data_1GBT
# 
_entry.id   1GBT 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1GBT         
WWPDB D_1000173508 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1GBT 
_pdbx_database_status.recvd_initial_deposition_date   1991-09-17 
_pdbx_database_status.deposit_site                    ? 
_pdbx_database_status.process_site                    ? 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Singer, P.T.' 1 
'Sweet, R.M.'  2 
# 
_citation.id                        primary 
_citation.title                     'Structure of an acyl-enzyme intermediate during catalysis: (guanidinobenzoyl)trypsin.' 
_citation.journal_abbrev            Biochemistry 
_citation.journal_volume            29 
_citation.page_first                8351 
_citation.page_last                 8357 
_citation.year                      1990 
_citation.journal_id_ASTM           BICHAW 
_citation.country                   US 
_citation.journal_id_ISSN           0006-2960 
_citation.journal_id_CSD            0033 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   2252895 
_citation.pdbx_database_id_DOI      10.1021/bi00488a022 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Mangel, W.F.'    1 
primary 'Singer, P.T.'    2 
primary 'Cyr, D.M.'       3 
primary 'Umland, T.C.'    4 
primary 'Toledo, D.L.'    5 
primary 'Stroud, R.M.'    6 
primary 'Pflugrath, J.W.' 7 
primary 'Sweet, R.M.'     8 
# 
_cell.entry_id           1GBT 
_cell.length_a           63.740 
_cell.length_b           63.540 
_cell.length_c           68.930 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1GBT 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
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 BETA-TRYPSIN              23324.287 1   3.4.21.4 ? ? ? 
2 non-polymer syn 'CALCIUM ION'             40.078    1   ?        ? ? ? 
3 non-polymer syn 'SULFATE ION'             96.063    2   ?        ? ? ? 
4 non-polymer syn '4-GUANIDINOBENZOIC ACID' 179.176   1   ?        ? ? ? 
5 water       nat water                     18.015    117 ?        ? ? ? 
# 
_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       
;IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEGNEQFISASKSIVHPSYNSNT
LNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNM
FCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEGNEQFISASKSIVHPSYNSNT
LNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNM
FCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN
;
_entity_poly.pdbx_strand_id                 A 
_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   ILE n 
1 2   VAL n 
1 3   GLY n 
1 4   GLY n 
1 5   TYR n 
1 6   THR n 
1 7   CYS n 
1 8   GLY n 
1 9   ALA n 
1 10  ASN n 
1 11  THR n 
1 12  VAL n 
1 13  PRO n 
1 14  TYR n 
1 15  GLN n 
1 16  VAL n 
1 17  SER n 
1 18  LEU n 
1 19  ASN n 
1 20  SER n 
1 21  GLY n 
1 22  TYR n 
1 23  HIS n 
1 24  PHE n 
1 25  CYS n 
1 26  GLY n 
1 27  GLY n 
1 28  SER n 
1 29  LEU n 
1 30  ILE n 
1 31  ASN n 
1 32  SER n 
1 33  GLN n 
1 34  TRP n 
1 35  VAL n 
1 36  VAL n 
1 37  SER n 
1 38  ALA n 
1 39  ALA n 
1 40  HIS n 
1 41  CYS n 
1 42  TYR n 
1 43  LYS n 
1 44  SER n 
1 45  GLY n 
1 46  ILE n 
1 47  GLN n 
1 48  VAL n 
1 49  ARG n 
1 50  LEU n 
1 51  GLY n 
1 52  GLU n 
1 53  ASP n 
1 54  ASN n 
1 55  ILE n 
1 56  ASN n 
1 57  VAL n 
1 58  VAL n 
1 59  GLU n 
1 60  GLY n 
1 61  ASN n 
1 62  GLU n 
1 63  GLN n 
1 64  PHE n 
1 65  ILE n 
1 66  SER n 
1 67  ALA n 
1 68  SER n 
1 69  LYS n 
1 70  SER n 
1 71  ILE n 
1 72  VAL n 
1 73  HIS n 
1 74  PRO n 
1 75  SER n 
1 76  TYR n 
1 77  ASN n 
1 78  SER n 
1 79  ASN n 
1 80  THR n 
1 81  LEU n 
1 82  ASN n 
1 83  ASN n 
1 84  ASP n 
1 85  ILE n 
1 86  MET n 
1 87  LEU n 
1 88  ILE n 
1 89  LYS n 
1 90  LEU n 
1 91  LYS n 
1 92  SER n 
1 93  ALA n 
1 94  ALA n 
1 95  SER n 
1 96  LEU n 
1 97  ASN n 
1 98  SER n 
1 99  ARG n 
1 100 VAL n 
1 101 ALA n 
1 102 SER n 
1 103 ILE n 
1 104 SER n 
1 105 LEU n 
1 106 PRO n 
1 107 THR n 
1 108 SER n 
1 109 CYS n 
1 110 ALA n 
1 111 SER n 
1 112 ALA n 
1 113 GLY n 
1 114 THR n 
1 115 GLN n 
1 116 CYS n 
1 117 LEU n 
1 118 ILE n 
1 119 SER n 
1 120 GLY n 
1 121 TRP n 
1 122 GLY n 
1 123 ASN n 
1 124 THR n 
1 125 LYS n 
1 126 SER n 
1 127 SER n 
1 128 GLY n 
1 129 THR n 
1 130 SER n 
1 131 TYR n 
1 132 PRO n 
1 133 ASP n 
1 134 VAL n 
1 135 LEU n 
1 136 LYS n 
1 137 CYS n 
1 138 LEU n 
1 139 LYS n 
1 140 ALA n 
1 141 PRO n 
1 142 ILE n 
1 143 LEU n 
1 144 SER n 
1 145 ASP n 
1 146 SER n 
1 147 SER n 
1 148 CYS n 
1 149 LYS n 
1 150 SER n 
1 151 ALA n 
1 152 TYR n 
1 153 PRO n 
1 154 GLY n 
1 155 GLN n 
1 156 ILE n 
1 157 THR n 
1 158 SER n 
1 159 ASN n 
1 160 MET n 
1 161 PHE n 
1 162 CYS n 
1 163 ALA n 
1 164 GLY n 
1 165 TYR n 
1 166 LEU n 
1 167 GLU n 
1 168 GLY n 
1 169 GLY n 
1 170 LYS n 
1 171 ASP n 
1 172 SER n 
1 173 CYS n 
1 174 GLN n 
1 175 GLY n 
1 176 ASP n 
1 177 SER n 
1 178 GLY n 
1 179 GLY n 
1 180 PRO n 
1 181 VAL n 
1 182 VAL n 
1 183 CYS n 
1 184 SER n 
1 185 GLY n 
1 186 LYS n 
1 187 LEU n 
1 188 GLN n 
1 189 GLY n 
1 190 ILE n 
1 191 VAL n 
1 192 SER n 
1 193 TRP n 
1 194 GLY n 
1 195 SER n 
1 196 GLY n 
1 197 CYS n 
1 198 ALA n 
1 199 GLN n 
1 200 LYS n 
1 201 ASN n 
1 202 LYS n 
1 203 PRO n 
1 204 GLY n 
1 205 VAL n 
1 206 TYR n 
1 207 THR n 
1 208 LYS n 
1 209 VAL n 
1 210 CYS n 
1 211 ASN n 
1 212 TYR n 
1 213 VAL n 
1 214 SER n 
1 215 TRP n 
1 216 ILE n 
1 217 LYS n 
1 218 GLN n 
1 219 THR n 
1 220 ILE n 
1 221 ALA n 
1 222 SER n 
1 223 ASN 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               cattle 
_entity_src_gen.gene_src_genus                     Bos 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Bos taurus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9913 
_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      ? 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     ? 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    TRY1_BOVIN 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          P00760 
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_seq_one_letter_code   
;FIFLALLGAAVAFPVDDDDKIVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEG
NEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKA
PILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTI
ASN
;
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              1GBT 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 223 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00760 
_struct_ref_seq.db_align_beg                  21 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  243 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       16 
_struct_ref_seq.pdbx_auth_seq_align_end       245 
# 
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 
GBS non-polymer         . '4-GUANIDINOBENZOIC ACID' ? 'C8 H9 N3 O2'    179.176 
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 
SER 'L-peptide linking' y SERINE                    ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'             ? 'O4 S -2'        96.063  
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          1GBT 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   ? 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.99 
_exptl_crystal.density_percent_sol   58.88 
_exptl_crystal.description           ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           ? 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   . 
_diffrn_radiation_wavelength.wt           1.0 
# 
_refine.entry_id                                 1GBT 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             7.0 
_refine.ls_d_res_high                            2.0 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          0.162 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1629 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         15 
_refine_hist.number_atoms_solvent             117 
_refine_hist.number_atoms_total               1761 
_refine_hist.d_res_high                       2.0 
_refine_hist.d_res_low                        7.0 
# 
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 
t_bond_d           0.018 ? ? ? 'X-RAY DIFFRACTION' ? 
t_angle_deg        3.6   ? ? ? 'X-RAY DIFFRACTION' ? 
t_dihedral_angle_d ?     ? ? ? 'X-RAY DIFFRACTION' ? 
t_incorr_chiral_ct ?     ? ? ? 'X-RAY DIFFRACTION' ? 
t_pseud_angle      ?     ? ? ? 'X-RAY DIFFRACTION' ? 
t_trig_c_planes    ?     ? ? ? 'X-RAY DIFFRACTION' ? 
t_gen_planes       ?     ? ? ? 'X-RAY DIFFRACTION' ? 
t_it               ?     ? ? ? 'X-RAY DIFFRACTION' ? 
t_nbd              ?     ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_struct.entry_id                  1GBT 
_struct.title                     'STRUCTURE OF AN ACYL-ENZYME INTERMEDIATE DURING CATALYSIS: (GUANIDINOBENZOYL) TRYPSIN' 
_struct.pdbx_descriptor           'BETA-TRYPSIN (E.C.3.4.21.4) GUANIDINOBENZOYLATED AT SERINE 195 (PH 5.5)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1GBT 
_struct_keywords.pdbx_keywords   'HYDROLASE(SERINE PROTEINASE)' 
_struct_keywords.text            'HYDROLASE(SERINE PROTEINASE)' 
# 
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 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_biol.id   1 
# 
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 H1 SER A 144 ? ILE A 156 ? SER A 164 ILE A 176 1 'SNGL ALPHA TURN,REST IRREG.' 13 
HELX_P HELX_P2 H2 LYS A 208 ? VAL A 213 ? LYS A 230 VAL A 235 5 'CONTIGUOUS WITH H3'          6  
HELX_P HELX_P3 H3 SER A 214 ? ASN A 223 ? SER A 236 ASN A 245 1 'CONTIGUOUS WITH H2'          10 
# 
_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 
disulf1 disulf ? ? A CYS 7   SG ? ? ? 1_555 A CYS 137 SG  ? ? A CYS 22  A CYS 157 1_555 ? ? ? ? ? ? ? 1.993 ? 
disulf2 disulf ? ? A CYS 25  SG ? ? ? 1_555 A CYS 41  SG  ? ? A CYS 42  A CYS 58  1_555 ? ? ? ? ? ? ? 2.045 ? 
disulf3 disulf ? ? A CYS 109 SG ? ? ? 1_555 A CYS 210 SG  ? ? A CYS 128 A CYS 232 1_555 ? ? ? ? ? ? ? 1.985 ? 
disulf4 disulf ? ? A CYS 116 SG ? ? ? 1_555 A CYS 183 SG  ? ? A CYS 136 A CYS 201 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf5 disulf ? ? A CYS 148 SG ? ? ? 1_555 A CYS 162 SG  ? ? A CYS 168 A CYS 182 1_555 ? ? ? ? ? ? ? 1.999 ? 
disulf6 disulf ? ? A CYS 173 SG ? ? ? 1_555 A CYS 197 SG  ? ? A CYS 191 A CYS 220 1_555 ? ? ? ? ? ? ? 2.086 ? 
covale1 covale ? ? A SER 177 OG ? ? ? 1_555 E GBS .   CD  ? ? A SER 195 A GBS 704 1_555 ? ? ? ? ? ? ? 1.240 ? 
metalc1 metalc ? ? B CA  .   CA ? ? ? 1_555 A GLU 52  OE1 ? ? A CA  701 A GLU 70  1_555 ? ? ? ? ? ? ? 2.249 ? 
metalc2 metalc ? ? B CA  .   CA ? ? ? 1_555 A ASN 54  O   ? ? A CA  701 A ASN 72  1_555 ? ? ? ? ? ? ? 2.065 ? 
metalc3 metalc ? ? B CA  .   CA ? ? ? 1_555 A VAL 57  O   ? ? A CA  701 A VAL 75  1_555 ? ? ? ? ? ? ? 2.226 ? 
metalc4 metalc ? ? B CA  .   CA ? ? ? 1_555 F HOH .   O   ? ? A CA  701 A HOH 275 1_555 ? ? ? ? ? ? ? 2.292 ? 
metalc5 metalc ? ? B CA  .   CA ? ? ? 1_555 A GLU 62  OE2 ? ? A CA  701 A GLU 80  1_555 ? ? ? ? ? ? ? 2.386 ? 
metalc6 metalc ? ? B CA  .   CA ? ? ? 1_555 F HOH .   O   ? ? A CA  701 A HOH 274 1_555 ? ? ? ? ? ? ? 2.258 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 7 ? 
B ? 7 ? 
# 
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 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
A 4 5 ? anti-parallel 
A 5 6 ? anti-parallel 
A 6 7 ? anti-parallel 
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
B 4 5 ? anti-parallel 
B 5 6 ? anti-parallel 
B 6 7 ? 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 TYR A 5   ? THR A 6   ? TYR A 20  THR A 21  
A 2 LYS A 136 ? PRO A 141 ? LYS A 156 PRO A 161 
A 3 GLN A 115 ? GLY A 120 ? GLN A 135 GLY A 140 
A 4 PRO A 180 ? CYS A 183 ? PRO A 198 CYS A 201 
A 5 LYS A 186 ? GLY A 194 ? LYS A 204 GLY A 216 
A 6 GLY A 204 ? LYS A 208 ? GLY A 226 LYS A 230 
A 7 MET A 160 ? ALA A 163 ? MET A 180 ALA A 183 
B 1 GLN A 15  ? ASN A 19  ? GLN A 30  ASN A 34  
B 2 HIS A 23  ? ASN A 31  ? HIS A 40  ASN A 48  
B 3 TRP A 34  ? SER A 37  ? TRP A 51  SER A 54  
B 4 MET A 86  ? LEU A 90  ? MET A 104 LEU A 108 
B 5 GLN A 63  ? VAL A 72  ? GLN A 81  VAL A 90  
B 6 GLN A 47  ? LEU A 50  ? GLN A 64  LEU A 66  
B 7 GLN A 15  ? ASN A 19  ? GLN A 30  ASN A 34  
# 
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 TYR A 5   ? O TYR A 20  N CYS A 137 ? N CYS A 157 
A 2 3 N ALA A 140 ? N ALA A 160 O CYS A 116 ? O CYS A 136 
A 3 4 N SER A 119 ? N SER A 139 O PRO A 180 ? O PRO A 198 
A 4 5 N CYS A 183 ? N CYS A 201 O LYS A 186 ? O LYS A 204 
A 5 6 O TRP A 193 ? O TRP A 215 N VAL A 205 ? N VAL A 227 
A 6 7 N TYR A 206 ? N TYR A 228 O PHE A 161 ? O PHE A 181 
B 1 2 O LEU A 18  ? O LEU A 33  N PHE A 24  ? N PHE A 41  
B 2 3 N ILE A 30  ? N ILE A 47  O TRP A 34  ? O TRP A 51  
B 3 4 O SER A 37  ? O SER A 54  N MET A 86  ? N MET A 104 
B 4 5 O LYS A 89  ? O LYS A 107 N SER A 68  ? N SER A 86  
B 5 6 N ILE A 65  ? N ILE A 83  O VAL A 48  ? O VAL A 65  
# 
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 ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA A 701'  
AC2 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE SO4 A 702' 
AC3 Software ? ? ? ? 14 'BINDING SITE FOR RESIDUE GBS A 704' 
# 
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 6  GLU A 52  ? GLU A 70  . ? 1_555 ? 
2  AC1 6  ASN A 54  ? ASN A 72  . ? 1_555 ? 
3  AC1 6  VAL A 57  ? VAL A 75  . ? 1_555 ? 
4  AC1 6  GLU A 62  ? GLU A 80  . ? 1_555 ? 
5  AC1 6  HOH F .   ? HOH A 274 . ? 1_555 ? 
6  AC1 6  HOH F .   ? HOH A 275 . ? 1_555 ? 
7  AC2 2  GLY A 154 ? GLY A 174 . ? 1_555 ? 
8  AC2 2  HOH F .   ? HOH A 902 . ? 1_555 ? 
9  AC3 14 ASP A 171 ? ASP A 189 . ? 1_555 ? 
10 AC3 14 SER A 172 ? SER A 190 . ? 1_555 ? 
11 AC3 14 CYS A 173 ? CYS A 191 . ? 1_555 ? 
12 AC3 14 GLN A 174 ? GLN A 192 . ? 1_555 ? 
13 AC3 14 GLY A 175 ? GLY A 193 . ? 1_555 ? 
14 AC3 14 SER A 177 ? SER A 195 . ? 1_555 ? 
15 AC3 14 VAL A 191 ? VAL A 213 . ? 1_555 ? 
16 AC3 14 SER A 192 ? SER A 214 . ? 1_555 ? 
17 AC3 14 TRP A 193 ? TRP A 215 . ? 1_555 ? 
18 AC3 14 GLY A 194 ? GLY A 216 . ? 1_555 ? 
19 AC3 14 GLY A 196 ? GLY A 219 . ? 1_555 ? 
20 AC3 14 GLY A 204 ? GLY A 226 . ? 1_555 ? 
21 AC3 14 HOH F .   ? HOH A 246 . ? 1_555 ? 
22 AC3 14 HOH F .   ? HOH A 340 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1GBT 
_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                    1GBT 
_atom_sites.fract_transf_matrix[1][1]   0.015689 
_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]   0.015738 
_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]   0.014507 
_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  
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   . ILE A 1 1   ? 52.964 -3.112  26.624 1.00 3.47  ? 16  ILE A N   1 
ATOM   2    C  CA  . ILE A 1 1   ? 53.055 -3.510  25.229 1.00 4.91  ? 16  ILE A CA  1 
ATOM   3    C  C   . ILE A 1 1   ? 53.304 -4.997  25.114 1.00 5.54  ? 16  ILE A C   1 
ATOM   4    O  O   . ILE A 1 1   ? 54.376 -5.474  25.448 1.00 6.12  ? 16  ILE A O   1 
ATOM   5    C  CB  . ILE A 1 1   ? 54.056 -2.740  24.416 1.00 5.05  ? 16  ILE A CB  1 
ATOM   6    C  CG1 . ILE A 1 1   ? 53.772 -1.246  24.573 1.00 5.56  ? 16  ILE A CG1 1 
ATOM   7    C  CG2 . ILE A 1 1   ? 54.001 -3.116  22.951 1.00 4.93  ? 16  ILE A CG2 1 
ATOM   8    C  CD1 . ILE A 1 1   ? 52.447 -0.761  23.966 1.00 3.83  ? 16  ILE A CD1 1 
ATOM   9    N  N   . VAL A 1 2   ? 52.416 -5.739  24.493 1.00 6.01  ? 17  VAL A N   1 
ATOM   10   C  CA  . VAL A 1 2   ? 52.672 -7.136  24.238 1.00 8.44  ? 17  VAL A CA  1 
ATOM   11   C  C   . VAL A 1 2   ? 53.275 -7.342  22.866 1.00 10.66 ? 17  VAL A C   1 
ATOM   12   O  O   . VAL A 1 2   ? 52.596 -6.953  21.957 1.00 10.65 ? 17  VAL A O   1 
ATOM   13   C  CB  . VAL A 1 2   ? 51.378 -7.980  24.329 1.00 7.91  ? 17  VAL A CB  1 
ATOM   14   C  CG1 . VAL A 1 2   ? 51.762 -9.408  24.033 1.00 6.75  ? 17  VAL A CG1 1 
ATOM   15   C  CG2 . VAL A 1 2   ? 50.901 -8.021  25.776 1.00 8.86  ? 17  VAL A CG2 1 
ATOM   16   N  N   . GLY A 1 3   ? 54.481 -7.952  22.658 1.00 12.12 ? 18  GLY A N   1 
ATOM   17   C  CA  . GLY A 1 3   ? 55.036 -8.189  21.363 1.00 11.29 ? 18  GLY A CA  1 
ATOM   18   C  C   . GLY A 1 3   ? 55.718 -7.019  20.696 1.00 10.21 ? 18  GLY A C   1 
ATOM   19   O  O   . GLY A 1 3   ? 55.820 -7.111  19.454 1.00 8.62  ? 18  GLY A O   1 
ATOM   20   N  N   . GLY A 1 4   ? 56.134 -6.020  21.468 1.00 10.23 ? 19  GLY A N   1 
ATOM   21   C  CA  . GLY A 1 4   ? 56.766 -4.851  20.860 1.00 10.88 ? 19  GLY A CA  1 
ATOM   22   C  C   . GLY A 1 4   ? 58.293 -4.975  20.976 1.00 12.40 ? 19  GLY A C   1 
ATOM   23   O  O   . GLY A 1 4   ? 58.702 -6.100  21.171 1.00 13.63 ? 19  GLY A O   1 
ATOM   24   N  N   . TYR A 1 5   ? 59.092 -3.921  20.909 1.00 11.43 ? 20  TYR A N   1 
ATOM   25   C  CA  . TYR A 1 5   ? 60.522 -3.909  21.002 1.00 10.85 ? 20  TYR A CA  1 
ATOM   26   C  C   . TYR A 1 5   ? 60.848 -2.771  21.959 1.00 10.55 ? 20  TYR A C   1 
ATOM   27   O  O   . TYR A 1 5   ? 60.034 -1.927  22.311 1.00 8.94  ? 20  TYR A O   1 
ATOM   28   C  CB  . TYR A 1 5   ? 61.055 -3.735  19.574 1.00 11.56 ? 20  TYR A CB  1 
ATOM   29   C  CG  . TYR A 1 5   ? 60.594 -2.496  18.858 1.00 11.88 ? 20  TYR A CG  1 
ATOM   30   C  CD1 . TYR A 1 5   ? 59.386 -2.497  18.148 1.00 13.06 ? 20  TYR A CD1 1 
ATOM   31   C  CD2 . TYR A 1 5   ? 61.306 -1.297  18.877 1.00 12.13 ? 20  TYR A CD2 1 
ATOM   32   C  CE1 . TYR A 1 5   ? 58.993 -1.394  17.410 1.00 12.97 ? 20  TYR A CE1 1 
ATOM   33   C  CE2 . TYR A 1 5   ? 60.849 -0.148  18.229 1.00 12.92 ? 20  TYR A CE2 1 
ATOM   34   C  CZ  . TYR A 1 5   ? 59.668 -0.183  17.502 1.00 13.23 ? 20  TYR A CZ  1 
ATOM   35   O  OH  . TYR A 1 5   ? 59.148 0.916   16.846 1.00 13.95 ? 20  TYR A OH  1 
ATOM   36   N  N   . THR A 1 6   ? 62.036 -2.780  22.569 1.00 10.73 ? 21  THR A N   1 
ATOM   37   C  CA  . THR A 1 6   ? 62.425 -1.656  23.394 1.00 7.73  ? 21  THR A CA  1 
ATOM   38   C  C   . THR A 1 6   ? 62.506 -0.454  22.497 1.00 5.49  ? 21  THR A C   1 
ATOM   39   O  O   . THR A 1 6   ? 63.197 -0.479  21.556 1.00 3.17  ? 21  THR A O   1 
ATOM   40   C  CB  . THR A 1 6   ? 63.793 -2.040  23.855 1.00 7.98  ? 21  THR A CB  1 
ATOM   41   O  OG1 . THR A 1 6   ? 63.396 -3.007  24.785 1.00 8.22  ? 21  THR A OG1 1 
ATOM   42   C  CG2 . THR A 1 6   ? 64.442 -0.913  24.661 1.00 8.93  ? 21  THR A CG2 1 
ATOM   43   N  N   . CYS A 1 7   ? 61.909 0.698   22.743 1.00 5.60  ? 22  CYS A N   1 
ATOM   44   C  CA  . CYS A 1 7   ? 62.150 1.776   21.826 1.00 6.40  ? 22  CYS A CA  1 
ATOM   45   C  C   . CYS A 1 7   ? 63.573 2.358   21.743 1.00 9.21  ? 22  CYS A C   1 
ATOM   46   O  O   . CYS A 1 7   ? 63.989 2.820   20.666 1.00 11.60 ? 22  CYS A O   1 
ATOM   47   C  CB  . CYS A 1 7   ? 61.296 2.901   22.439 1.00 5.96  ? 22  CYS A CB  1 
ATOM   48   S  SG  . CYS A 1 7   ? 59.527 2.623   22.667 1.00 5.96  ? 22  CYS A SG  1 
ATOM   49   N  N   . GLY A 1 8   ? 64.329 2.525   22.820 1.00 10.21 ? 23  GLY A N   1 
ATOM   50   C  CA  . GLY A 1 8   ? 65.582 3.242   22.720 1.00 10.85 ? 23  GLY A CA  1 
ATOM   51   C  C   . GLY A 1 8   ? 65.247 4.497   23.489 1.00 11.70 ? 23  GLY A C   1 
ATOM   52   O  O   . GLY A 1 8   ? 64.161 5.087   23.297 1.00 13.18 ? 23  GLY A O   1 
ATOM   53   N  N   . ALA A 1 9   ? 66.121 4.817   24.443 1.00 10.71 ? 24  ALA A N   1 
ATOM   54   C  CA  . ALA A 1 9   ? 65.950 5.894   25.394 1.00 10.01 ? 24  ALA A CA  1 
ATOM   55   C  C   . ALA A 1 9   ? 65.762 7.191   24.689 1.00 10.81 ? 24  ALA A C   1 
ATOM   56   O  O   . ALA A 1 9   ? 66.534 7.474   23.758 1.00 11.06 ? 24  ALA A O   1 
ATOM   57   C  CB  . ALA A 1 9   ? 67.159 6.074   26.287 1.00 9.67  ? 24  ALA A CB  1 
ATOM   58   N  N   . ASN A 1 10  ? 64.712 7.905   25.095 1.00 11.34 ? 25  ASN A N   1 
ATOM   59   C  CA  . ASN A 1 10  ? 64.325 9.230   24.611 1.00 12.67 ? 25  ASN A CA  1 
ATOM   60   C  C   . ASN A 1 10  ? 63.886 9.271   23.152 1.00 12.97 ? 25  ASN A C   1 
ATOM   61   O  O   . ASN A 1 10  ? 63.738 10.295  22.474 1.00 13.78 ? 25  ASN A O   1 
ATOM   62   C  CB  . ASN A 1 10  ? 65.381 10.361  24.929 1.00 13.36 ? 25  ASN A CB  1 
ATOM   63   C  CG  . ASN A 1 10  ? 65.617 10.308  26.428 1.00 14.02 ? 25  ASN A CG  1 
ATOM   64   O  OD1 . ASN A 1 10  ? 64.570 10.292  27.081 1.00 15.32 ? 25  ASN A OD1 1 
ATOM   65   N  ND2 . ASN A 1 10  ? 66.737 9.911   27.011 1.00 13.61 ? 25  ASN A ND2 1 
ATOM   66   N  N   . THR A 1 11  ? 63.598 8.135   22.559 1.00 12.15 ? 26  THR A N   1 
ATOM   67   C  CA  . THR A 1 11  ? 63.213 8.254   21.129 1.00 10.27 ? 26  THR A CA  1 
ATOM   68   C  C   . THR A 1 11  ? 61.772 8.586   20.912 1.00 8.57  ? 26  THR A C   1 
ATOM   69   O  O   . THR A 1 11  ? 61.265 8.732   19.788 1.00 9.45  ? 26  THR A O   1 
ATOM   70   C  CB  . THR A 1 11  ? 63.528 6.999   20.294 1.00 8.97  ? 26  THR A CB  1 
ATOM   71   O  OG1 . THR A 1 11  ? 62.999 5.909   21.019 1.00 8.80  ? 26  THR A OG1 1 
ATOM   72   C  CG2 . THR A 1 11  ? 65.071 6.934   20.245 1.00 8.92  ? 26  THR A CG2 1 
ATOM   73   N  N   . VAL A 1 12  ? 60.992 8.548   21.974 1.00 7.54  ? 27  VAL A N   1 
ATOM   74   C  CA  . VAL A 1 12  ? 59.558 8.858   21.857 1.00 6.55  ? 27  VAL A CA  1 
ATOM   75   C  C   . VAL A 1 12  ? 59.345 10.023  22.803 1.00 6.09  ? 27  VAL A C   1 
ATOM   76   O  O   . VAL A 1 12  ? 58.842 9.860   23.900 1.00 5.13  ? 27  VAL A O   1 
ATOM   77   C  CB  . VAL A 1 12  ? 58.727 7.661   22.311 1.00 7.26  ? 27  VAL A CB  1 
ATOM   78   C  CG1 . VAL A 1 12  ? 57.305 8.065   21.988 1.00 6.48  ? 27  VAL A CG1 1 
ATOM   79   C  CG2 . VAL A 1 12  ? 59.015 6.502   21.358 1.00 9.33  ? 27  VAL A CG2 1 
ATOM   80   N  N   . PRO A 1 13  ? 59.880 11.219  22.533 1.00 6.04  ? 28  PRO A N   1 
ATOM   81   C  CA  . PRO A 1 13  ? 59.973 12.375  23.460 1.00 6.35  ? 28  PRO A CA  1 
ATOM   82   C  C   . PRO A 1 13  ? 58.674 12.978  24.034 1.00 5.73  ? 28  PRO A C   1 
ATOM   83   O  O   . PRO A 1 13  ? 58.643 13.747  25.031 1.00 6.19  ? 28  PRO A O   1 
ATOM   84   C  CB  . PRO A 1 13  ? 60.804 13.450  22.711 1.00 7.15  ? 28  PRO A CB  1 
ATOM   85   C  CG  . PRO A 1 13  ? 60.677 13.013  21.234 1.00 6.78  ? 28  PRO A CG  1 
ATOM   86   C  CD  . PRO A 1 13  ? 60.336 11.517  21.184 1.00 5.45  ? 28  PRO A CD  1 
ATOM   87   N  N   . TYR A 1 14  ? 57.528 12.615  23.452 1.00 3.90  ? 29  TYR A N   1 
ATOM   88   C  CA  . TYR A 1 14  ? 56.265 13.145  23.922 1.00 3.63  ? 29  TYR A CA  1 
ATOM   89   C  C   . TYR A 1 14  ? 55.564 12.178  24.858 1.00 4.99  ? 29  TYR A C   1 
ATOM   90   O  O   . TYR A 1 14  ? 54.497 12.426  25.451 1.00 4.12  ? 29  TYR A O   1 
ATOM   91   C  CB  . TYR A 1 14  ? 55.326 13.334  22.705 1.00 2.97  ? 29  TYR A CB  1 
ATOM   92   C  CG  . TYR A 1 14  ? 55.268 12.120  21.809 1.00 2.92  ? 29  TYR A CG  1 
ATOM   93   C  CD1 . TYR A 1 14  ? 54.335 11.084  22.026 1.00 2.53  ? 29  TYR A CD1 1 
ATOM   94   C  CD2 . TYR A 1 14  ? 56.042 12.043  20.640 1.00 3.91  ? 29  TYR A CD2 1 
ATOM   95   C  CE1 . TYR A 1 14  ? 54.309 9.993   21.157 1.00 4.35  ? 29  TYR A CE1 1 
ATOM   96   C  CE2 . TYR A 1 14  ? 56.101 10.912  19.837 1.00 5.71  ? 29  TYR A CE2 1 
ATOM   97   C  CZ  . TYR A 1 14  ? 55.166 9.925   20.052 1.00 6.64  ? 29  TYR A CZ  1 
ATOM   98   O  OH  . TYR A 1 14  ? 55.183 8.833   19.221 1.00 8.13  ? 29  TYR A OH  1 
ATOM   99   N  N   . GLN A 1 15  ? 56.274 11.068  25.108 1.00 6.01  ? 30  GLN A N   1 
ATOM   100  C  CA  . GLN A 1 15  ? 55.702 10.063  25.950 1.00 4.57  ? 30  GLN A CA  1 
