450 C  CD    . LYS C 1 126 ? -11.541 52.130  38.618  1.00 87.99  ? 126 LYS C CD    1 
ATOM   4451 C  CE    . LYS C 1 126 ? -11.454 53.243  37.598  1.00 88.63  ? 126 LYS C CE    1 
ATOM   4452 N  NZ    . LYS C 1 126 ? -10.753 54.425  38.157  1.00 90.21  ? 126 LYS C NZ    1 
ATOM   4453 N  N     . ALA C 1 127 ? -11.151 47.396  37.072  1.00 89.94  ? 127 ALA C N     1 
ATOM   4454 C  CA    . ALA C 1 127 ? -10.445 47.015  35.851  1.00 89.13  ? 127 ALA C CA    1 
ATOM   4455 C  C     . ALA C 1 127 ? -11.055 45.718  35.349  1.00 89.13  ? 127 ALA C C     1 
ATOM   4456 O  O     . ALA C 1 127 ? -10.398 44.937  34.669  1.00 89.11  ? 127 ALA C O     1 
ATOM   4457 C  CB    . ALA C 1 127 ? -8.965  46.818  36.129  1.00 88.58  ? 127 ALA C CB    1 
ATOM   4458 N  N     . GLY C 1 128 ? -12.318 45.506  35.715  1.00 89.69  ? 128 GLY C N     1 
ATOM   4459 C  CA    . GLY C 1 128 ? -13.067 44.325  35.314  1.00 90.51  ? 128 GLY C CA    1 
ATOM   4460 C  C     . GLY C 1 128 ? -12.290 43.067  34.981  1.00 90.62  ? 128 GLY C C     1 
ATOM   4461 O  O     . GLY C 1 128 ? -12.356 42.561  33.860  1.00 90.03  ? 128 GLY C O     1 
ATOM   4462 N  N     . VAL C 1 129 ? -11.559 42.550  35.959  1.00 91.33  ? 129 VAL C N     1 
ATOM   4463 C  CA    . VAL C 1 129 ? -10.777 41.343  35.752  1.00 92.14  ? 129 VAL C CA    1 
ATOM   4464 C  C     . VAL C 1 129 ? -10.838 40.465  37.002  1.00 91.98  ? 129 VAL C C     1 
ATOM   4465 O  O     . VAL C 1 129 ? -10.229 39.390  37.052  1.00 92.07  ? 129 VAL C O     1 
ATOM   4466 C  CB    . VAL C 1 129 ? -9.309  41.689  35.431  1.00 93.15  ? 129 VAL C CB    1 
ATOM   4467 C  CG1   . VAL C 1 129 ? -8.590  42.150  36.701  1.00 93.85  ? 129 VAL C CG1   1 
ATOM   4468 C  CG2   . VAL C 1 129 ? -8.621  40.489  34.792  1.00 94.04  ? 129 VAL C CG2   1 
ATOM   4469 N  N     . ASP C 1 130 ? -11.578 40.940  38.006  1.00 91.45  ? 130 ASP C N     1 
ATOM   4470 C  CA    . ASP C 1 130 ? -11.754 40.213  39.261  1.00 90.28  ? 130 ASP C CA    1 
ATOM   4471 C  C     . ASP C 1 130 ? -12.526 38.913  39.045  1.00 89.04  ? 130 ASP C C     1 
ATOM   4472 O  O     . ASP C 1 130 ? -12.394 37.976  39.826  1.00 88.65  ? 130 ASP C O     1 
ATOM   4473 C  CB    . ASP C 1 130 ? -12.482 41.084  40.299  1.00 90.97  ? 130 ASP C CB    1 
ATOM   4474 C  CG    . ASP C 1 130 ? -13.794 41.665  39.776  1.00 92.23  ? 130 ASP C CG    1 
ATOM   4475 O  OD1   . ASP C 1 130 ? -13.750 42.587  38.929  1.00 93.09  ? 130 ASP C OD1   1 
ATOM   4476 O  OD2   . ASP C 1 130 ? -14.873 41.202  40.208  1.00 91.68  ? 130 ASP C OD2   1 
ATOM   4477 N  N     . HIS C 1 131 ? -13.310 38.856  37.972  1.00 87.87  ? 131 HIS C N     1 
ATOM   4478 C  CA    . HIS C 1 131 ? -14.104 37.675  37.651  1.00 87.46  ? 131 HIS C CA    1 
ATOM   4479 C  C     . HIS C 1 131 ? -13.251 36.426  37.416  1.00 88.10  ? 131 HIS C C     1 
ATOM   4480 O  O     . HIS C 1 131 ? -13.772 35.366  37.060  1.00 87.33  ? 131 HIS C O     1 
ATOM   4481 C  CB    . HIS C 1 131 ? -14.946 37.941  36.406  1.00 87.31  ? 131 HIS C CB    1 
ATOM   4482 C  CG    . HIS C 1 131 ? -14.169 37.889  35.127  1.00 87.71  ? 131 HIS C CG    1 
ATOM   4483 N  ND1   . HIS C 1 131 ? -13.295 38.884  34.743  1.00 87.35  ? 131 HIS C ND1   1 
ATOM   4484 C  CD2   . HIS C 1 131 ? -14.122 36.949  34.152  1.00 87.49  ? 131 HIS C CD2   1 
ATOM   4485 C  CE1   . HIS C 1 131 ? -12.745 38.559  33.586  1.00 88.18  ? 131 HIS C CE1   1 
ATOM   4486 N  NE2   . HIS C 1 131 ? -13.229 37.389  33.206  1.00 87.45  ? 131 HIS C NE2   1 
ATOM   4487 N  N     . LYS C 1 132 ? -11.941 36.563  37.605  1.00 89.60  ? 132 LYS C N     1 
ATOM   4488 C  CA    . LYS C 1 132 ? -10.994 35.459  37.412  1.00 90.09  ? 132 LYS C CA    1 
ATOM   4489 C  C     . LYS C 1 132 ? -10.414 34.963  38.737  1.00 90.19  ? 132 LYS C C     1 
ATOM   4490 O  O     . LYS C 1 132 ? -9.798  33.895  38.790  1.00 90.13  ? 132 LYS C O     1 
ATOM   4491 C  CB    . LYS C 1 132 ? -9.820  35.896  36.526  1.00 90.11  ? 132 LYS C CB    1 
ATOM   4492 C  CG    . LYS C 1 132 ? -10.166 36.367  35.131  1.00 89.06  ? 132 LYS C CG    1 
ATOM   4493 C  CD    . LYS C 1 132 ? -8.886  36.745  34.404  1.00 88.77  ? 132 LYS C CD    1 
ATOM   4494 C  CE    . LYS C 1 132 ? -9.159  37.343  33.041  1.00 88.13  ? 132 LYS C CE    1 
ATOM   4495 N  NZ    . LYS C 1 132 ? -7.894  37.680  32.338  1.00 87.42  ? 132 LYS C NZ    1 
ATOM   4496 N  N     . ILE C 1 133 ? -10.592 35.746  39.798  1.00 89.94  ? 133 ILE C N     1 
ATOM   4497 C  CA    . ILE C 1 133 ? -10.069 35.373  41.103  1.00 89.45  ? 133 ILE C CA    1 
ATOM   4498 C  C     . ILE C 1 133 ? -10.976 34.383  41.840  1.00 90.57  ? 133 ILE C C     1 
ATOM   4499 O  O     . ILE C 1 133 ? -12.187 34.304  41.597  1.00 90.54  ? 133 ILE C O     1 
ATOM   4500 C  CB    . ILE C 1 133 ? -9.843  36.611  41.999  1.00 88.18  ? 133 ILE C CB    1 
ATOM   4501 C  CG1   . ILE C 1 133 ? -8.842  37.564  41.356  1.00 88.19  ? 133 ILE C CG1   1 
ATOM   4502 C  CG2   . ILE C 1 133 ? -9.262  36.193  43.318  1.00 87.56  ? 133 ILE C CG2   1 
ATOM   4503 C  CD1   . ILE C 1 133 ? -9.296  38.138  40.044  1.00 88.92  ? 133 ILE C CD1   1 
ATOM   4504 N  N     . ASP C 1 134 ? -10.350 33.622  42.731  1.00 91.10  ? 134 ASP C N     1 
ATOM   4505 C  CA    . ASP C 1 134 ? -10.998 32.610  43.555  1.00 91.38  ? 134 ASP C CA    1 
ATOM   4506 C  C     . ASP C 1 134 ? -10.334 32.840  44.905  1.00 91.09  ? 134 ASP C C     1 
ATOM   4507 O  O     . ASP C 1 134 ? -9.741  31.938  45.486  1.00 91.38  ? 134 ASP C O     1 
ATOM   4508 C  CB    . ASP C 1 134 ? -10.649 31.213  43.011  1.00 92.67  ? 134 ASP C CB    1 
ATOM   4509 C  CG    . ASP C 1 134 ? -11.261 30.074  43.826  1.00 93.94  ? 134 ASP C CG    1 
ATOM   4510 O  OD1   . ASP C 1 134 ? -11.204 30.108  45.075  1.00 95.63  ? 134 ASP C OD1   1 
ATOM   4511 O  OD2   . ASP C 1 134 ? -11.782 29.120  43.208  1.00 94.23  ? 134 ASP C OD2   1 
ATOM   4512 N  N     . PHE C 1 135 ? -10.411 34.069  45.394  1.00 90.79  ? 135 PHE C N     1 
ATOM   4513 C  CA    . PHE C 1 135 ? -9.778  34.382  46.660  1.00 91.74  ? 135 PHE C CA    1 
ATOM   4514 C  C     . PHE C 1 135 ? -10.292 33.516  47.804  1.00 93.48  ? 135 PHE C C     1 
ATOM   4515 O  O     . PHE C 1 135 ? -11.446 33.063  47.794  1.00 94.16  ? 135 PHE C O     1 
ATOM   4516 C  CB    . PHE C 1 135 ? -9.962  35.860  47.001  1.00 90.14  ? 135 PHE C CB    1 
ATOM   4517 C  CG    . PHE C 1 135 ? -9.185  36.301  48.206  1.00 89.07  ? 135 PHE C CG    1 
ATOM   4518 C  CD1   . PHE C 1 135 ? -9.728  36.202  49.477  1.00 88.84  ? 135 PHE C CD1   1 
ATOM   4519 C  CD2   . PHE C 1 135 ? -7.898  36.796  48.069  1.00 89.64  ? 135 PHE C CD2   1 
ATOM   4520 C  CE1   . PHE C 1 135 ? -9.002  36.593  50.597  1.00 89.07  ? 135 PHE C CE1   1 
ATOM   4521 C  CE2   . PHE C 1 135 ? -7.159  37.190  49.184  1.00 90.12  ? 135 PHE C CE2   1 
ATOM   4522 C  CZ    . PHE C 1 135 ? -7.714  37.088  50.450  1.00 89.82  ? 135 PHE C CZ    1 
ATOM   4523 N  N     . ARG C 1 136 ? -9.405  33.279  48.772  1.00 93.65  ? 136 ARG C N     1 
ATOM   4524 C  CA    . ARG C 1 136 ? -9.691  32.495  49.969  1.00 93.38  ? 136 ARG C CA    1 
ATOM   4525 C  C     . ARG C 1 136 ? -8.916  33.152  51.091  1.00 95.22  ? 136 ARG C C     1 
ATOM   4526 O  O     . ARG C 1 136 ? -8.020  33.946  50.836  1.00 95.59  ? 136 ARG C O     1 
ATOM   4527 C  CB    . ARG C 1 136 ? -9.230  31.055  49.796  1.00 91.04  ? 136 ARG C CB    1 
ATOM   4528 C  CG    . ARG C 1 136 ? -9.885  30.372  48.622  1.00 89.74  ? 136 ARG C CG    1 
ATOM   4529 C  CD    . ARG C 1 136 ? -9.667  28.880  48.655  1.00 88.71  ? 136 ARG C CD    1 
ATOM   4530 N  NE    . ARG C 1 136 ? -10.204 28.250  47.457  1.00 88.82  ? 136 ARG C NE    1 
ATOM   4531 C  CZ    . ARG C 1 136 ? -10.170 26.943  47.227  1.00 89.93  ? 136 ARG C CZ    1 
ATOM   4532 N  NH1   . ARG C 1 136 ? -9.627  26.124  48.122  1.00 90.11  ? 136 ARG C NH1   1 
ATOM   4533 N  NH2   . ARG C 1 136 ? -10.663 26.457  46.095  1.00 90.15  ? 136 ARG C NH2   1 
ATOM   4534 N  N     . GLU C 1 137 ? -9.252  32.832  52.333  1.00 97.58  ? 137 GLU C N     1 
ATOM   4535 C  CA    . GLU C 1 137 ? -8.562  33.446  53.459  1.00 99.81  ? 137 GLU C CA    1 
ATOM   4536 C  C     . GLU C 1 137 ? -7.923  32.412  54.386  1.00 100.62 ? 137 GLU C C     1 
ATOM   4537 O  O     . GLU C 1 137 ? -8.235  31.224  54.309  1.00 100.92 ? 137 GLU C O     1 
ATOM   4538 C  CB    . GLU C 1 137 ? -9.545  34.330  54.232  1.00 100.49 ? 137 GLU C CB    1 
ATOM   4539 C  CG    . GLU C 1 137 ? -8.925  35.084  55.390  1.00 103.44 ? 137 GLU C CG    1 
ATOM   4540 C  CD    . GLU C 1 137 ? -9.918  35.986  56.094  1.00 105.09 ? 137 GLU C CD    1 
ATOM   4541 O  OE1   . GLU C 1 137 ? -11.018 35.501  56.444  1.00 105.64 ? 137 GLU C OE1   1 
ATOM   4542 O  OE2   . GLU C 1 137 ? -9.594  37.177  56.306  1.00 106.15 ? 137 GLU C OE2   1 
ATOM   4543 N  N     . GLY C 1 138 ? -7.014  32.866  55.245  1.00 101.45 ? 138 GLY C N     1 
ATOM   4544 C  CA    . GLY C 1 138 ? -6.356  31.966  56.179  1.00 102.77 ? 138 GLY C CA    1 
ATOM   4545 C  C     . GLY C 1 138 ? -5.344  31.034  55.540  1.00 103.64 ? 138 GLY C C     1 
ATOM   4546 O  O     . GLY C 1 138 ? -5.521  30.638  54.391  1.00 103.21 ? 138 GLY C O     1 
ATOM   4547 N  N     . PRO C 1 139 ? -4.281  30.645  56.271  1.00 104.63 ? 139 PRO C N     1 
ATOM   4548 C  CA    . PRO C 1 139 ? -3.226  29.754  55.779  1.00 105.37 ? 139 PRO C CA    1 
ATOM   4549 C  C     . PRO C 1 139 ? -3.603  28.799  54.648  1.00 105.65 ? 139 PRO C C     1 
ATOM   4550 O  O     . PRO C 1 139 ? -4.676  28.189  54.649  1.00 104.99 ? 139 PRO C O     1 
ATOM   4551 C  CB    . PRO C 1 139 ? -2.779  29.041  57.048  1.00 105.11 ? 139 PRO C CB    1 
ATOM   4552 C  CG    . PRO C 1 139 ? -2.779  30.175  58.023  1.00 104.85 ? 139 PRO C CG    1 
ATOM   4553 C  CD    . PRO C 1 139 ? -4.110  30.879  57.719  1.00 104.92 ? 139 PRO C CD    1 
ATOM   4554 N  N     . ALA C 1 140 ? -2.693  28.692  53.682  1.00 105.96 ? 140 ALA C N     1 
ATOM   4555 C  CA    . ALA C 1 140 ? -2.872  27.843  52.515  1.00 105.95 ? 140 ALA C CA    1 
ATOM   4556 C  C     . ALA C 1 140 ? -2.243  26.480  52.744  1.00 105.80 ? 140 ALA C C     1 
ATOM   4557 O  O     . ALA C 1 140 ? -2.642  25.492  52.121  1.00 105.47 ? 140 ALA C O     1 
ATOM   4558 C  CB    . ALA C 1 140 ? -2.248  28.507  51.293  1.00 106.53 ? 140 ALA C CB    1 
ATOM   4559 N  N     . LEU C 1 141 ? -1.253  26.437  53.632  1.00 105.59 ? 141 LEU C N     1 
ATOM   4560 C  CA    . LEU C 1 141 ? -0.566  25.193  53.961  1.00 105.83 ? 141 LEU C CA    1 
ATOM   4561 C  C     . LEU C 1 141 ? -1.599  24.064  54.005  1.00 106.39 ? 141 LEU C C     1 
ATOM   4562 O  O     . LEU C 1 141 ? -1.383  22.995  53.430  1.00 105.96 ? 141 LEU C O     1 
ATOM   4563 C  CB    . LEU C 1 141 ? 0.147   25.330  55.309  1.00 105.58 ? 141 LEU C CB    1 
ATOM   4564 C  CG    . LEU C 1 141 ? 1.037   26.569  55.502  1.00 106.10 ? 141 LEU C CG    1 
ATOM   4565 C  CD1   . LEU C 1 141 ? 0.193   27.847  55.630  1.00 104.78 ? 141 LEU C CD1   1 
ATOM   4566 C  CD2   . LEU C 1 141 ? 1.877   26.377  56.753  1.00 106.02 ? 141 LEU C CD2   1 
ATOM   4567 N  N     . PRO C 1 142 ? -2.743  24.293  54.687  1.00 107.28 ? 142 PRO C N     1 
ATOM   4568 C  CA    . PRO C 1 142 ? -3.809  23.288  54.790  1.00 107.27 ? 142 PRO C CA    1 
ATOM   4569 C  C     . PRO C 1 142 ? -4.417  22.927  53.433  1.00 107.32 ? 142 PRO C C     1 
ATOM   4570 O  O     . PRO C 1 142 ? -4.439  21.758  53.044  1.00 107.82 ? 142 PRO C O     1 
ATOM   4571 C  CB    . PRO C 1 142 ? -4.830  23.963  55.703  1.00 106.58 ? 142 PRO C CB    1 
ATOM   4572 C  CG    . PRO C 1 142 ? -3.969  24.770  56.609  1.00 106.93 ? 142 PRO C CG    1 
ATOM   4573 C  CD    . PRO C 1 142 ? -2.992  25.394  55.640  1.00 107.37 ? 142 PRO C CD    1 
ATOM   4574 N  N     . VAL C 1 143 ? -4.901  23.940  52.720  1.00 107.29 ? 143 VAL C N     1 
ATOM   4575 C  CA    . VAL C 1 143 ? -5.529  23.748  51.415  1.00 107.29 ? 143 VAL C CA    1 
ATOM   4576 C  C     . VAL C 1 143 ? -4.686  22.904  50.457  1.00 107.71 ? 143 VAL C C     1 
ATOM   4577 O  O     . VAL C 1 143 ? -5.222  22.074  49.717  1.00 107.08 ? 143 VAL C O     1 
ATOM   4578 C  CB    . VAL C 1 143 ? -5.827  25.098  50.735  1.00 106.65 ? 143 VAL C CB    1 
ATOM   4579 C  CG1   . VAL C 1 143 ? -6.924  24.920  49.701  1.00 106.29 ? 143 VAL C CG1   1 
ATOM   4580 C  CG2   . VAL C 1 143 ? -6.226  26.131  51.771  1.00 106.17 ? 143 VAL C CG2   1 
ATOM   4581 N  N     . LEU C 1 144 ? -3.372  23.121  50.474  1.00 108.02 ? 144 LEU C N     1 
ATOM   4582 C  CA    . LEU C 1 144 ? -2.458  22.379  49.608  1.00 108.33 ? 144 LEU C CA    1 
ATOM   4583 C  C     . LEU C 1 144 ? -2.404  20.899  49.987  1.00 108.88 ? 144 LEU C C     1 
ATOM   4584 O  O     . LEU C 1 144 ? -2.625  20.029  49.139  1.00 108.15 ? 144 LEU C O     1 
ATOM   4585 C  CB    . LEU C 1 144 ? -1.051  22.995  49.667  1.00 107.77 ? 144 LEU C CB    1 
ATOM   4586 C  CG    . LEU C 1 144 ? -0.665  24.065  48.633  1.00 106.11 ? 144 LEU C CG    1 
ATOM   4587 C  CD1   . LEU C 1 144 ? -1.762  25.098  48.485  1.00 105.57 ? 144 LEU C CD1   1 
ATOM   4588 C  CD2   . LEU C 1 144 ? 0.634   24.722  49.063  1.00 105.44 ? 144 LEU C CD2   1 
ATOM   4589 N  N     . ASP C 1 145 ? -2.108  20.616  51.255  1.00 109.81 ? 145 ASP C N     1 
ATOM   4590 C  CA    . ASP C 1 145 ? -2.044  19.237  51.733  1.00 110.51 ? 145 ASP C CA    1 
ATOM   4591 C  C     . ASP C 1 145 ? -3.327  18.516  51.327  1.00 110.74 ? 145 ASP C C     1 
ATOM   4592 O  O     . ASP C 1 145 ? -3.310  17.339  50.966  1.00 110.32 ? 145 ASP C O     1 
ATOM   4593 C  CB    . ASP C 1 145 ? -1.892  19.209  53.256  1.00 111.00 ? 145 ASP C CB    1 
ATOM   4594 C  CG    . ASP C 1 145 ? -0.530  19.697  53.718  1.00 111.46 ? 145 ASP C CG    1 
ATOM   4595 O  OD1   . ASP C 1 145 ? -0.145  20.822  53.339  1.00 111.94 ? 145 ASP C OD1   1 
ATOM   4596 O  OD2   . ASP C 1 145 ? 0.152   18.958  54.462  1.00 111.08 ? 145 ASP C OD2   1 
ATOM   4597 N  N     . GLU C 1 146 ? -4.437  19.246  51.386  1.00 111.39 ? 146 GLU C N     1 
ATOM   4598 C  CA    . GLU C 1 146 ? -5.744  18.718  51.020  1.00 112.39 ? 146 GLU C CA    1 
ATOM   4599 C  C     . GLU C 1 146 ? -5.804  18.489  49.518  1.00 112.62 ? 146 GLU C C     1 
ATOM   4600 O  O     . GLU C 1 146 ? -6.310  17.467  49.057  1.00 112.38 ? 146 GLU C O     1 
ATOM   4601 C  CB    . GLU C 1 146 ? -6.836  19.704  51.436  1.00 113.48 ? 146 GLU C CB    1 
ATOM   4602 C  CG    . GLU C 1 146 ? -6.879  19.975  52.938  1.00 115.08 ? 146 GLU C CG    1 
ATOM   4603 C  CD    . GLU C 1 146 ? -7.682  18.938  53.715  1.00 115.90 ? 146 GLU C CD    1 
ATOM   4604 O  OE1   . GLU C 1 146 ? -7.483  17.718  53.508  1.00 115.88 ? 146 GLU C OE1   1 
ATOM   4605 O  OE2   . GLU C 1 146 ? -8.516  19.355  54.546  1.00 116.42 ? 146 GLU C OE2   1 
ATOM   4606 N  N     . MET C 1 147 ? -5.285  19.452  48.761  1.00 113.62 ? 147 MET C N     1 
ATOM   4607 C  CA    . MET C 1 147 ? -5.262  19.361  47.302  1.00 114.30 ? 147 MET C CA    1 
ATOM   4608 C  C     . MET C 1 147 ? -4.422  18.166  46.843  1.00 114.15 ? 147 MET C C     1 
ATOM   4609 O  O     . MET C 1 147 ? -4.782  17.463  45.896  1.00 113.12 ? 147 MET C O     1 
ATOM   4610 C  CB    . MET C 1 147 ? -4.681  20.645  46.697  1.00 115.03 ? 147 MET C CB    1 
ATOM   4611 C  CG    . MET C 1 147 ? -5.457  21.910  47.020  1.00 115.94 ? 147 MET C CG    1 
ATOM   4612 S  SD    . MET C 1 147 ? -4.826  23.361  46.134  1.00 116.60 ? 147 MET C SD    1 
ATOM   4613 C  CE    . MET C 1 147 ? -6.081  23.527  44.856  1.00 115.62 ? 147 MET C CE    1 
ATOM   4614 N  N     . ILE C 1 148 ? -3.302  17.949  47.526  1.00 114.24 ? 148 ILE C N     1 
ATOM   4615 C  CA    . ILE C 1 148 ? -2.393  16.854  47.210  1.00 114.52 ? 148 ILE C CA    1 
ATOM   4616 C  C     . ILE C 1 148 ? -3.026  15.476  47.348  1.00 115.37 ? 148 ILE C C     1 
ATOM   4617 O  O     . ILE C 1 148 ? -2.855  14.622  46.476  1.00 115.57 ? 148 ILE C O     1 
ATOM   4618 C  CB    . ILE C 1 148 ? -1.149  16.895  48.114  1.00 114.05 ? 148 ILE C CB    1 
ATOM   4619 C  CG1   . ILE C 1 148 ? -0.279  18.094  47.745  1.00 114.39 ? 148 ILE C CG1   1 
ATOM   4620 C  CG2   . ILE C 1 148 ? -0.361  15.606  47.974  1.00 113.80 ? 148 ILE C CG2   1 
ATOM   4621 C  CD1   . ILE C 1 148 ? 0.279   18.033  46.332  1.00 114.45 ? 148 ILE C CD1   1 
ATOM   4622 N  N     . LYS C 1 149 ? -3.746  15.257  48.445  1.00 116.04 ? 149 LYS C N     1 
ATOM   4623 C  CA    . LYS C 1 149 ? -4.378  13.966  48.686  1.00 116.58 ? 149 LYS C CA    1 
ATOM   4624 C  C     . LYS C 1 149 ? -5.042  13.428  47.425  1.00 116.30 ? 149 LYS C C     1 
ATOM   4625 O  O     . LYS C 1 149 ? -4.927  12.243  47.115  1.00 116.18 ? 149 LYS C O     1 
ATOM   4626 C  CB    . LYS C 1 149 ? -5.400  14.065  49.822  1.00 117.29 ? 149 LYS C CB    1 
ATOM   4627 C  CG    . LYS C 1 149 ? -5.983  12.711  50.226  1.00 117.98 ? 149 LYS C CG    1 
ATOM   4628 C  CD    . LYS C 1 149 ? -4.874  11.699  50.529  1.00 117.91 ? 149 LYS C CD    1 
ATOM   4629 C  CE    . LYS C 1 149 ? -5.426  10.299  50.776  1.00 117.25 ? 149 LYS C CE    1 
ATOM   4630 N  NZ    . LYS C 1 149 ? -4.339  9.312   51.026  1.00 115.74 ? 149 LYS C NZ    1 
ATOM   4631 N  N     . ASP C 1 150 ? -5.740  14.297  46.703  1.00 116.53 ? 150 ASP C N     1 
ATOM   4632 C  CA    . ASP C 1 150 ? -6.381  13.891  45.460  1.00 117.20 ? 150 ASP C CA    1 
ATOM   4633 C  C     . ASP C 1 150 ? -5.247  13.686  44.454  1.00 117.57 ? 150 ASP C C     1 
ATOM   4634 O  O     . ASP C 1 150 ? -4.395  14.560  44.288  1.00 117.86 ? 150 ASP C O     1 
ATOM   4635 C  CB    . ASP C 1 150 ? -7.328  14.992  44.971  1.00 117.60 ? 150 ASP C CB    1 
ATOM   4636 C  CG    . ASP C 1 150 ? -8.050  14.620  43.682  1.00 118.63 ? 150 ASP C CG    1 
ATOM   4637 O  OD1   . ASP C 1 150 ? -7.372  14.286  42.686  1.00 119.14 ? 150 ASP C OD1   1 
ATOM   4638 O  OD2   . ASP C 1 150 ? -9.298  14.668  43.661  1.00 119.04 ? 150 ASP C OD2   1 
ATOM   4639 N  N     . GLU C 1 151 ? -5.222  12.535  43.791  1.00 117.73 ? 151 GLU C N     1 
ATOM   4640 C  CA    . GLU C 1 151 ? -4.165  12.259  42.824  1.00 117.63 ? 151 GLU C CA    1 
ATOM   4641 C  C     . GLU C 1 151 ? -4.473  12.833  41.442  1.00 116.25 ? 151 GLU C C     1 
ATOM   4642 O  O     . GLU C 1 151 ? -4.226  12.190  40.422  1.00 115.40 ? 151 GLU C O     1 
ATOM   4643 C  CB    . GLU C 1 151 ? -3.920  10.748  42.725  1.00 119.82 ? 151 GLU C CB    1 
ATOM   4644 N  N     . LYS C 1 152 ? -5.025  14.043  41.417  1.00 114.92 ? 152 LYS C N     1 
ATOM   4645 C  CA    . LYS C 1 152 ? -5.342  14.711  40.162  1.00 113.77 ? 152 LYS C CA    1 
ATOM   4646 C  C     . LYS C 1 152 ? -5.009  16.194  40.237  1.00 112.68 ? 152 LYS C C     1 
ATOM   4647 O  O     . LYS C 1 152 ? -4.804  16.848  39.212  1.00 112.89 ? 152 LYS C O     1 
ATOM   4648 C  CB    . LYS C 1 152 ? -6.815  14.536  39.786  1.00 114.00 ? 152 LYS C CB    1 
ATOM   4649 C  CG    . LYS C 1 152 ? -7.169  15.165  38.433  1.00 114.30 ? 152 LYS C CG    1 
ATOM   4650 C  CD    . LYS C 1 152 ? -6.220  14.688  37.320  1.00 114.17 ? 152 LYS C CD    1 
ATOM   4651 C  CE    . LYS C 1 152 ? -5.461  15.851  36.666  1.00 113.62 ? 152 LYS C CE    1 
ATOM   4652 N  NZ    . LYS C 1 152 ? -4.365  15.397  35.752  1.00 113.10 ? 152 LYS C NZ    1 
ATOM   4653 N  N     . ASN C 1 153 ? -4.972  16.741  41.445  1.00 110.98 ? 153 ASN C N     1 
ATOM   4654 C  CA    . ASN C 1 153 ? -4.611  18.142  41.589  1.00 109.45 ? 153 ASN C CA    1 
ATOM   4655 C  C     . ASN C 1 153 ? -3.113  18.210  41.286  1.00 107.88 ? 153 ASN C C     1 
ATOM   4656 O  O     . ASN C 1 153 ? -2.512  19.285  41.233  1.00 107.69 ? 153 ASN C O     1 
ATOM   4657 C  CB    . ASN C 1 153 ? -4.905  18.635  43.009  1.00 109.95 ? 153 ASN C CB    1 
ATOM   4658 C  CG    . ASN C 1 153 ? -5.944  19.746  43.038  1.00 109.92 ? 153 ASN C CG    1 
ATOM   4659 O  OD1   . ASN C 1 153 ? -6.190  20.357  44.079  1.00 109.79 ? 153 ASN C OD1   1 
ATOM   4660 N  ND2   . ASN C 1 153 ? -6.559  20.013  41.889  1.00 110.11 ? 153 ASN C ND2   1 
ATOM   4661 N  N     . HIS C 1 154 ? -2.526  17.034  41.080  1.00 105.93 ? 154 HIS C N     1 
ATOM   4662 C  CA    . HIS C 1 154 ? -1.114  16.910  40.765  1.00 103.65 ? 154 HIS C CA    1 
ATOM   4663 C  C     . HIS C 1 154 ? -0.801  17.471  39.386  1.00 101.92 ? 154 HIS C C     1 
ATOM   4664 O  O     . HIS C 1 154 ? -1.316  16.986  38.379  1.00 101.77 ? 154 HIS C O     1 
ATOM   4665 C  CB    . HIS C 1 154 ? -0.683  15.440  40.826  1.00 103.87 ? 154 HIS C CB    1 
ATOM   4666 C  CG    . HIS C 1 154 ? -0.470  14.930  42.217  1.00 104.57 ? 154 HIS C CG    1 
ATOM   4667 N  ND1   . HIS C 1 154 ? 0.600   14.128  42.559  1.00 104.56 ? 154 HIS C ND1   1 
ATOM   4668 C  CD2   . HIS C 1 154 ? -1.175  15.122  43.356  1.00 104.74 ? 154 HIS C CD2   1 
ATOM   4669 C  CE1   . HIS C 1 154 ? 0.546   13.853  43.850  1.00 104.64 ? 154 HIS C CE1   1 
ATOM   4670 N  NE2   . HIS C 1 154 ? -0.522  14.444  44.357  1.00 105.09 ? 154 HIS C NE2   1 
ATOM   4671 N  N     . GLY C 1 155 ? 0.041   18.499  39.352  1.00 100.01 ? 155 GLY C N     1 
ATOM   4672 C  CA    . GLY C 1 155 ? 0.435   19.112  38.095  1.00 97.45  ? 155 GLY C CA    1 
ATOM   4673 C  C     . GLY C 1 155 ? -0.728  19.613  37.270  1.00 95.65  ? 155 GLY C C     1 
ATOM   4674 O  O     . GLY C 1 155 ? -0.951  19.145  36.153  1.00 94.98  ? 155 GLY C O     1 
ATOM   4675 N  N     . SER C 1 156 ? -1.469  20.566  37.823  1.00 94.15  ? 156 SER C N     1 
ATOM   4676 C  CA    . SER C 1 156 ? -2.620  21.134  37.133  1.00 93.17  ? 156 SER C CA    1 
ATOM   4677 C  C     . SER C 1 156 ? -2.522  22.652  37.040  1.00 92.02  ? 156 SER C C     1 
ATOM   4678 O  O     . SER C 1 156 ? -3.356  23.296  36.400  1.00 92.09  ? 156 SER C O     1 
ATOM   4679 C  CB    . SER C 1 156 ? -3.915  20.743  37.854  1.00 93.59  ? 156 SER C CB    1 
ATOM   4680 O  OG    . SER C 1 156 ? -3.911  21.180  39.203  1.00 93.28  ? 156 SER C OG    1 
ATOM   4681 N  N     . TYR C 1 157 ? -1.504  23.216  37.684  1.00 90.25  ? 157 TYR C N     1 
ATOM   4682 C  CA    . TYR C 1 157 ? -1.290  24.657  37.668  1.00 88.28  ? 157 TYR C CA    1 
ATOM   4683 C  C     . TYR C 1 157 ? -0.144  25.024  36.735  1.00 86.37  ? 157 TYR C C     1 
ATOM   4684 O  O     . TYR C 1 157 ? 0.939   24.447  36.795  1.00 87.02  ? 157 TYR C O     1 
ATOM   4685 C  CB    . TYR C 1 157 ? -1.027  25.168  39.086  1.00 90.06  ? 157 TYR C CB    1 
ATOM   4686 C  CG    . TYR C 1 157 ? -2.238  25.006  39.973  1.00 92.42  ? 157 TYR C CG    1 
ATOM   4687 C  CD1   . TYR C 1 157 ? -2.493  23.801  40.627  1.00 93.26  ? 157 TYR C CD1   1 
ATOM   4688 C  CD2   . TYR C 1 157 ? -3.179  26.028  40.086  1.00 93.10  ? 157 TYR C CD2   1 
ATOM   4689 C  CE1   . TYR C 1 157 ? -3.656  23.615  41.364  1.00 94.26  ? 157 TYR C CE1   1 
ATOM   4690 C  CE2   . TYR C 1 157 ? -4.346  25.854  40.819  1.00 94.58  ? 157 TYR C CE2   1 
ATOM   4691 C  CZ    . TYR C 1 157 ? -4.580  24.644  41.453  1.00 95.16  ? 157 TYR C CZ    1 
ATOM   4692 O  OH    . TYR C 1 157 ? -5.747  24.457  42.157  1.00 96.78  ? 157 TYR C OH    1 
ATOM   4693 N  N     . ASP C 1 158 ? -0.399  25.989  35.862  1.00 83.45  ? 158 ASP C N     1 
ATOM   4694 C  CA    . ASP C 1 158 ? 0.588   26.417  34.889  1.00 80.27  ? 158 ASP C CA    1 
ATOM   4695 C  C     . ASP C 1 158 ? 1.609   27.380  35.452  1.00 78.32  ? 158 ASP C C     1 
ATOM   4696 O  O     . ASP C 1 158 ? 2.660   27.575  34.848  1.00 79.12  ? 158 ASP C O     1 
ATOM   4697 C  CB    . ASP C 1 158 ? -0.104  27.088  33.707  1.00 80.91  ? 158 ASP C CB    1 
ATOM   4698 C  CG    . ASP C 1 158 ? -1.243  26.261  33.156  1.00 83.20  ? 158 ASP C CG    1 
ATOM   4699 O  OD1   . ASP C 1 158 ? -1.022  25.053  32.917  1.00 84.37  ? 158 ASP C OD1   1 
ATOM   4700 O  OD2   . ASP C 1 158 ? -2.354  26.816  32.957  1.00 83.65  ? 158 ASP C OD2   1 
ATOM   4701 N  N     . PHE C 1 159 ? 1.306   27.975  36.604  1.00 74.93  ? 159 PHE C N     1 
ATOM   4702 C  CA    . PHE C 1 159 ? 2.187   28.969  37.217  1.00 71.27  ? 159 PHE C CA    1 
ATOM   4703 C  C     . PHE C 1 159 ? 1.759   29.254  38.647  1.00 69.92  ? 159 PHE C C     1 
ATOM   4704 O  O     . PHE C 1 159 ? 0.571   29.283  38.949  1.00 70.25  ? 159 PHE C O     1 
ATOM   4705 C  CB    . PHE C 1 159 ? 2.125   30.264  36.395  1.00 69.36  ? 159 PHE C CB    1 
ATOM   4706 C  CG    . PHE C 1 159 ? 2.638   31.479  37.113  1.00 67.35  ? 159 PHE C CG    1 
ATOM   4707 C  CD1   . PHE C 1 159 ? 3.997   31.645  37.362  1.00 66.26  ? 159 PHE C CD1   1 
ATOM   4708 C  CD2   . PHE C 1 159 ? 1.760   32.471  37.529  1.00 67.13  ? 159 PHE C CD2   1 
ATOM   4709 C  CE1   . PHE C 1 159 ? 4.474   32.786  38.016  1.00 64.67  ? 159 PHE C CE1   1 
ATOM   4710 C  CE2   . PHE C 1 159 ? 2.229   33.616  38.184  1.00 66.07  ? 159 PHE C CE2   1 
ATOM   4711 C  CZ    . PHE C 1 159 ? 3.588   33.769  38.426  1.00 64.95  ? 159 PHE C CZ    1 
ATOM   4712 N  N     . ILE C 1 160 ? 2.731   29.481  39.521  1.00 68.06  ? 160 ILE C N     1 
ATOM   4713 C  CA    . ILE C 1 160 ? 2.445   29.755  40.918  1.00 66.57  ? 160 ILE C CA    1 
ATOM   4714 C  C     . ILE C 1 160 ? 3.429   30.771  41.474  1.00 66.56  ? 160 ILE C C     1 
ATOM   4715 O  O     . ILE C 1 160 ? 4.628   30.511  41.563  1.00 66.13  ? 160 ILE C O     1 
ATOM   4716 C  CB    . ILE C 1 160 ? 2.542   28.465  41.763  1.00 67.15  ? 160 ILE C CB    1 
ATOM   4717 C  CG1   . ILE C 1 160 ? 1.589   27.404  41.212  1.00 66.13  ? 160 ILE C CG1   1 
ATOM   4718 C  CG2   . ILE C 1 160 ? 2.212   28.769  43.220  1.00 67.30  ? 160 ILE C CG2   1 
ATOM   4719 C  CD1   . ILE C 1 160 ? 1.639   26.103  41.947  1.00 65.50  ? 160 ILE C CD1   1 
ATOM   4720 N  N     . PHE C 1 161 ? 2.920   31.937  41.847  1.00 67.39  ? 161 PHE C N     1 
ATOM   4721 C  CA    . PHE C 1 161 ? 3.766   32.983  42.400  1.00 68.24  ? 161 PHE C CA    1 
ATOM   4722 C  C     . PHE C 1 161 ? 3.547   32.944  43.897  1.00 69.19  ? 161 PHE C C     1 
ATOM   4723 O  O     . PHE C 1 161 ? 2.406   32.913  44.363  1.00 69.03  ? 161 PHE C O     1 
ATOM   4724 C  CB    . PHE C 1 161 ? 3.374   34.354  41.834  1.00 68.03  ? 161 PHE C CB    1 
ATOM   4725 C  CG    . PHE C 1 161 ? 4.343   35.452  42.175  1.00 68.61  ? 161 PHE C CG    1 
ATOM   4726 C  CD1   . PHE C 1 161 ? 5.632   35.445  41.652  1.00 69.34  ? 161 PHE C CD1   1 
ATOM   4727 C  CD2   . PHE C 1 161 ? 3.976   36.486  43.036  1.00 68.44  ? 161 PHE C CD2   1 
ATOM   4728 C  CE1   . PHE C 1 161 ? 6.545   36.455  41.987  1.00 70.10  ? 161 PHE C CE1   1 
ATOM   4729 C  CE2   . PHE C 1 161 ? 4.878   37.500  43.377  1.00 68.11  ? 161 PHE C CE2   1 
ATOM   4730 C  CZ    . PHE C 1 161 ? 6.162   37.486  42.855  1.00 68.68  ? 161 PHE C CZ    1 
ATOM   4731 N  N     . VAL C 1 162 ? 4.644   32.944  44.643  1.00 70.34  ? 162 VAL C N     1 
ATOM   4732 C  CA    . VAL C 1 162 ? 4.591   32.874  46.091  1.00 72.27  ? 162 VAL C CA    1 
ATOM   4733 C  C     . VAL C 1 162 ? 5.232   34.070  46.777  1.00 74.53  ? 162 VAL C C     1 
ATOM   4734 O  O     . VAL C 1 162 ? 6.450   34.186  46.823  1.00 74.72  ? 162 VAL C O     1 
ATOM   4735 C  CB    . VAL C 1 162 ? 5.300   31.592  46.592  1.00 71.90  ? 162 VAL C CB    1 
ATOM   4736 C  CG1   . VAL C 1 162 ? 5.247   31.522  48.102  1.00 72.69  ? 162 VAL C CG1   1 
ATOM   4737 C  CG2   . VAL C 1 162 ? 4.658   30.369  45.978  1.00 70.59  ? 162 VAL C CG2   1 
ATOM   4738 N  N     . ASP C 1 163 ? 4.414   34.967  47.310  1.00 77.67  ? 163 ASP C N     1 
ATOM   4739 C  CA    . ASP C 1 163 ? 4.955   36.115  48.019  1.00 81.71  ? 163 ASP C CA    1 
ATOM   4740 C  C     . ASP C 1 163 ? 4.400   36.069  49.433  1.00 84.81  ? 163 ASP C C     1 
ATOM   4741 O  O     . ASP C 1 163 ? 3.993   37.087  49.993  1.00 85.90  ? 163 ASP C O     1 
ATOM   4742 C  CB    . ASP C 1 163 ? 4.536   37.423  47.359  1.00 82.12  ? 163 ASP C CB    1 
ATOM   4743 C  CG    . ASP C 1 163 ? 5.399   38.597  47.801  1.00 82.92  ? 163 ASP C CG    1 
ATOM   4744 O  OD1   . ASP C 1 163 ? 5.718   38.708  49.001  1.00 82.60  ? 163 ASP C OD1   1 
ATOM   4745 O  OD2   . ASP C 1 163 ? 5.760   39.422  46.942  1.00 85.29  ? 163 ASP C OD2   1 
ATOM   4746 N  N     . ALA C 1 164 ? 4.388   34.872  50.007  1.00 88.00  ? 164 ALA C N     1 
ATOM   4747 C  CA    . ALA C 1 164 ? 3.863   34.668  51.349  1.00 90.14  ? 164 ALA C CA    1 
ATOM   4748 C  C     . ALA C 1 164 ? 4.791   35.133  52.466  1.00 91.68  ? 164 ALA C C     1 
ATOM   4749 O  O     . ALA C 1 164 ? 5.534   36.108  52.322  1.00 91.60  ? 164 ALA C O     1 
ATOM   4750 C  CB    . ALA C 1 164 ? 3.509   33.200  51.542  1.00 90.94  ? 164 ALA C CB    1 
ATOM   4751 N  N     . ASP C 1 165 ? 4.738   34.419  53.583  1.00 93.88  ? 165 ASP C N     1 
ATOM   4752 C  CA    . ASP C 1 165 ? 5.536   34.756  54.751  1.00 96.38  ? 165 ASP C CA    1 
ATOM   4753 C  C     . ASP C 1 165 ? 7.019   34.840  54.447  1.00 96.02  ? 165 ASP C C     1 
ATOM   4754 O  O     . ASP C 1 165 ? 7.541   35.937  54.247  1.00 96.92  ? 165 ASP C O     1 
ATOM   4755 C  CB    . ASP C 1 165 ? 5.276   33.748  55.873  1.00 98.84  ? 165 ASP C CB    1 
ATOM   4756 C  CG    . ASP C 1 165 ? 3.794   33.607  56.189  1.00 101.08 ? 165 ASP C CG    1 
ATOM   4757 O  OD1   . ASP C 1 165 ? 3.090   32.909  55.417  1.00 101.52 ? 165 ASP C OD1   1 
ATOM   4758 O  OD2   . ASP C 1 165 ? 3.335   34.205  57.193  1.00 101.66 ? 165 ASP C OD2   1 
ATOM   4759 N  N     . LYS C 1 166 ? 7.690   33.690  54.423  1.00 94.64  ? 166 LYS C N     1 
ATOM   4760 C  CA    . LYS C 1 166 ? 9.119   33.631  54.133  1.00 93.85  ? 166 LYS C CA    1 
ATOM   4761 C  C     . LYS C 1 166 ? 9.681   32.325  54.644  1.00 94.00  ? 166 LYS C C     1 
ATOM   4762 O  O     . LYS C 1 166 ? 10.410  31.630  53.941  1.00 94.09  ? 166 LYS C O     1 
ATOM   4763 C  CB    . LYS C 1 166 ? 9.862   34.780  54.806  1.00 93.42  ? 166 LYS C CB    1 
ATOM   4764 C  CG    . LYS C 1 166 ? 11.130  35.187  54.075  1.00 93.67  ? 166 LYS C CG    1 
ATOM   4765 C  CD    . LYS C 1 166 ? 10.824  35.649  52.649  1.00 92.45  ? 166 LYS C CD    1 
ATOM   4766 C  CE    . LYS C 1 166 ? 9.901   36.863  52.625  1.00 91.21  ? 166 LYS C CE    1 
ATOM   4767 N  NZ    . LYS C 1 166 ? 9.284   37.078  51.286  1.00 89.95  ? 166 LYS C NZ    1 
ATOM   4768 N  N     . ASP C 1 167 ? 9.339   32.001  55.883  1.00 94.28  ? 167 ASP C N     1 
ATOM   4769 C  CA    . ASP C 1 167 ? 9.791   30.767  56.503  1.00 94.71  ? 167 ASP C CA    1 
ATOM   4770 C  C     . ASP C 1 167 ? 8.937   29.600  56.013  1.00 94.43  ? 167 ASP C C     1 
ATOM   4771 O  O     . ASP C 1 167 ? 9.236   28.430  56.283  1.00 94.64  ? 167 ASP C O     1 
ATOM   4772 C  CB    . ASP C 1 167 ? 9.688   30.883  58.022  1.00 95.47  ? 167 ASP C CB    1 
ATOM   4773 C  CG    . ASP C 1 167 ? 8.429   31.599  58.463  1.00 96.98  ? 167 ASP C CG    1 
ATOM   4774 O  OD1   . ASP C 1 167 ? 7.369   31.369  57.842  1.00 97.80  ? 167 ASP C OD1   1 
ATOM   4775 O  OD2   . ASP C 1 167 ? 8.497   32.384  59.432  1.00 97.24  ? 167 ASP C OD2   1 
ATOM   4776 N  N     . ASN C 1 168 ? 7.876   29.920  55.281  1.00 93.43  ? 168 ASN C N     1 
ATOM   4777 C  CA    . ASN C 1 168 ? 6.988   28.888  54.769  1.00 93.24  ? 168 ASN C CA    1 
ATOM   4778 C  C     . ASN C 1 168 ? 7.263   28.482  53.332  1.00 92.23  ? 168 ASN C C     1 
ATOM   4779 O  O     . ASN C 1 168 ? 6.661   27.531  52.829  1.00 91.15  ? 168 ASN C O     1 
ATOM   4780 C  CB    . ASN C 1 168 ? 5.535   29.338  54.901  1.00 94.50  ? 168 ASN C CB    1 
ATOM   4781 C  CG    . ASN C 1 168 ? 5.057   29.333  56.336  1.00 95.68  ? 168 ASN C CG    1 
ATOM   4782 O  OD1   . ASN C 1 168 ? 5.071   28.292  57.008  1.00 95.39  ? 168 ASN C OD1   1 
ATOM   4783 N  ND2   . ASN C 1 168 ? 4.631   30.497  56.820  1.00 95.34  ? 168 ASN C ND2   1 
ATOM   4784 N  N     . TYR C 1 169 ? 8.170   29.193  52.670  1.00 91.44  ? 169 TYR C N     1 
ATOM   4785 C  CA    . TYR C 1 169 ? 8.487   28.871  51.286  1.00 90.82  ? 169 TYR C CA    1 
ATOM   4786 C  C     . TYR C 1 169 ? 8.873   27.407  51.170  1.00 89.81  ? 169 TYR C C     1 
ATOM   4787 O  O     . TYR C 1 169 ? 8.219   26.627  50.468  1.00 88.26  ? 169 TYR C O     1 
ATOM   4788 C  CB    . TYR C 1 169 ? 9.640   29.741  50.760  1.00 91.33  ? 169 TYR C CB    1 
ATOM   4789 C  CG    . TYR C 1 169 ? 9.280   31.185  50.487  1.00 91.00  ? 169 TYR C CG    1 
ATOM   4790 C  CD1   . TYR C 1 169 ? 7.973   31.553  50.172  1.00 91.27  ? 169 TYR C CD1   1 
ATOM   4791 C  CD2   . TYR C 1 169 ? 10.251  32.182  50.531  1.00 91.51  ? 169 TYR C CD2   1 
ATOM   4792 C  CE1   . TYR C 1 169 ? 7.639   32.883  49.915  1.00 91.81  ? 169 TYR C CE1   1 
ATOM   4793 C  CE2   . TYR C 1 169 ? 9.928   33.516  50.273  1.00 91.97  ? 169 TYR C CE2   1 
ATOM   4794 C  CZ    . TYR C 1 169 ? 8.619   33.858  49.969  1.00 91.85  ? 169 TYR C CZ    1 
ATOM   4795 O  OH    . TYR C 1 169 ? 8.282   35.172  49.751  1.00 91.76  ? 169 TYR C OH    1 
ATOM   4796 N  N     . LEU C 1 170 ? 9.942   27.049  51.872  1.00 89.57  ? 170 LEU C N     1 
ATOM   4797 C  CA    . LEU C 1 170 ? 10.453  25.688  51.864  1.00 89.35  ? 170 LEU C CA    1 
ATOM   4798 C  C     . LEU C 1 170 ? 9.286   24.720  52.016  1.00 89.09  ? 170 LEU C C     1 
ATOM   4799 O  O     . LEU C 1 170 ? 9.171   23.736  51.269  1.00 88.92  ? 170 LEU C O     1 
ATOM   4800 C  CB    . LEU C 1 170 ? 11.450  25.501  53.009  1.00 88.80  ? 170 LEU C CB    1 
ATOM   4801 C  CG    . LEU C 1 170 ? 12.642  24.590  52.712  1.00 88.94  ? 170 LEU C CG    1 
ATOM   4802 C  CD1   . LEU C 1 170 ? 12.152  23.208  52.301  1.00 89.17  ? 170 LEU C CD1   1 
ATOM   4803 C  CD2   . LEU C 1 170 ? 13.488  25.210  51.605  1.00 88.72  ? 170 LEU C CD2   1 
ATOM   4804 N  N     . ASN C 1 171 ? 8.416   25.021  52.978  1.00 88.12  ? 171 ASN C N     1 
ATOM   4805 C  CA    . ASN C 1 171 ? 7.244   24.198  53.246  1.00 87.26  ? 171 ASN C CA    1 
ATOM   4806 C  C     . ASN C 1 171 ? 6.277   24.198  52.064  1.00 86.61  ? 171 ASN C C     1 
ATOM   4807 O  O     . ASN C 1 171 ? 5.772   23.141  51.683  1.00 86.01  ? 171 ASN C O     1 
ATOM   4808 C  CB    . ASN C 1 171 ? 6.533   24.690  54.507  1.00 87.79  ? 171 ASN C CB    1 
ATOM   4809 C  CG    . ASN C 1 171 ? 7.410   24.598  55.747  1.00 88.02  ? 171 ASN C CG    1 
ATOM   4810 O  OD1   . ASN C 1 171 ? 7.706   23.504  56.231  1.00 87.21  ? 171 ASN C OD1   1 
ATOM   4811 N  ND2   . ASN C 1 171 ? 7.834   25.752  56.265  1.00 87.98  ? 171 ASN C ND2   1 
ATOM   4812 N  N     . TYR C 1 172 ? 6.025   25.374  51.484  1.00 85.99  ? 172 TYR C N     1 
ATOM   4813 C  CA    . TYR C 1 172 ? 5.116   25.481  50.338  1.00 85.17  ? 172 TYR C CA    1 
ATOM   4814 C  C     . TYR C 1 172 ? 5.648   24.693  49.154  1.00 84.93  ? 172 TYR C C     1 
ATOM   4815 O  O     . TYR C 1 172 ? 4.915   23.944  48.502  1.00 83.93  ? 172 TYR C O     1 
ATOM   4816 C  CB    . TYR C 1 172 ? 4.949   26.934  49.892  1.00 85.16  ? 172 TYR C CB    1 
ATOM   4817 C  CG    . TYR C 1 172 ? 4.206   27.823  50.855  1.00 85.90  ? 172 TYR C CG    1 
ATOM   4818 C  CD1   . TYR C 1 172 ? 2.920   27.503  51.294  1.00 85.31  ? 172 TYR C CD1   1 
ATOM   4819 C  CD2   . TYR C 1 172 ? 4.790   28.995  51.325  1.00 86.34  ? 172 TYR C CD2   1 
ATOM   4820 C  CE1   . TYR C 1 172 ? 2.240   28.333  52.183  1.00 85.04  ? 172 TYR C CE1   1 
ATOM   4821 C  CE2   . TYR C 1 172 ? 4.121   29.827  52.207  1.00 86.28  ? 172 TYR C CE2   1 
ATOM   4822 C  CZ    . TYR C 1 172 ? 2.852   29.492  52.636  1.00 85.66  ? 172 TYR C CZ    1 
ATOM   4823 O  OH    . TYR C 1 172 ? 2.217   30.316  53.536  1.00 86.62  ? 172 TYR C OH    1 
ATOM   4824 N  N     . HIS C 1 173 ? 6.933   24.883  48.880  1.00 84.90  ? 173 HIS C N     1 
ATOM   4825 C  CA    . HIS C 1 173 ? 7.592   24.221  47.766  1.00 85.14  ? 173 HIS C CA    1 
ATOM   4826 C  C     . HIS C 1 173 ? 7.354   22.725  47.780  1.00 85.55  ? 173 HIS C C     1 
ATOM   4827 O  O     . HIS C 1 173 ? 7.209   22.099  46.728  1.00 84.50  ? 173 HIS C O     1 
ATOM   4828 C  CB    . HIS C 1 173 ? 9.092   24.499  47.809  1.00 85.08  ? 173 HIS C CB    1 
ATOM   4829 C  CG    . HIS C 1 173 ? 9.834   23.952  46.632  1.00 84.45  ? 173 HIS C CG    1 
ATOM   4830 N  ND1   . HIS C 1 173 ? 9.546   24.326  45.338  1.00 83.73  ? 173 HIS C ND1   1 
ATOM   4831 C  CD2   . HIS C 1 173 ? 10.833  23.043  46.551  1.00 83.94  ? 173 HIS C CD2   1 
ATOM   4832 C  CE1   . HIS C 1 173 ? 10.336  23.667  44.510  1.00 84.19  ? 173 HIS C CE1   1 
ATOM   4833 N  NE2   . HIS C 1 173 ? 11.125  22.881  45.220  1.00 83.48  ? 173 HIS C NE2   1 
ATOM   4834 N  N     . LYS C 1 174 ? 7.321   22.166  48.986  1.00 86.82  ? 174 LYS C N     1 
ATOM   4835 C  CA    . LYS C 1 174 ? 7.108   20.739  49.190  1.00 87.54  ? 174 LYS C CA    1 
ATOM   4836 C  C     . LYS C 1 174 ? 5.846   20.271  48.473  1.00 87.36  ? 174 LYS C C     1 
ATOM   4837 O  O     . LYS C 1 174 ? 5.881   19.336  47.676  1.00 86.90  ? 174 LYS C O     1 
ATOM   4838 C  CB    . LYS C 1 174 ? 7.000   20.447  50.690  1.00 89.29  ? 174 LYS C CB    1 
ATOM   4839 C  CG    . LYS C 1 174 ? 7.448   19.049  51.088  1.00 91.76  ? 174 LYS C CG    1 
ATOM   4840 C  CD    . LYS C 1 174 ? 8.833   18.740  50.524  1.00 94.44  ? 174 LYS C CD    1 
ATOM   4841 C  CE    . LYS C 1 174 ? 9.846   19.837  50.876  1.00 96.12  ? 174 LYS C CE    1 
ATOM   4842 N  NZ    . LYS C 1 174 ? 11.160  19.641  50.191  1.00 96.36  ? 174 LYS C NZ    1 
ATOM   4843 N  N     . ARG C 1 175 ? 4.729   20.931  48.758  1.00 87.54  ? 175 ARG C N     1 
ATOM   4844 C  CA    . ARG C 1 175 ? 3.459   20.584  48.132  1.00 87.36  ? 175 ARG C CA    1 
ATOM   4845 C  C     . ARG C 1 175 ? 3.379   21.228  46.747  1.00 86.17  ? 175 ARG C C     1 
ATOM   4846 O  O     . ARG C 1 175 ? 3.108   20.555  45.751  1.00 86.09  ? 175 ARG C O     1 
ATOM   4847 C  CB    . ARG C 1 175 ? 2.286   21.065  49.004  1.00 88.64  ? 175 ARG C CB    1 
ATOM   4848 C  CG    . ARG C 1 175 ? 2.700   21.789  50.292  1.00 91.36  ? 175 ARG C CG    1 
ATOM   4849 C  CD    . ARG C 1 175 ? 2.732   20.869  51.530  1.00 93.16  ? 175 ARG C CD    1 
ATOM   4850 N  NE    . ARG C 1 175 ? 3.594   21.400  52.594  1.00 94.78  ? 175 ARG C NE    1 
ATOM   4851 C  CZ    . ARG C 1 175 ? 3.678   20.906  53.829  1.00 94.87  ? 175 ARG C CZ    1 
ATOM   4852 N  NH1   . ARG C 1 175 ? 2.943   19.860  54.181  1.00 95.40  ? 175 ARG C NH1   1 
ATOM   4853 N  NH2   . ARG C 1 175 ? 4.515   21.448  54.709  1.00 94.45  ? 175 ARG C NH2   1 
ATOM   4854 N  N     . LEU C 1 176 ? 3.631   22.535  46.702  1.00 84.73  ? 176 LEU C N     1 
ATOM   4855 C  CA    . LEU C 1 176 ? 3.593   23.335  45.474  1.00 83.30  ? 176 LEU C CA    1 
ATOM   4856 C  C     . LEU C 1 176 ? 4.213   22.676  44.234  1.00 83.09  ? 176 LEU C C     1 
ATOM   4857 O  O     . LEU C 1 176 ? 3.688   22.810  43.126  1.00 82.87  ? 176 LEU C O     1 
ATOM   4858 C  CB    . LEU C 1 176 ? 4.281   24.679  45.736  1.00 82.12  ? 176 LEU C CB    1 
ATOM   4859 C  CG    . LEU C 1 176 ? 3.519   26.003  45.621  1.00 80.05  ? 176 LEU C CG    1 
ATOM   4860 C  CD1   . LEU C 1 176 ? 2.156   25.925  46.270  1.00 79.62  ? 176 LEU C CD1   1 
ATOM   4861 C  CD2   . LEU C 1 176 ? 4.348   27.080  46.278  1.00 78.93  ? 176 LEU C CD2   1 
ATOM   4862 N  N     . ILE C 1 177 ? 5.325   21.969  44.428  1.00 82.81  ? 177 ILE C N     1 
ATOM   4863 C  CA    . ILE C 1 177 ? 6.043   21.297  43.339  1.00 82.23  ? 177 ILE C CA    1 
ATOM   4864 C  C     . ILE C 1 177 ? 5.237   20.150  42.716  1.00 82.22  ? 177 ILE C C     1 
ATOM   4865 O  O     . ILE C 1 177 ? 5.484   19.734  41.582  1.00 80.99  ? 177 ILE C O     1 
ATOM   4866 C  CB    . ILE C 1 177 ? 7.417   20.757  43.852  1.00 81.67  ? 177 ILE C CB    1 
ATOM   4867 C  CG1   . ILE C 1 177 ? 8.430   20.687  42.710  1.00 81.42  ? 177 ILE C CG1   1 
ATOM   4868 C  CG2   . ILE C 1 177 ? 7.250   19.385  44.466  1.00 81.00  ? 177 ILE C CG2   1 
ATOM   4869 C  CD1   . ILE C 1 177 ? 8.120   19.665  41.653  1.00 82.43  ? 177 ILE C CD1   1 
ATOM   4870 N  N     . ASP C 1 178 ? 4.266   19.640  43.462  1.00 82.77  ? 178 ASP C N     1 
ATOM   4871 C  CA    . ASP C 1 178 ? 3.445   18.549  42.964  1.00 83.13  ? 178 ASP C CA    1 
ATOM   4872 C  C     . ASP C 1 178 ? 2.269   19.103  42.179  1.00 81.93  ? 178 ASP C C     1 
ATOM   4873 O  O     . ASP C 1 178 ? 1.742   18.424  41.297  1.00 81.46  ? 178 ASP C O     1 
ATOM   4874 C  CB    . ASP C 1 178 ? 2.928   17.682  44.123  1.00 85.84  ? 178 ASP C CB    1 
ATOM   4875 C  CG    . ASP C 1 178 ? 4.040   16.923  44.838  1.00 87.98  ? 178 ASP C CG    1 
ATOM   4876 O  OD1   . ASP C 1 178 ? 4.687   16.056  44.203  1.00 89.34  ? 178 ASP C OD1   1 
ATOM   4877 O  OD2   . ASP C 1 178 ? 4.263   17.196  46.040  1.00 88.79  ? 178 ASP C OD2   1 
ATOM   4878 N  N     . LEU C 1 179 ? 1.871   20.338  42.494  1.00 80.50  ? 179 LEU C N     1 
ATOM   4879 C  CA    . LEU C 1 179 ? 0.741   20.981  41.824  1.00 79.44  ? 179 LEU C CA    1 
ATOM   4880 C  C     . LEU C 1 179 ? 1.023   21.611  40.440  1.00 79.65  ? 179 LEU C C     1 
ATOM   4881 O  O     . LEU C 1 179 ? 0.117   21.672  39.609  1.00 79.61  ? 179 LEU C O     1 
ATOM   4882 C  CB    . LEU C 1 179 ? 0.092   22.024  42.752  1.00 78.02  ? 179 LEU C CB    1 
ATOM   4883 C  CG    . LEU C 1 179 ? -0.661  21.628  44.041  1.00 75.64  ? 179 LEU C CG    1 
ATOM   4884 C  CD1   . LEU C 1 179 ? -1.544  20.419  43.795  1.00 73.83  ? 179 LEU C CD1   1 
ATOM   4885 C  CD2   . LEU C 1 179 ? 0.326   21.333  45.141  1.00 74.85  ? 179 LEU C CD2   1 
ATOM   4886 N  N     . VAL C 1 180 ? 2.250   22.078  40.185  1.00 79.70  ? 180 VAL C N     1 
ATOM   4887 C  CA    . VAL C 1 180 ? 2.592   22.658  38.871  1.00 80.28  ? 180 VAL C CA    1 
ATOM   4888 C  C     . VAL C 1 180 ? 2.904   21.573  37.844  1.00 80.19  ? 180 VAL C C     1 
ATOM   4889 O  O     . VAL C 1 180 ? 3.419   20.519  38.195  1.00 80.45  ? 180 VAL C O     1 
ATOM   4890 C  CB    . VAL C 1 180 ? 3.823   23.593  38.930  1.00 80.40  ? 180 VAL C CB    1 
ATOM   4891 C  CG1   . VAL C 1 180 ? 3.379   25.016  39.194  1.00 80.49  ? 180 VAL C CG1   1 
ATOM   4892 C  CG2   . VAL C 1 180 ? 4.795   23.115  40.008  1.00 81.19  ? 180 VAL C CG2   1 
ATOM   4893 N  N     . LYS C 1 181 ? 2.620   21.839  36.574  1.00 80.53  ? 181 LYS C N     1 
ATOM   4894 C  CA    . LYS C 1 181 ? 2.865   20.845  35.531  1.00 81.75  ? 181 LYS C CA    1 
ATOM   4895 C  C     . LYS C 1 181 ? 4.329   20.751  35.073  1.00 82.08  ? 181 LYS C C     1 
