data_200L
# 
_entry.id   200L 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   200L         
WWPDB D_1000177550 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        200L 
_pdbx_database_status.recvd_initial_deposition_date   1995-11-06 
_pdbx_database_status.deposit_site                    ? 
_pdbx_database_status.process_site                    BNL 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Baldwin, E.'         1 
'Xu, J.'              2 
'Hajiseyedjavadi, O.' 3 
'Matthews, B.W.'      4 
# 
loop_
_citation.id 
_citation.title 
_citation.journal_abbrev 
_citation.journal_volume 
_citation.page_first 
_citation.page_last 
_citation.year 
_citation.journal_id_ASTM 
_citation.country 
_citation.journal_id_ISSN 
_citation.journal_id_CSD 
_citation.book_publisher 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_DOI 
primary 
;Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme.
;
J.Mol.Biol.        259 542  559 1996 JMOBAK UK 0022-2836 0070 ? 8676387 10.1006/jmbi.1996.0338 
1       'The Role of Backbone Flexibility in the Accommodation of Variants that Repack the Core of T4 Lysozyme'            Science 
262 1715 ?   1993 SCIEAS US 0036-8075 0038 ? ?       ?                      
2       'Control of Enzyme Activity by an Engineered Disulfide Bond'                                                       Science 
243 792  ?   1989 SCIEAS US 0036-8075 0038 ? ?       ?                      
3       'Expression and Nitrogen-15 Labeling of Proteins for Proton and Nitrogen-15 Nuclear Magnetic Resonance'            
'Methods Enzymol.' 177 44   ?   1989 MENZAU US 0076-6879 0878 ? ?       ?                      
4       'Structure of Bacteriophage T4 Lysozyme Refined at 1.7 Angstroms Resolution'                                       
J.Mol.Biol.        193 189  ?   1987 JMOBAK UK 0022-2836 0070 ? ?       ?                      
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Baldwin, E.'         1  
primary 'Xu, J.'              2  
primary 'Hajiseyedjavadi, O.' 3  
primary 'Baase, W.A.'         4  
primary 'Matthews, B.W.'      5  
1       'Baldwin, E.P.'       6  
1       'Hajiseyedjavadi, O.' 7  
1       'Baase, W.A.'         8  
1       'Matthews, B.W.'      9  
2       'Matsumura, M.'       10 
2       'Matthews, B.W.'      11 
3       'Muchmore, D.C.'      12 
3       'Mcintosh, L.P.'      13 
3       'Russell, C.B.'       14 
3       'Anderson, D.E.'      15 
3       'Dahlquist, F.W.'     16 
4       'Weaver, L.H.'        17 
4       'Matthews, B.W.'      18 
# 
_cell.entry_id           200L 
_cell.length_a           60.980 
_cell.length_b           60.980 
_cell.length_c           95.970 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              6 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         200L 
_symmetry.space_group_name_H-M             'P 32 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
# 
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 LYSOZYME             18586.283 1   3.2.1.17 'C54T, C97A, L121A' ? ? 
2 non-polymer syn 'CHLORIDE ION'       35.453    2   ?        ?                   ? ? 
3 non-polymer syn BETA-MERCAPTOETHANOL 78.133    2   ?        ?                   ? ? 
4 water       nat water                18.015    106 ?        ?                   ? ? 
# 
_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       
;MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMAQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA
YKNL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMAQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA
YKNL
;
_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   MET n 
1 2   ASN n 
1 3   ILE n 
1 4   PHE n 
1 5   GLU n 
1 6   MET n 
1 7   LEU n 
1 8   ARG n 
1 9   ILE n 
1 10  ASP n 
1 11  GLU n 
1 12  GLY n 
1 13  LEU n 
1 14  ARG n 
1 15  LEU n 
1 16  LYS n 
1 17  ILE n 
1 18  TYR n 
1 19  LYS n 
1 20  ASP n 
1 21  THR n 
1 22  GLU n 
1 23  GLY n 
1 24  TYR n 
1 25  TYR n 
1 26  THR n 
1 27  ILE n 
1 28  GLY n 
1 29  ILE n 
1 30  GLY n 
1 31  HIS n 
1 32  LEU n 
1 33  LEU n 
1 34  THR n 
1 35  LYS n 
1 36  SER n 
1 37  PRO n 
1 38  SER n 
1 39  LEU n 
1 40  ASN n 
1 41  ALA n 
1 42  ALA n 
1 43  LYS n 
1 44  SER n 
1 45  GLU n 
1 46  LEU n 
1 47  ASP n 
1 48  LYS n 
1 49  ALA n 
1 50  ILE n 
1 51  GLY n 
1 52  ARG n 
1 53  ASN n 
1 54  THR n 
1 55  ASN n 
1 56  GLY n 
1 57  VAL n 
1 58  ILE n 
1 59  THR n 
1 60  LYS n 
1 61  ASP n 
1 62  GLU n 
1 63  ALA n 
1 64  GLU n 
1 65  LYS n 
1 66  LEU n 
1 67  PHE n 
1 68  ASN n 
1 69  GLN n 
1 70  ASP n 
1 71  VAL n 
1 72  ASP n 
1 73  ALA n 
1 74  ALA n 
1 75  VAL n 
1 76  ARG n 
1 77  GLY n 
1 78  ILE n 
1 79  LEU n 
1 80  ARG n 
1 81  ASN n 
1 82  ALA n 
1 83  LYS n 
1 84  LEU n 
1 85  LYS n 
1 86  PRO n 
1 87  VAL n 
1 88  TYR n 
1 89  ASP n 
1 90  SER n 
1 91  LEU n 
1 92  ASP n 
1 93  ALA n 
1 94  VAL n 
1 95  ARG n 
1 96  ARG n 
1 97  ALA n 
1 98  ALA n 
1 99  LEU n 
1 100 ILE n 
1 101 ASN n 
1 102 MET n 
1 103 VAL n 
1 104 PHE n 
1 105 GLN n 
1 106 MET n 
1 107 GLY n 
1 108 GLU n 
1 109 THR n 
1 110 GLY n 
1 111 VAL n 
1 112 ALA n 
1 113 GLY n 
1 114 PHE n 
1 115 THR n 
1 116 ASN n 
1 117 SER n 
1 118 LEU n 
1 119 ARG n 
1 120 MET n 
1 121 ALA n 
1 122 GLN n 
1 123 GLN n 
1 124 LYS n 
1 125 ARG n 
1 126 TRP n 
1 127 ASP n 
1 128 GLU n 
1 129 ALA n 
1 130 ALA n 
1 131 VAL n 
1 132 ASN n 
1 133 LEU n 
1 134 ALA n 
1 135 LYS n 
1 136 SER n 
1 137 ARG n 
1 138 TRP n 
1 139 TYR n 
1 140 ASN n 
1 141 GLN n 
1 142 THR n 
1 143 PRO n 
1 144 ASN n 
1 145 ARG n 
1 146 ALA n 
1 147 LYS n 
1 148 ARG n 
1 149 VAL n 
1 150 ILE n 
1 151 THR n 
1 152 THR n 
1 153 PHE n 
1 154 ARG n 
1 155 THR n 
1 156 GLY n 
1 157 THR n 
1 158 TRP n 
1 159 ASP n 
1 160 ALA n 
1 161 TYR n 
1 162 LYS n 
1 163 ASN n 
1 164 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     'T4-like viruses' 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   'Enterobacteria phage T4 sensu lato' 
_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      'Enterobacteria phage T4' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10665 
_entity_src_gen.pdbx_gene_src_variant              'CYS-FREE WILDTYPE T4' 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     Escherichia 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_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                       M13 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   
;MUTANT GENE WAS DERIVED FROM SITE-DIRECTED MUTAGENESIS OF THE GENE FOR CYS-FREE WILDTYPE T4 LYSOZYME IN M13 USING THE METHOD OF KUNKEL AND THE VECTOR SYSTEM DESCRIBED IN REFERENCE 3 BELOW
;
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    LYCV_BPT4 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          P00720 
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_seq_one_letter_code   
;MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA
YKNL
;
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              200L 
_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                 164 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00720 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  164 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       164 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 200L THR A 54  ? UNP P00720 CYS 54  CONFLICT 54  1 
1 200L ALA A 97  ? UNP P00720 CYS 97  CONFLICT 97  2 
1 200L ALA A 121 ? UNP P00720 LEU 121 CONFLICT 121 3 
# 
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 
BME non-polymer         . BETA-MERCAPTOETHANOL ? 'C2 H6 O S'      78.133  
CL  non-polymer         . 'CHLORIDE ION'       ? 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE             ? 'C3 H7 N O2 S'   121.158 
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 
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          200L 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   ? 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.77 
_exptl_crystal.density_percent_sol   55.61 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.7 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    'pH 6.7' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           298 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'AREA DETECTOR' 
_diffrn_detector.type                   'XUONG-HAMLIN MULTIWIRE' 
_diffrn_detector.pdbx_collection_date   ? 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    GRAPHITE 
_diffrn_radiation.pdbx_diffrn_protocol             ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      ? 
_diffrn_source.type                        ? 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             1.5418 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     200L 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             ? 
_reflns.d_resolution_high            ? 
_reflns.number_obs                   ? 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         ? 
_reflns.pdbx_Rmerge_I_obs            0.032 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_refine.entry_id                                 200L 
_refine.ls_number_reflns_obs                     14362 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            1.95 
_refine.ls_percent_reflns_obs                    88. 
_refine.ls_R_factor_obs                          0.176 
_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                                  
;MUTANT SPACE GROUP, P3(2)21, IS ISOMORPHOUS TO WILD TYPE.
STARTING COORDINATES WERE BASED ON THE CYS-FREE WILD-TYPE
MODEL.
;
_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        1289 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         10 
_refine_hist.number_atoms_solvent             106 
_refine_hist.number_atoms_total               1405 
_refine_hist.d_res_high                       1.95 
_refine_hist.d_res_low                        . 
# 
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           0.015 ? ? ? 'X-RAY DIFFRACTION' ? 
t_angle_deg        2.03  ? ? ? '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                  200L 
_struct.title                     
;THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME
;
_struct.pdbx_descriptor           'LYSOZYME, BETA-MERCAPTOETHANOL' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        200L 
_struct_keywords.pdbx_keywords   'HYDROLASE (O-GLYCOSYL)' 
_struct_keywords.text            'CAVITIES, CORE-PACKING, PROTEIN STABILITY, HYDROLASE (O-GLYCOSYL)' 
# 
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 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
# 
_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  ILE A 3   ? GLU A 11  ? ILE A 3   GLU A 11  1 ? 9  
HELX_P HELX_P2  H2  LEU A 39  ? ILE A 50  ? LEU A 39  ILE A 50  1 ? 12 
HELX_P HELX_P3  H3  LYS A 60  ? ARG A 80  ? LYS A 60  ARG A 80  1 ? 21 
HELX_P HELX_P4  H4  ALA A 82  ? SER A 90  ? ALA A 82  SER A 90  1 ? 9  
HELX_P HELX_P5  H5  ALA A 93  ? MET A 106 ? ALA A 93  MET A 106 1 ? 14 
HELX_P HELX_P6  H6  GLU A 108 ? GLY A 113 ? GLU A 108 GLY A 113 1 ? 6  
HELX_P HELX_P7  H7  THR A 115 ? GLN A 123 ? THR A 115 GLN A 123 1 ? 9  
HELX_P HELX_P8  H8  TRP A 126 ? ALA A 134 ? TRP A 126 ALA A 134 1 ? 9  
HELX_P HELX_P9  H9  ARG A 137 ? GLN A 141 ? ARG A 137 GLN A 141 1 ? 5  
HELX_P HELX_P10 H10 PRO A 143 ? THR A 155 ? PRO A 143 THR A 155 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               A 
_struct_sheet.type             ? 
_struct_sheet.number_strands   2 
_struct_sheet.details          ? 
# 
_struct_sheet_order.sheet_id     A 
_struct_sheet_order.range_id_1   1 
_struct_sheet_order.range_id_2   2 
_struct_sheet_order.offset       ? 
_struct_sheet_order.sense        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 25 ? ILE A 27 ? TYR A 25 ILE A 27 
A 2 HIS A 31 ? THR A 34 ? HIS A 31 THR A 34 
# 
_pdbx_struct_sheet_hbond.sheet_id                A 
_pdbx_struct_sheet_hbond.range_id_1              1 
_pdbx_struct_sheet_hbond.range_id_2              2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_1_label_comp_id   TYR 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    25 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id    O 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id    TYR 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     25 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   N 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   THR 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    34 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id    N 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id    THR 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     34 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CL A 173'  
AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CL A 178'  
AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE BME A 901' 
AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE BME A 902' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 3 THR A 142 ? THR A 142 . ? 1_555 ? 
2  AC1 3 ARG A 145 ? ARG A 145 . ? 1_555 ? 
3  AC1 3 HOH F .   ? HOH A 291 . ? 4_655 ? 
4  AC2 3 LYS A 135 ? LYS A 135 . ? 3_665 ? 
5  AC2 3 SER A 136 ? SER A 136 . ? 3_665 ? 
6  AC2 3 HOH F .   ? HOH A 215 . ? 1_555 ? 
7  AC3 2 ASP A 72  ? ASP A 72  . ? 5_555 ? 
8  AC3 2 BME E .   ? BME A 902 . ? 1_555 ? 
9  AC4 4 ASP A 72  ? ASP A 72  . ? 5_555 ? 
10 AC4 4 ALA A 93  ? ALA A 93  . ? 1_555 ? 
11 AC4 4 HOH F .   ? HOH A 195 . ? 1_555 ? 
12 AC4 4 BME D .   ? BME A 901 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          200L 
_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                    200L 
_atom_sites.fract_transf_matrix[1][1]   0.016399 
_atom_sites.fract_transf_matrix[1][2]   0.009468 
_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]   0.018936 
_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]   0.010420 
_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  
CL 
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   . MET A 1 1   ? 43.914 -3.403 8.754   1.00 36.07  ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? 43.520 -2.018 8.895   1.00 20.51  ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? 42.097 -2.002 9.425   1.00 21.03  ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? 41.435 -2.993 9.298   1.00 20.03  ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? 43.693 -1.264 7.552   1.00 17.30  ? 1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? 42.903 0.020  7.457   1.00 34.28  ? 1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? 43.932 1.487  7.661   1.00 39.71  ? 1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? 45.484 0.739  7.149   1.00 37.02  ? 1   MET A CE  1 
ATOM   9    N  N   . ASN A 1 2   ? 41.661 -0.889 10.039  1.00 16.25  ? 2   ASN A N   1 
ATOM   10   C  CA  . ASN A 1 2   ? 40.332 -0.753 10.606  1.00 11.56  ? 2   ASN A CA  1 
ATOM   11   C  C   . ASN A 1 2   ? 39.944 0.729  10.691  1.00 17.42  ? 2   ASN A C   1 
ATOM   12   O  O   . ASN A 1 2   ? 40.751 1.572  10.393  1.00 11.73  ? 2   ASN A O   1 
ATOM   13   C  CB  . ASN A 1 2   ? 40.208 -1.491 11.989  1.00 15.25  ? 2   ASN A CB  1 
ATOM   14   C  CG  . ASN A 1 2   ? 41.128 -0.942 13.041  1.00 16.24  ? 2   ASN A CG  1 
ATOM   15   O  OD1 . ASN A 1 2   ? 41.131 0.268  13.300  1.00 18.64  ? 2   ASN A OD1 1 
ATOM   16   N  ND2 . ASN A 1 2   ? 41.929 -1.811 13.632  1.00 14.71  ? 2   ASN A ND2 1 
ATOM   17   N  N   . ILE A 1 3   ? 38.721 1.023  11.112  1.00 11.52  ? 3   ILE A N   1 
ATOM   18   C  CA  . ILE A 1 3   ? 38.177 2.386  11.200  1.00 17.48  ? 3   ILE A CA  1 
ATOM   19   C  C   . ILE A 1 3   ? 39.041 3.345  11.994  1.00 18.68  ? 3   ILE A C   1 
ATOM   20   O  O   . ILE A 1 3   ? 39.310 4.504  11.602  1.00 16.74  ? 3   ILE A O   1 
ATOM   21   C  CB  . ILE A 1 3   ? 36.655 2.439  11.530  1.00 13.22  ? 3   ILE A CB  1 
ATOM   22   C  CG1 . ILE A 1 3   ? 36.100 3.854  11.447  1.00 11.82  ? 3   ILE A CG1 1 
ATOM   23   C  CG2 . ILE A 1 3   ? 36.340 1.856  12.911  1.00 14.39  ? 3   ILE A CG2 1 
ATOM   24   C  CD1 . ILE A 1 3   ? 36.246 4.562  10.062  1.00 13.00  ? 3   ILE A CD1 1 
ATOM   25   N  N   . PHE A 1 4   ? 39.514 2.831  13.127  1.00 16.19  ? 4   PHE A N   1 
ATOM   26   C  CA  . PHE A 1 4   ? 40.361 3.595  14.018  1.00 12.72  ? 4   PHE A CA  1 
ATOM   27   C  C   . PHE A 1 4   ? 41.646 4.001  13.350  1.00 14.24  ? 4   PHE A C   1 
ATOM   28   O  O   . PHE A 1 4   ? 41.999 5.166  13.350  1.00 15.63  ? 4   PHE A O   1 
ATOM   29   C  CB  . PHE A 1 4   ? 40.614 2.835  15.327  1.00 14.05  ? 4   PHE A CB  1 
ATOM   30   C  CG  . PHE A 1 4   ? 39.367 2.876  16.191  1.00 13.58  ? 4   PHE A CG  1 
ATOM   31   C  CD1 . PHE A 1 4   ? 39.111 3.983  17.009  1.00 17.16  ? 4   PHE A CD1 1 
ATOM   32   C  CD2 . PHE A 1 4   ? 38.432 1.836  16.165  1.00 15.22  ? 4   PHE A CD2 1 
ATOM   33   C  CE1 . PHE A 1 4   ? 37.973 4.048  17.814  1.00 16.07  ? 4   PHE A CE1 1 
ATOM   34   C  CE2 . PHE A 1 4   ? 37.282 1.886  16.958  1.00 21.24  ? 4   PHE A CE2 1 
ATOM   35   C  CZ  . PHE A 1 4   ? 37.066 2.989  17.789  1.00 16.14  ? 4   PHE A CZ  1 
ATOM   36   N  N   . GLU A 1 5   ? 42.367 3.039  12.797  1.00 12.77  ? 5   GLU A N   1 
ATOM   37   C  CA  . GLU A 1 5   ? 43.638 3.367  12.116  1.00 15.20  ? 5   GLU A CA  1 
ATOM   38   C  C   . GLU A 1 5   ? 43.396 4.259  10.918  1.00 16.33  ? 5   GLU A C   1 
ATOM   39   O  O   . GLU A 1 5   ? 44.129 5.167  10.655  1.00 16.14  ? 5   GLU A O   1 
ATOM   40   C  CB  . GLU A 1 5   ? 44.391 2.123  11.620  1.00 17.88  ? 5   GLU A CB  1 
ATOM   41   C  CG  . GLU A 1 5   ? 44.571 1.056  12.729  1.00 27.69  ? 5   GLU A CG  1 
ATOM   42   C  CD  . GLU A 1 5   ? 45.300 -0.214 12.335  1.00 30.37  ? 5   GLU A CD  1 
ATOM   43   O  OE1 . GLU A 1 5   ? 45.278 -0.679 11.214  1.00 79.11  ? 5   GLU A OE1 1 
ATOM   44   O  OE2 . GLU A 1 5   ? 45.980 -0.758 13.323  1.00 100.00 ? 5   GLU A OE2 1 
ATOM   45   N  N   . MET A 1 6   ? 42.316 3.992  10.213  1.00 16.55  ? 6   MET A N   1 
ATOM   46   C  CA  . MET A 1 6   ? 41.955 4.766  9.046   1.00 13.75  ? 6   MET A CA  1 
ATOM   47   C  C   . MET A 1 6   ? 41.741 6.217  9.400   1.00 21.28  ? 6   MET A C   1 
ATOM   48   O  O   . MET A 1 6   ? 42.288 7.142  8.758   1.00 15.10  ? 6   MET A O   1 
ATOM   49   C  CB  . MET A 1 6   ? 40.653 4.195  8.445   1.00 15.17  ? 6   MET A CB  1 
ATOM   50   C  CG  . MET A 1 6   ? 40.202 4.950  7.219   1.00 11.83  ? 6   MET A CG  1 
ATOM   51   S  SD  . MET A 1 6   ? 38.485 4.587  6.820   1.00 14.65  ? 6   MET A SD  1 
ATOM   52   C  CE  . MET A 1 6   ? 38.493 4.662  5.009   1.00 17.96  ? 6   MET A CE  1 
ATOM   53   N  N   . LEU A 1 7   ? 40.917 6.450  10.419  1.00 14.10  ? 7   LEU A N   1 