ATOM   101  C  C   . GLN A 1 15  ? 55.835 10.458  27.393 1.00 5.68  ? 30  GLN A C   1 
ATOM   102  O  O   . GLN A 1 15  ? 56.870 10.851  27.912 1.00 7.35  ? 30  GLN A O   1 
ATOM   103  C  CB  . GLN A 1 15  ? 56.176 8.638   25.625 1.00 3.42  ? 30  GLN A CB  1 
ATOM   104  C  CG  . GLN A 1 15  ? 55.799 7.609   26.702 1.00 2.85  ? 30  GLN A CG  1 
ATOM   105  C  CD  . GLN A 1 15  ? 54.486 6.914   26.419 1.00 2.34  ? 30  GLN A CD  1 
ATOM   106  O  OE1 . GLN A 1 15  ? 53.675 6.682   27.339 1.00 2.42  ? 30  GLN A OE1 1 
ATOM   107  N  NE2 . GLN A 1 15  ? 54.410 6.414   25.216 1.00 2.00  ? 30  GLN A NE2 1 
ATOM   108  N  N   . VAL A 1 16  ? 54.701 10.407  28.094 1.00 4.79  ? 31  VAL A N   1 
ATOM   109  C  CA  . VAL A 1 16  ? 54.725 10.639  29.523 1.00 3.94  ? 31  VAL A CA  1 
ATOM   110  C  C   . VAL A 1 16  ? 54.211 9.446   30.336 1.00 3.32  ? 31  VAL A C   1 
ATOM   111  O  O   . VAL A 1 16  ? 53.481 8.582   29.861 1.00 2.00  ? 31  VAL A O   1 
ATOM   112  C  CB  . VAL A 1 16  ? 54.015 11.891  30.041 1.00 4.65  ? 31  VAL A CB  1 
ATOM   113  C  CG1 . VAL A 1 16  ? 54.078 12.966  28.961 1.00 6.20  ? 31  VAL A CG1 1 
ATOM   114  C  CG2 . VAL A 1 16  ? 52.575 11.810  30.445 1.00 2.85  ? 31  VAL A CG2 1 
ATOM   115  N  N   . SER A 1 17  ? 54.662 9.430   31.604 1.00 3.56  ? 32  SER A N   1 
ATOM   116  C  CA  . SER A 1 17  ? 54.317 8.409   32.590 1.00 3.65  ? 32  SER A CA  1 
ATOM   117  C  C   . SER A 1 17  ? 53.480 9.105   33.634 1.00 4.34  ? 32  SER A C   1 
ATOM   118  O  O   . SER A 1 17  ? 53.904 10.112  34.220 1.00 4.38  ? 32  SER A O   1 
ATOM   119  C  CB  . SER A 1 17  ? 55.527 7.918   33.410 1.00 2.22  ? 32  SER A CB  1 
ATOM   120  O  OG  . SER A 1 17  ? 55.083 6.936   34.313 1.00 2.00  ? 32  SER A OG  1 
ATOM   121  N  N   . LEU A 1 18  ? 52.250 8.628   33.893 1.00 5.29  ? 33  LEU A N   1 
ATOM   122  C  CA  . LEU A 1 18  ? 51.439 9.223   34.948 1.00 5.56  ? 33  LEU A CA  1 
ATOM   123  C  C   . LEU A 1 18  ? 51.805 8.475   36.235 1.00 4.56  ? 33  LEU A C   1 
ATOM   124  O  O   . LEU A 1 18  ? 51.784 7.261   36.230 1.00 4.45  ? 33  LEU A O   1 
ATOM   125  C  CB  . LEU A 1 18  ? 49.933 9.185   34.639 1.00 6.05  ? 33  LEU A CB  1 
ATOM   126  C  CG  . LEU A 1 18  ? 49.591 10.067  33.438 1.00 4.46  ? 33  LEU A CG  1 
ATOM   127  C  CD1 . LEU A 1 18  ? 48.086 10.162  33.387 1.00 3.07  ? 33  LEU A CD1 1 
ATOM   128  C  CD2 . LEU A 1 18  ? 50.245 11.424  33.367 1.00 2.16  ? 33  LEU A CD2 1 
ATOM   129  N  N   . ASN A 1 19  ? 52.156 9.117   37.355 1.00 4.95  ? 34  ASN A N   1 
ATOM   130  C  CA  . ASN A 1 19  ? 52.657 8.412   38.520 1.00 5.07  ? 34  ASN A CA  1 
ATOM   131  C  C   . ASN A 1 19  ? 52.026 8.853   39.845 1.00 5.85  ? 34  ASN A C   1 
ATOM   132  O  O   . ASN A 1 19  ? 51.937 9.987   40.205 1.00 6.50  ? 34  ASN A O   1 
ATOM   133  C  CB  . ASN A 1 19  ? 54.151 8.728   38.605 1.00 6.31  ? 34  ASN A CB  1 
ATOM   134  C  CG  . ASN A 1 19  ? 54.845 7.990   39.729 1.00 7.63  ? 34  ASN A CG  1 
ATOM   135  O  OD1 . ASN A 1 19  ? 55.624 7.031   39.502 1.00 10.31 ? 34  ASN A OD1 1 
ATOM   136  N  ND2 . ASN A 1 19  ? 54.668 8.451   40.935 1.00 6.46  ? 34  ASN A ND2 1 
ATOM   137  N  N   . SER A 1 20  ? 51.630 7.922   40.670 1.00 6.39  ? 37  SER A N   1 
ATOM   138  C  CA  . SER A 1 20  ? 51.154 8.182   41.984 1.00 9.65  ? 37  SER A CA  1 
ATOM   139  C  C   . SER A 1 20  ? 51.835 7.235   42.977 1.00 9.95  ? 37  SER A C   1 
ATOM   140  O  O   . SER A 1 20  ? 51.129 6.569   43.728 1.00 11.24 ? 37  SER A O   1 
ATOM   141  C  CB  . SER A 1 20  ? 49.621 7.942   42.034 1.00 12.81 ? 37  SER A CB  1 
ATOM   142  O  OG  . SER A 1 20  ? 49.193 6.592   41.821 1.00 15.01 ? 37  SER A OG  1 
ATOM   143  N  N   . GLY A 1 21  ? 53.168 7.057   42.936 1.00 8.71  ? 38  GLY A N   1 
ATOM   144  C  CA  . GLY A 1 21  ? 53.912 6.128   43.779 1.00 7.08  ? 38  GLY A CA  1 
ATOM   145  C  C   . GLY A 1 21  ? 54.232 4.933   42.913 1.00 6.38  ? 38  GLY A C   1 
ATOM   146  O  O   . GLY A 1 21  ? 54.915 4.096   43.451 1.00 7.15  ? 38  GLY A O   1 
ATOM   147  N  N   . TYR A 1 22  ? 53.797 4.918   41.651 1.00 5.63  ? 39  TYR A N   1 
ATOM   148  C  CA  . TYR A 1 22  ? 54.107 3.842   40.731 1.00 6.40  ? 39  TYR A CA  1 
ATOM   149  C  C   . TYR A 1 22  ? 53.487 4.351   39.428 1.00 5.92  ? 39  TYR A C   1 
ATOM   150  O  O   . TYR A 1 22  ? 52.727 5.301   39.561 1.00 5.44  ? 39  TYR A O   1 
ATOM   151  C  CB  . TYR A 1 22  ? 53.589 2.474   41.180 1.00 7.97  ? 39  TYR A CB  1 
ATOM   152  C  CG  . TYR A 1 22  ? 52.065 2.563   41.376 1.00 8.79  ? 39  TYR A CG  1 
ATOM   153  C  CD1 . TYR A 1 22  ? 51.500 3.226   42.461 1.00 8.73  ? 39  TYR A CD1 1 
ATOM   154  C  CD2 . TYR A 1 22  ? 51.157 2.071   40.445 1.00 9.20  ? 39  TYR A CD2 1 
ATOM   155  C  CE1 . TYR A 1 22  ? 50.175 3.594   42.577 1.00 8.09  ? 39  TYR A CE1 1 
ATOM   156  C  CE2 . TYR A 1 22  ? 49.778 2.305   40.559 1.00 9.03  ? 39  TYR A CE2 1 
ATOM   157  C  CZ  . TYR A 1 22  ? 49.322 3.083   41.616 1.00 9.14  ? 39  TYR A CZ  1 
ATOM   158  O  OH  . TYR A 1 22  ? 47.997 3.203   41.809 1.00 11.31 ? 39  TYR A OH  1 
ATOM   159  N  N   . HIS A 1 23  ? 53.874 3.780   38.285 1.00 5.06  ? 40  HIS A N   1 
ATOM   160  C  CA  . HIS A 1 23  ? 53.424 4.152   37.004 1.00 4.85  ? 40  HIS A CA  1 
ATOM   161  C  C   . HIS A 1 23  ? 52.048 3.569   36.855 1.00 5.88  ? 40  HIS A C   1 
ATOM   162  O  O   . HIS A 1 23  ? 51.868 2.396   37.115 1.00 5.66  ? 40  HIS A O   1 
ATOM   163  C  CB  . HIS A 1 23  ? 54.313 3.539   35.907 1.00 4.28  ? 40  HIS A CB  1 
ATOM   164  C  CG  . HIS A 1 23  ? 53.633 3.608   34.592 1.00 3.27  ? 40  HIS A CG  1 
ATOM   165  N  ND1 . HIS A 1 23  ? 53.671 4.718   33.765 1.00 2.95  ? 40  HIS A ND1 1 
ATOM   166  C  CD2 . HIS A 1 23  ? 52.917 2.648   33.956 1.00 4.29  ? 40  HIS A CD2 1 
ATOM   167  C  CE1 . HIS A 1 23  ? 53.011 4.428   32.661 1.00 3.34  ? 40  HIS A CE1 1 
ATOM   168  N  NE2 . HIS A 1 23  ? 52.480 3.192   32.749 1.00 3.76  ? 40  HIS A NE2 1 
ATOM   169  N  N   . PHE A 1 24  ? 51.069 4.388   36.461 1.00 7.41  ? 41  PHE A N   1 
ATOM   170  C  CA  . PHE A 1 24  ? 49.732 3.831   36.254 1.00 6.40  ? 41  PHE A CA  1 
ATOM   171  C  C   . PHE A 1 24  ? 49.090 4.094   34.912 1.00 6.21  ? 41  PHE A C   1 
ATOM   172  O  O   . PHE A 1 24  ? 48.098 3.426   34.587 1.00 7.44  ? 41  PHE A O   1 
ATOM   173  C  CB  . PHE A 1 24  ? 48.792 4.189   37.368 1.00 5.91  ? 41  PHE A CB  1 
ATOM   174  C  CG  . PHE A 1 24  ? 48.449 5.668   37.432 1.00 6.64  ? 41  PHE A CG  1 
ATOM   175  C  CD1 . PHE A 1 24  ? 47.366 6.179   36.716 1.00 6.05  ? 41  PHE A CD1 1 
ATOM   176  C  CD2 . PHE A 1 24  ? 49.180 6.549   38.225 1.00 6.03  ? 41  PHE A CD2 1 
ATOM   177  C  CE1 . PHE A 1 24  ? 46.972 7.507   36.782 1.00 5.59  ? 41  PHE A CE1 1 
ATOM   178  C  CE2 . PHE A 1 24  ? 48.749 7.868   38.346 1.00 6.53  ? 41  PHE A CE2 1 
ATOM   179  C  CZ  . PHE A 1 24  ? 47.659 8.383   37.627 1.00 5.97  ? 41  PHE A CZ  1 
ATOM   180  N  N   . CYS A 1 25  ? 49.547 5.091   34.171 1.00 3.82  ? 42  CYS A N   1 
ATOM   181  C  CA  . CYS A 1 25  ? 49.003 5.223   32.868 1.00 2.22  ? 42  CYS A CA  1 
ATOM   182  C  C   . CYS A 1 25  ? 49.984 6.018   32.023 1.00 2.00  ? 42  CYS A C   1 
ATOM   183  O  O   . CYS A 1 25  ? 50.840 6.608   32.626 1.00 2.00  ? 42  CYS A O   1 
ATOM   184  C  CB  . CYS A 1 25  ? 47.706 5.988   32.856 1.00 2.02  ? 42  CYS A CB  1 
ATOM   185  S  SG  . CYS A 1 25  ? 46.115 5.159   33.169 1.00 3.97  ? 42  CYS A SG  1 
ATOM   186  N  N   . GLY A 1 26  ? 49.852 6.103   30.719 1.00 2.00  ? 43  GLY A N   1 
ATOM   187  C  CA  . GLY A 1 26  ? 50.763 7.076   30.112 1.00 2.00  ? 43  GLY A CA  1 
ATOM   188  C  C   . GLY A 1 26  ? 49.942 8.301   29.670 1.00 2.37  ? 43  GLY A C   1 
ATOM   189  O  O   . GLY A 1 26  ? 48.781 8.576   30.027 1.00 2.00  ? 43  GLY A O   1 
ATOM   190  N  N   . GLY A 1 27  ? 50.560 9.092   28.854 1.00 2.87  ? 44  GLY A N   1 
ATOM   191  C  CA  . GLY A 1 27  ? 49.902 10.268  28.247 1.00 3.91  ? 44  GLY A CA  1 
ATOM   192  C  C   . GLY A 1 27  ? 50.911 10.782  27.200 1.00 3.33  ? 44  GLY A C   1 
ATOM   193  O  O   . GLY A 1 27  ? 52.002 10.170  27.042 1.00 2.00  ? 44  GLY A O   1 
ATOM   194  N  N   . SER A 1 28  ? 50.487 11.894  26.600 1.00 5.08  ? 45  SER A N   1 
ATOM   195  C  CA  . SER A 1 28  ? 51.350 12.500  25.558 1.00 5.95  ? 45  SER A CA  1 
ATOM   196  C  C   . SER A 1 28  ? 51.523 13.994  25.833 1.00 5.67  ? 45  SER A C   1 
ATOM   197  O  O   . SER A 1 28  ? 50.519 14.467  26.248 1.00 3.72  ? 45  SER A O   1 
ATOM   198  C  CB  . SER A 1 28  ? 50.499 12.539  24.333 1.00 5.34  ? 45  SER A CB  1 
ATOM   199  O  OG  . SER A 1 28  ? 50.292 11.223  23.995 1.00 5.71  ? 45  SER A OG  1 
ATOM   200  N  N   . LEU A 1 29  ? 52.680 14.650  25.635 1.00 5.80  ? 46  LEU A N   1 
ATOM   201  C  CA  . LEU A 1 29  ? 52.870 16.030  25.871 1.00 4.72  ? 46  LEU A CA  1 
ATOM   202  C  C   . LEU A 1 29  ? 52.416 16.691  24.579 1.00 5.17  ? 46  LEU A C   1 
ATOM   203  O  O   . LEU A 1 29  ? 52.757 16.413  23.443 1.00 4.83  ? 46  LEU A O   1 
ATOM   204  C  CB  . LEU A 1 29  ? 54.349 16.282  26.204 1.00 3.65  ? 46  LEU A CB  1 
ATOM   205  C  CG  . LEU A 1 29  ? 54.651 17.727  26.604 1.00 2.92  ? 46  LEU A CG  1 
ATOM   206  C  CD1 . LEU A 1 29  ? 54.318 17.868  28.084 1.00 2.30  ? 46  LEU A CD1 1 
ATOM   207  C  CD2 . LEU A 1 29  ? 56.137 17.960  26.417 1.00 2.77  ? 46  LEU A CD2 1 
ATOM   208  N  N   . ILE A 1 30  ? 51.436 17.564  24.713 1.00 6.61  ? 47  ILE A N   1 
ATOM   209  C  CA  . ILE A 1 30  ? 51.025 18.162  23.453 1.00 8.07  ? 47  ILE A CA  1 
ATOM   210  C  C   . ILE A 1 30  ? 51.436 19.607  23.455 1.00 8.73  ? 47  ILE A C   1 
ATOM   211  O  O   . ILE A 1 30  ? 51.322 20.229  22.430 1.00 8.25  ? 47  ILE A O   1 
ATOM   212  C  CB  . ILE A 1 30  ? 49.516 18.162  23.199 1.00 7.99  ? 47  ILE A CB  1 
ATOM   213  C  CG1 . ILE A 1 30  ? 48.913 18.731  24.442 1.00 7.63  ? 47  ILE A CG1 1 
ATOM   214  C  CG2 . ILE A 1 30  ? 48.891 16.779  23.132 1.00 9.39  ? 47  ILE A CG2 1 
ATOM   215  C  CD1 . ILE A 1 30  ? 47.392 18.664  24.301 1.00 8.85  ? 47  ILE A CD1 1 
ATOM   216  N  N   . ASN A 1 31  ? 51.944 20.088  24.564 1.00 9.53  ? 48  ASN A N   1 
ATOM   217  C  CA  . ASN A 1 31  ? 52.544 21.399  24.574 1.00 9.75  ? 48  ASN A CA  1 
ATOM   218  C  C   . ASN A 1 31  ? 53.312 21.622  25.847 1.00 9.98  ? 48  ASN A C   1 
ATOM   219  O  O   . ASN A 1 31  ? 53.166 20.792  26.715 1.00 11.08 ? 48  ASN A O   1 
ATOM   220  C  CB  . ASN A 1 31  ? 51.653 22.587  24.263 1.00 11.16 ? 48  ASN A CB  1 
ATOM   221  C  CG  . ASN A 1 31  ? 50.635 22.989  25.304 1.00 13.47 ? 48  ASN A CG  1 
ATOM   222  O  OD1 . ASN A 1 31  ? 50.695 22.854  26.551 1.00 15.23 ? 48  ASN A OD1 1 
ATOM   223  N  ND2 . ASN A 1 31  ? 49.457 23.133  24.683 1.00 13.88 ? 48  ASN A ND2 1 
ATOM   224  N  N   . SER A 1 32  ? 54.000 22.710  26.068 1.00 9.87  ? 49  SER A N   1 
ATOM   225  C  CA  . SER A 1 32  ? 54.771 22.789  27.263 1.00 12.29 ? 49  SER A CA  1 
ATOM   226  C  C   . SER A 1 32  ? 54.147 22.692  28.654 1.00 11.40 ? 49  SER A C   1 
ATOM   227  O  O   . SER A 1 32  ? 54.694 22.451  29.725 1.00 9.88  ? 49  SER A O   1 
ATOM   228  C  CB  . SER A 1 32  ? 55.651 23.982  27.063 1.00 15.06 ? 49  SER A CB  1 
ATOM   229  O  OG  . SER A 1 32  ? 54.822 24.906  27.717 1.00 15.39 ? 49  SER A OG  1 
ATOM   230  N  N   . GLN A 1 33  ? 52.850 22.786  28.611 1.00 12.08 ? 50  GLN A N   1 
ATOM   231  C  CA  . GLN A 1 33  ? 52.114 22.716  29.812 1.00 11.99 ? 50  GLN A CA  1 
ATOM   232  C  C   . GLN A 1 33  ? 50.917 21.813  29.780 1.00 8.74  ? 50  GLN A C   1 
ATOM   233  O  O   . GLN A 1 33  ? 50.224 21.802  30.784 1.00 7.59  ? 50  GLN A O   1 
ATOM   234  C  CB  . GLN A 1 33  ? 51.442 24.051  30.120 1.00 16.02 ? 50  GLN A CB  1 
ATOM   235  C  CG  . GLN A 1 33  ? 52.318 24.802  31.112 1.00 20.20 ? 50  GLN A CG  1 
ATOM   236  C  CD  . GLN A 1 33  ? 51.811 26.188  31.432 1.00 22.05 ? 50  GLN A CD  1 
ATOM   237  O  OE1 . GLN A 1 33  ? 51.337 26.226  32.569 1.00 21.94 ? 50  GLN A OE1 1 
ATOM   238  N  NE2 . GLN A 1 33  ? 51.713 27.090  30.408 1.00 22.94 ? 50  GLN A NE2 1 
ATOM   239  N  N   . TRP A 1 34  ? 50.621 21.097  28.703 1.00 6.65  ? 51  TRP A N   1 
ATOM   240  C  CA  . TRP A 1 34  ? 49.435 20.259  28.808 1.00 5.04  ? 51  TRP A CA  1 
ATOM   241  C  C   . TRP A 1 34  ? 49.668 18.912  28.174 1.00 3.53  ? 51  TRP A C   1 
ATOM   242  O  O   . TRP A 1 34  ? 50.321 18.835  27.167 1.00 2.30  ? 51  TRP A O   1 
ATOM   243  C  CB  . TRP A 1 34  ? 48.376 20.834  27.844 1.00 6.16  ? 51  TRP A CB  1 
ATOM   244  C  CG  . TRP A 1 34  ? 47.792 22.044  28.481 1.00 6.77  ? 51  TRP A CG  1 
ATOM   245  C  CD1 . TRP A 1 34  ? 48.086 23.339  28.162 1.00 6.93  ? 51  TRP A CD1 1 
ATOM   246  C  CD2 . TRP A 1 34  ? 46.565 22.065  29.216 1.00 6.32  ? 51  TRP A CD2 1 
ATOM   247  N  NE1 . TRP A 1 34  ? 47.221 24.191  28.800 1.00 6.46  ? 51  TRP A NE1 1 
ATOM   248  C  CE2 . TRP A 1 34  ? 46.263 23.425  29.441 1.00 7.29  ? 51  TRP A CE2 1 
ATOM   249  C  CE3 . TRP A 1 34  ? 45.744 21.099  29.762 1.00 5.10  ? 51  TRP A CE3 1 
ATOM   250  C  CZ2 . TRP A 1 34  ? 45.063 23.779  30.079 1.00 7.32  ? 51  TRP A CZ2 1 
ATOM   251  C  CZ3 . TRP A 1 34  ? 44.540 21.455  30.304 1.00 6.10  ? 51  TRP A CZ3 1 
ATOM   252  C  CH2 . TRP A 1 34  ? 44.285 22.778  30.644 1.00 7.32  ? 51  TRP A CH2 1 
ATOM   253  N  N   . VAL A 1 35  ? 49.229 17.871  28.880 1.00 4.70  ? 52  VAL A N   1 
ATOM   254  C  CA  . VAL A 1 35  ? 49.373 16.469  28.547 1.00 5.52  ? 52  VAL A CA  1 
ATOM   255  C  C   . VAL A 1 35  ? 47.950 15.932  28.238 1.00 6.09  ? 52  VAL A C   1 
ATOM   256  O  O   . VAL A 1 35  ? 46.977 16.373  28.828 1.00 6.05  ? 52  VAL A O   1 
ATOM   257  C  CB  . VAL A 1 35  ? 49.958 15.770  29.806 1.00 6.53  ? 52  VAL A CB  1 
ATOM   258  C  CG1 . VAL A 1 35  ? 49.729 14.256  29.706 1.00 7.55  ? 52  VAL A CG1 1 
ATOM   259  C  CG2 . VAL A 1 35  ? 51.411 16.169  30.031 1.00 6.78  ? 52  VAL A CG2 1 
ATOM   260  N  N   . VAL A 1 36  ? 47.779 15.062  27.219 1.00 6.33  ? 53  VAL A N   1 
ATOM   261  C  CA  . VAL A 1 36  ? 46.526 14.411  26.992 1.00 7.64  ? 53  VAL A CA  1 
ATOM   262  C  C   . VAL A 1 36  ? 46.728 12.910  27.407 1.00 5.71  ? 53  VAL A C   1 
ATOM   263  O  O   . VAL A 1 36  ? 47.720 12.192  27.120 1.00 4.88  ? 53  VAL A O   1 
ATOM   264  C  CB  . VAL A 1 36  ? 46.009 14.601  25.533 1.00 11.08 ? 53  VAL A CB  1 
ATOM   265  C  CG1 . VAL A 1 36  ? 47.106 14.022  24.702 1.00 13.29 ? 53  VAL A CG1 1 
ATOM   266  C  CG2 . VAL A 1 36  ? 44.901 13.594  25.282 1.00 11.90 ? 53  VAL A CG2 1 
ATOM   267  N  N   . SER A 1 37  ? 45.704 12.387  28.058 1.00 3.78  ? 54  SER A N   1 
ATOM   268  C  CA  . SER A 1 37  ? 45.634 11.039  28.559 1.00 2.37  ? 54  SER A CA  1 
ATOM   269  C  C   . SER A 1 37  ? 44.147 10.542  28.453 1.00 2.37  ? 54  SER A C   1 
ATOM   270  O  O   . SER A 1 37  ? 43.320 11.185  27.764 1.00 2.00  ? 54  SER A O   1 
ATOM   271  C  CB  . SER A 1 37  ? 46.199 11.055  29.960 1.00 2.00  ? 54  SER A CB  1 
ATOM   272  O  OG  . SER A 1 37  ? 46.172 9.709   30.383 1.00 2.00  ? 54  SER A OG  1 
ATOM   273  N  N   . ALA A 1 38  ? 43.799 9.372   29.067 1.00 2.00  ? 55  ALA A N   1 
ATOM   274  C  CA  . ALA A 1 38  ? 42.453 8.874   28.947 1.00 2.00  ? 55  ALA A CA  1 
ATOM   275  C  C   . ALA A 1 38  ? 41.748 9.302   30.239 1.00 2.59  ? 55  ALA A C   1 
ATOM   276  O  O   . ALA A 1 38  ? 42.294 9.432   31.311 1.00 2.00  ? 55  ALA A O   1 
ATOM   277  C  CB  . ALA A 1 38  ? 42.349 7.361   28.755 1.00 2.00  ? 55  ALA A CB  1 
ATOM   278  N  N   . ALA A 1 39  ? 40.443 9.593   30.123 1.00 3.39  ? 56  ALA A N   1 
ATOM   279  C  CA  . ALA A 1 39  ? 39.589 9.949   31.240 1.00 3.55  ? 56  ALA A CA  1 
ATOM   280  C  C   . ALA A 1 39  ? 39.601 8.827   32.277 1.00 5.25  ? 56  ALA A C   1 
ATOM   281  O  O   . ALA A 1 39  ? 39.585 9.061   33.509 1.00 5.69  ? 56  ALA A O   1 
ATOM   282  C  CB  . ALA A 1 39  ? 38.192 10.151  30.710 1.00 3.68  ? 56  ALA A CB  1 
ATOM   283  N  N   . HIS A 1 40  ? 39.685 7.578   31.876 1.00 6.88  ? 57  HIS A N   1 
ATOM   284  C  CA  . HIS A 1 40  ? 39.770 6.442   32.854 1.00 7.10  ? 57  HIS A CA  1 
ATOM   285  C  C   . HIS A 1 40  ? 41.083 6.378   33.662 1.00 6.76  ? 57  HIS A C   1 
ATOM   286  O  O   . HIS A 1 40  ? 41.106 5.661   34.662 1.00 8.03  ? 57  HIS A O   1 
ATOM   287  C  CB  . HIS A 1 40  ? 39.376 5.049   32.292 1.00 6.94  ? 57  HIS A CB  1 
ATOM   288  C  CG  . HIS A 1 40  ? 40.423 4.246   31.566 1.00 8.79  ? 57  HIS A CG  1 
ATOM   289  N  ND1 . HIS A 1 40  ? 40.634 4.223   30.154 1.00 8.19  ? 57  HIS A ND1 1 
ATOM   290  C  CD2 . HIS A 1 40  ? 41.331 3.390   32.118 1.00 9.52  ? 57  HIS A CD2 1 
ATOM   291  C  CE1 . HIS A 1 40  ? 41.608 3.373   29.876 1.00 8.81  ? 57  HIS A CE1 1 
ATOM   292  N  NE2 . HIS A 1 40  ? 42.028 2.839   31.050 1.00 9.85  ? 57  HIS A NE2 1 
ATOM   293  N  N   . CYS A 1 41  ? 42.112 7.169   33.348 1.00 4.74  ? 58  CYS A N   1 
ATOM   294  C  CA  . CYS A 1 41  ? 43.358 7.240   34.093 1.00 6.55  ? 58  CYS A CA  1 
ATOM   295  C  C   . CYS A 1 41  ? 43.268 8.247   35.233 1.00 9.44  ? 58  CYS A C   1 
ATOM   296  O  O   . CYS A 1 41  ? 44.081 8.397   36.141 1.00 9.62  ? 58  CYS A O   1 
ATOM   297  C  CB  . CYS A 1 41  ? 44.500 7.706   33.144 1.00 5.03  ? 58  CYS A CB  1 
ATOM   298  S  SG  . CYS A 1 41  ? 44.748 6.241   32.100 1.00 4.49  ? 58  CYS A SG  1 
ATOM   299  N  N   . TYR A 1 42  ? 42.129 8.861   35.282 1.00 10.40 ? 59  TYR A N   1 
ATOM   300  C  CA  . TYR A 1 42  ? 41.878 9.866   36.264 1.00 10.93 ? 59  TYR A CA  1 
ATOM   301  C  C   . TYR A 1 42  ? 42.019 9.452   37.692 1.00 10.04 ? 59  TYR A C   1 
ATOM   302  O  O   . TYR A 1 42  ? 41.440 8.467   38.162 1.00 9.17  ? 59  TYR A O   1 
ATOM   303  C  CB  . TYR A 1 42  ? 40.566 10.627  35.991 1.00 12.12 ? 59  TYR A CB  1 
ATOM   304  C  CG  . TYR A 1 42  ? 40.358 11.633  37.094 1.00 13.99 ? 59  TYR A CG  1 
ATOM   305  C  CD1 . TYR A 1 42  ? 40.959 12.876  37.065 1.00 14.71 ? 59  TYR A CD1 1 
ATOM   306  C  CD2 . TYR A 1 42  ? 39.668 11.260  38.240 1.00 15.53 ? 59  TYR A CD2 1 
ATOM   307  C  CE1 . TYR A 1 42  ? 40.864 13.767  38.136 1.00 15.67 ? 59  TYR A CE1 1 
ATOM   308  C  CE2 . TYR A 1 42  ? 39.572 12.090  39.356 1.00 16.76 ? 59  TYR A CE2 1 
ATOM   309  C  CZ  . TYR A 1 42  ? 40.198 13.348  39.293 1.00 17.07 ? 59  TYR A CZ  1 
ATOM   310  O  OH  . TYR A 1 42  ? 40.064 14.082  40.423 1.00 18.25 ? 59  TYR A OH  1 
ATOM   311  N  N   . LYS A 1 43  ? 42.794 10.258  38.395 1.00 8.64  ? 60  LYS A N   1 
ATOM   312  C  CA  . LYS A 1 43  ? 42.817 10.138  39.813 1.00 10.61 ? 60  LYS A CA  1 
ATOM   313  C  C   . LYS A 1 43  ? 43.425 11.412  40.328 1.00 11.03 ? 60  LYS A C   1 
ATOM   314  O  O   . LYS A 1 43  ? 44.048 12.207  39.633 1.00 9.71  ? 60  LYS A O   1 
ATOM   315  C  CB  . LYS A 1 43  ? 43.476 8.897   40.370 1.00 14.20 ? 60  LYS A CB  1 
ATOM   316  C  CG  . LYS A 1 43  ? 45.012 8.763   40.278 1.00 17.12 ? 60  LYS A CG  1 
ATOM   317  C  CD  . LYS A 1 43  ? 45.280 7.263   40.016 0.91 18.48 ? 60  LYS A CD  1 
ATOM   318  C  CE  . LYS A 1 43  ? 46.518 6.701   40.672 0.67 19.29 ? 60  LYS A CE  1 
ATOM   319  N  NZ  . LYS A 1 43  ? 46.459 5.246   40.875 0.31 19.75 ? 60  LYS A NZ  1 
ATOM   320  N  N   . SER A 1 44  ? 43.328 11.594  41.594 1.00 14.32 ? 61  SER A N   1 
ATOM   321  C  CA  . SER A 1 44  ? 43.992 12.744  42.172 1.00 17.89 ? 61  SER A CA  1 
ATOM   322  C  C   . SER A 1 44  ? 45.417 12.455  42.610 1.00 18.92 ? 61  SER A C   1 
ATOM   323  O  O   . SER A 1 44  ? 45.786 11.290  42.694 1.00 21.47 ? 61  SER A O   1 
ATOM   324  C  CB  . SER A 1 44  ? 43.325 13.197  43.431 1.00 20.58 ? 61  SER A CB  1 
ATOM   325  O  OG  . SER A 1 44  ? 43.654 12.116  44.298 1.00 23.36 ? 61  SER A OG  1 
ATOM   326  N  N   . GLY A 1 45  ? 46.247 13.459  42.912 1.00 17.31 ? 62  GLY A N   1 
ATOM   327  C  CA  . GLY A 1 45  ? 47.604 13.050  43.294 1.00 16.41 ? 62  GLY A CA  1 
ATOM   328  C  C   . GLY A 1 45  ? 48.435 12.478  42.160 1.00 16.32 ? 62  GLY A C   1 
ATOM   329  O  O   . GLY A 1 45  ? 49.263 11.598  42.446 1.00 19.18 ? 62  GLY A O   1 
ATOM   330  N  N   . ILE A 1 46  ? 48.368 13.044  40.962 1.00 13.07 ? 63  ILE A N   1 
ATOM   331  C  CA  . ILE A 1 46  ? 49.185 12.629  39.834 1.00 11.14 ? 63  ILE A CA  1 
ATOM   332  C  C   . ILE A 1 46  ? 50.411 13.534  39.612 1.00 10.41 ? 63  ILE A C   1 
ATOM   333  O  O   . ILE A 1 46  ? 50.282 14.745  39.661 1.00 11.23 ? 63  ILE A O   1 
ATOM   334  C  CB  . ILE A 1 46  ? 48.301 12.543  38.598 1.00 10.16 ? 63  ILE A CB  1 
ATOM   335  C  CG1 . ILE A 1 46  ? 47.061 11.699  38.694 1.00 8.67  ? 63  ILE A CG1 1 
ATOM   336  C  CG2 . ILE A 1 46  ? 49.012 12.501  37.252 1.00 10.34 ? 63  ILE A CG2 1 
ATOM   337  C  CD1 . ILE A 1 46  ? 46.239 12.000  37.443 1.00 8.86  ? 63  ILE A CD1 1 
ATOM   338  N  N   . GLN A 1 47  ? 51.593 12.934  39.470 1.00 9.19  ? 64  GLN A N   1 
ATOM   339  C  CA  . GLN A 1 47  ? 52.845 13.544  39.099 1.00 8.82  ? 64  GLN A CA  1 
ATOM   340  C  C   . GLN A 1 47  ? 53.104 13.112  37.656 1.00 9.12  ? 64  GLN A C   1 
ATOM   341  O  O   . GLN A 1 47  ? 53.001 11.903  37.396 1.00 10.68 ? 64  GLN A O   1 
ATOM   342  C  CB  . GLN A 1 47  ? 53.973 13.108  40.023 1.00 9.43  ? 64  GLN A CB  1 
ATOM   343  C  CG  . GLN A 1 47  ? 55.372 13.615  39.605 1.00 11.10 ? 64  GLN A CG  1 
ATOM   344  C  CD  . GLN A 1 47  ? 56.390 13.076  40.571 1.00 11.67 ? 64  GLN A CD  1 
ATOM   345  O  OE1 . GLN A 1 47  ? 56.602 13.788  41.530 1.00 13.07 ? 64  GLN A OE1 1 
ATOM   346  N  NE2 . GLN A 1 47  ? 56.765 11.802  40.472 1.00 10.76 ? 64  GLN A NE2 1 
ATOM   347  N  N   . VAL A 1 48  ? 53.286 14.049  36.740 1.00 7.01  ? 65  VAL A N   1 
ATOM   348  C  CA  . VAL A 1 48  ? 53.669 13.749  35.382 1.00 6.30  ? 65  VAL A CA  1 
ATOM   349  C  C   . VAL A 1 48  ? 55.206 13.616  35.303 1.00 8.06  ? 65  VAL A C   1 
ATOM   350  O  O   . VAL A 1 48  ? 55.958 14.520  35.809 1.00 8.49  ? 65  VAL A O   1 
ATOM   351  C  CB  . VAL A 1 48  ? 53.248 14.869  34.466 1.00 3.29  ? 65  VAL A CB  1 
ATOM   352  C  CG1 . VAL A 1 48  ? 53.443 14.503  32.976 1.00 2.74  ? 65  VAL A CG1 1 
ATOM   353  C  CG2 . VAL A 1 48  ? 51.746 15.034  34.758 1.00 3.04  ? 65  VAL A CG2 1 
ATOM   354  N  N   . ARG A 1 49  A 55.631 12.471  34.753 1.00 6.37  ? 65  ARG A N   1 
ATOM   355  C  CA  . ARG A 1 49  A 57.067 12.222  34.584 1.00 3.98  ? 65  ARG A CA  1 
ATOM   356  C  C   . ARG A 1 49  A 57.405 12.237  33.108 1.00 3.48  ? 65  ARG A C   1 
ATOM   357  O  O   . ARG A 1 49  A 56.930 11.359  32.379 1.00 3.23  ? 65  ARG A O   1 
ATOM   358  C  CB  . ARG A 1 49  A 57.472 10.926  35.247 1.00 3.99  ? 65  ARG A CB  1 
ATOM   359  C  CG  . ARG A 1 49  A 57.119 10.933  36.769 1.00 2.71  ? 65  ARG A CG  1 
ATOM   360  C  CD  . ARG A 1 49  A 57.612 9.704   37.542 1.00 2.00  ? 65  ARG A CD  1 
ATOM   361  N  NE  . ARG A 1 49  A 57.627 10.071  38.953 1.00 2.19  ? 65  ARG A NE  1 
ATOM   362  C  CZ  . ARG A 1 49  A 58.363 9.479   39.928 1.00 3.10  ? 65  ARG A CZ  1 
ATOM   363  N  NH1 . ARG A 1 49  A 59.087 8.429   39.638 1.00 2.00  ? 65  ARG A NH1 1 
ATOM   364  N  NH2 . ARG A 1 49  A 58.343 9.861   41.217 1.00 4.22  ? 65  ARG A NH2 1 
ATOM   365  N  N   . LEU A 1 50  ? 58.181 13.250  32.702 1.00 3.35  ? 66  LEU A N   1 
ATOM   366  C  CA  . LEU A 1 50  ? 58.699 13.455  31.347 1.00 5.28  ? 66  LEU A CA  1 
ATOM   367  C  C   . LEU A 1 50  ? 60.164 12.950  31.204 1.00 5.13  ? 66  LEU A C   1 