ATOM   4896 O  O     . LYS C 1 181 ? 5.257   20.851  35.879  1.00 81.56  ? 181 LYS C O     1 
ATOM   4897 C  CB    . LYS C 1 181 ? 1.963   21.128  34.323  1.00 81.72  ? 181 LYS C CB    1 
ATOM   4898 C  CG    . LYS C 1 181 ? 1.755   19.923  33.399  1.00 82.85  ? 181 LYS C CG    1 
ATOM   4899 C  CD    . LYS C 1 181 ? 1.028   18.774  34.117  1.00 83.13  ? 181 LYS C CD    1 
ATOM   4900 C  CE    . LYS C 1 181 ? 1.892   17.519  34.243  1.00 82.94  ? 181 LYS C CE    1 
ATOM   4901 N  NZ    . LYS C 1 181 ? 3.153   17.752  34.998  1.00 82.68  ? 181 LYS C NZ    1 
ATOM   4902 N  N     . VAL C 1 182 ? 4.510   20.525  33.772  1.00 83.11  ? 182 VAL C N     1 
ATOM   4903 C  CA    . VAL C 1 182 ? 5.825   20.423  33.144  1.00 82.86  ? 182 VAL C CA    1 
ATOM   4904 C  C     . VAL C 1 182 ? 6.679   21.643  33.526  1.00 82.31  ? 182 VAL C C     1 
ATOM   4905 O  O     . VAL C 1 182 ? 7.353   21.620  34.558  1.00 83.52  ? 182 VAL C O     1 
ATOM   4906 C  CB    . VAL C 1 182 ? 5.684   20.328  31.584  1.00 83.82  ? 182 VAL C CB    1 
ATOM   4907 C  CG1   . VAL C 1 182 ? 4.829   21.497  31.043  1.00 83.07  ? 182 VAL C CG1   1 
ATOM   4908 C  CG2   . VAL C 1 182 ? 7.066   20.316  30.925  1.00 83.88  ? 182 VAL C CG2   1 
ATOM   4909 N  N     . GLY C 1 183 ? 6.650   22.697  32.705  1.00 79.84  ? 183 GLY C N     1 
ATOM   4910 C  CA    . GLY C 1 183 ? 7.414   23.893  33.009  1.00 77.31  ? 183 GLY C CA    1 
ATOM   4911 C  C     . GLY C 1 183 ? 6.911   24.444  34.329  1.00 76.21  ? 183 GLY C C     1 
ATOM   4912 O  O     . GLY C 1 183 ? 7.678   24.749  35.253  1.00 75.99  ? 183 GLY C O     1 
ATOM   4913 N  N     . GLY C 1 184 ? 5.593   24.556  34.419  1.00 74.35  ? 184 GLY C N     1 
ATOM   4914 C  CA    . GLY C 1 184 ? 4.976   25.053  35.631  1.00 70.96  ? 184 GLY C CA    1 
ATOM   4915 C  C     . GLY C 1 184 ? 5.449   26.421  36.070  1.00 67.48  ? 184 GLY C C     1 
ATOM   4916 O  O     . GLY C 1 184 ? 4.713   27.402  35.977  1.00 68.42  ? 184 GLY C O     1 
ATOM   4917 N  N     . VAL C 1 185 ? 6.679   26.494  36.553  1.00 63.27  ? 185 VAL C N     1 
ATOM   4918 C  CA    . VAL C 1 185 ? 7.226   27.754  37.025  1.00 60.22  ? 185 VAL C CA    1 
ATOM   4919 C  C     . VAL C 1 185 ? 6.608   28.161  38.359  1.00 58.64  ? 185 VAL C C     1 
ATOM   4920 O  O     . VAL C 1 185 ? 5.421   28.458  38.466  1.00 57.97  ? 185 VAL C O     1 
ATOM   4921 C  CB    . VAL C 1 185 ? 7.010   28.938  36.021  1.00 58.51  ? 185 VAL C CB    1 
ATOM   4922 C  CG1   . VAL C 1 185 ? 7.710   30.187  36.544  1.00 55.19  ? 185 VAL C CG1   1 
ATOM   4923 C  CG2   . VAL C 1 185 ? 7.537   28.575  34.633  1.00 58.29  ? 185 VAL C CG2   1 
ATOM   4924 N  N     . ILE C 1 186 ? 7.437   28.154  39.383  1.00 56.82  ? 186 ILE C N     1 
ATOM   4925 C  CA    . ILE C 1 186 ? 7.014   28.563  40.689  1.00 55.41  ? 186 ILE C CA    1 
ATOM   4926 C  C     . ILE C 1 186 ? 7.885   29.780  40.908  1.00 55.24  ? 186 ILE C C     1 
ATOM   4927 O  O     . ILE C 1 186 ? 9.094   29.731  40.662  1.00 52.47  ? 186 ILE C O     1 
ATOM   4928 C  CB    . ILE C 1 186 ? 7.338   27.494  41.750  1.00 55.86  ? 186 ILE C CB    1 
ATOM   4929 C  CG1   . ILE C 1 186 ? 6.656   26.169  41.389  1.00 54.92  ? 186 ILE C CG1   1 
ATOM   4930 C  CG2   . ILE C 1 186 ? 6.865   27.972  43.111  1.00 55.27  ? 186 ILE C CG2   1 
ATOM   4931 C  CD1   . ILE C 1 186 ? 7.083   25.015  42.255  1.00 54.15  ? 186 ILE C CD1   1 
ATOM   4932 N  N     . GLY C 1 187 ? 7.272   30.876  41.341  1.00 55.72  ? 187 GLY C N     1 
ATOM   4933 C  CA    . GLY C 1 187 ? 8.038   32.081  41.575  1.00 56.68  ? 187 GLY C CA    1 
ATOM   4934 C  C     . GLY C 1 187 ? 8.036   32.447  43.034  1.00 57.53  ? 187 GLY C C     1 
ATOM   4935 O  O     . GLY C 1 187 ? 7.010   32.331  43.685  1.00 59.03  ? 187 GLY C O     1 
ATOM   4936 N  N     . TYR C 1 188 ? 9.176   32.886  43.550  1.00 57.77  ? 188 TYR C N     1 
ATOM   4937 C  CA    . TYR C 1 188 ? 9.265   33.272  44.944  1.00 60.75  ? 188 TYR C CA    1 
ATOM   4938 C  C     . TYR C 1 188 ? 9.791   34.700  45.062  1.00 61.61  ? 188 TYR C C     1 
ATOM   4939 O  O     . TYR C 1 188 ? 10.918  34.964  44.674  1.00 63.00  ? 188 TYR C O     1 
ATOM   4940 C  CB    . TYR C 1 188 ? 10.195  32.312  45.707  1.00 61.97  ? 188 TYR C CB    1 
ATOM   4941 C  CG    . TYR C 1 188 ? 9.735   30.865  45.735  1.00 63.51  ? 188 TYR C CG    1 
ATOM   4942 C  CD1   . TYR C 1 188 ? 9.980   30.014  44.662  1.00 64.13  ? 188 TYR C CD1   1 
ATOM   4943 C  CD2   . TYR C 1 188 ? 9.047   30.349  46.835  1.00 65.10  ? 188 TYR C CD2   1 
ATOM   4944 C  CE1   . TYR C 1 188 ? 9.556   28.685  44.680  1.00 64.03  ? 188 TYR C CE1   1 
ATOM   4945 C  CE2   . TYR C 1 188 ? 8.614   29.020  46.862  1.00 65.24  ? 188 TYR C CE2   1 
ATOM   4946 C  CZ    . TYR C 1 188 ? 8.875   28.195  45.780  1.00 65.13  ? 188 TYR C CZ    1 
ATOM   4947 O  OH    . TYR C 1 188 ? 8.458   26.882  45.797  1.00 65.11  ? 188 TYR C OH    1 
ATOM   4948 N  N     . ASP C 1 189 ? 8.992   35.619  45.601  1.00 62.71  ? 189 ASP C N     1 
ATOM   4949 C  CA    . ASP C 1 189 ? 9.437   37.009  45.739  1.00 64.66  ? 189 ASP C CA    1 
ATOM   4950 C  C     . ASP C 1 189 ? 10.477  37.153  46.863  1.00 64.32  ? 189 ASP C C     1 
ATOM   4951 O  O     . ASP C 1 189 ? 10.653  36.262  47.685  1.00 63.67  ? 189 ASP C O     1 
ATOM   4952 C  CB    . ASP C 1 189 ? 8.231   37.929  46.005  1.00 67.06  ? 189 ASP C CB    1 
ATOM   4953 C  CG    . ASP C 1 189 ? 8.539   39.428  45.770  1.00 69.37  ? 189 ASP C CG    1 
ATOM   4954 O  OD1   . ASP C 1 189 ? 9.558   39.945  46.273  1.00 72.14  ? 189 ASP C OD1   1 
ATOM   4955 O  OD2   . ASP C 1 189 ? 7.739   40.111  45.092  1.00 69.27  ? 189 ASP C OD2   1 
ATOM   4956 N  N     . ASN C 1 190 ? 11.167  38.288  46.859  1.00 65.25  ? 190 ASN C N     1 
ATOM   4957 C  CA    . ASN C 1 190 ? 12.204  38.651  47.827  1.00 66.84  ? 190 ASN C CA    1 
ATOM   4958 C  C     . ASN C 1 190 ? 13.339  37.659  48.009  1.00 67.55  ? 190 ASN C C     1 
ATOM   4959 O  O     . ASN C 1 190 ? 14.079  37.766  48.979  1.00 68.77  ? 190 ASN C O     1 
ATOM   4960 C  CB    . ASN C 1 190 ? 11.604  38.927  49.209  1.00 66.80  ? 190 ASN C CB    1 
ATOM   4961 C  CG    . ASN C 1 190 ? 10.369  39.802  49.152  1.00 68.04  ? 190 ASN C CG    1 
ATOM   4962 O  OD1   . ASN C 1 190 ? 9.263   39.313  48.895  1.00 68.27  ? 190 ASN C OD1   1 
ATOM   4963 N  ND2   . ASN C 1 190 ? 10.547  41.103  49.389  1.00 66.38  ? 190 ASN C ND2   1 
ATOM   4964 N  N     . THR C 1 191 ? 13.502  36.714  47.091  1.00 67.57  ? 191 THR C N     1 
ATOM   4965 C  CA    . THR C 1 191 ? 14.557  35.728  47.249  1.00 68.56  ? 191 THR C CA    1 
ATOM   4966 C  C     . THR C 1 191 ? 15.962  36.298  47.293  1.00 69.73  ? 191 THR C C     1 
ATOM   4967 O  O     . THR C 1 191 ? 16.935  35.556  47.292  1.00 70.32  ? 191 THR C O     1 
ATOM   4968 C  CB    . THR C 1 191 ? 14.491  34.683  46.164  1.00 68.32  ? 191 THR C CB    1 
ATOM   4969 O  OG1   . THR C 1 191 ? 14.418  35.335  44.895  1.00 69.34  ? 191 THR C OG1   1 
ATOM   4970 C  CG2   . THR C 1 191 ? 13.273  33.810  46.357  1.00 68.77  ? 191 THR C CG2   1 
ATOM   4971 N  N     . LEU C 1 192 ? 16.074  37.617  47.324  1.00 71.30  ? 192 LEU C N     1 
ATOM   4972 C  CA    . LEU C 1 192 ? 17.380  38.255  47.416  1.00 73.49  ? 192 LEU C CA    1 
ATOM   4973 C  C     . LEU C 1 192 ? 17.396  39.174  48.632  1.00 75.61  ? 192 LEU C C     1 
ATOM   4974 O  O     . LEU C 1 192 ? 18.383  39.857  48.902  1.00 75.69  ? 192 LEU C O     1 
ATOM   4975 C  CB    . LEU C 1 192 ? 17.693  39.038  46.138  1.00 72.68  ? 192 LEU C CB    1 
ATOM   4976 C  CG    . LEU C 1 192 ? 18.440  38.218  45.086  1.00 71.23  ? 192 LEU C CG    1 
ATOM   4977 C  CD1   . LEU C 1 192 ? 18.508  38.964  43.775  1.00 71.01  ? 192 LEU C CD1   1 
ATOM   4978 C  CD2   . LEU C 1 192 ? 19.826  37.918  45.607  1.00 69.89  ? 192 LEU C CD2   1 
ATOM   4979 N  N     . TRP C 1 193 ? 16.277  39.173  49.353  1.00 78.54  ? 193 TRP C N     1 
ATOM   4980 C  CA    . TRP C 1 193 ? 16.070  39.951  50.575  1.00 80.81  ? 193 TRP C CA    1 
ATOM   4981 C  C     . TRP C 1 193 ? 16.881  41.248  50.706  1.00 81.73  ? 193 TRP C C     1 
ATOM   4982 O  O     . TRP C 1 193 ? 17.743  41.373  51.580  1.00 80.85  ? 193 TRP C O     1 
ATOM   4983 C  CB    . TRP C 1 193 ? 16.317  39.041  51.791  1.00 82.57  ? 193 TRP C CB    1 
ATOM   4984 C  CG    . TRP C 1 193 ? 15.736  39.563  53.057  1.00 84.18  ? 193 TRP C CG    1 
ATOM   4985 C  CD1   . TRP C 1 193 ? 16.407  40.151  54.090  1.00 84.62  ? 193 TRP C CD1   1 
ATOM   4986 C  CD2   . TRP C 1 193 ? 14.346  39.633  53.388  1.00 85.08  ? 193 TRP C CD2   1 
ATOM   4987 N  NE1   . TRP C 1 193 ? 15.519  40.591  55.043  1.00 84.71  ? 193 TRP C NE1   1 
ATOM   4988 C  CE2   . TRP C 1 193 ? 14.246  40.286  54.637  1.00 85.32  ? 193 TRP C CE2   1 
ATOM   4989 C  CE3   . TRP C 1 193 ? 13.171  39.211  52.748  1.00 85.66  ? 193 TRP C CE3   1 
ATOM   4990 C  CZ2   . TRP C 1 193 ? 13.017  40.530  55.259  1.00 85.96  ? 193 TRP C CZ2   1 
ATOM   4991 C  CZ3   . TRP C 1 193 ? 11.945  39.455  53.368  1.00 86.14  ? 193 TRP C CZ3   1 
ATOM   4992 C  CH2   . TRP C 1 193 ? 11.880  40.109  54.610  1.00 86.19  ? 193 TRP C CH2   1 
ATOM   4993 N  N     . ASN C 1 194 ? 16.587  42.201  49.827  1.00 83.22  ? 194 ASN C N     1 
ATOM   4994 C  CA    . ASN C 1 194 ? 17.230  43.516  49.806  1.00 85.78  ? 194 ASN C CA    1 
ATOM   4995 C  C     . ASN C 1 194 ? 18.753  43.542  50.018  1.00 86.11  ? 194 ASN C C     1 
ATOM   4996 O  O     . ASN C 1 194 ? 19.322  44.596  50.302  1.00 85.21  ? 194 ASN C O     1 
ATOM   4997 C  CB    . ASN C 1 194 ? 16.559  44.421  50.850  1.00 88.53  ? 194 ASN C CB    1 
ATOM   4998 C  CG    . ASN C 1 194 ? 16.710  45.905  50.529  1.00 91.24  ? 194 ASN C CG    1 
ATOM   4999 O  OD1   . ASN C 1 194 ? 16.116  46.410  49.568  1.00 93.50  ? 194 ASN C OD1   1 
ATOM   5000 N  ND2   . ASN C 1 194 ? 17.508  46.609  51.328  1.00 90.80  ? 194 ASN C ND2   1 
ATOM   5001 N  N     . GLY C 1 195 ? 19.414  42.400  49.865  1.00 86.93  ? 195 GLY C N     1 
ATOM   5002 C  CA    . GLY C 1 195 ? 20.853  42.356  50.068  1.00 89.18  ? 195 GLY C CA    1 
ATOM   5003 C  C     . GLY C 1 195 ? 21.190  41.419  51.213  1.00 91.59  ? 195 GLY C C     1 
ATOM   5004 O  O     . GLY C 1 195 ? 21.645  41.848  52.271  1.00 91.57  ? 195 GLY C O     1 
ATOM   5005 N  N     . SER C 1 196 ? 20.949  40.128  50.995  1.00 94.18  ? 196 SER C N     1 
ATOM   5006 C  CA    . SER C 1 196 ? 21.203  39.088  51.993  1.00 95.51  ? 196 SER C CA    1 
ATOM   5007 C  C     . SER C 1 196 ? 22.640  39.122  52.491  1.00 97.74  ? 196 SER C C     1 
ATOM   5008 O  O     . SER C 1 196 ? 22.928  39.725  53.524  1.00 97.24  ? 196 SER C O     1 
ATOM   5009 C  CB    . SER C 1 196 ? 20.893  37.694  51.411  1.00 93.49  ? 196 SER C CB    1 
ATOM   5010 O  OG    . SER C 1 196 ? 21.812  37.316  50.400  1.00 89.21  ? 196 SER C OG    1 
ATOM   5011 N  N     . VAL C 1 197 ? 23.530  38.474  51.744  1.00 100.64 ? 197 VAL C N     1 
ATOM   5012 C  CA    . VAL C 1 197 ? 24.943  38.408  52.095  1.00 104.51 ? 197 VAL C CA    1 
ATOM   5013 C  C     . VAL C 1 197 ? 25.617  39.768  52.234  1.00 106.85 ? 197 VAL C C     1 
ATOM   5014 O  O     . VAL C 1 197 ? 26.228  40.284  51.293  1.00 106.28 ? 197 VAL C O     1 
ATOM   5015 C  CB    . VAL C 1 197 ? 25.732  37.574  51.071  1.00 105.00 ? 197 VAL C CB    1 
ATOM   5016 C  CG1   . VAL C 1 197 ? 25.309  36.112  51.167  1.00 105.40 ? 197 VAL C CG1   1 
ATOM   5017 C  CG2   . VAL C 1 197 ? 25.506  38.123  49.661  1.00 105.16 ? 197 VAL C CG2   1 
ATOM   5018 N  N     . VAL C 1 198 ? 25.502  40.332  53.430  1.00 109.91 ? 198 VAL C N     1 
ATOM   5019 C  CA    . VAL C 1 198 ? 26.092  41.622  53.745  1.00 113.03 ? 198 VAL C CA    1 
ATOM   5020 C  C     . VAL C 1 198 ? 27.360  41.356  54.534  1.00 114.66 ? 198 VAL C C     1 
ATOM   5021 O  O     . VAL C 1 198 ? 27.689  40.202  54.821  1.00 114.69 ? 198 VAL C O     1 
ATOM   5022 C  CB    . VAL C 1 198 ? 25.141  42.473  54.616  1.00 113.88 ? 198 VAL C CB    1 
ATOM   5023 C  CG1   . VAL C 1 198 ? 25.720  43.870  54.829  1.00 114.44 ? 198 VAL C CG1   1 
ATOM   5024 C  CG2   . VAL C 1 198 ? 23.776  42.559  53.955  1.00 114.87 ? 198 VAL C CG2   1 
ATOM   5025 N  N     . ALA C 1 199 ? 28.070  42.425  54.877  1.00 116.78 ? 199 ALA C N     1 
ATOM   5026 C  CA    . ALA C 1 199 ? 29.294  42.307  55.648  1.00 119.25 ? 199 ALA C CA    1 
ATOM   5027 C  C     . ALA C 1 199 ? 29.035  41.302  56.762  1.00 121.21 ? 199 ALA C C     1 
ATOM   5028 O  O     . ALA C 1 199 ? 27.987  41.345  57.409  1.00 121.20 ? 199 ALA C O     1 
ATOM   5029 C  CB    . ALA C 1 199 ? 29.672  43.659  56.236  1.00 118.67 ? 199 ALA C CB    1 
ATOM   5030 N  N     . PRO C 1 200 ? 29.977  40.367  56.983  1.00 123.26 ? 200 PRO C N     1 
ATOM   5031 C  CA    . PRO C 1 200 ? 29.851  39.343  58.028  1.00 124.54 ? 200 PRO C CA    1 
ATOM   5032 C  C     . PRO C 1 200 ? 29.402  39.957  59.358  1.00 125.49 ? 200 PRO C C     1 
ATOM   5033 O  O     . PRO C 1 200 ? 29.286  41.175  59.467  1.00 125.05 ? 200 PRO C O     1 
ATOM   5034 C  CB    . PRO C 1 200 ? 31.258  38.753  58.090  1.00 124.67 ? 200 PRO C CB    1 
ATOM   5035 C  CG    . PRO C 1 200 ? 31.687  38.808  56.648  1.00 124.41 ? 200 PRO C CG    1 
ATOM   5036 C  CD    . PRO C 1 200 ? 31.240  40.202  56.237  1.00 123.80 ? 200 PRO C CD    1 
ATOM   5037 N  N     . PRO C 1 201 ? 29.145  39.119  60.381  1.00 126.74 ? 201 PRO C N     1 
ATOM   5038 C  CA    . PRO C 1 201 ? 28.705  39.577  61.708  1.00 127.73 ? 201 PRO C CA    1 
ATOM   5039 C  C     . PRO C 1 201 ? 29.329  40.893  62.201  1.00 128.18 ? 201 PRO C C     1 
ATOM   5040 O  O     . PRO C 1 201 ? 30.104  40.911  63.161  1.00 128.34 ? 201 PRO C O     1 
ATOM   5041 C  CB    . PRO C 1 201 ? 29.049  38.388  62.601  1.00 127.87 ? 201 PRO C CB    1 
ATOM   5042 C  CG    . PRO C 1 201 ? 28.721  37.228  61.707  1.00 127.59 ? 201 PRO C CG    1 
ATOM   5043 C  CD    . PRO C 1 201 ? 29.315  37.651  60.368  1.00 127.00 ? 201 PRO C CD    1 
ATOM   5044 N  N     . ASP C 1 202 ? 28.966  41.989  61.538  1.00 128.23 ? 202 ASP C N     1 
ATOM   5045 C  CA    . ASP C 1 202 ? 29.460  43.323  61.869  1.00 128.13 ? 202 ASP C CA    1 
ATOM   5046 C  C     . ASP C 1 202 ? 28.655  44.339  61.067  1.00 127.47 ? 202 ASP C C     1 
ATOM   5047 O  O     . ASP C 1 202 ? 29.034  45.507  60.948  1.00 127.25 ? 202 ASP C O     1 
ATOM   5048 C  CB    . ASP C 1 202 ? 30.946  43.452  61.515  1.00 128.84 ? 202 ASP C CB    1 
ATOM   5049 C  CG    . ASP C 1 202 ? 31.194  43.445  60.019  1.00 129.42 ? 202 ASP C CG    1 
ATOM   5050 O  OD1   . ASP C 1 202 ? 30.785  44.410  59.337  1.00 129.69 ? 202 ASP C OD1   1 
ATOM   5051 O  OD2   . ASP C 1 202 ? 31.796  42.470  59.523  1.00 130.04 ? 202 ASP C OD2   1 
ATOM   5052 N  N     . ALA C 1 203 ? 27.540  43.876  60.512  1.00 126.66 ? 203 ALA C N     1 
ATOM   5053 C  CA    . ALA C 1 203 ? 26.669  44.731  59.720  1.00 125.45 ? 203 ALA C CA    1 
ATOM   5054 C  C     . ALA C 1 203 ? 25.546  45.301  60.584  1.00 124.30 ? 203 ALA C C     1 
ATOM   5055 O  O     . ALA C 1 203 ? 24.868  44.573  61.317  1.00 124.11 ? 203 ALA C O     1 
ATOM   5056 C  CB    . ALA C 1 203 ? 26.091  43.943  58.546  1.00 125.78 ? 203 ALA C CB    1 
ATOM   5057 N  N     . PRO C 1 204 ? 25.354  46.626  60.522  1.00 122.94 ? 204 PRO C N     1 
ATOM   5058 C  CA    . PRO C 1 204 ? 24.318  47.328  61.287  1.00 121.84 ? 204 PRO C CA    1 
ATOM   5059 C  C     . PRO C 1 204 ? 22.910  47.114  60.717  1.00 120.56 ? 204 PRO C C     1 
ATOM   5060 O  O     . PRO C 1 204 ? 22.183  48.083  60.482  1.00 121.06 ? 204 PRO C O     1 
ATOM   5061 C  CB    . PRO C 1 204 ? 24.751  48.793  61.188  1.00 121.91 ? 204 PRO C CB    1 
ATOM   5062 C  CG    . PRO C 1 204 ? 26.237  48.706  60.940  1.00 122.10 ? 204 PRO C CG    1 
ATOM   5063 C  CD    . PRO C 1 204 ? 26.319  47.584  59.957  1.00 122.27 ? 204 PRO C CD    1 
ATOM   5064 N  N     . LEU C 1 205 ? 22.521  45.858  60.502  1.00 118.32 ? 205 LEU C N     1 
ATOM   5065 C  CA    . LEU C 1 205 ? 21.201  45.574  59.941  1.00 116.13 ? 205 LEU C CA    1 
ATOM   5066 C  C     . LEU C 1 205 ? 20.123  45.293  60.988  1.00 114.26 ? 205 LEU C C     1 
ATOM   5067 O  O     . LEU C 1 205 ? 20.361  44.566  61.953  1.00 114.09 ? 205 LEU C O     1 
ATOM   5068 C  CB    . LEU C 1 205 ? 21.278  44.401  58.949  1.00 116.44 ? 205 LEU C CB    1 
ATOM   5069 C  CG    . LEU C 1 205 ? 21.697  43.012  59.441  1.00 116.64 ? 205 LEU C CG    1 
ATOM   5070 C  CD1   . LEU C 1 205 ? 21.427  41.974  58.365  1.00 115.91 ? 205 LEU C CD1   1 
ATOM   5071 C  CD2   . LEU C 1 205 ? 23.160  43.021  59.803  1.00 116.92 ? 205 LEU C CD2   1 
ATOM   5072 N  N     . ARG C 1 206 ? 18.943  45.882  60.780  1.00 111.94 ? 206 ARG C N     1 
ATOM   5073 C  CA    . ARG C 1 206 ? 17.797  45.713  61.675  1.00 109.43 ? 206 ARG C CA    1 
ATOM   5074 C  C     . ARG C 1 206 ? 17.532  44.238  61.947  1.00 107.74 ? 206 ARG C C     1 
ATOM   5075 O  O     . ARG C 1 206 ? 17.467  43.430  61.023  1.00 108.23 ? 206 ARG C O     1 
ATOM   5076 C  CB    . ARG C 1 206 ? 16.540  46.345  61.059  1.00 109.85 ? 206 ARG C CB    1 
ATOM   5077 C  CG    . ARG C 1 206 ? 16.401  47.844  61.279  1.00 110.56 ? 206 ARG C CG    1 
ATOM   5078 C  CD    . ARG C 1 206 ? 17.595  48.599  60.729  1.00 112.08 ? 206 ARG C CD    1 
ATOM   5079 N  NE    . ARG C 1 206 ? 17.607  50.000  61.143  1.00 112.61 ? 206 ARG C NE    1 
ATOM   5080 C  CZ    . ARG C 1 206 ? 18.595  50.850  60.872  1.00 113.03 ? 206 ARG C CZ    1 
ATOM   5081 N  NH1   . ARG C 1 206 ? 19.657  50.443  60.184  1.00 112.53 ? 206 ARG C NH1   1 
ATOM   5082 N  NH2   . ARG C 1 206 ? 18.526  52.107  61.295  1.00 112.77 ? 206 ARG C NH2   1 
ATOM   5083 N  N     . LYS C 1 207 ? 17.374  43.887  63.217  1.00 105.28 ? 207 LYS C N     1 
ATOM   5084 C  CA    . LYS C 1 207 ? 17.120  42.502  63.594  1.00 102.45 ? 207 LYS C CA    1 
ATOM   5085 C  C     . LYS C 1 207 ? 15.998  41.896  62.761  1.00 99.58  ? 207 LYS C C     1 
ATOM   5086 O  O     . LYS C 1 207 ? 16.034  40.713  62.436  1.00 98.88  ? 207 LYS C O     1 
ATOM   5087 C  CB    . LYS C 1 207 ? 16.758  42.416  65.078  1.00 104.11 ? 207 LYS C CB    1 
ATOM   5088 C  CG    . LYS C 1 207 ? 16.371  41.019  65.541  1.00 105.13 ? 207 LYS C CG    1 
ATOM   5089 C  CD    . LYS C 1 207 ? 15.477  41.076  66.771  1.00 105.55 ? 207 LYS C CD    1 
ATOM   5090 C  CE    . LYS C 1 207 ? 14.182  41.836  66.480  1.00 106.15 ? 207 LYS C CE    1 
ATOM   5091 N  NZ    . LYS C 1 207 ? 13.407  41.253  65.338  1.00 106.12 ? 207 LYS C NZ    1 
ATOM   5092 N  N     . TYR C 1 208 ? 15.003  42.711  62.421  1.00 97.01  ? 208 TYR C N     1 
ATOM   5093 C  CA    . TYR C 1 208 ? 13.872  42.245  61.624  1.00 94.81  ? 208 TYR C CA    1 
ATOM   5094 C  C     . TYR C 1 208 ? 14.298  41.591  60.315  1.00 93.71  ? 208 TYR C C     1 
ATOM   5095 O  O     . TYR C 1 208 ? 13.683  40.622  59.869  1.00 93.14  ? 208 TYR C O     1 
ATOM   5096 C  CB    . TYR C 1 208 ? 12.926  43.397  61.296  1.00 94.07  ? 208 TYR C CB    1 
ATOM   5097 C  CG    . TYR C 1 208 ? 11.919  43.030  60.229  1.00 94.45  ? 208 TYR C CG    1 
ATOM   5098 C  CD1   . TYR C 1 208 ? 10.986  42.019  60.444  1.00 95.06  ? 208 TYR C CD1   1 
ATOM   5099 C  CD2   . TYR C 1 208 ? 11.912  43.675  58.991  1.00 94.45  ? 208 TYR C CD2   1 
ATOM   5100 C  CE1   . TYR C 1 208 ? 10.068  41.658  59.453  1.00 94.49  ? 208 TYR C CE1   1 
ATOM   5101 C  CE2   . TYR C 1 208 ? 10.998  43.321  57.996  1.00 93.68  ? 208 TYR C CE2   1 
ATOM   5102 C  CZ    . TYR C 1 208 ? 10.081  42.313  58.237  1.00 93.77  ? 208 TYR C CZ    1 
ATOM   5103 O  OH    . TYR C 1 208 ? 9.163   41.966  57.277  1.00 93.36  ? 208 TYR C OH    1 
ATOM   5104 N  N     . VAL C 1 209 ? 15.340  42.132  59.690  1.00 92.50  ? 209 VAL C N     1 
ATOM   5105 C  CA    . VAL C 1 209 ? 15.820  41.584  58.430  1.00 90.81  ? 209 VAL C CA    1 
ATOM   5106 C  C     . VAL C 1 209 ? 16.671  40.334  58.682  1.00 90.24  ? 209 VAL C C     1 
ATOM   5107 O  O     . VAL C 1 209 ? 16.365  39.254  58.171  1.00 90.17  ? 209 VAL C O     1 
ATOM   5108 C  CB    . VAL C 1 209 ? 16.627  42.651  57.611  1.00 89.87  ? 209 VAL C CB    1 
ATOM   5109 C  CG1   . VAL C 1 209 ? 15.896  43.985  57.630  1.00 87.66  ? 209 VAL C CG1   1 
ATOM   5110 C  CG2   . VAL C 1 209 ? 18.025  42.812  58.157  1.00 89.72  ? 209 VAL C CG2   1 
ATOM   5111 N  N     . ARG C 1 210 ? 17.717  40.473  59.489  1.00 89.37  ? 210 ARG C N     1 
ATOM   5112 C  CA    . ARG C 1 210 ? 18.596  39.354  59.800  1.00 89.18  ? 210 ARG C CA    1 
ATOM   5113 C  C     . ARG C 1 210 ? 17.807  38.088  60.146  1.00 88.09  ? 210 ARG C C     1 
ATOM   5114 O  O     . ARG C 1 210 ? 18.254  36.972  59.884  1.00 86.62  ? 210 ARG C O     1 
ATOM   5115 C  CB    . ARG C 1 210 ? 19.503  39.724  60.968  1.00 90.34  ? 210 ARG C CB    1 
ATOM   5116 C  CG    . ARG C 1 210 ? 20.396  38.591  61.429  1.00 92.34  ? 210 ARG C CG    1 
ATOM   5117 C  CD    . ARG C 1 210 ? 20.953  38.895  62.800  1.00 94.37  ? 210 ARG C CD    1 
ATOM   5118 N  NE    . ARG C 1 210 ? 21.631  40.186  62.825  1.00 96.64  ? 210 ARG C NE    1 
ATOM   5119 C  CZ    . ARG C 1 210 ? 22.802  40.432  62.242  1.00 97.56  ? 210 ARG C CZ    1 
ATOM   5120 N  NH1   . ARG C 1 210 ? 23.437  39.468  61.580  1.00 97.30  ? 210 ARG C NH1   1 
ATOM   5121 N  NH2   . ARG C 1 210 ? 23.339  41.645  62.328  1.00 98.02  ? 210 ARG C NH2   1 
ATOM   5122 N  N     . TYR C 1 211 ? 16.632  38.274  60.738  1.00 87.59  ? 211 TYR C N     1 
ATOM   5123 C  CA    . TYR C 1 211 ? 15.778  37.158  61.132  1.00 87.38  ? 211 TYR C CA    1 
ATOM   5124 C  C     . TYR C 1 211 ? 15.270  36.406  59.916  1.00 87.12  ? 211 TYR C C     1 
ATOM   5125 O  O     . TYR C 1 211 ? 15.366  35.180  59.844  1.00 87.08  ? 211 TYR C O     1 
ATOM   5126 C  CB    . TYR C 1 211 ? 14.581  37.664  61.951  1.00 87.23  ? 211 TYR C CB    1 
ATOM   5127 C  CG    . TYR C 1 211 ? 13.507  36.617  62.199  1.00 86.74  ? 211 TYR C CG    1 
ATOM   5128 C  CD1   . TYR C 1 211 ? 13.722  35.555  63.080  1.00 87.01  ? 211 TYR C CD1   1 
ATOM   5129 C  CD2   . TYR C 1 211 ? 12.283  36.678  61.532  1.00 86.37  ? 211 TYR C CD2   1 
ATOM   5130 C  CE1   . TYR C 1 211 ? 12.739  34.574  63.290  1.00 86.45  ? 211 TYR C CE1   1 
ATOM   5131 C  CE2   . TYR C 1 211 ? 11.300  35.707  61.731  1.00 86.34  ? 211 TYR C CE2   1 
ATOM   5132 C  CZ    . TYR C 1 211 ? 11.532  34.658  62.610  1.00 86.27  ? 211 TYR C CZ    1 
ATOM   5133 O  OH    . TYR C 1 211 ? 10.561  33.698  62.797  1.00 85.28  ? 211 TYR C OH    1 
ATOM   5134 N  N     . TYR C 1 212 ? 14.717  37.150  58.965  1.00 86.96  ? 212 TYR C N     1 
ATOM   5135 C  CA    . TYR C 1 212 ? 14.180  36.552  57.754  1.00 86.49  ? 212 TYR C CA    1 
ATOM   5136 C  C     . TYR C 1 212 ? 15.270  36.194  56.752  1.00 86.39  ? 212 TYR C C     1 
ATOM   5137 O  O     . TYR C 1 212 ? 15.089  35.290  55.933  1.00 86.16  ? 212 TYR C O     1 
ATOM   5138 C  CB    . TYR C 1 212 ? 13.139  37.485  57.129  1.00 85.66  ? 212 TYR C CB    1 
ATOM   5139 C  CG    . TYR C 1 212 ? 11.767  37.361  57.771  1.00 85.63  ? 212 TYR C CG    1 
ATOM   5140 C  CD1   . TYR C 1 212 ? 11.004  36.204  57.604  1.00 85.68  ? 212 TYR C CD1   1 
ATOM   5141 C  CD2   . TYR C 1 212 ? 11.234  38.391  58.549  1.00 85.28  ? 212 TYR C CD2   1 
ATOM   5142 C  CE1   . TYR C 1 212 ? 9.747   36.073  58.190  1.00 85.60  ? 212 TYR C CE1   1 
ATOM   5143 C  CE2   . TYR C 1 212 ? 9.973   38.268  59.142  1.00 85.12  ? 212 TYR C CE2   1 
ATOM   5144 C  CZ    . TYR C 1 212 ? 9.238   37.106  58.957  1.00 85.30  ? 212 TYR C CZ    1 
ATOM   5145 O  OH    . TYR C 1 212 ? 7.997   36.965  59.535  1.00 84.65  ? 212 TYR C OH    1 
ATOM   5146 N  N     . ARG C 1 213 ? 16.404  36.889  56.825  1.00 85.80  ? 213 ARG C N     1 
ATOM   5147 C  CA    . ARG C 1 213 ? 17.516  36.601  55.929  1.00 85.35  ? 213 ARG C CA    1 
ATOM   5148 C  C     . ARG C 1 213 ? 17.810  35.115  55.995  1.00 85.80  ? 213 ARG C C     1 
ATOM   5149 O  O     . ARG C 1 213 ? 17.858  34.433  54.975  1.00 85.61  ? 213 ARG C O     1 
ATOM   5150 C  CB    . ARG C 1 213 ? 18.771  37.365  56.345  1.00 84.78  ? 213 ARG C CB    1 
ATOM   5151 C  CG    . ARG C 1 213 ? 20.011  36.934  55.578  1.00 85.07  ? 213 ARG C CG    1 
ATOM   5152 C  CD    . ARG C 1 213 ? 21.204  37.842  55.838  1.00 86.84  ? 213 ARG C CD    1 
ATOM   5153 N  NE    . ARG C 1 213 ? 22.053  37.392  56.942  1.00 88.94  ? 213 ARG C NE    1 
ATOM   5154 C  CZ    . ARG C 1 213 ? 23.108  38.070  57.397  1.00 89.77  ? 213 ARG C CZ    1 
ATOM   5155 N  NH1   . ARG C 1 213 ? 23.442  39.232  56.847  1.00 89.71  ? 213 ARG C NH1   1 
ATOM   5156 N  NH2   . ARG C 1 213 ? 23.837  37.591  58.399  1.00 89.59  ? 213 ARG C NH2   1 
ATOM   5157 N  N     . ASP C 1 214 ? 17.995  34.626  57.216  1.00 86.97  ? 214 ASP C N     1 
ATOM   5158 C  CA    . ASP C 1 214 ? 18.303  33.225  57.475  1.00 87.40  ? 214 ASP C CA    1 
ATOM   5159 C  C     . ASP C 1 214 ? 17.420  32.264  56.691  1.00 86.30  ? 214 ASP C C     1 
ATOM   5160 O  O     . ASP C 1 214 ? 17.920  31.339  56.051  1.00 85.83  ? 214 ASP C O     1 
ATOM   5161 C  CB    . ASP C 1 214 ? 18.187  32.939  58.979  1.00 90.26  ? 214 ASP C CB    1 
ATOM   5162 C  CG    . ASP C 1 214 ? 19.284  33.624  59.801  1.00 92.29  ? 214 ASP C CG    1 
ATOM   5163 O  OD1   . ASP C 1 214 ? 19.620  34.795  59.499  1.00 93.58  ? 214 ASP C OD1   1 
ATOM   5164 O  OD2   . ASP C 1 214 ? 19.799  32.993  60.755  1.00 92.49  ? 214 ASP C OD2   1 
ATOM   5165 N  N     . PHE C 1 215 ? 16.111  32.476  56.739  1.00 85.56  ? 215 PHE C N     1 
ATOM   5166 C  CA    . PHE C 1 215 ? 15.191  31.606  56.015  1.00 85.63  ? 215 PHE C CA    1 
ATOM   5167 C  C     . PHE C 1 215 ? 15.447  31.685  54.521  1.00 84.76  ? 215 PHE C C     1 
ATOM   5168 O  O     . PHE C 1 215 ? 15.406  30.673  53.821  1.00 84.74  ? 215 PHE C O     1 
ATOM   5169 C  CB    . PHE C 1 215 ? 13.752  32.008  56.303  1.00 86.70  ? 215 PHE C CB    1 
ATOM   5170 C  CG    . PHE C 1 215 ? 13.334  31.752  57.710  1.00 88.45  ? 215 PHE C CG    1 
ATOM   5171 C  CD1   . PHE C 1 215 ? 12.923  30.484  58.104  1.00 88.55  ? 215 PHE C CD1   1 
ATOM   5172 C  CD2   . PHE C 1 215 ? 13.360  32.776  58.652  1.00 89.54  ? 215 PHE C CD2   1 
ATOM   5173 C  CE1   . PHE C 1 215 ? 12.541  30.239  59.414  1.00 88.79  ? 215 PHE C CE1   1 
ATOM   5174 C  CE2   . PHE C 1 215 ? 12.981  32.542  59.968  1.00 89.28  ? 215 PHE C CE2   1 
ATOM   5175 C  CZ    . PHE C 1 215 ? 12.569  31.270  60.347  1.00 89.25  ? 215 PHE C CZ    1 
ATOM   5176 N  N     . VAL C 1 216 ? 15.701  32.902  54.044  1.00 83.90  ? 216 VAL C N     1 
ATOM   5177 C  CA    . VAL C 1 216 ? 15.978  33.152  52.635  1.00 81.57  ? 216 VAL C CA    1 
ATOM   5178 C  C     . VAL C 1 216 ? 17.265  32.434  52.239  1.00 80.25  ? 216 VAL C C     1 
ATOM   5179 O  O     . VAL C 1 216 ? 17.253  31.614  51.325  1.00 80.71  ? 216 VAL C O     1 
ATOM   5180 C  CB    . VAL C 1 216 ? 16.114  34.672  52.358  1.00 81.73  ? 216 VAL C CB    1 
ATOM   5181 C  CG1   . VAL C 1 216 ? 16.649  34.911  50.955  1.00 81.69  ? 216 VAL C CG1   1 
ATOM   5182 C  CG2   . VAL C 1 216 ? 14.757  35.351  52.523  1.00 80.93  ? 216 VAL C CG2   1 
ATOM   5183 N  N     . LEU C 1 217 ? 18.366  32.728  52.931  1.00 78.03  ? 217 LEU C N     1 
ATOM   5184 C  CA    . LEU C 1 217 ? 19.637  32.080  52.628  1.00 76.67  ? 217 LEU C CA    1 
ATOM   5185 C  C     . LEU C 1 217 ? 19.451  30.588  52.417  1.00 77.60  ? 217 LEU C C     1 
ATOM   5186 O  O     . LEU C 1 217 ? 19.988  30.008  51.474  1.00 78.39  ? 217 LEU C O     1 
ATOM   5187 C  CB    . LEU C 1 217 ? 20.635  32.283  53.758  1.00 74.28  ? 217 LEU C CB    1 
ATOM   5188 C  CG    . LEU C 1 217 ? 21.380  33.606  53.835  1.00 73.38  ? 217 LEU C CG    1 
ATOM   5189 C  CD1   . LEU C 1 217 ? 22.408  33.541  54.953  1.00 72.58  ? 217 LEU C CD1   1 
ATOM   5190 C  CD2   . LEU C 1 217 ? 22.069  33.872  52.518  1.00 73.70  ? 217 LEU C CD2   1 
ATOM   5191 N  N     . GLU C 1 218 ? 18.679  29.975  53.303  1.00 78.26  ? 218 GLU C N     1 
ATOM   5192 C  CA    . GLU C 1 218 ? 18.419  28.549  53.241  1.00 79.03  ? 218 GLU C CA    1 
ATOM   5193 C  C     . GLU C 1 218 ? 17.394  28.188  52.164  1.00 78.29  ? 218 GLU C C     1 
ATOM   5194 O  O     . GLU C 1 218 ? 17.442  27.098  51.590  1.00 77.96  ? 218 GLU C O     1 
ATOM   5195 C  CB    . GLU C 1 218 ? 17.965  28.071  54.621  1.00 81.72  ? 218 GLU C CB    1 
ATOM   5196 C  CG    . GLU C 1 218 ? 17.475  26.640  54.688  1.00 85.75  ? 218 GLU C CG    1 
ATOM   5197 C  CD    . GLU C 1 218 ? 15.987  26.573  54.987  1.00 88.75  ? 218 GLU C CD    1 
ATOM   5198 O  OE1   . GLU C 1 218 ? 15.567  27.122  56.035  1.00 89.69  ? 218 GLU C OE1   1 
ATOM   5199 O  OE2   . GLU C 1 218 ? 15.238  25.980  54.176  1.00 90.80  ? 218 GLU C OE2   1 
ATOM   5200 N  N     . LEU C 1 219 ? 16.470  29.103  51.887  1.00 77.73  ? 219 LEU C N     1 
ATOM   5201 C  CA    . LEU C 1 219 ? 15.452  28.875  50.858  1.00 76.80  ? 219 LEU C CA    1 
ATOM   5202 C  C     . LEU C 1 219 ? 16.155  28.823  49.503  1.00 76.24  ? 219 LEU C C     1 
ATOM   5203 O  O     . LEU C 1 219 ? 15.764  28.079  48.592  1.00 75.36  ? 219 LEU C O     1 
ATOM   5204 C  CB    . LEU C 1 219 ? 14.420  30.010  50.880  1.00 76.36  ? 219 LEU C CB    1 
ATOM   5205 C  CG    . LEU C 1 219 ? 13.238  29.977  49.900  1.00 76.67  ? 219 LEU C CG    1 
ATOM   5206 C  CD1   . LEU C 1 219 ? 13.658  30.488  48.535  1.00 77.07  ? 219 LEU C CD1   1 
ATOM   5207 C  CD2   . LEU C 1 219 ? 12.694  28.567  49.809  1.00 76.24  ? 219 LEU C CD2   1 
ATOM   5208 N  N     . ASN C 1 220 ? 17.211  29.621  49.393  1.00 75.46  ? 220 ASN C N     1 
ATOM   5209 C  CA    . ASN C 1 220 ? 18.004  29.693  48.183  1.00 75.67  ? 220 ASN C CA    1 
ATOM   5210 C  C     . ASN C 1 220 ? 18.860  28.440  48.004  1.00 76.18  ? 220 ASN C C     1 
ATOM   5211 O  O     . ASN C 1 220 ? 18.790  27.793  46.953  1.00 76.53  ? 220 ASN C O     1 
ATOM   5212 C  CB    . ASN C 1 220 ? 18.886  30.939  48.222  1.00 75.32  ? 220 ASN C CB    1 
ATOM   5213 C  CG    . ASN C 1 220 ? 18.088  32.225  48.067  1.00 74.95  ? 220 ASN C CG    1 
ATOM   5214 O  OD1   . ASN C 1 220 ? 18.540  33.297  48.477  1.00 74.02  ? 220 ASN C OD1   1 
ATOM   5215 N  ND2   . ASN C 1 220 ? 16.903  32.129  47.459  1.00 74.02  ? 220 ASN C ND2   1 
ATOM   5216 N  N     . LYS C 1 221 ? 19.655  28.089  49.020  1.00 75.78  ? 221 LYS C N     1 
ATOM   5217 C  CA    . LYS C 1 221 ? 20.509  26.899  48.938  1.00 74.94  ? 221 LYS C CA    1 
ATOM   5218 C  C     . LYS C 1 221 ? 19.675  25.664  48.615  1.00 74.01  ? 221 LYS C C     1 
ATOM   5219 O  O     . LYS C 1 221 ? 20.074  24.822  47.810  1.00 73.50  ? 221 LYS C O     1 
ATOM   5220 C  CB    . LYS C 1 221 ? 21.262  26.665  50.251  1.00 75.16  ? 221 LYS C CB    1 
ATOM   5221 C  CG    . LYS C 1 221 ? 22.090  27.849  50.726  1.00 78.48  ? 221 LYS C CG    1 
ATOM   5222 C  CD    . LYS C 1 221 ? 23.128  28.290  49.687  1.00 80.05  ? 221 LYS C CD    1 
ATOM   5223 C  CE    . LYS C 1 221 ? 23.876  29.576  50.111  1.00 80.92  ? 221 LYS C CE    1 
ATOM   5224 N  NZ    . LYS C 1 221 ? 23.005  30.795  50.230  1.00 77.91  ? 221 LYS C NZ    1 
ATOM   5225 N  N     . ALA C 1 222 ? 18.505  25.569  49.236  1.00 73.22  ? 222 ALA C N     1 
ATOM   5226 C  CA    . ALA C 1 222 ? 17.619  24.432  49.021  1.00 72.86  ? 222 ALA C CA    1 
ATOM   5227 C  C     . ALA C 1 222 ? 17.098  24.372  47.595  1.00 72.27  ? 222 ALA C C     1 
ATOM   5228 O  O     . ALA C 1 222 ? 17.189  23.341  46.929  1.00 72.58  ? 222 ALA C O     1 
ATOM   5229 C  CB    . ALA C 1 222 ? 16.451  24.498  49.994  1.00 73.78  ? 222 ALA C CB    1 
ATOM   5230 N  N     . LEU C 1 223 ? 16.547  25.485  47.131  1.00 71.82  ? 223 LEU C N     1 
ATOM   5231 C  CA    . LEU C 1 223 ? 15.994  25.562  45.791  1.00 71.01  ? 223 LEU C CA    1 
ATOM   5232 C  C     . LEU C 1 223 ? 17.082  25.344  44.734  1.00 70.57  ? 223 LEU C C     1 
ATOM   5233 O  O     . LEU C 1 223 ? 16.843  24.733  43.690  1.00 70.24  ? 223 LEU C O     1 
ATOM   5234 C  CB    . LEU C 1 223 ? 15.320  26.921  45.622  1.00 70.74  ? 223 LEU C CB    1 
ATOM   5235 C  CG    . LEU C 1 223 ? 13.885  26.948  45.090  1.00 70.93  ? 223 LEU C CG    1 
ATOM   5236 C  CD1   . LEU C 1 223 ? 13.117  25.701  45.501  1.00 70.17  ? 223 LEU C CD1   1 
ATOM   5237 C  CD2   . LEU C 1 223 ? 13.207  28.203  45.619  1.00 70.67  ? 223 LEU C CD2   1 
ATOM   5238 N  N     . ALA C 1 224 ? 18.283  25.830  45.023  1.00 69.85  ? 224 ALA C N     1 
ATOM   5239 C  CA    . ALA C 1 224 ? 19.400  25.683  44.106  1.00 69.96  ? 224 ALA C CA    1 
ATOM   5240 C  C     . ALA C 1 224 ? 19.751  24.217  43.846  1.00 70.77  ? 224 ALA C C     1 
ATOM   5241 O  O     . ALA C 1 224 ? 20.161  23.861  42.745  1.00 70.88  ? 224 ALA C O     1 
ATOM   5242 C  CB    . ALA C 1 224 ? 20.616  26.416  44.652  1.00 68.40  ? 224 ALA C CB    1 
ATOM   5243 N  N     . VAL C 1 225 ? 19.581  23.363  44.851  1.00 72.03  ? 225 VAL C N     1 
ATOM   5244 C  CA    . VAL C 1 225 ? 19.924  21.951  44.703  1.00 72.38  ? 225 VAL C CA    1 
ATOM   5245 C  C     . VAL C 1 225 ? 18.787  21.020  44.273  1.00 73.03  ? 225 VAL C C     1 
ATOM   5246 O  O     . VAL C 1 225 ? 19.039  19.929  43.761  1.00 72.83  ? 225 VAL C O     1 
ATOM   5247 C  CB    . VAL C 1 225 ? 20.557  21.415  46.003  1.00 71.28  ? 225 VAL C CB    1 
ATOM   5248 C  CG1   . VAL C 1 225 ? 20.917  19.947  45.855  1.00 71.61  ? 225 VAL C CG1   1 
ATOM   5249 C  CG2   . VAL C 1 225 ? 21.798  22.216  46.321  1.00 71.15  ? 225 VAL C CG2   1 
ATOM   5250 N  N     . ASP C 1 226 ? 17.543  21.440  44.467  1.00 73.93  ? 226 ASP C N     1 
ATOM   5251 C  CA    . ASP C 1 226 ? 16.424  20.596  44.077  1.00 75.41  ? 226 ASP C CA    1 
ATOM   5252 C  C     . ASP C 1 226 ? 16.583  20.204  42.601  1.00 75.71  ? 226 ASP C C     1 
ATOM   5253 O  O     . ASP C 1 226 ? 16.619  21.059  41.713  1.00 76.08  ? 226 ASP C O     1 
ATOM   5254 C  CB    . ASP C 1 226 ? 15.102  21.332  44.288  1.00 77.08  ? 226 ASP C CB    1 
ATOM   5255 C  CG    . ASP C 1 226 ? 13.896  20.426  44.117  1.00 79.28  ? 226 ASP C CG    1 
ATOM   5256 O  OD1   . ASP C 1 226 ? 13.951  19.486  43.290  1.00 79.72  ? 226 ASP C OD1   1 
ATOM   5257 O  OD2   . ASP C 1 226 ? 12.880  20.664  44.802  1.00 81.94  ? 226 ASP C OD2   1 
ATOM   5258 N  N     . PRO C 1 227 ? 16.703  18.896  42.330  1.00 75.56  ? 227 PRO C N     1 
ATOM   5259 C  CA    . PRO C 1 227 ? 16.867  18.334  40.988  1.00 75.18  ? 227 PRO C CA    1 
ATOM   5260 C  C     . PRO C 1 227 ? 15.598  18.210  40.159  1.00 74.92  ? 227 PRO C C     1 
ATOM   5261 O  O     . PRO C 1 227 ? 15.614  17.571  39.109  1.00 74.75  ? 227 PRO C O     1 
ATOM   5262 C  CB    . PRO C 1 227 ? 17.483  16.964  41.264  1.00 75.82  ? 227 PRO C CB    1 
ATOM   5263 C  CG    . PRO C 1 227 ? 18.144  17.132  42.595  1.00 75.52  ? 227 PRO C CG    1 
ATOM   5264 C  CD    . PRO C 1 227 ? 17.103  17.904  43.338  1.00 75.85  ? 227 PRO C CD    1 
ATOM   5265 N  N     . ARG C 1 228 ? 14.502  18.798  40.627  1.00 74.93  ? 228 ARG C N     1 
ATOM   5266 C  CA    . ARG C 1 228 ? 13.232  18.736  39.892  1.00 75.45  ? 228 ARG C CA    1 
ATOM   5267 C  C     . ARG C 1 228 ? 12.899  20.118  39.309  1.00 74.72  ? 228 ARG C C     1 
ATOM   5268 O  O     . ARG C 1 228 ? 11.871  20.307  38.650  1.00 74.27  ? 228 ARG C O     1 
ATOM   5269 C  CB    . ARG C 1 228 ? 12.095  18.297  40.823  1.00 76.71  ? 228 ARG C CB    1 
ATOM   5270 C  CG    . ARG C 1 228 ? 12.390  17.077  41.673  1.00 78.96  ? 228 ARG C CG    1 
ATOM   5271 C  CD    . ARG C 1 228 ? 11.284  16.873  42.694  1.00 80.53  ? 228 ARG C CD    1 
ATOM   5272 N  NE    . ARG C 1 228 ? 10.010  16.569  42.042  1.00 81.92  ? 228 ARG C NE    1 
ATOM   5273 C  CZ    . ARG C 1 228 ? 8.839   16.484  42.669  1.00 81.58  ? 228 ARG C CZ    1 
ATOM   5274 N  NH1   . ARG C 1 228 ? 8.763   16.682  43.979  1.00 81.69  ? 228 ARG C NH1   1 
ATOM   5275 N  NH2   . ARG C 1 228 ? 7.740   16.197  41.982  1.00 80.98  ? 228 ARG C NH2   1 
ATOM   5276 N  N     . ILE C 1 229 ? 13.778  21.081  39.565  1.00 73.25  ? 229 ILE C N     1 
ATOM   5277 C  CA    . ILE C 1 229 ? 13.590  22.438  39.086  1.00 70.18  ? 229 ILE C CA    1 
ATOM   5278 C  C     . ILE C 1 229 ? 14.909  22.974  38.528  1.00 70.10  ? 229 ILE C C     1 
ATOM   5279 O  O     . ILE C 1 229 ? 15.980  22.463  38.876  1.00 68.71  ? 229 ILE C O     1 
ATOM   5280 C  CB    . ILE C 1 229 ? 13.090  23.346  40.232  1.00 68.10  ? 229 ILE C CB    1 
ATOM   5281 C  CG1   . ILE C 1 229 ? 14.091  23.337  41.381  1.00 66.92  ? 229 ILE C CG1   1 
ATOM   5282 C  CG2   . ILE C 1 229 ? 11.758  22.840  40.750  1.00 65.51  ? 229 ILE C CG2   1 
ATOM   5283 C  CD1   . ILE C 1 229 ? 13.797  24.367  42.441  1.00 65.96  ? 229 ILE C CD1   1 
ATOM   5284 N  N     . GLU C 1 230 ? 14.823  23.986  37.655  1.00 70.70  ? 230 GLU C N     1 
ATOM   5285 C  CA    . GLU C 1 230 ? 16.006  24.607  37.045  1.00 71.18  ? 230 GLU C CA    1 
ATOM   5286 C  C     . GLU C 1 230 ? 16.361  25.955  37.694  1.00 70.31  ? 230 GLU C C     1 
ATOM   5287 O  O     . GLU C 1 230 ? 17.540  26.263  37.887  1.00 72.32  ? 230 GLU C O     1 
ATOM   5288 C  CB    . GLU C 1 230 ? 15.813  24.797  35.530  1.00 72.91  ? 230 GLU C CB    1 
ATOM   5289 C  CG    . GLU C 1 230 ? 15.817  23.504  34.707  1.00 75.07  ? 230 GLU C CG    1 
ATOM   5290 C  CD    . GLU C 1 230 ? 15.407  23.709  33.232  1.00 77.50  ? 230 GLU C CD    1 
ATOM   5291 O  OE1   . GLU C 1 230 ? 14.553  24.582  32.932  1.00 77.29  ? 230 GLU C OE1   1 
ATOM   5292 O  OE2   . GLU C 1 230 ? 15.927  22.969  32.369  1.00 78.13  ? 230 GLU C OE2   1 
ATOM   5293 N  N     . ILE C 1 231 ? 15.355  26.752  38.033  1.00 66.97  ? 231 ILE C N     1 
ATOM   5294 C  CA    . ILE C 1 231 ? 15.572  28.053  38.678  1.00 65.65  ? 231 ILE C CA    1 
ATOM   5295 C  C     . ILE C 1 231 ? 16.511  29.044  37.999  1.00 65.03  ? 231 ILE C C     1 
ATOM   5296 O  O     . ILE C 1 231 ? 17.457  28.688  37.301  1.00 63.81  ? 231 ILE C O     1 
ATOM   5297 C  CB    . ILE C 1 231 ? 16.066  27.940  40.149  1.00 64.53  ? 231 ILE C CB    1 
ATOM   5298 C  CG1   . ILE C 1 231 ? 17.592  27.924  40.202  1.00 63.32  ? 231 ILE C CG1   1 
ATOM   5299 C  CG2   . ILE C 1 231 ? 15.498  26.704  40.795  1.00 66.12  ? 231 ILE C CG2   1 
ATOM   5300 C  CD1   . ILE C 1 231 ? 18.139  28.121  41.586  1.00 62.24  ? 231 ILE C CD1   1 
ATOM   5301 N  N     . CYS C 1 232 ? 16.250  30.310  38.289  1.00 64.69  ? 232 CYS C N     1 
ATOM   5302 C  CA    . CYS C 1 232 ? 16.977  31.418  37.721  1.00 64.22  ? 232 CYS C CA    1 
ATOM   5303 C  C     . CYS C 1 232 ? 16.668  32.621  38.638  1.00 62.82  ? 232 CYS C C     1 
ATOM   5304 O  O     . CYS C 1 232 ? 15.511  32.998  38.782  1.00 62.76  ? 232 CYS C O     1 
ATOM   5305 C  CB    . CYS C 1 232 ? 16.436  31.587  36.298  1.00 65.33  ? 232 CYS C CB    1 
ATOM   5306 S  SG    . CYS C 1 232 ? 17.009  32.964  35.363  1.00 71.52  ? 232 CYS C SG    1 
ATOM   5307 N  N     . MET C 1 233 ? 17.689  33.199  39.274  1.00 62.44  ? 233 MET C N     1 
ATOM   5308 C  CA    . MET C 1 233 ? 17.506  34.337  40.200  1.00 63.16  ? 233 MET C CA    1 
ATOM   5309 C  C     . MET C 1 233 ? 17.611  35.733  39.592  1.00 63.05  ? 233 MET C C     1 
ATOM   5310 O  O     . MET C 1 233 ? 18.707  36.281  39.450  1.00 62.65  ? 233 MET C O     1 
ATOM   5311 C  CB    . MET C 1 233 ? 18.510  34.255  41.342  1.00 64.08  ? 233 MET C CB    1 
ATOM   5312 C  CG    . MET C 1 233 ? 18.227  33.160  42.330  1.00 68.60  ? 233 MET C CG    1 
ATOM   5313 S  SD    . MET C 1 233 ? 19.519  33.104  43.561  1.00 73.99  ? 233 MET C SD    1 
ATOM   5314 C  CE    . MET C 1 233 ? 19.445  34.796  44.191  1.00 72.90  ? 233 MET C CE    1 
ATOM   5315 N  N     . LEU C 1 234 ? 16.468  36.331  39.282  1.00 63.08  ? 234 LEU C N     1 
ATOM   5316 C  CA    . LEU C 1 234 ? 16.460  37.645  38.662  1.00 64.07  ? 234 LEU C CA    1 
ATOM   5317 C  C     . LEU C 1 234 ? 16.408  38.791  39.645  1.00 64.18  ? 234 LEU C C     1 
ATOM   5318 O  O     . LEU C 1 234 ? 15.702  38.726  40.640  1.00 64.54  ? 234 LEU C O     1 
ATOM   5319 C  CB    . LEU C 1 234 ? 15.273  37.762  37.715  1.00 64.16  ? 234 LEU C CB    1 
ATOM   5320 C  CG    . LEU C 1 234 ? 14.951  36.506  36.914  1.00 64.74  ? 234 LEU C CG    1 
ATOM   5321 C  CD1   . LEU C 1 234 ? 13.872  36.863  35.928  1.00 65.27  ? 234 LEU C CD1   1 
ATOM   5322 C  CD2   . LEU C 1 234 ? 16.181  35.971  36.191  1.00 64.26  ? 234 LEU C CD2   1 
ATOM   5323 N  N     . PRO C 1 235 ? 17.167  39.861  39.376  1.00 65.01  ? 235 PRO C N     1 
ATOM   5324 C  CA    . PRO C 1 235 ? 17.183  41.029  40.257  1.00 65.92  ? 235 PRO C CA    1 
ATOM   5325 C  C     . PRO C 1 235 ? 16.055  41.985  39.892  1.00 66.61  ? 235 PRO C C     1 
ATOM   5326 O  O     . PRO C 1 235 ? 16.286  43.150  39.576  1.00 67.66  ? 235 PRO C O     1 
ATOM   5327 C  CB    . PRO C 1 235 ? 18.557  41.626  40.001  1.00 65.84  ? 235 PRO C CB    1 
ATOM   5328 C  CG    . PRO C 1 235 ? 18.728  41.371  38.535  1.00 65.89  ? 235 PRO C CG    1 
ATOM   5329 C  CD    . PRO C 1 235 ? 18.270  39.932  38.403  1.00 64.72  ? 235 PRO C CD    1 
ATOM   5330 N  N     . VAL C 1 236 ? 14.832  41.471  39.917  1.00 66.86  ? 236 VAL C N     1 
ATOM   5331 C  CA    . VAL C 1 236 ? 13.658  42.272  39.614  1.00 67.27  ? 236 VAL C CA    1 
ATOM   5332 C  C     . VAL C 1 236 ? 13.097  42.725  40.951  1.00 68.49  ? 236 VAL C C     1 
ATOM   5333 O  O     . VAL C 1 236 ? 12.696  41.902  41.773  1.00 68.65  ? 236 VAL C O     1 
ATOM   5334 C  CB    . VAL C 1 236 ? 12.608  41.434  38.864  1.00 66.52  ? 236 VAL C CB    1 
ATOM   5335 C  CG1   . VAL C 1 236 ? 11.331  42.235  38.653  1.00 66.13  ? 236 VAL C CG1   1 
ATOM   5336 C  CG2   . VAL C 1 236 ? 13.177  41.002  37.536  1.00 66.85  ? 236 VAL C CG2   1 
ATOM   5337 N  N     . GLY C 1 237 ? 13.081  44.034  41.176  1.00 69.99  ? 237 GLY C N     1 
ATOM   5338 C  CA    . GLY C 1 237 ? 12.577  44.549  42.439  1.00 71.35  ? 237 GLY C CA    1 
ATOM   5339 C  C     . GLY C 1 237 ? 13.434  44.092  43.611  1.00 72.51  ? 237 GLY C C     1 
ATOM   5340 O  O     . GLY C 1 237 ? 14.554  44.580  43.805  1.00 72.54  ? 237 GLY C O     1 
ATOM   5341 N  N     . ASP C 1 238 ? 12.918  43.147  44.392  1.00 73.22  ? 238 ASP C N     1 