ATOM   54   C  CA  . LEU A 1 7   ? 40.680 7.857  10.778  1.00 13.50  ? 7   LEU A CA  1 
ATOM   55   C  C   . LEU A 1 7   ? 41.915 8.511  11.405  1.00 14.33  ? 7   LEU A C   1 
ATOM   56   O  O   . LEU A 1 7   ? 42.127 9.712  11.311  1.00 15.11  ? 7   LEU A O   1 
ATOM   57   C  CB  . LEU A 1 7   ? 39.435 8.068  11.662  1.00 15.92  ? 7   LEU A CB  1 
ATOM   58   C  CG  . LEU A 1 7   ? 38.150 8.014  10.875  1.00 15.79  ? 7   LEU A CG  1 
ATOM   59   C  CD1 . LEU A 1 7   ? 37.035 7.679  11.870  1.00 18.92  ? 7   LEU A CD1 1 
ATOM   60   C  CD2 . LEU A 1 7   ? 37.937 9.383  10.209  1.00 10.47  ? 7   LEU A CD2 1 
ATOM   61   N  N   . ARG A 1 8   ? 42.736 7.693  12.060  1.00 11.27  ? 8   ARG A N   1 
ATOM   62   C  CA  . ARG A 1 8   ? 43.899 8.255  12.668  1.00 13.02  ? 8   ARG A CA  1 
ATOM   63   C  C   . ARG A 1 8   ? 44.819 8.749  11.584  1.00 20.47  ? 8   ARG A C   1 
ATOM   64   O  O   . ARG A 1 8   ? 45.501 9.735  11.754  1.00 21.61  ? 8   ARG A O   1 
ATOM   65   C  CB  . ARG A 1 8   ? 44.581 7.285  13.627  1.00 25.98  ? 8   ARG A CB  1 
ATOM   66   C  CG  . ARG A 1 8   ? 45.984 7.706  14.070  1.00 25.97  ? 8   ARG A CG  1 
ATOM   67   C  CD  . ARG A 1 8   ? 46.027 8.841  15.078  1.00 30.45  ? 8   ARG A CD  1 
ATOM   68   N  NE  . ARG A 1 8   ? 47.342 8.978  15.715  1.00 42.49  ? 8   ARG A NE  1 
ATOM   69   C  CZ  . ARG A 1 8   ? 48.355 9.610  15.128  1.00 100.00 ? 8   ARG A CZ  1 
ATOM   70   N  NH1 . ARG A 1 8   ? 48.249 10.149 13.895  1.00 33.89  ? 8   ARG A NH1 1 
ATOM   71   N  NH2 . ARG A 1 8   ? 49.507 9.694  15.789  1.00 86.26  ? 8   ARG A NH2 1 
ATOM   72   N  N   . ILE A 1 9   ? 44.798 8.094  10.446  1.00 16.15  ? 9   ILE A N   1 
ATOM   73   C  CA  . ILE A 1 9   ? 45.624 8.520  9.329   1.00 13.98  ? 9   ILE A CA  1 
ATOM   74   C  C   . ILE A 1 9   ? 45.077 9.788  8.701   1.00 25.11  ? 9   ILE A C   1 
ATOM   75   O  O   . ILE A 1 9   ? 45.821 10.720 8.466   1.00 23.28  ? 9   ILE A O   1 
ATOM   76   C  CB  . ILE A 1 9   ? 45.807 7.429  8.288   1.00 16.76  ? 9   ILE A CB  1 
ATOM   77   C  CG1 . ILE A 1 9   ? 46.773 6.386  8.816   1.00 14.05  ? 9   ILE A CG1 1 
ATOM   78   C  CG2 . ILE A 1 9   ? 46.376 8.036  7.014   1.00 16.76  ? 9   ILE A CG2 1 
ATOM   79   C  CD1 . ILE A 1 9   ? 46.759 5.125  7.966   1.00 27.33  ? 9   ILE A CD1 1 
ATOM   80   N  N   . ASP A 1 10  ? 43.763 9.841  8.464   1.00 18.58  ? 10  ASP A N   1 
ATOM   81   C  CA  . ASP A 1 10  ? 43.144 11.002 7.890   1.00 11.82  ? 10  ASP A CA  1 
ATOM   82   C  C   . ASP A 1 10  ? 43.126 12.260 8.758   1.00 23.37  ? 10  ASP A C   1 
ATOM   83   O  O   . ASP A 1 10  ? 43.197 13.350 8.211   1.00 19.56  ? 10  ASP A O   1 
ATOM   84   C  CB  . ASP A 1 10  ? 41.697 10.681 7.449   1.00 14.69  ? 10  ASP A CB  1 
ATOM   85   C  CG  . ASP A 1 10  ? 41.714 9.778  6.252   1.00 20.09  ? 10  ASP A CG  1 
ATOM   86   O  OD1 . ASP A 1 10  ? 42.657 9.715  5.517   1.00 17.17  ? 10  ASP A OD1 1 
ATOM   87   O  OD2 . ASP A 1 10  ? 40.676 9.034  6.127   1.00 18.39  ? 10  ASP A OD2 1 
ATOM   88   N  N   . GLU A 1 11  ? 42.951 12.124 10.085  1.00 14.64  ? 11  GLU A N   1 
ATOM   89   C  CA  . GLU A 1 11  ? 42.829 13.271 10.970  1.00 13.73  ? 11  GLU A CA  1 
ATOM   90   C  C   . GLU A 1 11  ? 44.099 13.697 11.660  1.00 23.66  ? 11  GLU A C   1 
ATOM   91   O  O   . GLU A 1 11  ? 44.247 14.850 12.049  1.00 25.26  ? 11  GLU A O   1 
ATOM   92   C  CB  . GLU A 1 11  ? 41.766 12.984 12.044  1.00 7.92   ? 11  GLU A CB  1 
ATOM   93   C  CG  . GLU A 1 11  ? 40.439 12.680 11.375  1.00 15.76  ? 11  GLU A CG  1 
ATOM   94   C  CD  . GLU A 1 11  ? 39.823 13.937 10.811  1.00 21.21  ? 11  GLU A CD  1 
ATOM   95   O  OE1 . GLU A 1 11  ? 40.313 15.024 10.963  1.00 24.68  ? 11  GLU A OE1 1 
ATOM   96   O  OE2 . GLU A 1 11  ? 38.677 13.760 10.208  1.00 21.61  ? 11  GLU A OE2 1 
ATOM   97   N  N   . GLY A 1 12  ? 44.996 12.750 11.883  1.00 19.02  ? 12  GLY A N   1 
ATOM   98   C  CA  . GLY A 1 12  ? 46.208 13.029 12.625  1.00 19.58  ? 12  GLY A CA  1 
ATOM   99   C  C   . GLY A 1 12  ? 45.905 13.126 14.131  1.00 26.10  ? 12  GLY A C   1 
ATOM   100  O  O   . GLY A 1 12  ? 44.795 12.825 14.557  1.00 21.75  ? 12  GLY A O   1 
ATOM   101  N  N   . LEU A 1 13  ? 46.917 13.496 14.927  1.00 18.92  ? 13  LEU A N   1 
ATOM   102  C  CA  . LEU A 1 13  ? 46.789 13.649 16.367  1.00 22.93  ? 13  LEU A CA  1 
ATOM   103  C  C   . LEU A 1 13  ? 47.506 14.882 16.870  1.00 25.76  ? 13  LEU A C   1 
ATOM   104  O  O   . LEU A 1 13  ? 48.707 14.979 16.766  1.00 27.73  ? 13  LEU A O   1 
ATOM   105  C  CB  . LEU A 1 13  ? 47.337 12.455 17.114  1.00 23.44  ? 13  LEU A CB  1 
ATOM   106  C  CG  . LEU A 1 13  ? 47.403 12.711 18.611  1.00 30.40  ? 13  LEU A CG  1 
ATOM   107  C  CD1 . LEU A 1 13  ? 46.061 12.419 19.281  1.00 20.15  ? 13  LEU A CD1 1 
ATOM   108  C  CD2 . LEU A 1 13  ? 48.426 11.753 19.145  1.00 35.50  ? 13  LEU A CD2 1 
ATOM   109  N  N   . ARG A 1 14  ? 46.738 15.801 17.427  1.00 28.78  ? 14  ARG A N   1 
ATOM   110  C  CA  . ARG A 1 14  ? 47.223 17.037 17.997  1.00 25.26  ? 14  ARG A CA  1 
ATOM   111  C  C   . ARG A 1 14  ? 46.745 17.216 19.437  1.00 21.36  ? 14  ARG A C   1 
ATOM   112  O  O   . ARG A 1 14  ? 45.585 16.975 19.734  1.00 20.57  ? 14  ARG A O   1 
ATOM   113  C  CB  . ARG A 1 14  ? 46.844 18.162 17.084  1.00 19.85  ? 14  ARG A CB  1 
ATOM   114  C  CG  . ARG A 1 14  ? 47.427 17.805 15.734  1.00 30.78  ? 14  ARG A CG  1 
ATOM   115  C  CD  . ARG A 1 14  ? 47.639 18.989 14.816  1.00 43.71  ? 14  ARG A CD  1 
ATOM   116  N  NE  . ARG A 1 14  ? 48.510 20.017 15.381  1.00 57.04  ? 14  ARG A NE  1 
ATOM   117  C  CZ  . ARG A 1 14  ? 48.594 21.257 14.879  1.00 94.55  ? 14  ARG A CZ  1 
ATOM   118  N  NH1 . ARG A 1 14  ? 47.865 21.640 13.819  1.00 59.84  ? 14  ARG A NH1 1 
ATOM   119  N  NH2 . ARG A 1 14  ? 49.419 22.138 15.454  1.00 79.89  ? 14  ARG A NH2 1 
ATOM   120  N  N   . LEU A 1 15  ? 47.660 17.599 20.340  1.00 21.06  ? 15  LEU A N   1 
ATOM   121  C  CA  . LEU A 1 15  ? 47.342 17.716 21.749  1.00 23.09  ? 15  LEU A CA  1 
ATOM   122  C  C   . LEU A 1 15  ? 47.098 19.101 22.268  1.00 26.55  ? 15  LEU A C   1 
ATOM   123  O  O   . LEU A 1 15  ? 46.865 19.271 23.469  1.00 26.55  ? 15  LEU A O   1 
ATOM   124  C  CB  . LEU A 1 15  ? 48.424 17.064 22.588  1.00 14.98  ? 15  LEU A CB  1 
ATOM   125  C  CG  . LEU A 1 15  ? 48.538 15.617 22.224  1.00 25.27  ? 15  LEU A CG  1 
ATOM   126  C  CD1 . LEU A 1 15  ? 49.664 15.046 23.053  1.00 29.14  ? 15  LEU A CD1 1 
ATOM   127  C  CD2 . LEU A 1 15  ? 47.223 14.916 22.540  1.00 28.69  ? 15  LEU A CD2 1 
ATOM   128  N  N   . LYS A 1 16  ? 47.170 20.061 21.368  1.00 23.04  ? 16  LYS A N   1 
ATOM   129  C  CA  . LYS A 1 16  ? 46.929 21.447 21.698  1.00 24.23  ? 16  LYS A CA  1 
ATOM   130  C  C   . LYS A 1 16  ? 45.837 21.899 20.783  1.00 16.57  ? 16  LYS A C   1 
ATOM   131  O  O   . LYS A 1 16  ? 45.738 21.424 19.661  1.00 30.02  ? 16  LYS A O   1 
ATOM   132  C  CB  . LYS A 1 16  ? 48.133 22.364 21.423  1.00 34.03  ? 16  LYS A CB  1 
ATOM   133  C  CG  . LYS A 1 16  ? 48.998 22.674 22.627  1.00 60.51  ? 16  LYS A CG  1 
ATOM   134  C  CD  . LYS A 1 16  ? 50.419 22.142 22.469  1.00 89.38  ? 16  LYS A CD  1 
ATOM   135  C  CE  . LYS A 1 16  ? 51.371 22.558 23.589  1.00 100.00 ? 16  LYS A CE  1 
ATOM   136  N  NZ  . LYS A 1 16  ? 51.823 21.438 24.455  1.00 100.00 ? 16  LYS A NZ  1 
ATOM   137  N  N   . ILE A 1 17  ? 45.030 22.832 21.229  1.00 25.86  ? 17  ILE A N   1 
ATOM   138  C  CA  . ILE A 1 17  ? 43.973 23.319 20.379  1.00 22.01  ? 17  ILE A CA  1 
ATOM   139  C  C   . ILE A 1 17  ? 44.517 23.802 19.027  1.00 35.26  ? 17  ILE A C   1 
ATOM   140  O  O   . ILE A 1 17  ? 45.553 24.498 18.955  1.00 24.69  ? 17  ILE A O   1 
ATOM   141  C  CB  . ILE A 1 17  ? 43.158 24.419 21.068  1.00 23.53  ? 17  ILE A CB  1 
ATOM   142  C  CG1 . ILE A 1 17  ? 42.373 23.850 22.259  1.00 27.99  ? 17  ILE A CG1 1 
ATOM   143  C  CG2 . ILE A 1 17  ? 42.217 25.125 20.057  1.00 24.98  ? 17  ILE A CG2 1 
ATOM   144  C  CD1 . ILE A 1 17  ? 41.456 24.890 22.908  1.00 16.83  ? 17  ILE A CD1 1 
ATOM   145  N  N   . TYR A 1 18  ? 43.802 23.473 17.955  1.00 20.55  ? 18  TYR A N   1 
ATOM   146  C  CA  . TYR A 1 18  ? 44.248 23.905 16.645  1.00 26.21  ? 18  TYR A CA  1 
ATOM   147  C  C   . TYR A 1 18  ? 43.080 24.298 15.737  1.00 18.16  ? 18  TYR A C   1 
ATOM   148  O  O   . TYR A 1 18  ? 41.922 24.037 16.036  1.00 25.05  ? 18  TYR A O   1 
ATOM   149  C  CB  . TYR A 1 18  ? 45.224 22.845 16.044  1.00 18.56  ? 18  TYR A CB  1 
ATOM   150  C  CG  . TYR A 1 18  ? 44.540 21.574 15.538  1.00 24.40  ? 18  TYR A CG  1 
ATOM   151  C  CD1 . TYR A 1 18  ? 44.063 21.506 14.225  1.00 38.90  ? 18  TYR A CD1 1 
ATOM   152  C  CD2 . TYR A 1 18  ? 44.360 20.455 16.358  1.00 21.30  ? 18  TYR A CD2 1 
ATOM   153  C  CE1 . TYR A 1 18  ? 43.429 20.371 13.709  1.00 18.56  ? 18  TYR A CE1 1 
ATOM   154  C  CE2 . TYR A 1 18  ? 43.701 19.324 15.876  1.00 52.88  ? 18  TYR A CE2 1 
ATOM   155  C  CZ  . TYR A 1 18  ? 43.227 19.292 14.561  1.00 24.15  ? 18  TYR A CZ  1 
ATOM   156  O  OH  . TYR A 1 18  ? 42.611 18.168 14.087  1.00 40.88  ? 18  TYR A OH  1 
ATOM   157  N  N   . LYS A 1 19  ? 43.360 24.979 14.630  1.00 34.53  ? 19  LYS A N   1 
ATOM   158  C  CA  . LYS A 1 19  ? 42.304 25.313 13.689  1.00 22.78  ? 19  LYS A CA  1 
ATOM   159  C  C   . LYS A 1 19  ? 42.308 24.295 12.581  1.00 39.79  ? 19  LYS A C   1 
ATOM   160  O  O   . LYS A 1 19  ? 43.364 23.916 12.074  1.00 49.33  ? 19  LYS A O   1 
ATOM   161  C  CB  . LYS A 1 19  ? 42.396 26.679 13.086  1.00 24.80  ? 19  LYS A CB  1 
ATOM   162  C  CG  . LYS A 1 19  ? 42.135 27.735 14.131  1.00 26.88  ? 19  LYS A CG  1 
ATOM   163  C  CD  . LYS A 1 19  ? 41.248 28.864 13.641  1.00 85.14  ? 19  LYS A CD  1 
ATOM   164  C  CE  . LYS A 1 19  ? 41.800 30.249 13.992  1.00 47.32  ? 19  LYS A CE  1 
ATOM   165  N  NZ  . LYS A 1 19  ? 40.751 31.258 14.261  1.00 100.00 ? 19  LYS A NZ  1 
ATOM   166  N  N   . ASP A 1 20  ? 41.125 23.837 12.204  1.00 42.82  ? 20  ASP A N   1 
ATOM   167  C  CA  . ASP A 1 20  ? 41.044 22.842 11.160  1.00 33.02  ? 20  ASP A CA  1 
ATOM   168  C  C   . ASP A 1 20  ? 41.191 23.403 9.746   1.00 35.20  ? 20  ASP A C   1 
ATOM   169  O  O   . ASP A 1 20  ? 41.598 24.578 9.583   1.00 39.83  ? 20  ASP A O   1 
ATOM   170  C  CB  . ASP A 1 20  ? 39.947 21.781 11.365  1.00 21.59  ? 20  ASP A CB  1 
ATOM   171  C  CG  . ASP A 1 20  ? 38.594 22.310 10.972  1.00 29.26  ? 20  ASP A CG  1 
ATOM   172  O  OD1 . ASP A 1 20  ? 38.432 23.449 10.604  1.00 29.60  ? 20  ASP A OD1 1 
ATOM   173  O  OD2 . ASP A 1 20  ? 37.643 21.416 11.037  1.00 41.62  ? 20  ASP A OD2 1 
ATOM   174  N  N   . THR A 1 21  ? 40.891 22.556 8.725   1.00 42.12  ? 21  THR A N   1 
ATOM   175  C  CA  . THR A 1 21  ? 41.023 22.955 7.299   1.00 45.11  ? 21  THR A CA  1 
ATOM   176  C  C   . THR A 1 21  ? 40.100 24.085 6.860   1.00 51.46  ? 21  THR A C   1 
ATOM   177  O  O   . THR A 1 21  ? 40.290 24.586 5.733   1.00 42.59  ? 21  THR A O   1 
ATOM   178  C  CB  . THR A 1 21  ? 40.838 21.766 6.329   1.00 58.19  ? 21  THR A CB  1 
ATOM   179  O  OG1 . THR A 1 21  ? 39.628 21.099 6.654   1.00 66.24  ? 21  THR A OG1 1 
ATOM   180  C  CG2 . THR A 1 21  ? 41.986 20.773 6.466   1.00 64.49  ? 21  THR A CG2 1 
ATOM   181  N  N   . GLU A 1 22  ? 39.104 24.399 7.763   1.00 100.00 ? 22  GLU A N   1 
ATOM   182  C  CA  . GLU A 1 22  ? 38.011 25.408 7.659   1.00 42.68  ? 22  GLU A CA  1 
ATOM   183  C  C   . GLU A 1 22  ? 38.038 26.547 8.672   1.00 31.00  ? 22  GLU A C   1 
ATOM   184  O  O   . GLU A 1 22  ? 37.153 27.399 8.631   1.00 37.01  ? 22  GLU A O   1 
ATOM   185  C  CB  . GLU A 1 22  ? 36.611 24.818 7.785   1.00 26.73  ? 22  GLU A CB  1 
ATOM   186  C  CG  . GLU A 1 22  ? 36.510 23.409 7.185   1.00 68.67  ? 22  GLU A CG  1 
ATOM   187  C  CD  . GLU A 1 22  ? 35.881 23.453 5.834   1.00 57.88  ? 22  GLU A CD  1 
ATOM   188  O  OE1 . GLU A 1 22  ? 35.276 24.437 5.448   1.00 56.70  ? 22  GLU A OE1 1 
ATOM   189  O  OE2 . GLU A 1 22  ? 36.057 22.337 5.146   1.00 90.22  ? 22  GLU A OE2 1 
ATOM   190  N  N   . GLY A 1 23  ? 39.032 26.534 9.571   1.00 32.55  ? 23  GLY A N   1 
ATOM   191  C  CA  . GLY A 1 23  ? 39.217 27.567 10.564  1.00 29.06  ? 23  GLY A CA  1 
ATOM   192  C  C   . GLY A 1 23  ? 38.560 27.261 11.910  1.00 40.25  ? 23  GLY A C   1 
ATOM   193  O  O   . GLY A 1 23  ? 38.401 28.139 12.740  1.00 38.71  ? 23  GLY A O   1 
ATOM   194  N  N   . TYR A 1 24  ? 38.179 26.022 12.146  1.00 27.01  ? 24  TYR A N   1 
ATOM   195  C  CA  . TYR A 1 24  ? 37.549 25.744 13.413  1.00 25.32  ? 24  TYR A CA  1 
ATOM   196  C  C   . TYR A 1 24  ? 38.476 25.117 14.421  1.00 30.25  ? 24  TYR A C   1 
ATOM   197  O  O   . TYR A 1 24  ? 39.347 24.297 14.126  1.00 32.82  ? 24  TYR A O   1 
ATOM   198  C  CB  . TYR A 1 24  ? 36.361 24.843 13.231  1.00 18.47  ? 24  TYR A CB  1 
ATOM   199  C  CG  . TYR A 1 24  ? 35.356 25.391 12.262  1.00 32.31  ? 24  TYR A CG  1 
ATOM   200  C  CD1 . TYR A 1 24  ? 34.945 26.724 12.299  1.00 26.54  ? 24  TYR A CD1 1 
ATOM   201  C  CD2 . TYR A 1 24  ? 34.800 24.536 11.313  1.00 34.85  ? 24  TYR A CD2 1 
ATOM   202  C  CE1 . TYR A 1 24  ? 34.001 27.172 11.372  1.00 66.89  ? 24  TYR A CE1 1 
ATOM   203  C  CE2 . TYR A 1 24  ? 33.872 24.972 10.371  1.00 34.90  ? 24  TYR A CE2 1 
ATOM   204  C  CZ  . TYR A 1 24  ? 33.472 26.304 10.411  1.00 33.48  ? 24  TYR A CZ  1 
ATOM   205  O  OH  . TYR A 1 24  ? 32.537 26.736 9.493   1.00 59.26  ? 24  TYR A OH  1 
ATOM   206  N  N   . TYR A 1 25  ? 38.222 25.469 15.644  1.00 22.40  ? 25  TYR A N   1 
ATOM   207  C  CA  . TYR A 1 25  ? 39.003 24.942 16.728  1.00 25.41  ? 25  TYR A CA  1 
ATOM   208  C  C   . TYR A 1 25  ? 38.729 23.469 16.905  1.00 16.58  ? 25  TYR A C   1 
ATOM   209  O  O   . TYR A 1 25  ? 37.584 23.017 17.002  1.00 20.93  ? 25  TYR A O   1 
ATOM   210  C  CB  . TYR A 1 25  ? 38.642 25.711 17.968  1.00 32.64  ? 25  TYR A CB  1 
ATOM   211  C  CG  . TYR A 1 25  ? 39.212 27.082 17.893  1.00 26.98  ? 25  TYR A CG  1 
ATOM   212  C  CD1 . TYR A 1 25  ? 40.598 27.232 17.854  1.00 24.77  ? 25  TYR A CD1 1 
ATOM   213  C  CD2 . TYR A 1 25  ? 38.385 28.208 17.925  1.00 29.49  ? 25  TYR A CD2 1 
ATOM   214  C  CE1 . TYR A 1 25  ? 41.165 28.506 17.895  1.00 35.99  ? 25  TYR A CE1 1 
ATOM   215  C  CE2 . TYR A 1 25  ? 38.932 29.491 17.937  1.00 20.29  ? 25  TYR A CE2 1 
ATOM   216  C  CZ  . TYR A 1 25  ? 40.324 29.622 17.903  1.00 27.51  ? 25  TYR A CZ  1 
ATOM   217  O  OH  . TYR A 1 25  ? 40.872 30.876 17.904  1.00 49.13  ? 25  TYR A OH  1 
ATOM   218  N  N   . THR A 1 26  ? 39.804 22.741 16.966  1.00 14.60  ? 26  THR A N   1 
ATOM   219  C  CA  . THR A 1 26  ? 39.737 21.322 17.049  1.00 19.05  ? 26  THR A CA  1 
ATOM   220  C  C   . THR A 1 26  ? 40.823 20.906 17.948  1.00 21.27  ? 26  THR A C   1 
ATOM   221  O  O   . THR A 1 26  ? 41.685 21.701 18.256  1.00 21.68  ? 26  THR A O   1 
ATOM   222  C  CB  . THR A 1 26  ? 40.029 20.773 15.602  1.00 22.28  ? 26  THR A CB  1 
ATOM   223  O  OG1 . THR A 1 26  ? 39.107 21.373 14.735  1.00 22.44  ? 26  THR A OG1 1 
ATOM   224  C  CG2 . THR A 1 26  ? 39.926 19.244 15.480  1.00 11.23  ? 26  THR A CG2 1 
ATOM   225  N  N   . ILE A 1 27  ? 40.815 19.627 18.298  1.00 26.09  ? 27  ILE A N   1 
ATOM   226  C  CA  . ILE A 1 27  ? 41.853 19.044 19.126  1.00 18.49  ? 27  ILE A CA  1 
ATOM   227  C  C   . ILE A 1 27  ? 41.842 17.518 18.962  1.00 15.45  ? 27  ILE A C   1 
ATOM   228  O  O   . ILE A 1 27  ? 40.927 16.946 18.410  1.00 17.96  ? 27  ILE A O   1 
ATOM   229  C  CB  . ILE A 1 27  ? 41.762 19.456 20.611  1.00 31.37  ? 27  ILE A CB  1 
ATOM   230  C  CG1 . ILE A 1 27  ? 43.061 19.125 21.378  1.00 20.63  ? 27  ILE A CG1 1 
ATOM   231  C  CG2 . ILE A 1 27  ? 40.609 18.683 21.233  1.00 24.52  ? 27  ILE A CG2 1 
ATOM   232  C  CD1 . ILE A 1 27  ? 43.236 19.946 22.634  1.00 23.34  ? 27  ILE A CD1 1 
ATOM   233  N  N   . GLY A 1 28  ? 42.880 16.874 19.416  1.00 13.28  ? 28  GLY A N   1 
ATOM   234  C  CA  . GLY A 1 28  ? 43.007 15.422 19.384  1.00 16.57  ? 28  GLY A CA  1 
ATOM   235  C  C   . GLY A 1 28  ? 43.003 14.855 17.982  1.00 30.67  ? 28  GLY A C   1 
ATOM   236  O  O   . GLY A 1 28  ? 43.762 15.263 17.089  1.00 19.85  ? 28  GLY A O   1 
ATOM   237  N  N   . ILE A 1 29  ? 42.133 13.900 17.806  1.00 19.16  ? 29  ILE A N   1 
ATOM   238  C  CA  . ILE A 1 29  ? 42.006 13.265 16.526  1.00 12.52  ? 29  ILE A CA  1 
ATOM   239  C  C   . ILE A 1 29  ? 40.772 13.721 15.807  1.00 11.99  ? 29  ILE A C   1 
ATOM   240  O  O   . ILE A 1 29  ? 39.765 13.028 15.725  1.00 15.65  ? 29  ILE A O   1 
ATOM   241  C  CB  . ILE A 1 29  ? 42.053 11.754 16.685  1.00 26.48  ? 29  ILE A CB  1 
ATOM   242  C  CG1 . ILE A 1 29  ? 43.417 11.375 17.281  1.00 23.01  ? 29  ILE A CG1 1 
ATOM   243  C  CG2 . ILE A 1 29  ? 41.853 11.111 15.306  1.00 25.15  ? 29  ILE A CG2 1 
ATOM   244  C  CD1 . ILE A 1 29  ? 43.436 10.118 18.167  1.00 20.64  ? 29  ILE A CD1 1 
ATOM   245  N  N   . GLY A 1 30  ? 40.851 14.921 15.265  1.00 18.79  ? 30  GLY A N   1 
ATOM   246  C  CA  . GLY A 1 30  ? 39.724 15.448 14.544  1.00 10.59  ? 30  GLY A CA  1 
ATOM   247  C  C   . GLY A 1 30  ? 38.482 15.776 15.383  1.00 20.13  ? 30  GLY A C   1 
ATOM   248  O  O   . GLY A 1 30  ? 37.373 15.762 14.868  1.00 19.86  ? 30  GLY A O   1 
ATOM   249  N  N   . HIS A 1 31  ? 38.654 16.129 16.654  1.00 19.07  ? 31  HIS A N   1 
ATOM   250  C  CA  . HIS A 1 31  ? 37.507 16.472 17.500  1.00 11.10  ? 31  HIS A CA  1 
ATOM   251  C  C   . HIS A 1 31  ? 37.175 17.994 17.465  1.00 11.55  ? 31  HIS A C   1 
ATOM   252  O  O   . HIS A 1 31  ? 37.844 18.846 18.086  1.00 20.72  ? 31  HIS A O   1 
ATOM   253  C  CB  . HIS A 1 31  ? 37.723 15.945 18.934  1.00 13.37  ? 31  HIS A CB  1 
ATOM   254  C  CG  . HIS A 1 31  ? 36.530 16.212 19.804  1.00 20.06  ? 31  HIS A CG  1 
ATOM   255  N  ND1 . HIS A 1 31  ? 35.491 15.283 19.952  1.00 18.47  ? 31  HIS A ND1 1 
ATOM   256  C  CD2 . HIS A 1 31  ? 36.225 17.308 20.550  1.00 21.12  ? 31  HIS A CD2 1 
ATOM   257  C  CE1 . HIS A 1 31  ? 34.557 15.857 20.705  1.00 20.38  ? 31  HIS A CE1 1 
ATOM   258  N  NE2 . HIS A 1 31  ? 34.974 17.069 21.114  1.00 17.27  ? 31  HIS A NE2 1 
ATOM   259  N  N   . LEU A 1 32  ? 36.139 18.347 16.693  1.00 13.17  ? 32  LEU A N   1 
ATOM   260  C  CA  . LEU A 1 32  ? 35.760 19.739 16.537  1.00 25.37  ? 32  LEU A CA  1 
ATOM   261  C  C   . LEU A 1 32  ? 35.288 20.295 17.833  1.00 23.12  ? 32  LEU A C   1 
ATOM   262  O  O   . LEU A 1 32  ? 34.421 19.707 18.469  1.00 17.50  ? 32  LEU A O   1 
ATOM   263  C  CB  . LEU A 1 32  ? 34.632 19.887 15.529  1.00 25.96  ? 32  LEU A CB  1 
ATOM   264  C  CG  . LEU A 1 32  ? 34.021 21.295 15.490  1.00 44.37  ? 32  LEU A CG  1 