ATOM   368  O  O   . LEU A 1 50  ? 60.904 12.863  32.215 1.00 6.17  ? 66  LEU A O   1 
ATOM   369  C  CB  . LEU A 1 50  ? 58.635 14.956  30.936 1.00 6.29  ? 66  LEU A CB  1 
ATOM   370  C  CG  . LEU A 1 50  ? 57.332 15.753  31.227 1.00 9.88  ? 66  LEU A CG  1 
ATOM   371  C  CD1 . LEU A 1 50  ? 57.578 17.175  30.774 1.00 10.97 ? 66  LEU A CD1 1 
ATOM   372  C  CD2 . LEU A 1 50  ? 56.300 15.289  30.180 1.00 12.15 ? 66  LEU A CD2 1 
ATOM   373  N  N   . GLY A 1 51  ? 60.494 12.672  29.969 1.00 4.16  ? 69  GLY A N   1 
ATOM   374  C  CA  . GLY A 1 51  ? 61.833 12.301  29.641 1.00 3.56  ? 69  GLY A CA  1 
ATOM   375  C  C   . GLY A 1 51  ? 62.333 11.030  30.297 1.00 5.22  ? 69  GLY A C   1 
ATOM   376  O  O   . GLY A 1 51  ? 63.548 10.826  30.355 1.00 7.89  ? 69  GLY A O   1 
ATOM   377  N  N   . GLU A 1 52  ? 61.410 10.110  30.626 1.00 4.71  ? 70  GLU A N   1 
ATOM   378  C  CA  . GLU A 1 52  ? 61.769 8.829   31.147 1.00 3.21  ? 70  GLU A CA  1 
ATOM   379  C  C   . GLU A 1 52  ? 62.029 7.794   30.069 1.00 3.15  ? 70  GLU A C   1 
ATOM   380  O  O   . GLU A 1 52  ? 61.453 7.811   29.010 1.00 2.00  ? 70  GLU A O   1 
ATOM   381  C  CB  . GLU A 1 52  ? 60.631 8.196   31.902 1.00 2.26  ? 70  GLU A CB  1 
ATOM   382  C  CG  . GLU A 1 52  ? 60.304 9.016   33.165 1.00 3.05  ? 70  GLU A CG  1 
ATOM   383  C  CD  . GLU A 1 52  ? 61.095 8.506   34.308 1.00 6.55  ? 70  GLU A CD  1 
ATOM   384  O  OE1 . GLU A 1 52  ? 62.192 7.878   33.901 1.00 7.79  ? 70  GLU A OE1 1 
ATOM   385  O  OE2 . GLU A 1 52  ? 60.776 8.611   35.473 1.00 7.80  ? 70  GLU A OE2 1 
ATOM   386  N  N   . ASP A 1 53  ? 62.942 6.851   30.388 1.00 4.61  ? 71  ASP A N   1 
ATOM   387  C  CA  . ASP A 1 53  ? 63.238 5.604   29.656 1.00 4.98  ? 71  ASP A CA  1 
ATOM   388  C  C   . ASP A 1 53  ? 63.019 4.578   30.782 1.00 5.14  ? 71  ASP A C   1 
ATOM   389  O  O   . ASP A 1 53  ? 61.930 4.030   30.939 1.00 4.68  ? 71  ASP A O   1 
ATOM   390  C  CB  . ASP A 1 53  ? 64.659 5.448   29.105 1.00 5.53  ? 71  ASP A CB  1 
ATOM   391  C  CG  . ASP A 1 53  ? 64.645 4.318   28.153 1.00 7.20  ? 71  ASP A CG  1 
ATOM   392  O  OD1 . ASP A 1 53  ? 63.471 4.161   27.586 1.00 8.52  ? 71  ASP A OD1 1 
ATOM   393  O  OD2 . ASP A 1 53  ? 65.520 3.493   28.085 1.00 8.41  ? 71  ASP A OD2 1 
ATOM   394  N  N   . ASN A 1 54  ? 64.073 4.322   31.603 1.00 4.57  ? 72  ASN A N   1 
ATOM   395  C  CA  . ASN A 1 54  ? 63.847 3.415   32.703 1.00 5.25  ? 72  ASN A CA  1 
ATOM   396  C  C   . ASN A 1 54  ? 63.123 4.208   33.800 1.00 6.82  ? 72  ASN A C   1 
ATOM   397  O  O   . ASN A 1 54  ? 63.512 5.217   34.433 1.00 5.26  ? 72  ASN A O   1 
ATOM   398  C  CB  . ASN A 1 54  ? 65.203 2.926   33.198 1.00 5.18  ? 72  ASN A CB  1 
ATOM   399  C  CG  . ASN A 1 54  ? 65.062 1.792   34.224 1.00 7.22  ? 72  ASN A CG  1 
ATOM   400  O  OD1 . ASN A 1 54  ? 65.932 0.902   34.223 1.00 10.90 ? 72  ASN A OD1 1 
ATOM   401  N  ND2 . ASN A 1 54  ? 64.173 1.828   35.178 1.00 4.96  ? 72  ASN A ND2 1 
ATOM   402  N  N   . ILE A 1 55  ? 61.916 3.715   34.131 1.00 8.79  ? 73  ILE A N   1 
ATOM   403  C  CA  . ILE A 1 55  ? 61.005 4.326   35.098 1.00 8.61  ? 73  ILE A CA  1 
ATOM   404  C  C   . ILE A 1 55  ? 61.350 3.980   36.543 1.00 7.97  ? 73  ILE A C   1 
ATOM   405  O  O   . ILE A 1 55  ? 60.750 4.541   37.416 1.00 6.11  ? 73  ILE A O   1 
ATOM   406  C  CB  . ILE A 1 55  ? 59.497 4.068   34.885 1.00 7.72  ? 73  ILE A CB  1 
ATOM   407  C  CG1 . ILE A 1 55  ? 59.252 2.557   34.831 1.00 7.07  ? 73  ILE A CG1 1 
ATOM   408  C  CG2 . ILE A 1 55  ? 58.946 4.765   33.648 1.00 7.41  ? 73  ILE A CG2 1 
ATOM   409  C  CD1 . ILE A 1 55  ? 57.745 2.397   35.006 1.00 6.94  ? 73  ILE A CD1 1 
ATOM   410  N  N   . ASN A 1 56  ? 62.265 3.032   36.711 1.00 9.49  ? 74  ASN A N   1 
ATOM   411  C  CA  . ASN A 1 56  ? 62.753 2.683   38.027 1.00 11.31 ? 74  ASN A CA  1 
ATOM   412  C  C   . ASN A 1 56  ? 64.034 3.353   38.463 1.00 10.39 ? 74  ASN A C   1 
ATOM   413  O  O   . ASN A 1 56  ? 64.310 3.087   39.639 1.00 10.72 ? 74  ASN A O   1 
ATOM   414  C  CB  . ASN A 1 56  ? 62.937 1.191   38.313 1.00 13.23 ? 74  ASN A CB  1 
ATOM   415  C  CG  . ASN A 1 56  ? 61.494 0.674   38.319 1.00 15.04 ? 74  ASN A CG  1 
ATOM   416  O  OD1 . ASN A 1 56  ? 61.091 -0.047  37.400 1.00 16.42 ? 74  ASN A OD1 1 
ATOM   417  N  ND2 . ASN A 1 56  ? 60.665 1.249   39.180 1.00 14.34 ? 74  ASN A ND2 1 
ATOM   418  N  N   . VAL A 1 57  ? 64.734 4.048   37.573 1.00 8.75  ? 75  VAL A N   1 
ATOM   419  C  CA  . VAL A 1 57  ? 66.030 4.625   37.830 1.00 8.89  ? 75  VAL A CA  1 
ATOM   420  C  C   . VAL A 1 57  ? 66.076 6.076   37.382 1.00 8.98  ? 75  VAL A C   1 
ATOM   421  O  O   . VAL A 1 57  ? 65.662 6.391   36.284 1.00 9.56  ? 75  VAL A O   1 
ATOM   422  C  CB  . VAL A 1 57  ? 67.142 3.896   37.030 1.00 7.97  ? 75  VAL A CB  1 
ATOM   423  C  CG1 . VAL A 1 57  ? 68.484 4.574   37.128 1.00 7.75  ? 75  VAL A CG1 1 
ATOM   424  C  CG2 . VAL A 1 57  ? 67.142 2.484   37.565 1.00 7.41  ? 75  VAL A CG2 1 
ATOM   425  N  N   . VAL A 1 58  ? 66.590 6.955   38.212 1.00 8.01  ? 76  VAL A N   1 
ATOM   426  C  CA  . VAL A 1 58  ? 66.775 8.264   37.639 1.00 9.25  ? 76  VAL A CA  1 
ATOM   427  C  C   . VAL A 1 58  ? 68.105 8.208   36.786 1.00 9.23  ? 76  VAL A C   1 
ATOM   428  O  O   . VAL A 1 58  ? 69.165 8.019   37.351 1.00 8.70  ? 76  VAL A O   1 
ATOM   429  C  CB  . VAL A 1 58  ? 66.963 9.278   38.779 1.00 9.37  ? 76  VAL A CB  1 
ATOM   430  C  CG1 . VAL A 1 58  ? 67.257 10.648  38.238 1.00 8.97  ? 76  VAL A CG1 1 
ATOM   431  C  CG2 . VAL A 1 58  ? 65.737 9.382   39.643 1.00 9.53  ? 76  VAL A CG2 1 
ATOM   432  N  N   . GLU A 1 59  ? 68.062 8.452   35.491 1.00 9.93  ? 77  GLU A N   1 
ATOM   433  C  CA  . GLU A 1 59  ? 69.173 8.336   34.605 1.00 10.21 ? 77  GLU A CA  1 
ATOM   434  C  C   . GLU A 1 59  ? 69.646 9.648   34.016 1.00 9.46  ? 77  GLU A C   1 
ATOM   435  O  O   . GLU A 1 59  ? 70.709 9.635   33.409 1.00 8.97  ? 77  GLU A O   1 
ATOM   436  C  CB  . GLU A 1 59  ? 68.689 7.533   33.392 1.00 11.09 ? 77  GLU A CB  1 
ATOM   437  C  CG  . GLU A 1 59  ? 67.999 6.211   33.740 1.00 13.31 ? 77  GLU A CG  1 
ATOM   438  C  CD  . GLU A 1 59  ? 67.786 5.379   32.503 1.00 15.66 ? 77  GLU A CD  1 
ATOM   439  O  OE1 . GLU A 1 59  ? 66.699 5.777   31.883 1.00 16.50 ? 77  GLU A OE1 1 
ATOM   440  O  OE2 . GLU A 1 59  ? 68.491 4.466   32.078 1.00 16.57 ? 77  GLU A OE2 1 
ATOM   441  N  N   . GLY A 1 60  ? 68.854 10.686  34.289 1.00 8.89  ? 78  GLY A N   1 
ATOM   442  C  CA  . GLY A 1 60  ? 69.011 12.031  33.846 1.00 9.84  ? 78  GLY A CA  1 
ATOM   443  C  C   . GLY A 1 60  ? 67.989 12.290  32.727 1.00 12.81 ? 78  GLY A C   1 
ATOM   444  O  O   . GLY A 1 60  ? 67.478 11.358  32.084 1.00 14.81 ? 78  GLY A O   1 
ATOM   445  N  N   . ASN A 1 61  ? 67.675 13.530  32.461 1.00 12.28 ? 79  ASN A N   1 
ATOM   446  C  CA  . ASN A 1 61  ? 66.729 13.923  31.404 1.00 12.98 ? 79  ASN A CA  1 
ATOM   447  C  C   . ASN A 1 61  ? 65.304 13.967  31.883 1.00 10.88 ? 79  ASN A C   1 
ATOM   448  O  O   . ASN A 1 61  ? 64.398 14.532  31.274 1.00 10.54 ? 79  ASN A O   1 
ATOM   449  C  CB  . ASN A 1 61  ? 66.672 13.204  30.052 1.00 16.30 ? 79  ASN A CB  1 
ATOM   450  C  CG  . ASN A 1 61  ? 68.025 13.218  29.416 1.00 19.84 ? 79  ASN A CG  1 
ATOM   451  O  OD1 . ASN A 1 61  ? 68.546 14.321  29.183 1.00 20.73 ? 79  ASN A OD1 1 
ATOM   452  N  ND2 . ASN A 1 61  ? 68.580 12.000  29.325 1.00 21.35 ? 79  ASN A ND2 1 
ATOM   453  N  N   . GLU A 1 62  ? 65.059 13.395  33.056 1.00 9.72  ? 80  GLU A N   1 
ATOM   454  C  CA  . GLU A 1 62  ? 63.717 13.372  33.672 1.00 8.13  ? 80  GLU A CA  1 
ATOM   455  C  C   . GLU A 1 62  ? 63.294 14.732  34.209 1.00 5.40  ? 80  GLU A C   1 
ATOM   456  O  O   . GLU A 1 62  ? 64.062 15.519  34.761 1.00 3.71  ? 80  GLU A O   1 
ATOM   457  C  CB  . GLU A 1 62  ? 63.619 12.331  34.830 1.00 9.74  ? 80  GLU A CB  1 
ATOM   458  C  CG  . GLU A 1 62  ? 63.846 10.837  34.462 1.00 11.12 ? 80  GLU A CG  1 
ATOM   459  C  CD  . GLU A 1 62  ? 65.256 10.415  34.846 1.00 12.33 ? 80  GLU A CD  1 
ATOM   460  O  OE1 . GLU A 1 62  ? 66.167 11.224  34.952 1.00 12.16 ? 80  GLU A OE1 1 
ATOM   461  O  OE2 . GLU A 1 62  ? 65.324 9.138   35.123 1.00 13.15 ? 80  GLU A OE2 1 
ATOM   462  N  N   . GLN A 1 63  ? 61.966 14.992  34.198 1.00 3.82  ? 81  GLN A N   1 
ATOM   463  C  CA  . GLN A 1 63  ? 61.353 16.200  34.717 1.00 2.56  ? 81  GLN A CA  1 
ATOM   464  C  C   . GLN A 1 63  ? 60.089 15.612  35.330 1.00 2.71  ? 81  GLN A C   1 
ATOM   465  O  O   . GLN A 1 63  ? 59.284 14.882  34.696 1.00 3.47  ? 81  GLN A O   1 
ATOM   466  C  CB  . GLN A 1 63  ? 60.991 17.289  33.648 1.00 2.00  ? 81  GLN A CB  1 
ATOM   467  C  CG  . GLN A 1 63  ? 62.287 17.785  32.977 1.00 2.77  ? 81  GLN A CG  1 
ATOM   468  C  CD  . GLN A 1 63  ? 61.882 18.719  31.808 1.00 3.89  ? 81  GLN A CD  1 
ATOM   469  O  OE1 . GLN A 1 63  ? 61.001 19.524  32.049 1.00 4.92  ? 81  GLN A OE1 1 
ATOM   470  N  NE2 . GLN A 1 63  ? 62.240 18.549  30.574 1.00 3.17  ? 81  GLN A NE2 1 
ATOM   471  N  N   . PHE A 1 64  ? 59.990 15.817  36.636 1.00 2.00  ? 82  PHE A N   1 
ATOM   472  C  CA  . PHE A 1 64  ? 58.850 15.403  37.457 1.00 2.86  ? 82  PHE A CA  1 
ATOM   473  C  C   . PHE A 1 64  ? 58.032 16.672  37.787 1.00 5.80  ? 82  PHE A C   1 
ATOM   474  O  O   . PHE A 1 64  ? 58.318 17.516  38.629 1.00 5.71  ? 82  PHE A O   1 
ATOM   475  C  CB  . PHE A 1 64  ? 59.242 14.792  38.794 1.00 2.00  ? 82  PHE A CB  1 
ATOM   476  C  CG  . PHE A 1 64  ? 59.981 13.524  38.556 1.00 2.61  ? 82  PHE A CG  1 
ATOM   477  C  CD1 . PHE A 1 64  ? 60.028 12.931  37.293 1.00 2.48  ? 82  PHE A CD1 1 
ATOM   478  C  CD2 . PHE A 1 64  ? 60.454 12.795  39.659 1.00 3.90  ? 82  PHE A CD2 1 
ATOM   479  C  CE1 . PHE A 1 64  ? 60.767 11.783  36.996 1.00 3.85  ? 82  PHE A CE1 1 
ATOM   480  C  CE2 . PHE A 1 64  ? 61.117 11.605  39.336 1.00 5.21  ? 82  PHE A CE2 1 
ATOM   481  C  CZ  . PHE A 1 64  ? 61.237 11.051  38.070 1.00 4.25  ? 82  PHE A CZ  1 
ATOM   482  N  N   . ILE A 1 65  ? 56.859 16.867  37.151 1.00 8.24  ? 83  ILE A N   1 
ATOM   483  C  CA  . ILE A 1 65  ? 56.111 18.080  37.353 1.00 8.30  ? 83  ILE A CA  1 
ATOM   484  C  C   . ILE A 1 65  ? 54.768 17.669  37.838 1.00 8.79  ? 83  ILE A C   1 
ATOM   485  O  O   . ILE A 1 65  ? 54.142 16.756  37.310 1.00 8.28  ? 83  ILE A O   1 
ATOM   486  C  CB  . ILE A 1 65  ? 55.901 18.748  36.006 1.00 7.45  ? 83  ILE A CB  1 
ATOM   487  C  CG1 . ILE A 1 65  ? 57.272 19.163  35.495 1.00 4.90  ? 83  ILE A CG1 1 
ATOM   488  C  CG2 . ILE A 1 65  ? 55.071 19.993  36.374 1.00 7.94  ? 83  ILE A CG2 1 
ATOM   489  C  CD1 . ILE A 1 65  ? 57.093 19.655  34.066 1.00 3.12  ? 83  ILE A CD1 1 
ATOM   490  N  N   . SER A 1 66  ? 54.268 18.188  38.936 1.00 10.15 ? 84  SER A N   1 
ATOM   491  C  CA  . SER A 1 66  ? 52.928 17.729  39.324 1.00 10.71 ? 84  SER A CA  1 
ATOM   492  C  C   . SER A 1 66  ? 51.814 18.193  38.379 1.00 10.12 ? 84  SER A C   1 
ATOM   493  O  O   . SER A 1 66  ? 51.865 19.197  37.661 1.00 9.93  ? 84  SER A O   1 
ATOM   494  C  CB  . SER A 1 66  ? 52.380 18.375  40.590 1.00 12.86 ? 84  SER A CB  1 
ATOM   495  O  OG  . SER A 1 66  ? 53.194 18.250  41.727 1.00 15.29 ? 84  SER A OG  1 
ATOM   496  N  N   . ALA A 1 67  ? 50.619 17.586  38.528 1.00 10.41 ? 85  ALA A N   1 
ATOM   497  C  CA  . ALA A 1 67  ? 49.469 17.974  37.739 1.00 11.27 ? 85  ALA A CA  1 
ATOM   498  C  C   . ALA A 1 67  ? 48.763 19.129  38.413 1.00 12.06 ? 85  ALA A C   1 
ATOM   499  O  O   . ALA A 1 67  ? 48.720 19.216  39.623 1.00 11.70 ? 85  ALA A O   1 
ATOM   500  C  CB  . ALA A 1 67  ? 48.493 16.861  37.357 1.00 11.53 ? 85  ALA A CB  1 
ATOM   501  N  N   . SER A 1 68  ? 48.352 20.182  37.693 1.00 13.13 ? 86  SER A N   1 
ATOM   502  C  CA  . SER A 1 68  ? 47.793 21.195  38.579 1.00 15.35 ? 86  SER A CA  1 
ATOM   503  C  C   . SER A 1 68  ? 46.300 21.024  38.416 1.00 15.93 ? 86  SER A C   1 
ATOM   504  O  O   . SER A 1 68  ? 45.567 21.228  39.355 1.00 16.73 ? 86  SER A O   1 
ATOM   505  C  CB  . SER A 1 68  ? 48.126 22.611  38.262 1.00 17.88 ? 86  SER A CB  1 
ATOM   506  O  OG  . SER A 1 68  ? 47.214 22.956  37.250 1.00 19.80 ? 86  SER A OG  1 
ATOM   507  N  N   . LYS A 1 69  ? 45.805 20.493  37.309 1.00 15.56 ? 87  LYS A N   1 
ATOM   508  C  CA  . LYS A 1 69  ? 44.396 20.140  37.245 1.00 16.10 ? 87  LYS A CA  1 
ATOM   509  C  C   . LYS A 1 69  ? 44.175 19.106  36.176 1.00 13.39 ? 87  LYS A C   1 
ATOM   510  O  O   . LYS A 1 69  ? 44.787 19.164  35.125 1.00 14.08 ? 87  LYS A O   1 
ATOM   511  C  CB  . LYS A 1 69  ? 43.512 21.317  36.902 1.00 18.60 ? 87  LYS A CB  1 
ATOM   512  C  CG  . LYS A 1 69  ? 43.863 21.931  35.579 1.00 21.90 ? 87  LYS A CG  1 
ATOM   513  C  CD  . LYS A 1 69  ? 42.633 22.754  35.218 1.00 25.40 ? 87  LYS A CD  1 
ATOM   514  C  CE  . LYS A 1 69  ? 42.409 24.033  36.013 1.00 26.91 ? 87  LYS A CE  1 
ATOM   515  N  NZ  . LYS A 1 69  ? 43.087 25.223  35.443 1.00 27.76 ? 87  LYS A NZ  1 
ATOM   516  N  N   . SER A 1 70  ? 43.234 18.226  36.387 1.00 11.05 ? 88  SER A N   1 
ATOM   517  C  CA  . SER A 1 70  ? 42.931 17.285  35.313 1.00 8.50  ? 88  SER A CA  1 
ATOM   518  C  C   . SER A 1 70  ? 41.514 17.493  34.871 1.00 7.42  ? 88  SER A C   1 
ATOM   519  O  O   . SER A 1 70  ? 40.590 17.437  35.689 1.00 8.33  ? 88  SER A O   1 
ATOM   520  C  CB  . SER A 1 70  ? 42.969 15.862  35.820 1.00 8.55  ? 88  SER A CB  1 
ATOM   521  O  OG  . SER A 1 70  ? 44.261 15.622  36.331 1.00 9.64  ? 88  SER A OG  1 
ATOM   522  N  N   . ILE A 1 71  ? 41.267 17.543  33.581 1.00 5.23  ? 89  ILE A N   1 
ATOM   523  C  CA  . ILE A 1 71  ? 39.923 17.807  33.094 1.00 5.17  ? 89  ILE A CA  1 
ATOM   524  C  C   . ILE A 1 71  ? 39.354 16.645  32.305 1.00 4.25  ? 89  ILE A C   1 
ATOM   525  O  O   . ILE A 1 71  ? 39.674 16.477  31.153 1.00 3.74  ? 89  ILE A O   1 
ATOM   526  C  CB  . ILE A 1 71  ? 39.971 19.015  32.163 1.00 6.92  ? 89  ILE A CB  1 
ATOM   527  C  CG1 . ILE A 1 71  ? 40.663 20.197  32.881 1.00 8.83  ? 89  ILE A CG1 1 
ATOM   528  C  CG2 . ILE A 1 71  ? 38.595 19.367  31.569 1.00 6.53  ? 89  ILE A CG2 1 
ATOM   529  C  CD1 . ILE A 1 71  ? 40.972 21.439  32.033 1.00 9.12  ? 89  ILE A CD1 1 
ATOM   530  N  N   . VAL A 1 72  ? 38.537 15.829  32.959 1.00 5.28  ? 90  VAL A N   1 
ATOM   531  C  CA  . VAL A 1 72  ? 37.942 14.678  32.324 1.00 6.70  ? 90  VAL A CA  1 
ATOM   532  C  C   . VAL A 1 72  ? 36.951 15.247  31.330 1.00 8.49  ? 90  VAL A C   1 
ATOM   533  O  O   . VAL A 1 72  ? 36.340 16.233  31.717 1.00 11.04 ? 90  VAL A O   1 
ATOM   534  C  CB  . VAL A 1 72  ? 37.329 13.821  33.445 1.00 7.29  ? 90  VAL A CB  1 
ATOM   535  C  CG1 . VAL A 1 72  ? 36.728 12.589  32.780 1.00 7.61  ? 90  VAL A CG1 1 
ATOM   536  C  CG2 . VAL A 1 72  ? 38.461 13.366  34.376 1.00 8.11  ? 90  VAL A CG2 1 
ATOM   537  N  N   . HIS A 1 73  ? 36.757 14.730  30.126 1.00 7.85  ? 91  HIS A N   1 
ATOM   538  C  CA  . HIS A 1 73  ? 35.708 15.177  29.216 1.00 7.28  ? 91  HIS A CA  1 
ATOM   539  C  C   . HIS A 1 73  ? 34.330 15.023  29.925 1.00 8.75  ? 91  HIS A C   1 
ATOM   540  O  O   . HIS A 1 73  ? 33.908 13.990  30.472 1.00 9.23  ? 91  HIS A O   1 
ATOM   541  C  CB  . HIS A 1 73  ? 35.729 14.254  28.007 1.00 6.75  ? 91  HIS A CB  1 
ATOM   542  C  CG  . HIS A 1 73  ? 34.974 14.813  26.835 1.00 5.51  ? 91  HIS A CG  1 
ATOM   543  N  ND1 . HIS A 1 73  ? 33.573 14.795  26.732 1.00 4.31  ? 91  HIS A ND1 1 
ATOM   544  C  CD2 . HIS A 1 73  ? 35.523 15.458  25.792 1.00 5.11  ? 91  HIS A CD2 1 
ATOM   545  C  CE1 . HIS A 1 73  ? 33.275 15.429  25.626 1.00 3.74  ? 91  HIS A CE1 1 
ATOM   546  N  NE2 . HIS A 1 73  ? 34.421 15.811  25.062 1.00 4.21  ? 91  HIS A NE2 1 
ATOM   547  N  N   . PRO A 1 74  ? 33.526 16.096  29.858 1.00 8.70  ? 92  PRO A N   1 
ATOM   548  C  CA  . PRO A 1 74  ? 32.196 16.122  30.471 1.00 7.22  ? 92  PRO A CA  1 
ATOM   549  C  C   . PRO A 1 74  ? 31.198 14.971  30.131 1.00 6.24  ? 92  PRO A C   1 
ATOM   550  O  O   . PRO A 1 74  ? 30.390 14.614  30.977 1.00 3.94  ? 92  PRO A O   1 
ATOM   551  C  CB  . PRO A 1 74  ? 31.736 17.549  30.172 1.00 7.31  ? 92  PRO A CB  1 
ATOM   552  C  CG  . PRO A 1 74  ? 32.921 18.410  29.775 1.00 7.55  ? 92  PRO A CG  1 
ATOM   553  C  CD  . PRO A 1 74  ? 33.953 17.425  29.294 1.00 8.66  ? 92  PRO A CD  1 
ATOM   554  N  N   . SER A 1 75  ? 31.294 14.319  28.938 1.00 7.21  ? 93  SER A N   1 
ATOM   555  C  CA  . SER A 1 75  ? 30.419 13.220  28.585 1.00 7.65  ? 93  SER A CA  1 
ATOM   556  C  C   . SER A 1 75  ? 31.105 11.859  28.596 1.00 7.89  ? 93  SER A C   1 
ATOM   557  O  O   . SER A 1 75  ? 30.621 10.887  27.959 1.00 7.97  ? 93  SER A O   1 
ATOM   558  C  CB  . SER A 1 75  ? 29.957 13.306  27.164 1.00 8.00  ? 93  SER A CB  1 
ATOM   559  O  OG  . SER A 1 75  ? 29.419 14.603  27.077 1.00 8.92  ? 93  SER A OG  1 
ATOM   560  N  N   . TYR A 1 76  ? 32.234 11.846  29.253 1.00 8.21  ? 94  TYR A N   1 
ATOM   561  C  CA  . TYR A 1 76  ? 32.937 10.597  29.346 1.00 8.08  ? 94  TYR A CA  1 
ATOM   562  C  C   . TYR A 1 76  ? 31.986 9.616   30.023 1.00 10.76 ? 94  TYR A C   1 
ATOM   563  O  O   . TYR A 1 76  ? 31.352 9.938   31.057 1.00 10.25 ? 94  TYR A O   1 
ATOM   564  C  CB  . TYR A 1 76  ? 34.079 10.796  30.330 1.00 5.61  ? 94  TYR A CB  1 
ATOM   565  C  CG  . TYR A 1 76  ? 34.588 9.485   30.820 1.00 4.78  ? 94  TYR A CG  1 
ATOM   566  C  CD1 . TYR A 1 76  ? 35.081 8.485   29.972 1.00 5.90  ? 94  TYR A CD1 1 
ATOM   567  C  CD2 . TYR A 1 76  ? 34.678 9.275   32.203 1.00 3.92  ? 94  TYR A CD2 1 
ATOM   568  C  CE1 . TYR A 1 76  ? 35.616 7.290   30.446 1.00 6.20  ? 94  TYR A CE1 1 
ATOM   569  C  CE2 . TYR A 1 76  ? 35.191 8.074   32.710 1.00 4.52  ? 94  TYR A CE2 1 
ATOM   570  C  CZ  . TYR A 1 76  ? 35.585 7.072   31.818 1.00 7.31  ? 94  TYR A CZ  1 
ATOM   571  O  OH  . TYR A 1 76  ? 36.179 5.960   32.408 1.00 10.51 ? 94  TYR A OH  1 
ATOM   572  N  N   . ASN A 1 77  ? 31.817 8.392   29.487 1.00 12.73 ? 95  ASN A N   1 
ATOM   573  C  CA  . ASN A 1 77  ? 30.901 7.487   30.174 1.00 14.06 ? 95  ASN A CA  1 
ATOM   574  C  C   . ASN A 1 77  ? 31.698 6.286   30.606 1.00 14.89 ? 95  ASN A C   1 
ATOM   575  O  O   . ASN A 1 77  ? 32.184 5.617   29.698 1.00 14.11 ? 95  ASN A O   1 
ATOM   576  C  CB  . ASN A 1 77  ? 29.875 6.956   29.170 1.00 16.08 ? 95  ASN A CB  1 
ATOM   577  C  CG  . ASN A 1 77  ? 29.042 5.833   29.797 1.00 17.38 ? 95  ASN A CG  1 
ATOM   578  O  OD1 . ASN A 1 77  ? 29.425 4.857   30.451 1.00 17.66 ? 95  ASN A OD1 1 
ATOM   579  N  ND2 . ASN A 1 77  ? 27.763 6.055   29.904 1.00 17.96 ? 95  ASN A ND2 1 
ATOM   580  N  N   . SER A 1 78  ? 31.748 5.982   31.912 1.00 16.30 ? 96  SER A N   1 
ATOM   581  C  CA  . SER A 1 78  ? 32.596 4.890   32.338 1.00 18.34 ? 96  SER A CA  1 
ATOM   582  C  C   . SER A 1 78  ? 32.113 3.512   31.968 1.00 18.69 ? 96  SER A C   1 
ATOM   583  O  O   . SER A 1 78  ? 32.945 2.637   31.817 1.00 19.38 ? 96  SER A O   1 
ATOM   584  C  CB  . SER A 1 78  ? 32.862 4.833   33.812 1.00 20.08 ? 96  SER A CB  1 
ATOM   585  O  OG  . SER A 1 78  ? 31.707 5.432   34.346 1.00 20.99 ? 96  SER A OG  1 
ATOM   586  N  N   . ASN A 1 79  ? 30.834 3.324   31.726 1.00 19.24 ? 97  ASN A N   1 
ATOM   587  C  CA  . ASN A 1 79  ? 30.350 2.008   31.327 1.00 20.81 ? 97  ASN A CA  1 
ATOM   588  C  C   . ASN A 1 79  ? 30.726 1.652   29.879 1.00 20.87 ? 97  ASN A C   1 
ATOM   589  O  O   . ASN A 1 79  ? 31.259 0.554   29.637 1.00 23.59 ? 97  ASN A O   1 
ATOM   590  C  CB  . ASN A 1 79  ? 28.874 1.836   31.695 0.86 22.38 ? 97  ASN A CB  1 
ATOM   591  C  CG  . ASN A 1 79  ? 28.612 2.536   33.027 0.35 22.88 ? 97  ASN A CG  1 
ATOM   592  O  OD1 . ASN A 1 79  ? 28.809 1.922   34.085 0.62 22.59 ? 97  ASN A OD1 1 
ATOM   593  N  ND2 . ASN A 1 79  ? 28.295 3.847   33.016 0.67 23.46 ? 97  ASN A ND2 1 
ATOM   594  N  N   . THR A 1 80  ? 30.566 2.571   28.938 1.00 17.47 ? 98  THR A N   1 
ATOM   595  C  CA  . THR A 1 80  ? 31.019 2.350   27.602 1.00 16.07 ? 98  THR A CA  1 
ATOM   596  C  C   . THR A 1 80  ? 32.499 2.755   27.298 1.00 15.76 ? 98  THR A C   1 
ATOM   597  O  O   . THR A 1 80  ? 33.031 2.209   26.323 1.00 16.99 ? 98  THR A O   1 
ATOM   598  C  CB  . THR A 1 80  ? 30.041 3.024   26.632 1.00 15.73 ? 98  THR A CB  1 
ATOM   599  O  OG1 . THR A 1 80  ? 30.013 4.379   26.865 1.00 15.34 ? 98  THR A OG1 1 
ATOM   600  C  CG2 . THR A 1 80  ? 28.617 2.850   27.063 1.00 16.43 ? 98  THR A CG2 1 
ATOM   601  N  N   . LEU A 1 81  ? 33.108 3.766   27.980 1.00 12.17 ? 99  LEU A N   1 
ATOM   602  C  CA  . LEU A 1 81  ? 34.385 4.328   27.650 1.00 10.30 ? 99  LEU A CA  1 
ATOM   603  C  C   . LEU A 1 81  ? 34.246 5.240   26.445 1.00 8.92  ? 99  LEU A C   1 
ATOM   604  O  O   . LEU A 1 81  ? 35.199 5.645   25.736 1.00 6.79  ? 99  LEU A O   1 
ATOM   605  C  CB  . LEU A 1 81  ? 35.580 3.368   27.448 1.00 10.98 ? 99  LEU A CB  1 
ATOM   606  C  CG  . LEU A 1 81  ? 35.921 2.649   28.753 1.00 12.26 ? 99  LEU A CG  1 
ATOM   607  C  CD1 . LEU A 1 81  ? 37.127 1.758   28.522 0.56 12.33 ? 99  LEU A CD1 1 
ATOM   608  C  CD2 . LEU A 1 81  ? 36.237 3.617   29.895 0.85 13.36 ? 99  LEU A CD2 1 
ATOM   609  N  N   . ASN A 1 82  ? 32.999 5.680   26.173 1.00 9.39  ? 100 ASN A N   1 
ATOM   610  C  CA  . ASN A 1 82  ? 32.975 6.667   25.095 1.00 8.42  ? 100 ASN A CA  1 
ATOM   611  C  C   . ASN A 1 82  ? 33.482 8.021   25.633 1.00 7.95  ? 100 ASN A C   1 
ATOM   612  O  O   . ASN A 1 82  ? 33.179 8.370   26.782 1.00 7.91  ? 100 ASN A O   1 
ATOM   613  C  CB  . ASN A 1 82  ? 31.494 6.855   24.818 1.00 8.27  ? 100 ASN A CB  1 
ATOM   614  C  CG  . ASN A 1 82  ? 31.242 7.510   23.509 1.00 8.74  ? 100 ASN A CG  1 
ATOM   615  O  OD1 . ASN A 1 82  ? 31.839 7.363   22.423 1.00 9.07  ? 100 ASN A OD1 1 
ATOM   616  N  ND2 . ASN A 1 82  ? 30.245 8.355   23.616 1.00 9.60  ? 100 ASN A ND2 1 
ATOM   617  N  N   . ASN A 1 83  ? 34.226 8.829   24.838 1.00 7.39  ? 101 ASN A N   1 
ATOM   618  C  CA  . ASN A 1 83  ? 34.764 10.121  25.246 1.00 6.80  ? 101 ASN A CA  1 
ATOM   619  C  C   . ASN A 1 83  ? 35.821 9.927   26.309 1.00 5.54  ? 101 ASN A C   1 
ATOM   620  O  O   . ASN A 1 83  ? 35.856 10.714  27.287 1.00 3.88  ? 101 ASN A O   1 
ATOM   621  C  CB  . ASN A 1 83  ? 33.733 11.139  25.800 1.00 7.50  ? 101 ASN A CB  1 
ATOM   622  C  CG  . ASN A 1 83  ? 32.703 11.396  24.739 1.00 8.28  ? 101 ASN A CG  1 
ATOM   623  O  OD1 . ASN A 1 83  ? 33.016 11.788  23.607 1.00 9.24  ? 101 ASN A OD1 1 
ATOM   624  N  ND2 . ASN A 1 83  ? 31.457 11.041  25.025 1.00 7.33  ? 101 ASN A ND2 1 
ATOM   625  N  N   . ASP A 1 84  ? 36.591 8.831   26.089 1.00 5.50  ? 102 ASP A N   1 
ATOM   626  C  CA  . ASP A 1 84  ? 37.681 8.407   26.966 1.00 6.38  ? 102 ASP A CA  1 
ATOM   627  C  C   . ASP A 1 84  ? 38.957 9.241   26.711 1.00 6.18  ? 102 ASP A C   1 
ATOM   628  O  O   . ASP A 1 84  ? 39.949 8.798   26.097 1.00 7.28  ? 102 ASP A O   1 
ATOM   629  C  CB  . ASP A 1 84  ? 37.805 6.881   27.157 1.00 6.18  ? 102 ASP A CB  1 
ATOM   630  C  CG  . ASP A 1 84  ? 38.896 6.588   28.142 1.00 5.61  ? 102 ASP A CG  1 
ATOM   631  O  OD1 . ASP A 1 84  ? 39.051 7.215   29.154 1.00 6.10  ? 102 ASP A OD1 1 
ATOM   632  O  OD2 . ASP A 1 84  ? 39.618 5.547   27.881 1.00 5.04  ? 102 ASP A OD2 1 
ATOM   633  N  N   . ILE A 1 85  ? 38.843 10.513  27.084 1.00 4.89  ? 103 ILE A N   1 
ATOM   634  C  CA  . ILE A 1 85  ? 39.882 11.530  26.887 1.00 2.98  ? 103 ILE A CA  1 