ATOM   5342 C  CA    . ASP C 1 238 ? 13.656  42.635  45.541  1.00 73.28  ? 238 ASP C CA    1 
ATOM   5343 C  C     . ASP C 1 238 ? 14.156  41.210  45.279  1.00 71.23  ? 238 ASP C C     1 
ATOM   5344 O  O     . ASP C 1 238 ? 14.466  40.457  46.199  1.00 69.64  ? 238 ASP C O     1 
ATOM   5345 C  CB    . ASP C 1 238 ? 12.767  42.679  46.788  1.00 76.99  ? 238 ASP C CB    1 
ATOM   5346 C  CG    . ASP C 1 238 ? 13.559  42.500  48.074  1.00 80.89  ? 238 ASP C CG    1 
ATOM   5347 O  OD1   . ASP C 1 238 ? 14.591  43.202  48.230  1.00 82.37  ? 238 ASP C OD1   1 
ATOM   5348 O  OD2   . ASP C 1 238 ? 13.147  41.667  48.923  1.00 81.52  ? 238 ASP C OD2   1 
ATOM   5349 N  N     . GLY C 1 239 ? 14.246  40.853  44.004  1.00 70.29  ? 239 GLY C N     1 
ATOM   5350 C  CA    . GLY C 1 239 ? 14.719  39.533  43.639  1.00 67.98  ? 239 GLY C CA    1 
ATOM   5351 C  C     . GLY C 1 239 ? 13.577  38.552  43.547  1.00 66.67  ? 239 GLY C C     1 
ATOM   5352 O  O     . GLY C 1 239 ? 12.758  38.473  44.449  1.00 68.46  ? 239 GLY C O     1 
ATOM   5353 N  N     . ILE C 1 240 ? 13.513  37.812  42.449  1.00 64.72  ? 240 ILE C N     1 
ATOM   5354 C  CA    . ILE C 1 240 ? 12.464  36.824  42.255  1.00 62.83  ? 240 ILE C CA    1 
ATOM   5355 C  C     . ILE C 1 240 ? 13.104  35.586  41.668  1.00 62.44  ? 240 ILE C C     1 
ATOM   5356 O  O     . ILE C 1 240 ? 13.754  35.657  40.632  1.00 62.69  ? 240 ILE C O     1 
ATOM   5357 C  CB    . ILE C 1 240 ? 11.392  37.324  41.278  1.00 62.06  ? 240 ILE C CB    1 
ATOM   5358 C  CG1   . ILE C 1 240 ? 10.749  38.595  41.831  1.00 62.96  ? 240 ILE C CG1   1 
ATOM   5359 C  CG2   . ILE C 1 240 ? 10.355  36.244  41.046  1.00 59.66  ? 240 ILE C CG2   1 
ATOM   5360 C  CD1   . ILE C 1 240 ? 9.611   39.130  40.982  1.00 64.86  ? 240 ILE C CD1   1 
ATOM   5361 N  N     . THR C 1 241 ? 12.944  34.454  42.338  1.00 61.92  ? 241 THR C N     1 
ATOM   5362 C  CA    . THR C 1 241 ? 13.514  33.221  41.831  1.00 62.30  ? 241 THR C CA    1 
ATOM   5363 C  C     . THR C 1 241 ? 12.444  32.484  41.036  1.00 62.92  ? 241 THR C C     1 
ATOM   5364 O  O     . THR C 1 241 ? 11.415  32.086  41.582  1.00 63.52  ? 241 THR C O     1 
ATOM   5365 C  CB    . THR C 1 241 ? 14.023  32.296  42.969  1.00 61.95  ? 241 THR C CB    1 
ATOM   5366 O  OG1   . THR C 1 241 ? 15.207  32.849  43.564  1.00 60.66  ? 241 THR C OG1   1 
ATOM   5367 C  CG2   . THR C 1 241 ? 14.347  30.910  42.417  1.00 62.65  ? 241 THR C CG2   1 
ATOM   5368 N  N     . ILE C 1 242 ? 12.677  32.335  39.735  1.00 62.93  ? 242 ILE C N     1 
ATOM   5369 C  CA    . ILE C 1 242 ? 11.752  31.622  38.871  1.00 62.32  ? 242 ILE C CA    1 
ATOM   5370 C  C     . ILE C 1 242 ? 12.217  30.183  38.914  1.00 62.94  ? 242 ILE C C     1 
ATOM   5371 O  O     . ILE C 1 242 ? 13.409  29.915  38.821  1.00 61.94  ? 242 ILE C O     1 
ATOM   5372 C  CB    . ILE C 1 242 ? 11.810  32.154  37.416  1.00 62.01  ? 242 ILE C CB    1 
ATOM   5373 C  CG1   . ILE C 1 242 ? 10.706  33.175  37.192  1.00 61.81  ? 242 ILE C CG1   1 
ATOM   5374 C  CG2   . ILE C 1 242 ? 11.616  31.030  36.424  1.00 62.38  ? 242 ILE C CG2   1 
ATOM   5375 C  CD1   . ILE C 1 242 ? 10.672  34.265  38.219  1.00 63.62  ? 242 ILE C CD1   1 
ATOM   5376 N  N     . CYS C 1 243 ? 11.283  29.258  39.085  1.00 64.63  ? 243 CYS C N     1 
ATOM   5377 C  CA    . CYS C 1 243 ? 11.631  27.847  39.139  1.00 65.98  ? 243 CYS C CA    1 
ATOM   5378 C  C     . CYS C 1 243 ? 10.893  27.138  38.025  1.00 67.04  ? 243 CYS C C     1 
ATOM   5379 O  O     . CYS C 1 243 ? 9.730   27.415  37.765  1.00 65.80  ? 243 CYS C O     1 
ATOM   5380 C  CB    . CYS C 1 243 ? 11.232  27.236  40.489  1.00 66.14  ? 243 CYS C CB    1 
ATOM   5381 S  SG    . CYS C 1 243 ? 12.096  27.897  41.949  1.00 69.08  ? 243 CYS C SG    1 
ATOM   5382 N  N     . ARG C 1 244 ? 11.573  26.231  37.347  1.00 68.70  ? 244 ARG C N     1 
ATOM   5383 C  CA    . ARG C 1 244 ? 10.925  25.498  36.285  1.00 70.82  ? 244 ARG C CA    1 
ATOM   5384 C  C     . ARG C 1 244 ? 11.005  24.031  36.650  1.00 73.18  ? 244 ARG C C     1 
ATOM   5385 O  O     . ARG C 1 244 ? 12.095  23.486  36.805  1.00 74.77  ? 244 ARG C O     1 
ATOM   5386 C  CB    . ARG C 1 244 ? 11.622  25.762  34.950  1.00 70.26  ? 244 ARG C CB    1 
ATOM   5387 C  CG    . ARG C 1 244 ? 11.119  24.879  33.828  1.00 69.25  ? 244 ARG C CG    1 
ATOM   5388 C  CD    . ARG C 1 244 ? 11.451  25.430  32.466  1.00 67.98  ? 244 ARG C CD    1 
ATOM   5389 N  NE    . ARG C 1 244 ? 11.015  24.499  31.436  1.00 68.01  ? 244 ARG C NE    1 
ATOM   5390 C  CZ    . ARG C 1 244 ? 11.687  23.407  31.083  1.00 68.56  ? 244 ARG C CZ    1 
ATOM   5391 N  NH1   . ARG C 1 244 ? 12.843  23.109  31.673  1.00 66.66  ? 244 ARG C NH1   1 
ATOM   5392 N  NH2   . ARG C 1 244 ? 11.191  22.602  30.149  1.00 68.87  ? 244 ARG C NH2   1 
ATOM   5393 N  N     . ARG C 1 245 ? 9.854   23.390  36.806  1.00 74.60  ? 245 ARG C N     1 
ATOM   5394 C  CA    . ARG C 1 245 ? 9.846   21.983  37.162  1.00 76.74  ? 245 ARG C CA    1 
ATOM   5395 C  C     . ARG C 1 245 ? 10.313  21.151  35.975  1.00 77.56  ? 245 ARG C C     1 
ATOM   5396 O  O     . ARG C 1 245 ? 9.791   21.283  34.873  1.00 76.14  ? 245 ARG C O     1 
ATOM   5397 C  CB    . ARG C 1 245 ? 8.440   21.552  37.575  1.00 78.62  ? 245 ARG C CB    1 
ATOM   5398 C  CG    . ARG C 1 245 ? 8.395   20.192  38.232  1.00 79.69  ? 245 ARG C CG    1 
ATOM   5399 C  CD    . ARG C 1 245 ? 6.984   19.650  38.307  1.00 80.93  ? 245 ARG C CD    1 
ATOM   5400 N  NE    . ARG C 1 245 ? 6.964   18.386  39.035  1.00 82.41  ? 245 ARG C NE    1 
ATOM   5401 C  CZ    . ARG C 1 245 ? 5.943   17.538  39.044  1.00 82.54  ? 245 ARG C CZ    1 
ATOM   5402 N  NH1   . ARG C 1 245 ? 4.839   17.809  38.362  1.00 82.34  ? 245 ARG C NH1   1 
ATOM   5403 N  NH2   . ARG C 1 245 ? 6.033   16.412  39.733  1.00 83.48  ? 245 ARG C NH2   1 
ATOM   5404 N  N     . ILE C 1 246 ? 11.303  20.297  36.202  1.00 79.34  ? 246 ILE C N     1 
ATOM   5405 C  CA    . ILE C 1 246 ? 11.824  19.454  35.137  1.00 81.83  ? 246 ILE C CA    1 
ATOM   5406 C  C     . ILE C 1 246 ? 11.475  17.990  35.362  1.00 84.33  ? 246 ILE C C     1 
ATOM   5407 O  O     . ILE C 1 246 ? 11.305  17.234  34.402  1.00 84.74  ? 246 ILE C O     1 
ATOM   5408 C  CB    . ILE C 1 246 ? 13.347  19.575  35.023  1.00 80.99  ? 246 ILE C CB    1 
ATOM   5409 C  CG1   . ILE C 1 246 ? 14.003  19.170  36.343  1.00 81.52  ? 246 ILE C CG1   1 
ATOM   5410 C  CG2   . ILE C 1 246 ? 13.715  20.988  34.656  1.00 80.65  ? 246 ILE C CG2   1 
ATOM   5411 C  CD1   . ILE C 1 246 ? 15.515  19.147  36.303  1.00 81.44  ? 246 ILE C CD1   1 
ATOM   5412 N  N     . LYS C 1 247 ? 11.377  17.587  36.626  1.00 86.32  ? 247 LYS C N     1 
ATOM   5413 C  CA    . LYS C 1 247 ? 11.040  16.203  36.946  1.00 87.90  ? 247 LYS C CA    1 
ATOM   5414 C  C     . LYS C 1 247 ? 9.674   16.135  37.611  1.00 88.27  ? 247 LYS C C     1 
ATOM   5415 O  O     . LYS C 1 247 ? 9.342   17.083  38.359  1.00 88.60  ? 247 LYS C O     1 
ATOM   5416 C  CB    . LYS C 1 247 ? 12.091  15.601  37.881  1.00 89.21  ? 247 LYS C CB    1 
ATOM   5417 C  CG    . LYS C 1 247 ? 13.476  15.479  37.272  1.00 91.40  ? 247 LYS C CG    1 
ATOM   5418 C  CD    . LYS C 1 247 ? 14.469  14.912  38.285  1.00 92.58  ? 247 LYS C CD    1 
ATOM   5419 C  CE    . LYS C 1 247 ? 15.884  14.871  37.726  1.00 92.76  ? 247 LYS C CE    1 
ATOM   5420 N  NZ    . LYS C 1 247 ? 16.835  14.324  38.726  1.00 92.60  ? 247 LYS C NZ    1 
ATOM   5421 O  OXT   . LYS C 1 247 ? 8.964   15.130  37.387  1.00 87.90  ? 247 LYS C OXT   1 
ATOM   5422 N  N     . LYS D 1 21  ? 5.538   43.233  93.370  1.00 109.60 ? 21  LYS D N     1 
ATOM   5423 C  CA    . LYS D 1 21  ? 5.542   43.053  91.888  1.00 109.56 ? 21  LYS D CA    1 
ATOM   5424 C  C     . LYS D 1 21  ? 4.966   44.292  91.197  1.00 109.41 ? 21  LYS D C     1 
ATOM   5425 O  O     . LYS D 1 21  ? 4.944   45.385  91.777  1.00 109.54 ? 21  LYS D O     1 
ATOM   5426 C  CB    . LYS D 1 21  ? 4.727   41.807  91.509  1.00 109.89 ? 21  LYS D CB    1 
ATOM   5427 C  CG    . LYS D 1 21  ? 4.858   41.385  90.050  1.00 110.66 ? 21  LYS D CG    1 
ATOM   5428 C  CD    . LYS D 1 21  ? 4.349   39.975  89.830  1.00 111.66 ? 21  LYS D CD    1 
ATOM   5429 C  CE    . LYS D 1 21  ? 2.877   39.853  90.175  1.00 112.82 ? 21  LYS D CE    1 
ATOM   5430 N  NZ    . LYS D 1 21  ? 2.419   38.434  90.084  1.00 112.97 ? 21  LYS D NZ    1 
ATOM   5431 N  N     . SER D 1 22  ? 4.505   44.114  89.961  1.00 108.68 ? 22  SER D N     1 
ATOM   5432 C  CA    . SER D 1 22  ? 3.931   45.201  89.171  1.00 107.19 ? 22  SER D CA    1 
ATOM   5433 C  C     . SER D 1 22  ? 2.477   44.912  88.795  1.00 105.72 ? 22  SER D C     1 
ATOM   5434 O  O     . SER D 1 22  ? 1.925   43.875  89.172  1.00 105.31 ? 22  SER D O     1 
ATOM   5435 C  CB    . SER D 1 22  ? 4.758   45.408  87.897  1.00 107.52 ? 22  SER D CB    1 
ATOM   5436 O  OG    . SER D 1 22  ? 4.122   46.313  87.010  1.00 107.10 ? 22  SER D OG    1 
ATOM   5437 N  N     . LEU D 1 23  ? 1.874   45.841  88.055  1.00 103.99 ? 23  LEU D N     1 
ATOM   5438 C  CA    . LEU D 1 23  ? 0.490   45.722  87.596  1.00 102.23 ? 23  LEU D CA    1 
ATOM   5439 C  C     . LEU D 1 23  ? 0.423   45.476  86.092  1.00 101.25 ? 23  LEU D C     1 
ATOM   5440 O  O     . LEU D 1 23  ? -0.656  45.536  85.497  1.00 100.51 ? 23  LEU D O     1 
ATOM   5441 C  CB    . LEU D 1 23  ? -0.289  47.000  87.917  1.00 101.98 ? 23  LEU D CB    1 
ATOM   5442 C  CG    . LEU D 1 23  ? -0.743  47.246  89.357  1.00 102.50 ? 23  LEU D CG    1 
ATOM   5443 C  CD1   . LEU D 1 23  ? -1.345  48.640  89.474  1.00 102.12 ? 23  LEU D CD1   1 
ATOM   5444 C  CD2   . LEU D 1 23  ? -1.765  46.191  89.758  1.00 101.92 ? 23  LEU D CD2   1 
ATOM   5445 N  N     . LEU D 1 24  ? 1.574   45.196  85.484  1.00 100.54 ? 24  LEU D N     1 
ATOM   5446 C  CA    . LEU D 1 24  ? 1.655   44.963  84.041  1.00 99.85  ? 24  LEU D CA    1 
ATOM   5447 C  C     . LEU D 1 24  ? 1.556   43.488  83.631  1.00 99.83  ? 24  LEU D C     1 
ATOM   5448 O  O     . LEU D 1 24  ? 0.913   42.690  84.314  1.00 99.63  ? 24  LEU D O     1 
ATOM   5449 C  CB    . LEU D 1 24  ? 2.946   45.581  83.501  1.00 98.40  ? 24  LEU D CB    1 
ATOM   5450 C  CG    . LEU D 1 24  ? 3.069   47.079  83.802  1.00 97.52  ? 24  LEU D CG    1 
ATOM   5451 C  CD1   . LEU D 1 24  ? 4.429   47.584  83.365  1.00 96.87  ? 24  LEU D CD1   1 
ATOM   5452 C  CD2   . LEU D 1 24  ? 1.956   47.842  83.101  1.00 96.10  ? 24  LEU D CD2   1 
ATOM   5453 N  N     . GLN D 1 25  ? 2.190   43.128  82.517  1.00 99.67  ? 25  GLN D N     1 
ATOM   5454 C  CA    . GLN D 1 25  ? 2.132   41.752  82.024  1.00 99.14  ? 25  GLN D CA    1 
ATOM   5455 C  C     . GLN D 1 25  ? 3.296   40.891  82.475  1.00 98.95  ? 25  GLN D C     1 
ATOM   5456 O  O     . GLN D 1 25  ? 3.161   39.678  82.619  1.00 98.60  ? 25  GLN D O     1 
ATOM   5457 C  CB    . GLN D 1 25  ? 2.099   41.724  80.494  1.00 99.72  ? 25  GLN D CB    1 
ATOM   5458 C  CG    . GLN D 1 25  ? 1.085   42.643  79.832  1.00 99.06  ? 25  GLN D CG    1 
ATOM   5459 C  CD    . GLN D 1 25  ? 1.065   42.479  78.317  1.00 98.45  ? 25  GLN D CD    1 
ATOM   5460 O  OE1   . GLN D 1 25  ? 2.114   42.481  77.665  1.00 97.67  ? 25  GLN D OE1   1 
ATOM   5461 N  NE2   . GLN D 1 25  ? -0.130  42.338  77.751  1.00 97.30  ? 25  GLN D NE2   1 
ATOM   5462 N  N     . SER D 1 26  ? 4.445   41.516  82.683  1.00 99.36  ? 26  SER D N     1 
ATOM   5463 C  CA    . SER D 1 26  ? 5.624   40.772  83.089  1.00 101.08 ? 26  SER D CA    1 
ATOM   5464 C  C     . SER D 1 26  ? 6.569   41.631  83.904  1.00 102.49 ? 26  SER D C     1 
ATOM   5465 O  O     . SER D 1 26  ? 6.656   42.842  83.692  1.00 102.47 ? 26  SER D O     1 
ATOM   5466 C  CB    . SER D 1 26  ? 6.369   40.280  81.854  1.00 101.11 ? 26  SER D CB    1 
ATOM   5467 O  OG    . SER D 1 26  ? 6.895   41.381  81.131  1.00 100.73 ? 26  SER D OG    1 
ATOM   5468 N  N     . ASP D 1 27  ? 7.285   41.002  84.833  1.00 103.28 ? 27  ASP D N     1 
ATOM   5469 C  CA    . ASP D 1 27  ? 8.256   41.728  85.645  1.00 104.79 ? 27  ASP D CA    1 
ATOM   5470 C  C     . ASP D 1 27  ? 9.176   42.443  84.648  1.00 104.41 ? 27  ASP D C     1 
ATOM   5471 O  O     . ASP D 1 27  ? 9.790   43.467  84.962  1.00 104.30 ? 27  ASP D O     1 
ATOM   5472 C  CB    . ASP D 1 27  ? 9.089   40.749  86.499  1.00 106.16 ? 27  ASP D CB    1 
ATOM   5473 C  CG    . ASP D 1 27  ? 8.607   40.654  87.950  1.00 107.56 ? 27  ASP D CG    1 
ATOM   5474 O  OD1   . ASP D 1 27  ? 8.743   41.658  88.689  1.00 107.42 ? 27  ASP D OD1   1 
ATOM   5475 O  OD2   . ASP D 1 27  ? 8.100   39.576  88.348  1.00 107.30 ? 27  ASP D OD2   1 
ATOM   5476 N  N     . ALA D 1 28  ? 9.228   41.890  83.435  1.00 103.05 ? 28  ALA D N     1 
ATOM   5477 C  CA    . ALA D 1 28  ? 10.074  42.385  82.353  1.00 102.22 ? 28  ALA D CA    1 
ATOM   5478 C  C     . ALA D 1 28  ? 9.588   43.596  81.552  1.00 102.05 ? 28  ALA D C     1 
ATOM   5479 O  O     . ALA D 1 28  ? 10.405  44.424  81.149  1.00 100.59 ? 28  ALA D O     1 
ATOM   5480 C  CB    . ALA D 1 28  ? 10.391  41.238  81.404  1.00 100.81 ? 28  ALA D CB    1 
ATOM   5481 N  N     . LEU D 1 29  ? 8.286   43.700  81.294  1.00 101.51 ? 29  LEU D N     1 
ATOM   5482 C  CA    . LEU D 1 29  ? 7.789   44.846  80.537  1.00 102.73 ? 29  LEU D CA    1 
ATOM   5483 C  C     . LEU D 1 29  ? 8.087   46.050  81.413  1.00 104.31 ? 29  LEU D C     1 
ATOM   5484 O  O     . LEU D 1 29  ? 8.610   47.063  80.948  1.00 104.80 ? 29  LEU D O     1 
ATOM   5485 C  CB    . LEU D 1 29  ? 6.278   44.734  80.275  1.00 101.07 ? 29  LEU D CB    1 
ATOM   5486 C  CG    . LEU D 1 29  ? 5.706   45.540  79.093  1.00 98.93  ? 29  LEU D CG    1 
ATOM   5487 C  CD1   . LEU D 1 29  ? 4.257   45.147  78.864  1.00 98.10  ? 29  LEU D CD1   1 
ATOM   5488 C  CD2   . LEU D 1 29  ? 5.827   47.040  79.339  1.00 98.32  ? 29  LEU D CD2   1 
ATOM   5489 N  N     . TYR D 1 30  ? 7.758   45.912  82.694  1.00 105.75 ? 30  TYR D N     1 
ATOM   5490 C  CA    . TYR D 1 30  ? 7.990   46.953  83.694  1.00 107.65 ? 30  TYR D CA    1 
ATOM   5491 C  C     . TYR D 1 30  ? 9.508   47.119  83.807  1.00 108.08 ? 30  TYR D C     1 
ATOM   5492 O  O     . TYR D 1 30  ? 10.034  48.236  83.864  1.00 106.75 ? 30  TYR D O     1 
ATOM   5493 C  CB    . TYR D 1 30  ? 7.384   46.503  85.039  1.00 107.72 ? 30  TYR D CB    1 
ATOM   5494 C  CG    . TYR D 1 30  ? 7.433   47.516  86.174  1.00 108.75 ? 30  TYR D CG    1 
ATOM   5495 C  CD1   . TYR D 1 30  ? 8.630   47.808  86.836  1.00 108.94 ? 30  TYR D CD1   1 
ATOM   5496 C  CD2   . TYR D 1 30  ? 6.278   48.179  86.588  1.00 109.33 ? 30  TYR D CD2   1 
ATOM   5497 C  CE1   . TYR D 1 30  ? 8.673   48.736  87.880  1.00 108.53 ? 30  TYR D CE1   1 
ATOM   5498 C  CE2   . TYR D 1 30  ? 6.310   49.107  87.628  1.00 109.56 ? 30  TYR D CE2   1 
ATOM   5499 C  CZ    . TYR D 1 30  ? 7.509   49.383  88.268  1.00 109.36 ? 30  TYR D CZ    1 
ATOM   5500 O  OH    . TYR D 1 30  ? 7.541   50.323  89.276  1.00 109.49 ? 30  TYR D OH    1 
ATOM   5501 N  N     . GLN D 1 31  ? 10.202  45.986  83.814  1.00 109.17 ? 31  GLN D N     1 
ATOM   5502 C  CA    . GLN D 1 31  ? 11.652  45.967  83.916  1.00 111.53 ? 31  GLN D CA    1 
ATOM   5503 C  C     . GLN D 1 31  ? 12.321  46.787  82.817  1.00 112.44 ? 31  GLN D C     1 
ATOM   5504 O  O     . GLN D 1 31  ? 13.393  47.354  83.020  1.00 111.92 ? 31  GLN D O     1 
ATOM   5505 C  CB    . GLN D 1 31  ? 12.155  44.527  83.858  1.00 112.28 ? 31  GLN D CB    1 
ATOM   5506 C  CG    . GLN D 1 31  ? 13.603  44.402  84.242  1.00 113.22 ? 31  GLN D CG    1 
ATOM   5507 C  CD    . GLN D 1 31  ? 13.929  45.279  85.431  1.00 113.67 ? 31  GLN D CD    1 
ATOM   5508 O  OE1   . GLN D 1 31  ? 13.240  45.241  86.454  1.00 112.66 ? 31  GLN D OE1   1 
ATOM   5509 N  NE2   . GLN D 1 31  ? 14.981  46.082  85.302  1.00 113.70 ? 31  GLN D NE2   1 
ATOM   5510 N  N     . TYR D 1 32  ? 11.689  46.833  81.648  1.00 114.53 ? 32  TYR D N     1 
ATOM   5511 C  CA    . TYR D 1 32  ? 12.217  47.591  80.517  1.00 115.61 ? 32  TYR D CA    1 
ATOM   5512 C  C     . TYR D 1 32  ? 12.029  49.071  80.812  1.00 115.71 ? 32  TYR D C     1 
ATOM   5513 O  O     . TYR D 1 32  ? 12.979  49.849  80.761  1.00 115.91 ? 32  TYR D O     1 
ATOM   5514 C  CB    . TYR D 1 32  ? 11.477  47.209  79.223  1.00 116.49 ? 32  TYR D CB    1 
ATOM   5515 C  CG    . TYR D 1 32  ? 11.918  47.968  77.975  1.00 117.93 ? 32  TYR D CG    1 
ATOM   5516 C  CD1   . TYR D 1 32  ? 13.254  47.971  77.562  1.00 117.73 ? 32  TYR D CD1   1 
ATOM   5517 C  CD2   . TYR D 1 32  ? 10.991  48.673  77.199  1.00 118.28 ? 32  TYR D CD2   1 
ATOM   5518 C  CE1   . TYR D 1 32  ? 13.654  48.657  76.408  1.00 117.67 ? 32  TYR D CE1   1 
ATOM   5519 C  CE2   . TYR D 1 32  ? 11.382  49.360  76.043  1.00 117.83 ? 32  TYR D CE2   1 
ATOM   5520 C  CZ    . TYR D 1 32  ? 12.711  49.348  75.657  1.00 117.77 ? 32  TYR D CZ    1 
ATOM   5521 O  OH    . TYR D 1 32  ? 13.095  50.032  74.527  1.00 117.86 ? 32  TYR D OH    1 
ATOM   5522 N  N     . ILE D 1 33  ? 10.797  49.448  81.137  1.00 115.86 ? 33  ILE D N     1 
ATOM   5523 C  CA    . ILE D 1 33  ? 10.472  50.833  81.437  1.00 116.06 ? 33  ILE D CA    1 
ATOM   5524 C  C     . ILE D 1 33  ? 11.409  51.417  82.485  1.00 116.56 ? 33  ILE D C     1 
ATOM   5525 O  O     . ILE D 1 33  ? 11.646  52.623  82.513  1.00 116.25 ? 33  ILE D O     1 
ATOM   5526 C  CB    . ILE D 1 33  ? 9.028   50.962  81.938  1.00 115.98 ? 33  ILE D CB    1 
ATOM   5527 C  CG1   . ILE D 1 33  ? 8.089   50.210  80.995  1.00 116.14 ? 33  ILE D CG1   1 
ATOM   5528 C  CG2   . ILE D 1 33  ? 8.629   52.431  81.999  1.00 115.53 ? 33  ILE D CG2   1 
ATOM   5529 C  CD1   . ILE D 1 33  ? 6.635   50.269  81.405  1.00 116.91 ? 33  ILE D CD1   1 
ATOM   5530 N  N     . LEU D 1 34  ? 11.943  50.563  83.349  1.00 117.55 ? 34  LEU D N     1 
ATOM   5531 C  CA    . LEU D 1 34  ? 12.859  51.031  84.379  1.00 119.15 ? 34  LEU D CA    1 
ATOM   5532 C  C     . LEU D 1 34  ? 14.251  51.269  83.805  1.00 120.03 ? 34  LEU D C     1 
ATOM   5533 O  O     . LEU D 1 34  ? 14.849  52.324  84.016  1.00 120.22 ? 34  LEU D O     1 
ATOM   5534 C  CB    . LEU D 1 34  ? 12.953  50.015  85.524  1.00 119.82 ? 34  LEU D CB    1 
ATOM   5535 C  CG    . LEU D 1 34  ? 11.739  49.792  86.431  1.00 120.04 ? 34  LEU D CG    1 
ATOM   5536 C  CD1   . LEU D 1 34  ? 12.104  48.793  87.525  1.00 119.80 ? 34  LEU D CD1   1 
ATOM   5537 C  CD2   . LEU D 1 34  ? 11.300  51.112  87.048  1.00 120.00 ? 34  LEU D CD2   1 
ATOM   5538 N  N     . GLU D 1 35  ? 14.752  50.278  83.072  1.00 121.05 ? 35  GLU D N     1 
ATOM   5539 C  CA    . GLU D 1 35  ? 16.078  50.332  82.464  1.00 121.94 ? 35  GLU D CA    1 
ATOM   5540 C  C     . GLU D 1 35  ? 16.272  51.476  81.469  1.00 122.53 ? 35  GLU D C     1 
ATOM   5541 O  O     . GLU D 1 35  ? 17.113  52.352  81.674  1.00 122.80 ? 35  GLU D O     1 
ATOM   5542 C  CB    . GLU D 1 35  ? 16.372  49.005  81.763  1.00 122.50 ? 35  GLU D CB    1 
ATOM   5543 C  CG    . GLU D 1 35  ? 16.153  47.783  82.636  1.00 123.74 ? 35  GLU D CG    1 
ATOM   5544 C  CD    . GLU D 1 35  ? 17.152  47.687  83.768  1.00 124.32 ? 35  GLU D CD    1 
ATOM   5545 O  OE1   . GLU D 1 35  ? 17.428  48.723  84.411  1.00 124.25 ? 35  GLU D OE1   1 
ATOM   5546 O  OE2   . GLU D 1 35  ? 17.655  46.571  84.021  1.00 124.47 ? 35  GLU D OE2   1 
ATOM   5547 N  N     . THR D 1 36  ? 15.492  51.461  80.392  1.00 122.99 ? 36  THR D N     1 
ATOM   5548 C  CA    . THR D 1 36  ? 15.596  52.475  79.347  1.00 123.26 ? 36  THR D CA    1 
ATOM   5549 C  C     . THR D 1 36  ? 14.629  53.647  79.510  1.00 123.52 ? 36  THR D C     1 
ATOM   5550 O  O     . THR D 1 36  ? 13.884  53.975  78.583  1.00 123.40 ? 36  THR D O     1 
ATOM   5551 C  CB    . THR D 1 36  ? 15.359  51.846  77.953  1.00 123.62 ? 36  THR D CB    1 
ATOM   5552 O  OG1   . THR D 1 36  ? 14.008  51.380  77.865  1.00 123.34 ? 36  THR D OG1   1 
ATOM   5553 C  CG2   . THR D 1 36  ? 16.306  50.670  77.722  1.00 123.20 ? 36  THR D CG2   1 
ATOM   5554 N  N     . SER D 1 37  ? 14.643  54.283  80.677  1.00 124.00 ? 37  SER D N     1 
ATOM   5555 C  CA    . SER D 1 37  ? 13.757  55.417  80.919  1.00 124.79 ? 37  SER D CA    1 
ATOM   5556 C  C     . SER D 1 37  ? 14.001  56.122  82.253  1.00 125.49 ? 37  SER D C     1 
ATOM   5557 O  O     . SER D 1 37  ? 14.785  57.069  82.335  1.00 125.70 ? 37  SER D O     1 
ATOM   5558 C  CB    . SER D 1 37  ? 12.294  54.966  80.843  1.00 124.31 ? 37  SER D CB    1 
ATOM   5559 O  OG    . SER D 1 37  ? 11.404  56.052  81.044  1.00 124.01 ? 37  SER D OG    1 
ATOM   5560 N  N     . VAL D 1 38  ? 13.325  55.657  83.297  1.00 126.14 ? 38  VAL D N     1 
ATOM   5561 C  CA    . VAL D 1 38  ? 13.447  56.261  84.615  1.00 126.54 ? 38  VAL D CA    1 
ATOM   5562 C  C     . VAL D 1 38  ? 14.859  56.249  85.181  1.00 126.93 ? 38  VAL D C     1 
ATOM   5563 O  O     . VAL D 1 38  ? 15.494  57.297  85.273  1.00 127.18 ? 38  VAL D O     1 
ATOM   5564 C  CB    . VAL D 1 38  ? 12.496  55.585  85.621  1.00 126.42 ? 38  VAL D CB    1 
ATOM   5565 C  CG1   . VAL D 1 38  ? 11.059  55.825  85.205  1.00 126.13 ? 38  VAL D CG1   1 
ATOM   5566 C  CG2   . VAL D 1 38  ? 12.770  54.099  85.684  1.00 126.70 ? 38  VAL D CG2   1 
ATOM   5567 N  N     . PHE D 1 39  ? 15.347  55.069  85.555  1.00 127.55 ? 39  PHE D N     1 
ATOM   5568 C  CA    . PHE D 1 39  ? 16.684  54.930  86.128  1.00 128.68 ? 39  PHE D CA    1 
ATOM   5569 C  C     . PHE D 1 39  ? 17.726  55.881  85.531  1.00 129.78 ? 39  PHE D C     1 
ATOM   5570 O  O     . PHE D 1 39  ? 18.530  56.463  86.261  1.00 129.40 ? 39  PHE D O     1 
ATOM   5571 C  CB    . PHE D 1 39  ? 17.174  53.481  85.997  1.00 128.51 ? 39  PHE D CB    1 
ATOM   5572 C  CG    . PHE D 1 39  ? 16.588  52.537  87.018  1.00 128.33 ? 39  PHE D CG    1 
ATOM   5573 C  CD1   . PHE D 1 39  ? 15.218  52.291  87.062  1.00 128.11 ? 39  PHE D CD1   1 
ATOM   5574 C  CD2   . PHE D 1 39  ? 17.413  51.885  87.932  1.00 128.01 ? 39  PHE D CD2   1 
ATOM   5575 C  CE1   . PHE D 1 39  ? 14.678  51.410  87.997  1.00 127.29 ? 39  PHE D CE1   1 
ATOM   5576 C  CE2   . PHE D 1 39  ? 16.884  51.004  88.869  1.00 127.78 ? 39  PHE D CE2   1 
ATOM   5577 C  CZ    . PHE D 1 39  ? 15.512  50.767  88.901  1.00 127.56 ? 39  PHE D CZ    1 
ATOM   5578 N  N     . PRO D 1 40  ? 17.740  56.037  84.195  1.00 130.91 ? 40  PRO D N     1 
ATOM   5579 C  CA    . PRO D 1 40  ? 18.708  56.934  83.555  1.00 131.80 ? 40  PRO D CA    1 
ATOM   5580 C  C     . PRO D 1 40  ? 18.422  58.414  83.803  1.00 133.25 ? 40  PRO D C     1 
ATOM   5581 O  O     . PRO D 1 40  ? 17.522  58.998  83.198  1.00 133.02 ? 40  PRO D O     1 
ATOM   5582 C  CB    . PRO D 1 40  ? 18.592  56.567  82.080  1.00 131.43 ? 40  PRO D CB    1 
ATOM   5583 C  CG    . PRO D 1 40  ? 18.221  55.119  82.129  1.00 131.05 ? 40  PRO D CG    1 
ATOM   5584 C  CD    . PRO D 1 40  ? 17.158  55.124  83.196  1.00 131.05 ? 40  PRO D CD    1 
ATOM   5585 N  N     . ARG D 1 41  ? 19.199  59.004  84.705  1.00 135.57 ? 41  ARG D N     1 
ATOM   5586 C  CA    . ARG D 1 41  ? 19.076  60.417  85.062  1.00 137.68 ? 41  ARG D CA    1 
ATOM   5587 C  C     . ARG D 1 41  ? 17.756  60.820  85.726  1.00 137.96 ? 41  ARG D C     1 
ATOM   5588 O  O     . ARG D 1 41  ? 16.698  60.823  85.089  1.00 137.79 ? 41  ARG D O     1 
ATOM   5589 C  CB    . ARG D 1 41  ? 19.336  61.289  83.826  1.00 138.51 ? 41  ARG D CB    1 
ATOM   5590 C  CG    . ARG D 1 41  ? 20.815  61.623  83.586  1.00 139.79 ? 41  ARG D CG    1 
ATOM   5591 C  CD    . ARG D 1 41  ? 21.711  60.382  83.513  1.00 140.45 ? 41  ARG D CD    1 
ATOM   5592 N  NE    . ARG D 1 41  ? 21.790  59.649  84.780  1.00 140.88 ? 41  ARG D NE    1 
ATOM   5593 C  CZ    . ARG D 1 41  ? 22.279  60.144  85.917  1.00 140.68 ? 41  ARG D CZ    1 
ATOM   5594 N  NH1   . ARG D 1 41  ? 22.744  61.386  85.964  1.00 140.42 ? 41  ARG D NH1   1 
ATOM   5595 N  NH2   . ARG D 1 41  ? 22.301  59.395  87.013  1.00 140.26 ? 41  ARG D NH2   1 
ATOM   5596 N  N     . GLU D 1 42  ? 17.841  61.158  87.014  1.00 138.37 ? 42  GLU D N     1 
ATOM   5597 C  CA    . GLU D 1 42  ? 16.680  61.578  87.798  1.00 138.44 ? 42  GLU D CA    1 
ATOM   5598 C  C     . GLU D 1 42  ? 17.014  62.150  89.182  1.00 138.80 ? 42  GLU D C     1 
ATOM   5599 O  O     . GLU D 1 42  ? 16.516  61.669  90.199  1.00 139.04 ? 42  GLU D O     1 
ATOM   5600 C  CB    . GLU D 1 42  ? 15.680  60.418  87.936  1.00 137.13 ? 42  GLU D CB    1 
ATOM   5601 C  CG    . GLU D 1 42  ? 16.304  59.035  88.050  1.00 136.10 ? 42  GLU D CG    1 
ATOM   5602 C  CD    . GLU D 1 42  ? 17.131  58.852  89.307  1.00 135.95 ? 42  GLU D CD    1 
ATOM   5603 O  OE1   . GLU D 1 42  ? 18.117  59.598  89.500  1.00 135.48 ? 42  GLU D OE1   1 
ATOM   5604 O  OE2   . GLU D 1 42  ? 16.792  57.952  90.104  1.00 135.59 ? 42  GLU D OE2   1 
ATOM   5605 N  N     . HIS D 1 43  ? 17.862  63.178  89.204  1.00 139.42 ? 43  HIS D N     1 
ATOM   5606 C  CA    . HIS D 1 43  ? 18.265  63.875  90.432  1.00 139.31 ? 43  HIS D CA    1 
ATOM   5607 C  C     . HIS D 1 43  ? 19.194  63.139  91.403  1.00 138.25 ? 43  HIS D C     1 
ATOM   5608 O  O     . HIS D 1 43  ? 19.761  63.763  92.304  1.00 138.09 ? 43  HIS D O     1 
ATOM   5609 C  CB    . HIS D 1 43  ? 17.020  64.354  91.187  1.00 140.06 ? 43  HIS D CB    1 
ATOM   5610 N  N     . GLU D 1 44  ? 19.348  61.829  91.224  1.00 136.82 ? 44  GLU D N     1 
ATOM   5611 C  CA    . GLU D 1 44  ? 20.219  61.018  92.078  1.00 135.46 ? 44  GLU D CA    1 
ATOM   5612 C  C     . GLU D 1 44  ? 19.721  60.864  93.510  1.00 134.70 ? 44  GLU D C     1 
ATOM   5613 O  O     . GLU D 1 44  ? 19.778  59.772  94.073  1.00 134.81 ? 44  GLU D O     1 
ATOM   5614 C  CB    . GLU D 1 44  ? 21.634  61.601  92.119  1.00 134.89 ? 44  GLU D CB    1 
ATOM   5615 C  CG    . GLU D 1 44  ? 22.601  60.792  92.970  1.00 134.77 ? 44  GLU D CG    1 
ATOM   5616 C  CD    . GLU D 1 44  ? 23.945  61.475  93.144  1.00 135.21 ? 44  GLU D CD    1 
ATOM   5617 O  OE1   . GLU D 1 44  ? 24.558  61.852  92.122  1.00 135.25 ? 44  GLU D OE1   1 
ATOM   5618 O  OE2   . GLU D 1 44  ? 24.392  61.628  94.302  1.00 135.14 ? 44  GLU D OE2   1 
ATOM   5619 N  N     . ALA D 1 45  ? 19.255  61.961  94.103  1.00 133.92 ? 45  ALA D N     1 
ATOM   5620 C  CA    . ALA D 1 45  ? 18.749  61.939  95.474  1.00 132.64 ? 45  ALA D CA    1 
ATOM   5621 C  C     . ALA D 1 45  ? 17.798  60.762  95.659  1.00 131.47 ? 45  ALA D C     1 
ATOM   5622 O  O     . ALA D 1 45  ? 17.815  60.093  96.694  1.00 131.54 ? 45  ALA D O     1 
ATOM   5623 C  CB    . ALA D 1 45  ? 18.029  63.250  95.788  1.00 132.72 ? 45  ALA D CB    1 
ATOM   5624 N  N     . MET D 1 46  ? 16.976  60.517  94.641  1.00 129.64 ? 46  MET D N     1 
ATOM   5625 C  CA    . MET D 1 46  ? 16.011  59.425  94.656  1.00 127.91 ? 46  MET D CA    1 
ATOM   5626 C  C     . MET D 1 46  ? 16.764  58.112  94.821  1.00 127.43 ? 46  MET D C     1 
ATOM   5627 O  O     . MET D 1 46  ? 16.334  57.219  95.550  1.00 126.93 ? 46  MET D O     1 
ATOM   5628 C  CB    . MET D 1 46  ? 15.237  59.396  93.341  1.00 127.18 ? 46  MET D CB    1 
ATOM   5629 C  CG    . MET D 1 46  ? 14.934  60.767  92.760  1.00 126.12 ? 46  MET D CG    1 
ATOM   5630 S  SD    . MET D 1 46  ? 13.741  61.721  93.695  1.00 126.12 ? 46  MET D SD    1 
ATOM   5631 C  CE    . MET D 1 46  ? 12.238  61.373  92.781  1.00 125.40 ? 46  MET D CE    1 
ATOM   5632 N  N     . LYS D 1 47  ? 17.891  58.005  94.124  1.00 127.36 ? 47  LYS D N     1 
ATOM   5633 C  CA    . LYS D 1 47  ? 18.727  56.812  94.180  1.00 127.58 ? 47  LYS D CA    1 
ATOM   5634 C  C     . LYS D 1 47  ? 19.352  56.668  95.562  1.00 127.47 ? 47  LYS D C     1 
ATOM   5635 O  O     . LYS D 1 47  ? 19.265  55.609  96.185  1.00 127.09 ? 47  LYS D O     1 
ATOM   5636 C  CB    . LYS D 1 47  ? 19.832  56.889  93.120  1.00 127.87 ? 47  LYS D CB    1 
ATOM   5637 C  CG    . LYS D 1 47  ? 19.335  56.839  91.681  1.00 128.32 ? 47  LYS D CG    1 
ATOM   5638 C  CD    . LYS D 1 47  ? 18.668  55.506  91.371  1.00 128.22 ? 47  LYS D CD    1 
ATOM   5639 C  CE    . LYS D 1 47  ? 18.246  55.410  89.910  1.00 128.40 ? 47  LYS D CE    1 
ATOM   5640 N  NZ    . LYS D 1 47  ? 19.399  55.488  88.966  1.00 127.79 ? 47  LYS D NZ    1 
ATOM   5641 N  N     . GLU D 1 48  ? 19.984  57.740  96.034  1.00 127.57 ? 48  GLU D N     1 
ATOM   5642 C  CA    . GLU D 1 48  ? 20.621  57.737  97.345  1.00 127.63 ? 48  GLU D CA    1 
ATOM   5643 C  C     . GLU D 1 48  ? 19.613  57.315  98.414  1.00 127.35 ? 48  GLU D C     1 
ATOM   5644 O  O     . GLU D 1 48  ? 19.870  56.404  99.202  1.00 127.42 ? 48  GLU D O     1 
ATOM   5645 C  CB    . GLU D 1 48  ? 21.184  59.131  97.666  1.00 128.05 ? 48  GLU D CB    1 
ATOM   5646 C  CG    . GLU D 1 48  ? 21.901  59.219  99.017  1.00 128.85 ? 48  GLU D CG    1 
ATOM   5647 C  CD    . GLU D 1 48  ? 22.568  60.569  99.269  1.00 128.87 ? 48  GLU D CD    1 
ATOM   5648 O  OE1   . GLU D 1 48  ? 21.879  61.610  99.198  1.00 128.78 ? 48  GLU D OE1   1 
ATOM   5649 O  OE2   . GLU D 1 48  ? 23.787  60.584  99.549  1.00 128.78 ? 48  GLU D OE2   1 
ATOM   5650 N  N     . LEU D 1 49  ? 18.461  57.976  98.425  1.00 126.84 ? 49  LEU D N     1 
ATOM   5651 C  CA    . LEU D 1 49  ? 17.413  57.677  99.391  1.00 126.54 ? 49  LEU D CA    1 
ATOM   5652 C  C     . LEU D 1 49  ? 17.082  56.191  99.424  1.00 126.70 ? 49  LEU D C     1 
ATOM   5653 O  O     . LEU D 1 49  ? 17.046  55.581  100.492 1.00 126.07 ? 49  LEU D O     1 
ATOM   5654 C  CB    . LEU D 1 49  ? 16.154  58.484  99.059  1.00 126.32 ? 49  LEU D CB    1 
ATOM   5655 C  CG    . LEU D 1 49  ? 14.946  58.344  99.989  1.00 125.89 ? 49  LEU D CG    1 
ATOM   5656 C  CD1   . LEU D 1 49  ? 15.375  58.610  101.416 1.00 126.18 ? 49  LEU D CD1   1 
ATOM   5657 C  CD2   . LEU D 1 49  ? 13.856  59.321  99.577  1.00 125.46 ? 49  LEU D CD2   1 
ATOM   5658 N  N     . ARG D 1 50  ? 16.853  55.613  98.249  1.00 127.57 ? 50  ARG D N     1 
ATOM   5659 C  CA    . ARG D 1 50  ? 16.508  54.200  98.137  1.00 128.64 ? 50  ARG D CA    1 
ATOM   5660 C  C     . ARG D 1 50  ? 17.579  53.236  98.616  1.00 129.20 ? 50  ARG D C     1 
ATOM   5661 O  O     . ARG D 1 50  ? 17.269  52.105  98.989  1.00 129.05 ? 50  ARG D O     1 
ATOM   5662 C  CB    . ARG D 1 50  ? 16.142  53.854  96.698  1.00 128.79 ? 50  ARG D CB    1 
ATOM   5663 C  CG    . ARG D 1 50  ? 14.873  54.511  96.223  1.00 129.97 ? 50  ARG D CG    1 
ATOM   5664 C  CD    . ARG D 1 50  ? 14.435  53.946  94.885  1.00 130.99 ? 50  ARG D CD    1 
ATOM   5665 N  NE    . ARG D 1 50  ? 15.507  53.996  93.896  1.00 131.71 ? 50  ARG D NE    1 
ATOM   5666 C  CZ    . ARG D 1 50  ? 15.350  53.704  92.610  1.00 131.63 ? 50  ARG D CZ    1 
ATOM   5667 N  NH1   . ARG D 1 50  ? 14.158  53.344  92.154  1.00 131.56 ? 50  ARG D NH1   1 
ATOM   5668 N  NH2   . ARG D 1 50  ? 16.384  53.771  91.782  1.00 131.25 ? 50  ARG D NH2   1 
ATOM   5669 N  N     . GLU D 1 51  ? 18.837  53.667  98.589  1.00 130.16 ? 51  GLU D N     1 
ATOM   5670 C  CA    . GLU D 1 51  ? 19.923  52.811  99.053  1.00 131.11 ? 51  GLU D CA    1 
ATOM   5671 C  C     . GLU D 1 51  ? 19.602  52.410  100.486 1.00 130.84 ? 51  GLU D C     1 
ATOM   5672 O  O     . GLU D 1 51  ? 19.783  51.258  100.885 1.00 130.63 ? 51  GLU D O     1 
ATOM   5673 C  CB    . GLU D 1 51  ? 21.258  53.562  99.044  1.00 132.81 ? 51  GLU D CB    1 
ATOM   5674 C  CG    . GLU D 1 51  ? 21.775  53.964  97.674  1.00 135.44 ? 51  GLU D CG    1 
ATOM   5675 C  CD    . GLU D 1 51  ? 23.147  54.625  97.748  1.00 136.73 ? 51  GLU D CD    1 
ATOM   5676 O  OE1   . GLU D 1 51  ? 24.091  53.984  98.263  1.00 137.33 ? 51  GLU D OE1   1 
ATOM   5677 O  OE2   . GLU D 1 51  ? 23.282  55.784  97.293  1.00 137.37 ? 51  GLU D OE2   1 
ATOM   5678 N  N     . VAL D 1 52  ? 19.114  53.385  101.249 1.00 130.22 ? 52  VAL D N     1 
ATOM   5679 C  CA    . VAL D 1 52  ? 18.765  53.181  102.647 1.00 129.24 ? 52  VAL D CA    1 
ATOM   5680 C  C     . VAL D 1 52  ? 17.306  52.779  102.839 1.00 128.62 ? 52  VAL D C     1 
ATOM   5681 O  O     . VAL D 1 52  ? 17.000  51.967  103.708 1.00 128.58 ? 52  VAL D O     1 
ATOM   5682 C  CB    . VAL D 1 52  ? 19.037  54.457  103.469 1.00 129.46 ? 52  VAL D CB    1 
ATOM   5683 C  CG1   . VAL D 1 52  ? 18.708  54.215  104.937 1.00 129.43 ? 52  VAL D CG1   1 
ATOM   5684 C  CG2   . VAL D 1 52  ? 20.492  54.874  103.305 1.00 129.19 ? 52  VAL D CG2   1 
ATOM   5685 N  N     . THR D 1 53  ? 16.413  53.342  102.028 1.00 128.01 ? 53  THR D N     1 
ATOM   5686 C  CA    . THR D 1 53  ? 14.983  53.041  102.125 1.00 127.54 ? 53  THR D CA    1 
ATOM   5687 C  C     . THR D 1 53  ? 14.682  51.556  101.929 1.00 127.98 ? 53  THR D C     1 
ATOM   5688 O  O     . THR D 1 53  ? 13.525  51.130  101.969 1.00 127.71 ? 53  THR D O     1 
ATOM   5689 C  CB    . THR D 1 53  ? 14.178  53.848  101.093 1.00 126.89 ? 53  THR D CB    1 
ATOM   5690 O  OG1   . THR D 1 53  ? 14.535  55.232  101.194 1.00 126.68 ? 53  THR D OG1   1 
ATOM   5691 C  CG2   . THR D 1 53  ? 12.682  53.701  101.346 1.00 125.25 ? 53  THR D CG2   1 
ATOM   5692 N  N     . ALA D 1 54  ? 15.735  50.774  101.715 1.00 128.94 ? 54  ALA D N     1 
ATOM   5693 C  CA    . ALA D 1 54  ? 15.607  49.336  101.530 1.00 129.53 ? 54  ALA D CA    1 
ATOM   5694 C  C     . ALA D 1 54  ? 15.875  48.640  102.865 1.00 129.97 ? 54  ALA D C     1 
ATOM   5695 O  O     . ALA D 1 54  ? 15.756  47.419  102.981 1.00 129.89 ? 54  ALA D O     1 
ATOM   5696 C  CB    . ALA D 1 54  ? 16.597  48.859  100.477 1.00 129.59 ? 54  ALA D CB    1 
ATOM   5697 N  N     . LYS D 1 55  ? 16.236  49.433  103.870 1.00 130.40 ? 55  LYS D N     1 
ATOM   5698 C  CA    . LYS D 1 55  ? 16.523  48.920  105.206 1.00 130.00 ? 55  LYS D CA    1 
ATOM   5699 C  C     . LYS D 1 55  ? 15.273  48.968  106.088 1.00 130.16 ? 55  LYS D C     1 
ATOM   5700 O  O     . LYS D 1 55  ? 14.906  47.967  106.701 1.00 129.85 ? 55  LYS D O     1 
ATOM   5701 C  CB    . LYS D 1 55  ? 17.650  49.736  105.852 1.00 129.76 ? 55  LYS D CB    1 
ATOM   5702 N  N     . HIS D 1 56  ? 14.625  50.128  106.157 1.00 129.96 ? 56  HIS D N     1 
ATOM   5703 C  CA    . HIS D 1 56  ? 13.420  50.257  106.966 1.00 129.76 ? 56  HIS D CA    1 
ATOM   5704 C  C     . HIS D 1 56  ? 12.473  49.120  106.593 1.00 129.20 ? 56  HIS D C     1 
ATOM   5705 O  O     . HIS D 1 56  ? 11.974  49.062  105.470 1.00 130.04 ? 56  HIS D O     1 
ATOM   5706 C  CB    . HIS D 1 56  ? 12.739  51.599  106.709 1.00 130.46 ? 56  HIS D CB    1 
ATOM   5707 N  N     . PRO D 1 57  ? 12.212  48.203  107.540 1.00 128.02 ? 57  PRO D N     1 
ATOM   5708 C  CA    . PRO D 1 57  ? 11.337  47.035  107.376 1.00 126.34 ? 57  PRO D CA    1 
ATOM   5709 C  C     . PRO D 1 57  ? 10.144  47.169  106.419 1.00 125.27 ? 57  PRO D C     1 
ATOM   5710 O  O     . PRO D 1 57  ? 9.842   46.243  105.667 1.00 124.48 ? 57  PRO D O     1 
ATOM   5711 C  CB    . PRO D 1 57  ? 10.911  46.741  108.809 1.00 126.78 ? 57  PRO D CB    1 
ATOM   5712 C  CG    . PRO D 1 57  ? 12.165  47.035  109.567 1.00 126.63 ? 57  PRO D CG    1 
ATOM   5713 C  CD    . PRO D 1 57  ? 12.622  48.346  108.951 1.00 127.20 ? 57  PRO D CD    1 
ATOM   5714 N  N     . TRP D 1 58  ? 9.469   48.312  106.450 1.00 124.52 ? 58  TRP D N     1 
ATOM   5715 C  CA    . TRP D 1 58  ? 8.313   48.534  105.585 1.00 123.77 ? 58  TRP D CA    1 
ATOM   5716 C  C     . TRP D 1 58  ? 8.666   49.255  104.297 1.00 122.82 ? 58  TRP D C     1 
ATOM   5717 O  O     . TRP D 1 58  ? 8.056   50.268  103.958 1.00 122.76 ? 58  TRP D O     1 
ATOM   5718 C  CB    . TRP D 1 58  ? 7.235   49.319  106.340 1.00 125.10 ? 58  TRP D CB    1 
ATOM   5719 C  CG    . TRP D 1 58  ? 6.490   48.473  107.320 1.00 126.14 ? 58  TRP D CG    1 
ATOM   5720 C  CD1   . TRP D 1 58  ? 5.383   47.712  107.071 1.00 126.10 ? 58  TRP D CD1   1 
ATOM   5721 C  CD2   . TRP D 1 58  ? 6.856   48.215  108.680 1.00 126.68 ? 58  TRP D CD2   1 
ATOM   5722 N  NE1   . TRP D 1 58  ? 5.042   46.990  108.189 1.00 126.47 ? 58  TRP D NE1   1 
ATOM   5723 C  CE2   . TRP D 1 58  ? 5.930   47.279  109.192 1.00 126.92 ? 58  TRP D CE2   1 
ATOM   5724 C  CE3   . TRP D 1 58  ? 7.883   48.679  109.516 1.00 126.96 ? 58  TRP D CE3   1 
ATOM   5725 C  CZ2   . TRP D 1 58  ? 5.999   46.797  110.504 1.00 127.50 ? 58  TRP D CZ2   1 
ATOM   5726 C  CZ3   . TRP D 1 58  ? 7.952   48.200  110.821 1.00 127.20 ? 58  TRP D CZ3   1 
ATOM   5727 C  CH2   . TRP D 1 58  ? 7.015   47.267  111.301 1.00 127.66 ? 58  TRP D CH2   1 
ATOM   5728 N  N     . ASN D 1 59  ? 9.650   48.726  103.578 1.00 121.78 ? 59  ASN D N     1 
ATOM   5729 C  CA    . ASN D 1 59  ? 10.078  49.322  102.318 1.00 120.04 ? 59  ASN D CA    1 
ATOM   5730 C  C     . ASN D 1 59  ? 9.068   48.984  101.233 1.00 118.99 ? 59  ASN D C     1 
ATOM   5731 O  O     . ASN D 1 59  ? 9.038   49.617  100.181 1.00 119.24 ? 59  ASN D O     1 
ATOM   5732 C  CB    . ASN D 1 59  ? 11.470  48.805  101.919 1.00 119.85 ? 59  ASN D CB    1 
ATOM   5733 C  CG    . ASN D 1 59  ? 11.506  47.296  101.711 1.00 119.69 ? 59  ASN D CG    1 
ATOM   5734 O  OD1   . ASN D 1 59  ? 10.818  46.760  100.842 1.00 119.68 ? 59  ASN D OD1   1 
ATOM   5735 N  ND2   . ASN D 1 59  ? 12.317  46.607  102.508 1.00 119.12 ? 59  ASN D ND2   1 
ATOM   5736 N  N     . ILE D 1 60  ? 8.229   47.990  101.511 1.00 117.48 ? 60  ILE D N     1 
ATOM   5737 C  CA    . ILE D 1 60  ? 7.215   47.544  100.569 1.00 116.13 ? 60  ILE D CA    1 
ATOM   5738 C  C     . ILE D 1 60  ? 6.152   48.619  100.314 1.00 115.30 ? 60  ILE D C     1 
ATOM   5739 O  O     . ILE D 1 60  ? 5.147   48.370  99.653  1.00 114.94 ? 60  ILE D O     1 
ATOM   5740 C  CB    . ILE D 1 60  ? 6.543   46.253  101.085 1.00 116.18 ? 60  ILE D CB    1 
ATOM   5741 C  CG1   . ILE D 1 60  ? 5.758   45.581  99.960  1.00 116.90 ? 60  ILE D CG1   1 
ATOM   5742 C  CG2   . ILE D 1 60  ? 5.635   46.574  102.253 1.00 116.45 ? 60  ILE D CG2   1 
ATOM   5743 C  CD1   . ILE D 1 60  ? 6.631   45.109  98.811  1.00 118.30 ? 60  ILE D CD1   1 
ATOM   5744 N  N     . MET D 1 61  ? 6.383   49.817  100.837 1.00 115.02 ? 61  MET D N     1 
ATOM   5745 C  CA    . MET D 1 61  ? 5.448   50.921  100.660 1.00 115.28 ? 61  MET D CA    1 
ATOM   5746 C  C     . MET D 1 61  ? 6.071   52.035  99.852  1.00 115.26 ? 61  MET D C     1 
ATOM   5747 O  O     . MET D 1 61  ? 5.370   52.769  99.155  1.00 115.64 ? 61  MET D O     1 
ATOM   5748 C  CB    . MET D 1 61  ? 5.012   51.485  102.013 1.00 116.04 ? 61  MET D CB    1 
ATOM   5749 C  CG    . MET D 1 61  ? 3.738   50.880  102.572 1.00 116.89 ? 61  MET D CG    1 
ATOM   5750 S  SD    . MET D 1 61  ? 3.340   51.527  104.207 1.00 116.37 ? 61  MET D SD    1 
ATOM   5751 C  CE    . MET D 1 61  ? 4.095   50.269  105.238 1.00 116.62 ? 61  MET D CE    1 
ATOM   5752 N  N     . THR D 1 62  ? 7.389   52.164  99.960  1.00 115.08 ? 62  THR D N     1 
ATOM   5753 C  CA    . THR D 1 62  ? 8.115   53.200  99.240  1.00 115.24 ? 62  THR D CA    1 
ATOM   5754 C  C     . THR D 1 62  ? 7.582   53.285  97.825  1.00 115.66 ? 62  THR D C     1 
ATOM   5755 O  O     . THR D 1 62  ? 7.385   52.265  97.170  1.00 115.71 ? 62  THR D O     1 
ATOM   5756 C  CB    . THR D 1 62  ? 9.616   52.890  99.153  1.00 114.96 ? 62  THR D CB    1 
ATOM   5757 O  OG1   . THR D 1 62  ? 10.103  52.491  100.439 1.00 115.91 ? 62  THR D OG1   1 
ATOM   5758 C  CG2   . THR D 1 62  ? 10.379  54.123  98.689  1.00 115.09 ? 62  THR D CG2   1 
ATOM   5759 N  N     . THR D 1 63  ? 7.335   54.500  97.355  1.00 116.21 ? 63  THR D N     1 
ATOM   5760 C  CA    . THR D 1 63  ? 6.834   54.680  96.004  1.00 116.89 ? 63  THR D CA    1 
ATOM   5761 C  C     . THR D 1 63  ? 7.941   54.308  95.011  1.00 117.13 ? 63  THR D C     1 
ATOM   5762 O  O     . THR D 1 63  ? 9.117   54.619  95.232  1.00 117.24 ? 63  THR D O     1 
ATOM   5763 C  CB    . THR D 1 63  ? 6.391   56.135  95.777  1.00 117.10 ? 63  THR D CB    1 
ATOM   5764 O  OG1   . THR D 1 63  ? 6.010   56.316  94.408  1.00 117.35 ? 63  THR D OG1   1 
ATOM   5765 C  CG2   . THR D 1 63  ? 7.515   57.087  96.132  1.00 117.44 ? 63  THR D CG2   1 
ATOM   5766 N  N     . SER D 1 64  ? 7.561   53.631  93.927  1.00 116.99 ? 64  SER D N     1 
ATOM   5767 C  CA    . SER D 1 64  ? 8.510   53.204  92.898  1.00 116.31 ? 64  SER D CA    1 
ATOM   5768 C  C     . SER D 1 64  ? 8.998   54.374  92.043  1.00 116.24 ? 64  SER D C     1 
ATOM   5769 O  O     . SER D 1 64  ? 8.219   55.278  91.718  1.00 116.47 ? 64  SER D O     1 
ATOM   5770 C  CB    . SER D 1 64  ? 7.860   52.154  91.987  1.00 116.13 ? 64  SER D CB    1 
ATOM   5771 O  OG    . SER D 1 64  ? 6.746   52.688  91.284  1.00 114.89 ? 64  SER D OG    1 
ATOM   5772 N  N     . ALA D 1 65  ? 10.285  54.355  91.684  1.00 115.37 ? 65  ALA D N     1 
ATOM   5773 C  CA    . ALA D 1 65  ? 10.869  55.407  90.849  1.00 113.94 ? 65  ALA D CA    1 
ATOM   5774 C  C     . ALA D 1 65  ? 9.949   55.577  89.648  1.00 113.15 ? 65  ALA D C     1 
ATOM   5775 O  O     . ALA D 1 65  ? 9.768   56.677  89.126  1.00 112.33 ? 65  ALA D O     1 
ATOM   5776 C  CB    . ALA D 1 65  ? 12.264  55.002  90.395  1.00 113.21 ? 65  ALA D CB    1 
ATOM   5777 N  N     . ASP D 1 66  ? 9.367   54.459  89.231  1.00 112.95 ? 66  ASP D N     1 
ATOM   5778 C  CA    . ASP D 1 66  ? 8.428   54.415  88.126  1.00 113.04 ? 66  ASP D CA    1 
ATOM   5779 C  C     . ASP D 1 66  ? 7.416   55.536  88.327  1.00 113.27 ? 66  ASP D C     1 
ATOM   5780 O  O     . ASP D 1 66  ? 7.203   56.366  87.444  1.00 113.26 ? 66  ASP D O     1 
ATOM   5781 C  CB    . ASP D 1 66  ? 7.709   53.061  88.132  1.00 113.50 ? 66  ASP D CB    1 
ATOM   5782 C  CG    . ASP D 1 66  ? 6.605   52.969  87.089  1.00 114.55 ? 66  ASP D CG    1 
ATOM   5783 O  OD1   . ASP D 1 66  ? 5.896   53.975  86.870  1.00 115.19 ? 66  ASP D OD1   1 
ATOM   5784 O  OD2   . ASP D 1 66  ? 6.427   51.882  86.497  1.00 114.58 ? 66  ASP D OD2   1 
ATOM   5785 N  N     . GLU D 1 67  ? 6.802   55.553  89.507  1.00 113.80 ? 67  GLU D N     1 
ATOM   5786 C  CA    . GLU D 1 67  ? 5.794   56.551  89.846  1.00 113.86 ? 67  GLU D CA    1 
ATOM   5787 C  C     . GLU D 1 67  ? 6.428   57.900  90.160  1.00 113.77 ? 67  GLU D C     1 
ATOM   5788 O  O     . GLU D 1 67  ? 5.868   58.953  89.841  1.00 113.47 ? 67  GLU D O     1 