ATOM   265  C  CD1 . LEU A 1 32  ? 34.951 22.265 14.766  1.00 33.55  ? 32  LEU A CD1 1 
ATOM   266  C  CD2 . LEU A 1 32  ? 32.673 21.249 14.773  1.00 25.77  ? 32  LEU A CD2 1 
ATOM   267  N  N   . LEU A 1 33  ? 35.853 21.386 18.246  1.00 16.94  ? 33  LEU A N   1 
ATOM   268  C  CA  . LEU A 1 33  ? 35.395 21.884 19.514  1.00 21.93  ? 33  LEU A CA  1 
ATOM   269  C  C   . LEU A 1 33  ? 34.247 22.819 19.317  1.00 28.28  ? 33  LEU A C   1 
ATOM   270  O  O   . LEU A 1 33  ? 33.182 22.674 19.946  1.00 27.42  ? 33  LEU A O   1 
ATOM   271  C  CB  . LEU A 1 33  ? 36.500 22.504 20.394  1.00 16.55  ? 33  LEU A CB  1 
ATOM   272  C  CG  . LEU A 1 33  ? 37.549 21.483 20.837  1.00 17.65  ? 33  LEU A CG  1 
ATOM   273  C  CD1 . LEU A 1 33  ? 38.857 22.204 21.129  1.00 16.75  ? 33  LEU A CD1 1 
ATOM   274  C  CD2 . LEU A 1 33  ? 37.057 20.812 22.110  1.00 18.95  ? 33  LEU A CD2 1 
ATOM   275  N  N   . THR A 1 34  ? 34.468 23.783 18.439  1.00 19.63  ? 34  THR A N   1 
ATOM   276  C  CA  . THR A 1 34  ? 33.441 24.760 18.162  1.00 41.85  ? 34  THR A CA  1 
ATOM   277  C  C   . THR A 1 34  ? 33.597 25.458 16.839  1.00 24.47  ? 34  THR A C   1 
ATOM   278  O  O   . THR A 1 34  ? 34.714 25.576 16.346  1.00 33.45  ? 34  THR A O   1 
ATOM   279  C  CB  . THR A 1 34  ? 33.333 25.828 19.278  1.00 37.52  ? 34  THR A CB  1 
ATOM   280  O  OG1 . THR A 1 34  ? 32.405 26.776 18.824  1.00 32.97  ? 34  THR A OG1 1 
ATOM   281  C  CG2 . THR A 1 34  ? 34.675 26.501 19.643  1.00 17.66  ? 34  THR A CG2 1 
ATOM   282  N  N   . LYS A 1 35  ? 32.471 25.955 16.301  1.00 26.43  ? 35  LYS A N   1 
ATOM   283  C  CA  . LYS A 1 35  ? 32.505 26.712 15.039  1.00 40.91  ? 35  LYS A CA  1 
ATOM   284  C  C   . LYS A 1 35  ? 32.784 28.205 15.295  1.00 28.14  ? 35  LYS A C   1 
ATOM   285  O  O   . LYS A 1 35  ? 33.087 28.982 14.393  1.00 42.53  ? 35  LYS A O   1 
ATOM   286  C  CB  . LYS A 1 35  ? 31.265 26.543 14.179  1.00 37.86  ? 35  LYS A CB  1 
ATOM   287  C  CG  . LYS A 1 35  ? 30.891 25.101 13.844  1.00 60.21  ? 35  LYS A CG  1 
ATOM   288  C  CD  . LYS A 1 35  ? 30.417 24.907 12.399  1.00 43.05  ? 35  LYS A CD  1 
ATOM   289  C  CE  . LYS A 1 35  ? 29.186 24.017 12.243  1.00 76.99  ? 35  LYS A CE  1 
ATOM   290  N  NZ  . LYS A 1 35  ? 28.205 24.507 11.245  1.00 100.00 ? 35  LYS A NZ  1 
ATOM   291  N  N   . SER A 1 36  ? 32.723 28.588 16.562  1.00 41.95  ? 36  SER A N   1 
ATOM   292  C  CA  . SER A 1 36  ? 32.979 29.948 17.033  1.00 23.68  ? 36  SER A CA  1 
ATOM   293  C  C   . SER A 1 36  ? 34.431 30.395 16.929  1.00 39.52  ? 36  SER A C   1 
ATOM   294  O  O   . SER A 1 36  ? 35.396 29.698 17.267  1.00 29.78  ? 36  SER A O   1 
ATOM   295  C  CB  . SER A 1 36  ? 32.432 30.219 18.448  1.00 28.61  ? 36  SER A CB  1 
ATOM   296  O  OG  . SER A 1 36  ? 33.322 31.039 19.200  1.00 53.15  ? 36  SER A OG  1 
ATOM   297  N  N   . PRO A 1 37  ? 34.548 31.643 16.504  1.00 55.50  ? 37  PRO A N   1 
ATOM   298  C  CA  . PRO A 1 37  ? 35.797 32.338 16.293  1.00 36.96  ? 37  PRO A CA  1 
ATOM   299  C  C   . PRO A 1 37  ? 36.573 32.566 17.567  1.00 45.79  ? 37  PRO A C   1 
ATOM   300  O  O   . PRO A 1 37  ? 37.761 32.948 17.550  1.00 57.36  ? 37  PRO A O   1 
ATOM   301  C  CB  . PRO A 1 37  ? 35.409 33.672 15.690  1.00 53.26  ? 37  PRO A CB  1 
ATOM   302  C  CG  . PRO A 1 37  ? 33.929 33.607 15.334  1.00 56.60  ? 37  PRO A CG  1 
ATOM   303  C  CD  . PRO A 1 37  ? 33.377 32.340 15.935  1.00 54.94  ? 37  PRO A CD  1 
ATOM   304  N  N   . SER A 1 38  ? 35.903 32.252 18.674  1.00 41.82  ? 38  SER A N   1 
ATOM   305  C  CA  . SER A 1 38  ? 36.472 32.427 19.997  1.00 31.86  ? 38  SER A CA  1 
ATOM   306  C  C   . SER A 1 38  ? 37.301 31.273 20.627  1.00 28.27  ? 38  SER A C   1 
ATOM   307  O  O   . SER A 1 38  ? 36.803 30.167 20.894  1.00 45.20  ? 38  SER A O   1 
ATOM   308  C  CB  . SER A 1 38  ? 35.384 32.907 20.951  1.00 48.35  ? 38  SER A CB  1 
ATOM   309  O  OG  . SER A 1 38  ? 35.982 33.189 22.205  1.00 61.71  ? 38  SER A OG  1 
ATOM   310  N  N   . LEU A 1 39  ? 38.567 31.588 20.960  1.00 31.69  ? 39  LEU A N   1 
ATOM   311  C  CA  . LEU A 1 39  ? 39.480 30.650 21.608  1.00 35.66  ? 39  LEU A CA  1 
ATOM   312  C  C   . LEU A 1 39  ? 39.041 30.292 23.020  1.00 34.63  ? 39  LEU A C   1 
ATOM   313  O  O   . LEU A 1 39  ? 39.260 29.183 23.535  1.00 26.58  ? 39  LEU A O   1 
ATOM   314  C  CB  . LEU A 1 39  ? 40.948 31.118 21.579  1.00 32.48  ? 39  LEU A CB  1 
ATOM   315  C  CG  . LEU A 1 39  ? 41.904 29.998 22.006  1.00 38.96  ? 39  LEU A CG  1 
ATOM   316  C  CD1 . LEU A 1 39  ? 41.979 28.907 20.952  1.00 37.75  ? 39  LEU A CD1 1 
ATOM   317  C  CD2 . LEU A 1 39  ? 43.296 30.548 22.202  1.00 27.27  ? 39  LEU A CD2 1 
ATOM   318  N  N   . ASN A 1 40  ? 38.418 31.261 23.653  1.00 30.95  ? 40  ASN A N   1 
ATOM   319  C  CA  . ASN A 1 40  ? 37.918 31.047 24.983  1.00 38.25  ? 40  ASN A CA  1 
ATOM   320  C  C   . ASN A 1 40  ? 36.736 30.132 24.894  1.00 26.26  ? 40  ASN A C   1 
ATOM   321  O  O   . ASN A 1 40  ? 36.593 29.176 25.662  1.00 36.27  ? 40  ASN A O   1 
ATOM   322  C  CB  . ASN A 1 40  ? 37.562 32.346 25.720  1.00 47.30  ? 40  ASN A CB  1 
ATOM   323  C  CG  . ASN A 1 40  ? 38.822 33.069 26.115  1.00 44.64  ? 40  ASN A CG  1 
ATOM   324  O  OD1 . ASN A 1 40  ? 39.910 32.454 26.194  1.00 83.05  ? 40  ASN A OD1 1 
ATOM   325  N  ND2 . ASN A 1 40  ? 38.701 34.380 26.295  1.00 100.00 ? 40  ASN A ND2 1 
ATOM   326  N  N   . ALA A 1 41  ? 35.919 30.404 23.902  1.00 20.55  ? 41  ALA A N   1 
ATOM   327  C  CA  . ALA A 1 41  ? 34.787 29.540 23.745  1.00 20.29  ? 41  ALA A CA  1 
ATOM   328  C  C   . ALA A 1 41  ? 35.293 28.115 23.553  1.00 34.72  ? 41  ALA A C   1 
ATOM   329  O  O   . ALA A 1 41  ? 34.770 27.156 24.120  1.00 29.56  ? 41  ALA A O   1 
ATOM   330  C  CB  . ALA A 1 41  ? 33.899 29.981 22.608  1.00 21.87  ? 41  ALA A CB  1 
ATOM   331  N  N   . ALA A 1 42  ? 36.335 28.000 22.754  1.00 27.60  ? 42  ALA A N   1 
ATOM   332  C  CA  . ALA A 1 42  ? 36.914 26.711 22.483  1.00 26.82  ? 42  ALA A CA  1 
ATOM   333  C  C   . ALA A 1 42  ? 37.530 26.107 23.737  1.00 23.34  ? 42  ALA A C   1 
ATOM   334  O  O   . ALA A 1 42  ? 37.382 24.888 23.977  1.00 16.61  ? 42  ALA A O   1 
ATOM   335  C  CB  . ALA A 1 42  ? 37.892 26.769 21.314  1.00 23.95  ? 42  ALA A CB  1 
ATOM   336  N  N   . LYS A 1 43  ? 38.222 26.933 24.562  1.00 20.05  ? 43  LYS A N   1 
ATOM   337  C  CA  . LYS A 1 43  ? 38.821 26.364 25.783  1.00 15.70  ? 43  LYS A CA  1 
ATOM   338  C  C   . LYS A 1 43  ? 37.741 25.840 26.718  1.00 19.42  ? 43  LYS A C   1 
ATOM   339  O  O   . LYS A 1 43  ? 37.811 24.750 27.293  1.00 24.17  ? 43  LYS A O   1 
ATOM   340  C  CB  . LYS A 1 43  ? 39.822 27.233 26.505  1.00 20.61  ? 43  LYS A CB  1 
ATOM   341  C  CG  . LYS A 1 43  ? 40.980 27.742 25.662  1.00 35.12  ? 43  LYS A CG  1 
ATOM   342  C  CD  . LYS A 1 43  ? 41.824 28.809 26.377  1.00 82.84  ? 43  LYS A CD  1 
ATOM   343  C  CE  . LYS A 1 43  ? 43.338 28.623 26.235  1.00 100.00 ? 43  LYS A CE  1 
ATOM   344  N  NZ  . LYS A 1 43  ? 44.128 29.041 27.416  1.00 92.00  ? 43  LYS A NZ  1 
ATOM   345  N  N   . SER A 1 44  ? 36.676 26.595 26.772  1.00 18.67  ? 44  SER A N   1 
ATOM   346  C  CA  . SER A 1 44  ? 35.559 26.195 27.586  1.00 29.85  ? 44  SER A CA  1 
ATOM   347  C  C   . SER A 1 44  ? 34.960 24.879 27.088  1.00 29.75  ? 44  SER A C   1 
ATOM   348  O  O   . SER A 1 44  ? 34.646 23.969 27.865  1.00 29.91  ? 44  SER A O   1 
ATOM   349  C  CB  . SER A 1 44  ? 34.540 27.329 27.776  1.00 21.49  ? 44  SER A CB  1 
ATOM   350  O  OG  . SER A 1 44  ? 33.269 26.782 28.083  1.00 67.09  ? 44  SER A OG  1 
ATOM   351  N  N   . GLU A 1 45  ? 34.838 24.773 25.767  1.00 38.92  ? 45  GLU A N   1 
ATOM   352  C  CA  . GLU A 1 45  ? 34.338 23.564 25.179  1.00 22.69  ? 45  GLU A CA  1 
ATOM   353  C  C   . GLU A 1 45  ? 35.263 22.420 25.526  1.00 19.51  ? 45  GLU A C   1 
ATOM   354  O  O   . GLU A 1 45  ? 34.811 21.381 25.925  1.00 24.22  ? 45  GLU A O   1 
ATOM   355  C  CB  . GLU A 1 45  ? 34.121 23.689 23.683  1.00 19.09  ? 45  GLU A CB  1 
ATOM   356  C  CG  . GLU A 1 45  ? 32.891 24.545 23.370  1.00 19.84  ? 45  GLU A CG  1 
ATOM   357  C  CD  . GLU A 1 45  ? 31.584 23.933 23.847  1.00 30.47  ? 45  GLU A CD  1 
ATOM   358  O  OE1 . GLU A 1 45  ? 31.262 22.776 23.678  1.00 32.24  ? 45  GLU A OE1 1 
ATOM   359  O  OE2 . GLU A 1 45  ? 30.772 24.791 24.399  1.00 38.70  ? 45  GLU A OE2 1 
ATOM   360  N  N   . LEU A 1 46  ? 36.557 22.628 25.451  1.00 16.58  ? 46  LEU A N   1 
ATOM   361  C  CA  . LEU A 1 46  ? 37.502 21.577 25.804  1.00 23.73  ? 46  LEU A CA  1 
ATOM   362  C  C   . LEU A 1 46  ? 37.382 21.065 27.262  1.00 27.32  ? 46  LEU A C   1 
ATOM   363  O  O   . LEU A 1 46  ? 37.422 19.853 27.543  1.00 20.70  ? 46  LEU A O   1 
ATOM   364  C  CB  . LEU A 1 46  ? 38.951 22.069 25.535  1.00 14.88  ? 46  LEU A CB  1 
ATOM   365  C  CG  . LEU A 1 46  ? 40.002 21.017 25.834  1.00 19.74  ? 46  LEU A CG  1 
ATOM   366  C  CD1 . LEU A 1 46  ? 39.696 19.760 25.055  1.00 17.05  ? 46  LEU A CD1 1 
ATOM   367  C  CD2 . LEU A 1 46  ? 41.380 21.530 25.450  1.00 17.49  ? 46  LEU A CD2 1 
ATOM   368  N  N   . ASP A 1 47  ? 37.274 21.999 28.222  1.00 20.03  ? 47  ASP A N   1 
ATOM   369  C  CA  . ASP A 1 47  ? 37.196 21.612 29.630  1.00 28.68  ? 47  ASP A CA  1 
ATOM   370  C  C   . ASP A 1 47  ? 35.970 20.814 29.953  1.00 18.02  ? 47  ASP A C   1 
ATOM   371  O  O   . ASP A 1 47  ? 36.042 19.822 30.673  1.00 21.32  ? 47  ASP A O   1 
ATOM   372  C  CB  . ASP A 1 47  ? 37.375 22.764 30.606  1.00 23.55  ? 47  ASP A CB  1 
ATOM   373  C  CG  . ASP A 1 47  ? 38.710 23.432 30.488  1.00 37.60  ? 47  ASP A CG  1 
ATOM   374  O  OD1 . ASP A 1 47  ? 39.723 22.929 30.024  1.00 31.92  ? 47  ASP A OD1 1 
ATOM   375  O  OD2 . ASP A 1 47  ? 38.648 24.640 30.922  1.00 30.28  ? 47  ASP A OD2 1 
ATOM   376  N  N   . LYS A 1 48  ? 34.855 21.251 29.364  1.00 20.23  ? 48  LYS A N   1 
ATOM   377  C  CA  . LYS A 1 48  ? 33.566 20.583 29.478  1.00 19.43  ? 48  LYS A CA  1 
ATOM   378  C  C   . LYS A 1 48  ? 33.649 19.119 28.893  1.00 22.33  ? 48  LYS A C   1 
ATOM   379  O  O   . LYS A 1 48  ? 33.130 18.124 29.421  1.00 27.82  ? 48  LYS A O   1 
ATOM   380  C  CB  . LYS A 1 48  ? 32.608 21.481 28.699  1.00 16.42  ? 48  LYS A CB  1 
ATOM   381  C  CG  . LYS A 1 48  ? 31.223 20.945 28.470  1.00 18.56  ? 48  LYS A CG  1 
ATOM   382  C  CD  . LYS A 1 48  ? 30.186 22.057 28.388  1.00 28.71  ? 48  LYS A CD  1 
ATOM   383  C  CE  . LYS A 1 48  ? 29.959 22.620 26.993  1.00 30.55  ? 48  LYS A CE  1 
ATOM   384  N  NZ  . LYS A 1 48  ? 29.794 21.605 25.937  1.00 19.85  ? 48  LYS A NZ  1 
ATOM   385  N  N   . ALA A 1 49  ? 34.362 18.986 27.789  1.00 21.24  ? 49  ALA A N   1 
ATOM   386  C  CA  . ALA A 1 49  ? 34.529 17.722 27.121  1.00 14.04  ? 49  ALA A CA  1 
ATOM   387  C  C   . ALA A 1 49  ? 35.418 16.794 27.914  1.00 18.33  ? 49  ALA A C   1 
ATOM   388  O  O   . ALA A 1 49  ? 35.162 15.601 28.003  1.00 18.22  ? 49  ALA A O   1 
ATOM   389  C  CB  . ALA A 1 49  ? 35.222 17.978 25.797  1.00 17.14  ? 49  ALA A CB  1 
ATOM   390  N  N   . ILE A 1 50  ? 36.496 17.358 28.442  1.00 22.98  ? 50  ILE A N   1 
ATOM   391  C  CA  . ILE A 1 50  ? 37.493 16.593 29.159  1.00 22.26  ? 50  ILE A CA  1 
ATOM   392  C  C   . ILE A 1 50  ? 37.114 16.391 30.625  1.00 26.06  ? 50  ILE A C   1 
ATOM   393  O  O   . ILE A 1 50  ? 37.493 15.409 31.275  1.00 27.39  ? 50  ILE A O   1 
ATOM   394  C  CB  . ILE A 1 50  ? 38.879 17.301 29.035  1.00 19.97  ? 50  ILE A CB  1 
ATOM   395  C  CG1 . ILE A 1 50  ? 39.283 17.340 27.568  1.00 27.44  ? 50  ILE A CG1 1 
ATOM   396  C  CG2 . ILE A 1 50  ? 39.933 16.480 29.756  1.00 23.37  ? 50  ILE A CG2 1 
ATOM   397  C  CD1 . ILE A 1 50  ? 39.192 15.925 27.002  1.00 22.09  ? 50  ILE A CD1 1 
ATOM   398  N  N   . GLY A 1 51  ? 36.402 17.356 31.166  1.00 27.06  ? 51  GLY A N   1 
ATOM   399  C  CA  . GLY A 1 51  ? 36.049 17.265 32.565  1.00 24.07  ? 51  GLY A CA  1 
ATOM   400  C  C   . GLY A 1 51  ? 37.134 17.837 33.490  1.00 29.95  ? 51  GLY A C   1 
ATOM   401  O  O   . GLY A 1 51  ? 37.284 17.392 34.621  1.00 29.03  ? 51  GLY A O   1 
ATOM   402  N  N   . ARG A 1 52  ? 37.893 18.830 33.035  1.00 35.71  ? 52  ARG A N   1 
ATOM   403  C  CA  . ARG A 1 52  ? 38.930 19.423 33.862  1.00 19.17  ? 52  ARG A CA  1 
ATOM   404  C  C   . ARG A 1 52  ? 39.434 20.691 33.242  1.00 20.10  ? 52  ARG A C   1 
ATOM   405  O  O   . ARG A 1 52  ? 39.171 20.985 32.071  1.00 24.52  ? 52  ARG A O   1 
ATOM   406  C  CB  . ARG A 1 52  ? 40.091 18.478 34.147  1.00 26.67  ? 52  ARG A CB  1 
ATOM   407  C  CG  . ARG A 1 52  ? 41.114 18.331 33.018  1.00 33.51  ? 52  ARG A CG  1 
ATOM   408  C  CD  . ARG A 1 52  ? 42.115 17.211 33.280  1.00 23.92  ? 52  ARG A CD  1 
ATOM   409  N  NE  . ARG A 1 52  ? 43.037 16.975 32.164  1.00 24.23  ? 52  ARG A NE  1 
ATOM   410  C  CZ  . ARG A 1 52  ? 43.911 17.868 31.714  1.00 38.82  ? 52  ARG A CZ  1 
ATOM   411  N  NH1 . ARG A 1 52  ? 44.009 19.073 32.246  1.00 36.85  ? 52  ARG A NH1 1 
ATOM   412  N  NH2 . ARG A 1 52  ? 44.715 17.550 30.708  1.00 28.35  ? 52  ARG A NH2 1 
ATOM   413  N  N   . ASN A 1 53  ? 40.124 21.465 34.044  1.00 27.70  ? 53  ASN A N   1 
ATOM   414  C  CA  . ASN A 1 53  ? 40.682 22.702 33.558  1.00 24.69  ? 53  ASN A CA  1 
ATOM   415  C  C   . ASN A 1 53  ? 41.878 22.329 32.730  1.00 32.05  ? 53  ASN A C   1 
ATOM   416  O  O   . ASN A 1 53  ? 42.890 21.905 33.273  1.00 34.54  ? 53  ASN A O   1 
ATOM   417  C  CB  . ASN A 1 53  ? 41.088 23.654 34.694  1.00 32.55  ? 53  ASN A CB  1 
ATOM   418  C  CG  . ASN A 1 53  ? 40.241 24.902 34.662  1.00 60.68  ? 53  ASN A CG  1 
ATOM   419  O  OD1 . ASN A 1 53  ? 39.005 24.837 34.820  1.00 91.86  ? 53  ASN A OD1 1 
ATOM   420  N  ND2 . ASN A 1 53  ? 40.891 26.035 34.390  1.00 58.49  ? 53  ASN A ND2 1 
ATOM   421  N  N   . THR A 1 54  ? 41.737 22.402 31.413  1.00 26.64  ? 54  THR A N   1 
ATOM   422  C  CA  . THR A 1 54  ? 42.824 21.984 30.572  1.00 29.23  ? 54  THR A CA  1 
ATOM   423  C  C   . THR A 1 54  ? 43.820 23.032 30.228  1.00 32.47  ? 54  THR A C   1 
ATOM   424  O  O   . THR A 1 54  ? 44.979 22.707 29.996  1.00 48.79  ? 54  THR A O   1 
ATOM   425  C  CB  . THR A 1 54  ? 42.357 21.350 29.276  1.00 18.42  ? 54  THR A CB  1 
ATOM   426  O  OG1 . THR A 1 54  ? 41.593 22.282 28.535  1.00 32.08  ? 54  THR A OG1 1 
ATOM   427  C  CG2 . THR A 1 54  ? 41.591 20.090 29.610  1.00 17.98  ? 54  THR A CG2 1 
ATOM   428  N  N   . ASN A 1 55  ? 43.385 24.257 30.085  1.00 32.44  ? 55  ASN A N   1 
ATOM   429  C  CA  . ASN A 1 55  ? 44.384 25.188 29.667  1.00 57.95  ? 55  ASN A CA  1 
ATOM   430  C  C   . ASN A 1 55  ? 44.790 24.898 28.201  1.00 100.00 ? 55  ASN A C   1 
ATOM   431  O  O   . ASN A 1 55  ? 45.883 25.232 27.724  1.00 55.25  ? 55  ASN A O   1 
ATOM   432  C  CB  . ASN A 1 55  ? 45.522 25.261 30.722  1.00 42.19  ? 55  ASN A CB  1 
ATOM   433  C  CG  . ASN A 1 55  ? 46.955 25.509 30.281  1.00 100.00 ? 55  ASN A CG  1 
ATOM   434  O  OD1 . ASN A 1 55  ? 47.339 26.686 30.109  1.00 100.00 ? 55  ASN A OD1 1 
ATOM   435  N  ND2 . ASN A 1 55  ? 47.771 24.423 30.210  1.00 50.77  ? 55  ASN A ND2 1 
ATOM   436  N  N   . GLY A 1 56  ? 43.867 24.248 27.467  1.00 36.39  ? 56  GLY A N   1 
ATOM   437  C  CA  . GLY A 1 56  ? 43.999 23.967 26.025  1.00 29.86  ? 56  GLY A CA  1 
ATOM   438  C  C   . GLY A 1 56  ? 44.959 22.879 25.540  1.00 19.23  ? 56  GLY A C   1 
ATOM   439  O  O   . GLY A 1 56  ? 45.233 22.790 24.348  1.00 27.88  ? 56  GLY A O   1 
ATOM   440  N  N   . VAL A 1 57  ? 45.445 22.057 26.454  1.00 20.12  ? 57  VAL A N   1 
ATOM   441  C  CA  . VAL A 1 57  ? 46.337 20.979 26.141  1.00 20.31  ? 57  VAL A CA  1 
ATOM   442  C  C   . VAL A 1 57  ? 45.787 19.700 26.764  1.00 34.69  ? 57  VAL A C   1 
ATOM   443  O  O   . VAL A 1 57  ? 45.376 19.697 27.914  1.00 28.80  ? 57  VAL A O   1 
ATOM   444  C  CB  . VAL A 1 57  ? 47.733 21.308 26.690  1.00 20.12  ? 57  VAL A CB  1 
ATOM   445  C  CG1 . VAL A 1 57  ? 48.737 20.212 26.343  1.00 23.37  ? 57  VAL A CG1 1 
ATOM   446  C  CG2 . VAL A 1 57  ? 48.193 22.581 26.007  1.00 43.38  ? 57  VAL A CG2 1 
ATOM   447  N  N   . ILE A 1 58  ? 45.739 18.604 26.024  1.00 25.90  ? 58  ILE A N   1 
ATOM   448  C  CA  . ILE A 1 58  ? 45.242 17.367 26.616  1.00 15.95  ? 58  ILE A CA  1 
ATOM   449  C  C   . ILE A 1 58  ? 46.308 16.340 26.492  1.00 14.97  ? 58  ILE A C   1 
ATOM   450  O  O   . ILE A 1 58  ? 47.360 16.603 25.882  1.00 20.80  ? 58  ILE A O   1 
ATOM   451  C  CB  . ILE A 1 58  ? 43.939 16.881 26.007  1.00 22.84  ? 58  ILE A CB  1 
ATOM   452  C  CG1 . ILE A 1 58  ? 44.169 16.579 24.525  1.00 20.62  ? 58  ILE A CG1 1 
ATOM   453  C  CG2 . ILE A 1 58  ? 42.851 17.954 26.172  1.00 18.75  ? 58  ILE A CG2 1 
ATOM   454  C  CD1 . ILE A 1 58  ? 43.006 15.823 23.893  1.00 17.96  ? 58  ILE A CD1 1 
ATOM   455  N  N   . THR A 1 59  ? 46.068 15.184 27.089  1.00 19.85  ? 59  THR A N   1 
ATOM   456  C  CA  . THR A 1 59  ? 47.017 14.109 26.979  1.00 17.43  ? 59  THR A CA  1 
ATOM   457  C  C   . THR A 1 59  ? 46.589 13.149 25.868  1.00 25.28  ? 59  THR A C   1 
ATOM   458  O  O   . THR A 1 59  ? 45.443 13.133 25.406  1.00 21.28  ? 59  THR A O   1 
ATOM   459  C  CB  . THR A 1 59  ? 47.146 13.320 28.289  1.00 29.53  ? 59  THR A CB  1 
ATOM   460  O  OG1 . THR A 1 59  ? 46.001 12.506 28.490  1.00 24.43  ? 59  THR A OG1 1 
ATOM   461  C  CG2 . THR A 1 59  ? 47.321 14.290 29.432  1.00 32.09  ? 59  THR A CG2 1 
ATOM   462  N  N   . LYS A 1 60  ? 47.521 12.304 25.490  1.00 20.01  ? 60  LYS A N   1 
ATOM   463  C  CA  . LYS A 1 60  ? 47.286 11.325 24.465  1.00 21.32  ? 60  LYS A CA  1 
ATOM   464  C  C   . LYS A 1 60  ? 46.142 10.458 24.857  1.00 18.13  ? 60  LYS A C   1 
ATOM   465  O  O   . LYS A 1 60  ? 45.264 10.118 24.057  1.00 21.84  ? 60  LYS A O   1 
ATOM   466  C  CB  . LYS A 1 60  ? 48.532 10.473 24.207  1.00 28.83  ? 60  LYS A CB  1 
ATOM   467  C  CG  . LYS A 1 60  ? 48.503 9.664  22.908  1.00 49.45  ? 60  LYS A CG  1 
ATOM   468  C  CD  . LYS A 1 60  ? 49.879 9.511  22.245  1.00 95.81  ? 60  LYS A CD  1 
ATOM   469  C  CE  . LYS A 1 60  ? 49.904 8.515  21.079  1.00 100.00 ? 60  LYS A CE  1 
ATOM   470  N  NZ  . LYS A 1 60  ? 50.413 9.067  19.800  1.00 100.00 ? 60  LYS A NZ  1 
ATOM   471  N  N   . ASP A 1 61  ? 46.161 10.076 26.114  1.00 26.21  ? 61  ASP A N   1 
ATOM   472  C  CA  . ASP A 1 61  ? 45.103 9.233  26.597  1.00 18.61  ? 61  ASP A CA  1 
ATOM   473  C  C   . ASP A 1 61  ? 43.768 9.960  26.497  1.00 22.17  ? 61  ASP A C   1 
ATOM   474  O  O   . ASP A 1 61  ? 42.738 9.345  26.179  1.00 21.06  ? 61  ASP A O   1 
ATOM   475  C  CB  . ASP A 1 61  ? 45.345 8.786  28.047  1.00 20.10  ? 61  ASP A CB  1 
ATOM   476  C  CG  . ASP A 1 61  ? 46.590 7.957  28.129  1.00 70.92  ? 61  ASP A CG  1 