ATOM   635  C  C   . ILE A 1 85  ? 40.042 12.499  28.083 1.00 3.14  ? 103 ILE A C   1 
ATOM   636  O  O   . ILE A 1 85  ? 39.096 12.915  28.712 1.00 3.70  ? 103 ILE A O   1 
ATOM   637  C  CB  . ILE A 1 85  ? 39.689 12.195  25.516 1.00 2.51  ? 103 ILE A CB  1 
ATOM   638  C  CG1 . ILE A 1 85  ? 40.797 13.218  25.182 1.00 2.75  ? 103 ILE A CG1 1 
ATOM   639  C  CG2 . ILE A 1 85  ? 38.286 12.774  25.610 1.00 2.00  ? 103 ILE A CG2 1 
ATOM   640  C  CD1 . ILE A 1 85  ? 40.922 13.759  23.747 1.00 2.69  ? 103 ILE A CD1 1 
ATOM   641  N  N   . MET A 1 86  ? 41.229 12.970  28.509 1.00 2.57  ? 104 MET A N   1 
ATOM   642  C  CA  . MET A 1 86  ? 41.326 13.849  29.638 1.00 3.31  ? 104 MET A CA  1 
ATOM   643  C  C   . MET A 1 86  ? 42.515 14.789  29.365 1.00 4.87  ? 104 MET A C   1 
ATOM   644  O  O   . MET A 1 86  ? 43.483 14.315  28.767 1.00 6.35  ? 104 MET A O   1 
ATOM   645  C  CB  . MET A 1 86  ? 41.678 12.910  30.809 1.00 4.05  ? 104 MET A CB  1 
ATOM   646  C  CG  . MET A 1 86  ? 42.285 13.609  31.992 1.00 6.23  ? 104 MET A CG  1 
ATOM   647  S  SD  . MET A 1 86  ? 42.279 12.543  33.438 1.00 8.56  ? 104 MET A SD  1 
ATOM   648  C  CE  . MET A 1 86  ? 43.820 11.640  33.469 1.00 6.51  ? 104 MET A CE  1 
ATOM   649  N  N   . LEU A 1 87  ? 42.483 16.012  29.862 1.00 4.22  ? 105 LEU A N   1 
ATOM   650  C  CA  . LEU A 1 87  ? 43.634 16.887  29.690 1.00 6.80  ? 105 LEU A CA  1 
ATOM   651  C  C   . LEU A 1 87  ? 44.225 17.197  31.075 1.00 8.52  ? 105 LEU A C   1 
ATOM   652  O  O   . LEU A 1 87  ? 43.447 17.413  32.001 1.00 8.72  ? 105 LEU A O   1 
ATOM   653  C  CB  . LEU A 1 87  ? 43.211 18.204  28.990 1.00 7.41  ? 105 LEU A CB  1 
ATOM   654  C  CG  . LEU A 1 87  ? 42.658 18.076  27.567 1.00 9.04  ? 105 LEU A CG  1 
ATOM   655  C  CD1 . LEU A 1 87  ? 41.966 19.362  27.096 1.00 9.14  ? 105 LEU A CD1 1 
ATOM   656  C  CD2 . LEU A 1 87  ? 43.869 18.079  26.667 1.00 10.78 ? 105 LEU A CD2 1 
ATOM   657  N  N   . ILE A 1 88  ? 45.560 17.117  31.217 1.00 8.96  ? 106 ILE A N   1 
ATOM   658  C  CA  . ILE A 1 88  ? 46.185 17.474  32.475 1.00 7.91  ? 106 ILE A CA  1 
ATOM   659  C  C   . ILE A 1 88  ? 46.955 18.792  32.274 1.00 6.54  ? 106 ILE A C   1 
ATOM   660  O  O   . ILE A 1 88  ? 47.684 18.783  31.298 1.00 5.89  ? 106 ILE A O   1 
ATOM   661  C  CB  . ILE A 1 88  ? 47.166 16.406  32.905 1.00 8.02  ? 106 ILE A CB  1 
ATOM   662  C  CG1 . ILE A 1 88  ? 46.251 15.169  32.782 1.00 10.17 ? 106 ILE A CG1 1 
ATOM   663  C  CG2 . ILE A 1 88  ? 47.703 16.707  34.317 1.00 5.73  ? 106 ILE A CG2 1 
ATOM   664  C  CD1 . ILE A 1 88  ? 46.926 13.809  32.960 1.00 11.04 ? 106 ILE A CD1 1 
ATOM   665  N  N   . LYS A 1 89  ? 46.692 19.799  33.148 1.00 6.01  ? 107 LYS A N   1 
ATOM   666  C  CA  . LYS A 1 89  ? 47.534 20.958  33.212 1.00 7.34  ? 107 LYS A CA  1 
ATOM   667  C  C   . LYS A 1 89  ? 48.751 20.773  34.116 1.00 6.88  ? 107 LYS A C   1 
ATOM   668  O  O   . LYS A 1 89  ? 48.534 20.317  35.258 1.00 6.53  ? 107 LYS A O   1 
ATOM   669  C  CB  . LYS A 1 89  ? 46.833 22.258  33.569 1.00 9.02  ? 107 LYS A CB  1 
ATOM   670  C  CG  . LYS A 1 89  ? 47.711 23.280  32.852 1.00 11.10 ? 107 LYS A CG  1 
ATOM   671  C  CD  . LYS A 1 89  ? 46.940 24.522  32.591 1.00 13.71 ? 107 LYS A CD  1 
ATOM   672  C  CE  . LYS A 1 89  ? 46.517 25.262  33.847 1.00 16.36 ? 107 LYS A CE  1 
ATOM   673  N  NZ  . LYS A 1 89  ? 47.431 26.449  33.914 1.00 18.49 ? 107 LYS A NZ  1 
ATOM   674  N  N   . LEU A 1 90  ? 49.983 21.095  33.648 1.00 6.83  ? 108 LEU A N   1 
ATOM   675  C  CA  . LEU A 1 90  ? 51.138 20.906  34.516 1.00 6.48  ? 108 LEU A CA  1 
ATOM   676  C  C   . LEU A 1 90  ? 51.202 22.171  35.366 1.00 8.67  ? 108 LEU A C   1 
ATOM   677  O  O   . LEU A 1 90  ? 50.705 23.218  34.957 1.00 10.28 ? 108 LEU A O   1 
ATOM   678  C  CB  . LEU A 1 90  ? 52.411 20.819  33.666 1.00 5.26  ? 108 LEU A CB  1 
ATOM   679  C  CG  . LEU A 1 90  ? 52.389 19.681  32.604 1.00 5.86  ? 108 LEU A CG  1 
ATOM   680  C  CD1 . LEU A 1 90  ? 53.784 19.677  31.938 1.00 6.22  ? 108 LEU A CD1 1 
ATOM   681  C  CD2 . LEU A 1 90  ? 52.089 18.446  33.424 1.00 6.01  ? 108 LEU A CD2 1 
ATOM   682  N  N   . LYS A 1 91  ? 51.681 22.030  36.584 1.00 9.22  ? 109 LYS A N   1 
ATOM   683  C  CA  . LYS A 1 91  ? 51.888 23.089  37.536 1.00 11.62 ? 109 LYS A CA  1 
ATOM   684  C  C   . LYS A 1 91  ? 52.989 24.043  37.030 1.00 13.65 ? 109 LYS A C   1 
ATOM   685  O  O   . LYS A 1 91  ? 52.800 25.244  37.108 1.00 14.70 ? 109 LYS A O   1 
ATOM   686  C  CB  . LYS A 1 91  ? 52.116 22.499  38.898 1.00 13.54 ? 109 LYS A CB  1 
ATOM   687  C  CG  . LYS A 1 91  ? 52.443 23.576  39.908 1.00 16.00 ? 109 LYS A CG  1 
ATOM   688  C  CD  . LYS A 1 91  ? 53.221 22.909  41.023 0.69 18.01 ? 109 LYS A CD  1 
ATOM   689  C  CE  . LYS A 1 91  ? 54.141 21.806  40.463 0.10 18.40 ? 109 LYS A CE  1 
ATOM   690  N  NZ  . LYS A 1 91  ? 55.226 21.168  41.259 0.73 18.37 ? 109 LYS A NZ  1 
ATOM   691  N  N   . SER A 1 92  ? 54.064 23.608  36.407 1.00 13.44 ? 110 SER A N   1 
ATOM   692  C  CA  . SER A 1 92  ? 54.940 24.523  35.710 1.00 14.19 ? 110 SER A CA  1 
ATOM   693  C  C   . SER A 1 92  ? 55.118 23.906  34.317 1.00 12.59 ? 110 SER A C   1 
ATOM   694  O  O   . SER A 1 92  ? 54.815 22.722  34.190 1.00 11.59 ? 110 SER A O   1 
ATOM   695  C  CB  . SER A 1 92  ? 56.340 24.525  36.235 1.00 16.00 ? 110 SER A CB  1 
ATOM   696  O  OG  . SER A 1 92  ? 56.165 24.184  37.567 1.00 18.57 ? 110 SER A OG  1 
ATOM   697  N  N   . ALA A 1 93  ? 55.617 24.720  33.396 1.00 12.13 ? 111 ALA A N   1 
ATOM   698  C  CA  . ALA A 1 93  ? 55.902 24.333  32.034 1.00 13.74 ? 111 ALA A CA  1 
ATOM   699  C  C   . ALA A 1 93  ? 57.102 23.408  32.092 1.00 15.05 ? 111 ALA A C   1 
ATOM   700  O  O   . ALA A 1 93  ? 57.937 23.634  32.984 1.00 16.33 ? 111 ALA A O   1 
ATOM   701  C  CB  . ALA A 1 93  ? 56.167 25.533  31.101 1.00 12.83 ? 111 ALA A CB  1 
ATOM   702  N  N   . ALA A 1 94  ? 57.138 22.442  31.151 1.00 14.28 ? 112 ALA A N   1 
ATOM   703  C  CA  . ALA A 1 94  ? 58.227 21.552  30.978 1.00 13.14 ? 112 ALA A CA  1 
ATOM   704  C  C   . ALA A 1 94  ? 59.337 22.270  30.143 1.00 13.81 ? 112 ALA A C   1 
ATOM   705  O  O   . ALA A 1 94  ? 59.003 23.163  29.355 1.00 12.69 ? 112 ALA A O   1 
ATOM   706  C  CB  . ALA A 1 94  ? 57.576 20.462  30.139 1.00 12.34 ? 112 ALA A CB  1 
ATOM   707  N  N   . SER A 1 95  ? 60.629 21.840  30.300 1.00 14.06 ? 113 SER A N   1 
ATOM   708  C  CA  . SER A 1 95  ? 61.716 22.349  29.461 1.00 15.28 ? 113 SER A CA  1 
ATOM   709  C  C   . SER A 1 95  ? 61.742 21.450  28.270 1.00 14.50 ? 113 SER A C   1 
ATOM   710  O  O   . SER A 1 95  ? 62.177 20.354  28.428 1.00 15.13 ? 113 SER A O   1 
ATOM   711  C  CB  . SER A 1 95  ? 63.119 22.348  30.060 1.00 15.98 ? 113 SER A CB  1 
ATOM   712  O  OG  . SER A 1 95  ? 62.752 22.967  31.259 1.00 16.61 ? 113 SER A OG  1 
ATOM   713  N  N   . LEU A 1 96  ? 61.271 21.913  27.157 1.00 13.78 ? 114 LEU A N   1 
ATOM   714  C  CA  . LEU A 1 96  ? 61.359 21.138  25.982 1.00 14.92 ? 114 LEU A CA  1 
ATOM   715  C  C   . LEU A 1 96  ? 62.780 21.203  25.424 1.00 16.16 ? 114 LEU A C   1 
ATOM   716  O  O   . LEU A 1 96  ? 63.466 22.240  25.440 1.00 17.05 ? 114 LEU A O   1 
ATOM   717  C  CB  . LEU A 1 96  ? 60.305 21.608  24.965 1.00 15.13 ? 114 LEU A CB  1 
ATOM   718  C  CG  . LEU A 1 96  ? 58.883 21.643  25.504 1.00 15.19 ? 114 LEU A CG  1 
ATOM   719  C  CD1 . LEU A 1 96  ? 57.989 21.971  24.338 1.00 14.84 ? 114 LEU A CD1 1 
ATOM   720  C  CD2 . LEU A 1 96  ? 58.451 20.270  25.919 1.00 16.01 ? 114 LEU A CD2 1 
ATOM   721  N  N   . ASN A 1 97  ? 63.204 20.054  24.913 1.00 16.07 ? 115 ASN A N   1 
ATOM   722  C  CA  . ASN A 1 97  ? 64.512 19.840  24.417 1.00 15.81 ? 115 ASN A CA  1 
ATOM   723  C  C   . ASN A 1 97  ? 64.444 18.679  23.481 1.00 17.67 ? 115 ASN A C   1 
ATOM   724  O  O   . ASN A 1 97  ? 63.393 18.331  22.988 1.00 17.43 ? 115 ASN A O   1 
ATOM   725  C  CB  . ASN A 1 97  ? 65.533 19.655  25.529 1.00 14.43 ? 115 ASN A CB  1 
ATOM   726  C  CG  . ASN A 1 97  ? 65.051 18.673  26.555 1.00 15.00 ? 115 ASN A CG  1 
ATOM   727  O  OD1 . ASN A 1 97  ? 64.616 17.589  26.176 1.00 14.13 ? 115 ASN A OD1 1 
ATOM   728  N  ND2 . ASN A 1 97  ? 65.035 19.063  27.843 1.00 15.19 ? 115 ASN A ND2 1 
ATOM   729  N  N   . SER A 1 98  ? 65.615 18.135  23.189 1.00 20.31 ? 116 SER A N   1 
ATOM   730  C  CA  . SER A 1 98  ? 65.558 17.033  22.243 1.00 22.01 ? 116 SER A CA  1 
ATOM   731  C  C   . SER A 1 98  ? 65.039 15.757  22.890 1.00 22.39 ? 116 SER A C   1 
ATOM   732  O  O   . SER A 1 98  ? 64.760 14.810  22.154 1.00 24.38 ? 116 SER A O   1 
ATOM   733  C  CB  . SER A 1 98  ? 66.907 16.843  21.515 1.00 22.78 ? 116 SER A CB  1 
ATOM   734  O  OG  . SER A 1 98  ? 67.832 16.194  22.376 1.00 23.36 ? 116 SER A OG  1 
ATOM   735  N  N   . ARG A 1 99  ? 64.926 15.696  24.221 1.00 20.61 ? 117 ARG A N   1 
ATOM   736  C  CA  . ARG A 1 99  ? 64.531 14.505  24.947 1.00 19.85 ? 117 ARG A CA  1 
ATOM   737  C  C   . ARG A 1 99  ? 63.124 14.637  25.497 1.00 17.00 ? 117 ARG A C   1 
ATOM   738  O  O   . ARG A 1 99  ? 62.471 13.668  25.958 1.00 17.39 ? 117 ARG A O   1 
ATOM   739  C  CB  . ARG A 1 99  ? 65.540 14.061  26.010 1.00 22.18 ? 117 ARG A CB  1 
ATOM   740  C  CG  . ARG A 1 99  ? 66.991 14.413  25.696 1.00 25.33 ? 117 ARG A CG  1 
ATOM   741  C  CD  . ARG A 1 99  ? 67.731 13.579  24.640 0.90 28.18 ? 117 ARG A CD  1 
ATOM   742  N  NE  . ARG A 1 99  ? 68.171 12.305  25.180 0.50 30.07 ? 117 ARG A NE  1 
ATOM   743  C  CZ  . ARG A 1 99  ? 69.214 12.235  25.991 0.10 31.45 ? 117 ARG A CZ  1 
ATOM   744  N  NH1 . ARG A 1 99  ? 69.858 13.372  26.239 0.42 31.95 ? 117 ARG A NH1 1 
ATOM   745  N  NH2 . ARG A 1 99  ? 69.615 11.084  26.523 0.26 31.86 ? 117 ARG A NH2 1 
ATOM   746  N  N   . VAL A 1 100 ? 62.600 15.856  25.438 1.00 14.09 ? 118 VAL A N   1 
ATOM   747  C  CA  . VAL A 1 100 ? 61.241 16.197  25.903 1.00 12.17 ? 118 VAL A CA  1 
ATOM   748  C  C   . VAL A 1 100 ? 60.598 17.161  24.877 1.00 11.28 ? 118 VAL A C   1 
ATOM   749  O  O   . VAL A 1 100 ? 60.916 18.336  24.733 1.00 11.43 ? 118 VAL A O   1 
ATOM   750  C  CB  . VAL A 1 100 ? 61.165 16.711  27.339 1.00 11.11 ? 118 VAL A CB  1 
ATOM   751  C  CG1 . VAL A 1 100 ? 59.806 17.201  27.858 1.00 8.78  ? 118 VAL A CG1 1 
ATOM   752  C  CG2 . VAL A 1 100 ? 61.905 15.829  28.343 1.00 12.02 ? 118 VAL A CG2 1 
ATOM   753  N  N   . ALA A 1 101 ? 59.652 16.663  24.123 1.00 9.63  ? 119 ALA A N   1 
ATOM   754  C  CA  . ALA A 1 101 ? 59.077 17.437  23.045 1.00 10.08 ? 119 ALA A CA  1 
ATOM   755  C  C   . ALA A 1 101 ? 57.574 17.185  22.861 1.00 9.90  ? 119 ALA A C   1 
ATOM   756  O  O   . ALA A 1 101 ? 56.987 16.223  23.330 1.00 10.02 ? 119 ALA A O   1 
ATOM   757  C  CB  . ALA A 1 101 ? 59.814 17.097  21.782 1.00 9.26  ? 119 ALA A CB  1 
ATOM   758  N  N   . SER A 1 102 ? 56.841 18.108  22.261 1.00 9.35  ? 120 SER A N   1 
ATOM   759  C  CA  . SER A 1 102 ? 55.437 17.745  22.218 1.00 9.31  ? 120 SER A CA  1 
ATOM   760  C  C   . SER A 1 102 ? 55.092 17.151  20.871 1.00 9.10  ? 120 SER A C   1 
ATOM   761  O  O   . SER A 1 102 ? 55.951 17.111  19.994 1.00 9.43  ? 120 SER A O   1 
ATOM   762  C  CB  . SER A 1 102 ? 54.612 18.941  22.549 1.00 10.05 ? 120 SER A CB  1 
ATOM   763  O  OG  . SER A 1 102 ? 54.891 19.787  21.464 1.00 11.51 ? 120 SER A OG  1 
ATOM   764  N  N   . ILE A 1 103 ? 53.909 16.519  20.722 1.00 8.18  ? 121 ILE A N   1 
ATOM   765  C  CA  . ILE A 1 103 ? 53.495 15.816  19.487 1.00 7.73  ? 121 ILE A CA  1 
ATOM   766  C  C   . ILE A 1 103 ? 52.317 16.602  18.905 1.00 7.68  ? 121 ILE A C   1 
ATOM   767  O  O   . ILE A 1 103 ? 51.566 17.155  19.718 1.00 7.47  ? 121 ILE A O   1 
ATOM   768  C  CB  . ILE A 1 103 ? 53.059 14.390  19.813 1.00 6.87  ? 121 ILE A CB  1 
ATOM   769  C  CG1 . ILE A 1 103 ? 52.714 13.583  18.578 1.00 6.36  ? 121 ILE A CG1 1 
ATOM   770  C  CG2 . ILE A 1 103 ? 52.050 14.303  20.946 1.00 6.20  ? 121 ILE A CG2 1 
ATOM   771  C  CD1 . ILE A 1 103 ? 54.004 13.386  17.761 1.00 5.06  ? 121 ILE A CD1 1 
ATOM   772  N  N   . SER A 1 104 ? 52.199 16.737  17.587 1.00 8.28  ? 122 SER A N   1 
ATOM   773  C  CA  . SER A 1 104 ? 51.141 17.528  16.963 1.00 9.80  ? 122 SER A CA  1 
ATOM   774  C  C   . SER A 1 104 ? 49.766 16.878  17.036 1.00 9.60  ? 122 SER A C   1 
ATOM   775  O  O   . SER A 1 104 ? 49.604 15.670  17.173 1.00 11.09 ? 122 SER A O   1 
ATOM   776  C  CB  . SER A 1 104 ? 51.342 17.851  15.525 1.00 12.65 ? 122 SER A CB  1 
ATOM   777  O  OG  . SER A 1 104 ? 52.729 18.234  15.422 1.00 16.38 ? 122 SER A OG  1 
ATOM   778  N  N   . LEU A 1 105 ? 48.732 17.724  17.062 1.00 8.21  ? 123 LEU A N   1 
ATOM   779  C  CA  . LEU A 1 105 ? 47.358 17.221  17.034 1.00 7.27  ? 123 LEU A CA  1 
ATOM   780  C  C   . LEU A 1 105 ? 47.032 17.033  15.574 1.00 9.14  ? 123 LEU A C   1 
ATOM   781  O  O   . LEU A 1 105 ? 47.745 17.605  14.743 1.00 9.16  ? 123 LEU A O   1 
ATOM   782  C  CB  . LEU A 1 105 ? 46.375 18.133  17.707 1.00 4.59  ? 123 LEU A CB  1 
ATOM   783  C  CG  . LEU A 1 105 ? 46.543 18.265  19.223 1.00 2.79  ? 123 LEU A CG  1 
ATOM   784  C  CD1 . LEU A 1 105 ? 45.574 19.362  19.596 1.00 3.85  ? 123 LEU A CD1 1 
ATOM   785  C  CD2 . LEU A 1 105 ? 46.178 16.902  19.828 1.00 2.64  ? 123 LEU A CD2 1 
ATOM   786  N  N   . PRO A 1 106 ? 46.045 16.189  15.226 1.00 11.59 ? 124 PRO A N   1 
ATOM   787  C  CA  . PRO A 1 106 ? 45.812 15.962  13.807 1.00 13.60 ? 124 PRO A CA  1 
ATOM   788  C  C   . PRO A 1 106 ? 44.886 17.010  13.194 1.00 15.41 ? 124 PRO A C   1 
ATOM   789  O  O   . PRO A 1 106 ? 44.179 17.765  13.880 1.00 15.44 ? 124 PRO A O   1 
ATOM   790  C  CB  . PRO A 1 106 ? 45.236 14.582  13.638 1.00 13.70 ? 124 PRO A CB  1 
ATOM   791  C  CG  . PRO A 1 106 ? 44.608 14.358  14.997 1.00 13.62 ? 124 PRO A CG  1 
ATOM   792  C  CD  . PRO A 1 106 ? 45.399 15.129  16.034 1.00 12.18 ? 124 PRO A CD  1 
ATOM   793  N  N   . THR A 1 107 ? 45.000 17.139  11.878 1.00 16.83 ? 125 THR A N   1 
ATOM   794  C  CA  . THR A 1 107 ? 44.175 18.097  11.182 1.00 19.80 ? 125 THR A CA  1 
ATOM   795  C  C   . THR A 1 107 ? 43.051 17.377  10.467 1.00 19.81 ? 125 THR A C   1 
ATOM   796  O  O   . THR A 1 107 ? 42.091 17.973  10.035 1.00 20.91 ? 125 THR A O   1 
ATOM   797  C  CB  . THR A 1 107 ? 45.009 18.978  10.245 1.00 22.40 ? 125 THR A CB  1 
ATOM   798  O  OG1 . THR A 1 107 ? 45.745 18.084  9.432  1.00 23.99 ? 125 THR A OG1 1 
ATOM   799  C  CG2 . THR A 1 107 ? 45.976 19.701  11.209 1.00 22.27 ? 125 THR A CG2 1 
ATOM   800  N  N   . SER A 1 108 ? 43.153 16.069  10.457 1.00 18.45 ? 127 SER A N   1 
ATOM   801  C  CA  . SER A 1 108 ? 42.224 15.142  9.855  1.00 17.05 ? 127 SER A CA  1 
ATOM   802  C  C   . SER A 1 108 ? 42.488 13.741  10.410 1.00 14.17 ? 127 SER A C   1 
ATOM   803  O  O   . SER A 1 108 ? 43.583 13.351  10.837 1.00 12.95 ? 127 SER A O   1 
ATOM   804  C  CB  . SER A 1 108 ? 42.341 15.197  8.332  1.00 18.13 ? 127 SER A CB  1 
ATOM   805  O  OG  . SER A 1 108 ? 43.696 14.846  8.032  1.00 18.77 ? 127 SER A OG  1 
ATOM   806  N  N   . CYS A 1 109 ? 41.419 12.990  10.383 1.00 12.50 ? 128 CYS A N   1 
ATOM   807  C  CA  . CYS A 1 109 ? 41.444 11.636  10.795 1.00 11.80 ? 128 CYS A CA  1 
ATOM   808  C  C   . CYS A 1 109 ? 42.190 10.753  9.813  1.00 13.03 ? 128 CYS A C   1 
ATOM   809  O  O   . CYS A 1 109 ? 42.227 11.027  8.593  1.00 12.11 ? 128 CYS A O   1 
ATOM   810  C  CB  . CYS A 1 109 ? 39.964 11.221  10.705 1.00 10.35 ? 128 CYS A CB  1 
ATOM   811  S  SG  . CYS A 1 109 ? 38.994 12.196  11.865 1.00 8.68  ? 128 CYS A SG  1 
ATOM   812  N  N   . ALA A 1 110 ? 42.798 9.736   10.429 1.00 13.82 ? 129 ALA A N   1 
ATOM   813  C  CA  . ALA A 1 110 ? 43.608 8.752   9.776  1.00 14.93 ? 129 ALA A CA  1 
ATOM   814  C  C   . ALA A 1 110 ? 42.713 7.668   9.196  1.00 16.59 ? 129 ALA A C   1 
ATOM   815  O  O   . ALA A 1 110 ? 41.688 7.294   9.743  1.00 19.12 ? 129 ALA A O   1 
ATOM   816  C  CB  . ALA A 1 110 ? 44.346 8.098   10.912 1.00 14.43 ? 129 ALA A CB  1 
ATOM   817  N  N   . SER A 1 111 ? 43.082 7.126   8.060  1.00 15.36 ? 130 SER A N   1 
ATOM   818  C  CA  . SER A 1 111 ? 42.372 6.103   7.373  1.00 14.97 ? 130 SER A CA  1 
ATOM   819  C  C   . SER A 1 111 ? 42.881 4.718   7.761  1.00 14.98 ? 130 SER A C   1 
ATOM   820  O  O   . SER A 1 111 ? 44.035 4.440   8.203  1.00 16.21 ? 130 SER A O   1 
ATOM   821  C  CB  . SER A 1 111 ? 42.471 6.425   5.865  1.00 16.20 ? 130 SER A CB  1 
ATOM   822  O  OG  . SER A 1 111 ? 43.826 6.321   5.376  1.00 18.49 ? 130 SER A OG  1 
ATOM   823  N  N   . ALA A 1 112 ? 41.994 3.791   7.486  1.00 13.65 ? 132 ALA A N   1 
ATOM   824  C  CA  . ALA A 1 112 ? 42.335 2.405   7.712  1.00 11.84 ? 132 ALA A CA  1 
ATOM   825  C  C   . ALA A 1 112 ? 43.644 2.076   7.042  1.00 10.30 ? 132 ALA A C   1 
ATOM   826  O  O   . ALA A 1 112 ? 43.765 2.622   5.972  1.00 9.62  ? 132 ALA A O   1 
ATOM   827  C  CB  . ALA A 1 112 ? 41.230 1.558   7.111  1.00 10.32 ? 132 ALA A CB  1 
ATOM   828  N  N   . GLY A 1 113 ? 44.492 1.193   7.594  1.00 9.15  ? 133 GLY A N   1 
ATOM   829  C  CA  . GLY A 1 113 ? 45.687 0.838   6.911  1.00 8.56  ? 133 GLY A CA  1 
ATOM   830  C  C   . GLY A 1 113 ? 46.808 1.741   7.379  1.00 10.61 ? 133 GLY A C   1 
ATOM   831  O  O   . GLY A 1 113 ? 47.960 1.413   7.242  1.00 11.56 ? 133 GLY A O   1 
ATOM   832  N  N   . THR A 1 114 ? 46.557 2.901   7.931  1.00 12.28 ? 134 THR A N   1 
ATOM   833  C  CA  . THR A 1 114 ? 47.655 3.720   8.429  1.00 12.34 ? 134 THR A CA  1 
ATOM   834  C  C   . THR A 1 114 ? 48.343 3.033   9.547  1.00 13.00 ? 134 THR A C   1 
ATOM   835  O  O   . THR A 1 114 ? 47.717 2.477   10.457 1.00 12.33 ? 134 THR A O   1 
ATOM   836  C  CB  . THR A 1 114 ? 47.186 5.073   8.944  1.00 12.29 ? 134 THR A CB  1 
ATOM   837  O  OG1 . THR A 1 114 ? 46.454 5.648   7.846  1.00 13.17 ? 134 THR A OG1 1 
ATOM   838  C  CG2 . THR A 1 114 ? 48.483 5.821   9.270  1.00 10.15 ? 134 THR A CG2 1 
ATOM   839  N  N   . GLN A 1 115 ? 49.683 3.108   9.436  1.00 13.79 ? 135 GLN A N   1 
ATOM   840  C  CA  . GLN A 1 115 ? 50.571 2.508   10.390 1.00 13.91 ? 135 GLN A CA  1 
ATOM   841  C  C   . GLN A 1 115 ? 50.831 3.587   11.422 1.00 11.09 ? 135 GLN A C   1 
ATOM   842  O  O   . GLN A 1 115 ? 51.201 4.731   11.073 1.00 11.36 ? 135 GLN A O   1 
ATOM   843  C  CB  . GLN A 1 115 ? 51.874 2.221   9.585  1.00 17.83 ? 135 GLN A CB  1 
ATOM   844  C  CG  . GLN A 1 115 ? 52.659 0.995   10.140 1.00 21.55 ? 135 GLN A CG  1 
ATOM   845  C  CD  . GLN A 1 115 ? 51.961 -0.361  10.145 1.00 23.60 ? 135 GLN A CD  1 
ATOM   846  O  OE1 . GLN A 1 115 ? 52.348 -1.226  10.983 1.00 25.28 ? 135 GLN A OE1 1 
ATOM   847  N  NE2 . GLN A 1 115 ? 51.182 -0.643  9.065  1.00 23.15 ? 135 GLN A NE2 1 
ATOM   848  N  N   . CYS A 1 116 ? 50.844 3.149   12.670 1.00 7.52  ? 136 CYS A N   1 
ATOM   849  C  CA  . CYS A 1 116 ? 51.071 4.063   13.751 1.00 7.64  ? 136 CYS A CA  1 
ATOM   850  C  C   . CYS A 1 116 ? 52.019 3.441   14.756 1.00 7.73  ? 136 CYS A C   1 
ATOM   851  O  O   . CYS A 1 116 ? 52.121 2.227   14.691 1.00 6.18  ? 136 CYS A O   1 
ATOM   852  C  CB  . CYS A 1 116 ? 49.732 4.282   14.459 1.00 8.54  ? 136 CYS A CB  1 
ATOM   853  S  SG  . CYS A 1 116 ? 48.434 4.921   13.370 1.00 9.03  ? 136 CYS A SG  1 
ATOM   854  N  N   . LEU A 1 117 ? 52.460 4.256   15.754 1.00 8.38  ? 137 LEU A N   1 
ATOM   855  C  CA  . LEU A 1 117 ? 53.384 3.830   16.795 1.00 6.83  ? 137 LEU A CA  1 
ATOM   856  C  C   . LEU A 1 117 ? 52.629 4.092   18.083 1.00 7.24  ? 137 LEU A C   1 
ATOM   857  O  O   . LEU A 1 117 ? 52.175 5.216   18.310 1.00 5.71  ? 137 LEU A O   1 
ATOM   858  C  CB  . LEU A 1 117 ? 54.730 4.636   16.819 1.00 6.49  ? 137 LEU A CB  1 
ATOM   859  C  CG  . LEU A 1 117 ? 55.801 4.175   17.885 1.00 4.45  ? 137 LEU A CG  1 
ATOM   860  C  CD1 . LEU A 1 117 ? 56.463 2.913   17.329 1.00 4.69  ? 137 LEU A CD1 1 
ATOM   861  C  CD2 . LEU A 1 117 ? 56.870 5.304   17.902 1.00 2.80  ? 137 LEU A CD2 1 
ATOM   862  N  N   . ILE A 1 118 ? 52.429 2.988   18.850 1.00 8.36  ? 138 ILE A N   1 
ATOM   863  C  CA  . ILE A 1 118 ? 51.954 2.822   20.207 1.00 8.55  ? 138 ILE A CA  1 
ATOM   864  C  C   . ILE A 1 118 ? 53.151 2.565   21.144 1.00 9.27  ? 138 ILE A C   1 
ATOM   865  O  O   . ILE A 1 118 ? 54.029 1.755   20.815 1.00 10.98 ? 138 ILE A O   1 
ATOM   866  C  CB  . ILE A 1 118 ? 51.083 1.595   20.175 1.00 7.77  ? 138 ILE A CB  1 
ATOM   867  C  CG1 . ILE A 1 118 ? 50.123 1.837   18.982 1.00 6.59  ? 138 ILE A CG1 1 
ATOM   868  C  CG2 . ILE A 1 118 ? 50.223 1.547   21.438 1.00 7.98  ? 138 ILE A CG2 1 
ATOM   869  C  CD1 . ILE A 1 118 ? 48.952 0.898   18.878 1.00 4.84  ? 138 ILE A CD1 1 
ATOM   870  N  N   . SER A 1 119 ? 53.285 3.246   22.302 1.00 6.84  ? 139 SER A N   1 
ATOM   871  C  CA  . SER A 1 119 ? 54.422 3.080   23.184 1.00 5.94  ? 139 SER A CA  1 
ATOM   872  C  C   . SER A 1 119 ? 53.920 3.015   24.623 1.00 5.74  ? 139 SER A C   1 
ATOM   873  O  O   . SER A 1 119 ? 52.929 3.630   24.971 1.00 6.15  ? 139 SER A O   1 
ATOM   874  C  CB  . SER A 1 119 ? 55.345 4.260   22.975 1.00 5.19  ? 139 SER A CB  1 
ATOM   875  O  OG  . SER A 1 119 ? 54.686 5.497   22.802 1.00 5.19  ? 139 SER A OG  1 
ATOM   876  N  N   . GLY A 1 120 ? 54.544 2.407   25.614 1.00 5.91  ? 140 GLY A N   1 
ATOM   877  C  CA  . GLY A 1 120 ? 53.937 2.438   26.967 1.00 5.27  ? 140 GLY A CA  1 
ATOM   878  C  C   . GLY A 1 120 ? 54.827 1.541   27.879 1.00 6.08  ? 140 GLY A C   1 
ATOM   879  O  O   . GLY A 1 120 ? 55.680 0.797   27.417 1.00 5.76  ? 140 GLY A O   1 
ATOM   880  N  N   . TRP A 1 121 ? 54.612 1.604   29.181 1.00 6.01  ? 141 TRP A N   1 
ATOM   881  C  CA  . TRP A 1 121 ? 55.356 0.818   30.114 1.00 6.46  ? 141 TRP A CA  1 
ATOM   882  C  C   . TRP A 1 121 ? 54.398 -0.230  30.697 1.00 8.48  ? 141 TRP A C   1 
ATOM   883  O  O   . TRP A 1 121 ? 54.613 -0.764  31.811 1.00 9.78  ? 141 TRP A O   1 
ATOM   884  C  CB  . TRP A 1 121 ? 55.859 1.708   31.265 1.00 5.63  ? 141 TRP A CB  1 
ATOM   885  C  CG  . TRP A 1 121 ? 57.046 2.568   30.913 1.00 5.32  ? 141 TRP A CG  1 
ATOM   886  C  CD1 . TRP A 1 121 ? 58.355 2.218   30.964 1.00 4.64  ? 141 TRP A CD1 1 
ATOM   887  C  CD2 . TRP A 1 121 ? 56.964 3.931   30.460 1.00 5.40  ? 141 TRP A CD2 1 
ATOM   888  N  NE1 . TRP A 1 121 ? 59.128 3.313   30.627 1.00 6.04  ? 141 TRP A NE1 1 
ATOM   889  C  CE2 . TRP A 1 121 ? 58.287 4.375   30.298 1.00 7.54  ? 141 TRP A CE2 1 
ATOM   890  C  CE3 . TRP A 1 121 ? 55.921 4.845   30.341 1.00 5.02  ? 141 TRP A CE3 1 
ATOM   891  C  CZ2 . TRP A 1 121 ? 58.544 5.727   29.968 1.00 8.38  ? 141 TRP A CZ2 1 
ATOM   892  C  CZ3 . TRP A 1 121 ? 56.145 6.151   30.004 1.00 5.51  ? 141 TRP A CZ3 1 
ATOM   893  C  CH2 . TRP A 1 121 ? 57.481 6.589   29.898 1.00 7.12  ? 141 TRP A CH2 1 
ATOM   894  N  N   . GLY A 1 122 ? 53.334 -0.501  29.942 1.00 8.28  ? 142 GLY A N   1 
ATOM   895  C  CA  . GLY A 1 122 ? 52.369 -1.504  30.371 1.00 9.52  ? 142 GLY A CA  1 
ATOM   896  C  C   . GLY A 1 122 ? 52.895 -2.943  30.327 1.00 10.25 ? 142 GLY A C   1 
ATOM   897  O  O   . GLY A 1 122 ? 54.066 -3.231  29.961 1.00 9.92  ? 142 GLY A O   1 
ATOM   898  N  N   . ASN A 1 123 ? 52.005 -3.836  30.714 1.00 9.64  ? 143 ASN A N   1 
ATOM   899  C  CA  . ASN A 1 123 ? 52.317 -5.260  30.668 1.00 10.38 ? 143 ASN A CA  1 
ATOM   900  C  C   . ASN A 1 123 ? 52.742 -5.785  29.289 1.00 12.18 ? 143 ASN A C   1 
ATOM   901  O  O   . ASN A 1 123 ? 52.096 -5.399  28.309 1.00 12.65 ? 143 ASN A O   1 