ATOM   5789 C  CB    . GLU D 1 67  ? 4.973   56.068  91.043  1.00 113.98 ? 67  GLU D CB    1 
ATOM   5790 C  CG    . GLU D 1 67  ? 3.674   56.831  91.251  1.00 115.13 ? 67  GLU D CG    1 
ATOM   5791 C  CD    . GLU D 1 67  ? 2.806   56.218  92.333  1.00 115.73 ? 67  GLU D CD    1 
ATOM   5792 O  OE1   . GLU D 1 67  ? 3.238   56.201  93.506  1.00 116.54 ? 67  GLU D OE1   1 
ATOM   5793 O  OE2   . GLU D 1 67  ? 1.692   55.748  92.010  1.00 115.87 ? 67  GLU D OE2   1 
ATOM   5794 N  N     . GLY D 1 68  ? 7.600   57.859  90.783  1.00 113.71 ? 68  GLY D N     1 
ATOM   5795 C  CA    . GLY D 1 68  ? 8.297   59.083  91.128  1.00 114.12 ? 68  GLY D CA    1 
ATOM   5796 C  C     . GLY D 1 68  ? 8.468   59.986  89.926  1.00 114.51 ? 68  GLY D C     1 
ATOM   5797 O  O     . GLY D 1 68  ? 8.326   61.206  90.031  1.00 114.15 ? 68  GLY D O     1 
ATOM   5798 N  N     . GLN D 1 69  ? 8.768   59.386  88.776  1.00 115.00 ? 69  GLN D N     1 
ATOM   5799 C  CA    . GLN D 1 69  ? 8.956   60.154  87.555  1.00 114.91 ? 69  GLN D CA    1 
ATOM   5800 C  C     . GLN D 1 69  ? 7.659   60.830  87.129  1.00 114.28 ? 69  GLN D C     1 
ATOM   5801 O  O     . GLN D 1 69  ? 7.646   62.031  86.874  1.00 114.37 ? 69  GLN D O     1 
ATOM   5802 C  CB    . GLN D 1 69  ? 9.456   59.263  86.413  1.00 115.95 ? 69  GLN D CB    1 
ATOM   5803 C  CG    . GLN D 1 69  ? 9.967   60.063  85.211  1.00 118.32 ? 69  GLN D CG    1 
ATOM   5804 C  CD    . GLN D 1 69  ? 10.102  59.240  83.933  1.00 119.45 ? 69  GLN D CD    1 
ATOM   5805 O  OE1   . GLN D 1 69  ? 10.681  59.701  82.945  1.00 119.90 ? 69  GLN D OE1   1 
ATOM   5806 N  NE2   . GLN D 1 69  ? 9.556   58.027  83.942  1.00 119.50 ? 69  GLN D NE2   1 
ATOM   5807 N  N     . PHE D 1 70  ? 6.570   60.066  87.058  1.00 113.68 ? 70  PHE D N     1 
ATOM   5808 C  CA    . PHE D 1 70  ? 5.287   60.630  86.642  1.00 113.11 ? 70  PHE D CA    1 
ATOM   5809 C  C     . PHE D 1 70  ? 4.924   61.896  87.401  1.00 113.23 ? 70  PHE D C     1 
ATOM   5810 O  O     . PHE D 1 70  ? 4.415   62.852  86.815  1.00 112.99 ? 70  PHE D O     1 
ATOM   5811 C  CB    . PHE D 1 70  ? 4.149   59.627  86.814  1.00 112.36 ? 70  PHE D CB    1 
ATOM   5812 C  CG    . PHE D 1 70  ? 2.806   60.182  86.425  1.00 111.85 ? 70  PHE D CG    1 
ATOM   5813 C  CD1   . PHE D 1 70  ? 2.480   60.377  85.090  1.00 112.21 ? 70  PHE D CD1   1 
ATOM   5814 C  CD2   . PHE D 1 70  ? 1.885   60.557  87.395  1.00 111.97 ? 70  PHE D CD2   1 
ATOM   5815 C  CE1   . PHE D 1 70  ? 1.254   60.941  84.726  1.00 112.27 ? 70  PHE D CE1   1 
ATOM   5816 C  CE2   . PHE D 1 70  ? 0.658   61.122  87.040  1.00 111.69 ? 70  PHE D CE2   1 
ATOM   5817 C  CZ    . PHE D 1 70  ? 0.345   61.314  85.706  1.00 111.68 ? 70  PHE D CZ    1 
ATOM   5818 N  N     . LEU D 1 71  ? 5.170   61.902  88.706  1.00 113.19 ? 71  LEU D N     1 
ATOM   5819 C  CA    . LEU D 1 71  ? 4.852   63.074  89.508  1.00 113.37 ? 71  LEU D CA    1 
ATOM   5820 C  C     . LEU D 1 71  ? 5.717   64.262  89.109  1.00 113.23 ? 71  LEU D C     1 
ATOM   5821 O  O     . LEU D 1 71  ? 5.193   65.318  88.762  1.00 112.98 ? 71  LEU D O     1 
ATOM   5822 C  CB    . LEU D 1 71  ? 5.029   62.775  91.000  1.00 113.57 ? 71  LEU D CB    1 
ATOM   5823 C  CG    . LEU D 1 71  ? 3.982   61.884  91.684  1.00 112.85 ? 71  LEU D CG    1 
ATOM   5824 C  CD1   . LEU D 1 71  ? 4.372   61.727  93.139  1.00 112.39 ? 71  LEU D CD1   1 
ATOM   5825 C  CD2   . LEU D 1 71  ? 2.584   62.491  91.575  1.00 111.83 ? 71  LEU D CD2   1 
ATOM   5826 N  N     . SER D 1 72  ? 7.036   64.080  89.154  1.00 113.53 ? 72  SER D N     1 
ATOM   5827 C  CA    . SER D 1 72  ? 7.984   65.136  88.789  1.00 113.95 ? 72  SER D CA    1 
ATOM   5828 C  C     . SER D 1 72  ? 7.547   65.829  87.505  1.00 114.02 ? 72  SER D C     1 
ATOM   5829 O  O     . SER D 1 72  ? 7.571   67.054  87.403  1.00 114.20 ? 72  SER D O     1 
ATOM   5830 C  CB    . SER D 1 72  ? 9.385   64.552  88.572  1.00 113.69 ? 72  SER D CB    1 
ATOM   5831 O  OG    . SER D 1 72  ? 9.859   63.880  89.722  1.00 114.00 ? 72  SER D OG    1 
ATOM   5832 N  N     . MET D 1 73  ? 7.148   65.022  86.530  1.00 114.30 ? 73  MET D N     1 
ATOM   5833 C  CA    . MET D 1 73  ? 6.707   65.508  85.232  1.00 114.61 ? 73  MET D CA    1 
ATOM   5834 C  C     . MET D 1 73  ? 5.455   66.371  85.353  1.00 114.08 ? 73  MET D C     1 
ATOM   5835 O  O     . MET D 1 73  ? 5.378   67.455  84.781  1.00 113.85 ? 73  MET D O     1 
ATOM   5836 C  CB    . MET D 1 73  ? 6.411   64.316  84.317  1.00 116.08 ? 73  MET D CB    1 
ATOM   5837 C  CG    . MET D 1 73  ? 6.466   64.619  82.830  1.00 117.58 ? 73  MET D CG    1 
ATOM   5838 S  SD    . MET D 1 73  ? 8.163   64.878  82.285  1.00 119.43 ? 73  MET D SD    1 
ATOM   5839 C  CE    . MET D 1 73  ? 8.339   66.634  82.589  1.00 119.28 ? 73  MET D CE    1 
ATOM   5840 N  N     . LEU D 1 74  ? 4.484   65.873  86.111  1.00 113.95 ? 74  LEU D N     1 
ATOM   5841 C  CA    . LEU D 1 74  ? 3.202   66.544  86.312  1.00 113.99 ? 74  LEU D CA    1 
ATOM   5842 C  C     . LEU D 1 74  ? 3.271   67.890  87.039  1.00 114.00 ? 74  LEU D C     1 
ATOM   5843 O  O     . LEU D 1 74  ? 2.489   68.799  86.751  1.00 113.42 ? 74  LEU D O     1 
ATOM   5844 C  CB    . LEU D 1 74  ? 2.255   65.591  87.053  1.00 113.44 ? 74  LEU D CB    1 
ATOM   5845 C  CG    . LEU D 1 74  ? 0.781   65.968  87.196  1.00 112.57 ? 74  LEU D CG    1 
ATOM   5846 C  CD1   . LEU D 1 74  ? 0.234   66.503  85.878  1.00 112.29 ? 74  LEU D CD1   1 
ATOM   5847 C  CD2   . LEU D 1 74  ? 0.011   64.738  87.648  1.00 112.01 ? 74  LEU D CD2   1 
ATOM   5848 N  N     . LEU D 1 75  ? 4.204   68.011  87.979  1.00 114.67 ? 75  LEU D N     1 
ATOM   5849 C  CA    . LEU D 1 75  ? 4.380   69.242  88.747  1.00 115.58 ? 75  LEU D CA    1 
ATOM   5850 C  C     . LEU D 1 75  ? 5.002   70.350  87.901  1.00 116.20 ? 75  LEU D C     1 
ATOM   5851 O  O     . LEU D 1 75  ? 4.800   71.536  88.167  1.00 115.95 ? 75  LEU D O     1 
ATOM   5852 C  CB    . LEU D 1 75  ? 5.265   68.975  89.971  1.00 115.91 ? 75  LEU D CB    1 
ATOM   5853 C  CG    . LEU D 1 75  ? 4.651   68.285  91.197  1.00 116.06 ? 75  LEU D CG    1 
ATOM   5854 C  CD1   . LEU D 1 75  ? 3.959   66.994  90.807  1.00 116.14 ? 75  LEU D CD1   1 
ATOM   5855 C  CD2   . LEU D 1 75  ? 5.751   68.014  92.211  1.00 116.53 ? 75  LEU D CD2   1 
ATOM   5856 N  N     . LYS D 1 76  ? 5.765   69.945  86.887  1.00 117.08 ? 76  LYS D N     1 
ATOM   5857 C  CA    . LYS D 1 76  ? 6.437   70.871  85.977  1.00 117.24 ? 76  LYS D CA    1 
ATOM   5858 C  C     . LYS D 1 76  ? 5.483   71.249  84.844  1.00 117.74 ? 76  LYS D C     1 
ATOM   5859 O  O     . LYS D 1 76  ? 5.527   72.364  84.323  1.00 116.97 ? 76  LYS D O     1 
ATOM   5860 C  CB    . LYS D 1 76  ? 7.689   70.204  85.398  1.00 116.82 ? 76  LYS D CB    1 
ATOM   5861 C  CG    . LYS D 1 76  ? 8.611   69.587  86.443  1.00 116.28 ? 76  LYS D CG    1 
ATOM   5862 C  CD    . LYS D 1 76  ? 9.585   70.589  87.035  1.00 116.14 ? 76  LYS D CD    1 
ATOM   5863 C  CE    . LYS D 1 76  ? 10.755  70.835  86.096  1.00 116.63 ? 76  LYS D CE    1 
ATOM   5864 N  NZ    . LYS D 1 76  ? 11.790  71.725  86.701  1.00 117.21 ? 76  LYS D NZ    1 
ATOM   5865 N  N     . LEU D 1 77  ? 4.623   70.305  84.473  1.00 118.98 ? 77  LEU D N     1 
ATOM   5866 C  CA    . LEU D 1 77  ? 3.646   70.511  83.409  1.00 120.52 ? 77  LEU D CA    1 
ATOM   5867 C  C     . LEU D 1 77  ? 2.483   71.382  83.872  1.00 121.80 ? 77  LEU D C     1 
ATOM   5868 O  O     . LEU D 1 77  ? 1.579   71.677  83.089  1.00 122.13 ? 77  LEU D O     1 
ATOM   5869 C  CB    . LEU D 1 77  ? 3.092   69.167  82.912  1.00 119.97 ? 77  LEU D CB    1 
ATOM   5870 C  CG    . LEU D 1 77  ? 3.981   68.239  82.082  1.00 119.31 ? 77  LEU D CG    1 
ATOM   5871 C  CD1   . LEU D 1 77  ? 3.272   66.915  81.855  1.00 118.58 ? 77  LEU D CD1   1 
ATOM   5872 C  CD2   . LEU D 1 77  ? 4.308   68.900  80.761  1.00 119.18 ? 77  LEU D CD2   1 
ATOM   5873 N  N     . ILE D 1 78  ? 2.495   71.783  85.140  1.00 123.05 ? 78  ILE D N     1 
ATOM   5874 C  CA    . ILE D 1 78  ? 1.421   72.622  85.666  1.00 124.65 ? 78  ILE D CA    1 
ATOM   5875 C  C     . ILE D 1 78  ? 1.946   73.767  86.540  1.00 125.68 ? 78  ILE D C     1 
ATOM   5876 O  O     . ILE D 1 78  ? 1.206   74.701  86.861  1.00 125.28 ? 78  ILE D O     1 
ATOM   5877 C  CB    . ILE D 1 78  ? 0.400   71.785  86.490  1.00 124.55 ? 78  ILE D CB    1 
ATOM   5878 C  CG1   . ILE D 1 78  ? 1.074   71.205  87.733  1.00 124.73 ? 78  ILE D CG1   1 
ATOM   5879 C  CG2   . ILE D 1 78  ? -0.157  70.647  85.644  1.00 124.03 ? 78  ILE D CG2   1 
ATOM   5880 C  CD1   . ILE D 1 78  ? 0.122   70.459  88.637  1.00 124.68 ? 78  ILE D CD1   1 
ATOM   5881 N  N     . ASN D 1 79  ? 3.226   73.693  86.904  1.00 127.28 ? 79  ASN D N     1 
ATOM   5882 C  CA    . ASN D 1 79  ? 3.867   74.702  87.750  1.00 128.71 ? 79  ASN D CA    1 
ATOM   5883 C  C     . ASN D 1 79  ? 3.179   74.769  89.110  1.00 129.25 ? 79  ASN D C     1 
ATOM   5884 O  O     . ASN D 1 79  ? 2.163   75.444  89.271  1.00 128.92 ? 79  ASN D O     1 
ATOM   5885 C  CB    . ASN D 1 79  ? 3.828   76.080  87.077  1.00 129.31 ? 79  ASN D CB    1 
ATOM   5886 C  CG    . ASN D 1 79  ? 4.731   76.162  85.857  1.00 130.01 ? 79  ASN D CG    1 
ATOM   5887 O  OD1   . ASN D 1 79  ? 5.946   75.977  85.952  1.00 130.11 ? 79  ASN D OD1   1 
ATOM   5888 N  ND2   . ASN D 1 79  ? 4.138   76.444  84.702  1.00 130.38 ? 79  ASN D ND2   1 
ATOM   5889 N  N     . ALA D 1 80  ? 3.746   74.069  90.087  1.00 130.16 ? 80  ALA D N     1 
ATOM   5890 C  CA    . ALA D 1 80  ? 3.175   74.026  91.428  1.00 131.12 ? 80  ALA D CA    1 
ATOM   5891 C  C     . ALA D 1 80  ? 3.896   74.906  92.451  1.00 131.68 ? 80  ALA D C     1 
ATOM   5892 O  O     . ALA D 1 80  ? 4.925   74.518  93.007  1.00 131.53 ? 80  ALA D O     1 
ATOM   5893 C  CB    . ALA D 1 80  ? 3.142   72.586  91.916  1.00 131.15 ? 80  ALA D CB    1 
ATOM   5894 N  N     . LYS D 1 81  ? 3.336   76.086  92.704  1.00 132.43 ? 81  LYS D N     1 
ATOM   5895 C  CA    . LYS D 1 81  ? 3.910   77.023  93.668  1.00 132.99 ? 81  LYS D CA    1 
ATOM   5896 C  C     . LYS D 1 81  ? 3.834   76.414  95.065  1.00 133.17 ? 81  LYS D C     1 
ATOM   5897 O  O     . LYS D 1 81  ? 4.848   76.040  95.651  1.00 132.68 ? 81  LYS D O     1 
ATOM   5898 C  CB    . LYS D 1 81  ? 3.135   78.350  93.650  1.00 132.91 ? 81  LYS D CB    1 
ATOM   5899 C  CG    . LYS D 1 81  ? 3.018   78.998  92.274  1.00 132.71 ? 81  LYS D CG    1 
ATOM   5900 C  CD    . LYS D 1 81  ? 4.366   79.483  91.743  1.00 131.92 ? 81  LYS D CD    1 
ATOM   5901 C  CE    . LYS D 1 81  ? 4.770   80.811  92.359  1.00 131.19 ? 81  LYS D CE    1 
ATOM   5902 N  NZ    . LYS D 1 81  ? 3.832   81.902  91.977  1.00 130.11 ? 81  LYS D NZ    1 
ATOM   5903 N  N     . ASN D 1 82  ? 2.615   76.311  95.581  1.00 133.71 ? 82  ASN D N     1 
ATOM   5904 C  CA    . ASN D 1 82  ? 2.379   75.760  96.908  1.00 134.17 ? 82  ASN D CA    1 
ATOM   5905 C  C     . ASN D 1 82  ? 1.721   74.388  96.780  1.00 133.90 ? 82  ASN D C     1 
ATOM   5906 O  O     . ASN D 1 82  ? 0.741   74.225  96.053  1.00 133.23 ? 82  ASN D O     1 
ATOM   5907 C  CB    . ASN D 1 82  ? 1.479   76.712  97.704  1.00 135.25 ? 82  ASN D CB    1 
ATOM   5908 C  CG    . ASN D 1 82  ? 1.572   76.493  99.206  1.00 136.41 ? 82  ASN D CG    1 
ATOM   5909 O  OD1   . ASN D 1 82  ? 2.656   76.562  99.792  1.00 136.62 ? 82  ASN D OD1   1 
ATOM   5910 N  ND2   . ASN D 1 82  ? 0.431   76.237  99.838  1.00 137.02 ? 82  ASN D ND2   1 
ATOM   5911 N  N     . THR D 1 83  ? 2.263   73.406  97.494  1.00 133.90 ? 83  THR D N     1 
ATOM   5912 C  CA    . THR D 1 83  ? 1.733   72.047  97.446  1.00 133.83 ? 83  THR D CA    1 
ATOM   5913 C  C     . THR D 1 83  ? 1.535   71.442  98.834  1.00 133.53 ? 83  THR D C     1 
ATOM   5914 O  O     . THR D 1 83  ? 1.518   72.152  99.838  1.00 133.16 ? 83  THR D O     1 
ATOM   5915 C  CB    . THR D 1 83  ? 2.673   71.126  96.652  1.00 134.09 ? 83  THR D CB    1 
ATOM   5916 O  OG1   . THR D 1 83  ? 3.880   70.915  97.398  1.00 134.34 ? 83  THR D OG1   1 
ATOM   5917 C  CG2   . THR D 1 83  ? 3.018   71.755  95.312  1.00 133.87 ? 83  THR D CG2   1 
ATOM   5918 N  N     . MET D 1 84  ? 1.394   70.119  98.874  1.00 133.57 ? 84  MET D N     1 
ATOM   5919 C  CA    . MET D 1 84  ? 1.195   69.382  100.119 1.00 133.53 ? 84  MET D CA    1 
ATOM   5920 C  C     . MET D 1 84  ? 1.128   67.876  99.856  1.00 132.86 ? 84  MET D C     1 
ATOM   5921 O  O     . MET D 1 84  ? 0.777   67.447  98.758  1.00 132.91 ? 84  MET D O     1 
ATOM   5922 C  CB    . MET D 1 84  ? -0.102  69.831  100.793 1.00 134.50 ? 84  MET D CB    1 
ATOM   5923 C  CG    . MET D 1 84  ? -0.464  69.036  102.039 1.00 135.63 ? 84  MET D CG    1 
ATOM   5924 S  SD    . MET D 1 84  ? -2.091  69.461  102.688 1.00 136.95 ? 84  MET D SD    1 
ATOM   5925 C  CE    . MET D 1 84  ? -1.659  70.757  103.857 1.00 136.42 ? 84  MET D CE    1 
ATOM   5926 N  N     . GLU D 1 85  ? 1.460   67.076  100.864 1.00 132.06 ? 85  GLU D N     1 
ATOM   5927 C  CA    . GLU D 1 85  ? 1.414   65.624  100.722 1.00 131.30 ? 85  GLU D CA    1 
ATOM   5928 C  C     . GLU D 1 85  ? 1.007   64.925  102.018 1.00 129.86 ? 85  GLU D C     1 
ATOM   5929 O  O     . GLU D 1 85  ? 1.687   65.036  103.037 1.00 130.11 ? 85  GLU D O     1 
ATOM   5930 C  CB    . GLU D 1 85  ? 2.771   65.085  100.245 1.00 132.51 ? 85  GLU D CB    1 
ATOM   5931 C  CG    . GLU D 1 85  ? 2.828   63.557  100.125 1.00 133.89 ? 85  GLU D CG    1 
ATOM   5932 C  CD    . GLU D 1 85  ? 4.083   63.057  99.425  1.00 134.50 ? 85  GLU D CD    1 
ATOM   5933 O  OE1   . GLU D 1 85  ? 4.268   63.383  98.232  1.00 135.35 ? 85  GLU D OE1   1 
ATOM   5934 O  OE2   . GLU D 1 85  ? 4.883   62.338  100.064 1.00 134.33 ? 85  GLU D OE2   1 
ATOM   5935 N  N     . ILE D 1 86  ? -0.111  64.206  101.966 1.00 127.92 ? 86  ILE D N     1 
ATOM   5936 C  CA    . ILE D 1 86  ? -0.618  63.473  103.119 1.00 125.75 ? 86  ILE D CA    1 
ATOM   5937 C  C     . ILE D 1 86  ? 0.010   62.080  103.118 1.00 124.59 ? 86  ILE D C     1 
ATOM   5938 O  O     . ILE D 1 86  ? -0.303  61.245  102.269 1.00 124.58 ? 86  ILE D O     1 
ATOM   5939 C  CB    . ILE D 1 86  ? -2.153  63.342  103.054 1.00 125.28 ? 86  ILE D CB    1 
ATOM   5940 C  CG1   . ILE D 1 86  ? -2.779  64.725  102.854 1.00 124.66 ? 86  ILE D CG1   1 
ATOM   5941 C  CG2   . ILE D 1 86  ? -2.673  62.694  104.327 1.00 124.65 ? 86  ILE D CG2   1 
ATOM   5942 C  CD1   . ILE D 1 86  ? -4.269  64.703  102.590 1.00 124.13 ? 86  ILE D CD1   1 
ATOM   5943 N  N     . GLY D 1 87  ? 0.902   61.840  104.070 1.00 123.00 ? 87  GLY D N     1 
ATOM   5944 C  CA    . GLY D 1 87  ? 1.575   60.558  104.145 1.00 121.53 ? 87  GLY D CA    1 
ATOM   5945 C  C     . GLY D 1 87  ? 2.926   60.669  103.468 1.00 120.56 ? 87  GLY D C     1 
ATOM   5946 O  O     . GLY D 1 87  ? 2.998   60.975  102.280 1.00 120.71 ? 87  GLY D O     1 
ATOM   5947 N  N     . VAL D 1 88  ? 3.997   60.424  104.216 1.00 119.49 ? 88  VAL D N     1 
ATOM   5948 C  CA    . VAL D 1 88  ? 5.339   60.526  103.664 1.00 118.34 ? 88  VAL D CA    1 
ATOM   5949 C  C     . VAL D 1 88  ? 6.153   59.243  103.743 1.00 118.25 ? 88  VAL D C     1 
ATOM   5950 O  O     . VAL D 1 88  ? 6.257   58.515  102.761 1.00 118.87 ? 88  VAL D O     1 
ATOM   5951 C  CB    . VAL D 1 88  ? 6.130   61.650  104.354 1.00 117.67 ? 88  VAL D CB    1 
ATOM   5952 C  CG1   . VAL D 1 88  ? 7.558   61.669  103.851 1.00 117.67 ? 88  VAL D CG1   1 
ATOM   5953 C  CG2   . VAL D 1 88  ? 5.466   62.981  104.083 1.00 117.31 ? 88  VAL D CG2   1 
ATOM   5954 N  N     . TYR D 1 89  ? 6.734   58.968  104.906 1.00 118.05 ? 89  TYR D N     1 
ATOM   5955 C  CA    . TYR D 1 89  ? 7.558   57.776  105.085 1.00 117.73 ? 89  TYR D CA    1 
ATOM   5956 C  C     . TYR D 1 89  ? 8.796   57.880  104.212 1.00 117.96 ? 89  TYR D C     1 
ATOM   5957 O  O     . TYR D 1 89  ? 8.694   57.843  102.988 1.00 118.76 ? 89  TYR D O     1 
ATOM   5958 C  CB    . TYR D 1 89  ? 6.792   56.510  104.691 1.00 116.85 ? 89  TYR D CB    1 
ATOM   5959 C  CG    . TYR D 1 89  ? 7.649   55.260  104.703 1.00 115.71 ? 89  TYR D CG    1 
ATOM   5960 C  CD1   . TYR D 1 89  ? 8.374   54.904  105.839 1.00 115.28 ? 89  TYR D CD1   1 
ATOM   5961 C  CD2   . TYR D 1 89  ? 7.726   54.425  103.588 1.00 114.59 ? 89  TYR D CD2   1 
ATOM   5962 C  CE1   . TYR D 1 89  ? 9.148   53.753  105.868 1.00 114.19 ? 89  TYR D CE1   1 
ATOM   5963 C  CE2   . TYR D 1 89  ? 8.502   53.268  103.610 1.00 113.56 ? 89  TYR D CE2   1 
ATOM   5964 C  CZ    . TYR D 1 89  ? 9.208   52.939  104.754 1.00 113.55 ? 89  TYR D CZ    1 
ATOM   5965 O  OH    . TYR D 1 89  ? 9.967   51.794  104.791 1.00 112.67 ? 89  TYR D OH    1 
ATOM   5966 N  N     . THR D 1 90  ? 9.962   58.000  104.835 1.00 117.86 ? 90  THR D N     1 
ATOM   5967 C  CA    . THR D 1 90  ? 11.207  58.104  104.082 1.00 117.89 ? 90  THR D CA    1 
ATOM   5968 C  C     . THR D 1 90  ? 11.264  59.417  103.309 1.00 118.44 ? 90  THR D C     1 
ATOM   5969 O  O     . THR D 1 90  ? 12.220  60.181  103.440 1.00 118.83 ? 90  THR D O     1 
ATOM   5970 C  CB    . THR D 1 90  ? 11.355  56.926  103.096 1.00 117.17 ? 90  THR D CB    1 
ATOM   5971 O  OG1   . THR D 1 90  ? 11.693  55.738  103.821 1.00 116.19 ? 90  THR D OG1   1 
ATOM   5972 C  CG2   . THR D 1 90  ? 12.423  57.217  102.063 1.00 117.22 ? 90  THR D CG2   1 
ATOM   5973 N  N     . GLY D 1 91  ? 10.244  59.671  102.497 1.00 118.84 ? 91  GLY D N     1 
ATOM   5974 C  CA    . GLY D 1 91  ? 10.199  60.904  101.735 1.00 119.01 ? 91  GLY D CA    1 
ATOM   5975 C  C     . GLY D 1 91  ? 10.477  60.782  100.250 1.00 119.08 ? 91  GLY D C     1 
ATOM   5976 O  O     . GLY D 1 91  ? 10.653  61.796  99.582  1.00 119.58 ? 91  GLY D O     1 
ATOM   5977 N  N     . TYR D 1 92  ? 10.517  59.562  99.721  1.00 118.93 ? 92  TYR D N     1 
ATOM   5978 C  CA    . TYR D 1 92  ? 10.778  59.383  98.296  1.00 118.40 ? 92  TYR D CA    1 
ATOM   5979 C  C     . TYR D 1 92  ? 9.716   60.100  97.462  1.00 117.62 ? 92  TYR D C     1 
ATOM   5980 O  O     . TYR D 1 92  ? 10.038  60.968  96.656  1.00 117.53 ? 92  TYR D O     1 
ATOM   5981 C  CB    . TYR D 1 92  ? 10.818  57.893  97.933  1.00 119.15 ? 92  TYR D CB    1 
ATOM   5982 C  CG    . TYR D 1 92  ? 11.344  57.623  96.536  1.00 119.48 ? 92  TYR D CG    1 
ATOM   5983 C  CD1   . TYR D 1 92  ? 10.576  57.911  95.408  1.00 119.82 ? 92  TYR D CD1   1 
ATOM   5984 C  CD2   . TYR D 1 92  ? 12.626  57.113  96.342  1.00 119.57 ? 92  TYR D CD2   1 
ATOM   5985 C  CE1   . TYR D 1 92  ? 11.070  57.698  94.122  1.00 119.78 ? 92  TYR D CE1   1 
ATOM   5986 C  CE2   . TYR D 1 92  ? 13.130  56.901  95.061  1.00 119.65 ? 92  TYR D CE2   1 
ATOM   5987 C  CZ    . TYR D 1 92  ? 12.349  57.193  93.957  1.00 119.93 ? 92  TYR D CZ    1 
ATOM   5988 O  OH    . TYR D 1 92  ? 12.847  56.977  92.690  1.00 119.44 ? 92  TYR D OH    1 
ATOM   5989 N  N     . SER D 1 93  ? 8.454   59.738  97.662  1.00 116.97 ? 93  SER D N     1 
ATOM   5990 C  CA    . SER D 1 93  ? 7.352   60.359  96.931  1.00 116.53 ? 93  SER D CA    1 
ATOM   5991 C  C     . SER D 1 93  ? 7.307   61.868  97.161  1.00 116.21 ? 93  SER D C     1 
ATOM   5992 O  O     . SER D 1 93  ? 6.661   62.605  96.414  1.00 115.22 ? 93  SER D O     1 
ATOM   5993 C  CB    . SER D 1 93  ? 6.020   59.738  97.367  1.00 117.03 ? 93  SER D CB    1 
ATOM   5994 O  OG    . SER D 1 93  ? 5.837   59.839  98.771  1.00 117.03 ? 93  SER D OG    1 
ATOM   5995 N  N     . LEU D 1 94  ? 8.001   62.320  98.200  1.00 116.41 ? 94  LEU D N     1 
ATOM   5996 C  CA    . LEU D 1 94  ? 8.036   63.735  98.549  1.00 116.52 ? 94  LEU D CA    1 
ATOM   5997 C  C     . LEU D 1 94  ? 9.268   64.423  97.956  1.00 116.38 ? 94  LEU D C     1 
ATOM   5998 O  O     . LEU D 1 94  ? 9.175   65.536  97.437  1.00 116.31 ? 94  LEU D O     1 
ATOM   5999 C  CB    . LEU D 1 94  ? 8.027   63.882  100.078 1.00 116.77 ? 94  LEU D CB    1 
ATOM   6000 C  CG    . LEU D 1 94  ? 7.652   65.223  100.723 1.00 116.92 ? 94  LEU D CG    1 
ATOM   6001 C  CD1   . LEU D 1 94  ? 8.698   66.280  100.420 1.00 117.17 ? 94  LEU D CD1   1 
ATOM   6002 C  CD2   . LEU D 1 94  ? 6.285   65.654  100.223 1.00 117.01 ? 94  LEU D CD2   1 
ATOM   6003 N  N     . LEU D 1 95  ? 10.416  63.751  98.036  1.00 116.17 ? 95  LEU D N     1 
ATOM   6004 C  CA    . LEU D 1 95  ? 11.675  64.283  97.515  1.00 115.55 ? 95  LEU D CA    1 
ATOM   6005 C  C     . LEU D 1 95  ? 11.473  64.759  96.083  1.00 115.39 ? 95  LEU D C     1 
ATOM   6006 O  O     . LEU D 1 95  ? 12.065  65.748  95.653  1.00 114.86 ? 95  LEU D O     1 
ATOM   6007 C  CB    . LEU D 1 95  ? 12.759  63.202  97.568  1.00 114.92 ? 95  LEU D CB    1 
ATOM   6008 C  CG    . LEU D 1 95  ? 14.206  63.623  97.314  1.00 114.44 ? 95  LEU D CG    1 
ATOM   6009 C  CD1   . LEU D 1 95  ? 15.144  62.494  97.704  1.00 114.57 ? 95  LEU D CD1   1 
ATOM   6010 C  CD2   . LEU D 1 95  ? 14.388  63.989  95.866  1.00 113.98 ? 95  LEU D CD2   1 
ATOM   6011 N  N     . ALA D 1 96  ? 10.627  64.041  95.354  1.00 115.73 ? 96  ALA D N     1 
ATOM   6012 C  CA    . ALA D 1 96  ? 10.312  64.379  93.974  1.00 116.28 ? 96  ALA D CA    1 
ATOM   6013 C  C     . ALA D 1 96  ? 9.560   65.701  93.947  1.00 116.70 ? 96  ALA D C     1 
ATOM   6014 O  O     . ALA D 1 96  ? 9.967   66.648  93.278  1.00 116.89 ? 96  ALA D O     1 
ATOM   6015 C  CB    . ALA D 1 96  ? 9.458   63.283  93.352  1.00 116.04 ? 96  ALA D CB    1 
ATOM   6016 N  N     . THR D 1 97  ? 8.454   65.757  94.679  1.00 117.67 ? 97  THR D N     1 
ATOM   6017 C  CA    . THR D 1 97  ? 7.648   66.966  94.744  1.00 118.50 ? 97  THR D CA    1 
ATOM   6018 C  C     . THR D 1 97  ? 8.560   68.148  95.067  1.00 119.68 ? 97  THR D C     1 
ATOM   6019 O  O     . THR D 1 97  ? 8.348   69.260  94.580  1.00 119.54 ? 97  THR D O     1 
ATOM   6020 C  CB    . THR D 1 97  ? 6.564   66.856  95.844  1.00 117.91 ? 97  THR D CB    1 
ATOM   6021 O  OG1   . THR D 1 97  ? 5.866   65.611  95.714  1.00 116.95 ? 97  THR D OG1   1 
ATOM   6022 C  CG2   . THR D 1 97  ? 5.566   67.996  95.721  1.00 117.39 ? 97  THR D CG2   1 
ATOM   6023 N  N     . ALA D 1 98  ? 9.585   67.884  95.879  1.00 120.94 ? 98  ALA D N     1 
ATOM   6024 C  CA    . ALA D 1 98  ? 10.545  68.901  96.309  1.00 122.10 ? 98  ALA D CA    1 
ATOM   6025 C  C     . ALA D 1 98  ? 11.527  69.340  95.228  1.00 122.99 ? 98  ALA D C     1 
ATOM   6026 O  O     . ALA D 1 98  ? 11.620  70.529  94.916  1.00 123.40 ? 98  ALA D O     1 
ATOM   6027 C  CB    . ALA D 1 98  ? 11.314  68.401  97.525  1.00 121.76 ? 98  ALA D CB    1 
ATOM   6028 N  N     . LEU D 1 99  ? 12.265  68.385  94.666  1.00 123.64 ? 99  LEU D N     1 
ATOM   6029 C  CA    . LEU D 1 99  ? 13.245  68.691  93.628  1.00 124.04 ? 99  LEU D CA    1 
ATOM   6030 C  C     . LEU D 1 99  ? 12.632  69.250  92.351  1.00 125.06 ? 99  LEU D C     1 
ATOM   6031 O  O     . LEU D 1 99  ? 13.294  69.977  91.613  1.00 124.97 ? 99  LEU D O     1 
ATOM   6032 C  CB    . LEU D 1 99  ? 14.068  67.449  93.285  1.00 122.80 ? 99  LEU D CB    1 
ATOM   6033 C  CG    . LEU D 1 99  ? 14.939  66.879  94.402  1.00 122.23 ? 99  LEU D CG    1 
ATOM   6034 C  CD1   . LEU D 1 99  ? 15.842  65.810  93.838  1.00 121.97 ? 99  LEU D CD1   1 
ATOM   6035 C  CD2   . LEU D 1 99  ? 15.775  67.980  95.016  1.00 122.65 ? 99  LEU D CD2   1 
ATOM   6036 N  N     . ALA D 1 100 ? 11.372  68.914  92.093  1.00 126.80 ? 100 ALA D N     1 
ATOM   6037 C  CA    . ALA D 1 100 ? 10.686  69.386  90.893  1.00 129.16 ? 100 ALA D CA    1 
ATOM   6038 C  C     . ALA D 1 100 ? 10.243  70.844  91.015  1.00 130.89 ? 100 ALA D C     1 
ATOM   6039 O  O     . ALA D 1 100 ? 10.585  71.681  90.174  1.00 131.15 ? 100 ALA D O     1 
ATOM   6040 C  CB    . ALA D 1 100 ? 9.482   68.494  90.595  1.00 128.89 ? 100 ALA D CB    1 
ATOM   6041 N  N     . ILE D 1 101 ? 9.477   71.143  92.059  1.00 132.90 ? 101 ILE D N     1 
ATOM   6042 C  CA    . ILE D 1 101 ? 8.995   72.500  92.286  1.00 134.58 ? 101 ILE D CA    1 
ATOM   6043 C  C     . ILE D 1 101 ? 10.165  73.485  92.258  1.00 136.13 ? 101 ILE D C     1 
ATOM   6044 O  O     . ILE D 1 101 ? 11.313  73.101  92.491  1.00 136.10 ? 101 ILE D O     1 
ATOM   6045 C  CB    . ILE D 1 101 ? 8.276   72.608  93.646  1.00 134.21 ? 101 ILE D CB    1 
ATOM   6046 C  CG1   . ILE D 1 101 ? 9.224   72.177  94.765  1.00 133.78 ? 101 ILE D CG1   1 
ATOM   6047 C  CG2   . ILE D 1 101 ? 7.019   71.748  93.638  1.00 133.63 ? 101 ILE D CG2   1 
ATOM   6048 C  CD1   . ILE D 1 101 ? 8.606   72.215  96.137  1.00 134.07 ? 101 ILE D CD1   1 
ATOM   6049 N  N     . PRO D 1 102 ? 9.888   74.770  91.969  1.00 137.55 ? 102 PRO D N     1 
ATOM   6050 C  CA    . PRO D 1 102 ? 10.932  75.800  91.912  1.00 138.57 ? 102 PRO D CA    1 
ATOM   6051 C  C     . PRO D 1 102 ? 11.674  76.018  93.237  1.00 139.55 ? 102 PRO D C     1 
ATOM   6052 O  O     . PRO D 1 102 ? 11.990  75.060  93.947  1.00 139.81 ? 102 PRO D O     1 
ATOM   6053 C  CB    . PRO D 1 102 ? 10.162  77.041  91.452  1.00 138.43 ? 102 PRO D CB    1 
ATOM   6054 C  CG    . PRO D 1 102 ? 8.793   76.818  92.023  1.00 138.05 ? 102 PRO D CG    1 
ATOM   6055 C  CD    . PRO D 1 102 ? 8.559   75.359  91.718  1.00 137.83 ? 102 PRO D CD    1 
ATOM   6056 N  N     . GLU D 1 103 ? 11.953  77.280  93.559  1.00 140.55 ? 103 GLU D N     1 
ATOM   6057 C  CA    . GLU D 1 103 ? 12.659  77.634  94.789  1.00 140.95 ? 103 GLU D CA    1 
ATOM   6058 C  C     . GLU D 1 103 ? 11.749  78.383  95.769  1.00 140.96 ? 103 GLU D C     1 
ATOM   6059 O  O     . GLU D 1 103 ? 12.077  78.528  96.948  1.00 140.74 ? 103 GLU D O     1 
ATOM   6060 C  CB    . GLU D 1 103 ? 13.884  78.499  94.460  1.00 141.33 ? 103 GLU D CB    1 
ATOM   6061 C  CG    . GLU D 1 103 ? 14.738  78.867  95.668  1.00 142.31 ? 103 GLU D CG    1 
ATOM   6062 C  CD    . GLU D 1 103 ? 15.495  77.679  96.240  1.00 142.91 ? 103 GLU D CD    1 
ATOM   6063 O  OE1   . GLU D 1 103 ? 14.885  76.601  96.393  1.00 143.49 ? 103 GLU D OE1   1 
ATOM   6064 O  OE2   . GLU D 1 103 ? 16.699  77.824  96.545  1.00 142.81 ? 103 GLU D OE2   1 
ATOM   6065 N  N     . ASP D 1 104 ? 10.604  78.849  95.279  1.00 141.18 ? 104 ASP D N     1 
ATOM   6066 C  CA    . ASP D 1 104 ? 9.664   79.588  96.115  1.00 141.37 ? 104 ASP D CA    1 
ATOM   6067 C  C     . ASP D 1 104 ? 8.564   78.690  96.669  1.00 141.12 ? 104 ASP D C     1 
ATOM   6068 O  O     . ASP D 1 104 ? 7.814   79.089  97.561  1.00 141.04 ? 104 ASP D O     1 
ATOM   6069 C  CB    . ASP D 1 104 ? 9.037   80.742  95.318  1.00 142.05 ? 104 ASP D CB    1 
ATOM   6070 C  CG    . ASP D 1 104 ? 7.947   80.280  94.362  1.00 142.34 ? 104 ASP D CG    1 
ATOM   6071 O  OD1   . ASP D 1 104 ? 8.212   79.389  93.528  1.00 142.59 ? 104 ASP D OD1   1 
ATOM   6072 O  OD2   . ASP D 1 104 ? 6.822   80.820  94.445  1.00 142.29 ? 104 ASP D OD2   1 
ATOM   6073 N  N     . GLY D 1 105 ? 8.475   77.475  96.138  1.00 140.73 ? 105 GLY D N     1 
ATOM   6074 C  CA    . GLY D 1 105 ? 7.456   76.547  96.590  1.00 140.28 ? 105 GLY D CA    1 
ATOM   6075 C  C     . GLY D 1 105 ? 7.704   75.977  97.973  1.00 139.90 ? 105 GLY D C     1 
ATOM   6076 O  O     . GLY D 1 105 ? 8.841   75.917  98.439  1.00 139.90 ? 105 GLY D O     1 
ATOM   6077 N  N     . LYS D 1 106 ? 6.627   75.565  98.635  1.00 139.50 ? 106 LYS D N     1 
ATOM   6078 C  CA    . LYS D 1 106 ? 6.703   74.978  99.969  1.00 138.82 ? 106 LYS D CA    1 
ATOM   6079 C  C     . LYS D 1 106 ? 5.688   73.845  100.095 1.00 138.13 ? 106 LYS D C     1 
ATOM   6080 O  O     . LYS D 1 106 ? 4.529   73.989  99.702  1.00 137.83 ? 106 LYS D O     1 
ATOM   6081 C  CB    . LYS D 1 106 ? 6.418   76.030  101.052 1.00 139.02 ? 106 LYS D CB    1 
ATOM   6082 C  CG    . LYS D 1 106 ? 7.635   76.811  101.558 1.00 139.01 ? 106 LYS D CG    1 
ATOM   6083 C  CD    . LYS D 1 106 ? 8.087   77.890  100.587 1.00 139.03 ? 106 LYS D CD    1 
ATOM   6084 C  CE    . LYS D 1 106 ? 9.179   78.766  101.196 1.00 138.81 ? 106 LYS D CE    1 
ATOM   6085 N  NZ    . LYS D 1 106 ? 10.417  78.004  101.519 1.00 138.89 ? 106 LYS D NZ    1 
ATOM   6086 N  N     . ILE D 1 107 ? 6.131   72.717  100.639 1.00 137.46 ? 107 ILE D N     1 
ATOM   6087 C  CA    . ILE D 1 107 ? 5.259   71.565  100.828 1.00 136.87 ? 107 ILE D CA    1 
ATOM   6088 C  C     . ILE D 1 107 ? 4.813   71.508  102.289 1.00 136.47 ? 107 ILE D C     1 
ATOM   6089 O  O     . ILE D 1 107 ? 5.465   72.075  103.167 1.00 136.23 ? 107 ILE D O     1 
ATOM   6090 C  CB    . ILE D 1 107 ? 5.986   70.245  100.475 1.00 136.55 ? 107 ILE D CB    1 
ATOM   6091 C  CG1   . ILE D 1 107 ? 6.584   70.339  99.072  1.00 136.00 ? 107 ILE D CG1   1 
ATOM   6092 C  CG2   . ILE D 1 107 ? 5.009   69.076  100.535 1.00 136.22 ? 107 ILE D CG2   1 
ATOM   6093 C  CD1   . ILE D 1 107 ? 7.397   69.130  98.676  1.00 135.77 ? 107 ILE D CD1   1 
ATOM   6094 N  N     . LEU D 1 108 ? 3.694   70.835  102.538 1.00 135.97 ? 108 LEU D N     1 
ATOM   6095 C  CA    . LEU D 1 108 ? 3.158   70.690  103.887 1.00 135.19 ? 108 LEU D CA    1 
ATOM   6096 C  C     . LEU D 1 108 ? 2.948   69.202  104.150 1.00 134.46 ? 108 LEU D C     1 
ATOM   6097 O  O     . LEU D 1 108 ? 1.818   68.720  104.194 1.00 134.12 ? 108 LEU D O     1 
ATOM   6098 C  CB    . LEU D 1 108 ? 1.823   71.438  104.022 1.00 135.63 ? 108 LEU D CB    1 
ATOM   6099 C  CG    . LEU D 1 108 ? 1.748   72.968  103.851 1.00 136.02 ? 108 LEU D CG    1 
ATOM   6100 C  CD1   . LEU D 1 108 ? 2.651   73.646  104.868 1.00 135.74 ? 108 LEU D CD1   1 
ATOM   6101 C  CD2   . LEU D 1 108 ? 2.141   73.372  102.437 1.00 135.85 ? 108 LEU D CD2   1 
ATOM   6102 N  N     . ALA D 1 109 ? 4.051   68.481  104.320 1.00 133.97 ? 109 ALA D N     1 
ATOM   6103 C  CA    . ALA D 1 109 ? 4.016   67.043  104.562 1.00 133.98 ? 109 ALA D CA    1 
ATOM   6104 C  C     . ALA D 1 109 ? 3.395   66.662  105.903 1.00 133.95 ? 109 ALA D C     1 
ATOM   6105 O  O     . ALA D 1 109 ? 3.461   67.418  106.870 1.00 134.37 ? 109 ALA D O     1 
ATOM   6106 C  CB    . ALA D 1 109 ? 5.425   66.474  104.467 1.00 134.19 ? 109 ALA D CB    1 
ATOM   6107 N  N     . MET D 1 110 ? 2.797   65.475  105.949 1.00 133.72 ? 110 MET D N     1 
ATOM   6108 C  CA    . MET D 1 110 ? 2.159   64.958  107.158 1.00 133.48 ? 110 MET D CA    1 
ATOM   6109 C  C     . MET D 1 110 ? 2.271   63.440  107.188 1.00 133.49 ? 110 MET D C     1 
ATOM   6110 O  O     . MET D 1 110 ? 2.020   62.778  106.182 1.00 133.63 ? 110 MET D O     1 
ATOM   6111 C  CB    . MET D 1 110 ? 0.684   65.338  107.187 1.00 133.17 ? 110 MET D CB    1 
ATOM   6112 C  CG    . MET D 1 110 ? 0.420   66.818  107.218 1.00 132.82 ? 110 MET D CG    1 
ATOM   6113 S  SD    . MET D 1 110 ? -1.324  67.108  106.972 1.00 132.95 ? 110 MET D SD    1 
ATOM   6114 C  CE    . MET D 1 110 ? -1.417  67.025  105.181 1.00 133.02 ? 110 MET D CE    1 
ATOM   6115 N  N     . ASP D 1 111 ? 2.633   62.891  108.344 1.00 133.31 ? 111 ASP D N     1 
ATOM   6116 C  CA    . ASP D 1 111 ? 2.783   61.448  108.484 1.00 133.06 ? 111 ASP D CA    1 
ATOM   6117 C  C     . ASP D 1 111 ? 2.845   61.047  109.954 1.00 132.92 ? 111 ASP D C     1 
ATOM   6118 O  O     . ASP D 1 111 ? 3.554   61.667  110.747 1.00 132.83 ? 111 ASP D O     1 
ATOM   6119 C  CB    . ASP D 1 111 ? 4.060   60.995  107.769 1.00 133.33 ? 111 ASP D CB    1 
ATOM   6120 C  CG    . ASP D 1 111 ? 4.169   59.486  107.655 1.00 133.63 ? 111 ASP D CG    1 
ATOM   6121 O  OD1   . ASP D 1 111 ? 4.127   58.800  108.696 1.00 134.12 ? 111 ASP D OD1   1 
ATOM   6122 O  OD2   . ASP D 1 111 ? 4.307   58.987  106.519 1.00 133.78 ? 111 ASP D OD2   1 
ATOM   6123 N  N     . ILE D 1 112 ? 2.094   60.010  110.312 1.00 132.79 ? 112 ILE D N     1 
ATOM   6124 C  CA    . ILE D 1 112 ? 2.075   59.512  111.682 1.00 132.71 ? 112 ILE D CA    1 
ATOM   6125 C  C     . ILE D 1 112 ? 3.498   59.336  112.215 1.00 132.78 ? 112 ILE D C     1 
ATOM   6126 O  O     . ILE D 1 112 ? 3.914   60.028  113.146 1.00 132.81 ? 112 ILE D O     1 
ATOM   6127 C  CB    . ILE D 1 112 ? 1.364   58.143  111.772 1.00 132.58 ? 112 ILE D CB    1 
ATOM   6128 C  CG1   . ILE D 1 112 ? -0.124  58.298  111.469 1.00 132.71 ? 112 ILE D CG1   1 
ATOM   6129 C  CG2   . ILE D 1 112 ? 1.555   57.545  113.153 1.00 132.86 ? 112 ILE D CG2   1 
ATOM   6130 C  CD1   . ILE D 1 112 ? -0.887  56.983  111.531 1.00 133.41 ? 112 ILE D CD1   1 
ATOM   6131 N  N     . ASN D 1 113 ? 4.237   58.405  111.616 1.00 132.46 ? 113 ASN D N     1 
ATOM   6132 C  CA    . ASN D 1 113 ? 5.604   58.122  112.033 1.00 132.47 ? 113 ASN D CA    1 
ATOM   6133 C  C     . ASN D 1 113 ? 6.568   59.211  111.565 1.00 132.95 ? 113 ASN D C     1 
ATOM   6134 O  O     . ASN D 1 113 ? 7.010   59.212  110.417 1.00 133.27 ? 113 ASN D O     1 
ATOM   6135 C  CB    . ASN D 1 113 ? 6.047   56.763  111.481 1.00 131.69 ? 113 ASN D CB    1 
ATOM   6136 C  CG    . ASN D 1 113 ? 7.167   56.139  112.295 1.00 131.12 ? 113 ASN D CG    1 
ATOM   6137 O  OD1   . ASN D 1 113 ? 8.200   56.762  112.534 1.00 130.57 ? 113 ASN D OD1   1 
ATOM   6138 N  ND2   . ASN D 1 113 ? 6.964   54.900  112.724 1.00 130.65 ? 113 ASN D ND2   1 
ATOM   6139 N  N     . LYS D 1 114 ? 6.890   60.136  112.467 1.00 133.66 ? 114 LYS D N     1 
ATOM   6140 C  CA    . LYS D 1 114 ? 7.799   61.240  112.163 1.00 133.95 ? 114 LYS D CA    1 
ATOM   6141 C  C     . LYS D 1 114 ? 9.236   60.773  111.999 1.00 134.12 ? 114 LYS D C     1 
ATOM   6142 O  O     . LYS D 1 114 ? 9.968   61.268  111.144 1.00 134.31 ? 114 LYS D O     1 
ATOM   6143 C  CB    . LYS D 1 114 ? 7.750   62.294  113.274 1.00 133.91 ? 114 LYS D CB    1 
ATOM   6144 C  CG    . LYS D 1 114 ? 8.727   63.444  113.071 1.00 133.14 ? 114 LYS D CG    1 
ATOM   6145 C  CD    . LYS D 1 114 ? 8.471   64.567  114.053 1.00 132.77 ? 114 LYS D CD    1 
ATOM   6146 C  CE    . LYS D 1 114 ? 9.280   65.798  113.690 1.00 132.71 ? 114 LYS D CE    1 
ATOM   6147 N  NZ    . LYS D 1 114 ? 8.948   66.949  114.572 1.00 132.78 ? 114 LYS D NZ    1 
ATOM   6148 N  N     . GLU D 1 115 ? 9.633   59.821  112.832 1.00 134.12 ? 115 GLU D N     1 
ATOM   6149 C  CA    . GLU D 1 115 ? 10.984  59.289  112.801 1.00 134.51 ? 115 GLU D CA    1 
ATOM   6150 C  C     . GLU D 1 115 ? 11.393  58.792  111.417 1.00 134.25 ? 115 GLU D C     1 
ATOM   6151 O  O     . GLU D 1 115 ? 12.524  59.012  110.984 1.00 134.65 ? 115 GLU D O     1 
ATOM   6152 C  CB    . GLU D 1 115 ? 11.098  58.169  113.828 1.00 135.38 ? 115 GLU D CB    1 
ATOM   6153 C  CG    . GLU D 1 115 ? 10.514  58.564  115.171 1.00 136.96 ? 115 GLU D CG    1 
ATOM   6154 C  CD    . GLU D 1 115 ? 10.574  57.445  116.180 1.00 137.78 ? 115 GLU D CD    1 
ATOM   6155 O  OE1   . GLU D 1 115 ? 10.087  56.339  115.860 1.00 138.23 ? 115 GLU D OE1   1 
ATOM   6156 O  OE2   . GLU D 1 115 ? 11.103  57.676  117.290 1.00 137.93 ? 115 GLU D OE2   1 
ATOM   6157 N  N     . ASN D 1 116 ? 10.475  58.125  110.723 1.00 133.64 ? 116 ASN D N     1 
ATOM   6158 C  CA    . ASN D 1 116 ? 10.756  57.612  109.384 1.00 132.63 ? 116 ASN D CA    1 
ATOM   6159 C  C     . ASN D 1 116 ? 11.069  58.736  108.405 1.00 132.81 ? 116 ASN D C     1 
ATOM   6160 O  O     . ASN D 1 116 ? 12.127  58.740  107.780 1.00 132.67 ? 116 ASN D O     1 
ATOM   6161 C  CB    . ASN D 1 116 ? 9.572   56.793  108.873 1.00 130.90 ? 116 ASN D CB    1 
ATOM   6162 C  CG    . ASN D 1 116 ? 9.574   55.387  109.411 1.00 129.14 ? 116 ASN D CG    1 
ATOM   6163 O  OD1   . ASN D 1 116 ? 8.601   54.652  109.257 1.00 128.03 ? 116 ASN D OD1   1 
ATOM   6164 N  ND2   . ASN D 1 116 ? 10.678  54.998  110.040 1.00 127.83 ? 116 ASN D ND2   1 
ATOM   6165 N  N     . TYR D 1 117 ? 10.145  59.681  108.264 1.00 132.85 ? 117 TYR D N     1 
ATOM   6166 C  CA    . TYR D 1 117 ? 10.354  60.809  107.367 1.00 132.70 ? 117 TYR D CA    1 
ATOM   6167 C  C     . TYR D 1 117 ? 11.766  61.353  107.548 1.00 132.66 ? 117 TYR D C     1 
ATOM   6168 O  O     . TYR D 1 117 ? 12.511  61.522  106.586 1.00 132.51 ? 117 TYR D O     1 
ATOM   6169 C  CB    . TYR D 1 117 ? 9.347   61.919  107.666 1.00 132.87 ? 117 TYR D CB    1 
ATOM   6170 C  CG    . TYR D 1 117 ? 9.882   63.300  107.364 1.00 133.36 ? 117 TYR D CG    1 
ATOM   6171 C  CD1   . TYR D 1 117 ? 10.215  63.673  106.063 1.00 133.71 ? 117 TYR D CD1   1 
ATOM   6172 C  CD2   . TYR D 1 117 ? 10.100  64.220  108.388 1.00 133.61 ? 117 TYR D CD2   1 
ATOM   6173 C  CE1   . TYR D 1 117 ? 10.756  64.930  105.788 1.00 133.93 ? 117 TYR D CE1   1 
ATOM   6174 C  CE2   . TYR D 1 117 ? 10.640  65.480  108.125 1.00 133.72 ? 117 TYR D CE2   1 
ATOM   6175 C  CZ    . TYR D 1 117 ? 10.966  65.827  106.824 1.00 133.66 ? 117 TYR D CZ    1 
ATOM   6176 O  OH    . TYR D 1 117 ? 11.506  67.064  106.561 1.00 133.03 ? 117 TYR D OH    1 
ATOM   6177 N  N     . GLU D 1 118 ? 12.124  61.625  108.794 1.00 133.09 ? 118 GLU D N     1 
ATOM   6178 C  CA    . GLU D 1 118 ? 13.438  62.159  109.111 1.00 133.84 ? 118 GLU D CA    1 
ATOM   6179 C  C     . GLU D 1 118 ? 14.541  61.132  108.865 1.00 134.06 ? 118 GLU D C     1 
ATOM   6180 O  O     . GLU D 1 118 ? 15.722  61.475  108.862 1.00 134.38 ? 118 GLU D O     1 
ATOM   6181 C  CB    . GLU D 1 118 ? 13.475  62.625  110.571 1.00 134.43 ? 118 GLU D CB    1 
ATOM   6182 C  CG    . GLU D 1 118 ? 12.424  63.679  110.918 1.00 135.32 ? 118 GLU D CG    1 
ATOM   6183 C  CD    . GLU D 1 118 ? 12.477  64.123  112.375 1.00 135.69 ? 118 GLU D CD    1 
ATOM   6184 O  OE1   . GLU D 1 118 ? 12.322  63.266  113.274 1.00 135.85 ? 118 GLU D OE1   1 
ATOM   6185 O  OE2   . GLU D 1 118 ? 12.671  65.333  112.621 1.00 135.97 ? 118 GLU D OE2   1 
ATOM   6186 N  N     . LEU D 1 119 ? 14.159  59.875  108.660 1.00 134.08 ? 119 LEU D N     1 
ATOM   6187 C  CA    . LEU D 1 119 ? 15.141  58.822  108.417 1.00 134.20 ? 119 LEU D CA    1 
ATOM   6188 C  C     . LEU D 1 119 ? 15.807  59.070  107.072 1.00 134.38 ? 119 LEU D C     1 
ATOM   6189 O  O     . LEU D 1 119 ? 16.972  58.727  106.869 1.00 134.56 ? 119 LEU D O     1 
ATOM   6190 C  CB    . LEU D 1 119 ? 14.471  57.443  108.419 1.00 133.94 ? 119 LEU D CB    1 
ATOM   6191 C  CG    . LEU D 1 119 ? 15.395  56.221  108.412 1.00 133.52 ? 119 LEU D CG    1 
ATOM   6192 C  CD1   . LEU D 1 119 ? 16.233  56.209  109.684 1.00 133.23 ? 119 LEU D CD1   1 
ATOM   6193 C  CD2   . LEU D 1 119 ? 14.565  54.953  108.314 1.00 133.23 ? 119 LEU D CD2   1 
ATOM   6194 N  N     . GLY D 1 120 ? 15.055  59.676  106.157 1.00 134.39 ? 120 GLY D N     1 
ATOM   6195 C  CA    . GLY D 1 120 ? 15.580  59.974  104.839 1.00 134.52 ? 120 GLY D CA    1 
ATOM   6196 C  C     . GLY D 1 120 ? 15.832  61.459  104.651 1.00 134.82 ? 120 GLY D C     1 
ATOM   6197 O  O     . GLY D 1 120 ? 16.060  61.920  103.532 1.00 134.99 ? 120 GLY D O     1 
ATOM   6198 N  N     . LEU D 1 121 ? 15.791  62.210  105.749 1.00 134.92 ? 121 LEU D N     1 
ATOM   6199 C  CA    . LEU D 1 121 ? 16.019  63.652  105.707 1.00 134.27 ? 121 LEU D CA    1 
ATOM   6200 C  C     . LEU D 1 121 ? 17.469  63.980  105.352 1.00 134.32 ? 121 LEU D C     1 
ATOM   6201 O  O     . LEU D 1 121 ? 17.727  64.945  104.637 1.00 134.50 ? 121 LEU D O     1 
ATOM   6202 C  CB    . LEU D 1 121 ? 15.648  64.287  107.049 1.00 133.61 ? 121 LEU D CB    1 
ATOM   6203 C  CG    . LEU D 1 121 ? 15.514  65.810  107.060 1.00 133.22 ? 121 LEU D CG    1 
ATOM   6204 C  CD1   . LEU D 1 121 ? 14.520  66.239  105.998 1.00 132.90 ? 121 LEU D CD1   1 
ATOM   6205 C  CD2   . LEU D 1 121 ? 15.060  66.278  108.436 1.00 133.22 ? 121 LEU D CD2   1 
ATOM   6206 N  N     . PRO D 1 122 ? 18.439  63.190  105.854 1.00 134.44 ? 122 PRO D N     1 
ATOM   6207 C  CA    . PRO D 1 122 ? 19.839  63.476  105.523 1.00 134.77 ? 122 PRO D CA    1 
ATOM   6208 C  C     . PRO D 1 122 ? 20.035  63.486  104.005 1.00 135.16 ? 122 PRO D C     1 
ATOM   6209 O  O     . PRO D 1 122 ? 21.022  64.018  103.490 1.00 135.60 ? 122 PRO D O     1 
ATOM   6210 C  CB    . PRO D 1 122 ? 20.591  62.329  106.194 1.00 134.35 ? 122 PRO D CB    1 
ATOM   6211 C  CG    . PRO D 1 122 ? 19.764  62.058  107.399 1.00 134.30 ? 122 PRO D CG    1 
ATOM   6212 C  CD    . PRO D 1 122 ? 18.356  62.100  106.843 1.00 134.47 ? 122 PRO D CD    1 
ATOM   6213 N  N     . VAL D 1 123 ? 19.081  62.884  103.300 1.00 135.05 ? 123 VAL D N     1 
ATOM   6214 C  CA    . VAL D 1 123 ? 19.114  62.811  101.847 1.00 134.62 ? 123 VAL D CA    1 
ATOM   6215 C  C     . VAL D 1 123 ? 18.053  63.753  101.287 1.00 134.71 ? 123 VAL D C     1 
ATOM   6216 O  O     . VAL D 1 123 ? 17.335  63.425  100.343 1.00 134.78 ? 123 VAL D O     1 
ATOM   6217 C  CB    . VAL D 1 123 ? 18.853  61.366  101.361 1.00 134.30 ? 123 VAL D CB    1 
ATOM   6218 C  CG1   . VAL D 1 123 ? 18.933  61.294  99.844  1.00 133.95 ? 123 VAL D CG1   1 
ATOM   6219 C  CG2   . VAL D 1 123 ? 19.871  60.423  101.989 1.00 133.80 ? 123 VAL D CG2   1 
ATOM   6220 N  N     . ILE D 1 124 ? 17.955  64.924  101.906 1.00 134.78 ? 124 ILE D N     1 
ATOM   6221 C  CA    . ILE D 1 124 ? 17.022  65.971  101.506 1.00 135.40 ? 124 ILE D CA    1 
ATOM   6222 C  C     . ILE D 1 124 ? 17.634  67.258  102.045 1.00 135.93 ? 124 ILE D C     1 
ATOM   6223 O  O     . ILE D 1 124 ? 17.364  68.355  101.555 1.00 135.78 ? 124 ILE D O     1 
ATOM   6224 C  CB    . ILE D 1 124 ? 15.616  65.778  102.128 1.00 135.55 ? 124 ILE D CB    1 
ATOM   6225 C  CG1   . ILE D 1 124 ? 15.050  64.405  101.750 1.00 135.59 ? 124 ILE D CG1   1 
ATOM   6226 C  CG2   . ILE D 1 124 ? 14.677  66.874  101.629 1.00 135.53 ? 124 ILE D CG2   1 
ATOM   6227 C  CD1   . ILE D 1 124 ? 13.666  64.123  102.310 1.00 135.85 ? 124 ILE D CD1   1 
ATOM   6228 N  N     . LYS D 1 125 ? 18.463  67.096  103.073 1.00 136.59 ? 125 LYS D N     1 
ATOM   6229 C  CA    . LYS D 1 125 ? 19.170  68.204  103.705 1.00 136.98 ? 125 LYS D CA    1 
ATOM   6230 C  C     . LYS D 1 125 ? 20.385  68.400  102.805 1.00 137.25 ? 125 LYS D C     1 
ATOM   6231 O  O     . LYS D 1 125 ? 20.835  69.520  102.559 1.00 137.25 ? 125 LYS D O     1 
ATOM   6232 C  CB    . LYS D 1 125 ? 19.638  67.800  105.107 1.00 136.84 ? 125 LYS D CB    1 
ATOM   6233 C  CG    . LYS D 1 125 ? 19.398  68.827  106.204 1.00 136.89 ? 125 LYS D CG    1 
ATOM   6234 C  CD    . LYS D 1 125 ? 18.078  68.568  106.916 1.00 137.01 ? 125 LYS D CD    1 