ATOM   477  O  OD1 . ASP A 1 61  ? 47.002 7.267  27.203  1.00 64.89  ? 61  ASP A OD1 1 
ATOM   478  O  OD2 . ASP A 1 61  ? 47.212 8.103  29.277  1.00 100.00 ? 61  ASP A OD2 1 
ATOM   479  N  N   . GLU A 1 62  ? 43.794 11.277 26.775  1.00 21.30  ? 62  GLU A N   1 
ATOM   480  C  CA  . GLU A 1 62  ? 42.578 12.084 26.699  1.00 20.27  ? 62  GLU A CA  1 
ATOM   481  C  C   . GLU A 1 62  ? 42.033 12.152 25.287  1.00 22.32  ? 62  GLU A C   1 
ATOM   482  O  O   . GLU A 1 62  ? 40.832 11.966 25.079  1.00 19.99  ? 62  GLU A O   1 
ATOM   483  C  CB  . GLU A 1 62  ? 42.772 13.469 27.293  1.00 14.12  ? 62  GLU A CB  1 
ATOM   484  C  CG  . GLU A 1 62  ? 42.794 13.348 28.819  1.00 21.68  ? 62  GLU A CG  1 
ATOM   485  C  CD  . GLU A 1 62  ? 43.243 14.610 29.470  1.00 18.39  ? 62  GLU A CD  1 
ATOM   486  O  OE1 . GLU A 1 62  ? 43.795 15.500 28.853  1.00 32.73  ? 62  GLU A OE1 1 
ATOM   487  O  OE2 . GLU A 1 62  ? 42.862 14.691 30.715  1.00 32.39  ? 62  GLU A OE2 1 
ATOM   488  N  N   . ALA A 1 63  ? 42.966 12.375 24.337  1.00 15.14  ? 63  ALA A N   1 
ATOM   489  C  CA  . ALA A 1 63  ? 42.646 12.439 22.910  1.00 22.83  ? 63  ALA A CA  1 
ATOM   490  C  C   . ALA A 1 63  ? 41.999 11.146 22.404  1.00 20.24  ? 63  ALA A C   1 
ATOM   491  O  O   . ALA A 1 63  ? 41.083 11.160 21.581  1.00 18.73  ? 63  ALA A O   1 
ATOM   492  C  CB  . ALA A 1 63  ? 43.880 12.777 22.092  1.00 17.42  ? 63  ALA A CB  1 
ATOM   493  N  N   . GLU A 1 64  ? 42.502 10.027 22.901  1.00 23.64  ? 64  GLU A N   1 
ATOM   494  C  CA  . GLU A 1 64  ? 42.029 8.726  22.531  1.00 14.15  ? 64  GLU A CA  1 
ATOM   495  C  C   . GLU A 1 64  ? 40.683 8.419  23.068  1.00 19.29  ? 64  GLU A C   1 
ATOM   496  O  O   . GLU A 1 64  ? 39.885 7.783  22.389  1.00 13.48  ? 64  GLU A O   1 
ATOM   497  C  CB  . GLU A 1 64  ? 43.034 7.629  22.839  1.00 21.98  ? 64  GLU A CB  1 
ATOM   498  C  CG  . GLU A 1 64  ? 44.078 7.595  21.722  1.00 40.91  ? 64  GLU A CG  1 
ATOM   499  C  CD  . GLU A 1 64  ? 45.210 6.742  22.119  1.00 63.87  ? 64  GLU A CD  1 
ATOM   500  O  OE1 . GLU A 1 64  ? 45.290 6.263  23.235  1.00 54.14  ? 64  GLU A OE1 1 
ATOM   501  O  OE2 . GLU A 1 64  ? 46.061 6.571  21.150  1.00 45.87  ? 64  GLU A OE2 1 
ATOM   502  N  N   . LYS A 1 65  ? 40.384 8.956  24.235  1.00 15.30  ? 65  LYS A N   1 
ATOM   503  C  CA  . LYS A 1 65  ? 39.040 8.747  24.793  1.00 15.53  ? 65  LYS A CA  1 
ATOM   504  C  C   . LYS A 1 65  ? 38.012 9.544  24.003  1.00 13.64  ? 65  LYS A C   1 
ATOM   505  O  O   . LYS A 1 65  ? 36.921 9.053  23.704  1.00 20.24  ? 65  LYS A O   1 
ATOM   506  C  CB  . LYS A 1 65  ? 38.935 9.151  26.263  1.00 19.11  ? 65  LYS A CB  1 
ATOM   507  C  CG  . LYS A 1 65  ? 37.648 8.649  26.930  1.00 60.26  ? 65  LYS A CG  1 
ATOM   508  C  CD  . LYS A 1 65  ? 37.383 9.291  28.297  1.00 100.00 ? 65  LYS A CD  1 
ATOM   509  C  CE  . LYS A 1 65  ? 36.586 8.415  29.264  1.00 100.00 ? 65  LYS A CE  1 
ATOM   510  N  NZ  . LYS A 1 65  ? 36.534 8.963  30.629  1.00 72.33  ? 65  LYS A NZ  1 
ATOM   511  N  N   . LEU A 1 66  ? 38.358 10.789 23.641  1.00 18.41  ? 66  LEU A N   1 
ATOM   512  C  CA  . LEU A 1 66  ? 37.432 11.587 22.827  1.00 11.06  ? 66  LEU A CA  1 
ATOM   513  C  C   . LEU A 1 66  ? 37.199 10.869 21.474  1.00 14.19  ? 66  LEU A C   1 
ATOM   514  O  O   . LEU A 1 66  ? 36.099 10.782 20.987  1.00 15.58  ? 66  LEU A O   1 
ATOM   515  C  CB  . LEU A 1 66  ? 38.029 12.961 22.490  1.00 16.68  ? 66  LEU A CB  1 
ATOM   516  C  CG  . LEU A 1 66  ? 38.069 13.923 23.658  1.00 24.53  ? 66  LEU A CG  1 
ATOM   517  C  CD1 . LEU A 1 66  ? 38.615 15.264 23.202  1.00 23.88  ? 66  LEU A CD1 1 
ATOM   518  C  CD2 . LEU A 1 66  ? 36.658 14.088 24.179  1.00 25.69  ? 66  LEU A CD2 1 
ATOM   519  N  N   . PHE A 1 67  ? 38.261 10.358 20.886  1.00 15.77  ? 67  PHE A N   1 
ATOM   520  C  CA  . PHE A 1 67  ? 38.214 9.651  19.621  1.00 18.32  ? 67  PHE A CA  1 
ATOM   521  C  C   . PHE A 1 67  ? 37.293 8.409  19.680  1.00 18.69  ? 67  PHE A C   1 
ATOM   522  O  O   . PHE A 1 67  ? 36.439 8.176  18.790  1.00 14.87  ? 67  PHE A O   1 
ATOM   523  C  CB  . PHE A 1 67  ? 39.659 9.330  19.199  1.00 15.40  ? 67  PHE A CB  1 
ATOM   524  C  CG  . PHE A 1 67  ? 39.837 8.612  17.876  1.00 20.91  ? 67  PHE A CG  1 
ATOM   525  C  CD1 . PHE A 1 67  ? 39.134 9.016  16.737  1.00 22.12  ? 67  PHE A CD1 1 
ATOM   526  C  CD2 . PHE A 1 67  ? 40.741 7.551  17.772  1.00 17.73  ? 67  PHE A CD2 1 
ATOM   527  C  CE1 . PHE A 1 67  ? 39.336 8.395  15.503  1.00 21.66  ? 67  PHE A CE1 1 
ATOM   528  C  CE2 . PHE A 1 67  ? 40.994 6.929  16.552  1.00 18.24  ? 67  PHE A CE2 1 
ATOM   529  C  CZ  . PHE A 1 67  ? 40.264 7.351  15.438  1.00 24.39  ? 67  PHE A CZ  1 
ATOM   530  N  N   . ASN A 1 68  ? 37.422 7.626  20.754  1.00 17.86  ? 68  ASN A N   1 
ATOM   531  C  CA  . ASN A 1 68  ? 36.551 6.471  20.965  1.00 12.23  ? 68  ASN A CA  1 
ATOM   532  C  C   . ASN A 1 68  ? 35.082 6.890  20.988  1.00 11.91  ? 68  ASN A C   1 
ATOM   533  O  O   . ASN A 1 68  ? 34.171 6.298  20.379  1.00 17.51  ? 68  ASN A O   1 
ATOM   534  C  CB  . ASN A 1 68  ? 36.857 5.775  22.319  1.00 20.62  ? 68  ASN A CB  1 
ATOM   535  C  CG  . ASN A 1 68  ? 38.005 4.801  22.266  1.00 36.89  ? 68  ASN A CG  1 
ATOM   536  O  OD1 . ASN A 1 68  ? 38.126 4.061  21.296  1.00 44.68  ? 68  ASN A OD1 1 
ATOM   537  N  ND2 . ASN A 1 68  ? 38.813 4.759  23.330  1.00 42.18  ? 68  ASN A ND2 1 
ATOM   538  N  N   . GLN A 1 69  ? 34.844 7.947  21.706  1.00 14.08  ? 69  GLN A N   1 
ATOM   539  C  CA  . GLN A 1 69  ? 33.497 8.411  21.776  1.00 11.20  ? 69  GLN A CA  1 
ATOM   540  C  C   . GLN A 1 69  ? 32.943 8.872  20.431  1.00 14.23  ? 69  GLN A C   1 
ATOM   541  O  O   . GLN A 1 69  ? 31.783 8.613  20.072  1.00 19.39  ? 69  GLN A O   1 
ATOM   542  C  CB  . GLN A 1 69  ? 33.385 9.573  22.795  1.00 14.63  ? 69  GLN A CB  1 
ATOM   543  C  CG  . GLN A 1 69  ? 33.695 9.142  24.225  1.00 19.86  ? 69  GLN A CG  1 
ATOM   544  C  CD  . GLN A 1 69  ? 33.854 10.292 25.238  1.00 32.56  ? 69  GLN A CD  1 
ATOM   545  O  OE1 . GLN A 1 69  ? 33.944 10.042 26.425  1.00 26.81  ? 69  GLN A OE1 1 
ATOM   546  N  NE2 . GLN A 1 69  ? 33.871 11.549 24.804  1.00 19.77  ? 69  GLN A NE2 1 
ATOM   547  N  N   . ASP A 1 70  ? 33.753 9.613  19.685  1.00 16.66  ? 70  ASP A N   1 
ATOM   548  C  CA  . ASP A 1 70  ? 33.333 10.165 18.398  1.00 12.89  ? 70  ASP A CA  1 
ATOM   549  C  C   . ASP A 1 70  ? 33.050 9.074  17.361  1.00 11.42  ? 70  ASP A C   1 
ATOM   550  O  O   . ASP A 1 70  ? 32.125 9.205  16.565  1.00 17.33  ? 70  ASP A O   1 
ATOM   551  C  CB  . ASP A 1 70  ? 34.428 11.105 17.865  1.00 13.34  ? 70  ASP A CB  1 
ATOM   552  C  CG  . ASP A 1 70  ? 34.463 12.403 18.589  1.00 23.19  ? 70  ASP A CG  1 
ATOM   553  O  OD1 . ASP A 1 70  ? 33.542 12.732 19.289  1.00 19.48  ? 70  ASP A OD1 1 
ATOM   554  O  OD2 . ASP A 1 70  ? 35.595 13.082 18.423  1.00 20.40  ? 70  ASP A OD2 1 
ATOM   555  N  N   . VAL A 1 71  ? 33.878 8.004  17.368  1.00 11.76  ? 71  VAL A N   1 
ATOM   556  C  CA  . VAL A 1 71  ? 33.665 6.894  16.458  1.00 18.42  ? 71  VAL A CA  1 
ATOM   557  C  C   . VAL A 1 71  ? 32.335 6.242  16.828  1.00 17.07  ? 71  VAL A C   1 
ATOM   558  O  O   . VAL A 1 71  ? 31.391 6.004  15.999  1.00 19.10  ? 71  VAL A O   1 
ATOM   559  C  CB  . VAL A 1 71  ? 34.844 5.894  16.474  1.00 22.49  ? 71  VAL A CB  1 
ATOM   560  C  CG1 . VAL A 1 71  ? 34.519 4.644  15.633  1.00 19.58  ? 71  VAL A CG1 1 
ATOM   561  C  CG2 . VAL A 1 71  ? 36.091 6.565  15.922  1.00 14.15  ? 71  VAL A CG2 1 
ATOM   562  N  N   . ASP A 1 72  ? 32.237 5.986  18.119  1.00 15.80  ? 72  ASP A N   1 
ATOM   563  C  CA  . ASP A 1 72  ? 30.999 5.399  18.597  1.00 18.96  ? 72  ASP A CA  1 
ATOM   564  C  C   . ASP A 1 72  ? 29.814 6.266  18.217  1.00 21.02  ? 72  ASP A C   1 
ATOM   565  O  O   . ASP A 1 72  ? 28.762 5.810  17.805  1.00 19.65  ? 72  ASP A O   1 
ATOM   566  C  CB  . ASP A 1 72  ? 31.030 5.155  20.119  1.00 16.00  ? 72  ASP A CB  1 
ATOM   567  C  CG  . ASP A 1 72  ? 30.010 4.121  20.518  1.00 21.21  ? 72  ASP A CG  1 
ATOM   568  O  OD1 . ASP A 1 72  ? 29.805 3.105  19.906  1.00 65.54  ? 72  ASP A OD1 1 
ATOM   569  O  OD2 . ASP A 1 72  ? 29.324 4.450  21.532  1.00 32.90  ? 72  ASP A OD2 1 
ATOM   570  N  N   . ALA A 1 73  ? 29.938 7.551  18.388  1.00 15.84  ? 73  ALA A N   1 
ATOM   571  C  CA  . ALA A 1 73  ? 28.801 8.381  18.065  1.00 14.42  ? 73  ALA A CA  1 
ATOM   572  C  C   . ALA A 1 73  ? 28.491 8.339  16.587  1.00 32.93  ? 73  ALA A C   1 
ATOM   573  O  O   . ALA A 1 73  ? 27.326 8.416  16.186  1.00 18.53  ? 73  ALA A O   1 
ATOM   574  C  CB  . ALA A 1 73  ? 29.013 9.832  18.502  1.00 13.21  ? 73  ALA A CB  1 
ATOM   575  N  N   . ALA A 1 74  ? 29.542 8.278  15.760  1.00 27.28  ? 74  ALA A N   1 
ATOM   576  C  CA  . ALA A 1 74  ? 29.377 8.236  14.302  1.00 24.48  ? 74  ALA A CA  1 
ATOM   577  C  C   . ALA A 1 74  ? 28.561 7.002  13.886  1.00 23.23  ? 74  ALA A C   1 
ATOM   578  O  O   . ALA A 1 74  ? 27.588 7.078  13.128  1.00 22.86  ? 74  ALA A O   1 
ATOM   579  C  CB  . ALA A 1 74  ? 30.743 8.255  13.602  1.00 16.97  ? 74  ALA A CB  1 
ATOM   580  N  N   . VAL A 1 75  ? 28.960 5.854  14.410  1.00 13.86  ? 75  VAL A N   1 
ATOM   581  C  CA  . VAL A 1 75  ? 28.216 4.644  14.103  1.00 18.21  ? 75  VAL A CA  1 
ATOM   582  C  C   . VAL A 1 75  ? 26.776 4.734  14.531  1.00 28.80  ? 75  VAL A C   1 
ATOM   583  O  O   . VAL A 1 75  ? 25.874 4.418  13.770  1.00 29.30  ? 75  VAL A O   1 
ATOM   584  C  CB  . VAL A 1 75  ? 28.821 3.416  14.739  1.00 29.58  ? 75  VAL A CB  1 
ATOM   585  C  CG1 . VAL A 1 75  ? 28.007 2.170  14.329  1.00 24.32  ? 75  VAL A CG1 1 
ATOM   586  C  CG2 . VAL A 1 75  ? 30.271 3.308  14.284  1.00 30.90  ? 75  VAL A CG2 1 
ATOM   587  N  N   . ARG A 1 76  ? 26.542 5.148  15.758  1.00 19.82  ? 76  ARG A N   1 
ATOM   588  C  CA  . ARG A 1 76  ? 25.178 5.174  16.179  1.00 25.10  ? 76  ARG A CA  1 
ATOM   589  C  C   . ARG A 1 76  ? 24.378 6.229  15.431  1.00 26.13  ? 76  ARG A C   1 
ATOM   590  O  O   . ARG A 1 76  ? 23.236 6.061  15.070  1.00 30.90  ? 76  ARG A O   1 
ATOM   591  C  CB  . ARG A 1 76  ? 25.016 4.989  17.671  1.00 30.61  ? 76  ARG A CB  1 
ATOM   592  C  CG  . ARG A 1 76  ? 25.784 3.741  18.151  1.00 56.35  ? 76  ARG A CG  1 
ATOM   593  C  CD  . ARG A 1 76  ? 25.550 3.343  19.614  1.00 45.85  ? 76  ARG A CD  1 
ATOM   594  N  NE  . ARG A 1 76  ? 26.439 4.010  20.580  1.00 79.60  ? 76  ARG A NE  1 
ATOM   595  C  CZ  . ARG A 1 76  ? 26.526 5.351  20.727  1.00 100.00 ? 76  ARG A CZ  1 
ATOM   596  N  NH1 . ARG A 1 76  ? 25.793 6.207  20.029  1.00 100.00 ? 76  ARG A NH1 1 
ATOM   597  N  NH2 . ARG A 1 76  ? 27.372 5.883  21.594  1.00 61.76  ? 76  ARG A NH2 1 
ATOM   598  N  N   . GLY A 1 77  ? 25.028 7.290  15.054  1.00 15.22  ? 77  GLY A N   1 
ATOM   599  C  CA  . GLY A 1 77  ? 24.334 8.273  14.242  1.00 24.57  ? 77  GLY A CA  1 
ATOM   600  C  C   . GLY A 1 77  ? 23.860 7.658  12.919  1.00 42.77  ? 77  GLY A C   1 
ATOM   601  O  O   . GLY A 1 77  ? 22.794 7.955  12.408  1.00 44.07  ? 77  GLY A O   1 
ATOM   602  N  N   . ILE A 1 78  ? 24.672 6.796  12.341  1.00 27.45  ? 78  ILE A N   1 
ATOM   603  C  CA  . ILE A 1 78  ? 24.328 6.138  11.085  1.00 21.55  ? 78  ILE A CA  1 
ATOM   604  C  C   . ILE A 1 78  ? 23.138 5.211  11.289  1.00 25.30  ? 78  ILE A C   1 
ATOM   605  O  O   . ILE A 1 78  ? 22.189 5.202  10.512  1.00 22.96  ? 78  ILE A O   1 
ATOM   606  C  CB  . ILE A 1 78  ? 25.492 5.304  10.480  1.00 14.36  ? 78  ILE A CB  1 
ATOM   607  C  CG1 . ILE A 1 78  ? 26.440 6.203  9.680   1.00 15.49  ? 78  ILE A CG1 1 
ATOM   608  C  CG2 . ILE A 1 78  ? 24.973 4.187  9.565   1.00 9.32   ? 78  ILE A CG2 1 
ATOM   609  C  CD1 . ILE A 1 78  ? 27.863 5.645  9.662   1.00 13.89  ? 78  ILE A CD1 1 
ATOM   610  N  N   . LEU A 1 79  ? 23.237 4.375  12.322  1.00 24.73  ? 79  LEU A N   1 
ATOM   611  C  CA  . LEU A 1 79  ? 22.218 3.350  12.619  1.00 34.02  ? 79  LEU A CA  1 
ATOM   612  C  C   . LEU A 1 79  ? 20.870 3.910  13.000  1.00 47.17  ? 79  LEU A C   1 
ATOM   613  O  O   . LEU A 1 79  ? 19.884 3.182  13.027  1.00 49.95  ? 79  LEU A O   1 
ATOM   614  C  CB  . LEU A 1 79  ? 22.698 2.286  13.628  1.00 23.14  ? 79  LEU A CB  1 
ATOM   615  C  CG  . LEU A 1 79  ? 23.946 1.565  13.130  1.00 24.65  ? 79  LEU A CG  1 
ATOM   616  C  CD1 . LEU A 1 79  ? 24.409 0.537  14.150  1.00 31.06  ? 79  LEU A CD1 1 
ATOM   617  C  CD2 . LEU A 1 79  ? 23.631 0.848  11.838  1.00 27.56  ? 79  LEU A CD2 1 
ATOM   618  N  N   . ARG A 1 80  ? 20.864 5.211  13.291  1.00 30.22  ? 80  ARG A N   1 
ATOM   619  C  CA  . ARG A 1 80  ? 19.673 5.953  13.667  1.00 48.77  ? 80  ARG A CA  1 
ATOM   620  C  C   . ARG A 1 80  ? 19.170 6.881  12.549  1.00 40.37  ? 80  ARG A C   1 
ATOM   621  O  O   . ARG A 1 80  ? 18.132 7.518  12.658  1.00 57.27  ? 80  ARG A O   1 
ATOM   622  C  CB  . ARG A 1 80  ? 19.871 6.697  15.000  1.00 63.77  ? 80  ARG A CB  1 
ATOM   623  C  CG  . ARG A 1 80  ? 19.338 5.873  16.183  1.00 86.60  ? 80  ARG A CG  1 
ATOM   624  C  CD  . ARG A 1 80  ? 20.331 5.576  17.322  1.00 100.00 ? 80  ARG A CD  1 
ATOM   625  N  NE  . ARG A 1 80  ? 21.241 4.429  17.096  1.00 100.00 ? 80  ARG A NE  1 
ATOM   626  C  CZ  . ARG A 1 80  ? 21.688 3.552  18.034  1.00 100.00 ? 80  ARG A CZ  1 
ATOM   627  N  NH1 . ARG A 1 80  ? 21.350 3.614  19.337  1.00 100.00 ? 80  ARG A NH1 1 
ATOM   628  N  NH2 . ARG A 1 80  ? 22.551 2.600  17.647  1.00 100.00 ? 80  ARG A NH2 1 
ATOM   629  N  N   . ASN A 1 81  ? 19.917 6.993  11.465  1.00 31.61  ? 81  ASN A N   1 
ATOM   630  C  CA  . ASN A 1 81  ? 19.470 7.831  10.406  1.00 18.98  ? 81  ASN A CA  1 
ATOM   631  C  C   . ASN A 1 81  ? 18.693 6.959  9.412   1.00 45.27  ? 81  ASN A C   1 
ATOM   632  O  O   . ASN A 1 81  ? 19.075 5.840  9.068   1.00 31.17  ? 81  ASN A O   1 
ATOM   633  C  CB  . ASN A 1 81  ? 20.614 8.663  9.824   1.00 23.91  ? 81  ASN A CB  1 
ATOM   634  C  CG  . ASN A 1 81  ? 20.118 9.557  8.729   1.00 25.42  ? 81  ASN A CG  1 
ATOM   635  O  OD1 . ASN A 1 81  ? 19.616 9.070  7.720   1.00 42.31  ? 81  ASN A OD1 1 
ATOM   636  N  ND2 . ASN A 1 81  ? 20.280 10.856 8.904   1.00 40.33  ? 81  ASN A ND2 1 
ATOM   637  N  N   . ALA A 1 82  ? 17.538 7.423  9.001   1.00 40.13  ? 82  ALA A N   1 
ATOM   638  C  CA  . ALA A 1 82  ? 16.695 6.630  8.116   1.00 38.38  ? 82  ALA A CA  1 
ATOM   639  C  C   . ALA A 1 82  ? 17.230 6.507  6.701   1.00 27.56  ? 82  ALA A C   1 
ATOM   640  O  O   . ALA A 1 82  ? 17.003 5.522  6.006   1.00 37.98  ? 82  ALA A O   1 
ATOM   641  C  CB  . ALA A 1 82  ? 15.280 7.189  8.122   1.00 45.84  ? 82  ALA A CB  1 
ATOM   642  N  N   . LYS A 1 83  ? 17.921 7.536  6.239   1.00 24.95  ? 83  LYS A N   1 
ATOM   643  C  CA  . LYS A 1 83  ? 18.447 7.415  4.924   1.00 32.29  ? 83  LYS A CA  1 
ATOM   644  C  C   . LYS A 1 83  ? 19.714 6.588  4.974   1.00 42.47  ? 83  LYS A C   1 
ATOM   645  O  O   . LYS A 1 83  ? 19.984 5.804  4.087   1.00 37.18  ? 83  LYS A O   1 
ATOM   646  C  CB  . LYS A 1 83  ? 18.716 8.762  4.271   1.00 65.45  ? 83  LYS A CB  1 
ATOM   647  C  CG  . LYS A 1 83  ? 17.516 9.698  4.282   1.00 51.59  ? 83  LYS A CG  1 
ATOM   648  C  CD  . LYS A 1 83  ? 17.809 11.043 4.948   1.00 70.84  ? 83  LYS A CD  1 
ATOM   649  C  CE  . LYS A 1 83  ? 18.006 10.968 6.468   1.00 100.00 ? 83  LYS A CE  1 
ATOM   650  N  NZ  . LYS A 1 83  ? 18.840 12.051 7.045   1.00 100.00 ? 83  LYS A NZ  1 
ATOM   651  N  N   . LEU A 1 84  ? 20.473 6.751  6.049   1.00 31.02  ? 84  LEU A N   1 
ATOM   652  C  CA  . LEU A 1 84  ? 21.755 6.093  6.175   1.00 30.81  ? 84  LEU A CA  1 
ATOM   653  C  C   . LEU A 1 84  ? 21.763 4.608  6.513   1.00 22.80  ? 84  LEU A C   1 
ATOM   654  O  O   . LEU A 1 84  ? 22.583 3.870  5.992   1.00 25.40  ? 84  LEU A O   1 
ATOM   655  C  CB  . LEU A 1 84  ? 22.719 6.873  7.112   1.00 23.68  ? 84  LEU A CB  1 
ATOM   656  C  CG  . LEU A 1 84  ? 22.967 8.298  6.675   1.00 24.09  ? 84  LEU A CG  1 
ATOM   657  C  CD1 . LEU A 1 84  ? 23.932 8.951  7.629   1.00 27.02  ? 84  LEU A CD1 1 
ATOM   658  C  CD2 . LEU A 1 84  ? 23.566 8.318  5.291   1.00 21.35  ? 84  LEU A CD2 1 
ATOM   659  N  N   . LYS A 1 85  ? 20.918 4.197  7.445   1.00 22.77  ? 85  LYS A N   1 
ATOM   660  C  CA  . LYS A 1 85  ? 20.917 2.836  7.936   1.00 17.08  ? 85  LYS A CA  1 
ATOM   661  C  C   . LYS A 1 85  ? 20.874 1.762  6.879   1.00 22.12  ? 85  LYS A C   1 
ATOM   662  O  O   . LYS A 1 85  ? 21.647 0.798  6.902   1.00 23.85  ? 85  LYS A O   1 
ATOM   663  C  CB  . LYS A 1 85  ? 19.843 2.639  8.998   1.00 23.45  ? 85  LYS A CB  1 
ATOM   664  C  CG  . LYS A 1 85  ? 20.150 1.463  9.898   1.00 24.01  ? 85  LYS A CG  1 
ATOM   665  C  CD  . LYS A 1 85  ? 18.971 0.957  10.707  1.00 30.95  ? 85  LYS A CD  1 
ATOM   666  C  CE  . LYS A 1 85  ? 18.898 -0.563 10.689  1.00 35.04  ? 85  LYS A CE  1 
ATOM   667  N  NZ  . LYS A 1 85  ? 20.227 -1.190 10.778  1.00 47.91  ? 85  LYS A NZ  1 
ATOM   668  N  N   . PRO A 1 86  ? 19.922 1.908  5.970   1.00 18.37  ? 86  PRO A N   1 
ATOM   669  C  CA  . PRO A 1 86  ? 19.739 0.926  4.930   1.00 35.65  ? 86  PRO A CA  1 
ATOM   670  C  C   . PRO A 1 86  ? 20.962 0.836  4.036   1.00 28.12  ? 86  PRO A C   1 
ATOM   671  O  O   . PRO A 1 86  ? 21.346 -0.220 3.587   1.00 21.26  ? 86  PRO A O   1 
ATOM   672  C  CB  . PRO A 1 86  ? 18.492 1.345  4.137   1.00 28.76  ? 86  PRO A CB  1 
ATOM   673  C  CG  . PRO A 1 86  ? 18.024 2.678  4.698   1.00 33.29  ? 86  PRO A CG  1 
ATOM   674  C  CD  . PRO A 1 86  ? 18.973 3.036  5.832   1.00 22.64  ? 86  PRO A CD  1 
ATOM   675  N  N   . VAL A 1 87  ? 21.613 1.938  3.790   1.00 20.83  ? 87  VAL A N   1 
ATOM   676  C  CA  . VAL A 1 87  ? 22.808 1.828  2.979   1.00 16.19  ? 87  VAL A CA  1 
ATOM   677  C  C   . VAL A 1 87  ? 23.847 1.039  3.717   1.00 13.64  ? 87  VAL A C   1 
ATOM   678  O  O   . VAL A 1 87  ? 24.454 0.121  3.210   1.00 19.31  ? 87  VAL A O   1 
ATOM   679  C  CB  . VAL A 1 87  ? 23.420 3.192  2.713   1.00 24.28  ? 87  VAL A CB  1 
ATOM   680  C  CG1 . VAL A 1 87  ? 24.602 3.085  1.735   1.00 22.52  ? 87  VAL A CG1 1 
ATOM   681  C  CG2 . VAL A 1 87  ? 22.323 4.145  2.263   1.00 18.71  ? 87  VAL A CG2 1 
ATOM   682  N  N   . TYR A 1 88  ? 24.111 1.475  4.924   1.00 19.19  ? 88  TYR A N   1 
ATOM   683  C  CA  . TYR A 1 88  ? 25.101 0.843  5.741   1.00 12.34  ? 88  TYR A CA  1 
ATOM   684  C  C   . TYR A 1 88  ? 24.855 -0.639 5.844   1.00 22.00  ? 88  TYR A C   1 
ATOM   685  O  O   . TYR A 1 88  ? 25.746 -1.476 5.707   1.00 16.20  ? 88  TYR A O   1 
ATOM   686  C  CB  . TYR A 1 88  ? 24.989 1.443  7.123   1.00 20.95  ? 88  TYR A CB  1 
ATOM   687  C  CG  . TYR A 1 88  ? 26.057 0.984  8.062   1.00 22.16  ? 88  TYR A CG  1 
