data_8XCB
# 
_entry.id   8XCB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8XCB         pdb_00008xcb 10.2210/pdb8xcb/pdb 
WWPDB D_1300043049 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-11 
_pdbx_audit_revision_history.part_number         ? 
# 
_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         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8XCB 
_pdbx_database_status.recvd_initial_deposition_date   2023-12-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              min.lu@shsmu.edu.cn 
_pdbx_contact_author.name_first         Min 
_pdbx_contact_author.name_last          Lu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6902-3751 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wang, Z.'   1 ? 
'Shujun, X.' 2 ? 
'Yigang, T.' 3 ? 
'Derun, Z.'  4 ? 
'Jiaqi, W.'  5 ? 
'Kai, K.'    6 ? 
'Lu, M.'     7 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Cocrystal structure of p53 in complex of B20' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wang, Z.'     1  ? 
primary 'Taijie, G.'   2  ? 
primary 'Shujun, X.'   3  ? 
primary 'Yigang, T.'   4  ? 
primary 'Fangfang, S.' 5  ? 
primary 'Kai, K.'      6  ? 
primary 'Lirong, Z.'   7  ? 
primary 'Derun, Z.'    8  ? 
primary 'Jiaqi, W.'    9  ? 
primary 'Jingyi, C.'   10 ? 
primary 'Hesong, Z.'   11 ? 
primary 'Jiajia, D.'   12 ? 
primary 'Lu, M.'       13 ? 
# 
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 'Cellular tumor antigen p53'                                        22505.582 4   ? ? ? ? 
2 non-polymer syn 'ZINC ION'                                                          65.409    4   ? ? ? ? 
3 non-polymer syn GLYCEROL                                                            92.094    3   ? ? ? ? 
4 non-polymer syn '2-[2,4-bis(oxidanylidene)-1,3-thiazolidin-5-ylidene]ethanoic acid' 173.147   2   ? ? ? ? 
5 water       nat water                                                               18.015    468 ? ? ? ? 
# 
_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       
;SSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVV
RRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILT
IITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVV
RRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILT
IITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKG
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                          ZN    
3 GLYCEROL                                                            GOL   
4 '2-[2,4-bis(oxidanylidene)-1,3-thiazolidin-5-ylidene]ethanoic acid' A1LUZ 
5 water                                                               HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   SER n 
1 3   SER n 
1 4   VAL n 
1 5   PRO n 
1 6   SER n 
1 7   GLN n 
1 8   LYS n 
1 9   THR n 
1 10  TYR n 
1 11  GLN n 
1 12  GLY n 
1 13  SER n 
1 14  TYR n 
1 15  GLY n 
1 16  PHE n 
1 17  ARG n 
1 18  LEU n 
1 19  GLY n 
1 20  PHE n 
1 21  LEU n 
1 22  HIS n 
1 23  SER n 
1 24  GLY n 
1 25  THR n 
1 26  ALA n 
1 27  LYS n 
1 28  SER n 
1 29  VAL n 
1 30  THR n 
1 31  CYS n 
1 32  THR n 
1 33  TYR n 
1 34  SER n 
1 35  PRO n 
1 36  ALA n 
1 37  LEU n 
1 38  ASN n 
1 39  LYS n 
1 40  MET n 
1 41  PHE n 
1 42  CYS n 
1 43  GLN n 
1 44  LEU n 
1 45  ALA n 
1 46  LYS n 
1 47  THR n 
1 48  CYS n 
1 49  PRO n 
1 50  VAL n 
1 51  GLN n 
1 52  LEU n 
1 53  TRP n 
1 54  VAL n 
1 55  ASP n 
1 56  SER n 
1 57  THR n 
1 58  PRO n 
1 59  PRO n 
1 60  PRO n 
1 61  GLY n 
1 62  THR n 
1 63  ARG n 
1 64  VAL n 
1 65  ARG n 
1 66  ALA n 
1 67  MET n 
1 68  ALA n 
1 69  ILE n 
1 70  TYR n 
1 71  LYS n 
1 72  GLN n 
1 73  SER n 
1 74  GLN n 
1 75  HIS n 
1 76  MET n 
1 77  THR n 
1 78  GLU n 
1 79  VAL n 
1 80  VAL n 
1 81  ARG n 
1 82  ARG n 
1 83  CYS n 
1 84  PRO n 
1 85  HIS n 
1 86  HIS n 
1 87  GLU n 
1 88  ARG n 
1 89  CYS n 
1 90  SER n 
1 91  ASP n 
1 92  SER n 
1 93  ASP n 
1 94  GLY n 
1 95  LEU n 
1 96  ALA n 
1 97  PRO n 
1 98  PRO n 
1 99  GLN n 
1 100 HIS n 
1 101 LEU n 
1 102 ILE n 
1 103 ARG n 
1 104 VAL n 
1 105 GLU n 
1 106 GLY n 
1 107 ASN n 
1 108 LEU n 
1 109 ARG n 
1 110 VAL n 
1 111 GLU n 
1 112 TYR n 
1 113 LEU n 
1 114 ASP n 
1 115 ASP n 
1 116 ARG n 
1 117 ASN n 
1 118 THR n 
1 119 PHE n 
1 120 ARG n 
1 121 HIS n 
1 122 SER n 
1 123 VAL n 
1 124 VAL n 
1 125 VAL n 
1 126 PRO n 
1 127 TYR n 
1 128 GLU n 
1 129 PRO n 
1 130 PRO n 
1 131 GLU n 
1 132 VAL n 
1 133 GLY n 
1 134 SER n 
1 135 ASP n 
1 136 CYS n 
1 137 THR n 
1 138 THR n 
1 139 ILE n 
1 140 HIS n 
1 141 TYR n 
1 142 ASN n 
1 143 TYR n 
1 144 MET n 
1 145 CYS n 
1 146 ASN n 
1 147 SER n 
1 148 SER n 
1 149 CYS n 
1 150 MET n 
1 151 GLY n 
1 152 GLY n 
1 153 MET n 
1 154 ASN n 
1 155 ARG n 
1 156 ARG n 
1 157 PRO n 
1 158 ILE n 
1 159 LEU n 
1 160 THR n 
1 161 ILE n 
1 162 ILE n 
1 163 THR n 
1 164 LEU n 
1 165 GLU n 
1 166 ASP n 
1 167 SER n 
1 168 SER n 
1 169 GLY n 
1 170 ASN n 
1 171 LEU n 
1 172 LEU n 
1 173 GLY n 
1 174 ARG n 
1 175 ASN n 
1 176 SER n 
1 177 PHE n 
1 178 GLU n 
1 179 VAL n 
1 180 ARG n 
1 181 VAL n 
1 182 CYS n 
1 183 ALA n 
1 184 CYS n 
1 185 PRO n 
1 186 GLY n 
1 187 ARG n 
1 188 ASP n 
1 189 ARG n 
1 190 ARG n 
1 191 THR n 
1 192 GLU n 
1 193 GLU n 
1 194 GLU n 
1 195 ASN n 
1 196 LEU n 
1 197 ARG n 
1 198 LYS n 
1 199 LYS n 
1 200 GLY 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                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   200 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 TP53 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
A1LUZ non-polymer         . '2-[2,4-bis(oxidanylidene)-1,3-thiazolidin-5-ylidene]ethanoic acid' ?                               
'C5 H3 N O4 S'   173.147 
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 
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  
GOL   non-polymer         . GLYCEROL                                                            'GLYCERIN; PROPANE-1,2,3-TRIOL' 
'C3 H8 O3'       92.094  
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 
ZN    non-polymer         . 'ZINC ION'                                                          ?                               
'Zn 2'           65.409  
# 
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   SER 1   94  ?   ?   ?   A . n 
A 1 2   SER 2   95  ?   ?   ?   A . n 
A 1 3   SER 3   96  ?   ?   ?   A . n 
A 1 4   VAL 4   97  97  VAL VAL A . n 
A 1 5   PRO 5   98  98  PRO PRO A . n 
A 1 6   SER 6   99  99  SER SER A . n 
A 1 7   GLN 7   100 100 GLN GLN A . n 
A 1 8   LYS 8   101 101 LYS LYS A . n 
A 1 9   THR 9   102 102 THR THR A . n 
A 1 10  TYR 10  103 103 TYR TYR A . n 
A 1 11  GLN 11  104 104 GLN GLN A . n 
A 1 12  GLY 12  105 105 GLY GLY A . n 
A 1 13  SER 13  106 106 SER SER A . n 
A 1 14  TYR 14  107 107 TYR TYR A . n 
A 1 15  GLY 15  108 108 GLY GLY A . n 
A 1 16  PHE 16  109 109 PHE PHE A . n 
A 1 17  ARG 17  110 110 ARG ARG A . n 
A 1 18  LEU 18  111 111 LEU LEU A . n 
A 1 19  GLY 19  112 112 GLY GLY A . n 
A 1 20  PHE 20  113 113 PHE PHE A . n 
A 1 21  LEU 21  114 114 LEU LEU A . n 
A 1 22  HIS 22  115 115 HIS HIS A . n 
A 1 23  SER 23  116 116 SER SER A . n 
A 1 24  GLY 24  117 117 GLY GLY A . n 
A 1 25  THR 25  118 118 THR THR A . n 
A 1 26  ALA 26  119 119 ALA ALA A . n 
A 1 27  LYS 27  120 120 LYS LYS A . n 
A 1 28  SER 28  121 121 SER SER A . n 
A 1 29  VAL 29  122 122 VAL VAL A . n 
A 1 30  THR 30  123 123 THR THR A . n 
A 1 31  CYS 31  124 124 CYS CYS A . n 
A 1 32  THR 32  125 125 THR THR A . n 
A 1 33  TYR 33  126 126 TYR TYR A . n 
A 1 34  SER 34  127 127 SER SER A . n 
A 1 35  PRO 35  128 128 PRO PRO A . n 
A 1 36  ALA 36  129 129 ALA ALA A . n 
A 1 37  LEU 37  130 130 LEU LEU A . n 
A 1 38  ASN 38  131 131 ASN ASN A . n 
A 1 39  LYS 39  132 132 LYS LYS A . n 
A 1 40  MET 40  133 133 MET MET A . n 
A 1 41  PHE 41  134 134 PHE PHE A . n 
A 1 42  CYS 42  135 135 CYS CYS A . n 
A 1 43  GLN 43  136 136 GLN GLN A . n 
A 1 44  LEU 44  137 137 LEU LEU A . n 
A 1 45  ALA 45  138 138 ALA ALA A . n 
A 1 46  LYS 46  139 139 LYS LYS A . n 
A 1 47  THR 47  140 140 THR THR A . n 
A 1 48  CYS 48  141 141 CYS CYS A . n 
A 1 49  PRO 49  142 142 PRO PRO A . n 
A 1 50  VAL 50  143 143 VAL VAL A . n 
A 1 51  GLN 51  144 144 GLN GLN A . n 
A 1 52  LEU 52  145 145 LEU LEU A . n 
A 1 53  TRP 53  146 146 TRP TRP A . n 
A 1 54  VAL 54  147 147 VAL VAL A . n 
A 1 55  ASP 55  148 148 ASP ASP A . n 
A 1 56  SER 56  149 149 SER SER A . n 
A 1 57  THR 57  150 150 THR THR A . n 
A 1 58  PRO 58  151 151 PRO PRO A . n 
A 1 59  PRO 59  152 152 PRO PRO A . n 
A 1 60  PRO 60  153 153 PRO PRO A . n 
A 1 61  GLY 61  154 154 GLY GLY A . n 
A 1 62  THR 62  155 155 THR THR A . n 
A 1 63  ARG 63  156 156 ARG ARG A . n 
A 1 64  VAL 64  157 157 VAL VAL A . n 
A 1 65  ARG 65  158 158 ARG ARG A . n 
A 1 66  ALA 66  159 159 ALA ALA A . n 
A 1 67  MET 67  160 160 MET MET A . n 
A 1 68  ALA 68  161 161 ALA ALA A . n 
A 1 69  ILE 69  162 162 ILE ILE A . n 
A 1 70  TYR 70  163 163 TYR TYR A . n 
A 1 71  LYS 71  164 164 LYS LYS A . n 
A 1 72  GLN 72  165 165 GLN GLN A . n 
A 1 73  SER 73  166 166 SER SER A . n 
A 1 74  GLN 74  167 167 GLN GLN A . n 
A 1 75  HIS 75  168 168 HIS HIS A . n 
A 1 76  MET 76  169 169 MET MET A . n 
A 1 77  THR 77  170 170 THR THR A . n 
A 1 78  GLU 78  171 171 GLU GLU A . n 
A 1 79  VAL 79  172 172 VAL VAL A . n 
A 1 80  VAL 80  173 173 VAL VAL A . n 
A 1 81  ARG 81  174 174 ARG ARG A . n 
A 1 82  ARG 82  175 175 ARG ARG A . n 
A 1 83  CYS 83  176 176 CYS CYS A . n 
A 1 84  PRO 84  177 177 PRO PRO A . n 
A 1 85  HIS 85  178 178 HIS HIS A . n 
A 1 86  HIS 86  179 179 HIS HIS A . n 
A 1 87  GLU 87  180 180 GLU GLU A . n 
A 1 88  ARG 88  181 181 ARG ARG A . n 
A 1 89  CYS 89  182 182 CYS CYS A . n 
A 1 90  SER 90  183 183 SER SER A . n 
A 1 91  ASP 91  184 184 ASP ASP A . n 
A 1 92  SER 92  185 185 SER SER A . n 
A 1 93  ASP 93  186 186 ASP ASP A . n 
A 1 94  GLY 94  187 187 GLY GLY A . n 
A 1 95  LEU 95  188 188 LEU LEU A . n 
A 1 96  ALA 96  189 189 ALA ALA A . n 
A 1 97  PRO 97  190 190 PRO PRO A . n 
A 1 98  PRO 98  191 191 PRO PRO A . n 
A 1 99  GLN 99  192 192 GLN GLN A . n 
A 1 100 HIS 100 193 193 HIS HIS A . n 
A 1 101 LEU 101 194 194 LEU LEU A . n 
A 1 102 ILE 102 195 195 ILE ILE A . n 
A 1 103 ARG 103 196 196 ARG ARG A . n 
A 1 104 VAL 104 197 197 VAL VAL A . n 
A 1 105 GLU 105 198 198 GLU GLU A . n 
A 1 106 GLY 106 199 199 GLY GLY A . n 
A 1 107 ASN 107 200 200 ASN ASN A . n 
A 1 108 LEU 108 201 201 LEU LEU A . n 
A 1 109 ARG 109 202 202 ARG ARG A . n 
A 1 110 VAL 110 203 203 VAL VAL A . n 
A 1 111 GLU 111 204 204 GLU GLU A . n 
A 1 112 TYR 112 205 205 TYR TYR A . n 
A 1 113 LEU 113 206 206 LEU LEU A . n 
A 1 114 ASP 114 207 207 ASP ASP A . n 
A 1 115 ASP 115 208 208 ASP ASP A . n 
A 1 116 ARG 116 209 209 ARG ARG A . n 
A 1 117 ASN 117 210 210 ASN ASN A . n 
A 1 118 THR 118 211 211 THR THR A . n 
A 1 119 PHE 119 212 212 PHE PHE A . n 
A 1 120 ARG 120 213 213 ARG ARG A . n 
A 1 121 HIS 121 214 214 HIS HIS A . n 
A 1 122 SER 122 215 215 SER SER A . n 
A 1 123 VAL 123 216 216 VAL VAL A . n 
A 1 124 VAL 124 217 217 VAL VAL A . n 
A 1 125 VAL 125 218 218 VAL VAL A . n 
A 1 126 PRO 126 219 219 PRO PRO A . n 
A 1 127 TYR 127 220 220 TYR TYR A . n 
A 1 128 GLU 128 221 221 GLU GLU A . n 
A 1 129 PRO 129 222 222 PRO PRO A . n 
A 1 130 PRO 130 223 223 PRO PRO A . n 
A 1 131 GLU 131 224 224 GLU GLU A . n 
A 1 132 VAL 132 225 225 VAL VAL A . n 
A 1 133 GLY 133 226 226 GLY GLY A . n 
A 1 134 SER 134 227 227 SER SER A . n 
A 1 135 ASP 135 228 228 ASP ASP A . n 
A 1 136 CYS 136 229 229 CYS CYS A . n 
A 1 137 THR 137 230 230 THR THR A . n 
A 1 138 THR 138 231 231 THR THR A . n 
A 1 139 ILE 139 232 232 ILE ILE A . n 
A 1 140 HIS 140 233 233 HIS HIS A . n 
A 1 141 TYR 141 234 234 TYR TYR A . n 
A 1 142 ASN 142 235 235 ASN ASN A . n 
A 1 143 TYR 143 236 236 TYR TYR A . n 
A 1 144 MET 144 237 237 MET MET A . n 
A 1 145 CYS 145 238 238 CYS CYS A . n 
A 1 146 ASN 146 239 239 ASN ASN A . n 
A 1 147 SER 147 240 240 SER SER A . n 
A 1 148 SER 148 241 241 SER SER A . n 
A 1 149 CYS 149 242 242 CYS CYS A . n 
A 1 150 MET 150 243 243 MET MET A . n 
A 1 151 GLY 151 244 244 GLY GLY A . n 
A 1 152 GLY 152 245 245 GLY GLY A . n 
A 1 153 MET 153 246 246 MET MET A . n 
A 1 154 ASN 154 247 247 ASN ASN A . n 
A 1 155 ARG 155 248 248 ARG ARG A . n 
A 1 156 ARG 156 249 249 ARG ARG A . n 
A 1 157 PRO 157 250 250 PRO PRO A . n 
A 1 158 ILE 158 251 251 ILE ILE A . n 
A 1 159 LEU 159 252 252 LEU LEU A . n 
A 1 160 THR 160 253 253 THR THR A . n 
A 1 161 ILE 161 254 254 ILE ILE A . n 
A 1 162 ILE 162 255 255 ILE ILE A . n 
A 1 163 THR 163 256 256 THR THR A . n 
A 1 164 LEU 164 257 257 LEU LEU A . n 
A 1 165 GLU 165 258 258 GLU GLU A . n 
A 1 166 ASP 166 259 259 ASP ASP A . n 
A 1 167 SER 167 260 260 SER SER A . n 
A 1 168 SER 168 261 261 SER SER A . n 
A 1 169 GLY 169 262 262 GLY GLY A . n 
A 1 170 ASN 170 263 263 ASN ASN A . n 
A 1 171 LEU 171 264 264 LEU LEU A . n 
A 1 172 LEU 172 265 265 LEU LEU A . n 
A 1 173 GLY 173 266 266 GLY GLY A . n 
A 1 174 ARG 174 267 267 ARG ARG A . n 
A 1 175 ASN 175 268 268 ASN ASN A . n 
A 1 176 SER 176 269 269 SER SER A . n 
A 1 177 PHE 177 270 270 PHE PHE A . n 
A 1 178 GLU 178 271 271 GLU GLU A . n 
A 1 179 VAL 179 272 272 VAL VAL A . n 
A 1 180 ARG 180 273 273 ARG ARG A . n 
A 1 181 VAL 181 274 274 VAL VAL A . n 
A 1 182 CYS 182 275 275 CYS CYS A . n 
A 1 183 ALA 183 276 276 ALA ALA A . n 
A 1 184 CYS 184 277 277 CYS CYS A . n 
A 1 185 PRO 185 278 278 PRO PRO A . n 
A 1 186 GLY 186 279 279 GLY GLY A . n 
A 1 187 ARG 187 280 280 ARG ARG A . n 
A 1 188 ASP 188 281 281 ASP ASP A . n 
A 1 189 ARG 189 282 282 ARG ARG A . n 
A 1 190 ARG 190 283 283 ARG ARG A . n 
A 1 191 THR 191 284 284 THR THR A . n 
A 1 192 GLU 192 285 285 GLU GLU A . n 
A 1 193 GLU 193 286 286 GLU GLU A . n 
A 1 194 GLU 194 287 287 GLU GLU A . n 
A 1 195 ASN 195 288 288 ASN ASN A . n 
A 1 196 LEU 196 289 289 LEU LEU A . n 
A 1 197 ARG 197 290 ?   ?   ?   A . n 
A 1 198 LYS 198 291 ?   ?   ?   A . n 
A 1 199 LYS 199 292 ?   ?   ?   A . n 
A 1 200 GLY 200 293 ?   ?   ?   A . n 
B 1 1   SER 1   94  ?   ?   ?   B . n 
B 1 2   SER 2   95  ?   ?   ?   B . n 
B 1 3   SER 3   96  96  SER SER B . n 
B 1 4   VAL 4   97  97  VAL VAL B . n 
B 1 5   PRO 5   98  98  PRO PRO B . n 
B 1 6   SER 6   99  99  SER SER B . n 
B 1 7   GLN 7   100 100 GLN GLN B . n 
B 1 8   LYS 8   101 101 LYS LYS B . n 
B 1 9   THR 9   102 102 THR THR B . n 
B 1 10  TYR 10  103 103 TYR TYR B . n 
B 1 11  GLN 11  104 104 GLN GLN B . n 
B 1 12  GLY 12  105 105 GLY GLY B . n 
B 1 13  SER 13  106 106 SER SER B . n 
B 1 14  TYR 14  107 107 TYR TYR B . n 
B 1 15  GLY 15  108 108 GLY GLY B . n 
B 1 16  PHE 16  109 109 PHE PHE B . n 
B 1 17  ARG 17  110 110 ARG ARG B . n 
B 1 18  LEU 18  111 111 LEU LEU B . n 
B 1 19  GLY 19  112 112 GLY GLY B . n 
B 1 20  PHE 20  113 113 PHE PHE B . n 
B 1 21  LEU 21  114 114 LEU LEU B . n 
B 1 22  HIS 22  115 115 HIS HIS B . n 
B 1 23  SER 23  116 116 SER SER B . n 
B 1 24  GLY 24  117 117 GLY GLY B . n 
B 1 25  THR 25  118 118 THR THR B . n 
B 1 26  ALA 26  119 119 ALA ALA B . n 
B 1 27  LYS 27  120 120 LYS LYS B . n 
B 1 28  SER 28  121 121 SER SER B . n 
B 1 29  VAL 29  122 122 VAL VAL B . n 
B 1 30  THR 30  123 123 THR THR B . n 
B 1 31  CYS 31  124 124 CYS CYS B . n 
B 1 32  THR 32  125 125 THR THR B . n 
B 1 33  TYR 33  126 126 TYR TYR B . n 
B 1 34  SER 34  127 127 SER SER B . n 
B 1 35  PRO 35  128 128 PRO PRO B . n 
B 1 36  ALA 36  129 129 ALA ALA B . n 
B 1 37  LEU 37  130 130 LEU LEU B . n 
B 1 38  ASN 38  131 131 ASN ASN B . n 
B 1 39  LYS 39  132 132 LYS LYS B . n 
B 1 40  MET 40  133 133 MET MET B . n 
B 1 41  PHE 41  134 134 PHE PHE B . n 
B 1 42  CYS 42  135 135 CYS CYS B . n 
B 1 43  GLN 43  136 136 GLN GLN B . n 
B 1 44  LEU 44  137 137 LEU LEU B . n 
B 1 45  ALA 45  138 138 ALA ALA B . n 
B 1 46  LYS 46  139 139 LYS LYS B . n 
B 1 47  THR 47  140 140 THR THR B . n 
B 1 48  CYS 48  141 141 CYS CYS B . n 
B 1 49  PRO 49  142 142 PRO PRO B . n 
B 1 50  VAL 50  143 143 VAL VAL B . n 
B 1 51  GLN 51  144 144 GLN GLN B . n 
B 1 52  LEU 52  145 145 LEU LEU B . n 
B 1 53  TRP 53  146 146 TRP TRP B . n 
B 1 54  VAL 54  147 147 VAL VAL B . n 
B 1 55  ASP 55  148 148 ASP ASP B . n 
B 1 56  SER 56  149 149 SER SER B . n 
B 1 57  THR 57  150 150 THR THR B . n 
B 1 58  PRO 58  151 151 PRO PRO B . n 
B 1 59  PRO 59  152 152 PRO PRO B . n 
B 1 60  PRO 60  153 153 PRO PRO B . n 
B 1 61  GLY 61  154 154 GLY GLY B . n 
B 1 62  THR 62  155 155 THR THR B . n 
B 1 63  ARG 63  156 156 ARG ARG B . n 
B 1 64  VAL 64  157 157 VAL VAL B . n 
B 1 65  ARG 65  158 158 ARG ARG B . n 
B 1 66  ALA 66  159 159 ALA ALA B . n 
B 1 67  MET 67  160 160 MET MET B . n 
B 1 68  ALA 68  161 161 ALA ALA B . n 
B 1 69  ILE 69  162 162 ILE ILE B . n 
B 1 70  TYR 70  163 163 TYR TYR B . n 
B 1 71  LYS 71  164 164 LYS LYS B . n 
B 1 72  GLN 72  165 165 GLN GLN B . n 
B 1 73  SER 73  166 166 SER SER B . n 
B 1 74  GLN 74  167 167 GLN GLN B . n 
B 1 75  HIS 75  168 168 HIS HIS B . n 
B 1 76  MET 76  169 169 MET MET B . n 
B 1 77  THR 77  170 170 THR THR B . n 
B 1 78  GLU 78  171 171 GLU GLU B . n 
B 1 79  VAL 79  172 172 VAL VAL B . n 
B 1 80  VAL 80  173 173 VAL VAL B . n 
B 1 81  ARG 81  174 174 ARG ARG B . n 
B 1 82  ARG 82  175 175 ARG ARG B . n 
B 1 83  CYS 83  176 176 CYS CYS B . n 
B 1 84  PRO 84  177 177 PRO PRO B . n 
B 1 85  HIS 85  178 178 HIS HIS B . n 
B 1 86  HIS 86  179 179 HIS HIS B . n 
B 1 87  GLU 87  180 180 GLU GLU B . n 
B 1 88  ARG 88  181 181 ARG ARG B . n 
B 1 89  CYS 89  182 182 CYS CYS B . n 
B 1 90  SER 90  183 183 SER SER B . n 
B 1 91  ASP 91  184 184 ASP ASP B . n 
B 1 92  SER 92  185 185 SER SER B . n 
B 1 93  ASP 93  186 186 ASP ASP B . n 
B 1 94  GLY 94  187 187 GLY GLY B . n 
B 1 95  LEU 95  188 188 LEU LEU B . n 
B 1 96  ALA 96  189 189 ALA ALA B . n 
B 1 97  PRO 97  190 190 PRO PRO B . n 
B 1 98  PRO 98  191 191 PRO PRO B . n 
B 1 99  GLN 99  192 192 GLN GLN B . n 
B 1 100 HIS 100 193 193 HIS HIS B . n 
B 1 101 LEU 101 194 194 LEU LEU B . n 
B 1 102 ILE 102 195 195 ILE ILE B . n 
B 1 103 ARG 103 196 196 ARG ARG B . n 
B 1 104 VAL 104 197 197 VAL VAL B . n 
B 1 105 GLU 105 198 198 GLU GLU B . n 
B 1 106 GLY 106 199 199 GLY GLY B . n 
B 1 107 ASN 107 200 200 ASN ASN B . n 
B 1 108 LEU 108 201 201 LEU LEU B . n 
B 1 109 ARG 109 202 202 ARG ARG B . n 
B 1 110 VAL 110 203 203 VAL VAL B . n 
B 1 111 GLU 111 204 204 GLU GLU B . n 
B 1 112 TYR 112 205 205 TYR TYR B . n 
B 1 113 LEU 113 206 206 LEU LEU B . n 
B 1 114 ASP 114 207 207 ASP ASP B . n 
B 1 115 ASP 115 208 208 ASP ASP B . n 
B 1 116 ARG 116 209 209 ARG ARG B . n 
B 1 117 ASN 117 210 210 ASN ASN B . n 
B 1 118 THR 118 211 211 THR THR B . n 
B 1 119 PHE 119 212 212 PHE PHE B . n 
B 1 120 ARG 120 213 213 ARG ARG B . n 
B 1 121 HIS 121 214 214 HIS HIS B . n 
B 1 122 SER 122 215 215 SER SER B . n 
B 1 123 VAL 123 216 216 VAL VAL B . n 
B 1 124 VAL 124 217 217 VAL VAL B . n 
B 1 125 VAL 125 218 218 VAL VAL B . n 
B 1 126 PRO 126 219 219 PRO PRO B . n 
B 1 127 TYR 127 220 220 TYR TYR B . n 
B 1 128 GLU 128 221 221 GLU GLU B . n 
B 1 129 PRO 129 222 222 PRO PRO B . n 
B 1 130 PRO 130 223 223 PRO PRO B . n 
B 1 131 GLU 131 224 224 GLU GLU B . n 
B 1 132 VAL 132 225 225 VAL VAL B . n 
B 1 133 GLY 133 226 226 GLY GLY B . n 
B 1 134 SER 134 227 227 SER SER B . n 
B 1 135 ASP 135 228 228 ASP ASP B . n 
B 1 136 CYS 136 229 229 CYS CYS B . n 
B 1 137 THR 137 230 230 THR THR B . n 
B 1 138 THR 138 231 231 THR THR B . n 
B 1 139 ILE 139 232 232 ILE ILE B . n 
B 1 140 HIS 140 233 233 HIS HIS B . n 
B 1 141 TYR 141 234 234 TYR TYR B . n 
B 1 142 ASN 142 235 235 ASN ASN B . n 
B 1 143 TYR 143 236 236 TYR TYR B . n 
B 1 144 MET 144 237 237 MET MET B . n 
B 1 145 CYS 145 238 238 CYS CYS B . n 
B 1 146 ASN 146 239 239 ASN ASN B . n 
B 1 147 SER 147 240 240 SER SER B . n 
B 1 148 SER 148 241 241 SER SER B . n 
B 1 149 CYS 149 242 242 CYS CYS B . n 
B 1 150 MET 150 243 243 MET MET B . n 
B 1 151 GLY 151 244 244 GLY GLY B . n 
B 1 152 GLY 152 245 245 GLY GLY B . n 
B 1 153 MET 153 246 246 MET MET B . n 
B 1 154 ASN 154 247 247 ASN ASN B . n 
B 1 155 ARG 155 248 248 ARG ARG B . n 
B 1 156 ARG 156 249 249 ARG ARG B . n 
B 1 157 PRO 157 250 250 PRO PRO B . n 
B 1 158 ILE 158 251 251 ILE ILE B . n 
B 1 159 LEU 159 252 252 LEU LEU B . n 
B 1 160 THR 160 253 253 THR THR B . n 
B 1 161 ILE 161 254 254 ILE ILE B . n 
B 1 162 ILE 162 255 255 ILE ILE B . n 
B 1 163 THR 163 256 256 THR THR B . n 
B 1 164 LEU 164 257 257 LEU LEU B . n 
B 1 165 GLU 165 258 258 GLU GLU B . n 
B 1 166 ASP 166 259 259 ASP ASP B . n 
B 1 167 SER 167 260 260 SER SER B . n 
B 1 168 SER 168 261 261 SER SER B . n 
B 1 169 GLY 169 262 262 GLY GLY B . n 
B 1 170 ASN 170 263 263 ASN ASN B . n 
B 1 171 LEU 171 264 264 LEU LEU B . n 
B 1 172 LEU 172 265 265 LEU LEU B . n 
B 1 173 GLY 173 266 266 GLY GLY B . n 
B 1 174 ARG 174 267 267 ARG ARG B . n 
B 1 175 ASN 175 268 268 ASN ASN B . n 
B 1 176 SER 176 269 269 SER SER B . n 
B 1 177 PHE 177 270 270 PHE PHE B . n 
B 1 178 GLU 178 271 271 GLU GLU B . n 
B 1 179 VAL 179 272 272 VAL VAL B . n 
B 1 180 ARG 180 273 273 ARG ARG B . n 
B 1 181 VAL 181 274 274 VAL VAL B . n 
B 1 182 CYS 182 275 275 CYS CYS B . n 
B 1 183 ALA 183 276 276 ALA ALA B . n 
B 1 184 CYS 184 277 277 CYS CYS B . n 
B 1 185 PRO 185 278 278 PRO PRO B . n 
B 1 186 GLY 186 279 279 GLY GLY B . n 
B 1 187 ARG 187 280 280 ARG ARG B . n 
B 1 188 ASP 188 281 281 ASP ASP B . n 
B 1 189 ARG 189 282 282 ARG ARG B . n 
B 1 190 ARG 190 283 283 ARG ARG B . n 
B 1 191 THR 191 284 284 THR THR B . n 
B 1 192 GLU 192 285 285 GLU GLU B . n 
B 1 193 GLU 193 286 286 GLU GLU B . n 
B 1 194 GLU 194 287 287 GLU GLU B . n 
B 1 195 ASN 195 288 288 ASN ASN B . n 
B 1 196 LEU 196 289 289 LEU LEU B . n 
B 1 197 ARG 197 290 ?   ?   ?   B . n 
B 1 198 LYS 198 291 ?   ?   ?   B . n 
B 1 199 LYS 199 292 ?   ?   ?   B . n 
B 1 200 GLY 200 293 ?   ?   ?   B . n 
C 1 1   SER 1   94  ?   ?   ?   C . n 
C 1 2   SER 2   95  ?   ?   ?   C . n 
C 1 3   SER 3   96  96  SER SER C . n 
C 1 4   VAL 4   97  97  VAL VAL C . n 
C 1 5   PRO 5   98  98  PRO PRO C . n 
C 1 6   SER 6   99  99  SER SER C . n 
C 1 7   GLN 7   100 100 GLN GLN C . n 
C 1 8   LYS 8   101 101 LYS LYS C . n 
C 1 9   THR 9   102 102 THR THR C . n 
C 1 10  TYR 10  103 103 TYR TYR C . n 
C 1 11  GLN 11  104 104 GLN GLN C . n 
C 1 12  GLY 12  105 105 GLY GLY C . n 
C 1 13  SER 13  106 106 SER SER C . n 
C 1 14  TYR 14  107 107 TYR TYR C . n 
C 1 15  GLY 15  108 108 GLY GLY C . n 
C 1 16  PHE 16  109 109 PHE PHE C . n 
C 1 17  ARG 17  110 110 ARG ARG C . n 
C 1 18  LEU 18  111 111 LEU LEU C . n 
C 1 19  GLY 19  112 112 GLY GLY C . n 
C 1 20  PHE 20  113 113 PHE PHE C . n 
C 1 21  LEU 21  114 114 LEU LEU C . n 
C 1 22  HIS 22  115 115 HIS HIS C . n 
C 1 23  SER 23  116 116 SER SER C . n 
C 1 24  GLY 24  117 117 GLY GLY C . n 
C 1 25  THR 25  118 118 THR THR C . n 
C 1 26  ALA 26  119 119 ALA ALA C . n 
C 1 27  LYS 27  120 120 LYS LYS C . n 
C 1 28  SER 28  121 121 SER SER C . n 
C 1 29  VAL 29  122 122 VAL VAL C . n 
C 1 30  THR 30  123 123 THR THR C . n 
C 1 31  CYS 31  124 124 CYS CYS C . n 
C 1 32  THR 32  125 125 THR THR C . n 
C 1 33  TYR 33  126 126 TYR TYR C . n 
C 1 34  SER 34  127 127 SER SER C . n 
C 1 35  PRO 35  128 128 PRO PRO C . n 
C 1 36  ALA 36  129 129 ALA ALA C . n 
C 1 37  LEU 37  130 130 LEU LEU C . n 
C 1 38  ASN 38  131 131 ASN ASN C . n 
C 1 39  LYS 39  132 132 LYS LYS C . n 
C 1 40  MET 40  133 133 MET MET C . n 
C 1 41  PHE 41  134 134 PHE PHE C . n 
C 1 42  CYS 42  135 135 CYS CYS C . n 
C 1 43  GLN 43  136 136 GLN GLN C . n 
C 1 44  LEU 44  137 137 LEU LEU C . n 
C 1 45  ALA 45  138 138 ALA ALA C . n 
C 1 46  LYS 46  139 139 LYS LYS C . n 
C 1 47  THR 47  140 140 THR THR C . n 
C 1 48  CYS 48  141 141 CYS CYS C . n 
C 1 49  PRO 49  142 142 PRO PRO C . n 
C 1 50  VAL 50  143 143 VAL VAL C . n 
C 1 51  GLN 51  144 144 GLN GLN C . n 
C 1 52  LEU 52  145 145 LEU LEU C . n 
C 1 53  TRP 53  146 146 TRP TRP C . n 
C 1 54  VAL 54  147 147 VAL VAL C . n 
C 1 55  ASP 55  148 148 ASP ASP C . n 
C 1 56  SER 56  149 149 SER SER C . n 
C 1 57  THR 57  150 150 THR THR C . n 
C 1 58  PRO 58  151 151 PRO PRO C . n 
C 1 59  PRO 59  152 152 PRO PRO C . n 
C 1 60  PRO 60  153 153 PRO PRO C . n 
C 1 61  GLY 61  154 154 GLY GLY C . n 
C 1 62  THR 62  155 155 THR THR C . n 
C 1 63  ARG 63  156 156 ARG ARG C . n 
C 1 64  VAL 64  157 157 VAL VAL C . n 
C 1 65  ARG 65  158 158 ARG ARG C . n 
C 1 66  ALA 66  159 159 ALA ALA C . n 
C 1 67  MET 67  160 160 MET MET C . n 
C 1 68  ALA 68  161 161 ALA ALA C . n 
C 1 69  ILE 69  162 162 ILE ILE C . n 
C 1 70  TYR 70  163 163 TYR TYR C . n 
C 1 71  LYS 71  164 164 LYS LYS C . n 
C 1 72  GLN 72  165 165 GLN GLN C . n 
C 1 73  SER 73  166 166 SER SER C . n 
C 1 74  GLN 74  167 167 GLN GLN C . n 
C 1 75  HIS 75  168 168 HIS HIS C . n 
C 1 76  MET 76  169 169 MET MET C . n 
C 1 77  THR 77  170 170 THR THR C . n 
C 1 78  GLU 78  171 171 GLU GLU C . n 
C 1 79  VAL 79  172 172 VAL VAL C . n 
C 1 80  VAL 80  173 173 VAL VAL C . n 
C 1 81  ARG 81  174 174 ARG ARG C . n 
C 1 82  ARG 82  175 175 ARG ARG C . n 
C 1 83  CYS 83  176 176 CYS CYS C . n 
C 1 84  PRO 84  177 177 PRO PRO C . n 
C 1 85  HIS 85  178 178 HIS HIS C . n 
C 1 86  HIS 86  179 179 HIS HIS C . n 
C 1 87  GLU 87  180 180 GLU GLU C . n 
C 1 88  ARG 88  181 181 ARG ARG C . n 
C 1 89  CYS 89  182 182 CYS CYS C . n 
C 1 90  SER 90  183 183 SER SER C . n 
C 1 91  ASP 91  184 184 ASP ASP C . n 
C 1 92  SER 92  185 185 SER SER C . n 
C 1 93  ASP 93  186 186 ASP ASP C . n 
C 1 94  GLY 94  187 187 GLY GLY C . n 
C 1 95  LEU 95  188 188 LEU LEU C . n 
C 1 96  ALA 96  189 189 ALA ALA C . n 
C 1 97  PRO 97  190 190 PRO PRO C . n 
C 1 98  PRO 98  191 191 PRO PRO C . n 
C 1 99  GLN 99  192 192 GLN GLN C . n 
C 1 100 HIS 100 193 193 HIS HIS C . n 
C 1 101 LEU 101 194 194 LEU LEU C . n 
C 1 102 ILE 102 195 195 ILE ILE C . n 
C 1 103 ARG 103 196 196 ARG ARG C . n 
C 1 104 VAL 104 197 197 VAL VAL C . n 
C 1 105 GLU 105 198 198 GLU GLU C . n 
C 1 106 GLY 106 199 199 GLY GLY C . n 
C 1 107 ASN 107 200 200 ASN ASN C . n 
C 1 108 LEU 108 201 201 LEU LEU C . n 
C 1 109 ARG 109 202 202 ARG ARG C . n 
C 1 110 VAL 110 203 203 VAL VAL C . n 
C 1 111 GLU 111 204 204 GLU GLU C . n 
C 1 112 TYR 112 205 205 TYR TYR C . n 
C 1 113 LEU 113 206 206 LEU LEU C . n 
C 1 114 ASP 114 207 207 ASP ASP C . n 
C 1 115 ASP 115 208 208 ASP ASP C . n 
C 1 116 ARG 116 209 209 ARG ARG C . n 
C 1 117 ASN 117 210 210 ASN ASN C . n 
C 1 118 THR 118 211 211 THR THR C . n 
C 1 119 PHE 119 212 212 PHE PHE C . n 
C 1 120 ARG 120 213 213 ARG ARG C . n 
C 1 121 HIS 121 214 214 HIS HIS C . n 
C 1 122 SER 122 215 215 SER SER C . n 
C 1 123 VAL 123 216 216 VAL VAL C . n 
C 1 124 VAL 124 217 217 VAL VAL C . n 
C 1 125 VAL 125 218 218 VAL VAL C . n 
C 1 126 PRO 126 219 219 PRO PRO C . n 
C 1 127 TYR 127 220 220 TYR TYR C . n 
C 1 128 GLU 128 221 221 GLU GLU C . n 
C 1 129 PRO 129 222 222 PRO PRO C . n 
C 1 130 PRO 130 223 223 PRO PRO C . n 
C 1 131 GLU 131 224 224 GLU GLU C . n 
C 1 132 VAL 132 225 ?   ?   ?   C . n 
C 1 133 GLY 133 226 ?   ?   ?   C . n 
C 1 134 SER 134 227 227 SER SER C . n 
C 1 135 ASP 135 228 228 ASP ASP C . n 
C 1 136 CYS 136 229 229 CYS CYS C . n 
C 1 137 THR 137 230 230 THR THR C . n 
C 1 138 THR 138 231 231 THR THR C . n 
C 1 139 ILE 139 232 232 ILE ILE C . n 
C 1 140 HIS 140 233 233 HIS HIS C . n 
C 1 141 TYR 141 234 234 TYR TYR C . n 
C 1 142 ASN 142 235 235 ASN ASN C . n 
C 1 143 TYR 143 236 236 TYR TYR C . n 
C 1 144 MET 144 237 237 MET MET C . n 
C 1 145 CYS 145 238 238 CYS CYS C . n 
C 1 146 ASN 146 239 239 ASN ASN C . n 
C 1 147 SER 147 240 240 SER SER C . n 
C 1 148 SER 148 241 241 SER SER C . n 
C 1 149 CYS 149 242 242 CYS CYS C . n 
C 1 150 MET 150 243 243 MET MET C . n 
C 1 151 GLY 151 244 244 GLY GLY C . n 
C 1 152 GLY 152 245 245 GLY GLY C . n 
C 1 153 MET 153 246 246 MET MET C . n 
C 1 154 ASN 154 247 247 ASN ASN C . n 
C 1 155 ARG 155 248 248 ARG ARG C . n 
C 1 156 ARG 156 249 249 ARG ARG C . n 
C 1 157 PRO 157 250 250 PRO PRO C . n 
C 1 158 ILE 158 251 251 ILE ILE C . n 
C 1 159 LEU 159 252 252 LEU LEU C . n 
C 1 160 THR 160 253 253 THR THR C . n 
C 1 161 ILE 161 254 254 ILE ILE C . n 
C 1 162 ILE 162 255 255 ILE ILE C . n 
C 1 163 THR 163 256 256 THR THR C . n 
C 1 164 LEU 164 257 257 LEU LEU C . n 
C 1 165 GLU 165 258 258 GLU GLU C . n 
C 1 166 ASP 166 259 259 ASP ASP C . n 
C 1 167 SER 167 260 260 SER SER C . n 
C 1 168 SER 168 261 261 SER SER C . n 
C 1 169 GLY 169 262 262 GLY GLY C . n 
C 1 170 ASN 170 263 263 ASN ASN C . n 
C 1 171 LEU 171 264 264 LEU LEU C . n 
C 1 172 LEU 172 265 265 LEU LEU C . n 
C 1 173 GLY 173 266 266 GLY GLY C . n 
C 1 174 ARG 174 267 267 ARG ARG C . n 
C 1 175 ASN 175 268 268 ASN ASN C . n 
C 1 176 SER 176 269 269 SER SER C . n 
C 1 177 PHE 177 270 270 PHE PHE C . n 
C 1 178 GLU 178 271 271 GLU GLU C . n 
C 1 179 VAL 179 272 272 VAL VAL C . n 
C 1 180 ARG 180 273 273 ARG ARG C . n 
C 1 181 VAL 181 274 274 VAL VAL C . n 
C 1 182 CYS 182 275 275 CYS CYS C . n 
C 1 183 ALA 183 276 276 ALA ALA C . n 
C 1 184 CYS 184 277 277 CYS CYS C . n 
C 1 185 PRO 185 278 278 PRO PRO C . n 
C 1 186 GLY 186 279 279 GLY GLY C . n 
C 1 187 ARG 187 280 280 ARG ARG C . n 
C 1 188 ASP 188 281 281 ASP ASP C . n 
C 1 189 ARG 189 282 282 ARG ARG C . n 
C 1 190 ARG 190 283 283 ARG ARG C . n 
C 1 191 THR 191 284 284 THR THR C . n 
C 1 192 GLU 192 285 285 GLU GLU C . n 
C 1 193 GLU 193 286 286 GLU GLU C . n 
C 1 194 GLU 194 287 287 GLU GLU C . n 
C 1 195 ASN 195 288 288 ASN ASN C . n 
C 1 196 LEU 196 289 289 LEU LEU C . n 
C 1 197 ARG 197 290 ?   ?   ?   C . n 
C 1 198 LYS 198 291 ?   ?   ?   C . n 
C 1 199 LYS 199 292 ?   ?   ?   C . n 
C 1 200 GLY 200 293 ?   ?   ?   C . n 
D 1 1   SER 1   94  ?   ?   ?   D . n 
D 1 2   SER 2   95  ?   ?   ?   D . n 
D 1 3   SER 3   96  96  SER SER D . n 
D 1 4   VAL 4   97  97  VAL VAL D . n 
D 1 5   PRO 5   98  98  PRO PRO D . n 
D 1 6   SER 6   99  99  SER SER D . n 
D 1 7   GLN 7   100 100 GLN GLN D . n 
D 1 8   LYS 8   101 101 LYS LYS D . n 
D 1 9   THR 9   102 102 THR THR D . n 
D 1 10  TYR 10  103 103 TYR TYR D . n 
D 1 11  GLN 11  104 104 GLN GLN D . n 
D 1 12  GLY 12  105 105 GLY GLY D . n 
D 1 13  SER 13  106 106 SER SER D . n 
D 1 14  TYR 14  107 107 TYR TYR D . n 
D 1 15  GLY 15  108 108 GLY GLY D . n 
D 1 16  PHE 16  109 109 PHE PHE D . n 
D 1 17  ARG 17  110 110 ARG ARG D . n 
D 1 18  LEU 18  111 111 LEU LEU D . n 
D 1 19  GLY 19  112 112 GLY GLY D . n 
D 1 20  PHE 20  113 113 PHE PHE D . n 
D 1 21  LEU 21  114 114 LEU LEU D . n 
D 1 22  HIS 22  115 115 HIS HIS D . n 
D 1 23  SER 23  116 116 SER SER D . n 
D 1 24  GLY 24  117 117 GLY GLY D . n 
D 1 25  THR 25  118 118 THR THR D . n 
D 1 26  ALA 26  119 119 ALA ALA D . n 
D 1 27  LYS 27  120 120 LYS LYS D . n 
D 1 28  SER 28  121 121 SER SER D . n 
D 1 29  VAL 29  122 122 VAL VAL D . n 
D 1 30  THR 30  123 123 THR THR D . n 
D 1 31  CYS 31  124 124 CYS CYS D . n 
D 1 32  THR 32  125 125 THR THR D . n 
D 1 33  TYR 33  126 126 TYR TYR D . n 
D 1 34  SER 34  127 127 SER SER D . n 
D 1 35  PRO 35  128 128 PRO PRO D . n 
D 1 36  ALA 36  129 129 ALA ALA D . n 
D 1 37  LEU 37  130 130 LEU LEU D . n 
D 1 38  ASN 38  131 131 ASN ASN D . n 
D 1 39  LYS 39  132 132 LYS LYS D . n 
D 1 40  MET 40  133 133 MET MET D . n 
D 1 41  PHE 41  134 134 PHE PHE D . n 
D 1 42  CYS 42  135 135 CYS CYS D . n 
D 1 43  GLN 43  136 136 GLN GLN D . n 
D 1 44  LEU 44  137 137 LEU LEU D . n 
D 1 45  ALA 45  138 138 ALA ALA D . n 
D 1 46  LYS 46  139 139 LYS LYS D . n 
D 1 47  THR 47  140 140 THR THR D . n 
D 1 48  CYS 48  141 141 CYS CYS D . n 
D 1 49  PRO 49  142 142 PRO PRO D . n 
D 1 50  VAL 50  143 143 VAL VAL D . n 
D 1 51  GLN 51  144 144 GLN GLN D . n 
D 1 52  LEU 52  145 145 LEU LEU D . n 
D 1 53  TRP 53  146 146 TRP TRP D . n 
D 1 54  VAL 54  147 147 VAL VAL D . n 
D 1 55  ASP 55  148 148 ASP ASP D . n 
D 1 56  SER 56  149 149 SER SER D . n 
D 1 57  THR 57  150 150 THR THR D . n 
D 1 58  PRO 58  151 151 PRO PRO D . n 
D 1 59  PRO 59  152 152 PRO PRO D . n 
D 1 60  PRO 60  153 153 PRO PRO D . n 
D 1 61  GLY 61  154 154 GLY GLY D . n 
D 1 62  THR 62  155 155 THR THR D . n 
D 1 63  ARG 63  156 156 ARG ARG D . n 
D 1 64  VAL 64  157 157 VAL VAL D . n 
D 1 65  ARG 65  158 158 ARG ARG D . n 
D 1 66  ALA 66  159 159 ALA ALA D . n 
D 1 67  MET 67  160 160 MET MET D . n 
D 1 68  ALA 68  161 161 ALA ALA D . n 
D 1 69  ILE 69  162 162 ILE ILE D . n 
D 1 70  TYR 70  163 163 TYR TYR D . n 
D 1 71  LYS 71  164 164 LYS LYS D . n 
D 1 72  GLN 72  165 165 GLN GLN D . n 
D 1 73  SER 73  166 166 SER SER D . n 
D 1 74  GLN 74  167 167 GLN GLN D . n 
D 1 75  HIS 75  168 168 HIS HIS D . n 
D 1 76  MET 76  169 169 MET MET D . n 
D 1 77  THR 77  170 170 THR THR D . n 
D 1 78  GLU 78  171 171 GLU GLU D . n 
D 1 79  VAL 79  172 172 VAL VAL D . n 
D 1 80  VAL 80  173 173 VAL VAL D . n 
D 1 81  ARG 81  174 174 ARG ARG D . n 
D 1 82  ARG 82  175 175 ARG ARG D . n 
D 1 83  CYS 83  176 176 CYS CYS D . n 
D 1 84  PRO 84  177 177 PRO PRO D . n 
D 1 85  HIS 85  178 178 HIS HIS D . n 
D 1 86  HIS 86  179 179 HIS HIS D . n 
D 1 87  GLU 87  180 180 GLU GLU D . n 
D 1 88  ARG 88  181 181 ARG ARG D . n 
D 1 89  CYS 89  182 182 CYS CYS D . n 
D 1 90  SER 90  183 183 SER SER D . n 
D 1 91  ASP 91  184 184 ASP ASP D . n 
D 1 92  SER 92  185 185 SER SER D . n 
D 1 93  ASP 93  186 186 ASP ASP D . n 
D 1 94  GLY 94  187 187 GLY GLY D . n 
D 1 95  LEU 95  188 188 LEU LEU D . n 
D 1 96  ALA 96  189 189 ALA ALA D . n 
D 1 97  PRO 97  190 190 PRO PRO D . n 
D 1 98  PRO 98  191 191 PRO PRO D . n 
D 1 99  GLN 99  192 192 GLN GLN D . n 
D 1 100 HIS 100 193 193 HIS HIS D . n 
D 1 101 LEU 101 194 194 LEU LEU D . n 
D 1 102 ILE 102 195 195 ILE ILE D . n 
D 1 103 ARG 103 196 196 ARG ARG D . n 
D 1 104 VAL 104 197 197 VAL VAL D . n 
D 1 105 GLU 105 198 198 GLU GLU D . n 
D 1 106 GLY 106 199 199 GLY GLY D . n 
D 1 107 ASN 107 200 200 ASN ASN D . n 
D 1 108 LEU 108 201 201 LEU LEU D . n 
D 1 109 ARG 109 202 202 ARG ARG D . n 
D 1 110 VAL 110 203 203 VAL VAL D . n 
D 1 111 GLU 111 204 204 GLU GLU D . n 
D 1 112 TYR 112 205 205 TYR TYR D . n 
D 1 113 LEU 113 206 206 LEU LEU D . n 
D 1 114 ASP 114 207 207 ASP ASP D . n 
D 1 115 ASP 115 208 208 ASP ASP D . n 
D 1 116 ARG 116 209 209 ARG ARG D . n 
D 1 117 ASN 117 210 210 ASN ASN D . n 
D 1 118 THR 118 211 211 THR THR D . n 
D 1 119 PHE 119 212 212 PHE PHE D . n 
D 1 120 ARG 120 213 213 ARG ARG D . n 
D 1 121 HIS 121 214 214 HIS HIS D . n 
D 1 122 SER 122 215 215 SER SER D . n 
D 1 123 VAL 123 216 216 VAL VAL D . n 
D 1 124 VAL 124 217 217 VAL VAL D . n 
D 1 125 VAL 125 218 218 VAL VAL D . n 
D 1 126 PRO 126 219 219 PRO PRO D . n 
D 1 127 TYR 127 220 220 TYR TYR D . n 
D 1 128 GLU 128 221 221 GLU GLU D . n 
D 1 129 PRO 129 222 222 PRO PRO D . n 
D 1 130 PRO 130 223 223 PRO PRO D . n 
D 1 131 GLU 131 224 224 GLU GLU D . n 
D 1 132 VAL 132 225 225 VAL VAL D . n 
D 1 133 GLY 133 226 226 GLY GLY D . n 
D 1 134 SER 134 227 227 SER SER D . n 
D 1 135 ASP 135 228 228 ASP ASP D . n 
D 1 136 CYS 136 229 229 CYS CYS D . n 
D 1 137 THR 137 230 230 THR THR D . n 
D 1 138 THR 138 231 231 THR THR D . n 
D 1 139 ILE 139 232 232 ILE ILE D . n 
D 1 140 HIS 140 233 233 HIS HIS D . n 
D 1 141 TYR 141 234 234 TYR TYR D . n 
D 1 142 ASN 142 235 235 ASN ASN D . n 
D 1 143 TYR 143 236 236 TYR TYR D . n 
D 1 144 MET 144 237 237 MET MET D . n 
D 1 145 CYS 145 238 238 CYS CYS D . n 
D 1 146 ASN 146 239 239 ASN ASN D . n 
D 1 147 SER 147 240 240 SER SER D . n 
D 1 148 SER 148 241 241 SER SER D . n 
D 1 149 CYS 149 242 242 CYS CYS D . n 
D 1 150 MET 150 243 243 MET MET D . n 
D 1 151 GLY 151 244 244 GLY GLY D . n 
D 1 152 GLY 152 245 245 GLY GLY D . n 
D 1 153 MET 153 246 246 MET MET D . n 
D 1 154 ASN 154 247 247 ASN ASN D . n 
D 1 155 ARG 155 248 248 ARG ARG D . n 
D 1 156 ARG 156 249 249 ARG ARG D . n 
D 1 157 PRO 157 250 250 PRO PRO D . n 
D 1 158 ILE 158 251 251 ILE ILE D . n 
D 1 159 LEU 159 252 252 LEU LEU D . n 
D 1 160 THR 160 253 253 THR THR D . n 
D 1 161 ILE 161 254 254 ILE ILE D . n 
D 1 162 ILE 162 255 255 ILE ILE D . n 
D 1 163 THR 163 256 256 THR THR D . n 
D 1 164 LEU 164 257 257 LEU LEU D . n 
D 1 165 GLU 165 258 258 GLU GLU D . n 
D 1 166 ASP 166 259 259 ASP ASP D . n 
D 1 167 SER 167 260 260 SER SER D . n 
D 1 168 SER 168 261 261 SER SER D . n 
D 1 169 GLY 169 262 262 GLY GLY D . n 
D 1 170 ASN 170 263 263 ASN ASN D . n 
D 1 171 LEU 171 264 264 LEU LEU D . n 
D 1 172 LEU 172 265 265 LEU LEU D . n 
D 1 173 GLY 173 266 266 GLY GLY D . n 
D 1 174 ARG 174 267 267 ARG ARG D . n 
D 1 175 ASN 175 268 268 ASN ASN D . n 
D 1 176 SER 176 269 269 SER SER D . n 
D 1 177 PHE 177 270 270 PHE PHE D . n 
D 1 178 GLU 178 271 271 GLU GLU D . n 
D 1 179 VAL 179 272 272 VAL VAL D . n 
D 1 180 ARG 180 273 273 ARG ARG D . n 
D 1 181 VAL 181 274 274 VAL VAL D . n 
D 1 182 CYS 182 275 275 CYS CYS D . n 
D 1 183 ALA 183 276 276 ALA ALA D . n 
D 1 184 CYS 184 277 277 CYS CYS D . n 
D 1 185 PRO 185 278 278 PRO PRO D . n 
D 1 186 GLY 186 279 279 GLY GLY D . n 
D 1 187 ARG 187 280 280 ARG ARG D . n 
D 1 188 ASP 188 281 281 ASP ASP D . n 
D 1 189 ARG 189 282 282 ARG ARG D . n 
D 1 190 ARG 190 283 283 ARG ARG D . n 
D 1 191 THR 191 284 284 THR THR D . n 
D 1 192 GLU 192 285 285 GLU GLU D . n 
D 1 193 GLU 193 286 286 GLU GLU D . n 
D 1 194 GLU 194 287 287 GLU GLU D . n 
D 1 195 ASN 195 288 288 ASN ASN D . n 
D 1 196 LEU 196 289 289 LEU LEU D . n 
D 1 197 ARG 197 290 ?   ?   ?   D . n 
D 1 198 LYS 198 291 ?   ?   ?   D . n 
D 1 199 LYS 199 292 ?   ?   ?   D . n 
D 1 200 GLY 200 293 ?   ?   ?   D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 ZN    1   301 1   ZN    ZN  A . 
F 3 GOL   1   302 2   GOL   GOL A . 
G 4 A1LUZ 1   301 1   A1LUZ LIG B . 
H 2 ZN    1   302 2   ZN    ZN  B . 
I 2 ZN    1   301 3   ZN    ZN  C . 
J 3 GOL   1   302 1   GOL   GOL C . 
K 4 A1LUZ 1   301 2   A1LUZ LIG D . 
L 2 ZN    1   302 4   ZN    ZN  D . 
M 3 GOL   1   303 3   GOL   GOL D . 
N 5 HOH   1   401 438 HOH   HOH A . 
N 5 HOH   2   402 291 HOH   HOH A . 
N 5 HOH   3   403 90  HOH   HOH A . 
N 5 HOH   4   404 87  HOH   HOH A . 
N 5 HOH   5   405 293 HOH   HOH A . 
N 5 HOH   6   406 352 HOH   HOH A . 
N 5 HOH   7   407 266 HOH   HOH A . 
N 5 HOH   8   408 328 HOH   HOH A . 
N 5 HOH   9   409 49  HOH   HOH A . 
N 5 HOH   10  410 194 HOH   HOH A . 
N 5 HOH   11  411 386 HOH   HOH A . 
N 5 HOH   12  412 172 HOH   HOH A . 
N 5 HOH   13  413 353 HOH   HOH A . 
N 5 HOH   14  414 81  HOH   HOH A . 
N 5 HOH   15  415 462 HOH   HOH A . 
N 5 HOH   16  416 125 HOH   HOH A . 
N 5 HOH   17  417 105 HOH   HOH A . 
N 5 HOH   18  418 303 HOH   HOH A . 
N 5 HOH   19  419 284 HOH   HOH A . 
N 5 HOH   20  420 297 HOH   HOH A . 
N 5 HOH   21  421 11  HOH   HOH A . 
N 5 HOH   22  422 432 HOH   HOH A . 
N 5 HOH   23  423 235 HOH   HOH A . 
N 5 HOH   24  424 298 HOH   HOH A . 
N 5 HOH   25  425 128 HOH   HOH A . 
N 5 HOH   26  426 86  HOH   HOH A . 
N 5 HOH   27  427 1   HOH   HOH A . 
N 5 HOH   28  428 200 HOH   HOH A . 
N 5 HOH   29  429 213 HOH   HOH A . 
N 5 HOH   30  430 348 HOH   HOH A . 
N 5 HOH   31  431 104 HOH   HOH A . 
N 5 HOH   32  432 459 HOH   HOH A . 
N 5 HOH   33  433 369 HOH   HOH A . 
N 5 HOH   34  434 4   HOH   HOH A . 
N 5 HOH   35  435 370 HOH   HOH A . 
N 5 HOH   36  436 168 HOH   HOH A . 
N 5 HOH   37  437 219 HOH   HOH A . 
N 5 HOH   38  438 224 HOH   HOH A . 
N 5 HOH   39  439 154 HOH   HOH A . 
N 5 HOH   40  440 85  HOH   HOH A . 
N 5 HOH   41  441 334 HOH   HOH A . 
N 5 HOH   42  442 88  HOH   HOH A . 
N 5 HOH   43  443 76  HOH   HOH A . 
N 5 HOH   44  444 126 HOH   HOH A . 
N 5 HOH   45  445 102 HOH   HOH A . 
N 5 HOH   46  446 238 HOH   HOH A . 
N 5 HOH   47  447 84  HOH   HOH A . 
N 5 HOH   48  448 156 HOH   HOH A . 
N 5 HOH   49  449 100 HOH   HOH A . 
N 5 HOH   50  450 197 HOH   HOH A . 
N 5 HOH   51  451 320 HOH   HOH A . 
N 5 HOH   52  452 192 HOH   HOH A . 
N 5 HOH   53  453 114 HOH   HOH A . 
N 5 HOH   54  454 132 HOH   HOH A . 
N 5 HOH   55  455 292 HOH   HOH A . 
N 5 HOH   56  456 245 HOH   HOH A . 
N 5 HOH   57  457 166 HOH   HOH A . 
N 5 HOH   58  458 257 HOH   HOH A . 
N 5 HOH   59  459 79  HOH   HOH A . 
N 5 HOH   60  460 103 HOH   HOH A . 
N 5 HOH   61  461 208 HOH   HOH A . 
N 5 HOH   62  462 179 HOH   HOH A . 
N 5 HOH   63  463 7   HOH   HOH A . 
N 5 HOH   64  464 239 HOH   HOH A . 
N 5 HOH   65  465 59  HOH   HOH A . 
N 5 HOH   66  466 211 HOH   HOH A . 
N 5 HOH   67  467 232 HOH   HOH A . 
N 5 HOH   68  468 346 HOH   HOH A . 
N 5 HOH   69  469 180 HOH   HOH A . 
N 5 HOH   70  470 304 HOH   HOH A . 
N 5 HOH   71  471 322 HOH   HOH A . 
N 5 HOH   72  472 212 HOH   HOH A . 
N 5 HOH   73  473 345 HOH   HOH A . 
N 5 HOH   74  474 77  HOH   HOH A . 
N 5 HOH   75  475 244 HOH   HOH A . 
N 5 HOH   76  476 83  HOH   HOH A . 
N 5 HOH   77  477 106 HOH   HOH A . 
N 5 HOH   78  478 113 HOH   HOH A . 
N 5 HOH   79  479 157 HOH   HOH A . 
N 5 HOH   80  480 410 HOH   HOH A . 
N 5 HOH   81  481 80  HOH   HOH A . 
N 5 HOH   82  482 131 HOH   HOH A . 
N 5 HOH   83  483 367 HOH   HOH A . 
N 5 HOH   84  484 111 HOH   HOH A . 
N 5 HOH   85  485 368 HOH   HOH A . 
N 5 HOH   86  486 120 HOH   HOH A . 
N 5 HOH   87  487 142 HOH   HOH A . 
N 5 HOH   88  488 433 HOH   HOH A . 
N 5 HOH   89  489 138 HOH   HOH A . 
N 5 HOH   90  490 221 HOH   HOH A . 
N 5 HOH   91  491 78  HOH   HOH A . 
N 5 HOH   92  492 89  HOH   HOH A . 
N 5 HOH   93  493 319 HOH   HOH A . 
N 5 HOH   94  494 101 HOH   HOH A . 
N 5 HOH   95  495 299 HOH   HOH A . 
N 5 HOH   96  496 163 HOH   HOH A . 
N 5 HOH   97  497 155 HOH   HOH A . 
N 5 HOH   98  498 347 HOH   HOH A . 
N 5 HOH   99  499 158 HOH   HOH A . 
N 5 HOH   100 500 445 HOH   HOH A . 
N 5 HOH   101 501 160 HOH   HOH A . 
N 5 HOH   102 502 440 HOH   HOH A . 
N 5 HOH   103 503 302 HOH   HOH A . 
N 5 HOH   104 504 437 HOH   HOH A . 
N 5 HOH   105 505 198 HOH   HOH A . 
N 5 HOH   106 506 129 HOH   HOH A . 
N 5 HOH   107 507 321 HOH   HOH A . 
N 5 HOH   108 508 195 HOH   HOH A . 
N 5 HOH   109 509 159 HOH   HOH A . 
N 5 HOH   110 510 58  HOH   HOH A . 
N 5 HOH   111 511 424 HOH   HOH A . 
N 5 HOH   112 512 426 HOH   HOH A . 
N 5 HOH   113 513 285 HOH   HOH A . 
N 5 HOH   114 514 344 HOH   HOH A . 
N 5 HOH   115 515 436 HOH   HOH A . 
O 5 HOH   1   401 336 HOH   HOH B . 
O 5 HOH   2   402 216 HOH   HOH B . 
O 5 HOH   3   403 333 HOH   HOH B . 
O 5 HOH   4   404 282 HOH   HOH B . 
O 5 HOH   5   405 226 HOH   HOH B . 
O 5 HOH   6   406 3   HOH   HOH B . 
O 5 HOH   7   407 331 HOH   HOH B . 
O 5 HOH   8   408 268 HOH   HOH B . 
O 5 HOH   9   409 315 HOH   HOH B . 
O 5 HOH   10  410 199 HOH   HOH B . 
O 5 HOH   11  411 34  HOH   HOH B . 
O 5 HOH   12  412 124 HOH   HOH B . 
O 5 HOH   13  413 18  HOH   HOH B . 
O 5 HOH   14  414 225 HOH   HOH B . 
O 5 HOH   15  415 371 HOH   HOH B . 
O 5 HOH   16  416 188 HOH   HOH B . 
O 5 HOH   17  417 246 HOH   HOH B . 
O 5 HOH   18  418 8   HOH   HOH B . 
O 5 HOH   19  419 189 HOH   HOH B . 
O 5 HOH   20  420 202 HOH   HOH B . 
O 5 HOH   21  421 288 HOH   HOH B . 
O 5 HOH   22  422 135 HOH   HOH B . 
O 5 HOH   23  423 461 HOH   HOH B . 
O 5 HOH   24  424 384 HOH   HOH B . 
O 5 HOH   25  425 164 HOH   HOH B . 
O 5 HOH   26  426 463 HOH   HOH B . 
O 5 HOH   27  427 354 HOH   HOH B . 
O 5 HOH   28  428 191 HOH   HOH B . 
O 5 HOH   29  429 314 HOH   HOH B . 
O 5 HOH   30  430 16  HOH   HOH B . 
O 5 HOH   31  431 32  HOH   HOH B . 
O 5 HOH   32  432 249 HOH   HOH B . 
O 5 HOH   33  433 169 HOH   HOH B . 
O 5 HOH   34  434 22  HOH   HOH B . 
O 5 HOH   35  435 349 HOH   HOH B . 
O 5 HOH   36  436 171 HOH   HOH B . 
O 5 HOH   37  437 204 HOH   HOH B . 
O 5 HOH   38  438 332 HOH   HOH B . 
O 5 HOH   39  439 175 HOH   HOH B . 
O 5 HOH   40  440 382 HOH   HOH B . 
O 5 HOH   41  441 366 HOH   HOH B . 
O 5 HOH   42  442 313 HOH   HOH B . 
O 5 HOH   43  443 396 HOH   HOH B . 
O 5 HOH   44  444 399 HOH   HOH B . 
O 5 HOH   45  445 174 HOH   HOH B . 
O 5 HOH   46  446 107 HOH   HOH B . 
O 5 HOH   47  447 23  HOH   HOH B . 
O 5 HOH   48  448 265 HOH   HOH B . 
O 5 HOH   49  449 351 HOH   HOH B . 
O 5 HOH   50  450 355 HOH   HOH B . 
O 5 HOH   51  451 457 HOH   HOH B . 
O 5 HOH   52  452 390 HOH   HOH B . 
O 5 HOH   53  453 19  HOH   HOH B . 
O 5 HOH   54  454 279 HOH   HOH B . 
O 5 HOH   55  455 178 HOH   HOH B . 
O 5 HOH   56  456 21  HOH   HOH B . 
O 5 HOH   57  457 144 HOH   HOH B . 
O 5 HOH   58  458 220 HOH   HOH B . 
O 5 HOH   59  459 20  HOH   HOH B . 
O 5 HOH   60  460 258 HOH   HOH B . 
O 5 HOH   61  461 26  HOH   HOH B . 
O 5 HOH   62  462 17  HOH   HOH B . 
O 5 HOH   63  463 454 HOH   HOH B . 
O 5 HOH   64  464 122 HOH   HOH B . 
O 5 HOH   65  465 478 HOH   HOH B . 