ATOM   902  C  CB  . ASN A 1 123 ? 50.989 -5.974  31.055 1.00 8.03  ? 143 ASN A CB  1 
ATOM   903  C  CG  . ASN A 1 123 ? 51.185 -7.331  31.636 1.00 7.27  ? 143 ASN A CG  1 
ATOM   904  O  OD1 . ASN A 1 123 ? 52.266 -7.929  31.674 0.73 7.70  ? 143 ASN A OD1 1 
ATOM   905  N  ND2 . ASN A 1 123 ? 50.061 -7.930  32.003 0.49 6.91  ? 143 ASN A ND2 1 
ATOM   906  N  N   . THR A 1 124 ? 53.742 -6.697  29.271 1.00 13.89 ? 144 THR A N   1 
ATOM   907  C  CA  . THR A 1 124 ? 54.346 -7.341  28.088 1.00 15.58 ? 144 THR A CA  1 
ATOM   908  C  C   . THR A 1 124 ? 53.843 -8.773  27.856 1.00 17.77 ? 144 THR A C   1 
ATOM   909  O  O   . THR A 1 124 ? 54.220 -9.417  26.875 1.00 17.75 ? 144 THR A O   1 
ATOM   910  C  CB  . THR A 1 124 ? 55.900 -7.345  28.176 1.00 14.38 ? 144 THR A CB  1 
ATOM   911  O  OG1 . THR A 1 124 ? 56.069 -7.941  29.454 1.00 15.78 ? 144 THR A OG1 1 
ATOM   912  C  CG2 . THR A 1 124 ? 56.518 -5.975  28.322 1.00 12.19 ? 144 THR A CG2 1 
ATOM   913  N  N   . LYS A 1 125 ? 53.025 -9.274  28.791 1.00 20.62 ? 145 LYS A N   1 
ATOM   914  C  CA  . LYS A 1 125 ? 52.523 -10.615 28.817 1.00 23.28 ? 145 LYS A CA  1 
ATOM   915  C  C   . LYS A 1 125 ? 51.023 -10.656 28.600 1.00 25.64 ? 145 LYS A C   1 
ATOM   916  O  O   . LYS A 1 125 ? 50.204 -9.986  29.225 1.00 24.84 ? 145 LYS A O   1 
ATOM   917  C  CB  . LYS A 1 125 ? 53.027 -11.409 30.015 1.00 23.79 ? 145 LYS A CB  1 
ATOM   918  C  CG  . LYS A 1 125 ? 54.410 -12.065 29.876 0.91 25.10 ? 145 LYS A CG  1 
ATOM   919  C  CD  . LYS A 1 125 ? 55.273 -11.452 28.766 0.10 26.01 ? 145 LYS A CD  1 
ATOM   920  C  CE  . LYS A 1 125 ? 56.624 -12.081 28.441 0.21 26.54 ? 145 LYS A CE  1 
ATOM   921  N  NZ  . LYS A 1 125 ? 57.456 -11.172 27.635 0.50 26.70 ? 145 LYS A NZ  1 
ATOM   922  N  N   . SER A 1 126 ? 50.679 -11.508 27.659 1.00 28.32 ? 146 SER A N   1 
ATOM   923  C  CA  . SER A 1 126 ? 49.308 -11.735 27.300 1.00 30.90 ? 146 SER A CA  1 
ATOM   924  C  C   . SER A 1 126 ? 48.544 -12.572 28.325 1.00 33.63 ? 146 SER A C   1 
ATOM   925  O  O   . SER A 1 126 ? 47.349 -12.406 28.580 1.00 34.50 ? 146 SER A O   1 
ATOM   926  C  CB  . SER A 1 126 ? 49.351 -12.512 26.011 1.00 31.12 ? 146 SER A CB  1 
ATOM   927  O  OG  . SER A 1 126 ? 48.206 -11.996 25.377 1.00 31.64 ? 146 SER A OG  1 
ATOM   928  N  N   . SER A 1 127 ? 49.220 -13.558 28.885 1.00 34.90 ? 147 SER A N   1 
ATOM   929  C  CA  . SER A 1 127 ? 48.736 -14.478 29.893 1.00 35.92 ? 147 SER A CA  1 
ATOM   930  C  C   . SER A 1 127 ? 49.756 -14.349 31.010 1.00 36.17 ? 147 SER A C   1 
ATOM   931  O  O   . SER A 1 127 ? 50.830 -14.986 31.040 1.00 36.12 ? 147 SER A O   1 
ATOM   932  C  CB  . SER A 1 127 ? 48.685 -15.924 29.377 1.00 36.57 ? 147 SER A CB  1 
ATOM   933  O  OG  . SER A 1 127 ? 48.086 -16.773 30.337 0.25 36.59 ? 147 SER A OG  1 
ATOM   934  N  N   . GLY A 1 128 ? 49.445 -13.401 31.863 1.00 36.37 ? 148 GLY A N   1 
ATOM   935  C  CA  . GLY A 1 128 ? 50.355 -13.196 32.980 1.00 36.98 ? 148 GLY A CA  1 
ATOM   936  C  C   . GLY A 1 128 ? 50.587 -11.726 33.266 1.00 37.06 ? 148 GLY A C   1 
ATOM   937  O  O   . GLY A 1 128 ? 49.874 -10.954 32.607 1.00 37.10 ? 148 GLY A O   1 
ATOM   938  N  N   . THR A 1 129 ? 51.586 -11.450 34.140 1.00 36.14 ? 149 THR A N   1 
ATOM   939  C  CA  . THR A 1 129 ? 52.039 -10.129 34.557 1.00 35.74 ? 149 THR A CA  1 
ATOM   940  C  C   . THR A 1 129 ? 53.521 -9.753  34.487 1.00 34.83 ? 149 THR A C   1 
ATOM   941  O  O   . THR A 1 129 ? 54.383 -10.163 35.282 1.00 36.02 ? 149 THR A O   1 
ATOM   942  C  CB  . THR A 1 129 ? 51.391 -9.748  35.877 1.00 36.79 ? 149 THR A CB  1 
ATOM   943  O  OG1 . THR A 1 129 ? 50.039 -9.648  35.438 1.00 37.20 ? 149 THR A OG1 1 
ATOM   944  C  CG2 . THR A 1 129 ? 51.926 -8.417  36.391 1.00 37.02 ? 149 THR A CG2 1 
ATOM   945  N  N   . SER A 1 130 ? 53.866 -8.905  33.537 1.00 32.10 ? 150 SER A N   1 
ATOM   946  C  CA  . SER A 1 130 ? 55.268 -8.567  33.449 1.00 28.49 ? 150 SER A CA  1 
ATOM   947  C  C   . SER A 1 130 ? 55.478 -7.146  32.998 1.00 24.87 ? 150 SER A C   1 
ATOM   948  O  O   . SER A 1 130 ? 55.425 -6.865  31.824 1.00 24.00 ? 150 SER A O   1 
ATOM   949  C  CB  . SER A 1 130 ? 55.952 -9.506  32.500 1.00 28.73 ? 150 SER A CB  1 
ATOM   950  O  OG  . SER A 1 130 ? 57.336 -9.254  32.674 1.00 29.02 ? 150 SER A OG  1 
ATOM   951  N  N   . TYR A 1 131 ? 55.783 -6.306  33.971 1.00 22.65 ? 151 TYR A N   1 
ATOM   952  C  CA  . TYR A 1 131 ? 56.019 -4.954  33.667 1.00 21.95 ? 151 TYR A CA  1 
ATOM   953  C  C   . TYR A 1 131 ? 57.455 -4.671  33.308 1.00 19.33 ? 151 TYR A C   1 
ATOM   954  O  O   . TYR A 1 131 ? 58.347 -5.140  34.010 1.00 21.13 ? 151 TYR A O   1 
ATOM   955  C  CB  . TYR A 1 131 ? 55.638 -4.121  34.876 1.00 24.04 ? 151 TYR A CB  1 
ATOM   956  C  CG  . TYR A 1 131 ? 54.153 -4.107  35.040 1.00 25.37 ? 151 TYR A CG  1 
ATOM   957  C  CD1 . TYR A 1 131 ? 53.357 -3.454  34.096 1.00 26.23 ? 151 TYR A CD1 1 
ATOM   958  C  CD2 . TYR A 1 131 ? 53.570 -4.867  36.051 1.00 25.78 ? 151 TYR A CD2 1 
ATOM   959  C  CE1 . TYR A 1 131 ? 51.967 -3.482  34.188 1.00 26.73 ? 151 TYR A CE1 1 
ATOM   960  C  CE2 . TYR A 1 131 ? 52.176 -4.910  36.141 1.00 26.52 ? 151 TYR A CE2 1 
ATOM   961  C  CZ  . TYR A 1 131 ? 51.392 -4.210  35.236 1.00 26.70 ? 151 TYR A CZ  1 
ATOM   962  O  OH  . TYR A 1 131 ? 50.049 -4.344  35.329 1.00 26.72 ? 151 TYR A OH  1 
ATOM   963  N  N   . PRO A 1 132 ? 57.656 -3.871  32.278 1.00 15.30 ? 152 PRO A N   1 
ATOM   964  C  CA  . PRO A 1 132 ? 58.985 -3.536  31.894 1.00 15.18 ? 152 PRO A CA  1 
ATOM   965  C  C   . PRO A 1 132 ? 59.534 -2.353  32.663 1.00 15.07 ? 152 PRO A C   1 
ATOM   966  O  O   . PRO A 1 132 ? 58.759 -1.540  33.162 1.00 15.78 ? 152 PRO A O   1 
ATOM   967  C  CB  . PRO A 1 132 ? 58.827 -3.028  30.485 1.00 15.50 ? 152 PRO A CB  1 
ATOM   968  C  CG  . PRO A 1 132 ? 57.370 -2.711  30.250 1.00 14.59 ? 152 PRO A CG  1 
ATOM   969  C  CD  . PRO A 1 132 ? 56.642 -3.332  31.394 1.00 13.48 ? 152 PRO A CD  1 
ATOM   970  N  N   . ASP A 1 133 ? 60.846 -2.232  32.592 1.00 13.86 ? 153 ASP A N   1 
ATOM   971  C  CA  . ASP A 1 133 ? 61.471 -1.087  33.167 1.00 14.57 ? 153 ASP A CA  1 
ATOM   972  C  C   . ASP A 1 133 ? 61.568 0.081   32.136 1.00 10.55 ? 153 ASP A C   1 
ATOM   973  O  O   . ASP A 1 133 ? 61.397 1.222   32.590 1.00 9.67  ? 153 ASP A O   1 
ATOM   974  C  CB  . ASP A 1 133 ? 62.913 -1.479  33.603 1.00 18.22 ? 153 ASP A CB  1 
ATOM   975  C  CG  . ASP A 1 133 ? 63.125 -2.083  34.966 1.00 21.07 ? 153 ASP A CG  1 
ATOM   976  O  OD1 . ASP A 1 133 ? 62.121 -1.894  35.778 1.00 20.82 ? 153 ASP A OD1 1 
ATOM   977  O  OD2 . ASP A 1 133 ? 64.187 -2.624  35.284 1.00 23.51 ? 153 ASP A OD2 1 
ATOM   978  N  N   . VAL A 1 134 ? 61.983 -0.251  30.920 1.00 7.45  ? 154 VAL A N   1 
ATOM   979  C  CA  . VAL A 1 134 ? 62.187 0.653   29.836 1.00 7.07  ? 154 VAL A CA  1 
ATOM   980  C  C   . VAL A 1 134 ? 60.966 0.743   28.974 1.00 6.51  ? 154 VAL A C   1 
ATOM   981  O  O   . VAL A 1 134 ? 60.111 -0.105  28.953 1.00 7.38  ? 154 VAL A O   1 
ATOM   982  C  CB  . VAL A 1 134 ? 63.450 0.389   28.999 1.00 7.72  ? 154 VAL A CB  1 
ATOM   983  C  CG1 . VAL A 1 134 ? 64.676 0.671   29.894 1.00 8.47  ? 154 VAL A CG1 1 
ATOM   984  C  CG2 . VAL A 1 134 ? 63.347 -0.901  28.148 1.00 5.95  ? 154 VAL A CG2 1 
ATOM   985  N  N   . LEU A 1 135 ? 60.897 1.763   28.211 1.00 6.18  ? 155 LEU A N   1 
ATOM   986  C  CA  . LEU A 1 135 ? 59.747 1.961   27.324 1.00 6.59  ? 155 LEU A CA  1 
ATOM   987  C  C   . LEU A 1 135 ? 59.779 0.987   26.189 1.00 6.96  ? 155 LEU A C   1 
ATOM   988  O  O   . LEU A 1 135 ? 60.812 0.914   25.477 1.00 7.49  ? 155 LEU A O   1 
ATOM   989  C  CB  . LEU A 1 135 ? 59.795 3.412   26.754 1.00 4.82  ? 155 LEU A CB  1 
ATOM   990  C  CG  . LEU A 1 135 ? 58.602 3.950   26.004 1.00 4.06  ? 155 LEU A CG  1 
ATOM   991  C  CD1 . LEU A 1 135 ? 57.302 4.112   26.766 1.00 2.00  ? 155 LEU A CD1 1 
ATOM   992  C  CD2 . LEU A 1 135 ? 58.877 5.211   25.192 1.00 4.44  ? 155 LEU A CD2 1 
ATOM   993  N  N   . LYS A 1 136 ? 58.583 0.406   25.941 1.00 6.87  ? 156 LYS A N   1 
ATOM   994  C  CA  . LYS A 1 136 ? 58.333 -0.442  24.786 1.00 7.32  ? 156 LYS A CA  1 
ATOM   995  C  C   . LYS A 1 136 ? 57.460 0.191   23.659 1.00 6.61  ? 156 LYS A C   1 
ATOM   996  O  O   . LYS A 1 136 ? 56.648 1.080   23.860 1.00 6.81  ? 156 LYS A O   1 
ATOM   997  C  CB  . LYS A 1 136 ? 57.628 -1.708  25.223 1.00 8.87  ? 156 LYS A CB  1 
ATOM   998  C  CG  . LYS A 1 136 ? 58.427 -2.408  26.315 1.00 8.90  ? 156 LYS A CG  1 
ATOM   999  C  CD  . LYS A 1 136 ? 59.704 -3.028  25.741 1.00 10.18 ? 156 LYS A CD  1 
ATOM   1000 C  CE  . LYS A 1 136 ? 60.479 -3.732  26.836 0.52 11.03 ? 156 LYS A CE  1 
ATOM   1001 N  NZ  . LYS A 1 136 ? 61.526 -4.589  26.253 0.70 11.84 ? 156 LYS A NZ  1 
ATOM   1002 N  N   . CYS A 1 137 ? 57.580 -0.272  22.414 1.00 4.56  ? 157 CYS A N   1 
ATOM   1003 C  CA  . CYS A 1 137 ? 57.069 0.316   21.197 1.00 5.72  ? 157 CYS A CA  1 
ATOM   1004 C  C   . CYS A 1 137 ? 56.467 -0.762  20.361 1.00 5.57  ? 157 CYS A C   1 
ATOM   1005 O  O   . CYS A 1 137 ? 56.866 -1.897  20.513 1.00 4.62  ? 157 CYS A O   1 
ATOM   1006 C  CB  . CYS A 1 137 ? 58.100 1.013   20.306 1.00 6.14  ? 157 CYS A CB  1 
ATOM   1007 S  SG  . CYS A 1 137 ? 58.506 2.648   20.955 1.00 8.58  ? 157 CYS A SG  1 
ATOM   1008 N  N   . LEU A 1 138 ? 55.511 -0.403  19.507 1.00 6.25  ? 158 LEU A N   1 
ATOM   1009 C  CA  . LEU A 1 138 ? 54.843 -1.369  18.643 1.00 5.39  ? 158 LEU A CA  1 
ATOM   1010 C  C   . LEU A 1 138 ? 54.255 -0.652  17.462 1.00 5.43  ? 158 LEU A C   1 
ATOM   1011 O  O   . LEU A 1 138 ? 53.602 0.347   17.640 1.00 3.05  ? 158 LEU A O   1 
ATOM   1012 C  CB  . LEU A 1 138 ? 53.710 -2.082  19.413 1.00 5.72  ? 158 LEU A CB  1 
ATOM   1013 C  CG  . LEU A 1 138 ? 52.773 -3.026  18.593 1.00 5.64  ? 158 LEU A CG  1 
ATOM   1014 C  CD1 . LEU A 1 138 ? 53.378 -4.372  18.360 1.00 4.68  ? 158 LEU A CD1 1 
ATOM   1015 C  CD2 . LEU A 1 138 ? 51.511 -3.414  19.365 1.00 6.50  ? 158 LEU A CD2 1 
ATOM   1016 N  N   . LYS A 1 139 ? 54.614 -1.076  16.265 1.00 7.45  ? 159 LYS A N   1 
ATOM   1017 C  CA  . LYS A 1 139 ? 54.055 -0.454  15.073 1.00 11.09 ? 159 LYS A CA  1 
ATOM   1018 C  C   . LYS A 1 139 ? 52.731 -1.155  14.769 1.00 9.30  ? 159 LYS A C   1 
ATOM   1019 O  O   . LYS A 1 139 ? 52.627 -2.372  14.960 1.00 9.21  ? 159 LYS A O   1 
ATOM   1020 C  CB  . LYS A 1 139 ? 55.068 -0.430  13.964 1.00 15.27 ? 159 LYS A CB  1 
ATOM   1021 C  CG  . LYS A 1 139 ? 56.352 0.210   14.474 1.00 19.34 ? 159 LYS A CG  1 
ATOM   1022 C  CD  . LYS A 1 139 ? 56.940 1.254   13.533 1.00 22.74 ? 159 LYS A CD  1 
ATOM   1023 C  CE  . LYS A 1 139 ? 56.179 2.572   13.581 1.00 25.46 ? 159 LYS A CE  1 
ATOM   1024 N  NZ  . LYS A 1 139 ? 55.759 3.127   12.259 1.00 27.44 ? 159 LYS A NZ  1 
ATOM   1025 N  N   . ALA A 1 140 ? 51.638 -0.476  14.391 1.00 8.43  ? 160 ALA A N   1 
ATOM   1026 C  CA  . ALA A 1 140 ? 50.379 -1.238  14.241 1.00 7.02  ? 160 ALA A CA  1 
ATOM   1027 C  C   . ALA A 1 140 ? 49.446 -0.444  13.352 1.00 7.99  ? 160 ALA A C   1 
ATOM   1028 O  O   . ALA A 1 140 ? 49.391 0.749   13.490 1.00 8.61  ? 160 ALA A O   1 
ATOM   1029 C  CB  . ALA A 1 140 ? 49.724 -1.504  15.584 1.00 5.06  ? 160 ALA A CB  1 
ATOM   1030 N  N   . PRO A 1 141 ? 48.733 -1.084  12.451 1.00 7.07  ? 161 PRO A N   1 
ATOM   1031 C  CA  . PRO A 1 141 ? 47.960 -0.370  11.504 1.00 7.96  ? 161 PRO A CA  1 
ATOM   1032 C  C   . PRO A 1 141 ? 46.556 -0.136  12.094 1.00 10.53 ? 161 PRO A C   1 
ATOM   1033 O  O   . PRO A 1 141 ? 46.020 -0.856  12.945 1.00 11.24 ? 161 PRO A O   1 
ATOM   1034 C  CB  . PRO A 1 141 ? 47.874 -1.339  10.348 1.00 6.06  ? 161 PRO A CB  1 
ATOM   1035 C  CG  . PRO A 1 141 ? 47.961 -2.704  11.005 1.00 4.92  ? 161 PRO A CG  1 
ATOM   1036 C  CD  . PRO A 1 141 ? 48.511 -2.534  12.384 1.00 5.89  ? 161 PRO A CD  1 
ATOM   1037 N  N   . ILE A 1 142 ? 45.897 0.953   11.664 1.00 11.53 ? 162 ILE A N   1 
ATOM   1038 C  CA  . ILE A 1 142 ? 44.524 1.256   12.075 1.00 9.75  ? 162 ILE A CA  1 
ATOM   1039 C  C   . ILE A 1 142 ? 43.670 0.289   11.272 1.00 10.02 ? 162 ILE A C   1 
ATOM   1040 O  O   . ILE A 1 142 ? 43.860 0.134   10.046 1.00 10.41 ? 162 ILE A O   1 
ATOM   1041 C  CB  . ILE A 1 142 ? 44.213 2.751   11.792 1.00 8.11  ? 162 ILE A CB  1 
ATOM   1042 C  CG1 . ILE A 1 142 ? 45.040 3.787   12.582 1.00 8.54  ? 162 ILE A CG1 1 
ATOM   1043 C  CG2 . ILE A 1 142 ? 42.719 2.959   11.935 1.00 5.69  ? 162 ILE A CG2 1 
ATOM   1044 C  CD1 . ILE A 1 142 ? 44.942 5.189   11.968 1.00 9.17  ? 162 ILE A CD1 1 
ATOM   1045 N  N   . LEU A 1 143 ? 42.717 -0.414  11.894 1.00 10.32 ? 163 LEU A N   1 
ATOM   1046 C  CA  . LEU A 1 143 ? 41.904 -1.412  11.164 1.00 9.19  ? 163 LEU A CA  1 
ATOM   1047 C  C   . LEU A 1 143 ? 40.651 -0.764  10.574 1.00 9.75  ? 163 LEU A C   1 
ATOM   1048 O  O   . LEU A 1 143 ? 40.340 0.301   11.022 1.00 10.36 ? 163 LEU A O   1 
ATOM   1049 C  CB  . LEU A 1 143 ? 41.446 -2.520  12.168 1.00 7.78  ? 163 LEU A CB  1 
ATOM   1050 C  CG  . LEU A 1 143 ? 42.630 -3.316  12.758 1.00 8.47  ? 163 LEU A CG  1 
ATOM   1051 C  CD1 . LEU A 1 143 ? 42.092 -4.518  13.491 1.00 10.08 ? 163 LEU A CD1 1 
ATOM   1052 C  CD2 . LEU A 1 143 ? 43.655 -3.799  11.729 1.00 6.85  ? 163 LEU A CD2 1 
ATOM   1053 N  N   . SER A 1 144 ? 39.912 -1.357  9.607  1.00 10.01 ? 164 SER A N   1 
ATOM   1054 C  CA  . SER A 1 144 ? 38.699 -0.828  9.059  1.00 10.62 ? 164 SER A CA  1 
ATOM   1055 C  C   . SER A 1 144 ? 37.602 -0.882  10.146 1.00 11.95 ? 164 SER A C   1 
ATOM   1056 O  O   . SER A 1 144 ? 37.507 -1.624  11.146 1.00 12.60 ? 164 SER A O   1 
ATOM   1057 C  CB  . SER A 1 144 ? 38.292 -1.588  7.810  1.00 11.05 ? 164 SER A CB  1 
ATOM   1058 O  OG  . SER A 1 144 ? 37.860 -2.809  8.374  1.00 11.52 ? 164 SER A OG  1 
ATOM   1059 N  N   . ASP A 1 145 ? 36.665 -0.011  9.949  1.00 13.20 ? 165 ASP A N   1 
ATOM   1060 C  CA  . ASP A 1 145 ? 35.607 0.116   10.914 1.00 14.94 ? 165 ASP A CA  1 
ATOM   1061 C  C   . ASP A 1 145 ? 34.698 -1.097  10.897 1.00 12.58 ? 165 ASP A C   1 
ATOM   1062 O  O   . ASP A 1 145 ? 34.175 -1.526  11.921 1.00 10.29 ? 165 ASP A O   1 
ATOM   1063 C  CB  . ASP A 1 145 ? 34.946 1.382   10.464 1.00 20.12 ? 165 ASP A CB  1 
ATOM   1064 C  CG  . ASP A 1 145 ? 33.569 1.438   11.041 1.00 26.01 ? 165 ASP A CG  1 
ATOM   1065 O  OD1 . ASP A 1 145 ? 32.548 0.944   10.460 1.00 29.38 ? 165 ASP A OD1 1 
ATOM   1066 O  OD2 . ASP A 1 145 ? 33.511 2.164   12.147 1.00 27.05 ? 165 ASP A OD2 1 
ATOM   1067 N  N   . SER A 1 146 ? 34.664 -1.703  9.701  1.00 13.16 ? 166 SER A N   1 
ATOM   1068 C  CA  . SER A 1 146 ? 33.950 -2.938  9.504  1.00 12.66 ? 166 SER A CA  1 
ATOM   1069 C  C   . SER A 1 146 ? 34.467 -4.005  10.432 1.00 13.81 ? 166 SER A C   1 
ATOM   1070 O  O   . SER A 1 146 ? 33.674 -4.694  11.075 1.00 14.06 ? 166 SER A O   1 
ATOM   1071 C  CB  . SER A 1 146 ? 33.693 -3.390  8.079  1.00 12.58 ? 166 SER A CB  1 
ATOM   1072 O  OG  . SER A 1 146 ? 34.823 -3.498  7.184  1.00 13.42 ? 166 SER A OG  1 
ATOM   1073 N  N   . SER A 1 147 ? 35.801 -4.215  10.423 1.00 13.71 ? 167 SER A N   1 
ATOM   1074 C  CA  . SER A 1 147 ? 36.424 -5.233  11.209 1.00 13.81 ? 167 SER A CA  1 
ATOM   1075 C  C   . SER A 1 147 ? 36.396 -4.883  12.684 1.00 12.18 ? 167 SER A C   1 
ATOM   1076 O  O   . SER A 1 147 ? 36.345 -5.781  13.530 1.00 12.05 ? 167 SER A O   1 
ATOM   1077 C  CB  . SER A 1 147 ? 37.869 -5.376  10.724 1.00 15.55 ? 167 SER A CB  1 
ATOM   1078 O  OG  . SER A 1 147 ? 37.879 -5.839  9.399  1.00 16.55 ? 167 SER A OG  1 
ATOM   1079 N  N   . CYS A 1 148 ? 36.469 -3.580  12.965 1.00 10.25 ? 168 CYS A N   1 
ATOM   1080 C  CA  . CYS A 1 148 ? 36.491 -3.195  14.374 1.00 9.33  ? 168 CYS A CA  1 
ATOM   1081 C  C   . CYS A 1 148 ? 35.166 -3.578  15.016 1.00 9.27  ? 168 CYS A C   1 
ATOM   1082 O  O   . CYS A 1 148 ? 35.062 -4.137  16.114 1.00 6.91  ? 168 CYS A O   1 
ATOM   1083 C  CB  . CYS A 1 148 ? 36.725 -1.687  14.450 1.00 9.72  ? 168 CYS A CB  1 
ATOM   1084 S  SG  . CYS A 1 148 ? 36.931 -0.977  16.083 1.00 10.61 ? 168 CYS A SG  1 
ATOM   1085 N  N   . LYS A 1 149 ? 34.108 -3.292  14.248 1.00 12.23 ? 169 LYS A N   1 
ATOM   1086 C  CA  . LYS A 1 149 ? 32.771 -3.591  14.698 1.00 13.83 ? 169 LYS A CA  1 
ATOM   1087 C  C   . LYS A 1 149 ? 32.440 -5.025  14.681 1.00 13.23 ? 169 LYS A C   1 
ATOM   1088 O  O   . LYS A 1 149 ? 31.635 -5.441  15.507 1.00 11.60 ? 169 LYS A O   1 
ATOM   1089 C  CB  . LYS A 1 149 ? 31.568 -2.938  14.042 1.00 14.83 ? 169 LYS A CB  1 
ATOM   1090 C  CG  . LYS A 1 149 ? 31.566 -1.645  14.815 1.00 15.56 ? 169 LYS A CG  1 
ATOM   1091 C  CD  . LYS A 1 149 ? 31.970 -0.552  13.840 1.00 16.39 ? 169 LYS A CD  1 
ATOM   1092 C  CE  . LYS A 1 149 ? 30.728 0.255   13.461 1.00 17.94 ? 169 LYS A CE  1 
ATOM   1093 N  NZ  . LYS A 1 149 ? 30.875 1.711   13.257 1.00 18.35 ? 169 LYS A NZ  1 
ATOM   1094 N  N   . SER A 1 150 ? 32.976 -5.737  13.702 1.00 15.19 ? 170 SER A N   1 
ATOM   1095 C  CA  . SER A 1 150 ? 32.609 -7.107  13.801 1.00 15.32 ? 170 SER A CA  1 
ATOM   1096 C  C   . SER A 1 150 ? 33.376 -7.759  14.934 1.00 12.92 ? 170 SER A C   1 
ATOM   1097 O  O   . SER A 1 150 ? 32.928 -8.746  15.454 1.00 14.17 ? 170 SER A O   1 
ATOM   1098 C  CB  . SER A 1 150 ? 32.633 -7.767  12.453 1.00 18.08 ? 170 SER A CB  1 
ATOM   1099 O  OG  . SER A 1 150 ? 34.016 -7.950  12.319 1.00 20.69 ? 170 SER A OG  1 
ATOM   1100 N  N   . ALA A 1 151 ? 34.406 -7.192  15.531 1.00 10.53 ? 171 ALA A N   1 
ATOM   1101 C  CA  . ALA A 1 151 ? 35.054 -7.763  16.674 1.00 9.86  ? 171 ALA A CA  1 
ATOM   1102 C  C   . ALA A 1 151 ? 34.398 -7.335  17.987 1.00 10.28 ? 171 ALA A C   1 
ATOM   1103 O  O   . ALA A 1 151 ? 34.575 -7.952  19.025 1.00 10.80 ? 171 ALA A O   1 
ATOM   1104 C  CB  . ALA A 1 151 ? 36.495 -7.233  16.665 1.00 9.75  ? 171 ALA A CB  1 
ATOM   1105 N  N   . TYR A 1 152 ? 33.722 -6.184  18.042 1.00 9.18  ? 172 TYR A N   1 
ATOM   1106 C  CA  . TYR A 1 152 ? 33.209 -5.711  19.283 1.00 9.72  ? 172 TYR A CA  1 
ATOM   1107 C  C   . TYR A 1 152 ? 31.851 -5.202  18.990 1.00 12.39 ? 172 TYR A C   1 
ATOM   1108 O  O   . TYR A 1 152 ? 31.640 -3.983  19.000 1.00 12.98 ? 172 TYR A O   1 
ATOM   1109 C  CB  . TYR A 1 152 ? 33.972 -4.532  19.906 1.00 9.20  ? 172 TYR A CB  1 
ATOM   1110 C  CG  . TYR A 1 152 ? 35.345 -4.935  20.395 1.00 10.97 ? 172 TYR A CG  1 
ATOM   1111 C  CD1 . TYR A 1 152 ? 35.517 -5.606  21.620 1.00 11.36 ? 172 TYR A CD1 1 
ATOM   1112 C  CD2 . TYR A 1 152 ? 36.480 -4.690  19.609 1.00 12.04 ? 172 TYR A CD2 1 
ATOM   1113 C  CE1 . TYR A 1 152 ? 36.802 -6.039  22.048 1.00 12.13 ? 172 TYR A CE1 1 
ATOM   1114 C  CE2 . TYR A 1 152 ? 37.739 -5.019  20.060 1.00 13.11 ? 172 TYR A CE2 1 
ATOM   1115 C  CZ  . TYR A 1 152 ? 37.890 -5.662  21.274 1.00 13.15 ? 172 TYR A CZ  1 
ATOM   1116 O  OH  . TYR A 1 152 ? 39.141 -5.901  21.756 1.00 14.31 ? 172 TYR A OH  1 
ATOM   1117 N  N   . PRO A 1 153 ? 30.968 -6.158  18.626 1.00 14.88 ? 173 PRO A N   1 
ATOM   1118 C  CA  . PRO A 1 153 ? 29.632 -5.760  18.238 1.00 15.83 ? 173 PRO A CA  1 
ATOM   1119 C  C   . PRO A 1 153 ? 28.890 -4.991  19.301 1.00 17.04 ? 173 PRO A C   1 
ATOM   1120 O  O   . PRO A 1 153 ? 28.806 -5.351  20.491 1.00 18.79 ? 173 PRO A O   1 
ATOM   1121 C  CB  . PRO A 1 153 ? 28.828 -7.007  17.917 1.00 15.67 ? 173 PRO A CB  1 
ATOM   1122 C  CG  . PRO A 1 153 ? 29.819 -8.133  17.870 1.00 16.47 ? 173 PRO A CG  1 
ATOM   1123 C  CD  . PRO A 1 153 ? 31.161 -7.608  18.328 1.00 15.50 ? 173 PRO A CD  1 
ATOM   1124 N  N   . GLY A 1 154 ? 28.288 -3.913  18.818 1.00 16.34 ? 174 GLY A N   1 
ATOM   1125 C  CA  . GLY A 1 154 ? 27.574 -3.046  19.742 1.00 16.05 ? 174 GLY A CA  1 
ATOM   1126 C  C   . GLY A 1 154 ? 28.452 -2.194  20.681 1.00 14.33 ? 174 GLY A C   1 
ATOM   1127 O  O   . GLY A 1 154 ? 27.833 -1.394  21.355 1.00 13.39 ? 174 GLY A O   1 
ATOM   1128 N  N   . GLN A 1 155 ? 29.804 -2.298  20.713 1.00 13.00 ? 175 GLN A N   1 
ATOM   1129 C  CA  . GLN A 1 155 ? 30.611 -1.492  21.601 1.00 11.44 ? 175 GLN A CA  1 
ATOM   1130 C  C   . GLN A 1 155 ? 31.469 -0.385  21.034 1.00 10.18 ? 175 GLN A C   1 
ATOM   1131 O  O   . GLN A 1 155 ? 32.057 0.344   21.819 1.00 8.95  ? 175 GLN A O   1 
ATOM   1132 C  CB  . GLN A 1 155 ? 31.318 -2.283  22.688 1.00 13.06 ? 175 GLN A CB  1 
ATOM   1133 C  CG  . GLN A 1 155 ? 30.556 -3.548  23.014 1.00 15.86 ? 175 GLN A CG  1 
ATOM   1134 C  CD  . GLN A 1 155 ? 31.498 -4.758  23.093 1.00 19.19 ? 175 GLN A CD  1 
ATOM   1135 O  OE1 . GLN A 1 155 ? 32.403 -4.759  23.923 1.00 20.47 ? 175 GLN A OE1 1 
ATOM   1136 N  NE2 . GLN A 1 155 ? 31.269 -5.828  22.305 1.00 19.99 ? 175 GLN A NE2 1 
ATOM   1137 N  N   . ILE A 1 156 ? 31.495 -0.207  19.711 1.00 10.32 ? 176 ILE A N   1 
ATOM   1138 C  CA  . ILE A 1 156 ? 32.341 0.793   19.058 1.00 9.83  ? 176 ILE A CA  1 
ATOM   1139 C  C   . ILE A 1 156 ? 31.469 2.018   18.739 1.00 9.82  ? 176 ILE A C   1 
ATOM   1140 O  O   . ILE A 1 156 ? 30.482 1.900   17.988 1.00 9.82  ? 176 ILE A O   1 
ATOM   1141 C  CB  . ILE A 1 156 ? 33.056 0.212   17.813 1.00 8.21  ? 176 ILE A CB  1 
ATOM   1142 C  CG1 . ILE A 1 156 ? 33.844 -1.054  18.165 1.00 6.20  ? 176 ILE A CG1 1 
ATOM   1143 C  CG2 . ILE A 1 156 ? 33.984 1.172   17.075 1.00 9.53  ? 176 ILE A CG2 1 
ATOM   1144 C  CD1 . ILE A 1 156 ? 34.927 -0.998  19.258 1.00 4.74  ? 176 ILE A CD1 1 
ATOM   1145 N  N   . THR A 1 157 ? 31.846 3.199   19.268 1.00 8.12  ? 177 THR A N   1 
ATOM   1146 C  CA  . THR A 1 157 ? 31.202 4.456   18.975 1.00 7.77  ? 177 THR A CA  1 
ATOM   1147 C  C   . THR A 1 157 ? 31.927 5.155   17.882 1.00 8.84  ? 177 THR A C   1 
ATOM   1148 O  O   . THR A 1 157 ? 33.045 4.827   17.490 1.00 11.42 ? 177 THR A O   1 
ATOM   1149 C  CB  . THR A 1 157 ? 31.169 5.380   20.161 1.00 8.22  ? 177 THR A CB  1 
ATOM   1150 O  OG1 . THR A 1 157 ? 32.518 5.741   20.526 1.00 9.42  ? 177 THR A OG1 1 
ATOM   1151 C  CG2 . THR A 1 157 ? 30.624 4.544   21.267 1.00 7.78  ? 177 THR A CG2 1 
ATOM   1152 N  N   . SER A 1 158 ? 31.368 6.217   17.368 1.00 8.00  ? 178 SER A N   1 
ATOM   1153 C  CA  . SER A 1 158 ? 32.154 6.888   16.360 1.00 9.35  ? 178 SER A CA  1 
ATOM   1154 C  C   . SER A 1 158 ? 33.403 7.627   16.884 1.00 8.82  ? 178 SER A C   1 
ATOM   1155 O  O   . SER A 1 158 ? 34.148 8.192   16.100 1.00 9.30  ? 178 SER A O   1 
ATOM   1156 C  CB  . SER A 1 158 ? 31.196 7.850   15.709 1.00 11.94 ? 178 SER A CB  1 
ATOM   1157 O  OG  . SER A 1 158 ? 30.864 8.857   16.692 1.00 14.09 ? 178 SER A OG  1 
ATOM   1158 N  N   . ASN A 1 159 ? 33.669 7.558   18.173 1.00 7.01  ? 179 ASN A N   1 
ATOM   1159 C  CA  . ASN A 1 159 ? 34.836 8.150   18.797 1.00 5.47  ? 179 ASN A CA  1 
ATOM   1160 C  C   . ASN A 1 159 ? 35.908 7.129   19.140 1.00 4.33  ? 179 ASN A C   1 
ATOM   1161 O  O   . ASN A 1 159 ? 36.723 7.423   20.034 1.00 3.65  ? 179 ASN A O   1 
ATOM   1162 C  CB  . ASN A 1 159 ? 34.375 8.748   20.113 1.00 5.29  ? 179 ASN A CB  1 
ATOM   1163 C  CG  . ASN A 1 159 ? 33.434 9.934   19.885 1.00 4.85  ? 179 ASN A CG  1 
ATOM   1164 O  OD1 . ASN A 1 159 ? 33.547 10.737  18.969 1.00 4.20  ? 179 ASN A OD1 1 
ATOM   1165 N  ND2 . ASN A 1 159 ? 32.335 9.833   20.605 1.00 4.58  ? 179 ASN A ND2 1 
ATOM   1166 N  N   . MET A 1 160 ? 35.855 5.996   18.417 1.00 3.39  ? 180 MET A N   1 
ATOM   1167 C  CA  . MET A 1 160 ? 36.835 4.960   18.633 1.00 4.22  ? 180 MET A CA  1 
ATOM   1168 C  C   . MET A 1 160 ? 37.232 4.347   17.339 1.00 4.03  ? 180 MET A C   1 