ATOM   688  C  CD1 . TYR A 1 88  ? 27.276 1.656  8.132   1.00 15.35  ? 88  TYR A CD1 1 
ATOM   689  C  CD2 . TYR A 1 88  ? 25.814 -0.099 8.906   1.00 29.86  ? 88  TYR A CD2 1 
ATOM   690  C  CE1 . TYR A 1 88  ? 28.217 1.264  9.087   1.00 19.62  ? 88  TYR A CE1 1 
ATOM   691  C  CE2 . TYR A 1 88  ? 26.777 -0.540 9.809   1.00 34.93  ? 88  TYR A CE2 1 
ATOM   692  C  CZ  . TYR A 1 88  ? 27.986 0.151  9.892   1.00 35.32  ? 88  TYR A CZ  1 
ATOM   693  O  OH  . TYR A 1 88  ? 28.941 -0.248 10.794  1.00 32.87  ? 88  TYR A OH  1 
ATOM   694  N  N   . ASP A 1 89  ? 23.625 -0.978 6.102   1.00 16.35  ? 89  ASP A N   1 
ATOM   695  C  CA  . ASP A 1 89  ? 23.316 -2.400 6.224   1.00 15.15  ? 89  ASP A CA  1 
ATOM   696  C  C   . ASP A 1 89  ? 23.619 -3.159 4.960   1.00 23.06  ? 89  ASP A C   1 
ATOM   697  O  O   . ASP A 1 89  ? 23.854 -4.343 5.019   1.00 24.11  ? 89  ASP A O   1 
ATOM   698  C  CB  . ASP A 1 89  ? 21.818 -2.669 6.519   1.00 15.16  ? 89  ASP A CB  1 
ATOM   699  C  CG  . ASP A 1 89  ? 21.433 -2.358 7.928   1.00 22.61  ? 89  ASP A CG  1 
ATOM   700  O  OD1 . ASP A 1 89  ? 22.203 -2.357 8.841   1.00 30.18  ? 89  ASP A OD1 1 
ATOM   701  O  OD2 . ASP A 1 89  ? 20.198 -2.027 8.030   1.00 30.77  ? 89  ASP A OD2 1 
ATOM   702  N  N   . SER A 1 90  ? 23.540 -2.514 3.789   1.00 24.54  ? 90  SER A N   1 
ATOM   703  C  CA  . SER A 1 90  ? 23.765 -3.206 2.532   1.00 14.80  ? 90  SER A CA  1 
ATOM   704  C  C   . SER A 1 90  ? 25.261 -3.401 2.169   1.00 20.94  ? 90  SER A C   1 
ATOM   705  O  O   . SER A 1 90  ? 25.614 -4.135 1.245   1.00 17.57  ? 90  SER A O   1 
ATOM   706  C  CB  . SER A 1 90  ? 23.051 -2.414 1.448   1.00 17.18  ? 90  SER A CB  1 
ATOM   707  O  OG  . SER A 1 90  ? 23.863 -1.311 1.055   1.00 22.32  ? 90  SER A OG  1 
ATOM   708  N  N   . LEU A 1 91  ? 26.169 -2.723 2.867   1.00 12.87  ? 91  LEU A N   1 
ATOM   709  C  CA  . LEU A 1 91  ? 27.575 -2.797 2.499   1.00 10.17  ? 91  LEU A CA  1 
ATOM   710  C  C   . LEU A 1 91  ? 28.427 -3.865 3.204   1.00 21.05  ? 91  LEU A C   1 
ATOM   711  O  O   . LEU A 1 91  ? 28.073 -4.334 4.298   1.00 17.08  ? 91  LEU A O   1 
ATOM   712  C  CB  . LEU A 1 91  ? 28.215 -1.410 2.782   1.00 17.55  ? 91  LEU A CB  1 
ATOM   713  C  CG  . LEU A 1 91  ? 27.572 -0.161 2.111   1.00 28.12  ? 91  LEU A CG  1 
ATOM   714  C  CD1 . LEU A 1 91  ? 28.165 1.133  2.687   1.00 19.29  ? 91  LEU A CD1 1 
ATOM   715  C  CD2 . LEU A 1 91  ? 27.734 -0.165 0.592   1.00 19.54  ? 91  LEU A CD2 1 
ATOM   716  N  N   . ASP A 1 92  ? 29.586 -4.184 2.591   1.00 17.28  ? 92  ASP A N   1 
ATOM   717  C  CA  . ASP A 1 92  ? 30.586 -5.085 3.196   1.00 12.62  ? 92  ASP A CA  1 
ATOM   718  C  C   . ASP A 1 92  ? 31.347 -4.274 4.263   1.00 15.30  ? 92  ASP A C   1 
ATOM   719  O  O   . ASP A 1 92  ? 31.168 -3.074 4.376   1.00 14.57  ? 92  ASP A O   1 
ATOM   720  C  CB  . ASP A 1 92  ? 31.575 -5.580 2.169   1.00 18.78  ? 92  ASP A CB  1 
ATOM   721  C  CG  . ASP A 1 92  ? 32.225 -4.400 1.525   1.00 21.63  ? 92  ASP A CG  1 
ATOM   722  O  OD1 . ASP A 1 92  ? 31.485 -3.875 0.575   1.00 19.72  ? 92  ASP A OD1 1 
ATOM   723  O  OD2 . ASP A 1 92  ? 33.298 -3.953 1.903   1.00 24.29  ? 92  ASP A OD2 1 
ATOM   724  N  N   . ALA A 1 93  ? 32.186 -4.905 5.085   1.00 20.52  ? 93  ALA A N   1 
ATOM   725  C  CA  . ALA A 1 93  ? 32.874 -4.225 6.178   1.00 20.74  ? 93  ALA A CA  1 
ATOM   726  C  C   . ALA A 1 93  ? 33.804 -3.064 5.807   1.00 19.67  ? 93  ALA A C   1 
ATOM   727  O  O   . ALA A 1 93  ? 33.928 -2.122 6.577   1.00 17.14  ? 93  ALA A O   1 
ATOM   728  C  CB  . ALA A 1 93  ? 33.568 -5.234 7.131   1.00 18.68  ? 93  ALA A CB  1 
ATOM   729  N  N   . VAL A 1 94  ? 34.541 -3.167 4.694   1.00 19.51  ? 94  VAL A N   1 
ATOM   730  C  CA  . VAL A 1 94  ? 35.434 -2.089 4.335   1.00 14.46  ? 94  VAL A CA  1 
ATOM   731  C  C   . VAL A 1 94  ? 34.647 -0.870 3.908   1.00 16.35  ? 94  VAL A C   1 
ATOM   732  O  O   . VAL A 1 94  ? 34.880 0.255  4.348   1.00 19.71  ? 94  VAL A O   1 
ATOM   733  C  CB  . VAL A 1 94  ? 36.375 -2.559 3.245   1.00 18.00  ? 94  VAL A CB  1 
ATOM   734  C  CG1 . VAL A 1 94  ? 37.373 -1.469 2.878   1.00 12.02  ? 94  VAL A CG1 1 
ATOM   735  C  CG2 . VAL A 1 94  ? 37.104 -3.747 3.806   1.00 12.47  ? 94  VAL A CG2 1 
ATOM   736  N  N   . ARG A 1 95  ? 33.678 -1.078 3.044   1.00 18.93  ? 95  ARG A N   1 
ATOM   737  C  CA  . ARG A 1 95  ? 32.897 0.061  2.588   1.00 12.93  ? 95  ARG A CA  1 
ATOM   738  C  C   . ARG A 1 95  ? 32.167 0.737  3.710   1.00 18.63  ? 95  ARG A C   1 
ATOM   739  O  O   . ARG A 1 95  ? 31.963 1.956  3.689   1.00 15.34  ? 95  ARG A O   1 
ATOM   740  C  CB  . ARG A 1 95  ? 31.934 -0.292 1.473   1.00 14.26  ? 95  ARG A CB  1 
ATOM   741  C  CG  . ARG A 1 95  ? 32.654 -0.616 0.185   1.00 11.25  ? 95  ARG A CG  1 
ATOM   742  C  CD  . ARG A 1 95  ? 31.643 -0.974 -0.898  1.00 20.48  ? 95  ARG A CD  1 
ATOM   743  N  NE  . ARG A 1 95  ? 32.282 -1.184 -2.191  1.00 22.27  ? 95  ARG A NE  1 
ATOM   744  C  CZ  . ARG A 1 95  ? 32.734 -2.364 -2.616  1.00 30.66  ? 95  ARG A CZ  1 
ATOM   745  N  NH1 . ARG A 1 95  ? 32.649 -3.472 -1.875  1.00 13.22  ? 95  ARG A NH1 1 
ATOM   746  N  NH2 . ARG A 1 95  ? 33.288 -2.420 -3.813  1.00 16.45  ? 95  ARG A NH2 1 
ATOM   747  N  N   . ARG A 1 96  ? 31.741 -0.061 4.688   1.00 18.29  ? 96  ARG A N   1 
ATOM   748  C  CA  . ARG A 1 96  ? 31.063 0.492  5.873   1.00 12.86  ? 96  ARG A CA  1 
ATOM   749  C  C   . ARG A 1 96  ? 32.013 1.472  6.579   1.00 16.17  ? 96  ARG A C   1 
ATOM   750  O  O   . ARG A 1 96  ? 31.594 2.542  7.008   1.00 15.66  ? 96  ARG A O   1 
ATOM   751  C  CB  . ARG A 1 96  ? 30.669 -0.580 6.882   1.00 11.34  ? 96  ARG A CB  1 
ATOM   752  C  CG  . ARG A 1 96  ? 29.333 -1.210 6.584   1.00 10.59  ? 96  ARG A CG  1 
ATOM   753  C  CD  . ARG A 1 96  ? 29.009 -2.360 7.556   1.00 19.52  ? 96  ARG A CD  1 
ATOM   754  N  NE  . ARG A 1 96  ? 27.788 -3.008 7.106   1.00 25.15  ? 96  ARG A NE  1 
ATOM   755  C  CZ  . ARG A 1 96  ? 27.342 -4.189 7.501   1.00 40.14  ? 96  ARG A CZ  1 
ATOM   756  N  NH1 . ARG A 1 96  ? 28.007 -4.886 8.382   1.00 25.68  ? 96  ARG A NH1 1 
ATOM   757  N  NH2 . ARG A 1 96  ? 26.218 -4.710 6.986   1.00 17.13  ? 96  ARG A NH2 1 
ATOM   758  N  N   . ALA A 1 97  ? 33.318 1.131  6.648   1.00 13.07  ? 97  ALA A N   1 
ATOM   759  C  CA  . ALA A 1 97  ? 34.286 2.026  7.262   1.00 19.31  ? 97  ALA A CA  1 
ATOM   760  C  C   . ALA A 1 97  ? 34.357 3.326  6.484   1.00 16.28  ? 97  ALA A C   1 
ATOM   761  O  O   . ALA A 1 97  ? 34.539 4.395  7.046   1.00 14.26  ? 97  ALA A O   1 
ATOM   762  C  CB  . ALA A 1 97  ? 35.676 1.408  7.355   1.00 12.09  ? 97  ALA A CB  1 
ATOM   763  N  N   . ALA A 1 98  ? 34.247 3.235  5.176   1.00 15.94  ? 98  ALA A N   1 
ATOM   764  C  CA  . ALA A 1 98  ? 34.306 4.460  4.368   1.00 11.07  ? 98  ALA A CA  1 
ATOM   765  C  C   . ALA A 1 98  ? 33.130 5.368  4.728   1.00 16.91  ? 98  ALA A C   1 
ATOM   766  O  O   . ALA A 1 98  ? 33.223 6.577  4.808   1.00 12.21  ? 98  ALA A O   1 
ATOM   767  C  CB  . ALA A 1 98  ? 34.269 4.093  2.887   1.00 16.54  ? 98  ALA A CB  1 
ATOM   768  N  N   . LEU A 1 99  ? 31.985 4.772  4.955   1.00 11.12  ? 99  LEU A N   1 
ATOM   769  C  CA  . LEU A 1 99  ? 30.805 5.553  5.329   1.00 7.33   ? 99  LEU A CA  1 
ATOM   770  C  C   . LEU A 1 99  ? 30.971 6.185  6.707   1.00 16.04  ? 99  LEU A C   1 
ATOM   771  O  O   . LEU A 1 99  ? 30.587 7.332  6.913   1.00 12.68  ? 99  LEU A O   1 
ATOM   772  C  CB  . LEU A 1 99  ? 29.530 4.659  5.267   1.00 12.23  ? 99  LEU A CB  1 
ATOM   773  C  CG  . LEU A 1 99  ? 28.205 5.402  5.404   1.00 17.47  ? 99  LEU A CG  1 
ATOM   774  C  CD1 . LEU A 1 99  ? 27.973 6.317  4.216   1.00 28.92  ? 99  LEU A CD1 1 
ATOM   775  C  CD2 . LEU A 1 99  ? 27.070 4.381  5.430   1.00 17.31  ? 99  LEU A CD2 1 
ATOM   776  N  N   . ILE A 1 100 ? 31.569 5.429  7.663   1.00 9.24   ? 100 ILE A N   1 
ATOM   777  C  CA  . ILE A 1 100 ? 31.792 5.976  8.980   1.00 7.99   ? 100 ILE A CA  1 
ATOM   778  C  C   . ILE A 1 100 ? 32.758 7.163  8.939   1.00 11.30  ? 100 ILE A C   1 
ATOM   779  O  O   . ILE A 1 100 ? 32.557 8.216  9.605   1.00 16.60  ? 100 ILE A O   1 
ATOM   780  C  CB  . ILE A 1 100 ? 32.274 4.916  9.949   1.00 15.66  ? 100 ILE A CB  1 
ATOM   781  C  CG1 . ILE A 1 100 ? 31.213 3.821  10.084  1.00 10.27  ? 100 ILE A CG1 1 
ATOM   782  C  CG2 . ILE A 1 100 ? 32.618 5.575  11.288  1.00 10.82  ? 100 ILE A CG2 1 
ATOM   783  C  CD1 . ILE A 1 100 ? 31.846 2.573  10.698  1.00 7.76   ? 100 ILE A CD1 1 
ATOM   784  N  N   . ASN A 1 101 ? 33.830 7.026  8.124   1.00 13.09  ? 101 ASN A N   1 
ATOM   785  C  CA  . ASN A 1 101 ? 34.799 8.126  7.941   1.00 7.58   ? 101 ASN A CA  1 
ATOM   786  C  C   . ASN A 1 101 ? 34.134 9.444  7.505   1.00 13.19  ? 101 ASN A C   1 
ATOM   787  O  O   . ASN A 1 101 ? 34.407 10.530 8.043   1.00 17.28  ? 101 ASN A O   1 
ATOM   788  C  CB  . ASN A 1 101 ? 35.830 7.688  6.867   1.00 11.21  ? 101 ASN A CB  1 
ATOM   789  C  CG  . ASN A 1 101 ? 37.022 8.597  6.776   1.00 18.12  ? 101 ASN A CG  1 
ATOM   790  O  OD1 . ASN A 1 101 ? 36.870 9.827  6.560   1.00 16.43  ? 101 ASN A OD1 1 
ATOM   791  N  ND2 . ASN A 1 101 ? 38.213 8.005  6.967   1.00 13.30  ? 101 ASN A ND2 1 
ATOM   792  N  N   . MET A 1 102 ? 33.209 9.323  6.527   1.00 11.31  ? 102 MET A N   1 
ATOM   793  C  CA  . MET A 1 102 ? 32.499 10.470 5.993   1.00 17.49  ? 102 MET A CA  1 
ATOM   794  C  C   . MET A 1 102 ? 31.600 11.105 7.074   1.00 15.85  ? 102 MET A C   1 
ATOM   795  O  O   . MET A 1 102 ? 31.526 12.329 7.222   1.00 18.70  ? 102 MET A O   1 
ATOM   796  C  CB  . MET A 1 102 ? 31.653 10.077 4.762   1.00 7.87   ? 102 MET A CB  1 
ATOM   797  C  CG  . MET A 1 102 ? 32.412 9.796  3.460   1.00 12.70  ? 102 MET A CG  1 
ATOM   798  S  SD  . MET A 1 102 ? 31.240 9.227  2.173   1.00 23.22  ? 102 MET A SD  1 
ATOM   799  C  CE  . MET A 1 102 ? 30.682 10.845 1.629   1.00 27.20  ? 102 MET A CE  1 
ATOM   800  N  N   . VAL A 1 103 ? 30.882 10.259 7.794   1.00 16.18  ? 103 VAL A N   1 
ATOM   801  C  CA  . VAL A 1 103 ? 30.003 10.755 8.835   1.00 16.60  ? 103 VAL A CA  1 
ATOM   802  C  C   . VAL A 1 103 ? 30.843 11.386 9.934   1.00 18.82  ? 103 VAL A C   1 
ATOM   803  O  O   . VAL A 1 103 ? 30.502 12.444 10.456  1.00 26.34  ? 103 VAL A O   1 
ATOM   804  C  CB  . VAL A 1 103 ? 29.047 9.693  9.368   1.00 21.86  ? 103 VAL A CB  1 
ATOM   805  C  CG1 . VAL A 1 103 ? 28.492 10.133 10.711  1.00 20.20  ? 103 VAL A CG1 1 
ATOM   806  C  CG2 . VAL A 1 103 ? 27.872 9.521  8.430   1.00 12.25  ? 103 VAL A CG2 1 
ATOM   807  N  N   . PHE A 1 104 ? 32.001 10.793 10.228  1.00 12.86  ? 104 PHE A N   1 
ATOM   808  C  CA  . PHE A 1 104 ? 32.878 11.366 11.228  1.00 10.86  ? 104 PHE A CA  1 
ATOM   809  C  C   . PHE A 1 104 ? 33.271 12.786 10.821  1.00 17.55  ? 104 PHE A C   1 
ATOM   810  O  O   . PHE A 1 104 ? 33.246 13.722 11.575  1.00 18.65  ? 104 PHE A O   1 
ATOM   811  C  CB  . PHE A 1 104 ? 34.134 10.465 11.357  1.00 8.21   ? 104 PHE A CB  1 
ATOM   812  C  CG  . PHE A 1 104 ? 35.069 10.848 12.484  1.00 13.65  ? 104 PHE A CG  1 
ATOM   813  C  CD1 . PHE A 1 104 ? 36.035 11.836 12.311  1.00 16.73  ? 104 PHE A CD1 1 
ATOM   814  C  CD2 . PHE A 1 104 ? 35.032 10.227 13.728  1.00 15.52  ? 104 PHE A CD2 1 
ATOM   815  C  CE1 . PHE A 1 104 ? 36.918 12.190 13.333  1.00 20.56  ? 104 PHE A CE1 1 
ATOM   816  C  CE2 . PHE A 1 104 ? 35.928 10.545 14.749  1.00 11.87  ? 104 PHE A CE2 1 
ATOM   817  C  CZ  . PHE A 1 104 ? 36.890 11.527 14.556  1.00 14.65  ? 104 PHE A CZ  1 
ATOM   818  N  N   . GLN A 1 105 ? 33.637 12.960 9.589   1.00 20.47  ? 105 GLN A N   1 
ATOM   819  C  CA  . GLN A 1 105 ? 34.105 14.238 9.094   1.00 13.61  ? 105 GLN A CA  1 
ATOM   820  C  C   . GLN A 1 105 ? 33.014 15.256 8.881   1.00 21.78  ? 105 GLN A C   1 
ATOM   821  O  O   . GLN A 1 105 ? 33.185 16.424 9.156   1.00 27.42  ? 105 GLN A O   1 
ATOM   822  C  CB  . GLN A 1 105 ? 34.829 14.048 7.719   1.00 15.67  ? 105 GLN A CB  1 
ATOM   823  C  CG  . GLN A 1 105 ? 35.427 15.376 7.195   1.00 20.37  ? 105 GLN A CG  1 
ATOM   824  C  CD  . GLN A 1 105 ? 36.096 15.289 5.843   1.00 28.76  ? 105 GLN A CD  1 
ATOM   825  O  OE1 . GLN A 1 105 ? 36.099 14.227 5.217   1.00 24.99  ? 105 GLN A OE1 1 
ATOM   826  N  NE2 . GLN A 1 105 ? 36.701 16.394 5.394   1.00 19.72  ? 105 GLN A NE2 1 
ATOM   827  N  N   . MET A 1 106 ? 31.909 14.855 8.300   1.00 19.23  ? 106 MET A N   1 
ATOM   828  C  CA  . MET A 1 106 ? 30.943 15.864 7.981   1.00 16.97  ? 106 MET A CA  1 
ATOM   829  C  C   . MET A 1 106 ? 29.586 15.765 8.615   1.00 29.88  ? 106 MET A C   1 
ATOM   830  O  O   . MET A 1 106 ? 28.706 16.571 8.363   1.00 30.80  ? 106 MET A O   1 
ATOM   831  C  CB  . MET A 1 106 ? 30.885 16.145 6.475   1.00 31.39  ? 106 MET A CB  1 
ATOM   832  C  CG  . MET A 1 106 ? 30.309 15.085 5.589   1.00 35.69  ? 106 MET A CG  1 
ATOM   833  S  SD  . MET A 1 106 ? 30.943 15.362 3.903   1.00 35.28  ? 106 MET A SD  1 
ATOM   834  C  CE  . MET A 1 106 ? 31.627 13.744 3.570   1.00 27.24  ? 106 MET A CE  1 
ATOM   835  N  N   . GLY A 1 107 ? 29.400 14.785 9.441   1.00 18.42  ? 107 GLY A N   1 
ATOM   836  C  CA  . GLY A 1 107 ? 28.134 14.697 10.098  1.00 10.89  ? 107 GLY A CA  1 
ATOM   837  C  C   . GLY A 1 107 ? 27.098 13.976 9.305   1.00 17.62  ? 107 GLY A C   1 
ATOM   838  O  O   . GLY A 1 107 ? 27.179 13.860 8.099   1.00 23.66  ? 107 GLY A O   1 
ATOM   839  N  N   . GLU A 1 108 ? 26.138 13.474 10.084  1.00 22.94  ? 108 GLU A N   1 
ATOM   840  C  CA  . GLU A 1 108 ? 24.996 12.699 9.674   1.00 23.36  ? 108 GLU A CA  1 
ATOM   841  C  C   . GLU A 1 108 ? 24.197 13.403 8.593   1.00 40.15  ? 108 GLU A C   1 
ATOM   842  O  O   . GLU A 1 108 ? 23.695 12.802 7.648   1.00 39.54  ? 108 GLU A O   1 
ATOM   843  C  CB  . GLU A 1 108 ? 24.118 12.531 10.933  1.00 36.88  ? 108 GLU A CB  1 
ATOM   844  C  CG  . GLU A 1 108 ? 23.132 11.355 10.954  1.00 35.59  ? 108 GLU A CG  1 
ATOM   845  C  CD  . GLU A 1 108 ? 22.475 11.231 12.313  1.00 51.27  ? 108 GLU A CD  1 
ATOM   846  O  OE1 . GLU A 1 108 ? 23.103 11.314 13.356  1.00 100.00 ? 108 GLU A OE1 1 
ATOM   847  O  OE2 . GLU A 1 108 ? 21.177 11.040 12.266  1.00 65.80  ? 108 GLU A OE2 1 
ATOM   848  N  N   . THR A 1 109 ? 24.043 14.699 8.782   1.00 37.10  ? 109 THR A N   1 
ATOM   849  C  CA  . THR A 1 109 ? 23.300 15.509 7.841   1.00 38.17  ? 109 THR A CA  1 
ATOM   850  C  C   . THR A 1 109 ? 24.044 15.727 6.528   1.00 36.06  ? 109 THR A C   1 
ATOM   851  O  O   . THR A 1 109 ? 23.476 15.538 5.445   1.00 46.86  ? 109 THR A O   1 
ATOM   852  C  CB  . THR A 1 109 ? 22.872 16.856 8.454   1.00 55.67  ? 109 THR A CB  1 
ATOM   853  O  OG1 . THR A 1 109 ? 22.742 16.719 9.842   1.00 46.93  ? 109 THR A OG1 1 
ATOM   854  C  CG2 . THR A 1 109 ? 21.548 17.304 7.850   1.00 57.60  ? 109 THR A CG2 1 
ATOM   855  N  N   . GLY A 1 110 ? 25.313 16.125 6.638   1.00 29.37  ? 110 GLY A N   1 
ATOM   856  C  CA  . GLY A 1 110 ? 26.137 16.356 5.466   1.00 21.45  ? 110 GLY A CA  1 
ATOM   857  C  C   . GLY A 1 110 ? 26.059 15.125 4.635   1.00 21.63  ? 110 GLY A C   1 
ATOM   858  O  O   . GLY A 1 110 ? 25.711 15.171 3.478   1.00 31.71  ? 110 GLY A O   1 
ATOM   859  N  N   . VAL A 1 111 ? 26.333 13.999 5.259   1.00 22.76  ? 111 VAL A N   1 
ATOM   860  C  CA  . VAL A 1 111 ? 26.324 12.745 4.529   1.00 14.02  ? 111 VAL A CA  1 
ATOM   861  C  C   . VAL A 1 111 ? 24.991 12.341 3.991   1.00 28.41  ? 111 VAL A C   1 
ATOM   862  O  O   . VAL A 1 111 ? 24.903 11.802 2.913   1.00 22.65  ? 111 VAL A O   1 
ATOM   863  C  CB  . VAL A 1 111 ? 26.915 11.663 5.323   1.00 25.47  ? 111 VAL A CB  1 
ATOM   864  C  CG1 . VAL A 1 111 ? 26.975 10.432 4.418   1.00 18.82  ? 111 VAL A CG1 1 
ATOM   865  C  CG2 . VAL A 1 111 ? 28.296 12.176 5.725   1.00 15.61  ? 111 VAL A CG2 1 
ATOM   866  N  N   . ALA A 1 112 ? 23.940 12.631 4.734   1.00 38.00  ? 112 ALA A N   1 
ATOM   867  C  CA  . ALA A 1 112 ? 22.597 12.327 4.290   1.00 31.26  ? 112 ALA A CA  1 
ATOM   868  C  C   . ALA A 1 112 ? 22.260 13.070 2.950   1.00 62.45  ? 112 ALA A C   1 
ATOM   869  O  O   . ALA A 1 112 ? 21.347 12.687 2.206   1.00 45.23  ? 112 ALA A O   1 
ATOM   870  C  CB  . ALA A 1 112 ? 21.607 12.525 5.455   1.00 26.81  ? 112 ALA A CB  1 
ATOM   871  N  N   . GLY A 1 113 ? 23.062 14.113 2.618   1.00 31.67  ? 113 GLY A N   1 
ATOM   872  C  CA  . GLY A 1 113 ? 22.992 14.918 1.364   1.00 40.25  ? 113 GLY A CA  1 
ATOM   873  C  C   . GLY A 1 113 ? 23.718 14.347 0.097   1.00 40.55  ? 113 GLY A C   1 
ATOM   874  O  O   . GLY A 1 113 ? 23.726 14.931 -0.990  1.00 54.46  ? 113 GLY A O   1 
ATOM   875  N  N   . PHE A 1 114 ? 24.349 13.206 0.242   1.00 28.31  ? 114 PHE A N   1 
ATOM   876  C  CA  . PHE A 1 114 ? 24.989 12.560 -0.845  1.00 21.79  ? 114 PHE A CA  1 
ATOM   877  C  C   . PHE A 1 114 ? 24.009 11.538 -1.303  1.00 25.11  ? 114 PHE A C   1 
ATOM   878  O  O   . PHE A 1 114 ? 24.287 10.397 -1.551  1.00 25.44  ? 114 PHE A O   1 
ATOM   879  C  CB  . PHE A 1 114 ? 26.252 11.905 -0.382  1.00 19.32  ? 114 PHE A CB  1 
ATOM   880  C  CG  . PHE A 1 114 ? 27.327 12.926 -0.152  1.00 23.63  ? 114 PHE A CG  1 
ATOM   881  C  CD1 . PHE A 1 114 ? 27.343 13.711 0.994   1.00 42.66  ? 114 PHE A CD1 1 
ATOM   882  C  CD2 . PHE A 1 114 ? 28.352 13.102 -1.080  1.00 45.31  ? 114 PHE A CD2 1 
ATOM   883  C  CE1 . PHE A 1 114 ? 28.352 14.646 1.227   1.00 55.69  ? 114 PHE A CE1 1 
ATOM   884  C  CE2 . PHE A 1 114 ? 29.380 14.021 -0.859  1.00 39.62  ? 114 PHE A CE2 1 
ATOM   885  C  CZ  . PHE A 1 114 ? 29.384 14.796 0.302   1.00 30.05  ? 114 PHE A CZ  1 
ATOM   886  N  N   . THR A 1 115 ? 22.832 12.016 -1.411  1.00 23.48  ? 115 THR A N   1 
ATOM   887  C  CA  . THR A 1 115 ? 21.708 11.229 -1.760  1.00 23.57  ? 115 THR A CA  1 
ATOM   888  C  C   . THR A 1 115 ? 21.868 10.372 -2.950  1.00 28.53  ? 115 THR A C   1 
ATOM   889  O  O   . THR A 1 115 ? 21.503 9.206  -2.966  1.00 27.78  ? 115 THR A O   1 
ATOM   890  C  CB  . THR A 1 115 ? 20.631 12.217 -2.133  1.00 42.66  ? 115 THR A CB  1 
ATOM   891  O  OG1 . THR A 1 115 ? 19.993 12.636 -0.956  1.00 77.72  ? 115 THR A OG1 1 
ATOM   892  C  CG2 . THR A 1 115 ? 19.663 11.513 -3.063  1.00 83.21  ? 115 THR A CG2 1 
ATOM   893  N  N   . ASN A 1 116 ? 22.298 11.018 -3.993  1.00 27.47  ? 116 ASN A N   1 
ATOM   894  C  CA  . ASN A 1 116 ? 22.468 10.358 -5.244  1.00 22.71  ? 116 ASN A CA  1 
ATOM   895  C  C   . ASN A 1 116 ? 23.515 9.289  -5.146  1.00 19.65  ? 116 ASN A C   1 
ATOM   896  O  O   . ASN A 1 116 ? 23.289 8.160  -5.548  1.00 32.21  ? 116 ASN A O   1 
ATOM   897  C  CB  . ASN A 1 116 ? 22.717 11.364 -6.395  1.00 38.12  ? 116 ASN A CB  1 
ATOM   898  C  CG  . ASN A 1 116 ? 21.539 12.333 -6.603  1.00 57.82  ? 116 ASN A CG  1 
ATOM   899  O  OD1 . ASN A 1 116 ? 20.386 11.982 -6.353  1.00 40.88  ? 116 ASN A OD1 1 