O 5 HOH   66  466 338 HOH   HOH B . 
O 5 HOH   67  467 453 HOH   HOH B . 
O 5 HOH   68  468 460 HOH   HOH B . 
O 5 HOH   69  469 29  HOH   HOH B . 
O 5 HOH   70  470 447 HOH   HOH B . 
O 5 HOH   71  471 230 HOH   HOH B . 
O 5 HOH   72  472 286 HOH   HOH B . 
O 5 HOH   73  473 277 HOH   HOH B . 
O 5 HOH   74  474 33  HOH   HOH B . 
O 5 HOH   75  475 27  HOH   HOH B . 
O 5 HOH   76  476 383 HOH   HOH B . 
O 5 HOH   77  477 190 HOH   HOH B . 
O 5 HOH   78  478 252 HOH   HOH B . 
O 5 HOH   79  479 446 HOH   HOH B . 
O 5 HOH   80  480 325 HOH   HOH B . 
O 5 HOH   81  481 31  HOH   HOH B . 
O 5 HOH   82  482 392 HOH   HOH B . 
O 5 HOH   83  483 439 HOH   HOH B . 
O 5 HOH   84  484 14  HOH   HOH B . 
O 5 HOH   85  485 391 HOH   HOH B . 
O 5 HOH   86  486 444 HOH   HOH B . 
O 5 HOH   87  487 253 HOH   HOH B . 
O 5 HOH   88  488 30  HOH   HOH B . 
O 5 HOH   89  489 161 HOH   HOH B . 
O 5 HOH   90  490 365 HOH   HOH B . 
O 5 HOH   91  491 456 HOH   HOH B . 
O 5 HOH   92  492 136 HOH   HOH B . 
O 5 HOH   93  493 350 HOH   HOH B . 
O 5 HOH   94  494 280 HOH   HOH B . 
O 5 HOH   95  495 401 HOH   HOH B . 
O 5 HOH   96  496 412 HOH   HOH B . 
O 5 HOH   97  497 395 HOH   HOH B . 
O 5 HOH   98  498 283 HOH   HOH B . 
O 5 HOH   99  499 24  HOH   HOH B . 
O 5 HOH   100 500 379 HOH   HOH B . 
O 5 HOH   101 501 411 HOH   HOH B . 
O 5 HOH   102 502 28  HOH   HOH B . 
O 5 HOH   103 503 375 HOH   HOH B . 
O 5 HOH   104 504 329 HOH   HOH B . 
O 5 HOH   105 505 402 HOH   HOH B . 
O 5 HOH   106 506 397 HOH   HOH B . 
O 5 HOH   107 507 455 HOH   HOH B . 
O 5 HOH   108 508 269 HOH   HOH B . 
O 5 HOH   109 509 254 HOH   HOH B . 
O 5 HOH   110 510 398 HOH   HOH B . 
O 5 HOH   111 511 458 HOH   HOH B . 
O 5 HOH   112 512 394 HOH   HOH B . 
O 5 HOH   113 513 267 HOH   HOH B . 
O 5 HOH   114 514 413 HOH   HOH B . 
O 5 HOH   115 515 381 HOH   HOH B . 
O 5 HOH   116 516 448 HOH   HOH B . 
O 5 HOH   117 517 450 HOH   HOH B . 
O 5 HOH   118 518 316 HOH   HOH B . 
O 5 HOH   119 519 385 HOH   HOH B . 
O 5 HOH   120 520 464 HOH   HOH B . 
O 5 HOH   121 521 393 HOH   HOH B . 
O 5 HOH   122 522 71  HOH   HOH B . 
O 5 HOH   123 523 223 HOH   HOH B . 
O 5 HOH   124 524 330 HOH   HOH B . 
O 5 HOH   125 525 474 HOH   HOH B . 
P 5 HOH   1   401 356 HOH   HOH C . 
P 5 HOH   2   402 295 HOH   HOH C . 
P 5 HOH   3   403 110 HOH   HOH C . 
P 5 HOH   4   404 109 HOH   HOH C . 
P 5 HOH   5   405 205 HOH   HOH C . 
P 5 HOH   6   406 466 HOH   HOH C . 
P 5 HOH   7   407 247 HOH   HOH C . 
P 5 HOH   8   408 471 HOH   HOH C . 
P 5 HOH   9   409 75  HOH   HOH C . 
P 5 HOH   10  410 115 HOH   HOH C . 
P 5 HOH   11  411 5   HOH   HOH C . 
P 5 HOH   12  412 240 HOH   HOH C . 
P 5 HOH   13  413 243 HOH   HOH C . 
P 5 HOH   14  414 99  HOH   HOH C . 
P 5 HOH   15  415 127 HOH   HOH C . 
P 5 HOH   16  416 229 HOH   HOH C . 
P 5 HOH   17  417 307 HOH   HOH C . 
P 5 HOH   18  418 96  HOH   HOH C . 
P 5 HOH   19  419 91  HOH   HOH C . 
P 5 HOH   20  420 227 HOH   HOH C . 
P 5 HOH   21  421 342 HOH   HOH C . 
P 5 HOH   22  422 359 HOH   HOH C . 
P 5 HOH   23  423 185 HOH   HOH C . 
P 5 HOH   24  424 435 HOH   HOH C . 
P 5 HOH   25  425 442 HOH   HOH C . 
P 5 HOH   26  426 98  HOH   HOH C . 
P 5 HOH   27  427 300 HOH   HOH C . 
P 5 HOH   28  428 67  HOH   HOH C . 
P 5 HOH   29  429 117 HOH   HOH C . 
P 5 HOH   30  430 206 HOH   HOH C . 
P 5 HOH   31  431 62  HOH   HOH C . 
P 5 HOH   32  432 231 HOH   HOH C . 
P 5 HOH   33  433 176 HOH   HOH C . 
P 5 HOH   34  434 340 HOH   HOH C . 
P 5 HOH   35  435 422 HOH   HOH C . 
P 5 HOH   36  436 308 HOH   HOH C . 
P 5 HOH   37  437 2   HOH   HOH C . 
P 5 HOH   38  438 184 HOH   HOH C . 
P 5 HOH   39  439 66  HOH   HOH C . 
P 5 HOH   40  440 183 HOH   HOH C . 
P 5 HOH   41  441 207 HOH   HOH C . 
P 5 HOH   42  442 69  HOH   HOH C . 
P 5 HOH   43  443 248 HOH   HOH C . 
P 5 HOH   44  444 92  HOH   HOH C . 
P 5 HOH   45  445 97  HOH   HOH C . 
P 5 HOH   46  446 140 HOH   HOH C . 
P 5 HOH   47  447 237 HOH   HOH C . 
P 5 HOH   48  448 203 HOH   HOH C . 
P 5 HOH   49  449 93  HOH   HOH C . 
P 5 HOH   50  450 290 HOH   HOH C . 
P 5 HOH   51  451 337 HOH   HOH C . 
P 5 HOH   52  452 170 HOH   HOH C . 
P 5 HOH   53  453 234 HOH   HOH C . 
P 5 HOH   54  454 6   HOH   HOH C . 
P 5 HOH   55  455 143 HOH   HOH C . 
P 5 HOH   56  456 222 HOH   HOH C . 
P 5 HOH   57  457 94  HOH   HOH C . 
P 5 HOH   58  458 256 HOH   HOH C . 
P 5 HOH   59  459 312 HOH   HOH C . 
P 5 HOH   60  460 362 HOH   HOH C . 
P 5 HOH   61  461 465 HOH   HOH C . 
P 5 HOH   62  462 130 HOH   HOH C . 
P 5 HOH   63  463 468 HOH   HOH C . 
P 5 HOH   64  464 364 HOH   HOH C . 
P 5 HOH   65  465 259 HOH   HOH C . 
P 5 HOH   66  466 441 HOH   HOH C . 
P 5 HOH   67  467 339 HOH   HOH C . 
P 5 HOH   68  468 361 HOH   HOH C . 
P 5 HOH   69  469 409 HOH   HOH C . 
P 5 HOH   70  470 228 HOH   HOH C . 
P 5 HOH   71  471 116 HOH   HOH C . 
P 5 HOH   72  472 55  HOH   HOH C . 
P 5 HOH   73  473 260 HOH   HOH C . 
P 5 HOH   74  474 61  HOH   HOH C . 
P 5 HOH   75  475 119 HOH   HOH C . 
P 5 HOH   76  476 210 HOH   HOH C . 
P 5 HOH   77  477 251 HOH   HOH C . 
P 5 HOH   78  478 389 HOH   HOH C . 
P 5 HOH   79  479 139 HOH   HOH C . 
P 5 HOH   80  480 423 HOH   HOH C . 
P 5 HOH   81  481 363 HOH   HOH C . 
P 5 HOH   82  482 112 HOH   HOH C . 
P 5 HOH   83  483 60  HOH   HOH C . 
P 5 HOH   84  484 137 HOH   HOH C . 
P 5 HOH   85  485 421 HOH   HOH C . 
P 5 HOH   86  486 309 HOH   HOH C . 
P 5 HOH   87  487 40  HOH   HOH C . 
P 5 HOH   88  488 56  HOH   HOH C . 
P 5 HOH   89  489 95  HOH   HOH C . 
P 5 HOH   90  490 262 HOH   HOH C . 
P 5 HOH   91  491 57  HOH   HOH C . 
P 5 HOH   92  492 469 HOH   HOH C . 
P 5 HOH   93  493 341 HOH   HOH C . 
P 5 HOH   94  494 408 HOH   HOH C . 
P 5 HOH   95  495 470 HOH   HOH C . 
P 5 HOH   96  496 360 HOH   HOH C . 
P 5 HOH   97  497 141 HOH   HOH C . 
P 5 HOH   98  498 431 HOH   HOH C . 
P 5 HOH   99  499 118 HOH   HOH C . 
P 5 HOH   100 500 311 HOH   HOH C . 
P 5 HOH   101 501 233 HOH   HOH C . 
P 5 HOH   102 502 54  HOH   HOH C . 
P 5 HOH   103 503 296 HOH   HOH C . 
P 5 HOH   104 504 472 HOH   HOH C . 
P 5 HOH   105 505 357 HOH   HOH C . 
P 5 HOH   106 506 434 HOH   HOH C . 
P 5 HOH   107 507 68  HOH   HOH C . 
P 5 HOH   108 508 70  HOH   HOH C . 
P 5 HOH   109 509 388 HOH   HOH C . 
P 5 HOH   110 510 310 HOH   HOH C . 
P 5 HOH   111 511 387 HOH   HOH C . 
P 5 HOH   112 512 358 HOH   HOH C . 
P 5 HOH   113 513 343 HOH   HOH C . 
Q 5 HOH   1   401 215 HOH   HOH D . 
Q 5 HOH   2   402 376 HOH   HOH D . 
Q 5 HOH   3   403 181 HOH   HOH D . 
Q 5 HOH   4   404 123 HOH   HOH D . 
Q 5 HOH   5   405 475 HOH   HOH D . 
Q 5 HOH   6   406 48  HOH   HOH D . 
Q 5 HOH   7   407 173 HOH   HOH D . 
Q 5 HOH   8   408 301 HOH   HOH D . 
Q 5 HOH   9   409 167 HOH   HOH D . 
Q 5 HOH   10  410 452 HOH   HOH D . 
Q 5 HOH   11  411 414 HOH   HOH D . 
Q 5 HOH   12  412 10  HOH   HOH D . 
Q 5 HOH   13  413 13  HOH   HOH D . 
Q 5 HOH   14  414 306 HOH   HOH D . 
Q 5 HOH   15  415 45  HOH   HOH D . 
Q 5 HOH   16  416 217 HOH   HOH D . 
Q 5 HOH   17  417 74  HOH   HOH D . 
Q 5 HOH   18  418 374 HOH   HOH D . 
Q 5 HOH   19  419 378 HOH   HOH D . 
Q 5 HOH   20  420 477 HOH   HOH D . 
Q 5 HOH   21  421 261 HOH   HOH D . 
Q 5 HOH   22  422 270 HOH   HOH D . 
Q 5 HOH   23  423 451 HOH   HOH D . 
Q 5 HOH   24  424 9   HOH   HOH D . 
Q 5 HOH   25  425 177 HOH   HOH D . 
Q 5 HOH   26  426 264 HOH   HOH D . 
Q 5 HOH   27  427 327 HOH   HOH D . 
Q 5 HOH   28  428 133 HOH   HOH D . 
Q 5 HOH   29  429 47  HOH   HOH D . 
Q 5 HOH   30  430 418 HOH   HOH D . 
Q 5 HOH   31  431 165 HOH   HOH D . 
Q 5 HOH   32  432 323 HOH   HOH D . 
Q 5 HOH   33  433 373 HOH   HOH D . 
Q 5 HOH   34  434 305 HOH   HOH D . 
Q 5 HOH   35  435 242 HOH   HOH D . 
Q 5 HOH   36  436 44  HOH   HOH D . 
Q 5 HOH   37  437 15  HOH   HOH D . 
Q 5 HOH   38  438 39  HOH   HOH D . 
Q 5 HOH   39  439 193 HOH   HOH D . 
Q 5 HOH   40  440 403 HOH   HOH D . 
Q 5 HOH   41  441 250 HOH   HOH D . 
Q 5 HOH   42  442 186 HOH   HOH D . 
Q 5 HOH   43  443 318 HOH   HOH D . 
Q 5 HOH   44  444 271 HOH   HOH D . 
Q 5 HOH   45  445 273 HOH   HOH D . 
Q 5 HOH   46  446 372 HOH   HOH D . 
Q 5 HOH   47  447 255 HOH   HOH D . 
Q 5 HOH   48  448 72  HOH   HOH D . 
Q 5 HOH   49  449 187 HOH   HOH D . 
Q 5 HOH   50  450 236 HOH   HOH D . 
Q 5 HOH   51  451 425 HOH   HOH D . 
Q 5 HOH   52  452 404 HOH   HOH D . 
Q 5 HOH   53  453 162 HOH   HOH D . 
Q 5 HOH   54  454 201 HOH   HOH D . 
Q 5 HOH   55  455 335 HOH   HOH D . 
Q 5 HOH   56  456 287 HOH   HOH D . 
Q 5 HOH   57  457 479 HOH   HOH D . 
Q 5 HOH   58  458 12  HOH   HOH D . 
Q 5 HOH   59  459 108 HOH   HOH D . 
Q 5 HOH   60  460 276 HOH   HOH D . 
Q 5 HOH   61  461 182 HOH   HOH D . 
Q 5 HOH   62  462 43  HOH   HOH D . 
Q 5 HOH   63  463 443 HOH   HOH D . 
Q 5 HOH   64  464 149 HOH   HOH D . 
Q 5 HOH   65  465 153 HOH   HOH D . 
Q 5 HOH   66  466 405 HOH   HOH D . 
Q 5 HOH   67  467 241 HOH   HOH D . 
Q 5 HOH   68  468 196 HOH   HOH D . 
Q 5 HOH   69  469 147 HOH   HOH D . 
Q 5 HOH   70  470 46  HOH   HOH D . 
Q 5 HOH   71  471 214 HOH   HOH D . 
Q 5 HOH   72  472 294 HOH   HOH D . 
Q 5 HOH   73  473 415 HOH   HOH D . 
Q 5 HOH   74  474 65  HOH   HOH D . 
Q 5 HOH   75  475 429 HOH   HOH D . 
Q 5 HOH   76  476 420 HOH   HOH D . 
Q 5 HOH   77  477 42  HOH   HOH D . 
Q 5 HOH   78  478 473 HOH   HOH D . 
Q 5 HOH   79  479 324 HOH   HOH D . 
Q 5 HOH   80  480 209 HOH   HOH D . 
Q 5 HOH   81  481 377 HOH   HOH D . 
Q 5 HOH   82  482 428 HOH   HOH D . 
Q 5 HOH   83  483 145 HOH   HOH D . 
Q 5 HOH   84  484 476 HOH   HOH D . 
Q 5 HOH   85  485 25  HOH   HOH D . 
Q 5 HOH   86  486 417 HOH   HOH D . 
Q 5 HOH   87  487 38  HOH   HOH D . 
Q 5 HOH   88  488 427 HOH   HOH D . 
Q 5 HOH   89  489 134 HOH   HOH D . 
Q 5 HOH   90  490 73  HOH   HOH D . 
Q 5 HOH   91  491 152 HOH   HOH D . 
Q 5 HOH   92  492 289 HOH   HOH D . 
Q 5 HOH   93  493 406 HOH   HOH D . 
Q 5 HOH   94  494 407 HOH   HOH D . 
Q 5 HOH   95  495 317 HOH   HOH D . 
Q 5 HOH   96  496 467 HOH   HOH D . 
Q 5 HOH   97  497 416 HOH   HOH D . 
Q 5 HOH   98  498 37  HOH   HOH D . 
Q 5 HOH   99  499 400 HOH   HOH D . 
Q 5 HOH   100 500 41  HOH   HOH D . 
Q 5 HOH   101 501 449 HOH   HOH D . 
Q 5 HOH   102 502 146 HOH   HOH D . 
Q 5 HOH   103 503 380 HOH   HOH D . 
Q 5 HOH   104 504 326 HOH   HOH D . 
Q 5 HOH   105 505 274 HOH   HOH D . 
Q 5 HOH   106 506 148 HOH   HOH D . 
Q 5 HOH   107 507 272 HOH   HOH D . 
Q 5 HOH   108 508 278 HOH   HOH D . 
Q 5 HOH   109 509 263 HOH   HOH D . 
Q 5 HOH   110 510 281 HOH   HOH D . 
Q 5 HOH   111 511 419 HOH   HOH D . 
Q 5 HOH   112 512 275 HOH   HOH D . 
Q 5 HOH   113 513 218 HOH   HOH D . 
Q 5 HOH   114 514 430 HOH   HOH D . 
Q 5 HOH   115 515 150 HOH   HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0267 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XSCALE      ? ? ? .        2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        3 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .        5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   89.97 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XCB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     68.853 
_cell.length_a_esd                 ? 
_cell.length_b                     69.782 
_cell.length_b_esd                 ? 
_cell.length_c                     83.669 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8XCB 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8XCB 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.23 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.91 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M Tris pH 8.5, 10% w/v PEG3350 and 0.2M Magnesium chloride' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-12-07 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.978530 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.978530 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XCB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.83 
_reflns.d_resolution_low                               83.67 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     69672 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.088 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.83 
_reflns_shell.d_res_low                                     1.87 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4316 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.8 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.43 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.42 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.09 
_refine.aniso_B[2][2]                            1.28 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.86 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               21.803 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.935 
_refine.correlation_coeff_Fo_to_Fc_free          0.908 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8XCB 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.83 
_refine.ls_d_res_low                             83.67 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     64766 
_refine.ls_number_reflns_R_free                  3558 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.52 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.21627 
_refine.ls_R_factor_R_free                       0.24540 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.21465 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.169 
_refine.pdbx_overall_ESU_R_Free                  0.148 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             4.318 
_refine.overall_SU_ML                            0.126 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.83 
_refine_hist.d_res_low                        83.67 
_refine_hist.number_atoms_solvent             468 
_refine_hist.number_atoms_total               6588 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        6076 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         44 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  0.013  6369  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.014  5809  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.322  1.670  8653  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.273  1.578  13414 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.987  5.000  796   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 30.008 20.110 364   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.887 15.000 1053  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.174 15.000 69    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.122  0.200  818   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.004  0.020  7290  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1516  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 0.981  2.250  3145  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.981  2.249  3144  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.689  3.363  3942  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.688  3.364  3943  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.074  2.381  3224  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.074  2.381  3225  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.780  3.517  4708  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.534  26.269 6745  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 3.424  26.085 6655  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.830 
_refine_ls_shell.d_res_low                        1.877 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             239 
_refine_ls_shell.number_reflns_R_work             4793 
_refine_ls_shell.percent_reflns_obs               98.05 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.300 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.311 
# 
_struct.entry_id                     8XCB 
_struct.title                        'Cocrystal structure of p53 in complex of B20' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8XCB 
_struct_keywords.text            'ANTITUMOR PROTEIN-Inhibitor Complex' 
_struct_keywords.pdbx_keywords   'ANTITUMOR PROTEIN/INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 2 ? 
I N N 2 ? 
J N N 3 ? 
K N N 4 ? 
L N N 2 ? 
M N N 3 ? 
N N N 5 ? 
O N N 5 ? 
P N N 5 ? 
Q N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    P53_HUMAN 
_struct_ref.pdbx_db_accession          P04637 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVV
RRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILT
IITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKG
;
_struct_ref.pdbx_align_begin           94 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8XCB A 1 ? 200 ? P04637 94 ? 293 ? 94 293 
2 1 8XCB B 1 ? 200 ? P04637 94 ? 293 ? 94 293 
3 1 8XCB C 1 ? 200 ? P04637 94 ? 293 ? 94 293 
4 1 8XCB D 1 ? 200 ? P04637 94 ? 293 ? 94 293 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 860   ? 
1 MORE         -7    ? 
1 'SSA (A^2)'  19300 ? 
2 'ABSA (A^2)' 980   ? 
2 MORE         -8    ? 
2 'SSA (A^2)'  19090 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E,F,N   
1 2 B,G,H,O   
2 1 C,I,J,P   
2 2 D,K,L,M,Q 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   cross-linking 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0000000000 0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000   
2 'crystal symmetry operation' 1_554 x,y,z-1 1.0000000000 0.0000000000 0.0000000000 -0.0438089840 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 -83.6689885308 
# 
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  AA1 GLN A 72  ? MET A 76  ? GLN A 165 MET A 169 5 ? 5  
HELX_P HELX_P2  AA2 CYS A 83  ? CYS A 89  ? CYS A 176 CYS A 182 1 ? 7  
HELX_P HELX_P3  AA3 CYS A 184 ? ASN A 195 ? CYS A 277 ASN A 288 1 ? 12 
HELX_P HELX_P4  AA4 GLN B 72  ? MET B 76  ? GLN B 165 MET B 169 5 ? 5  
HELX_P HELX_P5  AA5 CYS B 83  ? ARG B 88  ? CYS B 176 ARG B 181 1 ? 6  
HELX_P HELX_P6  AA6 CYS B 184 ? ASN B 195 ? CYS B 277 ASN B 288 1 ? 12 
HELX_P HELX_P7  AA7 GLN C 72  ? MET C 76  ? GLN C 165 MET C 169 5 ? 5  
HELX_P HELX_P8  AA8 CYS C 83  ? CYS C 89  ? CYS C 176 CYS C 182 1 ? 7  
HELX_P HELX_P9  AA9 CYS C 184 ? ASN C 195 ? CYS C 277 ASN C 288 1 ? 12 
HELX_P HELX_P10 AB1 GLN D 72  ? MET D 76  ? GLN D 165 MET D 169 5 ? 5  
HELX_P HELX_P11 AB2 CYS D 83  ? ARG D 88  ? CYS D 176 ARG D 181 1 ? 6  
HELX_P HELX_P12 AB3 CYS D 184 ? ASN D 195 ? CYS D 277 ASN D 288 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A MET 40  SD  A ? ? 1_555 A CYS 48 SG A ? A MET 133 A CYS 141 1_555 ? ? ? ? ? ? ? 2.118 ? ? 
metalc1  metalc ? ? A CYS 83  SG  ? ? ? 1_555 E ZN  .  ZN ? ? A CYS 176 A ZN  301 1_555 ? ? ? ? ? ? ? 2.335 ? ? 
metalc2  metalc ? ? A HIS 86  ND1 ? ? ? 1_555 E ZN  .  ZN ? ? A HIS 179 A ZN  301 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
metalc3  metalc ? ? A CYS 145 SG  ? ? ? 1_555 E ZN  .  ZN ? ? A CYS 238 A ZN  301 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
metalc4  metalc ? ? A CYS 149 SG  ? ? ? 1_555 E ZN  .  ZN ? ? A CYS 242 A ZN  301 1_555 ? ? ? ? ? ? ? 2.323 ? ? 
metalc5  metalc ? ? B CYS 83  SG  ? ? ? 1_555 H ZN  .  ZN ? ? B CYS 176 B ZN  302 1_555 ? ? ? ? ? ? ? 2.344 ? ? 
metalc6  metalc ? ? B HIS 86  ND1 ? ? ? 1_555 H ZN  .  ZN ? ? B HIS 179 B ZN  302 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
metalc7  metalc ? ? B CYS 145 SG  ? ? ? 1_555 H ZN  .  ZN ? ? B CYS 238 B ZN  302 1_555 ? ? ? ? ? ? ? 2.334 ? ? 
metalc8  metalc ? ? B CYS 149 SG  ? ? ? 1_555 H ZN  .  ZN ? ? B CYS 242 B ZN  302 1_555 ? ? ? ? ? ? ? 2.309 ? ? 
metalc9  metalc ? ? C CYS 83  SG  ? ? ? 1_555 I ZN  .  ZN ? ? C CYS 176 C ZN  301 1_555 ? ? ? ? ? ? ? 2.357 ? ? 
metalc10 metalc ? ? C HIS 86  ND1 ? ? ? 1_555 I ZN  .  ZN ? ? C HIS 179 C ZN  301 1_555 ? ? ? ? ? ? ? 1.930 ? ? 
metalc11 metalc ? ? C CYS 145 SG  ? ? ? 1_555 I ZN  .  ZN ? ? C CYS 238 C ZN  301 1_555 ? ? ? ? ? ? ? 2.338 ? ? 
metalc12 metalc ? ? C CYS 149 SG  ? ? ? 1_555 I ZN  .  ZN ? ? C CYS 242 C ZN  301 1_555 ? ? ? ? ? ? ? 2.332 ? ? 
metalc13 metalc ? ? D CYS 83  SG  ? ? ? 1_555 L ZN  .  ZN ? ? D CYS 176 D ZN  302 1_555 ? ? ? ? ? ? ? 2.359 ? ? 
metalc14 metalc ? ? D HIS 86  ND1 ? ? ? 1_555 L ZN  .  ZN ? ? D HIS 179 D ZN  302 1_555 ? ? ? ? ? ? ? 1.968 ? ? 
metalc15 metalc ? ? D CYS 145 SG  ? ? ? 1_555 L ZN  .  ZN ? ? D CYS 238 D ZN  302 1_555 ? ? ? ? ? ? ? 2.341 ? ? 
metalc16 metalc ? ? D CYS 149 SG  ? ? ? 1_555 L ZN  .  ZN ? ? D CYS 242 D ZN  302 1_555 ? ? ? ? ? ? ? 2.336 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG  ? A CYS 83  ? A CYS 176 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 86  ? A HIS 179 ? 1_555 106.7 ? 
2  SG  ? A CYS 83  ? A CYS 176 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 SG  ? A CYS 145 ? A CYS 238 ? 1_555 112.4 ? 
3  ND1 ? A HIS 86  ? A HIS 179 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 SG  ? A CYS 145 ? A CYS 238 ? 1_555 100.1 ? 
4  SG  ? A CYS 83  ? A CYS 176 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 SG  ? A CYS 149 ? A CYS 242 ? 1_555 110.6 ? 
5  ND1 ? A HIS 86  ? A HIS 179 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 SG  ? A CYS 149 ? A CYS 242 ? 1_555 101.4 ? 
6  SG  ? A CYS 145 ? A CYS 238 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 SG  ? A CYS 149 ? A CYS 242 ? 1_555 123.0 ? 
7  SG  ? B CYS 83  ? B CYS 176 ? 1_555 ZN ? H ZN . ? B ZN 302 ? 1_555 ND1 ? B HIS 86  ? B HIS 179 ? 1_555 105.7 ? 
8  SG  ? B CYS 83  ? B CYS 176 ? 1_555 ZN ? H ZN . ? B ZN 302 ? 1_555 SG  ? B CYS 145 ? B CYS 238 ? 1_555 113.1 ? 
9  ND1 ? B HIS 86  ? B HIS 179 ? 1_555 ZN ? H ZN . ? B ZN 302 ? 1_555 SG  ? B CYS 145 ? B CYS 238 ? 1_555 117.7 ? 
10 SG  ? B CYS 83  ? B CYS 176 ? 1_555 ZN ? H ZN . ? B ZN 302 ? 1_555 SG  ? B CYS 149 ? B CYS 242 ? 1_555 113.3 ? 
11 ND1 ? B HIS 86  ? B HIS 179 ? 1_555 ZN ? H ZN . ? B ZN 302 ? 1_555 SG  ? B CYS 149 ? B CYS 242 ? 1_555 102.1 ? 
12 SG  ? B CYS 145 ? B CYS 238 ? 1_555 ZN ? H ZN . ? B ZN 302 ? 1_555 SG  ? B CYS 149 ? B CYS 242 ? 1_555 104.5 ? 
13 SG  ? C CYS 83  ? C CYS 176 ? 1_555 ZN ? I ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 86  ? C HIS 179 ? 1_555 108.2 ? 
14 SG  ? C CYS 83  ? C CYS 176 ? 1_555 ZN ? I ZN . ? C ZN 301 ? 1_555 SG  ? C CYS 145 ? C CYS 238 ? 1_555 111.2 ? 
15 ND1 ? C HIS 86  ? C HIS 179 ? 1_555 ZN ? I ZN . ? C ZN 301 ? 1_555 SG  ? C CYS 145 ? C CYS 238 ? 1_555 104.9 ? 
16 SG  ? C CYS 83  ? C CYS 176 ? 1_555 ZN ? I ZN . ? C ZN 301 ? 1_555 SG  ? C CYS 149 ? C CYS 242 ? 1_555 114.9 ? 
17 ND1 ? C HIS 86  ? C HIS 179 ? 1_555 ZN ? I ZN . ? C ZN 301 ? 1_555 SG  ? C CYS 149 ? C CYS 242 ? 1_555 98.4  ? 
18 SG  ? C CYS 145 ? C CYS 238 ? 1_555 ZN ? I ZN . ? C ZN 301 ? 1_555 SG  ? C CYS 149 ? C CYS 242 ? 1_555 117.4 ? 
19 SG  ? D CYS 83  ? D CYS 176 ? 1_555 ZN ? L ZN . ? D ZN 302 ? 1_555 ND1 ? D HIS 86  ? D HIS 179 ? 1_555 107.6 ? 
20 SG  ? D CYS 83  ? D CYS 176 ? 1_555 ZN ? L ZN . ? D ZN 302 ? 1_555 SG  ? D CYS 145 ? D CYS 238 ? 1_555 112.1 ? 
21 ND1 ? D HIS 86  ? D HIS 179 ? 1_555 ZN ? L ZN . ? D ZN 302 ? 1_555 SG  ? D CYS 145 ? D CYS 238 ? 1_555 118.3 ? 
22 SG  ? D CYS 83  ? D CYS 176 ? 1_555 ZN ? L ZN . ? D ZN 302 ? 1_555 SG  ? D CYS 149 ? D CYS 242 ? 1_555 110.4 ? 
23 ND1 ? D HIS 86  ? D HIS 179 ? 1_555 ZN ? L ZN . ? D ZN 302 ? 1_555 SG  ? D CYS 149 ? D CYS 242 ? 1_555 104.3 ? 
24 SG  ? D CYS 145 ? D CYS 238 ? 1_555 ZN ? L ZN . ? D ZN 302 ? 1_555 SG  ? D CYS 149 ? D CYS 242 ? 1_555 103.6 ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      MET 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       40 
_pdbx_modification_feature.label_alt_id                       A 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      48 
_pdbx_modification_feature.modified_residue_label_alt_id      A 
_pdbx_modification_feature.auth_comp_id                       MET 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        133 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       141 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SD 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 7 ? 
AA3 ? 4 ? 
AA4 ? 7 ? 
AA5 ? 4 ? 
AA6 ? 7 ? 
AA7 ? 4 ? 
AA8 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? parallel      
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA8 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 17  ? GLY A 19  ? ARG A 110 GLY A 112 
AA1 2 CYS A 48  ? TRP A 53  ? CYS A 141 TRP A 146 
AA1 3 THR A 137 ? TYR A 143 ? THR A 230 TYR A 236 
AA1 4 ILE A 102 ? VAL A 104 ? ILE A 195 VAL A 197 
AA2 1 CYS A 31  ? SER A 34  ? CYS A 124 SER A 127 
AA2 2 LYS A 39  ? CYS A 42  ? LYS A 132 CYS A 135 
AA2 3 LEU A 171 ? VAL A 181 ? LEU A 264 VAL A 274 
AA2 4 ILE A 158 ? GLU A 165 ? ILE A 251 GLU A 258 
AA2 5 ARG A 63  ? TYR A 70  ? ARG A 156 TYR A 163 
AA2 6 HIS A 121 ? PRO A 126 ? HIS A 214 PRO A 219 
AA2 7 GLU A 111 ? ASP A 114 ? GLU A 204 ASP A 207 
AA3 1 ARG B 17  ? GLY B 19  ? ARG B 110 GLY B 112 
AA3 2 CYS B 48  ? TRP B 53  ? CYS B 141 TRP B 146 
AA3 3 THR B 137 ? TYR B 143 ? THR B 230 TYR B 236 
AA3 4 ILE B 102 ? VAL B 104 ? ILE B 195 VAL B 197 
AA4 1 CYS B 31  ? SER B 34  ? CYS B 124 SER B 127 
AA4 2 LYS B 39  ? CYS B 42  ? LYS B 132 CYS B 135 
AA4 3 LEU B 171 ? VAL B 181 ? LEU B 264 VAL B 274 
AA4 4 ILE B 158 ? GLU B 165 ? ILE B 251 GLU B 258 
AA4 5 ARG B 63  ? TYR B 70  ? ARG B 156 TYR B 163 
AA4 6 HIS B 121 ? PRO B 126 ? HIS B 214 PRO B 219 
AA4 7 GLU B 111 ? ASP B 114 ? GLU B 204 ASP B 207 
AA5 1 ARG C 17  ? GLY C 19  ? ARG C 110 GLY C 112 
AA5 2 CYS C 48  ? TRP C 53  ? CYS C 141 TRP C 146 
AA5 3 THR C 137 ? TYR C 143 ? THR C 230 TYR C 236 
AA5 4 ILE C 102 ? GLU C 105 ? ILE C 195 GLU C 198 
AA6 1 CYS C 31  ? SER C 34  ? CYS C 124 SER C 127 
AA6 2 LYS C 39  ? CYS C 42  ? LYS C 132 CYS C 135 
AA6 3 LEU C 171 ? VAL C 181 ? LEU C 264 VAL C 274 
AA6 4 ILE C 158 ? GLU C 165 ? ILE C 251 GLU C 258 
AA6 5 ARG C 63  ? TYR C 70  ? ARG C 156 TYR C 163 
AA6 6 HIS C 121 ? PRO C 126 ? HIS C 214 PRO C 219 
AA6 7 GLU C 111 ? ASP C 114 ? GLU C 204 ASP C 207 
AA7 1 ARG D 17  ? GLY D 19  ? ARG D 110 GLY D 112 
AA7 2 CYS D 48  ? TRP D 53  ? CYS D 141 TRP D 146 
AA7 3 THR D 137 ? TYR D 143 ? THR D 230 TYR D 236 
AA7 4 ILE D 102 ? VAL D 104 ? ILE D 195 VAL D 197 
AA8 1 CYS D 31  ? SER D 34  ? CYS D 124 SER D 127 
AA8 2 LYS D 39  ? CYS D 42  ? LYS D 132 CYS D 135 
AA8 3 LEU D 171 ? VAL D 181 ? LEU D 264 VAL D 274 
AA8 4 ILE D 158 ? GLU D 165 ? ILE D 251 GLU D 258 
AA8 5 ARG D 63  ? TYR D 70  ? ARG D 156 TYR D 163 
AA8 6 HIS D 121 ? PRO D 126 ? HIS D 214 PRO D 219 
AA8 7 GLU D 111 ? ASP D 114 ? GLU D 204 ASP D 207 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ARG A 17  ? N ARG A 110 O TRP A 53  ? O TRP A 146 
AA1 2 3 N LEU A 52  ? N LEU A 145 O THR A 137 ? O THR A 230 
AA1 3 4 O ASN A 142 ? O ASN A 235 N ARG A 103 ? N ARG A 196 
AA2 1 2 N SER A 34  ? N SER A 127 O LYS A 39  ? O LYS A 132 
AA2 2 3 N MET A 40  ? N MET A 133 O GLU A 178 ? O GLU A 271 
AA2 3 4 O LEU A 172 ? O LEU A 265 N LEU A 164 ? N LEU A 257 
AA2 4 5 O GLU A 165 ? O GLU A 258 N ARG A 63  ? N ARG A 156 
AA2 5 6 N VAL A 64  ? N VAL A 157 O VAL A 125 ? O VAL A 218 
AA2 6 7 O VAL A 124 ? O VAL A 217 N GLU A 111 ? N GLU A 204 
AA3 1 2 N ARG B 17  ? N ARG B 110 O TRP B 53  ? O TRP B 146 
AA3 2 3 N LEU B 52  ? N LEU B 145 O THR B 137 ? O THR B 230 
AA3 3 4 O ASN B 142 ? O ASN B 235 N ARG B 103 ? N ARG B 196 
AA4 1 2 N THR B 32  ? N THR B 125 O PHE B 41  ? O PHE B 134 
AA4 2 3 N MET B 40  ? N MET B 133 O GLU B 178 ? O GLU B 271 
AA4 3 4 O LEU B 172 ? O LEU B 265 N LEU B 164 ? N LEU B 257 
AA4 4 5 O GLU B 165 ? O GLU B 258 N ARG B 63  ? N ARG B 156 
AA4 5 6 N ALA B 66  ? N ALA B 159 O VAL B 123 ? O VAL B 216 
AA4 6 7 O VAL B 124 ? O VAL B 217 N GLU B 111 ? N GLU B 204 
AA5 1 2 N GLY C 19  ? N GLY C 112 O GLN C 51  ? O GLN C 144 
AA5 2 3 N LEU C 52  ? N LEU C 145 O THR C 137 ? O THR C 230 
AA5 3 4 O HIS C 140 ? O HIS C 233 N GLU C 105 ? N GLU C 198 
AA6 1 2 N SER C 34  ? N SER C 127 O LYS C 39  ? O LYS C 132 
AA6 2 3 N MET C 40  ? N MET C 133 O GLU C 178 ? O GLU C 271 
AA6 3 4 O LEU C 172 ? O LEU C 265 N LEU C 164 ? N LEU C 257 
AA6 4 5 O ILE C 161 ? O ILE C 254 N MET C 67  ? N MET C 160 
AA6 5 6 N VAL C 64  ? N VAL C 157 O VAL C 125 ? O VAL C 218 
AA6 6 7 O VAL C 124 ? O VAL C 217 N GLU C 111 ? N GLU C 204 
AA7 1 2 N GLY D 19  ? N GLY D 112 O GLN D 51  ? O GLN D 144 
AA7 2 3 N LEU D 52  ? N LEU D 145 O THR D 137 ? O THR D 230 
AA7 3 4 O ASN D 142 ? O ASN D 235 N ARG D 103 ? N ARG D 196 
AA8 1 2 N SER D 34  ? N SER D 127 O LYS D 39  ? O LYS D 132 
AA8 2 3 N MET D 40  ? N MET D 133 O GLU D 178 ? O GLU D 271 
AA8 3 4 O LEU D 172 ? O LEU D 265 N LEU D 164 ? N LEU D 257 
AA8 4 5 O GLU D 165 ? O GLU D 258 N ARG D 63  ? N ARG D 156 
AA8 5 6 N VAL D 64  ? N VAL D 157 O VAL D 125 ? O VAL D 218 
AA8 6 7 O VAL D 124 ? O VAL D 217 N GLU D 111 ? N GLU D 204 
# 
_pdbx_entry_details.entry_id                   8XCB 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 SG B CYS 182 ? ? C4 B A1LUZ 301 ? ? 1.64 
2 1 SG D CYS 182 ? ? C4 D A1LUZ 301 ? ? 1.64 
3 1 O  A HOH 418 ? ? O  A HOH   470 ? ? 1.86 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 248 ? ? 80.34   0.17   
2 1 LEU C 188 ? ? -125.06 -50.01 
3 1 ARG C 248 ? ? 80.09   -1.06  
4 1 LEU D 188 ? ? -120.93 -50.28 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? B HOH 525 ? 6.95 . 
2 1 O ? D HOH 515 ? 7.11 . 
# 
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 SER 94  ? A SER 1   
2  1 Y 1 A SER 95  ? A SER 2   
3  1 Y 1 A SER 96  ? A SER 3   
4  1 Y 1 A ARG 290 ? A ARG 197 
5  1 Y 1 A LYS 291 ? A LYS 198 
6  1 Y 1 A LYS 292 ? A LYS 199 
7  1 Y 1 A GLY 293 ? A GLY 200 
8  1 Y 1 B SER 94  ? B SER 1   
9  1 Y 1 B SER 95  ? B SER 2   
10 1 Y 1 B ARG 290 ? B ARG 197 
11 1 Y 1 B LYS 291 ? B LYS 198 
12 1 Y 1 B LYS 292 ? B LYS 199 
13 1 Y 1 B GLY 293 ? B GLY 200 
14 1 Y 1 C SER 94  ? C SER 1   
15 1 Y 1 C SER 95  ? C SER 2   
16 1 Y 1 C VAL 225 ? C VAL 132 
17 1 Y 1 C GLY 226 ? C GLY 133 
18 1 Y 1 C ARG 290 ? C ARG 197 
19 1 Y 1 C LYS 291 ? C LYS 198 
20 1 Y 1 C LYS 292 ? C LYS 199 
21 1 Y 1 C GLY 293 ? C GLY 200 
22 1 Y 1 D SER 94  ? D SER 1   
23 1 Y 1 D SER 95  ? D SER 2   
24 1 Y 1 D ARG 290 ? D ARG 197 
25 1 Y 1 D LYS 291 ? D LYS 198 
26 1 Y 1 D LYS 292 ? D LYS 199 
27 1 Y 1 D GLY 293 ? D GLY 200 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1LUZ C4   C  N N 1   
A1LUZ C5   C  N N 2   
A1LUZ C1   C  N N 3   
A1LUZ N    N  N N 4   
A1LUZ C2   C  N N 5   
A1LUZ S    S  N N 6   
A1LUZ C3   C  N N 7   
A1LUZ O1   O  N N 8   
A1LUZ O2   O  N N 9   
A1LUZ O3   O  N N 10  
A1LUZ O4   O  N N 11  
A1LUZ H1   H  N N 12  
A1LUZ H3   H  N N 13  
A1LUZ H5   H  N N 14  
ALA   N    N  N N 15  
ALA   CA   C  N S 16  
ALA   C    C  N N 17  
ALA   O    O  N N 18  
ALA   CB   C  N N 19  
ALA   OXT  O  N N 20  
ALA   H    H  N N 21  
ALA   H2   H  N N 22  
ALA   HA   H  N N 23  
ALA   HB1  H  N N 24  
ALA   HB2  H  N N 25  
ALA   HB3  H  N N 26  
ALA   HXT  H  N N 27  
ARG   N    N  N N 28  
ARG   CA   C  N S 29  
ARG   C    C  N N 30  
ARG   O    O  N N 31  
ARG   CB   C  N N 32  
ARG   CG   C  N N 33  
ARG   CD   C  N N 34  
ARG   NE   N  N N 35  
ARG   CZ   C  N N 36  
ARG   NH1  N  N N 37  
ARG   NH2  N  N N 38  
ARG   OXT  O  N N 39  
ARG   H    H  N N 40  
ARG   H2   H  N N 41  
ARG   HA   H  N N 42  
ARG   HB2  H  N N 43  
ARG   HB3  H  N N 44  
ARG   HG2  H  N N 45  
ARG   HG3  H  N N 46  
ARG   HD2  H  N N 47  
ARG   HD3  H  N N 48  
ARG   HE   H  N N 49  
ARG   HH11 H  N N 50  
ARG   HH12 H  N N 51  
ARG   HH21 H  N N 52  
ARG   HH22 H  N N 53  
ARG   HXT  H  N N 54  
ASN   N    N  N N 55  
ASN   CA   C  N S 56  
ASN   C    C  N N 57  
ASN   O    O  N N 58  
ASN   CB   C  N N 59  
ASN   CG   C  N N 60  
ASN   OD1  O  N N 61  
ASN   ND2  N  N N 62  
ASN   OXT  O  N N 63  
ASN   H    H  N N 64  
ASN   H2   H  N N 65  
ASN   HA   H  N N 66  
ASN   HB2  H  N N 67  
ASN   HB3  H  N N 68  
ASN   HD21 H  N N 69  
ASN   HD22 H  N N 70  
ASN   HXT  H  N N 71  
ASP   N    N  N N 72  
ASP   CA   C  N S 73  
ASP   C    C  N N 74  
ASP   O    O  N N 75  
ASP   CB   C  N N 76  
ASP   CG   C  N N 77  
ASP   OD1  O  N N 78  
ASP   OD2  O  N N 79  
ASP   OXT  O  N N 80  
ASP   H    H  N N 81  
ASP   H2   H  N N 82  
ASP   HA   H  N N 83  
ASP   HB2  H  N N 84  
ASP   HB3  H  N N 85  
ASP   HD2  H  N N 86  
ASP   HXT  H  N N 87  
CYS   N    N  N N 88  
CYS   CA   C  N R 89  
CYS   C    C  N N 90  
CYS   O    O  N N 91  
CYS   CB   C  N N 92  
CYS   SG   S  N N 93  
CYS   OXT  O  N N 94  
CYS   H    H  N N 95  
CYS   H2   H  N N 96  
CYS   HA   H  N N 97  
CYS   HB2  H  N N 98  
CYS   HB3  H  N N 99  
CYS   HG   H  N N 100 
CYS   HXT  H  N N 101 
GLN   N    N  N N 102 
GLN   CA   C  N S 103 
GLN   C    C  N N 104 
GLN   O    O  N N 105 
GLN   CB   C  N N 106 
GLN   CG   C  N N 107 
GLN   CD   C  N N 108 
GLN   OE1  O  N N 109 
GLN   NE2  N  N N 110 
GLN   OXT  O  N N 111 
GLN   H    H  N N 112 
GLN   H2   H  N N 113 
GLN   HA   H  N N 114 
GLN   HB2  H  N N 115 
GLN   HB3  H  N N 116 
GLN   HG2  H  N N 117 
GLN   HG3  H  N N 118 
GLN   HE21 H  N N 119 
GLN   HE22 H  N N 120 
GLN   HXT  H  N N 121 
GLU   N    N  N N 122 
GLU   CA   C  N S 123 
GLU   C    C  N N 124 
GLU   O    O  N N 125 
GLU   CB   C  N N 126 
GLU   CG   C  N N 127 
GLU   CD   C  N N 128 
GLU   OE1  O  N N 129 
GLU   OE2  O  N N 130 
GLU   OXT  O  N N 131 
GLU   H    H  N N 132 
GLU   H2   H  N N 133 
GLU   HA   H  N N 134 
GLU   HB2  H  N N 135 
GLU   HB3  H  N N 136 
GLU   HG2  H  N N 137 
GLU   HG3  H  N N 138 
GLU   HE2  H  N N 139 
GLU   HXT  H  N N 140 
GLY   N    N  N N 141 
GLY   CA   C  N N 142 
GLY   C    C  N N 143 
GLY   O    O  N N 144 
GLY   OXT  O  N N 145 
GLY   H    H  N N 146 
GLY   H2   H  N N 147 
GLY   HA2  H  N N 148 
GLY   HA3  H  N N 149 
GLY   HXT  H  N N 150 
GOL   C1   C  N N 151 
GOL   O1   O  N N 152 
GOL   C2   C  N N 153 
GOL   O2   O  N N 154 
GOL   C3   C  N N 155 
GOL   O3   O  N N 156 
GOL   H11  H  N N 157 
GOL   H12  H  N N 158 
GOL   HO1  H  N N 159 
GOL   H2   H  N N 160 
GOL   HO2  H  N N 161 
GOL   H31  H  N N 162 
GOL   H32  H  N N 163 
GOL   HO3  H  N N 164 
HIS   N    N  N N 165 
HIS   CA   C  N S 166 
HIS   C    C  N N 167 
HIS   O    O  N N 168 
HIS   CB   C  N N 169 
HIS   CG   C  Y N 170 
HIS   ND1  N  Y N 171 
HIS   CD2  C  Y N 172 
HIS   CE1  C  Y N 173 
HIS   NE2  N  Y N 174 
HIS   OXT  O  N N 175 
HIS   H    H  N N 176 
HIS   H2   H  N N 177 
HIS   HA   H  N N 178 
HIS   HB2  H  N N 179 
HIS   HB3  H  N N 180 
HIS   HD1  H  N N 181 
HIS   HD2  H  N N 182 
HIS   HE1  H  N N 183 
HIS   HE2  H  N N 184 
HIS   HXT  H  N N 185 
HOH   O    O  N N 186 
HOH   H1   H  N N 187 
HOH   H2   H  N N 188 
ILE   N    N  N N 189 
ILE   CA   C  N S 190 
ILE   C    C  N N 191 
ILE   O    O  N N 192 
ILE   CB   C  N S 193 
ILE   CG1  C  N N 194 
ILE   CG2  C  N N 195 
ILE   CD1  C  N N 196 
ILE   OXT  O  N N 197 
ILE   H    H  N N 198 
ILE   H2   H  N N 199 
ILE   HA   H  N N 200 
ILE   HB   H  N N 201 
ILE   HG12 H  N N 202 
ILE   HG13 H  N N 203 
ILE   HG21 H  N N 204 
ILE   HG22 H  N N 205 
ILE   HG23 H  N N 206 
ILE   HD11 H  N N 207 
ILE   HD12 H  N N 208 
ILE   HD13 H  N N 209 
ILE   HXT  H  N N 210 
LEU   N    N  N N 211 
LEU   CA   C  N S 212 
LEU   C    C  N N 213 
LEU   O    O  N N 214 
LEU   CB   C  N N 215 
LEU   CG   C  N N 216 
LEU   CD1  C  N N 217 
LEU   CD2  C  N N 218 
LEU   OXT  O  N N 219 
LEU   H    H  N N 220 
LEU   H2   H  N N 221 
LEU   HA   H  N N 222 
LEU   HB2  H  N N 223 
LEU   HB3  H  N N 224 
LEU   HG   H  N N 225 
LEU   HD11 H  N N 226 
LEU   HD12 H  N N 227 
LEU   HD13 H  N N 228 
LEU   HD21 H  N N 229 
LEU   HD22 H  N N 230 
LEU   HD23 H  N N 231 
LEU   HXT  H  N N 232 
LYS   N    N  N N 233 
LYS   CA   C  N S 234 
LYS   C    C  N N 235 
LYS   O    O  N N 236 
LYS   CB   C  N N 237 
LYS   CG   C  N N 238 
LYS   CD   C  N N 239 
LYS   CE   C  N N 240 
LYS   NZ   N  N N 241 
LYS   OXT  O  N N 242 
LYS   H    H  N N 243 
LYS   H2   H  N N 244 
LYS   HA   H  N N 245 
LYS   HB2  H  N N 246 
LYS   HB3  H  N N 247 
LYS   HG2  H  N N 248 
LYS   HG3  H  N N 249 
LYS   HD2  H  N N 250 
LYS   HD3  H  N N 251 
LYS   HE2  H  N N 252 
LYS   HE3  H  N N 253 
LYS   HZ1  H  N N 254 
LYS   HZ2  H  N N 255 
LYS   HZ3  H  N N 256 
LYS   HXT  H  N N 257 
MET   N    N  N N 258 
MET   CA   C  N S 259 
MET   C    C  N N 260 
MET   O    O  N N 261 
MET   CB   C  N N 262 
MET   CG   C  N N 263 
MET   SD   S  N N 264 
MET   CE   C  N N 265 
MET   OXT  O  N N 266 
MET   H    H  N N 267 
MET   H2   H  N N 268 
MET   HA   H  N N 269 
MET   HB2  H  N N 270 
MET   HB3  H  N N 271 
MET   HG2  H  N N 272 
MET   HG3  H  N N 273 
MET   HE1  H  N N 274 
MET   HE2  H  N N 275 
MET   HE3  H  N N 276 
MET   HXT  H  N N 277 
PHE   N    N  N N 278 
PHE   CA   C  N S 279 
PHE   C    C  N N 280 
PHE   O    O  N N 281 
PHE   CB   C  N N 282 
PHE   CG   C  Y N 283 
PHE   CD1  C  Y N 284 
PHE   CD2  C  Y N 285 
PHE   CE1  C  Y N 286 
PHE   CE2  C  Y N 287 
PHE   CZ   C  Y N 288 
PHE   OXT  O  N N 289 
PHE   H    H  N N 290 
PHE   H2   H  N N 291 
PHE   HA   H  N N 292 
PHE   HB2  H  N N 293 
PHE   HB3  H  N N 294 
PHE   HD1  H  N N 295 
PHE   HD2  H  N N 296 
PHE   HE1  H  N N 297 
PHE   HE2  H  N N 298 
PHE   HZ   H  N N 299 
PHE   HXT  H  N N 300 
PRO   N    N  N N 301 
PRO   CA   C  N S 302 
PRO   C    C  N N 303 
PRO   O    O  N N 304 
PRO   CB   C  N N 305 
PRO   CG   C  N N 306 
PRO   CD   C  N N 307 
PRO   OXT  O  N N 308 
PRO   H    H  N N 309 
PRO   HA   H  N N 310 
PRO   HB2  H  N N 311 
PRO   HB3  H  N N 312 
PRO   HG2  H  N N 313 
PRO   HG3  H  N N 314 
PRO   HD2  H  N N 315 
PRO   HD3  H  N N 316 
PRO   HXT  H  N N 317 
SER   N    N  N N 318 
SER   CA   C  N S 319 
SER   C    C  N N 320 
SER   O    O  N N 321 
SER   CB   C  N N 322 
SER   OG   O  N N 323 
SER   OXT  O  N N 324 
SER   H    H  N N 325 
SER   H2   H  N N 326 
SER   HA   H  N N 327 
SER   HB2  H  N N 328 
SER   HB3  H  N N 329 
SER   HG   H  N N 330 
SER   HXT  H  N N 331 
THR   N    N  N N 332 
THR   CA   C  N S 333 
THR   C    C  N N 334 
THR   O    O  N N 335 
THR   CB   C  N R 336 
THR   OG1  O  N N 337 
THR   CG2  C  N N 338 
THR   OXT  O  N N 339 
THR   H    H  N N 340 
THR   H2   H  N N 341 
THR   HA   H  N N 342 
THR   HB   H  N N 343 
THR   HG1  H  N N 344 
THR   HG21 H  N N 345 
THR   HG22 H  N N 346 
THR   HG23 H  N N 347 
THR   HXT  H  N N 348 
TRP   N    N  N N 349 
TRP   CA   C  N S 350 
TRP   C    C  N N 351 
TRP   O    O  N N 352 
TRP   CB   C  N N 353 
TRP   CG   C  Y N 354 
TRP   CD1  C  Y N 355 
TRP   CD2  C  Y N 356 
TRP   NE1  N  Y N 357 
TRP   CE2  C  Y N 358 
TRP   CE3  C  Y N 359 
TRP   CZ2  C  Y N 360 
TRP   CZ3  C  Y N 361 
TRP   CH2  C  Y N 362 
TRP   OXT  O  N N 363 
TRP   H    H  N N 364 
TRP   H2   H  N N 365 
TRP   HA   H  N N 366 
TRP   HB2  H  N N 367 
TRP   HB3  H  N N 368 
TRP   HD1  H  N N 369 
TRP   HE1  H  N N 370 
TRP   HE3  H  N N 371 
TRP   HZ2  H  N N 372 
TRP   HZ3  H  N N 373 
TRP   HH2  H  N N 374 
TRP   HXT  H  N N 375 
TYR   N    N  N N 376 
TYR   CA   C  N S 377 
TYR   C    C  N N 378 
TYR   O    O  N N 379 
TYR   CB   C  N N 380 
TYR   CG   C  Y N 381 
TYR   CD1  C  Y N 382 
TYR   CD2  C  Y N 383 
TYR   CE1  C  Y N 384 
TYR   CE2  C  Y N 385 
TYR   CZ   C  Y N 386 
TYR   OH   O  N N 387 
TYR   OXT  O  N N 388 
TYR   H    H  N N 389 
TYR   H2   H  N N 390 
TYR   HA   H  N N 391 
TYR   HB2  H  N N 392 
TYR   HB3  H  N N 393 
TYR   HD1  H  N N 394 
TYR   HD2  H  N N 395 
TYR   HE1  H  N N 396 
TYR   HE2  H  N N 397 
TYR   HH   H  N N 398 
TYR   HXT  H  N N 399 
VAL   N    N  N N 400 
VAL   CA   C  N S 401 
VAL   C    C  N N 402 
VAL   O    O  N N 403 
VAL   CB   C  N N 404 
VAL   CG1  C  N N 405 
VAL   CG2  C  N N 406 
VAL   OXT  O  N N 407 
VAL   H    H  N N 408 
VAL   H2   H  N N 409 
VAL   HA   H  N N 410 
VAL   HB   H  N N 411 
VAL   HG11 H  N N 412 
VAL   HG12 H  N N 413 
VAL   HG13 H  N N 414 
VAL   HG21 H  N N 415 
VAL   HG22 H  N N 416 
VAL   HG23 H  N N 417 
VAL   HXT  H  N N 418 
ZN    ZN   ZN N N 419 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1LUZ O3  C5   doub N N 1   
A1LUZ C5  O2   sing N N 2   
A1LUZ C5  C4   sing N N 3   
A1LUZ O1  C1   doub N N 4   
A1LUZ C4  C3   doub N Z 5   
A1LUZ C1  C3   sing N N 6   
A1LUZ C1  N    sing N N 7   
A1LUZ C3  S    sing N N 8   
A1LUZ N   C2   sing N N 9   
A1LUZ S   C2   sing N N 10  
A1LUZ C2  O4   doub N N 11  
A1LUZ C4  H1   sing N N 12  
A1LUZ N   H3   sing N N 13  
A1LUZ O2  H5   sing N N 14  
ALA   N   CA   sing N N 15  
ALA   N   H    sing N N 16  
ALA   N   H2   sing N N 17  
ALA   CA  C    sing N N 18  
ALA   CA  CB   sing N N 19  
ALA   CA  HA   sing N N 20  
ALA   C   O    doub N N 21  
ALA   C   OXT  sing N N 22  
ALA   CB  HB1  sing N N 23  
ALA   CB  HB2  sing N N 24  
ALA   CB  HB3  sing N N 25  
ALA   OXT HXT  sing N N 26  
ARG   N   CA   sing N N 27  
ARG   N   H    sing N N 28  
ARG   N   H2   sing N N 29  
ARG   CA  C    sing N N 30  
ARG   CA  CB   sing N N 31  
ARG   CA  HA   sing N N 32  
ARG   C   O    doub N N 33  
ARG   C   OXT  sing N N 34  
ARG   CB  CG   sing N N 35  
ARG   CB  HB2  sing N N 36  
ARG   CB  HB3  sing N N 37  
ARG   CG  CD   sing N N 38  
ARG   CG  HG2  sing N N 39  
ARG   CG  HG3  sing N N 40  
ARG   CD  NE   sing N N 41  
ARG   CD  HD2  sing N N 42  
ARG   CD  HD3  sing N N 43  
ARG   NE  CZ   sing N N 44  
ARG   NE  HE   sing N N 45  
ARG   CZ  NH1  sing N N 46  
ARG   CZ  NH2  doub N N 47  
ARG   NH1 HH11 sing N N 48  
ARG   NH1 HH12 sing N N 49  
ARG   NH2 HH21 sing N N 50  
ARG   NH2 HH22 sing N N 51  
ARG   OXT HXT  sing N N 52  
ASN   N   CA   sing N N 53  
ASN   N   H    sing N N 54  
ASN   N   H2   sing N N 55  
ASN   CA  C    sing N N 56  
ASN   CA  CB   sing N N 57  
ASN   CA  HA   sing N N 58  
ASN   C   O    doub N N 59  
ASN   C   OXT  sing N N 60  
ASN   CB  CG   sing N N 61  
ASN   CB  HB2  sing N N 62  
ASN   CB  HB3  sing N N 63  
ASN   CG  OD1  doub N N 64  
ASN   CG  ND2  sing N N 65  
ASN   ND2 HD21 sing N N 66  
ASN   ND2 HD22 sing N N 67  
ASN   OXT HXT  sing N N 68  
ASP   N   CA   sing N N 69  
ASP   N   H    sing N N 70  
ASP   N   H2   sing N N 71  
ASP   CA  C    sing N N 72  
ASP   CA  CB   sing N N 73  
ASP   CA  HA   sing N N 74  
ASP   C   O    doub N N 75  
ASP   C   OXT  sing N N 76  
ASP   CB  CG   sing N N 77  
ASP   CB  HB2  sing N N 78  
ASP   CB  HB3  sing N N 79  
ASP   CG  OD1  doub N N 80  
ASP   CG  OD2  sing N N 81  
ASP   OD2 HD2  sing N N 82  
ASP   OXT HXT  sing N N 83  
CYS   N   CA   sing N N 84  
CYS   N   H    sing N N 85  
CYS   N   H2   sing N N 86  
CYS   CA  C    sing N N 87  
CYS   CA  CB   sing N N 88  
CYS   CA  HA   sing N N 89  
CYS   C   O    doub N N 90  
CYS   C   OXT  sing N N 91  
CYS   CB  SG   sing N N 92  
CYS   CB  HB2  sing N N 93  
CYS   CB  HB3  sing N N 94  
CYS   SG  HG   sing N N 95  
CYS   OXT HXT  sing N N 96  
GLN   N   CA   sing N N 97  
GLN   N   H    sing N N 98  
GLN   N   H2   sing N N 99  
GLN   CA  C    sing N N 100 
GLN   CA  CB   sing N N 101 
GLN   CA  HA   sing N N 102 
GLN   C   O    doub N N 103 
GLN   C   OXT  sing N N 104 
GLN   CB  CG   sing N N 105 
GLN   CB  HB2  sing N N 106 
GLN   CB  HB3  sing N N 107 
GLN   CG  CD   sing N N 108 
GLN   CG  HG2  sing N N 109 
GLN   CG  HG3  sing N N 110 
GLN   CD  OE1  doub N N 111 
GLN   CD  NE2  sing N N 112 
GLN   NE2 HE21 sing N N 113 
GLN   NE2 HE22 sing N N 114 
GLN   OXT HXT  sing N N 115 
GLU   N   CA   sing N N 116 
GLU   N   H    sing N N 117 
GLU   N   H2   sing N N 118 
GLU   CA  C    sing N N 119 
GLU   CA  CB   sing N N 120 
GLU   CA  HA   sing N N 121 
GLU   C   O    doub N N 122 
GLU   C   OXT  sing N N 123 
GLU   CB  CG   sing N N 124 
GLU   CB  HB2  sing N N 125 
GLU   CB  HB3  sing N N 126 
GLU   CG  CD   sing N N 127 
GLU   CG  HG2  sing N N 128 
GLU   CG  HG3  sing N N 129 
GLU   CD  OE1  doub N N 130 
GLU   CD  OE2  sing N N 131 
GLU   OE2 HE2  sing N N 132 
GLU   OXT HXT  sing N N 133 
GLY   N   CA   sing N N 134 
GLY   N   H    sing N N 135 
GLY   N   H2   sing N N 136 
GLY   CA  C    sing N N 137 
GLY   CA  HA2  sing N N 138 
GLY   CA  HA3  sing N N 139 
GLY   C   O    doub N N 140 
GLY   C   OXT  sing N N 141 
GLY   OXT HXT  sing N N 142 
GOL   C1  O1   sing N N 143 
GOL   C1  C2   sing N N 144 
GOL   C1  H11  sing N N 145 
GOL   C1  H12  sing N N 146 
GOL   O1  HO1  sing N N 147 
GOL   C2  O2   sing N N 148 
GOL   C2  C3   sing N N 149 
GOL   C2  H2   sing N N 150 
GOL   O2  HO2  sing N N 151 
GOL   C3  O3   sing N N 152 
GOL   C3  H31  sing N N 153 
GOL   C3  H32  sing N N 154 
GOL   O3  HO3  sing N N 155 
HIS   N   CA   sing N N 156 
HIS   N   H    sing N N 157 
HIS   N   H2   sing N N 158 
HIS   CA  C    sing N N 159 
HIS   CA  CB   sing N N 160 
HIS   CA  HA   sing N N 161 
HIS   C   O    doub N N 162 
HIS   C   OXT  sing N N 163 
HIS   CB  CG   sing N N 164 
HIS   CB  HB2  sing N N 165 
HIS   CB  HB3  sing N N 166 
HIS   CG  ND1  sing Y N 167 
HIS   CG  CD2  doub Y N 168 
HIS   ND1 CE1  doub Y N 169 
HIS   ND1 HD1  sing N N 170 
HIS   CD2 NE2  sing Y N 171 
HIS   CD2 HD2  sing N N 172 
HIS   CE1 NE2  sing Y N 173 
HIS   CE1 HE1  sing N N 174 
HIS   NE2 HE2  sing N N 175 
HIS   OXT HXT  sing N N 176 
HOH   O   H1   sing N N 177 
HOH   O   H2   sing N N 178 
ILE   N   CA   sing N N 179 
ILE   N   H    sing N N 180 
ILE   N   H2   sing N N 181 
ILE   CA  C    sing N N 182 
ILE   CA  CB   sing N N 183 
ILE   CA  HA   sing N N 184 
ILE   C   O    doub N N 185 
ILE   C   OXT  sing N N 186 
ILE   CB  CG1  sing N N 187 
ILE   CB  CG2  sing N N 188 
ILE   CB  HB   sing N N 189 
ILE   CG1 CD1  sing N N 190 
ILE   CG1 HG12 sing N N 191 
ILE   CG1 HG13 sing N N 192 
ILE   CG2 HG21 sing N N 193 
ILE   CG2 HG22 sing N N 194 
ILE   CG2 HG23 sing N N 195 
ILE   CD1 HD11 sing N N 196 
ILE   CD1 HD12 sing N N 197 
ILE   CD1 HD13 sing N N 198 
ILE   OXT HXT  sing N N 199 
LEU   N   CA   sing N N 200 
LEU   N   H    sing N N 201 
LEU   N   H2   sing N N 202 
LEU   CA  C    sing N N 203 
LEU   CA  CB   sing N N 204 
LEU   CA  HA   sing N N 205 
LEU   C   O    doub N N 206 
LEU   C   OXT  sing N N 207 
LEU   CB  CG   sing N N 208 
LEU   CB  HB2  sing N N 209 
LEU   CB  HB3  sing N N 210 
LEU   CG  CD1  sing N N 211 
LEU   CG  CD2  sing N N 212 
LEU   CG  HG   sing N N 213 
LEU   CD1 HD11 sing N N 214 
LEU   CD1 HD12 sing N N 215 
LEU   CD1 HD13 sing N N 216 
LEU   CD2 HD21 sing N N 217 
LEU   CD2 HD22 sing N N 218 
LEU   CD2 HD23 sing N N 219 
LEU   OXT HXT  sing N N 220 
LYS   N   CA   sing N N 221 
LYS   N   H    sing N N 222 
LYS   N   H2   sing N N 223 
LYS   CA  C    sing N N 224 
LYS   CA  CB   sing N N 225 
LYS   CA  HA   sing N N 226 
LYS   C   O    doub N N 227 
LYS   C   OXT  sing N N 228 
LYS   CB  CG   sing N N 229 
LYS   CB  HB2  sing N N 230 
LYS   CB  HB3  sing N N 231 
LYS   CG  CD   sing N N 232 
LYS   CG  HG2  sing N N 233 
LYS   CG  HG3  sing N N 234 
LYS   CD  CE   sing N N 235 
LYS   CD  HD2  sing N N 236 
LYS   CD  HD3  sing N N 237 
LYS   CE  NZ   sing N N 238 
LYS   CE  HE2  sing N N 239 
LYS   CE  HE3  sing N N 240 
LYS   NZ  HZ1  sing N N 241 
LYS   NZ  HZ2  sing N N 242 
LYS   NZ  HZ3  sing N N 243 
LYS   OXT HXT  sing N N 244 
MET   N   CA   sing N N 245 
MET   N   H    sing N N 246 
MET   N   H2   sing N N 247 
MET   CA  C    sing N N 248 
MET   CA  CB   sing N N 249 
MET   CA  HA   sing N N 250 
MET   C   O    doub N N 251 
MET   C   OXT  sing N N 252 
MET   CB  CG   sing N N 253 
MET   CB  HB2  sing N N 254 
MET   CB  HB3  sing N N 255 
MET   CG  SD   sing N N 256 
MET   CG  HG2  sing N N 257 
MET   CG  HG3  sing N N 258 
MET   SD  CE   sing N N 259 
MET   CE  HE1  sing N N 260 
MET   CE  HE2  sing N N 261 
MET   CE  HE3  sing N N 262 
MET   OXT HXT  sing N N 263 
PHE   N   CA   sing N N 264 
PHE   N   H    sing N N 265 
PHE   N   H2   sing N N 266 
PHE   CA  C    sing N N 267 
PHE   CA  CB   sing N N 268 
PHE   CA  HA   sing N N 269 
PHE   C   O    doub N N 270 
PHE   C   OXT  sing N N 271 
PHE   CB  CG   sing N N 272 
PHE   CB  HB2  sing N N 273 
PHE   CB  HB3  sing N N 274 
PHE   CG  CD1  doub Y N 275 
PHE   CG  CD2  sing Y N 276 
PHE   CD1 CE1  sing Y N 277 
PHE   CD1 HD1  sing N N 278 
PHE   CD2 CE2  doub Y N 279 
PHE   CD2 HD2  sing N N 280 
PHE   CE1 CZ   doub Y N 281 
PHE   CE1 HE1  sing N N 282 
PHE   CE2 CZ   sing Y N 283 
PHE   CE2 HE2  sing N N 284 
PHE   CZ  HZ   sing N N 285 
PHE   OXT HXT  sing N N 286 
PRO   N   CA   sing N N 287 
PRO   N   CD   sing N N 288 
PRO   N   H    sing N N 289 
PRO   CA  C    sing N N 290 
PRO   CA  CB   sing N N 291 
PRO   CA  HA   sing N N 292 
PRO   C   O    doub N N 293 
PRO   C   OXT  sing N N 294 
PRO   CB  CG   sing N N 295 
PRO   CB  HB2  sing N N 296 
PRO   CB  HB3  sing N N 297 
PRO   CG  CD   sing N N 298 
PRO   CG  HG2  sing N N 299 
PRO   CG  HG3  sing N N 300 
PRO   CD  HD2  sing N N 301 
PRO   CD  HD3  sing N N 302 
PRO   OXT HXT  sing N N 303 
SER   N   CA   sing N N 304 
SER   N   H    sing N N 305 
SER   N   H2   sing N N 306 
SER   CA  C    sing N N 307 
SER   CA  CB   sing N N 308 
SER   CA  HA   sing N N 309 
SER   C   O    doub N N 310 
SER   C   OXT  sing N N 311 
SER   CB  OG   sing N N 312 
SER   CB  HB2  sing N N 313 
SER   CB  HB3  sing N N 314 
SER   OG  HG   sing N N 315 
SER   OXT HXT  sing N N 316 
THR   N   CA   sing N N 317 
THR   N   H    sing N N 318 
THR   N   H2   sing N N 319 
THR   CA  C    sing N N 320 
THR   CA  CB   sing N N 321 
THR   CA  HA   sing N N 322 
THR   C   O    doub N N 323 
THR   C   OXT  sing N N 324 
THR   CB  OG1  sing N N 325 
THR   CB  CG2  sing N N 326 
THR   CB  HB   sing N N 327 
THR   OG1 HG1  sing N N 328 
THR   CG2 HG21 sing N N 329 
THR   CG2 HG22 sing N N 330 
THR   CG2 HG23 sing N N 331 
THR   OXT HXT  sing N N 332 
TRP   N   CA   sing N N 333 
TRP   N   H    sing N N 334 
TRP   N   H2   sing N N 335 
TRP   CA  C    sing N N 336 
TRP   CA  CB   sing N N 337 
TRP   CA  HA   sing N N 338 
TRP   C   O    doub N N 339 
TRP   C   OXT  sing N N 340 
TRP   CB  CG   sing N N 341 
TRP   CB  HB2  sing N N 342 
TRP   CB  HB3  sing N N 343 
TRP   CG  CD1  doub Y N 344 
TRP   CG  CD2  sing Y N 345 
TRP   CD1 NE1  sing Y N 346 
TRP   CD1 HD1  sing N N 347 
TRP   CD2 CE2  doub Y N 348 
TRP   CD2 CE3  sing Y N 349 
TRP   NE1 CE2  sing Y N 350 
TRP   NE1 HE1  sing N N 351 
TRP   CE2 CZ2  sing Y N 352 
TRP   CE3 CZ3  doub Y N 353 
TRP   CE3 HE3  sing N N 354 
TRP   CZ2 CH2  doub Y N 355 
TRP   CZ2 HZ2  sing N N 356 
TRP   CZ3 CH2  sing Y N 357 
TRP   CZ3 HZ3  sing N N 358 
TRP   CH2 HH2  sing N N 359 
TRP   OXT HXT  sing N N 360 
TYR   N   CA   sing N N 361 
TYR   N   H    sing N N 362 
TYR   N   H2   sing N N 363 
TYR   CA  C    sing N N 364 
TYR   CA  CB   sing N N 365 
TYR   CA  HA   sing N N 366 
TYR   C   O    doub N N 367 
TYR   C   OXT  sing N N 368 
TYR   CB  CG   sing N N 369 
TYR   CB  HB2  sing N N 370 
TYR   CB  HB3  sing N N 371 
TYR   CG  CD1  doub Y N 372 
TYR   CG  CD2  sing Y N 373 
TYR   CD1 CE1  sing Y N 374 
TYR   CD1 HD1  sing N N 375 
TYR   CD2 CE2  doub Y N 376 
TYR   CD2 HD2  sing N N 377 
TYR   CE1 CZ   doub Y N 378 
TYR   CE1 HE1  sing N N 379 
TYR   CE2 CZ   sing Y N 380 
TYR   CE2 HE2  sing N N 381 
TYR   CZ  OH   sing N N 382 
TYR   OH  HH   sing N N 383 
TYR   OXT HXT  sing N N 384 
VAL   N   CA   sing N N 385 
VAL   N   H    sing N N 386 
VAL   N   H2   sing N N 387 
VAL   CA  C    sing N N 388 
VAL   CA  CB   sing N N 389 
VAL   CA  HA   sing N N 390 
VAL   C   O    doub N N 391 
VAL   C   OXT  sing N N 392 
VAL   CB  CG1  sing N N 393 
VAL   CB  CG2  sing N N 394 
VAL   CB  HB   sing N N 395 
VAL   CG1 HG11 sing N N 396 
VAL   CG1 HG12 sing N N 397 
VAL   CG1 HG13 sing N N 398 
VAL   CG2 HG21 sing N N 399 
VAL   CG2 HG22 sing N N 400 
VAL   CG2 HG23 sing N N 401 
VAL   OXT HXT  sing N N 402 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Natural Science Foundation of China (NSFC)' China 81622002 1 
'National Natural Science Foundation of China (NSFC)' China 81861130368 2 
'Other government'                                    ?     'Shanghai Youth Talent Development Program (2017275)' 3 
'Other government'                                    ?     