ATOM   6235 C  CE    . LYS D 1 125 ? 17.971  69.369  108.206 1.00 137.17 ? 125 LYS D CE    1 
ATOM   6236 N  NZ    . LYS D 1 125 ? 16.767  68.999  109.008 1.00 137.23 ? 125 LYS D NZ    1 
ATOM   6237 N  N     . LYS D 1 126 ? 20.896  67.273  102.318 1.00 137.40 ? 126 LYS D N     1 
ATOM   6238 C  CA    . LYS D 1 126 ? 22.052  67.229  101.435 1.00 137.20 ? 126 LYS D CA    1 
ATOM   6239 C  C     . LYS D 1 126 ? 21.703  67.826  100.078 1.00 137.10 ? 126 LYS D C     1 
ATOM   6240 O  O     . LYS D 1 126 ? 22.403  68.704  99.581  1.00 137.05 ? 126 LYS D O     1 
ATOM   6241 C  CB    . LYS D 1 126 ? 22.502  65.776  101.270 1.00 137.19 ? 126 LYS D CB    1 
ATOM   6242 C  CG    . LYS D 1 126 ? 23.665  65.565  100.326 1.00 137.64 ? 126 LYS D CG    1 
ATOM   6243 C  CD    . LYS D 1 126 ? 24.036  64.089  100.273 1.00 138.36 ? 126 LYS D CD    1 
ATOM   6244 C  CE    . LYS D 1 126 ? 25.258  63.842  99.397  1.00 138.84 ? 126 LYS D CE    1 
ATOM   6245 N  NZ    . LYS D 1 126 ? 25.736  62.428  99.472  1.00 138.34 ? 126 LYS D NZ    1 
ATOM   6246 N  N     . ALA D 1 127 ? 20.609  67.350  99.490  1.00 137.31 ? 127 ALA D N     1 
ATOM   6247 C  CA    . ALA D 1 127 ? 20.159  67.826  98.185  1.00 137.62 ? 127 ALA D CA    1 
ATOM   6248 C  C     . ALA D 1 127 ? 19.419  69.156  98.276  1.00 137.92 ? 127 ALA D C     1 
ATOM   6249 O  O     . ALA D 1 127 ? 18.880  69.641  97.283  1.00 137.45 ? 127 ALA D O     1 
ATOM   6250 C  CB    . ALA D 1 127 ? 19.263  66.778  97.530  1.00 137.37 ? 127 ALA D CB    1 
ATOM   6251 N  N     . GLY D 1 128 ? 19.392  69.742  99.467  1.00 138.54 ? 128 GLY D N     1 
ATOM   6252 C  CA    . GLY D 1 128 ? 18.709  71.012  99.641  1.00 139.74 ? 128 GLY D CA    1 
ATOM   6253 C  C     . GLY D 1 128 ? 17.204  70.901  99.488  1.00 140.83 ? 128 GLY D C     1 
ATOM   6254 O  O     . GLY D 1 128 ? 16.613  69.888  99.862  1.00 141.15 ? 128 GLY D O     1 
ATOM   6255 N  N     . VAL D 1 129 ? 16.588  71.950  98.942  1.00 141.63 ? 129 VAL D N     1 
ATOM   6256 C  CA    . VAL D 1 129 ? 15.136  72.015  98.724  1.00 141.96 ? 129 VAL D CA    1 
ATOM   6257 C  C     . VAL D 1 129 ? 14.363  71.598  99.977  1.00 141.96 ? 129 VAL D C     1 
ATOM   6258 O  O     . VAL D 1 129 ? 13.157  71.345  99.930  1.00 141.57 ? 129 VAL D O     1 
ATOM   6259 C  CB    . VAL D 1 129 ? 14.704  71.118  97.523  1.00 141.97 ? 129 VAL D CB    1 
ATOM   6260 C  CG1   . VAL D 1 129 ? 14.543  69.670  97.963  1.00 142.18 ? 129 VAL D CG1   1 
ATOM   6261 C  CG2   . VAL D 1 129 ? 13.420  71.639  96.920  1.00 141.76 ? 129 VAL D CG2   1 
ATOM   6262 N  N     . ASP D 1 130 ? 15.072  71.548  101.099 1.00 142.06 ? 130 ASP D N     1 
ATOM   6263 C  CA    . ASP D 1 130 ? 14.487  71.148  102.367 1.00 142.24 ? 130 ASP D CA    1 
ATOM   6264 C  C     . ASP D 1 130 ? 13.858  72.311  103.115 1.00 141.91 ? 130 ASP D C     1 
ATOM   6265 O  O     . ASP D 1 130 ? 13.391  72.143  104.239 1.00 142.13 ? 130 ASP D O     1 
ATOM   6266 C  CB    . ASP D 1 130 ? 15.553  70.499  103.248 1.00 143.20 ? 130 ASP D CB    1 
ATOM   6267 C  CG    . ASP D 1 130 ? 16.619  71.481  103.686 1.00 144.36 ? 130 ASP D CG    1 
ATOM   6268 O  OD1   . ASP D 1 130 ? 17.235  72.119  102.805 1.00 145.22 ? 130 ASP D OD1   1 
ATOM   6269 O  OD2   . ASP D 1 130 ? 16.841  71.616  104.909 1.00 145.06 ? 130 ASP D OD2   1 
ATOM   6270 N  N     . HIS D 1 131 ? 13.854  73.493  102.508 1.00 141.50 ? 131 HIS D N     1 
ATOM   6271 C  CA    . HIS D 1 131 ? 13.254  74.651  103.160 1.00 141.34 ? 131 HIS D CA    1 
ATOM   6272 C  C     . HIS D 1 131 ? 11.814  74.797  102.694 1.00 141.11 ? 131 HIS D C     1 
ATOM   6273 O  O     . HIS D 1 131 ? 11.154  75.802  102.969 1.00 140.98 ? 131 HIS D O     1 
ATOM   6274 C  CB    . HIS D 1 131 ? 14.033  75.929  102.839 1.00 141.52 ? 131 HIS D CB    1 
ATOM   6275 C  CG    . HIS D 1 131 ? 14.049  76.284  101.385 1.00 141.44 ? 131 HIS D CG    1 
ATOM   6276 N  ND1   . HIS D 1 131 ? 14.788  75.584  100.456 1.00 141.23 ? 131 HIS D ND1   1 
ATOM   6277 C  CD2   . HIS D 1 131 ? 13.420  77.270  100.702 1.00 141.13 ? 131 HIS D CD2   1 
ATOM   6278 C  CE1   . HIS D 1 131 ? 14.615  76.126  99.263  1.00 141.26 ? 131 HIS D CE1   1 
ATOM   6279 N  NE2   . HIS D 1 131 ? 13.789  77.150  99.385  1.00 141.09 ? 131 HIS D NE2   1 
ATOM   6280 N  N     . LYS D 1 132 ? 11.335  73.776  101.991 1.00 140.84 ? 132 LYS D N     1 
ATOM   6281 C  CA    . LYS D 1 132 ? 9.977   73.761  101.465 1.00 140.62 ? 132 LYS D CA    1 
ATOM   6282 C  C     . LYS D 1 132 ? 9.120   72.740  102.207 1.00 140.09 ? 132 LYS D C     1 
ATOM   6283 O  O     . LYS D 1 132 ? 7.913   72.921  102.359 1.00 139.78 ? 132 LYS D O     1 
ATOM   6284 C  CB    . LYS D 1 132 ? 10.003  73.398  99.983  1.00 141.27 ? 132 LYS D CB    1 
ATOM   6285 C  CG    . LYS D 1 132 ? 10.965  74.217  99.148  1.00 142.15 ? 132 LYS D CG    1 
ATOM   6286 C  CD    . LYS D 1 132 ? 11.083  73.620  97.756  1.00 143.12 ? 132 LYS D CD    1 
ATOM   6287 C  CE    . LYS D 1 132 ? 11.852  74.523  96.813  1.00 143.44 ? 132 LYS D CE    1 
ATOM   6288 N  NZ    . LYS D 1 132 ? 11.100  75.779  96.546  1.00 143.98 ? 132 LYS D NZ    1 
ATOM   6289 N  N     . ILE D 1 133 ? 9.758   71.666  102.664 1.00 139.49 ? 133 ILE D N     1 
ATOM   6290 C  CA    . ILE D 1 133 ? 9.064   70.599  103.375 1.00 138.94 ? 133 ILE D CA    1 
ATOM   6291 C  C     . ILE D 1 133 ? 8.635   70.981  104.794 1.00 138.35 ? 133 ILE D C     1 
ATOM   6292 O  O     . ILE D 1 133 ? 9.398   70.821  105.747 1.00 138.43 ? 133 ILE D O     1 
ATOM   6293 C  CB    . ILE D 1 133 ? 9.945   69.323  103.465 1.00 139.24 ? 133 ILE D CB    1 
ATOM   6294 C  CG1   . ILE D 1 133 ? 10.390  68.887  102.065 1.00 139.30 ? 133 ILE D CG1   1 
ATOM   6295 C  CG2   . ILE D 1 133 ? 9.165   68.194  104.135 1.00 139.48 ? 133 ILE D CG2   1 
ATOM   6296 C  CD1   . ILE D 1 133 ? 11.289  67.655  102.056 1.00 138.82 ? 133 ILE D CD1   1 
ATOM   6297 N  N     . ASP D 1 134 ? 7.414   71.491  104.933 1.00 137.50 ? 134 ASP D N     1 
ATOM   6298 C  CA    . ASP D 1 134 ? 6.900   71.849  106.248 1.00 136.18 ? 134 ASP D CA    1 
ATOM   6299 C  C     . ASP D 1 134 ? 6.196   70.622  106.809 1.00 134.81 ? 134 ASP D C     1 
ATOM   6300 O  O     . ASP D 1 134 ? 5.008   70.405  106.576 1.00 134.34 ? 134 ASP D O     1 
ATOM   6301 C  CB    . ASP D 1 134 ? 5.921   73.020  106.159 1.00 137.26 ? 134 ASP D CB    1 
ATOM   6302 C  CG    . ASP D 1 134 ? 5.223   73.293  107.481 1.00 138.15 ? 134 ASP D CG    1 
ATOM   6303 O  OD1   . ASP D 1 134 ? 5.881   73.149  108.536 1.00 138.51 ? 134 ASP D OD1   1 
ATOM   6304 O  OD2   . ASP D 1 134 ? 4.026   73.657  107.469 1.00 138.53 ? 134 ASP D OD2   1 
ATOM   6305 N  N     . PHE D 1 135 ? 6.953   69.819  107.543 1.00 133.33 ? 135 PHE D N     1 
ATOM   6306 C  CA    . PHE D 1 135 ? 6.441   68.594  108.132 1.00 132.15 ? 135 PHE D CA    1 
ATOM   6307 C  C     . PHE D 1 135 ? 5.570   68.886  109.351 1.00 131.62 ? 135 PHE D C     1 
ATOM   6308 O  O     . PHE D 1 135 ? 5.634   69.974  109.920 1.00 131.70 ? 135 PHE D O     1 
ATOM   6309 C  CB    . PHE D 1 135 ? 7.620   67.703  108.528 1.00 131.57 ? 135 PHE D CB    1 
ATOM   6310 C  CG    . PHE D 1 135 ? 7.252   66.272  108.756 1.00 131.57 ? 135 PHE D CG    1 
ATOM   6311 C  CD1   . PHE D 1 135 ? 6.626   65.536  107.755 1.00 131.58 ? 135 PHE D CD1   1 
ATOM   6312 C  CD2   . PHE D 1 135 ? 7.547   65.649  109.961 1.00 131.74 ? 135 PHE D CD2   1 
ATOM   6313 C  CE1   . PHE D 1 135 ? 6.301   64.198  107.952 1.00 131.82 ? 135 PHE D CE1   1 
ATOM   6314 C  CE2   . PHE D 1 135 ? 7.225   64.310  110.168 1.00 132.02 ? 135 PHE D CE2   1 
ATOM   6315 C  CZ    . PHE D 1 135 ? 6.601   63.583  109.161 1.00 131.84 ? 135 PHE D CZ    1 
ATOM   6316 N  N     . ARG D 1 136 ? 4.746   67.915  109.733 1.00 130.88 ? 136 ARG D N     1 
ATOM   6317 C  CA    . ARG D 1 136 ? 3.878   68.044  110.899 1.00 130.10 ? 136 ARG D CA    1 
ATOM   6318 C  C     . ARG D 1 136 ? 3.896   66.737  111.690 1.00 129.56 ? 136 ARG D C     1 
ATOM   6319 O  O     . ARG D 1 136 ? 4.949   66.109  111.805 1.00 129.40 ? 136 ARG D O     1 
ATOM   6320 C  CB    . ARG D 1 136 ? 2.450   68.409  110.482 1.00 130.44 ? 136 ARG D CB    1 
ATOM   6321 C  CG    . ARG D 1 136 ? 2.110   69.887  110.692 1.00 131.09 ? 136 ARG D CG    1 
ATOM   6322 C  CD    . ARG D 1 136 ? 2.884   70.793  109.739 1.00 131.90 ? 136 ARG D CD    1 
ATOM   6323 N  NE    . ARG D 1 136 ? 2.814   72.213  110.099 1.00 132.69 ? 136 ARG D NE    1 
ATOM   6324 C  CZ    . ARG D 1 136 ? 1.689   72.911  110.244 1.00 133.45 ? 136 ARG D CZ    1 
ATOM   6325 N  NH1   . ARG D 1 136 ? 0.508   72.332  110.068 1.00 133.98 ? 136 ARG D NH1   1 
ATOM   6326 N  NH2   . ARG D 1 136 ? 1.743   74.199  110.562 1.00 133.59 ? 136 ARG D NH2   1 
ATOM   6327 N  N     . GLU D 1 137 ? 2.752   66.316  112.229 1.00 128.91 ? 137 GLU D N     1 
ATOM   6328 C  CA    . GLU D 1 137 ? 2.713   65.080  113.015 1.00 128.04 ? 137 GLU D CA    1 
ATOM   6329 C  C     . GLU D 1 137 ? 1.388   64.318  113.094 1.00 127.55 ? 137 GLU D C     1 
ATOM   6330 O  O     . GLU D 1 137 ? 0.311   64.857  112.816 1.00 127.55 ? 137 GLU D O     1 
ATOM   6331 C  CB    . GLU D 1 137 ? 3.201   65.361  114.440 1.00 127.94 ? 137 GLU D CB    1 
ATOM   6332 C  CG    . GLU D 1 137 ? 4.697   65.168  114.640 1.00 127.65 ? 137 GLU D CG    1 
ATOM   6333 C  CD    . GLU D 1 137 ? 5.093   63.703  114.667 1.00 127.37 ? 137 GLU D CD    1 
ATOM   6334 O  OE1   . GLU D 1 137 ? 4.677   62.959  113.753 1.00 127.40 ? 137 GLU D OE1   1 
ATOM   6335 O  OE2   . GLU D 1 137 ? 5.823   63.297  115.598 1.00 126.60 ? 137 GLU D OE2   1 
ATOM   6336 N  N     . GLY D 1 138 ? 1.505   63.049  113.482 1.00 126.72 ? 138 GLY D N     1 
ATOM   6337 C  CA    . GLY D 1 138 ? 0.365   62.159  113.639 1.00 125.85 ? 138 GLY D CA    1 
ATOM   6338 C  C     . GLY D 1 138 ? -0.829  62.344  112.722 1.00 125.15 ? 138 GLY D C     1 
ATOM   6339 O  O     . GLY D 1 138 ? -0.672  62.586  111.527 1.00 124.84 ? 138 GLY D O     1 
ATOM   6340 N  N     . PRO D 1 139 ? -2.051  62.216  113.265 1.00 124.76 ? 139 PRO D N     1 
ATOM   6341 C  CA    . PRO D 1 139 ? -3.286  62.368  112.496 1.00 124.16 ? 139 PRO D CA    1 
ATOM   6342 C  C     . PRO D 1 139 ? -3.190  63.487  111.475 1.00 123.71 ? 139 PRO D C     1 
ATOM   6343 O  O     . PRO D 1 139 ? -2.625  64.546  111.748 1.00 123.39 ? 139 PRO D O     1 
ATOM   6344 C  CB    . PRO D 1 139 ? -4.321  62.642  113.577 1.00 124.33 ? 139 PRO D CB    1 
ATOM   6345 C  CG    . PRO D 1 139 ? -3.855  61.740  114.678 1.00 124.71 ? 139 PRO D CG    1 
ATOM   6346 C  CD    . PRO D 1 139 ? -2.352  61.986  114.692 1.00 124.87 ? 139 PRO D CD    1 
ATOM   6347 N  N     . ALA D 1 140 ? -3.743  63.233  110.294 1.00 123.38 ? 140 ALA D N     1 
ATOM   6348 C  CA    . ALA D 1 140 ? -3.715  64.197  109.205 1.00 123.04 ? 140 ALA D CA    1 
ATOM   6349 C  C     . ALA D 1 140 ? -5.071  64.845  108.985 1.00 122.66 ? 140 ALA D C     1 
ATOM   6350 O  O     . ALA D 1 140 ? -5.152  66.022  108.635 1.00 122.47 ? 140 ALA D O     1 
ATOM   6351 C  CB    . ALA D 1 140 ? -3.255  63.514  107.923 1.00 123.18 ? 140 ALA D CB    1 
ATOM   6352 N  N     . LEU D 1 141 ? -6.136  64.076  109.186 1.00 122.43 ? 141 LEU D N     1 
ATOM   6353 C  CA    . LEU D 1 141 ? -7.475  64.605  108.989 1.00 122.57 ? 141 LEU D CA    1 
ATOM   6354 C  C     . LEU D 1 141 ? -7.695  65.840  109.861 1.00 123.54 ? 141 LEU D C     1 
ATOM   6355 O  O     . LEU D 1 141 ? -8.150  66.874  109.371 1.00 123.92 ? 141 LEU D O     1 
ATOM   6356 C  CB    . LEU D 1 141 ? -8.526  63.538  109.305 1.00 121.56 ? 141 LEU D CB    1 
ATOM   6357 C  CG    . LEU D 1 141 ? -9.915  63.763  108.698 1.00 121.26 ? 141 LEU D CG    1 
ATOM   6358 C  CD1   . LEU D 1 141 ? -10.803 62.574  109.022 1.00 121.49 ? 141 LEU D CD1   1 
ATOM   6359 C  CD2   . LEU D 1 141 ? -10.526 65.047  109.225 1.00 121.03 ? 141 LEU D CD2   1 
ATOM   6360 N  N     . PRO D 1 142 ? -7.378  65.750  111.167 1.00 124.17 ? 142 PRO D N     1 
ATOM   6361 C  CA    . PRO D 1 142 ? -7.560  66.895  112.067 1.00 124.14 ? 142 PRO D CA    1 
ATOM   6362 C  C     . PRO D 1 142 ? -6.691  68.095  111.693 1.00 124.25 ? 142 PRO D C     1 
ATOM   6363 O  O     . PRO D 1 142 ? -7.160  69.231  111.695 1.00 124.03 ? 142 PRO D O     1 
ATOM   6364 C  CB    . PRO D 1 142 ? -7.194  66.319  113.431 1.00 124.33 ? 142 PRO D CB    1 
ATOM   6365 C  CG    . PRO D 1 142 ? -7.608  64.884  113.304 1.00 124.37 ? 142 PRO D CG    1 
ATOM   6366 C  CD    . PRO D 1 142 ? -7.062  64.536  111.941 1.00 124.54 ? 142 PRO D CD    1 
ATOM   6367 N  N     . VAL D 1 143 ? -5.424  67.837  111.377 1.00 124.70 ? 143 VAL D N     1 
ATOM   6368 C  CA    . VAL D 1 143 ? -4.499  68.903  110.996 1.00 125.24 ? 143 VAL D CA    1 
ATOM   6369 C  C     . VAL D 1 143 ? -4.962  69.543  109.696 1.00 125.54 ? 143 VAL D C     1 
ATOM   6370 O  O     . VAL D 1 143 ? -4.461  70.592  109.293 1.00 125.40 ? 143 VAL D O     1 
ATOM   6371 C  CB    . VAL D 1 143 ? -3.062  68.366  110.778 1.00 125.31 ? 143 VAL D CB    1 
ATOM   6372 C  CG1   . VAL D 1 143 ? -2.099  69.528  110.548 1.00 124.41 ? 143 VAL D CG1   1 
ATOM   6373 C  CG2   . VAL D 1 143 ? -2.626  67.526  111.974 1.00 125.14 ? 143 VAL D CG2   1 
ATOM   6374 N  N     . LEU D 1 144 ? -5.923  68.899  109.044 1.00 126.29 ? 144 LEU D N     1 
ATOM   6375 C  CA    . LEU D 1 144 ? -6.459  69.388  107.783 1.00 127.36 ? 144 LEU D CA    1 
ATOM   6376 C  C     . LEU D 1 144 ? -7.680  70.269  108.036 1.00 128.23 ? 144 LEU D C     1 
ATOM   6377 O  O     . LEU D 1 144 ? -8.124  70.995  107.149 1.00 128.55 ? 144 LEU D O     1 
ATOM   6378 C  CB    . LEU D 1 144 ? -6.835  68.201  106.888 1.00 127.08 ? 144 LEU D CB    1 
ATOM   6379 C  CG    . LEU D 1 144 ? -7.008  68.424  105.383 1.00 126.73 ? 144 LEU D CG    1 
ATOM   6380 C  CD1   . LEU D 1 144 ? -5.691  68.876  104.767 1.00 126.11 ? 144 LEU D CD1   1 
ATOM   6381 C  CD2   . LEU D 1 144 ? -7.471  67.130  104.733 1.00 126.29 ? 144 LEU D CD2   1 
ATOM   6382 N  N     . ASP D 1 145 ? -8.215  70.206  109.252 1.00 129.51 ? 145 ASP D N     1 
ATOM   6383 C  CA    . ASP D 1 145 ? -9.385  70.999  109.623 1.00 130.60 ? 145 ASP D CA    1 
ATOM   6384 C  C     . ASP D 1 145 ? -8.999  72.403  110.073 1.00 131.75 ? 145 ASP D C     1 
ATOM   6385 O  O     . ASP D 1 145 ? -9.862  73.227  110.376 1.00 131.55 ? 145 ASP D O     1 
ATOM   6386 C  CB    . ASP D 1 145 ? -10.168 70.301  110.736 1.00 129.78 ? 145 ASP D CB    1 
ATOM   6387 C  CG    . ASP D 1 145 ? -10.832 69.022  110.266 1.00 129.15 ? 145 ASP D CG    1 
ATOM   6388 O  OD1   . ASP D 1 145 ? -11.661 69.093  109.336 1.00 128.75 ? 145 ASP D OD1   1 
ATOM   6389 O  OD2   . ASP D 1 145 ? -10.527 67.949  110.825 1.00 128.64 ? 145 ASP D OD2   1 
ATOM   6390 N  N     . GLU D 1 146 ? -7.698  72.666  110.120 1.00 133.50 ? 146 GLU D N     1 
ATOM   6391 C  CA    . GLU D 1 146 ? -7.195  73.974  110.520 1.00 135.24 ? 146 GLU D CA    1 
ATOM   6392 C  C     . GLU D 1 146 ? -7.559  74.962  109.422 1.00 136.14 ? 146 GLU D C     1 
ATOM   6393 O  O     . GLU D 1 146 ? -8.134  76.024  109.672 1.00 136.46 ? 146 GLU D O     1 
ATOM   6394 C  CB    . GLU D 1 146 ? -5.668  73.931  110.678 1.00 135.78 ? 146 GLU D CB    1 
ATOM   6395 C  CG    . GLU D 1 146 ? -4.909  73.632  109.379 1.00 136.21 ? 146 GLU D CG    1 
ATOM   6396 C  CD    . GLU D 1 146 ? -3.396  73.679  109.540 1.00 136.84 ? 146 GLU D CD    1 
ATOM   6397 O  OE1   . GLU D 1 146 ? -2.846  72.839  110.287 1.00 137.07 ? 146 GLU D OE1   1 
ATOM   6398 O  OE2   . GLU D 1 146 ? -2.757  74.556  108.918 1.00 136.40 ? 146 GLU D OE2   1 
ATOM   6399 N  N     . MET D 1 147 ? -7.220  74.576  108.198 1.00 136.85 ? 147 MET D N     1 
ATOM   6400 C  CA    . MET D 1 147 ? -7.462  75.379  107.013 1.00 137.59 ? 147 MET D CA    1 
ATOM   6401 C  C     . MET D 1 147 ? -8.947  75.452  106.671 1.00 138.00 ? 147 MET D C     1 
ATOM   6402 O  O     . MET D 1 147 ? -9.427  76.481  106.202 1.00 138.14 ? 147 MET D O     1 
ATOM   6403 C  CB    . MET D 1 147 ? -6.682  74.777  105.844 1.00 137.87 ? 147 MET D CB    1 
ATOM   6404 C  CG    . MET D 1 147 ? -5.211  74.527  106.161 1.00 137.79 ? 147 MET D CG    1 
ATOM   6405 S  SD    . MET D 1 147 ? -4.484  73.186  105.187 1.00 137.48 ? 147 MET D SD    1 
ATOM   6406 C  CE    . MET D 1 147 ? -4.634  71.824  106.327 1.00 136.76 ? 147 MET D CE    1 
ATOM   6407 N  N     . ILE D 1 148 ? -9.669  74.359  106.908 1.00 138.52 ? 148 ILE D N     1 
ATOM   6408 C  CA    . ILE D 1 148 ? -11.100 74.309  106.618 1.00 139.28 ? 148 ILE D CA    1 
ATOM   6409 C  C     . ILE D 1 148 ? -11.817 75.480  107.283 1.00 140.44 ? 148 ILE D C     1 
ATOM   6410 O  O     . ILE D 1 148 ? -12.910 75.870  106.868 1.00 140.96 ? 148 ILE D O     1 
ATOM   6411 C  CB    . ILE D 1 148 ? -11.743 73.005  107.141 1.00 138.86 ? 148 ILE D CB    1 
ATOM   6412 C  CG1   . ILE D 1 148 ? -10.932 71.792  106.688 1.00 138.49 ? 148 ILE D CG1   1 
ATOM   6413 C  CG2   . ILE D 1 148 ? -13.170 72.889  106.622 1.00 138.49 ? 148 ILE D CG2   1 
ATOM   6414 C  CD1   . ILE D 1 148 ? -10.894 71.600  105.192 1.00 138.75 ? 148 ILE D CD1   1 
ATOM   6415 N  N     . LYS D 1 149 ? -11.190 76.035  108.315 1.00 141.56 ? 149 LYS D N     1 
ATOM   6416 C  CA    . LYS D 1 149 ? -11.755 77.154  109.062 1.00 142.48 ? 149 LYS D CA    1 
ATOM   6417 C  C     . LYS D 1 149 ? -11.611 78.484  108.326 1.00 143.07 ? 149 LYS D C     1 
ATOM   6418 O  O     . LYS D 1 149 ? -12.604 79.047  107.861 1.00 143.27 ? 149 LYS D O     1 
ATOM   6419 C  CB    . LYS D 1 149 ? -11.090 77.229  110.437 1.00 142.05 ? 149 LYS D CB    1 
ATOM   6420 C  CG    . LYS D 1 149 ? -11.267 75.951  111.241 1.00 141.46 ? 149 LYS D CG    1 
ATOM   6421 C  CD    . LYS D 1 149 ? -10.286 75.855  112.394 1.00 140.78 ? 149 LYS D CD    1 
ATOM   6422 C  CE    . LYS D 1 149 ? -10.407 74.508  113.088 1.00 139.99 ? 149 LYS D CE    1 
ATOM   6423 N  NZ    . LYS D 1 149 ? -9.354  74.315  114.121 1.00 139.52 ? 149 LYS D NZ    1 
ATOM   6424 N  N     . ASP D 1 150 ? -10.380 78.983  108.220 1.00 143.88 ? 150 ASP D N     1 
ATOM   6425 C  CA    . ASP D 1 150 ? -10.125 80.249  107.534 1.00 144.80 ? 150 ASP D CA    1 
ATOM   6426 C  C     . ASP D 1 150 ? -10.861 80.329  106.202 1.00 145.33 ? 150 ASP D C     1 
ATOM   6427 O  O     . ASP D 1 150 ? -10.497 79.647  105.244 1.00 144.66 ? 150 ASP D O     1 
ATOM   6428 C  CB    . ASP D 1 150 ? -8.626  80.429  107.285 1.00 144.86 ? 150 ASP D CB    1 
ATOM   6429 C  CG    . ASP D 1 150 ? -7.843  80.632  108.564 1.00 145.79 ? 150 ASP D CG    1 
ATOM   6430 O  OD1   . ASP D 1 150 ? -8.133  81.609  109.289 1.00 145.75 ? 150 ASP D OD1   1 
ATOM   6431 O  OD2   . ASP D 1 150 ? -6.935  79.818  108.842 1.00 145.86 ? 150 ASP D OD2   1 
ATOM   6432 N  N     . GLU D 1 151 ? -11.896 81.164  106.146 1.00 146.74 ? 151 GLU D N     1 
ATOM   6433 C  CA    . GLU D 1 151 ? -12.676 81.335  104.923 1.00 147.31 ? 151 GLU D CA    1 
ATOM   6434 C  C     . GLU D 1 151 ? -11.724 81.612  103.760 1.00 147.06 ? 151 GLU D C     1 
ATOM   6435 O  O     . GLU D 1 151 ? -12.045 81.341  102.602 1.00 146.74 ? 151 GLU D O     1 
ATOM   6436 C  CB    . GLU D 1 151 ? -13.673 82.494  105.071 1.00 148.34 ? 151 GLU D CB    1 
ATOM   6437 N  N     . LYS D 1 152 ? -10.555 82.162  104.086 1.00 146.32 ? 152 LYS D N     1 
ATOM   6438 C  CA    . LYS D 1 152 ? -9.526  82.459  103.095 1.00 145.13 ? 152 LYS D CA    1 
ATOM   6439 C  C     . LYS D 1 152 ? -8.292  81.614  103.391 1.00 144.53 ? 152 LYS D C     1 
ATOM   6440 O  O     . LYS D 1 152 ? -7.419  81.991  104.178 1.00 144.40 ? 152 LYS D O     1 
ATOM   6441 C  CB    . LYS D 1 152 ? -9.168  83.951  103.101 1.00 144.35 ? 152 LYS D CB    1 
ATOM   6442 C  CG    . LYS D 1 152 ? -9.740  84.728  101.911 1.00 143.25 ? 152 LYS D CG    1 
ATOM   6443 C  CD    . LYS D 1 152 ? -9.243  84.143  100.587 1.00 141.68 ? 152 LYS D CD    1 
ATOM   6444 C  CE    . LYS D 1 152 ? -9.845  84.845  99.379  1.00 139.96 ? 152 LYS D CE    1 
ATOM   6445 N  NZ    . LYS D 1 152 ? -9.389  84.222  98.103  1.00 138.20 ? 152 LYS D NZ    1 
ATOM   6446 N  N     . ASN D 1 153 ? -8.251  80.456  102.745 1.00 143.88 ? 153 ASN D N     1 
ATOM   6447 C  CA    . ASN D 1 153 ? -7.178  79.484  102.887 1.00 143.13 ? 153 ASN D CA    1 
ATOM   6448 C  C     . ASN D 1 153 ? -7.687  78.314  102.057 1.00 142.45 ? 153 ASN D C     1 
ATOM   6449 O  O     . ASN D 1 153 ? -7.020  77.292  101.902 1.00 142.36 ? 153 ASN D O     1 
ATOM   6450 C  CB    . ASN D 1 153 ? -7.034  79.076  104.358 1.00 142.50 ? 153 ASN D CB    1 
ATOM   6451 C  CG    . ASN D 1 153 ? -5.814  78.213  104.613 1.00 141.92 ? 153 ASN D CG    1 
ATOM   6452 O  OD1   . ASN D 1 153 ? -5.578  77.776  105.741 1.00 140.89 ? 153 ASN D OD1   1 
ATOM   6453 N  ND2   . ASN D 1 153 ? -5.031  77.964  103.569 1.00 141.99 ? 153 ASN D ND2   1 
ATOM   6454 N  N     . HIS D 1 154 ? -8.892  78.500  101.526 1.00 141.97 ? 154 HIS D N     1 
ATOM   6455 C  CA    . HIS D 1 154 ? -9.565  77.508  100.701 1.00 141.79 ? 154 HIS D CA    1 
ATOM   6456 C  C     . HIS D 1 154 ? -9.025  77.470  99.278  1.00 141.44 ? 154 HIS D C     1 
ATOM   6457 O  O     . HIS D 1 154 ? -9.621  78.053  98.374  1.00 141.30 ? 154 HIS D O     1 
ATOM   6458 C  CB    . HIS D 1 154 ? -11.070 77.802  100.638 1.00 142.24 ? 154 HIS D CB    1 
ATOM   6459 C  CG    . HIS D 1 154 ? -11.808 77.507  101.908 1.00 142.94 ? 154 HIS D CG    1 
ATOM   6460 N  ND1   . HIS D 1 154 ? -13.166 77.710  102.039 1.00 143.07 ? 154 HIS D ND1   1 
ATOM   6461 C  CD2   . HIS D 1 154 ? -11.387 77.011  103.096 1.00 143.06 ? 154 HIS D CD2   1 
ATOM   6462 C  CE1   . HIS D 1 154 ? -13.549 77.351  103.251 1.00 143.14 ? 154 HIS D CE1   1 
ATOM   6463 N  NE2   . HIS D 1 154 ? -12.489 76.922  103.912 1.00 143.23 ? 154 HIS D NE2   1 
ATOM   6464 N  N     . GLY D 1 155 ? -7.903  76.785  99.075  1.00 141.03 ? 155 GLY D N     1 
ATOM   6465 C  CA    . GLY D 1 155 ? -7.345  76.691  97.738  1.00 140.30 ? 155 GLY D CA    1 
ATOM   6466 C  C     . GLY D 1 155 ? -5.893  77.096  97.588  1.00 139.88 ? 155 GLY D C     1 
ATOM   6467 O  O     . GLY D 1 155 ? -5.362  77.076  96.481  1.00 139.79 ? 155 GLY D O     1 
ATOM   6468 N  N     . SER D 1 156 ? -5.244  77.457  98.691  1.00 139.83 ? 156 SER D N     1 
ATOM   6469 C  CA    . SER D 1 156 ? -3.845  77.874  98.647  1.00 139.66 ? 156 SER D CA    1 
ATOM   6470 C  C     . SER D 1 156 ? -2.942  76.744  98.163  1.00 139.22 ? 156 SER D C     1 
ATOM   6471 O  O     . SER D 1 156 ? -1.716  76.829  98.253  1.00 139.07 ? 156 SER D O     1 
ATOM   6472 C  CB    . SER D 1 156 ? -3.383  78.358  100.031 1.00 139.82 ? 156 SER D CB    1 
ATOM   6473 O  OG    . SER D 1 156 ? -3.542  77.355  101.021 1.00 139.75 ? 156 SER D OG    1 
ATOM   6474 N  N     . TYR D 1 157 ? -3.556  75.688  97.640  1.00 138.72 ? 157 TYR D N     1 
ATOM   6475 C  CA    . TYR D 1 157 ? -2.803  74.544  97.150  1.00 138.38 ? 157 TYR D CA    1 
ATOM   6476 C  C     . TYR D 1 157 ? -3.073  74.239  95.677  1.00 137.50 ? 157 TYR D C     1 
ATOM   6477 O  O     . TYR D 1 157 ? -4.217  74.272  95.219  1.00 136.86 ? 157 TYR D O     1 
ATOM   6478 C  CB    . TYR D 1 157 ? -3.102  73.313  98.017  1.00 138.90 ? 157 TYR D CB    1 
ATOM   6479 C  CG    . TYR D 1 157 ? -2.658  73.477  99.457  1.00 139.11 ? 157 TYR D CG    1 
ATOM   6480 C  CD1   . TYR D 1 157 ? -3.354  74.311  100.336 1.00 139.10 ? 157 TYR D CD1   1 
ATOM   6481 C  CD2   . TYR D 1 157 ? -1.505  72.847  99.925  1.00 139.21 ? 157 TYR D CD2   1 
ATOM   6482 C  CE1   . TYR D 1 157 ? -2.909  74.516  101.643 1.00 138.93 ? 157 TYR D CE1   1 
ATOM   6483 C  CE2   . TYR D 1 157 ? -1.052  73.048  101.229 1.00 139.06 ? 157 TYR D CE2   1 
ATOM   6484 C  CZ    . TYR D 1 157 ? -1.756  73.883  102.078 1.00 138.85 ? 157 TYR D CZ    1 
ATOM   6485 O  OH    . TYR D 1 157 ? -1.297  74.094  103.355 1.00 138.69 ? 157 TYR D OH    1 
ATOM   6486 N  N     . ASP D 1 158 ? -2.000  73.953  94.942  1.00 136.70 ? 158 ASP D N     1 
ATOM   6487 C  CA    . ASP D 1 158 ? -2.086  73.636  93.519  1.00 135.55 ? 158 ASP D CA    1 
ATOM   6488 C  C     . ASP D 1 158 ? -1.971  72.129  93.305  1.00 134.40 ? 158 ASP D C     1 
ATOM   6489 O  O     . ASP D 1 158 ? -2.633  71.562  92.437  1.00 134.03 ? 158 ASP D O     1 
ATOM   6490 C  CB    . ASP D 1 158 ? -0.956  74.326  92.742  1.00 135.81 ? 158 ASP D CB    1 
ATOM   6491 C  CG    . ASP D 1 158 ? -0.863  75.810  93.031  1.00 136.03 ? 158 ASP D CG    1 
ATOM   6492 O  OD1   . ASP D 1 158 ? -1.893  76.504  92.905  1.00 136.39 ? 158 ASP D OD1   1 
ATOM   6493 O  OD2   . ASP D 1 158 ? 0.243   76.282  93.376  1.00 135.94 ? 158 ASP D OD2   1 
ATOM   6494 N  N     . PHE D 1 159 ? -1.119  71.494  94.105  1.00 133.16 ? 159 PHE D N     1 
ATOM   6495 C  CA    . PHE D 1 159 ? -0.872  70.058  94.014  1.00 132.01 ? 159 PHE D CA    1 
ATOM   6496 C  C     . PHE D 1 159 ? -0.923  69.388  95.392  1.00 131.11 ? 159 PHE D C     1 
ATOM   6497 O  O     . PHE D 1 159 ? -0.163  69.749  96.292  1.00 130.92 ? 159 PHE D O     1 
ATOM   6498 C  CB    . PHE D 1 159 ? 0.503   69.833  93.368  1.00 131.96 ? 159 PHE D CB    1 
ATOM   6499 C  CG    . PHE D 1 159 ? 0.956   68.397  93.353  1.00 131.72 ? 159 PHE D CG    1 
ATOM   6500 C  CD1   . PHE D 1 159 ? 0.317   67.454  92.560  1.00 131.35 ? 159 PHE D CD1   1 
ATOM   6501 C  CD2   . PHE D 1 159 ? 2.041   67.993  94.126  1.00 131.71 ? 159 PHE D CD2   1 
ATOM   6502 C  CE1   . PHE D 1 159 ? 0.748   66.131  92.533  1.00 131.64 ? 159 PHE D CE1   1 
ATOM   6503 C  CE2   . PHE D 1 159 ? 2.483   66.672  94.108  1.00 131.56 ? 159 PHE D CE2   1 
ATOM   6504 C  CZ    . PHE D 1 159 ? 1.834   65.739  93.309  1.00 131.64 ? 159 PHE D CZ    1 
ATOM   6505 N  N     . ILE D 1 160 ? -1.830  68.423  95.550  1.00 129.88 ? 160 ILE D N     1 
ATOM   6506 C  CA    . ILE D 1 160 ? -1.972  67.678  96.805  1.00 128.16 ? 160 ILE D CA    1 
ATOM   6507 C  C     . ILE D 1 160 ? -1.964  66.176  96.520  1.00 126.83 ? 160 ILE D C     1 
ATOM   6508 O  O     . ILE D 1 160 ? -2.777  65.671  95.742  1.00 126.32 ? 160 ILE D O     1 
ATOM   6509 C  CB    . ILE D 1 160 ? -3.278  68.045  97.555  1.00 128.27 ? 160 ILE D CB    1 
ATOM   6510 C  CG1   . ILE D 1 160 ? -3.209  69.494  98.044  1.00 128.46 ? 160 ILE D CG1   1 
ATOM   6511 C  CG2   . ILE D 1 160 ? -3.476  67.115  98.742  1.00 128.07 ? 160 ILE D CG2   1 
ATOM   6512 C  CD1   . ILE D 1 160 ? -4.413  69.931  98.856  1.00 128.55 ? 160 ILE D CD1   1 
ATOM   6513 N  N     . PHE D 1 161 ? -1.037  65.473  97.164  1.00 125.37 ? 161 PHE D N     1 
ATOM   6514 C  CA    . PHE D 1 161 ? -0.873  64.035  96.980  1.00 124.17 ? 161 PHE D CA    1 
ATOM   6515 C  C     . PHE D 1 161 ? -1.357  63.228  98.187  1.00 123.67 ? 161 PHE D C     1 
ATOM   6516 O  O     . PHE D 1 161 ? -0.684  63.155  99.214  1.00 123.59 ? 161 PHE D O     1 
ATOM   6517 C  CB    . PHE D 1 161 ? 0.608   63.737  96.700  1.00 123.42 ? 161 PHE D CB    1 
ATOM   6518 C  CG    . PHE D 1 161 ? 0.889   62.317  96.284  1.00 122.45 ? 161 PHE D CG    1 
ATOM   6519 C  CD1   . PHE D 1 161 ? 0.174   61.722  95.245  1.00 121.83 ? 161 PHE D CD1   1 
ATOM   6520 C  CD2   . PHE D 1 161 ? 1.901   61.588  96.906  1.00 121.83 ? 161 PHE D CD2   1 
ATOM   6521 C  CE1   . PHE D 1 161 ? 0.465   60.422  94.832  1.00 121.71 ? 161 PHE D CE1   1 
ATOM   6522 C  CE2   . PHE D 1 161 ? 2.200   60.288  96.501  1.00 121.51 ? 161 PHE D CE2   1 
ATOM   6523 C  CZ    . PHE D 1 161 ? 1.481   59.704  95.462  1.00 121.60 ? 161 PHE D CZ    1 
ATOM   6524 N  N     . VAL D 1 162 ? -2.532  62.623  98.053  1.00 123.10 ? 162 VAL D N     1 
ATOM   6525 C  CA    . VAL D 1 162 ? -3.106  61.809  99.116  1.00 122.28 ? 162 VAL D CA    1 
ATOM   6526 C  C     . VAL D 1 162 ? -2.527  60.404  99.028  1.00 122.23 ? 162 VAL D C     1 
ATOM   6527 O  O     . VAL D 1 162 ? -2.897  59.632  98.150  1.00 121.88 ? 162 VAL D O     1 
ATOM   6528 C  CB    . VAL D 1 162 ? -4.636  61.711  98.974  1.00 121.72 ? 162 VAL D CB    1 
ATOM   6529 C  CG1   . VAL D 1 162 ? -5.198  60.793  100.033 1.00 121.51 ? 162 VAL D CG1   1 
ATOM   6530 C  CG2   . VAL D 1 162 ? -5.256  63.085  99.084  1.00 121.62 ? 162 VAL D CG2   1 
ATOM   6531 N  N     . ASP D 1 163 ? -1.613  60.072  99.931  1.00 122.73 ? 163 ASP D N     1 
ATOM   6532 C  CA    . ASP D 1 163 ? -1.007  58.748  99.917  1.00 123.98 ? 163 ASP D CA    1 
ATOM   6533 C  C     . ASP D 1 163 ? -0.556  58.342  101.314 1.00 124.58 ? 163 ASP D C     1 
ATOM   6534 O  O     . ASP D 1 163 ? 0.570   58.622  101.726 1.00 124.43 ? 163 ASP D O     1 
ATOM   6535 C  CB    . ASP D 1 163 ? 0.176   58.721  98.939  1.00 124.28 ? 163 ASP D CB    1 
ATOM   6536 C  CG    . ASP D 1 163 ? 0.702   57.315  98.684  1.00 124.24 ? 163 ASP D CG    1 
ATOM   6537 O  OD1   . ASP D 1 163 ? -0.116  56.377  98.561  1.00 124.86 ? 163 ASP D OD1   1 
ATOM   6538 O  OD2   . ASP D 1 163 ? 1.935   57.150  98.585  1.00 123.28 ? 163 ASP D OD2   1 
ATOM   6539 N  N     . ALA D 1 164 ? -1.455  57.675  102.033 1.00 125.61 ? 164 ALA D N     1 
ATOM   6540 C  CA    . ALA D 1 164 ? -1.194  57.216  103.392 1.00 126.46 ? 164 ALA D CA    1 
ATOM   6541 C  C     . ALA D 1 164 ? -2.108  56.036  103.700 1.00 127.03 ? 164 ALA D C     1 
ATOM   6542 O  O     . ALA D 1 164 ? -1.864  54.919  103.244 1.00 126.93 ? 164 ALA D O     1 
ATOM   6543 C  CB    . ALA D 1 164 ? -1.447  58.347  104.369 1.00 126.75 ? 164 ALA D CB    1 
ATOM   6544 N  N     . ASP D 1 165 ? -3.159  56.281  104.480 1.00 127.82 ? 165 ASP D N     1 
ATOM   6545 C  CA    . ASP D 1 165 ? -4.113  55.227  104.810 1.00 128.55 ? 165 ASP D CA    1 
ATOM   6546 C  C     . ASP D 1 165 ? -4.918  55.008  103.536 1.00 128.65 ? 165 ASP D C     1 
ATOM   6547 O  O     . ASP D 1 165 ? -4.411  55.256  102.443 1.00 129.35 ? 165 ASP D O     1 
ATOM   6548 C  CB    . ASP D 1 165 ? -5.033  55.664  105.958 1.00 128.79 ? 165 ASP D CB    1 
ATOM   6549 C  CG    . ASP D 1 165 ? -5.959  56.805  105.571 1.00 129.39 ? 165 ASP D CG    1 
ATOM   6550 O  OD1   . ASP D 1 165 ? -6.808  56.617  104.674 1.00 129.06 ? 165 ASP D OD1   1 
ATOM   6551 O  OD2   . ASP D 1 165 ? -5.842  57.893  106.171 1.00 130.03 ? 165 ASP D OD2   1 
ATOM   6552 N  N     . LYS D 1 166 ? -6.155  54.540  103.658 1.00 128.15 ? 166 LYS D N     1 
ATOM   6553 C  CA    . LYS D 1 166 ? -6.983  54.330  102.477 1.00 127.83 ? 166 LYS D CA    1 
ATOM   6554 C  C     . LYS D 1 166 ? -8.464  54.595  102.739 1.00 127.30 ? 166 LYS D C     1 
ATOM   6555 O  O     . LYS D 1 166 ? -9.176  55.101  101.871 1.00 127.32 ? 166 LYS D O     1 
ATOM   6556 C  CB    . LYS D 1 166 ? -6.803  52.905  101.927 1.00 128.69 ? 166 LYS D CB    1 
ATOM   6557 C  CG    . LYS D 1 166 ? -5.525  52.656  101.104 1.00 128.90 ? 166 LYS D CG    1 
ATOM   6558 C  CD    . LYS D 1 166 ? -4.305  52.357  101.973 1.00 128.91 ? 166 LYS D CD    1 
ATOM   6559 C  CE    . LYS D 1 166 ? -3.069  52.055  101.124 1.00 128.72 ? 166 LYS D CE    1 
ATOM   6560 N  NZ    . LYS D 1 166 ? -2.622  53.208  100.284 1.00 127.95 ? 166 LYS D NZ    1 
ATOM   6561 N  N     . ASP D 1 167 ? -8.928  54.259  103.936 1.00 126.51 ? 167 ASP D N     1 
ATOM   6562 C  CA    . ASP D 1 167 ? -10.328 54.462  104.291 1.00 125.32 ? 167 ASP D CA    1 
ATOM   6563 C  C     . ASP D 1 167 ? -10.725 55.934  104.418 1.00 124.77 ? 167 ASP D C     1 
ATOM   6564 O  O     . ASP D 1 167 ? -11.840 56.309  104.056 1.00 124.88 ? 167 ASP D O     1 
ATOM   6565 C  CB    . ASP D 1 167 ? -10.630 53.726  105.588 1.00 124.04 ? 167 ASP D CB    1 
ATOM   6566 C  CG    . ASP D 1 167 ? -9.423  53.625  106.473 1.00 123.13 ? 167 ASP D CG    1 
ATOM   6567 O  OD1   . ASP D 1 167 ? -8.851  54.682  106.808 1.00 122.16 ? 167 ASP D OD1   1 
ATOM   6568 O  OD2   . ASP D 1 167 ? -9.040  52.491  106.822 1.00 122.89 ? 167 ASP D OD2   1 
ATOM   6569 N  N     . ASN D 1 168 ? -9.825  56.769  104.927 1.00 123.93 ? 168 ASN D N     1 
ATOM   6570 C  CA    . ASN D 1 168 ? -10.132 58.189  105.070 1.00 122.97 ? 168 ASN D CA    1 
ATOM   6571 C  C     . ASN D 1 168 ? -10.033 58.942  103.747 1.00 122.05 ? 168 ASN D C     1 
ATOM   6572 O  O     . ASN D 1 168 ? -10.228 60.155  103.708 1.00 121.78 ? 168 ASN D O     1 
ATOM   6573 C  CB    . ASN D 1 168 ? -9.211  58.850  106.102 1.00 123.00 ? 168 ASN D CB    1 
ATOM   6574 C  CG    . ASN D 1 168 ? -9.584  58.502  107.532 1.00 122.74 ? 168 ASN D CG    1 
ATOM   6575 O  OD1   . ASN D 1 168 ? -10.727 58.688  107.953 1.00 121.91 ? 168 ASN D OD1   1 
ATOM   6576 N  ND2   . ASN D 1 168 ? -8.615  58.002  108.288 1.00 122.60 ? 168 ASN D ND2   1 
ATOM   6577 N  N     . TYR D 1 169 ? -9.731  58.222  102.669 1.00 121.40 ? 169 TYR D N     1 
ATOM   6578 C  CA    . TYR D 1 169 ? -9.616  58.830  101.343 1.00 120.64 ? 169 TYR D CA    1 
ATOM   6579 C  C     . TYR D 1 169 ? -10.917 59.495  100.932 1.00 120.01 ? 169 TYR D C     1 
ATOM   6580 O  O     . TYR D 1 169 ? -10.935 60.666  100.552 1.00 119.59 ? 169 TYR D O     1 
ATOM   6581 C  CB    . TYR D 1 169 ? -9.245  57.775  100.296 1.00 120.63 ? 169 TYR D CB    1 
ATOM   6582 C  CG    . TYR D 1 169 ? -7.762  57.533  100.156 1.00 120.38 ? 169 TYR D CG    1 
ATOM   6583 C  CD1   . TYR D 1 169 ? -6.925  57.563  101.268 1.00 120.42 ? 169 TYR D CD1   1 
ATOM   6584 C  CD2   . TYR D 1 169 ? -7.200  57.239  98.917  1.00 120.49 ? 169 TYR D CD2   1 
ATOM   6585 C  CE1   . TYR D 1 169 ? -5.568  57.308  101.154 1.00 120.29 ? 169 TYR D CE1   1 
ATOM   6586 C  CE2   . TYR D 1 169 ? -5.838  56.976  98.792  1.00 120.79 ? 169 TYR D CE2   1 
ATOM   6587 C  CZ    . TYR D 1 169 ? -5.029  57.012  99.918  1.00 120.50 ? 169 TYR D CZ    1 
ATOM   6588 O  OH    . TYR D 1 169 ? -3.683  56.740  99.817  1.00 120.78 ? 169 TYR D OH    1 
ATOM   6589 N  N     . LEU D 1 170 ? -12.005 58.737  101.000 1.00 119.36 ? 170 LEU D N     1 
ATOM   6590 C  CA    . LEU D 1 170 ? -13.305 59.266  100.636 1.00 118.85 ? 170 LEU D CA    1 
ATOM   6591 C  C     . LEU D 1 170 ? -13.610 60.446  101.562 1.00 119.12 ? 170 LEU D C     1 
ATOM   6592 O  O     . LEU D 1 170 ? -14.395 61.332  101.214 1.00 119.33 ? 170 LEU D O     1 
ATOM   6593 C  CB    . LEU D 1 170 ? -14.368 58.175  100.775 1.00 118.41 ? 170 LEU D CB    1 
ATOM   6594 C  CG    . LEU D 1 170 ? -15.548 58.250  99.801  1.00 118.46 ? 170 LEU D CG    1 
ATOM   6595 C  CD1   . LEU D 1 170 ? -16.444 57.036  99.994  1.00 118.20 ? 170 LEU D CD1   1 
ATOM   6596 C  CD2   . LEU D 1 170 ? -16.330 59.541  100.015 1.00 118.26 ? 170 LEU D CD2   1 
ATOM   6597 N  N     . ASN D 1 171 ? -12.972 60.457  102.736 1.00 118.87 ? 171 ASN D N     1 
ATOM   6598 C  CA    . ASN D 1 171 ? -13.154 61.532  103.715 1.00 118.12 ? 171 ASN D CA    1 
ATOM   6599 C  C     . ASN D 1 171 ? -12.271 62.732  103.377 1.00 117.56 ? 171 ASN D C     1 
ATOM   6600 O  O     . ASN D 1 171 ? -12.776 63.815  103.080 1.00 117.33 ? 171 ASN D O     1 
ATOM   6601 C  CB    . ASN D 1 171 ? -12.824 61.052  105.137 1.00 118.72 ? 171 ASN D CB    1 
ATOM   6602 C  CG    . ASN D 1 171 ? -13.800 59.997  105.654 1.00 119.19 ? 171 ASN D CG    1 
ATOM   6603 O  OD1   . ASN D 1 171 ? -14.948 59.912  105.205 1.00 118.68 ? 171 ASN D OD1   1 
ATOM   6604 N  ND2   . ASN D 1 171 ? -13.349 59.202  106.622 1.00 118.99 ? 171 ASN D ND2   1 
ATOM   6605 N  N     . TYR D 1 172 ? -10.955 62.538  103.435 1.00 117.14 ? 172 TYR D N     1 
ATOM   6606 C  CA    . TYR D 1 172 ? -10.013 63.606  103.115 1.00 117.06 ? 172 TYR D CA    1 
ATOM   6607 C  C     . TYR D 1 172 ? -10.579 64.398  101.948 1.00 117.56 ? 172 TYR D C     1 
ATOM   6608 O  O     . TYR D 1 172 ? -10.622 65.623  101.972 1.00 117.24 ? 172 TYR D O     1 
ATOM   6609 C  CB    . TYR D 1 172 ? -8.659  63.028  102.704 1.00 116.33 ? 172 TYR D CB    1 
ATOM   6610 C  CG    . TYR D 1 172 ? -7.891  62.327  103.806 1.00 116.21 ? 172 TYR D CG    1 
ATOM   6611 C  CD1   . TYR D 1 172 ? -7.439  63.025  104.922 1.00 115.95 ? 172 TYR D CD1   1 
ATOM   6612 C  CD2   . TYR D 1 172 ? -7.578  60.970  103.712 1.00 116.11 ? 172 TYR D CD2   1 
ATOM   6613 C  CE1   . TYR D 1 172 ? -6.690  62.390  105.917 1.00 115.70 ? 172 TYR D CE1   1 
ATOM   6614 C  CE2   . TYR D 1 172 ? -6.831  60.328  104.700 1.00 115.55 ? 172 TYR D CE2   1 
ATOM   6615 C  CZ    . TYR D 1 172 ? -6.390  61.043  105.799 1.00 115.49 ? 172 TYR D CZ    1 
ATOM   6616 O  OH    . TYR D 1 172 ? -5.643  60.422  106.775 1.00 115.65 ? 172 TYR D OH    1 
ATOM   6617 N  N     . HIS D 1 173 ? -11.033 63.665  100.936 1.00 118.96 ? 173 HIS D N     1 
ATOM   6618 C  CA    . HIS D 1 173 ? -11.604 64.240  99.720  1.00 120.22 ? 173 HIS D CA    1 
ATOM   6619 C  C     . HIS D 1 173 ? -12.494 65.452  99.974  1.00 120.79 ? 173 HIS D C     1 
ATOM   6620 O  O     . HIS D 1 173 ? -12.201 66.551  99.504  1.00 120.88 ? 173 HIS D O     1 
ATOM   6621 C  CB    . HIS D 1 173 ? -12.391 63.161  98.955  1.00 120.05 ? 173 HIS D CB    1 
ATOM   6622 C  CG    . HIS D 1 173 ? -12.969 63.631  97.652  1.00 120.56 ? 173 HIS D CG    1 
ATOM   6623 N  ND1   . HIS D 1 173 ? -12.210 64.230  96.669  1.00 120.24 ? 173 HIS D ND1   1 
ATOM   6624 C  CD2   . HIS D 1 173 ? -14.232 63.569  97.165  1.00 120.67 ? 173 HIS D CD2   1 
ATOM   6625 C  CE1   . HIS D 1 173 ? -12.980 64.518  95.634  1.00 120.32 ? 173 HIS D CE1   1 
ATOM   6626 N  NE2   . HIS D 1 173 ? -14.212 64.127  95.909  1.00 120.22 ? 173 HIS D NE2   1 
ATOM   6627 N  N     . LYS D 1 174 ? -13.573 65.257  100.723 1.00 121.73 ? 174 LYS D N     1 
ATOM   6628 C  CA    . LYS D 1 174 ? -14.498 66.347  101.002 1.00 122.45 ? 174 LYS D CA    1 
ATOM   6629 C  C     . LYS D 1 174 ? -13.846 67.541  101.691 1.00 123.00 ? 174 LYS D C     1 
ATOM   6630 O  O     . LYS D 1 174 ? -14.159 68.690  101.381 1.00 122.47 ? 174 LYS D O     1 
ATOM   6631 C  CB    . LYS D 1 174 ? -15.672 65.836  101.836 1.00 122.23 ? 174 LYS D CB    1 
ATOM   6632 C  CG    . LYS D 1 174 ? -17.021 66.155  101.217 1.00 122.41 ? 174 LYS D CG    1 
ATOM   6633 C  CD    . LYS D 1 174 ? -17.110 65.652  99.773  1.00 122.87 ? 174 LYS D CD    1 
ATOM   6634 C  CE    . LYS D 1 174 ? -16.943 64.133  99.689  1.00 123.24 ? 174 LYS D CE    1 
ATOM   6635 N  NZ    . LYS D 1 174 ? -17.103 63.600  98.303  1.00 122.78 ? 174 LYS D NZ    1 
ATOM   6636 N  N     . ARG D 1 175 ? -12.940 67.276  102.623 1.00 123.89 ? 175 ARG D N     1 
ATOM   6637 C  CA    . ARG D 1 175 ? -12.268 68.362  103.322 1.00 125.30 ? 175 ARG D CA    1 
ATOM   6638 C  C     . ARG D 1 175 ? -10.927 68.699  102.675 1.00 125.87 ? 175 ARG D C     1 
ATOM   6639 O  O     . ARG D 1 175 ? -10.077 69.348  103.288 1.00 126.10 ? 175 ARG D O     1 
ATOM   6640 C  CB    . ARG D 1 175 ? -12.068 68.007  104.802 1.00 125.97 ? 175 ARG D CB    1 
ATOM   6641 C  CG    . ARG D 1 175 ? -13.357 68.025  105.623 1.00 126.90 ? 175 ARG D CG    1 
ATOM   6642 C  CD    . ARG D 1 175 ? -13.087 67.900  107.125 1.00 127.59 ? 175 ARG D CD    1 
ATOM   6643 N  NE    . ARG D 1 175 ? -12.671 66.555  107.526 1.00 127.97 ? 175 ARG D NE    1 
ATOM   6644 C  CZ    . ARG D 1 175 ? -13.475 65.494  107.544 1.00 127.83 ? 175 ARG D CZ    1 
ATOM   6645 N  NH1   . ARG D 1 175 ? -14.746 65.616  107.183 1.00 128.04 ? 175 ARG D NH1   1 
ATOM   6646 N  NH2   . ARG D 1 175 ? -13.010 64.310  107.920 1.00 127.32 ? 175 ARG D NH2   1 
ATOM   6647 N  N     . LEU D 1 176 ? -10.746 68.259  101.432 1.00 126.16 ? 176 LEU D N     1 
ATOM   6648 C  CA    . LEU D 1 176 ? -9.507  68.520  100.702 1.00 126.27 ? 176 LEU D CA    1 
ATOM   6649 C  C     . LEU D 1 176 ? -9.800  68.977  99.271  1.00 126.03 ? 176 LEU D C     1 
ATOM   6650 O  O     . LEU D 1 176 ? -8.900  69.421  98.557  1.00 126.23 ? 176 LEU D O     1 
ATOM   6651 C  CB    . LEU D 1 176 ? -8.625  67.264  100.685 1.00 126.35 ? 176 LEU D CB    1 
ATOM   6652 C  CG    . LEU D 1 176 ? -7.171  67.395  100.219 1.00 126.27 ? 176 LEU D CG    1 
ATOM   6653 C  CD1   . LEU D 1 176 ? -6.440  68.461  101.032 1.00 125.96 ? 176 LEU D CD1   1 
ATOM   6654 C  CD2   . LEU D 1 176 ? -6.485  66.050  100.372 1.00 126.26 ? 176 LEU D CD2   1 
ATOM   6655 N  N     . ILE D 1 177 ? -11.061 68.868  98.862  1.00 125.42 ? 177 ILE D N     1 
ATOM   6656 C  CA    . ILE D 1 177 ? -11.469 69.283  97.526  1.00 124.85 ? 177 ILE D CA    1 
ATOM   6657 C  C     . ILE D 1 177 ? -11.473 70.804  97.508  1.00 125.56 ? 177 ILE D C     1 
ATOM   6658 O  O     . ILE D 1 177 ? -11.317 71.425  96.457  1.00 125.85 ? 177 ILE D O     1 
ATOM   6659 C  CB    . ILE D 1 177 ? -12.891 68.763  97.189  1.00 123.94 ? 177 ILE D CB    1 
ATOM   6660 C  CG1   . ILE D 1 177 ? -13.091 68.690  95.672  1.00 123.58 ? 177 ILE D CG1   1 
ATOM   6661 C  CG2   . ILE D 1 177 ? -13.940 69.672  97.804  1.00 123.37 ? 177 ILE D CG2   1 
ATOM   6662 C  CD1   . ILE D 1 177 ? -13.191 70.025  94.977  1.00 123.11 ? 177 ILE D CD1   1 
ATOM   6663 N  N     . ASP D 1 178 ? -11.632 71.393  98.693  1.00 126.37 ? 178 ASP D N     1 
ATOM   6664 C  CA    . ASP D 1 178 ? -11.678 72.846  98.851  1.00 127.01 ? 178 ASP D CA    1 
ATOM   6665 C  C     . ASP D 1 178 ? -10.367 73.498  99.295  1.00 127.29 ? 178 ASP D C     1 
ATOM   6666 O  O     . ASP D 1 178 ? -10.376 74.637  99.758  1.00 127.40 ? 178 ASP D O     1 
ATOM   6667 C  CB    . ASP D 1 178 ? -12.782 73.230  99.843  1.00 126.96 ? 178 ASP D CB    1 
ATOM   6668 C  CG    . ASP D 1 178 ? -14.147 72.710  99.431  1.00 127.26 ? 178 ASP D CG    1 
ATOM   6669 O  OD1   . ASP D 1 178 ? -14.561 72.962  98.279  1.00 127.82 ? 178 ASP D OD1   1 
ATOM   6670 O  OD2   . ASP D 1 178 ? -14.810 72.055  100.262 1.00 127.06 ? 178 ASP D OD2   1 
ATOM   6671 N  N     . LEU D 1 179 ? -9.251  72.785  99.158  1.00 127.87 ? 179 LEU D N     1 
ATOM   6672 C  CA    . LEU D 1 179 ? -7.938  73.320  99.537  1.00 127.90 ? 179 LEU D CA    1 
ATOM   6673 C  C     . LEU D 1 179 ? -7.054  73.517  98.306  1.00 128.32 ? 179 LEU D C     1 
ATOM   6674 O  O     . LEU D 1 179 ? -6.060  74.249  98.351  1.00 128.21 ? 179 LEU D O     1 
ATOM   6675 C  CB    . LEU D 1 179 ? -7.231  72.385  100.524 1.00 127.18 ? 179 LEU D CB    1 
ATOM   6676 C  CG    . LEU D 1 179 ? -7.699  72.409  101.979 1.00 126.53 ? 179 LEU D CG    1 
ATOM   6677 C  CD1   . LEU D 1 179 ? -7.498  73.807  102.544 1.00 125.76 ? 179 LEU D CD1   1 
ATOM   6678 C  CD2   . LEU D 1 179 ? -9.157  71.989  102.067 1.00 126.06 ? 179 LEU D CD2   1 
ATOM   6679 N  N     . VAL D 1 180 ? -7.422  72.845  97.216  1.00 128.57 ? 180 VAL D N     1 
ATOM   6680 C  CA    . VAL D 1 180 ? -6.698  72.936  95.951  1.00 128.25 ? 180 VAL D CA    1 