ATOM   900  N  ND2 . ASN A 1 116 ? 21.796 13.567 -7.039  1.00 34.56  ? 116 ASN A ND2 1 
ATOM   901  N  N   . SER A 1 117 ? 24.654 9.644  -4.581  1.00 23.74  ? 117 SER A N   1 
ATOM   902  C  CA  . SER A 1 117 ? 25.755 8.704  -4.441  1.00 19.04  ? 117 SER A CA  1 
ATOM   903  C  C   . SER A 1 117 ? 25.366 7.515  -3.630  1.00 22.45  ? 117 SER A C   1 
ATOM   904  O  O   . SER A 1 117 ? 25.779 6.419  -3.932  1.00 28.79  ? 117 SER A O   1 
ATOM   905  C  CB  . SER A 1 117 ? 27.064 9.266  -3.877  1.00 24.22  ? 117 SER A CB  1 
ATOM   906  O  OG  . SER A 1 117 ? 27.175 10.656 -4.037  1.00 31.73  ? 117 SER A OG  1 
ATOM   907  N  N   . LEU A 1 118 ? 24.645 7.794  -2.559  1.00 29.22  ? 118 LEU A N   1 
ATOM   908  C  CA  . LEU A 1 118 ? 24.144 6.832  -1.593  1.00 35.26  ? 118 LEU A CA  1 
ATOM   909  C  C   . LEU A 1 118 ? 23.274 5.806  -2.323  1.00 36.44  ? 118 LEU A C   1 
ATOM   910  O  O   . LEU A 1 118 ? 23.405 4.616  -2.159  1.00 37.04  ? 118 LEU A O   1 
ATOM   911  C  CB  . LEU A 1 118 ? 23.251 7.566  -0.521  1.00 44.29  ? 118 LEU A CB  1 
ATOM   912  C  CG  . LEU A 1 118 ? 23.796 7.836  0.919   1.00 47.38  ? 118 LEU A CG  1 
ATOM   913  C  CD1 . LEU A 1 118 ? 25.321 7.904  1.042   1.00 22.63  ? 118 LEU A CD1 1 
ATOM   914  C  CD2 . LEU A 1 118 ? 23.153 9.105  1.494   1.00 33.52  ? 118 LEU A CD2 1 
ATOM   915  N  N   . ARG A 1 119 ? 22.366 6.284  -3.135  1.00 21.50  ? 119 ARG A N   1 
ATOM   916  C  CA  . ARG A 1 119 ? 21.465 5.409  -3.850  1.00 30.07  ? 119 ARG A CA  1 
ATOM   917  C  C   . ARG A 1 119 ? 22.203 4.497  -4.815  1.00 37.88  ? 119 ARG A C   1 
ATOM   918  O  O   . ARG A 1 119 ? 21.898 3.299  -4.922  1.00 34.95  ? 119 ARG A O   1 
ATOM   919  C  CB  . ARG A 1 119 ? 20.399 6.255  -4.542  1.00 28.07  ? 119 ARG A CB  1 
ATOM   920  C  CG  . ARG A 1 119 ? 19.547 5.499  -5.543  1.00 71.75  ? 119 ARG A CG  1 
ATOM   921  C  CD  . ARG A 1 119 ? 18.933 6.424  -6.600  1.00 100.00 ? 119 ARG A CD  1 
ATOM   922  N  NE  . ARG A 1 119 ? 19.047 5.888  -7.961  1.00 100.00 ? 119 ARG A NE  1 
ATOM   923  C  CZ  . ARG A 1 119 ? 19.438 6.586  -9.032  1.00 100.00 ? 119 ARG A CZ  1 
ATOM   924  N  NH1 . ARG A 1 119 ? 19.762 7.887  -8.949  1.00 100.00 ? 119 ARG A NH1 1 
ATOM   925  N  NH2 . ARG A 1 119 ? 19.506 5.953  -10.213 1.00 89.77  ? 119 ARG A NH2 1 
ATOM   926  N  N   . MET A 1 120 ? 23.217 5.060  -5.503  1.00 31.30  ? 120 MET A N   1 
ATOM   927  C  CA  . MET A 1 120 ? 24.043 4.265  -6.424  1.00 28.22  ? 120 MET A CA  1 
ATOM   928  C  C   . MET A 1 120 ? 24.789 3.153  -5.658  1.00 28.92  ? 120 MET A C   1 
ATOM   929  O  O   . MET A 1 120 ? 24.825 1.997  -6.069  1.00 45.30  ? 120 MET A O   1 
ATOM   930  C  CB  . MET A 1 120 ? 25.050 5.131  -7.229  1.00 30.16  ? 120 MET A CB  1 
ATOM   931  C  CG  . MET A 1 120 ? 24.409 6.065  -8.279  1.00 40.41  ? 120 MET A CG  1 
ATOM   932  S  SD  . MET A 1 120 ? 25.557 7.347  -8.898  1.00 51.10  ? 120 MET A SD  1 
ATOM   933  C  CE  . MET A 1 120 ? 24.466 8.670  -9.465  1.00 25.42  ? 120 MET A CE  1 
ATOM   934  N  N   . ALA A 1 121 ? 25.380 3.525  -4.519  1.00 30.24  ? 121 ALA A N   1 
ATOM   935  C  CA  . ALA A 1 121 ? 26.128 2.593  -3.702  1.00 33.68  ? 121 ALA A CA  1 
ATOM   936  C  C   . ALA A 1 121 ? 25.202 1.502  -3.247  1.00 34.31  ? 121 ALA A C   1 
ATOM   937  O  O   . ALA A 1 121 ? 25.553 0.341  -3.188  1.00 34.78  ? 121 ALA A O   1 
ATOM   938  C  CB  . ALA A 1 121 ? 26.776 3.276  -2.504  1.00 31.20  ? 121 ALA A CB  1 
ATOM   939  N  N   . GLN A 1 122 ? 23.989 1.882  -2.942  1.00 34.28  ? 122 GLN A N   1 
ATOM   940  C  CA  . GLN A 1 122 ? 23.079 0.873  -2.530  1.00 37.89  ? 122 GLN A CA  1 
ATOM   941  C  C   . GLN A 1 122 ? 22.933 -0.135 -3.650  1.00 69.08  ? 122 GLN A C   1 
ATOM   942  O  O   . GLN A 1 122 ? 22.955 -1.340 -3.404  1.00 53.41  ? 122 GLN A O   1 
ATOM   943  C  CB  . GLN A 1 122 ? 21.737 1.422  -2.052  1.00 22.91  ? 122 GLN A CB  1 
ATOM   944  C  CG  . GLN A 1 122 ? 21.130 0.434  -1.059  1.00 34.77  ? 122 GLN A CG  1 
ATOM   945  C  CD  . GLN A 1 122 ? 19.826 0.908  -0.500  1.00 100.00 ? 122 GLN A CD  1 
ATOM   946  O  OE1 . GLN A 1 122 ? 19.621 2.129  -0.316  1.00 51.24  ? 122 GLN A OE1 1 
ATOM   947  N  NE2 . GLN A 1 122 ? 18.946 -0.065 -0.233  1.00 100.00 ? 122 GLN A NE2 1 
ATOM   948  N  N   . GLN A 1 123 ? 22.844 0.382  -4.885  1.00 31.08  ? 123 GLN A N   1 
ATOM   949  C  CA  . GLN A 1 123 ? 22.730 -0.453 -6.080  1.00 27.92  ? 123 GLN A CA  1 
ATOM   950  C  C   . GLN A 1 123 ? 24.028 -1.100 -6.456  1.00 37.85  ? 123 GLN A C   1 
ATOM   951  O  O   . GLN A 1 123 ? 24.067 -1.804 -7.465  1.00 42.37  ? 123 GLN A O   1 
ATOM   952  C  CB  . GLN A 1 123 ? 22.262 0.296  -7.321  1.00 20.72  ? 123 GLN A CB  1 
ATOM   953  C  CG  . GLN A 1 123 ? 20.910 0.930  -7.075  1.00 33.00  ? 123 GLN A CG  1 
ATOM   954  C  CD  . GLN A 1 123 ? 20.421 1.528  -8.351  1.00 53.33  ? 123 GLN A CD  1 
ATOM   955  O  OE1 . GLN A 1 123 ? 20.260 0.799  -9.339  1.00 99.39  ? 123 GLN A OE1 1 
ATOM   956  N  NE2 . GLN A 1 123 ? 20.246 2.848  -8.356  1.00 70.38  ? 123 GLN A NE2 1 
ATOM   957  N  N   . LYS A 1 124 ? 25.087 -0.813 -5.665  1.00 26.54  ? 124 LYS A N   1 
ATOM   958  C  CA  . LYS A 1 124 ? 26.423 -1.375 -5.856  1.00 40.91  ? 124 LYS A CA  1 
ATOM   959  C  C   . LYS A 1 124 ? 27.113 -0.947 -7.160  1.00 58.82  ? 124 LYS A C   1 
ATOM   960  O  O   . LYS A 1 124 ? 27.966 -1.686 -7.668  1.00 33.14  ? 124 LYS A O   1 
ATOM   961  C  CB  . LYS A 1 124 ? 26.531 -2.898 -5.583  1.00 38.80  ? 124 LYS A CB  1 
ATOM   962  C  CG  . LYS A 1 124 ? 25.823 -3.391 -4.312  1.00 46.20  ? 124 LYS A CG  1 
ATOM   963  C  CD  . LYS A 1 124 ? 26.293 -4.758 -3.780  1.00 24.81  ? 124 LYS A CD  1 
ATOM   964  C  CE  . LYS A 1 124 ? 25.897 -4.999 -2.315  1.00 35.94  ? 124 LYS A CE  1 
ATOM   965  N  NZ  . LYS A 1 124 ? 26.665 -4.159 -1.371  1.00 28.29  ? 124 LYS A NZ  1 
ATOM   966  N  N   . ARG A 1 125 ? 26.731 0.238  -7.688  1.00 31.26  ? 125 ARG A N   1 
ATOM   967  C  CA  . ARG A 1 125 ? 27.332 0.832  -8.911  1.00 26.61  ? 125 ARG A CA  1 
ATOM   968  C  C   . ARG A 1 125 ? 28.545 1.624  -8.472  1.00 21.21  ? 125 ARG A C   1 
ATOM   969  O  O   . ARG A 1 125 ? 28.529 2.842  -8.463  1.00 30.29  ? 125 ARG A O   1 
ATOM   970  C  CB  . ARG A 1 125 ? 26.400 1.830  -9.597  1.00 30.07  ? 125 ARG A CB  1 
ATOM   971  C  CG  . ARG A 1 125 ? 24.975 1.368  -9.868  1.00 27.52  ? 125 ARG A CG  1 
ATOM   972  C  CD  . ARG A 1 125 ? 24.186 2.513  -10.512 1.00 41.33  ? 125 ARG A CD  1 
ATOM   973  N  NE  . ARG A 1 125 ? 23.281 2.084  -11.571 1.00 68.64  ? 125 ARG A NE  1 
ATOM   974  C  CZ  . ARG A 1 125 ? 22.505 0.978  -11.472 1.00 100.00 ? 125 ARG A CZ  1 
ATOM   975  N  NH1 . ARG A 1 125 ? 22.512 0.171  -10.387 1.00 100.00 ? 125 ARG A NH1 1 
ATOM   976  N  NH2 . ARG A 1 125 ? 21.692 0.661  -12.491 1.00 100.00 ? 125 ARG A NH2 1 
ATOM   977  N  N   . TRP A 1 126 ? 29.571 0.920  -8.049  1.00 34.32  ? 126 TRP A N   1 
ATOM   978  C  CA  . TRP A 1 126 ? 30.768 1.540  -7.519  1.00 38.95  ? 126 TRP A CA  1 
ATOM   979  C  C   . TRP A 1 126 ? 31.348 2.716  -8.284  1.00 47.10  ? 126 TRP A C   1 
ATOM   980  O  O   . TRP A 1 126 ? 31.764 3.696  -7.680  1.00 26.76  ? 126 TRP A O   1 
ATOM   981  C  CB  . TRP A 1 126 ? 31.855 0.510  -7.091  1.00 25.25  ? 126 TRP A CB  1 
ATOM   982  C  CG  . TRP A 1 126 ? 31.263 -0.603 -6.263  1.00 51.50  ? 126 TRP A CG  1 
ATOM   983  C  CD1 . TRP A 1 126 ? 31.354 -1.941 -6.507  1.00 48.52  ? 126 TRP A CD1 1 
ATOM   984  C  CD2 . TRP A 1 126 ? 30.427 -0.470 -5.107  1.00 32.53  ? 126 TRP A CD2 1 
ATOM   985  N  NE1 . TRP A 1 126 ? 30.672 -2.657 -5.555  1.00 52.71  ? 126 TRP A NE1 1 
ATOM   986  C  CE2 . TRP A 1 126 ? 30.090 -1.776 -4.685  1.00 58.75  ? 126 TRP A CE2 1 
ATOM   987  C  CE3 . TRP A 1 126 ? 29.971 0.622  -4.370  1.00 24.83  ? 126 TRP A CE3 1 
ATOM   988  C  CZ2 . TRP A 1 126 ? 29.294 -1.998 -3.566  1.00 33.30  ? 126 TRP A CZ2 1 
ATOM   989  C  CZ3 . TRP A 1 126 ? 29.171 0.402  -3.264  1.00 26.30  ? 126 TRP A CZ3 1 
ATOM   990  C  CH2 . TRP A 1 126 ? 28.850 -0.900 -2.860  1.00 34.00  ? 126 TRP A CH2 1 
ATOM   991  N  N   . ASP A 1 127 ? 31.416 2.605  -9.600  1.00 40.54  ? 127 ASP A N   1 
ATOM   992  C  CA  . ASP A 1 127 ? 32.060 3.625  -10.390 1.00 31.20  ? 127 ASP A CA  1 
ATOM   993  C  C   . ASP A 1 127 ? 31.299 4.898  -10.496 1.00 23.38  ? 127 ASP A C   1 
ATOM   994  O  O   . ASP A 1 127 ? 31.839 6.017  -10.359 1.00 21.46  ? 127 ASP A O   1 
ATOM   995  C  CB  . ASP A 1 127 ? 32.667 3.081  -11.709 1.00 29.57  ? 127 ASP A CB  1 
ATOM   996  C  CG  . ASP A 1 127 ? 33.631 1.953  -11.389 1.00 33.96  ? 127 ASP A CG  1 
ATOM   997  O  OD1 . ASP A 1 127 ? 33.271 0.895  -10.885 1.00 100.00 ? 127 ASP A OD1 1 
ATOM   998  O  OD2 . ASP A 1 127 ? 34.888 2.258  -11.585 1.00 56.05  ? 127 ASP A OD2 1 
ATOM   999  N  N   . GLU A 1 128 ? 30.024 4.717  -10.698 1.00 22.65  ? 128 GLU A N   1 
ATOM   1000 C  CA  . GLU A 1 128 ? 29.182 5.858  -10.834 1.00 28.84  ? 128 GLU A CA  1 
ATOM   1001 C  C   . GLU A 1 128 ? 29.036 6.586  -9.505  1.00 43.81  ? 128 GLU A C   1 
ATOM   1002 O  O   . GLU A 1 128 ? 28.902 7.795  -9.452  1.00 21.04  ? 128 GLU A O   1 
ATOM   1003 C  CB  . GLU A 1 128 ? 27.859 5.382  -11.403 1.00 30.64  ? 128 GLU A CB  1 
ATOM   1004 C  CG  . GLU A 1 128 ? 27.955 3.859  -11.622 1.00 61.31  ? 128 GLU A CG  1 
ATOM   1005 C  CD  . GLU A 1 128 ? 27.367 3.425  -12.928 1.00 51.47  ? 128 GLU A CD  1 
ATOM   1006 O  OE1 . GLU A 1 128 ? 26.181 3.956  -13.155 1.00 75.79  ? 128 GLU A OE1 1 
ATOM   1007 O  OE2 . GLU A 1 128 ? 27.935 2.648  -13.686 1.00 100.00 ? 128 GLU A OE2 1 
ATOM   1008 N  N   . ALA A 1 129 ? 29.074 5.854  -8.416  1.00 22.14  ? 129 ALA A N   1 
ATOM   1009 C  CA  . ALA A 1 129 ? 28.943 6.491  -7.120  1.00 32.20  ? 129 ALA A CA  1 
ATOM   1010 C  C   . ALA A 1 129 ? 30.189 7.325  -6.803  1.00 27.11  ? 129 ALA A C   1 
ATOM   1011 O  O   . ALA A 1 129 ? 30.142 8.449  -6.286  1.00 26.03  ? 129 ALA A O   1 
ATOM   1012 C  CB  . ALA A 1 129 ? 28.775 5.417  -6.062  1.00 20.81  ? 129 ALA A CB  1 
ATOM   1013 N  N   . ALA A 1 130 ? 31.313 6.733  -7.142  1.00 14.66  ? 130 ALA A N   1 
ATOM   1014 C  CA  . ALA A 1 130 ? 32.591 7.351  -6.923  1.00 16.03  ? 130 ALA A CA  1 
ATOM   1015 C  C   . ALA A 1 130 ? 32.691 8.655  -7.672  1.00 23.70  ? 130 ALA A C   1 
ATOM   1016 O  O   . ALA A 1 130 ? 33.096 9.660  -7.128  1.00 21.56  ? 130 ALA A O   1 
ATOM   1017 C  CB  . ALA A 1 130 ? 33.677 6.390  -7.336  1.00 13.14  ? 130 ALA A CB  1 
ATOM   1018 N  N   . VAL A 1 131 ? 32.258 8.656  -8.919  1.00 21.91  ? 131 VAL A N   1 
ATOM   1019 C  CA  . VAL A 1 131 ? 32.306 9.881  -9.695  1.00 18.25  ? 131 VAL A CA  1 
ATOM   1020 C  C   . VAL A 1 131 ? 31.413 10.941 -9.075  1.00 18.73  ? 131 VAL A C   1 
ATOM   1021 O  O   . VAL A 1 131 ? 31.795 12.090 -8.936  1.00 21.19  ? 131 VAL A O   1 
ATOM   1022 C  CB  . VAL A 1 131 ? 31.912 9.584  -11.161 1.00 29.90  ? 131 VAL A CB  1 
ATOM   1023 C  CG1 . VAL A 1 131 ? 31.494 10.840 -11.914 1.00 32.57  ? 131 VAL A CG1 1 
ATOM   1024 C  CG2 . VAL A 1 131 ? 33.071 8.916  -11.916 1.00 22.80  ? 131 VAL A CG2 1 
ATOM   1025 N  N   . ASN A 1 132 ? 30.189 10.536 -8.734  1.00 15.17  ? 132 ASN A N   1 
ATOM   1026 C  CA  . ASN A 1 132 ? 29.224 11.392 -8.098  1.00 16.39  ? 132 ASN A CA  1 
ATOM   1027 C  C   . ASN A 1 132 ? 29.749 11.922 -6.756  1.00 18.86  ? 132 ASN A C   1 
ATOM   1028 O  O   . ASN A 1 132 ? 29.549 13.080 -6.384  1.00 18.41  ? 132 ASN A O   1 
ATOM   1029 C  CB  . ASN A 1 132 ? 27.893 10.651 -7.910  1.00 11.69  ? 132 ASN A CB  1 
ATOM   1030 C  CG  . ASN A 1 132 ? 26.778 11.582 -7.510  1.00 20.49  ? 132 ASN A CG  1 
ATOM   1031 O  OD1 . ASN A 1 132 ? 26.515 11.798 -6.304  1.00 21.09  ? 132 ASN A OD1 1 
ATOM   1032 N  ND2 . ASN A 1 132 ? 26.133 12.171 -8.507  1.00 27.11  ? 132 ASN A ND2 1 
ATOM   1033 N  N   . LEU A 1 133 ? 30.430 11.084 -6.010  1.00 16.43  ? 133 LEU A N   1 
ATOM   1034 C  CA  . LEU A 1 133 ? 30.957 11.565 -4.739  1.00 10.14  ? 133 LEU A CA  1 
ATOM   1035 C  C   . LEU A 1 133 ? 31.945 12.707 -4.966  1.00 11.80  ? 133 LEU A C   1 
ATOM   1036 O  O   . LEU A 1 133 ? 32.033 13.681 -4.188  1.00 15.85  ? 133 LEU A O   1 
ATOM   1037 C  CB  . LEU A 1 133 ? 31.677 10.392 -3.998  1.00 13.74  ? 133 LEU A CB  1 
ATOM   1038 C  CG  . LEU A 1 133 ? 30.707 9.402  -3.290  1.00 23.21  ? 133 LEU A CG  1 
ATOM   1039 C  CD1 . LEU A 1 133 ? 31.434 8.165  -2.729  1.00 16.63  ? 133 LEU A CD1 1 
ATOM   1040 C  CD2 . LEU A 1 133 ? 29.953 10.124 -2.174  1.00 21.74  ? 133 LEU A CD2 1 
ATOM   1041 N  N   . ALA A 1 134 ? 32.715 12.576 -6.031  1.00 19.23  ? 134 ALA A N   1 
ATOM   1042 C  CA  . ALA A 1 134 ? 33.724 13.563 -6.403  1.00 17.28  ? 134 ALA A CA  1 
ATOM   1043 C  C   . ALA A 1 134 ? 33.196 14.959 -6.780  1.00 16.35  ? 134 ALA A C   1 
ATOM   1044 O  O   . ALA A 1 134 ? 33.892 16.002 -6.724  1.00 16.39  ? 134 ALA A O   1 
ATOM   1045 C  CB  . ALA A 1 134 ? 34.672 12.993 -7.454  1.00 15.00  ? 134 ALA A CB  1 
ATOM   1046 N  N   . LYS A 1 135 ? 31.958 15.002 -7.163  1.00 16.92  ? 135 LYS A N   1 
ATOM   1047 C  CA  . LYS A 1 135 ? 31.353 16.279 -7.523  1.00 14.73  ? 135 LYS A CA  1 
ATOM   1048 C  C   . LYS A 1 135 ? 30.780 16.957 -6.302  1.00 21.57  ? 135 LYS A C   1 
ATOM   1049 O  O   . LYS A 1 135 ? 29.574 17.081 -6.125  1.00 20.06  ? 135 LYS A O   1 
ATOM   1050 C  CB  . LYS A 1 135 ? 30.298 16.040 -8.566  1.00 16.44  ? 135 LYS A CB  1 
ATOM   1051 C  CG  . LYS A 1 135 ? 30.940 15.716 -9.905  1.00 18.57  ? 135 LYS A CG  1 
ATOM   1052 C  CD  . LYS A 1 135 ? 29.957 15.789 -11.047 1.00 61.93  ? 135 LYS A CD  1 
ATOM   1053 C  CE  . LYS A 1 135 ? 29.798 14.460 -11.759 1.00 66.64  ? 135 LYS A CE  1 
ATOM   1054 N  NZ  . LYS A 1 135 ? 28.386 14.057 -11.907 1.00 73.25  ? 135 LYS A NZ  1 
ATOM   1055 N  N   . SER A 1 136 ? 31.661 17.367 -5.414  1.00 12.01  ? 136 SER A N   1 
ATOM   1056 C  CA  . SER A 1 136 ? 31.198 17.920 -4.174  1.00 14.16  ? 136 SER A CA  1 
ATOM   1057 C  C   . SER A 1 136 ? 32.198 18.897 -3.659  1.00 16.73  ? 136 SER A C   1 
ATOM   1058 O  O   . SER A 1 136 ? 33.386 18.834 -3.986  1.00 14.11  ? 136 SER A O   1 
ATOM   1059 C  CB  . SER A 1 136 ? 31.114 16.777 -3.144  1.00 12.50  ? 136 SER A CB  1 
ATOM   1060 O  OG  . SER A 1 136 ? 32.390 16.100 -3.050  1.00 15.16  ? 136 SER A OG  1 
ATOM   1061 N  N   . ARG A 1 137 ? 31.702 19.774 -2.803  1.00 13.93  ? 137 ARG A N   1 
ATOM   1062 C  CA  . ARG A 1 137 ? 32.563 20.726 -2.121  1.00 14.87  ? 137 ARG A CA  1 
ATOM   1063 C  C   . ARG A 1 137 ? 33.626 19.972 -1.349  1.00 14.68  ? 137 ARG A C   1 
ATOM   1064 O  O   . ARG A 1 137 ? 34.824 20.271 -1.345  1.00 18.55  ? 137 ARG A O   1 
ATOM   1065 C  CB  . ARG A 1 137 ? 31.732 21.543 -1.113  1.00 20.65  ? 137 ARG A CB  1 
ATOM   1066 C  CG  . ARG A 1 137 ? 32.640 22.515 -0.347  1.00 31.90  ? 137 ARG A CG  1 
ATOM   1067 C  CD  . ARG A 1 137 ? 31.966 23.331 0.773   1.00 26.57  ? 137 ARG A CD  1 
ATOM   1068 N  NE  . ARG A 1 137 ? 32.514 24.684 0.845   1.00 50.59  ? 137 ARG A NE  1 
ATOM   1069 C  CZ  . ARG A 1 137 ? 33.530 25.021 1.635   1.00 100.00 ? 137 ARG A CZ  1 
ATOM   1070 N  NH1 . ARG A 1 137 ? 34.088 24.105 2.437   1.00 48.38  ? 137 ARG A NH1 1 
ATOM   1071 N  NH2 . ARG A 1 137 ? 33.993 26.289 1.630   1.00 74.11  ? 137 ARG A NH2 1 
ATOM   1072 N  N   . TRP A 1 138 ? 33.137 18.915 -0.722  1.00 20.77  ? 138 TRP A N   1 
ATOM   1073 C  CA  . TRP A 1 138 ? 33.948 18.006 0.062   1.00 15.11  ? 138 TRP A CA  1 
ATOM   1074 C  C   . TRP A 1 138 ? 35.188 17.595 -0.714  1.00 19.39  ? 138 TRP A C   1 
ATOM   1075 O  O   . TRP A 1 138 ? 36.307 17.823 -0.273  1.00 20.81  ? 138 TRP A O   1 
ATOM   1076 C  CB  . TRP A 1 138 ? 33.093 16.759 0.426   1.00 24.26  ? 138 TRP A CB  1 
ATOM   1077 C  CG  . TRP A 1 138 ? 33.874 15.619 1.036   1.00 26.29  ? 138 TRP A CG  1 
ATOM   1078 C  CD1 . TRP A 1 138 ? 34.626 15.702 2.176   1.00 17.71  ? 138 TRP A CD1 1 
ATOM   1079 C  CD2 . TRP A 1 138 ? 33.958 14.236 0.598   1.00 15.05  ? 138 TRP A CD2 1 
ATOM   1080 N  NE1 . TRP A 1 138 ? 35.214 14.487 2.439   1.00 16.71  ? 138 TRP A NE1 1 
ATOM   1081 C  CE2 . TRP A 1 138 ? 34.765 13.548 1.543   1.00 15.01  ? 138 TRP A CE2 1 
ATOM   1082 C  CE3 . TRP A 1 138 ? 33.401 13.527 -0.450  1.00 12.59  ? 138 TRP A CE3 1 
ATOM   1083 C  CZ2 . TRP A 1 138 ? 35.044 12.185 1.455   1.00 13.29  ? 138 TRP A CZ2 1 
ATOM   1084 C  CZ3 . TRP A 1 138 ? 33.682 12.183 -0.540  1.00 22.57  ? 138 TRP A CZ3 1 
ATOM   1085 C  CH2 . TRP A 1 138 ? 34.466 11.509 0.407   1.00 19.85  ? 138 TRP A CH2 1 
ATOM   1086 N  N   . TYR A 1 139 ? 35.005 17.019 -1.908  1.00 16.39  ? 139 TYR A N   1 
ATOM   1087 C  CA  . TYR A 1 139 ? 36.186 16.618 -2.649  1.00 12.47  ? 139 TYR A CA  1 
ATOM   1088 C  C   . TYR A 1 139 ? 37.061 17.791 -2.994  1.00 20.95  ? 139 TYR A C   1 
ATOM   1089 O  O   . TYR A 1 139 ? 38.274 17.678 -3.000  1.00 19.38  ? 139 TYR A O   1 
ATOM   1090 C  CB  . TYR A 1 139 ? 35.723 15.955 -3.933  1.00 11.48  ? 139 TYR A CB  1 
ATOM   1091 C  CG  . TYR A 1 139 ? 36.822 15.530 -4.888  1.00 25.60  ? 139 TYR A CG  1 
ATOM   1092 C  CD1 . TYR A 1 139 ? 37.381 14.255 -4.800  1.00 27.47  ? 139 TYR A CD1 1 
ATOM   1093 C  CD2 . TYR A 1 139 ? 37.225 16.339 -5.953  1.00 31.08  ? 139 TYR A CD2 1 
ATOM   1094 C  CE1 . TYR A 1 139 ? 38.347 13.803 -5.703  1.00 36.43  ? 139 TYR A CE1 1 
ATOM   1095 C  CE2 . TYR A 1 139 ? 38.185 15.908 -6.871  1.00 37.12  ? 139 TYR A CE2 1 
ATOM   1096 C  CZ  . TYR A 1 139 ? 38.736 14.632 -6.755  1.00 44.37  ? 139 TYR A CZ  1 
ATOM   1097 O  OH  . TYR A 1 139 ? 39.685 14.201 -7.648  1.00 70.38  ? 139 TYR A OH  1 
ATOM   1098 N  N   . ASN A 1 140 ? 36.437 18.915 -3.366  1.00 15.20  ? 140 ASN A N   1 
ATOM   1099 C  CA  . ASN A 1 140 ? 37.198 20.098 -3.781  1.00 17.67  ? 140 ASN A CA  1 
ATOM   1100 C  C   . ASN A 1 140 ? 37.974 20.763 -2.651  1.00 21.96  ? 140 ASN A C   1 
ATOM   1101 O  O   . ASN A 1 140 ? 39.062 21.329 -2.816  1.00 23.29  ? 140 ASN A O   1 
ATOM   1102 C  CB  . ASN A 1 140 ? 36.303 21.110 -4.526  1.00 20.81  ? 140 ASN A CB  1 
ATOM   1103 C  CG  . ASN A 1 140 ? 36.074 20.617 -5.930  1.00 24.77  ? 140 ASN A CG  1 
ATOM   1104 O  OD1 . ASN A 1 140 ? 34.964 20.202 -6.294  1.00 34.74  ? 140 ASN A OD1 1 
ATOM   1105 N  ND2 . ASN A 1 140 ? 37.152 20.603 -6.717  1.00 32.27  ? 140 ASN A ND2 1 
ATOM   1106 N  N   . GLN A 1 141 ? 37.443 20.662 -1.461  1.00 15.45  ? 141 GLN A N   1 
ATOM   1107 C  CA  . GLN A 1 141 ? 38.161 21.266 -0.353  1.00 16.26  ? 141 GLN A CA  1 
ATOM   1108 C  C   . GLN A 1 141 ? 39.278 20.409 0.193   1.00 27.46  ? 141 GLN A C   1 
ATOM   1109 O  O   . GLN A 1 141 ? 40.299 20.961 0.571   1.00 24.01  ? 141 GLN A O   1 
ATOM   1110 C  CB  . GLN A 1 141 ? 37.234 21.675 0.799   1.00 17.85  ? 141 GLN A CB  1 