'Foundation of National Facility for Translational Medicine (Shanghai) (TMSK-2020-003)' 4 
'Other government'                                    ?     
'Foundation of National Facility for Translational Medicine (Shanghai) (TMSK-2020-003)' 5 
'Other government'                                    ?     
'Shanghai Medical and Health Excellent Discipline Leader Development Plan (2018BR36)'   6 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'Previously P53 structure' 
# 
_atom_sites.entry_id                    8XCB 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.014524 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   -0.000007 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014330 
_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]   0.011952 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
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   . VAL   A 1 4   ? 9.781   -20.599 -72.519  1.00 29.80 ? 97  VAL   A N   1 
ATOM   2    C  CA  . VAL   A 1 4   ? 8.691   -19.633 -72.853  1.00 28.73 ? 97  VAL   A CA  1 
ATOM   3    C  C   . VAL   A 1 4   ? 8.323   -18.833 -71.604  1.00 26.87 ? 97  VAL   A C   1 
ATOM   4    O  O   . VAL   A 1 4   ? 8.081   -19.409 -70.547  1.00 25.49 ? 97  VAL   A O   1 
ATOM   5    C  CB  . VAL   A 1 4   ? 7.460   -20.357 -73.433  1.00 30.09 ? 97  VAL   A CB  1 
ATOM   6    C  CG1 . VAL   A 1 4   ? 6.344   -19.386 -73.779  1.00 30.23 ? 97  VAL   A CG1 1 
ATOM   7    C  CG2 . VAL   A 1 4   ? 7.820   -21.203 -74.647  1.00 30.10 ? 97  VAL   A CG2 1 
ATOM   8    N  N   . PRO   A 1 5   ? 8.277   -17.482 -71.684  1.00 25.22 ? 98  PRO   A N   1 
ATOM   9    C  CA  . PRO   A 1 5   ? 7.757   -16.659 -70.589  1.00 23.98 ? 98  PRO   A CA  1 
ATOM   10   C  C   . PRO   A 1 5   ? 6.310   -17.011 -70.204  1.00 22.81 ? 98  PRO   A C   1 
ATOM   11   O  O   . PRO   A 1 5   ? 5.515   -17.267 -71.087  1.00 22.17 ? 98  PRO   A O   1 
ATOM   12   C  CB  . PRO   A 1 5   ? 7.815   -15.229 -71.149  1.00 24.75 ? 98  PRO   A CB  1 
ATOM   13   C  CG  . PRO   A 1 5   ? 8.887   -15.290 -72.223  1.00 25.61 ? 98  PRO   A CG  1 
ATOM   14   C  CD  . PRO   A 1 5   ? 8.760   -16.675 -72.816  1.00 25.43 ? 98  PRO   A CD  1 
ATOM   15   N  N   . SER   A 1 6   ? 6.002   -17.007 -68.905  1.00 22.21 ? 99  SER   A N   1 
ATOM   16   C  CA  . SER   A 1 6   ? 4.640   -17.251 -68.364  1.00 21.93 ? 99  SER   A CA  1 
ATOM   17   C  C   . SER   A 1 6   ? 3.703   -16.110 -68.785  1.00 21.98 ? 99  SER   A C   1 
ATOM   18   O  O   . SER   A 1 6   ? 4.136   -14.940 -68.739  1.00 21.68 ? 99  SER   A O   1 
ATOM   19   C  CB  . SER   A 1 6   ? 4.662   -17.411 -66.869  1.00 21.99 ? 99  SER   A CB  1 
ATOM   20   O  OG  . SER   A 1 6   ? 3.340   -17.441 -66.352  1.00 22.20 ? 99  SER   A OG  1 
ATOM   21   N  N   . GLN   A 1 7   ? 2.465   -16.443 -69.169  1.00 21.45 ? 100 GLN   A N   1 
ATOM   22   C  CA  . GLN   A 1 7   ? 1.385   -15.460 -69.464  1.00 21.61 ? 100 GLN   A CA  1 
ATOM   23   C  C   . GLN   A 1 7   ? 0.257   -15.602 -68.431  1.00 20.83 ? 100 GLN   A C   1 
ATOM   24   O  O   . GLN   A 1 7   ? -0.789  -14.964 -68.621  1.00 20.33 ? 100 GLN   A O   1 
ATOM   25   C  CB  . GLN   A 1 7   ? 0.867   -15.633 -70.895  1.00 21.67 ? 100 GLN   A CB  1 
ATOM   26   C  CG  . GLN   A 1 7   ? 0.366   -17.032 -71.222  1.00 22.62 ? 100 GLN   A CG  1 
ATOM   27   C  CD  . GLN   A 1 7   ? -0.240  -17.096 -72.601  1.00 23.15 ? 100 GLN   A CD  1 
ATOM   28   O  OE1 . GLN   A 1 7   ? 0.440   -17.369 -73.588  1.00 25.66 ? 100 GLN   A OE1 1 
ATOM   29   N  NE2 . GLN   A 1 7   ? -1.529  -16.817 -72.684  1.00 23.21 ? 100 GLN   A NE2 1 
ATOM   30   N  N   . LYS   A 1 8   ? 0.477   -16.376 -67.361  1.00 20.80 ? 101 LYS   A N   1 
ATOM   31   C  CA  . LYS   A 1 8   ? -0.509  -16.584 -66.267  1.00 20.92 ? 101 LYS   A CA  1 
ATOM   32   C  C   . LYS   A 1 8   ? -0.882  -15.240 -65.631  1.00 20.58 ? 101 LYS   A C   1 
ATOM   33   O  O   . LYS   A 1 8   ? 0.019   -14.561 -65.104  1.00 20.40 ? 101 LYS   A O   1 
ATOM   34   C  CB  . LYS   A 1 8   ? 0.051   -17.513 -65.192  1.00 21.21 ? 101 LYS   A CB  1 
ATOM   35   C  CG  . LYS   A 1 8   ? 0.234   -18.955 -65.625  1.00 21.57 ? 101 LYS   A CG  1 
ATOM   36   C  CD  . LYS   A 1 8   ? 0.948   -19.784 -64.587  1.00 21.99 ? 101 LYS   A CD  1 
ATOM   37   C  CE  . LYS   A 1 8   ? 0.952   -21.255 -64.931  1.00 22.29 ? 101 LYS   A CE  1 
ATOM   38   N  NZ  . LYS   A 1 8   ? 1.731   -22.026 -63.943  1.00 22.74 ? 101 LYS   A NZ  1 
ATOM   39   N  N   . THR   A 1 9   ? -2.169  -14.890 -65.661  1.00 20.30 ? 102 THR   A N   1 
ATOM   40   C  CA  . THR   A 1 9   ? -2.727  -13.691 -64.983  1.00 21.13 ? 102 THR   A CA  1 
ATOM   41   C  C   . THR   A 1 9   ? -2.470  -13.821 -63.479  1.00 21.38 ? 102 THR   A C   1 
ATOM   42   O  O   . THR   A 1 9   ? -2.661  -14.921 -62.932  1.00 21.48 ? 102 THR   A O   1 
ATOM   43   C  CB  . THR   A 1 9   ? -4.215  -13.510 -65.308  1.00 21.44 ? 102 THR   A CB  1 
ATOM   44   O  OG1 . THR   A 1 9   ? -4.286  -13.250 -66.711  1.00 21.62 ? 102 THR   A OG1 1 
ATOM   45   C  CG2 . THR   A 1 9   ? -4.872  -12.397 -64.518  1.00 21.67 ? 102 THR   A CG2 1 
ATOM   46   N  N   . TYR   A 1 10  ? -2.022  -12.739 -62.852  1.00 22.02 ? 103 TYR   A N   1 
ATOM   47   C  CA  . TYR   A 1 10  ? -1.641  -12.696 -61.420  1.00 22.81 ? 103 TYR   A CA  1 
ATOM   48   C  C   . TYR   A 1 10  ? -1.897  -11.286 -60.891  1.00 22.88 ? 103 TYR   A C   1 
ATOM   49   O  O   . TYR   A 1 10  ? -1.095  -10.376 -61.180  1.00 23.33 ? 103 TYR   A O   1 
ATOM   50   C  CB  . TYR   A 1 10  ? -0.179  -13.119 -61.249  1.00 23.33 ? 103 TYR   A CB  1 
ATOM   51   C  CG  . TYR   A 1 10  ? 0.319   -13.097 -59.825  1.00 24.06 ? 103 TYR   A CG  1 
ATOM   52   C  CD1 . TYR   A 1 10  ? -0.412  -13.673 -58.797  1.00 24.55 ? 103 TYR   A CD1 1 
ATOM   53   C  CD2 . TYR   A 1 10  ? 1.536   -12.514 -59.505  1.00 24.62 ? 103 TYR   A CD2 1 
ATOM   54   C  CE1 . TYR   A 1 10  ? 0.044   -13.654 -57.486  1.00 25.09 ? 103 TYR   A CE1 1 
ATOM   55   C  CE2 . TYR   A 1 10  ? 2.007   -12.489 -58.203  1.00 24.95 ? 103 TYR   A CE2 1 
ATOM   56   C  CZ  . TYR   A 1 10  ? 1.256   -13.056 -57.188  1.00 25.49 ? 103 TYR   A CZ  1 
ATOM   57   O  OH  . TYR   A 1 10  ? 1.717   -13.029 -55.904  1.00 25.93 ? 103 TYR   A OH  1 
ATOM   58   N  N   . GLN   A 1 11  ? -2.990  -11.108 -60.151  1.00 23.51 ? 104 GLN   A N   1 
ATOM   59   C  CA  . GLN   A 1 11  ? -3.366  -9.794  -59.568  1.00 24.49 ? 104 GLN   A CA  1 
ATOM   60   C  C   . GLN   A 1 11  ? -2.443  -9.499  -58.381  1.00 23.99 ? 104 GLN   A C   1 
ATOM   61   O  O   . GLN   A 1 11  ? -2.104  -8.316  -58.182  1.00 22.42 ? 104 GLN   A O   1 
ATOM   62   C  CB  . GLN   A 1 11  ? -4.856  -9.779  -59.233  1.00 26.00 ? 104 GLN   A CB  1 
ATOM   63   C  CG  . GLN   A 1 11  ? -5.714  -9.866  -60.487  1.00 28.19 ? 104 GLN   A CG  1 
ATOM   64   C  CD  . GLN   A 1 11  ? -7.185  -9.668  -60.226  1.00 29.82 ? 104 GLN   A CD  1 
ATOM   65   O  OE1 . GLN   A 1 11  ? -7.693  -9.985  -59.156  1.00 32.96 ? 104 GLN   A OE1 1 
ATOM   66   N  NE2 . GLN   A 1 11  ? -7.883  -9.145  -61.222  1.00 31.43 ? 104 GLN   A NE2 1 
ATOM   67   N  N   . GLY   A 1 12  ? -2.012  -10.542 -57.665  1.00 24.24 ? 105 GLY   A N   1 
ATOM   68   C  CA  . GLY   A 1 12  ? -1.038  -10.447 -56.560  1.00 24.17 ? 105 GLY   A CA  1 
ATOM   69   C  C   . GLY   A 1 12  ? -1.568  -9.625  -55.396  1.00 24.01 ? 105 GLY   A C   1 
ATOM   70   O  O   . GLY   A 1 12  ? -2.803  -9.404  -55.325  1.00 23.42 ? 105 GLY   A O   1 
ATOM   71   N  N   . SER   A 1 13  ? -0.663  -9.169  -54.527  1.00 23.31 ? 106 SER   A N   1 
ATOM   72   C  CA  . SER   A 1 13  ? -0.978  -8.514  -53.231  1.00 23.49 ? 106 SER   A CA  1 
ATOM   73   C  C   . SER   A 1 13  ? -1.645  -7.153  -53.455  1.00 23.09 ? 106 SER   A C   1 
ATOM   74   O  O   . SER   A 1 13  ? -2.417  -6.734  -52.576  1.00 22.77 ? 106 SER   A O   1 
ATOM   75   C  CB  . SER   A 1 13  ? 0.260   -8.368  -52.383  1.00 23.74 ? 106 SER   A CB  1 
ATOM   76   O  OG  . SER   A 1 13  ? 0.760   -9.636  -52.008  1.00 24.14 ? 106 SER   A OG  1 
ATOM   77   N  N   . TYR   A 1 14  ? -1.349  -6.490  -54.580  1.00 22.22 ? 107 TYR   A N   1 
ATOM   78   C  CA  . TYR   A 1 14  ? -1.672  -5.061  -54.828  1.00 22.14 ? 107 TYR   A CA  1 
ATOM   79   C  C   . TYR   A 1 14  ? -2.903  -4.931  -55.735  1.00 21.06 ? 107 TYR   A C   1 
ATOM   80   O  O   . TYR   A 1 14  ? -3.287  -3.789  -56.008  1.00 20.73 ? 107 TYR   A O   1 
ATOM   81   C  CB  . TYR   A 1 14  ? -0.433  -4.351  -55.378  1.00 22.76 ? 107 TYR   A CB  1 
ATOM   82   C  CG  . TYR   A 1 14  ? 0.753   -4.466  -54.456  1.00 23.48 ? 107 TYR   A CG  1 
ATOM   83   C  CD1 . TYR   A 1 14  ? 0.837   -3.683  -53.316  1.00 24.44 ? 107 TYR   A CD1 1 
ATOM   84   C  CD2 . TYR   A 1 14  ? 1.760   -5.390  -54.684  1.00 24.05 ? 107 TYR   A CD2 1 
ATOM   85   C  CE1 . TYR   A 1 14  ? 1.902   -3.793  -52.438  1.00 24.59 ? 107 TYR   A CE1 1 
ATOM   86   C  CE2 . TYR   A 1 14  ? 2.834   -5.513  -53.815  1.00 24.66 ? 107 TYR   A CE2 1 
ATOM   87   C  CZ  . TYR   A 1 14  ? 2.902   -4.713  -52.687  1.00 25.17 ? 107 TYR   A CZ  1 
ATOM   88   O  OH  . TYR   A 1 14  ? 3.947   -4.820  -51.818  1.00 27.44 ? 107 TYR   A OH  1 
ATOM   89   N  N   . GLY   A 1 15  ? -3.512  -6.049  -56.149  1.00 20.95 ? 108 GLY   A N   1 
ATOM   90   C  CA  . GLY   A 1 15  ? -4.748  -6.066  -56.958  1.00 20.76 ? 108 GLY   A CA  1 
ATOM   91   C  C   . GLY   A 1 15  ? -4.496  -5.498  -58.342  1.00 20.89 ? 108 GLY   A C   1 
ATOM   92   O  O   . GLY   A 1 15  ? -5.257  -4.608  -58.779  1.00 20.29 ? 108 GLY   A O   1 
ATOM   93   N  N   . PHE   A 1 16  ? -3.438  -5.980  -58.999  1.00 20.72 ? 109 PHE   A N   1 
ATOM   94   C  CA  . PHE   A 1 16  ? -2.904  -5.410  -60.260  1.00 20.77 ? 109 PHE   A CA  1 
ATOM   95   C  C   . PHE   A 1 16  ? -3.716  -5.962  -61.432  1.00 20.95 ? 109 PHE   A C   1 
ATOM   96   O  O   . PHE   A 1 16  ? -3.816  -7.196  -61.569  1.00 21.69 ? 109 PHE   A O   1 
ATOM   97   C  CB  . PHE   A 1 16  ? -1.412  -5.715  -60.408  1.00 20.73 ? 109 PHE   A CB  1 
ATOM   98   C  CG  . PHE   A 1 16  ? -0.842  -5.387  -61.764  1.00 21.04 ? 109 PHE   A CG  1 
ATOM   99   C  CD1 . PHE   A 1 16  ? -0.828  -4.080  -62.225  1.00 21.23 ? 109 PHE   A CD1 1 
ATOM   100  C  CD2 . PHE   A 1 16  ? -0.325  -6.382  -62.577  1.00 20.51 ? 109 PHE   A CD2 1 
ATOM   101  C  CE1 . PHE   A 1 16  ? -0.305  -3.777  -63.473  1.00 21.30 ? 109 PHE   A CE1 1 
ATOM   102  C  CE2 . PHE   A 1 16  ? 0.203   -6.076  -63.822  1.00 20.58 ? 109 PHE   A CE2 1 
ATOM   103  C  CZ  . PHE   A 1 16  ? 0.208   -4.775  -64.269  1.00 21.03 ? 109 PHE   A CZ  1 
ATOM   104  N  N   . ARG   A 1 17  ? -4.277  -5.072  -62.249  1.00 20.70 ? 110 ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 17  ? -4.887  -5.442  -63.552  1.00 20.83 ? 110 ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 17  ? -4.671  -4.302  -64.549  1.00 19.97 ? 110 ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 17  ? -4.177  -3.227  -64.144  1.00 19.58 ? 110 ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 17  ? -6.360  -5.825  -63.377  1.00 22.46 ? 110 ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 17  ? -7.281  -4.684  -62.980  1.00 23.89 ? 110 ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 17  ? -7.366  -4.465  -61.485  1.00 25.11 ? 110 ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 17  ? -8.427  -3.505  -61.198  1.00 26.22 ? 110 ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 17  ? -8.496  -2.722  -60.125  1.00 26.90 ? 110 ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 17  ? -9.521  -1.896  -59.994  1.00 27.38 ? 110 ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 17  ? -7.553  -2.752  -59.196  1.00 26.39 ? 110 ARG   A NH2 1 
ATOM   115  N  N   . LEU   A 1 18  ? -5.001  -4.553  -65.815  1.00 18.58 ? 111 LEU   A N   1 
ATOM   116  C  CA  . LEU   A 1 18  ? -4.835  -3.578  -66.916  1.00 17.92 ? 111 LEU   A CA  1 
ATOM   117  C  C   . LEU   A 1 18  ? -6.191  -2.943  -67.217  1.00 17.37 ? 111 LEU   A C   1 
ATOM   118  O  O   . LEU   A 1 18  ? -7.230  -3.588  -66.971  1.00 17.15 ? 111 LEU   A O   1 
ATOM   119  C  CB  . LEU   A 1 18  ? -4.265  -4.280  -68.151  1.00 17.63 ? 111 LEU   A CB  1 
ATOM   120  C  CG  . LEU   A 1 18  ? -2.880  -4.887  -67.967  1.00 17.35 ? 111 LEU   A CG  1 
ATOM   121  C  CD1 . LEU   A 1 18  ? -2.427  -5.575  -69.247  1.00 17.36 ? 111 LEU   A CD1 1 
ATOM   122  C  CD2 . LEU   A 1 18  ? -1.870  -3.827  -67.534  1.00 17.38 ? 111 LEU   A CD2 1 
ATOM   123  N  N   . GLY   A 1 19  ? -6.154  -1.707  -67.704  1.00 16.86 ? 112 GLY   A N   1 
ATOM   124  C  CA  . GLY   A 1 19  ? -7.302  -1.016  -68.310  1.00 16.69 ? 112 GLY   A CA  1 
ATOM   125  C  C   . GLY   A 1 19  ? -6.905  -0.412  -69.640  1.00 16.92 ? 112 GLY   A C   1 
ATOM   126  O  O   . GLY   A 1 19  ? -5.681  -0.213  -69.879  1.00 16.31 ? 112 GLY   A O   1 
ATOM   127  N  N   . PHE   A 1 20  ? -7.895  -0.133  -70.481  1.00 16.78 ? 113 PHE   A N   1 
ATOM   128  C  CA  . PHE   A 1 20  ? -7.713  0.462   -71.826  1.00 16.83 ? 113 PHE   A CA  1 
ATOM   129  C  C   . PHE   A 1 20  ? -8.770  1.551   -72.023  1.00 16.79 ? 113 PHE   A C   1 
ATOM   130  O  O   . PHE   A 1 20  ? -9.831  1.472   -71.388  1.00 15.63 ? 113 PHE   A O   1 
ATOM   131  C  CB  . PHE   A 1 20  ? -7.784  -0.639  -72.885  1.00 16.96 ? 113 PHE   A CB  1 
ATOM   132  C  CG  . PHE   A 1 20  ? -6.839  -1.788  -72.629  1.00 17.04 ? 113 PHE   A CG  1 
ATOM   133  C  CD1 . PHE   A 1 20  ? -5.560  -1.781  -73.157  1.00 17.41 ? 113 PHE   A CD1 1 
ATOM   134  C  CD2 . PHE   A 1 20  ? -7.217  -2.860  -71.834  1.00 16.97 ? 113 PHE   A CD2 1 
ATOM   135  C  CE1 . PHE   A 1 20  ? -4.686  -2.831  -72.914  1.00 17.62 ? 113 PHE   A CE1 1 
ATOM   136  C  CE2 . PHE   A 1 20  ? -6.342  -3.906  -71.587  1.00 17.28 ? 113 PHE   A CE2 1 
ATOM   137  C  CZ  . PHE   A 1 20  ? -5.080  -3.892  -72.132  1.00 17.36 ? 113 PHE   A CZ  1 
ATOM   138  N  N   . LEU   A 1 21  ? -8.470  2.541   -72.865  1.00 16.80 ? 114 LEU   A N   1 
ATOM   139  C  CA  . LEU   A 1 21  ? -9.450  3.581   -73.265  1.00 17.35 ? 114 LEU   A CA  1 
ATOM   140  C  C   . LEU   A 1 21  ? -10.608 2.900   -73.999  1.00 17.37 ? 114 LEU   A C   1 
ATOM   141  O  O   . LEU   A 1 21  ? -10.351 1.934   -74.746  1.00 16.64 ? 114 LEU   A O   1 
ATOM   142  C  CB  . LEU   A 1 21  ? -8.770  4.618   -74.158  1.00 17.56 ? 114 LEU   A CB  1 
ATOM   143  C  CG  . LEU   A 1 21  ? -7.695  5.460   -73.480  1.00 18.05 ? 114 LEU   A CG  1 
ATOM   144  C  CD1 . LEU   A 1 21  ? -7.073  6.424   -74.479  1.00 17.96 ? 114 LEU   A CD1 1 
ATOM   145  C  CD2 . LEU   A 1 21  ? -8.258  6.198   -72.274  1.00 18.17 ? 114 LEU   A CD2 1 
ATOM   146  N  N   . HIS   A 1 22  ? -11.830 3.390   -73.783  1.00 17.39 ? 115 HIS   A N   1 
ATOM   147  C  CA  . HIS   A 1 22  ? -13.066 2.904   -74.450  1.00 17.68 ? 115 HIS   A CA  1 
ATOM   148  C  C   . HIS   A 1 22  ? -13.258 3.737   -75.721  1.00 17.01 ? 115 HIS   A C   1 
ATOM   149  O  O   . HIS   A 1 22  ? -14.155 4.591   -75.745  1.00 16.90 ? 115 HIS   A O   1 
ATOM   150  C  CB  . HIS   A 1 22  ? -14.229 2.917   -73.450  1.00 17.82 ? 115 HIS   A CB  1 
ATOM   151  C  CG  . HIS   A 1 22  ? -13.895 2.175   -72.198  1.00 18.31 ? 115 HIS   A CG  1 
ATOM   152  N  ND1 . HIS   A 1 22  ? -13.516 0.850   -72.215  1.00 18.13 ? 115 HIS   A ND1 1 
ATOM   153  C  CD2 . HIS   A 1 22  ? -13.819 2.577   -70.908  1.00 18.28 ? 115 HIS   A CD2 1 
ATOM   154  C  CE1 . HIS   A 1 22  ? -13.244 0.457   -70.985  1.00 18.69 ? 115 HIS   A CE1 1 
ATOM   155  N  NE2 . HIS   A 1 22  ? -13.424 1.499   -70.161  1.00 18.55 ? 115 HIS   A NE2 1 
ATOM   156  N  N   . SER   A 1 23  ? -12.415 3.483   -76.724  1.00 16.48 ? 116 SER   A N   1 
ATOM   157  C  CA  . SER   A 1 23  ? -12.145 4.381   -77.879  1.00 16.67 ? 116 SER   A CA  1 
ATOM   158  C  C   . SER   A 1 23  ? -13.136 4.143   -79.029  1.00 16.46 ? 116 SER   A C   1 
ATOM   159  O  O   . SER   A 1 23  ? -13.286 5.050   -79.868  1.00 16.58 ? 116 SER   A O   1 
ATOM   160  C  CB  . SER   A 1 23  ? -10.719 4.220   -78.341  1.00 16.81 ? 116 SER   A CB  1 
ATOM   161  O  OG  . SER   A 1 23  ? -9.814  4.514   -77.281  1.00 17.07 ? 116 SER   A OG  1 
ATOM   162  N  N   . GLY   A 1 24  ? -13.785 2.980   -79.077  1.00 16.14 ? 117 GLY   A N   1 
ATOM   163  C  CA  . GLY   A 1 24  ? -14.717 2.627   -80.167  1.00 16.16 ? 117 GLY   A CA  1 
ATOM   164  C  C   . GLY   A 1 24  ? -13.978 2.338   -81.463  1.00 15.96 ? 117 GLY   A C   1 
ATOM   165  O  O   . GLY   A 1 24  ? -12.735 2.230   -81.427  1.00 16.01 ? 117 GLY   A O   1 
ATOM   166  N  N   . THR   A 1 25  ? -14.705 2.218   -82.578  1.00 16.38 ? 118 THR   A N   1 
ATOM   167  C  CA  . THR   A 1 25  ? -14.166 1.695   -83.859  1.00 16.71 ? 118 THR   A CA  1 
ATOM   168  C  C   . THR   A 1 25  ? -14.375 2.683   -85.011  1.00 17.52 ? 118 THR   A C   1 
ATOM   169  O  O   . THR   A 1 25  ? -14.336 2.222   -86.158  1.00 16.91 ? 118 THR   A O   1 
ATOM   170  C  CB  . THR   A 1 25  ? -14.777 0.329   -84.197  1.00 16.54 ? 118 THR   A CB  1 
ATOM   171  O  OG1 . THR   A 1 25  ? -16.170 0.499   -84.462  1.00 16.29 ? 118 THR   A OG1 1 
ATOM   172  C  CG2 . THR   A 1 25  ? -14.563 -0.696  -83.103  1.00 16.54 ? 118 THR   A CG2 1 
ATOM   173  N  N   . ALA   A 1 26  ? -14.539 3.983   -84.742  1.00 18.87 ? 119 ALA   A N   1 
ATOM   174  C  CA  . ALA   A 1 26  ? -14.534 5.032   -85.793  1.00 19.80 ? 119 ALA   A CA  1 
ATOM   175  C  C   . ALA   A 1 26  ? -13.228 4.929   -86.598  1.00 21.07 ? 119 ALA   A C   1 
ATOM   176  O  O   . ALA   A 1 26  ? -12.186 4.589   -86.003  1.00 19.88 ? 119 ALA   A O   1 
ATOM   177  C  CB  . ALA   A 1 26  ? -14.706 6.405   -85.186  1.00 19.60 ? 119 ALA   A CB  1 
ATOM   178  N  N   . LYS   A 1 27  ? -13.289 5.227   -87.901  1.00 24.00 ? 120 LYS   A N   1 
ATOM   179  C  CA  . LYS   A 1 27  ? -12.145 5.165   -88.855  1.00 25.83 ? 120 LYS   A CA  1 
ATOM   180  C  C   . LYS   A 1 27  ? -10.950 5.970   -88.320  1.00 24.98 ? 120 LYS   A C   1 
ATOM   181  O  O   . LYS   A 1 27  ? -9.802  5.576   -88.596  1.00 23.56 ? 120 LYS   A O   1 
ATOM   182  C  CB  . LYS   A 1 27  ? -12.568 5.701   -90.229  1.00 29.24 ? 120 LYS   A CB  1 
ATOM   183  C  CG  . LYS   A 1 27  ? -11.679 5.284   -91.396  1.00 31.93 ? 120 LYS   A CG  1 
ATOM   184  C  CD  . LYS   A 1 27  ? -11.889 6.099   -92.667  1.00 33.80 ? 120 LYS   A CD  1 
ATOM   185  C  CE  . LYS   A 1 27  ? -13.258 5.919   -93.293  1.00 35.62 ? 120 LYS   A CE  1 
ATOM   186  N  NZ  . LYS   A 1 27  ? -13.352 4.670   -94.089  1.00 36.60 ? 120 LYS   A NZ  1 
ATOM   187  N  N   . SER   A 1 28  ? -11.209 7.051   -87.583  1.00 24.97 ? 121 SER   A N   1 
ATOM   188  C  CA  . SER   A 1 28  ? -10.189 8.031   -87.120  1.00 25.63 ? 121 SER   A CA  1 
ATOM   189  C  C   . SER   A 1 28  ? -9.339  7.481   -85.966  1.00 24.29 ? 121 SER   A C   1 
ATOM   190  O  O   . SER   A 1 28  ? -8.277  8.070   -85.719  1.00 24.91 ? 121 SER   A O   1 
ATOM   191  C  CB  . SER   A 1 28  ? -10.840 9.320   -86.708  1.00 25.59 ? 121 SER   A CB  1 
ATOM   192  O  OG  . SER   A 1 28  ? -11.680 9.112   -85.582  1.00 27.39 ? 121 SER   A OG  1 
ATOM   193  N  N   . VAL   A 1 29  ? -9.780  6.430   -85.264  1.00 23.20 ? 122 VAL   A N   1 
ATOM   194  C  CA  . VAL   A 1 29  ? -9.105  5.963   -84.014  1.00 22.16 ? 122 VAL   A CA  1 
ATOM   195  C  C   . VAL   A 1 29  ? -7.708  5.440   -84.371  1.00 22.32 ? 122 VAL   A C   1 
ATOM   196  O  O   . VAL   A 1 29  ? -7.576  4.723   -85.372  1.00 23.00 ? 122 VAL   A O   1 
ATOM   197  C  CB  . VAL   A 1 29  ? -9.925  4.923   -83.222  1.00 21.62 ? 122 VAL   A CB  1 
ATOM   198  C  CG1 . VAL   A 1 29  ? -11.290 5.470   -82.830  1.00 21.51 ? 122 VAL   A CG1 1 
ATOM   199  C  CG2 . VAL   A 1 29  ? -10.052 3.592   -83.947  1.00 21.24 ? 122 VAL   A CG2 1 
ATOM   200  N  N   . THR   A 1 30  ? -6.709  5.828   -83.580  1.00 22.78 ? 123 THR   A N   1 
ATOM   201  C  CA  . THR   A 1 30  ? -5.279  5.458   -83.746  1.00 23.73 ? 123 THR   A CA  1 
ATOM   202  C  C   . THR   A 1 30  ? -5.015  4.117   -83.053  1.00 22.13 ? 123 THR   A C   1 
ATOM   203  O  O   . THR   A 1 30  ? -4.118  3.387   -83.490  1.00 22.90 ? 123 THR   A O   1 
ATOM   204  C  CB  . THR   A 1 30  ? -4.374  6.575   -83.213  1.00 25.26 ? 123 THR   A CB  1 
ATOM   205  O  OG1 . THR   A 1 30  ? -4.553  7.720   -84.049  1.00 30.01 ? 123 THR   A OG1 1 
ATOM   206  C  CG2 . THR   A 1 30  ? -2.912  6.196   -83.192  1.00 26.48 ? 123 THR   A CG2 1 
ATOM   207  N  N   A CYS   A 1 31  ? -5.827  3.801   -82.035  0.50 21.46 ? 124 CYS   A N   1 
ATOM   208  N  N   B CYS   A 1 31  ? -5.751  3.827   -81.979  0.50 21.91 ? 124 CYS   A N   1 
ATOM   209  C  CA  A CYS   A 1 31  ? -5.649  2.684   -81.070  0.50 20.73 ? 124 CYS   A CA  1 
ATOM   210  C  CA  B CYS   A 1 31  ? -5.660  2.553   -81.227  0.50 21.44 ? 124 CYS   A CA  1 
ATOM   211  C  C   A CYS   A 1 31  ? -7.025  2.320   -80.490  0.50 20.29 ? 124 CYS   A C   1 
ATOM   212  C  C   B CYS   A 1 31  ? -6.994  2.299   -80.519  0.50 20.74 ? 124 CYS   A C   1 
ATOM   213  O  O   A CYS   A 1 31  ? -7.748  3.257   -80.098  0.50 20.36 ? 124 CYS   A O   1 
ATOM   214  O  O   B CYS   A 1 31  ? -7.627  3.271   -80.063  0.50 20.97 ? 124 CYS   A O   1 
ATOM   215  C  CB  A CYS   A 1 31  ? -4.677  3.128   -79.980  0.50 20.80 ? 124 CYS   A CB  1 
ATOM   216  C  CB  B CYS   A 1 31  ? -4.500  2.583   -80.241  0.50 22.07 ? 124 CYS   A CB  1 
ATOM   217  S  SG  A CYS   A 1 31  ? -4.301  1.867   -78.737  0.50 20.81 ? 124 CYS   A SG  1 
ATOM   218  S  SG  B CYS   A 1 31  ? -4.802  3.654   -78.817  0.50 23.22 ? 124 CYS   A SG  1 
ATOM   219  N  N   . THR   A 1 32  ? -7.405  1.035   -80.464  1.00 19.13 ? 125 THR   A N   1 
ATOM   220  C  CA  . THR   A 1 32  ? -8.704  0.608   -79.882  1.00 18.58 ? 125 THR   A CA  1 
ATOM   221  C  C   . THR   A 1 32  ? -8.595  -0.827  -79.366  1.00 17.79 ? 125 THR   A C   1 
ATOM   222  O  O   . THR   A 1 32  ? -8.033  -1.681  -80.080  1.00 18.91 ? 125 THR   A O   1 
ATOM   223  C  CB  . THR   A 1 32  ? -9.853  0.772   -80.884  1.00 18.01 ? 125 THR   A CB  1 
ATOM   224  O  OG1 . THR   A 1 32  ? -11.066 0.537   -80.167  1.00 17.01 ? 125 THR   A OG1 1 
ATOM   225  C  CG2 . THR   A 1 32  ? -9.756  -0.163  -82.071  1.00 17.96 ? 125 THR   A CG2 1 
ATOM   226  N  N   . TYR   A 1 33  ? -9.134  -1.064  -78.172  1.00 16.40 ? 126 TYR   A N   1 
ATOM   227  C  CA  . TYR   A 1 33  ? -9.063  -2.357  -77.454  1.00 16.16 ? 126 TYR   A CA  1 
ATOM   228  C  C   . TYR   A 1 33  ? -10.424 -3.057  -77.539  1.00 16.01 ? 126 TYR   A C   1 
ATOM   229  O  O   . TYR   A 1 33  ? -11.453 -2.430  -77.256  1.00 15.68 ? 126 TYR   A O   1 
ATOM   230  C  CB  . TYR   A 1 33  ? -8.604  -2.127  -76.014  1.00 15.83 ? 126 TYR   A CB  1 
ATOM   231  C  CG  . TYR   A 1 33  ? -8.732  -3.340  -75.130  1.00 15.51 ? 126 TYR   A CG  1 
ATOM   232  C  CD1 . TYR   A 1 33  ? -7.810  -4.369  -75.198  1.00 15.27 ? 126 TYR   A CD1 1 
ATOM   233  C  CD2 . TYR   A 1 33  ? -9.783  -3.464  -74.234  1.00 15.67 ? 126 TYR   A CD2 1 
ATOM   234  C  CE1 . TYR   A 1 33  ? -7.920  -5.489  -74.392  1.00 15.37 ? 126 TYR   A CE1 1 
ATOM   235  C  CE2 . TYR   A 1 33  ? -9.912  -4.582  -73.426  1.00 15.64 ? 126 TYR   A CE2 1 
ATOM   236  C  CZ  . TYR   A 1 33  ? -8.974  -5.596  -73.502  1.00 15.70 ? 126 TYR   A CZ  1 
ATOM   237  O  OH  . TYR   A 1 33  ? -9.086  -6.700  -72.708  1.00 16.02 ? 126 TYR   A OH  1 
ATOM   238  N  N   . SER   A 1 34  ? -10.410 -4.331  -77.930  1.00 16.33 ? 127 SER   A N   1 
ATOM   239  C  CA  . SER   A 1 34  ? -11.579 -5.244  -77.940  1.00 16.42 ? 127 SER   A CA  1 
ATOM   240  C  C   . SER   A 1 34  ? -11.619 -6.016  -76.625  1.00 16.44 ? 127 SER   A C   1 
ATOM   241  O  O   . SER   A 1 34  ? -10.761 -6.865  -76.389  1.00 16.91 ? 127 SER   A O   1 
ATOM   242  C  CB  . SER   A 1 34  ? -11.515 -6.183  -79.110  1.00 16.36 ? 127 SER   A CB  1 
ATOM   243  O  OG  . SER   A 1 34  ? -12.551 -7.151  -79.035  1.00 16.30 ? 127 SER   A OG  1 
ATOM   244  N  N   . PRO   A 1 35  ? -12.585 -5.722  -75.722  1.00 16.26 ? 128 PRO   A N   1 
ATOM   245  C  CA  . PRO   A 1 35  ? -12.829 -6.555  -74.546  1.00 16.66 ? 128 PRO   A CA  1 
ATOM   246  C  C   . PRO   A 1 35  ? -13.159 -8.016  -74.879  1.00 16.76 ? 128 PRO   A C   1 
ATOM   247  O  O   . PRO   A 1 35  ? -12.659 -8.884  -74.192  1.00 17.35 ? 128 PRO   A O   1 
ATOM   248  C  CB  . PRO   A 1 35  ? -14.048 -5.910  -73.863  1.00 16.44 ? 128 PRO   A CB  1 
ATOM   249  C  CG  . PRO   A 1 35  ? -14.077 -4.486  -74.372  1.00 16.47 ? 128 PRO   A CG  1 
ATOM   250  C  CD  . PRO   A 1 35  ? -13.447 -4.530  -75.748  1.00 16.28 ? 128 PRO   A CD  1 
ATOM   251  N  N   . ALA   A 1 36  ? -14.008 -8.251  -75.885  1.00 16.75 ? 129 ALA   A N   1 
ATOM   252  C  CA  . ALA   A 1 36  ? -14.449 -9.603  -76.308  1.00 17.20 ? 129 ALA   A CA  1 
ATOM   253  C  C   . ALA   A 1 36  ? -13.236 -10.460 -76.694  1.00 17.59 ? 129 ALA   A C   1 
ATOM   254  O  O   . ALA   A 1 36  ? -13.224 -11.657 -76.352  1.00 17.78 ? 129 ALA   A O   1 
ATOM   255  C  CB  . ALA   A 1 36  ? -15.432 -9.501  -77.451  1.00 17.36 ? 129 ALA   A CB  1 
ATOM   256  N  N   . LEU   A 1 37  ? -12.263 -9.878  -77.399  1.00 18.41 ? 130 LEU   A N   1 
ATOM   257  C  CA  . LEU   A 1 37  ? -11.082 -10.605 -77.944  1.00 18.54 ? 130 LEU   A CA  1 
ATOM   258  C  C   . LEU   A 1 37  ? -9.867  -10.436 -77.024  1.00 18.45 ? 130 LEU   A C   1 
ATOM   259  O  O   . LEU   A 1 37  ? -8.839  -11.079 -77.301  1.00 18.89 ? 130 LEU   A O   1 
ATOM   260  C  CB  . LEU   A 1 37  ? -10.771 -10.060 -79.340  1.00 18.71 ? 130 LEU   A CB  1 
ATOM   261  C  CG  . LEU   A 1 37  ? -11.872 -10.234 -80.386  1.00 18.96 ? 130 LEU   A CG  1 
ATOM   262  C  CD1 . LEU   A 1 37  ? -11.548 -9.432  -81.634  1.00 18.66 ? 130 LEU   A CD1 1 
ATOM   263  C  CD2 . LEU   A 1 37  ? -12.067 -11.701 -80.728  1.00 19.19 ? 130 LEU   A CD2 1 
ATOM   264  N  N   . ASN   A 1 38  ? -9.969  -9.591  -75.992  1.00 18.24 ? 131 ASN   A N   1 
ATOM   265  C  CA  . ASN   A 1 38  ? -8.818  -9.135  -75.163  1.00 17.58 ? 131 ASN   A CA  1 
ATOM   266  C  C   . ASN   A 1 38  ? -7.677  -8.755  -76.115  1.00 17.26 ? 131 ASN   A C   1 
ATOM   267  O  O   . ASN   A 1 38  ? -6.554  -9.296  -75.981  1.00 16.40 ? 131 ASN   A O   1 
ATOM   268  C  CB  . ASN   A 1 38  ? -8.419  -10.186 -74.121  1.00 17.68 ? 131 ASN   A CB  1 
ATOM   269  C  CG  . ASN   A 1 38  ? -7.342  -9.704  -73.168  1.00 17.64 ? 131 ASN   A CG  1 
ATOM   270  O  OD1 . ASN   A 1 38  ? -7.229  -8.510  -72.896  1.00 16.81 ? 131 ASN   A OD1 1 
ATOM   271  N  ND2 . ASN   A 1 38  ? -6.537  -10.626 -72.664  1.00 18.08 ? 131 ASN   A ND2 1 
ATOM   272  N  N   . LYS   A 1 39  ? -7.970  -7.877  -77.072  1.00 17.01 ? 132 LYS   A N   1 
ATOM   273  C  CA  . LYS   A 1 39  ? -7.061  -7.585  -78.204  1.00 17.27 ? 132 LYS   A CA  1 
ATOM   274  C  C   . LYS   A 1 39  ? -6.980  -6.074  -78.429  1.00 17.23 ? 132 LYS   A C   1 
ATOM   275  O  O   . LYS   A 1 39  ? -8.037  -5.435  -78.606  1.00 15.70 ? 132 LYS   A O   1 
ATOM   276  C  CB  . LYS   A 1 39  ? -7.542  -8.324  -79.455  1.00 17.99 ? 132 LYS   A CB  1 
ATOM   277  C  CG  . LYS   A 1 39  ? -6.566  -8.327  -80.621  1.00 18.34 ? 132 LYS   A CG  1 
ATOM   278  C  CD  . LYS   A 1 39  ? -6.972  -9.278  -81.715  1.00 18.75 ? 132 LYS   A CD  1 
ATOM   279  C  CE  . LYS   A 1 39  ? -6.016  -9.278  -82.888  1.00 19.81 ? 132 LYS   A CE  1 
ATOM   280  N  NZ  . LYS   A 1 39  ? -6.402  -10.296 -83.895  1.00 20.29 ? 132 LYS   A NZ  1 
ATOM   281  N  N   . MET   A 1 40  ? -5.752  -5.550  -78.390  1.00 17.07 ? 133 MET   A N   1 
ATOM   282  C  CA  A MET   A 1 40  ? -5.422  -4.150  -78.762  0.42 17.35 ? 133 MET   A CA  1 
ATOM   283  C  CA  B MET   A 1 40  ? -5.418  -4.152  -78.760  0.58 17.08 ? 133 MET   A CA  1 
ATOM   284  C  C   . MET   A 1 40  ? -5.160  -4.095  -80.272  1.00 17.61 ? 133 MET   A C   1 
ATOM   285  O  O   . MET   A 1 40  ? -4.337  -4.900  -80.758  1.00 17.70 ? 133 MET   A O   1 
ATOM   286  C  CB  A MET   A 1 40  ? -4.181  -3.655  -78.012  0.42 17.52 ? 133 MET   A CB  1 
ATOM   287  C  CB  B MET   A 1 40  ? -4.173  -3.678  -78.000  0.58 16.96 ? 133 MET   A CB  1 
ATOM   288  C  CG  A MET   A 1 40  ? -3.696  -2.289  -78.470  0.42 17.67 ? 133 MET   A CG  1 
ATOM   289  C  CG  B MET   A 1 40  ? -3.704  -2.287  -78.381  0.58 16.85 ? 133 MET   A CG  1 
ATOM   290  S  SD  A MET   A 1 40  ? -2.147  -1.803  -77.678  0.42 18.15 ? 133 MET   A SD  1 
ATOM   291  S  SD  B MET   A 1 40  ? -4.959  -1.014  -78.106  0.58 17.00 ? 133 MET   A SD  1 
ATOM   292  C  CE  A MET   A 1 40  ? -2.774  -1.152  -76.130  0.42 18.17 ? 133 MET   A CE  1 
ATOM   293  C  CE  B MET   A 1 40  ? -4.768  -0.746  -76.345  0.58 16.78 ? 133 MET   A CE  1 
ATOM   294  N  N   . PHE   A 1 41  ? -5.850  -3.192  -80.967  1.00 17.54 ? 134 PHE   A N   1 
ATOM   295  C  CA  . PHE   A 1 41  ? -5.613  -2.853  -82.391  1.00 17.84 ? 134 PHE   A CA  1 
ATOM   296  C  C   . PHE   A 1 41  ? -4.954  -1.475  -82.398  1.00 17.66 ? 134 PHE   A C   1 
ATOM   297  O  O   . PHE   A 1 41  ? -5.558  -0.553  -81.846  1.00 17.53 ? 134 PHE   A O   1 
ATOM   298  C  CB  . PHE   A 1 41  ? -6.922  -2.871  -83.183  1.00 17.77 ? 134 PHE   A CB  1 
ATOM   299  C  CG  . PHE   A 1 41  ? -7.611  -4.211  -83.223  1.00 18.25 ? 134 PHE   A CG  1 
ATOM   300  C  CD1 . PHE   A 1 41  ? -8.306  -4.687  -82.119  1.00 18.01 ? 134 PHE   A CD1 1 
ATOM   301  C  CD2 . PHE   A 1 41  ? -7.559  -5.004  -84.362  1.00 18.09 ? 134 PHE   A CD2 1 
ATOM   302  C  CE1 . PHE   A 1 41  ? -8.928  -5.926  -82.153  1.00 18.33 ? 134 PHE   A CE1 1 
ATOM   303  C  CE2 . PHE   A 1 41  ? -8.192  -6.238  -84.395  1.00 18.39 ? 134 PHE   A CE2 1 
ATOM   304  C  CZ  . PHE   A 1 41  ? -8.878  -6.697  -83.294  1.00 18.33 ? 134 PHE   A CZ  1 
ATOM   305  N  N   . CYS   A 1 42  ? -3.745  -1.345  -82.946  1.00 18.53 ? 135 CYS   A N   1 
ATOM   306  C  CA  . CYS   A 1 42  ? -2.969  -0.078  -82.900  1.00 19.32 ? 135 CYS   A CA  1 
ATOM   307  C  C   . CYS   A 1 42  ? -2.177  0.126   -84.195  1.00 20.15 ? 135 CYS   A C   1 
ATOM   308  O  O   . CYS   A 1 42  ? -1.980  -0.850  -84.933  1.00 19.95 ? 135 CYS   A O   1 
ATOM   309  C  CB  . CYS   A 1 42  ? -2.038  -0.054  -81.696  1.00 20.19 ? 135 CYS   A CB  1 
ATOM   310  S  SG  . CYS   A 1 42  ? -0.784  -1.361  -81.703  1.00 20.60 ? 135 CYS   A SG  1 
ATOM   311  N  N   . GLN   A 1 43  ? -1.760  1.366   -84.450  1.00 20.74 ? 136 GLN   A N   1 
ATOM   312  C  CA  . GLN   A 1 43  ? -0.971  1.762   -85.643  1.00 21.84 ? 136 GLN   A CA  1 
ATOM   313  C  C   . GLN   A 1 43  ? 0.520   1.725   -85.301  1.00 22.17 ? 136 GLN   A C   1 
ATOM   314  O  O   . GLN   A 1 43  ? 0.874   1.992   -84.125  1.00 21.97 ? 136 GLN   A O   1 
ATOM   315  C  CB  . GLN   A 1 43  ? -1.370  3.164   -86.105  1.00 23.12 ? 136 GLN   A CB  1 
ATOM   316  C  CG  . GLN   A 1 43  ? -2.796  3.253   -86.627  1.00 24.51 ? 136 GLN   A CG  1 
ATOM   317  C  CD  . GLN   A 1 43  ? -3.141  4.650   -87.084  1.00 25.57 ? 136 GLN   A CD  1 
ATOM   318  O  OE1 . GLN   A 1 43  ? -2.378  5.592   -86.894  1.00 27.33 ? 136 GLN   A OE1 1 
ATOM   319  N  NE2 . GLN   A 1 43  ? -4.300  4.796   -87.703  1.00 27.48 ? 136 GLN   A NE2 1 
ATOM   320  N  N   . LEU   A 1 44  ? 1.345   1.413   -86.305  1.00 22.43 ? 137 LEU   A N   1 
ATOM   321  C  CA  . LEU   A 1 44  ? 2.831   1.447   -86.254  1.00 22.75 ? 137 LEU   A CA  1 
ATOM   322  C  C   . LEU   A 1 44  ? 3.306   2.773   -85.643  1.00 22.15 ? 137 LEU   A C   1 
ATOM   323  O  O   . LEU   A 1 44  ? 2.922   3.845   -86.162  1.00 20.62 ? 137 LEU   A O   1 
ATOM   324  C  CB  . LEU   A 1 44  ? 3.351   1.279   -87.685  1.00 24.04 ? 137 LEU   A CB  1 
ATOM   325  C  CG  . LEU   A 1 44  ? 4.868   1.245   -87.853  1.00 24.93 ? 137 LEU   A CG  1 
ATOM   326  C  CD1 . LEU   A 1 44  ? 5.440   -0.027  -87.256  1.00 24.78 ? 137 LEU   A CD1 1 
ATOM   327  C  CD2 . LEU   A 1 44  ? 5.248   1.363   -89.325  1.00 25.35 ? 137 LEU   A CD2 1 
ATOM   328  N  N   . ALA   A 1 45  ? 4.085   2.694   -84.559  1.00 21.79 ? 138 ALA   A N   1 
ATOM   329  C  CA  . ALA   A 1 45  ? 4.833   3.816   -83.941  1.00 22.01 ? 138 ALA   A CA  1 
ATOM   330  C  C   . ALA   A 1 45  ? 3.892   4.888   -83.377  1.00 22.60 ? 138 ALA   A C   1 
ATOM   331  O  O   . ALA   A 1 45  ? 4.387   5.996   -83.113  1.00 24.25 ? 138 ALA   A O   1 
ATOM   332  C  CB  . ALA   A 1 45  ? 5.776   4.415   -84.957  1.00 22.40 ? 138 ALA   A CB  1 
ATOM   333  N  N   . LYS   A 1 46  ? 2.600   4.595   -83.203  1.00 21.64 ? 139 LYS   A N   1 
ATOM   334  C  CA  . LYS   A 1 46  ? 1.615   5.561   -82.644  1.00 21.90 ? 139 LYS   A CA  1 
ATOM   335  C  C   . LYS   A 1 46  ? 1.375   5.235   -81.168  1.00 20.73 ? 139 LYS   A C   1 
ATOM   336  O  O   . LYS   A 1 46  ? 1.585   4.075   -80.766  1.00 18.43 ? 139 LYS   A O   1 
ATOM   337  C  CB  . LYS   A 1 46  ? 0.306   5.535   -83.434  1.00 23.10 ? 139 LYS   A CB  1 
ATOM   338  C  CG  . LYS   A 1 46  ? 0.422   6.014   -84.875  1.00 24.98 ? 139 LYS   A CG  1 
ATOM   339  C  CD  . LYS   A 1 46  ? 0.758   7.484   -85.013  1.00 26.47 ? 139 LYS   A CD  1 
ATOM   340  C  CE  . LYS   A 1 46  ? 0.993   7.895   -86.451  1.00 27.87 ? 139 LYS   A CE  1 
ATOM   341  N  NZ  . LYS   A 1 46  ? -0.183  7.587   -87.299  1.00 29.18 ? 139 LYS   A NZ  1 
ATOM   342  N  N   . THR   A 1 47  ? 0.953   6.238   -80.396  1.00 20.33 ? 140 THR   A N   1 
ATOM   343  C  CA  . THR   A 1 47  ? 0.670   6.116   -78.946  1.00 19.89 ? 140 THR   A CA  1 
ATOM   344  C  C   . THR   A 1 47  ? -0.345  4.988   -78.732  1.00 19.86 ? 140 THR   A C   1 
ATOM   345  O  O   . THR   A 1 47  ? -1.424  5.021   -79.354  1.00 20.44 ? 140 THR   A O   1 
ATOM   346  C  CB  . THR   A 1 47  ? 0.183   7.448   -78.368  1.00 19.96 ? 140 THR   A CB  1 
ATOM   347  O  OG1 . THR   A 1 47  ? 1.155   8.439   -78.702  1.00 20.12 ? 140 THR   A OG1 1 
ATOM   348  C  CG2 . THR   A 1 47  ? -0.003  7.400   -76.869  1.00 20.30 ? 140 THR   A CG2 1 
ATOM   349  N  N   A CYS   A 1 48  ? 0.001   4.031   -77.870  0.50 19.16 ? 141 CYS   A N   1 
ATOM   350  N  N   B CYS   A 1 48  ? 0.024   4.001   -77.908  0.50 20.38 ? 141 CYS   A N   1 
ATOM   351  C  CA  A CYS   A 1 48  ? -0.869  2.913   -77.425  0.50 18.45 ? 141 CYS   A CA  1 
ATOM   352  C  CA  B CYS   A 1 48  ? -0.850  2.907   -77.404  0.50 20.34 ? 141 CYS   A CA  1 
ATOM   353  C  C   A CYS   A 1 48  ? -0.993  2.979   -75.906  0.50 18.42 ? 141 CYS   A C   1 
ATOM   354  C  C   B CYS   A 1 48  ? -0.959  3.022   -75.891  0.50 19.49 ? 141 CYS   A C   1 
ATOM   355  O  O   A CYS   A 1 48  ? -0.181  2.381   -75.207  0.50 18.08 ? 141 CYS   A O   1 
ATOM   356  O  O   B CYS   A 1 48  ? -0.110  2.492   -75.181  0.50 19.02 ? 141 CYS   A O   1 
ATOM   357  C  CB  A CYS   A 1 48  ? -0.290  1.571   -77.855  0.50 18.17 ? 141 CYS   A CB  1 
ATOM   358  C  CB  B CYS   A 1 48  ? -0.286  1.527   -77.707  0.50 21.39 ? 141 CYS   A CB  1 
ATOM   359  S  SG  A CYS   A 1 48  ? -1.390  0.170   -77.531  0.50 17.64 ? 141 CYS   A SG  1 
ATOM   360  S  SG  B CYS   A 1 48  ? -0.232  1.138   -79.470  0.50 23.79 ? 141 CYS   A SG  1 
ATOM   361  N  N   . PRO   A 1 49  ? -1.972  3.740   -75.357  1.00 18.56 ? 142 PRO   A N   1 
ATOM   362  C  CA  . PRO   A 1 49  ? -2.144  3.857   -73.911  1.00 18.44 ? 142 PRO   A CA  1 
ATOM   363  C  C   . PRO   A 1 49  ? -2.505  2.507   -73.279  1.00 18.44 ? 142 PRO   A C   1 
ATOM   364  O  O   . PRO   A 1 49  ? -3.425  1.852   -73.754  1.00 18.44 ? 142 PRO   A O   1 
ATOM   365  C  CB  . PRO   A 1 49  ? -3.298  4.862   -73.745  1.00 18.40 ? 142 PRO   A CB  1 
ATOM   366  C  CG  . PRO   A 1 49  ? -3.398  5.558   -75.085  1.00 18.39 ? 142 PRO   A CG  1 
ATOM   367  C  CD  . PRO   A 1 49  ? -2.972  4.520   -76.099  1.00 18.54 ? 142 PRO   A CD  1 
ATOM   368  N  N   . VAL   A 1 50  ? -1.752  2.116   -72.252  1.00 17.75 ? 143 VAL   A N   1 
ATOM   369  C  CA  . VAL   A 1 50  ? -2.051  0.930   -71.401  1.00 17.64 ? 143 VAL   A CA  1 
ATOM   370  C  C   . VAL   A 1 50  ? -2.138  1.427   -69.957  1.00 17.01 ? 143 VAL   A C   1 
ATOM   371  O  O   . VAL   A 1 50  ? -1.200  2.112   -69.506  1.00 16.67 ? 143 VAL   A O   1 
ATOM   372  C  CB  . VAL   A 1 50  ? -1.013  -0.196  -71.579  1.00 17.27 ? 143 VAL   A CB  1 
ATOM   373  C  CG1 . VAL   A 1 50  ? -1.311  -1.381  -70.672  1.00 17.41 ? 143 VAL   A CG1 1 
ATOM   374  C  CG2 . VAL   A 1 50  ? -0.925  -0.657  -73.027  1.00 17.69 ? 143 VAL   A CG2 1 
ATOM   375  N  N   . GLN   A 1 51  ? -3.245  1.119   -69.282  1.00 16.83 ? 144 GLN   A N   1 
ATOM   376  C  CA  . GLN   A 1 51  ? -3.529  1.587   -67.905  1.00 16.96 ? 144 GLN   A CA  1 
ATOM   377  C  C   . GLN   A 1 51  ? -3.175  0.488   -66.902  1.00 16.99 ? 144 GLN   A C   1 
ATOM   378  O  O   . GLN   A 1 51  ? -3.587  -0.673  -67.113  1.00 16.54 ? 144 GLN   A O   1 
ATOM   379  C  CB  . GLN   A 1 51  ? -4.998  1.974   -67.759  1.00 17.01 ? 144 GLN   A CB  1 
ATOM   380  C  CG  . GLN   A 1 51  ? -5.440  3.060   -68.722  1.00 16.90 ? 144 GLN   A CG  1 
ATOM   381  C  CD  . GLN   A 1 51  ? -6.925  3.299   -68.642  1.00 17.26 ? 144 GLN   A CD  1 
ATOM   382  O  OE1 . GLN   A 1 51  ? -7.657  2.555   -67.991  1.00 16.86 ? 144 GLN   A OE1 1 
ATOM   383  N  NE2 . GLN   A 1 51  ? -7.384  4.337   -69.324  1.00 17.32 ? 144 GLN   A NE2 1 
ATOM   384  N  N   . LEU   A 1 52  ? -2.448  0.860   -65.848  1.00 16.74 ? 145 LEU   A N   1 
ATOM   385  C  CA  . LEU   A 1 52  ? -2.181  -0.001  -64.670  1.00 17.24 ? 145 LEU   A CA  1 
ATOM   386  C  C   . LEU   A 1 52  ? -3.186  0.387   -63.583  1.00 17.50 ? 145 LEU   A C   1 
ATOM   387  O  O   . LEU   A 1 52  ? -3.219  1.579   -63.223  1.00 17.71 ? 145 LEU   A O   1 
ATOM   388  C  CB  . LEU   A 1 52  ? -0.741  0.204   -64.190  1.00 17.03 ? 145 LEU   A CB  1 
ATOM   389  C  CG  . LEU   A 1 52  ? 0.335   0.221   -65.275  1.00 17.01 ? 145 LEU   A CG  1 
ATOM   390  C  CD1 . LEU   A 1 52  ? 1.709   0.421   -64.652  1.00 16.93 ? 145 LEU   A CD1 1 
ATOM   391  C  CD2 . LEU   A 1 52  ? 0.300   -1.055  -66.104  1.00 16.96 ? 145 LEU   A CD2 1 
ATOM   392  N  N   . TRP   A 1 53  ? -3.984  -0.574  -63.116  1.00 17.90 ? 146 TRP   A N   1 
ATOM   393  C  CA  . TRP   A 1 53  ? -4.931  -0.413  -61.979  1.00 18.62 ? 146 TRP   A CA  1 
ATOM   394  C  C   . TRP   A 1 53  ? -4.446  -1.283  -60.814  1.00 18.75 ? 146 TRP   A C   1 
ATOM   395  O  O   . TRP   A 1 53  ? -4.171  -2.476  -61.053  1.00 17.96 ? 146 TRP   A O   1 
ATOM   396  C  CB  . TRP   A 1 53  ? -6.360  -0.782  -62.395  1.00 19.24 ? 146 TRP   A CB  1 
ATOM   397  C  CG  . TRP   A 1 53  ? -6.975  0.135   -63.408  1.00 19.61 ? 146 TRP   A CG  1 
ATOM   398  C  CD1 . TRP   A 1 53  ? -6.626  0.249   -64.721  1.00 19.84 ? 146 TRP   A CD1 1 
ATOM   399  C  CD2 . TRP   A 1 53  ? -8.069  1.050   -63.206  1.00 20.25 ? 146 TRP   A CD2 1 
ATOM   400  N  NE1 . TRP   A 1 53  ? -7.419  1.170   -65.347  1.00 19.99 ? 146 TRP   A NE1 1 
ATOM   401  C  CE2 . TRP   A 1 53  ? -8.313  1.680   -64.445  1.00 20.25 ? 146 TRP   A CE2 1 
ATOM   402  C  CE3 . TRP   A 1 53  ? -8.868  1.398   -62.108  1.00 20.83 ? 146 TRP   A CE3 1 
ATOM   403  C  CZ2 . TRP   A 1 53  ? -9.313  2.639   -64.611  1.00 21.09 ? 146 TRP   A CZ2 1 
ATOM   404  C  CZ3 . TRP   A 1 53  ? -9.861  2.339   -62.274  1.00 20.61 ? 146 TRP   A CZ3 1 
ATOM   405  C  CH2 . TRP   A 1 53  ? -10.079 2.950   -63.510  1.00 21.28 ? 146 TRP   A CH2 1 
ATOM   406  N  N   . VAL   A 1 54  ? -4.317  -0.696  -59.619  1.00 19.03 ? 147 VAL   A N   1 
ATOM   407  C  CA  . VAL   A 1 54  ? -3.955  -1.409  -58.354  1.00 19.95 ? 147 VAL   A CA  1 
ATOM   408  C  C   . VAL   A 1 54  ? -4.971  -1.016  -57.272  1.00 20.73 ? 147 VAL   A C   1 
ATOM   409  O  O   . VAL   A 1 54  ? -5.491  0.111   -57.342  1.00 20.99 ? 147 VAL   A O   1 
ATOM   410  C  CB  . VAL   A 1 54  ? -2.507  -1.107  -57.918  1.00 19.67 ? 147 VAL   A CB  1 
ATOM   411  C  CG1 . VAL   A 1 54  ? -1.493  -1.688  -58.892  1.00 19.83 ? 147 VAL   A CG1 1 
ATOM   412  C  CG2 . VAL   A 1 54  ? -2.261  0.382   -57.718  1.00 19.67 ? 147 VAL   A CG2 1 
ATOM   413  N  N   . ASP   A 1 55  ? -5.242  -1.917  -56.322  1.00 21.41 ? 148 ASP   A N   1 
ATOM   414  C  CA  . ASP   A 1 55  ? -6.123  -1.644  -55.154  1.00 22.87 ? 148 ASP   A CA  1 
ATOM   415  C  C   . ASP   A 1 55  ? -5.292  -0.981  -54.049  1.00 23.73 ? 148 ASP   A C   1 
ATOM   416  O  O   . ASP   A 1 55  ? -5.887  -0.277  -53.216  1.00 23.37 ? 148 ASP   A O   1 
ATOM   417  C  CB  . ASP   A 1 55  ? -6.829  -2.911  -54.663  1.00 23.15 ? 148 ASP   A CB  1 
ATOM   418  C  CG  . ASP   A 1 55  ? -7.744  -3.553  -55.694  1.00 23.64 ? 148 ASP   A CG  1 
ATOM   419  O  OD1 . ASP   A 1 55  ? -8.330  -2.807  -56.506  1.00 24.16 ? 148 ASP   A OD1 1 
ATOM   420  O  OD2 . ASP   A 1 55  ? -7.852  -4.798  -55.683  1.00 23.99 ? 148 ASP   A OD2 1 
ATOM   421  N  N   . SER   A 1 56  ? -3.968  -1.184  -54.050  1.00 25.20 ? 149 SER   A N   1 
ATOM   422  C  CA  . SER   A 1 56  ? -3.022  -0.571  -53.077  1.00 26.07 ? 149 SER   A CA  1 
ATOM   423  C  C   . SER   A 1 56  ? -1.671  -0.291  -53.745  1.00 25.60 ? 149 SER   A C   1 
ATOM   424  O  O   . SER   A 1 56  ? -1.245  -1.089  -54.603  1.00 23.46 ? 149 SER   A O   1 
ATOM   425  C  CB  . SER   A 1 56  ? -2.861  -1.430  -51.853  1.00 26.91 ? 149 SER   A CB  1 
ATOM   426  O  OG  . SER   A 1 56  ? -2.293  -2.680  -52.189  1.00 29.74 ? 149 SER   A OG  1 
ATOM   427  N  N   . THR   A 1 57  ? -1.025  0.804   -53.341  1.00 25.18 ? 150 THR   A N   1 
ATOM   428  C  CA  . THR   A 1 57  ? 0.229   1.327   -53.943  1.00 25.86 ? 150 THR   A CA  1 
ATOM   429  C  C   . THR   A 1 57  ? 1.334   0.285   -53.783  1.00 25.33 ? 150 THR   A C   1 
ATOM   430  O  O   . THR   A 1 57  ? 1.655   -0.120  -52.668  1.00 24.99 ? 150 THR   A O   1 
ATOM   431  C  CB  . THR   A 1 57  ? 0.602   2.677   -53.321  1.00 26.85 ? 150 THR   A CB  1 
ATOM   432  O  OG1 . THR   A 1 57  ? -0.587  3.467   -53.267  1.00 28.81 ? 150 THR   A OG1 1 
ATOM   433  C  CG2 . THR   A 1 57  ? 1.672   3.414   -54.094  1.00 26.51 ? 150 THR   A CG2 1 
ATOM   434  N  N   . PRO   A 1 58  ? 1.927   -0.207  -54.893  1.00 24.15 ? 151 PRO   A N   1 
ATOM   435  C  CA  . PRO   A 1 58  ? 3.145   -1.015  -54.823  1.00 24.38 ? 151 PRO   A CA  1 
ATOM   436  C  C   . PRO   A 1 58  ? 4.274   -0.272  -54.110  1.00 23.88 ? 151 PRO   A C   1 
ATOM   437  O  O   . PRO   A 1 58  ? 4.268   0.955   -54.043  1.00 23.94 ? 151 PRO   A O   1 
ATOM   438  C  CB  . PRO   A 1 58  ? 3.528   -1.266  -56.290  1.00 24.29 ? 151 PRO   A CB  1 
ATOM   439  C  CG  . PRO   A 1 58  ? 2.246   -1.040  -57.070  1.00 24.38 ? 151 PRO   A CG  1 
ATOM   440  C  CD  . PRO   A 1 58  ? 1.444   -0.037  -56.271  1.00 24.62 ? 151 PRO   A CD  1 
ATOM   441  N  N   . PRO   A 1 59  ? 5.285   -0.984  -53.568  1.00 24.25 ? 152 PRO   A N   1 