ATOM   6681 C  C     . VAL D 1 180 ? -7.385  74.010  95.118  1.00 127.80 ? 180 VAL D C     1 
ATOM   6682 O  O     . VAL D 1 180 ? -6.738  74.886  94.538  1.00 127.53 ? 180 VAL D O     1 
ATOM   6683 C  CB    . VAL D 1 180 ? -6.739  71.594  95.186  1.00 128.31 ? 180 VAL D CB    1 
ATOM   6684 C  CG1   . VAL D 1 180 ? -5.929  70.551  95.935  1.00 128.32 ? 180 VAL D CG1   1 
ATOM   6685 C  CG2   . VAL D 1 180 ? -8.184  71.124  95.026  1.00 127.77 ? 180 VAL D CG2   1 
ATOM   6686 N  N     . LYS D 1 181 ? -8.710  73.917  95.079  1.00 127.24 ? 181 LYS D N     1 
ATOM   6687 C  CA    . LYS D 1 181 ? -9.561  74.859  94.368  1.00 126.82 ? 181 LYS D CA    1 
ATOM   6688 C  C     . LYS D 1 181 ? -9.178  75.221  92.933  1.00 125.89 ? 181 LYS D C     1 
ATOM   6689 O  O     . LYS D 1 181 ? -8.002  75.244  92.562  1.00 125.15 ? 181 LYS D O     1 
ATOM   6690 C  CB    . LYS D 1 181 ? -9.693  76.143  95.196  1.00 127.38 ? 181 LYS D CB    1 
ATOM   6691 C  CG    . LYS D 1 181 ? -10.469 75.970  96.500  1.00 126.98 ? 181 LYS D CG    1 
ATOM   6692 C  CD    . LYS D 1 181 ? -11.805 76.696  96.451  1.00 126.41 ? 181 LYS D CD    1 
ATOM   6693 C  CE    . LYS D 1 181 ? -11.609 78.191  96.224  1.00 125.65 ? 181 LYS D CE    1 
ATOM   6694 N  NZ    . LYS D 1 181 ? -12.901 78.916  96.093  1.00 125.44 ? 181 LYS D NZ    1 
ATOM   6695 N  N     . VAL D 1 182 ? -10.206 75.503  92.137  1.00 124.79 ? 182 VAL D N     1 
ATOM   6696 C  CA    . VAL D 1 182 ? -10.051 75.899  90.746  1.00 124.03 ? 182 VAL D CA    1 
ATOM   6697 C  C     . VAL D 1 182 ? -9.044  75.051  89.965  1.00 123.52 ? 182 VAL D C     1 
ATOM   6698 O  O     . VAL D 1 182 ? -9.422  74.079  89.308  1.00 123.25 ? 182 VAL D O     1 
ATOM   6699 C  CB    . VAL D 1 182 ? -9.646  77.387  90.668  1.00 124.30 ? 182 VAL D CB    1 
ATOM   6700 C  CG1   . VAL D 1 182 ? -9.535  77.833  89.214  1.00 124.86 ? 182 VAL D CG1   1 
ATOM   6701 C  CG2   . VAL D 1 182 ? -10.667 78.234  91.415  1.00 123.61 ? 182 VAL D CG2   1 
ATOM   6702 N  N     . GLY D 1 183 ? -7.770  75.432  90.036  1.00 122.85 ? 183 GLY D N     1 
ATOM   6703 C  CA    . GLY D 1 183 ? -6.723  74.712  89.327  1.00 121.75 ? 183 GLY D CA    1 
ATOM   6704 C  C     . GLY D 1 183 ? -6.909  73.206  89.257  1.00 120.97 ? 183 GLY D C     1 
ATOM   6705 O  O     . GLY D 1 183 ? -6.945  72.634  88.167  1.00 120.69 ? 183 GLY D O     1 
ATOM   6706 N  N     . GLY D 1 184 ? -7.021  72.565  90.420  1.00 120.32 ? 184 GLY D N     1 
ATOM   6707 C  CA    . GLY D 1 184 ? -7.204  71.125  90.470  1.00 118.60 ? 184 GLY D CA    1 
ATOM   6708 C  C     . GLY D 1 184 ? -5.919  70.363  90.738  1.00 117.63 ? 184 GLY D C     1 
ATOM   6709 O  O     . GLY D 1 184 ? -4.845  70.961  90.834  1.00 117.13 ? 184 GLY D O     1 
ATOM   6710 N  N     . VAL D 1 185 ? -6.046  69.042  90.865  1.00 116.76 ? 185 VAL D N     1 
ATOM   6711 C  CA    . VAL D 1 185 ? -4.931  68.124  91.115  1.00 115.72 ? 185 VAL D CA    1 
ATOM   6712 C  C     . VAL D 1 185 ? -5.370  66.942  91.998  1.00 115.56 ? 185 VAL D C     1 
ATOM   6713 O  O     . VAL D 1 185 ? -6.065  66.040  91.525  1.00 115.57 ? 185 VAL D O     1 
ATOM   6714 C  CB    . VAL D 1 185 ? -3.713  68.840  91.768  1.00 115.09 ? 185 VAL D CB    1 
ATOM   6715 C  CG1   . VAL D 1 185 ? -4.085  69.411  93.133  1.00 114.23 ? 185 VAL D CG1   1 
ATOM   6716 C  CG2   . VAL D 1 185 ? -2.558  67.879  91.873  1.00 114.20 ? 185 VAL D CG2   1 
ATOM   6717 N  N     . ILE D 1 186 ? -4.969  66.955  93.271  1.00 114.62 ? 186 ILE D N     1 
ATOM   6718 C  CA    . ILE D 1 186 ? -5.307  65.899  94.226  1.00 113.44 ? 186 ILE D CA    1 
ATOM   6719 C  C     . ILE D 1 186 ? -5.193  64.512  93.609  1.00 112.51 ? 186 ILE D C     1 
ATOM   6720 O  O     . ILE D 1 186 ? -6.092  64.060  92.892  1.00 112.21 ? 186 ILE D O     1 
ATOM   6721 C  CB    . ILE D 1 186 ? -6.748  66.050  94.779  1.00 113.67 ? 186 ILE D CB    1 
ATOM   6722 C  CG1   . ILE D 1 186 ? -6.955  67.450  95.351  1.00 113.86 ? 186 ILE D CG1   1 
ATOM   6723 C  CG2   . ILE D 1 186 ? -6.986  65.035  95.886  1.00 113.36 ? 186 ILE D CG2   1 
ATOM   6724 C  CD1   . ILE D 1 186 ? -8.359  67.688  95.863  1.00 113.79 ? 186 ILE D CD1   1 
ATOM   6725 N  N     . GLY D 1 187 ? -4.088  63.835  93.895  1.00 111.22 ? 187 GLY D N     1 
ATOM   6726 C  CA    . GLY D 1 187 ? -3.897  62.502  93.363  1.00 110.08 ? 187 GLY D CA    1 
ATOM   6727 C  C     . GLY D 1 187 ? -3.896  61.447  94.452  1.00 109.07 ? 187 GLY D C     1 
ATOM   6728 O  O     . GLY D 1 187 ? -2.953  61.374  95.241  1.00 109.06 ? 187 GLY D O     1 
ATOM   6729 N  N     . TYR D 1 188 ? -4.950  60.636  94.509  1.00 107.80 ? 188 TYR D N     1 
ATOM   6730 C  CA    . TYR D 1 188 ? -5.031  59.579  95.511  1.00 106.53 ? 188 TYR D CA    1 
ATOM   6731 C  C     . TYR D 1 188 ? -4.267  58.362  95.002  1.00 105.06 ? 188 TYR D C     1 
ATOM   6732 O  O     . TYR D 1 188 ? -4.703  57.679  94.080  1.00 105.19 ? 188 TYR D O     1 
ATOM   6733 C  CB    . TYR D 1 188 ? -6.488  59.201  95.791  1.00 107.80 ? 188 TYR D CB    1 
ATOM   6734 C  CG    . TYR D 1 188 ? -7.356  60.363  96.221  1.00 108.87 ? 188 TYR D CG    1 
ATOM   6735 C  CD1   . TYR D 1 188 ? -8.025  61.141  95.279  1.00 109.17 ? 188 TYR D CD1   1 
ATOM   6736 C  CD2   . TYR D 1 188 ? -7.501  60.693  97.570  1.00 108.89 ? 188 TYR D CD2   1 
ATOM   6737 C  CE1   . TYR D 1 188 ? -8.819  62.215  95.666  1.00 109.64 ? 188 TYR D CE1   1 
ATOM   6738 C  CE2   . TYR D 1 188 ? -8.290  61.771  97.969  1.00 108.96 ? 188 TYR D CE2   1 
ATOM   6739 C  CZ    . TYR D 1 188 ? -8.947  62.527  97.009  1.00 109.33 ? 188 TYR D CZ    1 
ATOM   6740 O  OH    . TYR D 1 188 ? -9.731  63.598  97.377  1.00 108.88 ? 188 TYR D OH    1 
ATOM   6741 N  N     . ASP D 1 189 ? -3.121  58.102  95.618  1.00 103.32 ? 189 ASP D N     1 
ATOM   6742 C  CA    . ASP D 1 189 ? -2.257  56.997  95.235  1.00 101.92 ? 189 ASP D CA    1 
ATOM   6743 C  C     . ASP D 1 189 ? -2.771  55.611  95.615  1.00 100.59 ? 189 ASP D C     1 
ATOM   6744 O  O     . ASP D 1 189 ? -3.528  55.452  96.566  1.00 99.88  ? 189 ASP D O     1 
ATOM   6745 C  CB    . ASP D 1 189 ? -0.870  57.223  95.842  1.00 102.84 ? 189 ASP D CB    1 
ATOM   6746 C  CG    . ASP D 1 189 ? 0.109   56.116  95.507  1.00 104.10 ? 189 ASP D CG    1 
ATOM   6747 O  OD1   . ASP D 1 189 ? 0.268   55.801  94.308  1.00 105.91 ? 189 ASP D OD1   1 
ATOM   6748 O  OD2   . ASP D 1 189 ? 0.728   55.564  96.442  1.00 103.94 ? 189 ASP D OD2   1 
ATOM   6749 N  N     . ASN D 1 190 ? -2.353  54.616  94.839  1.00 99.57  ? 190 ASN D N     1 
ATOM   6750 C  CA    . ASN D 1 190 ? -2.709  53.220  95.058  1.00 98.18  ? 190 ASN D CA    1 
ATOM   6751 C  C     . ASN D 1 190 ? -4.169  52.852  94.801  1.00 97.70  ? 190 ASN D C     1 
ATOM   6752 O  O     . ASN D 1 190 ? -4.616  51.807  95.259  1.00 97.44  ? 190 ASN D O     1 
ATOM   6753 C  CB    . ASN D 1 190 ? -2.329  52.807  96.486  1.00 98.23  ? 190 ASN D CB    1 
ATOM   6754 C  CG    . ASN D 1 190 ? -0.841  52.974  96.777  1.00 98.35  ? 190 ASN D CG    1 
ATOM   6755 O  OD1   . ASN D 1 190 ? -0.403  52.873  97.925  1.00 98.68  ? 190 ASN D OD1   1 
ATOM   6756 N  ND2   . ASN D 1 190 ? -0.058  53.223  95.737  1.00 98.98  ? 190 ASN D ND2   1 
ATOM   6757 N  N     . THR D 1 191 ? -4.910  53.678  94.063  1.00 97.55  ? 191 THR D N     1 
ATOM   6758 C  CA    . THR D 1 191 ? -6.320  53.374  93.805  1.00 98.31  ? 191 THR D CA    1 
ATOM   6759 C  C     . THR D 1 191 ? -6.527  52.110  92.992  1.00 98.39  ? 191 THR D C     1 
ATOM   6760 O  O     . THR D 1 191 ? -7.625  51.862  92.494  1.00 97.94  ? 191 THR D O     1 
ATOM   6761 C  CB    . THR D 1 191 ? -7.048  54.505  93.065  1.00 99.05  ? 191 THR D CB    1 
ATOM   6762 O  OG1   . THR D 1 191 ? -6.476  54.670  91.764  1.00 101.00 ? 191 THR D OG1   1 
ATOM   6763 C  CG2   . THR D 1 191 ? -6.938  55.799  93.832  1.00 100.24 ? 191 THR D CG2   1 
ATOM   6764 N  N     . LEU D 1 192 ? -5.466  51.326  92.839  1.00 99.06  ? 192 LEU D N     1 
ATOM   6765 C  CA    . LEU D 1 192 ? -5.532  50.061  92.116  1.00 99.85  ? 192 LEU D CA    1 
ATOM   6766 C  C     . LEU D 1 192 ? -5.160  48.959  93.092  1.00 100.23 ? 192 LEU D C     1 
ATOM   6767 O  O     . LEU D 1 192 ? -5.238  47.772  92.777  1.00 99.35  ? 192 LEU D O     1 
ATOM   6768 C  CB    . LEU D 1 192 ? -4.571  50.056  90.932  1.00 100.28 ? 192 LEU D CB    1 
ATOM   6769 C  CG    . LEU D 1 192 ? -5.054  50.815  89.699  1.00 100.61 ? 192 LEU D CG    1 
ATOM   6770 C  CD1   . LEU D 1 192 ? -3.968  50.792  88.639  1.00 100.51 ? 192 LEU D CD1   1 
ATOM   6771 C  CD2   . LEU D 1 192 ? -6.338  50.178  89.177  1.00 100.08 ? 192 LEU D CD2   1 
ATOM   6772 N  N     . TRP D 1 193 ? -4.747  49.390  94.281  1.00 101.18 ? 193 TRP D N     1 
ATOM   6773 C  CA    . TRP D 1 193 ? -4.374  48.507  95.377  1.00 102.28 ? 193 TRP D CA    1 
ATOM   6774 C  C     . TRP D 1 193 ? -4.167  47.072  94.887  1.00 102.86 ? 193 TRP D C     1 
ATOM   6775 O  O     . TRP D 1 193 ? -5.004  46.194  95.109  1.00 103.35 ? 193 TRP D O     1 
ATOM   6776 C  CB    . TRP D 1 193 ? -5.476  48.565  96.447  1.00 101.98 ? 193 TRP D CB    1 
ATOM   6777 C  CG    . TRP D 1 193 ? -5.138  47.951  97.770  1.00 100.95 ? 193 TRP D CG    1 
ATOM   6778 C  CD1   . TRP D 1 193 ? -5.837  46.978  98.418  1.00 100.53 ? 193 TRP D CD1   1 
ATOM   6779 C  CD2   . TRP D 1 193 ? -4.050  48.305  98.631  1.00 100.90 ? 193 TRP D CD2   1 
ATOM   6780 N  NE1   . TRP D 1 193 ? -5.256  46.703  99.630  1.00 100.70 ? 193 TRP D NE1   1 
ATOM   6781 C  CE2   . TRP D 1 193 ? -4.157  47.504  99.787  1.00 100.78 ? 193 TRP D CE2   1 
ATOM   6782 C  CE3   . TRP D 1 193 ? -2.996  49.222  98.538  1.00 102.15 ? 193 TRP D CE3   1 
ATOM   6783 C  CZ2   . TRP D 1 193 ? -3.249  47.590  100.848 1.00 101.18 ? 193 TRP D CZ2   1 
ATOM   6784 C  CZ3   . TRP D 1 193 ? -2.089  49.309  99.596  1.00 102.46 ? 193 TRP D CZ3   1 
ATOM   6785 C  CH2   . TRP D 1 193 ? -2.225  48.496  100.735 1.00 102.13 ? 193 TRP D CH2   1 
ATOM   6786 N  N     . ASN D 1 194 ? -3.057  46.850  94.194  1.00 103.05 ? 194 ASN D N     1 
ATOM   6787 C  CA    . ASN D 1 194 ? -2.730  45.528  93.682  1.00 103.43 ? 194 ASN D CA    1 
ATOM   6788 C  C     . ASN D 1 194 ? -3.913  44.900  92.941  1.00 103.99 ? 194 ASN D C     1 
ATOM   6789 O  O     . ASN D 1 194 ? -4.457  45.494  92.012  1.00 103.97 ? 194 ASN D O     1 
ATOM   6790 C  CB    . ASN D 1 194 ? -2.305  44.627  94.838  1.00 102.66 ? 194 ASN D CB    1 
ATOM   6791 C  CG    . ASN D 1 194 ? -1.101  43.798  94.499  1.00 102.71 ? 194 ASN D CG    1 
ATOM   6792 O  OD1   . ASN D 1 194 ? -1.042  43.190  93.431  1.00 102.71 ? 194 ASN D OD1   1 
ATOM   6793 N  ND2   . ASN D 1 194 ? -0.127  43.762  95.404  1.00 101.95 ? 194 ASN D ND2   1 
ATOM   6794 N  N     . GLY D 1 195 ? -4.303  43.698  93.353  1.00 104.54 ? 195 GLY D N     1 
ATOM   6795 C  CA    . GLY D 1 195 ? -5.425  43.024  92.723  1.00 105.14 ? 195 GLY D CA    1 
ATOM   6796 C  C     . GLY D 1 195 ? -6.765  43.487  93.272  1.00 105.79 ? 195 GLY D C     1 
ATOM   6797 O  O     . GLY D 1 195 ? -7.328  42.877  94.186  1.00 105.50 ? 195 GLY D O     1 
ATOM   6798 N  N     . SER D 1 196 ? -7.278  44.578  92.715  1.00 106.06 ? 196 SER D N     1 
ATOM   6799 C  CA    . SER D 1 196 ? -8.558  45.124  93.143  1.00 106.14 ? 196 SER D CA    1 
ATOM   6800 C  C     . SER D 1 196 ? -9.667  44.132  92.833  1.00 106.80 ? 196 SER D C     1 
ATOM   6801 O  O     . SER D 1 196 ? -10.264 43.551  93.735  1.00 106.56 ? 196 SER D O     1 
ATOM   6802 C  CB    . SER D 1 196 ? -8.832  46.449  92.426  1.00 105.28 ? 196 SER D CB    1 
ATOM   6803 O  OG    . SER D 1 196 ? -10.133 46.929  92.705  1.00 103.64 ? 196 SER D OG    1 
ATOM   6804 N  N     . VAL D 1 197 ? -9.922  43.932  91.547  1.00 108.19 ? 197 VAL D N     1 
ATOM   6805 C  CA    . VAL D 1 197 ? -10.968 43.020  91.101  1.00 109.88 ? 197 VAL D CA    1 
ATOM   6806 C  C     . VAL D 1 197 ? -10.451 41.584  90.913  1.00 110.50 ? 197 VAL D C     1 
ATOM   6807 O  O     . VAL D 1 197 ? -10.547 41.014  89.826  1.00 110.52 ? 197 VAL D O     1 
ATOM   6808 C  CB    . VAL D 1 197 ? -11.616 43.545  89.772  1.00 110.60 ? 197 VAL D CB    1 
ATOM   6809 C  CG1   . VAL D 1 197 ? -10.623 43.446  88.608  1.00 109.20 ? 197 VAL D CG1   1 
ATOM   6810 C  CG2   . VAL D 1 197 ? -12.904 42.783  89.474  1.00 110.71 ? 197 VAL D CG2   1 
ATOM   6811 N  N     . VAL D 1 198 ? -9.910  41.000  91.981  1.00 111.20 ? 198 VAL D N     1 
ATOM   6812 C  CA    . VAL D 1 198 ? -9.390  39.633  91.924  1.00 111.86 ? 198 VAL D CA    1 
ATOM   6813 C  C     . VAL D 1 198 ? -10.518 38.609  92.128  1.00 112.77 ? 198 VAL D C     1 
ATOM   6814 O  O     . VAL D 1 198 ? -11.641 38.977  92.486  1.00 112.23 ? 198 VAL D O     1 
ATOM   6815 C  CB    . VAL D 1 198 ? -8.271  39.412  92.988  1.00 111.29 ? 198 VAL D CB    1 
ATOM   6816 C  CG1   . VAL D 1 198 ? -8.863  39.436  94.380  1.00 111.78 ? 198 VAL D CG1   1 
ATOM   6817 C  CG2   . VAL D 1 198 ? -7.540  38.100  92.730  1.00 110.26 ? 198 VAL D CG2   1 
ATOM   6818 N  N     . ALA D 1 199 ? -10.209 37.333  91.887  1.00 113.97 ? 199 ALA D N     1 
ATOM   6819 C  CA    . ALA D 1 199 ? -11.166 36.231  92.012  1.00 115.14 ? 199 ALA D CA    1 
ATOM   6820 C  C     . ALA D 1 199 ? -12.029 36.323  93.270  1.00 116.91 ? 199 ALA D C     1 
ATOM   6821 O  O     . ALA D 1 199 ? -11.768 37.144  94.146  1.00 117.45 ? 199 ALA D O     1 
ATOM   6822 C  CB    . ALA D 1 199 ? -10.419 34.904  91.986  1.00 114.06 ? 199 ALA D CB    1 
ATOM   6823 N  N     . PRO D 1 200 ? -13.079 35.484  93.373  1.00 118.56 ? 200 PRO D N     1 
ATOM   6824 C  CA    . PRO D 1 200 ? -13.971 35.489  94.540  1.00 119.93 ? 200 PRO D CA    1 
ATOM   6825 C  C     . PRO D 1 200 ? -13.173 35.219  95.814  1.00 121.15 ? 200 PRO D C     1 
ATOM   6826 O  O     . PRO D 1 200 ? -11.945 35.114  95.761  1.00 121.04 ? 200 PRO D O     1 
ATOM   6827 C  CB    . PRO D 1 200 ? -14.950 34.358  94.229  1.00 119.64 ? 200 PRO D CB    1 
ATOM   6828 C  CG    . PRO D 1 200 ? -15.018 34.369  92.746  1.00 119.58 ? 200 PRO D CG    1 
ATOM   6829 C  CD    . PRO D 1 200 ? -13.559 34.520  92.368  1.00 119.38 ? 200 PRO D CD    1 
ATOM   6830 N  N     . PRO D 1 201 ? -13.854 35.104  96.977  1.00 122.27 ? 201 PRO D N     1 
ATOM   6831 C  CA    . PRO D 1 201 ? -13.115 34.838  98.220  1.00 122.38 ? 201 PRO D CA    1 
ATOM   6832 C  C     . PRO D 1 201 ? -12.164 33.658  98.004  1.00 121.99 ? 201 PRO D C     1 
ATOM   6833 O  O     . PRO D 1 201 ? -11.359 33.319  98.877  1.00 122.17 ? 201 PRO D O     1 
ATOM   6834 C  CB    . PRO D 1 201 ? -14.227 34.518  99.220  1.00 122.61 ? 201 PRO D CB    1 
ATOM   6835 C  CG    . PRO D 1 201 ? -15.352 35.390  98.749  1.00 122.55 ? 201 PRO D CG    1 
ATOM   6836 C  CD    . PRO D 1 201 ? -15.304 35.199  97.241  1.00 122.59 ? 201 PRO D CD    1 
ATOM   6837 N  N     . ASP D 1 202 ? -12.289 33.045  96.825  1.00 120.60 ? 202 ASP D N     1 
ATOM   6838 C  CA    . ASP D 1 202 ? -11.476 31.917  96.402  1.00 118.74 ? 202 ASP D CA    1 
ATOM   6839 C  C     . ASP D 1 202 ? -10.119 32.441  95.969  1.00 117.31 ? 202 ASP D C     1 
ATOM   6840 O  O     . ASP D 1 202 ? -9.284  31.691  95.476  1.00 117.58 ? 202 ASP D O     1 
ATOM   6841 C  CB    . ASP D 1 202 ? -12.143 31.210  95.227  1.00 119.42 ? 202 ASP D CB    1 
ATOM   6842 C  CG    . ASP D 1 202 ? -13.532 30.714  95.560  1.00 119.82 ? 202 ASP D CG    1 
ATOM   6843 O  OD1   . ASP D 1 202 ? -13.647 29.738  96.330  1.00 119.77 ? 202 ASP D OD1   1 
ATOM   6844 O  OD2   . ASP D 1 202 ? -14.510 31.307  95.056  1.00 120.67 ? 202 ASP D OD2   1 
ATOM   6845 N  N     . ALA D 1 203 ? -9.919  33.740  96.139  1.00 115.60 ? 203 ALA D N     1 
ATOM   6846 C  CA    . ALA D 1 203 ? -8.663  34.377  95.786  1.00 114.45 ? 203 ALA D CA    1 
ATOM   6847 C  C     . ALA D 1 203 ? -7.961  34.731  97.086  1.00 113.62 ? 203 ALA D C     1 
ATOM   6848 O  O     . ALA D 1 203 ? -8.152  35.811  97.630  1.00 113.50 ? 203 ALA D O     1 
ATOM   6849 C  CB    . ALA D 1 203 ? -8.919  35.630  94.965  1.00 114.59 ? 203 ALA D CB    1 
ATOM   6850 N  N     . PRO D 1 204 ? -7.143  33.809  97.605  1.00 112.97 ? 204 PRO D N     1 
ATOM   6851 C  CA    . PRO D 1 204 ? -6.389  33.975  98.851  1.00 112.81 ? 204 PRO D CA    1 
ATOM   6852 C  C     . PRO D 1 204 ? -5.526  35.234  98.955  1.00 112.17 ? 204 PRO D C     1 
ATOM   6853 O  O     . PRO D 1 204 ? -4.319  35.177  98.725  1.00 111.80 ? 204 PRO D O     1 
ATOM   6854 C  CB    . PRO D 1 204 ? -5.550  32.700  98.907  1.00 113.46 ? 204 PRO D CB    1 
ATOM   6855 C  CG    . PRO D 1 204 ? -6.442  31.692  98.243  1.00 113.31 ? 204 PRO D CG    1 
ATOM   6856 C  CD    . PRO D 1 204 ? -6.936  32.462  97.046  1.00 112.81 ? 204 PRO D CD    1 
ATOM   6857 N  N     . LEU D 1 205 ? -6.134  36.363  99.315  1.00 111.87 ? 205 LEU D N     1 
ATOM   6858 C  CA    . LEU D 1 205 ? -5.377  37.605  99.449  1.00 111.72 ? 205 LEU D CA    1 
ATOM   6859 C  C     . LEU D 1 205 ? -5.034  37.902  100.904 1.00 111.87 ? 205 LEU D C     1 
ATOM   6860 O  O     . LEU D 1 205 ? -5.700  37.410  101.815 1.00 112.11 ? 205 LEU D O     1 
ATOM   6861 C  CB    . LEU D 1 205 ? -6.137  38.785  98.829  1.00 111.32 ? 205 LEU D CB    1 
ATOM   6862 C  CG    . LEU D 1 205 ? -7.545  39.194  99.262  1.00 111.18 ? 205 LEU D CG    1 
ATOM   6863 C  CD1   . LEU D 1 205 ? -7.895  40.507  98.574  1.00 110.83 ? 205 LEU D CD1   1 
ATOM   6864 C  CD2   . LEU D 1 205 ? -8.556  38.128  98.902  1.00 110.81 ? 205 LEU D CD2   1 
ATOM   6865 N  N     . ARG D 1 206 ? -3.992  38.706  101.112 1.00 112.05 ? 206 ARG D N     1 
ATOM   6866 C  CA    . ARG D 1 206 ? -3.520  39.055  102.452 1.00 112.21 ? 206 ARG D CA    1 
ATOM   6867 C  C     . ARG D 1 206 ? -4.501  39.801  103.355 1.00 112.02 ? 206 ARG D C     1 
ATOM   6868 O  O     . ARG D 1 206 ? -5.608  40.167  102.949 1.00 112.16 ? 206 ARG D O     1 
ATOM   6869 C  CB    . ARG D 1 206 ? -2.226  39.864  102.363 1.00 112.86 ? 206 ARG D CB    1 
ATOM   6870 C  CG    . ARG D 1 206 ? -1.068  39.106  101.757 1.00 114.36 ? 206 ARG D CG    1 
ATOM   6871 C  CD    . ARG D 1 206 ? 0.129   40.016  101.563 1.00 115.43 ? 206 ARG D CD    1 
ATOM   6872 N  NE    . ARG D 1 206 ? 0.824   39.718  100.314 1.00 116.47 ? 206 ARG D NE    1 
ATOM   6873 C  CZ    . ARG D 1 206 ? 0.255   39.766  99.112  1.00 117.09 ? 206 ARG D CZ    1 
ATOM   6874 N  NH1   . ARG D 1 206 ? -1.026  40.101  98.989  1.00 117.04 ? 206 ARG D NH1   1 
ATOM   6875 N  NH2   . ARG D 1 206 ? 0.966   39.477  98.028  1.00 117.11 ? 206 ARG D NH2   1 
ATOM   6876 N  N     . LYS D 1 207 ? -4.057  40.021  104.592 1.00 111.20 ? 207 LYS D N     1 
ATOM   6877 C  CA    . LYS D 1 207 ? -4.837  40.698  105.623 1.00 109.80 ? 207 LYS D CA    1 
ATOM   6878 C  C     . LYS D 1 207 ? -5.241  42.111  105.199 1.00 108.23 ? 207 LYS D C     1 
ATOM   6879 O  O     . LYS D 1 207 ? -6.293  42.317  104.585 1.00 107.80 ? 207 LYS D O     1 
ATOM   6880 C  CB    . LYS D 1 207 ? -4.015  40.765  106.916 1.00 110.53 ? 207 LYS D CB    1 
ATOM   6881 C  CG    . LYS D 1 207 ? -4.821  40.975  108.195 1.00 111.40 ? 207 LYS D CG    1 
ATOM   6882 C  CD    . LYS D 1 207 ? -5.307  39.648  108.761 1.00 112.34 ? 207 LYS D CD    1 
ATOM   6883 C  CE    . LYS D 1 207 ? -5.932  39.819  110.140 1.00 113.14 ? 207 LYS D CE    1 
ATOM   6884 N  NZ    . LYS D 1 207 ? -6.309  38.517  110.773 1.00 113.32 ? 207 LYS D NZ    1 
ATOM   6885 N  N     . TYR D 1 208 ? -4.391  43.076  105.537 1.00 105.99 ? 208 TYR D N     1 
ATOM   6886 C  CA    . TYR D 1 208 ? -4.623  44.480  105.226 1.00 104.32 ? 208 TYR D CA    1 
ATOM   6887 C  C     . TYR D 1 208 ? -5.213  44.697  103.836 1.00 102.64 ? 208 TYR D C     1 
ATOM   6888 O  O     . TYR D 1 208 ? -6.101  45.533  103.651 1.00 102.30 ? 208 TYR D O     1 
ATOM   6889 C  CB    . TYR D 1 208 ? -3.312  45.259  105.353 1.00 105.12 ? 208 TYR D CB    1 
ATOM   6890 C  CG    . TYR D 1 208 ? -2.254  44.833  104.356 1.00 106.40 ? 208 TYR D CG    1 
ATOM   6891 C  CD1   . TYR D 1 208 ? -1.854  43.497  104.257 1.00 106.94 ? 208 TYR D CD1   1 
ATOM   6892 C  CD2   . TYR D 1 208 ? -1.656  45.765  103.504 1.00 107.09 ? 208 TYR D CD2   1 
ATOM   6893 C  CE1   . TYR D 1 208 ? -0.881  43.097  103.331 1.00 107.61 ? 208 TYR D CE1   1 
ATOM   6894 C  CE2   . TYR D 1 208 ? -0.682  45.378  102.573 1.00 107.58 ? 208 TYR D CE2   1 
ATOM   6895 C  CZ    . TYR D 1 208 ? -0.301  44.043  102.492 1.00 107.62 ? 208 TYR D CZ    1 
ATOM   6896 O  OH    . TYR D 1 208 ? 0.650   43.656  101.573 1.00 106.76 ? 208 TYR D OH    1 
ATOM   6897 N  N     . VAL D 1 209 ? -4.720  43.939  102.860 1.00 100.51 ? 209 VAL D N     1 
ATOM   6898 C  CA    . VAL D 1 209 ? -5.195  44.073  101.488 1.00 97.66  ? 209 VAL D CA    1 
ATOM   6899 C  C     . VAL D 1 209 ? -6.666  43.703  101.363 1.00 95.59  ? 209 VAL D C     1 
ATOM   6900 O  O     . VAL D 1 209 ? -7.438  44.426  100.732 1.00 94.89  ? 209 VAL D O     1 
ATOM   6901 C  CB    . VAL D 1 209 ? -4.347  43.215  100.508 1.00 97.74  ? 209 VAL D CB    1 
ATOM   6902 C  CG1   . VAL D 1 209 ? -4.449  41.752  100.856 1.00 97.43  ? 209 VAL D CG1   1 
ATOM   6903 C  CG2   . VAL D 1 209 ? -4.806  43.456  99.086  1.00 98.06  ? 209 VAL D CG2   1 
ATOM   6904 N  N     . ARG D 1 210 ? -7.056  42.585  101.966 1.00 93.64  ? 210 ARG D N     1 
ATOM   6905 C  CA    . ARG D 1 210 ? -8.449  42.163  101.917 1.00 92.12  ? 210 ARG D CA    1 
ATOM   6906 C  C     . ARG D 1 210 ? -9.287  43.206  102.619 1.00 92.34  ? 210 ARG D C     1 
ATOM   6907 O  O     . ARG D 1 210 ? -10.460 43.405  102.300 1.00 91.62  ? 210 ARG D O     1 
ATOM   6908 C  CB    . ARG D 1 210 ? -8.640  40.829  102.621 1.00 90.60  ? 210 ARG D CB    1 
ATOM   6909 C  CG    . ARG D 1 210 ? -10.095 40.478  102.807 1.00 88.48  ? 210 ARG D CG    1 
ATOM   6910 C  CD    . ARG D 1 210 ? -10.239 39.032  103.170 1.00 87.72  ? 210 ARG D CD    1 
ATOM   6911 N  NE    . ARG D 1 210 ? -11.040 38.322  102.183 1.00 86.71  ? 210 ARG D NE    1 
ATOM   6912 C  CZ    . ARG D 1 210 ? -10.649 37.205  101.583 1.00 86.33  ? 210 ARG D CZ    1 
ATOM   6913 N  NH1   . ARG D 1 210 ? -9.464  36.679  101.876 1.00 83.82  ? 210 ARG D NH1   1 
ATOM   6914 N  NH2   . ARG D 1 210 ? -11.446 36.614  100.697 1.00 86.25  ? 210 ARG D NH2   1 
ATOM   6915 N  N     . TYR D 1 211 ? -8.661  43.865  103.588 1.00 92.98  ? 211 TYR D N     1 
ATOM   6916 C  CA    . TYR D 1 211 ? -9.316  44.900  104.364 1.00 93.44  ? 211 TYR D CA    1 
ATOM   6917 C  C     . TYR D 1 211 ? -9.531  46.151  103.518 1.00 93.34  ? 211 TYR D C     1 
ATOM   6918 O  O     . TYR D 1 211 ? -10.662 46.471  103.142 1.00 93.54  ? 211 TYR D O     1 
ATOM   6919 C  CB    . TYR D 1 211 ? -8.477  45.236  105.614 1.00 93.99  ? 211 TYR D CB    1 
ATOM   6920 C  CG    . TYR D 1 211 ? -8.996  46.426  106.405 1.00 94.53  ? 211 TYR D CG    1 
ATOM   6921 C  CD1   . TYR D 1 211 ? -10.273 46.414  106.970 1.00 93.86  ? 211 TYR D CD1   1 
ATOM   6922 C  CD2   . TYR D 1 211 ? -8.238  47.592  106.524 1.00 94.33  ? 211 TYR D CD2   1 
ATOM   6923 C  CE1   . TYR D 1 211 ? -10.784 47.531  107.620 1.00 93.53  ? 211 TYR D CE1   1 
ATOM   6924 C  CE2   . TYR D 1 211 ? -8.741  48.715  107.172 1.00 94.12  ? 211 TYR D CE2   1 
ATOM   6925 C  CZ    . TYR D 1 211 ? -10.015 48.679  107.714 1.00 93.92  ? 211 TYR D CZ    1 
ATOM   6926 O  OH    . TYR D 1 211 ? -10.526 49.803  108.326 1.00 93.43  ? 211 TYR D OH    1 
ATOM   6927 N  N     . TYR D 1 212 ? -8.439  46.841  103.208 1.00 93.10  ? 212 TYR D N     1 
ATOM   6928 C  CA    . TYR D 1 212 ? -8.495  48.073  102.432 1.00 92.91  ? 212 TYR D CA    1 
ATOM   6929 C  C     . TYR D 1 212 ? -9.254  47.992  101.109 1.00 92.84  ? 212 TYR D C     1 
ATOM   6930 O  O     . TYR D 1 212 ? -9.868  48.971  100.683 1.00 92.27  ? 212 TYR D O     1 
ATOM   6931 C  CB    . TYR D 1 212 ? -7.078  48.585  102.196 1.00 92.86  ? 212 TYR D CB    1 
ATOM   6932 C  CG    . TYR D 1 212 ? -6.470  49.284  103.397 1.00 93.23  ? 212 TYR D CG    1 
ATOM   6933 C  CD1   . TYR D 1 212 ? -7.048  50.442  103.919 1.00 93.60  ? 212 TYR D CD1   1 
ATOM   6934 C  CD2   . TYR D 1 212 ? -5.284  48.829  103.969 1.00 93.50  ? 212 TYR D CD2   1 
ATOM   6935 C  CE1   . TYR D 1 212 ? -6.453  51.137  104.972 1.00 93.88  ? 212 TYR D CE1   1 
ATOM   6936 C  CE2   . TYR D 1 212 ? -4.680  49.518  105.026 1.00 93.76  ? 212 TYR D CE2   1 
ATOM   6937 C  CZ    . TYR D 1 212 ? -5.268  50.670  105.516 1.00 93.78  ? 212 TYR D CZ    1 
ATOM   6938 O  OH    . TYR D 1 212 ? -4.660  51.370  106.530 1.00 94.16  ? 212 TYR D OH    1 
ATOM   6939 N  N     . ARG D 1 213 ? -9.216  46.829  100.466 1.00 93.22  ? 213 ARG D N     1 
ATOM   6940 C  CA    . ARG D 1 213 ? -9.907  46.628  99.195  1.00 93.78  ? 213 ARG D CA    1 
ATOM   6941 C  C     . ARG D 1 213 ? -11.278 47.307  99.174  1.00 94.62  ? 213 ARG D C     1 
ATOM   6942 O  O     . ARG D 1 213 ? -11.563 48.135  98.307  1.00 94.48  ? 213 ARG D O     1 
ATOM   6943 C  CB    . ARG D 1 213 ? -10.096 45.132  98.923  1.00 92.94  ? 213 ARG D CB    1 
ATOM   6944 C  CG    . ARG D 1 213 ? -10.966 44.857  97.705  1.00 92.47  ? 213 ARG D CG    1 
ATOM   6945 C  CD    . ARG D 1 213 ? -11.702 43.527  97.786  1.00 92.81  ? 213 ARG D CD    1 
ATOM   6946 N  NE    . ARG D 1 213 ? -10.818 42.366  97.705  1.00 92.84  ? 213 ARG D NE    1 
ATOM   6947 C  CZ    . ARG D 1 213 ? -11.244 41.129  97.458  1.00 92.93  ? 213 ARG D CZ    1 
ATOM   6948 N  NH1   . ARG D 1 213 ? -12.541 40.899  97.269  1.00 92.19  ? 213 ARG D NH1   1 
ATOM   6949 N  NH2   . ARG D 1 213 ? -10.378 40.124  97.388  1.00 92.16  ? 213 ARG D NH2   1 
ATOM   6950 N  N     . ASP D 1 214 ? -12.113 46.938  100.141 1.00 95.75  ? 214 ASP D N     1 
ATOM   6951 C  CA    . ASP D 1 214 ? -13.477 47.449  100.284 1.00 95.90  ? 214 ASP D CA    1 
ATOM   6952 C  C     . ASP D 1 214 ? -13.624 48.954  100.180 1.00 95.49  ? 214 ASP D C     1 
ATOM   6953 O  O     . ASP D 1 214 ? -14.598 49.454  99.616  1.00 94.03  ? 214 ASP D O     1 
ATOM   6954 C  CB    . ASP D 1 214 ? -14.052 46.994  101.620 1.00 96.86  ? 214 ASP D CB    1 
ATOM   6955 C  CG    . ASP D 1 214 ? -14.122 45.492  101.736 1.00 97.96  ? 214 ASP D CG    1 
ATOM   6956 O  OD1   . ASP D 1 214 ? -13.057 44.837  101.684 1.00 98.41  ? 214 ASP D OD1   1 
ATOM   6957 O  OD2   . ASP D 1 214 ? -15.248 44.969  101.875 1.00 99.05  ? 214 ASP D OD2   1 
ATOM   6958 N  N     . PHE D 1 215 ? -12.666 49.677  100.745 1.00 96.00  ? 215 PHE D N     1 
ATOM   6959 C  CA    . PHE D 1 215 ? -12.715 51.126  100.703 1.00 97.51  ? 215 PHE D CA    1 
ATOM   6960 C  C     . PHE D 1 215 ? -12.224 51.652  99.363  1.00 97.29  ? 215 PHE D C     1 
ATOM   6961 O  O     . PHE D 1 215 ? -12.826 52.564  98.795  1.00 97.79  ? 215 PHE D O     1 
ATOM   6962 C  CB    . PHE D 1 215 ? -11.906 51.707  101.865 1.00 99.01  ? 215 PHE D CB    1 
ATOM   6963 C  CG    . PHE D 1 215 ? -12.453 51.321  103.203 1.00 101.30 ? 215 PHE D CG    1 
ATOM   6964 C  CD1   . PHE D 1 215 ? -13.735 51.718  103.577 1.00 102.15 ? 215 PHE D CD1   1 
ATOM   6965 C  CD2   . PHE D 1 215 ? -11.733 50.489  104.055 1.00 102.19 ? 215 PHE D CD2   1 
ATOM   6966 C  CE1   . PHE D 1 215 ? -14.296 51.285  104.775 1.00 102.68 ? 215 PHE D CE1   1 
ATOM   6967 C  CE2   . PHE D 1 215 ? -12.283 50.049  105.258 1.00 102.15 ? 215 PHE D CE2   1 
ATOM   6968 C  CZ    . PHE D 1 215 ? -13.569 50.446  105.617 1.00 102.76 ? 215 PHE D CZ    1 
ATOM   6969 N  N     . VAL D 1 216 ? -11.145 51.070  98.846  1.00 96.11  ? 216 VAL D N     1 
ATOM   6970 C  CA    . VAL D 1 216 ? -10.627 51.503  97.559  1.00 94.17  ? 216 VAL D CA    1 
ATOM   6971 C  C     . VAL D 1 216 ? -11.784 51.411  96.580  1.00 93.51  ? 216 VAL D C     1 
ATOM   6972 O  O     . VAL D 1 216 ? -12.142 52.395  95.943  1.00 93.30  ? 216 VAL D O     1 
ATOM   6973 C  CB    . VAL D 1 216 ? -9.493  50.600  97.067  1.00 93.83  ? 216 VAL D CB    1 
ATOM   6974 C  CG1   . VAL D 1 216 ? -8.844  51.219  95.850  1.00 93.73  ? 216 VAL D CG1   1 
ATOM   6975 C  CG2   . VAL D 1 216 ? -8.470  50.400  98.168  1.00 94.36  ? 216 VAL D CG2   1 
ATOM   6976 N  N     . LEU D 1 217 ? -12.380 50.226  96.485  1.00 93.31  ? 217 LEU D N     1 
ATOM   6977 C  CA    . LEU D 1 217 ? -13.512 50.004  95.588  1.00 93.37  ? 217 LEU D CA    1 
ATOM   6978 C  C     . LEU D 1 217 ? -14.559 51.090  95.805  1.00 94.07  ? 217 LEU D C     1 
ATOM   6979 O  O     . LEU D 1 217 ? -15.226 51.523  94.868  1.00 93.75  ? 217 LEU D O     1 
ATOM   6980 C  CB    . LEU D 1 217 ? -14.141 48.626  95.837  1.00 91.91  ? 217 LEU D CB    1 
ATOM   6981 C  CG    . LEU D 1 217 ? -13.254 47.386  95.723  1.00 90.76  ? 217 LEU D CG    1 
ATOM   6982 C  CD1   . LEU D 1 217 ? -14.099 46.134  95.842  1.00 89.97  ? 217 LEU D CD1   1 
ATOM   6983 C  CD2   . LEU D 1 217 ? -12.540 47.393  94.393  1.00 90.62  ? 217 LEU D CD2   1 
ATOM   6984 N  N     . GLU D 1 218 ? -14.694 51.524  97.052  1.00 95.51  ? 218 GLU D N     1 
ATOM   6985 C  CA    . GLU D 1 218 ? -15.648 52.562  97.415  1.00 96.92  ? 218 GLU D CA    1 
ATOM   6986 C  C     . GLU D 1 218 ? -15.111 53.929  97.011  1.00 96.58  ? 218 GLU D C     1 
ATOM   6987 O  O     . GLU D 1 218 ? -15.841 54.760  96.471  1.00 96.53  ? 218 GLU D O     1 
ATOM   6988 C  CB    . GLU D 1 218 ? -15.898 52.530  98.922  1.00 99.44  ? 218 GLU D CB    1 
ATOM   6989 C  CG    . GLU D 1 218 ? -16.416 53.842  99.494  1.00 102.36 ? 218 GLU D CG    1 
ATOM   6990 C  CD    . GLU D 1 218 ? -16.530 53.818  101.005 1.00 103.38 ? 218 GLU D CD    1 
ATOM   6991 O  OE1   . GLU D 1 218 ? -15.540 53.444  101.675 1.00 103.60 ? 218 GLU D OE1   1 
ATOM   6992 O  OE2   . GLU D 1 218 ? -17.612 54.180  101.517 1.00 104.68 ? 218 GLU D OE2   1 
ATOM   6993 N  N     . LEU D 1 219 ? -13.834 54.155  97.295  1.00 96.12  ? 219 LEU D N     1 
ATOM   6994 C  CA    . LEU D 1 219 ? -13.164 55.403  96.959  1.00 96.26  ? 219 LEU D CA    1 
ATOM   6995 C  C     . LEU D 1 219 ? -13.330 55.669  95.465  1.00 97.14  ? 219 LEU D C     1 
ATOM   6996 O  O     . LEU D 1 219 ? -13.824 56.722  95.062  1.00 96.34  ? 219 LEU D O     1 
ATOM   6997 C  CB    . LEU D 1 219 ? -11.681 55.294  97.325  1.00 95.63  ? 219 LEU D CB    1 
ATOM   6998 C  CG    . LEU D 1 219 ? -10.649 56.317  96.848  1.00 95.23  ? 219 LEU D CG    1 
ATOM   6999 C  CD1   . LEU D 1 219 ? -10.319 56.062  95.396  1.00 95.64  ? 219 LEU D CD1   1 
ATOM   7000 C  CD2   . LEU D 1 219 ? -11.167 57.722  97.060  1.00 95.48  ? 219 LEU D CD2   1 
ATOM   7001 N  N     . ASN D 1 220 ? -12.925 54.691  94.655  1.00 98.15  ? 220 ASN D N     1 
ATOM   7002 C  CA    . ASN D 1 220 ? -13.016 54.787  93.204  1.00 98.20  ? 220 ASN D CA    1 
ATOM   7003 C  C     . ASN D 1 220 ? -14.460 54.923  92.727  1.00 98.86  ? 220 ASN D C     1 
ATOM   7004 O  O     . ASN D 1 220 ? -14.777 55.835  91.970  1.00 99.58  ? 220 ASN D O     1 
ATOM   7005 C  CB    . ASN D 1 220 ? -12.371 53.560  92.542  1.00 98.05  ? 220 ASN D CB    1 
ATOM   7006 C  CG    . ASN D 1 220 ? -10.850 53.512  92.723  1.00 98.52  ? 220 ASN D CG    1 
ATOM   7007 O  OD1   . ASN D 1 220 ? -10.159 54.537  92.644  1.00 97.56  ? 220 ASN D OD1   1 
ATOM   7008 N  ND2   . ASN D 1 220 ? -10.323 52.309  92.940  1.00 97.70  ? 220 ASN D ND2   1 
ATOM   7009 N  N     . LYS D 1 221 ? -15.329 54.018  93.173  1.00 99.82  ? 221 LYS D N     1 
ATOM   7010 C  CA    . LYS D 1 221 ? -16.750 54.020  92.798  1.00 100.41 ? 221 LYS D CA    1 
ATOM   7011 C  C     . LYS D 1 221 ? -17.432 55.373  92.973  1.00 100.90 ? 221 LYS D C     1 
ATOM   7012 O  O     . LYS D 1 221 ? -18.412 55.672  92.291  1.00 100.24 ? 221 LYS D O     1 
ATOM   7013 C  CB    . LYS D 1 221 ? -17.513 52.994  93.634  1.00 100.57 ? 221 LYS D CB    1 
ATOM   7014 C  CG    . LYS D 1 221 ? -18.113 51.845  92.858  1.00 101.71 ? 221 LYS D CG    1 
ATOM   7015 C  CD    . LYS D 1 221 ? -19.212 52.311  91.928  1.00 102.81 ? 221 LYS D CD    1 
ATOM   7016 C  CE    . LYS D 1 221 ? -20.095 51.137  91.500  1.00 103.46 ? 221 LYS D CE    1 
ATOM   7017 N  NZ    . LYS D 1 221 ? -19.321 49.997  90.922  1.00 103.70 ? 221 LYS D NZ    1 
ATOM   7018 N  N     . ALA D 1 222 ? -16.912 56.180  93.896  1.00 101.97 ? 222 ALA D N     1 
ATOM   7019 C  CA    . ALA D 1 222 ? -17.477 57.493  94.192  1.00 102.26 ? 222 ALA D CA    1 
ATOM   7020 C  C     . ALA D 1 222 ? -16.585 58.632  93.732  1.00 102.32 ? 222 ALA D C     1 
ATOM   7021 O  O     . ALA D 1 222 ? -17.074 59.659  93.270  1.00 103.01 ? 222 ALA D O     1 
ATOM   7022 C  CB    . ALA D 1 222 ? -17.737 57.616  95.686  1.00 102.53 ? 222 ALA D CB    1 
ATOM   7023 N  N     . LEU D 1 223 ? -15.278 58.455  93.868  1.00 102.38 ? 223 LEU D N     1 
ATOM   7024 C  CA    . LEU D 1 223 ? -14.328 59.482  93.452  1.00 102.77 ? 223 LEU D CA    1 
ATOM   7025 C  C     . LEU D 1 223 ? -14.472 59.736  91.954  1.00 103.34 ? 223 LEU D C     1 
ATOM   7026 O  O     . LEU D 1 223 ? -13.970 60.727  91.426  1.00 103.60 ? 223 LEU D O     1 
ATOM   7027 C  CB    . LEU D 1 223 ? -12.901 59.032  93.772  1.00 101.72 ? 223 LEU D CB    1 
ATOM   7028 C  CG    . LEU D 1 223 ? -11.754 60.015  93.546  1.00 101.23 ? 223 LEU D CG    1 
ATOM   7029 C  CD1   . LEU D 1 223 ? -12.008 61.318  94.289  1.00 100.67 ? 223 LEU D CD1   1 
ATOM   7030 C  CD2   . LEU D 1 223 ? -10.464 59.371  94.022  1.00 100.94 ? 223 LEU D CD2   1 
ATOM   7031 N  N     . ALA D 1 224 ? -15.173 58.832  91.280  1.00 104.13 ? 224 ALA D N     1 
ATOM   7032 C  CA    . ALA D 1 224 ? -15.401 58.929  89.845  1.00 104.77 ? 224 ALA D CA    1 
ATOM   7033 C  C     . ALA D 1 224 ? -16.853 59.287  89.547  1.00 105.25 ? 224 ALA D C     1 
ATOM   7034 O  O     . ALA D 1 224 ? -17.357 59.002  88.465  1.00 104.98 ? 224 ALA D O     1 
ATOM   7035 C  CB    . ALA D 1 224 ? -15.047 57.607  89.178  1.00 104.61 ? 224 ALA D CB    1 
ATOM   7036 N  N     . VAL D 1 225 ? -17.523 59.907  90.513  1.00 106.23 ? 225 VAL D N     1 
ATOM   7037 C  CA    . VAL D 1 225 ? -18.920 60.297  90.343  1.00 107.10 ? 225 VAL D CA    1 
ATOM   7038 C  C     . VAL D 1 225 ? -19.110 61.742  90.779  1.00 107.86 ? 225 VAL D C     1 
ATOM   7039 O  O     . VAL D 1 225 ? -20.154 62.344  90.537  1.00 107.31 ? 225 VAL D O     1 
ATOM   7040 C  CB    . VAL D 1 225 ? -19.861 59.400  91.180  1.00 106.86 ? 225 VAL D CB    1 
ATOM   7041 C  CG1   . VAL D 1 225 ? -21.313 59.746  90.884  1.00 106.00 ? 225 VAL D CG1   1 
ATOM   7042 C  CG2   . VAL D 1 225 ? -19.584 57.935  90.879  1.00 106.66 ? 225 VAL D CG2   1 
ATOM   7043 N  N     . ASP D 1 226 ? -18.082 62.289  91.418  1.00 109.36 ? 226 ASP D N     1 
ATOM   7044 C  CA    . ASP D 1 226 ? -18.107 63.661  91.907  1.00 111.44 ? 226 ASP D CA    1 
ATOM   7045 C  C     . ASP D 1 226 ? -18.019 64.677  90.772  1.00 112.66 ? 226 ASP D C     1 
ATOM   7046 O  O     . ASP D 1 226 ? -16.974 64.826  90.141  1.00 113.22 ? 226 ASP D O     1 
ATOM   7047 C  CB    . ASP D 1 226 ? -16.955 63.872  92.892  1.00 112.26 ? 226 ASP D CB    1 
ATOM   7048 C  CG    . ASP D 1 226 ? -16.815 65.313  93.321  1.00 113.11 ? 226 ASP D CG    1 
ATOM   7049 O  OD1   . ASP D 1 226 ? -17.846 66.017  93.377  1.00 113.81 ? 226 ASP D OD1   1 
ATOM   7050 O  OD2   . ASP D 1 226 ? -15.678 65.739  93.613  1.00 113.61 ? 226 ASP D OD2   1 
ATOM   7051 N  N     . PRO D 1 227 ? -19.120 65.397  90.504  1.00 113.67 ? 227 PRO D N     1 
ATOM   7052 C  CA    . PRO D 1 227 ? -19.165 66.402  89.436  1.00 114.24 ? 227 PRO D CA    1 
ATOM   7053 C  C     . PRO D 1 227 ? -18.190 67.548  89.643  1.00 114.60 ? 227 PRO D C     1 
ATOM   7054 O  O     . PRO D 1 227 ? -18.232 68.537  88.917  1.00 115.28 ? 227 PRO D O     1 
ATOM   7055 C  CB    . PRO D 1 227 ? -20.615 66.882  89.468  1.00 114.22 ? 227 PRO D CB    1 
ATOM   7056 C  CG    . PRO D 1 227 ? -21.359 65.698  90.001  1.00 114.50 ? 227 PRO D CG    1 
ATOM   7057 C  CD    . PRO D 1 227 ? -20.449 65.239  91.117  1.00 114.26 ? 227 PRO D CD    1 
ATOM   7058 N  N     . ARG D 1 228 ? -17.315 67.419  90.631  1.00 115.08 ? 228 ARG D N     1 
ATOM   7059 C  CA    . ARG D 1 228 ? -16.344 68.469  90.909  1.00 116.27 ? 228 ARG D CA    1 
ATOM   7060 C  C     . ARG D 1 228 ? -14.939 68.103  90.416  1.00 116.57 ? 228 ARG D C     1 
ATOM   7061 O  O     . ARG D 1 228 ? -13.977 68.839  90.656  1.00 116.87 ? 228 ARG D O     1 
ATOM   7062 C  CB    . ARG D 1 228 ? -16.314 68.765  92.413  1.00 117.01 ? 228 ARG D CB    1 
ATOM   7063 C  CG    . ARG D 1 228 ? -17.696 69.013  93.021  1.00 118.35 ? 228 ARG D CG    1 
ATOM   7064 C  CD    . ARG D 1 228 ? -17.618 69.408  94.494  1.00 118.82 ? 228 ARG D CD    1 
ATOM   7065 N  NE    . ARG D 1 228 ? -17.063 70.748  94.675  1.00 119.37 ? 228 ARG D NE    1 
ATOM   7066 C  CZ    . ARG D 1 228 ? -16.807 71.299  95.857  1.00 119.03 ? 228 ARG D CZ    1 
ATOM   7067 N  NH1   . ARG D 1 228 ? -17.055 70.625  96.971  1.00 119.41 ? 228 ARG D NH1   1 
ATOM   7068 N  NH2   . ARG D 1 228 ? -16.304 72.525  95.923  1.00 118.21 ? 228 ARG D NH2   1 
ATOM   7069 N  N     . ILE D 1 229 ? -14.826 66.973  89.721  1.00 116.39 ? 229 ILE D N     1 
ATOM   7070 C  CA    . ILE D 1 229 ? -13.538 66.518  89.204  1.00 115.83 ? 229 ILE D CA    1 
ATOM   7071 C  C     . ILE D 1 229 ? -13.655 65.725  87.899  1.00 116.26 ? 229 ILE D C     1 
ATOM   7072 O  O     . ILE D 1 229 ? -14.723 65.197  87.570  1.00 116.12 ? 229 ILE D O     1 
ATOM   7073 C  CB    . ILE D 1 229 ? -12.797 65.646  90.250  1.00 115.15 ? 229 ILE D CB    1 
ATOM   7074 C  CG1   . ILE D 1 229 ? -13.721 64.537  90.751  1.00 114.77 ? 229 ILE D CG1   1 
ATOM   7075 C  CG2   . ILE D 1 229 ? -12.311 66.507  91.408  1.00 114.19 ? 229 ILE D CG2   1 
ATOM   7076 C  CD1   . ILE D 1 229 ? -13.079 63.621  91.767  1.00 115.04 ? 229 ILE D CD1   1 
ATOM   7077 N  N     . GLU D 1 230 ? -12.546 65.649  87.163  1.00 116.49 ? 230 GLU D N     1 
ATOM   7078 C  CA    . GLU D 1 230 ? -12.497 64.927  85.893  1.00 116.45 ? 230 GLU D CA    1 
ATOM   7079 C  C     . GLU D 1 230 ? -11.837 63.552  86.036  1.00 116.34 ? 230 GLU D C     1 
ATOM   7080 O  O     . GLU D 1 230 ? -12.137 62.633  85.270  1.00 116.72 ? 230 GLU D O     1 
ATOM   7081 C  CB    . GLU D 1 230 ? -11.756 65.765  84.841  1.00 116.77 ? 230 GLU D CB    1 
ATOM   7082 C  CG    . GLU D 1 230 ? -12.489 67.050  84.450  1.00 117.34 ? 230 GLU D CG    1 
ATOM   7083 C  CD    . GLU D 1 230 ? -11.780 67.843  83.360  1.00 117.46 ? 230 GLU D CD    1 
ATOM   7084 O  OE1   . GLU D 1 230 ? -10.602 68.206  83.556  1.00 117.29 ? 230 GLU D OE1   1 
ATOM   7085 O  OE2   . GLU D 1 230 ? -12.405 68.112  82.310  1.00 116.87 ? 230 GLU D OE2   1 
ATOM   7086 N  N     . ILE D 1 231 ? -10.946 63.425  87.019  1.00 115.59 ? 231 ILE D N     1 
ATOM   7087 C  CA    . ILE D 1 231 ? -10.226 62.179  87.320  1.00 114.89 ? 231 ILE D CA    1 
ATOM   7088 C  C     . ILE D 1 231 ? -9.570  61.445  86.146  1.00 114.51 ? 231 ILE D C     1 
ATOM   7089 O  O     . ILE D 1 231 ? -9.801  61.763  84.978  1.00 115.17 ? 231 ILE D O     1 
ATOM   7090 C  CB    . ILE D 1 231 ? -11.129 61.142  88.043  1.00 114.50 ? 231 ILE D CB    1 
ATOM   7091 C  CG1   . ILE D 1 231 ? -12.006 60.409  87.026  1.00 114.08 ? 231 ILE D CG1   1 
ATOM   7092 C  CG2   . ILE D 1 231 ? -11.993 61.834  89.085  1.00 114.37 ? 231 ILE D CG2   1 
ATOM   7093 C  CD1   . ILE D 1 231 ? -12.760 59.247  87.603  1.00 113.34 ? 231 ILE D CD1   1 
ATOM   7094 N  N     . CYS D 1 232 ? -8.755  60.446  86.483  1.00 113.32 ? 232 CYS D N     1 
ATOM   7095 C  CA    . CYS D 1 232 ? -8.047  59.632  85.496  1.00 111.71 ? 232 CYS D CA    1 
ATOM   7096 C  C     . CYS D 1 232 ? -7.180  58.580  86.195  1.00 109.52 ? 232 CYS D C     1 
ATOM   7097 O  O     . CYS D 1 232 ? -6.177  58.911  86.832  1.00 108.39 ? 232 CYS D O     1 
ATOM   7098 C  CB    . CYS D 1 232 ? -7.168  60.521  84.610  1.00 112.78 ? 232 CYS D CB    1 
ATOM   7099 S  SG    . CYS D 1 232 ? -6.327  59.631  83.280  1.00 115.67 ? 232 CYS D SG    1 
ATOM   7100 N  N     . MET D 1 233 ? -7.572  57.314  86.063  1.00 107.44 ? 233 MET D N     1 
ATOM   7101 C  CA    . MET D 1 233 ? -6.855  56.199  86.685  1.00 105.63 ? 233 MET D CA    1 
ATOM   7102 C  C     . MET D 1 233 ? -5.649  55.739  85.873  1.00 103.59 ? 233 MET D C     1 
ATOM   7103 O  O     . MET D 1 233 ? -5.795  55.075  84.846  1.00 103.24 ? 233 MET D O     1 
ATOM   7104 C  CB    . MET D 1 233 ? -7.818  55.029  86.901  1.00 106.84 ? 233 MET D CB    1 
ATOM   7105 C  CG    . MET D 1 233 ? -8.876  55.299  87.964  1.00 107.95 ? 233 MET D CG    1 
ATOM   7106 S  SD    . MET D 1 233 ? -10.212 54.084  88.007  1.00 109.87 ? 233 MET D SD    1 
ATOM   7107 C  CE    . MET D 1 233 ? -9.329  52.623  88.596  1.00 109.17 ? 233 MET D CE    1 
ATOM   7108 N  N     . LEU D 1 234 ? -4.456  56.076  86.353  1.00 101.26 ? 234 LEU D N     1 
ATOM   7109 C  CA    . LEU D 1 234 ? -3.222  55.726  85.656  1.00 99.38  ? 234 LEU D CA    1 
ATOM   7110 C  C     . LEU D 1 234 ? -2.442  54.572  86.271  1.00 97.51  ? 234 LEU D C     1 
ATOM   7111 O  O     . LEU D 1 234 ? -1.878  54.705  87.355  1.00 96.89  ? 234 LEU D O     1 
ATOM   7112 C  CB    . LEU D 1 234 ? -2.306  56.949  85.575  1.00 99.58  ? 234 LEU D CB    1 
ATOM   7113 C  CG    . LEU D 1 234 ? -2.934  58.212  84.983  1.00 99.97  ? 234 LEU D CG    1 
ATOM   7114 C  CD1   . LEU D 1 234 ? -1.902  59.322  84.964  1.00 99.80  ? 234 LEU D CD1   1 
ATOM   7115 C  CD2   . LEU D 1 234 ? -3.457  57.927  83.578  1.00 100.26 ? 234 LEU D CD2   1 
ATOM   7116 N  N     . PRO D 1 235 ? -2.397  53.423  85.576  1.00 95.98  ? 235 PRO D N     1 
ATOM   7117 C  CA    . PRO D 1 235 ? -1.676  52.245  86.059  1.00 95.10  ? 235 PRO D CA    1 
ATOM   7118 C  C     . PRO D 1 235 ? -0.179  52.464  86.246  1.00 94.88  ? 235 PRO D C     1 
ATOM   7119 O  O     . PRO D 1 235 ? 0.635   51.661  85.806  1.00 94.21  ? 235 PRO D O     1 
ATOM   7120 C  CB    . PRO D 1 235 ? -1.999  51.182  85.006  1.00 94.48  ? 235 PRO D CB    1 
ATOM   7121 C  CG    . PRO D 1 235 ? -2.360  51.971  83.797  1.00 94.55  ? 235 PRO D CG    1 
ATOM   7122 C  CD    . PRO D 1 235 ? -3.163  53.094  84.364  1.00 95.23  ? 235 PRO D CD    1 
ATOM   7123 N  N     . VAL D 1 236 ? 0.169   53.562  86.907  1.00 95.72  ? 236 VAL D N     1 
ATOM   7124 C  CA    . VAL D 1 236 ? 1.557   53.908  87.202  1.00 96.80  ? 236 VAL D CA    1 
ATOM   7125 C  C     . VAL D 1 236 ? 1.844   53.392  88.622  1.00 97.50  ? 236 VAL D C     1 
ATOM   7126 O  O     . VAL D 1 236 ? 1.123   53.731  89.560  1.00 97.92  ? 236 VAL D O     1 