ATOM   1111 C  CG  . GLN A 1 141 ? 36.317 22.844 0.401   1.00 21.05  ? 141 GLN A CG  1 
ATOM   1112 C  CD  . GLN A 1 141 ? 37.025 24.078 -0.154  1.00 37.93  ? 141 GLN A CD  1 
ATOM   1113 O  OE1 . GLN A 1 141 ? 36.804 24.504 -1.323  1.00 30.34  ? 141 GLN A OE1 1 
ATOM   1114 N  NE2 . GLN A 1 141 ? 37.810 24.707 0.710   1.00 29.01  ? 141 GLN A NE2 1 
ATOM   1115 N  N   . THR A 1 142 ? 39.065 19.077 0.289   1.00 16.63  ? 142 THR A N   1 
ATOM   1116 C  CA  . THR A 1 142 ? 40.072 18.134 0.797   1.00 14.65  ? 142 THR A CA  1 
ATOM   1117 C  C   . THR A 1 142 ? 40.198 16.945 -0.137  1.00 21.14  ? 142 THR A C   1 
ATOM   1118 O  O   . THR A 1 142 ? 39.809 15.837 0.193   1.00 19.77  ? 142 THR A O   1 
ATOM   1119 C  CB  . THR A 1 142 ? 39.708 17.615 2.218   1.00 21.39  ? 142 THR A CB  1 
ATOM   1120 O  OG1 . THR A 1 142 ? 38.404 17.058 2.209   1.00 25.14  ? 142 THR A OG1 1 
ATOM   1121 C  CG2 . THR A 1 142 ? 39.658 18.794 3.165   1.00 19.98  ? 142 THR A CG2 1 
ATOM   1122 N  N   . PRO A 1 143 ? 40.736 17.181 -1.308  1.00 26.23  ? 143 PRO A N   1 
ATOM   1123 C  CA  . PRO A 1 143 ? 40.853 16.158 -2.342  1.00 22.82  ? 143 PRO A CA  1 
ATOM   1124 C  C   . PRO A 1 143 ? 41.604 14.865 -1.984  1.00 12.83  ? 143 PRO A C   1 
ATOM   1125 O  O   . PRO A 1 143 ? 41.181 13.757 -2.330  1.00 19.00  ? 143 PRO A O   1 
ATOM   1126 C  CB  . PRO A 1 143 ? 41.553 16.874 -3.525  1.00 19.03  ? 143 PRO A CB  1 
ATOM   1127 C  CG  . PRO A 1 143 ? 42.091 18.228 -3.023  1.00 18.30  ? 143 PRO A CG  1 
ATOM   1128 C  CD  . PRO A 1 143 ? 41.491 18.434 -1.639  1.00 21.10  ? 143 PRO A CD  1 
ATOM   1129 N  N   . ASN A 1 144 ? 42.790 15.006 -1.390  1.00 10.42  ? 144 ASN A N   1 
ATOM   1130 C  CA  . ASN A 1 144 ? 43.550 13.830 -1.113  1.00 11.91  ? 144 ASN A CA  1 
ATOM   1131 C  C   . ASN A 1 144 ? 42.824 12.923 -0.172  1.00 19.53  ? 144 ASN A C   1 
ATOM   1132 O  O   . ASN A 1 144 ? 42.798 11.716 -0.376  1.00 17.25  ? 144 ASN A O   1 
ATOM   1133 C  CB  . ASN A 1 144 ? 44.901 14.170 -0.529  1.00 11.97  ? 144 ASN A CB  1 
ATOM   1134 C  CG  . ASN A 1 144 ? 45.823 14.730 -1.580  1.00 36.55  ? 144 ASN A CG  1 
ATOM   1135 O  OD1 . ASN A 1 144 ? 45.568 14.643 -2.783  1.00 41.89  ? 144 ASN A OD1 1 
ATOM   1136 N  ND2 . ASN A 1 144 ? 46.878 15.346 -1.115  1.00 26.23  ? 144 ASN A ND2 1 
ATOM   1137 N  N   . ARG A 1 145 ? 42.223 13.513 0.859   1.00 18.22  ? 145 ARG A N   1 
ATOM   1138 C  CA  . ARG A 1 145 ? 41.479 12.709 1.821   1.00 16.71  ? 145 ARG A CA  1 
ATOM   1139 C  C   . ARG A 1 145 ? 40.219 12.139 1.166   1.00 14.66  ? 145 ARG A C   1 
ATOM   1140 O  O   . ARG A 1 145 ? 39.920 10.939 1.258   1.00 21.28  ? 145 ARG A O   1 
ATOM   1141 C  CB  . ARG A 1 145 ? 41.113 13.441 3.126   1.00 14.07  ? 145 ARG A CB  1 
ATOM   1142 C  CG  . ARG A 1 145 ? 40.565 12.482 4.203   1.00 26.73  ? 145 ARG A CG  1 
ATOM   1143 C  CD  . ARG A 1 145 ? 39.216 12.924 4.712   1.00 22.22  ? 145 ARG A CD  1 
ATOM   1144 N  NE  . ARG A 1 145 ? 38.698 12.182 5.868   1.00 20.01  ? 145 ARG A NE  1 
ATOM   1145 C  CZ  . ARG A 1 145 ? 38.715 12.643 7.124   1.00 29.46  ? 145 ARG A CZ  1 
ATOM   1146 N  NH1 . ARG A 1 145 ? 39.289 13.781 7.406   1.00 17.83  ? 145 ARG A NH1 1 
ATOM   1147 N  NH2 . ARG A 1 145 ? 38.151 11.971 8.134   1.00 14.55  ? 145 ARG A NH2 1 
ATOM   1148 N  N   . ALA A 1 146 ? 39.492 13.017 0.457   1.00 11.47  ? 146 ALA A N   1 
ATOM   1149 C  CA  . ALA A 1 146 ? 38.286 12.591 -0.205  1.00 8.42   ? 146 ALA A CA  1 
ATOM   1150 C  C   . ALA A 1 146 ? 38.600 11.434 -1.143  1.00 17.99  ? 146 ALA A C   1 
ATOM   1151 O  O   . ALA A 1 146 ? 37.834 10.486 -1.259  1.00 19.17  ? 146 ALA A O   1 
ATOM   1152 C  CB  . ALA A 1 146 ? 37.584 13.737 -0.907  1.00 14.60  ? 146 ALA A CB  1 
ATOM   1153 N  N   . LYS A 1 147 ? 39.735 11.555 -1.829  1.00 17.25  ? 147 LYS A N   1 
ATOM   1154 C  CA  . LYS A 1 147 ? 40.220 10.558 -2.784  1.00 22.59  ? 147 LYS A CA  1 
ATOM   1155 C  C   . LYS A 1 147 ? 40.411 9.180  -2.123  1.00 19.19  ? 147 LYS A C   1 
ATOM   1156 O  O   . LYS A 1 147 ? 40.095 8.120  -2.692  1.00 17.40  ? 147 LYS A O   1 
ATOM   1157 C  CB  . LYS A 1 147 ? 41.547 11.046 -3.360  1.00 21.78  ? 147 LYS A CB  1 
ATOM   1158 C  CG  . LYS A 1 147 ? 41.801 10.564 -4.762  1.00 48.35  ? 147 LYS A CG  1 
ATOM   1159 C  CD  . LYS A 1 147 ? 42.995 11.248 -5.394  1.00 100.00 ? 147 LYS A CD  1 
ATOM   1160 C  CE  . LYS A 1 147 ? 42.601 12.241 -6.471  1.00 100.00 ? 147 LYS A CE  1 
ATOM   1161 N  NZ  . LYS A 1 147 ? 42.534 13.619 -5.971  1.00 47.70  ? 147 LYS A NZ  1 
ATOM   1162 N  N   . ARG A 1 148 ? 40.967 9.188  -0.921  1.00 13.46  ? 148 ARG A N   1 
ATOM   1163 C  CA  . ARG A 1 148 ? 41.165 7.952  -0.214  1.00 9.35   ? 148 ARG A CA  1 
ATOM   1164 C  C   . ARG A 1 148 ? 39.876 7.312  0.194   1.00 13.56  ? 148 ARG A C   1 
ATOM   1165 O  O   . ARG A 1 148 ? 39.715 6.110  0.052   1.00 19.16  ? 148 ARG A O   1 
ATOM   1166 C  CB  . ARG A 1 148 ? 41.995 8.161  1.006   1.00 12.81  ? 148 ARG A CB  1 
ATOM   1167 C  CG  . ARG A 1 148 ? 43.437 8.477  0.693   1.00 18.85  ? 148 ARG A CG  1 
ATOM   1168 C  CD  . ARG A 1 148 ? 44.328 8.349  1.914   1.00 12.54  ? 148 ARG A CD  1 
ATOM   1169 N  NE  . ARG A 1 148 ? 44.043 9.393  2.916   1.00 19.81  ? 148 ARG A NE  1 
ATOM   1170 C  CZ  . ARG A 1 148 ? 44.689 10.563 2.966   1.00 23.83  ? 148 ARG A CZ  1 
ATOM   1171 N  NH1 . ARG A 1 148 ? 45.612 10.915 2.075   1.00 16.36  ? 148 ARG A NH1 1 
ATOM   1172 N  NH2 . ARG A 1 148 ? 44.397 11.402 3.929   1.00 16.04  ? 148 ARG A NH2 1 
ATOM   1173 N  N   . VAL A 1 149 ? 38.951 8.097  0.683   1.00 12.20  ? 149 VAL A N   1 
ATOM   1174 C  CA  . VAL A 1 149 ? 37.663 7.542  1.103   1.00 8.79   ? 149 VAL A CA  1 
ATOM   1175 C  C   . VAL A 1 149 ? 36.837 7.039  -0.034  1.00 11.46  ? 149 VAL A C   1 
ATOM   1176 O  O   . VAL A 1 149 ? 36.175 5.998  0.061   1.00 12.53  ? 149 VAL A O   1 
ATOM   1177 C  CB  . VAL A 1 149 ? 36.904 8.563  1.911   1.00 16.72  ? 149 VAL A CB  1 
ATOM   1178 C  CG1 . VAL A 1 149 ? 35.522 8.026  2.265   1.00 10.80  ? 149 VAL A CG1 1 
ATOM   1179 C  CG2 . VAL A 1 149 ? 37.720 8.844  3.163   1.00 11.00  ? 149 VAL A CG2 1 
ATOM   1180 N  N   . ILE A 1 150 ? 36.875 7.788  -1.132  1.00 12.92  ? 150 ILE A N   1 
ATOM   1181 C  CA  . ILE A 1 150 ? 36.125 7.380  -2.327  1.00 15.35  ? 150 ILE A CA  1 
ATOM   1182 C  C   . ILE A 1 150 ? 36.659 6.073  -2.946  1.00 16.76  ? 150 ILE A C   1 
ATOM   1183 O  O   . ILE A 1 150 ? 35.903 5.223  -3.438  1.00 20.59  ? 150 ILE A O   1 
ATOM   1184 C  CB  . ILE A 1 150 ? 36.000 8.449  -3.422  1.00 27.08  ? 150 ILE A CB  1 
ATOM   1185 C  CG1 . ILE A 1 150 ? 35.191 9.638  -2.932  1.00 20.54  ? 150 ILE A CG1 1 
ATOM   1186 C  CG2 . ILE A 1 150 ? 35.272 7.814  -4.607  1.00 22.20  ? 150 ILE A CG2 1 
ATOM   1187 C  CD1 . ILE A 1 150 ? 35.399 10.846 -3.809  1.00 13.08  ? 150 ILE A CD1 1 
ATOM   1188 N  N   . THR A 1 151 ? 37.972 5.923  -2.941  1.00 13.23  ? 151 THR A N   1 
ATOM   1189 C  CA  . THR A 1 151 ? 38.564 4.695  -3.456  1.00 20.77  ? 151 THR A CA  1 
ATOM   1190 C  C   . THR A 1 151 ? 38.180 3.497  -2.615  1.00 19.04  ? 151 THR A C   1 
ATOM   1191 O  O   . THR A 1 151 ? 37.982 2.391  -3.115  1.00 26.18  ? 151 THR A O   1 
ATOM   1192 C  CB  . THR A 1 151 ? 40.097 4.789  -3.503  1.00 25.64  ? 151 THR A CB  1 
ATOM   1193 O  OG1 . THR A 1 151 ? 40.416 5.662  -4.545  1.00 41.29  ? 151 THR A OG1 1 
ATOM   1194 C  CG2 . THR A 1 151 ? 40.768 3.410  -3.706  1.00 18.36  ? 151 THR A CG2 1 
ATOM   1195 N  N   . THR A 1 152 ? 38.133 3.728  -1.311  1.00 19.26  ? 152 THR A N   1 
ATOM   1196 C  CA  . THR A 1 152 ? 37.802 2.687  -0.359  1.00 17.63  ? 152 THR A CA  1 
ATOM   1197 C  C   . THR A 1 152 ? 36.352 2.286  -0.589  1.00 27.23  ? 152 THR A C   1 
ATOM   1198 O  O   . THR A 1 152 ? 35.935 1.146  -0.591  1.00 16.04  ? 152 THR A O   1 
ATOM   1199 C  CB  . THR A 1 152 ? 38.002 3.206  1.099   1.00 9.25   ? 152 THR A CB  1 
ATOM   1200 O  OG1 . THR A 1 152 ? 39.351 3.612  1.326   1.00 15.01  ? 152 THR A OG1 1 
ATOM   1201 C  CG2 . THR A 1 152 ? 37.696 2.088  2.082   1.00 14.77  ? 152 THR A CG2 1 
ATOM   1202 N  N   . PHE A 1 153 ? 35.569 3.286  -0.806  1.00 18.54  ? 153 PHE A N   1 
ATOM   1203 C  CA  . PHE A 1 153 ? 34.189 3.071  -1.038  1.00 14.79  ? 153 PHE A CA  1 
ATOM   1204 C  C   . PHE A 1 153 ? 33.931 2.344  -2.359  1.00 20.57  ? 153 PHE A C   1 
ATOM   1205 O  O   . PHE A 1 153 ? 33.117 1.453  -2.493  1.00 22.35  ? 153 PHE A O   1 
ATOM   1206 C  CB  . PHE A 1 153 ? 33.607 4.485  -1.103  1.00 27.72  ? 153 PHE A CB  1 
ATOM   1207 C  CG  . PHE A 1 153 ? 32.163 4.346  -0.934  1.00 23.83  ? 153 PHE A CG  1 
ATOM   1208 C  CD1 . PHE A 1 153 ? 31.627 4.287  0.350   1.00 67.87  ? 153 PHE A CD1 1 
ATOM   1209 C  CD2 . PHE A 1 153 ? 31.333 4.162  -2.040  1.00 78.36  ? 153 PHE A CD2 1 
ATOM   1210 C  CE1 . PHE A 1 153 ? 30.261 4.084  0.527   1.00 43.65  ? 153 PHE A CE1 1 
ATOM   1211 C  CE2 . PHE A 1 153 ? 29.958 3.976  -1.881  1.00 65.18  ? 153 PHE A CE2 1 
ATOM   1212 C  CZ  . PHE A 1 153 ? 29.434 3.938  -0.589  1.00 81.50  ? 153 PHE A CZ  1 
ATOM   1213 N  N   . ARG A 1 154 ? 34.636 2.748  -3.366  1.00 20.81  ? 154 ARG A N   1 
ATOM   1214 C  CA  . ARG A 1 154 ? 34.461 2.154  -4.657  1.00 20.71  ? 154 ARG A CA  1 
ATOM   1215 C  C   . ARG A 1 154 ? 34.915 0.712  -4.735  1.00 31.59  ? 154 ARG A C   1 
ATOM   1216 O  O   . ARG A 1 154 ? 34.216 -0.128 -5.251  1.00 30.68  ? 154 ARG A O   1 
ATOM   1217 C  CB  . ARG A 1 154 ? 35.299 2.916  -5.677  1.00 24.90  ? 154 ARG A CB  1 
ATOM   1218 C  CG  . ARG A 1 154 ? 35.053 2.408  -7.103  1.00 46.14  ? 154 ARG A CG  1 
ATOM   1219 C  CD  . ARG A 1 154 ? 35.539 3.366  -8.188  1.00 53.44  ? 154 ARG A CD  1 
ATOM   1220 N  NE  . ARG A 1 154 ? 36.975 3.598  -8.094  1.00 32.09  ? 154 ARG A NE  1 
ATOM   1221 C  CZ  . ARG A 1 154 ? 37.891 2.737  -8.514  1.00 100.00 ? 154 ARG A CZ  1 
ATOM   1222 N  NH1 . ARG A 1 154 ? 37.561 1.574  -9.102  1.00 78.00  ? 154 ARG A NH1 1 
ATOM   1223 N  NH2 . ARG A 1 154 ? 39.177 3.065  -8.343  1.00 67.64  ? 154 ARG A NH2 1 
ATOM   1224 N  N   . THR A 1 155 ? 36.122 0.464  -4.243  1.00 23.88  ? 155 THR A N   1 
ATOM   1225 C  CA  . THR A 1 155 ? 36.781 -0.812 -4.306  1.00 25.58  ? 155 THR A CA  1 
ATOM   1226 C  C   . THR A 1 155 ? 36.518 -1.797 -3.198  1.00 32.21  ? 155 THR A C   1 
ATOM   1227 O  O   . THR A 1 155 ? 36.708 -2.981 -3.389  1.00 30.19  ? 155 THR A O   1 
ATOM   1228 C  CB  . THR A 1 155 ? 38.297 -0.642 -4.514  1.00 25.10  ? 155 THR A CB  1 
ATOM   1229 O  OG1 . THR A 1 155 ? 38.933 -0.247 -3.320  1.00 24.71  ? 155 THR A OG1 1 
ATOM   1230 C  CG2 . THR A 1 155 ? 38.512 0.411  -5.577  1.00 23.74  ? 155 THR A CG2 1 
ATOM   1231 N  N   . GLY A 1 156 ? 36.139 -1.315 -2.033  1.00 19.43  ? 156 GLY A N   1 
ATOM   1232 C  CA  . GLY A 1 156 ? 35.934 -2.183 -0.926  1.00 16.14  ? 156 GLY A CA  1 
ATOM   1233 C  C   . GLY A 1 156 ? 37.254 -2.797 -0.453  1.00 23.73  ? 156 GLY A C   1 
ATOM   1234 O  O   . GLY A 1 156 ? 37.233 -3.860 0.146   1.00 22.47  ? 156 GLY A O   1 
ATOM   1235 N  N   . THR A 1 157 ? 38.411 -2.135 -0.712  1.00 19.20  ? 157 THR A N   1 
ATOM   1236 C  CA  . THR A 1 157 ? 39.731 -2.601 -0.217  1.00 18.17  ? 157 THR A CA  1 
ATOM   1237 C  C   . THR A 1 157 ? 40.393 -1.439 0.507   1.00 17.17  ? 157 THR A C   1 
ATOM   1238 O  O   . THR A 1 157 ? 39.943 -0.341 0.334   1.00 23.89  ? 157 THR A O   1 
ATOM   1239 C  CB  . THR A 1 157 ? 40.687 -2.952 -1.370  1.00 30.02  ? 157 THR A CB  1 
ATOM   1240 O  OG1 . THR A 1 157 ? 40.995 -1.746 -2.037  1.00 33.97  ? 157 THR A OG1 1 
ATOM   1241 C  CG2 . THR A 1 157 ? 40.027 -3.919 -2.353  1.00 21.49  ? 157 THR A CG2 1 
ATOM   1242 N  N   . TRP A 1 158 ? 41.491 -1.674 1.211   1.00 21.61  ? 158 TRP A N   1 
ATOM   1243 C  CA  . TRP A 1 158 ? 42.225 -0.643 1.941   1.00 21.75  ? 158 TRP A CA  1 
ATOM   1244 C  C   . TRP A 1 158 ? 43.417 -0.132 1.180   1.00 21.25  ? 158 TRP A C   1 
ATOM   1245 O  O   . TRP A 1 158 ? 44.300 0.522  1.738   1.00 22.92  ? 158 TRP A O   1 
ATOM   1246 C  CB  . TRP A 1 158 ? 42.798 -1.220 3.257   1.00 19.57  ? 158 TRP A CB  1 
ATOM   1247 C  CG  . TRP A 1 158 ? 41.732 -1.612 4.245   1.00 16.20  ? 158 TRP A CG  1 
ATOM   1248 C  CD1 . TRP A 1 158 ? 41.431 -2.869 4.611   1.00 17.01  ? 158 TRP A CD1 1 
ATOM   1249 C  CD2 . TRP A 1 158 ? 40.851 -0.747 4.994   1.00 19.47  ? 158 TRP A CD2 1 
ATOM   1250 N  NE1 . TRP A 1 158 ? 40.380 -2.874 5.476   1.00 18.48  ? 158 TRP A NE1 1 
ATOM   1251 C  CE2 . TRP A 1 158 ? 40.014 -1.584 5.774   1.00 15.74  ? 158 TRP A CE2 1 
ATOM   1252 C  CE3 . TRP A 1 158 ? 40.710 0.634  5.128   1.00 19.15  ? 158 TRP A CE3 1 
ATOM   1253 C  CZ2 . TRP A 1 158 ? 39.061 -1.093 6.669   1.00 16.27  ? 158 TRP A CZ2 1 
ATOM   1254 C  CZ3 . TRP A 1 158 ? 39.732 1.099  5.998   1.00 18.78  ? 158 TRP A CZ3 1 
ATOM   1255 C  CH2 . TRP A 1 158 ? 38.925 0.260  6.771   1.00 16.78  ? 158 TRP A CH2 1 
ATOM   1256 N  N   . ASP A 1 159 ? 43.468 -0.460 -0.082  1.00 19.67  ? 159 ASP A N   1 
ATOM   1257 C  CA  . ASP A 1 159 ? 44.611 -0.059 -0.866  1.00 23.89  ? 159 ASP A CA  1 
ATOM   1258 C  C   . ASP A 1 159 ? 45.062 1.385  -0.722  1.00 33.00  ? 159 ASP A C   1 
ATOM   1259 O  O   . ASP A 1 159 ? 46.249 1.624  -0.586  1.00 25.30  ? 159 ASP A O   1 
ATOM   1260 C  CB  . ASP A 1 159 ? 44.565 -0.559 -2.314  1.00 31.34  ? 159 ASP A CB  1 
ATOM   1261 C  CG  . ASP A 1 159 ? 44.415 -2.062 -2.321  1.00 54.29  ? 159 ASP A CG  1 
ATOM   1262 O  OD1 . ASP A 1 159 ? 44.861 -2.794 -1.437  1.00 48.78  ? 159 ASP A OD1 1 
ATOM   1263 O  OD2 . ASP A 1 159 ? 43.727 -2.499 -3.348  1.00 64.76  ? 159 ASP A OD2 1 
ATOM   1264 N  N   . ALA A 1 160 ? 44.108 2.333  -0.742  1.00 16.18  ? 160 ALA A N   1 
ATOM   1265 C  CA  . ALA A 1 160 ? 44.397 3.745  -0.618  1.00 15.07  ? 160 ALA A CA  1 
ATOM   1266 C  C   . ALA A 1 160 ? 45.078 4.049  0.682   1.00 20.79  ? 160 ALA A C   1 
ATOM   1267 O  O   . ALA A 1 160 ? 45.739 5.058  0.840   1.00 22.25  ? 160 ALA A O   1 
ATOM   1268 C  CB  . ALA A 1 160 ? 43.153 4.602  -0.797  1.00 26.44  ? 160 ALA A CB  1 
ATOM   1269 N  N   . TYR A 1 161 ? 44.970 3.162  1.634   1.00 19.94  ? 161 TYR A N   1 
ATOM   1270 C  CA  . TYR A 1 161 ? 45.634 3.514  2.841   1.00 16.16  ? 161 TYR A CA  1 
ATOM   1271 C  C   . TYR A 1 161 ? 46.890 2.716  3.036   1.00 40.36  ? 161 TYR A C   1 
ATOM   1272 O  O   . TYR A 1 161 ? 47.490 2.789  4.098   1.00 41.31  ? 161 TYR A O   1 
ATOM   1273 C  CB  . TYR A 1 161 ? 44.720 3.268  4.024   1.00 13.99  ? 161 TYR A CB  1 
ATOM   1274 C  CG  . TYR A 1 161 ? 43.674 4.312  4.103   1.00 12.57  ? 161 TYR A CG  1 
ATOM   1275 C  CD1 . TYR A 1 161 ? 42.500 4.130  3.386   1.00 14.25  ? 161 TYR A CD1 1 
ATOM   1276 C  CD2 . TYR A 1 161 ? 43.857 5.464  4.872   1.00 13.94  ? 161 TYR A CD2 1 
ATOM   1277 C  CE1 . TYR A 1 161 ? 41.471 5.062  3.476   1.00 15.01  ? 161 TYR A CE1 1 
ATOM   1278 C  CE2 . TYR A 1 161 ? 42.830 6.405  4.945   1.00 10.42  ? 161 TYR A CE2 1 
ATOM   1279 C  CZ  . TYR A 1 161 ? 41.649 6.231  4.216   1.00 20.39  ? 161 TYR A CZ  1 
ATOM   1280 O  OH  . TYR A 1 161 ? 40.603 7.165  4.293   1.00 11.65  ? 161 TYR A OH  1 
ATOM   1281 N  N   . LYS A 1 162 ? 47.277 1.926  2.049   1.00 62.26  ? 162 LYS A N   1 
ATOM   1282 C  CA  . LYS A 1 162 ? 48.477 1.123  2.213   1.00 54.27  ? 162 LYS A CA  1 
ATOM   1283 C  C   . LYS A 1 162 ? 49.641 1.719  1.439   1.00 60.41  ? 162 LYS A C   1 
ATOM   1284 O  O   . LYS A 1 162 ? 50.530 2.351  2.017   1.00 70.31  ? 162 LYS A O   1 
ATOM   1285 C  CB  . LYS A 1 162 ? 48.215 -0.325 1.862   1.00 100.00 ? 162 LYS A CB  1 
ATOM   1286 C  CG  . LYS A 1 162 ? 47.174 -0.938 2.789   1.00 94.67  ? 162 LYS A CG  1 
ATOM   1287 C  CD  . LYS A 1 162 ? 46.039 -1.628 2.049   1.00 100.00 ? 162 LYS A CD  1 
ATOM   1288 C  CE  . LYS A 1 162 ? 46.481 -2.314 0.767   1.00 100.00 ? 162 LYS A CE  1 
ATOM   1289 N  NZ  . LYS A 1 162 ? 45.751 -3.572 0.513   1.00 98.79  ? 162 LYS A NZ  1 
HETATM 1290 CL CL  . CL  B 2 .   ? 43.020 16.286 2.253   1.00 13.71  ? 173 CL  A CL  1 
HETATM 1291 CL CL  . CL  C 2 .   ? 31.919 15.523 23.871  0.50 17.64  ? 178 CL  A CL  1 
HETATM 1292 C  C1  . BME D 3 .   ? 32.002 -1.361 15.020  1.00 30.40  ? 901 BME A C1  1 
HETATM 1293 C  C2  . BME D 3 .   ? 31.950 -1.062 13.537  1.00 44.74  ? 901 BME A C2  1 
HETATM 1294 O  O1  . BME D 3 .   ? 33.164 -0.704 15.577  1.00 38.75  ? 901 BME A O1  1 
HETATM 1295 S  S2  . BME D 3 .   ? 33.606 -1.290 12.888  1.00 49.45  ? 901 BME A S2  1 
HETATM 1296 C  C1  . BME E 3 .   ? 33.696 -3.221 9.472   1.00 90.11  ? 902 BME A C1  1 
HETATM 1297 C  C2  . BME E 3 .   ? 32.720 -2.159 10.015  1.00 47.76  ? 902 BME A C2  1 
HETATM 1298 O  O1  . BME E 3 .   ? 34.924 -2.602 9.146   1.00 64.77  ? 902 BME A O1  1 
HETATM 1299 S  S2  . BME E 3 .   ? 33.551 -0.796 10.888  1.00 98.43  ? 902 BME A S2  1 
HETATM 1300 O  O   . HOH F 4 .   ? 38.227 12.488 18.112  1.00 15.58  ? 171 HOH A O   1 
HETATM 1301 O  O   . HOH F 4 .   ? 35.181 19.239 3.240   1.00 54.39  ? 172 HOH A O   1 
HETATM 1302 O  O   . HOH F 4 .   ? 42.160 22.990 0.912   1.00 22.75  ? 174 HOH A O   1 
HETATM 1303 O  O   . HOH F 4 .   ? 41.358 1.973  0.032   1.00 26.56  ? 175 HOH A O   1 
HETATM 1304 O  O   . HOH F 4 .   ? 40.556 26.066 29.063  1.00 52.66  ? 176 HOH A O   1 
HETATM 1305 O  O   . HOH F 4 .   ? 33.065 -7.904 4.160   1.00 37.20  ? 177 HOH A O   1 
HETATM 1306 O  O   . HOH F 4 .   ? 40.367 13.079 19.813  1.00 15.19  ? 179 HOH A O   1 
HETATM 1307 O  O   . HOH F 4 .   ? 44.727 10.696 -1.966  1.00 26.91  ? 180 HOH A O   1 
HETATM 1308 O  O   . HOH F 4 .   ? 28.423 -7.084 5.032   1.00 29.49  ? 181 HOH A O   1 
HETATM 1309 O  O   . HOH F 4 .   ? 33.398 12.924 22.224  1.00 33.70  ? 182 HOH A O   1 
HETATM 1310 O  O   . HOH F 4 .   ? 34.331 11.461 28.594  1.00 35.61  ? 183 HOH A O   1 
HETATM 1311 O  O   . HOH F 4 .   ? 48.762 10.006 28.207  1.00 53.87  ? 184 HOH A O   1 
HETATM 1312 O  O   . HOH F 4 .   ? 31.050 5.450  22.986  1.00 49.35  ? 185 HOH A O   1 
HETATM 1313 O  O   . HOH F 4 .   ? 40.727 5.342  20.520  1.00 37.99  ? 186 HOH A O   1 
HETATM 1314 O  O   . HOH F 4 .   ? 44.675 -3.614 11.504  1.00 43.08  ? 187 HOH A O   1 
HETATM 1315 O  O   . HOH F 4 .   ? 39.291 22.821 -6.892  1.00 37.62  ? 188 HOH A O   1 
HETATM 1316 O  O   . HOH F 4 .   ? 50.659 18.067 19.251  1.00 51.93  ? 189 HOH A O   1 
HETATM 1317 O  O   . HOH F 4 .   ? 36.455 27.542 15.787  1.00 52.62  ? 190 HOH A O   1 
HETATM 1318 O  O   . HOH F 4 .   ? 37.026 29.847 14.159  1.00 44.16  ? 191 HOH A O   1 
HETATM 1319 O  O   . HOH F 4 .   ? 19.523 -2.381 3.078   1.00 33.27  ? 193 HOH A O   1 
HETATM 1320 O  O   . HOH F 4 .   ? 35.268 5.873  -11.554 1.00 61.07  ? 194 HOH A O   1 
HETATM 1321 O  O   . HOH F 4 .   ? 36.891 -1.259 10.611  1.00 23.12  ? 195 HOH A O   1 
HETATM 1322 O  O   . HOH F 4 .   ? 46.341 20.501 30.539  1.00 41.43  ? 196 HOH A O   1 