ATOM   442  C  CA  . PRO   A 1 59  ? 6.342   -0.345  -52.785  1.00 24.67 ? 152 PRO   A CA  1 
ATOM   443  C  C   . PRO   A 1 59  ? 7.309   0.470   -53.639  1.00 24.05 ? 152 PRO   A C   1 
ATOM   444  O  O   . PRO   A 1 59  ? 7.294   0.371   -54.865  1.00 22.40 ? 152 PRO   A O   1 
ATOM   445  C  CB  . PRO   A 1 59  ? 7.067   -1.528  -52.131  1.00 24.54 ? 152 PRO   A CB  1 
ATOM   446  C  CG  . PRO   A 1 59  ? 6.843   -2.677  -53.087  1.00 24.99 ? 152 PRO   A CG  1 
ATOM   447  C  CD  . PRO   A 1 59  ? 5.467   -2.437  -53.676  1.00 24.46 ? 152 PRO   A CD  1 
ATOM   448  N  N   . PRO   A 1 60  ? 8.178   1.299   -53.013  1.00 23.73 ? 153 PRO   A N   1 
ATOM   449  C  CA  . PRO   A 1 60  ? 9.180   2.067   -53.751  1.00 23.34 ? 153 PRO   A CA  1 
ATOM   450  C  C   . PRO   A 1 60  ? 10.069  1.159   -54.612  1.00 22.01 ? 153 PRO   A C   1 
ATOM   451  O  O   . PRO   A 1 60  ? 10.360  0.054   -54.181  1.00 22.84 ? 153 PRO   A O   1 
ATOM   452  C  CB  . PRO   A 1 60  ? 10.014  2.746   -52.652  1.00 23.99 ? 153 PRO   A CB  1 
ATOM   453  C  CG  . PRO   A 1 60  ? 9.073   2.807   -51.460  1.00 24.34 ? 153 PRO   A CG  1 
ATOM   454  C  CD  . PRO   A 1 60  ? 8.241   1.544   -51.561  1.00 24.11 ? 153 PRO   A CD  1 
ATOM   455  N  N   . GLY   A 1 61  ? 10.460  1.638   -55.796  1.00 20.84 ? 154 GLY   A N   1 
ATOM   456  C  CA  . GLY   A 1 61  ? 11.383  0.935   -56.711  1.00 19.81 ? 154 GLY   A CA  1 
ATOM   457  C  C   . GLY   A 1 61  ? 10.688  -0.132  -57.542  1.00 18.89 ? 154 GLY   A C   1 
ATOM   458  O  O   . GLY   A 1 61  ? 11.394  -0.820  -58.309  1.00 18.63 ? 154 GLY   A O   1 
ATOM   459  N  N   . THR   A 1 62  ? 9.363   -0.283  -57.413  1.00 17.84 ? 155 THR   A N   1 
ATOM   460  C  CA  . THR   A 1 62  ? 8.549   -1.212  -58.247  1.00 16.98 ? 155 THR   A CA  1 
ATOM   461  C  C   . THR   A 1 62  ? 8.760   -0.825  -59.714  1.00 16.40 ? 155 THR   A C   1 
ATOM   462  O  O   . THR   A 1 62  ? 8.912   0.382   -59.986  1.00 16.01 ? 155 THR   A O   1 
ATOM   463  C  CB  . THR   A 1 62  ? 7.059   -1.186  -57.875  1.00 17.33 ? 155 THR   A CB  1 
ATOM   464  O  OG1 . THR   A 1 62  ? 6.903   -1.712  -56.558  1.00 17.58 ? 155 THR   A OG1 1 
ATOM   465  C  CG2 . THR   A 1 62  ? 6.189   -1.982  -58.825  1.00 17.22 ? 155 THR   A CG2 1 
ATOM   466  N  N   . ARG   A 1 63  ? 8.795   -1.816  -60.607  1.00 15.81 ? 156 ARG   A N   1 
ATOM   467  C  CA  . ARG   A 1 63  ? 9.069   -1.615  -62.052  1.00 15.82 ? 156 ARG   A CA  1 
ATOM   468  C  C   . ARG   A 1 63  ? 7.978   -2.297  -62.878  1.00 15.34 ? 156 ARG   A C   1 
ATOM   469  O  O   . ARG   A 1 63  ? 7.312   -3.226  -62.358  1.00 15.17 ? 156 ARG   A O   1 
ATOM   470  C  CB  . ARG   A 1 63  ? 10.483  -2.103  -62.378  1.00 16.14 ? 156 ARG   A CB  1 
ATOM   471  C  CG  . ARG   A 1 63  ? 11.540  -1.030  -62.161  1.00 16.37 ? 156 ARG   A CG  1 
ATOM   472  C  CD  . ARG   A 1 63  ? 12.890  -1.562  -61.729  1.00 16.50 ? 156 ARG   A CD  1 
ATOM   473  N  NE  . ARG   A 1 63  ? 13.520  -2.519  -62.640  1.00 16.70 ? 156 ARG   A NE  1 
ATOM   474  C  CZ  . ARG   A 1 63  ? 14.358  -2.225  -63.636  1.00 16.53 ? 156 ARG   A CZ  1 
ATOM   475  N  NH1 . ARG   A 1 63  ? 14.643  -0.972  -63.944  1.00 16.72 ? 156 ARG   A NH1 1 
ATOM   476  N  NH2 . ARG   A 1 63  ? 14.892  -3.203  -64.349  1.00 16.57 ? 156 ARG   A NH2 1 
ATOM   477  N  N   . VAL   A 1 64  ? 7.777   -1.803  -64.101  1.00 14.72 ? 157 VAL   A N   1 
ATOM   478  C  CA  . VAL   A 1 64  ? 6.712   -2.271  -65.032  1.00 14.62 ? 157 VAL   A CA  1 
ATOM   479  C  C   . VAL   A 1 64  ? 7.386   -2.680  -66.341  1.00 14.71 ? 157 VAL   A C   1 
ATOM   480  O  O   . VAL   A 1 64  ? 7.916   -1.785  -67.039  1.00 14.51 ? 157 VAL   A O   1 
ATOM   481  C  CB  . VAL   A 1 64  ? 5.631   -1.201  -65.269  1.00 14.65 ? 157 VAL   A CB  1 
ATOM   482  C  CG1 . VAL   A 1 64  ? 4.452   -1.785  -66.038  1.00 14.80 ? 157 VAL   A CG1 1 
ATOM   483  C  CG2 . VAL   A 1 64  ? 5.161   -0.560  -63.972  1.00 14.74 ? 157 VAL   A CG2 1 
ATOM   484  N  N   . ARG   A 1 65  ? 7.344   -3.977  -66.651  1.00 14.50 ? 158 ARG   A N   1 
ATOM   485  C  CA  . ARG   A 1 65  ? 8.021   -4.584  -67.822  1.00 14.50 ? 158 ARG   A CA  1 
ATOM   486  C  C   . ARG   A 1 65  ? 6.967   -5.008  -68.853  1.00 14.17 ? 158 ARG   A C   1 
ATOM   487  O  O   . ARG   A 1 65  ? 5.898   -5.520  -68.457  1.00 13.93 ? 158 ARG   A O   1 
ATOM   488  C  CB  . ARG   A 1 65  ? 8.905   -5.752  -67.373  1.00 14.41 ? 158 ARG   A CB  1 
ATOM   489  C  CG  . ARG   A 1 65  ? 9.688   -6.409  -68.501  1.00 14.72 ? 158 ARG   A CG  1 
ATOM   490  C  CD  . ARG   A 1 65  ? 10.549  -7.558  -68.016  1.00 14.62 ? 158 ARG   A CD  1 
ATOM   491  N  NE  . ARG   A 1 65  ? 11.381  -7.120  -66.910  1.00 14.70 ? 158 ARG   A NE  1 
ATOM   492  C  CZ  . ARG   A 1 65  ? 12.542  -6.479  -67.028  1.00 14.88 ? 158 ARG   A CZ  1 
ATOM   493  N  NH1 . ARG   A 1 65  ? 13.056  -6.216  -68.218  1.00 14.53 ? 158 ARG   A NH1 1 
ATOM   494  N  NH2 . ARG   A 1 65  ? 13.201  -6.114  -65.942  1.00 15.24 ? 158 ARG   A NH2 1 
ATOM   495  N  N   . ALA   A 1 66  ? 7.275   -4.785  -70.133  1.00 14.47 ? 159 ALA   A N   1 
ATOM   496  C  CA  . ALA   A 1 66  ? 6.469   -5.201  -71.298  1.00 14.73 ? 159 ALA   A CA  1 
ATOM   497  C  C   . ALA   A 1 66  ? 7.333   -6.108  -72.184  1.00 15.25 ? 159 ALA   A C   1 
ATOM   498  O  O   . ALA   A 1 66  ? 8.519   -5.776  -72.418  1.00 14.37 ? 159 ALA   A O   1 
ATOM   499  C  CB  . ALA   A 1 66  ? 5.962   -3.989  -72.040  1.00 14.85 ? 159 ALA   A CB  1 
ATOM   500  N  N   . MET   A 1 67  ? 6.764   -7.236  -72.609  1.00 15.76 ? 160 MET   A N   1 
ATOM   501  C  CA  . MET   A 1 67  ? 7.439   -8.258  -73.452  1.00 16.23 ? 160 MET   A CA  1 
ATOM   502  C  C   . MET   A 1 67  ? 6.395   -8.866  -74.390  1.00 16.50 ? 160 MET   A C   1 
ATOM   503  O  O   . MET   A 1 67  ? 5.272   -9.148  -73.930  1.00 16.35 ? 160 MET   A O   1 
ATOM   504  C  CB  . MET   A 1 67  ? 8.073   -9.356  -72.591  1.00 16.56 ? 160 MET   A CB  1 
ATOM   505  C  CG  . MET   A 1 67  ? 8.845   -10.395 -73.391  1.00 17.21 ? 160 MET   A CG  1 
ATOM   506  S  SD  . MET   A 1 67  ? 9.391   -11.798 -72.383  1.00 17.72 ? 160 MET   A SD  1 
ATOM   507  C  CE  . MET   A 1 67  ? 10.565  -11.003 -71.286  1.00 18.21 ? 160 MET   A CE  1 
ATOM   508  N  N   . ALA   A 1 68  ? 6.754   -9.027  -75.662  1.00 16.79 ? 161 ALA   A N   1 
ATOM   509  C  CA  . ALA   A 1 68  ? 5.918   -9.664  -76.703  1.00 16.97 ? 161 ALA   A CA  1 
ATOM   510  C  C   . ALA   A 1 68  ? 6.341   -11.128 -76.846  1.00 17.60 ? 161 ALA   A C   1 
ATOM   511  O  O   . ALA   A 1 68  ? 7.555   -11.409 -76.803  1.00 17.05 ? 161 ALA   A O   1 
ATOM   512  C  CB  . ALA   A 1 68  ? 6.048   -8.919  -78.006  1.00 16.68 ? 161 ALA   A CB  1 
ATOM   513  N  N   . ILE   A 1 69  ? 5.366   -12.026 -76.973  1.00 18.11 ? 162 ILE   A N   1 
ATOM   514  C  CA  . ILE   A 1 69  ? 5.590   -13.454 -77.338  1.00 18.89 ? 162 ILE   A CA  1 
ATOM   515  C  C   . ILE   A 1 69  ? 4.604   -13.791 -78.458  1.00 19.99 ? 162 ILE   A C   1 
ATOM   516  O  O   . ILE   A 1 69  ? 3.561   -13.116 -78.547  1.00 19.65 ? 162 ILE   A O   1 
ATOM   517  C  CB  . ILE   A 1 69  ? 5.451   -14.388 -76.115  1.00 18.92 ? 162 ILE   A CB  1 
ATOM   518  C  CG1 . ILE   A 1 69  ? 4.011   -14.490 -75.598  1.00 19.43 ? 162 ILE   A CG1 1 
ATOM   519  C  CG2 . ILE   A 1 69  ? 6.411   -13.969 -75.010  1.00 18.71 ? 162 ILE   A CG2 1 
ATOM   520  C  CD1 . ILE   A 1 69  ? 3.778   -15.671 -74.678  1.00 19.77 ? 162 ILE   A CD1 1 
ATOM   521  N  N   . TYR   A 1 70  ? 4.924   -14.778 -79.294  1.00 20.85 ? 163 TYR   A N   1 
ATOM   522  C  CA  . TYR   A 1 70  ? 3.970   -15.322 -80.294  1.00 21.18 ? 163 TYR   A CA  1 
ATOM   523  C  C   . TYR   A 1 70  ? 2.888   -16.086 -79.528  1.00 22.21 ? 163 TYR   A C   1 
ATOM   524  O  O   . TYR   A 1 70  ? 3.221   -16.789 -78.548  1.00 21.08 ? 163 TYR   A O   1 
ATOM   525  C  CB  . TYR   A 1 70  ? 4.709   -16.125 -81.368  1.00 20.48 ? 163 TYR   A CB  1 
ATOM   526  C  CG  . TYR   A 1 70  ? 5.500   -15.247 -82.302  1.00 20.27 ? 163 TYR   A CG  1 
ATOM   527  C  CD1 . TYR   A 1 70  ? 4.859   -14.322 -83.113  1.00 19.87 ? 163 TYR   A CD1 1 
ATOM   528  C  CD2 . TYR   A 1 70  ? 6.885   -15.301 -82.349  1.00 19.86 ? 163 TYR   A CD2 1 
ATOM   529  C  CE1 . TYR   A 1 70  ? 5.566   -13.489 -83.962  1.00 20.19 ? 163 TYR   A CE1 1 
ATOM   530  C  CE2 . TYR   A 1 70  ? 7.607   -14.481 -83.204  1.00 20.33 ? 163 TYR   A CE2 1 
ATOM   531  C  CZ  . TYR   A 1 70  ? 6.946   -13.569 -84.009  1.00 20.10 ? 163 TYR   A CZ  1 
ATOM   532  O  OH  . TYR   A 1 70  ? 7.647   -12.745 -84.840  1.00 20.76 ? 163 TYR   A OH  1 
ATOM   533  N  N   . LYS   A 1 71  ? 1.628   -15.895 -79.933  1.00 23.68 ? 164 LYS   A N   1 
ATOM   534  C  CA  . LYS   A 1 71  ? 0.426   -16.450 -79.255  1.00 25.72 ? 164 LYS   A CA  1 
ATOM   535  C  C   . LYS   A 1 71  ? 0.301   -17.954 -79.544  1.00 26.13 ? 164 LYS   A C   1 
ATOM   536  O  O   . LYS   A 1 71  ? -0.190  -18.675 -78.657  1.00 27.00 ? 164 LYS   A O   1 
ATOM   537  C  CB  . LYS   A 1 71  ? -0.826  -15.694 -79.709  1.00 26.57 ? 164 LYS   A CB  1 
ATOM   538  C  CG  . LYS   A 1 71  ? -2.124  -16.136 -79.045  1.00 27.86 ? 164 LYS   A CG  1 
ATOM   539  C  CD  . LYS   A 1 71  ? -3.358  -15.489 -79.631  1.00 28.91 ? 164 LYS   A CD  1 
ATOM   540  C  CE  . LYS   A 1 71  ? -4.613  -15.837 -78.860  1.00 29.92 ? 164 LYS   A CE  1 
ATOM   541  N  NZ  . LYS   A 1 71  ? -5.834  -15.481 -79.619  1.00 30.66 ? 164 LYS   A NZ  1 
ATOM   542  N  N   . GLN   A 1 72  ? 0.714   -18.401 -80.735  1.00 27.30 ? 165 GLN   A N   1 
ATOM   543  C  CA  . GLN   A 1 72  ? 0.549   -19.804 -81.206  1.00 28.75 ? 165 GLN   A CA  1 
ATOM   544  C  C   . GLN   A 1 72  ? 1.686   -20.668 -80.650  1.00 29.08 ? 165 GLN   A C   1 
ATOM   545  O  O   . GLN   A 1 72  ? 2.853   -20.239 -80.734  1.00 26.48 ? 165 GLN   A O   1 
ATOM   546  C  CB  . GLN   A 1 72  ? 0.510   -19.860 -82.734  1.00 29.76 ? 165 GLN   A CB  1 
ATOM   547  C  CG  . GLN   A 1 72  ? -0.730  -19.202 -83.329  1.00 31.08 ? 165 GLN   A CG  1 
ATOM   548  C  CD  . GLN   A 1 72  ? -0.545  -18.824 -84.778  1.00 31.16 ? 165 GLN   A CD  1 
ATOM   549  O  OE1 . GLN   A 1 72  ? 0.405   -18.140 -85.144  1.00 31.95 ? 165 GLN   A OE1 1 
ATOM   550  N  NE2 . GLN   A 1 72  ? -1.464  -19.262 -85.623  1.00 33.76 ? 165 GLN   A NE2 1 
ATOM   551  N  N   . SER   A 1 73  ? 1.331   -21.846 -80.122  1.00 30.28 ? 166 SER   A N   1 
ATOM   552  C  CA  A SER   A 1 73  ? 2.262   -22.837 -79.517  0.15 29.90 ? 166 SER   A CA  1 
ATOM   553  C  CA  B SER   A 1 73  ? 2.259   -22.845 -79.523  0.85 30.67 ? 166 SER   A CA  1 
ATOM   554  C  C   . SER   A 1 73  ? 3.468   -23.087 -80.433  1.00 29.87 ? 166 SER   A C   1 
ATOM   555  O  O   . SER   A 1 73  ? 4.589   -23.164 -79.902  1.00 31.24 ? 166 SER   A O   1 
ATOM   556  C  CB  A SER   A 1 73  ? 1.540   -24.124 -79.211  0.15 29.80 ? 166 SER   A CB  1 
ATOM   557  C  CB  B SER   A 1 73  ? 1.542   -24.141 -79.239  0.85 31.63 ? 166 SER   A CB  1 
ATOM   558  O  OG  A SER   A 1 73  ? 0.998   -24.693 -80.393  0.15 29.36 ? 166 SER   A OG  1 
ATOM   559  O  OG  B SER   A 1 73  ? 0.716   -24.019 -78.091  0.85 33.29 ? 166 SER   A OG  1 
ATOM   560  N  N   . GLN   A 1 74  ? 3.233   -23.206 -81.744  1.00 29.91 ? 167 GLN   A N   1 
ATOM   561  C  CA  . GLN   A 1 74  ? 4.258   -23.625 -82.742  1.00 30.11 ? 167 GLN   A CA  1 
ATOM   562  C  C   . GLN   A 1 74  ? 5.281   -22.509 -82.996  1.00 30.00 ? 167 GLN   A C   1 
ATOM   563  O  O   . GLN   A 1 74  ? 6.296   -22.803 -83.657  1.00 27.90 ? 167 GLN   A O   1 
ATOM   564  C  CB  . GLN   A 1 74  ? 3.611   -24.077 -84.055  1.00 31.10 ? 167 GLN   A CB  1 
ATOM   565  C  CG  . GLN   A 1 74  ? 2.811   -22.999 -84.775  1.00 31.84 ? 167 GLN   A CG  1 
ATOM   566  C  CD  . GLN   A 1 74  ? 1.327   -23.081 -84.507  1.00 31.81 ? 167 GLN   A CD  1 
ATOM   567  O  OE1 . GLN   A 1 74  ? 0.887   -23.462 -83.425  1.00 31.67 ? 167 GLN   A OE1 1 
ATOM   568  N  NE2 . GLN   A 1 74  ? 0.538   -22.713 -85.502  1.00 33.90 ? 167 GLN   A NE2 1 
ATOM   569  N  N   . HIS   A 1 75  ? 5.025   -21.287 -82.512  1.00 28.95 ? 168 HIS   A N   1 
ATOM   570  C  CA  . HIS   A 1 75  ? 5.902   -20.100 -82.711  1.00 28.37 ? 168 HIS   A CA  1 
ATOM   571  C  C   . HIS   A 1 75  ? 6.416   -19.556 -81.370  1.00 27.62 ? 168 HIS   A C   1 
ATOM   572  O  O   . HIS   A 1 75  ? 7.222   -18.615 -81.413  1.00 27.73 ? 168 HIS   A O   1 
ATOM   573  C  CB  . HIS   A 1 75  ? 5.149   -19.012 -83.492  1.00 28.48 ? 168 HIS   A CB  1 
ATOM   574  C  CG  . HIS   A 1 75  ? 4.716   -19.433 -84.858  1.00 28.63 ? 168 HIS   A CG  1 
ATOM   575  N  ND1 . HIS   A 1 75  ? 5.619   -19.758 -85.851  1.00 28.33 ? 168 HIS   A ND1 1 
ATOM   576  C  CD2 . HIS   A 1 75  ? 3.487   -19.565 -85.407  1.00 28.70 ? 168 HIS   A CD2 1 
ATOM   577  C  CE1 . HIS   A 1 75  ? 4.966   -20.082 -86.948  1.00 28.40 ? 168 HIS   A CE1 1 
ATOM   578  N  NE2 . HIS   A 1 75  ? 3.658   -19.974 -86.702  1.00 28.36 ? 168 HIS   A NE2 1 
ATOM   579  N  N   . MET   A 1 76  ? 5.987   -20.128 -80.238  1.00 27.51 ? 169 MET   A N   1 
ATOM   580  C  CA  . MET   A 1 76  ? 6.141   -19.528 -78.882  1.00 28.47 ? 169 MET   A CA  1 
ATOM   581  C  C   . MET   A 1 76  ? 7.619   -19.363 -78.492  1.00 26.51 ? 169 MET   A C   1 
ATOM   582  O  O   . MET   A 1 76  ? 7.903   -18.436 -77.709  1.00 24.05 ? 169 MET   A O   1 
ATOM   583  C  CB  . MET   A 1 76  ? 5.450   -20.371 -77.806  1.00 31.58 ? 169 MET   A CB  1 
ATOM   584  C  CG  . MET   A 1 76  ? 4.041   -19.917 -77.497  1.00 35.18 ? 169 MET   A CG  1 
ATOM   585  S  SD  . MET   A 1 76  ? 3.671   -19.952 -75.728  1.00 38.17 ? 169 MET   A SD  1 
ATOM   586  C  CE  . MET   A 1 76  ? 1.946   -19.468 -75.770  1.00 39.41 ? 169 MET   A CE  1 
ATOM   587  N  N   . THR   A 1 77  ? 8.514   -20.233 -78.974  1.00 25.32 ? 170 THR   A N   1 
ATOM   588  C  CA  . THR   A 1 77  ? 9.954   -20.250 -78.591  1.00 24.68 ? 170 THR   A CA  1 
ATOM   589  C  C   . THR   A 1 77  ? 10.745  -19.258 -79.455  1.00 24.59 ? 170 THR   A C   1 
ATOM   590  O  O   . THR   A 1 77  ? 11.919  -19.010 -79.118  1.00 23.88 ? 170 THR   A O   1 
ATOM   591  C  CB  . THR   A 1 77  ? 10.550  -21.666 -78.646  1.00 24.66 ? 170 THR   A CB  1 
ATOM   592  O  OG1 . THR   A 1 77  ? 10.660  -22.083 -80.005  1.00 24.92 ? 170 THR   A OG1 1 
ATOM   593  C  CG2 . THR   A 1 77  ? 9.740   -22.682 -77.868  1.00 25.06 ? 170 THR   A CG2 1 
ATOM   594  N  N   . GLU   A 1 78  ? 10.145  -18.712 -80.520  1.00 23.96 ? 171 GLU   A N   1 
ATOM   595  C  CA  . GLU   A 1 78  ? 10.795  -17.716 -81.414  1.00 24.86 ? 171 GLU   A CA  1 
ATOM   596  C  C   . GLU   A 1 78  ? 10.699  -16.329 -80.767  1.00 24.37 ? 171 GLU   A C   1 
ATOM   597  O  O   . GLU   A 1 78  ? 9.571   -15.907 -80.421  1.00 24.70 ? 171 GLU   A O   1 
ATOM   598  C  CB  . GLU   A 1 78  ? 10.151  -17.710 -82.802  1.00 26.60 ? 171 GLU   A CB  1 
ATOM   599  C  CG  . GLU   A 1 78  ? 10.863  -16.808 -83.798  1.00 28.54 ? 171 GLU   A CG  1 
ATOM   600  C  CD  . GLU   A 1 78  ? 10.377  -16.923 -85.234  1.00 30.26 ? 171 GLU   A CD  1 
ATOM   601  O  OE1 . GLU   A 1 78  ? 9.693   -17.918 -85.550  1.00 32.13 ? 171 GLU   A OE1 1 
ATOM   602  O  OE2 . GLU   A 1 78  ? 10.678  -16.018 -86.036  1.00 32.33 ? 171 GLU   A OE2 1 
ATOM   603  N  N   . VAL   A 1 79  ? 11.838  -15.650 -80.609  1.00 22.75 ? 172 VAL   A N   1 
ATOM   604  C  CA  . VAL   A 1 79  ? 11.912  -14.276 -80.027  1.00 21.96 ? 172 VAL   A CA  1 
ATOM   605  C  C   . VAL   A 1 79  ? 11.182  -13.326 -80.981  1.00 20.74 ? 172 VAL   A C   1 
ATOM   606  O  O   . VAL   A 1 79  ? 11.526  -13.313 -82.180  1.00 19.93 ? 172 VAL   A O   1 
ATOM   607  C  CB  . VAL   A 1 79  ? 13.369  -13.833 -79.792  1.00 21.80 ? 172 VAL   A CB  1 
ATOM   608  C  CG1 . VAL   A 1 79  ? 13.466  -12.346 -79.474  1.00 22.03 ? 172 VAL   A CG1 1 
ATOM   609  C  CG2 . VAL   A 1 79  ? 14.043  -14.665 -78.710  1.00 21.67 ? 172 VAL   A CG2 1 
ATOM   610  N  N   . VAL   A 1 80  ? 10.208  -12.572 -80.469  1.00 19.98 ? 173 VAL   A N   1 
ATOM   611  C  CA  . VAL   A 1 80  ? 9.500   -11.511 -81.240  1.00 19.92 ? 173 VAL   A CA  1 
ATOM   612  C  C   . VAL   A 1 80  ? 10.462  -10.333 -81.397  1.00 20.02 ? 173 VAL   A C   1 
ATOM   613  O  O   . VAL   A 1 80  ? 10.906  -9.788  -80.364  1.00 19.10 ? 173 VAL   A O   1 
ATOM   614  C  CB  . VAL   A 1 80  ? 8.180   -11.079 -80.575  1.00 19.67 ? 173 VAL   A CB  1 
ATOM   615  C  CG1 . VAL   A 1 80  ? 7.526   -9.933  -81.335  1.00 19.58 ? 173 VAL   A CG1 1 
ATOM   616  C  CG2 . VAL   A 1 80  ? 7.216   -12.248 -80.432  1.00 19.71 ? 173 VAL   A CG2 1 
ATOM   617  N  N   . ARG   A 1 81  ? 10.782  -9.983  -82.645  1.00 20.36 ? 174 ARG   A N   1 
ATOM   618  C  CA  . ARG   A 1 81  ? 11.698  -8.865  -82.991  1.00 21.78 ? 174 ARG   A CA  1 
ATOM   619  C  C   . ARG   A 1 81  ? 11.209  -8.212  -84.285  1.00 20.95 ? 174 ARG   A C   1 
ATOM   620  O  O   . ARG   A 1 81  ? 10.413  -8.838  -85.015  1.00 18.75 ? 174 ARG   A O   1 
ATOM   621  C  CB  . ARG   A 1 81  ? 13.149  -9.350  -83.119  1.00 24.51 ? 174 ARG   A CB  1 
ATOM   622  C  CG  . ARG   A 1 81  ? 13.347  -10.582 -83.994  1.00 27.13 ? 174 ARG   A CG  1 
ATOM   623  C  CD  . ARG   A 1 81  ? 14.815  -10.969 -84.117  1.00 29.98 ? 174 ARG   A CD  1 
ATOM   624  N  NE  . ARG   A 1 81  ? 15.505  -10.197 -85.147  1.00 32.96 ? 174 ARG   A NE  1 
ATOM   625  C  CZ  . ARG   A 1 81  ? 16.812  -10.242 -85.406  1.00 35.98 ? 174 ARG   A CZ  1 
ATOM   626  N  NH1 . ARG   A 1 81  ? 17.317  -9.488  -86.370  1.00 37.33 ? 174 ARG   A NH1 1 
ATOM   627  N  NH2 . ARG   A 1 81  ? 17.611  -11.030 -84.705  1.00 37.07 ? 174 ARG   A NH2 1 
ATOM   628  N  N   . ARG   A 1 82  ? 11.683  -6.996  -84.545  1.00 20.96 ? 175 ARG   A N   1 
ATOM   629  C  CA  . ARG   A 1 82  ? 11.357  -6.221  -85.764  1.00 21.62 ? 175 ARG   A CA  1 
ATOM   630  C  C   . ARG   A 1 82  ? 11.911  -6.956  -86.988  1.00 21.13 ? 175 ARG   A C   1 
ATOM   631  O  O   . ARG   A 1 82  ? 12.943  -7.662  -86.851  1.00 20.10 ? 175 ARG   A O   1 
ATOM   632  C  CB  . ARG   A 1 82  ? 11.937  -4.809  -85.661  1.00 22.17 ? 175 ARG   A CB  1 
ATOM   633  C  CG  . ARG   A 1 82  ? 11.359  -3.983  -84.523  1.00 22.95 ? 175 ARG   A CG  1 
ATOM   634  C  CD  . ARG   A 1 82  ? 12.062  -2.645  -84.448  1.00 23.95 ? 175 ARG   A CD  1 
ATOM   635  N  NE  . ARG   A 1 82  ? 11.421  -1.662  -85.293  1.00 25.38 ? 175 ARG   A NE  1 
ATOM   636  C  CZ  . ARG   A 1 82  ? 11.933  -0.485  -85.627  1.00 25.37 ? 175 ARG   A CZ  1 
ATOM   637  N  NH1 . ARG   A 1 82  ? 13.135  -0.114  -85.211  1.00 25.26 ? 175 ARG   A NH1 1 
ATOM   638  N  NH2 . ARG   A 1 82  ? 11.224  0.316   -86.397  1.00 25.85 ? 175 ARG   A NH2 1 
ATOM   639  N  N   . CYS   A 1 83  ? 11.253  -6.787  -88.138  1.00 20.97 ? 176 CYS   A N   1 
ATOM   640  C  CA  . CYS   A 1 83  ? 11.702  -7.331  -89.446  1.00 21.02 ? 176 CYS   A CA  1 
ATOM   641  C  C   . CYS   A 1 83  ? 13.023  -6.658  -89.814  1.00 21.38 ? 176 CYS   A C   1 
ATOM   642  O  O   . CYS   A 1 83  ? 13.348  -5.601  -89.280  1.00 21.77 ? 176 CYS   A O   1 
ATOM   643  C  CB  . CYS   A 1 83  ? 10.633  -7.136  -90.518  1.00 19.71 ? 176 CYS   A CB  1 
ATOM   644  S  SG  . CYS   A 1 83  ? 10.356  -5.439  -90.889  1.00 19.21 ? 176 CYS   A SG  1 
ATOM   645  N  N   . PRO   A 1 84  ? 13.846  -7.245  -90.713  1.00 23.01 ? 177 PRO   A N   1 
ATOM   646  C  CA  . PRO   A 1 84  ? 15.093  -6.604  -91.131  1.00 22.94 ? 177 PRO   A CA  1 
ATOM   647  C  C   . PRO   A 1 84  ? 14.896  -5.137  -91.554  1.00 22.76 ? 177 PRO   A C   1 
ATOM   648  O  O   . PRO   A 1 84  ? 15.702  -4.311  -91.185  1.00 23.10 ? 177 PRO   A O   1 
ATOM   649  C  CB  . PRO   A 1 84  ? 15.560  -7.484  -92.303  1.00 23.56 ? 177 PRO   A CB  1 
ATOM   650  C  CG  . PRO   A 1 84  ? 14.983  -8.850  -91.986  1.00 23.29 ? 177 PRO   A CG  1 
ATOM   651  C  CD  . PRO   A 1 84  ? 13.646  -8.563  -91.336  1.00 23.17 ? 177 PRO   A CD  1 
ATOM   652  N  N   . HIS   A 1 85  ? 13.820  -4.841  -92.293  1.00 22.74 ? 178 HIS   A N   1 
ATOM   653  C  CA  . HIS   A 1 85  ? 13.483  -3.483  -92.800  1.00 22.34 ? 178 HIS   A CA  1 
ATOM   654  C  C   . HIS   A 1 85  ? 13.373  -2.475  -91.646  1.00 22.56 ? 178 HIS   A C   1 
ATOM   655  O  O   . HIS   A 1 85  ? 14.105  -1.459  -91.662  1.00 23.71 ? 178 HIS   A O   1 
ATOM   656  C  CB  . HIS   A 1 85  ? 12.193  -3.521  -93.639  1.00 22.08 ? 178 HIS   A CB  1 
ATOM   657  C  CG  . HIS   A 1 85  ? 11.593  -2.173  -93.853  1.00 21.17 ? 178 HIS   A CG  1 
ATOM   658  N  ND1 . HIS   A 1 85  ? 12.297  -1.140  -94.434  1.00 20.32 ? 178 HIS   A ND1 1 
ATOM   659  C  CD2 . HIS   A 1 85  ? 10.372  -1.682  -93.550  1.00 21.10 ? 178 HIS   A CD2 1 
ATOM   660  C  CE1 . HIS   A 1 85  ? 11.537  -0.069  -94.485  1.00 21.03 ? 178 HIS   A CE1 1 
ATOM   661  N  NE2 . HIS   A 1 85  ? 10.351  -0.372  -93.943  1.00 21.04 ? 178 HIS   A NE2 1 
ATOM   662  N  N   . HIS   A 1 86  ? 12.469  -2.719  -90.699  1.00 23.08 ? 179 HIS   A N   1 
ATOM   663  C  CA  . HIS   A 1 86  ? 12.168  -1.784  -89.581  1.00 23.59 ? 179 HIS   A CA  1 
ATOM   664  C  C   . HIS   A 1 86  ? 13.376  -1.671  -88.644  1.00 24.79 ? 179 HIS   A C   1 
ATOM   665  O  O   . HIS   A 1 86  ? 13.609  -0.572  -88.120  1.00 24.32 ? 179 HIS   A O   1 
ATOM   666  C  CB  . HIS   A 1 86  ? 10.872  -2.195  -88.875  1.00 22.36 ? 179 HIS   A CB  1 
ATOM   667  C  CG  . HIS   A 1 86  ? 9.660   -1.690  -89.580  1.00 21.18 ? 179 HIS   A CG  1 
ATOM   668  N  ND1 . HIS   A 1 86  ? 8.638   -2.519  -89.985  1.00 19.71 ? 179 HIS   A ND1 1 
ATOM   669  C  CD2 . HIS   A 1 86  ? 9.319   -0.440  -89.969  1.00 21.14 ? 179 HIS   A CD2 1 
ATOM   670  C  CE1 . HIS   A 1 86  ? 7.713   -1.796  -90.587  1.00 20.51 ? 179 HIS   A CE1 1 
ATOM   671  N  NE2 . HIS   A 1 86  ? 8.105   -0.518  -90.588  1.00 20.74 ? 179 HIS   A NE2 1 
ATOM   672  N  N   . GLU   A 1 87  ? 14.134  -2.754  -88.478  1.00 28.22 ? 180 GLU   A N   1 
ATOM   673  C  CA  . GLU   A 1 87  ? 15.410  -2.769  -87.709  1.00 32.02 ? 180 GLU   A CA  1 
ATOM   674  C  C   . GLU   A 1 87  ? 16.391  -1.758  -88.323  1.00 34.93 ? 180 GLU   A C   1 
ATOM   675  O  O   . GLU   A 1 87  ? 17.145  -1.135  -87.553  1.00 34.92 ? 180 GLU   A O   1 
ATOM   676  C  CB  . GLU   A 1 87  ? 15.984  -4.188  -87.682  1.00 32.10 ? 180 GLU   A CB  1 
ATOM   677  C  CG  . GLU   A 1 87  ? 17.307  -4.303  -86.947  1.00 33.81 ? 180 GLU   A CG  1 
ATOM   678  C  CD  . GLU   A 1 87  ? 17.872  -5.711  -86.867  1.00 33.69 ? 180 GLU   A CD  1 
ATOM   679  O  OE1 . GLU   A 1 87  ? 17.091  -6.675  -86.958  1.00 33.65 ? 180 GLU   A OE1 1 
ATOM   680  O  OE2 . GLU   A 1 87  ? 19.095  -5.839  -86.709  1.00 36.95 ? 180 GLU   A OE2 1 
ATOM   681  N  N   . ARG   A 1 88  ? 16.355  -1.582  -89.651  1.00 38.77 ? 181 ARG   A N   1 
ATOM   682  C  CA  . ARG   A 1 88  ? 17.311  -0.744  -90.427  1.00 42.13 ? 181 ARG   A CA  1 
ATOM   683  C  C   . ARG   A 1 88  ? 16.798  0.693   -90.567  1.00 42.33 ? 181 ARG   A C   1 
ATOM   684  O  O   . ARG   A 1 88  ? 17.632  1.575   -90.844  1.00 43.09 ? 181 ARG   A O   1 
ATOM   685  C  CB  . ARG   A 1 88  ? 17.526  -1.338  -91.822  1.00 45.67 ? 181 ARG   A CB  1 
ATOM   686  C  CG  . ARG   A 1 88  ? 18.896  -1.057  -92.424  1.00 49.25 ? 181 ARG   A CG  1 
ATOM   687  C  CD  . ARG   A 1 88  ? 19.333  -2.199  -93.322  1.00 52.49 ? 181 ARG   A CD  1 
ATOM   688  N  NE  . ARG   A 1 88  ? 19.420  -3.452  -92.576  1.00 55.59 ? 181 ARG   A NE  1 
ATOM   689  C  CZ  . ARG   A 1 88  ? 19.394  -4.675  -93.106  1.00 58.25 ? 181 ARG   A CZ  1 
ATOM   690  N  NH1 . ARG   A 1 88  ? 19.477  -5.732  -92.314  1.00 60.10 ? 181 ARG   A NH1 1 
ATOM   691  N  NH2 . ARG   A 1 88  ? 19.283  -4.850  -94.413  1.00 58.10 ? 181 ARG   A NH2 1 
ATOM   692  N  N   . CYS   A 1 89  ? 15.487  0.920   -90.417  1.00 43.11 ? 182 CYS   A N   1 
ATOM   693  C  CA  . CYS   A 1 89  ? 14.847  2.260   -90.538  1.00 43.65 ? 182 CYS   A CA  1 
ATOM   694  C  C   . CYS   A 1 89  ? 15.533  3.243   -89.582  1.00 44.19 ? 182 CYS   A C   1 
ATOM   695  O  O   . CYS   A 1 89  ? 15.983  2.801   -88.503  1.00 42.70 ? 182 CYS   A O   1 
ATOM   696  C  CB  . CYS   A 1 89  ? 13.351  2.203   -90.244  1.00 44.26 ? 182 CYS   A CB  1 
ATOM   697  S  SG  . CYS   A 1 89  ? 12.384  1.489   -91.601  1.00 45.53 ? 182 CYS   A SG  1 
ATOM   698  N  N   . SER   A 1 90  ? 15.616  4.519   -89.977  1.00 43.13 ? 183 SER   A N   1 
ATOM   699  C  CA  . SER   A 1 90  ? 16.156  5.634   -89.154  1.00 42.79 ? 183 SER   A CA  1 
ATOM   700  C  C   . SER   A 1 90  ? 15.006  6.268   -88.362  1.00 40.67 ? 183 SER   A C   1 
ATOM   701  O  O   . SER   A 1 90  ? 14.741  7.472   -88.554  1.00 41.12 ? 183 SER   A O   1 
ATOM   702  C  CB  . SER   A 1 90  ? 16.891  6.643   -90.009  1.00 43.78 ? 183 SER   A CB  1 
ATOM   703  O  OG  . SER   A 1 90  ? 16.032  7.197   -90.993  1.00 46.11 ? 183 SER   A OG  1 
ATOM   704  N  N   . ASP   A 1 91  ? 14.359  5.469   -87.505  1.00 37.90 ? 184 ASP   A N   1 
ATOM   705  C  CA  . ASP   A 1 91  ? 13.200  5.863   -86.657  1.00 36.20 ? 184 ASP   A CA  1 
ATOM   706  C  C   . ASP   A 1 91  ? 13.602  5.818   -85.174  1.00 35.24 ? 184 ASP   A C   1 
ATOM   707  O  O   . ASP   A 1 91  ? 12.689  5.765   -84.326  1.00 34.30 ? 184 ASP   A O   1 
ATOM   708  C  CB  . ASP   A 1 91  ? 11.996  4.956   -86.932  1.00 35.49 ? 184 ASP   A CB  1 
ATOM   709  C  CG  . ASP   A 1 91  ? 12.228  3.485   -86.614  1.00 34.92 ? 184 ASP   A CG  1 
ATOM   710  O  OD1 . ASP   A 1 91  ? 13.200  3.177   -85.896  1.00 34.94 ? 184 ASP   A OD1 1 
ATOM   711  O  OD2 . ASP   A 1 91  ? 11.433  2.652   -87.085  1.00 33.51 ? 184 ASP   A OD2 1 
ATOM   712  N  N   . SER   A 1 92  ? 14.909  5.832   -84.877  1.00 32.97 ? 185 SER   A N   1 
ATOM   713  C  CA  . SER   A 1 92  ? 15.475  5.735   -83.505  1.00 31.73 ? 185 SER   A CA  1 
ATOM   714  C  C   . SER   A 1 92  ? 15.055  6.948   -82.667  1.00 30.35 ? 185 SER   A C   1 
ATOM   715  O  O   . SER   A 1 92  ? 14.990  8.058   -83.223  1.00 30.25 ? 185 SER   A O   1 
ATOM   716  C  CB  . SER   A 1 92  ? 16.973  5.601   -83.542  1.00 32.02 ? 185 SER   A CB  1 
ATOM   717  O  OG  . SER   A 1 92  ? 17.488  5.369   -82.240  1.00 31.52 ? 185 SER   A OG  1 
ATOM   718  N  N   . ASP   A 1 93  ? 14.783  6.728   -81.376  1.00 28.78 ? 186 ASP   A N   1 
ATOM   719  C  CA  . ASP   A 1 93  ? 14.470  7.787   -80.380  1.00 26.52 ? 186 ASP   A CA  1 
ATOM   720  C  C   . ASP   A 1 93  ? 15.684  8.000   -79.466  1.00 26.13 ? 186 ASP   A C   1 
ATOM   721  O  O   . ASP   A 1 93  ? 15.560  8.790   -78.508  1.00 26.77 ? 186 ASP   A O   1 
ATOM   722  C  CB  . ASP   A 1 93  ? 13.203  7.447   -79.588  1.00 26.48 ? 186 ASP   A CB  1 
ATOM   723  C  CG  . ASP   A 1 93  ? 13.330  6.260   -78.646  1.00 25.96 ? 186 ASP   A CG  1 
ATOM   724  O  OD1 . ASP   A 1 93  ? 14.299  5.483   -78.791  1.00 24.79 ? 186 ASP   A OD1 1 
ATOM   725  O  OD2 . ASP   A 1 93  ? 12.459  6.128   -77.772  1.00 24.09 ? 186 ASP   A OD2 1 
ATOM   726  N  N   . GLY   A 1 94  ? 16.799  7.317   -79.754  1.00 24.65 ? 187 GLY   A N   1 
ATOM   727  C  CA  . GLY   A 1 94  ? 18.087  7.447   -79.046  1.00 24.82 ? 187 GLY   A CA  1 
ATOM   728  C  C   . GLY   A 1 94  ? 18.180  6.538   -77.831  1.00 24.43 ? 187 GLY   A C   1 
ATOM   729  O  O   . GLY   A 1 94  ? 19.270  6.490   -77.222  1.00 26.44 ? 187 GLY   A O   1 
ATOM   730  N  N   . LEU   A 1 95  ? 17.094  5.836   -77.488  1.00 23.24 ? 188 LEU   A N   1 
ATOM   731  C  CA  . LEU   A 1 95  ? 16.974  5.029   -76.244  1.00 22.14 ? 188 LEU   A CA  1 
ATOM   732  C  C   . LEU   A 1 95  ? 16.749  3.551   -76.580  1.00 21.26 ? 188 LEU   A C   1 
ATOM   733  O  O   . LEU   A 1 95  ? 17.506  2.715   -76.049  1.00 20.95 ? 188 LEU   A O   1 
ATOM   734  C  CB  . LEU   A 1 95  ? 15.833  5.599   -75.398  1.00 21.93 ? 188 LEU   A CB  1 
ATOM   735  C  CG  . LEU   A 1 95  ? 16.011  7.052   -74.955  1.00 21.62 ? 188 LEU   A CG  1 
ATOM   736  C  CD1 . LEU   A 1 95  ? 14.808  7.526   -74.159  1.00 22.06 ? 188 LEU   A CD1 1 
ATOM   737  C  CD2 . LEU   A 1 95  ? 17.288  7.229   -74.146  1.00 21.00 ? 188 LEU   A CD2 1 
ATOM   738  N  N   . ALA   A 1 96  ? 15.756  3.242   -77.422  1.00 20.41 ? 189 ALA   A N   1 
ATOM   739  C  CA  . ALA   A 1 96  ? 15.334  1.861   -77.758  1.00 19.64 ? 189 ALA   A CA  1 
ATOM   740  C  C   . ALA   A 1 96  ? 16.369  1.191   -78.662  1.00 19.53 ? 189 ALA   A C   1 
ATOM   741  O  O   . ALA   A 1 96  ? 16.887  1.804   -79.593  1.00 18.77 ? 189 ALA   A O   1 
ATOM   742  C  CB  . ALA   A 1 96  ? 13.969  1.879   -78.406  1.00 19.79 ? 189 ALA   A CB  1 
ATOM   743  N  N   . PRO   A 1 97  ? 16.724  -0.087  -78.404  1.00 19.14 ? 190 PRO   A N   1 
ATOM   744  C  CA  . PRO   A 1 97  ? 17.482  -0.883  -79.367  1.00 19.21 ? 190 PRO   A CA  1 
ATOM   745  C  C   . PRO   A 1 97  ? 16.709  -1.023  -80.676  1.00 19.59 ? 190 PRO   A C   1 
ATOM   746  O  O   . PRO   A 1 97  ? 15.488  -1.184  -80.656  1.00 18.74 ? 190 PRO   A O   1 
ATOM   747  C  CB  . PRO   A 1 97  ? 17.644  -2.251  -78.692  1.00 18.95 ? 190 PRO   A CB  1 
ATOM   748  C  CG  . PRO   A 1 97  ? 17.445  -1.974  -77.216  1.00 18.69 ? 190 PRO   A CG  1 
ATOM   749  C  CD  . PRO   A 1 97  ? 16.473  -0.816  -77.154  1.00 19.19 ? 190 PRO   A CD  1 
ATOM   750  N  N   . PRO   A 1 98  ? 17.387  -0.952  -81.845  1.00 19.51 ? 191 PRO   A N   1 
ATOM   751  C  CA  . PRO   A 1 98  ? 16.696  -1.000  -83.134  1.00 19.55 ? 191 PRO   A CA  1 
ATOM   752  C  C   . PRO   A 1 98  ? 15.927  -2.303  -83.423  1.00 19.32 ? 191 PRO   A C   1 
ATOM   753  O  O   . PRO   A 1 98  ? 15.078  -2.264  -84.285  1.00 20.40 ? 191 PRO   A O   1 
ATOM   754  C  CB  . PRO   A 1 98  ? 17.821  -0.805  -84.170  1.00 19.78 ? 191 PRO   A CB  1 
ATOM   755  C  CG  . PRO   A 1 98  ? 19.099  -1.153  -83.435  1.00 19.70 ? 191 PRO   A CG  1 
ATOM   756  C  CD  . PRO   A 1 98  ? 18.843  -0.790  -81.989  1.00 19.66 ? 191 PRO   A CD  1 
ATOM   757  N  N   . GLN   A 1 99  ? 16.226  -3.408  -82.733  1.00 18.51 ? 192 GLN   A N   1 
ATOM   758  C  CA  . GLN   A 1 99  ? 15.570  -4.730  -82.962  1.00 19.34 ? 192 GLN   A CA  1 
ATOM   759  C  C   . GLN   A 1 99  ? 14.262  -4.859  -82.168  1.00 17.51 ? 192 GLN   A C   1 
ATOM   760  O  O   . GLN   A 1 99  ? 13.472  -5.783  -82.481  1.00 16.30 ? 192 GLN   A O   1 
ATOM   761  C  CB  . GLN   A 1 99  ? 16.475  -5.885  -82.539  1.00 20.77 ? 192 GLN   A CB  1 
ATOM   762  C  CG  . GLN   A 1 99  ? 17.690  -6.086  -83.430  1.00 23.38 ? 192 GLN   A CG  1 
ATOM   763  C  CD  . GLN   A 1 99  ? 18.456  -7.322  -83.021  1.00 25.76 ? 192 GLN   A CD  1 
ATOM   764  O  OE1 . GLN   A 1 99  ? 18.390  -7.771  -81.876  1.00 29.43 ? 192 GLN   A OE1 1 
ATOM   765  N  NE2 . GLN   A 1 99  ? 19.184  -7.895  -83.965  1.00 27.58 ? 192 GLN   A NE2 1 
ATOM   766  N  N   . HIS   A 1 100 ? 14.068  -4.019  -81.148  1.00 16.04 ? 193 HIS   A N   1 
ATOM   767  C  CA  . HIS   A 1 100 ? 12.948  -4.110  -80.169  1.00 15.44 ? 193 HIS   A CA  1 
ATOM   768  C  C   . HIS   A 1 100 ? 11.625  -3.648  -80.789  1.00 14.73 ? 193 HIS   A C   1 
ATOM   769  O  O   . HIS   A 1 100 ? 11.549  -2.500  -81.257  1.00 14.76 ? 193 HIS   A O   1 
ATOM   770  C  CB  . HIS   A 1 100 ? 13.265  -3.302  -78.905  1.00 15.04 ? 193 HIS   A CB  1 
ATOM   771  C  CG  . HIS   A 1 100 ? 14.174  -4.015  -77.969  1.00 15.25 ? 193 HIS   A CG  1 
ATOM   772  N  ND1 . HIS   A 1 100 ? 13.924  -4.076  -76.614  1.00 15.47 ? 193 HIS   A ND1 1 
ATOM   773  C  CD2 . HIS   A 1 100 ? 15.309  -4.715  -78.182  1.00 15.30 ? 193 HIS   A CD2 1 
ATOM   774  C  CE1 . HIS   A 1 100 ? 14.881  -4.764  -76.026  1.00 15.30 ? 193 HIS   A CE1 1 
ATOM   775  N  NE2 . HIS   A 1 100 ? 15.736  -5.177  -76.964  1.00 15.21 ? 193 HIS   A NE2 1 
ATOM   776  N  N   . LEU   A 1 101 ? 10.604  -4.502  -80.720  1.00 14.44 ? 194 LEU   A N   1 
ATOM   777  C  CA  . LEU   A 1 101 ? 9.225   -4.208  -81.193  1.00 14.33 ? 194 LEU   A CA  1 
ATOM   778  C  C   . LEU   A 1 101 ? 8.572   -3.148  -80.304  1.00 14.06 ? 194 LEU   A C   1 
ATOM   779  O  O   . LEU   A 1 101 ? 7.925   -2.238  -80.852  1.00 14.44 ? 194 LEU   A O   1 
ATOM   780  C  CB  . LEU   A 1 101 ? 8.411   -5.502  -81.155  1.00 14.47 ? 194 LEU   A CB  1 
ATOM   781  C  CG  . LEU   A 1 101 ? 6.935   -5.359  -81.524  1.00 14.60 ? 194 LEU   A CG  1 
ATOM   782  C  CD1 . LEU   A 1 101 ? 6.780   -4.877  -82.956  1.00 14.86 ? 194 LEU   A CD1 1 
ATOM   783  C  CD2 . LEU   A 1 101 ? 6.211   -6.677  -81.324  1.00 14.79 ? 194 LEU   A CD2 1 
ATOM   784  N  N   . ILE   A 1 102 ? 8.674   -3.301  -78.981  1.00 14.53 ? 195 ILE   A N   1 
ATOM   785  C  CA  . ILE   A 1 102 ? 7.923   -2.472  -77.994  1.00 14.75 ? 195 ILE   A CA  1 
ATOM   786  C  C   . ILE   A 1 102 ? 8.859   -1.389  -77.455  1.00 15.25 ? 195 ILE   A C   1 
ATOM   787  O  O   . ILE   A 1 102 ? 9.909   -1.739  -76.874  1.00 15.15 ? 195 ILE   A O   1 
ATOM   788  C  CB  . ILE   A 1 102 ? 7.324   -3.317  -76.850  1.00 14.62 ? 195 ILE   A CB  1 
ATOM   789  C  CG1 . ILE   A 1 102 ? 6.525   -4.518  -77.365  1.00 14.53 ? 195 ILE   A CG1 1 
ATOM   790  C  CG2 . ILE   A 1 102 ? 6.483   -2.438  -75.931  1.00 14.51 ? 195 ILE   A CG2 1 
ATOM   791  C  CD1 . ILE   A 1 102 ? 5.881   -5.348  -76.271  1.00 14.59 ? 195 ILE   A CD1 1 
ATOM   792  N  N   . ARG   A 1 103 ? 8.465   -0.127  -77.628  1.00 15.76 ? 196 ARG   A N   1 
ATOM   793  C  CA  . ARG   A 1 103 ? 9.104   1.042   -76.979  1.00 16.26 ? 196 ARG   A CA  1 
ATOM   794  C  C   . ARG   A 1 103 ? 8.117   1.678   -76.003  1.00 16.10 ? 196 ARG   A C   1 
ATOM   795  O  O   . ARG   A 1 103 ? 6.904   1.416   -76.113  1.00 16.04 ? 196 ARG   A O   1 
ATOM   796  C  CB  . ARG   A 1 103 ? 9.518   2.087   -78.018  1.00 16.82 ? 196 ARG   A CB  1 
ATOM   797  C  CG  . ARG   A 1 103 ? 10.449  1.556   -79.092  1.00 17.71 ? 196 ARG   A CG  1 
ATOM   798  C  CD  . ARG   A 1 103 ? 10.929  2.683   -79.983  1.00 18.61 ? 196 ARG   A CD  1 
ATOM   799  N  NE  . ARG   A 1 103 ? 11.788  2.195   -81.053  1.00 19.50 ? 196 ARG   A NE  1 
ATOM   800  C  CZ  . ARG   A 1 103 ? 12.185  2.930   -82.086  1.00 20.18 ? 196 ARG   A CZ  1 
ATOM   801  N  NH1 . ARG   A 1 103 ? 11.808  4.195   -82.189  1.00 20.64 ? 196 ARG   A NH1 1 
ATOM   802  N  NH2 . ARG   A 1 103 ? 12.960  2.396   -83.012  1.00 20.67 ? 196 ARG   A NH2 1 
ATOM   803  N  N   . VAL   A 1 104 ? 8.635   2.476   -75.075  1.00 16.23 ? 197 VAL   A N   1 
ATOM   804  C  CA  . VAL   A 1 104 ? 7.831   3.444   -74.279  1.00 16.77 ? 197 VAL   A CA  1 
ATOM   805  C  C   . VAL   A 1 104 ? 8.200   4.845   -74.774  1.00 17.89 ? 197 VAL   A C   1 
ATOM   806  O  O   . VAL   A 1 104 ? 9.407   5.144   -74.858  1.00 17.57 ? 197 VAL   A O   1 
ATOM   807  C  CB  . VAL   A 1 104 ? 8.066   3.284   -72.765  1.00 16.39 ? 197 VAL   A CB  1 
ATOM   808  C  CG1 . VAL   A 1 104 ? 7.400   4.405   -71.975  1.00 15.94 ? 197 VAL   A CG1 1 
ATOM   809  C  CG2 . VAL   A 1 104 ? 7.610   1.921   -72.270  1.00 16.11 ? 197 VAL   A CG2 1 
ATOM   810  N  N   . GLU   A 1 105 ? 7.197   5.664   -75.091  1.00 19.47 ? 198 GLU   A N   1 
ATOM   811  C  CA  . GLU   A 1 105 ? 7.385   7.085   -75.486  1.00 20.95 ? 198 GLU   A CA  1 
ATOM   812  C  C   . GLU   A 1 105 ? 7.164   7.944   -74.234  1.00 20.84 ? 198 GLU   A C   1 
ATOM   813  O  O   . GLU   A 1 105 ? 6.447   7.484   -73.324  1.00 20.41 ? 198 GLU   A O   1 
ATOM   814  C  CB  . GLU   A 1 105 ? 6.461   7.437   -76.658  1.00 22.14 ? 198 GLU   A CB  1 
ATOM   815  C  CG  . GLU   A 1 105 ? 5.239   8.259   -76.284  1.00 23.41 ? 198 GLU   A CG  1 
ATOM   816  C  CD  . GLU   A 1 105 ? 4.238   8.482   -77.408  1.00 24.25 ? 198 GLU   A CD  1 
ATOM   817  O  OE1 . GLU   A 1 105 ? 4.111   9.635   -77.854  1.00 25.92 ? 198 GLU   A OE1 1 
ATOM   818  O  OE2 . GLU   A 1 105 ? 3.561   7.510   -77.809  1.00 23.90 ? 198 GLU   A OE2 1 
ATOM   819  N  N   . GLY   A 1 106 ? 7.804   9.115   -74.181  1.00 20.52 ? 199 GLY   A N   1 
ATOM   820  C  CA  . GLY   A 1 106 ? 7.600   10.146  -73.146  1.00 20.72 ? 199 GLY   A CA  1 
ATOM   821  C  C   . GLY   A 1 106 ? 8.028   9.704   -71.757  1.00 20.54 ? 199 GLY   A C   1 
ATOM   822  O  O   . GLY   A 1 106 ? 7.350   10.101  -70.797  1.00 20.82 ? 199 GLY   A O   1 
ATOM   823  N  N   . ASN   A 1 107 ? 9.119   8.935   -71.632  1.00 20.65 ? 200 ASN   A N   1 
ATOM   824  C  CA  . ASN   A 1 107 ? 9.666   8.510   -70.313  1.00 20.31 ? 200 ASN   A CA  1 
ATOM   825  C  C   . ASN   A 1 107 ? 11.186  8.317   -70.421  1.00 21.19 ? 200 ASN   A C   1 
ATOM   826  O  O   . ASN   A 1 107 ? 11.616  7.251   -70.916  1.00 21.18 ? 200 ASN   A O   1 
ATOM   827  C  CB  . ASN   A 1 107 ? 8.955   7.255   -69.791  1.00 19.57 ? 200 ASN   A CB  1 
ATOM   828  C  CG  . ASN   A 1 107 ? 9.243   6.970   -68.330  1.00 18.76 ? 200 ASN   A CG  1 
ATOM   829  O  OD1 . ASN   A 1 107 ? 10.311  7.301   -67.824  1.00 18.94 ? 200 ASN   A OD1 1 
ATOM   830  N  ND2 . ASN   A 1 107 ? 8.303   6.346   -67.641  1.00 18.90 ? 200 ASN   A ND2 1 
ATOM   831  N  N   . LEU   A 1 108 ? 11.966  9.290   -69.930  1.00 21.82 ? 201 LEU   A N   1 
ATOM   832  C  CA  . LEU   A 1 108 ? 13.456  9.298   -69.998  1.00 22.72 ? 201 LEU   A CA  1 
ATOM   833  C  C   . LEU   A 1 108 ? 14.064  8.219   -69.090  1.00 22.02 ? 201 LEU   A C   1 
ATOM   834  O  O   . LEU   A 1 108 ? 15.278  7.975   -69.227  1.00 22.16 ? 201 LEU   A O   1 
ATOM   835  C  CB  . LEU   A 1 108 ? 13.988  10.679  -69.592  1.00 24.43 ? 201 LEU   A CB  1 
ATOM   836  C  CG  . LEU   A 1 108 ? 14.100  11.717  -70.707  1.00 26.30 ? 201 LEU   A CG  1 
ATOM   837  C  CD1 . LEU   A 1 108 ? 14.781  12.978  -70.190  1.00 27.26 ? 201 LEU   A CD1 1 
ATOM   838  C  CD2 . LEU   A 1 108 ? 14.856  11.164  -71.908  1.00 27.21 ? 201 LEU   A CD2 1 
ATOM   839  N  N   . ARG   A 1 109 ? 13.282  7.620   -68.185  1.00 21.66 ? 202 ARG   A N   1 
ATOM   840  C  CA  . ARG   A 1 109 ? 13.773  6.617   -67.201  1.00 21.70 ? 202 ARG   A CA  1 
ATOM   841  C  C   . ARG   A 1 109 ? 13.562  5.199   -67.746  1.00 19.69 ? 202 ARG   A C   1 
ATOM   842  O  O   . ARG   A 1 109 ? 13.799  4.237   -66.987  1.00 19.65 ? 202 ARG   A O   1 
ATOM   843  C  CB  . ARG   A 1 109 ? 13.069  6.816   -65.856  1.00 23.99 ? 202 ARG   A CB  1 
ATOM   844  C  CG  . ARG   A 1 109 ? 13.246  8.210   -65.271  1.00 26.79 ? 202 ARG   A CG  1 
ATOM   845  C  CD  . ARG   A 1 109 ? 12.524  8.370   -63.953  1.00 29.67 ? 202 ARG   A CD  1 
ATOM   846  N  NE  . ARG   A 1 109 ? 13.063  7.468   -62.941  1.00 33.18 ? 202 ARG   A NE  1 
ATOM   847  C  CZ  . ARG   A 1 109 ? 12.546  7.280   -61.728  1.00 33.74 ? 202 ARG   A CZ  1 
ATOM   848  N  NH1 . ARG   A 1 109 ? 11.460  7.937   -61.352  1.00 33.16 ? 202 ARG   A NH1 1 
ATOM   849  N  NH2 . ARG   A 1 109 ? 13.120  6.426   -60.896  1.00 35.40 ? 202 ARG   A NH2 1 
ATOM   850  N  N   . VAL   A 1 110 ? 13.149  5.078   -69.011  1.00 17.97 ? 203 VAL   A N   1 
ATOM   851  C  CA  . VAL   A 1 110 ? 12.885  3.777   -69.692  1.00 16.74 ? 203 VAL   A CA  1 
ATOM   852  C  C   . VAL   A 1 110 ? 14.190  2.975   -69.768  1.00 15.75 ? 203 VAL   A C   1 
ATOM   853  O  O   . VAL   A 1 110 ? 15.265  3.578   -69.991  1.00 15.40 ? 203 VAL   A O   1 
ATOM   854  C  CB  . VAL   A 1 110 ? 12.259  3.983   -71.088  1.00 16.66 ? 203 VAL   A CB  1 
ATOM   855  C  CG1 . VAL   A 1 110 ? 13.228  4.624   -72.074  1.00 16.46 ? 203 VAL   A CG1 1 
ATOM   856  C  CG2 . VAL   A 1 110 ? 11.715  2.681   -71.648  1.00 16.87 ? 203 VAL   A CG2 1 
ATOM   857  N  N   . GLU   A 1 111 ? 14.101  1.657   -69.597  1.00 14.58 ? 204 GLU   A N   1 
ATOM   858  C  CA  . GLU   A 1 111 ? 15.269  0.741   -69.690  1.00 14.29 ? 204 GLU   A CA  1 
ATOM   859  C  C   . GLU   A 1 111 ? 14.903  -0.415  -70.628  1.00 14.18 ? 204 GLU   A C   1 
ATOM   860  O  O   . GLU   A 1 111 ? 13.760  -0.899  -70.548  1.00 13.85 ? 204 GLU   A O   1 
ATOM   861  C  CB  . GLU   A 1 111 ? 15.669  0.316   -68.277  1.00 14.38 ? 204 GLU   A CB  1 
ATOM   862  C  CG  . GLU   A 1 111 ? 16.617  -0.864  -68.206  1.00 14.59 ? 204 GLU   A CG  1 
ATOM   863  C  CD  . GLU   A 1 111 ? 16.770  -1.436  -66.809  1.00 14.32 ? 204 GLU   A CD  1 
ATOM   864  O  OE1 . GLU   A 1 111 ? 16.845  -0.640  -65.865  1.00 14.47 ? 204 GLU   A OE1 1 
ATOM   865  O  OE2 . GLU   A 1 111 ? 16.805  -2.677  -66.669  1.00 14.04 ? 204 GLU   A OE2 1 
ATOM   866  N  N   . TYR   A 1 112 ? 15.831  -0.807  -71.505  1.00 14.47 ? 205 TYR   A N   1 
ATOM   867  C  CA  . TYR   A 1 112 ? 15.652  -1.904  -72.491  1.00 14.33 ? 205 TYR   A CA  1 
ATOM   868  C  C   . TYR   A 1 112 ? 16.603  -3.054  -72.148  1.00 14.49 ? 205 TYR   A C   1 
ATOM   869  O  O   . TYR   A 1 112 ? 17.778  -2.799  -71.796  1.00 15.02 ? 205 TYR   A O   1 
ATOM   870  C  CB  . TYR   A 1 112 ? 15.857  -1.376  -73.913  1.00 14.78 ? 205 TYR   A CB  1 
ATOM   871  C  CG  . TYR   A 1 112 ? 14.772  -0.433  -74.367  1.00 14.46 ? 205 TYR   A CG  1 
ATOM   872  C  CD1 . TYR   A 1 112 ? 13.631  -0.915  -74.984  1.00 14.17 ? 205 TYR   A CD1 1 
ATOM   873  C  CD2 . TYR   A 1 112 ? 14.866  0.935   -74.148  1.00 14.71 ? 205 TYR   A CD2 1 
ATOM   874  C  CE1 . TYR   A 1 112 ? 12.615  -0.068  -75.393  1.00 14.40 ? 205 TYR   A CE1 1 
ATOM   875  C  CE2 . TYR   A 1 112 ? 13.859  1.798   -74.554  1.00 14.67 ? 205 TYR   A CE2 1 
ATOM   876  C  CZ  . TYR   A 1 112 ? 12.733  1.294   -75.184  1.00 14.36 ? 205 TYR   A CZ  1 
ATOM   877  O  OH  . TYR   A 1 112 ? 11.723  2.117   -75.577  1.00 14.48 ? 205 TYR   A OH  1 
ATOM   878  N  N   . LEU   A 1 113 ? 16.099  -4.285  -72.237  1.00 14.15 ? 206 LEU   A N   1 
ATOM   879  C  CA  . LEU   A 1 113 ? 16.859  -5.517  -71.912  1.00 14.61 ? 206 LEU   A CA  1 
ATOM   880  C  C   . LEU   A 1 113 ? 16.849  -6.477  -73.104  1.00 14.87 ? 206 LEU   A C   1 
ATOM   881  O  O   . LEU   A 1 113 ? 15.767  -6.753  -73.642  1.00 14.14 ? 206 LEU   A O   1 
ATOM   882  C  CB  . LEU   A 1 113 ? 16.257  -6.193  -70.678  1.00 14.20 ? 206 LEU   A CB  1 
ATOM   883  C  CG  . LEU   A 1 113 ? 16.931  -7.506  -70.277  1.00 13.97 ? 206 LEU   A CG  1 
ATOM   884  C  CD1 . LEU   A 1 113 ? 18.388  -7.271  -69.898  1.00 13.84 ? 206 LEU   A CD1 1 
ATOM   885  C  CD2 . LEU   A 1 113 ? 16.176  -8.186  -69.142  1.00 13.78 ? 206 LEU   A CD2 1 
ATOM   886  N  N   . ASP   A 1 114 ? 18.034  -6.964  -73.470  1.00 15.73 ? 207 ASP   A N   1 
ATOM   887  C  CA  . ASP   A 1 114 ? 18.249  -8.213  -74.243  1.00 17.26 ? 207 ASP   A CA  1 
ATOM   888  C  C   . ASP   A 1 114 ? 18.627  -9.305  -73.231  1.00 17.86 ? 207 ASP   A C   1 
ATOM   889  O  O   . ASP   A 1 114 ? 19.755  -9.255  -72.707  1.00 17.63 ? 207 ASP   A O   1 
ATOM   890  C  CB  . ASP   A 1 114 ? 19.362  -8.044  -75.282  1.00 17.92 ? 207 ASP   A CB  1 
ATOM   891  C  CG  . ASP   A 1 114 ? 19.046  -7.164  -76.485  1.00 18.55 ? 207 ASP   A CG  1 
ATOM   892  O  OD1 . ASP   A 1 114 ? 17.864  -6.817  -76.696  1.00 17.80 ? 207 ASP   A OD1 1 
ATOM   893  O  OD2 . ASP   A 1 114 ? 19.997  -6.853  -77.218  1.00 18.92 ? 207 ASP   A OD2 1 