ATOM   1169 O  O   . MET A 1 160 ? 36.386 4.381   16.464 1.00 4.77  ? 180 MET A O   1 
ATOM   1170 C  CB  . MET A 1 160 ? 36.231 3.785   19.402 1.00 5.46  ? 180 MET A CB  1 
ATOM   1171 C  CG  . MET A 1 160 ? 35.529 4.224   20.703 1.00 7.82  ? 180 MET A CG  1 
ATOM   1172 S  SD  . MET A 1 160 ? 34.574 2.894   21.541 1.00 9.07  ? 180 MET A SD  1 
ATOM   1173 C  CE  . MET A 1 160 ? 33.799 3.659   23.004 1.00 6.48  ? 180 MET A CE  1 
ATOM   1174 N  N   . PHE A 1 161 ? 38.405 3.698   17.324 1.00 4.24  ? 181 PHE A N   1 
ATOM   1175 C  CA  . PHE A 1 161 ? 38.895 3.000   16.162 1.00 6.43  ? 181 PHE A CA  1 
ATOM   1176 C  C   . PHE A 1 161 ? 39.706 1.874   16.800 1.00 7.14  ? 181 PHE A C   1 
ATOM   1177 O  O   . PHE A 1 161 ? 39.976 1.975   18.015 1.00 8.36  ? 181 PHE A O   1 
ATOM   1178 C  CB  . PHE A 1 161 ? 39.744 3.802   15.153 1.00 6.95  ? 181 PHE A CB  1 
ATOM   1179 C  CG  . PHE A 1 161 ? 41.078 4.263   15.733 1.00 5.81  ? 181 PHE A CG  1 
ATOM   1180 C  CD1 . PHE A 1 161 ? 42.210 3.509   15.540 1.00 3.04  ? 181 PHE A CD1 1 
ATOM   1181 C  CD2 . PHE A 1 161 ? 41.207 5.542   16.240 1.00 5.33  ? 181 PHE A CD2 1 
ATOM   1182 C  CE1 . PHE A 1 161 ? 43.423 3.972   16.020 1.00 2.00  ? 181 PHE A CE1 1 
ATOM   1183 C  CE2 . PHE A 1 161 ? 42.400 5.996   16.812 1.00 2.40  ? 181 PHE A CE2 1 
ATOM   1184 C  CZ  . PHE A 1 161 ? 43.561 5.221   16.638 1.00 2.00  ? 181 PHE A CZ  1 
ATOM   1185 N  N   . CYS A 1 162 ? 39.931 0.788   16.040 1.00 7.06  ? 182 CYS A N   1 
ATOM   1186 C  CA  . CYS A 1 162 ? 40.675 -0.383  16.481 1.00 7.22  ? 182 CYS A CA  1 
ATOM   1187 C  C   . CYS A 1 162 ? 41.933 -0.315  15.683 1.00 5.90  ? 182 CYS A C   1 
ATOM   1188 O  O   . CYS A 1 162 ? 41.839 0.267   14.606 1.00 6.87  ? 182 CYS A O   1 
ATOM   1189 C  CB  . CYS A 1 162 ? 39.996 -1.739  16.084 1.00 9.46  ? 182 CYS A CB  1 
ATOM   1190 S  SG  . CYS A 1 162 ? 38.413 -2.035  16.907 1.00 11.54 ? 182 CYS A SG  1 
ATOM   1191 N  N   . ALA A 1 163 ? 43.036 -0.783  16.269 1.00 5.57  ? 183 ALA A N   1 
ATOM   1192 C  CA  . ALA A 1 163 ? 44.276 -0.843  15.570 1.00 6.87  ? 183 ALA A CA  1 
ATOM   1193 C  C   . ALA A 1 163 ? 45.017 -2.088  16.063 1.00 6.76  ? 183 ALA A C   1 
ATOM   1194 O  O   . ALA A 1 163 ? 44.984 -2.416  17.280 1.00 6.11  ? 183 ALA A O   1 
ATOM   1195 C  CB  . ALA A 1 163 ? 45.105 0.328   16.051 1.00 7.87  ? 183 ALA A CB  1 
ATOM   1196 N  N   . GLY A 1 164 ? 45.795 -2.744  15.167 1.00 7.04  ? 184 GLY A N   1 
ATOM   1197 C  CA  . GLY A 1 164 ? 46.525 -3.830  15.771 1.00 7.26  ? 184 GLY A CA  1 
ATOM   1198 C  C   . GLY A 1 164 ? 46.510 -5.024  14.871 1.00 7.62  ? 184 GLY A C   1 
ATOM   1199 O  O   . GLY A 1 164 ? 46.448 -4.829  13.656 1.00 6.80  ? 184 GLY A O   1 
ATOM   1200 N  N   . TYR A 1 165 A 46.448 -6.214  15.478 1.00 9.04  ? 184 TYR A N   1 
ATOM   1201 C  CA  . TYR A 1 165 A 46.520 -7.482  14.726 1.00 9.90  ? 184 TYR A CA  1 
ATOM   1202 C  C   . TYR A 1 165 A 45.436 -8.490  15.136 1.00 11.10 ? 184 TYR A C   1 
ATOM   1203 O  O   . TYR A 1 165 A 45.260 -8.916  16.285 1.00 10.93 ? 184 TYR A O   1 
ATOM   1204 C  CB  . TYR A 1 165 A 47.955 -8.052  15.009 1.00 7.51  ? 184 TYR A CB  1 
ATOM   1205 C  CG  . TYR A 1 165 A 49.021 -7.123  14.581 1.00 6.64  ? 184 TYR A CG  1 
ATOM   1206 C  CD1 . TYR A 1 165 A 49.474 -6.045  15.344 1.00 7.73  ? 184 TYR A CD1 1 
ATOM   1207 C  CD2 . TYR A 1 165 A 49.662 -7.309  13.368 1.00 7.10  ? 184 TYR A CD2 1 
ATOM   1208 C  CE1 . TYR A 1 165 A 50.552 -5.215  15.010 1.00 8.12  ? 184 TYR A CE1 1 
ATOM   1209 C  CE2 . TYR A 1 165 A 50.666 -6.417  12.963 1.00 8.22  ? 184 TYR A CE2 1 
ATOM   1210 C  CZ  . TYR A 1 165 A 51.095 -5.375  13.754 1.00 8.41  ? 184 TYR A CZ  1 
ATOM   1211 O  OH  . TYR A 1 165 A 52.044 -4.501  13.306 1.00 9.56  ? 184 TYR A OH  1 
ATOM   1212 N  N   . LEU A 1 166 ? 44.702 -8.989  14.170 1.00 11.90 ? 185 LEU A N   1 
ATOM   1213 C  CA  . LEU A 1 166 ? 43.675 -9.967  14.475 1.00 12.29 ? 185 LEU A CA  1 
ATOM   1214 C  C   . LEU A 1 166 ? 44.220 -11.330 14.811 1.00 14.28 ? 185 LEU A C   1 
ATOM   1215 O  O   . LEU A 1 166 ? 43.504 -12.113 15.392 1.00 12.99 ? 185 LEU A O   1 
ATOM   1216 C  CB  . LEU A 1 166 ? 42.734 -10.100 13.299 1.00 11.52 ? 185 LEU A CB  1 
ATOM   1217 C  CG  . LEU A 1 166 ? 42.000 -8.819  13.000 1.00 11.90 ? 185 LEU A CG  1 
ATOM   1218 C  CD1 . LEU A 1 166 ? 41.107 -9.100  11.805 1.00 11.11 ? 185 LEU A CD1 1 
ATOM   1219 C  CD2 . LEU A 1 166 ? 41.157 -8.453  14.220 1.00 13.28 ? 185 LEU A CD2 1 
ATOM   1220 N  N   . GLU A 1 167 ? 45.467 -11.602 14.407 1.00 18.34 ? 186 GLU A N   1 
ATOM   1221 C  CA  . GLU A 1 167 ? 46.138 -12.865 14.637 1.00 21.75 ? 186 GLU A CA  1 
ATOM   1222 C  C   . GLU A 1 167 ? 46.393 -13.012 16.090 1.00 22.01 ? 186 GLU A C   1 
ATOM   1223 O  O   . GLU A 1 167 ? 46.683 -14.162 16.440 1.00 23.82 ? 186 GLU A O   1 
ATOM   1224 C  CB  . GLU A 1 167 ? 47.638 -12.906 14.184 1.00 25.08 ? 186 GLU A CB  1 
ATOM   1225 C  CG  . GLU A 1 167 ? 48.096 -12.396 12.792 1.00 27.23 ? 186 GLU A CG  1 
ATOM   1226 C  CD  . GLU A 1 167 ? 48.248 -10.931 12.556 1.00 28.43 ? 186 GLU A CD  1 
ATOM   1227 O  OE1 . GLU A 1 167 ? 47.299 -10.162 12.536 1.00 28.66 ? 186 GLU A OE1 1 
ATOM   1228 O  OE2 . GLU A 1 167 ? 49.437 -10.649 12.075 1.00 28.96 ? 186 GLU A OE2 1 
ATOM   1229 N  N   . GLY A 1 168 ? 46.527 -11.875 16.817 1.00 21.08 ? 187 GLY A N   1 
ATOM   1230 C  CA  . GLY A 1 168 ? 46.956 -11.799 18.219 1.00 19.56 ? 187 GLY A CA  1 
ATOM   1231 C  C   . GLY A 1 168 ? 48.465 -11.661 18.370 1.00 19.24 ? 187 GLY A C   1 
ATOM   1232 O  O   . GLY A 1 168 ? 49.161 -11.434 17.378 1.00 20.66 ? 187 GLY A O   1 
ATOM   1233 N  N   . GLY A 1 169 ? 48.962 -11.702 19.619 1.00 17.57 ? 188 GLY A N   1 
ATOM   1234 C  CA  . GLY A 1 169 ? 50.394 -11.607 19.951 1.00 17.32 ? 188 GLY A CA  1 
ATOM   1235 C  C   . GLY A 1 169 ? 51.107 -10.287 19.981 1.00 17.44 ? 188 GLY A C   1 
ATOM   1236 O  O   . GLY A 1 169 ? 52.290 -10.254 20.240 1.00 18.14 ? 188 GLY A O   1 
ATOM   1237 N  N   . LYS A 1 170 A 50.390 -9.213  19.619 1.00 16.89 ? 188 LYS A N   1 
ATOM   1238 C  CA  . LYS A 1 170 A 50.929 -7.874  19.558 1.00 14.46 ? 188 LYS A CA  1 
ATOM   1239 C  C   . LYS A 1 170 A 49.774 -6.933  19.901 1.00 11.36 ? 188 LYS A C   1 
ATOM   1240 O  O   . LYS A 1 170 A 48.842 -6.789  19.120 1.00 10.52 ? 188 LYS A O   1 
ATOM   1241 C  CB  . LYS A 1 170 A 51.379 -7.650  18.132 1.00 15.20 ? 188 LYS A CB  1 
ATOM   1242 C  CG  . LYS A 1 170 A 52.667 -8.313  17.699 1.00 17.07 ? 188 LYS A CG  1 
ATOM   1243 C  CD  . LYS A 1 170 A 52.883 -8.119  16.218 1.00 19.98 ? 188 LYS A CD  1 
ATOM   1244 C  CE  . LYS A 1 170 A 54.126 -7.313  15.934 1.00 23.43 ? 188 LYS A CE  1 
ATOM   1245 N  NZ  . LYS A 1 170 A 53.952 -6.046  15.172 1.00 26.08 ? 188 LYS A NZ  1 
ATOM   1246 N  N   . ASP A 1 171 ? 49.832 -6.214  21.010 1.00 8.76  ? 189 ASP A N   1 
ATOM   1247 C  CA  . ASP A 1 171 ? 48.827 -5.187  21.335 1.00 5.93  ? 189 ASP A CA  1 
ATOM   1248 C  C   . ASP A 1 171 ? 49.326 -4.372  22.558 1.00 4.50  ? 189 ASP A C   1 
ATOM   1249 O  O   . ASP A 1 171 ? 50.297 -4.678  23.228 1.00 4.21  ? 189 ASP A O   1 
ATOM   1250 C  CB  . ASP A 1 171 ? 47.644 -6.050  21.784 1.00 5.15  ? 189 ASP A CB  1 
ATOM   1251 C  CG  . ASP A 1 171 ? 46.244 -5.506  21.794 1.00 6.62  ? 189 ASP A CG  1 
ATOM   1252 O  OD1 . ASP A 1 171 ? 46.116 -4.232  21.488 1.00 6.88  ? 189 ASP A OD1 1 
ATOM   1253 O  OD2 . ASP A 1 171 ? 45.330 -6.171  22.272 1.00 7.83  ? 189 ASP A OD2 1 
ATOM   1254 N  N   . SER A 1 172 ? 48.579 -3.359  22.908 1.00 2.74  ? 190 SER A N   1 
ATOM   1255 C  CA  . SER A 1 172 ? 48.769 -2.571  24.071 1.00 3.06  ? 190 SER A CA  1 
ATOM   1256 C  C   . SER A 1 172 ? 48.172 -3.348  25.221 1.00 3.58  ? 190 SER A C   1 
ATOM   1257 O  O   . SER A 1 172 ? 47.460 -4.313  25.046 1.00 5.89  ? 190 SER A O   1 
ATOM   1258 C  CB  . SER A 1 172 ? 48.124 -1.213  23.846 1.00 3.10  ? 190 SER A CB  1 
ATOM   1259 O  OG  . SER A 1 172 ? 46.753 -1.331  23.543 1.00 4.98  ? 190 SER A OG  1 
ATOM   1260 N  N   . CYS A 1 173 ? 48.359 -3.017  26.437 1.00 4.02  ? 191 CYS A N   1 
ATOM   1261 C  CA  . CYS A 1 173 ? 47.782 -3.800  27.515 1.00 5.08  ? 191 CYS A CA  1 
ATOM   1262 C  C   . CYS A 1 173 ? 47.728 -2.911  28.777 1.00 5.88  ? 191 CYS A C   1 
ATOM   1263 O  O   . CYS A 1 173 ? 48.097 -1.723  28.802 1.00 4.45  ? 191 CYS A O   1 
ATOM   1264 C  CB  . CYS A 1 173 ? 48.649 -5.103  27.620 1.00 6.76  ? 191 CYS A CB  1 
ATOM   1265 S  SG  . CYS A 1 173 ? 48.071 -6.391  28.791 1.00 8.06  ? 191 CYS A SG  1 
ATOM   1266 N  N   . GLN A 1 174 ? 47.390 -3.459  29.953 1.00 6.50  ? 192 GLN A N   1 
ATOM   1267 C  CA  . GLN A 1 174 ? 47.340 -2.634  31.142 1.00 8.90  ? 192 GLN A CA  1 
ATOM   1268 C  C   . GLN A 1 174 ? 48.602 -1.843  31.478 1.00 8.74  ? 192 GLN A C   1 
ATOM   1269 O  O   . GLN A 1 174 ? 49.686 -2.447  31.533 1.00 9.49  ? 192 GLN A O   1 
ATOM   1270 C  CB  . GLN A 1 174 ? 46.875 -3.406  32.352 1.00 12.96 ? 192 GLN A CB  1 
ATOM   1271 C  CG  . GLN A 1 174 ? 46.001 -4.598  31.920 1.00 16.44 ? 192 GLN A CG  1 
ATOM   1272 C  CD  . GLN A 1 174 ? 44.524 -4.309  31.715 0.10 18.51 ? 192 GLN A CD  1 
ATOM   1273 O  OE1 . GLN A 1 174 ? 43.968 -3.337  32.240 0.46 18.97 ? 192 GLN A OE1 1 
ATOM   1274 N  NE2 . GLN A 1 174 ? 43.854 -5.211  31.005 0.65 19.39 ? 192 GLN A NE2 1 
ATOM   1275 N  N   . GLY A 1 175 ? 48.410 -0.518  31.679 1.00 6.33  ? 193 GLY A N   1 
ATOM   1276 C  CA  . GLY A 1 175 ? 49.501 0.381   32.017 1.00 4.91  ? 193 GLY A CA  1 
ATOM   1277 C  C   . GLY A 1 175 ? 49.908 1.194   30.797 1.00 4.11  ? 193 GLY A C   1 
ATOM   1278 O  O   . GLY A 1 175 ? 50.675 2.117   31.016 1.00 4.78  ? 193 GLY A O   1 
ATOM   1279 N  N   . ASP A 1 176 ? 49.383 0.859   29.600 1.00 2.11  ? 194 ASP A N   1 
ATOM   1280 C  CA  . ASP A 1 176 ? 49.701 1.528   28.385 1.00 3.35  ? 194 ASP A CA  1 
ATOM   1281 C  C   . ASP A 1 176 ? 48.583 2.553   28.230 1.00 5.21  ? 194 ASP A C   1 
ATOM   1282 O  O   . ASP A 1 176 ? 48.598 3.436   27.357 1.00 6.30  ? 194 ASP A O   1 
ATOM   1283 C  CB  . ASP A 1 176 ? 49.553 0.440   27.294 1.00 3.23  ? 194 ASP A CB  1 
ATOM   1284 C  CG  . ASP A 1 176 ? 50.838 -0.389  27.136 1.00 5.20  ? 194 ASP A CG  1 
ATOM   1285 O  OD1 . ASP A 1 176 ? 51.907 -0.026  27.638 1.00 4.46  ? 194 ASP A OD1 1 
ATOM   1286 O  OD2 . ASP A 1 176 ? 50.640 -1.598  26.611 1.00 5.02  ? 194 ASP A OD2 1 
ATOM   1287 N  N   . SER A 1 177 ? 47.544 2.344   28.996 1.00 4.80  ? 195 SER A N   1 
ATOM   1288 C  CA  . SER A 1 177 ? 46.329 3.133   28.835 1.00 6.98  ? 195 SER A CA  1 
ATOM   1289 C  C   . SER A 1 177 ? 46.615 4.609   29.131 1.00 6.70  ? 195 SER A C   1 
ATOM   1290 O  O   . SER A 1 177 ? 47.425 4.939   29.972 1.00 7.51  ? 195 SER A O   1 
ATOM   1291 C  CB  . SER A 1 177 ? 44.994 2.629   29.468 1.00 7.30  ? 195 SER A CB  1 
ATOM   1292 O  OG  . SER A 1 177 ? 44.538 1.421   28.539 1.00 8.08  ? 195 SER A OG  1 
ATOM   1293 N  N   . GLY A 1 178 ? 46.071 5.495   28.316 1.00 5.88  ? 196 GLY A N   1 
ATOM   1294 C  CA  . GLY A 1 178 ? 46.424 6.880   28.435 1.00 5.83  ? 196 GLY A CA  1 
ATOM   1295 C  C   . GLY A 1 178 ? 47.439 7.307   27.389 1.00 6.05  ? 196 GLY A C   1 
ATOM   1296 O  O   . GLY A 1 178 ? 47.362 8.489   27.021 1.00 7.99  ? 196 GLY A O   1 
ATOM   1297 N  N   . GLY A 1 179 ? 48.280 6.387   26.864 1.00 4.31  ? 197 GLY A N   1 
ATOM   1298 C  CA  . GLY A 1 179 ? 49.366 6.715   25.973 1.00 2.00  ? 197 GLY A CA  1 
ATOM   1299 C  C   . GLY A 1 179 ? 48.948 6.864   24.556 1.00 2.00  ? 197 GLY A C   1 
ATOM   1300 O  O   . GLY A 1 179 ? 47.798 6.658   24.193 1.00 2.46  ? 197 GLY A O   1 
ATOM   1301 N  N   . PRO A 1 180 ? 49.908 7.223   23.764 1.00 2.00  ? 198 PRO A N   1 
ATOM   1302 C  CA  . PRO A 1 180 ? 49.709 7.685   22.420 1.00 2.36  ? 198 PRO A CA  1 
ATOM   1303 C  C   . PRO A 1 180 ? 49.668 6.661   21.316 1.00 3.77  ? 198 PRO A C   1 
ATOM   1304 O  O   . PRO A 1 180 ? 50.310 5.617   21.535 1.00 5.84  ? 198 PRO A O   1 
ATOM   1305 C  CB  . PRO A 1 180 ? 50.910 8.616   22.218 1.00 2.63  ? 198 PRO A CB  1 
ATOM   1306 C  CG  . PRO A 1 180 ? 52.076 7.899   22.961 1.00 2.46  ? 198 PRO A CG  1 
ATOM   1307 C  CD  . PRO A 1 180 ? 51.393 7.380   24.212 1.00 2.00  ? 198 PRO A CD  1 
ATOM   1308 N  N   . VAL A 1 181 ? 48.955 6.975   20.245 1.00 2.00  ? 199 VAL A N   1 
ATOM   1309 C  CA  . VAL A 1 181 ? 48.983 6.236   19.005 1.00 2.47  ? 199 VAL A CA  1 
ATOM   1310 C  C   . VAL A 1 181 ? 49.431 7.276   18.013 1.00 2.61  ? 199 VAL A C   1 
ATOM   1311 O  O   . VAL A 1 181 ? 48.587 8.130   17.860 1.00 2.56  ? 199 VAL A O   1 
ATOM   1312 C  CB  . VAL A 1 181 ? 47.723 5.451   18.518 1.00 2.13  ? 199 VAL A CB  1 
ATOM   1313 C  CG1 . VAL A 1 181 ? 47.930 4.712   17.174 1.00 2.00  ? 199 VAL A CG1 1 
ATOM   1314 C  CG2 . VAL A 1 181 ? 47.244 4.625   19.713 1.00 2.00  ? 199 VAL A CG2 1 
ATOM   1315 N  N   . VAL A 1 182 ? 50.719 7.329   17.533 1.00 2.37  ? 200 VAL A N   1 
ATOM   1316 C  CA  . VAL A 1 182 ? 51.097 8.408   16.689 1.00 2.69  ? 200 VAL A CA  1 
ATOM   1317 C  C   . VAL A 1 182 ? 51.122 7.963   15.242 1.00 5.32  ? 200 VAL A C   1 
ATOM   1318 O  O   . VAL A 1 182 ? 51.766 6.907   15.053 1.00 4.98  ? 200 VAL A O   1 
ATOM   1319 C  CB  . VAL A 1 182 ? 52.419 8.982   17.232 1.00 2.00  ? 200 VAL A CB  1 
ATOM   1320 C  CG1 . VAL A 1 182 ? 52.926 9.961   16.235 1.00 2.00  ? 200 VAL A CG1 1 
ATOM   1321 C  CG2 . VAL A 1 182 ? 52.139 9.734   18.514 1.00 2.00  ? 200 VAL A CG2 1 
ATOM   1322 N  N   . CYS A 1 183 ? 50.479 8.730   14.285 1.00 7.81  ? 201 CYS A N   1 
ATOM   1323 C  CA  . CYS A 1 183 ? 50.451 8.434   12.858 1.00 10.06 ? 201 CYS A CA  1 
ATOM   1324 C  C   . CYS A 1 183 ? 50.879 9.590   11.965 1.00 12.71 ? 201 CYS A C   1 
ATOM   1325 O  O   . CYS A 1 183 ? 50.292 10.666  12.003 1.00 11.36 ? 201 CYS A O   1 
ATOM   1326 C  CB  . CYS A 1 183 ? 49.134 7.812   12.368 1.00 9.76  ? 201 CYS A CB  1 
ATOM   1327 S  SG  . CYS A 1 183 ? 48.330 6.919   13.722 1.00 11.38 ? 201 CYS A SG  1 
ATOM   1328 N  N   . SER A 1 184 ? 51.987 9.296   11.233 1.00 16.32 ? 202 SER A N   1 
ATOM   1329 C  CA  . SER A 1 184 ? 52.753 10.212  10.415 1.00 18.70 ? 202 SER A CA  1 
ATOM   1330 C  C   . SER A 1 184 ? 52.868 11.474  11.232 1.00 18.91 ? 202 SER A C   1 
ATOM   1331 O  O   . SER A 1 184 ? 52.239 12.480  10.903 1.00 19.96 ? 202 SER A O   1 
ATOM   1332 C  CB  . SER A 1 184 ? 52.205 10.500  9.031  1.00 20.90 ? 202 SER A CB  1 
ATOM   1333 O  OG  . SER A 1 184 ? 50.839 10.135  9.056  1.00 22.83 ? 202 SER A OG  1 
ATOM   1334 N  N   . GLY A 1 185 ? 53.483 11.325  12.387 1.00 17.98 ? 203 GLY A N   1 
ATOM   1335 C  CA  . GLY A 1 185 ? 53.671 12.533  13.114 1.00 16.87 ? 203 GLY A CA  1 
ATOM   1336 C  C   . GLY A 1 185 ? 52.519 13.174  13.772 1.00 15.61 ? 203 GLY A C   1 
ATOM   1337 O  O   . GLY A 1 185 ? 52.739 14.212  14.331 1.00 14.94 ? 203 GLY A O   1 
ATOM   1338 N  N   . LYS A 1 186 ? 51.326 12.576  13.814 1.00 14.82 ? 204 LYS A N   1 
ATOM   1339 C  CA  . LYS A 1 186 ? 50.381 13.251  14.647 1.00 13.07 ? 204 LYS A CA  1 
ATOM   1340 C  C   . LYS A 1 186 ? 49.728 12.352  15.671 1.00 10.59 ? 204 LYS A C   1 
ATOM   1341 O  O   . LYS A 1 186 ? 49.678 11.159  15.436 1.00 11.13 ? 204 LYS A O   1 
ATOM   1342 C  CB  . LYS A 1 186 ? 49.229 13.971  14.058 1.00 16.05 ? 204 LYS A CB  1 
ATOM   1343 C  CG  . LYS A 1 186 ? 48.862 13.507  12.709 1.00 18.65 ? 204 LYS A CG  1 
ATOM   1344 C  CD  . LYS A 1 186 ? 49.622 14.521  11.894 1.00 21.03 ? 204 LYS A CD  1 
ATOM   1345 C  CE  . LYS A 1 186 ? 50.196 15.708  12.641 1.00 22.34 ? 204 LYS A CE  1 
ATOM   1346 N  NZ  . LYS A 1 186 ? 50.920 16.380  11.520 1.00 23.21 ? 204 LYS A NZ  1 
ATOM   1347 N  N   . LEU A 1 187 ? 49.128 12.939  16.733 1.00 7.08  ? 209 LEU A N   1 
ATOM   1348 C  CA  . LEU A 1 187 ? 48.549 12.144  17.748 1.00 5.05  ? 209 LEU A CA  1 
ATOM   1349 C  C   . LEU A 1 187 ? 47.209 11.692  17.261 1.00 5.70  ? 209 LEU A C   1 
ATOM   1350 O  O   . LEU A 1 187 ? 46.359 12.546  17.258 1.00 6.54  ? 209 LEU A O   1 
ATOM   1351 C  CB  . LEU A 1 187 ? 48.221 13.000  18.931 1.00 5.43  ? 209 LEU A CB  1 
ATOM   1352 C  CG  . LEU A 1 187 ? 47.827 12.134  20.149 1.00 6.72  ? 209 LEU A CG  1 
ATOM   1353 C  CD1 . LEU A 1 187 ? 48.774 10.998  20.564 1.00 6.89  ? 209 LEU A CD1 1 
ATOM   1354 C  CD2 . LEU A 1 187 ? 47.551 13.009  21.351 1.00 7.46  ? 209 LEU A CD2 1 
ATOM   1355 N  N   . GLN A 1 188 ? 46.954 10.455  16.775 1.00 5.63  ? 210 GLN A N   1 
ATOM   1356 C  CA  . GLN A 1 188 ? 45.595 10.132  16.337 1.00 5.17  ? 210 GLN A CA  1 
ATOM   1357 C  C   . GLN A 1 188 ? 44.833 9.361   17.383 1.00 4.55  ? 210 GLN A C   1 
ATOM   1358 O  O   . GLN A 1 188 ? 43.640 9.214   17.259 1.00 4.27  ? 210 GLN A O   1 
ATOM   1359 C  CB  . GLN A 1 188 ? 45.607 9.260   15.053 1.00 5.73  ? 210 GLN A CB  1 
ATOM   1360 C  CG  . GLN A 1 188 ? 46.122 9.932   13.747 1.00 7.69  ? 210 GLN A CG  1 
ATOM   1361 C  CD  . GLN A 1 188 ? 45.185 10.959  13.163 1.00 9.82  ? 210 GLN A CD  1 
ATOM   1362 O  OE1 . GLN A 1 188 ? 45.213 11.418  12.019 1.00 12.44 ? 210 GLN A OE1 1 
ATOM   1363 N  NE2 . GLN A 1 188 ? 44.071 11.119  13.781 1.00 9.47  ? 210 GLN A NE2 1 
ATOM   1364 N  N   . GLY A 1 189 ? 45.445 8.658   18.349 1.00 3.69  ? 211 GLY A N   1 
ATOM   1365 C  CA  . GLY A 1 189 ? 44.678 7.853   19.257 1.00 3.20  ? 211 GLY A CA  1 
ATOM   1366 C  C   . GLY A 1 189 ? 45.243 7.857   20.646 1.00 3.73  ? 211 GLY A C   1 
ATOM   1367 O  O   . GLY A 1 189 ? 46.413 8.228   20.929 1.00 5.07  ? 211 GLY A O   1 
ATOM   1368 N  N   . ILE A 1 190 ? 44.369 7.435   21.562 1.00 2.00  ? 212 ILE A N   1 
ATOM   1369 C  CA  . ILE A 1 190 ? 44.746 7.345   22.929 1.00 2.00  ? 212 ILE A CA  1 
ATOM   1370 C  C   . ILE A 1 190 ? 44.487 5.905   23.337 1.00 2.00  ? 212 ILE A C   1 
ATOM   1371 O  O   . ILE A 1 190 ? 43.414 5.409   22.963 1.00 2.00  ? 212 ILE A O   1 
ATOM   1372 C  CB  . ILE A 1 190 ? 43.876 8.239   23.818 1.00 2.26  ? 212 ILE A CB  1 
ATOM   1373 C  CG1 . ILE A 1 190 ? 43.935 9.695   23.364 1.00 4.29  ? 212 ILE A CG1 1 
ATOM   1374 C  CG2 . ILE A 1 190 ? 44.094 8.112   25.307 1.00 2.00  ? 212 ILE A CG2 1 
ATOM   1375 C  CD1 . ILE A 1 190 ? 43.261 10.654  24.315 1.00 6.11  ? 212 ILE A CD1 1 
ATOM   1376 N  N   . VAL A 1 191 ? 45.459 5.220   23.959 1.00 2.00  ? 213 VAL A N   1 
ATOM   1377 C  CA  . VAL A 1 191 ? 45.269 3.817   24.356 1.00 2.81  ? 213 VAL A CA  1 
ATOM   1378 C  C   . VAL A 1 191 ? 44.053 3.758   25.247 1.00 2.93  ? 213 VAL A C   1 
ATOM   1379 O  O   . VAL A 1 191 ? 44.024 4.328   26.317 1.00 2.00  ? 213 VAL A O   1 
ATOM   1380 C  CB  . VAL A 1 191 ? 46.512 3.236   24.973 1.00 3.36  ? 213 VAL A CB  1 
ATOM   1381 C  CG1 . VAL A 1 191 ? 46.186 1.765   25.225 1.00 2.15  ? 213 VAL A CG1 1 
ATOM   1382 C  CG2 . VAL A 1 191 ? 47.589 3.398   23.884 1.00 5.74  ? 213 VAL A CG2 1 
ATOM   1383 N  N   . SER A 1 192 ? 42.928 3.102   24.877 1.00 3.65  ? 214 SER A N   1 
ATOM   1384 C  CA  . SER A 1 192 ? 41.762 3.158   25.762 1.00 2.49  ? 214 SER A CA  1 
ATOM   1385 C  C   . SER A 1 192 ? 41.374 1.810   26.364 1.00 6.16  ? 214 SER A C   1 
ATOM   1386 O  O   . SER A 1 192 ? 41.385 1.607   27.611 1.00 4.97  ? 214 SER A O   1 
ATOM   1387 C  CB  . SER A 1 192 ? 40.553 3.714   24.987 1.00 2.32  ? 214 SER A CB  1 
ATOM   1388 O  OG  . SER A 1 192 ? 39.396 3.977   25.808 1.00 2.10  ? 214 SER A OG  1 
ATOM   1389 N  N   . TRP A 1 193 ? 40.932 0.865   25.487 1.00 8.12  ? 215 TRP A N   1 
ATOM   1390 C  CA  . TRP A 1 193 ? 40.540 -0.456  26.046 1.00 9.18  ? 215 TRP A CA  1 
ATOM   1391 C  C   . TRP A 1 193 ? 40.691 -1.642  25.064 1.00 7.99  ? 215 TRP A C   1 
ATOM   1392 O  O   . TRP A 1 193 ? 40.930 -1.502  23.882 1.00 6.99  ? 215 TRP A O   1 
ATOM   1393 C  CB  . TRP A 1 193 ? 39.062 -0.326  26.559 1.00 10.02 ? 215 TRP A CB  1 
ATOM   1394 C  CG  . TRP A 1 193 ? 37.965 -0.086  25.553 1.00 9.61  ? 215 TRP A CG  1 
ATOM   1395 C  CD1 . TRP A 1 193 ? 37.739 1.086   24.949 1.00 8.72  ? 215 TRP A CD1 1 
ATOM   1396 C  CD2 . TRP A 1 193 ? 37.011 -1.024  24.946 1.00 10.16 ? 215 TRP A CD2 1 
ATOM   1397 N  NE1 . TRP A 1 193 ? 36.661 0.986   24.107 1.00 8.99  ? 215 TRP A NE1 1 
ATOM   1398 C  CE2 . TRP A 1 193 ? 36.235 -0.296  24.006 1.00 9.56  ? 215 TRP A CE2 1 
ATOM   1399 C  CE3 . TRP A 1 193 ? 36.750 -2.393  25.057 1.00 10.01 ? 215 TRP A CE3 1 
ATOM   1400 C  CZ2 . TRP A 1 193 ? 35.360 -0.902  23.118 1.00 10.02 ? 215 TRP A CZ2 1 
ATOM   1401 C  CZ3 . TRP A 1 193 ? 35.811 -2.991  24.252 1.00 9.97  ? 215 TRP A CZ3 1 
ATOM   1402 C  CH2 . TRP A 1 193 ? 35.168 -2.256  23.263 1.00 9.91  ? 215 TRP A CH2 1 
ATOM   1403 N  N   . GLY A 1 194 ? 40.388 -2.839  25.460 1.00 6.76  ? 216 GLY A N   1 
ATOM   1404 C  CA  . GLY A 1 194 ? 40.327 -3.935  24.498 1.00 6.89  ? 216 GLY A CA  1 
ATOM   1405 C  C   . GLY A 1 194 ? 39.866 -5.147  25.312 1.00 8.40  ? 216 GLY A C   1 
ATOM   1406 O  O   . GLY A 1 194 ? 39.778 -5.045  26.546 1.00 9.57  ? 216 GLY A O   1 
ATOM   1407 N  N   . SER A 1 195 ? 39.666 -6.332  24.701 1.00 10.07 ? 217 SER A N   1 
ATOM   1408 C  CA  . SER A 1 195 ? 39.339 -7.482  25.535 1.00 12.20 ? 217 SER A CA  1 
ATOM   1409 C  C   . SER A 1 195 ? 40.612 -8.297  25.782 1.00 12.09 ? 217 SER A C   1 
ATOM   1410 O  O   . SER A 1 195 ? 41.210 -8.753  24.800 1.00 12.67 ? 217 SER A O   1 
ATOM   1411 C  CB  . SER A 1 195 ? 38.278 -8.282  24.832 1.00 13.81 ? 217 SER A CB  1 
ATOM   1412 O  OG  . SER A 1 195 ? 37.922 -9.272  25.770 1.00 15.54 ? 217 SER A OG  1 
ATOM   1413 N  N   . GLY A 1 196 ? 41.051 -8.440  27.033 1.00 11.95 ? 219 GLY A N   1 
ATOM   1414 C  CA  . GLY A 1 196 ? 42.343 -9.124  27.303 1.00 12.94 ? 219 GLY A CA  1 
ATOM   1415 C  C   . GLY A 1 196 ? 43.449 -8.251  26.688 1.00 11.84 ? 219 GLY A C   1 
ATOM   1416 O  O   . GLY A 1 196 ? 43.154 -7.046  26.475 1.00 11.37 ? 219 GLY A O   1 
ATOM   1417 N  N   . CYS A 1 197 ? 44.588 -8.896  26.366 1.00 10.89 ? 220 CYS A N   1 
ATOM   1418 C  CA  . CYS A 1 197 ? 45.625 -8.234  25.631 1.00 9.04  ? 220 CYS A CA  1 
ATOM   1419 C  C   . CYS A 1 197 ? 46.167 -9.210  24.599 1.00 8.89  ? 220 CYS A C   1 
ATOM   1420 O  O   . CYS A 1 197 ? 46.411 -10.365 24.916 1.00 8.98  ? 220 CYS A O   1 
ATOM   1421 C  CB  . CYS A 1 197 ? 46.728 -7.765  26.545 1.00 9.33  ? 220 CYS A CB  1 
ATOM   1422 S  SG  . CYS A 1 197 ? 46.201 -6.785  27.956 1.00 10.16 ? 220 CYS A SG  1 
ATOM   1423 N  N   . ALA A 1 198 ? 46.340 -8.768  23.364 1.00 7.86  ? 221 ALA A N   1 
ATOM   1424 C  CA  . ALA A 1 198 ? 46.975 -9.574  22.414 1.00 10.04 ? 221 ALA A CA  1 
ATOM   1425 C  C   . ALA A 1 198 ? 46.253 -10.847 21.988 1.00 13.17 ? 221 ALA A C   1 
ATOM   1426 O  O   . ALA A 1 198 ? 46.901 -11.675 21.359 1.00 13.76 ? 221 ALA A O   1 
ATOM   1427 C  CB  . ALA A 1 198 ? 48.489 -9.582  22.706 1.00 10.18 ? 221 ALA A CB  1 
ATOM   1428 N  N   . GLN A 1 199 A 44.952 -11.041 22.348 1.00 14.14 ? 221 GLN A N   1 
ATOM   1429 C  CA  . GLN A 1 199 A 44.064 -12.144 21.936 1.00 15.79 ? 221 GLN A CA  1 
ATOM   1430 C  C   . GLN A 1 199 A 43.637 -12.060 20.486 1.00 16.66 ? 221 GLN A C   1 
ATOM   1431 O  O   . GLN A 1 199 A 43.418 -10.979 19.975 1.00 17.61 ? 221 GLN A O   1 
ATOM   1432 C  CB  . GLN A 1 199 A 42.666 -12.072 22.567 1.00 17.04 ? 221 GLN A CB  1 
ATOM   1433 C  CG  . GLN A 1 199 A 42.702 -12.089 24.081 1.00 18.65 ? 221 GLN A CG  1 
ATOM   1434 C  CD  . GLN A 1 199 A 43.841 -12.973 24.587 1.00 20.38 ? 221 GLN A CD  1 
ATOM   1435 O  OE1 . GLN A 1 199 A 43.667 -14.190 24.658 0.32 21.11 ? 221 GLN A OE1 1 