HETATM 1323 O  O   . HOH F 4 .   ? 24.682 12.397 -4.380  1.00 48.33  ? 197 HOH A O   1 
HETATM 1324 O  O   . HOH F 4 .   ? 31.055 25.745 28.121  1.00 31.11  ? 198 HOH A O   1 
HETATM 1325 O  O   . HOH F 4 .   ? 33.084 18.422 22.402  1.00 32.06  ? 200 HOH A O   1 
HETATM 1326 O  O   . HOH F 4 .   ? 29.640 8.138  22.191  1.00 29.44  ? 201 HOH A O   1 
HETATM 1327 O  O   . HOH F 4 .   ? 37.687 19.595 12.909  1.00 35.61  ? 203 HOH A O   1 
HETATM 1328 O  O   . HOH F 4 .   ? 39.927 18.672 11.287  1.00 48.54  ? 204 HOH A O   1 
HETATM 1329 O  O   . HOH F 4 .   ? 26.005 17.620 9.581   1.00 43.81  ? 206 HOH A O   1 
HETATM 1330 O  O   . HOH F 4 .   ? 41.085 16.595 8.543   1.00 54.10  ? 207 HOH A O   1 
HETATM 1331 O  O   . HOH F 4 .   ? 35.430 11.589 4.963   1.00 17.24  ? 208 HOH A O   1 
HETATM 1332 O  O   . HOH F 4 .   ? 35.210 -5.719 0.774   1.00 28.76  ? 210 HOH A O   1 
HETATM 1333 O  O   . HOH F 4 .   ? 46.529 9.992  -0.466  1.00 30.65  ? 211 HOH A O   1 
HETATM 1334 O  O   . HOH F 4 .   ? 25.419 -1.733 -1.416  1.00 32.45  ? 213 HOH A O   1 
HETATM 1335 O  O   . HOH F 4 .   ? 33.196 14.214 26.117  1.00 18.10  ? 215 HOH A O   1 
HETATM 1336 O  O   . HOH F 4 .   ? 36.251 9.635  -9.155  1.00 38.09  ? 216 HOH A O   1 
HETATM 1337 O  O   . HOH F 4 .   ? 33.347 -0.958 -9.541  1.00 46.27  ? 217 HOH A O   1 
HETATM 1338 O  O   . HOH F 4 .   ? 28.360 8.904  -11.900 1.00 48.78  ? 218 HOH A O   1 
HETATM 1339 O  O   . HOH F 4 .   ? 27.241 11.779 -11.344 1.00 31.46  ? 219 HOH A O   1 
HETATM 1340 O  O   . HOH F 4 .   ? 34.253 18.245 -8.639  1.00 52.24  ? 220 HOH A O   1 
HETATM 1341 O  O   . HOH F 4 .   ? 44.297 5.825  17.342  1.00 43.73  ? 221 HOH A O   1 
HETATM 1342 O  O   . HOH F 4 .   ? 29.658 25.479 17.606  1.00 43.78  ? 222 HOH A O   1 
HETATM 1343 O  O   . HOH F 4 .   ? 42.506 -4.618 12.650  1.00 29.34  ? 223 HOH A O   1 
HETATM 1344 O  O   . HOH F 4 .   ? 36.097 17.152 12.483  1.00 58.85  ? 224 HOH A O   1 
HETATM 1345 O  O   . HOH F 4 .   ? 34.137 15.944 13.179  1.00 54.62  ? 225 HOH A O   1 
HETATM 1346 O  O   . HOH F 4 .   ? 23.790 -2.540 10.497  1.00 56.00  ? 226 HOH A O   1 
HETATM 1347 O  O   . HOH F 4 .   ? 49.084 7.092  11.542  1.00 41.08  ? 227 HOH A O   1 
HETATM 1348 O  O   . HOH F 4 .   ? 42.193 17.064 11.661  1.00 46.79  ? 229 HOH A O   1 
HETATM 1349 O  O   . HOH F 4 .   ? 42.835 -4.702 1.335   1.00 42.57  ? 231 HOH A O   1 
HETATM 1350 O  O   . HOH F 4 .   ? 29.999 0.545  -11.596 1.00 47.53  ? 235 HOH A O   1 
HETATM 1351 O  O   . HOH F 4 .   ? 46.695 19.279 12.012  1.00 60.28  ? 236 HOH A O   1 
HETATM 1352 O  O   . HOH F 4 .   ? 40.638 16.266 6.135   1.00 49.49  ? 237 HOH A O   1 
HETATM 1353 O  O   . HOH F 4 .   ? 35.445 -2.273 -7.504  1.00 38.45  ? 238 HOH A O   1 
HETATM 1354 O  O   . HOH F 4 .   ? 36.100 12.842 28.338  1.00 32.70  ? 239 HOH A O   1 
HETATM 1355 O  O   . HOH F 4 .   ? 43.793 5.331  25.367  1.00 33.44  ? 240 HOH A O   1 
HETATM 1356 O  O   . HOH F 4 .   ? 25.595 10.371 17.290  1.00 57.32  ? 242 HOH A O   1 
HETATM 1357 O  O   . HOH F 4 .   ? 47.059 4.239  11.582  1.00 39.48  ? 244 HOH A O   1 
HETATM 1358 O  O   . HOH F 4 .   ? 47.404 13.727 2.944   1.00 52.36  ? 245 HOH A O   1 
HETATM 1359 O  O   . HOH F 4 .   ? 30.641 16.068 20.205  1.00 52.22  ? 246 HOH A O   1 
HETATM 1360 O  O   . HOH F 4 .   ? 37.776 9.914  -7.492  1.00 32.97  ? 249 HOH A O   1 
HETATM 1361 O  O   . HOH F 4 .   ? 33.944 13.873 -11.028 1.00 57.50  ? 251 HOH A O   1 
HETATM 1362 O  O   . HOH F 4 .   ? 18.539 5.894  1.226   1.00 55.72  ? 253 HOH A O   1 
HETATM 1363 O  O   . HOH F 4 .   ? 37.027 15.489 10.674  1.00 36.05  ? 256 HOH A O   1 
HETATM 1364 O  O   . HOH F 4 .   ? 46.409 7.131  18.177  1.00 62.16  ? 257 HOH A O   1 
HETATM 1365 O  O   . HOH F 4 .   ? 46.745 10.911 30.622  1.00 66.92  ? 260 HOH A O   1 
HETATM 1366 O  O   . HOH F 4 .   ? 37.911 7.080  -7.814  1.00 48.46  ? 261 HOH A O   1 
HETATM 1367 O  O   . HOH F 4 .   ? 44.369 16.963 8.989   1.00 66.06  ? 263 HOH A O   1 
HETATM 1368 O  O   . HOH F 4 .   ? 34.261 15.571 15.935  1.00 50.07  ? 266 HOH A O   1 
HETATM 1369 O  O   . HOH F 4 .   ? 44.414 21.972 9.960   1.00 43.40  ? 269 HOH A O   1 
HETATM 1370 O  O   . HOH F 4 .   ? 30.028 18.515 -0.090  1.00 24.37  ? 270 HOH A O   1 
HETATM 1371 O  O   . HOH F 4 .   ? 31.235 12.046 15.289  1.00 32.21  ? 274 HOH A O   1 
HETATM 1372 O  O   . HOH F 4 .   ? 34.156 -4.306 -5.931  1.00 58.46  ? 277 HOH A O   1 
HETATM 1373 O  O   . HOH F 4 .   ? 41.260 25.963 31.231  1.00 47.35  ? 278 HOH A O   1 
HETATM 1374 O  O   . HOH F 4 .   ? 32.683 17.678 18.605  1.00 49.96  ? 280 HOH A O   1 
HETATM 1375 O  O   . HOH F 4 .   ? 32.050 20.539 21.035  1.00 43.31  ? 281 HOH A O   1 
HETATM 1376 O  O   . HOH F 4 .   ? 32.781 20.175 24.421  1.00 48.26  ? 282 HOH A O   1 
HETATM 1377 O  O   . HOH F 4 .   ? 44.557 3.962  16.050  1.00 44.96  ? 283 HOH A O   1 
HETATM 1378 O  O   . HOH F 4 .   ? 43.442 16.101 14.617  1.00 51.21  ? 285 HOH A O   1 
HETATM 1379 O  O   . HOH F 4 .   ? 50.133 16.749 27.302  1.00 60.05  ? 286 HOH A O   1 
HETATM 1380 O  O   . HOH F 4 .   ? 43.960 -1.206 15.465  1.00 38.19  ? 288 HOH A O   1 
HETATM 1381 O  O   . HOH F 4 .   ? 20.973 -6.556 5.152   1.00 49.90  ? 290 HOH A O   1 
HETATM 1382 O  O   . HOH F 4 .   ? 23.694 -5.954 -0.115  1.00 24.32  ? 291 HOH A O   1 
HETATM 1383 O  O   . HOH F 4 .   ? 47.543 1.529  10.496  1.00 54.83  ? 294 HOH A O   1 
HETATM 1384 O  O   . HOH F 4 .   ? 47.069 3.738  14.628  1.00 47.75  ? 295 HOH A O   1 
HETATM 1385 O  O   . HOH F 4 .   ? 33.124 13.531 14.805  1.00 32.22  ? 299 HOH A O   1 
HETATM 1386 O  O   . HOH F 4 .   ? 36.863 19.574 -9.785  1.00 59.28  ? 300 HOH A O   1 
HETATM 1387 O  O   . HOH F 4 .   ? 19.752 5.090  -1.343  1.00 66.90  ? 301 HOH A O   1 
HETATM 1388 O  O   . HOH F 4 .   ? 18.131 -1.637 6.769   1.00 59.38  ? 302 HOH A O   1 
HETATM 1389 O  O   . HOH F 4 .   ? 32.676 19.814 3.144   1.00 38.55  ? 303 HOH A O   1 
HETATM 1390 O  O   . HOH F 4 .   ? 33.994 19.532 5.351   1.00 61.94  ? 314 HOH A O   1 
HETATM 1391 O  O   . HOH F 4 .   ? 49.928 13.335 13.059  1.00 52.52  ? 315 HOH A O   1 
HETATM 1392 O  O   . HOH F 4 .   ? 37.642 18.862 7.324   1.00 52.28  ? 321 HOH A O   1 
HETATM 1393 O  O   . HOH F 4 .   ? 49.693 21.104 18.423  1.00 65.63  ? 322 HOH A O   1 
HETATM 1394 O  O   . HOH F 4 .   ? 46.795 26.249 23.999  1.00 68.09  ? 401 HOH A O   1 
HETATM 1395 O  O   . HOH F 4 .   ? 18.262 -3.812 5.251   1.00 50.28  ? 402 HOH A O   1 
HETATM 1396 O  O   . HOH F 4 .   ? 29.890 23.235 20.248  1.00 58.89  ? 403 HOH A O   1 
HETATM 1397 O  O   . HOH F 4 .   ? 30.302 22.474 17.175  1.00 54.87  ? 404 HOH A O   1 
HETATM 1398 O  O   . HOH F 4 .   ? 44.072 19.956 35.435  1.00 52.21  ? 405 HOH A O   1 
HETATM 1399 O  O   . HOH F 4 .   ? 38.400 12.186 27.438  1.00 54.82  ? 406 HOH A O   1 
HETATM 1400 O  O   . HOH F 4 .   ? 44.205 -5.786 -2.398  1.00 58.22  ? 407 HOH A O   1 
HETATM 1401 O  O   . HOH F 4 .   ? 33.886 20.758 33.647  1.00 44.01  ? 408 HOH A O   1 
HETATM 1402 O  O   . HOH F 4 .   ? 46.214 11.900 -4.147  1.00 53.79  ? 409 HOH A O   1 
HETATM 1403 O  O   . HOH F 4 .   ? 29.253 18.992 2.911   1.00 52.34  ? 410 HOH A O   1 
HETATM 1404 O  O   . HOH F 4 .   ? 28.404 1.677  18.457  1.00 59.41  ? 411 HOH A O   1 
HETATM 1405 O  O   . HOH F 4 .   ? 51.753 19.512 21.483  1.00 61.35  ? 412 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   MET 1   1   1   MET MET A . n 
A 1 2   ASN 2   2   2   ASN ASN A . n 
A 1 3   ILE 3   3   3   ILE ILE A . n 
A 1 4   PHE 4   4   4   PHE PHE A . n 
A 1 5   GLU 5   5   5   GLU GLU A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   ARG 8   8   8   ARG ARG A . n 
A 1 9   ILE 9   9   9   ILE ILE A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  ARG 14  14  14  ARG ARG A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  LYS 16  16  16  LYS LYS A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  TYR 18  18  18  TYR TYR A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASP 20  20  20  ASP ASP A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  GLU 22  22  22  GLU GLU A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  TYR 25  25  25  TYR TYR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  ILE 27  27  27  ILE ILE A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  ILE 29  29  29  ILE ILE A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  HIS 31  31  31  HIS HIS A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  THR 34  34  34  THR THR A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  SER 36  36  36  SER SER A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  SER 38  38  38  SER SER A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  LYS 43  43  43  LYS LYS A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  GLU 45  45  45  GLU GLU A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  ALA 49  49  49  ALA ALA A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ARG 52  52  52  ARG ARG A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ASN 55  55  55  ASN ASN A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  ILE 58  58  58  ILE ILE A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  LYS 65  65  65  LYS LYS A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  PHE 67  67  67  PHE PHE A . n 
A 1 68  ASN 68  68  68  ASN ASN A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ASP 70  70  70  ASP ASP A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  ASN 81  81  81  ASN ASN A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  LYS 85  85  85  LYS LYS A . n 
A 1 86  PRO 86  86  86  PRO PRO A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ASP 89  89  89  ASP ASP A . n 
A 1 90  SER 90  90  90  SER SER A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ARG 95  95  95  ARG ARG A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 MET 102 102 102 MET MET A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 PHE 104 104 104 PHE PHE A . n 
A 1 105 GLN 105 105 105 GLN GLN A . n 
A 1 106 MET 106 106 106 MET MET A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 GLU 108 108 108 GLU GLU A . n 
A 1 109 THR 109 109 109 THR THR A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 VAL 111 111 111 VAL VAL A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 THR 115 115 115 THR THR A . n 
A 1 116 ASN 116 116 116 ASN ASN A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 ARG 119 119 119 ARG ARG A . n 
A 1 120 MET 120 120 120 MET MET A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 GLN 122 122 122 GLN GLN A . n 
A 1 123 GLN 123 123 123 GLN GLN A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 ARG 125 125 125 ARG ARG A . n 
A 1 126 TRP 126 126 126 TRP TRP A . n 
A 1 127 ASP 127 127 127 ASP ASP A . n 
A 1 128 GLU 128 128 128 GLU GLU A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 VAL 131 131 131 VAL VAL A . n 
A 1 132 ASN 132 132 132 ASN ASN A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 ARG 137 137 137 ARG ARG A . n 
A 1 138 TRP 138 138 138 TRP TRP A . n 
A 1 139 TYR 139 139 139 TYR TYR A . n 
A 1 140 ASN 140 140 140 ASN ASN A . n 
A 1 141 GLN 141 141 141 GLN GLN A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 ASN 144 144 144 ASN ASN A . n 
A 1 145 ARG 145 145 145 ARG ARG A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 LYS 147 147 147 LYS LYS A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 VAL 149 149 149 VAL VAL A . n 
A 1 150 ILE 150 150 150 ILE ILE A . n 
A 1 151 THR 151 151 151 THR THR A . n 
A 1 152 THR 152 152 152 THR THR A . n 
A 1 153 PHE 153 153 153 PHE PHE A . n 
A 1 154 ARG 154 154 154 ARG ARG A . n 
A 1 155 THR 155 155 155 THR THR A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 TRP 158 158 158 TRP TRP A . n 
A 1 159 ASP 159 159 159 ASP ASP A . n 
A 1 160 ALA 160 160 160 ALA ALA A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 ASN 163 163 ?   ?   ?   A . n 
A 1 164 LEU 164 164 ?   ?   ?   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 CL  1   173 173 CL  CL  A . 
C 2 CL  1   178 178 CL  CL  A . 
D 3 BME 1   901 901 BME BME A . 
E 3 BME 1   902 902 BME BME A . 
F 4 HOH 1   171 171 HOH HOH A . 
F 4 HOH 2   172 172 HOH HOH A . 
F 4 HOH 3   174 174 HOH HOH A . 
F 4 HOH 4   175 175 HOH HOH A . 
F 4 HOH 5   176 176 HOH HOH A . 
F 4 HOH 6   177 177 HOH HOH A . 
F 4 HOH 7   179 179 HOH HOH A . 
F 4 HOH 8   180 180 HOH HOH A . 
F 4 HOH 9   181 181 HOH HOH A . 
F 4 HOH 10  182 182 HOH HOH A . 
F 4 HOH 11  183 183 HOH HOH A . 
F 4 HOH 12  184 184 HOH HOH A . 
F 4 HOH 13  185 185 HOH HOH A . 
F 4 HOH 14  186 186 HOH HOH A . 
F 4 HOH 15  187 187 HOH HOH A . 
F 4 HOH 16  188 188 HOH HOH A . 
F 4 HOH 17  189 189 HOH HOH A . 
F 4 HOH 18  190 190 HOH HOH A . 
F 4 HOH 19  191 191 HOH HOH A . 
F 4 HOH 20  193 193 HOH HOH A . 
F 4 HOH 21  194 194 HOH HOH A . 
F 4 HOH 22  195 195 HOH HOH A . 
F 4 HOH 23  196 196 HOH HOH A . 
F 4 HOH 24  197 197 HOH HOH A . 
F 4 HOH 25  198 198 HOH HOH A . 
F 4 HOH 26  200 200 HOH HOH A . 
F 4 HOH 27  201 201 HOH HOH A . 
F 4 HOH 28  203 203 HOH HOH A . 
F 4 HOH 29  204 204 HOH HOH A . 
F 4 HOH 30  206 206 HOH HOH A . 
F 4 HOH 31  207 207 HOH HOH A . 
F 4 HOH 32  208 208 HOH HOH A . 
F 4 HOH 33  210 210 HOH HOH A . 
F 4 HOH 34  211 211 HOH HOH A . 
F 4 HOH 35  213 213 HOH HOH A . 
F 4 HOH 36  215 215 HOH HOH A . 
F 4 HOH 37  216 216 HOH HOH A . 
F 4 HOH 38  217 217 HOH HOH A . 
F 4 HOH 39  218 218 HOH HOH A . 
F 4 HOH 40  219 219 HOH HOH A . 
F 4 HOH 41  220 220 HOH HOH A . 
F 4 HOH 42  221 221 HOH HOH A . 
F 4 HOH 43  222 222 HOH HOH A . 
F 4 HOH 44  223 223 HOH HOH A . 
F 4 HOH 45  224 224 HOH HOH A . 
F 4 HOH 46  225 225 HOH HOH A . 
F 4 HOH 47  226 226 HOH HOH A . 
F 4 HOH 48  227 227 HOH HOH A . 
F 4 HOH 49  229 229 HOH HOH A . 
F 4 HOH 50  231 231 HOH HOH A . 
F 4 HOH 51  235 235 HOH HOH A . 
F 4 HOH 52  236 236 HOH HOH A . 
F 4 HOH 53  237 237 HOH HOH A . 
F 4 HOH 54  238 238 HOH HOH A . 
F 4 HOH 55  239 239 HOH HOH A . 
F 4 HOH 56  240 240 HOH HOH A . 
F 4 HOH 57  242 242 HOH HOH A . 
F 4 HOH 58  244 244 HOH HOH A . 
F 4 HOH 59  245 245 HOH HOH A . 
F 4 HOH 60  246 246 HOH HOH A . 
F 4 HOH 61  249 249 HOH HOH A . 
F 4 HOH 62  251 251 HOH HOH A . 
F 4 HOH 63  253 253 HOH HOH A . 
F 4 HOH 64  256 256 HOH HOH A . 
F 4 HOH 65  257 257 HOH HOH A . 
F 4 HOH 66  260 260 HOH HOH A . 
F 4 HOH 67  261 261 HOH HOH A . 
F 4 HOH 68  263 263 HOH HOH A . 
F 4 HOH 69  266 266 HOH HOH A . 
F 4 HOH 70  269 269 HOH HOH A . 
F 4 HOH 71  270 270 HOH HOH A . 
F 4 HOH 72  274 274 HOH HOH A . 
F 4 HOH 73  277 277 HOH HOH A . 
F 4 HOH 74  278 278 HOH HOH A . 
F 4 HOH 75  280 280 HOH HOH A . 
F 4 HOH 76  281 281 HOH HOH A . 
F 4 HOH 77  282 282 HOH HOH A . 
F 4 HOH 78  283 283 HOH HOH A . 
F 4 HOH 79  285 285 HOH HOH A . 
F 4 HOH 80  286 286 HOH HOH A . 
F 4 HOH 81  288 288 HOH HOH A . 
F 4 HOH 82  290 290 HOH HOH A . 
F 4 HOH 83  291 291 HOH HOH A . 
F 4 HOH 84  294 294 HOH HOH A . 
F 4 HOH 85  295 295 HOH HOH A . 
F 4 HOH 86  299 299 HOH HOH A . 
F 4 HOH 87  300 300 HOH HOH A . 
F 4 HOH 88  301 301 HOH HOH A . 
F 4 HOH 89  302 302 HOH HOH A . 
F 4 HOH 90  303 303 HOH HOH A . 
F 4 HOH 91  314 314 HOH HOH A . 
F 4 HOH 92  315 315 HOH HOH A . 
F 4 HOH 93  321 321 HOH HOH A . 
F 4 HOH 94  322 322 HOH HOH A . 
F 4 HOH 95  401 401 HOH HOH A . 
F 4 HOH 96  402 402 HOH HOH A . 
F 4 HOH 97  403 403 HOH HOH A . 
F 4 HOH 98  404 404 HOH HOH A . 
F 4 HOH 99  405 405 HOH HOH A . 
F 4 HOH 100 406 406 HOH HOH A . 
F 4 HOH 101 407 407 HOH HOH A . 
F 4 HOH 102 408 408 HOH HOH A . 
F 4 HOH 103 409 409 HOH HOH A . 
F 4 HOH 104 410 410 HOH HOH A . 
F 4 HOH 105 411 411 HOH HOH A . 
F 4 HOH 106 412 412 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_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 1996-03-08 
2 'Structure model' 1 1 2008-03-24 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2017-11-29 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Derived calculations'      
4 4 'Structure model' Other                       
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' pdbx_database_status 
2 4 'Structure model' struct_conf          
3 4 'Structure model' struct_conf_type     
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    4 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_pdbx_database_status.process_site' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
TNT          refinement       .                   ? 1 
XUONG-HAMLIN 'data reduction' '(DETECTOR SYSTEM)' ? 2 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   S2 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   BME 
_pdbx_validate_close_contact.auth_seq_id_1    901 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   S2 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   BME 
_pdbx_validate_close_contact.auth_seq_id_2    902 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.06 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O1 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    BME 
_pdbx_validate_symm_contact.auth_seq_id_1     901 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O1 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    BME 
_pdbx_validate_symm_contact.auth_seq_id_2     901 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   5_555 
_pdbx_validate_symm_contact.dist              1.64 
# 
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 22  ? ? OE2 A GLU 22  ? ? 1.323 1.252 0.071 0.011 N 
2 1 CD A GLU 128 ? ? OE1 A GLU 128 ? ? 1.319 1.252 0.067 0.011 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 CB A ASP 47  ? ? CG A ASP 47  ? ? OD1 A ASP 47  ? ? 125.81 118.30 7.51  0.90 N 
2 1 CB A ASP 47  ? ? CG A ASP 47  ? ? OD2 A ASP 47  ? ? 110.47 118.30 -7.83 0.90 N 
3 1 CB A ASP 61  ? ? CG A ASP 61  ? ? OD2 A ASP 61  ? ? 112.32 118.30 -5.98 0.90 N 
4 1 CB A ASP 72  ? ? CG A ASP 72  ? ? OD1 A ASP 72  ? ? 124.06 118.30 5.76  0.90 N 
5 1 NE A ARG 80  ? ? CZ A ARG 80  ? ? NH1 A ARG 80  ? ? 123.70 120.30 3.40  0.50 N 
6 1 CB A ASP 89  ? ? CG A ASP 89  ? ? OD1 A ASP 89  ? ? 123.72 118.30 5.42  0.90 N 
7 1 CB A ASP 89  ? ? CG A ASP 89  ? ? OD2 A ASP 89  ? ? 112.15 118.30 -6.15 0.90 N 
8 1 CB A ASP 92  ? ? CG A ASP 92  ? ? OD1 A ASP 92  ? ? 112.49 118.30 -5.81 0.90 N 
9 1 CB A ASP 159 ? ? CG A ASP 159 ? ? OD2 A ASP 159 ? ? 112.79 118.30 -5.51 0.90 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 20  ? ? -78.92  -168.86 
2 1 ILE A 29  ? ? -104.90 76.49   
3 1 PHE A 114 ? ? -97.94  46.46   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ASN 163 ? A ASN 163 
2 1 Y 1 A LEU 164 ? A LEU 164 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CHLORIDE ION'       CL  
3 BETA-MERCAPTOETHANOL BME 
4 water                HOH 
# 