ATOM   894  N  N   . ASP   A 1 115 ? 17.718  -10.226 -72.915  1.00 18.12 ? 208 ASP   A N   1 
ATOM   895  C  CA  . ASP   A 1 115 ? 17.952  -11.236 -71.849  1.00 18.71 ? 208 ASP   A CA  1 
ATOM   896  C  C   . ASP   A 1 115 ? 19.181  -12.077 -72.227  1.00 19.51 ? 208 ASP   A C   1 
ATOM   897  O  O   . ASP   A 1 115 ? 19.250  -12.557 -73.370  1.00 18.28 ? 208 ASP   A O   1 
ATOM   898  C  CB  . ASP   A 1 115 ? 16.710  -12.083 -71.583  1.00 18.59 ? 208 ASP   A CB  1 
ATOM   899  C  CG  . ASP   A 1 115 ? 16.854  -12.932 -70.332  1.00 18.80 ? 208 ASP   A CG  1 
ATOM   900  O  OD1 . ASP   A 1 115 ? 17.615  -13.912 -70.387  1.00 18.79 ? 208 ASP   A OD1 1 
ATOM   901  O  OD2 . ASP   A 1 115 ? 16.238  -12.580 -69.303  1.00 19.13 ? 208 ASP   A OD2 1 
ATOM   902  N  N   . ARG   A 1 116 ? 20.130  -12.228 -71.302  1.00 21.91 ? 209 ARG   A N   1 
ATOM   903  C  CA  . ARG   A 1 116 ? 21.441  -12.879 -71.582  1.00 24.18 ? 209 ARG   A CA  1 
ATOM   904  C  C   . ARG   A 1 116 ? 21.257  -14.393 -71.787  1.00 24.01 ? 209 ARG   A C   1 
ATOM   905  O  O   . ARG   A 1 116 ? 22.129  -15.003 -72.434  1.00 25.45 ? 209 ARG   A O   1 
ATOM   906  C  CB  . ARG   A 1 116 ? 22.447  -12.555 -70.472  1.00 26.55 ? 209 ARG   A CB  1 
ATOM   907  C  CG  . ARG   A 1 116 ? 22.152  -13.206 -69.129  1.00 28.88 ? 209 ARG   A CG  1 
ATOM   908  C  CD  . ARG   A 1 116 ? 23.183  -12.804 -68.091  1.00 30.81 ? 209 ARG   A CD  1 
ATOM   909  N  NE  . ARG   A 1 116 ? 23.019  -13.561 -66.859  1.00 32.79 ? 209 ARG   A NE  1 
ATOM   910  C  CZ  . ARG   A 1 116 ? 23.477  -14.795 -66.644  1.00 34.85 ? 209 ARG   A CZ  1 
ATOM   911  N  NH1 . ARG   A 1 116 ? 24.150  -15.447 -67.581  1.00 34.85 ? 209 ARG   A NH1 1 
ATOM   912  N  NH2 . ARG   A 1 116 ? 23.257  -15.374 -65.476  1.00 35.77 ? 209 ARG   A NH2 1 
ATOM   913  N  N   . ASN   A 1 117 ? 20.175  -14.983 -71.270  1.00 23.19 ? 210 ASN   A N   1 
ATOM   914  C  CA  . ASN   A 1 117 ? 19.915  -16.447 -71.349  1.00 22.89 ? 210 ASN   A CA  1 
ATOM   915  C  C   . ASN   A 1 117 ? 18.856  -16.764 -72.415  1.00 22.20 ? 210 ASN   A C   1 
ATOM   916  O  O   . ASN   A 1 117 ? 19.078  -17.727 -73.169  1.00 21.06 ? 210 ASN   A O   1 
ATOM   917  C  CB  . ASN   A 1 117 ? 19.516  -17.016 -69.987  1.00 23.71 ? 210 ASN   A CB  1 
ATOM   918  C  CG  . ASN   A 1 117 ? 20.628  -16.900 -68.966  1.00 23.86 ? 210 ASN   A CG  1 
ATOM   919  O  OD1 . ASN   A 1 117 ? 20.437  -16.318 -67.902  1.00 24.96 ? 210 ASN   A OD1 1 
ATOM   920  N  ND2 . ASN   A 1 117 ? 21.793  -17.435 -69.287  1.00 24.28 ? 210 ASN   A ND2 1 
ATOM   921  N  N   . THR   A 1 118 ? 17.759  -16.000 -72.480  1.00 21.29 ? 211 THR   A N   1 
ATOM   922  C  CA  . THR   A 1 118 ? 16.579  -16.291 -73.345  1.00 21.72 ? 211 THR   A CA  1 
ATOM   923  C  C   . THR   A 1 118 ? 16.628  -15.493 -74.656  1.00 21.23 ? 211 THR   A C   1 
ATOM   924  O  O   . THR   A 1 118 ? 15.880  -15.865 -75.579  1.00 22.19 ? 211 THR   A O   1 
ATOM   925  C  CB  . THR   A 1 118 ? 15.264  -16.008 -72.607  1.00 22.03 ? 211 THR   A CB  1 
ATOM   926  O  OG1 . THR   A 1 118 ? 15.083  -14.593 -72.520  1.00 22.06 ? 211 THR   A OG1 1 
ATOM   927  C  CG2 . THR   A 1 118 ? 15.221  -16.622 -71.225  1.00 22.04 ? 211 THR   A CG2 1 
ATOM   928  N  N   . PHE   A 1 119 ? 17.424  -14.419 -74.716  1.00 20.63 ? 212 PHE   A N   1 
ATOM   929  C  CA  . PHE   A 1 119 ? 17.579  -13.495 -75.877  1.00 20.99 ? 212 PHE   A CA  1 
ATOM   930  C  C   . PHE   A 1 119 ? 16.288  -12.703 -76.113  1.00 19.78 ? 212 PHE   A C   1 
ATOM   931  O  O   . PHE   A 1 119 ? 16.190  -12.021 -77.159  1.00 19.03 ? 212 PHE   A O   1 
ATOM   932  C  CB  . PHE   A 1 119 ? 18.003  -14.247 -77.141  1.00 21.76 ? 212 PHE   A CB  1 
ATOM   933  C  CG  . PHE   A 1 119 ? 19.162  -15.186 -76.925  1.00 23.52 ? 212 PHE   A CG  1 
ATOM   934  C  CD1 . PHE   A 1 119 ? 20.362  -14.715 -76.417  1.00 24.32 ? 212 PHE   A CD1 1 
ATOM   935  C  CD2 . PHE   A 1 119 ? 19.046  -16.540 -77.205  1.00 24.48 ? 212 PHE   A CD2 1 
ATOM   936  C  CE1 . PHE   A 1 119 ? 21.426  -15.577 -76.199  1.00 24.66 ? 212 PHE   A CE1 1 
ATOM   937  C  CE2 . PHE   A 1 119 ? 20.111  -17.400 -76.984  1.00 25.16 ? 212 PHE   A CE2 1 
ATOM   938  C  CZ  . PHE   A 1 119 ? 21.299  -16.917 -76.485  1.00 25.07 ? 212 PHE   A CZ  1 
ATOM   939  N  N   . ARG   A 1 120 ? 15.356  -12.755 -75.157  1.00 18.54 ? 213 ARG   A N   1 
ATOM   940  C  CA  . ARG   A 1 120 ? 14.049  -12.053 -75.217  1.00 17.99 ? 213 ARG   A CA  1 
ATOM   941  C  C   . ARG   A 1 120 ? 14.277  -10.557 -74.999  1.00 16.99 ? 213 ARG   A C   1 
ATOM   942  O  O   . ARG   A 1 120 ? 15.124  -10.185 -74.150  1.00 15.83 ? 213 ARG   A O   1 
ATOM   943  C  CB  . ARG   A 1 120 ? 13.093  -12.588 -74.149  1.00 18.69 ? 213 ARG   A CB  1 
ATOM   944  C  CG  . ARG   A 1 120 ? 12.793  -14.075 -74.262  1.00 19.53 ? 213 ARG   A CG  1 
ATOM   945  C  CD  . ARG   A 1 120 ? 11.504  -14.325 -74.996  1.00 19.42 ? 213 ARG   A CD  1 
ATOM   946  N  NE  . ARG   A 1 120 ? 11.182  -15.741 -75.121  1.00 19.34 ? 213 ARG   A NE  1 
ATOM   947  C  CZ  . ARG   A 1 120 ? 10.301  -16.226 -75.990  1.00 19.62 ? 213 ARG   A CZ  1 
ATOM   948  N  NH1 . ARG   A 1 120 ? 9.649   -15.408 -76.803  1.00 19.16 ? 213 ARG   A NH1 1 
ATOM   949  N  NH2 . ARG   A 1 120 ? 10.072  -17.526 -76.044  1.00 19.80 ? 213 ARG   A NH2 1 
ATOM   950  N  N   . HIS   A 1 121 ? 13.545  -9.739  -75.752  1.00 16.22 ? 214 HIS   A N   1 
ATOM   951  C  CA  . HIS   A 1 121 ? 13.522  -8.262  -75.627  1.00 14.91 ? 214 HIS   A CA  1 
ATOM   952  C  C   . HIS   A 1 121 ? 12.451  -7.884  -74.606  1.00 14.57 ? 214 HIS   A C   1 
ATOM   953  O  O   . HIS   A 1 121 ? 11.383  -8.507  -74.606  1.00 14.15 ? 214 HIS   A O   1 
ATOM   954  C  CB  . HIS   A 1 121 ? 13.253  -7.608  -76.988  1.00 14.81 ? 214 HIS   A CB  1 
ATOM   955  C  CG  . HIS   A 1 121 ? 14.240  -7.977  -78.043  1.00 14.79 ? 214 HIS   A CG  1 
ATOM   956  N  ND1 . HIS   A 1 121 ? 14.023  -7.695  -79.376  1.00 14.85 ? 214 HIS   A ND1 1 
ATOM   957  C  CD2 . HIS   A 1 121 ? 15.431  -8.612  -77.969  1.00 14.73 ? 214 HIS   A CD2 1 
ATOM   958  C  CE1 . HIS   A 1 121 ? 15.045  -8.134  -80.085  1.00 15.04 ? 214 HIS   A CE1 1 
ATOM   959  N  NE2 . HIS   A 1 121 ? 15.923  -8.706  -79.242  1.00 14.98 ? 214 HIS   A NE2 1 
ATOM   960  N  N   . SER   A 1 122 ? 12.724  -6.888  -73.772  1.00 14.23 ? 215 SER   A N   1 
ATOM   961  C  CA  . SER   A 1 122 ? 11.700  -6.270  -72.902  1.00 13.95 ? 215 SER   A CA  1 
ATOM   962  C  C   . SER   A 1 122 ? 12.054  -4.806  -72.668  1.00 14.13 ? 215 SER   A C   1 
ATOM   963  O  O   . SER   A 1 122 ? 13.226  -4.404  -72.891  1.00 14.54 ? 215 SER   A O   1 
ATOM   964  C  CB  . SER   A 1 122 ? 11.509  -7.042  -71.618  1.00 14.01 ? 215 SER   A CB  1 
ATOM   965  O  OG  . SER   A 1 122 ? 12.712  -7.134  -70.873  1.00 13.38 ? 215 SER   A OG  1 
ATOM   966  N  N   . VAL   A 1 123 ? 11.049  -4.038  -72.276  1.00 13.96 ? 216 VAL   A N   1 
ATOM   967  C  CA  . VAL   A 1 123 ? 11.184  -2.594  -71.956  1.00 13.73 ? 216 VAL   A CA  1 
ATOM   968  C  C   . VAL   A 1 123 ? 10.549  -2.400  -70.585  1.00 13.96 ? 216 VAL   A C   1 
ATOM   969  O  O   . VAL   A 1 123 ? 9.458   -2.964  -70.344  1.00 13.64 ? 216 VAL   A O   1 
ATOM   970  C  CB  . VAL   A 1 123 ? 10.557  -1.702  -73.041  1.00 13.55 ? 216 VAL   A CB  1 
ATOM   971  C  CG1 . VAL   A 1 123 ? 9.106   -2.063  -73.316  1.00 13.70 ? 216 VAL   A CG1 1 
ATOM   972  C  CG2 . VAL   A 1 123 ? 10.700  -0.227  -72.694  1.00 13.53 ? 216 VAL   A CG2 1 
ATOM   973  N  N   . VAL   A 1 124 ? 11.231  -1.668  -69.710  1.00 14.38 ? 217 VAL   A N   1 
ATOM   974  C  CA  . VAL   A 1 124 ? 10.819  -1.536  -68.289  1.00 15.06 ? 217 VAL   A CA  1 
ATOM   975  C  C   . VAL   A 1 124 ? 10.926  -0.065  -67.899  1.00 15.49 ? 217 VAL   A C   1 
ATOM   976  O  O   . VAL   A 1 124 ? 11.885  0.604   -68.330  1.00 15.77 ? 217 VAL   A O   1 
ATOM   977  C  CB  . VAL   A 1 124 ? 11.634  -2.477  -67.382  1.00 15.57 ? 217 VAL   A CB  1 
ATOM   978  C  CG1 . VAL   A 1 124 ? 13.129  -2.214  -67.449  1.00 15.87 ? 217 VAL   A CG1 1 
ATOM   979  C  CG2 . VAL   A 1 124 ? 11.142  -2.436  -65.945  1.00 15.86 ? 217 VAL   A CG2 1 
ATOM   980  N  N   . VAL   A 1 125 ? 9.936   0.413   -67.147  1.00 15.48 ? 218 VAL   A N   1 
ATOM   981  C  CA  . VAL   A 1 125 ? 9.896   1.794   -66.591  1.00 15.98 ? 218 VAL   A CA  1 
ATOM   982  C  C   . VAL   A 1 125 ? 9.650   1.681   -65.093  1.00 16.08 ? 218 VAL   A C   1 
ATOM   983  O  O   . VAL   A 1 125 ? 9.059   0.699   -64.638  1.00 15.15 ? 218 VAL   A O   1 
ATOM   984  C  CB  . VAL   A 1 125 ? 8.813   2.655   -67.268  1.00 15.77 ? 218 VAL   A CB  1 
ATOM   985  C  CG1 . VAL   A 1 125 ? 9.095   2.853   -68.751  1.00 16.02 ? 218 VAL   A CG1 1 
ATOM   986  C  CG2 . VAL   A 1 125 ? 7.416   2.089   -67.053  1.00 16.30 ? 218 VAL   A CG2 1 
ATOM   987  N  N   . PRO   A 1 126 ? 10.079  2.687   -64.298  1.00 16.71 ? 219 PRO   A N   1 
ATOM   988  C  CA  . PRO   A 1 126 ? 9.687   2.774   -62.891  1.00 16.90 ? 219 PRO   A CA  1 
ATOM   989  C  C   . PRO   A 1 126 ? 8.160   2.868   -62.788  1.00 17.67 ? 219 PRO   A C   1 
ATOM   990  O  O   . PRO   A 1 126 ? 7.563   3.607   -63.569  1.00 16.87 ? 219 PRO   A O   1 
ATOM   991  C  CB  . PRO   A 1 126 ? 10.335  4.076   -62.392  1.00 16.96 ? 219 PRO   A CB  1 
ATOM   992  C  CG  . PRO   A 1 126 ? 11.445  4.353   -63.387  1.00 17.20 ? 219 PRO   A CG  1 
ATOM   993  C  CD  . PRO   A 1 126 ? 10.955  3.795   -64.706  1.00 16.96 ? 219 PRO   A CD  1 
ATOM   994  N  N   . TYR   A 1 127 ? 7.557   2.117   -61.866  1.00 18.36 ? 220 TYR   A N   1 
ATOM   995  C  CA  . TYR   A 1 127 ? 6.119   2.261   -61.539  1.00 19.25 ? 220 TYR   A CA  1 
ATOM   996  C  C   . TYR   A 1 127 ? 5.910   3.625   -60.879  1.00 20.98 ? 220 TYR   A C   1 
ATOM   997  O  O   . TYR   A 1 127 ? 6.611   3.932   -59.891  1.00 20.24 ? 220 TYR   A O   1 
ATOM   998  C  CB  . TYR   A 1 127 ? 5.601   1.182   -60.589  1.00 19.31 ? 220 TYR   A CB  1 
ATOM   999  C  CG  . TYR   A 1 127 ? 4.196   1.478   -60.133  1.00 19.49 ? 220 TYR   A CG  1 
ATOM   1000 C  CD1 . TYR   A 1 127 ? 3.108   1.116   -60.912  1.00 20.03 ? 220 TYR   A CD1 1 
ATOM   1001 C  CD2 . TYR   A 1 127 ? 3.952   2.179   -58.963  1.00 19.96 ? 220 TYR   A CD2 1 
ATOM   1002 C  CE1 . TYR   A 1 127 ? 1.813   1.412   -60.523  1.00 19.86 ? 220 TYR   A CE1 1 
ATOM   1003 C  CE2 . TYR   A 1 127 ? 2.661   2.481   -58.558  1.00 19.86 ? 220 TYR   A CE2 1 
ATOM   1004 C  CZ  . TYR   A 1 127 ? 1.589   2.097   -59.342  1.00 19.95 ? 220 TYR   A CZ  1 
ATOM   1005 O  OH  . TYR   A 1 127 ? 0.311   2.386   -58.960  1.00 20.04 ? 220 TYR   A OH  1 
ATOM   1006 N  N   . GLU   A 1 128 ? 4.976   4.409   -61.415  1.00 23.31 ? 221 GLU   A N   1 
ATOM   1007 C  CA  . GLU   A 1 128 ? 4.511   5.686   -60.820  1.00 25.46 ? 221 GLU   A CA  1 
ATOM   1008 C  C   . GLU   A 1 128 ? 3.070   5.491   -60.367  1.00 25.30 ? 221 GLU   A C   1 
ATOM   1009 O  O   . GLU   A 1 128 ? 2.277   4.876   -61.074  1.00 23.88 ? 221 GLU   A O   1 
ATOM   1010 C  CB  . GLU   A 1 128 ? 4.638   6.820   -61.837  1.00 28.59 ? 221 GLU   A CB  1 
ATOM   1011 C  CG  . GLU   A 1 128 ? 6.079   7.149   -62.192  1.00 30.90 ? 221 GLU   A CG  1 
ATOM   1012 C  CD  . GLU   A 1 128 ? 6.259   7.937   -63.481  1.00 34.54 ? 221 GLU   A CD  1 
ATOM   1013 O  OE1 . GLU   A 1 128 ? 5.437   7.764   -64.408  1.00 37.78 ? 221 GLU   A OE1 1 
ATOM   1014 O  OE2 . GLU   A 1 128 ? 7.234   8.712   -63.564  1.00 37.72 ? 221 GLU   A OE2 1 
ATOM   1015 N  N   . PRO   A 1 129 ? 2.684   5.966   -59.164  1.00 25.65 ? 222 PRO   A N   1 
ATOM   1016 C  CA  . PRO   A 1 129 ? 1.279   5.951   -58.772  1.00 25.56 ? 222 PRO   A CA  1 
ATOM   1017 C  C   . PRO   A 1 129 ? 0.492   6.851   -59.720  1.00 25.78 ? 222 PRO   A C   1 
ATOM   1018 O  O   . PRO   A 1 129 ? 1.076   7.675   -60.426  1.00 25.41 ? 222 PRO   A O   1 
ATOM   1019 C  CB  . PRO   A 1 129 ? 1.255   6.483   -57.331  1.00 26.42 ? 222 PRO   A CB  1 
ATOM   1020 C  CG  . PRO   A 1 129 ? 2.706   6.477   -56.873  1.00 27.12 ? 222 PRO   A CG  1 
ATOM   1021 C  CD  . PRO   A 1 129 ? 3.558   6.526   -58.124  1.00 26.36 ? 222 PRO   A CD  1 
ATOM   1022 N  N   . PRO   A 1 130 ? -0.851  6.719   -59.777  1.00 25.79 ? 223 PRO   A N   1 
ATOM   1023 C  CA  . PRO   A 1 130 ? -1.677  7.638   -60.559  1.00 27.53 ? 223 PRO   A CA  1 
ATOM   1024 C  C   . PRO   A 1 130 ? -1.443  9.101   -60.152  1.00 29.45 ? 223 PRO   A C   1 
ATOM   1025 O  O   . PRO   A 1 130 ? -1.213  9.356   -58.976  1.00 27.14 ? 223 PRO   A O   1 
ATOM   1026 C  CB  . PRO   A 1 130 ? -3.116  7.222   -60.220  1.00 26.68 ? 223 PRO   A CB  1 
ATOM   1027 C  CG  . PRO   A 1 130 ? -2.994  5.778   -59.775  1.00 26.71 ? 223 PRO   A CG  1 
ATOM   1028 C  CD  . PRO   A 1 130 ? -1.645  5.687   -59.093  1.00 25.94 ? 223 PRO   A CD  1 
ATOM   1029 N  N   . GLU   A 1 131 ? -1.507  10.018  -61.122  1.00 33.32 ? 224 GLU   A N   1 
ATOM   1030 C  CA  . GLU   A 1 131 ? -1.586  11.480  -60.859  1.00 37.19 ? 224 GLU   A CA  1 
ATOM   1031 C  C   . GLU   A 1 131 ? -2.753  11.712  -59.896  1.00 38.69 ? 224 GLU   A C   1 
ATOM   1032 O  O   . GLU   A 1 131 ? -3.745  10.963  -59.978  1.00 37.82 ? 224 GLU   A O   1 
ATOM   1033 C  CB  . GLU   A 1 131 ? -1.750  12.271  -62.158  1.00 39.72 ? 224 GLU   A CB  1 
ATOM   1034 C  CG  . GLU   A 1 131 ? -0.544  12.165  -63.075  1.00 42.90 ? 224 GLU   A CG  1 
ATOM   1035 C  CD  . GLU   A 1 131 ? -0.358  13.321  -64.041  1.00 44.48 ? 224 GLU   A CD  1 
ATOM   1036 O  OE1 . GLU   A 1 131 ? -1.367  13.957  -64.411  1.00 46.37 ? 224 GLU   A OE1 1 
ATOM   1037 O  OE2 . GLU   A 1 131 ? 0.802   13.590  -64.411  1.00 47.61 ? 224 GLU   A OE2 1 
ATOM   1038 N  N   . VAL   A 1 132 ? -2.615  12.686  -58.996  1.00 41.84 ? 225 VAL   A N   1 
ATOM   1039 C  CA  . VAL   A 1 132 ? -3.570  12.932  -57.874  1.00 43.99 ? 225 VAL   A CA  1 
ATOM   1040 C  C   . VAL   A 1 132 ? -4.957  13.224  -58.463  1.00 43.44 ? 225 VAL   A C   1 
ATOM   1041 O  O   . VAL   A 1 132 ? -5.063  14.149  -59.296  1.00 45.25 ? 225 VAL   A O   1 
ATOM   1042 C  CB  . VAL   A 1 132 ? -3.070  14.069  -56.962  1.00 47.16 ? 225 VAL   A CB  1 
ATOM   1043 C  CG1 . VAL   A 1 132 ? -4.115  14.466  -55.933  1.00 47.85 ? 225 VAL   A CG1 1 
ATOM   1044 C  CG2 . VAL   A 1 132 ? -1.759  13.703  -56.279  1.00 47.29 ? 225 VAL   A CG2 1 
ATOM   1045 N  N   . GLY   A 1 133 ? -5.967  12.442  -58.062  1.00 40.81 ? 226 GLY   A N   1 
ATOM   1046 C  CA  . GLY   A 1 133 ? -7.357  12.543  -58.552  1.00 39.90 ? 226 GLY   A CA  1 
ATOM   1047 C  C   . GLY   A 1 133 ? -7.652  11.582  -59.697  1.00 38.87 ? 226 GLY   A C   1 
ATOM   1048 O  O   . GLY   A 1 133 ? -8.803  11.596  -60.179  1.00 38.80 ? 226 GLY   A O   1 
ATOM   1049 N  N   . SER   A 1 134 ? -6.661  10.786  -60.128  1.00 35.85 ? 227 SER   A N   1 
ATOM   1050 C  CA  . SER   A 1 134 ? -6.797  9.740   -61.179  1.00 33.69 ? 227 SER   A CA  1 
ATOM   1051 C  C   . SER   A 1 134 ? -6.729  8.357   -60.526  1.00 31.56 ? 227 SER   A C   1 
ATOM   1052 O  O   . SER   A 1 134 ? -6.133  8.241   -59.442  1.00 30.61 ? 227 SER   A O   1 
ATOM   1053 C  CB  . SER   A 1 134 ? -5.750  9.894   -62.255  1.00 34.06 ? 227 SER   A CB  1 
ATOM   1054 O  OG  . SER   A 1 134 ? -5.869  8.868   -63.232  1.00 34.58 ? 227 SER   A OG  1 
ATOM   1055 N  N   . ASP   A 1 135 ? -7.315  7.347   -61.174  1.00 30.02 ? 228 ASP   A N   1 
ATOM   1056 C  CA  . ASP   A 1 135 ? -7.513  5.993   -60.592  1.00 29.62 ? 228 ASP   A CA  1 
ATOM   1057 C  C   . ASP   A 1 135 ? -6.573  4.969   -61.241  1.00 26.48 ? 228 ASP   A C   1 
ATOM   1058 O  O   . ASP   A 1 135 ? -6.613  3.804   -60.814  1.00 25.82 ? 228 ASP   A O   1 
ATOM   1059 C  CB  . ASP   A 1 135 ? -8.975  5.563   -60.725  1.00 32.56 ? 228 ASP   A CB  1 
ATOM   1060 C  CG  . ASP   A 1 135 ? -9.924  6.268   -59.768  1.00 35.46 ? 228 ASP   A CG  1 
ATOM   1061 O  OD1 . ASP   A 1 135 ? -9.435  6.943   -58.825  1.00 36.06 ? 228 ASP   A OD1 1 
ATOM   1062 O  OD2 . ASP   A 1 135 ? -11.150 6.132   -59.969  1.00 38.16 ? 228 ASP   A OD2 1 
ATOM   1063 N  N   . CYS   A 1 136 ? -5.747  5.366   -62.215  1.00 24.36 ? 229 CYS   A N   1 
ATOM   1064 C  CA  . CYS   A 1 136 ? -4.802  4.437   -62.894  1.00 23.20 ? 229 CYS   A CA  1 
ATOM   1065 C  C   . CYS   A 1 136 ? -3.541  5.162   -63.377  1.00 21.86 ? 229 CYS   A C   1 
ATOM   1066 O  O   . CYS   A 1 136 ? -3.551  6.401   -63.494  1.00 21.76 ? 229 CYS   A O   1 
ATOM   1067 C  CB  . CYS   A 1 136 ? -5.480  3.712   -64.049  1.00 22.49 ? 229 CYS   A CB  1 
ATOM   1068 S  SG  . CYS   A 1 136 ? -6.134  4.811   -65.333  1.00 22.45 ? 229 CYS   A SG  1 
ATOM   1069 N  N   . THR   A 1 137 ? -2.482  4.387   -63.617  1.00 21.20 ? 230 THR   A N   1 
ATOM   1070 C  CA  . THR   A 1 137 ? -1.211  4.847   -64.230  1.00 20.36 ? 230 THR   A CA  1 
ATOM   1071 C  C   . THR   A 1 137 ? -1.246  4.479   -65.712  1.00 19.51 ? 230 THR   A C   1 
ATOM   1072 O  O   . THR   A 1 137 ? -1.473  3.299   -66.008  1.00 19.38 ? 230 THR   A O   1 
ATOM   1073 C  CB  . THR   A 1 137 ? 0.009   4.235   -63.532  1.00 19.89 ? 230 THR   A CB  1 
ATOM   1074 O  OG1 . THR   A 1 137 ? -0.093  4.529   -62.139  1.00 20.35 ? 230 THR   A OG1 1 
ATOM   1075 C  CG2 . THR   A 1 137 ? 1.317   4.761   -64.080  1.00 20.08 ? 230 THR   A CG2 1 
ATOM   1076 N  N   . THR   A 1 138 ? -1.036  5.454   -66.597  1.00 19.19 ? 231 THR   A N   1 
ATOM   1077 C  CA  . THR   A 1 138 ? -1.011  5.244   -68.066  1.00 18.72 ? 231 THR   A CA  1 
ATOM   1078 C  C   . THR   A 1 138 ? 0.446   5.192   -68.526  1.00 18.57 ? 231 THR   A C   1 
ATOM   1079 O  O   . THR   A 1 138 ? 1.227   6.082   -68.132  1.00 17.79 ? 231 THR   A O   1 
ATOM   1080 C  CB  . THR   A 1 138 ? -1.813  6.313   -68.815  1.00 18.79 ? 231 THR   A CB  1 
ATOM   1081 O  OG1 . THR   A 1 138 ? -3.169  6.211   -68.389  1.00 18.68 ? 231 THR   A OG1 1 
ATOM   1082 C  CG2 . THR   A 1 138 ? -1.755  6.150   -70.318  1.00 18.95 ? 231 THR   A CG2 1 
ATOM   1083 N  N   . ILE   A 1 139 ? 0.790   4.153   -69.287  1.00 17.71 ? 232 ILE   A N   1 
ATOM   1084 C  CA  . ILE   A 1 139 ? 2.083   4.039   -70.017  1.00 17.69 ? 232 ILE   A CA  1 
ATOM   1085 C  C   . ILE   A 1 139 ? 1.749   4.141   -71.506  1.00 17.16 ? 232 ILE   A C   1 
ATOM   1086 O  O   . ILE   A 1 139 ? 0.737   3.532   -71.930  1.00 16.77 ? 232 ILE   A O   1 
ATOM   1087 C  CB  . ILE   A 1 139 ? 2.827   2.739   -69.647  1.00 17.48 ? 232 ILE   A CB  1 
ATOM   1088 C  CG1 . ILE   A 1 139 ? 3.138   2.684   -68.147  1.00 18.18 ? 232 ILE   A CG1 1 
ATOM   1089 C  CG2 . ILE   A 1 139 ? 4.085   2.578   -70.488  1.00 17.64 ? 232 ILE   A CG2 1 
ATOM   1090 C  CD1 . ILE   A 1 139 ? 3.788   1.398   -67.693  1.00 18.11 ? 232 ILE   A CD1 1 
ATOM   1091 N  N   . HIS   A 1 140 ? 2.523   4.939   -72.242  1.00 16.83 ? 233 HIS   A N   1 
ATOM   1092 C  CA  . HIS   A 1 140 ? 2.401   5.110   -73.711  1.00 16.97 ? 233 HIS   A CA  1 
ATOM   1093 C  C   . HIS   A 1 140 ? 3.390   4.170   -74.401  1.00 16.45 ? 233 HIS   A C   1 
ATOM   1094 O  O   . HIS   A 1 140 ? 4.587   4.510   -74.482  1.00 16.27 ? 233 HIS   A O   1 
ATOM   1095 C  CB  . HIS   A 1 140 ? 2.602   6.574   -74.114  1.00 17.75 ? 233 HIS   A CB  1 
ATOM   1096 C  CG  . HIS   A 1 140 ? 1.456   7.451   -73.740  1.00 18.66 ? 233 HIS   A CG  1 
ATOM   1097 N  ND1 . HIS   A 1 140 ? 1.539   8.828   -73.784  1.00 19.78 ? 233 HIS   A ND1 1 
ATOM   1098 C  CD2 . HIS   A 1 140 ? 0.207   7.157   -73.319  1.00 18.74 ? 233 HIS   A CD2 1 
ATOM   1099 C  CE1 . HIS   A 1 140 ? 0.384   9.344   -73.415  1.00 19.96 ? 233 HIS   A CE1 1 
ATOM   1100 N  NE2 . HIS   A 1 140 ? -0.447  8.339   -73.118  1.00 19.56 ? 233 HIS   A NE2 1 
ATOM   1101 N  N   . TYR   A 1 141 ? 2.894   3.030   -74.876  1.00 15.41 ? 234 TYR   A N   1 
ATOM   1102 C  CA  . TYR   A 1 141 ? 3.679   2.058   -75.670  1.00 15.39 ? 234 TYR   A CA  1 
ATOM   1103 C  C   . TYR   A 1 141 ? 3.612   2.454   -77.146  1.00 15.74 ? 234 TYR   A C   1 
ATOM   1104 O  O   . TYR   A 1 141 ? 2.611   3.073   -77.566  1.00 16.29 ? 234 TYR   A O   1 
ATOM   1105 C  CB  . TYR   A 1 141 ? 3.175   0.638   -75.420  1.00 15.12 ? 234 TYR   A CB  1 
ATOM   1106 C  CG  . TYR   A 1 141 ? 3.519   0.130   -74.046  1.00 14.96 ? 234 TYR   A CG  1 
ATOM   1107 C  CD1 . TYR   A 1 141 ? 4.830   -0.149  -73.699  1.00 14.45 ? 234 TYR   A CD1 1 
ATOM   1108 C  CD2 . TYR   A 1 141 ? 2.540   -0.052  -73.086  1.00 14.52 ? 234 TYR   A CD2 1 
ATOM   1109 C  CE1 . TYR   A 1 141 ? 5.162   -0.598  -72.432  1.00 14.50 ? 234 TYR   A CE1 1 
ATOM   1110 C  CE2 . TYR   A 1 141 ? 2.853   -0.508  -71.817  1.00 14.65 ? 234 TYR   A CE2 1 
ATOM   1111 C  CZ  . TYR   A 1 141 ? 4.167   -0.785  -71.489  1.00 14.45 ? 234 TYR   A CZ  1 
ATOM   1112 O  OH  . TYR   A 1 141 ? 4.470   -1.240  -70.241  1.00 14.46 ? 234 TYR   A OH  1 
ATOM   1113 N  N   . ASN   A 1 142 ? 4.680   2.142   -77.881  1.00 15.60 ? 235 ASN   A N   1 
ATOM   1114 C  CA  . ASN   A 1 142 ? 4.768   2.238   -79.359  1.00 16.17 ? 235 ASN   A CA  1 
ATOM   1115 C  C   . ASN   A 1 142 ? 5.176   0.859   -79.880  1.00 16.11 ? 235 ASN   A C   1 
ATOM   1116 O  O   . ASN   A 1 142 ? 6.167   0.309   -79.366  1.00 16.17 ? 235 ASN   A O   1 
ATOM   1117 C  CB  . ASN   A 1 142 ? 5.791   3.278   -79.828  1.00 16.71 ? 235 ASN   A CB  1 
ATOM   1118 C  CG  . ASN   A 1 142 ? 5.483   4.706   -79.426  1.00 17.24 ? 235 ASN   A CG  1 
ATOM   1119 O  OD1 . ASN   A 1 142 ? 6.361   5.564   -79.483  1.00 18.03 ? 235 ASN   A OD1 1 
ATOM   1120 N  ND2 . ASN   A 1 142 ? 4.251   4.986   -79.038  1.00 17.38 ? 235 ASN   A ND2 1 
ATOM   1121 N  N   . TYR   A 1 143 ? 4.433   0.314   -80.843  1.00 16.08 ? 236 TYR   A N   1 
ATOM   1122 C  CA  . TYR   A 1 143 ? 4.777   -0.945  -81.549  1.00 16.14 ? 236 TYR   A CA  1 
ATOM   1123 C  C   . TYR   A 1 143 ? 5.412   -0.562  -82.887  1.00 16.62 ? 236 TYR   A C   1 
ATOM   1124 O  O   . TYR   A 1 143 ? 4.767   0.148   -83.676  1.00 16.34 ? 236 TYR   A O   1 
ATOM   1125 C  CB  . TYR   A 1 143 ? 3.546   -1.839  -81.687  1.00 15.83 ? 236 TYR   A CB  1 
ATOM   1126 C  CG  . TYR   A 1 143 ? 3.059   -2.409  -80.380  1.00 15.28 ? 236 TYR   A CG  1 
ATOM   1127 C  CD1 . TYR   A 1 143 ? 2.202   -1.687  -79.571  1.00 15.35 ? 236 TYR   A CD1 1 
ATOM   1128 C  CD2 . TYR   A 1 143 ? 3.474   -3.655  -79.938  1.00 15.39 ? 236 TYR   A CD2 1 
ATOM   1129 C  CE1 . TYR   A 1 143 ? 1.756   -2.185  -78.360  1.00 15.29 ? 236 TYR   A CE1 1 
ATOM   1130 C  CE2 . TYR   A 1 143 ? 3.039   -4.173  -78.727  1.00 15.25 ? 236 TYR   A CE2 1 
ATOM   1131 C  CZ  . TYR   A 1 143 ? 2.179   -3.432  -77.934  1.00 15.38 ? 236 TYR   A CZ  1 
ATOM   1132 O  OH  . TYR   A 1 143 ? 1.738   -3.912  -76.738  1.00 15.41 ? 236 TYR   A OH  1 
ATOM   1133 N  N   . MET   A 1 144 ? 6.642   -1.019  -83.123  1.00 17.85 ? 237 MET   A N   1 
ATOM   1134 C  CA  . MET   A 1 144 ? 7.549   -0.442  -84.151  1.00 18.00 ? 237 MET   A CA  1 
ATOM   1135 C  C   . MET   A 1 144 ? 7.652   -1.355  -85.378  1.00 18.61 ? 237 MET   A C   1 
ATOM   1136 O  O   . MET   A 1 144 ? 8.503   -1.076  -86.234  1.00 17.23 ? 237 MET   A O   1 
ATOM   1137 C  CB  . MET   A 1 144 ? 8.932   -0.214  -83.541  1.00 18.27 ? 237 MET   A CB  1 
ATOM   1138 C  CG  . MET   A 1 144 ? 8.905   0.770   -82.390  1.00 18.34 ? 237 MET   A CG  1 
ATOM   1139 S  SD  . MET   A 1 144 ? 8.067   2.323   -82.798  1.00 18.59 ? 237 MET   A SD  1 
ATOM   1140 C  CE  . MET   A 1 144 ? 9.104   2.929   -84.130  1.00 18.57 ? 237 MET   A CE  1 
ATOM   1141 N  N   . CYS   A 1 145 ? 6.796   -2.378  -85.463  1.00 19.78 ? 238 CYS   A N   1 
ATOM   1142 C  CA  . CYS   A 1 145 ? 6.587   -3.252  -86.653  1.00 21.33 ? 238 CYS   A CA  1 
ATOM   1143 C  C   . CYS   A 1 145 ? 5.094   -3.543  -86.806  1.00 22.23 ? 238 CYS   A C   1 
ATOM   1144 O  O   . CYS   A 1 145 ? 4.404   -3.613  -85.770  1.00 21.60 ? 238 CYS   A O   1 
ATOM   1145 C  CB  . CYS   A 1 145 ? 7.305   -4.589  -86.517  1.00 21.98 ? 238 CYS   A CB  1 
ATOM   1146 S  SG  . CYS   A 1 145 ? 8.809   -4.663  -87.417  1.00 23.05 ? 238 CYS   A SG  1 
ATOM   1147 N  N   . ASN   A 1 146 ? 4.634   -3.720  -88.046  1.00 22.81 ? 239 ASN   A N   1 
ATOM   1148 C  CA  . ASN   A 1 146 ? 3.237   -4.108  -88.379  1.00 23.85 ? 239 ASN   A CA  1 
ATOM   1149 C  C   . ASN   A 1 146 ? 3.112   -5.630  -88.281  1.00 22.78 ? 239 ASN   A C   1 
ATOM   1150 O  O   . ASN   A 1 146 ? 4.112   -6.330  -88.547  1.00 22.43 ? 239 ASN   A O   1 
ATOM   1151 C  CB  . ASN   A 1 146 ? 2.823   -3.598  -89.762  1.00 25.31 ? 239 ASN   A CB  1 
ATOM   1152 C  CG  . ASN   A 1 146 ? 2.306   -2.177  -89.726  1.00 27.24 ? 239 ASN   A CG  1 
ATOM   1153 O  OD1 . ASN   A 1 146 ? 1.526   -1.819  -88.845  1.00 30.23 ? 239 ASN   A OD1 1 
ATOM   1154 N  ND2 . ASN   A 1 146 ? 2.729   -1.359  -90.676  1.00 28.94 ? 239 ASN   A ND2 1 
ATOM   1155 N  N   . SER   A 1 147 ? 1.927   -6.124  -87.923  1.00 22.60 ? 240 SER   A N   1 
ATOM   1156 C  CA  . SER   A 1 147 ? 1.625   -7.577  -87.831  1.00 23.47 ? 240 SER   A CA  1 
ATOM   1157 C  C   . SER   A 1 147 ? 1.907   -8.257  -89.177  1.00 24.61 ? 240 SER   A C   1 
ATOM   1158 O  O   . SER   A 1 147 ? 2.294   -9.438  -89.153  1.00 25.36 ? 240 SER   A O   1 
ATOM   1159 C  CB  . SER   A 1 147 ? 0.211   -7.823  -87.371  1.00 23.29 ? 240 SER   A CB  1 
ATOM   1160 O  OG  . SER   A 1 147 ? 0.058   -7.464  -86.005  1.00 22.49 ? 240 SER   A OG  1 
ATOM   1161 N  N   . SER   A 1 148 ? 1.756   -7.531  -90.293  1.00 25.21 ? 241 SER   A N   1 
ATOM   1162 C  CA  . SER   A 1 148 ? 1.863   -8.060  -91.683  1.00 26.04 ? 241 SER   A CA  1 
ATOM   1163 C  C   . SER   A 1 148 ? 3.302   -8.009  -92.228  1.00 27.34 ? 241 SER   A C   1 
ATOM   1164 O  O   . SER   A 1 148 ? 3.505   -8.475  -93.368  1.00 28.76 ? 241 SER   A O   1 
ATOM   1165 C  CB  . SER   A 1 148 ? 0.923   -7.316  -92.593  1.00 26.32 ? 241 SER   A CB  1 
ATOM   1166 O  OG  . SER   A 1 148 ? 1.299   -5.950  -92.696  1.00 27.07 ? 241 SER   A OG  1 
ATOM   1167 N  N   . CYS   A 1 149 ? 4.269   -7.471  -91.478  1.00 26.92 ? 242 CYS   A N   1 
ATOM   1168 C  CA  . CYS   A 1 149 ? 5.702   -7.386  -91.892  1.00 27.70 ? 242 CYS   A CA  1 
ATOM   1169 C  C   . CYS   A 1 149 ? 6.287   -8.772  -92.214  1.00 29.34 ? 242 CYS   A C   1 
ATOM   1170 O  O   . CYS   A 1 149 ? 6.326   -9.608  -91.296  1.00 30.51 ? 242 CYS   A O   1 
ATOM   1171 C  CB  . CYS   A 1 149 ? 6.552   -6.780  -90.785  1.00 24.87 ? 242 CYS   A CB  1 
ATOM   1172 S  SG  . CYS   A 1 149 ? 6.547   -5.034  -90.808  1.00 23.25 ? 242 CYS   A SG  1 
ATOM   1173 N  N   . MET   A 1 150 ? 6.770   -8.998  -93.447  1.00 33.40 ? 243 MET   A N   1 
ATOM   1174 C  CA  . MET   A 1 150 ? 7.566   -10.214 -93.796  1.00 35.19 ? 243 MET   A CA  1 
ATOM   1175 C  C   . MET   A 1 150 ? 8.970   -10.052 -93.213  1.00 33.19 ? 243 MET   A C   1 
ATOM   1176 O  O   . MET   A 1 150 ? 9.509   -8.925  -93.265  1.00 31.06 ? 243 MET   A O   1 
ATOM   1177 C  CB  . MET   A 1 150 ? 7.708   -10.470 -95.302  1.00 39.06 ? 243 MET   A CB  1 
ATOM   1178 C  CG  . MET   A 1 150 ? 6.771   -11.538 -95.832  1.00 41.69 ? 243 MET   A CG  1 
ATOM   1179 S  SD  . MET   A 1 150 ? 7.407   -13.213 -95.546  1.00 48.64 ? 243 MET   A SD  1 
ATOM   1180 C  CE  . MET   A 1 150 ? 8.432   -13.434 -97.001  1.00 47.36 ? 243 MET   A CE  1 
ATOM   1181 N  N   . GLY   A 1 151 ? 9.533   -11.147 -92.703  1.00 32.88 ? 244 GLY   A N   1 
ATOM   1182 C  CA  . GLY   A 1 151 ? 10.845  -11.166 -92.032  1.00 32.80 ? 244 GLY   A CA  1 
ATOM   1183 C  C   . GLY   A 1 151 ? 10.709  -10.944 -90.536  1.00 31.63 ? 244 GLY   A C   1 
ATOM   1184 O  O   . GLY   A 1 151 ? 11.687  -11.209 -89.817  1.00 33.08 ? 244 GLY   A O   1 
ATOM   1185 N  N   . GLY   A 1 152 ? 9.539   -10.484 -90.083  1.00 30.67 ? 245 GLY   A N   1 
ATOM   1186 C  CA  . GLY   A 1 152 ? 9.242   -10.223 -88.665  1.00 30.12 ? 245 GLY   A CA  1 
ATOM   1187 C  C   . GLY   A 1 152 ? 8.123   -11.117 -88.168  1.00 29.73 ? 245 GLY   A C   1 
ATOM   1188 O  O   . GLY   A 1 152 ? 8.270   -12.352 -88.245  1.00 30.83 ? 245 GLY   A O   1 
ATOM   1189 N  N   . MET   A 1 153 ? 7.036   -10.517 -87.680  1.00 28.30 ? 246 MET   A N   1 
ATOM   1190 C  CA  . MET   A 1 153 ? 5.858   -11.249 -87.146  1.00 26.82 ? 246 MET   A CA  1 
ATOM   1191 C  C   . MET   A 1 153 ? 5.138   -11.977 -88.289  1.00 27.16 ? 246 MET   A C   1 
ATOM   1192 O  O   . MET   A 1 153 ? 4.646   -13.088 -88.049  1.00 27.14 ? 246 MET   A O   1 
ATOM   1193 C  CB  . MET   A 1 153 ? 4.905   -10.287 -86.435  1.00 26.08 ? 246 MET   A CB  1 
ATOM   1194 C  CG  . MET   A 1 153 ? 5.482   -9.736  -85.147  1.00 25.13 ? 246 MET   A CG  1 
ATOM   1195 S  SD  . MET   A 1 153 ? 4.351   -8.585  -84.342  1.00 23.85 ? 246 MET   A SD  1 
ATOM   1196 C  CE  . MET   A 1 153 ? 4.670   -7.085  -85.268  1.00 24.44 ? 246 MET   A CE  1 
ATOM   1197 N  N   . ASN   A 1 154 ? 5.083   -11.376 -89.481  1.00 29.31 ? 247 ASN   A N   1 
ATOM   1198 C  CA  . ASN   A 1 154 ? 4.620   -12.043 -90.730  1.00 30.71 ? 247 ASN   A CA  1 
ATOM   1199 C  C   . ASN   A 1 154 ? 3.213   -12.620 -90.514  1.00 31.20 ? 247 ASN   A C   1 
ATOM   1200 O  O   . ASN   A 1 154 ? 2.993   -13.797 -90.868  1.00 31.19 ? 247 ASN   A O   1 
ATOM   1201 C  CB  . ASN   A 1 154 ? 5.624   -13.114 -91.172  1.00 31.89 ? 247 ASN   A CB  1 
ATOM   1202 C  CG  . ASN   A 1 154 ? 5.285   -13.747 -92.507  1.00 32.46 ? 247 ASN   A CG  1 
ATOM   1203 O  OD1 . ASN   A 1 154 ? 4.642   -13.125 -93.352  1.00 32.32 ? 247 ASN   A OD1 1 
ATOM   1204 N  ND2 . ASN   A 1 154 ? 5.710   -14.986 -92.701  1.00 31.98 ? 247 ASN   A ND2 1 
ATOM   1205 N  N   . ARG   A 1 155 ? 2.318   -11.821 -89.917  1.00 30.24 ? 248 ARG   A N   1 
ATOM   1206 C  CA  . ARG   A 1 155 ? 0.863   -12.088 -89.733  1.00 30.72 ? 248 ARG   A CA  1 
ATOM   1207 C  C   . ARG   A 1 155 ? 0.618   -13.019 -88.540  1.00 28.05 ? 248 ARG   A C   1 
ATOM   1208 O  O   . ARG   A 1 155 ? -0.556  -13.298 -88.260  1.00 26.51 ? 248 ARG   A O   1 
ATOM   1209 C  CB  . ARG   A 1 155 ? 0.235   -12.664 -91.007  1.00 33.30 ? 248 ARG   A CB  1 
ATOM   1210 C  CG  . ARG   A 1 155 ? 0.395   -11.774 -92.231  1.00 35.85 ? 248 ARG   A CG  1 
ATOM   1211 C  CD  . ARG   A 1 155 ? -0.309  -12.334 -93.451  1.00 38.80 ? 248 ARG   A CD  1 
ATOM   1212 N  NE  . ARG   A 1 155 ? -1.760  -12.344 -93.310  1.00 41.68 ? 248 ARG   A NE  1 
ATOM   1213 C  CZ  . ARG   A 1 155 ? -2.612  -12.782 -94.237  1.00 44.83 ? 248 ARG   A CZ  1 
ATOM   1214 N  NH1 . ARG   A 1 155 ? -3.914  -12.747 -94.005  1.00 46.30 ? 248 ARG   A NH1 1 
ATOM   1215 N  NH2 . ARG   A 1 155 ? -2.166  -13.255 -95.390  1.00 45.58 ? 248 ARG   A NH2 1 
ATOM   1216 N  N   . ARG   A 1 156 ? 1.662   -13.462 -87.834  1.00 26.29 ? 249 ARG   A N   1 
ATOM   1217 C  CA  . ARG   A 1 156 ? 1.492   -14.316 -86.629  1.00 25.75 ? 249 ARG   A CA  1 
ATOM   1218 C  C   . ARG   A 1 156 ? 1.022   -13.436 -85.473  1.00 24.03 ? 249 ARG   A C   1 
ATOM   1219 O  O   . ARG   A 1 156 ? 1.647   -12.423 -85.172  1.00 23.84 ? 249 ARG   A O   1 
ATOM   1220 C  CB  . ARG   A 1 156 ? 2.789   -15.047 -86.278  1.00 26.13 ? 249 ARG   A CB  1 
ATOM   1221 C  CG  . ARG   A 1 156 ? 3.264   -16.010 -87.356  1.00 26.93 ? 249 ARG   A CG  1 
ATOM   1222 C  CD  . ARG   A 1 156 ? 4.641   -16.554 -87.054  1.00 27.74 ? 249 ARG   A CD  1 
ATOM   1223 N  NE  . ARG   A 1 156 ? 5.680   -15.538 -87.167  1.00 28.48 ? 249 ARG   A NE  1 
ATOM   1224 C  CZ  . ARG   A 1 156 ? 6.980   -15.766 -87.004  1.00 29.23 ? 249 ARG   A CZ  1 
ATOM   1225 N  NH1 . ARG   A 1 156 ? 7.410   -16.981 -86.710  1.00 29.76 ? 249 ARG   A NH1 1 
ATOM   1226 N  NH2 . ARG   A 1 156 ? 7.846   -14.776 -87.134  1.00 29.13 ? 249 ARG   A NH2 1 
ATOM   1227 N  N   . PRO   A 1 157 ? -0.084  -13.789 -84.784  1.00 23.38 ? 250 PRO   A N   1 
ATOM   1228 C  CA  . PRO   A 1 157 ? -0.546  -13.002 -83.643  1.00 22.48 ? 250 PRO   A CA  1 
ATOM   1229 C  C   . PRO   A 1 157 ? 0.456   -13.070 -82.483  1.00 21.41 ? 250 PRO   A C   1 
ATOM   1230 O  O   . PRO   A 1 157 ? 1.072   -14.112 -82.281  1.00 20.34 ? 250 PRO   A O   1 
ATOM   1231 C  CB  . PRO   A 1 157 ? -1.895  -13.629 -83.268  1.00 22.92 ? 250 PRO   A CB  1 
ATOM   1232 C  CG  . PRO   A 1 157 ? -1.828  -15.037 -83.820  1.00 23.98 ? 250 PRO   A CG  1 
ATOM   1233 C  CD  . PRO   A 1 157 ? -0.942  -14.953 -85.046  1.00 23.89 ? 250 PRO   A CD  1 
ATOM   1234 N  N   . ILE   A 1 158 ? 0.608   -11.955 -81.765  1.00 20.01 ? 251 ILE   A N   1 
ATOM   1235 C  CA  . ILE   A 1 158 ? 1.486   -11.843 -80.563  1.00 19.39 ? 251 ILE   A CA  1 
ATOM   1236 C  C   . ILE   A 1 158 ? 0.623   -11.498 -79.347  1.00 18.55 ? 251 ILE   A C   1 
ATOM   1237 O  O   . ILE   A 1 158 ? -0.479  -10.953 -79.531  1.00 17.19 ? 251 ILE   A O   1 
ATOM   1238 C  CB  . ILE   A 1 158 ? 2.588   -10.788 -80.775  1.00 19.04 ? 251 ILE   A CB  1 
ATOM   1239 C  CG1 . ILE   A 1 158 ? 1.999   -9.420  -81.135  1.00 19.48 ? 251 ILE   A CG1 1 
ATOM   1240 C  CG2 . ILE   A 1 158 ? 3.598   -11.266 -81.809  1.00 19.14 ? 251 ILE   A CG2 1 
ATOM   1241 C  CD1 . ILE   A 1 158 ? 2.954   -8.262  -80.932  1.00 19.75 ? 251 ILE   A CD1 1 
ATOM   1242 N  N   . LEU   A 1 159 ? 1.131   -11.803 -78.153  1.00 19.16 ? 252 LEU   A N   1 
ATOM   1243 C  CA  . LEU   A 1 159 ? 0.615   -11.285 -76.860  1.00 19.75 ? 252 LEU   A CA  1 
ATOM   1244 C  C   . LEU   A 1 159 ? 1.654   -10.312 -76.318  1.00 18.39 ? 252 LEU   A C   1 
ATOM   1245 O  O   . LEU   A 1 159 ? 2.853   -10.596 -76.493  1.00 18.27 ? 252 LEU   A O   1 
ATOM   1246 C  CB  . LEU   A 1 159 ? 0.411   -12.432 -75.867  1.00 21.46 ? 252 LEU   A CB  1 
ATOM   1247 C  CG  . LEU   A 1 159 ? -0.481  -13.576 -76.339  1.00 23.02 ? 252 LEU   A CG  1 
ATOM   1248 C  CD1 . LEU   A 1 159 ? -0.736  -14.551 -75.202  1.00 23.82 ? 252 LEU   A CD1 1 
ATOM   1249 C  CD2 . LEU   A 1 159 ? -1.794  -13.054 -76.894  1.00 24.02 ? 252 LEU   A CD2 1 
ATOM   1250 N  N   . THR   A 1 160 ? 1.214   -9.216  -75.704  1.00 16.76 ? 253 THR   A N   1 
ATOM   1251 C  CA  . THR   A 1 160 ? 2.057   -8.390  -74.807  1.00 16.08 ? 253 THR   A CA  1 
ATOM   1252 C  C   . THR   A 1 160 ? 1.778   -8.834  -73.371  1.00 15.85 ? 253 THR   A C   1 
ATOM   1253 O  O   . THR   A 1 160 ? 0.591   -8.895  -72.993  1.00 15.37 ? 253 THR   A O   1 
ATOM   1254 C  CB  . THR   A 1 160 ? 1.827   -6.894  -75.036  1.00 15.93 ? 253 THR   A CB  1 
ATOM   1255 O  OG1 . THR   A 1 160 ? 2.196   -6.635  -76.389  1.00 15.97 ? 253 THR   A OG1 1 
ATOM   1256 C  CG2 . THR   A 1 160 ? 2.628   -6.016  -74.100  1.00 15.92 ? 253 THR   A CG2 1 
ATOM   1257 N  N   . ILE   A 1 161 ? 2.840   -9.161  -72.630  1.00 15.50 ? 254 ILE   A N   1 
ATOM   1258 C  CA  . ILE   A 1 161 ? 2.802   -9.546  -71.188  1.00 15.47 ? 254 ILE   A CA  1 
ATOM   1259 C  C   . ILE   A 1 161 ? 3.311   -8.348  -70.384  1.00 15.41 ? 254 ILE   A C   1 
ATOM   1260 O  O   . ILE   A 1 161 ? 4.465   -7.920  -70.631  1.00 14.82 ? 254 ILE   A O   1 
ATOM   1261 C  CB  . ILE   A 1 161 ? 3.643   -10.815 -70.942  1.00 16.18 ? 254 ILE   A CB  1 
ATOM   1262 C  CG1 . ILE   A 1 161 ? 3.226   -11.950 -71.880  1.00 16.23 ? 254 ILE   A CG1 1 
ATOM   1263 C  CG2 . ILE   A 1 161 ? 3.590   -11.249 -69.482  1.00 16.23 ? 254 ILE   A CG2 1 
ATOM   1264 C  CD1 . ILE   A 1 161 ? 4.085   -13.173 -71.766  1.00 16.73 ? 254 ILE   A CD1 1 
ATOM   1265 N  N   . ILE   A 1 162 ? 2.460   -7.788  -69.515  1.00 15.05 ? 255 ILE   A N   1 
ATOM   1266 C  CA  . ILE   A 1 162 ? 2.831   -6.682  -68.587  1.00 15.09 ? 255 ILE   A CA  1 
ATOM   1267 C  C   . ILE   A 1 162 ? 3.051   -7.309  -67.211  1.00 15.94 ? 255 ILE   A C   1 
ATOM   1268 O  O   . ILE   A 1 162 ? 2.119   -7.969  -66.702  1.00 15.76 ? 255 ILE   A O   1 
ATOM   1269 C  CB  . ILE   A 1 162 ? 1.772   -5.560  -68.541  1.00 14.57 ? 255 ILE   A CB  1 
ATOM   1270 C  CG1 . ILE   A 1 162 ? 1.359   -5.088  -69.937  1.00 14.20 ? 255 ILE   A CG1 1 
ATOM   1271 C  CG2 . ILE   A 1 162 ? 2.260   -4.405  -67.678  1.00 14.19 ? 255 ILE   A CG2 1 
ATOM   1272 C  CD1 . ILE   A 1 162 ? 2.474   -4.466  -70.740  1.00 14.08 ? 255 ILE   A CD1 1 
ATOM   1273 N  N   . THR   A 1 163 ? 4.251   -7.141  -66.661  1.00 16.93 ? 256 THR   A N   1 
ATOM   1274 C  CA  . THR   A 1 163 ? 4.635   -7.659  -65.327  1.00 18.23 ? 256 THR   A CA  1 
ATOM   1275 C  C   . THR   A 1 163 ? 4.973   -6.475  -64.421  1.00 18.63 ? 256 THR   A C   1 
ATOM   1276 O  O   . THR   A 1 163 ? 5.726   -5.579  -64.859  1.00 19.06 ? 256 THR   A O   1 
ATOM   1277 C  CB  . THR   A 1 163 ? 5.782   -8.672  -65.429  1.00 19.55 ? 256 THR   A CB  1 
ATOM   1278 O  OG1 . THR   A 1 163 ? 6.920   -8.037  -66.005  1.00 20.77 ? 256 THR   A OG1 1 
ATOM   1279 C  CG2 . THR   A 1 163 ? 5.417   -9.876  -66.265  1.00 20.25 ? 256 THR   A CG2 1 
ATOM   1280 N  N   . LEU   A 1 164 ? 4.382   -6.467  -63.227  1.00 18.66 ? 257 LEU   A N   1 
ATOM   1281 C  CA  . LEU   A 1 164 ? 4.819   -5.649  -62.070  1.00 19.09 ? 257 LEU   A CA  1 
ATOM   1282 C  C   . LEU   A 1 164 ? 5.903   -6.455  -61.343  1.00 19.07 ? 257 LEU   A C   1 
ATOM   1283 O  O   . LEU   A 1 164 ? 5.633   -7.627  -61.022  1.00 19.04 ? 257 LEU   A O   1 
ATOM   1284 C  CB  . LEU   A 1 164 ? 3.596   -5.401  -61.182  1.00 19.50 ? 257 LEU   A CB  1 
ATOM   1285 C  CG  . LEU   A 1 164 ? 3.644   -4.182  -60.267  1.00 20.46 ? 257 LEU   A CG  1 
ATOM   1286 C  CD1 . LEU   A 1 164 ? 3.607   -2.888  -61.065  1.00 20.68 ? 257 LEU   A CD1 1 
ATOM   1287 C  CD2 . LEU   A 1 164 ? 2.483   -4.232  -59.284  1.00 21.14 ? 257 LEU   A CD2 1 
ATOM   1288 N  N   . GLU   A 1 165 ? 7.092   -5.881  -61.151  1.00 18.66 ? 258 GLU   A N   1 
ATOM   1289 C  CA  . GLU   A 1 165 ? 8.186   -6.512  -60.367  1.00 18.72 ? 258 GLU   A CA  1 
ATOM   1290 C  C   . GLU   A 1 165 ? 8.712   -5.519  -59.333  1.00 17.72 ? 258 GLU   A C   1 
ATOM   1291 O  O   . GLU   A 1 165 ? 8.645   -4.299  -59.578  1.00 16.92 ? 258 GLU   A O   1 
ATOM   1292 C  CB  . GLU   A 1 165 ? 9.343   -7.009  -61.237  1.00 19.55 ? 258 GLU   A CB  1 
ATOM   1293 C  CG  . GLU   A 1 165 ? 9.422   -6.396  -62.615  1.00 20.65 ? 258 GLU   A CG  1 
ATOM   1294 C  CD  . GLU   A 1 165 ? 10.597  -6.904  -63.430  1.00 20.69 ? 258 GLU   A CD  1 
ATOM   1295 O  OE1 . GLU   A 1 165 ? 10.375  -7.772  -64.299  1.00 22.50 ? 258 GLU   A OE1 1 
ATOM   1296 O  OE2 . GLU   A 1 165 ? 11.729  -6.446  -63.179  1.00 20.43 ? 258 GLU   A OE2 1 
ATOM   1297 N  N   . ASP   A 1 166 ? 9.231   -6.046  -58.226  1.00 17.67 ? 259 ASP   A N   1 
ATOM   1298 C  CA  . ASP   A 1 166 ? 9.897   -5.238  -57.174  1.00 18.26 ? 259 ASP   A CA  1 
ATOM   1299 C  C   . ASP   A 1 166 ? 11.285  -4.858  -57.707  1.00 18.43 ? 259 ASP   A C   1 
ATOM   1300 O  O   . ASP   A 1 166 ? 11.635  -5.300  -58.825  1.00 18.83 ? 259 ASP   A O   1 
ATOM   1301 C  CB  . ASP   A 1 166 ? 9.866   -5.964  -55.823  1.00 18.20 ? 259 ASP   A CB  1 
ATOM   1302 C  CG  . ASP   A 1 166 ? 10.790  -7.166  -55.690  1.00 18.55 ? 259 ASP   A CG  1 
ATOM   1303 O  OD1 . ASP   A 1 166 ? 11.570  -7.433  -56.633  1.00 18.11 ? 259 ASP   A OD1 1 
ATOM   1304 O  OD2 . ASP   A 1 166 ? 10.735  -7.819  -54.623  1.00 18.78 ? 259 ASP   A OD2 1 
ATOM   1305 N  N   . SER   A 1 167 ? 12.040  -4.055  -56.953  1.00 18.78 ? 260 SER   A N   1 
ATOM   1306 C  CA  . SER   A 1 167 ? 13.365  -3.514  -57.359  1.00 18.83 ? 260 SER   A CA  1 
ATOM   1307 C  C   . SER   A 1 167 ? 14.370  -4.648  -57.613  1.00 19.23 ? 260 SER   A C   1 
ATOM   1308 O  O   . SER   A 1 167 ? 15.374  -4.384  -58.287  1.00 19.98 ? 260 SER   A O   1 
ATOM   1309 C  CB  . SER   A 1 167 ? 13.883  -2.543  -56.326  1.00 18.87 ? 260 SER   A CB  1 
ATOM   1310 O  OG  . SER   A 1 167 ? 14.031  -3.184  -55.074  1.00 18.87 ? 260 SER   A OG  1 
ATOM   1311 N  N   . SER   A 1 168 ? 14.124  -5.858  -57.098  1.00 19.39 ? 261 SER   A N   1 
ATOM   1312 C  CA  . SER   A 1 168 ? 15.025  -7.034  -57.248  1.00 20.15 ? 261 SER   A CA  1 
ATOM   1313 C  C   . SER   A 1 168 ? 14.598  -7.911  -58.434  1.00 20.22 ? 261 SER   A C   1 
ATOM   1314 O  O   . SER   A 1 168 ? 15.339  -8.854  -58.751  1.00 21.17 ? 261 SER   A O   1 
ATOM   1315 C  CB  . SER   A 1 168 ? 15.091  -7.834  -55.970  1.00 19.82 ? 261 SER   A CB  1 
ATOM   1316 O  OG  . SER   A 1 168 ? 15.682  -7.072  -54.927  1.00 19.70 ? 261 SER   A OG  1 
ATOM   1317 N  N   . GLY   A 1 169 ? 13.449  -7.625  -59.055  1.00 20.59 ? 262 GLY   A N   1 
ATOM   1318 C  CA  . GLY   A 1 169 ? 12.924  -8.385  -60.209  1.00 20.64 ? 262 GLY   A CA  1 
ATOM   1319 C  C   . GLY   A 1 169 ? 11.927  -9.457  -59.799  1.00 20.82 ? 262 GLY   A C   1 
ATOM   1320 O  O   . GLY   A 1 169 ? 11.481  -10.198 -60.685  1.00 21.41 ? 262 GLY   A O   1 
ATOM   1321 N  N   . ASN   A 1 170 ? 11.573  -9.539  -58.512  1.00 20.91 ? 263 ASN   A N   1 
ATOM   1322 C  CA  . ASN   A 1 170 ? 10.570  -10.507 -57.992  1.00 20.82 ? 263 ASN   A CA  1 
ATOM   1323 C  C   . ASN   A 1 170 ? 9.191   -10.144 -58.560  1.00 20.25 ? 263 ASN   A C   1 
ATOM   1324 O  O   . ASN   A 1 170 ? 8.857   -8.951  -58.587  1.00 19.73 ? 263 ASN   A O   1 
ATOM   1325 C  CB  . ASN   A 1 170 ? 10.548  -10.554 -56.461  1.00 21.42 ? 263 ASN   A CB  1 
ATOM   1326 C  CG  . ASN   A 1 170 ? 11.887  -10.931 -55.862  1.00 21.68 ? 263 ASN   A CG  1 
ATOM   1327 O  OD1 . ASN   A 1 170 ? 12.450  -11.965 -56.213  1.00 21.93 ? 263 ASN   A OD1 1 
ATOM   1328 N  ND2 . ASN   A 1 170 ? 12.401  -10.107 -54.959  1.00 21.88 ? 263 ASN   A ND2 1 
ATOM   1329 N  N   . LEU   A 1 171 ? 8.426   -11.147 -58.991  1.00 20.10 ? 264 LEU   A N   1 
ATOM   1330 C  CA  . LEU   A 1 171 ? 7.083   -10.985 -59.610  1.00 19.85 ? 264 LEU   A CA  1 
ATOM   1331 C  C   . LEU   A 1 171 ? 6.090   -10.464 -58.562  1.00 19.35 ? 264 LEU   A C   1 
ATOM   1332 O  O   . LEU   A 1 171 ? 5.956   -11.122 -57.510  1.00 20.99 ? 264 LEU   A O   1 
ATOM   1333 C  CB  . LEU   A 1 171 ? 6.646   -12.344 -60.163  1.00 20.09 ? 264 LEU   A CB  1 
ATOM   1334 C  CG  . LEU   A 1 171 ? 5.284   -12.372 -60.853  1.00 20.93 ? 264 LEU   A CG  1 
ATOM   1335 C  CD1 . LEU   A 1 171 ? 5.343   -11.629 -62.181  1.00 20.47 ? 264 LEU   A CD1 1 
ATOM   1336 C  CD2 . LEU   A 1 171 ? 4.817   -13.806 -61.053  1.00 20.93 ? 264 LEU   A CD2 1 
ATOM   1337 N  N   . LEU   A 1 172 ? 5.438   -9.326  -58.827  1.00 18.22 ? 265 LEU   A N   1 
ATOM   1338 C  CA  . LEU   A 1 172 ? 4.341   -8.764  -57.983  1.00 17.68 ? 265 LEU   A CA  1 
ATOM   1339 C  C   . LEU   A 1 172 ? 2.978   -8.953  -58.661  1.00 17.68 ? 265 LEU   A C   1 
ATOM   1340 O  O   . LEU   A 1 172 ? 1.958   -8.975  -57.947  1.00 17.51 ? 265 LEU   A O   1 
ATOM   1341 C  CB  . LEU   A 1 172 ? 4.595   -7.275  -57.735  1.00 17.75 ? 265 LEU   A CB  1 
ATOM   1342 C  CG  . LEU   A 1 172 ? 5.883   -6.932  -56.990  1.00 17.38 ? 265 LEU   A CG  1 
ATOM   1343 C  CD1 . LEU   A 1 172 ? 6.011   -5.430  -56.804  1.00 17.01 ? 265 LEU   A CD1 1 
ATOM   1344 C  CD2 . LEU   A 1 172 ? 5.943   -7.643  -55.648  1.00 17.66 ? 265 LEU   A CD2 1 