ATOM   1436 N  NE2 . GLN A 1 199 A 44.877 -12.380 25.185 0.25 21.11 ? 221 GLN A NE2 1 
ATOM   1437 N  N   . LYS A 1 200 ? 43.456 -13.170 19.748 1.00 17.43 ? 222 LYS A N   1 
ATOM   1438 C  CA  . LYS A 1 200 ? 43.155 -13.018 18.350 1.00 18.34 ? 222 LYS A CA  1 
ATOM   1439 C  C   . LYS A 1 200 ? 41.705 -12.628 18.299 1.00 17.13 ? 222 LYS A C   1 
ATOM   1440 O  O   . LYS A 1 200 ? 40.998 -12.948 19.258 1.00 16.12 ? 222 LYS A O   1 
ATOM   1441 C  CB  . LYS A 1 200 ? 43.384 -14.278 17.559 1.00 20.83 ? 222 LYS A CB  1 
ATOM   1442 C  CG  . LYS A 1 200 ? 42.409 -15.354 17.999 0.85 22.26 ? 222 LYS A CG  1 
ATOM   1443 C  CD  . LYS A 1 200 ? 41.803 -16.003 16.771 0.63 23.26 ? 222 LYS A CD  1 
ATOM   1444 C  CE  . LYS A 1 200 ? 41.839 -17.519 16.827 0.10 23.81 ? 222 LYS A CE  1 
ATOM   1445 N  NZ  . LYS A 1 200 ? 41.449 -18.125 15.544 0.11 24.08 ? 222 LYS A NZ  1 
ATOM   1446 N  N   . ASN A 1 201 ? 41.390 -11.881 17.233 1.00 16.57 ? 223 ASN A N   1 
ATOM   1447 C  CA  . ASN A 1 201 ? 40.089 -11.304 17.012 1.00 17.61 ? 223 ASN A CA  1 
ATOM   1448 C  C   . ASN A 1 201 ? 39.607 -10.241 17.970 1.00 17.65 ? 223 ASN A C   1 
ATOM   1449 O  O   . ASN A 1 201 ? 38.466 -9.791  17.897 1.00 19.03 ? 223 ASN A O   1 
ATOM   1450 C  CB  . ASN A 1 201 ? 38.976 -12.258 16.548 1.00 20.31 ? 223 ASN A CB  1 
ATOM   1451 C  CG  . ASN A 1 201 ? 39.474 -13.144 15.400 1.00 23.21 ? 223 ASN A CG  1 
ATOM   1452 O  OD1 . ASN A 1 201 ? 39.487 -14.391 15.547 1.00 24.57 ? 223 ASN A OD1 1 
ATOM   1453 N  ND2 . ASN A 1 201 ? 40.028 -12.512 14.352 1.00 23.59 ? 223 ASN A ND2 1 
ATOM   1454 N  N   . LYS A 1 202 ? 40.416 -9.801  18.917 1.00 17.36 ? 224 LYS A N   1 
ATOM   1455 C  CA  . LYS A 1 202 ? 40.078 -8.760  19.863 1.00 18.40 ? 224 LYS A CA  1 
ATOM   1456 C  C   . LYS A 1 202 ? 41.197 -7.704  19.877 1.00 15.88 ? 224 LYS A C   1 
ATOM   1457 O  O   . LYS A 1 202 ? 42.042 -7.681  20.794 1.00 14.64 ? 224 LYS A O   1 
ATOM   1458 C  CB  . LYS A 1 202 ? 39.991 -9.259  21.288 1.00 22.15 ? 224 LYS A CB  1 
ATOM   1459 C  CG  . LYS A 1 202 ? 38.940 -10.316 21.540 1.00 24.45 ? 224 LYS A CG  1 
ATOM   1460 C  CD  . LYS A 1 202 ? 37.534 -9.736  21.465 1.00 26.42 ? 224 LYS A CD  1 
ATOM   1461 C  CE  . LYS A 1 202 ? 36.750 -10.258 20.266 1.00 28.74 ? 224 LYS A CE  1 
ATOM   1462 N  NZ  . LYS A 1 202 ? 35.285 -10.242 20.483 1.00 30.42 ? 224 LYS A NZ  1 
ATOM   1463 N  N   . PRO A 1 203 ? 41.106 -6.801  18.878 1.00 13.48 ? 225 PRO A N   1 
ATOM   1464 C  CA  . PRO A 1 203 ? 42.106 -5.778  18.790 1.00 11.54 ? 225 PRO A CA  1 
ATOM   1465 C  C   . PRO A 1 203 ? 41.889 -4.737  19.885 1.00 9.42  ? 225 PRO A C   1 
ATOM   1466 O  O   . PRO A 1 203 ? 40.912 -4.739  20.640 1.00 9.00  ? 225 PRO A O   1 
ATOM   1467 C  CB  . PRO A 1 203 ? 42.058 -5.177  17.388 1.00 10.67 ? 225 PRO A CB  1 
ATOM   1468 C  CG  . PRO A 1 203 ? 40.801 -5.697  16.740 1.00 11.26 ? 225 PRO A CG  1 
ATOM   1469 C  CD  . PRO A 1 203 ? 40.263 -6.780  17.677 1.00 12.49 ? 225 PRO A CD  1 
ATOM   1470 N  N   . GLY A 1 204 ? 42.877 -3.853  19.944 1.00 6.98  ? 226 GLY A N   1 
ATOM   1471 C  CA  . GLY A 1 204 ? 42.856 -2.752  20.899 1.00 3.73  ? 226 GLY A CA  1 
ATOM   1472 C  C   . GLY A 1 204 ? 41.937 -1.730  20.351 1.00 2.00  ? 226 GLY A C   1 
ATOM   1473 O  O   . GLY A 1 204 ? 41.875 -1.535  19.179 1.00 2.00  ? 226 GLY A O   1 
ATOM   1474 N  N   . VAL A 1 205 ? 41.339 -0.996  21.254 1.00 2.89  ? 227 VAL A N   1 
ATOM   1475 C  CA  . VAL A 1 205 ? 40.392 0.102   20.970 1.00 3.94  ? 227 VAL A CA  1 
ATOM   1476 C  C   . VAL A 1 205 ? 40.966 1.379   21.520 1.00 4.46  ? 227 VAL A C   1 
ATOM   1477 O  O   . VAL A 1 205 ? 41.439 1.402   22.693 1.00 5.85  ? 227 VAL A O   1 
ATOM   1478 C  CB  . VAL A 1 205 ? 38.970 -0.199  21.475 1.00 4.77  ? 227 VAL A CB  1 
ATOM   1479 C  CG1 . VAL A 1 205 ? 37.989 0.799   20.891 1.00 4.17  ? 227 VAL A CG1 1 
ATOM   1480 C  CG2 . VAL A 1 205 ? 38.548 -1.530  20.861 1.00 5.89  ? 227 VAL A CG2 1 
ATOM   1481 N  N   . TYR A 1 206 ? 40.821 2.410   20.690 1.00 3.88  ? 228 TYR A N   1 
ATOM   1482 C  CA  . TYR A 1 206 ? 41.499 3.674   20.880 1.00 4.63  ? 228 TYR A CA  1 
ATOM   1483 C  C   . TYR A 1 206 ? 40.555 4.850   20.749 1.00 5.08  ? 228 TYR A C   1 
ATOM   1484 O  O   . TYR A 1 206 ? 39.693 4.831   19.890 1.00 4.94  ? 228 TYR A O   1 
ATOM   1485 C  CB  . TYR A 1 206 ? 42.657 3.752   19.806 1.00 5.09  ? 228 TYR A CB  1 
ATOM   1486 C  CG  . TYR A 1 206 ? 43.702 2.650   20.098 1.00 5.94  ? 228 TYR A CG  1 
ATOM   1487 C  CD1 . TYR A 1 206 ? 44.636 2.717   21.105 1.00 6.66  ? 228 TYR A CD1 1 
ATOM   1488 C  CD2 . TYR A 1 206 ? 43.687 1.489   19.329 1.00 5.93  ? 228 TYR A CD2 1 
ATOM   1489 C  CE1 . TYR A 1 206 ? 45.473 1.642   21.320 1.00 7.66  ? 228 TYR A CE1 1 
ATOM   1490 C  CE2 . TYR A 1 206 ? 44.450 0.330   19.612 1.00 6.22  ? 228 TYR A CE2 1 
ATOM   1491 C  CZ  . TYR A 1 206 ? 45.399 0.411   20.645 1.00 7.31  ? 228 TYR A CZ  1 
ATOM   1492 O  OH  . TYR A 1 206 ? 46.253 -0.602  20.856 1.00 9.25  ? 228 TYR A OH  1 
ATOM   1493 N  N   . THR A 1 207 ? 40.705 5.811   21.643 1.00 4.22  ? 229 THR A N   1 
ATOM   1494 C  CA  . THR A 1 207 ? 39.970 7.078   21.575 1.00 3.01  ? 229 THR A CA  1 
ATOM   1495 C  C   . THR A 1 207 ? 40.350 7.809   20.314 1.00 3.66  ? 229 THR A C   1 
ATOM   1496 O  O   . THR A 1 207 ? 41.562 8.136   20.046 1.00 2.92  ? 229 THR A O   1 
ATOM   1497 C  CB  . THR A 1 207 ? 40.221 7.992   22.815 1.00 2.61  ? 229 THR A CB  1 
ATOM   1498 O  OG1 . THR A 1 207 ? 39.841 7.322   24.022 1.00 2.00  ? 229 THR A OG1 1 
ATOM   1499 C  CG2 . THR A 1 207 ? 39.253 9.163   22.731 1.00 3.95  ? 229 THR A CG2 1 
ATOM   1500 N  N   . LYS A 1 208 ? 39.321 8.130   19.560 1.00 3.08  ? 230 LYS A N   1 
ATOM   1501 C  CA  . LYS A 1 208 ? 39.523 8.765   18.341 1.00 4.62  ? 230 LYS A CA  1 
ATOM   1502 C  C   . LYS A 1 208 ? 39.912 10.267  18.387 1.00 6.82  ? 230 LYS A C   1 
ATOM   1503 O  O   . LYS A 1 208 ? 39.053 11.089  18.228 1.00 8.06  ? 230 LYS A O   1 
ATOM   1504 C  CB  . LYS A 1 208 ? 38.549 8.307   17.290 1.00 5.20  ? 230 LYS A CB  1 
ATOM   1505 C  CG  . LYS A 1 208 ? 38.711 9.094   16.029 1.00 8.32  ? 230 LYS A CG  1 
ATOM   1506 C  CD  . LYS A 1 208 ? 37.449 8.979   15.232 1.00 12.19 ? 230 LYS A CD  1 
ATOM   1507 C  CE  . LYS A 1 208 ? 37.663 8.710   13.781 1.00 16.21 ? 230 LYS A CE  1 
ATOM   1508 N  NZ  . LYS A 1 208 ? 38.558 7.558   13.578 1.00 19.71 ? 230 LYS A NZ  1 
ATOM   1509 N  N   . VAL A 1 209 ? 41.144 10.637  18.681 1.00 7.76  ? 231 VAL A N   1 
ATOM   1510 C  CA  . VAL A 1 209 ? 41.671 11.991  18.831 1.00 7.58  ? 231 VAL A CA  1 
ATOM   1511 C  C   . VAL A 1 209 ? 41.170 13.122  17.872 1.00 7.03  ? 231 VAL A C   1 
ATOM   1512 O  O   . VAL A 1 209 ? 40.774 14.193  18.294 1.00 6.28  ? 231 VAL A O   1 
ATOM   1513 C  CB  . VAL A 1 209 ? 43.173 12.013  19.218 1.00 6.86  ? 231 VAL A CB  1 
ATOM   1514 C  CG1 . VAL A 1 209 ? 43.690 13.449  19.311 1.00 6.85  ? 231 VAL A CG1 1 
ATOM   1515 C  CG2 . VAL A 1 209 ? 43.462 11.255  20.482 1.00 5.30  ? 231 VAL A CG2 1 
ATOM   1516 N  N   . CYS A 1 210 ? 41.135 12.924  16.565 1.00 7.97  ? 232 CYS A N   1 
ATOM   1517 C  CA  . CYS A 1 210 ? 40.676 13.858  15.505 1.00 8.86  ? 232 CYS A CA  1 
ATOM   1518 C  C   . CYS A 1 210 ? 39.240 14.354  15.762 1.00 10.39 ? 232 CYS A C   1 
ATOM   1519 O  O   . CYS A 1 210 ? 38.776 15.326  15.182 1.00 12.21 ? 232 CYS A O   1 
ATOM   1520 C  CB  . CYS A 1 210 ? 40.728 13.287  14.032 1.00 7.35  ? 232 CYS A CB  1 
ATOM   1521 S  SG  . CYS A 1 210 ? 39.598 11.864  13.726 1.00 7.72  ? 232 CYS A SG  1 
ATOM   1522 N  N   . ASN A 1 211 ? 38.425 13.590  16.496 1.00 8.60  ? 233 ASN A N   1 
ATOM   1523 C  CA  . ASN A 1 211 ? 37.091 14.087  16.735 1.00 7.22  ? 233 ASN A CA  1 
ATOM   1524 C  C   . ASN A 1 211 ? 37.045 15.065  17.891 1.00 6.52  ? 233 ASN A C   1 
ATOM   1525 O  O   . ASN A 1 211 ? 35.937 15.447  18.335 1.00 5.95  ? 233 ASN A O   1 
ATOM   1526 C  CB  . ASN A 1 211 ? 36.176 13.047  17.314 1.00 7.64  ? 233 ASN A CB  1 
ATOM   1527 C  CG  . ASN A 1 211 ? 35.689 12.148  16.224 1.00 9.55  ? 233 ASN A CG  1 
ATOM   1528 O  OD1 . ASN A 1 211 ? 36.045 12.337  15.054 1.00 9.16  ? 233 ASN A OD1 1 
ATOM   1529 N  ND2 . ASN A 1 211 ? 34.839 11.206  16.666 1.00 11.47 ? 233 ASN A ND2 1 
ATOM   1530 N  N   . TYR A 1 212 ? 38.146 15.148  18.615 1.00 6.07  ? 234 TYR A N   1 
ATOM   1531 C  CA  . TYR A 1 212 ? 38.298 16.008  19.762 1.00 6.29  ? 234 TYR A CA  1 
ATOM   1532 C  C   . TYR A 1 212 ? 39.124 17.282  19.539 1.00 5.79  ? 234 TYR A C   1 
ATOM   1533 O  O   . TYR A 1 212 ? 39.275 18.035  20.497 1.00 4.20  ? 234 TYR A O   1 
ATOM   1534 C  CB  . TYR A 1 212 ? 38.802 15.299  21.023 1.00 6.00  ? 234 TYR A CB  1 
ATOM   1535 C  CG  . TYR A 1 212 ? 37.816 14.218  21.423 1.00 6.01  ? 234 TYR A CG  1 
ATOM   1536 C  CD1 . TYR A 1 212 ? 36.702 14.501  22.195 1.00 5.16  ? 234 TYR A CD1 1 
ATOM   1537 C  CD2 . TYR A 1 212 ? 37.999 12.940  20.952 1.00 7.42  ? 234 TYR A CD2 1 
ATOM   1538 C  CE1 . TYR A 1 212 ? 35.823 13.436  22.478 1.00 6.14  ? 234 TYR A CE1 1 
ATOM   1539 C  CE2 . TYR A 1 212 ? 37.144 11.876  21.173 1.00 6.66  ? 234 TYR A CE2 1 
ATOM   1540 C  CZ  . TYR A 1 212 ? 36.004 12.143  21.929 1.00 5.86  ? 234 TYR A CZ  1 
ATOM   1541 O  OH  . TYR A 1 212 ? 35.164 11.129  22.258 1.00 6.10  ? 234 TYR A OH  1 
ATOM   1542 N  N   . VAL A 1 213 ? 39.677 17.563  18.332 1.00 7.64  ? 235 VAL A N   1 
ATOM   1543 C  CA  . VAL A 1 213 ? 40.569 18.717  18.149 1.00 9.06  ? 235 VAL A CA  1 
ATOM   1544 C  C   . VAL A 1 213 ? 40.054 20.067  18.612 1.00 9.47  ? 235 VAL A C   1 
ATOM   1545 O  O   . VAL A 1 213 ? 40.617 20.821  19.401 1.00 9.43  ? 235 VAL A O   1 
ATOM   1546 C  CB  . VAL A 1 213 ? 41.418 18.678  16.884 1.00 9.51  ? 235 VAL A CB  1 
ATOM   1547 C  CG1 . VAL A 1 213 ? 42.432 19.816  17.025 1.00 9.55  ? 235 VAL A CG1 1 
ATOM   1548 C  CG2 . VAL A 1 213 ? 42.068 17.292  16.857 1.00 9.45  ? 235 VAL A CG2 1 
ATOM   1549 N  N   . SER A 1 214 ? 38.809 20.314  18.231 1.00 10.38 ? 236 SER A N   1 
ATOM   1550 C  CA  . SER A 1 214 ? 38.164 21.554  18.661 1.00 13.03 ? 236 SER A CA  1 
ATOM   1551 C  C   . SER A 1 214 ? 37.954 21.621  20.183 1.00 11.74 ? 236 SER A C   1 
ATOM   1552 O  O   . SER A 1 214 ? 38.222 22.676  20.734 1.00 13.06 ? 236 SER A O   1 
ATOM   1553 C  CB  . SER A 1 214 ? 36.799 21.757  17.999 1.00 16.69 ? 236 SER A CB  1 
ATOM   1554 O  OG  . SER A 1 214 ? 36.868 21.682  16.560 1.00 19.66 ? 236 SER A OG  1 
ATOM   1555 N  N   . TRP A 1 215 ? 37.516 20.537  20.860 1.00 9.67  ? 237 TRP A N   1 
ATOM   1556 C  CA  . TRP A 1 215 ? 37.325 20.540  22.292 1.00 8.07  ? 237 TRP A CA  1 
ATOM   1557 C  C   . TRP A 1 215 ? 38.610 20.833  23.035 1.00 9.75  ? 237 TRP A C   1 
ATOM   1558 O  O   . TRP A 1 215 ? 38.659 21.646  23.987 1.00 11.97 ? 237 TRP A O   1 
ATOM   1559 C  CB  . TRP A 1 215 ? 36.618 19.248  22.746 1.00 7.67  ? 237 TRP A CB  1 
ATOM   1560 C  CG  . TRP A 1 215 ? 36.527 19.117  24.251 1.00 8.72  ? 237 TRP A CG  1 
ATOM   1561 C  CD1 . TRP A 1 215 ? 35.553 19.655  25.034 1.00 8.67  ? 237 TRP A CD1 1 
ATOM   1562 C  CD2 . TRP A 1 215 ? 37.378 18.376  25.184 1.00 9.59  ? 237 TRP A CD2 1 
ATOM   1563 N  NE1 . TRP A 1 215 ? 35.788 19.379  26.374 1.00 8.80  ? 237 TRP A NE1 1 
ATOM   1564 C  CE2 . TRP A 1 215 ? 36.840 18.505  26.493 1.00 9.10  ? 237 TRP A CE2 1 
ATOM   1565 C  CE3 . TRP A 1 215 ? 38.513 17.586  25.048 1.00 9.62  ? 237 TRP A CE3 1 
ATOM   1566 C  CZ2 . TRP A 1 215 ? 37.452 17.997  27.622 1.00 8.43  ? 237 TRP A CZ2 1 
ATOM   1567 C  CZ3 . TRP A 1 215 ? 39.103 17.039  26.163 1.00 9.56  ? 237 TRP A CZ3 1 
ATOM   1568 C  CH2 . TRP A 1 215 ? 38.583 17.271  27.424 1.00 9.29  ? 237 TRP A CH2 1 
ATOM   1569 N  N   . ILE A 1 216 ? 39.686 20.213  22.605 1.00 8.80  ? 238 ILE A N   1 
ATOM   1570 C  CA  . ILE A 1 216 ? 40.967 20.377  23.255 1.00 8.59  ? 238 ILE A CA  1 
ATOM   1571 C  C   . ILE A 1 216 ? 41.400 21.854  23.181 1.00 9.57  ? 238 ILE A C   1 
ATOM   1572 O  O   . ILE A 1 216 ? 41.749 22.509  24.190 1.00 9.23  ? 238 ILE A O   1 
ATOM   1573 C  CB  . ILE A 1 216 ? 41.977 19.421  22.559 1.00 7.21  ? 238 ILE A CB  1 
ATOM   1574 C  CG1 . ILE A 1 216 ? 41.865 17.985  23.026 1.00 6.39  ? 238 ILE A CG1 1 
ATOM   1575 C  CG2 . ILE A 1 216 ? 43.404 19.912  22.805 1.00 6.82  ? 238 ILE A CG2 1 
ATOM   1576 C  CD1 . ILE A 1 216 ? 42.499 17.157  21.906 1.00 7.39  ? 238 ILE A CD1 1 
ATOM   1577 N  N   . LYS A 1 217 ? 41.293 22.357  21.945 1.00 10.51 ? 239 LYS A N   1 
ATOM   1578 C  CA  . LYS A 1 217 ? 41.746 23.719  21.752 1.00 12.41 ? 239 LYS A CA  1 
ATOM   1579 C  C   . LYS A 1 217 ? 40.967 24.740  22.541 1.00 10.97 ? 239 LYS A C   1 
ATOM   1580 O  O   . LYS A 1 217 ? 41.437 25.693  23.149 1.00 10.14 ? 239 LYS A O   1 
ATOM   1581 C  CB  . LYS A 1 217 ? 41.694 24.035  20.290 1.00 14.99 ? 239 LYS A CB  1 
ATOM   1582 C  CG  . LYS A 1 217 ? 42.738 23.176  19.596 1.00 18.64 ? 239 LYS A CG  1 
ATOM   1583 C  CD  . LYS A 1 217 ? 42.910 23.799  18.226 1.00 22.19 ? 239 LYS A CD  1 
ATOM   1584 C  CE  . LYS A 1 217 ? 43.527 22.870  17.200 1.00 25.35 ? 239 LYS A CE  1 
ATOM   1585 N  NZ  . LYS A 1 217 ? 44.706 23.421  16.476 1.00 27.36 ? 239 LYS A NZ  1 
ATOM   1586 N  N   . GLN A 1 218 ? 39.687 24.457  22.587 1.00 11.48 ? 240 GLN A N   1 
ATOM   1587 C  CA  . GLN A 1 218 ? 38.813 25.392  23.320 1.00 11.13 ? 240 GLN A CA  1 
ATOM   1588 C  C   . GLN A 1 218 ? 39.038 25.303  24.795 1.00 9.30  ? 240 GLN A C   1 
ATOM   1589 O  O   . GLN A 1 218 ? 39.129 26.282  25.510 1.00 9.51  ? 240 GLN A O   1 
ATOM   1590 C  CB  . GLN A 1 218 ? 37.334 25.187  23.012 1.00 14.04 ? 240 GLN A CB  1 
ATOM   1591 C  CG  . GLN A 1 218 ? 37.010 25.606  21.589 1.00 17.27 ? 240 GLN A CG  1 
ATOM   1592 C  CD  . GLN A 1 218 ? 35.572 25.235  21.232 1.00 22.10 ? 240 GLN A CD  1 
ATOM   1593 O  OE1 . GLN A 1 218 ? 35.067 25.727  20.199 1.00 25.77 ? 240 GLN A OE1 1 
ATOM   1594 N  NE2 . GLN A 1 218 ? 34.901 24.347  21.991 1.00 22.36 ? 240 GLN A NE2 1 
ATOM   1595 N  N   . THR A 1 219 ? 39.137 24.102  25.291 1.00 8.62  ? 241 THR A N   1 
ATOM   1596 C  CA  . THR A 1 219 ? 39.375 23.828  26.690 1.00 8.13  ? 241 THR A CA  1 
ATOM   1597 C  C   . THR A 1 219 ? 40.693 24.368  27.216 1.00 9.48  ? 241 THR A C   1 
ATOM   1598 O  O   . THR A 1 219 ? 40.831 25.051  28.241 1.00 10.66 ? 241 THR A O   1 
ATOM   1599 C  CB  . THR A 1 219 ? 39.255 22.301  26.898 1.00 7.96  ? 241 THR A CB  1 
ATOM   1600 O  OG1 . THR A 1 219 ? 37.952 21.925  26.511 1.00 8.06  ? 241 THR A OG1 1 
ATOM   1601 C  CG2 . THR A 1 219 ? 39.352 22.122  28.406 1.00 8.27  ? 241 THR A CG2 1 
ATOM   1602 N  N   . ILE A 1 220 ? 41.684 24.103  26.434 1.00 10.43 ? 242 ILE A N   1 
ATOM   1603 C  CA  . ILE A 1 220 ? 42.970 24.608  26.795 1.00 12.10 ? 242 ILE A CA  1 
ATOM   1604 C  C   . ILE A 1 220 ? 42.924 26.121  26.756 1.00 14.19 ? 242 ILE A C   1 
ATOM   1605 O  O   . ILE A 1 220 ? 43.454 26.693  27.718 1.00 17.03 ? 242 ILE A O   1 
ATOM   1606 C  CB  . ILE A 1 220 ? 44.048 24.012  25.909 1.00 11.14 ? 242 ILE A CB  1 
ATOM   1607 C  CG1 . ILE A 1 220 ? 44.369 22.637  26.425 1.00 11.26 ? 242 ILE A CG1 1 
ATOM   1608 C  CG2 . ILE A 1 220 ? 45.245 24.845  26.174 1.00 10.56 ? 242 ILE A CG2 1 
ATOM   1609 C  CD1 . ILE A 1 220 ? 45.308 22.136  25.324 1.00 12.47 ? 242 ILE A CD1 1 
ATOM   1610 N  N   . ALA A 1 221 ? 42.350 26.748  25.743 1.00 13.73 ? 243 ALA A N   1 
ATOM   1611 C  CA  . ALA A 1 221 ? 42.296 28.212  25.632 1.00 14.39 ? 243 ALA A CA  1 
ATOM   1612 C  C   . ALA A 1 221 ? 41.541 28.932  26.729 1.00 14.86 ? 243 ALA A C   1 
ATOM   1613 O  O   . ALA A 1 221 ? 41.736 30.087  27.093 1.00 15.15 ? 243 ALA A O   1 
ATOM   1614 C  CB  . ALA A 1 221 ? 41.654 28.629  24.333 1.00 14.63 ? 243 ALA A CB  1 
ATOM   1615 N  N   . SER A 1 222 ? 40.717 28.229  27.446 1.00 14.74 ? 244 SER A N   1 
ATOM   1616 C  CA  . SER A 1 222 ? 40.088 28.882  28.568 1.00 13.54 ? 244 SER A CA  1 
ATOM   1617 C  C   . SER A 1 222 ? 40.563 28.509  29.963 1.00 12.97 ? 244 SER A C   1 
ATOM   1618 O  O   . SER A 1 222 ? 39.964 28.928  30.954 1.00 13.18 ? 244 SER A O   1 
ATOM   1619 C  CB  . SER A 1 222 ? 38.600 28.817  28.363 1.00 14.01 ? 244 SER A CB  1 
ATOM   1620 O  OG  . SER A 1 222 ? 38.118 27.507  28.176 1.00 15.00 ? 244 SER A OG  1 
ATOM   1621 N  N   . ASN A 1 223 ? 41.586 27.660  30.080 1.00 12.09 ? 245 ASN A N   1 
ATOM   1622 C  CA  . ASN A 1 223 ? 42.142 27.189  31.333 1.00 12.93 ? 245 ASN A CA  1 
ATOM   1623 C  C   . ASN A 1 223 ? 43.611 27.633  31.466 1.00 15.30 ? 245 ASN A C   1 
ATOM   1624 O  O   . ASN A 1 223 ? 44.334 27.146  32.397 1.00 17.09 ? 245 ASN A O   1 
ATOM   1625 C  CB  . ASN A 1 223 ? 42.107 25.662  31.414 1.00 10.53 ? 245 ASN A CB  1 
ATOM   1626 C  CG  . ASN A 1 223 ? 40.686 25.338  31.858 1.00 9.89  ? 245 ASN A CG  1 
ATOM   1627 O  OD1 . ASN A 1 223 ? 40.332 25.488  33.016 1.00 9.74  ? 245 ASN A OD1 1 
ATOM   1628 N  ND2 . ASN A 1 223 ? 39.819 25.010  30.923 1.00 9.61  ? 245 ASN A ND2 1 
ATOM   1629 O  OXT . ASN A 1 223 ? 43.936 28.425  30.563 1.00 15.22 ? 245 ASN A OXT 1 
HETATM 1630 CA CA  . CA  B 2 .   ? 64.025 7.142   34.976 1.00 14.27 ? 701 CA  A CA  1 
HETATM 1631 S  S   . SO4 C 3 .   ? 27.096 -2.608  15.592 1.00 29.58 ? 702 SO4 A S   1 
HETATM 1632 S  S   . SO4 D 3 .   ? 62.813 -5.011  29.972 0.90 41.80 ? 703 SO4 A S   1 
HETATM 1633 C  CD  . GBS E 4 .   ? 44.773 0.302   29.019 0.72 9.70  ? 704 GBS A CD  1 
HETATM 1634 O  OD  . GBS E 4 .   ? 45.445 0.082   30.108 0.60 10.72 ? 704 GBS A OD  1 
HETATM 1635 C  C1  . GBS E 4 .   ? 44.401 -0.910  28.186 0.84 9.18  ? 704 GBS A C1  1 
HETATM 1636 C  C21 . GBS E 4 .   ? 44.011 -0.726  26.847 1.00 7.84  ? 704 GBS A C21 1 
HETATM 1637 C  C22 . GBS E 4 .   ? 44.464 -2.221  28.683 0.78 9.59  ? 704 GBS A C22 1 
HETATM 1638 C  C31 . GBS E 4 .   ? 43.731 -1.815  26.004 1.00 8.04  ? 704 GBS A C31 1 
HETATM 1639 C  C32 . GBS E 4 .   ? 44.159 -3.285  27.851 0.75 9.42  ? 704 GBS A C32 1 
HETATM 1640 C  C4  . GBS E 4 .   ? 43.692 -3.093  26.557 0.75 9.20  ? 704 GBS A C4  1 
HETATM 1641 N  NE  . GBS E 4 .   ? 43.338 -4.216  25.817 1.00 10.93 ? 704 GBS A NE  1 
HETATM 1642 C  CZ  . GBS E 4 .   ? 43.751 -4.461  24.579 1.00 13.36 ? 704 GBS A CZ  1 
HETATM 1643 N  NH1 . GBS E 4 .   ? 44.530 -3.637  23.890 0.80 14.93 ? 704 GBS A NH1 1 
HETATM 1644 N  NH2 . GBS E 4 .   ? 43.359 -5.575  23.983 1.00 13.07 ? 704 GBS A NH2 1 
HETATM 1645 O  O   . HOH F 5 .   ? 43.537 -0.378  32.302 1.00 34.41 ? 246 HOH A O   1 
HETATM 1646 O  O   . HOH F 5 .   ? 60.603 8.257   43.181 0.99 24.55 ? 247 HOH A O   1 
HETATM 1647 O  O   . HOH F 5 .   ? 35.674 18.773  19.102 0.77 10.01 ? 250 HOH A O   1 
HETATM 1648 O  O   . HOH F 5 .   ? 30.428 -2.057  17.589 0.90 29.72 ? 251 HOH A O   1 
HETATM 1649 O  O   . HOH F 5 .   ? 35.923 7.415   23.158 1.00 10.41 ? 252 HOH A O   1 
HETATM 1650 O  O   . HOH F 5 .   ? 37.463 4.939   23.985 0.79 11.71 ? 253 HOH A O   1 
HETATM 1651 O  O   . HOH F 5 .   ? 36.566 6.002   35.094 0.91 17.74 ? 254 HOH A O   1 
HETATM 1652 O  O   . HOH F 5 .   ? 50.917 4.560   6.468  0.82 24.68 ? 255 HOH A O   1 
HETATM 1653 O  O   . HOH F 5 .   ? 48.633 -6.316  9.594  1.00 20.41 ? 256 HOH A O   1 
HETATM 1654 O  O   . HOH F 5 .   ? 46.682 -5.868  11.085 0.99 7.27  ? 257 HOH A O   1 
HETATM 1655 O  O   . HOH F 5 .   ? 56.498 -3.408  16.127 0.97 3.30  ? 258 HOH A O   1 
HETATM 1656 O  O   . HOH F 5 .   ? 46.387 -6.105  18.255 1.00 9.70  ? 259 HOH A O   1 
HETATM 1657 O  O   . HOH F 5 .   ? 46.781 -2.613  19.551 1.00 9.00  ? 260 HOH A O   1 
HETATM 1658 O  O   . HOH F 5 .   ? 53.972 6.647   20.256 0.98 5.39  ? 261 HOH A O   1 
HETATM 1659 O  O   . HOH F 5 .   ? 43.262 -8.861  23.383 1.00 6.79  ? 262 HOH A O   1 
HETATM 1660 O  O   . HOH F 5 .   ? 51.327 4.490   27.205 1.00 2.00  ? 264 HOH A O   1 
HETATM 1661 O  O   . HOH F 5 .   ? 55.059 -1.912  27.616 1.00 6.81  ? 265 HOH A O   1 
HETATM 1662 O  O   . HOH F 5 .   ? 52.377 3.656   29.410 1.00 2.00  ? 266 HOH A O   1 
HETATM 1663 O  O   . HOH F 5 .   ? 55.863 -0.809  34.249 1.00 8.31  ? 267 HOH A O   1 
HETATM 1664 O  O   . HOH F 5 .   ? 56.261 6.338   36.580 1.00 6.18  ? 268 HOH A O   1 
HETATM 1665 O  O   . HOH F 5 .   ? 63.572 -5.279  21.949 0.99 22.88 ? 269 HOH A O   1 
HETATM 1666 O  O   . HOH F 5 .   ? 62.994 2.186   25.585 0.87 2.00  ? 270 HOH A O   1 
HETATM 1667 O  O   . HOH F 5 .   ? 60.960 8.068   24.826 1.00 4.40  ? 271 HOH A O   1 
HETATM 1668 O  O   . HOH F 5 .   ? 62.253 6.633   26.666 1.00 11.35 ? 272 HOH A O   1 
HETATM 1669 O  O   . HOH F 5 .   ? 67.888 3.018   29.415 1.00 34.63 ? 273 HOH A O   1 
HETATM 1670 O  O   . HOH F 5 .   ? 64.850 7.108   32.874 1.00 3.14  ? 274 HOH A O   1 
HETATM 1671 O  O   . HOH F 5 .   ? 62.853 7.566   36.900 1.00 2.00  ? 275 HOH A O   1 
HETATM 1672 O  O   . HOH F 5 .   ? 62.679 6.735   39.132 1.00 19.28 ? 276 HOH A O   1 
HETATM 1673 O  O   . HOH F 5 .   ? 42.179 10.576  15.302 0.92 2.00  ? 277 HOH A O   1 
HETATM 1674 O  O   . HOH F 5 .   ? 47.856 10.304  25.003 1.00 3.44  ? 278 HOH A O   1 
HETATM 1675 O  O   . HOH F 5 .   ? 61.815 11.179  26.376 1.00 15.90 ? 279 HOH A O   1 
HETATM 1676 O  O   . HOH F 5 .   ? 58.940 12.869  27.693 1.00 6.81  ? 280 HOH A O   1 
HETATM 1677 O  O   . HOH F 5 .   ? 64.583 16.957  30.313 1.00 11.03 ? 281 HOH A O   1 
HETATM 1678 O  O   . HOH F 5 .   ? 66.614 15.769  34.470 0.55 27.97 ? 283 HOH A O   1 
HETATM 1679 O  O   . HOH F 5 .   ? 65.729 18.543  34.115 0.71 32.32 ? 284 HOH A O   1 
HETATM 1680 O  O   . HOH F 5 .   ? 44.281 0.106   23.605 0.69 23.90 ? 285 HOH A O   1 
HETATM 1681 O  O   . HOH F 5 .   ? 37.306 -8.773  12.834 1.00 28.88 ? 287 HOH A O   1 
HETATM 1682 O  O   . HOH F 5 .   ? 25.092 -5.738  17.033 0.87 29.53 ? 288 HOH A O   1 
HETATM 1683 O  O   . HOH F 5 .   ? 31.588 0.218   24.439 0.74 32.90 ? 289 HOH A O   1 
HETATM 1684 O  O   . HOH F 5 .   ? 27.777 6.760   25.744 0.98 55.94 ? 290 HOH A O   1 
HETATM 1685 O  O   . HOH F 5 .   ? 30.481 -1.338  26.048 0.89 39.59 ? 291 HOH A O   1 
HETATM 1686 O  O   . HOH F 5 .   ? 41.282 0.183   29.356 0.94 28.45 ? 292 HOH A O   1 
HETATM 1687 O  O   . HOH F 5 .   ? 66.002 1.836   26.310 0.91 13.89 ? 293 HOH A O   1 
HETATM 1688 O  O   . HOH F 5 .   ? 59.178 6.900   36.985 0.99 13.27 ? 294 HOH A O   1 
HETATM 1689 O  O   . HOH F 5 .   ? 67.605 6.086   40.700 1.00 18.02 ? 295 HOH A O   1 
HETATM 1690 O  O   . HOH F 5 .   ? 48.175 10.953  10.710 1.00 18.15 ? 296 HOH A O   1 
HETATM 1691 O  O   . HOH F 5 .   ? 46.258 15.297  40.663 0.72 44.02 ? 297 HOH A O   1 
HETATM 1692 O  O   . HOH F 5 .   ? 58.358 10.073  30.118 1.00 11.03 ? 298 HOH A O   1 
HETATM 1693 O  O   . HOH F 5 .   ? 59.981 9.367   27.186 1.00 11.13 ? 299 HOH A O   1 
HETATM 1694 O  O   . HOH F 5 .   ? 69.171 17.025  31.292 1.00 25.90 ? 300 HOH A O   1 
HETATM 1695 O  O   . HOH F 5 .   ? 44.933 -8.502  19.726 1.00 18.09 ? 302 HOH A O   1 
HETATM 1696 O  O   . HOH F 5 .   ? 65.396 -1.227  36.841 0.94 29.81 ? 304 HOH A O   1 
HETATM 1697 O  O   . HOH F 5 .   ? 35.916 23.438  26.522 0.80 4.91  ? 306 HOH A O   1 
HETATM 1698 O  O   . HOH F 5 .   ? 60.603 3.124   17.043 1.00 16.81 ? 308 HOH A O   1 
HETATM 1699 O  O   . HOH F 5 .   ? 54.588 25.065  24.264 1.00 26.88 ? 309 HOH A O   1 
HETATM 1700 O  O   . HOH F 5 .   ? 36.953 2.192   7.893  1.00 31.06 ? 310 HOH A O   1 
HETATM 1701 O  O   . HOH F 5 .   ? 37.648 8.491   35.506 0.90 14.95 ? 311 HOH A O   1 
HETATM 1702 O  O   . HOH F 5 .   ? 60.909 20.947  34.483 0.84 14.64 ? 312 HOH A O   1 