ATOM   7127 C  CB    . VAL D 1 236 ? 1.761   55.446  87.185  1.00 96.83  ? 236 VAL D CB    1 
ATOM   7128 C  CG1   . VAL D 1 236 ? 3.243   55.779  87.183  1.00 96.48  ? 236 VAL D CG1   1 
ATOM   7129 C  CG2   . VAL D 1 236 ? 1.059   56.054  85.986  1.00 96.32  ? 236 VAL D CG2   1 
ATOM   7130 N  N     . GLY D 1 237 ? 2.881   52.575  88.784  1.00 98.25  ? 237 GLY D N     1 
ATOM   7131 C  CA    . GLY D 1 237 ? 3.194   52.042  90.104  1.00 99.37  ? 237 GLY D CA    1 
ATOM   7132 C  C     . GLY D 1 237 ? 2.135   51.068  90.608  1.00 99.91  ? 237 GLY D C     1 
ATOM   7133 O  O     . GLY D 1 237 ? 2.126   49.895  90.228  1.00 100.18 ? 237 GLY D O     1 
ATOM   7134 N  N     . ASP D 1 238 ? 1.247   51.537  91.478  1.00 100.24 ? 238 ASP D N     1 
ATOM   7135 C  CA    . ASP D 1 238 ? 0.183   50.684  91.992  1.00 101.00 ? 238 ASP D CA    1 
ATOM   7136 C  C     . ASP D 1 238 ? -1.136  51.385  91.736  1.00 100.73 ? 238 ASP D C     1 
ATOM   7137 O  O     . ASP D 1 238 ? -2.188  50.967  92.215  1.00 100.19 ? 238 ASP D O     1 
ATOM   7138 C  CB    . ASP D 1 238 ? 0.365   50.416  93.491  1.00 102.73 ? 238 ASP D CB    1 
ATOM   7139 C  CG    . ASP D 1 238 ? -0.786  49.606  94.087  1.00 104.29 ? 238 ASP D CG    1 
ATOM   7140 O  OD1   . ASP D 1 238 ? -1.315  48.723  93.376  1.00 104.48 ? 238 ASP D OD1   1 
ATOM   7141 O  OD2   . ASP D 1 238 ? -1.154  49.845  95.265  1.00 104.92 ? 238 ASP D OD2   1 
ATOM   7142 N  N     . GLY D 1 239 ? -1.063  52.460  90.961  1.00 100.76 ? 239 GLY D N     1 
ATOM   7143 C  CA    . GLY D 1 239 ? -2.253  53.216  90.635  1.00 101.03 ? 239 GLY D CA    1 
ATOM   7144 C  C     . GLY D 1 239 ? -2.218  54.597  91.249  1.00 101.66 ? 239 GLY D C     1 
ATOM   7145 O  O     . GLY D 1 239 ? -1.597  54.813  92.290  1.00 101.83 ? 239 GLY D O     1 
ATOM   7146 N  N     . ILE D 1 240 ? -2.878  55.537  90.584  1.00 101.73 ? 240 ILE D N     1 
ATOM   7147 C  CA    . ILE D 1 240 ? -2.963  56.917  91.039  1.00 101.42 ? 240 ILE D CA    1 
ATOM   7148 C  C     . ILE D 1 240 ? -4.096  57.599  90.292  1.00 101.69 ? 240 ILE D C     1 
ATOM   7149 O  O     . ILE D 1 240 ? -3.958  57.932  89.118  1.00 101.69 ? 240 ILE D O     1 
ATOM   7150 C  CB    . ILE D 1 240 ? -1.651  57.704  90.777  1.00 100.66 ? 240 ILE D CB    1 
ATOM   7151 C  CG1   . ILE D 1 240 ? -0.648  57.443  91.901  1.00 100.32 ? 240 ILE D CG1   1 
ATOM   7152 C  CG2   . ILE D 1 240 ? -1.942  59.196  90.683  1.00 100.69 ? 240 ILE D CG2   1 
ATOM   7153 C  CD1   . ILE D 1 240 ? 0.569   58.351  91.873  1.00 99.91  ? 240 ILE D CD1   1 
ATOM   7154 N  N     . THR D 1 241 ? -5.225  57.787  90.965  1.00 102.13 ? 241 THR D N     1 
ATOM   7155 C  CA    . THR D 1 241 ? -6.355  58.452  90.335  1.00 102.90 ? 241 THR D CA    1 
ATOM   7156 C  C     . THR D 1 241 ? -6.117  59.958  90.453  1.00 104.16 ? 241 THR D C     1 
ATOM   7157 O  O     . THR D 1 241 ? -6.133  60.514  91.552  1.00 104.24 ? 241 THR D O     1 
ATOM   7158 C  CB    . THR D 1 241 ? -7.710  58.069  91.009  1.00 101.97 ? 241 THR D CB    1 
ATOM   7159 O  OG1   . THR D 1 241 ? -7.952  56.663  90.854  1.00 100.66 ? 241 THR D OG1   1 
ATOM   7160 C  CG2   . THR D 1 241 ? -8.861  58.833  90.368  1.00 100.40 ? 241 THR D CG2   1 
ATOM   7161 N  N     . ILE D 1 242 ? -5.862  60.599  89.315  1.00 105.26 ? 242 ILE D N     1 
ATOM   7162 C  CA    . ILE D 1 242 ? -5.624  62.036  89.263  1.00 106.50 ? 242 ILE D CA    1 
ATOM   7163 C  C     . ILE D 1 242 ? -6.928  62.745  88.918  1.00 107.35 ? 242 ILE D C     1 
ATOM   7164 O  O     . ILE D 1 242 ? -7.596  62.381  87.958  1.00 107.41 ? 242 ILE D O     1 
ATOM   7165 C  CB    . ILE D 1 242 ? -4.569  62.383  88.195  1.00 106.82 ? 242 ILE D CB    1 
ATOM   7166 C  CG1   . ILE D 1 242 ? -4.898  61.645  86.892  1.00 107.69 ? 242 ILE D CG1   1 
ATOM   7167 C  CG2   . ILE D 1 242 ? -3.178  62.029  88.703  1.00 106.76 ? 242 ILE D CG2   1 
ATOM   7168 C  CD1   . ILE D 1 242 ? -3.993  61.994  85.715  1.00 108.48 ? 242 ILE D CD1   1 
ATOM   7169 N  N     . CYS D 1 243 ? -7.289  63.756  89.701  1.00 108.51 ? 243 CYS D N     1 
ATOM   7170 C  CA    . CYS D 1 243 ? -8.528  64.493  89.469  1.00 109.63 ? 243 CYS D CA    1 
ATOM   7171 C  C     . CYS D 1 243 ? -8.263  65.971  89.195  1.00 110.56 ? 243 CYS D C     1 
ATOM   7172 O  O     . CYS D 1 243 ? -7.142  66.454  89.348  1.00 110.80 ? 243 CYS D O     1 
ATOM   7173 C  CB    . CYS D 1 243 ? -9.440  64.369  90.689  1.00 109.88 ? 243 CYS D CB    1 
ATOM   7174 S  SG    . CYS D 1 243 ? -9.513  62.720  91.400  1.00 109.92 ? 243 CYS D SG    1 
ATOM   7175 N  N     . ARG D 1 244 ? -9.307  66.695  88.807  1.00 111.23 ? 244 ARG D N     1 
ATOM   7176 C  CA    . ARG D 1 244 ? -9.166  68.113  88.515  1.00 112.02 ? 244 ARG D CA    1 
ATOM   7177 C  C     . ARG D 1 244 ? -10.353 68.923  89.041  1.00 112.71 ? 244 ARG D C     1 
ATOM   7178 O  O     . ARG D 1 244 ? -11.510 68.558  88.826  1.00 112.67 ? 244 ARG D O     1 
ATOM   7179 C  CB    . ARG D 1 244 ? -9.009  68.296  87.003  1.00 112.55 ? 244 ARG D CB    1 
ATOM   7180 C  CG    . ARG D 1 244 ? -8.878  69.731  86.533  1.00 112.70 ? 244 ARG D CG    1 
ATOM   7181 C  CD    . ARG D 1 244 ? -8.372  69.786  85.104  1.00 112.15 ? 244 ARG D CD    1 
ATOM   7182 N  NE    . ARG D 1 244 ? -8.733  71.038  84.449  1.00 112.45 ? 244 ARG D NE    1 
ATOM   7183 C  CZ    . ARG D 1 244 ? -9.965  71.347  84.054  1.00 112.42 ? 244 ARG D CZ    1 
ATOM   7184 N  NH1   . ARG D 1 244 ? -10.961 70.494  84.245  1.00 111.91 ? 244 ARG D NH1   1 
ATOM   7185 N  NH2   . ARG D 1 244 ? -10.205 72.512  83.466  1.00 112.61 ? 244 ARG D NH2   1 
ATOM   7186 N  N     . ARG D 1 245 ? -10.055 70.020  89.734  1.00 113.46 ? 245 ARG D N     1 
ATOM   7187 C  CA    . ARG D 1 245 ? -11.085 70.890  90.300  1.00 114.51 ? 245 ARG D CA    1 
ATOM   7188 C  C     . ARG D 1 245 ? -11.791 71.660  89.185  1.00 114.82 ? 245 ARG D C     1 
ATOM   7189 O  O     . ARG D 1 245 ? -11.229 72.597  88.615  1.00 113.78 ? 245 ARG D O     1 
ATOM   7190 C  CB    . ARG D 1 245 ? -10.448 71.879  91.283  1.00 115.41 ? 245 ARG D CB    1 
ATOM   7191 C  CG    . ARG D 1 245 ? -11.255 72.156  92.560  1.00 116.99 ? 245 ARG D CG    1 
ATOM   7192 C  CD    . ARG D 1 245 ? -12.629 72.776  92.287  1.00 117.68 ? 245 ARG D CD    1 
ATOM   7193 N  NE    . ARG D 1 245 ? -13.354 73.079  93.525  1.00 117.60 ? 245 ARG D NE    1 
ATOM   7194 C  CZ    . ARG D 1 245 ? -13.184 74.182  94.251  1.00 116.59 ? 245 ARG D CZ    1 
ATOM   7195 N  NH1   . ARG D 1 245 ? -12.317 75.105  93.867  1.00 115.56 ? 245 ARG D NH1   1 
ATOM   7196 N  NH2   . ARG D 1 245 ? -13.878 74.357  95.367  1.00 116.02 ? 245 ARG D NH2   1 
ATOM   7197 N  N     . ILE D 1 246 ? -13.024 71.264  88.881  1.00 116.05 ? 246 ILE D N     1 
ATOM   7198 C  CA    . ILE D 1 246 ? -13.797 71.915  87.826  1.00 117.28 ? 246 ILE D CA    1 
ATOM   7199 C  C     . ILE D 1 246 ? -14.890 72.821  88.380  1.00 118.73 ? 246 ILE D C     1 
ATOM   7200 O  O     . ILE D 1 246 ? -15.084 73.938  87.895  1.00 118.93 ? 246 ILE D O     1 
ATOM   7201 C  CB    . ILE D 1 246 ? -14.454 70.874  86.868  1.00 116.32 ? 246 ILE D CB    1 
ATOM   7202 C  CG1   . ILE D 1 246 ? -15.683 70.232  87.517  1.00 115.64 ? 246 ILE D CG1   1 
ATOM   7203 C  CG2   . ILE D 1 246 ? -13.449 69.787  86.523  1.00 115.83 ? 246 ILE D CG2   1 
ATOM   7204 C  CD1   . ILE D 1 246 ? -16.456 69.314  86.584  1.00 114.76 ? 246 ILE D CD1   1 
ATOM   7205 N  N     . LYS D 1 247 ? -15.600 72.332  89.393  1.00 120.31 ? 247 LYS D N     1 
ATOM   7206 C  CA    . LYS D 1 247 ? -16.682 73.085  90.018  1.00 121.33 ? 247 LYS D CA    1 
ATOM   7207 C  C     . LYS D 1 247 ? -16.406 73.296  91.507  1.00 122.08 ? 247 LYS D C     1 
ATOM   7208 O  O     . LYS D 1 247 ? -17.260 72.895  92.327  1.00 122.23 ? 247 LYS D O     1 
ATOM   7209 C  CB    . LYS D 1 247 ? -18.014 72.344  89.835  1.00 121.46 ? 247 LYS D CB    1 
ATOM   7210 O  OXT   . LYS D 1 247 ? -15.343 73.864  91.837  1.00 122.31 ? 247 LYS D OXT   1 
HETATM 7211 CA CA    . CA  E 2 .   ? 26.143  41.563  25.775  1.00 59.22  ? 305 CA  A CA    1 
HETATM 7212 N  N     . SAH F 3 .   ? 27.105  36.125  21.561  1.00 69.16  ? 301 SAH A N     1 
HETATM 7213 C  CA    . SAH F 3 .   ? 28.217  37.097  21.905  1.00 65.95  ? 301 SAH A CA    1 
HETATM 7214 C  CB    . SAH F 3 .   ? 27.741  38.540  21.788  1.00 65.61  ? 301 SAH A CB    1 
HETATM 7215 C  CG    . SAH F 3 .   ? 28.547  39.848  22.053  1.00 65.26  ? 301 SAH A CG    1 
HETATM 7216 S  SD    . SAH F 3 .   ? 29.795  40.326  20.764  1.00 64.15  ? 301 SAH A SD    1 
HETATM 7217 C  C     . SAH F 3 .   ? 28.654  36.646  23.340  1.00 64.99  ? 301 SAH A C     1 
HETATM 7218 O  O     . SAH F 3 .   ? 29.894  36.605  23.569  1.00 63.58  ? 301 SAH A O     1 
HETATM 7219 O  OXT   . SAH F 3 .   ? 27.761  36.312  24.168  1.00 62.40  ? 301 SAH A OXT   1 
HETATM 7220 C  "C5'" . SAH F 3 .   ? 28.836  40.350  19.260  1.00 63.09  ? 301 SAH A "C5'" 1 
HETATM 7221 C  "C4'" . SAH F 3 .   ? 29.543  40.629  17.929  1.00 57.25  ? 301 SAH A "C4'" 1 
HETATM 7222 O  "O4'" . SAH F 3 .   ? 28.825  41.485  17.041  1.00 50.98  ? 301 SAH A "O4'" 1 
HETATM 7223 C  "C3'" . SAH F 3 .   ? 30.945  41.279  17.892  1.00 56.16  ? 301 SAH A "C3'" 1 
HETATM 7224 O  "O3'" . SAH F 3 .   ? 31.837  40.323  18.447  1.00 55.90  ? 301 SAH A "O3'" 1 
HETATM 7225 C  "C2'" . SAH F 3 .   ? 31.175  41.491  16.357  1.00 54.34  ? 301 SAH A "C2'" 1 
HETATM 7226 O  "O2'" . SAH F 3 .   ? 32.124  40.782  15.645  1.00 55.65  ? 301 SAH A "O2'" 1 
HETATM 7227 C  "C1'" . SAH F 3 .   ? 29.741  41.481  15.897  1.00 50.81  ? 301 SAH A "C1'" 1 
HETATM 7228 N  N9    . SAH F 3 .   ? 29.224  42.490  14.963  1.00 45.90  ? 301 SAH A N9    1 
HETATM 7229 C  C8    . SAH F 3 .   ? 29.442  43.839  15.018  1.00 44.65  ? 301 SAH A C8    1 
HETATM 7230 N  N7    . SAH F 3 .   ? 28.844  44.430  14.058  1.00 42.47  ? 301 SAH A N7    1 
HETATM 7231 C  C5    . SAH F 3 .   ? 28.218  43.427  13.332  1.00 41.85  ? 301 SAH A C5    1 
HETATM 7232 C  C6    . SAH F 3 .   ? 27.355  43.475  12.135  1.00 41.82  ? 301 SAH A C6    1 
HETATM 7233 N  N6    . SAH F 3 .   ? 27.075  44.605  11.509  1.00 42.59  ? 301 SAH A N6    1 
HETATM 7234 N  N1    . SAH F 3 .   ? 26.926  42.281  11.732  1.00 42.61  ? 301 SAH A N1    1 
HETATM 7235 C  C2    . SAH F 3 .   ? 27.194  41.100  12.350  1.00 43.33  ? 301 SAH A C2    1 
HETATM 7236 N  N3    . SAH F 3 .   ? 27.956  41.020  13.432  1.00 41.70  ? 301 SAH A N3    1 
HETATM 7237 C  C4    . SAH F 3 .   ? 28.405  42.216  13.880  1.00 42.63  ? 301 SAH A C4    1 
HETATM 7238 N  N1A   . FRE G 4 .   ? 40.878  58.449  33.760  1.00 190.66 ? 306 FRE A N1A   1 
HETATM 7239 C  C2A   . FRE G 4 .   ? 40.486  57.890  34.948  1.00 190.71 ? 306 FRE A C2A   1 
HETATM 7240 N  N3A   . FRE G 4 .   ? 40.229  58.472  36.083  1.00 190.70 ? 306 FRE A N3A   1 
HETATM 7241 C  C4A   . FRE G 4 .   ? 40.400  59.808  35.991  1.00 190.56 ? 306 FRE A C4A   1 
HETATM 7242 C  C5A   . FRE G 4 .   ? 40.789  60.520  34.874  1.00 190.58 ? 306 FRE A C5A   1 
HETATM 7243 C  C6A   . FRE G 4 .   ? 41.043  59.798  33.691  1.00 190.63 ? 306 FRE A C6A   1 
HETATM 7244 N  N6A   . FRE G 4 .   ? 41.425  60.342  32.538  1.00 190.54 ? 306 FRE A N6A   1 
HETATM 7245 N  N7A   . FRE G 4 .   ? 40.857  61.871  35.149  1.00 190.45 ? 306 FRE A N7A   1 
HETATM 7246 C  C8A   . FRE G 4 .   ? 40.504  61.948  36.436  1.00 190.32 ? 306 FRE A C8A   1 
HETATM 7247 N  N9A   . FRE G 4 .   ? 40.217  60.739  36.992  1.00 190.32 ? 306 FRE A N9A   1 
HETATM 7248 C  C1B   . FRE G 4 .   ? 39.802  60.431  38.358  1.00 189.91 ? 306 FRE A C1B   1 
HETATM 7249 C  C2B   . FRE G 4 .   ? 39.188  61.620  39.075  1.00 189.69 ? 306 FRE A C2B   1 
HETATM 7250 O  O2B   . FRE G 4 .   ? 39.506  61.597  40.479  1.00 189.64 ? 306 FRE A O2B   1 
HETATM 7251 C  C3B   . FRE G 4 .   ? 37.691  61.438  38.824  1.00 189.46 ? 306 FRE A C3B   1 
HETATM 7252 O  O3B   . FRE G 4 .   ? 36.810  62.060  39.777  1.00 189.56 ? 306 FRE A O3B   1 
HETATM 7253 P  P3B   . FRE G 4 .   ? 36.429  63.604  39.591  1.00 189.65 ? 306 FRE A P3B   1 
HETATM 7254 O  O7A   . FRE G 4 .   ? 35.482  63.757  38.463  1.00 189.56 ? 306 FRE A O7A   1 
HETATM 7255 O  O8A   . FRE G 4 .   ? 37.647  64.394  39.306  1.00 189.66 ? 306 FRE A O8A   1 
HETATM 7256 O  O9A   . FRE G 4 .   ? 35.778  63.933  41.015  1.00 189.51 ? 306 FRE A O9A   1 
HETATM 7257 C  C4B   . FRE G 4 .   ? 37.595  59.923  38.885  1.00 189.08 ? 306 FRE A C4B   1 
HETATM 7258 O  O4B   . FRE G 4 .   ? 38.838  59.446  38.309  1.00 189.52 ? 306 FRE A O4B   1 
HETATM 7259 C  C5B   . FRE G 4 .   ? 36.442  59.301  38.133  1.00 188.14 ? 306 FRE A C5B   1 
HETATM 7260 O  O5B   . FRE G 4 .   ? 36.886  58.119  37.439  1.00 186.82 ? 306 FRE A O5B   1 
HETATM 7261 P  P1A   . FRE G 4 .   ? 35.836  57.300  36.552  1.00 185.96 ? 306 FRE A P1A   1 
HETATM 7262 O  O1A   . FRE G 4 .   ? 36.134  57.492  35.113  1.00 185.77 ? 306 FRE A O1A   1 
HETATM 7263 O  O2A   . FRE G 4 .   ? 34.461  57.776  36.824  1.00 185.83 ? 306 FRE A O2A   1 
HETATM 7264 O  O3A   . FRE G 4 .   ? 36.104  55.807  37.059  1.00 184.63 ? 306 FRE A O3A   1 
HETATM 7265 P  P2A   . FRE G 4 .   ? 35.248  54.456  37.102  1.00 183.21 ? 306 FRE A P2A   1 
HETATM 7266 O  O4A   . FRE G 4 .   ? 33.827  54.763  37.379  1.00 183.21 ? 306 FRE A O4A   1 
HETATM 7267 O  O5A   . FRE G 4 .   ? 35.763  53.565  38.163  1.00 183.07 ? 306 FRE A O5A   1 
HETATM 7268 O  O6A   . FRE G 4 .   ? 35.346  53.757  35.799  1.00 181.57 ? 306 FRE A O6A   1 
HETATM 7269 C  CBP   . FRE G 4 .   ? 36.145  51.787  34.643  1.00 176.88 ? 306 FRE A CBP   1 
HETATM 7270 C  CCP   . FRE G 4 .   ? 36.278  52.675  35.895  1.00 178.56 ? 306 FRE A CCP   1 
HETATM 7271 C  CDP   . FRE G 4 .   ? 34.862  52.149  33.876  1.00 176.86 ? 306 FRE A CDP   1 
HETATM 7272 C  CEP   . FRE G 4 .   ? 37.359  51.997  33.718  1.00 176.85 ? 306 FRE A CEP   1 
HETATM 7273 C  CAP   . FRE G 4 .   ? 36.025  50.289  35.011  1.00 174.77 ? 306 FRE A CAP   1 
HETATM 7274 O  OAP   . FRE G 4 .   ? 36.717  49.654  36.153  1.00 174.56 ? 306 FRE A OAP   1 
HETATM 7275 C  C9P   . FRE G 4 .   ? 35.151  49.179  34.286  1.00 173.55 ? 306 FRE A C9P   1 
HETATM 7276 O  O9P   . FRE G 4 .   ? 34.083  48.766  34.831  1.00 173.41 ? 306 FRE A O9P   1 
HETATM 7277 N  N8P   . FRE G 4 .   ? 35.685  48.756  33.114  1.00 172.26 ? 306 FRE A N8P   1 
HETATM 7278 C  C7P   . FRE G 4 .   ? 34.835  47.666  32.413  1.00 170.72 ? 306 FRE A C7P   1 
HETATM 7279 C  C6P   . FRE G 4 .   ? 33.529  47.451  33.163  1.00 169.20 ? 306 FRE A C6P   1 
HETATM 7280 C  C5P   . FRE G 4 .   ? 32.940  46.083  32.922  1.00 168.03 ? 306 FRE A C5P   1 
HETATM 7281 O  O5P   . FRE G 4 .   ? 32.305  45.695  33.909  1.00 167.85 ? 306 FRE A O5P   1 
HETATM 7282 N  N4P   . FRE G 4 .   ? 33.050  45.340  31.791  1.00 167.06 ? 306 FRE A N4P   1 
HETATM 7283 C  C3P   . FRE G 4 .   ? 31.681  44.907  31.224  1.00 165.84 ? 306 FRE A C3P   1 
HETATM 7284 C  C2P   . FRE G 4 .   ? 30.503  45.863  31.576  1.00 164.73 ? 306 FRE A C2P   1 
HETATM 7285 S  S1P   . FRE G 4 .   ? 29.463  46.014  30.126  1.00 163.46 ? 306 FRE A S1P   1 
HETATM 7286 C  C1    . FRE G 4 .   ? 29.404  45.186  22.591  1.00 159.33 ? 306 FRE A C1    1 
HETATM 7287 C  C2    . FRE G 4 .   ? 30.106  46.312  23.114  1.00 159.44 ? 306 FRE A C2    1 
HETATM 7288 C  C3    . FRE G 4 .   ? 30.210  46.546  24.503  1.00 159.73 ? 306 FRE A C3    1 
HETATM 7289 C  C4    . FRE G 4 .   ? 29.604  45.660  25.420  1.00 160.01 ? 306 FRE A C4    1 
HETATM 7290 C  C5    . FRE G 4 .   ? 28.898  44.532  24.879  1.00 159.70 ? 306 FRE A C5    1 
HETATM 7291 C  C6    . FRE G 4 .   ? 28.780  44.263  23.489  1.00 159.40 ? 306 FRE A C6    1 
HETATM 7292 C  C7    . FRE G 4 .   ? 29.647  45.862  26.915  1.00 160.68 ? 306 FRE A C7    1 
HETATM 7293 C  C8    . FRE G 4 .   ? 30.317  46.867  27.519  1.00 161.78 ? 306 FRE A C8    1 
HETATM 7294 C  C9    . FRE G 4 .   ? 30.343  47.061  28.979  1.00 162.61 ? 306 FRE A C9    1 
HETATM 7295 O  O10   . FRE G 4 .   ? 31.012  48.006  29.400  1.00 162.71 ? 306 FRE A O10   1 
HETATM 7296 O  O11   . FRE G 4 .   ? 30.653  47.134  22.190  0.00 159.59 ? 306 FRE A O11   1 
HETATM 7297 O  O12   . FRE G 4 .   ? 29.322  44.985  21.243  1.00 158.95 ? 306 FRE A O12   1 
HETATM 7298 O  O13   . FRE G 4 .   ? 28.109  43.187  22.952  1.00 159.29 ? 306 FRE A O13   1 
HETATM 7299 C  C13   . FRE G 4 .   ? 26.878  43.253  22.354  1.00 159.26 ? 306 FRE A C13   1 
HETATM 7300 CA CA    . CA  H 2 .   ? 10.227  8.819   -13.068 1.00 63.78  ? 306 CA  B CA    1 
HETATM 7301 N  N     . SAH I 3 .   ? 12.971  13.605  -11.212 1.00 120.08 ? 302 SAH B N     1 
HETATM 7302 C  CA    . SAH I 3 .   ? 12.919  12.373  -12.087 1.00 119.46 ? 302 SAH B CA    1 
HETATM 7303 C  CB    . SAH I 3 .   ? 13.293  12.695  -13.528 1.00 122.05 ? 302 SAH B CB    1 
HETATM 7304 C  CG    . SAH I 3 .   ? 13.356  11.706  -14.713 1.00 125.38 ? 302 SAH B CG    1 
HETATM 7305 S  SD    . SAH I 3 .   ? 12.236  12.181  -16.098 1.00 128.54 ? 302 SAH B SD    1 
HETATM 7306 C  C     . SAH I 3 .   ? 13.898  11.372  -11.389 1.00 117.88 ? 302 SAH B C     1 
HETATM 7307 O  O     . SAH I 3 .   ? 13.452  10.740  -10.386 1.00 116.80 ? 302 SAH B O     1 
HETATM 7308 O  OXT   . SAH I 3 .   ? 15.055  11.240  -11.860 1.00 116.70 ? 302 SAH B OXT   1 
HETATM 7309 C  "C5'" . SAH I 3 .   ? 13.467  12.330  -17.396 1.00 130.07 ? 302 SAH B "C5'" 1 
HETATM 7310 C  "C4'" . SAH I 3 .   ? 13.060  12.769  -18.799 1.00 132.15 ? 302 SAH B "C4'" 1 
HETATM 7311 O  "O4'" . SAH I 3 .   ? 13.829  12.089  -19.809 1.00 133.46 ? 302 SAH B "O4'" 1 
HETATM 7312 C  "C3'" . SAH I 3 .   ? 11.621  12.566  -19.338 1.00 132.74 ? 302 SAH B "C3'" 1 
HETATM 7313 O  "O3'" . SAH I 3 .   ? 10.789  13.474  -18.656 1.00 132.80 ? 302 SAH B "O3'" 1 
HETATM 7314 C  "C2'" . SAH I 3 .   ? 11.799  12.924  -20.847 1.00 133.42 ? 302 SAH B "C2'" 1 
HETATM 7315 O  "O2'" . SAH I 3 .   ? 11.246  14.056  -21.386 1.00 133.47 ? 302 SAH B "O2'" 1 
HETATM 7316 C  "C1'" . SAH I 3 .   ? 13.295  12.633  -21.064 1.00 133.91 ? 302 SAH B "C1'" 1 
HETATM 7317 N  N9    . SAH I 3 .   ? 13.677  11.569  -22.046 1.00 134.51 ? 302 SAH B N9    1 
HETATM 7318 C  C8    . SAH I 3 .   ? 12.745  10.803  -22.733 1.00 134.65 ? 302 SAH B C8    1 
HETATM 7319 N  N7    . SAH I 3 .   ? 13.304  9.969   -23.522 1.00 134.99 ? 302 SAH B N7    1 
HETATM 7320 C  C5    . SAH I 3 .   ? 14.675  10.169  -23.369 1.00 134.98 ? 302 SAH B C5    1 
HETATM 7321 C  C6    . SAH I 3 .   ? 15.820  9.505   -24.023 1.00 134.84 ? 302 SAH B C6    1 
HETATM 7322 N  N6    . SAH I 3 .   ? 15.643  8.545   -24.917 1.00 135.28 ? 302 SAH B N6    1 
HETATM 7323 N  N1    . SAH I 3 .   ? 17.017  9.964   -23.624 1.00 133.83 ? 302 SAH B N1    1 
HETATM 7324 C  C2    . SAH I 3 .   ? 17.212  10.951  -22.709 1.00 133.39 ? 302 SAH B C2    1 
HETATM 7325 N  N3    . SAH I 3 .   ? 16.204  11.584  -22.092 1.00 133.64 ? 302 SAH B N3    1 
HETATM 7326 C  C4    . SAH I 3 .   ? 14.968  11.153  -22.464 1.00 134.42 ? 302 SAH B C4    1 
HETATM 7327 CA CA    . CA  J 2 .   ? 7.480   40.923  48.527  1.00 90.89  ? 307 CA  C CA    1 
HETATM 7328 N  N     . SAH K 3 .   ? 4.108   42.715  44.560  1.00 169.79 ? 303 SAH C N     1 
HETATM 7329 C  CA    . SAH K 3 .   ? 4.352   41.760  45.706  1.00 169.59 ? 303 SAH C CA    1 
HETATM 7330 C  CB    . SAH K 3 .   ? 4.766   42.486  46.972  1.00 171.06 ? 303 SAH C CB    1 
HETATM 7331 C  CG    . SAH K 3 .   ? 5.090   41.826  48.329  1.00 173.50 ? 303 SAH C CG    1 
HETATM 7332 S  SD    . SAH K 3 .   ? 3.651   41.805  49.471  1.00 175.88 ? 303 SAH C SD    1 
HETATM 7333 C  C     . SAH K 3 .   ? 3.012   40.972  45.863  1.00 168.72 ? 303 SAH C C     1 
HETATM 7334 O  O     . SAH K 3 .   ? 3.076   39.705  45.806  1.00 167.84 ? 303 SAH C O     1 
HETATM 7335 O  OXT   . SAH K 3 .   ? 1.951   41.632  46.030  1.00 168.27 ? 303 SAH C OXT   1 
HETATM 7336 C  "C5'" . SAH K 3 .   ? 4.443   41.279  50.990  1.00 177.45 ? 303 SAH C "C5'" 1 
HETATM 7337 C  "C4'" . SAH K 3 .   ? 3.523   41.199  52.185  1.00 179.23 ? 303 SAH C "C4'" 1 
HETATM 7338 O  "O4'" . SAH K 3 .   ? 2.965   39.891  52.449  1.00 180.05 ? 303 SAH C "O4'" 1 
HETATM 7339 C  "C3'" . SAH K 3 .   ? 4.078   41.576  53.570  1.00 179.66 ? 303 SAH C "C3'" 1 
HETATM 7340 O  "O3'" . SAH K 3 .   ? 4.396   42.941  53.529  1.00 178.87 ? 303 SAH C "O3'" 1 
HETATM 7341 C  "C2'" . SAH K 3 .   ? 2.855   41.239  54.486  1.00 180.27 ? 303 SAH C "C2'" 1 
HETATM 7342 O  "O2'" . SAH K 3 .   ? 2.116   42.205  55.126  1.00 180.55 ? 303 SAH C "O2'" 1 
HETATM 7343 C  "C1'" . SAH K 3 .   ? 2.141   40.160  53.652  1.00 180.52 ? 303 SAH C "C1'" 1 
HETATM 7344 N  N9    . SAH K 3 .   ? 2.001   38.815  54.266  1.00 181.05 ? 303 SAH C N9    1 
HETATM 7345 C  C8    . SAH K 3 .   ? 2.560   38.482  55.492  1.00 181.28 ? 303 SAH C C8    1 
HETATM 7346 N  N7    . SAH K 3 .   ? 2.299   37.282  55.823  1.00 181.27 ? 303 SAH C N7    1 
HETATM 7347 C  C5    . SAH K 3 .   ? 1.536   36.776  54.787  1.00 181.07 ? 303 SAH C C5    1 
HETATM 7348 C  C6    . SAH K 3 .   ? 0.937   35.453  54.616  1.00 180.74 ? 303 SAH C C6    1 
HETATM 7349 N  N6    . SAH K 3 .   ? 1.087   34.509  55.524  1.00 180.31 ? 303 SAH C N6    1 
HETATM 7350 N  N1    . SAH K 3 .   ? 0.254   35.314  53.477  1.00 180.73 ? 303 SAH C N1    1 
HETATM 7351 C  C2    . SAH K 3 .   ? 0.092   36.284  52.535  1.00 181.17 ? 303 SAH C C2    1 
HETATM 7352 N  N3    . SAH K 3 .   ? 0.614   37.508  52.648  1.00 181.13 ? 303 SAH C N3    1 
HETATM 7353 C  C4    . SAH K 3 .   ? 1.314   37.690  53.792  1.00 181.17 ? 303 SAH C C4    1 
HETATM 7354 CA CA    . CA  L 2 .   ? 2.422   54.474  97.568  1.00 88.51  ? 308 CA  D CA    1 
HETATM 7355 N  N     . SAH M 3 .   ? 3.722   58.467  99.973  1.00 144.50 ? 304 SAH D N     1 
HETATM 7356 C  CA    . SAH M 3 .   ? 4.367   57.278  100.656 1.00 144.22 ? 304 SAH D CA    1 
HETATM 7357 C  CB    . SAH M 3 .   ? 3.337   56.208  101.022 1.00 144.62 ? 304 SAH D CB    1 
HETATM 7358 C  CG    . SAH M 3 .   ? 3.635   54.862  101.723 1.00 144.97 ? 304 SAH D CG    1 
HETATM 7359 S  SD    . SAH M 3 .   ? 2.892   54.656  103.414 1.00 145.47 ? 304 SAH D SD    1 
HETATM 7360 C  C     . SAH M 3 .   ? 5.473   56.781  99.650  1.00 143.86 ? 304 SAH D C     1 
HETATM 7361 O  O     . SAH M 3 .   ? 6.684   57.089  99.915  1.00 142.91 ? 304 SAH D O     1 
HETATM 7362 O  OXT   . SAH M 3 .   ? 5.106   56.115  98.640  1.00 143.76 ? 304 SAH D OXT   1 
HETATM 7363 C  "C5'" . SAH M 3 .   ? 3.266   56.251  104.135 1.00 144.54 ? 304 SAH D "C5'" 1 
HETATM 7364 C  "C4'" . SAH M 3 .   ? 2.849   56.497  105.567 1.00 143.30 ? 304 SAH D "C4'" 1 
HETATM 7365 O  "O4'" . SAH M 3 .   ? 1.533   57.062  105.720 1.00 142.27 ? 304 SAH D "O4'" 1 
HETATM 7366 C  "C3'" . SAH M 3 .   ? 2.799   55.316  106.549 1.00 142.88 ? 304 SAH D "C3'" 1 
HETATM 7367 O  "O3'" . SAH M 3 .   ? 4.127   54.873  106.723 1.00 142.72 ? 304 SAH D "O3'" 1 
HETATM 7368 C  "C2'" . SAH M 3 .   ? 2.185   56.002  107.816 1.00 142.42 ? 304 SAH D "C2'" 1 
HETATM 7369 O  "O2'" . SAH M 3 .   ? 2.917   56.206  108.958 1.00 143.22 ? 304 SAH D "O2'" 1 
HETATM 7370 C  "C1'" . SAH M 3 .   ? 1.413   57.175  107.187 1.00 141.49 ? 304 SAH D "C1'" 1 
HETATM 7371 N  N9    . SAH M 3 .   ? -0.048  57.190  107.382 1.00 140.37 ? 304 SAH D N9    1 
HETATM 7372 C  C8    . SAH M 3 .   ? -0.864  56.120  107.071 1.00 140.31 ? 304 SAH D C8    1 
HETATM 7373 N  N7    . SAH M 3 .   ? -2.086  56.370  107.331 1.00 139.95 ? 304 SAH D N7    1 
HETATM 7374 C  C5    . SAH M 3 .   ? -2.100  57.657  107.838 1.00 139.68 ? 304 SAH D C5    1 
HETATM 7375 C  C6    . SAH M 3 .   ? -3.216  58.478  108.309 1.00 139.37 ? 304 SAH D C6    1 
HETATM 7376 N  N6    . SAH M 3 .   ? -4.453  58.018  108.295 1.00 139.03 ? 304 SAH D N6    1 
HETATM 7377 N  N1    . SAH M 3 .   ? -2.853  59.695  108.737 1.00 139.08 ? 304 SAH D N1    1 
HETATM 7378 C  C2    . SAH M 3 .   ? -1.577  60.173  108.755 1.00 139.33 ? 304 SAH D C2    1 
HETATM 7379 N  N3    . SAH M 3 .   ? -0.529  59.456  108.335 1.00 139.36 ? 304 SAH D N3    1 
HETATM 7380 C  C4    . SAH M 3 .   ? -0.856  58.218  107.891 1.00 139.78 ? 304 SAH D C4    1 
HETATM 7381 O  O     . HOH N 5 .   ? 31.181  34.558  24.391  1.00 57.68  ? 307 HOH A O     1 
HETATM 7382 O  O     . HOH N 5 .   ? 29.143  43.897  18.674  1.00 92.11  ? 308 HOH A O     1 
HETATM 7383 O  O     . HOH N 5 .   ? 39.812  60.120  23.579  1.00 54.11  ? 309 HOH A O     1 
HETATM 7384 O  O     . HOH N 5 .   ? 33.404  38.316  16.612  1.00 57.90  ? 310 HOH A O     1 
HETATM 7385 O  O     . HOH N 5 .   ? 16.256  31.876  5.585   1.00 51.85  ? 311 HOH A O     1 
HETATM 7386 O  O     . HOH N 5 .   ? 3.804   43.314  7.587   1.00 60.96  ? 312 HOH A O     1 
HETATM 7387 O  O     . HOH N 5 .   ? 7.578   48.851  13.966  1.00 59.60  ? 313 HOH A O     1 
HETATM 7388 O  O     . HOH N 5 .   ? 15.754  32.656  2.328   1.00 55.11  ? 314 HOH A O     1 
HETATM 7389 O  O     . HOH N 5 .   ? 19.692  18.613  22.365  1.00 39.67  ? 315 HOH A O     1 
HETATM 7390 O  O     . HOH N 5 .   ? 27.876  50.182  12.952  1.00 61.90  ? 316 HOH A O     1 
HETATM 7391 O  O     . HOH N 5 .   ? 19.655  32.689  19.601  1.00 41.73  ? 317 HOH A O     1 
HETATM 7392 O  O     . HOH N 5 .   ? 25.689  47.615  8.915   1.00 45.89  ? 318 HOH A O     1 
HETATM 7393 O  O     . HOH N 5 .   ? 23.632  42.412  28.531  1.00 47.14  ? 319 HOH A O     1 
HETATM 7394 O  O     . HOH N 5 .   ? 15.300  16.509  21.854  1.00 66.23  ? 320 HOH A O     1 
HETATM 7395 O  O     . HOH N 5 .   ? 38.522  42.589  29.993  1.00 57.27  ? 321 HOH A O     1 
HETATM 7396 O  O     . HOH N 5 .   ? 38.011  59.762  26.696  1.00 82.39  ? 322 HOH A O     1 
HETATM 7397 O  O     . HOH N 5 .   ? 22.782  26.079  32.159  1.00 65.00  ? 323 HOH A O     1 
HETATM 7398 O  O     . HOH N 5 .   ? 1.056   41.690  7.519   1.00 56.67  ? 324 HOH A O     1 
HETATM 7399 O  O     . HOH N 5 .   ? 16.967  21.021  25.888  1.00 69.68  ? 325 HOH A O     1 
HETATM 7400 O  O     . HOH O 5 .   ? -5.191  7.083   -3.205  1.00 56.86  ? 307 HOH B O     1 
HETATM 7401 O  O     . HOH O 5 .   ? 17.642  6.794   -26.075 1.00 45.22  ? 308 HOH B O     1 
HETATM 7402 O  O     . HOH O 5 .   ? 16.953  12.927  2.716   1.00 35.36  ? 309 HOH B O     1 
HETATM 7403 O  O     . HOH O 5 .   ? -2.918  8.458   -15.873 1.00 29.92  ? 310 HOH B O     1 
HETATM 7404 O  O     . HOH O 5 .   ? 9.906   8.237   -10.702 1.00 45.60  ? 311 HOH B O     1 
HETATM 7405 O  O     . HOH O 5 .   ? 6.176   13.034  -2.962  1.00 45.25  ? 312 HOH B O     1 
HETATM 7406 O  O     . HOH O 5 .   ? 18.441  15.974  1.031   1.00 46.78  ? 313 HOH B O     1 
HETATM 7407 O  O     . HOH O 5 .   ? 22.119  -9.554  -3.388  1.00 56.77  ? 314 HOH B O     1 
HETATM 7408 O  O     . HOH O 5 .   ? 2.985   12.218  10.214  1.00 45.27  ? 315 HOH B O     1 
HETATM 7409 O  O     . HOH O 5 .   ? -2.831  -3.407  3.735   1.00 64.80  ? 316 HOH B O     1 
HETATM 7410 O  O     . HOH O 5 .   ? 0.224   11.202  8.299   1.00 38.59  ? 317 HOH B O     1 
HETATM 7411 O  O     . HOH O 5 .   ? 14.887  21.044  -26.353 1.00 54.69  ? 318 HOH B O     1 
HETATM 7412 O  O     . HOH O 5 .   ? 7.306   16.616  -19.994 1.00 54.21  ? 319 HOH B O     1 
HETATM 7413 O  O     . HOH O 5 .   ? 6.570   9.014   14.723  1.00 43.01  ? 320 HOH B O     1 
HETATM 7414 O  O     . HOH O 5 .   ? 34.385  -4.966  -17.193 1.00 40.06  ? 321 HOH B O     1 
HETATM 7415 O  O     . HOH O 5 .   ? 9.712   21.330  -24.043 1.00 52.46  ? 322 HOH B O     1 
HETATM 7416 O  O     . HOH O 5 .   ? -7.561  4.998   5.227   1.00 58.18  ? 323 HOH B O     1 
HETATM 7417 O  O     . HOH O 5 .   ? 30.755  17.166  -23.239 1.00 54.66  ? 324 HOH B O     1 
HETATM 7418 O  O     . HOH O 5 .   ? 8.634   5.165   0.832   1.00 55.37  ? 325 HOH B O     1 
HETATM 7419 O  O     . HOH O 5 .   ? 35.044  4.552   -6.742  1.00 56.20  ? 326 HOH B O     1 
HETATM 7420 O  O     . HOH O 5 .   ? 25.881  15.695  1.546   1.00 60.58  ? 327 HOH B O     1 
HETATM 7421 O  O     . HOH O 5 .   ? -5.033  10.959  3.717   1.00 42.83  ? 328 HOH B O     1 
HETATM 7422 O  O     . HOH O 5 .   ? 18.060  -16.338 -13.251 1.00 59.29  ? 329 HOH B O     1 
HETATM 7423 O  O     . HOH O 5 .   ? -15.211 0.271   -17.130 1.00 71.25  ? 330 HOH B O     1 
HETATM 7424 O  O     . HOH O 5 .   ? 31.740  14.492  3.857   1.00 58.20  ? 331 HOH B O     1 
HETATM 7425 O  O     . HOH O 5 .   ? 29.649  26.059  -2.091  1.00 64.27  ? 332 HOH B O     1 
HETATM 7426 O  O     . HOH O 5 .   ? 1.368   8.041   -9.696  1.00 50.27  ? 333 HOH B O     1 
HETATM 7427 O  O     . HOH O 5 .   ? 27.985  17.370  -24.953 1.00 53.22  ? 334 HOH B O     1 
HETATM 7428 O  O     . HOH O 5 .   ? -7.186  0.448   -22.242 1.00 69.62  ? 335 HOH B O     1 
HETATM 7429 O  O     . HOH O 5 .   ? 31.544  9.184   -24.216 1.00 48.95  ? 336 HOH B O     1 
HETATM 7430 O  O     . HOH O 5 .   ? 40.990  11.429  -3.324  1.00 63.00  ? 337 HOH B O     1 
HETATM 7431 O  O     . HOH P 5 .   ? 4.411   46.731  32.179  1.00 37.73  ? 308 HOH C O     1 
HETATM 7432 O  O     . HOH P 5 .   ? -0.444  42.759  32.742  1.00 50.43  ? 309 HOH C O     1 
HETATM 7433 O  O     . HOH P 5 .   ? -7.092  17.950  40.259  1.00 72.97  ? 310 HOH C O     1 
HETATM 7434 O  O     . HOH P 5 .   ? 11.196  28.563  53.831  1.00 67.35  ? 311 HOH C O     1 
HETATM 7435 O  O     . HOH P 5 .   ? 5.004   11.371  46.435  1.00 56.09  ? 312 HOH C O     1 
HETATM 7436 O  O     . HOH P 5 .   ? 2.827   45.732  47.080  1.00 51.11  ? 313 HOH C O     1 
HETATM 7437 O  O     . HOH P 5 .   ? 12.942  24.334  60.069  1.00 73.72  ? 314 HOH C O     1 
HETATM 7438 O  O     . HOH P 5 .   ? -6.795  39.044  59.654  1.00 68.85  ? 315 HOH C O     1 
HETATM 7439 O  O     . HOH P 5 .   ? -13.133 30.962  40.015  1.00 66.42  ? 316 HOH C O     1 
HETATM 7440 O  O     . HOH P 5 .   ? -10.578 30.874  23.520  1.00 71.37  ? 317 HOH C O     1 
HETATM 7441 O  O     . HOH P 5 .   ? 28.395  30.939  49.172  1.00 82.36  ? 318 HOH C O     1 
HETATM 7442 O  O     . HOH Q 5 .   ? -10.832 87.792  102.166 1.00 53.46  ? 309 HOH D O     1 
HETATM 7443 O  O     . HOH Q 5 .   ? 6.287   73.434  91.215  1.00 64.38  ? 310 HOH D O     1 
HETATM 7444 O  O     . HOH Q 5 .   ? 14.707  59.591  83.661  1.00 98.03  ? 311 HOH D O     1 
HETATM 7445 O  O     . HOH Q 5 .   ? 15.275  56.508  91.830  1.00 84.14  ? 312 HOH D O     1 
HETATM 7446 O  O     . HOH Q 5 .   ? -4.532  81.921  107.797 1.00 72.58  ? 313 HOH D O     1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   THR 3   3   ?   ?   ?   A . n 
A 1 4   ASN 4   4   ?   ?   ?   A . n 
A 1 5   GLU 5   5   ?   ?   ?   A . n 
A 1 6   ASP 6   6   ?   ?   ?   A . n 
A 1 7   GLN 7   7   ?   ?   ?   A . n 
A 1 8   LYS 8   8   ?   ?   ?   A . n 
A 1 9   GLN 9   9   ?   ?   ?   A . n 
A 1 10  THR 10  10  ?   ?   ?   A . n 
A 1 11  GLU 11  11  ?   ?   ?   A . n 
A 1 12  SER 12  12  ?   ?   ?   A . n 
A 1 13  GLY 13  13  ?   ?   ?   A . n 
A 1 14  ARG 14  14  ?   ?   ?   A . n 
A 1 15  HIS 15  15  ?   ?   ?   A . n 
A 1 16  GLN 16  16  ?   ?   ?   A . n 
A 1 17  GLU 17  17  ?   ?   ?   A . n 
A 1 18  VAL 18  18  ?   ?   ?   A . n 
A 1 19  GLY 19  19  ?   ?   ?   A . n 
A 1 20  HIS 20  20  ?   ?   ?   A . n 
A 1 21  LYS 21  21  21  LYS LYS A . n 
A 1 22  SER 22  22  22  SER SER A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  TYR 30  30  30  TYR TYR A . n 
A 1 31  GLN 31  31  31  GLN GLN A . n 
A 1 32  TYR 32  32  32  TYR TYR A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  SER 37  37  37  SER SER A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  PHE 39  39  39  PHE PHE A . n 
A 1 40  PRO 40  40  40  PRO PRO A . n 
A 1 41  ARG 41  41  41  ARG ARG A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  MET 46  46  46  MET MET A . n 
A 1 47  LYS 47  47  47  LYS LYS A . n 
A 1 48  GLU 48  48  48  GLU GLU A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  ARG 50  50  50  ARG ARG A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  THR 53  53  53  THR THR A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  HIS 56  56  56  HIS HIS A . n 
A 1 57  PRO 57  57  57  PRO PRO A . n 
A 1 58  TRP 58  58  58  TRP TRP A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ILE 60  60  60  ILE ILE A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  SER 64  64  64  SER SER A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  MET 73  73  73  MET MET A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  ASN 79  79  79  ASN ASN A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  LYS 81  81  81  LYS LYS A . n 
A 1 82  ASN 82  82  82  ASN ASN A . n 
A 1 83  THR 83  83  83  THR THR A . n 
A 1 84  MET 84  84  84  MET MET A . n 
A 1 85  GLU 85  85  85  GLU GLU A . n 
A 1 86  ILE 86  86  86  ILE ILE A . n 
A 1 87  GLY 87  87  87  GLY GLY A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  TYR 89  89  89  TYR TYR A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  GLY 91  91  91  GLY GLY A . n 
A 1 92  TYR 92  92  92  TYR TYR A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 ALA 100 100 100 ALA ALA A . n 
A 1 101 ILE 101 101 101 ILE ILE A . n 
A 1 102 PRO 102 102 102 PRO PRO A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 LYS 106 106 106 LYS LYS A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 MET 110 110 110 MET MET A . n 
A 1 111 ASP 111 111 111 ASP ASP A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ASN 113 113 113 ASN ASN A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 ASN 116 116 116 ASN ASN A . n 
A 1 117 TYR 117 117 117 TYR TYR A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 LYS 125 125 125 LYS LYS A . n 
A 1 126 LYS 126 126 126 LYS LYS A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 ASP 130 130 130 ASP ASP A . n 
A 1 131 HIS 131 131 131 HIS HIS A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 ILE 133 133 133 ILE ILE A . n 
A 1 134 ASP 134 134 134 ASP ASP A . n 
A 1 135 PHE 135 135 135 PHE PHE A . n 
A 1 136 ARG 136 136 136 ARG ARG A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 PRO 139 139 139 PRO PRO A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 PRO 142 142 142 PRO PRO A . n 
A 1 143 VAL 143 143 143 VAL VAL A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 MET 147 147 147 MET MET A . n 
A 1 148 ILE 148 148 148 ILE ILE A . n 
A 1 149 LYS 149 149 149 LYS LYS A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 GLU 151 151 151 GLU GLU A . n 
A 1 152 LYS 152 152 152 LYS LYS A . n 
A 1 153 ASN 153 153 153 ASN ASN A . n 
A 1 154 HIS 154 154 154 HIS HIS A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 TYR 157 157 157 TYR TYR A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 ILE 160 160 160 ILE ILE A . n 
A 1 161 PHE 161 161 161 PHE PHE A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 ASP 163 163 163 ASP ASP A . n 
A 1 164 ALA 164 164 164 ALA ALA A . n 
A 1 165 ASP 165 165 165 ASP ASP A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 ASP 167 167 167 ASP ASP A . n 
A 1 168 ASN 168 168 168 ASN ASN A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 ASN 171 171 171 ASN ASN A . n 
A 1 172 TYR 172 172 172 TYR TYR A . n 
A 1 173 HIS 173 173 173 HIS HIS A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 ARG 175 175 175 ARG ARG A . n 
A 1 176 LEU 176 176 176 LEU LEU A . n 
A 1 177 ILE 177 177 177 ILE ILE A . n 
A 1 178 ASP 178 178 178 ASP ASP A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 VAL 180 180 180 VAL VAL A . n 
A 1 181 LYS 181 181 181 LYS LYS A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 GLY 184 184 184 GLY GLY A . n 
A 1 185 VAL 185 185 185 VAL VAL A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 TYR 188 188 188 TYR TYR A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 ASN 190 190 190 ASN ASN A . n 
A 1 191 THR 191 191 191 THR THR A . n 
A 1 192 LEU 192 192 192 LEU LEU A . n 
A 1 193 TRP 193 193 193 TRP TRP A . n 
A 1 194 ASN 194 194 194 ASN ASN A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 VAL 198 198 198 VAL VAL A . n 
A 1 199 ALA 199 199 199 ALA ALA A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 ASP 202 202 202 ASP ASP A . n 
A 1 203 ALA 203 203 203 ALA ALA A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ARG 206 206 206 ARG ARG A . n 
A 1 207 LYS 207 207 207 LYS LYS A . n 
A 1 208 TYR 208 208 208 TYR TYR A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 ARG 210 210 210 ARG ARG A . n 
A 1 211 TYR 211 211 211 TYR TYR A . n 
A 1 212 TYR 212 212 212 TYR TYR A . n 
A 1 213 ARG 213 213 213 ARG ARG A . n 
A 1 214 ASP 214 214 214 ASP ASP A . n 
A 1 215 PHE 215 215 215 PHE PHE A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 GLU 218 218 218 GLU GLU A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 ASN 220 220 220 ASN ASN A . n 
A 1 221 LYS 221 221 221 LYS LYS A . n 
A 1 222 ALA 222 222 222 ALA ALA A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 ASP 226 226 226 ASP ASP A . n 
A 1 227 PRO 227 227 227 PRO PRO A . n 
A 1 228 ARG 228 228 228 ARG ARG A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 GLU 230 230 230 GLU GLU A . n 
A 1 231 ILE 231 231 231 ILE ILE A . n 
A 1 232 CYS 232 232 232 CYS CYS A . n 
A 1 233 MET 233 233 233 MET MET A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 PRO 235 235 235 PRO PRO A . n 
A 1 236 VAL 236 236 236 VAL VAL A . n 
A 1 237 GLY 237 237 237 GLY GLY A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 ILE 240 240 240 ILE ILE A . n 
A 1 241 THR 241 241 241 THR THR A . n 
A 1 242 ILE 242 242 242 ILE ILE A . n 
A 1 243 CYS 243 243 243 CYS CYS A . n 
A 1 244 ARG 244 244 244 ARG ARG A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 ILE 246 246 246 ILE ILE A . n 
A 1 247 LYS 247 247 247 LYS LYS A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ALA 2   2   ?   ?   ?   B . n 
B 1 3   THR 3   3   ?   ?   ?   B . n 
B 1 4   ASN 4   4   ?   ?   ?   B . n 
B 1 5   GLU 5   5   ?   ?   ?   B . n 
B 1 6   ASP 6   6   ?   ?   ?   B . n 
B 1 7   GLN 7   7   ?   ?   ?   B . n 
B 1 8   LYS 8   8   ?   ?   ?   B . n 
B 1 9   GLN 9   9   ?   ?   ?   B . n 
B 1 10  THR 10  10  ?   ?   ?   B . n 
B 1 11  GLU 11  11  ?   ?   ?   B . n 
B 1 12  SER 12  12  ?   ?   ?   B . n 
B 1 13  GLY 13  13  ?   ?   ?   B . n 
B 1 14  ARG 14  14  ?   ?   ?   B . n 
B 1 15  HIS 15  15  ?   ?   ?   B . n 
B 1 16  GLN 16  16  ?   ?   ?   B . n 
B 1 17  GLU 17  17  ?   ?   ?   B . n 
B 1 18  VAL 18  18  ?   ?   ?   B . n 
B 1 19  GLY 19  19  ?   ?   ?   B . n 
B 1 20  HIS 20  20  ?   ?   ?   B . n 
B 1 21  LYS 21  21  21  LYS LYS B . n 
B 1 22  SER 22  22  22  SER SER B . n 
B 1 23  LEU 23  23  23  LEU LEU B . n 
B 1 24  LEU 24  24  24  LEU LEU B . n 
B 1 25  GLN 25  25  25  GLN GLN B . n 
B 1 26  SER 26  26  26  SER SER B . n 
B 1 27  ASP 27  27  27  ASP ASP B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  LEU 29  29  29  LEU LEU B . n 
B 1 30  TYR 30  30  30  TYR TYR B . n 
B 1 31  GLN 31  31  31  GLN GLN B . n 
B 1 32  TYR 32  32  32  TYR TYR B . n 
B 1 33  ILE 33  33  33  ILE ILE B . n 
B 1 34  LEU 34  34  34  LEU LEU B . n 
B 1 35  GLU 35  35  35  GLU GLU B . n 
B 1 36  THR 36  36  36  THR THR B . n 
B 1 37  SER 37  37  37  SER SER B . n 
B 1 38  VAL 38  38  38  VAL VAL B . n 
B 1 39  PHE 39  39  39  PHE PHE B . n 
B 1 40  PRO 40  40  40  PRO PRO B . n 
B 1 41  ARG 41  41  41  ARG ARG B . n 
B 1 42  GLU 42  42  42  GLU GLU B . n 
B 1 43  HIS 43  43  43  HIS HIS B . n 
B 1 44  GLU 44  44  44  GLU GLU B . n 
B 1 45  ALA 45  45  45  ALA ALA B . n 
B 1 46  MET 46  46  46  MET MET B . n 
B 1 47  LYS 47  47  47  LYS LYS B . n 
B 1 48  GLU 48  48  48  GLU GLU B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  ARG 50  50  50  ARG ARG B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  VAL 52  52  52  VAL VAL B . n 
B 1 53  THR 53  53  53  THR THR B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  HIS 56  56  56  HIS HIS B . n 
B 1 57  PRO 57  57  57  PRO PRO B . n 
B 1 58  TRP 58  58  58  TRP TRP B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ILE 60  60  60  ILE ILE B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  THR 62  62  62  THR THR B . n 
B 1 63  THR 63  63  63  THR THR B . n 
B 1 64  SER 64  64  64  SER SER B . n 
B 1 65  ALA 65  65  65  ALA ALA B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  GLU 67  67  67  GLU GLU B . n 
B 1 68  GLY 68  68  68  GLY GLY B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  PHE 70  70  70  PHE PHE B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  MET 73  73  73  MET MET B . n 
B 1 74  LEU 74  74  74  LEU LEU B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  LEU 77  77  77  LEU LEU B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  ASN 79  79  79  ASN ASN B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  LYS 81  81  81  LYS LYS B . n 
B 1 82  ASN 82  82  82  ASN ASN B . n 
B 1 83  THR 83  83  83  THR THR B . n 
B 1 84  MET 84  84  84  MET MET B . n 
B 1 85  GLU 85  85  85  GLU GLU B . n 
B 1 86  ILE 86  86  86  ILE ILE B . n 
B 1 87  GLY 87  87  87  GLY GLY B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  TYR 89  89  89  TYR TYR B . n 
B 1 90  THR 90  90  90  THR THR B . n 
B 1 91  GLY 91  91  91  GLY GLY B . n 
B 1 92  TYR 92  92  92  TYR TYR B . n 
B 1 93  SER 93  93  93  SER SER B . n 
B 1 94  LEU 94  94  94  LEU LEU B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  ALA 96  96  96  ALA ALA B . n 
B 1 97  THR 97  97  97  THR THR B . n 
B 1 98  ALA 98  98  98  ALA ALA B . n 
B 1 99  LEU 99  99  99  LEU LEU B . n 
B 1 100 ALA 100 100 100 ALA ALA B . n 
B 1 101 ILE 101 101 101 ILE ILE B . n 
B 1 102 PRO 102 102 102 PRO PRO B . n 
B 1 103 GLU 103 103 103 GLU GLU B . n 
B 1 104 ASP 104 104 104 ASP ASP B . n 
B 1 105 GLY 105 105 105 GLY GLY B . n 
B 1 106 LYS 106 106 106 LYS LYS B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 MET 110 110 110 MET MET B . n 
B 1 111 ASP 111 111 111 ASP ASP B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 ASN 113 113 113 ASN ASN B . n 
B 1 114 LYS 114 114 114 LYS LYS B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 ASN 116 116 116 ASN ASN B . n 
B 1 117 TYR 117 117 117 TYR TYR B . n 
B 1 118 GLU 118 118 118 GLU GLU B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 LEU 121 121 121 LEU LEU B . n 
B 1 122 PRO 122 122 122 PRO PRO B . n 
B 1 123 VAL 123 123 123 VAL VAL B . n 
B 1 124 ILE 124 124 124 ILE ILE B . n 
B 1 125 LYS 125 125 125 LYS LYS B . n 