ATOM   1345 N  N   . GLY   A 1 173 ? 2.951   -9.054  -59.990  1.00 17.38 ? 266 GLY   A N   1 
ATOM   1346 C  CA  . GLY   A 1 173 ? 1.699   -9.075  -60.762  1.00 17.47 ? 266 GLY   A CA  1 
ATOM   1347 C  C   . GLY   A 1 173 ? 1.955   -9.249  -62.243  1.00 17.76 ? 266 GLY   A C   1 
ATOM   1348 O  O   . GLY   A 1 173 ? 3.030   -8.829  -62.720  1.00 17.69 ? 266 GLY   A O   1 
ATOM   1349 N  N   . ARG   A 1 174 ? 0.997   -9.843  -62.955  1.00 18.05 ? 267 ARG   A N   1 
ATOM   1350 C  CA  . ARG   A 1 174 ? 1.125   -10.094 -64.410  1.00 17.88 ? 267 ARG   A CA  1 
ATOM   1351 C  C   . ARG   A 1 174 ? -0.257  -10.055 -65.062  1.00 17.94 ? 267 ARG   A C   1 
ATOM   1352 O  O   . ARG   A 1 174 ? -1.228  -10.570 -64.476  1.00 18.03 ? 267 ARG   A O   1 
ATOM   1353 C  CB  . ARG   A 1 174 ? 1.810   -11.435 -64.685  1.00 18.54 ? 267 ARG   A CB  1 
ATOM   1354 C  CG  . ARG   A 1 174 ? 2.123   -11.672 -66.157  1.00 18.84 ? 267 ARG   A CG  1 
ATOM   1355 C  CD  . ARG   A 1 174 ? 2.535   -13.096 -66.487  1.00 19.46 ? 267 ARG   A CD  1 
ATOM   1356 N  NE  . ARG   A 1 174 ? 3.754   -13.519 -65.807  1.00 20.06 ? 267 ARG   A NE  1 
ATOM   1357 C  CZ  . ARG   A 1 174 ? 3.831   -14.350 -64.765  1.00 20.95 ? 267 ARG   A CZ  1 
ATOM   1358 N  NH1 . ARG   A 1 174 ? 2.748   -14.876 -64.213  1.00 21.14 ? 267 ARG   A NH1 1 
ATOM   1359 N  NH2 . ARG   A 1 174 ? 5.014   -14.652 -64.268  1.00 21.45 ? 267 ARG   A NH2 1 
ATOM   1360 N  N   A ASN   A 1 175 ? -0.317  -9.459  -66.255  0.50 17.70 ? 268 ASN   A N   1 
ATOM   1361 N  N   B ASN   A 1 175 ? -0.338  -9.447  -66.246  0.50 17.65 ? 268 ASN   A N   1 
ATOM   1362 C  CA  A ASN   A 1 175 ? -1.498  -9.466  -67.155  0.50 17.65 ? 268 ASN   A CA  1 
ATOM   1363 C  CA  B ASN   A 1 175 ? -1.514  -9.539  -67.148  0.50 17.57 ? 268 ASN   A CA  1 
ATOM   1364 C  C   A ASN   A 1 175 ? -0.992  -9.498  -68.598  0.50 17.14 ? 268 ASN   A C   1 
ATOM   1365 C  C   B ASN   A 1 175 ? -0.999  -9.514  -68.589  0.50 17.10 ? 268 ASN   A C   1 
ATOM   1366 O  O   A ASN   A 1 175 ? 0.225   -9.301  -68.809  0.50 16.94 ? 268 ASN   A O   1 
ATOM   1367 O  O   B ASN   A 1 175 ? 0.216   -9.294  -68.788  0.50 16.93 ? 268 ASN   A O   1 
ATOM   1368 C  CB  A ASN   A 1 175 ? -2.421  -8.278  -66.877  0.50 17.70 ? 268 ASN   A CB  1 
ATOM   1369 C  CB  B ASN   A 1 175 ? -2.546  -8.444  -66.864  0.50 17.54 ? 268 ASN   A CB  1 
ATOM   1370 C  CG  A ASN   A 1 175 ? -3.226  -8.466  -65.611  0.50 17.95 ? 268 ASN   A CG  1 
ATOM   1371 C  CG  B ASN   A 1 175 ? -3.972  -8.928  -67.025  0.50 17.70 ? 268 ASN   A CG  1 
ATOM   1372 O  OD1 A ASN   A 1 175 ? -4.163  -9.260  -65.579  0.50 18.24 ? 268 ASN   A OD1 1 
ATOM   1373 O  OD1 B ASN   A 1 175 ? -4.317  -9.550  -68.028  0.50 17.43 ? 268 ASN   A OD1 1 
ATOM   1374 N  ND2 A ASN   A 1 175 ? -2.848  -7.763  -64.556  0.50 18.12 ? 268 ASN   A ND2 1 
ATOM   1375 N  ND2 B ASN   A 1 175 ? -4.808  -8.654  -66.036  0.50 18.07 ? 268 ASN   A ND2 1 
ATOM   1376 N  N   . SER   A 1 176 ? -1.891  -9.750  -69.551  1.00 16.75 ? 269 SER   A N   1 
ATOM   1377 C  CA  . SER   A 1 176 ? -1.535  -9.888  -70.980  1.00 16.35 ? 269 SER   A CA  1 
ATOM   1378 C  C   . SER   A 1 176 ? -2.723  -9.511  -71.856  1.00 15.74 ? 269 SER   A C   1 
ATOM   1379 O  O   . SER   A 1 176 ? -3.871  -9.570  -71.378  1.00 16.15 ? 269 SER   A O   1 
ATOM   1380 C  CB  . SER   A 1 176 ? -1.065  -11.284 -71.265  1.00 16.18 ? 269 SER   A CB  1 
ATOM   1381 O  OG  . SER   A 1 176 ? -2.055  -12.224 -70.888  1.00 15.93 ? 269 SER   A OG  1 
ATOM   1382 N  N   . PHE   A 1 177 ? -2.431  -9.124  -73.091  1.00 15.45 ? 270 PHE   A N   1 
ATOM   1383 C  CA  . PHE   A 1 177 ? -3.436  -8.842  -74.143  1.00 15.18 ? 270 PHE   A CA  1 
ATOM   1384 C  C   . PHE   A 1 177 ? -2.822  -9.186  -75.497  1.00 15.41 ? 270 PHE   A C   1 
ATOM   1385 O  O   . PHE   A 1 177 ? -1.594  -9.042  -75.658  1.00 14.95 ? 270 PHE   A O   1 
ATOM   1386 C  CB  . PHE   A 1 177 ? -3.907  -7.389  -74.053  1.00 14.79 ? 270 PHE   A CB  1 
ATOM   1387 C  CG  . PHE   A 1 177 ? -2.807  -6.358  -74.079  1.00 14.61 ? 270 PHE   A CG  1 
ATOM   1388 C  CD1 . PHE   A 1 177 ? -2.138  -6.005  -72.917  1.00 14.64 ? 270 PHE   A CD1 1 
ATOM   1389 C  CD2 . PHE   A 1 177 ? -2.451  -5.729  -75.263  1.00 14.31 ? 270 PHE   A CD2 1 
ATOM   1390 C  CE1 . PHE   A 1 177 ? -1.139  -5.044  -72.938  1.00 14.47 ? 270 PHE   A CE1 1 
ATOM   1391 C  CE2 . PHE   A 1 177 ? -1.447  -4.773  -75.280  1.00 14.59 ? 270 PHE   A CE2 1 
ATOM   1392 C  CZ  . PHE   A 1 177 ? -0.787  -4.440  -74.121  1.00 14.50 ? 270 PHE   A CZ  1 
ATOM   1393 N  N   . GLU   A 1 178 ? -3.651  -9.669  -76.425  1.00 16.04 ? 271 GLU   A N   1 
ATOM   1394 C  CA  . GLU   A 1 178 ? -3.269  -9.846  -77.845  1.00 16.47 ? 271 GLU   A CA  1 
ATOM   1395 C  C   . GLU   A 1 178 ? -3.080  -8.456  -78.455  1.00 16.57 ? 271 GLU   A C   1 
ATOM   1396 O  O   . GLU   A 1 178 ? -3.741  -7.504  -77.999  1.00 15.93 ? 271 GLU   A O   1 
ATOM   1397 C  CB  . GLU   A 1 178 ? -4.320  -10.662 -78.599  1.00 17.37 ? 271 GLU   A CB  1 
ATOM   1398 C  CG  . GLU   A 1 178 ? -3.938  -10.924 -80.045  1.00 18.08 ? 271 GLU   A CG  1 
ATOM   1399 C  CD  . GLU   A 1 178 ? -4.736  -12.008 -80.748  1.00 18.81 ? 271 GLU   A CD  1 
ATOM   1400 O  OE1 . GLU   A 1 178 ? -5.408  -12.801 -80.055  1.00 19.97 ? 271 GLU   A OE1 1 
ATOM   1401 O  OE2 . GLU   A 1 178 ? -4.670  -12.061 -81.988  1.00 19.27 ? 271 GLU   A OE2 1 
ATOM   1402 N  N   . VAL   A 1 179 ? -2.197  -8.340  -79.445  1.00 17.24 ? 272 VAL   A N   1 
ATOM   1403 C  CA  . VAL   A 1 179 ? -1.966  -7.064  -80.180  1.00 17.82 ? 272 VAL   A CA  1 
ATOM   1404 C  C   . VAL   A 1 179 ? -1.937  -7.362  -81.676  1.00 17.99 ? 272 VAL   A C   1 
ATOM   1405 O  O   . VAL   A 1 179 ? -1.191  -8.269  -82.083  1.00 18.09 ? 272 VAL   A O   1 
ATOM   1406 C  CB  . VAL   A 1 179 ? -0.668  -6.365  -79.742  1.00 18.16 ? 272 VAL   A CB  1 
ATOM   1407 C  CG1 . VAL   A 1 179 ? -0.470  -5.058  -80.498  1.00 18.60 ? 272 VAL   A CG1 1 
ATOM   1408 C  CG2 . VAL   A 1 179 ? -0.636  -6.142  -78.243  1.00 18.99 ? 272 VAL   A CG2 1 
ATOM   1409 N  N   . ARG   A 1 180 ? -2.720  -6.606  -82.441  1.00 18.20 ? 273 ARG   A N   1 
ATOM   1410 C  CA  . ARG   A 1 180 ? -2.570  -6.463  -83.908  1.00 19.55 ? 273 ARG   A CA  1 
ATOM   1411 C  C   . ARG   A 1 180 ? -2.127  -5.025  -84.181  1.00 19.37 ? 273 ARG   A C   1 
ATOM   1412 O  O   . ARG   A 1 180 ? -2.846  -4.082  -83.761  1.00 18.89 ? 273 ARG   A O   1 
ATOM   1413 C  CB  . ARG   A 1 180 ? -3.875  -6.808  -84.625  1.00 21.06 ? 273 ARG   A CB  1 
ATOM   1414 C  CG  . ARG   A 1 180 ? -3.828  -6.632  -86.135  1.00 22.34 ? 273 ARG   A CG  1 
ATOM   1415 C  CD  . ARG   A 1 180 ? -5.127  -7.111  -86.740  1.00 23.97 ? 273 ARG   A CD  1 
ATOM   1416 N  NE  . ARG   A 1 180 ? -5.353  -6.647  -88.101  1.00 25.89 ? 273 ARG   A NE  1 
ATOM   1417 C  CZ  . ARG   A 1 180 ? -4.790  -7.158  -89.193  1.00 28.61 ? 273 ARG   A CZ  1 
ATOM   1418 N  NH1 . ARG   A 1 180 ? -5.100  -6.664  -90.383  1.00 28.31 ? 273 ARG   A NH1 1 
ATOM   1419 N  NH2 . ARG   A 1 180 ? -3.922  -8.155  -89.101  1.00 29.92 ? 273 ARG   A NH2 1 
ATOM   1420 N  N   . VAL   A 1 181 ? -0.950  -4.878  -84.786  1.00 19.40 ? 274 VAL   A N   1 
ATOM   1421 C  CA  . VAL   A 1 181 ? -0.433  -3.585  -85.311  1.00 19.48 ? 274 VAL   A CA  1 
ATOM   1422 C  C   . VAL   A 1 181 ? -0.875  -3.512  -86.777  1.00 19.63 ? 274 VAL   A C   1 
ATOM   1423 O  O   . VAL   A 1 181 ? -0.468  -4.388  -87.561  1.00 19.23 ? 274 VAL   A O   1 
ATOM   1424 C  CB  . VAL   A 1 181 ? 1.095   -3.476  -85.135  1.00 19.67 ? 274 VAL   A CB  1 
ATOM   1425 C  CG1 . VAL   A 1 181 ? 1.589   -2.072  -85.445  1.00 19.60 ? 274 VAL   A CG1 1 
ATOM   1426 C  CG2 . VAL   A 1 181 ? 1.534   -3.898  -83.737  1.00 19.92 ? 274 VAL   A CG2 1 
ATOM   1427 N  N   . CYS   A 1 182 ? -1.730  -2.548  -87.117  1.00 20.02 ? 275 CYS   A N   1 
ATOM   1428 C  CA  . CYS   A 1 182 ? -2.411  -2.459  -88.435  1.00 20.67 ? 275 CYS   A CA  1 
ATOM   1429 C  C   . CYS   A 1 182 ? -2.708  -0.997  -88.782  1.00 21.29 ? 275 CYS   A C   1 
ATOM   1430 O  O   . CYS   A 1 182 ? -2.606  -0.141  -87.889  1.00 22.15 ? 275 CYS   A O   1 
ATOM   1431 C  CB  . CYS   A 1 182 ? -3.695  -3.281  -88.438  1.00 21.01 ? 275 CYS   A CB  1 
ATOM   1432 S  SG  . CYS   A 1 182 ? -4.780  -2.937  -87.026  1.00 20.59 ? 275 CYS   A SG  1 
ATOM   1433 N  N   . ALA   A 1 183 ? -3.086  -0.748  -90.036  1.00 21.68 ? 276 ALA   A N   1 
ATOM   1434 C  CA  . ALA   A 1 183 ? -3.252  0.597   -90.630  1.00 22.57 ? 276 ALA   A CA  1 
ATOM   1435 C  C   . ALA   A 1 183 ? -4.566  1.229   -90.151  1.00 22.93 ? 276 ALA   A C   1 
ATOM   1436 O  O   . ALA   A 1 183 ? -4.583  2.457   -89.948  1.00 23.56 ? 276 ALA   A O   1 
ATOM   1437 C  CB  . ALA   A 1 183 ? -3.197  0.493   -92.135  1.00 22.73 ? 276 ALA   A CB  1 
ATOM   1438 N  N   . CYS   A 1 184 ? -5.623  0.432   -89.968  1.00 23.50 ? 277 CYS   A N   1 
ATOM   1439 C  CA  . CYS   A 1 184 ? -6.977  0.922   -89.577  1.00 23.70 ? 277 CYS   A CA  1 
ATOM   1440 C  C   . CYS   A 1 184 ? -7.506  0.088   -88.410  1.00 22.87 ? 277 CYS   A C   1 
ATOM   1441 O  O   . CYS   A 1 184 ? -8.329  -0.808  -88.593  1.00 22.71 ? 277 CYS   A O   1 
ATOM   1442 C  CB  . CYS   A 1 184 ? -7.930  0.912   -90.770  1.00 25.60 ? 277 CYS   A CB  1 
ATOM   1443 S  SG  . CYS   A 1 184 ? -9.279  2.117   -90.621  1.00 29.67 ? 277 CYS   A SG  1 
ATOM   1444 N  N   . PRO   A 1 185 ? -7.028  0.352   -87.172  1.00 21.55 ? 278 PRO   A N   1 
ATOM   1445 C  CA  . PRO   A 1 185 ? -7.475  -0.383  -85.986  1.00 21.36 ? 278 PRO   A CA  1 
ATOM   1446 C  C   . PRO   A 1 185 ? -9.002  -0.445  -85.850  1.00 21.45 ? 278 PRO   A C   1 
ATOM   1447 O  O   . PRO   A 1 185 ? -9.521  -1.516  -85.569  1.00 21.02 ? 278 PRO   A O   1 
ATOM   1448 C  CB  . PRO   A 1 185 ? -6.882  0.421   -84.822  1.00 21.18 ? 278 PRO   A CB  1 
ATOM   1449 C  CG  . PRO   A 1 185 ? -5.650  1.066   -85.406  1.00 21.76 ? 278 PRO   A CG  1 
ATOM   1450 C  CD  . PRO   A 1 185 ? -6.003  1.357   -86.850  1.00 21.67 ? 278 PRO   A CD  1 
ATOM   1451 N  N   . GLY   A 1 186 ? -9.671  0.697   -86.059  1.00 21.31 ? 279 GLY   A N   1 
ATOM   1452 C  CA  . GLY   A 1 186 ? -11.137 0.826   -85.966  1.00 21.84 ? 279 GLY   A CA  1 
ATOM   1453 C  C   . GLY   A 1 186 ? -11.845 -0.187  -86.852  1.00 22.43 ? 279 GLY   A C   1 
ATOM   1454 O  O   . GLY   A 1 186 ? -12.611 -1.013  -86.317  1.00 21.06 ? 279 GLY   A O   1 
ATOM   1455 N  N   . ARG   A 1 187 ? -11.577 -0.143  -88.162  1.00 23.86 ? 280 ARG   A N   1 
ATOM   1456 C  CA  . ARG   A 1 187 ? -12.174 -1.062  -89.170  1.00 25.28 ? 280 ARG   A CA  1 
ATOM   1457 C  C   . ARG   A 1 187 ? -11.775 -2.507  -88.844  1.00 24.00 ? 280 ARG   A C   1 
ATOM   1458 O  O   . ARG   A 1 187 ? -12.649 -3.387  -88.925  1.00 23.19 ? 280 ARG   A O   1 
ATOM   1459 C  CB  . ARG   A 1 187 ? -11.724 -0.673  -90.583  1.00 28.19 ? 280 ARG   A CB  1 
ATOM   1460 C  CG  . ARG   A 1 187 ? -12.282 -1.546  -91.700  1.00 30.67 ? 280 ARG   A CG  1 
ATOM   1461 C  CD  . ARG   A 1 187 ? -11.450 -1.423  -92.969  1.00 33.89 ? 280 ARG   A CD  1 
ATOM   1462 N  NE  . ARG   A 1 187 ? -10.100 -1.939  -92.751  1.00 37.23 ? 280 ARG   A NE  1 
ATOM   1463 C  CZ  . ARG   A 1 187 ? -9.020  -1.641  -93.476  1.00 38.76 ? 280 ARG   A CZ  1 
ATOM   1464 N  NH1 . ARG   A 1 187 ? -9.094  -0.809  -94.503  1.00 39.68 ? 280 ARG   A NH1 1 
ATOM   1465 N  NH2 . ARG   A 1 187 ? -7.855  -2.186  -93.160  1.00 39.25 ? 280 ARG   A NH2 1 
ATOM   1466 N  N   . ASP   A 1 188 ? -10.505 -2.753  -88.504  1.00 24.14 ? 281 ASP   A N   1 
ATOM   1467 C  CA  . ASP   A 1 188 ? -9.985  -4.127  -88.261  1.00 23.79 ? 281 ASP   A CA  1 
ATOM   1468 C  C   . ASP   A 1 188 ? -10.669 -4.725  -87.026  1.00 23.02 ? 281 ASP   A C   1 
ATOM   1469 O  O   . ASP   A 1 188 ? -11.027 -5.913  -87.077  1.00 22.65 ? 281 ASP   A O   1 
ATOM   1470 C  CB  . ASP   A 1 188 ? -8.458  -4.149  -88.143  1.00 25.31 ? 281 ASP   A CB  1 
ATOM   1471 C  CG  . ASP   A 1 188 ? -7.741  -4.021  -89.476  1.00 26.72 ? 281 ASP   A CG  1 
ATOM   1472 O  OD1 . ASP   A 1 188 ? -8.416  -3.743  -90.487  1.00 27.91 ? 281 ASP   A OD1 1 
ATOM   1473 O  OD2 . ASP   A 1 188 ? -6.514  -4.202  -89.492  1.00 28.96 ? 281 ASP   A OD2 1 
ATOM   1474 N  N   . ARG   A 1 189 ? -10.846 -3.943  -85.956  1.00 21.96 ? 282 ARG   A N   1 
ATOM   1475 C  CA  . ARG   A 1 189 ? -11.523 -4.415  -84.717  1.00 20.73 ? 282 ARG   A CA  1 
ATOM   1476 C  C   . ARG   A 1 189 ? -12.973 -4.775  -85.057  1.00 20.79 ? 282 ARG   A C   1 
ATOM   1477 O  O   . ARG   A 1 189 ? -13.417 -5.877  -84.676  1.00 20.65 ? 282 ARG   A O   1 
ATOM   1478 C  CB  . ARG   A 1 189 ? -11.484 -3.368  -83.599  1.00 19.89 ? 282 ARG   A CB  1 
ATOM   1479 C  CG  . ARG   A 1 189 ? -12.275 -3.790  -82.368  1.00 19.56 ? 282 ARG   A CG  1 
ATOM   1480 C  CD  . ARG   A 1 189 ? -12.138 -2.873  -81.173  1.00 18.78 ? 282 ARG   A CD  1 
ATOM   1481 N  NE  . ARG   A 1 189 ? -13.255 -3.107  -80.273  1.00 18.15 ? 282 ARG   A NE  1 
ATOM   1482 C  CZ  . ARG   A 1 189 ? -13.760 -2.229  -79.416  1.00 18.01 ? 282 ARG   A CZ  1 
ATOM   1483 N  NH1 . ARG   A 1 189 ? -13.246 -1.015  -79.297  1.00 17.56 ? 282 ARG   A NH1 1 
ATOM   1484 N  NH2 . ARG   A 1 189 ? -14.789 -2.582  -78.664  1.00 18.15 ? 282 ARG   A NH2 1 
ATOM   1485 N  N   . ARG   A 1 190 ? -13.685 -3.877  -85.741  1.00 21.27 ? 283 ARG   A N   1 
ATOM   1486 C  CA  . ARG   A 1 190 ? -15.124 -4.072  -86.065  1.00 21.80 ? 283 ARG   A CA  1 
ATOM   1487 C  C   . ARG   A 1 190 ? -15.268 -5.346  -86.907  1.00 23.12 ? 283 ARG   A C   1 
ATOM   1488 O  O   . ARG   A 1 190 ? -16.148 -6.168  -86.587  1.00 23.77 ? 283 ARG   A O   1 
ATOM   1489 C  CB  . ARG   A 1 190 ? -15.713 -2.847  -86.769  1.00 21.33 ? 283 ARG   A CB  1 
ATOM   1490 C  CG  . ARG   A 1 190 ? -17.232 -2.775  -86.681  1.00 21.08 ? 283 ARG   A CG  1 
ATOM   1491 C  CD  . ARG   A 1 190 ? -17.809 -1.599  -87.448  1.00 21.14 ? 283 ARG   A CD  1 
ATOM   1492 N  NE  . ARG   A 1 190 ? -17.430 -0.321  -86.864  1.00 20.94 ? 283 ARG   A NE  1 
ATOM   1493 C  CZ  . ARG   A 1 190 ? -17.782 0.872   -87.332  1.00 20.80 ? 283 ARG   A CZ  1 
ATOM   1494 N  NH1 . ARG   A 1 190 ? -18.548 0.970   -88.407  1.00 21.09 ? 283 ARG   A NH1 1 
ATOM   1495 N  NH2 . ARG   A 1 190 ? -17.367 1.966   -86.716  1.00 20.75 ? 283 ARG   A NH2 1 
ATOM   1496 N  N   . THR   A 1 191 ? -14.406 -5.518  -87.913  1.00 24.14 ? 284 THR   A N   1 
ATOM   1497 C  CA  . THR   A 1 191 ? -14.386 -6.696  -88.822  1.00 25.46 ? 284 THR   A CA  1 
ATOM   1498 C  C   . THR   A 1 191 ? -14.132 -7.979  -88.022  1.00 25.95 ? 284 THR   A C   1 
ATOM   1499 O  O   . THR   A 1 191 ? -14.783 -8.989  -88.339  1.00 26.45 ? 284 THR   A O   1 
ATOM   1500 C  CB  . THR   A 1 191 ? -13.347 -6.520  -89.937  1.00 25.46 ? 284 THR   A CB  1 
ATOM   1501 O  OG1 . THR   A 1 191 ? -13.762 -5.372  -90.677  1.00 24.90 ? 284 THR   A OG1 1 
ATOM   1502 C  CG2 . THR   A 1 191 ? -13.216 -7.729  -90.841  1.00 25.11 ? 284 THR   A CG2 1 
ATOM   1503 N  N   . GLU   A 1 192 ? -13.221 -7.954  -87.042  1.00 26.61 ? 285 GLU   A N   1 
ATOM   1504 C  CA  . GLU   A 1 192 ? -12.834 -9.162  -86.260  1.00 27.46 ? 285 GLU   A CA  1 
ATOM   1505 C  C   . GLU   A 1 192 ? -13.952 -9.539  -85.277  1.00 28.24 ? 285 GLU   A C   1 
ATOM   1506 O  O   . GLU   A 1 192 ? -14.108 -10.749 -85.011  1.00 29.07 ? 285 GLU   A O   1 
ATOM   1507 C  CB  . GLU   A 1 192 ? -11.500 -8.959  -85.535  1.00 27.46 ? 285 GLU   A CB  1 
ATOM   1508 C  CG  . GLU   A 1 192 ? -10.294 -9.190  -86.428  1.00 27.63 ? 285 GLU   A CG  1 
ATOM   1509 C  CD  . GLU   A 1 192 ? -8.979  -9.428  -85.705  1.00 27.54 ? 285 GLU   A CD  1 
ATOM   1510 O  OE1 . GLU   A 1 192 ? -9.010  -9.891  -84.549  1.00 27.35 ? 285 GLU   A OE1 1 
ATOM   1511 O  OE2 . GLU   A 1 192 ? -7.924  -9.154  -86.308  1.00 27.46 ? 285 GLU   A OE2 1 
ATOM   1512 N  N   . GLU   A 1 193 ? -14.701 -8.557  -84.765  1.00 29.25 ? 286 GLU   A N   1 
ATOM   1513 C  CA  . GLU   A 1 193 ? -15.819 -8.778  -83.803  1.00 30.91 ? 286 GLU   A CA  1 
ATOM   1514 C  C   . GLU   A 1 193 ? -17.083 -9.229  -84.551  1.00 34.35 ? 286 GLU   A C   1 
ATOM   1515 O  O   . GLU   A 1 193 ? -17.958 -9.830  -83.899  1.00 33.31 ? 286 GLU   A O   1 
ATOM   1516 C  CB  . GLU   A 1 193 ? -16.080 -7.516  -82.980  1.00 30.07 ? 286 GLU   A CB  1 
ATOM   1517 C  CG  . GLU   A 1 193 ? -14.970 -7.217  -81.987  1.00 30.20 ? 286 GLU   A CG  1 
ATOM   1518 C  CD  . GLU   A 1 193 ? -15.137 -5.945  -81.172  1.00 29.64 ? 286 GLU   A CD  1 
ATOM   1519 O  OE1 . GLU   A 1 193 ? -16.012 -5.124  -81.517  1.00 29.95 ? 286 GLU   A OE1 1 
ATOM   1520 O  OE2 . GLU   A 1 193 ? -14.385 -5.776  -80.191  1.00 28.23 ? 286 GLU   A OE2 1 
ATOM   1521 N  N   . GLU   A 1 194 ? -17.184 -8.938  -85.854  1.00 38.73 ? 287 GLU   A N   1 
ATOM   1522 C  CA  . GLU   A 1 194 ? -18.291 -9.389  -86.745  1.00 41.41 ? 287 GLU   A CA  1 
ATOM   1523 C  C   . GLU   A 1 194 ? -18.344 -10.923 -86.749  1.00 42.99 ? 287 GLU   A C   1 
ATOM   1524 O  O   . GLU   A 1 194 ? -19.461 -11.473 -86.745  1.00 44.27 ? 287 GLU   A O   1 
ATOM   1525 C  CB  . GLU   A 1 194 ? -18.083 -8.846  -88.162  1.00 44.62 ? 287 GLU   A CB  1 
ATOM   1526 C  CG  . GLU   A 1 194 ? -19.108 -9.331  -89.180  1.00 47.41 ? 287 GLU   A CG  1 
ATOM   1527 C  CD  . GLU   A 1 194 ? -18.560 -9.569  -90.579  1.00 50.78 ? 287 GLU   A CD  1 
ATOM   1528 O  OE1 . GLU   A 1 194 ? -17.428 -9.118  -90.860  1.00 52.59 ? 287 GLU   A OE1 1 
ATOM   1529 O  OE2 . GLU   A 1 194 ? -19.267 -10.214 -91.387  1.00 52.80 ? 287 GLU   A OE2 1 
ATOM   1530 N  N   . ASN   A 1 195 ? -17.178 -11.578 -86.727  1.00 45.77 ? 288 ASN   A N   1 
ATOM   1531 C  CA  . ASN   A 1 195 ? -17.027 -13.056 -86.834  1.00 47.26 ? 288 ASN   A CA  1 
ATOM   1532 C  C   . ASN   A 1 195 ? -17.476 -13.746 -85.537  1.00 48.09 ? 288 ASN   A C   1 
ATOM   1533 O  O   . ASN   A 1 195 ? -17.499 -14.994 -85.528  1.00 50.59 ? 288 ASN   A O   1 
ATOM   1534 C  CB  . ASN   A 1 195 ? -15.587 -13.445 -87.186  1.00 48.47 ? 288 ASN   A CB  1 
ATOM   1535 C  CG  . ASN   A 1 195 ? -15.153 -12.938 -88.547  1.00 50.17 ? 288 ASN   A CG  1 
ATOM   1536 O  OD1 . ASN   A 1 195 ? -14.177 -12.199 -88.657  1.00 48.42 ? 288 ASN   A OD1 1 
ATOM   1537 N  ND2 . ASN   A 1 195 ? -15.875 -13.323 -89.588  1.00 50.86 ? 288 ASN   A ND2 1 
ATOM   1538 N  N   . LEU   A 1 196 ? -17.809 -12.982 -84.488  1.00 46.95 ? 289 LEU   A N   1 
ATOM   1539 C  CA  . LEU   A 1 196 ? -18.291 -13.507 -83.179  1.00 46.50 ? 289 LEU   A CA  1 
ATOM   1540 C  C   . LEU   A 1 196 ? -19.790 -13.822 -83.273  1.00 45.36 ? 289 LEU   A C   1 
ATOM   1541 O  O   . LEU   A 1 196 ? -20.653 -13.027 -82.899  1.00 44.19 ? 289 LEU   A O   1 
ATOM   1542 C  CB  . LEU   A 1 196 ? -18.000 -12.480 -82.076  1.00 45.62 ? 289 LEU   A CB  1 
ATOM   1543 C  CG  . LEU   A 1 196 ? -16.525 -12.135 -81.861  1.00 44.63 ? 289 LEU   A CG  1 
ATOM   1544 C  CD1 . LEU   A 1 196 ? -16.372 -10.988 -80.872  1.00 43.70 ? 289 LEU   A CD1 1 
ATOM   1545 C  CD2 . LEU   A 1 196 ? -15.742 -13.350 -81.390  1.00 44.37 ? 289 LEU   A CD2 1 
ATOM   1546 N  N   . SER   B 1 3   ? 16.793  -21.303 -27.270  1.00 49.63 ? 96  SER   B N   1 
ATOM   1547 C  CA  . SER   B 1 3   ? 15.823  -20.831 -26.238  1.00 48.63 ? 96  SER   B CA  1 
ATOM   1548 C  C   . SER   B 1 3   ? 14.695  -20.033 -26.906  1.00 48.27 ? 96  SER   B C   1 
ATOM   1549 O  O   . SER   B 1 3   ? 14.781  -19.786 -28.133  1.00 49.94 ? 96  SER   B O   1 
ATOM   1550 C  CB  . SER   B 1 3   ? 16.524  -20.021 -25.174  1.00 49.19 ? 96  SER   B CB  1 
ATOM   1551 O  OG  . SER   B 1 3   ? 17.076  -18.833 -25.724  1.00 50.70 ? 96  SER   B OG  1 
ATOM   1552 N  N   . VAL   B 1 4   ? 13.673  -19.657 -26.128  1.00 44.69 ? 97  VAL   B N   1 
ATOM   1553 C  CA  . VAL   B 1 4   ? 12.495  -18.864 -26.594  1.00 40.63 ? 97  VAL   B CA  1 
ATOM   1554 C  C   . VAL   B 1 4   ? 12.175  -17.812 -25.534  1.00 37.22 ? 97  VAL   B C   1 
ATOM   1555 O  O   . VAL   B 1 4   ? 11.923  -18.159 -24.383  1.00 34.24 ? 97  VAL   B O   1 
ATOM   1556 C  CB  . VAL   B 1 4   ? 11.278  -19.767 -26.876  1.00 40.78 ? 97  VAL   B CB  1 
ATOM   1557 C  CG1 . VAL   B 1 4   ? 10.044  -18.961 -27.255  1.00 41.08 ? 97  VAL   B CG1 1 
ATOM   1558 C  CG2 . VAL   B 1 4   ? 11.583  -20.800 -27.949  1.00 41.38 ? 97  VAL   B CG2 1 
ATOM   1559 N  N   . PRO   B 1 5   ? 12.182  -16.503 -25.882  1.00 34.30 ? 98  PRO   B N   1 
ATOM   1560 C  CA  . PRO   B 1 5   ? 11.778  -15.459 -24.943  1.00 33.09 ? 98  PRO   B CA  1 
ATOM   1561 C  C   . PRO   B 1 5   ? 10.333  -15.681 -24.476  1.00 32.09 ? 98  PRO   B C   1 
ATOM   1562 O  O   . PRO   B 1 5   ? 9.500   -16.020 -25.299  1.00 31.45 ? 98  PRO   B O   1 
ATOM   1563 C  CB  . PRO   B 1 5   ? 11.883  -14.146 -25.736  1.00 33.69 ? 98  PRO   B CB  1 
ATOM   1564 C  CG  . PRO   B 1 5   ? 12.755  -14.478 -26.936  1.00 34.45 ? 98  PRO   B CG  1 
ATOM   1565 C  CD  . PRO   B 1 5   ? 12.574  -15.960 -27.191  1.00 34.21 ? 98  PRO   B CD  1 
ATOM   1566 N  N   . SER   B 1 6   ? 10.070  -15.497 -23.180  1.00 30.83 ? 99  SER   B N   1 
ATOM   1567 C  CA  . SER   B 1 6   ? 8.716   -15.616 -22.581  1.00 29.95 ? 99  SER   B CA  1 
ATOM   1568 C  C   . SER   B 1 6   ? 7.764   -14.630 -23.268  1.00 29.05 ? 99  SER   B C   1 
ATOM   1569 O  O   . SER   B 1 6   ? 8.183   -13.482 -23.511  1.00 28.79 ? 99  SER   B O   1 
ATOM   1570 C  CB  . SER   B 1 6   ? 8.748   -15.387 -21.094  1.00 30.09 ? 99  SER   B CB  1 
ATOM   1571 O  OG  . SER   B 1 6   ? 7.431   -15.422 -20.568  1.00 30.23 ? 99  SER   B OG  1 
ATOM   1572 N  N   . GLN   B 1 7   ? 6.540   -15.074 -23.564  1.00 27.64 ? 100 GLN   B N   1 
ATOM   1573 C  CA  . GLN   B 1 7   ? 5.427   -14.228 -24.068  1.00 28.81 ? 100 GLN   B CA  1 
ATOM   1574 C  C   . GLN   B 1 7   ? 4.327   -14.143 -23.000  1.00 27.86 ? 100 GLN   B C   1 
ATOM   1575 O  O   . GLN   B 1 7   ? 3.223   -13.680 -23.336  1.00 27.18 ? 100 GLN   B O   1 
ATOM   1576 C  CB  . GLN   B 1 7   ? 4.886   -14.782 -25.390  1.00 29.73 ? 100 GLN   B CB  1 
ATOM   1577 C  CG  . GLN   B 1 7   ? 4.360   -16.209 -25.297  1.00 30.79 ? 100 GLN   B CG  1 
ATOM   1578 C  CD  . GLN   B 1 7   ? 3.627   -16.632 -26.546  1.00 32.03 ? 100 GLN   B CD  1 
ATOM   1579 O  OE1 . GLN   B 1 7   ? 4.211   -17.183 -27.473  1.00 33.05 ? 100 GLN   B OE1 1 
ATOM   1580 N  NE2 . GLN   B 1 7   ? 2.330   -16.373 -26.581  1.00 33.90 ? 100 GLN   B NE2 1 
ATOM   1581 N  N   . LYS   B 1 8   ? 4.614   -14.560 -21.761  1.00 28.00 ? 101 LYS   B N   1 
ATOM   1582 C  CA  . LYS   B 1 8   ? 3.611   -14.623 -20.664  1.00 27.80 ? 101 LYS   B CA  1 
ATOM   1583 C  C   . LYS   B 1 8   ? 3.229   -13.198 -20.256  1.00 25.82 ? 101 LYS   B C   1 
ATOM   1584 O  O   . LYS   B 1 8   ? 4.131   -12.438 -19.864  1.00 24.84 ? 101 LYS   B O   1 
ATOM   1585 C  CB  . LYS   B 1 8   ? 4.145   -15.405 -19.458  1.00 29.96 ? 101 LYS   B CB  1 
ATOM   1586 C  CG  . LYS   B 1 8   ? 4.566   -16.840 -19.745  1.00 32.41 ? 101 LYS   B CG  1 
ATOM   1587 C  CD  . LYS   B 1 8   ? 3.477   -17.694 -20.377  1.00 33.85 ? 101 LYS   B CD  1 
ATOM   1588 C  CE  . LYS   B 1 8   ? 4.005   -18.676 -21.402  1.00 35.00 ? 101 LYS   B CE  1 
ATOM   1589 N  NZ  . LYS   B 1 8   ? 3.115   -18.765 -22.582  1.00 36.50 ? 101 LYS   B NZ  1 
ATOM   1590 N  N   . THR   B 1 9   ? 1.940   -12.863 -20.361  1.00 24.21 ? 102 THR   B N   1 
ATOM   1591 C  CA  . THR   B 1 9   ? 1.364   -11.565 -19.928  1.00 23.92 ? 102 THR   B CA  1 
ATOM   1592 C  C   . THR   B 1 9   ? 1.663   -11.376 -18.440  1.00 23.76 ? 102 THR   B C   1 
ATOM   1593 O  O   . THR   B 1 9   ? 1.418   -12.307 -17.656  1.00 22.57 ? 102 THR   B O   1 
ATOM   1594 C  CB  . THR   B 1 9   ? -0.139  -11.474 -20.218  1.00 23.62 ? 102 THR   B CB  1 
ATOM   1595 O  OG1 . THR   B 1 9   ? -0.295  -11.425 -21.635  1.00 25.19 ? 102 THR   B OG1 1 
ATOM   1596 C  CG2 . THR   B 1 9   ? -0.793  -10.255 -19.605  1.00 23.53 ? 102 THR   B CG2 1 
ATOM   1597 N  N   . TYR   B 1 10  ? 2.168   -10.199 -18.092  1.00 23.88 ? 103 TYR   B N   1 
ATOM   1598 C  CA  . TYR   B 1 10  ? 2.563   -9.801  -16.722  1.00 24.69 ? 103 TYR   B CA  1 
ATOM   1599 C  C   . TYR   B 1 10  ? 2.285   -8.302  -16.572  1.00 22.56 ? 103 TYR   B C   1 
ATOM   1600 O  O   . TYR   B 1 10  ? 3.061   -7.504  -17.120  1.00 22.34 ? 103 TYR   B O   1 
ATOM   1601 C  CB  . TYR   B 1 10  ? 4.026   -10.205 -16.510  1.00 27.62 ? 103 TYR   B CB  1 
ATOM   1602 C  CG  . TYR   B 1 10  ? 4.692   -9.605  -15.301  1.00 30.55 ? 103 TYR   B CG  1 
ATOM   1603 C  CD1 . TYR   B 1 10  ? 4.091   -9.672  -14.055  1.00 31.85 ? 103 TYR   B CD1 1 
ATOM   1604 C  CD2 . TYR   B 1 10  ? 5.931   -8.988  -15.396  1.00 31.75 ? 103 TYR   B CD2 1 
ATOM   1605 C  CE1 . TYR   B 1 10  ? 4.700   -9.129  -12.936  1.00 32.89 ? 103 TYR   B CE1 1 
ATOM   1606 C  CE2 . TYR   B 1 10  ? 6.551   -8.439  -14.288  1.00 31.80 ? 103 TYR   B CE2 1 
ATOM   1607 C  CZ  . TYR   B 1 10  ? 5.924   -8.499  -13.056  1.00 33.65 ? 103 TYR   B CZ  1 
ATOM   1608 O  OH  . TYR   B 1 10  ? 6.512   -7.966  -11.947  1.00 37.94 ? 103 TYR   B OH  1 
ATOM   1609 N  N   . GLN   B 1 11  ? 1.194   -7.928  -15.895  1.00 21.24 ? 104 GLN   B N   1 
ATOM   1610 C  CA  . GLN   B 1 11  ? 0.820   -6.501  -15.681  1.00 21.35 ? 104 GLN   B CA  1 
ATOM   1611 C  C   . GLN   B 1 11  ? 1.765   -5.877  -14.642  1.00 20.64 ? 104 GLN   B C   1 
ATOM   1612 O  O   . GLN   B 1 11  ? 2.081   -4.678  -14.767  1.00 20.15 ? 104 GLN   B O   1 
ATOM   1613 C  CB  . GLN   B 1 11  ? -0.663  -6.393  -15.316  1.00 22.42 ? 104 GLN   B CB  1 
ATOM   1614 C  CG  . GLN   B 1 11  ? -1.576  -6.799  -16.467  1.00 23.57 ? 104 GLN   B CG  1 
ATOM   1615 C  CD  . GLN   B 1 11  ? -3.035  -6.501  -16.223  1.00 25.43 ? 104 GLN   B CD  1 
ATOM   1616 O  OE1 . GLN   B 1 11  ? -3.485  -6.383  -15.087  1.00 26.77 ? 104 GLN   B OE1 1 
ATOM   1617 N  NE2 . GLN   B 1 11  ? -3.795  -6.393  -17.301  1.00 26.19 ? 104 GLN   B NE2 1 
ATOM   1618 N  N   . GLY   B 1 12  ? 2.201   -6.669  -13.660  1.00 20.48 ? 105 GLY   B N   1 
ATOM   1619 C  CA  . GLY   B 1 12  ? 3.217   -6.296  -12.658  1.00 20.21 ? 105 GLY   B CA  1 
ATOM   1620 C  C   . GLY   B 1 12  ? 2.830   -5.091  -11.814  1.00 20.48 ? 105 GLY   B C   1 
ATOM   1621 O  O   . GLY   B 1 12  ? 1.625   -4.772  -11.716  1.00 20.86 ? 105 GLY   B O   1 
ATOM   1622 N  N   . SER   B 1 13  ? 3.840   -4.443  -11.234  1.00 21.14 ? 106 SER   B N   1 
ATOM   1623 C  CA  . SER   B 1 13  ? 3.727   -3.390  -10.193  1.00 22.53 ? 106 SER   B CA  1 
ATOM   1624 C  C   . SER   B 1 13  ? 2.952   -2.172  -10.709  1.00 22.28 ? 106 SER   B C   1 
ATOM   1625 O  O   . SER   B 1 13  ? 2.271   -1.530  -9.895   1.00 22.53 ? 106 SER   B O   1 
ATOM   1626 C  CB  . SER   B 1 13  ? 5.088   -2.975  -9.717   1.00 22.49 ? 106 SER   B CB  1 
ATOM   1627 O  OG  . SER   B 1 13  ? 4.975   -2.028  -8.668   1.00 24.33 ? 106 SER   B OG  1 
ATOM   1628 N  N   . TYR   B 1 14  ? 3.070   -1.844  -11.999  1.00 21.92 ? 107 TYR   B N   1 
ATOM   1629 C  CA  . TYR   B 1 14  ? 2.572   -0.560  -12.564  1.00 21.76 ? 107 TYR   B CA  1 
ATOM   1630 C  C   . TYR   B 1 14  ? 1.263   -0.772  -13.337  1.00 21.06 ? 107 TYR   B C   1 
ATOM   1631 O  O   . TYR   B 1 14  ? 0.779   0.203   -13.945  1.00 20.90 ? 107 TYR   B O   1 
ATOM   1632 C  CB  . TYR   B 1 14  ? 3.686   0.095   -13.386  1.00 22.37 ? 107 TYR   B CB  1 
ATOM   1633 C  CG  . TYR   B 1 14  ? 4.911   0.409   -12.566  1.00 22.72 ? 107 TYR   B CG  1 
ATOM   1634 C  CD1 . TYR   B 1 14  ? 4.932   1.490   -11.698  1.00 23.66 ? 107 TYR   B CD1 1 
ATOM   1635 C  CD2 . TYR   B 1 14  ? 6.035   -0.398  -12.620  1.00 22.96 ? 107 TYR   B CD2 1 
ATOM   1636 C  CE1 . TYR   B 1 14  ? 6.040   1.773   -10.917  1.00 23.81 ? 107 TYR   B CE1 1 
ATOM   1637 C  CE2 . TYR   B 1 14  ? 7.156   -0.127  -11.853  1.00 23.73 ? 107 TYR   B CE2 1 
ATOM   1638 C  CZ  . TYR   B 1 14  ? 7.157   0.959   -10.995  1.00 24.10 ? 107 TYR   B CZ  1 
ATOM   1639 O  OH  . TYR   B 1 14  ? 8.251   1.221   -10.226  1.00 24.19 ? 107 TYR   B OH  1 
ATOM   1640 N  N   . GLY   B 1 15  ? 0.694   -1.981  -13.285  1.00 20.70 ? 108 GLY   B N   1 
ATOM   1641 C  CA  . GLY   B 1 15  ? -0.576  -2.328  -13.952  1.00 20.68 ? 108 GLY   B CA  1 
ATOM   1642 C  C   . GLY   B 1 15  ? -0.472  -2.130  -15.456  1.00 20.58 ? 108 GLY   B C   1 
ATOM   1643 O  O   . GLY   B 1 15  ? -1.357  -1.462  -16.033  1.00 20.10 ? 108 GLY   B O   1 
ATOM   1644 N  N   . PHE   B 1 16  ? 0.576   -2.696  -16.062  1.00 20.27 ? 109 PHE   B N   1 
ATOM   1645 C  CA  . PHE   B 1 16  ? 0.969   -2.493  -17.481  1.00 19.94 ? 109 PHE   B CA  1 
ATOM   1646 C  C   . PHE   B 1 16  ? 0.026   -3.274  -18.397  1.00 20.00 ? 109 PHE   B C   1 
ATOM   1647 O  O   . PHE   B 1 16  ? -0.054  -4.510  -18.261  1.00 18.98 ? 109 PHE   B O   1 
ATOM   1648 C  CB  . PHE   B 1 16  ? 2.426   -2.908  -17.704  1.00 19.94 ? 109 PHE   B CB  1 
ATOM   1649 C  CG  . PHE   B 1 16  ? 2.893   -2.836  -19.138  1.00 20.09 ? 109 PHE   B CG  1 
ATOM   1650 C  CD1 . PHE   B 1 16  ? 2.672   -1.702  -19.903  1.00 20.61 ? 109 PHE   B CD1 1 
ATOM   1651 C  CD2 . PHE   B 1 16  ? 3.559   -3.901  -19.722  1.00 19.61 ? 109 PHE   B CD2 1 
ATOM   1652 C  CE1 . PHE   B 1 16  ? 3.105   -1.634  -21.220  1.00 20.62 ? 109 PHE   B CE1 1 
ATOM   1653 C  CE2 . PHE   B 1 16  ? 3.999   -3.832  -21.036  1.00 20.37 ? 109 PHE   B CE2 1 
ATOM   1654 C  CZ  . PHE   B 1 16  ? 3.768   -2.700  -21.784  1.00 20.62 ? 109 PHE   B CZ  1 
ATOM   1655 N  N   . ARG   B 1 17  ? -0.671  -2.558  -19.284  1.00 20.42 ? 110 ARG   B N   1 
ATOM   1656 C  CA  . ARG   B 1 17  ? -1.500  -3.122  -20.385  1.00 21.04 ? 110 ARG   B CA  1 
ATOM   1657 C  C   . ARG   B 1 17  ? -1.165  -2.386  -21.684  1.00 19.16 ? 110 ARG   B C   1 
ATOM   1658 O  O   . ARG   B 1 17  ? -0.673  -1.233  -21.617  1.00 17.65 ? 110 ARG   B O   1 
ATOM   1659 C  CB  . ARG   B 1 17  ? -3.011  -2.959  -20.166  1.00 22.96 ? 110 ARG   B CB  1 
ATOM   1660 C  CG  . ARG   B 1 17  ? -3.533  -3.387  -18.805  1.00 25.84 ? 110 ARG   B CG  1 
ATOM   1661 C  CD  . ARG   B 1 17  ? -3.532  -2.213  -17.848  1.00 27.83 ? 110 ARG   B CD  1 
ATOM   1662 N  NE  . ARG   B 1 17  ? -4.597  -1.249  -18.095  1.00 30.09 ? 110 ARG   B NE  1 
ATOM   1663 C  CZ  . ARG   B 1 17  ? -4.720  -0.082  -17.458  1.00 30.46 ? 110 ARG   B CZ  1 
ATOM   1664 N  NH1 . ARG   B 1 17  ? -3.836  0.274   -16.540  1.00 30.01 ? 110 ARG   B NH1 1 
ATOM   1665 N  NH2 . ARG   B 1 17  ? -5.725  0.729   -17.747  1.00 30.81 ? 110 ARG   B NH2 1 
ATOM   1666 N  N   . LEU   B 1 18  ? -1.468  -3.023  -22.816  1.00 18.20 ? 111 LEU   B N   1 
ATOM   1667 C  CA  . LEU   B 1 18  ? -1.388  -2.409  -24.162  1.00 17.79 ? 111 LEU   B CA  1 
ATOM   1668 C  C   . LEU   B 1 18  ? -2.777  -1.918  -24.564  1.00 17.63 ? 111 LEU   B C   1 
ATOM   1669 O  O   . LEU   B 1 18  ? -3.775  -2.534  -24.148  1.00 17.15 ? 111 LEU   B O   1 
ATOM   1670 C  CB  . LEU   B 1 18  ? -0.844  -3.424  -25.169  1.00 17.51 ? 111 LEU   B CB  1 
ATOM   1671 C  CG  . LEU   B 1 18  ? 0.576   -3.905  -24.886  1.00 17.31 ? 111 LEU   B CG  1 
ATOM   1672 C  CD1 . LEU   B 1 18  ? 1.053   -4.855  -25.969  1.00 17.37 ? 111 LEU   B CD1 1 
ATOM   1673 C  CD2 . LEU   B 1 18  ? 1.527   -2.730  -24.731  1.00 17.52 ? 111 LEU   B CD2 1 
ATOM   1674 N  N   . GLY   B 1 19  ? -2.808  -0.824  -25.321  1.00 17.62 ? 112 GLY   B N   1 
ATOM   1675 C  CA  . GLY   B 1 19  ? -4.004  -0.302  -25.999  1.00 17.51 ? 112 GLY   B CA  1 
ATOM   1676 C  C   . GLY   B 1 19  ? -3.688  0.003   -27.447  1.00 17.44 ? 112 GLY   B C   1 
ATOM   1677 O  O   . GLY   B 1 19  ? -2.499  0.116   -27.789  1.00 17.40 ? 112 GLY   B O   1 
ATOM   1678 N  N   . PHE   B 1 20  ? -4.720  0.100   -28.277  1.00 16.76 ? 113 PHE   B N   1 
ATOM   1679 C  CA  . PHE   B 1 20  ? -4.603  0.381   -29.727  1.00 16.97 ? 113 PHE   B CA  1 
ATOM   1680 C  C   . PHE   B 1 20  ? -5.719  1.357   -30.079  1.00 16.37 ? 113 PHE   B C   1 
ATOM   1681 O  O   . PHE   B 1 20  ? -6.778  1.272   -29.432  1.00 15.67 ? 113 PHE   B O   1 
ATOM   1682 C  CB  . PHE   B 1 20  ? -4.662  -0.923  -30.528  1.00 16.87 ? 113 PHE   B CB  1 
ATOM   1683 C  CG  . PHE   B 1 20  ? -3.667  -1.963  -30.078  1.00 17.65 ? 113 PHE   B CG  1 
ATOM   1684 C  CD1 . PHE   B 1 20  ? -3.983  -2.854  -29.064  1.00 18.09 ? 113 PHE   B CD1 1 
ATOM   1685 C  CD2 . PHE   B 1 20  ? -2.404  -2.039  -30.651  1.00 17.91 ? 113 PHE   B CD2 1 
ATOM   1686 C  CE1 . PHE   B 1 20  ? -3.064  -3.802  -28.634  1.00 18.18 ? 113 PHE   B CE1 1 
ATOM   1687 C  CE2 . PHE   B 1 20  ? -1.489  -2.990  -30.223  1.00 17.68 ? 113 PHE   B CE2 1 
ATOM   1688 C  CZ  . PHE   B 1 20  ? -1.820  -3.870  -29.219  1.00 18.01 ? 113 PHE   B CZ  1 
ATOM   1689 N  N   . LEU   B 1 21  ? -5.464  2.263   -31.026  1.00 16.33 ? 114 LEU   B N   1 
ATOM   1690 C  CA  . LEU   B 1 21  ? -6.487  3.196   -31.562  1.00 16.31 ? 114 LEU   B CA  1 
ATOM   1691 C  C   . LEU   B 1 21  ? -7.648  2.350   -32.096  1.00 16.34 ? 114 LEU   B C   1 
ATOM   1692 O  O   . LEU   B 1 21  ? -7.377  1.267   -32.657  1.00 15.86 ? 114 LEU   B O   1 
ATOM   1693 C  CB  . LEU   B 1 21  ? -5.874  4.068   -32.664  1.00 16.39 ? 114 LEU   B CB  1 
ATOM   1694 C  CG  . LEU   B 1 21  ? -4.806  5.076   -32.225  1.00 16.57 ? 114 LEU   B CG  1 
ATOM   1695 C  CD1 . LEU   B 1 21  ? -4.151  5.725   -33.434  1.00 16.52 ? 114 LEU   B CD1 1 
ATOM   1696 C  CD2 . LEU   B 1 21  ? -5.385  6.144   -31.310  1.00 16.84 ? 114 LEU   B CD2 1 
ATOM   1697 N  N   . HIS   B 1 22  ? -8.888  2.807   -31.894  1.00 15.92 ? 115 HIS   B N   1 
ATOM   1698 C  CA  . HIS   B 1 22  ? -10.110 2.220   -32.509  1.00 15.45 ? 115 HIS   B CA  1 
ATOM   1699 C  C   . HIS   B 1 22  ? -10.231 2.751   -33.941  1.00 15.52 ? 115 HIS   B C   1 
ATOM   1700 O  O   . HIS   B 1 22  ? -11.084 3.617   -34.174  1.00 15.25 ? 115 HIS   B O   1 
ATOM   1701 C  CB  . HIS   B 1 22  ? -11.315 2.494   -31.603  1.00 15.28 ? 115 HIS   B CB  1 
ATOM   1702 C  CG  . HIS   B 1 22  ? -11.055 2.058   -30.204  1.00 15.06 ? 115 HIS   B CG  1 
ATOM   1703 N  ND1 . HIS   B 1 22  ? -11.007 2.944   -29.149  1.00 15.29 ? 115 HIS   B ND1 1 
ATOM   1704 C  CD2 . HIS   B 1 22  ? -10.770 0.842   -29.698  1.00 14.96 ? 115 HIS   B CD2 1 
ATOM   1705 C  CE1 . HIS   B 1 22  ? -10.729 2.286   -28.046  1.00 15.06 ? 115 HIS   B CE1 1 
ATOM   1706 N  NE2 . HIS   B 1 22  ? -10.577 0.997   -28.357  1.00 15.83 ? 115 HIS   B NE2 1 
ATOM   1707 N  N   . SER   B 1 23  ? -9.379  2.253   -34.848  1.00 15.95 ? 116 SER   B N   1 
ATOM   1708 C  CA  . SER   B 1 23  ? -9.093  2.838   -36.188  1.00 16.82 ? 116 SER   B CA  1 
ATOM   1709 C  C   . SER   B 1 23  ? -10.110 2.381   -37.244  1.00 16.92 ? 116 SER   B C   1 
ATOM   1710 O  O   . SER   B 1 23  ? -10.204 3.056   -38.290  1.00 17.28 ? 116 SER   B O   1 
ATOM   1711 C  CB  . SER   B 1 23  ? -7.689  2.494   -36.635  1.00 17.30 ? 116 SER   B CB  1 
ATOM   1712 O  OG  . SER   B 1 23  ? -6.732  2.919   -35.681  1.00 18.31 ? 116 SER   B OG  1 
ATOM   1713 N  N   . GLY   B 1 24  ? -10.821 1.276   -37.005  1.00 16.76 ? 117 GLY   B N   1 
ATOM   1714 C  CA  . GLY   B 1 24  ? -11.746 0.685   -37.989  1.00 17.01 ? 117 GLY   B CA  1 
ATOM   1715 C  C   . GLY   B 1 24  ? -10.980 0.070   -39.150  1.00 17.30 ? 117 GLY   B C   1 
ATOM   1716 O  O   . GLY   B 1 24  ? -9.747  -0.110  -39.024  1.00 17.67 ? 117 GLY   B O   1 
ATOM   1717 N  N   . THR   B 1 25  ? -11.667 -0.242  -40.249  1.00 17.57 ? 118 THR   B N   1 
ATOM   1718 C  CA  . THR   B 1 25  ? -11.124 -1.084  -41.348  1.00 17.70 ? 118 THR   B CA  1 
ATOM   1719 C  C   . THR   B 1 25  ? -11.391 -0.446  -42.718  1.00 18.27 ? 118 THR   B C   1 
ATOM   1720 O  O   . THR   B 1 25  ? -11.478 -1.209  -43.696  1.00 18.21 ? 118 THR   B O   1 
ATOM   1721 C  CB  . THR   B 1 25  ? -11.697 -2.509  -41.274  1.00 17.71 ? 118 THR   B CB  1 
ATOM   1722 O  OG1 . THR   B 1 25  ? -13.109 -2.444  -41.479  1.00 17.07 ? 118 THR   B OG1 1 
ATOM   1723 C  CG2 . THR   B 1 25  ? -11.398 -3.202  -39.961  1.00 17.51 ? 118 THR   B CG2 1 
ATOM   1724 N  N   . ALA   B 1 26  ? -11.490 0.885   -42.808  1.00 19.46 ? 119 ALA   B N   1 
ATOM   1725 C  CA  . ALA   B 1 26  ? -11.572 1.614   -44.098  1.00 21.66 ? 119 ALA   B CA  1 
ATOM   1726 C  C   . ALA   B 1 26  ? -10.283 1.358   -44.899  1.00 23.80 ? 119 ALA   B C   1 
ATOM   1727 O  O   . ALA   B 1 26  ? -9.229  1.142   -44.281  1.00 23.64 ? 119 ALA   B O   1 
ATOM   1728 C  CB  . ALA   B 1 26  ? -11.819 3.086   -43.863  1.00 21.45 ? 119 ALA   B CB  1 
ATOM   1729 N  N   . LYS   B 1 27  ? -10.364 1.365   -46.230  1.00 26.54 ? 120 LYS   B N   1 
ATOM   1730 C  CA  . LYS   B 1 27  ? -9.230  1.010   -47.131  1.00 29.29 ? 120 LYS   B CA  1 
ATOM   1731 C  C   . LYS   B 1 27  ? -8.009  1.889   -46.827  1.00 28.69 ? 120 LYS   B C   1 
ATOM   1732 O  O   . LYS   B 1 27  ? -6.883  1.393   -46.995  1.00 29.43 ? 120 LYS   B O   1 
ATOM   1733 C  CB  . LYS   B 1 27  ? -9.634  1.138   -48.605  1.00 31.83 ? 120 LYS   B CB  1 
ATOM   1734 C  CG  . LYS   B 1 27  ? -8.843  0.246   -49.557  1.00 34.27 ? 120 LYS   B CG  1 
ATOM   1735 C  CD  . LYS   B 1 27  ? -9.530  -0.037  -50.884  1.00 36.29 ? 120 LYS   B CD  1 
ATOM   1736 C  CE  . LYS   B 1 27  ? -10.677 -1.025  -50.785  1.00 37.20 ? 120 LYS   B CE  1 
ATOM   1737 N  NZ  . LYS   B 1 27  ? -11.979 -0.363  -50.522  1.00 37.60 ? 120 LYS   B NZ  1 
ATOM   1738 N  N   . SER   B 1 28  ? -8.219  3.126   -46.365  1.00 27.96 ? 121 SER   B N   1 
ATOM   1739 C  CA  . SER   B 1 28  ? -7.155  4.133   -46.106  1.00 27.89 ? 121 SER   B CA  1 
ATOM   1740 C  C   . SER   B 1 28  ? -6.367  3.839   -44.817  1.00 27.04 ? 121 SER   B C   1 
ATOM   1741 O  O   . SER   B 1 28  ? -5.293  4.459   -44.646  1.00 26.13 ? 121 SER   B O   1 
ATOM   1742 C  CB  . SER   B 1 28  ? -7.740  5.526   -46.076  1.00 28.63 ? 121 SER   B CB  1 
ATOM   1743 O  OG  . SER   B 1 28  ? -8.595  5.698   -44.955  1.00 29.78 ? 121 SER   B OG  1 
ATOM   1744 N  N   . VAL   B 1 29  ? -6.837  2.946   -43.934  1.00 25.81 ? 122 VAL   B N   1 
ATOM   1745 C  CA  . VAL   B 1 29  ? -6.169  2.715   -42.614  1.00 25.53 ? 122 VAL   B CA  1 
ATOM   1746 C  C   . VAL   B 1 29  ? -4.848  1.973   -42.840  1.00 24.92 ? 122 VAL   B C   1 
ATOM   1747 O  O   . VAL   B 1 29  ? -4.845  0.957   -43.564  1.00 24.68 ? 122 VAL   B O   1 
ATOM   1748 C  CB  . VAL   B 1 29  ? -7.059  1.982   -41.590  1.00 25.80 ? 122 VAL   B CB  1 
ATOM   1749 C  CG1 . VAL   B 1 29  ? -8.383  2.702   -41.390  1.00 26.18 ? 122 VAL   B CG1 1 
ATOM   1750 C  CG2 . VAL   B 1 29  ? -7.271  0.516   -41.942  1.00 26.00 ? 122 VAL   B CG2 1 
ATOM   1751 N  N   . THR   B 1 30  ? -3.776  2.467   -42.217  1.00 24.85 ? 123 THR   B N   1 
ATOM   1752 C  CA  . THR   B 1 30  ? -2.389  1.944   -42.327  1.00 24.80 ? 123 THR   B CA  1 
ATOM   1753 C  C   . THR   B 1 30  ? -2.115  0.940   -41.199  1.00 23.86 ? 123 THR   B C   1 
ATOM   1754 O  O   . THR   B 1 30  ? -1.159  0.156   -41.334  1.00 22.81 ? 123 THR   B O   1 
ATOM   1755 C  CB  . THR   B 1 30  ? -1.386  3.103   -42.311  1.00 25.95 ? 123 THR   B CB  1 
ATOM   1756 O  OG1 . THR   B 1 30  ? -1.422  3.699   -41.017  1.00 26.90 ? 123 THR   B OG1 1 
ATOM   1757 C  CG2 . THR   B 1 30  ? -1.679  4.159   -43.355  1.00 27.24 ? 123 THR   B CG2 1 
ATOM   1758 N  N   . CYS   B 1 31  ? -2.915  0.975   -40.125  1.00 23.06 ? 124 CYS   B N   1 
ATOM   1759 C  CA  . CYS   B 1 31  ? -2.751  0.142   -38.901  1.00 22.09 ? 124 CYS   B CA  1 
ATOM   1760 C  C   . CYS   B 1 31  ? -4.114  -0.018  -38.223  1.00 20.92 ? 124 CYS   B C   1 
ATOM   1761 O  O   . CYS   B 1 31  ? -4.732  1.011   -37.888  1.00 20.47 ? 124 CYS   B O   1 
ATOM   1762 C  CB  . CYS   B 1 31  ? -1.760  0.785   -37.937  1.00 22.05 ? 124 CYS   B CB  1 
ATOM   1763 S  SG  . CYS   B 1 31  ? -1.484  -0.160  -36.415  1.00 24.53 ? 124 CYS   B SG  1 
ATOM   1764 N  N   . THR   B 1 32  ? -4.583  -1.253  -38.049  1.00 19.65 ? 125 THR   B N   1 
ATOM   1765 C  CA  . THR   B 1 32  ? -5.881  -1.536  -37.386  1.00 19.09 ? 125 THR   B CA  1 
ATOM   1766 C  C   . THR   B 1 32  ? -5.753  -2.796  -36.534  1.00 18.76 ? 125 THR   B C   1 
ATOM   1767 O  O   . THR   B 1 32  ? -5.240  -3.816  -37.031  1.00 19.30 ? 125 THR   B O   1 
ATOM   1768 C  CB  . THR   B 1 32  ? -7.031  -1.647  -38.394  1.00 18.82 ? 125 THR   B CB  1 
ATOM   1769 O  OG1 . THR   B 1 32  ? -8.242  -1.691  -37.633  1.00 18.25 ? 125 THR   B OG1 1 
ATOM   1770 C  CG2 . THR   B 1 32  ? -6.925  -2.856  -39.300  1.00 18.43 ? 125 THR   B CG2 1 
ATOM   1771 N  N   . TYR   B 1 33  ? -6.230  -2.707  -35.295  1.00 18.10 ? 126 TYR   B N   1 
ATOM   1772 C  CA  . TYR   B 1 33  ? -6.151  -3.776  -34.277  1.00 17.10 ? 126 TYR   B CA  1 
ATOM   1773 C  C   . TYR   B 1 33  ? -7.520  -4.442  -34.127  1.00 16.69 ? 126 TYR   B C   1 
ATOM   1774 O  O   . TYR   B 1 33  ? -8.523  -3.722  -33.992  1.00 15.72 ? 126 TYR   B O   1 
ATOM   1775 C  CB  . TYR   B 1 33  ? -5.663  -3.181  -32.959  1.00 16.87 ? 126 TYR   B CB  1 
ATOM   1776 C  CG  . TYR   B 1 33  ? -5.739  -4.125  -31.793  1.00 16.80 ? 126 TYR   B CG  1 
ATOM   1777 C  CD1 . TYR   B 1 33  ? -4.800  -5.129  -31.627  1.00 16.50 ? 126 TYR   B CD1 1 
ATOM   1778 C  CD2 . TYR   B 1 33  ? -6.750  -4.007  -30.852  1.00 16.68 ? 126 TYR   B CD2 1 
ATOM   1779 C  CE1 . TYR   B 1 33  ? -4.858  -5.995  -30.548  1.00 16.60 ? 126 TYR   B CE1 1 
ATOM   1780 C  CE2 . TYR   B 1 33  ? -6.818  -4.858  -29.766  1.00 16.86 ? 126 TYR   B CE2 1 
ATOM   1781 C  CZ  . TYR   B 1 33  ? -5.869  -5.855  -29.614  1.00 16.68 ? 126 TYR   B CZ  1 
ATOM   1782 O  OH  . TYR   B 1 33  ? -5.943  -6.693  -28.546  1.00 17.11 ? 126 TYR   B OH  1 
ATOM   1783 N  N   . SER   B 1 34  ? -7.528  -5.775  -34.124  1.00 16.91 ? 127 SER   B N   1 
ATOM   1784 C  CA  . SER   B 1 34  ? -8.696  -6.646  -33.836  1.00 17.32 ? 127 SER   B CA  1 
ATOM   1785 C  C   . SER   B 1 34  ? -8.690  -7.021  -32.357  1.00 17.66 ? 127 SER   B C   1 
ATOM   1786 O  O   . SER   B 1 34  ? -7.864  -7.832  -31.932  1.00 17.05 ? 127 SER   B O   1 
ATOM   1787 C  CB  . SER   B 1 34  ? -8.668  -7.884  -34.699  1.00 17.60 ? 127 SER   B CB  1 
ATOM   1788 O  OG  . SER   B 1 34  ? -9.677  -8.803  -34.296  1.00 17.21 ? 127 SER   B OG  1 
ATOM   1789 N  N   . PRO   B 1 35  ? -9.589  -6.446  -31.521  1.00 18.36 ? 128 PRO   B N   1 
ATOM   1790 C  CA  . PRO   B 1 35  ? -9.747  -6.904  -30.143  1.00 19.04 ? 128 PRO   B CA  1 
ATOM   1791 C  C   . PRO   B 1 35  ? -10.092 -8.400  -30.060  1.00 19.39 ? 128 PRO   B C   1 
ATOM   1792 O  O   . PRO   B 1 35  ? -9.598  -9.050  -29.163  1.00 20.23 ? 128 PRO   B O   1 
ATOM   1793 C  CB  . PRO   B 1 35  ? -10.901 -6.059  -29.574  1.00 19.39 ? 128 PRO   B CB  1 
ATOM   1794 C  CG  . PRO   B 1 35  ? -11.015 -4.860  -30.490  1.00 19.20 ? 128 PRO   B CG  1 
ATOM   1795 C  CD  . PRO   B 1 35  ? -10.455 -5.299  -31.830  1.00 18.96 ? 128 PRO   B CD  1 
ATOM   1796 N  N   . ALA   B 1 36  ? -10.907 -8.909  -30.991  1.00 19.31 ? 129 ALA   B N   1 