HETATM 1703 O  O   . HOH F 5 .   ? 41.185 9.794   43.051 0.84 29.39 ? 313 HOH A O   1 
HETATM 1704 O  O   . HOH F 5 .   ? 33.994 16.272  22.335 1.00 26.49 ? 315 HOH A O   1 
HETATM 1705 O  O   . HOH F 5 .   ? 39.897 -9.985  9.072  1.00 39.26 ? 316 HOH A O   1 
HETATM 1706 O  O   . HOH F 5 .   ? 37.827 -8.350  9.853  0.87 38.55 ? 317 HOH A O   1 
HETATM 1707 O  O   . HOH F 5 .   ? 66.180 17.386  32.235 0.53 26.85 ? 318 HOH A O   1 
HETATM 1708 O  O   . HOH F 5 .   ? 52.737 -13.553 25.677 0.82 32.79 ? 319 HOH A O   1 
HETATM 1709 O  O   . HOH F 5 .   ? 69.510 15.352  32.992 1.00 9.56  ? 320 HOH A O   1 
HETATM 1710 O  O   . HOH F 5 .   ? 51.826 6.993   8.918  0.81 36.85 ? 321 HOH A O   1 
HETATM 1711 O  O   . HOH F 5 .   ? 32.041 14.188  17.302 0.52 29.83 ? 322 HOH A O   1 
HETATM 1712 O  O   . HOH F 5 .   ? 33.538 4.146   14.336 0.77 27.34 ? 323 HOH A O   1 
HETATM 1713 O  O   . HOH F 5 .   ? 65.696 9.507   31.578 1.00 16.29 ? 324 HOH A O   1 
HETATM 1714 O  O   . HOH F 5 .   ? 65.918 2.387   41.713 0.39 29.79 ? 325 HOH A O   1 
HETATM 1715 O  O   . HOH F 5 .   ? 29.820 12.484  32.169 0.84 14.66 ? 326 HOH A O   1 
HETATM 1716 O  O   . HOH F 5 .   ? 61.806 20.001  21.841 1.00 26.16 ? 327 HOH A O   1 
HETATM 1717 O  O   . HOH F 5 .   ? 54.877 16.053  15.514 0.82 29.03 ? 328 HOH A O   1 
HETATM 1718 O  O   . HOH F 5 .   ? 49.622 -9.173  9.894  1.00 29.78 ? 329 HOH A O   1 
HETATM 1719 O  O   . HOH F 5 .   ? 32.737 13.882  32.866 0.78 9.05  ? 330 HOH A O   1 
HETATM 1720 O  O   . HOH F 5 .   ? 58.870 20.570  20.993 0.84 18.08 ? 331 HOH A O   1 
HETATM 1721 O  O   . HOH F 5 .   ? 31.549 13.596  21.834 0.63 17.57 ? 332 HOH A O   1 
HETATM 1722 O  O   . HOH F 5 .   ? 46.364 6.880   3.496  0.80 28.36 ? 333 HOH A O   1 
HETATM 1723 O  O   . HOH F 5 .   ? 32.663 13.341  19.519 0.60 10.26 ? 334 HOH A O   1 
HETATM 1724 O  O   . HOH F 5 .   ? 37.928 -5.180  6.656  0.69 7.61  ? 335 HOH A O   1 
HETATM 1725 O  O   . HOH F 5 .   ? 41.428 8.607   12.946 1.00 27.39 ? 336 HOH A O   1 
HETATM 1726 O  O   . HOH F 5 .   ? 33.297 2.866   7.790  0.48 10.93 ? 337 HOH A O   1 
HETATM 1727 O  O   . HOH F 5 .   ? 32.753 4.389   9.975  0.48 30.30 ? 338 HOH A O   1 
HETATM 1728 O  O   . HOH F 5 .   ? 48.722 20.244  17.471 0.59 32.11 ? 339 HOH A O   1 
HETATM 1729 O  O   . HOH F 5 .   ? 46.683 1.766   32.233 1.00 28.19 ? 340 HOH A O   1 
HETATM 1730 O  O   . HOH F 5 .   ? 58.042 3.797   38.800 0.59 11.23 ? 341 HOH A O   1 
HETATM 1731 O  O   . HOH F 5 .   ? 32.994 -3.068  25.518 0.71 41.25 ? 342 HOH A O   1 
HETATM 1732 O  O   . HOH F 5 .   ? 50.602 19.782  19.725 0.74 27.55 ? 343 HOH A O   1 
HETATM 1733 O  O   . HOH F 5 .   ? 39.271 3.171   10.459 1.00 15.01 ? 344 HOH A O   1 
HETATM 1734 O  O   . HOH F 5 .   ? 43.151 2.885   34.464 0.69 32.72 ? 345 HOH A O   1 
HETATM 1735 O  O   . HOH F 5 .   ? 34.197 -0.612  26.711 0.60 20.08 ? 347 HOH A O   1 
HETATM 1736 O  O   . HOH F 5 .   ? 56.587 23.045  39.712 0.70 32.85 ? 348 HOH A O   1 
HETATM 1737 O  O   . HOH F 5 .   ? 36.477 0.491   6.387  0.24 33.36 ? 349 HOH A O   1 
HETATM 1738 O  O   . HOH F 5 .   ? 30.692 -5.263  10.709 0.40 5.91  ? 353 HOH A O   1 
HETATM 1739 O  O   . HOH F 5 .   ? 59.351 12.744  43.218 0.73 29.87 ? 355 HOH A O   1 
HETATM 1740 O  O   . HOH F 5 .   ? 60.652 23.193  18.623 0.37 14.90 ? 356 HOH A O   1 
HETATM 1741 O  O   . HOH F 5 .   ? 56.782 -5.743  24.203 0.96 15.87 ? 357 HOH A O   1 
HETATM 1742 O  O   . HOH F 5 .   ? 41.761 -5.479  28.503 0.81 17.89 ? 358 HOH A O   1 
HETATM 1743 O  O   . HOH F 5 .   ? 55.611 -12.514 25.687 0.85 28.63 ? 359 HOH A O   1 
HETATM 1744 O  O   . HOH F 5 .   ? 63.371 10.826  17.907 0.68 29.91 ? 360 HOH A O   1 
HETATM 1745 O  O   . HOH F 5 .   ? 41.041 -12.447 26.997 0.56 28.09 ? 361 HOH A O   1 
HETATM 1746 O  O   . HOH F 5 .   ? 58.053 18.823  18.818 0.61 17.74 ? 362 HOH A O   1 
HETATM 1747 O  O   . HOH F 5 .   ? 25.148 -2.272  12.009 0.76 28.10 ? 363 HOH A O   1 
HETATM 1748 O  O   . HOH F 5 .   ? 45.568 -14.643 27.287 0.53 31.31 ? 364 HOH A O   1 
HETATM 1749 O  O   . HOH F 5 .   ? 39.951 6.335   11.968 1.00 31.59 ? 365 HOH A O   1 
HETATM 1750 O  O   . HOH F 5 .   ? 44.417 -11.555 27.703 0.73 24.25 ? 366 HOH A O   1 
HETATM 1751 O  O   . HOH F 5 .   ? 46.766 29.142  30.736 0.62 30.45 ? 367 HOH A O   1 
HETATM 1752 O  O   . HOH F 5 .   ? 68.951 2.787   24.205 0.73 25.38 ? 801 HOH A O   1 
HETATM 1753 O  O   . HOH F 5 .   ? 46.698 27.034  29.194 0.77 28.04 ? 802 HOH A O   1 
HETATM 1754 O  O   . HOH F 5 .   ? 38.599 0.909   13.243 0.96 17.60 ? 803 HOH A O   1 
HETATM 1755 O  O   . HOH F 5 .   ? 69.714 3.121   26.960 0.72 33.25 ? 804 HOH A O   1 
HETATM 1756 O  O   . HOH F 5 .   ? 38.286 -0.524  5.042  0.73 31.50 ? 805 HOH A O   1 
HETATM 1757 O  O   . HOH F 5 .   ? 36.490 11.097  36.595 0.56 29.31 ? 806 HOH A O   1 
HETATM 1758 O  O   . HOH F 5 .   ? 37.232 4.680   12.749 0.24 30.91 ? 807 HOH A O   1 
HETATM 1759 O  O   . HOH F 5 .   ? 51.844 -15.419 27.360 0.65 38.22 ? 808 HOH A O   1 
HETATM 1760 O  O   . HOH F 5 .   ? 45.701 -8.490  11.247 1.00 27.01 ? 901 HOH A O   1 
HETATM 1761 O  O   . HOH F 5 .   ? 25.718 -0.529  14.378 0.61 49.35 ? 902 HOH A 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   ILE 1   16  16  ILE ILE A . n 
A 1 2   VAL 2   17  17  VAL VAL A . n 
A 1 3   GLY 3   18  18  GLY GLY A . n 
A 1 4   GLY 4   19  19  GLY GLY A . n 
A 1 5   TYR 5   20  20  TYR TYR A . n 
A 1 6   THR 6   21  21  THR THR A . n 
A 1 7   CYS 7   22  22  CYS CYS A . n 
A 1 8   GLY 8   23  23  GLY GLY A . n 
A 1 9   ALA 9   24  24  ALA ALA A . n 
A 1 10  ASN 10  25  25  ASN ASN A . n 
A 1 11  THR 11  26  26  THR THR A . n 
A 1 12  VAL 12  27  27  VAL VAL A . n 
A 1 13  PRO 13  28  28  PRO PRO A . n 
A 1 14  TYR 14  29  29  TYR TYR A . n 
A 1 15  GLN 15  30  30  GLN GLN A . n 
A 1 16  VAL 16  31  31  VAL VAL A . n 
A 1 17  SER 17  32  32  SER SER A . n 
A 1 18  LEU 18  33  33  LEU LEU A . n 
A 1 19  ASN 19  34  34  ASN ASN A . n 
A 1 20  SER 20  37  37  SER SER A . n 
A 1 21  GLY 21  38  38  GLY GLY A . n 
A 1 22  TYR 22  39  39  TYR TYR A . n 
A 1 23  HIS 23  40  40  HIS HIS A . n 
A 1 24  PHE 24  41  41  PHE PHE A . n 
A 1 25  CYS 25  42  42  CYS CYS A . n 
A 1 26  GLY 26  43  43  GLY GLY A . n 
A 1 27  GLY 27  44  44  GLY GLY A . n 
A 1 28  SER 28  45  45  SER SER A . n 
A 1 29  LEU 29  46  46  LEU LEU A . n 
A 1 30  ILE 30  47  47  ILE ILE A . n 
A 1 31  ASN 31  48  48  ASN ASN A . n 
A 1 32  SER 32  49  49  SER SER A . n 
A 1 33  GLN 33  50  50  GLN GLN A . n 
A 1 34  TRP 34  51  51  TRP TRP A . n 
A 1 35  VAL 35  52  52  VAL VAL A . n 
A 1 36  VAL 36  53  53  VAL VAL A . n 
A 1 37  SER 37  54  54  SER SER A . n 
A 1 38  ALA 38  55  55  ALA ALA A . n 
A 1 39  ALA 39  56  56  ALA ALA A . n 
A 1 40  HIS 40  57  57  HIS HIS A . n 
A 1 41  CYS 41  58  58  CYS CYS A . n 
A 1 42  TYR 42  59  59  TYR TYR A . n 
A 1 43  LYS 43  60  60  LYS LYS A . n 
A 1 44  SER 44  61  61  SER SER A . n 
A 1 45  GLY 45  62  62  GLY GLY A . n 
A 1 46  ILE 46  63  63  ILE ILE A . n 
A 1 47  GLN 47  64  64  GLN GLN A . n 
A 1 48  VAL 48  65  65  VAL VAL A . n 
A 1 49  ARG 49  65  65  ARG ARG A A n 
A 1 50  LEU 50  66  66  LEU LEU A . n 
A 1 51  GLY 51  69  69  GLY GLY A . n 
A 1 52  GLU 52  70  70  GLU GLU A . n 
A 1 53  ASP 53  71  71  ASP ASP A . n 
A 1 54  ASN 54  72  72  ASN ASN A . n 
A 1 55  ILE 55  73  73  ILE ILE A . n 
A 1 56  ASN 56  74  74  ASN ASN A . n 
A 1 57  VAL 57  75  75  VAL VAL A . n 
A 1 58  VAL 58  76  76  VAL VAL A . n 
A 1 59  GLU 59  77  77  GLU GLU A . n 
A 1 60  GLY 60  78  78  GLY GLY A . n 
A 1 61  ASN 61  79  79  ASN ASN A . n 
A 1 62  GLU 62  80  80  GLU GLU A . n 
A 1 63  GLN 63  81  81  GLN GLN A . n 
A 1 64  PHE 64  82  82  PHE PHE A . n 
A 1 65  ILE 65  83  83  ILE ILE A . n 
A 1 66  SER 66  84  84  SER SER A . n 
A 1 67  ALA 67  85  85  ALA ALA A . n 
A 1 68  SER 68  86  86  SER SER A . n 
A 1 69  LYS 69  87  87  LYS LYS A . n 
A 1 70  SER 70  88  88  SER SER A . n 
A 1 71  ILE 71  89  89  ILE ILE A . n 
A 1 72  VAL 72  90  90  VAL VAL A . n 
A 1 73  HIS 73  91  91  HIS HIS A . n 
A 1 74  PRO 74  92  92  PRO PRO A . n 
A 1 75  SER 75  93  93  SER SER A . n 
A 1 76  TYR 76  94  94  TYR TYR A . n 
A 1 77  ASN 77  95  95  ASN ASN A . n 
A 1 78  SER 78  96  96  SER SER A . n 
A 1 79  ASN 79  97  97  ASN ASN A . n 
A 1 80  THR 80  98  98  THR THR A . n 
A 1 81  LEU 81  99  99  LEU LEU A . n 
A 1 82  ASN 82  100 100 ASN ASN A . n 
A 1 83  ASN 83  101 101 ASN ASN A . n 
A 1 84  ASP 84  102 102 ASP ASP A . n 
A 1 85  ILE 85  103 103 ILE ILE A . n 
A 1 86  MET 86  104 104 MET MET A . n 
A 1 87  LEU 87  105 105 LEU LEU A . n 
A 1 88  ILE 88  106 106 ILE ILE A . n 
A 1 89  LYS 89  107 107 LYS LYS A . n 
A 1 90  LEU 90  108 108 LEU LEU A . n 
A 1 91  LYS 91  109 109 LYS LYS A . n 
A 1 92  SER 92  110 110 SER SER A . n 
A 1 93  ALA 93  111 111 ALA ALA A . n 
A 1 94  ALA 94  112 112 ALA ALA A . n 
A 1 95  SER 95  113 113 SER SER A . n 
A 1 96  LEU 96  114 114 LEU LEU A . n 
A 1 97  ASN 97  115 115 ASN ASN A . n 
A 1 98  SER 98  116 116 SER SER A . n 
A 1 99  ARG 99  117 117 ARG ARG A . n 
A 1 100 VAL 100 118 118 VAL VAL A . n 
A 1 101 ALA 101 119 119 ALA ALA A . n 
A 1 102 SER 102 120 120 SER SER A . n 
A 1 103 ILE 103 121 121 ILE ILE A . n 
A 1 104 SER 104 122 122 SER SER A . n 
A 1 105 LEU 105 123 123 LEU LEU A . n 
A 1 106 PRO 106 124 124 PRO PRO A . n 
A 1 107 THR 107 125 125 THR THR A . n 
A 1 108 SER 108 127 127 SER SER A . n 
A 1 109 CYS 109 128 128 CYS CYS A . n 
A 1 110 ALA 110 129 129 ALA ALA A . n 
A 1 111 SER 111 130 130 SER SER A . n 
A 1 112 ALA 112 132 132 ALA ALA A . n 
A 1 113 GLY 113 133 133 GLY GLY A . n 
A 1 114 THR 114 134 134 THR THR A . n 
A 1 115 GLN 115 135 135 GLN GLN A . n 
A 1 116 CYS 116 136 136 CYS CYS A . n 
A 1 117 LEU 117 137 137 LEU LEU A . n 
A 1 118 ILE 118 138 138 ILE ILE A . n 
A 1 119 SER 119 139 139 SER SER A . n 
A 1 120 GLY 120 140 140 GLY GLY A . n 
A 1 121 TRP 121 141 141 TRP TRP A . n 
A 1 122 GLY 122 142 142 GLY GLY A . n 
A 1 123 ASN 123 143 143 ASN ASN A . n 
A 1 124 THR 124 144 144 THR THR A . n 
A 1 125 LYS 125 145 145 LYS LYS A . n 
A 1 126 SER 126 146 146 SER SER A . n 
A 1 127 SER 127 147 147 SER SER A . n 
A 1 128 GLY 128 148 148 GLY GLY A . n 
A 1 129 THR 129 149 149 THR THR A . n 
A 1 130 SER 130 150 150 SER SER A . n 
A 1 131 TYR 131 151 151 TYR TYR A . n 
A 1 132 PRO 132 152 152 PRO PRO A . n 
A 1 133 ASP 133 153 153 ASP ASP A . n 
A 1 134 VAL 134 154 154 VAL VAL A . n 
A 1 135 LEU 135 155 155 LEU LEU A . n 
A 1 136 LYS 136 156 156 LYS LYS A . n 
A 1 137 CYS 137 157 157 CYS CYS A . n 
A 1 138 LEU 138 158 158 LEU LEU A . n 
A 1 139 LYS 139 159 159 LYS LYS A . n 
A 1 140 ALA 140 160 160 ALA ALA A . n 
A 1 141 PRO 141 161 161 PRO PRO A . n 
A 1 142 ILE 142 162 162 ILE ILE A . n 
A 1 143 LEU 143 163 163 LEU LEU A . n 
A 1 144 SER 144 164 164 SER SER A . n 
A 1 145 ASP 145 165 165 ASP ASP A . n 
A 1 146 SER 146 166 166 SER SER A . n 
A 1 147 SER 147 167 167 SER SER A . n 
A 1 148 CYS 148 168 168 CYS CYS A . n 
A 1 149 LYS 149 169 169 LYS LYS A . n 
A 1 150 SER 150 170 170 SER SER A . n 
A 1 151 ALA 151 171 171 ALA ALA A . n 
A 1 152 TYR 152 172 172 TYR TYR A . n 
A 1 153 PRO 153 173 173 PRO PRO A . n 
A 1 154 GLY 154 174 174 GLY GLY A . n 
A 1 155 GLN 155 175 175 GLN GLN A . n 
A 1 156 ILE 156 176 176 ILE ILE A . n 
A 1 157 THR 157 177 177 THR THR A . n 
A 1 158 SER 158 178 178 SER SER A . n 
A 1 159 ASN 159 179 179 ASN ASN A . n 
A 1 160 MET 160 180 180 MET MET A . n 
A 1 161 PHE 161 181 181 PHE PHE A . n 
A 1 162 CYS 162 182 182 CYS CYS A . n 
A 1 163 ALA 163 183 183 ALA ALA A . n 
A 1 164 GLY 164 184 184 GLY GLY A . n 
A 1 165 TYR 165 184 184 TYR TYR A A n 
A 1 166 LEU 166 185 185 LEU LEU A . n 
A 1 167 GLU 167 186 186 GLU GLU A . n 
A 1 168 GLY 168 187 187 GLY GLY A . n 
A 1 169 GLY 169 188 188 GLY GLY A . n 
A 1 170 LYS 170 188 188 LYS LYS A A n 
A 1 171 ASP 171 189 189 ASP ASP A . n 
A 1 172 SER 172 190 190 SER SER A . n 
A 1 173 CYS 173 191 191 CYS CYS A . n 
A 1 174 GLN 174 192 192 GLN GLN A . n 
A 1 175 GLY 175 193 193 GLY GLY A . n 
A 1 176 ASP 176 194 194 ASP ASP A . n 
A 1 177 SER 177 195 195 SER SER A . n 
A 1 178 GLY 178 196 196 GLY GLY A . n 
A 1 179 GLY 179 197 197 GLY GLY A . n 
A 1 180 PRO 180 198 198 PRO PRO A . n 
A 1 181 VAL 181 199 199 VAL VAL A . n 
A 1 182 VAL 182 200 200 VAL VAL A . n 
A 1 183 CYS 183 201 201 CYS CYS A . n 
A 1 184 SER 184 202 202 SER SER A . n 
A 1 185 GLY 185 203 203 GLY GLY A . n 
A 1 186 LYS 186 204 204 LYS LYS A . n 
A 1 187 LEU 187 209 209 LEU LEU A . n 
A 1 188 GLN 188 210 210 GLN GLN A . n 
A 1 189 GLY 189 211 211 GLY GLY A . n 
A 1 190 ILE 190 212 212 ILE ILE A . n 
A 1 191 VAL 191 213 213 VAL VAL A . n 
A 1 192 SER 192 214 214 SER SER A . n 
A 1 193 TRP 193 215 215 TRP TRP A . n 
A 1 194 GLY 194 216 216 GLY GLY A . n 
A 1 195 SER 195 217 217 SER SER A . n 
A 1 196 GLY 196 219 219 GLY GLY A . n 
A 1 197 CYS 197 220 220 CYS CYS A . n 
A 1 198 ALA 198 221 221 ALA ALA A . n 
A 1 199 GLN 199 221 221 GLN GLN A A n 
A 1 200 LYS 200 222 222 LYS LYS A . n 
A 1 201 ASN 201 223 223 ASN ASN A . n 
A 1 202 LYS 202 224 224 LYS LYS A . n 
A 1 203 PRO 203 225 225 PRO PRO A . n 
A 1 204 GLY 204 226 226 GLY GLY A . n 
A 1 205 VAL 205 227 227 VAL VAL A . n 
A 1 206 TYR 206 228 228 TYR TYR A . n 
A 1 207 THR 207 229 229 THR THR A . n 
A 1 208 LYS 208 230 230 LYS LYS A . n 
A 1 209 VAL 209 231 231 VAL VAL A . n 
A 1 210 CYS 210 232 232 CYS CYS A . n 
A 1 211 ASN 211 233 233 ASN ASN A . n 
A 1 212 TYR 212 234 234 TYR TYR A . n 
A 1 213 VAL 213 235 235 VAL VAL A . n 
A 1 214 SER 214 236 236 SER SER A . n 
A 1 215 TRP 215 237 237 TRP TRP A . n 
A 1 216 ILE 216 238 238 ILE ILE A . n 
A 1 217 LYS 217 239 239 LYS LYS A . n 
A 1 218 GLN 218 240 240 GLN GLN A . n 
A 1 219 THR 219 241 241 THR THR A . n 
A 1 220 ILE 220 242 242 ILE ILE A . n 
A 1 221 ALA 221 243 243 ALA ALA A . n 
A 1 222 SER 222 244 244 SER SER A . n 
A 1 223 ASN 223 245 245 ASN ASN A . 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 
B 2 CA  1   701 701 CA  CA  A . 
C 3 SO4 1   702 702 SO4 SO4 A . 
D 3 SO4 1   703 703 SO4 SO4 A . 
E 4 GBS 1   704 195 GBS GBS A . 
F 5 HOH 1   246 246 HOH HOH A . 
F 5 HOH 2   247 247 HOH HOH A . 
F 5 HOH 3   250 250 HOH HOH A . 
F 5 HOH 4   251 251 HOH HOH A . 
F 5 HOH 5   252 252 HOH HOH A . 
F 5 HOH 6   253 253 HOH HOH A . 
F 5 HOH 7   254 254 HOH HOH A . 
F 5 HOH 8   255 255 HOH HOH A . 
F 5 HOH 9   256 256 HOH HOH A . 
F 5 HOH 10  257 257 HOH HOH A . 
F 5 HOH 11  258 258 HOH HOH A . 
F 5 HOH 12  259 259 HOH HOH A . 
F 5 HOH 13  260 260 HOH HOH A . 
F 5 HOH 14  261 261 HOH HOH A . 
F 5 HOH 15  262 262 HOH HOH A . 
F 5 HOH 16  264 264 HOH HOH A . 
F 5 HOH 17  265 265 HOH HOH A . 
F 5 HOH 18  266 266 HOH HOH A . 
F 5 HOH 19  267 267 HOH HOH A . 
F 5 HOH 20  268 268 HOH HOH A . 
F 5 HOH 21  269 269 HOH HOH A . 
F 5 HOH 22  270 270 HOH HOH A . 
F 5 HOH 23  271 271 HOH HOH A . 
F 5 HOH 24  272 272 HOH HOH A . 
F 5 HOH 25  273 273 HOH HOH A . 
F 5 HOH 26  274 274 HOH HOH A . 
F 5 HOH 27  275 275 HOH HOH A . 
F 5 HOH 28  276 276 HOH HOH A . 
F 5 HOH 29  277 277 HOH HOH A . 
F 5 HOH 30  278 278 HOH HOH A . 
F 5 HOH 31  279 279 HOH HOH A . 
F 5 HOH 32  280 280 HOH HOH A . 
F 5 HOH 33  281 281 HOH HOH A . 
F 5 HOH 34  283 283 HOH HOH A . 
F 5 HOH 35  284 284 HOH HOH A . 
F 5 HOH 36  285 285 HOH HOH A . 
F 5 HOH 37  287 287 HOH HOH A . 
F 5 HOH 38  288 288 HOH HOH A . 
F 5 HOH 39  289 289 HOH HOH A . 
F 5 HOH 40  290 290 HOH HOH A . 
F 5 HOH 41  291 291 HOH HOH A . 
F 5 HOH 42  292 292 HOH HOH A . 
F 5 HOH 43  293 293 HOH HOH A . 
F 5 HOH 44  294 294 HOH HOH A . 
F 5 HOH 45  295 295 HOH HOH A . 
F 5 HOH 46  296 296 HOH HOH A . 
F 5 HOH 47  297 297 HOH HOH A . 
F 5 HOH 48  298 298 HOH HOH A . 
F 5 HOH 49  299 299 HOH HOH A . 
F 5 HOH 50  300 300 HOH HOH A . 
F 5 HOH 51  302 302 HOH HOH A . 
F 5 HOH 52  304 304 HOH HOH A . 
F 5 HOH 53  306 306 HOH HOH A . 
F 5 HOH 54  308 308 HOH HOH A . 
F 5 HOH 55  309 309 HOH HOH A . 
F 5 HOH 56  310 310 HOH HOH A . 
F 5 HOH 57  311 311 HOH HOH A . 
F 5 HOH 58  312 312 HOH HOH A . 
F 5 HOH 59  313 313 HOH HOH A . 
F 5 HOH 60  315 315 HOH HOH A . 
F 5 HOH 61  316 316 HOH HOH A . 
F 5 HOH 62  317 317 HOH HOH A . 
F 5 HOH 63  318 318 HOH HOH A . 
F 5 HOH 64  319 319 HOH HOH A . 
F 5 HOH 65  320 320 HOH HOH A . 
F 5 HOH 66  321 321 HOH HOH A . 
F 5 HOH 67  322 322 HOH HOH A . 
F 5 HOH 68  323 323 HOH HOH A . 
F 5 HOH 69  324 324 HOH HOH A . 
F 5 HOH 70  325 325 HOH HOH A . 
F 5 HOH 71  326 326 HOH HOH A . 
F 5 HOH 72  327 327 HOH HOH A . 
F 5 HOH 73  328 328 HOH HOH A . 
F 5 HOH 74  329 329 HOH HOH A . 
F 5 HOH 75  330 330 HOH HOH A . 
F 5 HOH 76  331 331 HOH HOH A . 
F 5 HOH 77  332 332 HOH HOH A . 
F 5 HOH 78  333 333 HOH HOH A . 
F 5 HOH 79  334 334 HOH HOH A . 
F 5 HOH 80  335 335 HOH HOH A . 
F 5 HOH 81  336 336 HOH HOH A . 
F 5 HOH 82  337 337 HOH HOH A . 
F 5 HOH 83  338 338 HOH HOH A . 
F 5 HOH 84  339 339 HOH HOH A . 
F 5 HOH 85  340 340 HOH HOH A . 
F 5 HOH 86  341 341 HOH HOH A . 
F 5 HOH 87  342 342 HOH HOH A . 
F 5 HOH 88  343 343 HOH HOH A . 
F 5 HOH 89  344 344 HOH HOH A . 
F 5 HOH 90  345 345 HOH HOH A . 
F 5 HOH 91  347 347 HOH HOH A . 
F 5 HOH 92  348 348 HOH HOH A . 
F 5 HOH 93  349 349 HOH HOH A . 
F 5 HOH 94  353 353 HOH HOH A . 
F 5 HOH 95  355 355 HOH HOH A . 
F 5 HOH 96  356 356 HOH HOH A . 
F 5 HOH 97  357 357 HOH HOH A . 
F 5 HOH 98  358 358 HOH HOH A . 
F 5 HOH 99  359 359 HOH HOH A . 
F 5 HOH 100 360 360 HOH HOH A . 
F 5 HOH 101 361 361 HOH HOH A . 
F 5 HOH 102 362 362 HOH HOH A . 
F 5 HOH 103 363 363 HOH HOH A . 
F 5 HOH 104 364 364 HOH HOH A . 
F 5 HOH 105 365 365 HOH HOH A . 
F 5 HOH 106 366 366 HOH HOH A . 
F 5 HOH 107 367 367 HOH HOH A . 
F 5 HOH 108 801 801 HOH HOH A . 
F 5 HOH 109 802 802 HOH HOH A . 
F 5 HOH 110 803 803 HOH HOH A . 
F 5 HOH 111 804 804 HOH HOH A . 
F 5 HOH 112 805 805 HOH HOH A . 
F 5 HOH 113 806 806 HOH HOH A . 
F 5 HOH 114 807 807 HOH HOH A . 
F 5 HOH 115 808 808 HOH HOH A . 
F 5 HOH 116 901 901 HOH HOH A . 
F 5 HOH 117 902 902 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
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  OE1 ? A GLU 52 ? A GLU 70  ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 O   ? A ASN 54 ? A ASN 72  ? 1_555 88.7  ? 
2  OE1 ? A GLU 52 ? A GLU 70  ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 O   ? A VAL 57 ? A VAL 75  ? 1_555 172.2 ? 
3  O   ? A ASN 54 ? A ASN 72  ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 O   ? A VAL 57 ? A VAL 75  ? 1_555 91.3  ? 
4  OE1 ? A GLU 52 ? A GLU 70  ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 O   ? F HOH .  ? A HOH 275 ? 1_555 85.6  ? 
5  O   ? A ASN 54 ? A ASN 72  ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 O   ? F HOH .  ? A HOH 275 ? 1_555 105.4 ? 
6  O   ? A VAL 57 ? A VAL 75  ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 O   ? F HOH .  ? A HOH 275 ? 1_555 86.9  ? 
7  OE1 ? A GLU 52 ? A GLU 70  ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 OE2 ? A GLU 62 ? A GLU 80  ? 1_555 101.5 ? 
8  O   ? A ASN 54 ? A ASN 72  ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 OE2 ? A GLU 62 ? A GLU 80  ? 1_555 158.6 ? 
9  O   ? A VAL 57 ? A VAL 75  ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 OE2 ? A GLU 62 ? A GLU 80  ? 1_555 81.1  ? 
10 O   ? F HOH .  ? A HOH 275 ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 OE2 ? A GLU 62 ? A GLU 80  ? 1_555 94.1  ? 
11 OE1 ? A GLU 52 ? A GLU 70  ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 O   ? F HOH .  ? A HOH 274 ? 1_555 81.8  ? 
12 O   ? A ASN 54 ? A ASN 72  ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 O   ? F HOH .  ? A HOH 274 ? 1_555 80.3  ? 
13 O   ? A VAL 57 ? A VAL 75  ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 O   ? F HOH .  ? A HOH 274 ? 1_555 105.9 ? 
14 O   ? F HOH .  ? A HOH 275 ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 O   ? F HOH .  ? A HOH 274 ? 1_555 166.1 ? 
15 OE2 ? A GLU 62 ? A GLU 80  ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 O   ? F HOH .  ? A HOH 274 ? 1_555 82.6  ? 
# 
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 1994-01-31 
2 'Structure model' 1 1 2008-03-24 
3 'Structure model' 1 2 2011-07-13 
# 
_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' 
# 
_software.name             TNT 
_software.classification   refinement 
_software.version          . 
_software.citation_id      ? 
_software.pdbx_ordinal     1 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CD A GLU 70  ? ? OE1 A GLU 70  ? ? 1.328 1.252 0.076 0.011 N 
2 1 CB A SER 195 ? ? OG  A SER 195 ? ? 1.591 1.418 0.173 0.013 N 
3 1 CD A PRO 198 ? ? N   A PRO 198 ? ? 1.559 1.474 0.085 0.014 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CA  A CYS 42  ? ? CB A CYS 42  ? ? SG  A CYS 42  ? ? 121.32 114.20 7.12   1.10 N 
2  1 CG1 A VAL 53  ? ? CB A VAL 53  ? ? CG2 A VAL 53  ? ? 100.78 110.90 -10.12 1.60 N 
3  1 CA  A CYS 58  ? ? CB A CYS 58  ? ? SG  A CYS 58  ? ? 102.08 114.00 -11.92 1.80 N 
4  1 NE  A ARG 65  A ? CZ A ARG 65  A ? NH2 A ARG 65  A ? 123.82 120.30 3.52   0.50 N 
5  1 CB  A ASP 71  ? ? CG A ASP 71  ? ? OD1 A ASP 71  ? ? 112.22 118.30 -6.08  0.90 N 
6  1 N   A ASN 79  ? ? CA A ASN 79  ? ? CB  A ASN 79  ? ? 122.15 110.60 11.55  1.80 N 
7  1 CB  A SER 84  ? ? CA A SER 84  ? ? C   A SER 84  ? ? 97.04  110.10 -13.06 1.90 N 
8  1 OG1 A THR 98  ? ? CB A THR 98  ? ? CG2 A THR 98  ? ? 92.66  110.00 -17.34 2.30 N 
9  1 CA  A ILE 106 ? ? CB A ILE 106 ? ? CG1 A ILE 106 ? ? 99.13  111.00 -11.87 1.90 N 
10 1 N   A ALA 112 ? ? CA A ALA 112 ? ? CB  A ALA 112 ? ? 100.86 110.10 -9.24  1.40 N 
11 1 NE  A ARG 117 ? ? CZ A ARG 117 ? ? NH1 A ARG 117 ? ? 116.79 120.30 -3.51  0.50 N 
12 1 CA  A THR 125 ? ? CB A THR 125 ? ? CG2 A THR 125 ? ? 103.18 112.40 -9.22  1.40 N 
13 1 CG1 A VAL 154 ? ? CB A VAL 154 ? ? CG2 A VAL 154 ? ? 121.56 110.90 10.66  1.60 N 
14 1 CB  A ASP 165 ? ? CG A ASP 165 ? ? OD2 A ASP 165 ? ? 112.55 118.30 -5.75  0.90 N 
15 1 CA  A LYS 169 ? ? CB A LYS 169 ? ? CG  A LYS 169 ? ? 98.54  113.40 -14.86 2.20 N 
16 1 CB  A GLU 186 ? ? CA A GLU 186 ? ? C   A GLU 186 ? ? 96.66  110.40 -13.74 2.00 N 
17 1 N   A SER 195 ? ? CA A SER 195 ? ? CB  A SER 195 ? ? 119.56 110.50 9.06   1.50 N 
18 1 CB  A ALA 221 ? ? CA A ALA 221 ? ? C   A ALA 221 ? ? 120.91 110.10 10.81  1.50 N 
19 1 CB  A GLN 221 A ? CA A GLN 221 A ? C   A GLN 221 A ? 97.71  110.40 -12.69 2.00 N 
20 1 CB  A ASN 233 ? ? CA A ASN 233 ? ? C   A ASN 233 ? ? 97.72  110.40 -12.68 2.00 N 
# 
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 ASP A 71 ? ? -124.02 -85.85 
2 1 ASN A 79 ? ? 88.18   -13.58 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             ASN 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              233 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   10.63 
# 
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 N 1 A SO4 702 ? O1 ? C SO4 1 O1 
2 1 N 1 A SO4 702 ? O2 ? C SO4 1 O2 
3 1 N 1 A SO4 702 ? O3 ? C SO4 1 O3 
4 1 N 1 A SO4 702 ? O4 ? C SO4 1 O4 
5 1 N 1 A SO4 703 ? O1 ? D SO4 1 O1 
6 1 N 1 A SO4 703 ? O2 ? D SO4 1 O2 
7 1 N 1 A SO4 703 ? O3 ? D SO4 1 O3 
8 1 N 1 A SO4 703 ? O4 ? D SO4 1 O4 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CALCIUM ION'             CA  
3 'SULFATE ION'             SO4 
4 '4-GUANIDINOBENZOIC ACID' GBS 
5 water                     HOH 
#