B 1 126 LYS 126 126 126 LYS LYS B . n 
B 1 127 ALA 127 127 127 ALA ALA B . n 
B 1 128 GLY 128 128 128 GLY GLY B . n 
B 1 129 VAL 129 129 129 VAL VAL B . n 
B 1 130 ASP 130 130 130 ASP ASP B . n 
B 1 131 HIS 131 131 131 HIS HIS B . n 
B 1 132 LYS 132 132 132 LYS LYS B . n 
B 1 133 ILE 133 133 133 ILE ILE B . n 
B 1 134 ASP 134 134 134 ASP ASP B . n 
B 1 135 PHE 135 135 135 PHE PHE B . n 
B 1 136 ARG 136 136 136 ARG ARG B . n 
B 1 137 GLU 137 137 137 GLU GLU B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 PRO 139 139 139 PRO PRO B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 PRO 142 142 142 PRO PRO B . n 
B 1 143 VAL 143 143 143 VAL VAL B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 GLU 146 146 146 GLU GLU B . n 
B 1 147 MET 147 147 147 MET MET B . n 
B 1 148 ILE 148 148 148 ILE ILE B . n 
B 1 149 LYS 149 149 149 LYS LYS B . n 
B 1 150 ASP 150 150 150 ASP ASP B . n 
B 1 151 GLU 151 151 151 GLU GLU B . n 
B 1 152 LYS 152 152 152 LYS LYS B . n 
B 1 153 ASN 153 153 153 ASN ASN B . n 
B 1 154 HIS 154 154 154 HIS HIS B . n 
B 1 155 GLY 155 155 155 GLY GLY B . n 
B 1 156 SER 156 156 156 SER SER B . n 
B 1 157 TYR 157 157 157 TYR TYR B . n 
B 1 158 ASP 158 158 158 ASP ASP B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 ILE 160 160 160 ILE ILE B . n 
B 1 161 PHE 161 161 161 PHE PHE B . n 
B 1 162 VAL 162 162 162 VAL VAL B . n 
B 1 163 ASP 163 163 163 ASP ASP B . n 
B 1 164 ALA 164 164 164 ALA ALA B . n 
B 1 165 ASP 165 165 165 ASP ASP B . n 
B 1 166 LYS 166 166 166 LYS LYS B . n 
B 1 167 ASP 167 167 167 ASP ASP B . n 
B 1 168 ASN 168 168 168 ASN ASN B . n 
B 1 169 TYR 169 169 169 TYR TYR B . n 
B 1 170 LEU 170 170 170 LEU LEU B . n 
B 1 171 ASN 171 171 171 ASN ASN B . n 
B 1 172 TYR 172 172 172 TYR TYR B . n 
B 1 173 HIS 173 173 173 HIS HIS B . n 
B 1 174 LYS 174 174 174 LYS LYS B . n 
B 1 175 ARG 175 175 175 ARG ARG B . n 
B 1 176 LEU 176 176 176 LEU LEU B . n 
B 1 177 ILE 177 177 177 ILE ILE B . n 
B 1 178 ASP 178 178 178 ASP ASP B . n 
B 1 179 LEU 179 179 179 LEU LEU B . n 
B 1 180 VAL 180 180 180 VAL VAL B . n 
B 1 181 LYS 181 181 181 LYS LYS B . n 
B 1 182 VAL 182 182 182 VAL VAL B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 GLY 184 184 184 GLY GLY B . n 
B 1 185 VAL 185 185 185 VAL VAL B . n 
B 1 186 ILE 186 186 186 ILE ILE B . n 
B 1 187 GLY 187 187 187 GLY GLY B . n 
B 1 188 TYR 188 188 188 TYR TYR B . n 
B 1 189 ASP 189 189 189 ASP ASP B . n 
B 1 190 ASN 190 190 190 ASN ASN B . n 
B 1 191 THR 191 191 191 THR THR B . n 
B 1 192 LEU 192 192 192 LEU LEU B . n 
B 1 193 TRP 193 193 193 TRP TRP B . n 
B 1 194 ASN 194 194 194 ASN ASN B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 VAL 197 197 197 VAL VAL B . n 
B 1 198 VAL 198 198 198 VAL VAL B . n 
B 1 199 ALA 199 199 199 ALA ALA B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 PRO 201 201 201 PRO PRO B . n 
B 1 202 ASP 202 202 202 ASP ASP B . n 
B 1 203 ALA 203 203 203 ALA ALA B . n 
B 1 204 PRO 204 204 204 PRO PRO B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ARG 206 206 206 ARG ARG B . n 
B 1 207 LYS 207 207 207 LYS LYS B . n 
B 1 208 TYR 208 208 208 TYR TYR B . n 
B 1 209 VAL 209 209 209 VAL VAL B . n 
B 1 210 ARG 210 210 210 ARG ARG B . n 
B 1 211 TYR 211 211 211 TYR TYR B . n 
B 1 212 TYR 212 212 212 TYR TYR B . n 
B 1 213 ARG 213 213 213 ARG ARG B . n 
B 1 214 ASP 214 214 214 ASP ASP B . n 
B 1 215 PHE 215 215 215 PHE PHE B . n 
B 1 216 VAL 216 216 216 VAL VAL B . n 
B 1 217 LEU 217 217 217 LEU LEU B . n 
B 1 218 GLU 218 218 218 GLU GLU B . n 
B 1 219 LEU 219 219 219 LEU LEU B . n 
B 1 220 ASN 220 220 220 ASN ASN B . n 
B 1 221 LYS 221 221 221 LYS LYS B . n 
B 1 222 ALA 222 222 222 ALA ALA B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 VAL 225 225 225 VAL VAL B . n 
B 1 226 ASP 226 226 226 ASP ASP B . n 
B 1 227 PRO 227 227 227 PRO PRO B . n 
B 1 228 ARG 228 228 228 ARG ARG B . n 
B 1 229 ILE 229 229 229 ILE ILE B . n 
B 1 230 GLU 230 230 230 GLU GLU B . n 
B 1 231 ILE 231 231 231 ILE ILE B . n 
B 1 232 CYS 232 232 232 CYS CYS B . n 
B 1 233 MET 233 233 233 MET MET B . n 
B 1 234 LEU 234 234 234 LEU LEU B . n 
B 1 235 PRO 235 235 235 PRO PRO B . n 
B 1 236 VAL 236 236 236 VAL VAL B . n 
B 1 237 GLY 237 237 237 GLY GLY B . n 
B 1 238 ASP 238 238 238 ASP ASP B . n 
B 1 239 GLY 239 239 239 GLY GLY B . n 
B 1 240 ILE 240 240 240 ILE ILE B . n 
B 1 241 THR 241 241 241 THR THR B . n 
B 1 242 ILE 242 242 242 ILE ILE B . n 
B 1 243 CYS 243 243 243 CYS CYS B . n 
B 1 244 ARG 244 244 244 ARG ARG B . n 
B 1 245 ARG 245 245 245 ARG ARG B . n 
B 1 246 ILE 246 246 246 ILE ILE B . n 
B 1 247 LYS 247 247 247 LYS LYS B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   ALA 2   2   ?   ?   ?   C . n 
C 1 3   THR 3   3   ?   ?   ?   C . n 
C 1 4   ASN 4   4   ?   ?   ?   C . n 
C 1 5   GLU 5   5   ?   ?   ?   C . n 
C 1 6   ASP 6   6   ?   ?   ?   C . n 
C 1 7   GLN 7   7   ?   ?   ?   C . n 
C 1 8   LYS 8   8   ?   ?   ?   C . n 
C 1 9   GLN 9   9   ?   ?   ?   C . n 
C 1 10  THR 10  10  ?   ?   ?   C . n 
C 1 11  GLU 11  11  ?   ?   ?   C . n 
C 1 12  SER 12  12  ?   ?   ?   C . n 
C 1 13  GLY 13  13  ?   ?   ?   C . n 
C 1 14  ARG 14  14  ?   ?   ?   C . n 
C 1 15  HIS 15  15  ?   ?   ?   C . n 
C 1 16  GLN 16  16  ?   ?   ?   C . n 
C 1 17  GLU 17  17  ?   ?   ?   C . n 
C 1 18  VAL 18  18  ?   ?   ?   C . n 
C 1 19  GLY 19  19  ?   ?   ?   C . n 
C 1 20  HIS 20  20  ?   ?   ?   C . n 
C 1 21  LYS 21  21  21  LYS LYS C . n 
C 1 22  SER 22  22  22  SER SER C . n 
C 1 23  LEU 23  23  23  LEU LEU C . n 
C 1 24  LEU 24  24  24  LEU LEU C . n 
C 1 25  GLN 25  25  25  GLN GLN C . n 
C 1 26  SER 26  26  26  SER SER C . n 
C 1 27  ASP 27  27  27  ASP ASP C . n 
C 1 28  ALA 28  28  28  ALA ALA C . n 
C 1 29  LEU 29  29  29  LEU LEU C . n 
C 1 30  TYR 30  30  30  TYR TYR C . n 
C 1 31  GLN 31  31  31  GLN GLN C . n 
C 1 32  TYR 32  32  32  TYR TYR C . n 
C 1 33  ILE 33  33  33  ILE ILE C . n 
C 1 34  LEU 34  34  34  LEU LEU C . n 
C 1 35  GLU 35  35  35  GLU GLU C . n 
C 1 36  THR 36  36  36  THR THR C . n 
C 1 37  SER 37  37  37  SER SER C . n 
C 1 38  VAL 38  38  38  VAL VAL C . n 
C 1 39  PHE 39  39  39  PHE PHE C . n 
C 1 40  PRO 40  40  40  PRO PRO C . n 
C 1 41  ARG 41  41  41  ARG ARG C . n 
C 1 42  GLU 42  42  42  GLU GLU C . n 
C 1 43  HIS 43  43  43  HIS HIS C . n 
C 1 44  GLU 44  44  44  GLU GLU C . n 
C 1 45  ALA 45  45  45  ALA ALA C . n 
C 1 46  MET 46  46  46  MET MET C . n 
C 1 47  LYS 47  47  47  LYS LYS C . n 
C 1 48  GLU 48  48  48  GLU GLU C . n 
C 1 49  LEU 49  49  49  LEU LEU C . n 
C 1 50  ARG 50  50  50  ARG ARG C . n 
C 1 51  GLU 51  51  51  GLU GLU C . n 
C 1 52  VAL 52  52  52  VAL VAL C . n 
C 1 53  THR 53  53  53  THR THR C . n 
C 1 54  ALA 54  54  54  ALA ALA C . n 
C 1 55  LYS 55  55  55  LYS LYS C . n 
C 1 56  HIS 56  56  56  HIS HIS C . n 
C 1 57  PRO 57  57  57  PRO PRO C . n 
C 1 58  TRP 58  58  58  TRP TRP C . n 
C 1 59  ASN 59  59  59  ASN ASN C . n 
C 1 60  ILE 60  60  60  ILE ILE C . n 
C 1 61  MET 61  61  61  MET MET C . n 
C 1 62  THR 62  62  62  THR THR C . n 
C 1 63  THR 63  63  63  THR THR C . n 
C 1 64  SER 64  64  64  SER SER C . n 
C 1 65  ALA 65  65  65  ALA ALA C . n 
C 1 66  ASP 66  66  66  ASP ASP C . n 
C 1 67  GLU 67  67  67  GLU GLU C . n 
C 1 68  GLY 68  68  68  GLY GLY C . n 
C 1 69  GLN 69  69  69  GLN GLN C . n 
C 1 70  PHE 70  70  70  PHE PHE C . n 
C 1 71  LEU 71  71  71  LEU LEU C . n 
C 1 72  SER 72  72  72  SER SER C . n 
C 1 73  MET 73  73  73  MET MET C . n 
C 1 74  LEU 74  74  74  LEU LEU C . n 
C 1 75  LEU 75  75  75  LEU LEU C . n 
C 1 76  LYS 76  76  76  LYS LYS C . n 
C 1 77  LEU 77  77  77  LEU LEU C . n 
C 1 78  ILE 78  78  78  ILE ILE C . n 
C 1 79  ASN 79  79  79  ASN ASN C . n 
C 1 80  ALA 80  80  80  ALA ALA C . n 
C 1 81  LYS 81  81  81  LYS LYS C . n 
C 1 82  ASN 82  82  82  ASN ASN C . n 
C 1 83  THR 83  83  83  THR THR C . n 
C 1 84  MET 84  84  84  MET MET C . n 
C 1 85  GLU 85  85  85  GLU GLU C . n 
C 1 86  ILE 86  86  86  ILE ILE C . n 
C 1 87  GLY 87  87  87  GLY GLY C . n 
C 1 88  VAL 88  88  88  VAL VAL C . n 
C 1 89  TYR 89  89  89  TYR TYR C . n 
C 1 90  THR 90  90  90  THR THR C . n 
C 1 91  GLY 91  91  91  GLY GLY C . n 
C 1 92  TYR 92  92  92  TYR TYR C . n 
C 1 93  SER 93  93  93  SER SER C . n 
C 1 94  LEU 94  94  94  LEU LEU C . n 
C 1 95  LEU 95  95  95  LEU LEU C . n 
C 1 96  ALA 96  96  96  ALA ALA C . n 
C 1 97  THR 97  97  97  THR THR C . n 
C 1 98  ALA 98  98  98  ALA ALA C . n 
C 1 99  LEU 99  99  99  LEU LEU C . n 
C 1 100 ALA 100 100 100 ALA ALA C . n 
C 1 101 ILE 101 101 101 ILE ILE C . n 
C 1 102 PRO 102 102 102 PRO PRO C . n 
C 1 103 GLU 103 103 103 GLU GLU C . n 
C 1 104 ASP 104 104 104 ASP ASP C . n 
C 1 105 GLY 105 105 105 GLY GLY C . n 
C 1 106 LYS 106 106 106 LYS LYS C . n 
C 1 107 ILE 107 107 107 ILE ILE C . n 
C 1 108 LEU 108 108 108 LEU LEU C . n 
C 1 109 ALA 109 109 109 ALA ALA C . n 
C 1 110 MET 110 110 110 MET MET C . n 
C 1 111 ASP 111 111 111 ASP ASP C . n 
C 1 112 ILE 112 112 112 ILE ILE C . n 
C 1 113 ASN 113 113 113 ASN ASN C . n 
C 1 114 LYS 114 114 114 LYS LYS C . n 
C 1 115 GLU 115 115 115 GLU GLU C . n 
C 1 116 ASN 116 116 116 ASN ASN C . n 
C 1 117 TYR 117 117 117 TYR TYR C . n 
C 1 118 GLU 118 118 118 GLU GLU C . n 
C 1 119 LEU 119 119 119 LEU LEU C . n 
C 1 120 GLY 120 120 120 GLY GLY C . n 
C 1 121 LEU 121 121 121 LEU LEU C . n 
C 1 122 PRO 122 122 122 PRO PRO C . n 
C 1 123 VAL 123 123 123 VAL VAL C . n 
C 1 124 ILE 124 124 124 ILE ILE C . n 
C 1 125 LYS 125 125 125 LYS LYS C . n 
C 1 126 LYS 126 126 126 LYS LYS C . n 
C 1 127 ALA 127 127 127 ALA ALA C . n 
C 1 128 GLY 128 128 128 GLY GLY C . n 
C 1 129 VAL 129 129 129 VAL VAL C . n 
C 1 130 ASP 130 130 130 ASP ASP C . n 
C 1 131 HIS 131 131 131 HIS HIS C . n 
C 1 132 LYS 132 132 132 LYS LYS C . n 
C 1 133 ILE 133 133 133 ILE ILE C . n 
C 1 134 ASP 134 134 134 ASP ASP C . n 
C 1 135 PHE 135 135 135 PHE PHE C . n 
C 1 136 ARG 136 136 136 ARG ARG C . n 
C 1 137 GLU 137 137 137 GLU GLU C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 PRO 139 139 139 PRO PRO C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 LEU 141 141 141 LEU LEU C . n 
C 1 142 PRO 142 142 142 PRO PRO C . n 
C 1 143 VAL 143 143 143 VAL VAL C . n 
C 1 144 LEU 144 144 144 LEU LEU C . n 
C 1 145 ASP 145 145 145 ASP ASP C . n 
C 1 146 GLU 146 146 146 GLU GLU C . n 
C 1 147 MET 147 147 147 MET MET C . n 
C 1 148 ILE 148 148 148 ILE ILE C . n 
C 1 149 LYS 149 149 149 LYS LYS C . n 
C 1 150 ASP 150 150 150 ASP ASP C . n 
C 1 151 GLU 151 151 151 GLU GLU C . n 
C 1 152 LYS 152 152 152 LYS LYS C . n 
C 1 153 ASN 153 153 153 ASN ASN C . n 
C 1 154 HIS 154 154 154 HIS HIS C . n 
C 1 155 GLY 155 155 155 GLY GLY C . n 
C 1 156 SER 156 156 156 SER SER C . n 
C 1 157 TYR 157 157 157 TYR TYR C . n 
C 1 158 ASP 158 158 158 ASP ASP C . n 
C 1 159 PHE 159 159 159 PHE PHE C . n 
C 1 160 ILE 160 160 160 ILE ILE C . n 
C 1 161 PHE 161 161 161 PHE PHE C . n 
C 1 162 VAL 162 162 162 VAL VAL C . n 
C 1 163 ASP 163 163 163 ASP ASP C . n 
C 1 164 ALA 164 164 164 ALA ALA C . n 
C 1 165 ASP 165 165 165 ASP ASP C . n 
C 1 166 LYS 166 166 166 LYS LYS C . n 
C 1 167 ASP 167 167 167 ASP ASP C . n 
C 1 168 ASN 168 168 168 ASN ASN C . n 
C 1 169 TYR 169 169 169 TYR TYR C . n 
C 1 170 LEU 170 170 170 LEU LEU C . n 
C 1 171 ASN 171 171 171 ASN ASN C . n 
C 1 172 TYR 172 172 172 TYR TYR C . n 
C 1 173 HIS 173 173 173 HIS HIS C . n 
C 1 174 LYS 174 174 174 LYS LYS C . n 
C 1 175 ARG 175 175 175 ARG ARG C . n 
C 1 176 LEU 176 176 176 LEU LEU C . n 
C 1 177 ILE 177 177 177 ILE ILE C . n 
C 1 178 ASP 178 178 178 ASP ASP C . n 
C 1 179 LEU 179 179 179 LEU LEU C . n 
C 1 180 VAL 180 180 180 VAL VAL C . n 
C 1 181 LYS 181 181 181 LYS LYS C . n 
C 1 182 VAL 182 182 182 VAL VAL C . n 
C 1 183 GLY 183 183 183 GLY GLY C . n 
C 1 184 GLY 184 184 184 GLY GLY C . n 
C 1 185 VAL 185 185 185 VAL VAL C . n 
C 1 186 ILE 186 186 186 ILE ILE C . n 
C 1 187 GLY 187 187 187 GLY GLY C . n 
C 1 188 TYR 188 188 188 TYR TYR C . n 
C 1 189 ASP 189 189 189 ASP ASP C . n 
C 1 190 ASN 190 190 190 ASN ASN C . n 
C 1 191 THR 191 191 191 THR THR C . n 
C 1 192 LEU 192 192 192 LEU LEU C . n 
C 1 193 TRP 193 193 193 TRP TRP C . n 
C 1 194 ASN 194 194 194 ASN ASN C . n 
C 1 195 GLY 195 195 195 GLY GLY C . n 
C 1 196 SER 196 196 196 SER SER C . n 
C 1 197 VAL 197 197 197 VAL VAL C . n 
C 1 198 VAL 198 198 198 VAL VAL C . n 
C 1 199 ALA 199 199 199 ALA ALA C . n 
C 1 200 PRO 200 200 200 PRO PRO C . n 
C 1 201 PRO 201 201 201 PRO PRO C . n 
C 1 202 ASP 202 202 202 ASP ASP C . n 
C 1 203 ALA 203 203 203 ALA ALA C . n 
C 1 204 PRO 204 204 204 PRO PRO C . n 
C 1 205 LEU 205 205 205 LEU LEU C . n 
C 1 206 ARG 206 206 206 ARG ARG C . n 
C 1 207 LYS 207 207 207 LYS LYS C . n 
C 1 208 TYR 208 208 208 TYR TYR C . n 
C 1 209 VAL 209 209 209 VAL VAL C . n 
C 1 210 ARG 210 210 210 ARG ARG C . n 
C 1 211 TYR 211 211 211 TYR TYR C . n 
C 1 212 TYR 212 212 212 TYR TYR C . n 
C 1 213 ARG 213 213 213 ARG ARG C . n 
C 1 214 ASP 214 214 214 ASP ASP C . n 
C 1 215 PHE 215 215 215 PHE PHE C . n 
C 1 216 VAL 216 216 216 VAL VAL C . n 
C 1 217 LEU 217 217 217 LEU LEU C . n 
C 1 218 GLU 218 218 218 GLU GLU C . n 
C 1 219 LEU 219 219 219 LEU LEU C . n 
C 1 220 ASN 220 220 220 ASN ASN C . n 
C 1 221 LYS 221 221 221 LYS LYS C . n 
C 1 222 ALA 222 222 222 ALA ALA C . n 
C 1 223 LEU 223 223 223 LEU LEU C . n 
C 1 224 ALA 224 224 224 ALA ALA C . n 
C 1 225 VAL 225 225 225 VAL VAL C . n 
C 1 226 ASP 226 226 226 ASP ASP C . n 
C 1 227 PRO 227 227 227 PRO PRO C . n 
C 1 228 ARG 228 228 228 ARG ARG C . n 
C 1 229 ILE 229 229 229 ILE ILE C . n 
C 1 230 GLU 230 230 230 GLU GLU C . n 
C 1 231 ILE 231 231 231 ILE ILE C . n 
C 1 232 CYS 232 232 232 CYS CYS C . n 
C 1 233 MET 233 233 233 MET MET C . n 
C 1 234 LEU 234 234 234 LEU LEU C . n 
C 1 235 PRO 235 235 235 PRO PRO C . n 
C 1 236 VAL 236 236 236 VAL VAL C . n 
C 1 237 GLY 237 237 237 GLY GLY C . n 
C 1 238 ASP 238 238 238 ASP ASP C . n 
C 1 239 GLY 239 239 239 GLY GLY C . n 
C 1 240 ILE 240 240 240 ILE ILE C . n 
C 1 241 THR 241 241 241 THR THR C . n 
C 1 242 ILE 242 242 242 ILE ILE C . n 
C 1 243 CYS 243 243 243 CYS CYS C . n 
C 1 244 ARG 244 244 244 ARG ARG C . n 
C 1 245 ARG 245 245 245 ARG ARG C . n 
C 1 246 ILE 246 246 246 ILE ILE C . n 
C 1 247 LYS 247 247 247 LYS LYS C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   ALA 2   2   ?   ?   ?   D . n 
D 1 3   THR 3   3   ?   ?   ?   D . n 
D 1 4   ASN 4   4   ?   ?   ?   D . n 
D 1 5   GLU 5   5   ?   ?   ?   D . n 
D 1 6   ASP 6   6   ?   ?   ?   D . n 
D 1 7   GLN 7   7   ?   ?   ?   D . n 
D 1 8   LYS 8   8   ?   ?   ?   D . n 
D 1 9   GLN 9   9   ?   ?   ?   D . n 
D 1 10  THR 10  10  ?   ?   ?   D . n 
D 1 11  GLU 11  11  ?   ?   ?   D . n 
D 1 12  SER 12  12  ?   ?   ?   D . n 
D 1 13  GLY 13  13  ?   ?   ?   D . n 
D 1 14  ARG 14  14  ?   ?   ?   D . n 
D 1 15  HIS 15  15  ?   ?   ?   D . n 
D 1 16  GLN 16  16  ?   ?   ?   D . n 
D 1 17  GLU 17  17  ?   ?   ?   D . n 
D 1 18  VAL 18  18  ?   ?   ?   D . n 
D 1 19  GLY 19  19  ?   ?   ?   D . n 
D 1 20  HIS 20  20  ?   ?   ?   D . n 
D 1 21  LYS 21  21  21  LYS LYS D . n 
D 1 22  SER 22  22  22  SER SER D . n 
D 1 23  LEU 23  23  23  LEU LEU D . n 
D 1 24  LEU 24  24  24  LEU LEU D . n 
D 1 25  GLN 25  25  25  GLN GLN D . n 
D 1 26  SER 26  26  26  SER SER D . n 
D 1 27  ASP 27  27  27  ASP ASP D . n 
D 1 28  ALA 28  28  28  ALA ALA D . n 
D 1 29  LEU 29  29  29  LEU LEU D . n 
D 1 30  TYR 30  30  30  TYR TYR D . n 
D 1 31  GLN 31  31  31  GLN GLN D . n 
D 1 32  TYR 32  32  32  TYR TYR D . n 
D 1 33  ILE 33  33  33  ILE ILE D . n 
D 1 34  LEU 34  34  34  LEU LEU D . n 
D 1 35  GLU 35  35  35  GLU GLU D . n 
D 1 36  THR 36  36  36  THR THR D . n 
D 1 37  SER 37  37  37  SER SER D . n 
D 1 38  VAL 38  38  38  VAL VAL D . n 
D 1 39  PHE 39  39  39  PHE PHE D . n 
D 1 40  PRO 40  40  40  PRO PRO D . n 
D 1 41  ARG 41  41  41  ARG ARG D . n 
D 1 42  GLU 42  42  42  GLU GLU D . n 
D 1 43  HIS 43  43  43  HIS HIS D . n 
D 1 44  GLU 44  44  44  GLU GLU D . n 
D 1 45  ALA 45  45  45  ALA ALA D . n 
D 1 46  MET 46  46  46  MET MET D . n 
D 1 47  LYS 47  47  47  LYS LYS D . n 
D 1 48  GLU 48  48  48  GLU GLU D . n 
D 1 49  LEU 49  49  49  LEU LEU D . n 
D 1 50  ARG 50  50  50  ARG ARG D . n 
D 1 51  GLU 51  51  51  GLU GLU D . n 
D 1 52  VAL 52  52  52  VAL VAL D . n 
D 1 53  THR 53  53  53  THR THR D . n 
D 1 54  ALA 54  54  54  ALA ALA D . n 
D 1 55  LYS 55  55  55  LYS LYS D . n 
D 1 56  HIS 56  56  56  HIS HIS D . n 
D 1 57  PRO 57  57  57  PRO PRO D . n 
D 1 58  TRP 58  58  58  TRP TRP D . n 
D 1 59  ASN 59  59  59  ASN ASN D . n 
D 1 60  ILE 60  60  60  ILE ILE D . n 
D 1 61  MET 61  61  61  MET MET D . n 
D 1 62  THR 62  62  62  THR THR D . n 
D 1 63  THR 63  63  63  THR THR D . n 
D 1 64  SER 64  64  64  SER SER D . n 
D 1 65  ALA 65  65  65  ALA ALA D . n 
D 1 66  ASP 66  66  66  ASP ASP D . n 
D 1 67  GLU 67  67  67  GLU GLU D . n 
D 1 68  GLY 68  68  68  GLY GLY D . n 
D 1 69  GLN 69  69  69  GLN GLN D . n 
D 1 70  PHE 70  70  70  PHE PHE D . n 
D 1 71  LEU 71  71  71  LEU LEU D . n 
D 1 72  SER 72  72  72  SER SER D . n 
D 1 73  MET 73  73  73  MET MET D . n 
D 1 74  LEU 74  74  74  LEU LEU D . n 
D 1 75  LEU 75  75  75  LEU LEU D . n 
D 1 76  LYS 76  76  76  LYS LYS D . n 
D 1 77  LEU 77  77  77  LEU LEU D . n 
D 1 78  ILE 78  78  78  ILE ILE D . n 
D 1 79  ASN 79  79  79  ASN ASN D . n 
D 1 80  ALA 80  80  80  ALA ALA D . n 
D 1 81  LYS 81  81  81  LYS LYS D . n 
D 1 82  ASN 82  82  82  ASN ASN D . n 
D 1 83  THR 83  83  83  THR THR D . n 
D 1 84  MET 84  84  84  MET MET D . n 
D 1 85  GLU 85  85  85  GLU GLU D . n 
D 1 86  ILE 86  86  86  ILE ILE D . n 
D 1 87  GLY 87  87  87  GLY GLY D . n 
D 1 88  VAL 88  88  88  VAL VAL D . n 
D 1 89  TYR 89  89  89  TYR TYR D . n 
D 1 90  THR 90  90  90  THR THR D . n 
D 1 91  GLY 91  91  91  GLY GLY D . n 
D 1 92  TYR 92  92  92  TYR TYR D . n 
D 1 93  SER 93  93  93  SER SER D . n 
D 1 94  LEU 94  94  94  LEU LEU D . n 
D 1 95  LEU 95  95  95  LEU LEU D . n 
D 1 96  ALA 96  96  96  ALA ALA D . n 
D 1 97  THR 97  97  97  THR THR D . n 
D 1 98  ALA 98  98  98  ALA ALA D . n 
D 1 99  LEU 99  99  99  LEU LEU D . n 
D 1 100 ALA 100 100 100 ALA ALA D . n 
D 1 101 ILE 101 101 101 ILE ILE D . n 
D 1 102 PRO 102 102 102 PRO PRO D . n 
D 1 103 GLU 103 103 103 GLU GLU D . n 
D 1 104 ASP 104 104 104 ASP ASP D . n 
D 1 105 GLY 105 105 105 GLY GLY D . n 
D 1 106 LYS 106 106 106 LYS LYS D . n 
D 1 107 ILE 107 107 107 ILE ILE D . n 
D 1 108 LEU 108 108 108 LEU LEU D . n 
D 1 109 ALA 109 109 109 ALA ALA D . n 
D 1 110 MET 110 110 110 MET MET D . n 
D 1 111 ASP 111 111 111 ASP ASP D . n 
D 1 112 ILE 112 112 112 ILE ILE D . n 
D 1 113 ASN 113 113 113 ASN ASN D . n 
D 1 114 LYS 114 114 114 LYS LYS D . n 
D 1 115 GLU 115 115 115 GLU GLU D . n 
D 1 116 ASN 116 116 116 ASN ASN D . n 
D 1 117 TYR 117 117 117 TYR TYR D . n 
D 1 118 GLU 118 118 118 GLU GLU D . n 
D 1 119 LEU 119 119 119 LEU LEU D . n 
D 1 120 GLY 120 120 120 GLY GLY D . n 
D 1 121 LEU 121 121 121 LEU LEU D . n 
D 1 122 PRO 122 122 122 PRO PRO D . n 
D 1 123 VAL 123 123 123 VAL VAL D . n 
D 1 124 ILE 124 124 124 ILE ILE D . n 
D 1 125 LYS 125 125 125 LYS LYS D . n 
D 1 126 LYS 126 126 126 LYS LYS D . n 
D 1 127 ALA 127 127 127 ALA ALA D . n 
D 1 128 GLY 128 128 128 GLY GLY D . n 
D 1 129 VAL 129 129 129 VAL VAL D . n 
D 1 130 ASP 130 130 130 ASP ASP D . n 
D 1 131 HIS 131 131 131 HIS HIS D . n 
D 1 132 LYS 132 132 132 LYS LYS D . n 
D 1 133 ILE 133 133 133 ILE ILE D . n 
D 1 134 ASP 134 134 134 ASP ASP D . n 
D 1 135 PHE 135 135 135 PHE PHE D . n 
D 1 136 ARG 136 136 136 ARG ARG D . n 
D 1 137 GLU 137 137 137 GLU GLU D . n 
D 1 138 GLY 138 138 138 GLY GLY D . n 
D 1 139 PRO 139 139 139 PRO PRO D . n 
D 1 140 ALA 140 140 140 ALA ALA D . n 
D 1 141 LEU 141 141 141 LEU LEU D . n 
D 1 142 PRO 142 142 142 PRO PRO D . n 
D 1 143 VAL 143 143 143 VAL VAL D . n 
D 1 144 LEU 144 144 144 LEU LEU D . n 
D 1 145 ASP 145 145 145 ASP ASP D . n 
D 1 146 GLU 146 146 146 GLU GLU D . n 
D 1 147 MET 147 147 147 MET MET D . n 
D 1 148 ILE 148 148 148 ILE ILE D . n 
D 1 149 LYS 149 149 149 LYS LYS D . n 
D 1 150 ASP 150 150 150 ASP ASP D . n 
D 1 151 GLU 151 151 151 GLU GLU D . n 
D 1 152 LYS 152 152 152 LYS LYS D . n 
D 1 153 ASN 153 153 153 ASN ASN D . n 
D 1 154 HIS 154 154 154 HIS HIS D . n 
D 1 155 GLY 155 155 155 GLY GLY D . n 
D 1 156 SER 156 156 156 SER SER D . n 
D 1 157 TYR 157 157 157 TYR TYR D . n 
D 1 158 ASP 158 158 158 ASP ASP D . n 
D 1 159 PHE 159 159 159 PHE PHE D . n 
D 1 160 ILE 160 160 160 ILE ILE D . n 
D 1 161 PHE 161 161 161 PHE PHE D . n 
D 1 162 VAL 162 162 162 VAL VAL D . n 
D 1 163 ASP 163 163 163 ASP ASP D . n 
D 1 164 ALA 164 164 164 ALA ALA D . n 
D 1 165 ASP 165 165 165 ASP ASP D . n 
D 1 166 LYS 166 166 166 LYS LYS D . n 
D 1 167 ASP 167 167 167 ASP ASP D . n 
D 1 168 ASN 168 168 168 ASN ASN D . n 
D 1 169 TYR 169 169 169 TYR TYR D . n 
D 1 170 LEU 170 170 170 LEU LEU D . n 
D 1 171 ASN 171 171 171 ASN ASN D . n 
D 1 172 TYR 172 172 172 TYR TYR D . n 
D 1 173 HIS 173 173 173 HIS HIS D . n 
D 1 174 LYS 174 174 174 LYS LYS D . n 
D 1 175 ARG 175 175 175 ARG ARG D . n 
D 1 176 LEU 176 176 176 LEU LEU D . n 
D 1 177 ILE 177 177 177 ILE ILE D . n 
D 1 178 ASP 178 178 178 ASP ASP D . n 
D 1 179 LEU 179 179 179 LEU LEU D . n 
D 1 180 VAL 180 180 180 VAL VAL D . n 
D 1 181 LYS 181 181 181 LYS LYS D . n 
D 1 182 VAL 182 182 182 VAL VAL D . n 
D 1 183 GLY 183 183 183 GLY GLY D . n 
D 1 184 GLY 184 184 184 GLY GLY D . n 
D 1 185 VAL 185 185 185 VAL VAL D . n 
D 1 186 ILE 186 186 186 ILE ILE D . n 
D 1 187 GLY 187 187 187 GLY GLY D . n 
D 1 188 TYR 188 188 188 TYR TYR D . n 
D 1 189 ASP 189 189 189 ASP ASP D . n 
D 1 190 ASN 190 190 190 ASN ASN D . n 
D 1 191 THR 191 191 191 THR THR D . n 
D 1 192 LEU 192 192 192 LEU LEU D . n 
D 1 193 TRP 193 193 193 TRP TRP D . n 
D 1 194 ASN 194 194 194 ASN ASN D . n 
D 1 195 GLY 195 195 195 GLY GLY D . n 
D 1 196 SER 196 196 196 SER SER D . n 
D 1 197 VAL 197 197 197 VAL VAL D . n 
D 1 198 VAL 198 198 198 VAL VAL D . n 
D 1 199 ALA 199 199 199 ALA ALA D . n 
D 1 200 PRO 200 200 200 PRO PRO D . n 
D 1 201 PRO 201 201 201 PRO PRO D . n 
D 1 202 ASP 202 202 202 ASP ASP D . n 
D 1 203 ALA 203 203 203 ALA ALA D . n 
D 1 204 PRO 204 204 204 PRO PRO D . n 
D 1 205 LEU 205 205 205 LEU LEU D . n 
D 1 206 ARG 206 206 206 ARG ARG D . n 
D 1 207 LYS 207 207 207 LYS LYS D . n 
D 1 208 TYR 208 208 208 TYR TYR D . n 
D 1 209 VAL 209 209 209 VAL VAL D . n 
D 1 210 ARG 210 210 210 ARG ARG D . n 
D 1 211 TYR 211 211 211 TYR TYR D . n 
D 1 212 TYR 212 212 212 TYR TYR D . n 
D 1 213 ARG 213 213 213 ARG ARG D . n 
D 1 214 ASP 214 214 214 ASP ASP D . n 
D 1 215 PHE 215 215 215 PHE PHE D . n 
D 1 216 VAL 216 216 216 VAL VAL D . n 
D 1 217 LEU 217 217 217 LEU LEU D . n 
D 1 218 GLU 218 218 218 GLU GLU D . n 
D 1 219 LEU 219 219 219 LEU LEU D . n 
D 1 220 ASN 220 220 220 ASN ASN D . n 
D 1 221 LYS 221 221 221 LYS LYS D . n 
D 1 222 ALA 222 222 222 ALA ALA D . n 
D 1 223 LEU 223 223 223 LEU LEU D . n 
D 1 224 ALA 224 224 224 ALA ALA D . n 
D 1 225 VAL 225 225 225 VAL VAL D . n 
D 1 226 ASP 226 226 226 ASP ASP D . n 
D 1 227 PRO 227 227 227 PRO PRO D . n 
D 1 228 ARG 228 228 228 ARG ARG D . n 
D 1 229 ILE 229 229 229 ILE ILE D . n 
D 1 230 GLU 230 230 230 GLU GLU D . n 
D 1 231 ILE 231 231 231 ILE ILE D . n 
D 1 232 CYS 232 232 232 CYS CYS D . n 
D 1 233 MET 233 233 233 MET MET D . n 
D 1 234 LEU 234 234 234 LEU LEU D . n 
D 1 235 PRO 235 235 235 PRO PRO D . n 
D 1 236 VAL 236 236 236 VAL VAL D . n 
D 1 237 GLY 237 237 237 GLY GLY D . n 
D 1 238 ASP 238 238 238 ASP ASP D . n 
D 1 239 GLY 239 239 239 GLY GLY D . n 
D 1 240 ILE 240 240 240 ILE ILE D . n 
D 1 241 THR 241 241 241 THR THR D . n 
D 1 242 ILE 242 242 242 ILE ILE D . n 
D 1 243 CYS 243 243 243 CYS CYS D . n 
D 1 244 ARG 244 244 244 ARG ARG D . n 
D 1 245 ARG 245 245 245 ARG ARG D . n 
D 1 246 ILE 246 246 246 ILE ILE D . n 
D 1 247 LYS 247 247 247 LYS LYS D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 CA  1  305 305 CA  CA  A . 
F 3 SAH 1  301 301 SAH SAH A . 
G 4 FRE 1  306 305 FRE FRE A . 
H 2 CA  1  306 306 CA  CA  B . 
I 3 SAH 1  302 302 SAH SAH B . 
J 2 CA  1  307 307 CA  CA  C . 
K 3 SAH 1  303 303 SAH SAH C . 
L 2 CA  1  308 308 CA  CA  D . 
M 3 SAH 1  304 304 SAH SAH D . 
N 5 HOH 1  307 4   HOH HOH A . 
N 5 HOH 2  308 9   HOH HOH A . 
N 5 HOH 3  309 10  HOH HOH A . 
N 5 HOH 4  310 13  HOH HOH A . 
N 5 HOH 5  311 14  HOH HOH A . 
N 5 HOH 6  312 16  HOH HOH A . 
N 5 HOH 7  313 29  HOH HOH A . 
N 5 HOH 8  314 33  HOH HOH A . 
N 5 HOH 9  315 35  HOH HOH A . 
N 5 HOH 10 316 36  HOH HOH A . 
N 5 HOH 11 317 37  HOH HOH A . 
N 5 HOH 12 318 38  HOH HOH A . 
N 5 HOH 13 319 42  HOH HOH A . 
N 5 HOH 14 320 45  HOH HOH A . 
N 5 HOH 15 321 48  HOH HOH A . 
N 5 HOH 16 322 55  HOH HOH A . 
N 5 HOH 17 323 57  HOH HOH A . 
N 5 HOH 18 324 60  HOH HOH A . 
N 5 HOH 19 325 61  HOH HOH A . 
O 5 HOH 1  307 1   HOH HOH B . 
O 5 HOH 2  308 3   HOH HOH B . 
O 5 HOH 3  309 5   HOH HOH B . 
O 5 HOH 4  310 6   HOH HOH B . 
O 5 HOH 5  311 7   HOH HOH B . 
O 5 HOH 6  312 12  HOH HOH B . 
O 5 HOH 7  313 17  HOH HOH B . 
O 5 HOH 8  314 18  HOH HOH B . 
O 5 HOH 9  315 21  HOH HOH B . 
O 5 HOH 10 316 22  HOH HOH B . 
O 5 HOH 11 317 24  HOH HOH B . 
O 5 HOH 12 318 26  HOH HOH B . 
O 5 HOH 13 319 27  HOH HOH B . 
O 5 HOH 14 320 28  HOH HOH B . 
O 5 HOH 15 321 30  HOH HOH B . 
O 5 HOH 16 322 32  HOH HOH B . 
O 5 HOH 17 323 34  HOH HOH B . 
O 5 HOH 18 324 39  HOH HOH B . 
O 5 HOH 19 325 40  HOH HOH B . 
O 5 HOH 20 326 41  HOH HOH B . 
O 5 HOH 21 327 43  HOH HOH B . 
O 5 HOH 22 328 44  HOH HOH B . 
O 5 HOH 23 329 46  HOH HOH B . 
O 5 HOH 24 330 49  HOH HOH B . 
O 5 HOH 25 331 52  HOH HOH B . 
O 5 HOH 26 332 53  HOH HOH B . 
O 5 HOH 27 333 54  HOH HOH B . 
O 5 HOH 28 334 56  HOH HOH B . 
O 5 HOH 29 335 58  HOH HOH B . 
O 5 HOH 30 336 64  HOH HOH B . 
O 5 HOH 31 337 66  HOH HOH B . 
P 5 HOH 1  308 2   HOH HOH C . 
P 5 HOH 2  309 11  HOH HOH C . 
P 5 HOH 3  310 15  HOH HOH C . 
P 5 HOH 4  311 20  HOH HOH C . 
P 5 HOH 5  312 25  HOH HOH C . 
P 5 HOH 6  313 47  HOH HOH C . 
P 5 HOH 7  314 50  HOH HOH C . 
P 5 HOH 8  315 62  HOH HOH C . 
P 5 HOH 9  316 63  HOH HOH C . 
P 5 HOH 10 317 65  HOH HOH C . 
P 5 HOH 11 318 67  HOH HOH C . 
Q 5 HOH 1  309 8   HOH HOH D . 
Q 5 HOH 2  310 23  HOH HOH D . 
Q 5 HOH 3  311 31  HOH HOH D . 
Q 5 HOH 4  312 51  HOH HOH D . 
Q 5 HOH 5  313 59  HOH HOH D . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_defined_assembly              ?    dimeric 2 
3 author_defined_assembly              ?    dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1   A,C,E,F,G,J,K,N,P 
2 1,2 B,H,I,O           
3 1,3 D,L,M,Q           
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4870  ? 
1 MORE         -48   ? 
1 'SSA (A^2)'  19900 ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z       1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000   
2 'crystal symmetry operation' 4_555 x,-y,-z     1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000   
3 'crystal symmetry operation' 3_555 -x,y,-z+1/2 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 166.3890000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD2 ? A ASP 163 ? A ASP 163 ? 1_555 CA ? E CA . ? A CA 305 ? 1_555 OD1 ? A ASP 163 ? A ASP 163 ? 1_555 44.9  ? 
2  OD2 ? A ASP 163 ? A ASP 163 ? 1_555 CA ? E CA . ? A CA 305 ? 1_555 OD2 ? A ASP 189 ? A ASP 189 ? 1_555 74.8  ? 
3  OD1 ? A ASP 163 ? A ASP 163 ? 1_555 CA ? E CA . ? A CA 305 ? 1_555 OD2 ? A ASP 189 ? A ASP 189 ? 1_555 74.3  ? 
4  OD2 ? A ASP 163 ? A ASP 163 ? 1_555 CA ? E CA . ? A CA 305 ? 1_555 OD1 ? A ASN 190 ? A ASN 190 ? 1_555 108.0 ? 
5  OD1 ? A ASP 163 ? A ASP 163 ? 1_555 CA ? E CA . ? A CA 305 ? 1_555 OD1 ? A ASN 190 ? A ASN 190 ? 1_555 63.0  ? 
6  OD2 ? A ASP 189 ? A ASP 189 ? 1_555 CA ? E CA . ? A CA 305 ? 1_555 OD1 ? A ASN 190 ? A ASN 190 ? 1_555 86.7  ? 
7  OD2 ? A ASP 163 ? A ASP 163 ? 1_555 CA ? E CA . ? A CA 305 ? 1_555 ND2 ? A ASN 190 ? A ASN 190 ? 1_555 150.1 ? 
8  OD1 ? A ASP 163 ? A ASP 163 ? 1_555 CA ? E CA . ? A CA 305 ? 1_555 ND2 ? A ASN 190 ? A ASN 190 ? 1_555 105.8 ? 
9  OD2 ? A ASP 189 ? A ASP 189 ? 1_555 CA ? E CA . ? A CA 305 ? 1_555 ND2 ? A ASN 190 ? A ASN 190 ? 1_555 106.8 ? 
10 OD1 ? A ASN 190 ? A ASN 190 ? 1_555 CA ? E CA . ? A CA 305 ? 1_555 ND2 ? A ASN 190 ? A ASN 190 ? 1_555 43.7  ? 
11 OD1 ? B ASN 190 ? B ASN 190 ? 1_555 CA ? H CA . ? B CA 306 ? 1_555 O   ? O HOH .   ? B HOH 311 ? 1_555 69.9  ? 
12 OD1 ? B ASN 190 ? B ASN 190 ? 1_555 CA ? H CA . ? B CA 306 ? 1_555 OD1 ? B ASP 163 ? B ASP 163 ? 1_555 81.4  ? 
13 O   ? O HOH .   ? B HOH 311 ? 1_555 CA ? H CA . ? B CA 306 ? 1_555 OD1 ? B ASP 163 ? B ASP 163 ? 1_555 124.3 ? 
14 OD1 ? B ASN 190 ? B ASN 190 ? 1_555 CA ? H CA . ? B CA 306 ? 1_555 OD2 ? B ASP 163 ? B ASP 163 ? 1_555 113.6 ? 
15 O   ? O HOH .   ? B HOH 311 ? 1_555 CA ? H CA . ? B CA 306 ? 1_555 OD2 ? B ASP 163 ? B ASP 163 ? 1_555 100.3 ? 
16 OD1 ? B ASP 163 ? B ASP 163 ? 1_555 CA ? H CA . ? B CA 306 ? 1_555 OD2 ? B ASP 163 ? B ASP 163 ? 1_555 49.7  ? 
17 OD1 ? B ASN 190 ? B ASN 190 ? 1_555 CA ? H CA . ? B CA 306 ? 1_555 OD2 ? B ASP 189 ? B ASP 189 ? 1_555 68.4  ? 
18 O   ? O HOH .   ? B HOH 311 ? 1_555 CA ? H CA . ? B CA 306 ? 1_555 OD2 ? B ASP 189 ? B ASP 189 ? 1_555 47.4  ? 
19 OD1 ? B ASP 163 ? B ASP 163 ? 1_555 CA ? H CA . ? B CA 306 ? 1_555 OD2 ? B ASP 189 ? B ASP 189 ? 1_555 78.2  ? 
20 OD2 ? B ASP 163 ? B ASP 163 ? 1_555 CA ? H CA . ? B CA 306 ? 1_555 OD2 ? B ASP 189 ? B ASP 189 ? 1_555 60.8  ? 
21 OD1 ? C ASP 189 ? C ASP 189 ? 1_555 CA ? J CA . ? C CA 307 ? 1_555 OD1 ? C ASP 163 ? C ASP 163 ? 1_555 106.1 ? 
22 OD1 ? C ASP 189 ? C ASP 189 ? 1_555 CA ? J CA . ? C CA 307 ? 1_555 OD1 ? C ASN 190 ? C ASN 190 ? 1_555 55.3  ? 
23 OD1 ? C ASP 163 ? C ASP 163 ? 1_555 CA ? J CA . ? C CA 307 ? 1_555 OD1 ? C ASN 190 ? C ASN 190 ? 1_555 85.1  ? 
24 OD1 ? C ASP 189 ? C ASP 189 ? 1_555 CA ? J CA . ? C CA 307 ? 1_555 ND2 ? C ASN 190 ? C ASN 190 ? 1_555 65.5  ? 
25 OD1 ? C ASP 163 ? C ASP 163 ? 1_555 CA ? J CA . ? C CA 307 ? 1_555 ND2 ? C ASN 190 ? C ASN 190 ? 1_555 126.1 ? 
26 OD1 ? C ASN 190 ? C ASN 190 ? 1_555 CA ? J CA . ? C CA 307 ? 1_555 ND2 ? C ASN 190 ? C ASN 190 ? 1_555 44.9  ? 
27 OD1 ? C ASP 189 ? C ASP 189 ? 1_555 CA ? J CA . ? C CA 307 ? 1_555 OD2 ? C ASP 163 ? C ASP 163 ? 1_555 80.6  ? 
28 OD1 ? C ASP 163 ? C ASP 163 ? 1_555 CA ? J CA . ? C CA 307 ? 1_555 OD2 ? C ASP 163 ? C ASP 163 ? 1_555 45.4  ? 
29 OD1 ? C ASN 190 ? C ASN 190 ? 1_555 CA ? J CA . ? C CA 307 ? 1_555 OD2 ? C ASP 163 ? C ASP 163 ? 1_555 100.5 ? 
30 ND2 ? C ASN 190 ? C ASN 190 ? 1_555 CA ? J CA . ? C CA 307 ? 1_555 OD2 ? C ASP 163 ? C ASP 163 ? 1_555 141.2 ? 
31 OD1 ? D ASP 163 ? D ASP 163 ? 1_555 CA ? L CA . ? D CA 308 ? 1_555 OD2 ? D ASP 163 ? D ASP 163 ? 1_555 40.5  ? 
32 OD1 ? D ASP 163 ? D ASP 163 ? 1_555 CA ? L CA . ? D CA 308 ? 1_555 OD2 ? D ASP 189 ? D ASP 189 ? 1_555 46.8  ? 
33 OD2 ? D ASP 163 ? D ASP 163 ? 1_555 CA ? L CA . ? D CA 308 ? 1_555 OD2 ? D ASP 189 ? D ASP 189 ? 1_555 67.2  ? 
34 OD1 ? D ASP 163 ? D ASP 163 ? 1_555 CA ? L CA . ? D CA 308 ? 1_555 OD1 ? D ASN 190 ? D ASN 190 ? 1_555 65.6  ? 
35 OD2 ? D ASP 163 ? D ASP 163 ? 1_555 CA ? L CA . ? D CA 308 ? 1_555 OD1 ? D ASN 190 ? D ASN 190 ? 1_555 105.6 ? 
36 OD2 ? D ASP 189 ? D ASP 189 ? 1_555 CA ? L CA . ? D CA 308 ? 1_555 OD1 ? D ASN 190 ? D ASN 190 ? 1_555 69.5  ? 
37 OD1 ? D ASP 163 ? D ASP 163 ? 1_555 CA ? L CA . ? D CA 308 ? 1_555 OXT ? M SAH .   ? D SAH 304 ? 1_555 103.7 ? 
38 OD2 ? D ASP 163 ? D ASP 163 ? 1_555 CA ? L CA . ? D CA 308 ? 1_555 OXT ? M SAH .   ? D SAH 304 ? 1_555 64.4  ? 
39 OD2 ? D ASP 189 ? D ASP 189 ? 1_555 CA ? L CA . ? D CA 308 ? 1_555 OXT ? M SAH .   ? D SAH 304 ? 1_555 121.1 ? 
40 OD1 ? D ASN 190 ? D ASN 190 ? 1_555 CA ? L CA . ? D CA 308 ? 1_555 OXT ? M SAH .   ? D SAH 304 ? 1_555 154.8 ? 
41 OD1 ? D ASP 163 ? D ASP 163 ? 1_555 CA ? L CA . ? D CA 308 ? 1_555 ND2 ? D ASN 190 ? D ASN 190 ? 1_555 79.1  ? 
42 OD2 ? D ASP 163 ? D ASP 163 ? 1_555 CA ? L CA . ? D CA 308 ? 1_555 ND2 ? D ASN 190 ? D ASN 190 ? 1_555 114.5 ? 
43 OD2 ? D ASP 189 ? D ASP 189 ? 1_555 CA ? L CA . ? D CA 308 ? 1_555 ND2 ? D ASN 190 ? D ASN 190 ? 1_555 50.3  ? 
44 OD1 ? D ASN 190 ? D ASN 190 ? 1_555 CA ? L CA . ? D CA 308 ? 1_555 ND2 ? D ASN 190 ? D ASN 190 ? 1_555 39.8  ? 
45 OXT ? M SAH .   ? D SAH 304 ? 1_555 CA ? L CA . ? D CA 308 ? 1_555 ND2 ? D ASN 190 ? D ASN 190 ? 1_555 164.8 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2005-03-15 
2 'Structure model' 1 1 2008-04-29 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2017-10-11 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' Advisory                    
4 4 'Structure model' 'Refinement description'    
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' pdbx_unobs_or_zero_occ_atoms 
2 4 'Structure model' software                     
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
DENZO     'data reduction' . ? 1 
SCALEPACK 'data scaling'   . ? 2 
SnB       phasing          . ? 3 
MLPHARE   phasing          . ? 4 
CNS       refinement       . ? 5 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1   1 ARG A 41  ? ? 73.09   72.17   
2   1 HIS A 43  ? ? 46.70   -62.83  
3   1 GLU A 44  ? ? 124.85  -45.82  
4   1 TYR A 89  ? ? 33.64   114.32  
5   1 THR A 90  ? ? 60.89   -41.37  
6   1 ASN A 113 ? ? -78.08  -84.68  
7   1 LYS A 114 ? ? 97.29   -29.58  
8   1 ALA A 164 ? ? -122.61 -136.32 
9   1 ASP A 165 ? ? -24.87  -93.30  
10  1 LYS A 166 ? ? 130.68  -54.19  
11  1 VAL A 185 ? ? 71.94   110.69  
12  1 TRP A 193 ? ? 26.60   57.44   
13  1 SER A 196 ? ? -52.41  -9.80   
14  1 VAL A 198 ? ? -141.29 16.24   
15  1 PRO A 201 ? ? -60.49  61.62   
16  1 ASP A 202 ? ? 170.07  8.35    
17  1 ALA A 203 ? ? -113.16 71.62   
18  1 PRO A 204 ? ? -32.32  135.57  
19  1 ILE A 231 ? ? 55.89   139.33  
20  1 PRO A 235 ? ? -79.63  34.06   
21  1 SER B 22  ? ? -118.95 -168.98 
22  1 PRO B 57  ? ? -26.60  -45.07  
23  1 ASN B 59  ? ? -69.31  78.50   
24  1 MET B 61  ? ? -157.83 -142.23 
25  1 THR B 62  ? ? 42.23   179.74  
26  1 THR B 63  ? ? 46.77   104.32  
27  1 VAL B 88  ? ? -94.25  -60.17  
28  1 TYR B 89  ? ? 43.73   101.42  
29  1 THR B 90  ? ? 66.35   -32.48  
30  1 GLU B 151 ? ? -51.25  2.78    
31  1 ASP B 163 ? ? -150.33 63.73   
32  1 ALA B 164 ? ? -115.00 -144.28 
33  1 ASP B 165 ? ? -38.49  -75.82  
34  1 LYS B 166 ? ? 132.39  -45.61  
35  1 TRP B 193 ? ? 34.17   44.49   
36  1 ASN B 194 ? ? 65.77   -70.17  
37  1 SER B 196 ? ? -140.59 23.45   
38  1 VAL B 197 ? ? -140.46 29.29   
39  1 ASP B 202 ? ? -48.75  91.32   
40  1 PRO B 204 ? ? -47.78  89.65   
41  1 LEU B 205 ? ? -170.92 102.62  
42  1 ILE B 231 ? ? 73.06   135.87  
43  1 SER C 22  ? ? -112.95 -156.21 
44  1 VAL C 38  ? ? -87.79  -76.82  
45  1 ALA C 45  ? ? 79.66   -12.43  
46  1 ASN C 59  ? ? 58.01   -12.54  
47  1 ILE C 60  ? ? 10.86   -78.88  
48  1 THR C 62  ? ? -39.80  125.47  
49  1 LYS C 81  ? ? -120.82 -50.35  
50  1 VAL C 88  ? ? -90.58  -99.23  
51  1 TYR C 89  ? ? 76.70   107.90  
52  1 THR C 90  ? ? 67.58   -52.09  
53  1 ASP C 104 ? ? -64.46  -96.24  
54  1 LEU C 108 ? ? -68.04  82.52   
55  1 ALA C 109 ? ? -69.50  50.53   
56  1 MET C 110 ? ? 1.01    -91.26  
57  1 ASP C 111 ? ? 177.73  -161.75 
58  1 GLU C 115 ? ? -103.02 57.91   
59  1 HIS C 131 ? ? -60.95  3.58    
60  1 PRO C 139 ? ? -25.13  137.27  
61  1 GLU C 151 ? ? -84.79  40.57   
62  1 ALA C 164 ? ? -76.38  -146.88 
63  1 ASP C 165 ? ? -55.43  -82.15  
64  1 LYS C 166 ? ? 160.14  -47.79  
65  1 LYS C 181 ? ? -79.53  -143.04 
66  1 VAL C 182 ? ? -51.43  -92.31  
67  1 VAL C 185 ? ? 73.23   113.10  
68  1 ASN C 190 ? ? 54.09   15.72   
69  1 THR C 191 ? ? -60.88  6.77    
70  1 TRP C 193 ? ? 27.35   65.68   
71  1 ASN C 194 ? ? 42.54   16.69   
72  1 SER C 196 ? ? -54.75  -84.30  
73  1 VAL C 197 ? ? -57.87  85.85   
74  1 PRO C 200 ? ? -46.64  174.99  
75  1 PRO C 201 ? ? -36.63  68.31   
76  1 ASP C 202 ? ? -170.43 14.45   
77  1 ILE C 231 ? ? 53.80   153.76  
78  1 CYS C 232 ? ? -162.57 118.55  
79  1 LEU D 24  ? ? -93.64  -150.56 
80  1 THR D 36  ? ? -94.31  53.59   
81  1 SER D 37  ? ? -173.99 -89.11  
82  1 VAL D 38  ? ? -59.58  -70.69  
83  1 ARG D 41  ? ? 64.21   110.79  
84  1 GLU D 42  ? ? -170.12 55.75   
85  1 HIS D 43  ? ? 71.44   -14.01  
86  1 GLU D 44  ? ? 68.38   -43.73  
87  1 THR D 53  ? ? -59.07  0.48    
88  1 TRP D 58  ? ? -94.96  52.81   
89  1 ILE D 60  ? ? -65.72  7.78    
90  1 ASN D 79  ? ? 61.23   96.52   
91  1 VAL D 88  ? ? -121.02 -80.67  
92  1 TYR D 89  ? ? 65.33   113.00  
93  1 THR D 90  ? ? 67.29   -54.62  
94  1 PRO D 102 ? ? -61.58  -139.60 
95  1 VAL D 123 ? ? -107.65 41.03   
96  1 ILE D 124 ? ? -156.65 -23.63  
97  1 VAL D 129 ? ? 48.13   14.55   
98  1 ARG D 136 ? ? -137.63 -141.31 
99  1 PRO D 139 ? ? -38.76  139.60  
100 1 ASP D 150 ? ? -45.89  108.36  
101 1 ASN D 153 ? ? 174.63  -1.99   
102 1 SER D 156 ? ? -62.65  11.78   
103 1 ALA D 164 ? ? -156.03 -103.75 
104 1 ASP D 165 ? ? -73.61  -153.24 
105 1 LYS D 166 ? ? -146.34 -35.57  
106 1 LYS D 181 ? ? 47.78   148.69  
107 1 VAL D 182 ? ? 44.68   -86.37  
108 1 VAL D 185 ? ? 146.06  -105.42 
109 1 ILE D 186 ? ? 41.88   100.47  
110 1 THR D 191 ? ? -64.21  12.14   
111 1 TRP D 193 ? ? 14.77   73.67   
112 1 ASN D 194 ? ? 49.09   -125.40 
113 1 ALA D 199 ? ? -43.64  169.65  
114 1 PRO D 200 ? ? -58.41  -175.87 
115 1 PRO D 201 ? ? -49.78  -6.32   
116 1 PRO D 204 ? ? -52.93  81.98   
117 1 LYS D 207 ? ? -58.78  -90.92  
118 1 TYR D 211 ? ? -71.51  -70.52  
119 1 PRO D 227 ? ? -62.01  8.73    
120 1 ILE D 231 ? ? 48.32   169.78  
121 1 CYS D 232 ? ? 179.36  110.89  
122 1 PRO D 235 ? ? -61.19  47.84   
123 1 ILE D 240 ? ? -163.58 103.70  
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    CAP 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    A 
_pdbx_validate_chiral.auth_comp_id    FRE 
_pdbx_validate_chiral.auth_seq_id     306 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         PLANAR 
_pdbx_validate_chiral.omega           . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 151 ? CG  ? A GLU 151 CG  
2  1 Y 1 A GLU 151 ? CD  ? A GLU 151 CD  
3  1 Y 1 A GLU 151 ? OE1 ? A GLU 151 OE1 
4  1 Y 1 A GLU 151 ? OE2 ? A GLU 151 OE2 
5  1 Y 1 B GLU 151 ? CG  ? B GLU 151 CG  
6  1 Y 1 B GLU 151 ? CD  ? B GLU 151 CD  
7  1 Y 1 B GLU 151 ? OE1 ? B GLU 151 OE1 
8  1 Y 1 B GLU 151 ? OE2 ? B GLU 151 OE2 
9  1 Y 1 C GLU 151 ? CG  ? C GLU 151 CG  
10 1 Y 1 C GLU 151 ? CD  ? C GLU 151 CD  
11 1 Y 1 C GLU 151 ? OE1 ? C GLU 151 OE1 
12 1 Y 1 C GLU 151 ? OE2 ? C GLU 151 OE2 
13 1 Y 1 D HIS 43  ? CG  ? D HIS 43  CG  
14 1 Y 1 D HIS 43  ? ND1 ? D HIS 43  ND1 
15 1 Y 1 D HIS 43  ? CD2 ? D HIS 43  CD2 
16 1 Y 1 D HIS 43  ? CE1 ? D HIS 43  CE1 
17 1 Y 1 D HIS 43  ? NE2 ? D HIS 43  NE2 
18 1 Y 1 D LYS 55  ? CG  ? D LYS 55  CG  
19 1 Y 1 D LYS 55  ? CD  ? D LYS 55  CD  
20 1 Y 1 D LYS 55  ? CE  ? D LYS 55  CE  
21 1 Y 1 D LYS 55  ? NZ  ? D LYS 55  NZ  
22 1 Y 1 D HIS 56  ? CG  ? D HIS 56  CG  
23 1 Y 1 D HIS 56  ? ND1 ? D HIS 56  ND1 
24 1 Y 1 D HIS 56  ? CD2 ? D HIS 56  CD2 
25 1 Y 1 D HIS 56  ? CE1 ? D HIS 56  CE1 
26 1 Y 1 D HIS 56  ? NE2 ? D HIS 56  NE2 
27 1 Y 1 D GLU 151 ? CG  ? D GLU 151 CG  
28 1 Y 1 D GLU 151 ? CD  ? D GLU 151 CD  
29 1 Y 1 D GLU 151 ? OE1 ? D GLU 151 OE1 
30 1 Y 1 D GLU 151 ? OE2 ? D GLU 151 OE2 
31 1 Y 1 D LYS 247 ? CG  ? D LYS 247 CG  
32 1 Y 1 D LYS 247 ? CD  ? D LYS 247 CD  
33 1 Y 1 D LYS 247 ? CE  ? D LYS 247 CE  
34 1 Y 1 D LYS 247 ? NZ  ? D LYS 247 NZ  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1  ? A MET 1  
2  1 Y 1 A ALA 2  ? A ALA 2  
3  1 Y 1 A THR 3  ? A THR 3  
4  1 Y 1 A ASN 4  ? A ASN 4  
5  1 Y 1 A GLU 5  ? A GLU 5  
6  1 Y 1 A ASP 6  ? A ASP 6  
7  1 Y 1 A GLN 7  ? A GLN 7  
8  1 Y 1 A LYS 8  ? A LYS 8  
9  1 Y 1 A GLN 9  ? A GLN 9  
10 1 Y 1 A THR 10 ? A THR 10 
11 1 Y 1 A GLU 11 ? A GLU 11 
12 1 Y 1 A SER 12 ? A SER 12 
13 1 Y 1 A GLY 13 ? A GLY 13 
14 1 Y 1 A ARG 14 ? A ARG 14 
15 1 Y 1 A HIS 15 ? A HIS 15 
16 1 Y 1 A GLN 16 ? A GLN 16 
17 1 Y 1 A GLU 17 ? A GLU 17 
18 1 Y 1 A VAL 18 ? A VAL 18 
19 1 Y 1 A GLY 19 ? A GLY 19 
20 1 Y 1 A HIS 20 ? A HIS 20 
21 1 Y 1 B MET 1  ? B MET 1  
22 1 Y 1 B ALA 2  ? B ALA 2  
23 1 Y 1 B THR 3  ? B THR 3  
24 1 Y 1 B ASN 4  ? B ASN 4  
25 1 Y 1 B GLU 5  ? B GLU 5  
26 1 Y 1 B ASP 6  ? B ASP 6  
27 1 Y 1 B GLN 7  ? B GLN 7  
28 1 Y 1 B LYS 8  ? B LYS 8  
29 1 Y 1 B GLN 9  ? B GLN 9  
30 1 Y 1 B THR 10 ? B THR 10 
31 1 Y 1 B GLU 11 ? B GLU 11 
32 1 Y 1 B SER 12 ? B SER 12 
33 1 Y 1 B GLY 13 ? B GLY 13 
34 1 Y 1 B ARG 14 ? B ARG 14 
35 1 Y 1 B HIS 15 ? B HIS 15 
36 1 Y 1 B GLN 16 ? B GLN 16 
37 1 Y 1 B GLU 17 ? B GLU 17 
38 1 Y 1 B VAL 18 ? B VAL 18 
39 1 Y 1 B GLY 19 ? B GLY 19 
40 1 Y 1 B HIS 20 ? B HIS 20 
41 1 Y 1 C MET 1  ? C MET 1  
42 1 Y 1 C ALA 2  ? C ALA 2  
43 1 Y 1 C THR 3  ? C THR 3  
44 1 Y 1 C ASN 4  ? C ASN 4  
45 1 Y 1 C GLU 5  ? C GLU 5  
46 1 Y 1 C ASP 6  ? C ASP 6  
47 1 Y 1 C GLN 7  ? C GLN 7  
48 1 Y 1 C LYS 8  ? C LYS 8  
49 1 Y 1 C GLN 9  ? C GLN 9  
50 1 Y 1 C THR 10 ? C THR 10 
51 1 Y 1 C GLU 11 ? C GLU 11 
52 1 Y 1 C SER 12 ? C SER 12 
53 1 Y 1 C GLY 13 ? C GLY 13 
54 1 Y 1 C ARG 14 ? C ARG 14 
55 1 Y 1 C HIS 15 ? C HIS 15 
56 1 Y 1 C GLN 16 ? C GLN 16 
57 1 Y 1 C GLU 17 ? C GLU 17 
58 1 Y 1 C VAL 18 ? C VAL 18 
59 1 Y 1 C GLY 19 ? C GLY 19 
60 1 Y 1 C HIS 20 ? C HIS 20 
61 1 Y 1 D MET 1  ? D MET 1  
62 1 Y 1 D ALA 2  ? D ALA 2  
63 1 Y 1 D THR 3  ? D THR 3  
64 1 Y 1 D ASN 4  ? D ASN 4  
65 1 Y 1 D GLU 5  ? D GLU 5  
66 1 Y 1 D ASP 6  ? D ASP 6  
67 1 Y 1 D GLN 7  ? D GLN 7  
68 1 Y 1 D LYS 8  ? D LYS 8  
69 1 Y 1 D GLN 9  ? D GLN 9  
70 1 Y 1 D THR 10 ? D THR 10 
71 1 Y 1 D GLU 11 ? D GLU 11 
72 1 Y 1 D SER 12 ? D SER 12 
73 1 Y 1 D GLY 13 ? D GLY 13 
74 1 Y 1 D ARG 14 ? D ARG 14 
75 1 Y 1 D HIS 15 ? D HIS 15 
76 1 Y 1 D GLN 16 ? D GLN 16 
77 1 Y 1 D GLU 17 ? D GLU 17 
78 1 Y 1 D VAL 18 ? D VAL 18 
79 1 Y 1 D GLY 19 ? D GLY 19 
80 1 Y 1 D HIS 20 ? D HIS 20 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CALCIUM ION'             CA  
3 S-ADENOSYL-L-HOMOCYSTEINE SAH 
4 'FERULOYL COENZYME A'     FRE 
5 water                     HOH 
#