ATOM   1797 C  CA  . ALA   B 1 36  ? -11.396 -10.309 -30.998  1.00 19.58 ? 129 ALA   B CA  1 
ATOM   1798 C  C   . ALA   B 1 36  ? -10.227 -11.276 -31.225  1.00 19.57 ? 129 ALA   B C   1 
ATOM   1799 O  O   . ALA   B 1 36  ? -10.228 -12.356 -30.608  1.00 20.72 ? 129 ALA   B O   1 
ATOM   1800 C  CB  . ALA   B 1 36  ? -12.472 -10.489 -32.041  1.00 19.33 ? 129 ALA   B CB  1 
ATOM   1801 N  N   . LEU   B 1 37  ? -9.265  -10.911 -32.074  1.00 19.59 ? 130 LEU   B N   1 
ATOM   1802 C  CA  . LEU   B 1 37  ? -8.102  -11.776 -32.414  1.00 19.41 ? 130 LEU   B CA  1 
ATOM   1803 C  C   . LEU   B 1 37  ? -6.851  -11.369 -31.618  1.00 18.91 ? 130 LEU   B C   1 
ATOM   1804 O  O   . LEU   B 1 37  ? -5.860  -12.124 -31.681  1.00 19.80 ? 130 LEU   B O   1 
ATOM   1805 C  CB  . LEU   B 1 37  ? -7.837  -11.676 -33.917  1.00 19.99 ? 130 LEU   B CB  1 
ATOM   1806 C  CG  . LEU   B 1 37  ? -8.982  -12.111 -34.830  1.00 20.34 ? 130 LEU   B CG  1 
ATOM   1807 C  CD1 . LEU   B 1 37  ? -8.655  -11.797 -36.280  1.00 20.72 ? 130 LEU   B CD1 1 
ATOM   1808 C  CD2 . LEU   B 1 37  ? -9.289  -13.592 -34.663  1.00 20.57 ? 130 LEU   B CD2 1 
ATOM   1809 N  N   . ASN   B 1 38  ? -6.872  -10.233 -30.909  1.00 17.44 ? 131 ASN   B N   1 
ATOM   1810 C  CA  . ASN   B 1 38  ? -5.659  -9.610  -30.305  1.00 17.06 ? 131 ASN   B CA  1 
ATOM   1811 C  C   . ASN   B 1 38  ? -4.564  -9.588  -31.374  1.00 16.83 ? 131 ASN   B C   1 
ATOM   1812 O  O   . ASN   B 1 38  ? -3.475  -10.157 -31.154  1.00 16.94 ? 131 ASN   B O   1 
ATOM   1813 C  CB  . ASN   B 1 38  ? -5.170  -10.331 -29.044  1.00 17.00 ? 131 ASN   B CB  1 
ATOM   1814 C  CG  . ASN   B 1 38  ? -3.965  -9.658  -28.415  1.00 16.87 ? 131 ASN   B CG  1 
ATOM   1815 O  OD1 . ASN   B 1 38  ? -3.863  -8.431  -28.413  1.00 16.27 ? 131 ASN   B OD1 1 
ATOM   1816 N  ND2 . ASN   B 1 38  ? -3.040  -10.446 -27.893  1.00 16.89 ? 131 ASN   B ND2 1 
ATOM   1817 N  N   . LYS   B 1 39  ? -4.873  -8.995  -32.521  1.00 16.90 ? 132 LYS   B N   1 
ATOM   1818 C  CA  . LYS   B 1 39  ? -3.995  -9.056  -33.711  1.00 16.98 ? 132 LYS   B CA  1 
ATOM   1819 C  C   . LYS   B 1 39  ? -3.995  -7.695  -34.400  1.00 16.74 ? 132 LYS   B C   1 
ATOM   1820 O  O   . LYS   B 1 39  ? -5.096  -7.170  -34.693  1.00 15.40 ? 132 LYS   B O   1 
ATOM   1821 C  CB  . LYS   B 1 39  ? -4.455  -10.173 -34.649  1.00 17.31 ? 132 LYS   B CB  1 
ATOM   1822 C  CG  . LYS   B 1 39  ? -3.537  -10.414 -35.838  1.00 17.46 ? 132 LYS   B CG  1 
ATOM   1823 C  CD  . LYS   B 1 39  ? -3.929  -11.612 -36.681  1.00 17.70 ? 132 LYS   B CD  1 
ATOM   1824 C  CE  . LYS   B 1 39  ? -2.972  -11.836 -37.832  1.00 18.06 ? 132 LYS   B CE  1 
ATOM   1825 N  NZ  . LYS   B 1 39  ? -3.123  -13.187 -38.425  1.00 18.63 ? 132 LYS   B NZ  1 
ATOM   1826 N  N   . MET   B 1 40  ? -2.795  -7.158  -34.627  1.00 16.76 ? 133 MET   B N   1 
ATOM   1827 C  CA  . MET   B 1 40  ? -2.566  -5.898  -35.375  1.00 17.54 ? 133 MET   B CA  1 
ATOM   1828 C  C   . MET   B 1 40  ? -2.380  -6.251  -36.851  1.00 17.00 ? 133 MET   B C   1 
ATOM   1829 O  O   . MET   B 1 40  ? -1.590  -7.160  -37.153  1.00 16.84 ? 133 MET   B O   1 
ATOM   1830 C  CB  . MET   B 1 40  ? -1.327  -5.147  -34.873  1.00 18.85 ? 133 MET   B CB  1 
ATOM   1831 C  CG  . MET   B 1 40  ? -0.989  -3.939  -35.734  1.00 20.66 ? 133 MET   B CG  1 
ATOM   1832 S  SD  . MET   B 1 40  ? 0.550   -3.145  -35.260  1.00 23.73 ? 133 MET   B SD  1 
ATOM   1833 C  CE  . MET   B 1 40  ? 0.007   -2.279  -33.788  1.00 23.32 ? 133 MET   B CE  1 
ATOM   1834 N  N   . PHE   B 1 41  ? -3.113  -5.567  -37.725  1.00 16.87 ? 134 PHE   B N   1 
ATOM   1835 C  CA  . PHE   B 1 41  ? -2.923  -5.589  -39.194  1.00 16.71 ? 134 PHE   B CA  1 
ATOM   1836 C  C   . PHE   B 1 41  ? -2.349  -4.233  -39.589  1.00 17.10 ? 134 PHE   B C   1 
ATOM   1837 O  O   . PHE   B 1 41  ? -2.981  -3.205  -39.268  1.00 16.74 ? 134 PHE   B O   1 
ATOM   1838 C  CB  . PHE   B 1 41  ? -4.246  -5.882  -39.903  1.00 16.75 ? 134 PHE   B CB  1 
ATOM   1839 C  CG  . PHE   B 1 41  ? -4.888  -7.179  -39.488  1.00 16.55 ? 134 PHE   B CG  1 
ATOM   1840 C  CD1 . PHE   B 1 41  ? -5.577  -7.282  -38.287  1.00 16.04 ? 134 PHE   B CD1 1 
ATOM   1841 C  CD2 . PHE   B 1 41  ? -4.793  -8.301  -40.297  1.00 16.42 ? 134 PHE   B CD2 1 
ATOM   1842 C  CE1 . PHE   B 1 41  ? -6.149  -8.486  -37.903  1.00 16.25 ? 134 PHE   B CE1 1 
ATOM   1843 C  CE2 . PHE   B 1 41  ? -5.372  -9.499  -39.914  1.00 16.18 ? 134 PHE   B CE2 1 
ATOM   1844 C  CZ  . PHE   B 1 41  ? -6.058  -9.588  -38.726  1.00 16.15 ? 134 PHE   B CZ  1 
ATOM   1845 N  N   . CYS   B 1 42  ? -1.199  -4.217  -40.261  1.00 17.34 ? 135 CYS   B N   1 
ATOM   1846 C  CA  . CYS   B 1 42  ? -0.531  -2.951  -40.648  1.00 18.53 ? 135 CYS   B CA  1 
ATOM   1847 C  C   . CYS   B 1 42  ? 0.156   -3.076  -42.007  1.00 19.21 ? 135 CYS   B C   1 
ATOM   1848 O  O   . CYS   B 1 42  ? 0.384   -4.208  -42.479  1.00 18.74 ? 135 CYS   B O   1 
ATOM   1849 C  CB  . CYS   B 1 42  ? 0.484   -2.528  -39.597  1.00 18.48 ? 135 CYS   B CB  1 
ATOM   1850 S  SG  . CYS   B 1 42  ? 1.756   -3.781  -39.308  1.00 18.65 ? 135 CYS   B SG  1 
ATOM   1851 N  N   . GLN   B 1 43  ? 0.458   -1.921  -42.594  1.00 20.31 ? 136 GLN   B N   1 
ATOM   1852 C  CA  . GLN   B 1 43  ? 1.158   -1.787  -43.890  1.00 21.72 ? 136 GLN   B CA  1 
ATOM   1853 C  C   . GLN   B 1 43  ? 2.659   -1.680  -43.639  1.00 21.20 ? 136 GLN   B C   1 
ATOM   1854 O  O   . GLN   B 1 43  ? 3.045   -1.031  -42.652  1.00 20.81 ? 136 GLN   B O   1 
ATOM   1855 C  CB  . GLN   B 1 43  ? 0.691   -0.532  -44.622  1.00 23.24 ? 136 GLN   B CB  1 
ATOM   1856 C  CG  . GLN   B 1 43  ? -0.637  -0.702  -45.336  1.00 24.78 ? 136 GLN   B CG  1 
ATOM   1857 C  CD  . GLN   B 1 43  ? -0.835  0.411   -46.333  1.00 26.31 ? 136 GLN   B CD  1 
ATOM   1858 O  OE1 . GLN   B 1 43  ? -1.041  0.172   -47.521  1.00 30.66 ? 136 GLN   B OE1 1 
ATOM   1859 N  NE2 . GLN   B 1 43  ? -0.750  1.640   -45.854  1.00 26.75 ? 136 GLN   B NE2 1 
ATOM   1860 N  N   . LEU   B 1 44  ? 3.447   -2.278  -44.533  1.00 20.82 ? 137 LEU   B N   1 
ATOM   1861 C  CA  . LEU   B 1 44  ? 4.924   -2.154  -44.608  1.00 21.39 ? 137 LEU   B CA  1 
ATOM   1862 C  C   . LEU   B 1 44  ? 5.343   -0.702  -44.353  1.00 20.82 ? 137 LEU   B C   1 
ATOM   1863 O  O   . LEU   B 1 44  ? 4.846   0.193   -45.065  1.00 19.65 ? 137 LEU   B O   1 
ATOM   1864 C  CB  . LEU   B 1 44  ? 5.369   -2.604  -46.003  1.00 21.99 ? 137 LEU   B CB  1 
ATOM   1865 C  CG  . LEU   B 1 44  ? 6.875   -2.654  -46.231  1.00 22.48 ? 137 LEU   B CG  1 
ATOM   1866 C  CD1 . LEU   B 1 44  ? 7.501   -3.754  -45.399  1.00 22.23 ? 137 LEU   B CD1 1 
ATOM   1867 C  CD2 . LEU   B 1 44  ? 7.187   -2.854  -47.707  1.00 23.14 ? 137 LEU   B CD2 1 
ATOM   1868 N  N   . ALA   B 1 45  ? 6.204   -0.490  -43.357  1.00 20.96 ? 138 ALA   B N   1 
ATOM   1869 C  CA  . ALA   B 1 45  ? 6.961   0.759   -43.111  1.00 21.86 ? 138 ALA   B CA  1 
ATOM   1870 C  C   . ALA   B 1 45  ? 6.036   1.927   -42.741  1.00 22.09 ? 138 ALA   B C   1 
ATOM   1871 O  O   . ALA   B 1 45  ? 6.525   3.070   -42.779  1.00 24.77 ? 138 ALA   B O   1 
ATOM   1872 C  CB  . ALA   B 1 45  ? 7.798   1.087   -44.329  1.00 22.03 ? 138 ALA   B CB  1 
ATOM   1873 N  N   . LYS   B 1 46  ? 4.779   1.666   -42.370  1.00 21.40 ? 139 LYS   B N   1 
ATOM   1874 C  CA  . LYS   B 1 46  ? 3.782   2.710   -42.001  1.00 20.96 ? 139 LYS   B CA  1 
ATOM   1875 C  C   . LYS   B 1 46  ? 3.671   2.809   -40.474  1.00 19.81 ? 139 LYS   B C   1 
ATOM   1876 O  O   . LYS   B 1 46  ? 4.038   1.842   -39.788  1.00 19.30 ? 139 LYS   B O   1 
ATOM   1877 C  CB  . LYS   B 1 46  ? 2.422   2.408   -42.637  1.00 22.04 ? 139 LYS   B CB  1 
ATOM   1878 C  CG  . LYS   B 1 46  ? 2.369   2.580   -44.150  1.00 23.43 ? 139 LYS   B CG  1 
ATOM   1879 C  CD  . LYS   B 1 46  ? 2.412   4.025   -44.603  1.00 24.83 ? 139 LYS   B CD  1 
ATOM   1880 C  CE  . LYS   B 1 46  ? 2.785   4.184   -46.064  1.00 26.58 ? 139 LYS   B CE  1 
ATOM   1881 N  NZ  . LYS   B 1 46  ? 1.952   3.333   -46.944  1.00 27.86 ? 139 LYS   B NZ  1 
ATOM   1882 N  N   . THR   B 1 47  ? 3.182   3.948   -39.976  1.00 19.31 ? 140 THR   B N   1 
ATOM   1883 C  CA  . THR   B 1 47  ? 3.051   4.259   -38.529  1.00 18.83 ? 140 THR   B CA  1 
ATOM   1884 C  C   . THR   B 1 47  ? 2.086   3.257   -37.890  1.00 18.53 ? 140 THR   B C   1 
ATOM   1885 O  O   . THR   B 1 47  ? 0.944   3.129   -38.383  1.00 18.35 ? 140 THR   B O   1 
ATOM   1886 C  CB  . THR   B 1 47  ? 2.601   5.709   -38.309  1.00 19.29 ? 140 THR   B CB  1 
ATOM   1887 O  OG1 . THR   B 1 47  ? 3.530   6.565   -38.980  1.00 18.28 ? 140 THR   B OG1 1 
ATOM   1888 C  CG2 . THR   B 1 47  ? 2.523   6.084   -36.845  1.00 19.14 ? 140 THR   B CG2 1 
ATOM   1889 N  N   . CYS   B 1 48  ? 2.549   2.558   -36.853  1.00 18.35 ? 141 CYS   B N   1 
ATOM   1890 C  CA  . CYS   B 1 48  ? 1.745   1.645   -36.002  1.00 18.33 ? 141 CYS   B CA  1 
ATOM   1891 C  C   . CYS   B 1 48  ? 1.742   2.148   -34.567  1.00 18.01 ? 141 CYS   B C   1 
ATOM   1892 O  O   . CYS   B 1 48  ? 2.662   1.843   -33.818  1.00 18.04 ? 141 CYS   B O   1 
ATOM   1893 C  CB  . CYS   B 1 48  ? 2.317   0.238   -36.003  1.00 19.19 ? 141 CYS   B CB  1 
ATOM   1894 S  SG  . CYS   B 1 48  ? 2.409   -0.465  -37.661  1.00 20.71 ? 141 CYS   B SG  1 
ATOM   1895 N  N   . PRO   B 1 49  ? 0.720   2.927   -34.142  1.00 17.61 ? 142 PRO   B N   1 
ATOM   1896 C  CA  . PRO   B 1 49  ? 0.615   3.351   -32.749  1.00 17.78 ? 142 PRO   B CA  1 
ATOM   1897 C  C   . PRO   B 1 49  ? 0.327   2.158   -31.824  1.00 17.39 ? 142 PRO   B C   1 
ATOM   1898 O  O   . PRO   B 1 49  ? -0.621  1.438   -32.056  1.00 17.66 ? 142 PRO   B O   1 
ATOM   1899 C  CB  . PRO   B 1 49  ? -0.530  4.378   -32.744  1.00 17.47 ? 142 PRO   B CB  1 
ATOM   1900 C  CG  . PRO   B 1 49  ? -0.720  4.745   -34.203  1.00 17.83 ? 142 PRO   B CG  1 
ATOM   1901 C  CD  . PRO   B 1 49  ? -0.349  3.497   -34.975  1.00 17.87 ? 142 PRO   B CD  1 
ATOM   1902 N  N   . VAL   B 1 50  ? 1.185   1.962   -30.824  1.00 17.20 ? 143 VAL   B N   1 
ATOM   1903 C  CA  . VAL   B 1 50  ? 0.969   0.997   -29.708  1.00 17.03 ? 143 VAL   B CA  1 
ATOM   1904 C  C   . VAL   B 1 50  ? 0.914   1.825   -28.425  1.00 17.01 ? 143 VAL   B C   1 
ATOM   1905 O  O   . VAL   B 1 50  ? 1.856   2.615   -28.188  1.00 17.57 ? 143 VAL   B O   1 
ATOM   1906 C  CB  . VAL   B 1 50  ? 2.062   -0.090  -29.668  1.00 17.26 ? 143 VAL   B CB  1 
ATOM   1907 C  CG1 . VAL   B 1 50  ? 1.934   -0.974  -28.435  1.00 17.48 ? 143 VAL   B CG1 1 
ATOM   1908 C  CG2 . VAL   B 1 50  ? 2.057   -0.937  -30.933  1.00 17.06 ? 143 VAL   B CG2 1 
ATOM   1909 N  N   . GLN   B 1 51  ? -0.176  1.705   -27.670  1.00 16.79 ? 144 GLN   B N   1 
ATOM   1910 C  CA  . GLN   B 1 51  ? -0.411  2.505   -26.438  1.00 17.33 ? 144 GLN   B CA  1 
ATOM   1911 C  C   . GLN   B 1 51  ? 0.059   1.709   -25.222  1.00 17.26 ? 144 GLN   B C   1 
ATOM   1912 O  O   . GLN   B 1 51  ? -0.233  0.497   -25.162  1.00 16.91 ? 144 GLN   B O   1 
ATOM   1913 C  CB  . GLN   B 1 51  ? -1.889  2.852   -26.269  1.00 17.35 ? 144 GLN   B CB  1 
ATOM   1914 C  CG  . GLN   B 1 51  ? -2.466  3.673   -27.409  1.00 17.64 ? 144 GLN   B CG  1 
ATOM   1915 C  CD  . GLN   B 1 51  ? -3.963  3.792   -27.286  1.00 17.39 ? 144 GLN   B CD  1 
ATOM   1916 O  OE1 . GLN   B 1 51  ? -4.620  2.989   -26.624  1.00 17.31 ? 144 GLN   B OE1 1 
ATOM   1917 N  NE2 . GLN   B 1 51  ? -4.516  4.804   -27.927  1.00 17.78 ? 144 GLN   B NE2 1 
ATOM   1918 N  N   . LEU   B 1 52  ? 0.740   2.384   -24.293  1.00 17.68 ? 145 LEU   B N   1 
ATOM   1919 C  CA  . LEU   B 1 52  ? 1.167   1.830   -22.984  1.00 17.94 ? 145 LEU   B CA  1 
ATOM   1920 C  C   . LEU   B 1 52  ? 0.254   2.413   -21.903  1.00 18.09 ? 145 LEU   B C   1 
ATOM   1921 O  O   . LEU   B 1 52  ? 0.276   3.650   -21.729  1.00 19.43 ? 145 LEU   B O   1 
ATOM   1922 C  CB  . LEU   B 1 52  ? 2.634   2.196   -22.723  1.00 17.55 ? 145 LEU   B CB  1 
ATOM   1923 C  CG  . LEU   B 1 52  ? 3.593   2.039   -23.905  1.00 17.55 ? 145 LEU   B CG  1 
ATOM   1924 C  CD1 . LEU   B 1 52  ? 5.002   2.447   -23.503  1.00 17.35 ? 145 LEU   B CD1 1 
ATOM   1925 C  CD2 . LEU   B 1 52  ? 3.591   0.613   -24.437  1.00 17.51 ? 145 LEU   B CD2 1 
ATOM   1926 N  N   . TRP   B 1 53  ? -0.535  1.561   -21.242  1.00 18.10 ? 146 TRP   B N   1 
ATOM   1927 C  CA  . TRP   B 1 53  ? -1.450  1.935   -20.133  1.00 18.56 ? 146 TRP   B CA  1 
ATOM   1928 C  C   . TRP   B 1 53  ? -0.868  1.426   -18.813  1.00 18.56 ? 146 TRP   B C   1 
ATOM   1929 O  O   . TRP   B 1 53  ? -0.533  0.229   -18.742  1.00 17.61 ? 146 TRP   B O   1 
ATOM   1930 C  CB  . TRP   B 1 53  ? -2.857  1.383   -20.384  1.00 19.26 ? 146 TRP   B CB  1 
ATOM   1931 C  CG  . TRP   B 1 53  ? -3.552  2.014   -21.552  1.00 19.89 ? 146 TRP   B CG  1 
ATOM   1932 C  CD1 . TRP   B 1 53  ? -3.350  1.736   -22.873  1.00 19.93 ? 146 TRP   B CD1 1 
ATOM   1933 C  CD2 . TRP   B 1 53  ? -4.569  3.032   -21.508  1.00 20.16 ? 146 TRP   B CD2 1 
ATOM   1934 N  NE1 . TRP   B 1 53  ? -4.168  2.509   -23.652  1.00 20.26 ? 146 TRP   B NE1 1 
ATOM   1935 C  CE2 . TRP   B 1 53  ? -4.934  3.308   -22.845  1.00 20.39 ? 146 TRP   B CE2 1 
ATOM   1936 C  CE3 . TRP   B 1 53  ? -5.213  3.727   -20.477  1.00 20.21 ? 146 TRP   B CE3 1 
ATOM   1937 C  CZ2 . TRP   B 1 53  ? -5.898  4.261   -23.172  1.00 20.48 ? 146 TRP   B CZ2 1 
ATOM   1938 C  CZ3 . TRP   B 1 53  ? -6.174  4.661   -20.802  1.00 20.27 ? 146 TRP   B CZ3 1 
ATOM   1939 C  CH2 . TRP   B 1 53  ? -6.508  4.925   -22.130  1.00 20.60 ? 146 TRP   B CH2 1 
ATOM   1940 N  N   . VAL   B 1 54  ? -0.776  2.301   -17.808  1.00 19.32 ? 147 VAL   B N   1 
ATOM   1941 C  CA  . VAL   B 1 54  ? -0.243  1.977   -16.451  1.00 20.55 ? 147 VAL   B CA  1 
ATOM   1942 C  C   . VAL   B 1 54  ? -1.204  2.535   -15.393  1.00 21.77 ? 147 VAL   B C   1 
ATOM   1943 O  O   . VAL   B 1 54  ? -1.817  3.589   -15.646  1.00 20.70 ? 147 VAL   B O   1 
ATOM   1944 C  CB  . VAL   B 1 54  ? 1.193   2.514   -16.266  1.00 20.90 ? 147 VAL   B CB  1 
ATOM   1945 C  CG1 . VAL   B 1 54  ? 2.174   1.794   -17.181  1.00 20.58 ? 147 VAL   B CG1 1 
ATOM   1946 C  CG2 . VAL   B 1 54  ? 1.289   4.023   -16.462  1.00 20.58 ? 147 VAL   B CG2 1 
ATOM   1947 N  N   . ASP   B 1 55  ? -1.341  1.824   -14.270  1.00 23.84 ? 148 ASP   B N   1 
ATOM   1948 C  CA  . ASP   B 1 55  ? -2.129  2.248   -13.080  1.00 25.43 ? 148 ASP   B CA  1 
ATOM   1949 C  C   . ASP   B 1 55  ? -1.314  3.264   -12.271  1.00 26.24 ? 148 ASP   B C   1 
ATOM   1950 O  O   . ASP   B 1 55  ? -1.930  4.101   -11.583  1.00 26.83 ? 148 ASP   B O   1 
ATOM   1951 C  CB  . ASP   B 1 55  ? -2.518  1.044   -12.218  1.00 26.37 ? 148 ASP   B CB  1 
ATOM   1952 C  CG  . ASP   B 1 55  ? -3.528  0.117   -12.872  1.00 27.13 ? 148 ASP   B CG  1 
ATOM   1953 O  OD1 . ASP   B 1 55  ? -4.207  0.564   -13.818  1.00 27.31 ? 148 ASP   B OD1 1 
ATOM   1954 O  OD2 . ASP   B 1 55  ? -3.622  -1.053  -12.431  1.00 29.34 ? 148 ASP   B OD2 1 
ATOM   1955 N  N   . SER   B 1 56  ? 0.019   3.192   -12.346  1.00 26.53 ? 149 SER   B N   1 
ATOM   1956 C  CA  . SER   B 1 56  ? 0.955   4.125   -11.664  1.00 26.59 ? 149 SER   B CA  1 
ATOM   1957 C  C   . SER   B 1 56  ? 2.187   4.373   -12.542  1.00 27.08 ? 149 SER   B C   1 
ATOM   1958 O  O   . SER   B 1 56  ? 2.591   3.455   -13.286  1.00 26.48 ? 149 SER   B O   1 
ATOM   1959 C  CB  . SER   B 1 56  ? 1.327   3.606   -10.301  1.00 26.20 ? 149 SER   B CB  1 
ATOM   1960 O  OG  . SER   B 1 56  ? 1.788   2.272   -10.384  1.00 26.61 ? 149 SER   B OG  1 
ATOM   1961 N  N   . THR   B 1 57  ? 2.755   5.576   -12.453  1.00 27.22 ? 150 THR   B N   1 
ATOM   1962 C  CA  . THR   B 1 57  ? 3.842   6.068   -13.337  1.00 28.29 ? 150 THR   B CA  1 
ATOM   1963 C  C   . THR   B 1 57  ? 5.138   5.344   -12.983  1.00 28.37 ? 150 THR   B C   1 
ATOM   1964 O  O   . THR   B 1 57  ? 5.617   5.460   -11.859  1.00 27.51 ? 150 THR   B O   1 
ATOM   1965 C  CB  . THR   B 1 57  ? 3.976   7.591   -13.233  1.00 28.69 ? 150 THR   B CB  1 
ATOM   1966 O  OG1 . THR   B 1 57  ? 2.683   8.130   -13.504  1.00 29.27 ? 150 THR   B OG1 1 
ATOM   1967 C  CG2 . THR   B 1 57  ? 4.989   8.173   -14.195  1.00 29.35 ? 150 THR   B CG2 1 
ATOM   1968 N  N   . PRO   B 1 58  ? 5.740   4.567   -13.917  1.00 28.34 ? 151 PRO   B N   1 
ATOM   1969 C  CA  . PRO   B 1 58  ? 7.056   3.973   -13.685  1.00 28.10 ? 151 PRO   B CA  1 
ATOM   1970 C  C   . PRO   B 1 58  ? 8.092   5.070   -13.455  1.00 27.43 ? 151 PRO   B C   1 
ATOM   1971 O  O   . PRO   B 1 58  ? 7.954   6.166   -13.991  1.00 26.83 ? 151 PRO   B O   1 
ATOM   1972 C  CB  . PRO   B 1 58  ? 7.361   3.178   -14.967  1.00 27.93 ? 151 PRO   B CB  1 
ATOM   1973 C  CG  . PRO   B 1 58  ? 6.015   2.999   -15.639  1.00 28.31 ? 151 PRO   B CG  1 
ATOM   1974 C  CD  . PRO   B 1 58  ? 5.187   4.198   -15.230  1.00 28.18 ? 151 PRO   B CD  1 
ATOM   1975 N  N   . PRO   B 1 59  ? 9.161   4.812   -12.667  1.00 28.31 ? 152 PRO   B N   1 
ATOM   1976 C  CA  . PRO   B 1 59  ? 10.150  5.843   -12.352  1.00 28.83 ? 152 PRO   B CA  1 
ATOM   1977 C  C   . PRO   B 1 59  ? 10.937  6.295   -13.579  1.00 30.10 ? 152 PRO   B C   1 
ATOM   1978 O  O   . PRO   B 1 59  ? 10.853  5.672   -14.639  1.00 29.18 ? 152 PRO   B O   1 
ATOM   1979 C  CB  . PRO   B 1 59  ? 11.075  5.165   -11.329  1.00 28.79 ? 152 PRO   B CB  1 
ATOM   1980 C  CG  . PRO   B 1 59  ? 10.927  3.685   -11.617  1.00 28.63 ? 152 PRO   B CG  1 
ATOM   1981 C  CD  . PRO   B 1 59  ? 9.483   3.520   -12.043  1.00 27.82 ? 152 PRO   B CD  1 
ATOM   1982 N  N   . PRO   B 1 60  ? 11.714  7.399   -13.465  1.00 31.23 ? 153 PRO   B N   1 
ATOM   1983 C  CA  . PRO   B 1 60  ? 12.594  7.853   -14.544  1.00 30.34 ? 153 PRO   B CA  1 
ATOM   1984 C  C   . PRO   B 1 60  ? 13.623  6.771   -14.899  1.00 27.56 ? 153 PRO   B C   1 
ATOM   1985 O  O   . PRO   B 1 60  ? 14.047  6.068   -14.001  1.00 27.99 ? 153 PRO   B O   1 
ATOM   1986 C  CB  . PRO   B 1 60  ? 13.317  9.080   -13.959  1.00 31.24 ? 153 PRO   B CB  1 
ATOM   1987 C  CG  . PRO   B 1 60  ? 12.442  9.529   -12.803  1.00 31.37 ? 153 PRO   B CG  1 
ATOM   1988 C  CD  . PRO   B 1 60  ? 11.800  8.264   -12.276  1.00 32.11 ? 153 PRO   B CD  1 
ATOM   1989 N  N   . GLY   B 1 61  ? 13.971  6.650   -16.183  1.00 25.34 ? 154 GLY   B N   1 
ATOM   1990 C  CA  . GLY   B 1 61  ? 14.955  5.669   -16.684  1.00 23.49 ? 154 GLY   B CA  1 
ATOM   1991 C  C   . GLY   B 1 61  ? 14.311  4.348   -17.078  1.00 21.97 ? 154 GLY   B C   1 
ATOM   1992 O  O   . GLY   B 1 61  ? 15.048  3.452   -17.533  1.00 20.81 ? 154 GLY   B O   1 
ATOM   1993 N  N   . THR   B 1 62  ? 12.990  4.216   -16.907  1.00 19.73 ? 155 THR   B N   1 
ATOM   1994 C  CA  . THR   B 1 62  ? 12.197  3.044   -17.366  1.00 18.60 ? 155 THR   B CA  1 
ATOM   1995 C  C   . THR   B 1 62  ? 12.303  2.970   -18.892  1.00 17.52 ? 155 THR   B C   1 
ATOM   1996 O  O   . THR   B 1 62  ? 12.322  4.044   -19.536  1.00 16.95 ? 155 THR   B O   1 
ATOM   1997 C  CB  . THR   B 1 62  ? 10.738  3.125   -16.898  1.00 18.71 ? 155 THR   B CB  1 
ATOM   1998 O  OG1 . THR   B 1 62  ? 10.735  3.170   -15.471  1.00 19.12 ? 155 THR   B OG1 1 
ATOM   1999 C  CG2 . THR   B 1 62  ? 9.899   1.953   -17.361  1.00 18.50 ? 155 THR   B CG2 1 
ATOM   2000 N  N   . ARG   B 1 63  ? 12.391  1.751   -19.434  1.00 16.51 ? 156 ARG   B N   1 
ATOM   2001 C  CA  . ARG   B 1 63  ? 12.594  1.499   -20.885  1.00 16.00 ? 156 ARG   B CA  1 
ATOM   2002 C  C   . ARG   B 1 63  ? 11.500  0.558   -21.401  1.00 15.48 ? 156 ARG   B C   1 
ATOM   2003 O  O   . ARG   B 1 63  ? 10.940  -0.213  -20.606  1.00 15.91 ? 156 ARG   B O   1 
ATOM   2004 C  CB  . ARG   B 1 63  ? 14.018  0.987   -21.115  1.00 15.79 ? 156 ARG   B CB  1 
ATOM   2005 C  CG  . ARG   B 1 63  ? 15.041  2.110   -21.214  1.00 16.01 ? 156 ARG   B CG  1 
ATOM   2006 C  CD  . ARG   B 1 63  ? 16.396  1.747   -20.638  1.00 15.77 ? 156 ARG   B CD  1 
ATOM   2007 N  NE  . ARG   B 1 63  ? 17.036  0.596   -21.265  1.00 16.13 ? 156 ARG   B NE  1 
ATOM   2008 C  CZ  . ARG   B 1 63  ? 17.754  0.632   -22.390  1.00 15.98 ? 156 ARG   B CZ  1 
ATOM   2009 N  NH1 . ARG   B 1 63  ? 17.893  1.760   -23.071  1.00 15.96 ? 156 ARG   B NH1 1 
ATOM   2010 N  NH2 . ARG   B 1 63  ? 18.306  -0.477  -22.844  1.00 15.51 ? 156 ARG   B NH2 1 
ATOM   2011 N  N   . VAL   B 1 64  ? 11.187  0.664   -22.692  1.00 15.03 ? 157 VAL   B N   1 
ATOM   2012 C  CA  . VAL   B 1 64  ? 10.122  -0.127  -23.368  1.00 14.96 ? 157 VAL   B CA  1 
ATOM   2013 C  C   . VAL   B 1 64  ? 10.748  -0.840  -24.569  1.00 14.99 ? 157 VAL   B C   1 
ATOM   2014 O  O   . VAL   B 1 64  ? 11.243  -0.143  -25.473  1.00 14.22 ? 157 VAL   B O   1 
ATOM   2015 C  CB  . VAL   B 1 64  ? 8.945   0.765   -23.796  1.00 15.11 ? 157 VAL   B CB  1 
ATOM   2016 C  CG1 . VAL   B 1 64  ? 7.779   -0.068  -24.304  1.00 15.39 ? 157 VAL   B CG1 1 
ATOM   2017 C  CG2 . VAL   B 1 64  ? 8.504   1.690   -22.671  1.00 15.18 ? 157 VAL   B CG2 1 
ATOM   2018 N  N   . ARG   B 1 65  ? 10.721  -2.173  -24.560  1.00 14.70 ? 158 ARG   B N   1 
ATOM   2019 C  CA  . ARG   B 1 65  ? 11.378  -3.036  -25.574  1.00 15.44 ? 158 ARG   B CA  1 
ATOM   2020 C  C   . ARG   B 1 65  ? 10.305  -3.745  -26.402  1.00 15.08 ? 158 ARG   B C   1 
ATOM   2021 O  O   . ARG   B 1 65  ? 9.324   -4.225  -25.805  1.00 15.67 ? 158 ARG   B O   1 
ATOM   2022 C  CB  . ARG   B 1 65  ? 12.295  -4.055  -24.891  1.00 15.38 ? 158 ARG   B CB  1 
ATOM   2023 C  CG  . ARG   B 1 65  ? 13.093  -4.926  -25.853  1.00 15.57 ? 158 ARG   B CG  1 
ATOM   2024 C  CD  . ARG   B 1 65  ? 14.019  -5.889  -25.128  1.00 15.66 ? 158 ARG   B CD  1 
ATOM   2025 N  NE  . ARG   B 1 65  ? 14.898  -5.166  -24.223  1.00 15.77 ? 158 ARG   B NE  1 
ATOM   2026 C  CZ  . ARG   B 1 65  ? 16.019  -4.537  -24.571  1.00 16.36 ? 158 ARG   B CZ  1 
ATOM   2027 N  NH1 . ARG   B 1 65  ? 16.442  -4.542  -25.825  1.00 16.48 ? 158 ARG   B NH1 1 
ATOM   2028 N  NH2 . ARG   B 1 65  ? 16.709  -3.884  -23.652  1.00 17.20 ? 158 ARG   B NH2 1 
ATOM   2029 N  N   . ALA   B 1 66  ? 10.498  -3.813  -27.719  1.00 15.06 ? 159 ALA   B N   1 
ATOM   2030 C  CA  . ALA   B 1 66  ? 9.653   -4.598  -28.651  1.00 15.09 ? 159 ALA   B CA  1 
ATOM   2031 C  C   . ALA   B 1 66  ? 10.512  -5.668  -29.331  1.00 14.99 ? 159 ALA   B C   1 
ATOM   2032 O  O   . ALA   B 1 66  ? 11.626  -5.338  -29.780  1.00 14.39 ? 159 ALA   B O   1 
ATOM   2033 C  CB  . ALA   B 1 66  ? 8.997   -3.699  -29.665  1.00 14.87 ? 159 ALA   B CB  1 
ATOM   2034 N  N   . MET   B 1 67  ? 9.999   -6.898  -29.402  1.00 15.35 ? 160 MET   B N   1 
ATOM   2035 C  CA  . MET   B 1 67  ? 10.676  -8.056  -30.040  1.00 15.79 ? 160 MET   B CA  1 
ATOM   2036 C  C   . MET   B 1 67  ? 9.621   -8.911  -30.754  1.00 15.58 ? 160 MET   B C   1 
ATOM   2037 O  O   . MET   B 1 67  ? 8.531   -9.138  -30.173  1.00 14.98 ? 160 MET   B O   1 
ATOM   2038 C  CB  . MET   B 1 67  ? 11.426  -8.883  -28.990  1.00 16.42 ? 160 MET   B CB  1 
ATOM   2039 C  CG  . MET   B 1 67  ? 12.080  -10.146 -29.529  1.00 17.02 ? 160 MET   B CG  1 
ATOM   2040 S  SD  . MET   B 1 67  ? 12.774  -11.186 -28.207  1.00 17.42 ? 160 MET   B SD  1 
ATOM   2041 C  CE  . MET   B 1 67  ? 14.094  -10.130 -27.606  1.00 17.01 ? 160 MET   B CE  1 
ATOM   2042 N  N   . ALA   B 1 68  ? 9.923   -9.348  -31.977  1.00 15.98 ? 161 ALA   B N   1 
ATOM   2043 C  CA  . ALA   B 1 68  ? 9.073   -10.271 -32.764  1.00 16.40 ? 161 ALA   B CA  1 
ATOM   2044 C  C   . ALA   B 1 68  ? 9.539   -11.710 -32.511  1.00 17.76 ? 161 ALA   B C   1 
ATOM   2045 O  O   . ALA   B 1 68  ? 10.755  -11.938 -32.503  1.00 17.86 ? 161 ALA   B O   1 
ATOM   2046 C  CB  . ALA   B 1 68  ? 9.141   -9.917  -34.228  1.00 16.31 ? 161 ALA   B CB  1 
ATOM   2047 N  N   . ILE   B 1 69  ? 8.602   -12.634 -32.282  1.00 18.68 ? 162 ILE   B N   1 
ATOM   2048 C  CA  . ILE   B 1 69  ? 8.850   -14.107 -32.309  1.00 19.44 ? 162 ILE   B CA  1 
ATOM   2049 C  C   . ILE   B 1 69  ? 7.778   -14.743 -33.200  1.00 19.88 ? 162 ILE   B C   1 
ATOM   2050 O  O   . ILE   B 1 69  ? 6.671   -14.167 -33.300  1.00 19.64 ? 162 ILE   B O   1 
ATOM   2051 C  CB  . ILE   B 1 69  ? 8.867   -14.720 -30.889  1.00 20.23 ? 162 ILE   B CB  1 
ATOM   2052 C  CG1 . ILE   B 1 69  ? 7.473   -14.775 -30.255  1.00 21.28 ? 162 ILE   B CG1 1 
ATOM   2053 C  CG2 . ILE   B 1 69  ? 9.856   -13.988 -29.993  1.00 20.42 ? 162 ILE   B CG2 1 
ATOM   2054 C  CD1 . ILE   B 1 69  ? 7.388   -15.691 -29.051  1.00 21.70 ? 162 ILE   B CD1 1 
ATOM   2055 N  N   . TYR   B 1 70  ? 8.099   -15.874 -33.835  1.00 19.89 ? 163 TYR   B N   1 
ATOM   2056 C  CA  . TYR   B 1 70  ? 7.129   -16.709 -34.591  1.00 20.09 ? 163 TYR   B CA  1 
ATOM   2057 C  C   . TYR   B 1 70  ? 6.105   -17.269 -33.600  1.00 21.01 ? 163 TYR   B C   1 
ATOM   2058 O  O   . TYR   B 1 70  ? 6.493   -17.649 -32.486  1.00 20.66 ? 163 TYR   B O   1 
ATOM   2059 C  CB  . TYR   B 1 70  ? 7.862   -17.778 -35.409  1.00 20.10 ? 163 TYR   B CB  1 
ATOM   2060 C  CG  . TYR   B 1 70  ? 8.555   -17.207 -36.619  1.00 19.95 ? 163 TYR   B CG  1 
ATOM   2061 C  CD1 . TYR   B 1 70  ? 7.813   -16.646 -37.646  1.00 19.72 ? 163 TYR   B CD1 1 
ATOM   2062 C  CD2 . TYR   B 1 70  ? 9.938   -17.180 -36.726  1.00 19.69 ? 163 TYR   B CD2 1 
ATOM   2063 C  CE1 . TYR   B 1 70  ? 8.421   -16.090 -38.757  1.00 19.54 ? 163 TYR   B CE1 1 
ATOM   2064 C  CE2 . TYR   B 1 70  ? 10.562  -16.628 -37.833  1.00 19.71 ? 163 TYR   B CE2 1 
ATOM   2065 C  CZ  . TYR   B 1 70  ? 9.800   -16.083 -38.853  1.00 19.48 ? 163 TYR   B CZ  1 
ATOM   2066 O  OH  . TYR   B 1 70  ? 10.391  -15.535 -39.954  1.00 20.36 ? 163 TYR   B OH  1 
ATOM   2067 N  N   . LYS   B 1 71  ? 4.826   -17.258 -33.982  1.00 22.46 ? 164 LYS   B N   1 
ATOM   2068 C  CA  . LYS   B 1 71  ? 3.693   -17.664 -33.111  1.00 24.03 ? 164 LYS   B CA  1 
ATOM   2069 C  C   . LYS   B 1 71  ? 3.670   -19.189 -32.952  1.00 24.85 ? 164 LYS   B C   1 
ATOM   2070 O  O   . LYS   B 1 71  ? 3.377   -19.654 -31.833  1.00 25.09 ? 164 LYS   B O   1 
ATOM   2071 C  CB  . LYS   B 1 71  ? 2.365   -17.173 -33.690  1.00 24.32 ? 164 LYS   B CB  1 
ATOM   2072 C  CG  . LYS   B 1 71  ? 1.151   -17.499 -32.834  1.00 25.21 ? 164 LYS   B CG  1 
ATOM   2073 C  CD  . LYS   B 1 71  ? -0.149  -17.011 -33.413  1.00 26.04 ? 164 LYS   B CD  1 
ATOM   2074 C  CE  . LYS   B 1 71  ? -1.311  -17.181 -32.459  1.00 26.68 ? 164 LYS   B CE  1 
ATOM   2075 N  NZ  . LYS   B 1 71  ? -2.607  -17.142 -33.178  1.00 27.42 ? 164 LYS   B NZ  1 
ATOM   2076 N  N   . GLN   B 1 72  ? 3.939   -19.928 -34.032  1.00 26.23 ? 165 GLN   B N   1 
ATOM   2077 C  CA  . GLN   B 1 72  ? 3.818   -21.413 -34.087  1.00 27.40 ? 165 GLN   B CA  1 
ATOM   2078 C  C   . GLN   B 1 72  ? 5.021   -22.066 -33.395  1.00 27.80 ? 165 GLN   B C   1 
ATOM   2079 O  O   . GLN   B 1 72  ? 6.157   -21.607 -33.613  1.00 27.59 ? 165 GLN   B O   1 
ATOM   2080 C  CB  . GLN   B 1 72  ? 3.707   -21.887 -35.536  1.00 27.76 ? 165 GLN   B CB  1 
ATOM   2081 C  CG  . GLN   B 1 72  ? 2.457   -21.384 -36.245  1.00 28.32 ? 165 GLN   B CG  1 
ATOM   2082 C  CD  . GLN   B 1 72  ? 2.610   -21.469 -37.742  1.00 28.93 ? 165 GLN   B CD  1 
ATOM   2083 O  OE1 . GLN   B 1 72  ? 3.533   -20.906 -38.320  1.00 29.11 ? 165 GLN   B OE1 1 
ATOM   2084 N  NE2 . GLN   B 1 72  ? 1.704   -22.185 -38.387  1.00 31.40 ? 165 GLN   B NE2 1 
ATOM   2085 N  N   . SER   B 1 73  ? 4.761   -23.114 -32.605  1.00 28.74 ? 166 SER   B N   1 
ATOM   2086 C  CA  . SER   B 1 73  ? 5.762   -23.887 -31.820  1.00 29.65 ? 166 SER   B CA  1 
ATOM   2087 C  C   . SER   B 1 73  ? 6.959   -24.276 -32.696  1.00 28.72 ? 166 SER   B C   1 
ATOM   2088 O  O   . SER   B 1 73  ? 8.099   -24.045 -32.256  1.00 29.63 ? 166 SER   B O   1 
ATOM   2089 C  CB  . SER   B 1 73  ? 5.130   -25.102 -31.196  1.00 30.33 ? 166 SER   B CB  1 
ATOM   2090 O  OG  . SER   B 1 73  ? 4.270   -24.726 -30.131  1.00 32.63 ? 166 SER   B OG  1 
ATOM   2091 N  N   . GLN   B 1 74  ? 6.709   -24.819 -33.893  1.00 28.68 ? 167 GLN   B N   1 
ATOM   2092 C  CA  . GLN   B 1 74  ? 7.758   -25.419 -34.763  1.00 29.68 ? 167 GLN   B CA  1 
ATOM   2093 C  C   . GLN   B 1 74  ? 8.703   -24.338 -35.310  1.00 28.94 ? 167 GLN   B C   1 
ATOM   2094 O  O   . GLN   B 1 74  ? 9.769   -24.718 -35.830  1.00 27.98 ? 167 GLN   B O   1 
ATOM   2095 C  CB  . GLN   B 1 74  ? 7.149   -26.240 -35.906  1.00 31.62 ? 167 GLN   B CB  1 
ATOM   2096 C  CG  . GLN   B 1 74  ? 6.322   -25.442 -36.907  1.00 32.21 ? 167 GLN   B CG  1 
ATOM   2097 C  CD  . GLN   B 1 74  ? 4.845   -25.451 -36.598  1.00 33.83 ? 167 GLN   B CD  1 
ATOM   2098 O  OE1 . GLN   B 1 74  ? 4.425   -25.454 -35.440  1.00 34.96 ? 167 GLN   B OE1 1 
ATOM   2099 N  NE2 . GLN   B 1 74  ? 4.036   -25.447 -37.646  1.00 35.28 ? 167 GLN   B NE2 1 
ATOM   2100 N  N   . HIS   B 1 75  ? 8.348   -23.051 -35.202  1.00 28.07 ? 168 HIS   B N   1 
ATOM   2101 C  CA  . HIS   B 1 75  ? 9.145   -21.921 -35.755  1.00 27.81 ? 168 HIS   B CA  1 
ATOM   2102 C  C   . HIS   B 1 75  ? 9.681   -21.000 -34.646  1.00 27.44 ? 168 HIS   B C   1 
ATOM   2103 O  O   . HIS   B 1 75  ? 10.409  -20.048 -34.982  1.00 25.97 ? 168 HIS   B O   1 
ATOM   2104 C  CB  . HIS   B 1 75  ? 8.304   -21.139 -36.771  1.00 27.49 ? 168 HIS   B CB  1 
ATOM   2105 C  CG  . HIS   B 1 75  ? 7.880   -21.943 -37.953  1.00 28.22 ? 168 HIS   B CG  1 
ATOM   2106 N  ND1 . HIS   B 1 75  ? 8.784   -22.601 -38.763  1.00 28.27 ? 168 HIS   B ND1 1 
ATOM   2107 C  CD2 . HIS   B 1 75  ? 6.658   -22.176 -38.482  1.00 29.22 ? 168 HIS   B CD2 1 
ATOM   2108 C  CE1 . HIS   B 1 75  ? 8.138   -23.215 -39.734  1.00 28.71 ? 168 HIS   B CE1 1 
ATOM   2109 N  NE2 . HIS   B 1 75  ? 6.832   -22.972 -39.583  1.00 28.90 ? 168 HIS   B NE2 1 
ATOM   2110 N  N   . MET   B 1 76  ? 9.361   -21.273 -33.380  1.00 28.24 ? 169 MET   B N   1 
ATOM   2111 C  CA  . MET   B 1 76  ? 9.592   -20.327 -32.253  1.00 29.19 ? 169 MET   B CA  1 
ATOM   2112 C  C   . MET   B 1 76  ? 11.089  -20.054 -32.057  1.00 27.80 ? 169 MET   B C   1 
ATOM   2113 O  O   . MET   B 1 76  ? 11.421  -18.914 -31.686  1.00 26.90 ? 169 MET   B O   1 
ATOM   2114 C  CB  . MET   B 1 76  ? 9.004   -20.861 -30.944  1.00 31.49 ? 169 MET   B CB  1 
ATOM   2115 C  CG  . MET   B 1 76  ? 7.528   -20.590 -30.808  1.00 34.54 ? 169 MET   B CG  1 
ATOM   2116 S  SD  . MET   B 1 76  ? 7.077   -20.034 -29.152  1.00 39.71 ? 169 MET   B SD  1 
ATOM   2117 C  CE  . MET   B 1 76  ? 5.940   -18.714 -29.575  1.00 37.73 ? 169 MET   B CE  1 
ATOM   2118 N  N   . THR   B 1 77  ? 11.953  -21.049 -32.281  1.00 26.67 ? 170 THR   B N   1 
ATOM   2119 C  CA  . THR   B 1 77  ? 13.418  -20.950 -32.034  1.00 26.37 ? 170 THR   B CA  1 
ATOM   2120 C  C   . THR   B 1 77  ? 14.099  -20.156 -33.156  1.00 25.21 ? 170 THR   B C   1 
ATOM   2121 O  O   . THR   B 1 77  ? 15.270  -19.779 -32.966  1.00 26.24 ? 170 THR   B O   1 
ATOM   2122 C  CB  . THR   B 1 77  ? 14.068  -22.331 -31.873  1.00 26.68 ? 170 THR   B CB  1 
ATOM   2123 O  OG1 . THR   B 1 77  ? 13.942  -23.030 -33.114  1.00 26.95 ? 170 THR   B OG1 1 
ATOM   2124 C  CG2 . THR   B 1 77  ? 13.459  -23.134 -30.744  1.00 27.05 ? 170 THR   B CG2 1 
ATOM   2125 N  N   . GLU   B 1 78  ? 13.417  -19.923 -34.283  1.00 23.64 ? 171 GLU   B N   1 
ATOM   2126 C  CA  . GLU   B 1 78  ? 13.991  -19.175 -35.433  1.00 23.06 ? 171 GLU   B CA  1 
ATOM   2127 C  C   . GLU   B 1 78  ? 13.891  -17.671 -35.147  1.00 22.46 ? 171 GLU   B C   1 
ATOM   2128 O  O   . GLU   B 1 78  ? 12.799  -17.214 -34.747  1.00 21.22 ? 171 GLU   B O   1 
ATOM   2129 C  CB  . GLU   B 1 78  ? 13.284  -19.553 -36.734  1.00 22.68 ? 171 GLU   B CB  1 
ATOM   2130 C  CG  . GLU   B 1 78  ? 13.972  -19.007 -37.967  1.00 23.33 ? 171 GLU   B CG  1 
ATOM   2131 C  CD  . GLU   B 1 78  ? 13.283  -19.334 -39.279  1.00 24.26 ? 171 GLU   B CD  1 
ATOM   2132 O  OE1 . GLU   B 1 78  ? 12.616  -20.386 -39.357  1.00 25.34 ? 171 GLU   B OE1 1 
ATOM   2133 O  OE2 . GLU   B 1 78  ? 13.399  -18.528 -40.215  1.00 25.59 ? 171 GLU   B OE2 1 
ATOM   2134 N  N   . VAL   B 1 79  ? 14.989  -16.936 -35.345  1.00 21.53 ? 172 VAL   B N   1 
ATOM   2135 C  CA  . VAL   B 1 79  ? 15.051  -15.458 -35.144  1.00 21.31 ? 172 VAL   B CA  1 
ATOM   2136 C  C   . VAL   B 1 79  ? 14.213  -14.796 -36.242  1.00 20.75 ? 172 VAL   B C   1 
ATOM   2137 O  O   . VAL   B 1 79  ? 14.418  -15.135 -37.431  1.00 19.85 ? 172 VAL   B O   1 
ATOM   2138 C  CB  . VAL   B 1 79  ? 16.499  -14.933 -35.144  1.00 22.07 ? 172 VAL   B CB  1 
ATOM   2139 C  CG1 . VAL   B 1 79  ? 16.545  -13.411 -35.098  1.00 22.34 ? 172 VAL   B CG1 1 
ATOM   2140 C  CG2 . VAL   B 1 79  ? 17.316  -15.528 -34.006  1.00 22.88 ? 172 VAL   B CG2 1 
ATOM   2141 N  N   . VAL   B 1 80  ? 13.289  -13.909 -35.863  1.00 19.78 ? 173 VAL   B N   1 
ATOM   2142 C  CA  . VAL   B 1 80  ? 12.470  -13.125 -36.834  1.00 19.53 ? 173 VAL   B CA  1 
ATOM   2143 C  C   . VAL   B 1 80  ? 13.357  -12.000 -37.378  1.00 19.58 ? 173 VAL   B C   1 
ATOM   2144 O  O   . VAL   B 1 80  ? 13.883  -11.217 -36.569  1.00 18.41 ? 173 VAL   B O   1 
ATOM   2145 C  CB  . VAL   B 1 80  ? 11.170  -12.581 -36.209  1.00 18.72 ? 173 VAL   B CB  1 
ATOM   2146 C  CG1 . VAL   B 1 80  ? 10.364  -11.771 -37.216  1.00 18.49 ? 173 VAL   B CG1 1 
ATOM   2147 C  CG2 . VAL   B 1 80  ? 10.316  -13.691 -35.623  1.00 18.71 ? 173 VAL   B CG2 1 
ATOM   2148 N  N   . ARG   B 1 81  ? 13.540  -11.957 -38.699  1.00 20.42 ? 174 ARG   B N   1 
ATOM   2149 C  CA  . ARG   B 1 81  ? 14.391  -10.960 -39.398  1.00 21.45 ? 174 ARG   B CA  1 
ATOM   2150 C  C   . ARG   B 1 81  ? 13.785  -10.648 -40.768  1.00 20.88 ? 174 ARG   B C   1 
ATOM   2151 O  O   . ARG   B 1 81  ? 12.931  -11.423 -41.240  1.00 20.85 ? 174 ARG   B O   1 
ATOM   2152 C  CB  . ARG   B 1 81  ? 15.820  -11.490 -39.554  1.00 23.27 ? 174 ARG   B CB  1 
ATOM   2153 C  CG  . ARG   B 1 81  ? 15.909  -12.828 -40.276  1.00 25.04 ? 174 ARG   B CG  1 
ATOM   2154 C  CD  . ARG   B 1 81  ? 17.340  -13.255 -40.556  1.00 26.90 ? 174 ARG   B CD  1 
ATOM   2155 N  NE  . ARG   B 1 81  ? 18.052  -13.622 -39.337  1.00 28.23 ? 174 ARG   B NE  1 
ATOM   2156 C  CZ  . ARG   B 1 81  ? 18.910  -12.845 -38.676  1.00 29.50 ? 174 ARG   B CZ  1 
ATOM   2157 N  NH1 . ARG   B 1 81  ? 19.201  -11.627 -39.106  1.00 30.73 ? 174 ARG   B NH1 1 
ATOM   2158 N  NH2 . ARG   B 1 81  ? 19.485  -13.298 -37.576  1.00 29.54 ? 174 ARG   B NH2 1 
ATOM   2159 N  N   . ARG   B 1 82  ? 14.220  -9.550  -41.386  1.00 20.35 ? 175 ARG   B N   1 
ATOM   2160 C  CA  . ARG   B 1 82  ? 13.741  -9.133  -42.726  1.00 20.29 ? 175 ARG   B CA  1 
ATOM   2161 C  C   . ARG   B 1 82  ? 14.264  -10.120 -43.772  1.00 20.62 ? 175 ARG   B C   1 
ATOM   2162 O  O   . ARG   B 1 82  ? 15.353  -10.713 -43.544  1.00 20.52 ? 175 ARG   B O   1 
ATOM   2163 C  CB  . ARG   B 1 82  ? 14.214  -7.719  -43.058  1.00 20.09 ? 175 ARG   B CB  1 
ATOM   2164 C  CG  . ARG   B 1 82  ? 13.678  -6.651  -42.121  1.00 20.27 ? 175 ARG   B CG  1 
ATOM   2165 C  CD  . ARG   B 1 82  ? 14.303  -5.319  -42.461  1.00 20.36 ? 175 ARG   B CD  1 
ATOM   2166 N  NE  . ARG   B 1 82  ? 13.577  -4.638  -43.513  1.00 20.96 ? 175 ARG   B NE  1 
ATOM   2167 C  CZ  . ARG   B 1 82  ? 14.020  -3.578  -44.172  1.00 20.78 ? 175 ARG   B CZ  1 
ATOM   2168 N  NH1 . ARG   B 1 82  ? 15.217  -3.074  -43.916  1.00 21.02 ? 175 ARG   B NH1 1 
ATOM   2169 N  NH2 . ARG   B 1 82  ? 13.254  -3.027  -45.092  1.00 21.05 ? 175 ARG   B NH2 1 
ATOM   2170 N  N   . CYS   B 1 83  ? 13.524  -10.275 -44.873  1.00 20.35 ? 176 CYS   B N   1 
ATOM   2171 C  CA  . CYS   B 1 83  ? 13.928  -11.082 -46.055  1.00 20.19 ? 176 CYS   B CA  1 
ATOM   2172 C  C   . CYS   B 1 83  ? 15.161  -10.442 -46.693  1.00 20.29 ? 176 CYS   B C   1 
ATOM   2173 O  O   . CYS   B 1 83  ? 15.457  -9.275  -46.454  1.00 18.57 ? 176 CYS   B O   1 
ATOM   2174 C  CB  . CYS   B 1 83  ? 12.779  -11.222 -47.049  1.00 19.86 ? 176 CYS   B CB  1 
ATOM   2175 S  SG  . CYS   B 1 83  ? 12.396  -9.738  -47.928  1.00 19.74 ? 176 CYS   B SG  1 
ATOM   2176 N  N   . PRO   B 1 84  ? 15.953  -11.195 -47.490  1.00 21.98 ? 177 PRO   B N   1 
ATOM   2177 C  CA  . PRO   B 1 84  ? 17.098  -10.622 -48.200  1.00 22.50 ? 177 PRO   B CA  1 
ATOM   2178 C  C   . PRO   B 1 84  ? 16.773  -9.341  -48.989  1.00 22.22 ? 177 PRO   B C   1 
ATOM   2179 O  O   . PRO   B 1 84  ? 17.549  -8.402  -48.908  1.00 22.73 ? 177 PRO   B O   1 
ATOM   2180 C  CB  . PRO   B 1 84  ? 17.520  -11.765 -49.132  1.00 22.94 ? 177 PRO   B CB  1 
ATOM   2181 C  CG  . PRO   B 1 84  ? 17.140  -13.008 -48.363  1.00 23.28 ? 177 PRO   B CG  1 
ATOM   2182 C  CD  . PRO   B 1 84  ? 15.825  -12.645 -47.704  1.00 22.92 ? 177 PRO   B CD  1 
ATOM   2183 N  N   . HIS   B 1 85  ? 15.647  -9.315  -49.710  1.00 22.88 ? 178 HIS   B N   1 
ATOM   2184 C  CA  . HIS   B 1 85  ? 15.235  -8.178  -50.581  1.00 22.48 ? 178 HIS   B CA  1 
ATOM   2185 C  C   . HIS   B 1 85  ? 15.081  -6.904  -49.741  1.00 22.64 ? 178 HIS   B C   1 
ATOM   2186 O  O   . HIS   B 1 85  ? 15.640  -5.858  -50.131  1.00 21.82 ? 178 HIS   B O   1 
ATOM   2187 C  CB  . HIS   B 1 85  ? 13.945  -8.502  -51.350  1.00 22.70 ? 178 HIS   B CB  1 
ATOM   2188 C  CG  . HIS   B 1 85  ? 13.273  -7.298  -51.922  1.00 22.67 ? 178 HIS   B CG  1 
ATOM   2189 N  ND1 . HIS   B 1 85  ? 13.726  -6.670  -53.065  1.00 22.85 ? 178 HIS   B ND1 1 
ATOM   2190 C  CD2 . HIS   B 1 85  ? 12.195  -6.597  -51.509  1.00 23.18 ? 178 HIS   B CD2 1 
ATOM   2191 C  CE1 . HIS   B 1 85  ? 12.954  -5.636  -53.332  1.00 23.66 ? 178 HIS   B CE1 1 
ATOM   2192 N  NE2 . HIS   B 1 85  ? 12.005  -5.571  -52.395  1.00 23.21 ? 178 HIS   B NE2 1 
ATOM   2193 N  N   . HIS   B 1 86  ? 14.330  -6.981  -48.643  1.00 22.35 ? 179 HIS   B N   1 
ATOM   2194 C  CA  . HIS   B 1 86  ? 14.028  -5.819  -47.767  1.00 23.15 ? 179 HIS   B CA  1 
ATOM   2195 C  C   . HIS   B 1 86  ? 15.289  -5.390  -47.008  1.00 24.31 ? 179 HIS   B C   1 
ATOM   2196 O  O   . HIS   B 1 86  ? 15.490  -4.173  -46.857  1.00 24.11 ? 179 HIS   B O   1 
ATOM   2197 C  CB  . HIS   B 1 86  ? 12.817  -6.121  -46.875  1.00 21.91 ? 179 HIS   B CB  1 
ATOM   2198 C  CG  . HIS   B 1 86  ? 11.528  -5.843  -47.574  1.00 21.65 ? 179 HIS   B CG  1 
ATOM   2199 N  ND1 . HIS   B 1 86  ? 10.525  -6.784  -47.702  1.00 20.84 ? 179 HIS   B ND1 1 
ATOM   2200 C  CD2 . HIS   B 1 86  ? 11.095  -4.734  -48.212  1.00 20.78 ? 179 HIS   B CD2 1 
ATOM   2201 C  CE1 . HIS   B 1 86  ? 9.523   -6.257  -48.376  1.00 21.17 ? 179 HIS   B CE1 1 
ATOM   2202 N  NE2 . HIS   B 1 86  ? 9.848   -5.001  -48.700  1.00 21.15 ? 179 HIS   B NE2 1 
ATOM   2203 N  N   . GLU   B 1 87  ? 16.116  -6.346  -46.577  1.00 26.72 ? 180 GLU   B N   1 
ATOM   2204 C  CA  . GLU   B 1 87  ? 17.429  -6.075  -45.929  1.00 28.58 ? 180 GLU   B CA  1 
ATOM   2205 C  C   . GLU   B 1 87  ? 18.268  -5.178  -46.849  1.00 31.08 ? 180 GLU   B C   1 
ATOM   2206 O  O   . GLU   B 1 87  ? 18.991  -4.311  -46.319  1.00 32.26 ? 180 GLU   B O   1 
ATOM   2207 C  CB  . GLU   B 1 87  ? 18.155  -7.384  -45.616  1.00 29.16 ? 180 GLU   B CB  1 
ATOM   2208 C  CG  . GLU   B 1 87  ? 19.461  -7.187  -44.869  1.00 30.40 ? 180 GLU   B CG  1 
ATOM   2209 C  CD  . GLU   B 1 87  ? 20.236  -8.459  -44.570  1.00 30.96 ? 180 GLU   B CD  1 
ATOM   2210 O  OE1 . GLU   B 1 87  ? 19.619  -9.544  -44.534  1.00 30.76 ? 180 GLU   B OE1 1 
ATOM   2211 O  OE2 . GLU   B 1 87  ? 21.461  -8.357  -44.367  1.00 32.74 ? 180 GLU   B OE2 1 
ATOM   2212 N  N   . ARG   B 1 88  ? 18.153  -5.367  -48.169  1.00 32.86 ? 181 ARG   B N   1 
ATOM   2213 C  CA  . ARG   B 1 88  ? 18.987  -4.689  -49.199  1.00 33.91 ? 181 ARG   B CA  1 
ATOM   2214 C  C   . ARG   B 1 88  ? 18.298  -3.420  -49.720  1.00 32.56 ? 181 ARG   B C   1 
ATOM   2215 O  O   . ARG   B 1 88  ? 18.964  -2.665  -50.446  1.00 31.61 ? 181 ARG   B O   1 
ATOM   2216 C  CB  . ARG   B 1 88  ? 19.296  -5.658  -50.346  1.00 37.29 ? 181 ARG   B CB  1 
ATOM   2217 C  CG  . ARG   B 1 88  ? 20.242  -6.790  -49.965  1.00 39.90 ? 181 ARG   B CG  1 
ATOM   2218 C  CD  . ARG   B 1 88  ? 20.763  -7.534  -51.182  1.00 42.71 ? 181 ARG   B CD  1 
ATOM   2219 N  NE  . ARG   B 1 88  ? 19.717  -8.273  -51.887  1.00 45.33 ? 181 ARG   B NE  1 
ATOM   2220 C  CZ  . ARG   B 1 88  ? 19.576  -9.601  -51.897  1.00 46.11 ? 181 ARG   B CZ  1 
ATOM   2221 N  NH1 . ARG   B 1 88  ? 20.421  -10.382 -51.243  1.00 46.71 ? 181 ARG   B NH1 1 
ATOM   2222 N  NH2 . ARG   B 1 88  ? 18.583  -10.149 -52.576  1.00 46.70 ? 181 ARG   B NH2 1 
ATOM   2223 N  N   . CYS   B 1 89  ? 17.027  -3.178  -49.374  1.00 32.02 ? 182 CYS   B N   1 
ATOM   2224 C  CA  . CYS   B 1 89  ? 16.293  -1.927  -49.724  1.00 32.65 ? 182 CYS   B CA  1 
ATOM   2225 C  C   . CYS   B 1 89  ? 17.021  -0.726  -49.105  1.00 33.28 ? 182 CYS   B C   1 
ATOM   2226 O  O   . CYS   B 1 89  ? 17.525  -0.862  -47.976  1.00 32.64 ? 182 CYS   B O   1 
ATOM   2227 C  CB  . CYS   B 1 89  ? 14.838  -1.967  -49.261  1.00 32.56 ? 182 CYS   B CB  1 
ATOM   2228 S  SG  . CYS   B 1 89  ? 13.741  -2.886  -50.375  1.00 33.21 ? 182 CYS   B SG  1 
ATOM   2229 N  N   . SER   B 1 90  ? 17.097  0.401   -49.822  1.00 34.07 ? 183 SER   B N   1 
ATOM   2230 C  CA  . SER   B 1 90  ? 17.778  1.644   -49.364  1.00 35.07 ? 183 SER   B CA  1 
ATOM   2231 C  C   . SER   B 1 90  ? 16.793  2.488   -48.546  1.00 33.47 ? 183 SER   B C   1 
ATOM   2232 O  O   . SER   B 1 90  ? 16.466  3.606   -48.978  1.00 34.77 ? 183 SER   B O   1 
ATOM   2233 C  CB  . SER   B 1 90  ? 18.360  2.420   -50.527  1.00 36.57 ? 183 SER   B CB  1 
ATOM   2234 O  OG  . SER   B 1 90  ? 17.338  2.827   -51.427  1.00 38.74 ? 183 SER   B OG  1 
ATOM   2235 N  N   . ASP   B 1 91  ? 16.338  1.954   -47.409  1.00 31.47 ? 184 ASP   B N   1 
ATOM   2236 C  CA  . ASP   B 1 91  ? 15.275  2.550   -46.555  1.00 30.86 ? 184 ASP   B CA  1 
ATOM   2237 C  C   . ASP   B 1 91  ? 15.842  2.849   -45.161  1.00 30.07 ? 184 ASP   B C   1 
ATOM   2238 O  O   . ASP   B 1 91  ? 15.038  3.026   -44.228  1.00 29.63 ? 184 ASP   B O   1 
ATOM   2239 C  CB  . ASP   B 1 91  ? 14.052  1.627   -46.493  1.00 30.16 ? 184 ASP   B CB  1 
ATOM   2240 C  CG  . ASP   B 1 91  ? 14.328  0.255   -45.899  1.00 29.92 ? 184 ASP   B CG  1 
ATOM   2241 O  OD1 . ASP   B 1 91  ? 15.457  0.035   -45.407  1.00 29.33 ? 184 ASP   B OD1 1 
ATOM   2242 O  OD2 . ASP   B 1 91  ? 13.409  -0.587  -45.929  1.00 28.59 ? 184 ASP   B OD2 1 
ATOM   2243 N  N   . SER   B 1 92  ? 17.172  2.904   -45.028  1.00 29.56 ? 185 SER   B N   1 
ATOM   2244 C  CA  . SER   B 1 92  ? 17.881  3.112   -43.736  1.00 30.15 ? 185 SER   B CA  1 
ATOM   2245 C  C   . SER   B 1 92  ? 17.531  4.492   -43.166  1.00 29.73 ? 185 SER   B C   1 
ATOM   2246 O  O   . SER   B 1 92  ? 17.415  5.445   -43.953  1.00 30.45 ? 185 SER   B O   1 
ATOM   2247 C  CB  . SER   B 1 92  ? 19.372  2.952   -43.888  1.00 29.90 ? 185 SER   B CB  1 
ATOM   2248 O  OG  . SER   B 1 92  ? 20.028  3.147   -42.641  1.00 29.64 ? 185 SER   B OG  1 
ATOM   2249 N  N   . ASP   B 1 93  ? 17.364  4.574   -41.843  1.00 30.12 ? 186 ASP   B N   1 
ATOM   2250 C  CA  . ASP   B 1 93  ? 17.129  5.832   -41.084  1.00 28.59 ? 186 ASP   B CA  1 
ATOM   2251 C  C   . ASP   B 1 93  ? 18.411  6.217   -40.335  1.00 28.87 ? 186 ASP   B C   1 
ATOM   2252 O  O   . ASP   B 1 93  ? 18.357  7.168   -39.529  1.00 31.02 ? 186 ASP   B O   1 
ATOM   2253 C  CB  . ASP   B 1 93  ? 15.927  5.688   -40.145  1.00 28.33 ? 186 ASP   B CB  1 
ATOM   2254 C  CG  . ASP   B 1 93  ? 16.107  4.725   -38.979  1.00 28.09 ? 186 ASP   B CG  1 
ATOM   2255 O  OD1 . ASP   B 1 93  ? 17.137  4.016   -38.929  1.00 26.33 ? 186 ASP   B OD1 1 
ATOM   2256 O  OD2 . ASP   B 1 93  ? 15.200  4.682   -38.127  1.00 28.86 ? 186 ASP   B OD2 1 
ATOM   2257 N  N   . GLY   B 1 94  ? 19.510  5.492   -40.577  1.00 28.32 ? 187 GLY   B N   1 
ATOM   2258 C  CA  . GLY   B 1 94  ? 20.829  5.716   -39.952  1.00 27.89 ? 187 GLY   B CA  1 
ATOM   2259 C  C   . GLY   B 1 94  ? 20.960  5.057   -38.585  1.00 27.30 ? 187 GLY   B C   1 
ATOM   2260 O  O   . GLY   B 1 94  ? 22.099  4.956   -38.096  1.00 27.68 ? 187 GLY   B O   1 
ATOM   2261 N  N   . LEU   B 1 95  ? 19.855  4.601   -37.985  1.00 25.74 ? 188 LEU   B N   1 
ATOM   2262 C  CA  . LEU   B 1 95  ? 19.829  4.092   -36.585  1.00 25.31 ? 188 LEU   B CA  1 
ATOM   2263 C  C   . LEU   B 1 95  ? 19.561  2.586   -36.574  1.00 24.21 ? 188 LEU   B C   1 
ATOM   2264 O  O   . LEU   B 1 95  ? 20.332  1.858   -35.923  1.00 24.60 ? 188 LEU   B O   1 
ATOM   2265 C  CB  . LEU   B 1 95  ? 18.749  4.837   -35.800  1.00 25.13 ? 188 LEU   B CB  1 
ATOM   2266 C  CG  . LEU   B 1 95  ? 18.860  6.358   -35.816  1.00 25.82 ? 188 LEU   B CG  1 
ATOM   2267 C  CD1 . LEU   B 1 95  ? 17.631  6.988   -35.178  1.00 25.86 ? 188 LEU   B CD1 1 
ATOM   2268 C  CD2 . LEU   B 1 95  ? 20.133  6.813   -35.117  1.00 25.91 ? 188 LEU   B CD2 1 
ATOM   2269 N  N   . ALA   B 1 96  ? 18.488  2.149   -37.237  1.00 23.46 ? 189 ALA   B N   1 
ATOM   2270 C  CA  . ALA   B 1 96  ? 18.025  0.743   -37.257  1.00 22.96 ? 189 ALA   B CA  1 
ATOM   2271 C  C   . ALA   B 1 96  ? 19.013  -0.107  -38.053  1.00 22.26 ? 189 ALA   B C   1 
ATOM   2272 O  O   . ALA   B 1 96  ? 19.433  0.281   -39.142  1.00 22.27 ? 189 ALA   B O   1 
ATOM   2273 C  CB  . ALA   B 1 96  ? 16.634  0.658   -37.840  1.00 23.12 ? 189 ALA   B CB  1 
ATOM   2274 N  N   . PRO   B 1 97  ? 19.430  -1.283  -37.533  1.00 21.58 ? 190 PRO   B N   1 
ATOM   2275 C  CA  . PRO   B 1 97  ? 20.152  -2.257  -38.347  1.00 21.46 ? 190 PRO   B CA  1 
ATOM   2276 C  C   . PRO   B 1 97  ? 19.265  -2.734  -39.494  1.00 21.07 ? 190 PRO   B C   1 
ATOM   2277 O  O   . PRO   B 1 97  ? 18.071  -2.967  -39.299  1.00 20.25 ? 190 PRO   B O   1 
ATOM   2278 C  CB  . PRO   B 1 97  ? 20.476  -3.417  -37.392  1.00 21.42 ? 190 PRO   B CB  1 
ATOM   2279 C  CG  . PRO   B 1 97  ? 20.269  -2.847  -36.001  1.00 21.64 ? 190 PRO   B CG  1 
ATOM   2280 C  CD  . PRO   B 1 97  ? 19.250  -1.736  -36.146  1.00 21.83 ? 190 PRO   B CD  1 
ATOM   2281 N  N   . PRO   B 1 98  ? 19.815  -2.904  -40.719  1.00 20.67 ? 191 PRO   B N   1 
ATOM   2282 C  CA  . PRO   B 1 98  ? 19.004  -3.280  -41.880  1.00 20.42 ? 191 PRO   B CA  1 
ATOM   2283 C  C   . PRO   B 1 98  ? 18.251  -4.618  -41.759  1.00 19.81 ? 191 PRO   B C   1 
ATOM   2284 O  O   . PRO   B 1 98  ? 17.288  -4.803  -42.470  1.00 19.54 ? 191 PRO   B O   1 
ATOM   2285 C  CB  . PRO   B 1 98  ? 20.013  -3.325  -43.044  1.00 20.77 ? 191 PRO   B CB  1 
ATOM   2286 C  CG  . PRO   B 1 98  ? 21.371  -3.421  -42.389  1.00 21.13 ? 191 PRO   B CG  1 
ATOM   2287 C  CD  . PRO   B 1 98  ? 21.232  -2.709  -41.060  1.00 20.98 ? 191 PRO   B CD  1 
ATOM   2288 N  N   A GLN   B 1 99  ? 18.702  -5.506  -40.868  0.50 20.18 ? 192 GLN   B N   1 
ATOM   2289 N  N   B GLN   B 1 99  ? 18.699  -5.506  -40.865  0.50 19.10 ? 192 GLN   B N   1 
ATOM   2290 C  CA  A GLN   B 1 99  ? 18.116  -6.858  -40.648  0.50 20.47 ? 192 GLN   B CA  1 
ATOM   2291 C  CA  B GLN   B 1 99  ? 18.112  -6.858  -40.650  0.50 18.72 ? 192 GLN   B CA  1 
ATOM   2292 C  C   A GLN   B 1 99  ? 16.853  -6.777  -39.779  0.50 19.37 ? 192 GLN   B C   1 
ATOM   2293 C  C   B GLN   B 1 99  ? 16.853  -6.779  -39.775  0.50 18.39 ? 192 GLN   B C   1 
ATOM   2294 O  O   A GLN   B 1 99  ? 16.038  -7.714  -39.853  0.50 18.80 ? 192 GLN   B O   1 
ATOM   2295 O  O   B GLN   B 1 99  ? 16.041  -7.720  -39.843  0.50 17.91 ? 192 GLN   B O   1 
ATOM   2296 C  CB  A GLN   B 1 99  ? 19.129  -7.777  -39.966  0.50 21.74 ? 192 GLN   B CB  1 
ATOM   2297 C  CB  B GLN   B 1 99  ? 19.123  -7.787  -39.977  0.50 18.57 ? 192 GLN   B CB  1 
ATOM   2298 C  CG  A GLN   B 1 99  ? 20.273  -8.219  -40.865  0.50 23.03 ? 192 GLN   B CG  1 
ATOM   2299 C  CG  B GLN   B 1 99  ? 20.406  -7.977  -40.771  0.50 18.50 ? 192 GLN   B CG  1 
ATOM   2300 C  CD  A GLN   B 1 99  ? 21.147  -9.242  -40.182  0.50 24.07 ? 192 GLN   B CD  1 
ATOM   2301 C  CD  B GLN   B 1 99  ? 21.361  -6.821  -40.607  0.50 18.06 ? 192 GLN   B CD  1 
ATOM   2302 O  OE1 A GLN   B 1 99  ? 21.153  -9.364  -38.957  0.50 25.25 ? 192 GLN   B OE1 1 
ATOM   2303 O  OE1 B GLN   B 1 99  ? 21.216  -5.987  -39.715  0.50 16.61 ? 192 GLN   B OE1 1 
ATOM   2304 N  NE2 A GLN   B 1 99  ? 21.893  -9.994  -40.975  0.50 25.28 ? 192 GLN   B NE2 1 
ATOM   2305 N  NE2 B GLN   B 1 99  ? 22.354  -6.767  -41.480  0.50 18.25 ? 192 GLN   B NE2 1 
ATOM   2306 N  N   . HIS   B 1 100 ? 16.709  -5.719  -38.971  1.00 18.49 ? 193 HIS   B N   1 
ATOM   2307 C  CA  . HIS   B 1 100 ? 15.629  -5.592  -37.951  1.00 17.34 ? 193 HIS   B CA  1 
ATOM   2308 C  C   . HIS   B 1 100 ? 14.257  -5.383  -38.604  1.00 16.89 ? 193 HIS   B C   1 
ATOM   2309 O  O   . HIS   B 1 100 ? 14.103  -4.420  -39.372  1.00 17.84 ? 193 HIS   B O   1 
ATOM   2310 C  CB  . HIS   B 1 100 ? 15.951  -4.480  -36.950  1.00 16.88 ? 193 HIS   B CB  1 
ATOM   2311 C  CG  . HIS   B 1 100 ? 16.926  -4.904  -35.905  1.00 16.51 ? 193 HIS   B CG  1 
ATOM   2312 N  ND1 . HIS   B 1 100 ? 16.784  -4.549  -34.581  1.00 15.97 ? 193 HIS   B ND1 1 
ATOM   2313 C  CD2 . HIS   B 1 100 ? 18.042  -5.663  -35.982  1.00 16.17 ? 193 HIS   B CD2 1 
ATOM   2314 C  CE1 . HIS   B 1 100 ? 17.788  -5.050  -33.885  1.00 16.13 ? 193 HIS   B CE1 1 
ATOM   2315 N  NE2 . HIS   B 1 100 ? 18.569  -5.751  -34.721  1.00 15.88 ? 193 HIS   B NE2 1 
ATOM   2316 N  N   . LEU   B 1 101 ? 13.290  -6.238  -38.260  1.00 16.60 ? 194 LEU   B N   1 
ATOM   2317 C  CA  . LEU   B 1 101 ? 11.873  -6.129  -38.703  1.00 15.85 ? 194 LEU   B CA  1 
ATOM   2318 C  C   . LEU   B 1 101 ? 11.228  -4.887  -38.075  1.00 15.71 ? 194 LEU   B C   1 
ATOM   2319 O  O   . LEU   B 1 101 ? 10.614  -4.101  -38.828  1.00 15.06 ? 194 LEU   B O   1 
ATOM   2320 C  CB  . LEU   B 1 101 ? 11.109  -7.397  -38.316  1.00 15.59 ? 194 LEU   B CB  1 
ATOM   2321 C  CG  . LEU   B 1 101 ? 9.616   -7.376  -38.641  1.00 15.59 ? 194 LEU   B CG  1 
ATOM   2322 C  CD1 . LEU   B 1 101 ? 9.388   -7.373  -40.143  1.00 15.72 ? 194 LEU   B CD1 1 
ATOM   2323 C  CD2 . LEU   B 1 101 ? 8.900   -8.547  -37.998  1.00 15.47 ? 194 LEU   B CD2 1 
ATOM   2324 N  N   . ILE   B 1 102 ? 11.363  -4.715  -36.755  1.00 15.48 ? 195 ILE   B N   1 
ATOM   2325 C  CA  . ILE   B 1 102 ? 10.647  -3.654  -35.987  1.00 15.34 ? 195 ILE   B CA  1 
ATOM   2326 C  C   . ILE   B 1 102 ? 11.576  -2.452  -35.784  1.00 15.13 ? 195 ILE   B C   1 
ATOM   2327 O  O   . ILE   B 1 102 ? 12.670  -2.628  -35.222  1.00 15.61 ? 195 ILE   B O   1 
ATOM   2328 C  CB  . ILE   B 1 102 ? 10.099  -4.182  -34.646  1.00 15.09 ? 195 ILE   B CB  1 
ATOM   2329 C  CG1 . ILE   B 1 102 ? 9.282   -5.465  -34.825  1.00 15.34 ? 195 ILE   B CG1 1 
ATOM   2330 C  CG2 . ILE   B 1 102 ? 9.287   -3.096  -33.954  1.00 14.98 ? 195 ILE   B CG2 1 
ATOM   2331 C  CD1 . ILE   B 1 102 ? 8.778   -6.069  -33.540  1.00 15.48 ? 195 ILE   B CD1 1 
ATOM   2332 N  N   . ARG   B 1 103 ? 11.119  -1.272  -36.197  1.00 15.45 ? 196 ARG   B N   1 
ATOM   2333 C  CA  . ARG   B 1 103 ? 11.754  0.034   -35.889  1.00 15.94 ? 196 ARG   B CA  1 
ATOM   2334 C  C   . ARG   B 1 103 ? 10.795  0.878   -35.042  1.00 16.55 ? 196 ARG   B C   1 
ATOM   2335 O  O   . ARG   B 1 103 ? 9.587   0.543   -34.980  1.00 16.39 ? 196 ARG   B O   1 
ATOM   2336 C  CB  . ARG   B 1 103 ? 12.107  0.785   -37.175  1.00 16.16 ? 196 ARG   B CB  1 
ATOM   2337 C  CG  . ARG   B 1 103 ? 13.067  0.037   -38.086  1.00 16.73 ? 196 ARG   B CG  1 
ATOM   2338 C  CD  . ARG   B 1 103 ? 13.380  0.848   -39.322  1.00 16.61 ? 196 ARG   B CD  1 
ATOM   2339 N  NE  . ARG   B 1 103 ? 14.203  0.115   -40.271  1.00 17.34 ? 196 ARG   B NE  1 
ATOM   2340 C  CZ  . ARG   B 1 103 ? 14.542  0.572   -41.475  1.00 17.35 ? 196 ARG   B CZ  1 
ATOM   2341 N  NH1 . ARG   B 1 103 ? 14.142  1.775   -41.862  1.00 17.25 ? 196 ARG   B NH1 1 
ATOM   2342 N  NH2 . ARG   B 1 103 ? 15.292  -0.164  -42.277  1.00 16.99 ? 196 ARG   B NH2 1 
ATOM   2343 N  N   . VAL   B 1 104 ? 11.328  1.924   -34.405  1.00 16.63 ? 197 VAL   B N   1 
ATOM   2344 C  CA  . VAL   B 1 104 ? 10.541  3.046   -33.816  1.00 16.99 ? 197 VAL   B CA  1 
ATOM   2345 C  C   . VAL   B 1 104 ? 10.836  4.292   -34.652  1.00 17.88 ? 197 VAL   B C   1 
ATOM   2346 O  O   . VAL   B 1 104 ? 12.016  4.542   -34.925  1.00 17.15 ? 197 VAL   B O   1 
ATOM   2347 C  CB  . VAL   B 1 104 ? 10.862  3.272   -32.326  1.00 16.35 ? 197 VAL   B CB  1 
ATOM   2348 C  CG1 . VAL   B 1 104 ? 10.175  4.526   -31.788  1.00 16.52 ? 197 VAL   B CG1 1 
ATOM   2349 C  CG2 . VAL   B 1 104 ? 10.495  2.060   -31.486  1.00 15.97 ? 197 VAL   B CG2 1 
ATOM   2350 N  N   . GLU   B 1 105 ? 9.790   5.010   -35.069  1.00 20.23 ? 198 GLU   B N   1 
ATOM   2351 C  CA  . GLU   B 1 105 ? 9.898   6.269   -35.851  1.00 21.53 ? 198 GLU   B CA  1 
ATOM   2352 C  C   . GLU   B 1 105 ? 9.721   7.450   -34.888  1.00 22.02 ? 198 GLU   B C   1 
ATOM   2353 O  O   . GLU   B 1 105 ? 9.023   7.280   -33.871  1.00 22.18 ? 198 GLU   B O   1 
ATOM   2354 C  CB  . GLU   B 1 105 ? 8.895   6.249   -37.011  1.00 23.23 ? 198 GLU   B CB  1 
ATOM   2355 C  CG  . GLU   B 1 105 ? 7.624   7.040   -36.781  1.00 24.23 ? 198 GLU   B CG  1 
ATOM   2356 C  CD  . GLU   B 1 105 ? 6.640   7.004   -37.939  1.00 25.14 ? 198 GLU   B CD  1 
ATOM   2357 O  OE1 . GLU   B 1 105 ? 6.529   8.021   -38.653  1.00 27.23 ? 198 GLU   B OE1 1 
ATOM   2358 O  OE2 . GLU   B 1 105 ? 5.977   5.967   -38.119  1.00 25.23 ? 198 GLU   B OE2 1 
ATOM   2359 N  N   . GLY   B 1 106 ? 10.377  8.578   -35.181  1.00 22.36 ? 199 GLY   B N   1 
ATOM   2360 C  CA  . GLY   B 1 106 ? 10.206  9.863   -34.476  1.00 22.40 ? 199 GLY   B CA  1 
ATOM   2361 C  C   . GLY   B 1 106 ? 10.768  9.850   -33.061  1.00 22.44 ? 199 GLY   B C   1 
ATOM   2362 O  O   . GLY   B 1 106 ? 10.224  10.579  -32.219  1.00 22.27 ? 199 GLY   B O   1 
ATOM   2363 N  N   . ASN   B 1 107 ? 11.829  9.080   -32.799  1.00 22.26 ? 200 ASN   B N   1 
ATOM   2364 C  CA  . ASN   B 1 107 ? 12.462  9.009   -31.453  1.00 22.60 ? 200 ASN   B CA  1 
ATOM   2365 C  C   . ASN   B 1 107 ? 13.979  8.845   -31.604  1.00 22.81 ? 200 ASN   B C   1 
ATOM   2366 O  O   . ASN   B 1 107 ? 14.442  7.712   -31.873  1.00 21.46 ? 200 ASN   B O   1 
ATOM   2367 C  CB  . ASN   B 1 107 ? 11.828  7.908   -30.598  1.00 22.58 ? 200 ASN   B CB  1 
ATOM   2368 C  CG  . ASN   B 1 107 ? 12.162  8.038   -29.127  1.00 22.46 ? 200 ASN   B CG  1 
ATOM   2369 O  OD1 . ASN   B 1 107 ? 13.244  8.500   -28.764  1.00 21.90 ? 200 ASN   B OD1 1 
ATOM   2370 N  ND2 . ASN   B 1 107 ? 11.246  7.616   -28.273  1.00 22.03 ? 200 ASN   B ND2 1 
ATOM   2371 N  N   . LEU   B 1 108 ? 14.724  9.932   -31.386  1.00 23.45 ? 201 LEU   B N   1 
ATOM   2372 C  CA  . LEU   B 1 108 ? 16.203  9.978   -31.548  1.00 24.63 ? 201 LEU   B CA  1 
ATOM   2373 C  C   . LEU   B 1 108 ? 16.911  9.259   -30.394  1.00 23.15 ? 201 LEU   B C   1 
ATOM   2374 O  O   . LEU   B 1 108 ? 18.148  9.162   -30.462  1.00 24.39 ? 201 LEU   B O   1 
ATOM   2375 C  CB  . LEU   B 1 108 ? 16.666  11.437  -31.643  1.00 25.90 ? 201 LEU   B CB  1 
ATOM   2376 C  CG  . LEU   B 1 108 ? 16.557  12.076  -33.027  1.00 27.82 ? 201 LEU   B CG  1 
ATOM   2377 C  CD1 . LEU   B 1 108 ? 17.239  13.436  -33.040  1.00 29.04 ? 201 LEU   B CD1 1 
ATOM   2378 C  CD2 . LEU   B 1 108 ? 17.157  11.174  -34.099  1.00 28.39 ? 201 LEU   B CD2 1 
ATOM   2379 N  N   . ARG   B 1 109 ? 16.173  8.785   -29.384  1.00 22.17 ? 202 ARG   B N   1 
ATOM   2380 C  CA  . ARG   B 1 109 ? 16.729  8.049   -28.215  1.00 21.84 ? 202 ARG   B CA  1 
ATOM   2381 C  C   . ARG   B 1 109 ? 16.548  6.537   -28.422  1.00 20.17 ? 202 ARG   B C   1 
ATOM   2382 O  O   . ARG   B 1 109 ? 16.877  5.765   -27.498  1.00 20.01 ? 202 ARG   B O   1 
ATOM   2383 C  CB  . ARG   B 1 109 ? 16.075  8.556   -26.926  1.00 22.59 ? 202 ARG   B CB  1 
ATOM   2384 C  CG  . ARG   B 1 109 ? 16.257  10.053  -26.700  1.00 24.36 ? 202 ARG   B CG  1 
ATOM   2385 C  CD  . ARG   B 1 109 ? 15.540  10.577  -25.472  1.00 24.92 ? 202 ARG   B CD  1 
ATOM   2386 N  NE  . ARG   B 1 109 ? 16.158  10.124  -24.231  1.00 26.25 ? 202 ARG   B NE  1 
ATOM   2387 C  CZ  . ARG   B 1 109 ? 15.592  10.184  -23.025  1.00 27.68 ? 202 ARG   B CZ  1 
ATOM   2388 N  NH1 . ARG   B 1 109 ? 14.377  10.681  -22.871  1.00 28.55 ? 202 ARG   B NH1 1 
ATOM   2389 N  NH2 . ARG   B 1 109 ? 16.248  9.737   -21.968  1.00 29.13 ? 202 ARG   B NH2 1 
ATOM   2390 N  N   . VAL   B 1 110 ? 16.068  6.124   -29.597  1.00 18.34 ? 203 VAL   B N   1 
ATOM   2391 C  CA  . VAL   B 1 110 ? 15.840  4.691   -29.942  1.00 17.26 ? 203 VAL   B CA  1 
ATOM   2392 C  C   . VAL   B 1 110 ? 17.177  3.949   -29.851  1.00 16.91 ? 203 VAL   B C   1 
ATOM   2393 O  O   . VAL   B 1 110 ? 18.219  4.525   -30.236  1.00 16.33 ? 203 VAL   B O   1 
ATOM   2394 C  CB  . VAL   B 1 110 ? 15.175  4.513   -31.323  1.00 17.43 ? 203 VAL   B CB  1 
ATOM   2395 C  CG1 . VAL   B 1 110 ? 16.072  4.955   -32.470  1.00 17.68 ? 203 VAL   B CG1 1 
ATOM   2396 C  CG2 . VAL   B 1 110 ? 14.719  3.077   -31.538  1.00 17.03 ? 203 VAL   B CG2 1 
ATOM   2397 N  N   . GLU   B 1 111 ? 17.128  2.714   -29.345  1.00 16.47 ? 204 GLU   B N   1 
ATOM   2398 C  CA  . GLU   B 1 111 ? 18.294  1.814   -29.167  1.00 15.73 ? 204 GLU   B CA  1 
ATOM   2399 C  C   . GLU   B 1 111 ? 17.928  0.447   -29.747  1.00 15.48 ? 204 GLU   B C   1 
ATOM   2400 O  O   . GLU   B 1 111 ? 16.791  -0.016  -29.506  1.00 15.13 ? 204 GLU   B O   1 
ATOM   2401 C  CB  . GLU   B 1 111 ? 18.652  1.737   -27.682  1.00 15.84 ? 204 GLU   B CB  1 
ATOM   2402 C  CG  . GLU   B 1 111 ? 19.740  0.737   -27.348  1.00 15.80 ? 204 GLU   B CG  1 
ATOM   2403 C  CD  . GLU   B 1 111 ? 19.949  0.575   -25.851  1.00 15.80 ? 204 GLU   B CD  1 
ATOM   2404 O  OE1 . GLU   B 1 111 ? 20.035  1.616   -25.150  1.00 15.84 ? 204 GLU   B OE1 1 
ATOM   2405 O  OE2 . GLU   B 1 111 ? 19.996  -0.587  -25.383  1.00 14.86 ? 204 GLU   B OE2 1 
ATOM   2406 N  N   . TYR   B 1 112 ? 18.851  -0.165  -30.492  1.00 15.30 ? 205 TYR   B N   1 
ATOM   2407 C  CA  . TYR   B 1 112 ? 18.650  -1.463  -31.183  1.00 15.40 ? 205 TYR   B CA  1 
ATOM   2408 C  C   . TYR   B 1 112 ? 19.637  -2.477  -30.607  1.00 15.97 ? 205 TYR   B C   1 
ATOM   2409 O  O   . TYR   B 1 112 ? 20.812  -2.118  -30.411  1.00 16.24 ? 205 TYR   B O   1 
ATOM   2410 C  CB  . TYR   B 1 112 ? 18.782  -1.284  -32.697  1.00 15.46 ? 205 TYR   B CB  1 
ATOM   2411 C  CG  . TYR   B 1 112 ? 17.643  -0.529  -33.331  1.00 15.30 ? 205 TYR   B CG  1 
ATOM   2412 C  CD1 . TYR   B 1 112 ? 16.491  -1.181  -33.734  1.00 15.32 ? 205 TYR   B CD1 1 
ATOM   2413 C  CD2 . TYR   B 1 112 ? 17.709  0.843   -33.522  1.00 15.72 ? 205 TYR   B CD2 1 
ATOM   2414 C  CE1 . TYR   B 1 112 ? 15.437  -0.496  -34.320  1.00 15.31 ? 205 TYR   B CE1 1 
ATOM   2415 C  CE2 . TYR   B 1 112 ? 16.659  1.547   -34.093  1.00 15.41 ? 205 TYR   B CE2 1 
ATOM   2416 C  CZ  . TYR   B 1 112 ? 15.516  0.875   -34.493  1.00 15.66 ? 205 TYR   B CZ  1 
ATOM   2417 O  OH  . TYR   B 1 112 ? 14.471  1.557   -35.051  1.00 15.00 ? 205 TYR   B OH  1 
ATOM   2418 N  N   . LEU   B 1 113 ? 19.155  -3.691  -30.331  1.00 16.37 ? 206 LEU   B N   1 
ATOM   2419 C  CA  . LEU   B 1 113 ? 19.951  -4.799  -29.747  1.00 16.80 ? 206 LEU   B CA  1 
ATOM   2420 C  C   . LEU   B 1 113 ? 19.955  -5.998  -30.701  1.00 17.55 ? 206 LEU   B C   1 
ATOM   2421 O  O   . LEU   B 1 113 ? 18.868  -6.425  -31.135  1.00 16.96 ? 206 LEU   B O   1 
ATOM   2422 C  CB  . LEU   B 1 113 ? 19.355  -5.187  -28.390  1.00 16.48 ? 206 LEU   B CB  1 
ATOM   2423 C  CG  . LEU   B 1 113 ? 20.065  -6.324  -27.657  1.00 16.43 ? 206 LEU   B CG  1 
ATOM   2424 C  CD1 . LEU   B 1 113 ? 21.528  -5.990  -27.413  1.00 16.92 ? 206 LEU   B CD1 1 
ATOM   2425 C  CD2 . LEU   B 1 113 ? 19.365  -6.630  -26.342  1.00 16.60 ? 206 LEU   B CD2 1 
ATOM   2426 N  N   . ASP   B 1 114 ? 21.151  -6.496  -31.018  1.00 18.21 ? 207 ASP   B N   1 
ATOM   2427 C  CA  . ASP   B 1 114 ? 21.391  -7.905  -31.426  1.00 19.64 ? 207 ASP   B CA  1 
ATOM   2428 C  C   . ASP   B 1 114 ? 21.862  -8.629  -30.162  1.00 19.60 ? 207 ASP   B C   1 
ATOM   2429 O  O   . ASP   B 1 114 ? 22.987  -8.344  -29.724  1.00 19.61 ? 207 ASP   B O   1 
ATOM   2430 C  CB  . ASP   B 1 114 ? 22.453  -8.017  -32.525  1.00 19.65 ? 207 ASP   B CB  1 
ATOM   2431 C  CG  . ASP   B 1 114 ? 22.052  -7.499  -33.897  1.00 20.46 ? 207 ASP   B CG  1 
ATOM   2432 O  OD1 . ASP   B 1 114 ? 20.860  -7.179  -34.098  1.00 20.07 ? 207 ASP   B OD1 1 
ATOM   2433 O  OD2 . ASP   B 1 114 ? 22.947  -7.429  -34.763  1.00 20.13 ? 207 ASP   B OD2 1 
ATOM   2434 N  N   . ASP   B 1 115 ? 21.019  -9.462  -29.550  1.00 20.95 ? 208 ASP   B N   1 
ATOM   2435 C  CA  . ASP   B 1 115 ? 21.393  -10.197 -28.312  1.00 22.31 ? 208 ASP   B CA  1 
ATOM   2436 C  C   . ASP   B 1 115 ? 22.650  -11.024 -28.610  1.00 22.67 ? 208 ASP   B C   1 
ATOM   2437 O  O   . ASP   B 1 115 ? 22.631  -11.775 -29.591  1.00 22.04 ? 208 ASP   B O   1 
ATOM   2438 C  CB  . ASP   B 1 115 ? 20.252  -11.078 -27.805  1.00 22.42 ? 208 ASP   B CB  1 
ATOM   2439 C  CG  . ASP   B 1 115 ? 20.480  -11.570 -26.384  1.00 23.04 ? 208 ASP   B CG  1 
ATOM   2440 O  OD1 . ASP   B 1 115 ? 21.262  -12.525 -26.215  1.00 22.74 ? 208 ASP   B OD1 1 
ATOM   2441 O  OD2 . ASP   B 1 115 ? 19.901  -10.971 -25.460  1.00 22.78 ? 208 ASP   B OD2 1 
ATOM   2442 N  N   . ARG   B 1 116 ? 23.709  -10.883 -27.808  1.00 24.84 ? 209 ARG   B N   1 
ATOM   2443 C  CA  . ARG   B 1 116 ? 25.019  -11.536 -28.089  1.00 26.83 ? 209 ARG   B CA  1 
ATOM   2444 C  C   . ARG   B 1 116 ? 24.883  -13.061 -27.962  1.00 26.80 ? 209 ARG   B C   1 
ATOM   2445 O  O   . ARG   B 1 116 ? 25.696  -13.768 -28.590  1.00 27.14 ? 209 ARG   B O   1 
ATOM   2446 C  CB  . ARG   B 1 116 ? 26.126  -10.984 -27.183  1.00 28.82 ? 209 ARG   B CB  1 
ATOM   2447 C  CG  . ARG   B 1 116 ? 25.994  -11.350 -25.712  1.00 31.79 ? 209 ARG   B CG  1 
ATOM   2448 C  CD  . ARG   B 1 116 ? 26.977  -10.581 -24.848  1.00 34.21 ? 209 ARG   B CD  1 
ATOM   2449 N  NE  . ARG   B 1 116 ? 26.850  -10.948 -23.444  1.00 36.78 ? 209 ARG   B NE  1 
ATOM   2450 C  CZ  . ARG   B 1 116 ? 27.401  -12.023 -22.878  1.00 37.81 ? 209 ARG   B CZ  1 
ATOM   2451 N  NH1 . ARG   B 1 116 ? 28.141  -12.860 -23.587  1.00 38.69 ? 209 ARG   B NH1 1 
ATOM   2452 N  NH2 . ARG   B 1 116 ? 27.211  -12.254 -21.592  1.00 38.59 ? 209 ARG   B NH2 1 
ATOM   2453 N  N   . ASN   B 1 117 ? 23.889  -13.544 -27.207  1.00 26.78 ? 210 ASN   B N   1 
ATOM   2454 C  CA  . ASN   B 1 117 ? 23.720  -14.984 -26.864  1.00 28.62 ? 210 ASN   B CA  1 
ATOM   2455 C  C   . ASN   B 1 117 ? 22.608  -15.614 -27.716  1.00 28.02 ? 210 ASN   B C   1 
ATOM   2456 O  O   . ASN   B 1 117 ? 22.857  -16.705 -28.270  1.00 27.58 ? 210 ASN   B O   1 
ATOM   2457 C  CB  . ASN   B 1 117 ? 23.487  -15.164 -25.359  1.00 30.04 ? 210 ASN   B CB  1 
ATOM   2458 C  CG  . ASN   B 1 117 ? 24.687  -14.737 -24.536  1.00 31.62 ? 210 ASN   B CG  1 
ATOM   2459 O  OD1 . ASN   B 1 117 ? 24.577  -13.890 -23.653  1.00 34.15 ? 210 ASN   B OD1 1 
ATOM   2460 N  ND2 . ASN   B 1 117 ? 25.848  -15.299 -24.828  1.00 32.80 ? 210 ASN   B ND2 1 
ATOM   2461 N  N   . THR   B 1 118 ? 21.437  -14.971 -27.824  1.00 27.39 ? 211 THR   B N   1 
ATOM   2462 C  CA  . THR   B 1 118 ? 20.233  -15.524 -28.511  1.00 26.77 ? 211 THR   B CA  1 
ATOM   2463 C  C   . THR   B 1 118 ? 20.175  -15.065 -29.976  1.00 25.82 ? 211 THR   B C   1 
ATOM   2464 O  O   . THR   B 1 118 ? 19.447  -15.707 -30.747  1.00 26.52 ? 211 THR   B O   1 
ATOM   2465 C  CB  . THR   B 1 118 ? 18.933  -15.135 -27.795  1.00 26.73 ? 211 THR   B CB  1 
ATOM   2466 O  OG1 . THR   B 1 118 ? 18.695  -13.748 -28.040  1.00 25.09 ? 211 THR   B OG1 1 
ATOM   2467 C  CG2 . THR   B 1 118 ? 18.969  -15.412 -26.307  1.00 26.76 ? 211 THR   B CG2 1 
ATOM   2468 N  N   . PHE   B 1 119 ? 20.878  -13.984 -30.333  1.00 24.66 ? 212 PHE   B N   1 
ATOM   2469 C  CA  . PHE   B 1 119 ? 20.912  -13.377 -31.695  1.00 24.50 ? 212 PHE   B CA  1 
ATOM   2470 C  C   . PHE   B 1 119 ? 19.574  -12.690 -32.019  1.00 22.63 ? 212 PHE   B C   1 
ATOM   2471 O  O   . PHE   B 1 119 ? 19.413  -12.216 -33.169  1.00 21.24 ? 212 PHE   B O   1 
ATOM   2472 C  CB  . PHE   B 1 119 ? 21.279  -14.422 -32.759  1.00 26.21 ? 212 PHE   B CB  1 
ATOM   2473 C  CG  . PHE   B 1 119 ? 22.498  -15.249 -32.431  1.00 27.59 ? 212 PHE   B CG  1 
ATOM   2474 C  CD1 . PHE   B 1 119 ? 23.690  -14.638 -32.070  1.00 29.04 ? 212 PHE   B CD1 1 
ATOM   2475 C  CD2 . PHE   B 1 119 ? 22.458  -16.635 -32.477  1.00 28.57 ? 212 PHE   B CD2 1 
ATOM   2476 C  CE1 . PHE   B 1 119 ? 24.811  -15.394 -31.753  1.00 29.65 ? 212 PHE   B CE1 1 
ATOM   2477 C  CE2 . PHE   B 1 119 ? 23.582  -17.388 -32.164  1.00 29.57 ? 212 PHE   B CE2 1 
ATOM   2478 C  CZ  . PHE   B 1 119 ? 24.755  -16.766 -31.802  1.00 29.62 ? 212 PHE   B CZ  1 
ATOM   2479 N  N   . ARG   B 1 120 ? 18.660  -12.606 -31.045  1.00 20.42 ? 213 ARG   B N   1 
ATOM   2480 C  CA  . ARG   B 1 120 ? 17.310  -11.999 -31.211  1.00 20.28 ? 213 ARG   B CA  1 
ATOM   2481 C  C   . ARG   B 1 120 ? 17.456  -10.485 -31.391  1.00 18.81 ? 213 ARG   B C   1 
ATOM   2482 O  O   . ARG   B 1 120 ? 18.333  -9.883  -30.731  1.00 17.99 ? 213 ARG   B O   1 
ATOM   2483 C  CB  . ARG   B 1 120 ? 16.422  -12.274 -29.994  1.00 21.20 ? 213 ARG   B CB  1 
ATOM   2484 C  CG  . ARG   B 1 120 ? 16.193  -13.749 -29.707  1.00 22.61 ? 213 ARG   B CG  1 
ATOM   2485 C  CD  . ARG   B 1 120 ? 14.943  -14.268 -30.375  1.00 23.31 ? 213 ARG   B CD  1 
ATOM   2486 N  NE  . ARG   B 1 120 ? 14.729  -15.684 -30.113  1.00 23.35 ? 213 ARG   B NE  1 
ATOM   2487 C  CZ  . ARG   B 1 120 ? 13.796  -16.423 -30.701  1.00 23.45 ? 213 ARG   B CZ  1 
ATOM   2488 N  NH1 . ARG   B 1 120 ? 12.976  -15.881 -31.587  1.00 23.54 ? 213 ARG   B NH1 1 
ATOM   2489 N  NH2 . ARG   B 1 120 ? 13.679  -17.705 -30.395  1.00 23.34 ? 213 ARG   B NH2 1 
ATOM   2490 N  N   . HIS   B 1 121 ? 16.617  -9.904  -32.249  1.00 17.41 ? 214 HIS   B N   1 
ATOM   2491 C  CA  . HIS   B 1 121 ? 16.533  -8.445  -32.507  1.00 16.61 ? 214 HIS   B CA  1 
ATOM   2492 C  C   . HIS   B 1 121 ? 15.487  -7.844  -31.570  1.00 15.91 ? 214 HIS   B C   1 
ATOM   2493 O  O   . HIS   B 1 121 ? 14.428  -8.473  -31.375  1.00 15.45 ? 214 HIS   B O   1 
ATOM   2494 C  CB  . HIS   B 1 121 ? 16.190  -8.167  -33.972  1.00 16.74 ? 214 HIS   B CB  1 
ATOM   2495 C  CG  . HIS   B 1 121 ? 17.143  -8.784  -34.938  1.00 17.22 ? 214 HIS   B CG  1 
ATOM   2496 N  ND1 . HIS   B 1 121 ? 16.823  -8.976  -36.262  1.00 17.70 ? 214 HIS   B ND1 1 
ATOM   2497 C  CD2 . HIS   B 1 121 ? 18.399  -9.257  -34.776  1.00 17.54 ? 214 HIS   B CD2 1 
ATOM   2498 C  CE1 . HIS   B 1 121 ? 17.850  -9.525  -36.883  1.00 18.01 ? 214 HIS   B CE1 1 
ATOM   2499 N  NE2 . HIS   B 1 121 ? 18.829  -9.706  -35.993  1.00 17.66 ? 214 HIS   B NE2 1 
ATOM   2500 N  N   . SER   B 1 122 ? 15.785  -6.680  -31.000  1.00 15.53 ? 215 SER   B N   1 
ATOM   2501 C  CA  . SER   B 1 122 ? 14.804  -5.879  -30.231  1.00 15.58 ? 215 SER   B CA  1 
ATOM   2502 C  C   . SER   B 1 122 ? 15.121  -4.395  -30.392  1.00 15.34 ? 215 SER   B C   1 
ATOM   2503 O  O   . SER   B 1 122 ? 16.278  -4.044  -30.715  1.00 15.35 ? 215 SER   B O   1 
ATOM   2504 C  CB  . SER   B 1 122 ? 14.766  -6.296  -28.786  1.00 15.47 ? 215 SER   B CB  1 
ATOM   2505 O  OG  . SER   B 1 122 ? 16.047  -6.176  -28.188  1.00 15.51 ? 215 SER   B OG  1 
ATOM   2506 N  N   . VAL   B 1 123 ? 14.108  -3.564  -30.184  1.00 15.20 ? 216 VAL   B N   1 
ATOM   2507 C  CA  . VAL   B 1 123 ? 14.208  -2.080  -30.255  1.00 15.29 ? 216 VAL   B CA  1 
ATOM   2508 C  C   . VAL   B 1 123 ? 13.628  -1.535  -28.950  1.00 15.43 ? 216 VAL   B C   1 
ATOM   2509 O  O   . VAL   B 1 123 ? 12.565  -2.018  -28.521  1.00 15.14 ? 216 VAL   B O   1 
ATOM   2510 C  CB  . VAL   B 1 123 ? 13.501  -1.539  -31.511  1.00 15.41 ? 216 VAL   B CB  1 
ATOM   2511 C  CG1 . VAL   B 1 123 ? 12.050  -1.995  -31.598  1.00 15.55 ? 216 VAL   B CG1 1 
ATOM   2512 C  CG2 . VAL   B 1 123 ? 13.607  -0.028  -31.608  1.00 15.38 ? 216 VAL   B CG2 1 
ATOM   2513 N  N   . VAL   B 1 124 ? 14.341  -0.618  -28.304  1.00 15.91 ? 217 VAL   B N   1 
ATOM   2514 C  CA  . VAL   B 1 124 ? 13.969  -0.112  -26.953  1.00 15.95 ? 217 VAL   B CA  1 
ATOM   2515 C  C   . VAL   B 1 124 ? 13.976  1.417   -27.010  1.00 15.82 ? 217 VAL   B C   1 
ATOM   2516 O  O   . VAL   B 1 124 ? 14.799  1.982   -27.757  1.00 15.04 ? 217 VAL   B O   1 
ATOM   2517 C  CB  . VAL   B 1 124 ? 14.882  -0.697  -25.855  1.00 16.37 ? 217 VAL   B CB  1 
ATOM   2518 C  CG1 . VAL   B 1 124 ? 16.356  -0.434  -26.099  1.00 16.62 ? 217 VAL   B CG1 1 
ATOM   2519 C  CG2 . VAL   B 1 124 ? 14.490  -0.219  -24.468  1.00 16.79 ? 217 VAL   B CG2 1 
ATOM   2520 N  N   . VAL   B 1 125 ? 13.038  2.048   -26.303  1.00 15.68 ? 218 VAL   B N   1 
ATOM   2521 C  CA  . VAL   B 1 125 ? 12.972  3.530   -26.152  1.00 15.95 ? 218 VAL   B CA  1 
ATOM   2522 C  C   . VAL   B 1 125 ? 12.791  3.849   -24.674  1.00 16.14 ? 218 VAL   B C   1 
ATOM   2523 O  O   . VAL   B 1 125 ? 12.272  3.032   -23.915  1.00 15.43 ? 218 VAL   B O   1 
ATOM   2524 C  CB  . VAL   B 1 125 ? 11.851  4.161   -26.999  1.00 16.21 ? 218 VAL   B CB  1 
ATOM   2525 C  CG1 . VAL   B 1 125 ? 12.186  4.140   -28.483  1.00 16.40 ? 218 VAL   B CG1 1 
ATOM   2526 C  CG2 . VAL   B 1 125 ? 10.494  3.524   -26.738  1.00 16.38 ? 218 VAL   B CG2 1 
ATOM   2527 N  N   . PRO   B 1 126 ? 13.191  5.060   -24.233  1.00 16.85 ? 219 PRO   B N   1 
ATOM   2528 C  CA  . PRO   B 1 126 ? 12.845  5.540   -22.900  1.00 17.37 ? 219 PRO   B CA  1 
ATOM   2529 C  C   . PRO   B 1 126 ? 11.320  5.615   -22.749  1.00 18.20 ? 219 PRO   B C   1 
ATOM   2530 O  O   . PRO   B 1 126 ? 10.654  6.060   -23.675  1.00 17.48 ? 219 PRO   B O   1 
ATOM   2531 C  CB  . PRO   B 1 126 ? 13.462  6.942   -22.837  1.00 17.40 ? 219 PRO   B CB  1 
ATOM   2532 C  CG  . PRO   B 1 126 ? 14.539  6.921   -23.891  1.00 17.23 ? 219 PRO   B CG  1 
ATOM   2533 C  CD  . PRO   B 1 126 ? 13.989  6.035   -24.988  1.00 17.22 ? 219 PRO   B CD  1 
ATOM   2534 N  N   . TYR   B 1 127 ? 10.802  5.148   -21.614  1.00 18.73 ? 220 TYR   B N   1 
ATOM   2535 C  CA  . TYR   B 1 127 ? 9.390   5.365   -21.226  1.00 19.72 ? 220 TYR   B CA  1 
ATOM   2536 C  C   . TYR   B 1 127 ? 9.222   6.853   -20.905  1.00 21.10 ? 220 TYR   B C   1 
ATOM   2537 O  O   . TYR   B 1 127 ? 10.036  7.380   -20.129  1.00 20.83 ? 220 TYR   B O   1 
ATOM   2538 C  CB  . TYR   B 1 127 ? 8.983   4.516   -20.023  1.00 19.42 ? 220 TYR   B CB  1 
ATOM   2539 C  CG  . TYR   B 1 127 ? 7.603   4.860   -19.530  1.00 19.07 ? 220 TYR   B CG  1 
ATOM   2540 C  CD1 . TYR   B 1 127 ? 6.483   4.231   -20.049  1.00 19.21 ? 220 TYR   B CD1 1 
ATOM   2541 C  CD2 . TYR   B 1 127 ? 7.412   5.863   -18.594  1.00 18.74 ? 220 TYR   B CD2 1 
ATOM   2542 C  CE1 . TYR   B 1 127 ? 5.208   4.560   -19.619  1.00 19.27 ? 220 TYR   B CE1 1 
ATOM   2543 C  CE2 . TYR   B 1 127 ? 6.146   6.207   -18.157  1.00 19.09 ? 220 TYR   B CE2 1 
ATOM   2544 C  CZ  . TYR   B 1 127 ? 5.040   5.557   -18.674  1.00 19.14 ? 220 TYR   B CZ  1 
ATOM   2545 O  OH  . TYR   B 1 127 ? 3.792   5.901   -18.243  1.00 19.28 ? 220 TYR   B OH  1 
ATOM   2546 N  N   . GLU   B 1 128 ? 8.232   7.506   -21.514  1.00 22.34 ? 221 GLU   B N   1 
ATOM   2547 C  CA  . GLU   B 1 128 ? 7.780   8.870   -21.132  1.00 24.50 ? 221 GLU   B CA  1 
ATOM   2548 C  C   . GLU   B 1 128 ? 6.343   8.765   -20.629  1.00 24.13 ? 221 GLU   B C   1 
ATOM   2549 O  O   . GLU   B 1 128 ? 5.563   7.962   -21.141  1.00 23.21 ? 221 GLU   B O   1 
ATOM   2550 C  CB  . GLU   B 1 128 ? 7.924   9.842   -22.304  1.00 27.13 ? 221 GLU   B CB  1 
ATOM   2551 C  CG  . GLU   B 1 128 ? 9.366   10.031  -22.743  1.00 29.94 ? 221 GLU   B CG  1 
ATOM   2552 C  CD  . GLU   B 1 128 ? 9.657   11.340  -23.459  1.00 33.79 ? 221 GLU   B CD  1 
ATOM   2553 O  OE1 . GLU   B 1 128 ? 8.812   11.776  -24.263  1.00 37.59 ? 221 GLU   B OE1 1 
ATOM   2554 O  OE2 . GLU   B 1 128 ? 10.733  11.922  -23.207  1.00 37.35 ? 221 GLU   B OE2 1 
ATOM   2555 N  N   . PRO   B 1 129 ? 5.962   9.539   -19.586  1.00 23.80 ? 222 PRO   B N   1 
ATOM   2556 C  CA  . PRO   B 1 129 ? 4.582   9.549   -19.098  1.00 24.07 ? 222 PRO   B CA  1 
ATOM   2557 C  C   . PRO   B 1 129 ? 3.608   10.007  -20.179  1.00 23.42 ? 222 PRO   B C   1 
ATOM   2558 O  O   . PRO   B 1 129 ? 4.024   10.626  -21.153  1.00 23.13 ? 222 PRO   B O   1 
ATOM   2559 C  CB  . PRO   B 1 129 ? 4.585   10.560  -17.938  1.00 24.33 ? 222 PRO   B CB  1 
ATOM   2560 C  CG  . PRO   B 1 129 ? 6.043   10.711  -17.554  1.00 24.70 ? 222 PRO   B CG  1 
ATOM   2561 C  CD  . PRO   B 1 129 ? 6.836   10.436  -18.817  1.00 24.28 ? 222 PRO   B CD  1 
ATOM   2562 N  N   . PRO   B 1 130 ? 2.292   9.720   -20.049  1.00 24.17 ? 223 PRO   B N   1 
ATOM   2563 C  CA  . PRO   B 1 130 ? 1.316   10.112  -21.064  1.00 25.25 ? 223 PRO   B CA  1 
ATOM   2564 C  C   . PRO   B 1 130 ? 1.424   11.589  -21.467  1.00 25.79 ? 223 PRO   B C   1 
ATOM   2565 O  O   . PRO   B 1 130 ? 1.543   12.423  -20.591  1.00 24.46 ? 223 PRO   B O   1 
ATOM   2566 C  CB  . PRO   B 1 130 ? -0.023  9.837   -20.371  1.00 25.09 ? 223 PRO   B CB  1 
ATOM   2567 C  CG  . PRO   B 1 130 ? 0.285   8.677   -19.469  1.00 24.79 ? 223 PRO   B CG  1 
ATOM   2568 C  CD  . PRO   B 1 130 ? 1.668   8.989   -18.937  1.00 24.41 ? 223 PRO   B CD  1 
ATOM   2569 N  N   . GLU   B 1 131 ? 1.388   11.862  -22.775  1.00 27.97 ? 224 GLU   B N   1 
ATOM   2570 C  CA  . GLU   B 1 131 ? 1.452   13.235  -23.340  1.00 29.67 ? 224 GLU   B CA  1 
ATOM   2571 C  C   . GLU   B 1 131 ? 0.137   13.965  -23.048  1.00 29.09 ? 224 GLU   B C   1 
ATOM   2572 O  O   . GLU   B 1 131 ? -0.853  13.305  -22.661  1.00 26.68 ? 224 GLU   B O   1 
ATOM   2573 C  CB  . GLU   B 1 131 ? 1.732   13.216  -24.845  1.00 32.51 ? 224 GLU   B CB  1 
ATOM   2574 C  CG  . GLU   B 1 131 ? 3.188   12.930  -25.185  1.00 34.60 ? 224 GLU   B CG  1 
ATOM   2575 C  CD  . GLU   B 1 131 ? 3.905   13.981  -26.020  1.00 36.87 ? 224 GLU   B CD  1 
ATOM   2576 O  OE1 . GLU   B 1 131 ? 3.226   14.863  -26.592  1.00 38.42 ? 224 GLU   B OE1 1 
ATOM   2577 O  OE2 . GLU   B 1 131 ? 5.154   13.922  -26.087  1.00 38.70 ? 224 GLU   B OE2 1 
ATOM   2578 N  N   . VAL   B 1 132 ? 0.148   15.286  -23.231  1.00 28.74 ? 225 VAL   B N   1 
ATOM   2579 C  CA  . VAL   B 1 132 ? -1.028  16.178  -23.017  1.00 28.57 ? 225 VAL   B CA  1 
ATOM   2580 C  C   . VAL   B 1 132 ? -2.187  15.662  -23.880  1.00 28.04 ? 225 VAL   B C   1 
ATOM   2581 O  O   . VAL   B 1 132 ? -1.954  15.362  -25.071  1.00 27.55 ? 225 VAL   B O   1 
ATOM   2582 C  CB  . VAL   B 1 132 ? -0.680  17.644  -23.341  1.00 28.49 ? 225 VAL   B CB  1 
ATOM   2583 C  CG1 . VAL   B 1 132 ? -1.926  18.519  -23.396  1.00 28.45 ? 225 VAL   B CG1 1 
ATOM   2584 C  CG2 . VAL   B 1 132 ? 0.337   18.203  -22.354  1.00 28.53 ? 225 VAL   B CG2 1 
ATOM   2585 N  N   . GLY   B 1 133 ? -3.377  15.543  -23.288  1.00 27.46 ? 226 GLY   B N   1 
ATOM   2586 C  CA  . GLY   B 1 133 ? -4.620  15.182  -23.994  1.00 27.45 ? 226 GLY   B CA  1 
ATOM   2587 C  C   . GLY   B 1 133 ? -4.806  13.678  -24.116  1.00 27.64 ? 226 GLY   B C   1 
ATOM   2588 O  O   . GLY   B 1 133 ? -5.788  13.268  -24.770  1.00 27.77 ? 226 GLY   B O   1 
ATOM   2589 N  N   . SER   B 1 134 ? -3.921  12.886  -23.500  1.00 26.49 ? 227 SER   B N   1 
ATOM   2590 C  CA  . SER   B 1 134 ? -3.903  11.400  -23.575  1.00 26.29 ? 227 SER   B CA  1 
ATOM   2591 C  C   . SER   B 1 134 ? -3.709  10.799  -22.180  1.00 24.90 ? 227 SER   B C   1 
ATOM   2592 O  O   . SER   B 1 134 ? -3.005  11.415  -21.362  1.00 24.41 ? 227 SER   B O   1 
ATOM   2593 C  CB  . SER   B 1 134 ? -2.827  10.911  -24.512  1.00 26.89 ? 227 SER   B CB  1 
ATOM   2594 O  OG  . SER   B 1 134 ? -2.909  9.500   -24.646  1.00 27.15 ? 227 SER   B OG  1 
ATOM   2595 N  N   . ASP   B 1 135 ? -4.300  9.626   -21.945  1.00 23.66 ? 228 ASP   B N   1 
ATOM   2596 C  CA  . ASP   B 1 135 ? -4.206  8.865   -20.672  1.00 23.96 ? 228 ASP   B CA  1 
ATOM   2597 C  C   . ASP   B 1 135 ? -3.182  7.732   -20.813  1.00 22.29 ? 228 ASP   B C   1 
ATOM   2598 O  O   . ASP   B 1 135 ? -3.008  6.974   -19.849  1.00 22.18 ? 228 ASP   B O   1 
ATOM   2599 C  CB  . ASP   B 1 135 ? -5.583  8.343   -20.264  1.00 25.31 ? 228 ASP   B CB  1 
ATOM   2600 C  CG  . ASP   B 1 135 ? -6.513  9.449   -19.800  1.00 27.04 ? 228 ASP   B CG  1 
ATOM   2601 O  OD1 . ASP   B 1 135 ? -6.002  10.439  -19.244  1.00 28.81 ? 228 ASP   B OD1 1 
ATOM   2602 O  OD2 . ASP   B 1 135 ? -7.735  9.320   -20.015  1.00 29.54 ? 228 ASP   B OD2 1 
ATOM   2603 N  N   . CYS   B 1 136 ? -2.513  7.626   -21.962  1.00 21.17 ? 229 CYS   B N   1 
ATOM   2604 C  CA  . CYS   B 1 136 ? -1.519  6.557   -22.237  1.00 20.41 ? 229 CYS   B CA  1 
ATOM   2605 C  C   . CYS   B 1 136 ? -0.289  7.136   -22.937  1.00 20.03 ? 229 CYS   B C   1 
ATOM   2606 O  O   . CYS   B 1 136 ? -0.335  8.291   -23.386  1.00 20.13 ? 229 CYS   B O   1 
ATOM   2607 C  CB  . CYS   B 1 136 ? -2.136  5.456   -23.087  1.00 20.07 ? 229 CYS   B CB  1 
ATOM   2608 S  SG  . CYS   B 1 136 ? -2.781  6.053   -24.669  1.00 19.57 ? 229 CYS   B SG  1 
ATOM   2609 N  N   . THR   B 1 137 ? 0.772   6.337   -23.013  1.00 19.30 ? 230 THR   B N   1 
ATOM   2610 C  CA  . THR   B 1 137 ? 1.999   6.630   -23.787  1.00 19.17 ? 230 THR   B CA  1 
ATOM   2611 C  C   . THR   B 1 137 ? 1.899   5.902   -25.127  1.00 18.68 ? 230 THR   B C   1 
ATOM   2612 O  O   . THR   B 1 137 ? 1.610   4.695   -25.112  1.00 17.96 ? 230 THR   B O   1 
ATOM   2613 C  CB  . THR   B 1 137 ? 3.239   6.200   -23.001  1.00 19.15 ? 230 THR   B CB  1 
ATOM   2614 O  OG1 . THR   B 1 137 ? 3.193   6.886   -21.751  1.00 19.74 ? 230 THR   B OG1 1 
ATOM   2615 C  CG2 . THR   B 1 137 ? 4.526   6.486   -23.739  1.00 19.09 ? 230 THR   B CG2 1 
ATOM   2616 N  N   . THR   B 1 138 ? 2.108   6.610   -26.234  1.00 18.50 ? 231 THR   B N   1 
ATOM   2617 C  CA  . THR   B 1 138 ? 2.056   6.033   -27.599  1.00 18.39 ? 231 THR   B CA  1 
ATOM   2618 C  C   . THR   B 1 138 ? 3.480   5.931   -28.145  1.00 18.42 ? 231 THR   B C   1 
ATOM   2619 O  O   . THR   B 1 138 ? 4.214   6.935   -28.087  1.00 18.73 ? 231 THR   B O   1 
ATOM   2620 C  CB  . THR   B 1 138 ? 1.140   6.836   -28.528  1.00 18.58 ? 231 THR   B CB  1 
ATOM   2621 O  OG1 . THR   B 1 138 ? -0.166  6.809   -27.954  1.00 18.60 ? 231 THR   B OG1 1 
ATOM   2622 C  CG2 . THR   B 1 138 ? 1.102   6.281   -29.935  1.00 18.38 ? 231 THR   B CG2 1 
ATOM   2623 N  N   . ILE   B 1 139 ? 3.849   4.739   -28.618  1.00 17.99 ? 232 ILE   B N   1 
ATOM   2624 C  CA  . ILE   B 1 139 ? 5.096   4.494   -29.394  1.00 17.70 ? 232 ILE   B CA  1 
ATOM   2625 C  C   . ILE   B 1 139 ? 4.668   4.239   -30.837  1.00 17.22 ? 232 ILE   B C   1 
ATOM   2626 O  O   . ILE   B 1 139 ? 3.705   3.475   -31.036  1.00 17.72 ? 232 ILE   B O   1 
ATOM   2627 C  CB  . ILE   B 1 139 ? 5.915   3.328   -28.807  1.00 17.85 ? 232 ILE   B CB  1 
ATOM   2628 C  CG1 . ILE   B 1 139 ? 6.344   3.611   -27.363  1.00 18.40 ? 232 ILE   B CG1 1 
ATOM   2629 C  CG2 . ILE   B 1 139 ? 7.105   3.013   -29.705  1.00 18.04 ? 232 ILE   B CG2 1 
ATOM   2630 C  CD1 . ILE   B 1 139 ? 7.005   2.444   -26.666  1.00 18.78 ? 232 ILE   B CD1 1 
ATOM   2631 N  N   . HIS   B 1 140 ? 5.336   4.876   -31.797  1.00 17.51 ? 233 HIS   B N   1 
ATOM   2632 C  CA  . HIS   B 1 140 ? 5.104   4.658   -33.250  1.00 17.60 ? 233 HIS   B CA  1 
ATOM   2633 C  C   . HIS   B 1 140 ? 6.082   3.595   -33.766  1.00 17.07 ? 233 HIS   B C   1 
ATOM   2634 O  O   . HIS   B 1 140 ? 7.266   3.920   -33.986  1.00 16.80 ? 233 HIS   B O   1 
ATOM   2635 C  CB  . HIS   B 1 140 ? 5.211   5.973   -34.026  1.00 18.46 ? 233 HIS   B CB  1 
ATOM   2636 C  CG  . HIS   B 1 140 ? 4.051   6.888   -33.822  1.00 19.10 ? 233 HIS   B CG  1 
ATOM   2637 N  ND1 . HIS   B 1 140 ? 4.058   8.192   -34.279  1.00 19.97 ? 233 HIS   B ND1 1 
ATOM   2638 C  CD2 . HIS   B 1 140 ? 2.853   6.697   -33.227  1.00 19.65 ? 233 HIS   B CD2 1 
ATOM   2639 C  CE1 . HIS   B 1 140 ? 2.912   8.766   -33.971  1.00 20.53 ? 233 HIS   B CE1 1 
ATOM   2640 N  NE2 . HIS   B 1 140 ? 2.155   7.869   -33.322  1.00 19.91 ? 233 HIS   B NE2 1 
ATOM   2641 N  N   . TYR   B 1 141 ? 5.596   2.367   -33.946  1.00 16.16 ? 234 TYR   B N   1 
ATOM   2642 C  CA  . TYR   B 1 141 ? 6.384   1.238   -34.502  1.00 15.43 ? 234 TYR   B CA  1 
ATOM   2643 C  C   . TYR   B 1 141 ? 6.225   1.225   -36.026  1.00 15.60 ? 234 TYR   B C   1 
ATOM   2644 O  O   . TYR   B 1 141 ? 5.167   1.667   -36.521  1.00 15.83 ? 234 TYR   B O   1 
ATOM   2645 C  CB  . TYR   B 1 141 ? 5.966   -0.081  -33.855  1.00 14.43 ? 234 TYR   B CB  1 
ATOM   2646 C  CG  . TYR   B 1 141 ? 6.401   -0.232  -32.419  1.00 14.27 ? 234 TYR   B CG  1 
ATOM   2647 C  CD1 . TYR   B 1 141 ? 7.730   -0.467  -32.090  1.00 13.85 ? 234 TYR   B CD1 1 
ATOM   2648 C  CD2 . TYR   B 1 141 ? 5.483   -0.159  -31.385  1.00 13.80 ? 234 TYR   B CD2 1 
ATOM   2649 C  CE1 . TYR   B 1 141 ? 8.130   -0.629  -30.771  1.00 13.95 ? 234 TYR   B CE1 1 
ATOM   2650 C  CE2 . TYR   B 1 141 ? 5.867   -0.316  -30.063  1.00 13.90 ? 234 TYR   B CE2 1 
ATOM   2651 C  CZ  . TYR   B 1 141 ? 7.196   -0.549  -29.752  1.00 14.05 ? 234 TYR   B CZ  1 
ATOM   2652 O  OH  . TYR   B 1 141 ? 7.578   -0.692  -28.446  1.00 14.10 ? 234 TYR   B OH  1 
ATOM   2653 N  N   . ASN   B 1 142 ? 7.270   0.777   -36.731  1.00 16.14 ? 235 ASN   B N   1 
ATOM   2654 C  CA  . ASN   B 1 142 ? 7.255   0.458   -38.187  1.00 16.69 ? 235 ASN   B CA  1 
ATOM   2655 C  C   . ASN   B 1 142 ? 7.690   -0.997  -38.365  1.00 16.41 ? 235 ASN   B C   1 
ATOM   2656 O  O   . ASN   B 1 142 ? 8.728   -1.373  -37.793  1.00 16.27 ? 235 ASN   B O   1 
ATOM   2657 C  CB  . ASN   B 1 142 ? 8.197   1.337   -39.013  1.00 17.85 ? 235 ASN   B CB  1 
ATOM   2658 C  CG  . ASN   B 1 142 ? 7.945   2.827   -38.905  1.00 18.74 ? 235 ASN   B CG  1 
ATOM   2659 O  OD1 . ASN   B 1 142 ? 8.855   3.620   -39.137  1.00 21.22 ? 235 ASN   B OD1 1 
ATOM   2660 N  ND2 . ASN   B 1 142 ? 6.728   3.225   -38.583  1.00 18.47 ? 235 ASN   B ND2 1 
ATOM   2661 N  N   . TYR   B 1 143 ? 6.937   -1.777  -39.141  1.00 15.92 ? 236 TYR   B N   1 
ATOM   2662 C  CA  . TYR   B 1 143 ? 7.281   -3.171  -39.520  1.00 15.94 ? 236 TYR   B CA  1 
ATOM   2663 C  C   . TYR   B 1 143 ? 7.791   -3.166  -40.967  1.00 16.71 ? 236 TYR   B C   1 
ATOM   2664 O  O   . TYR   B 1 143 ? 7.032   -2.756  -41.864  1.00 17.35 ? 236 TYR   B O   1 
ATOM   2665 C  CB  . TYR   B 1 143 ? 6.077   -4.085  -39.298  1.00 15.61 ? 236 TYR   B CB  1 
ATOM   2666 C  CG  . TYR   B 1 143 ? 5.710   -4.272  -37.849  1.00 15.22 ? 236 TYR   B CG  1 
ATOM   2667 C  CD1 . TYR   B 1 143 ? 4.904   -3.359  -37.187  1.00 15.39 ? 236 TYR   B CD1 1 
ATOM   2668 C  CD2 . TYR   B 1 143 ? 6.171   -5.368  -37.138  1.00 14.91 ? 236 TYR   B CD2 1 
ATOM   2669 C  CE1 . TYR   B 1 143 ? 4.551   -3.540  -35.858  1.00 15.25 ? 236 TYR   B CE1 1 
ATOM   2670 C  CE2 . TYR   B 1 143 ? 5.840   -5.557  -35.808  1.00 15.12 ? 236 TYR   B CE2 1 
ATOM   2671 C  CZ  . TYR   B 1 143 ? 5.032   -4.639  -35.165  1.00 15.24 ? 236 TYR   B CZ  1 
ATOM   2672 O  OH  . TYR   B 1 143 ? 4.704   -4.844  -33.860  1.00 15.72 ? 236 TYR   B OH  1 
ATOM   2673 N  N   . MET   B 1 144 ? 9.037   -3.603  -41.174  1.00 17.31 ? 237 MET   B N   1 
ATOM   2674 C  CA  . MET   B 1 144 ? 9.854   -3.271  -42.377  1.00 18.38 ? 237 MET   B CA  1 
ATOM   2675 C  C   . MET   B 1 144 ? 9.959   -4.476  -43.322  1.00 19.21 ? 237 MET   B C   1 
ATOM   2676 O  O   . MET   B 1 144 ? 10.899  -4.516  -44.150  1.00 19.24 ? 237 MET   B O   1 
ATOM   2677 C  CB  . MET   B 1 144 ? 11.256  -2.823  -41.952  1.00 18.56 ? 237 MET   B CB  1 
ATOM   2678 C  CG  . MET   B 1 144 ? 11.256  -1.636  -41.001  1.00 18.60 ? 237 MET   B CG  1 
ATOM   2679 S  SD  . MET   B 1 144 ? 10.389  -0.185  -41.644  1.00 19.49 ? 237 MET   B SD  1 
ATOM   2680 C  CE  . MET   B 1 144 ? 11.202  0.021   -43.228  1.00 19.65 ? 237 MET   B CE  1 
ATOM   2681 N  N   . CYS   B 1 145 ? 9.015   -5.410  -43.224  1.00 19.61 ? 238 CYS   B N   1 
ATOM   2682 C  CA  . CYS   B 1 145 ? 8.928   -6.628  -44.072  1.00 20.31 ? 238 CYS   B CA  1 
ATOM   2683 C  C   . CYS   B 1 145 ? 7.481   -7.125  -44.011  1.00 19.91 ? 238 CYS   B C   1 
ATOM   2684 O  O   . CYS   B 1 145 ? 6.868   -7.006  -42.928  1.00 19.15 ? 238 CYS   B O   1 
ATOM   2685 C  CB  . CYS   B 1 145 ? 9.907   -7.677  -43.558  1.00 21.23 ? 238 CYS   B CB  1 
ATOM   2686 S  SG  . CYS   B 1 145 ? 10.428  -8.961  -44.648  1.00 22.54 ? 238 CYS   B SG  1 
ATOM   2687 N  N   . ASN   B 1 146 ? 6.942   -7.616  -45.126  1.00 19.71 ? 239 ASN   B N   1 
ATOM   2688 C  CA  . ASN   B 1 146 ? 5.552   -8.142  -45.202  1.00 19.83 ? 239 ASN   B CA  1 
ATOM   2689 C  C   . ASN   B 1 146 ? 5.518   -9.560  -44.626  1.00 19.74 ? 239 ASN   B C   1 
ATOM   2690 O  O   . ASN   B 1 146 ? 6.535   -10.259 -44.746  1.00 19.70 ? 239 ASN   B O   1 
ATOM   2691 C  CB  . ASN   B 1 146 ? 5.025   -8.096  -46.636  1.00 20.28 ? 239 ASN   B CB  1 
ATOM   2692 C  CG  . ASN   B 1 146 ? 4.744   -6.681  -47.089  1.00 20.73 ? 239 ASN   B CG  1 
ATOM   2693 O  OD1 . ASN   B 1 146 ? 4.084   -5.923  -46.380  1.00 22.16 ? 239 ASN   B OD1 1 
ATOM   2694 N  ND2 . ASN   B 1 146 ? 5.228   -6.319  -48.263  1.00 20.95 ? 239 ASN   B ND2 1 
ATOM   2695 N  N   . SER   B 1 147 ? 4.393   -9.966  -44.026  1.00 19.92 ? 240 SER   B N   1 
ATOM   2696 C  CA  . SER   B 1 147 ? 4.151   -11.351 -43.538  1.00 20.76 ? 240 SER   B CA  1 
ATOM   2697 C  C   . SER   B 1 147 ? 4.385   -12.368 -44.669  1.00 21.83 ? 240 SER   B C   1 
ATOM   2698 O  O   . SER   B 1 147 ? 4.912   -13.460 -44.376  1.00 21.52 ? 240 SER   B O   1 
ATOM   2699 C  CB  . SER   B 1 147 ? 2.761   -11.489 -42.960  1.00 20.77 ? 240 SER   B CB  1 
ATOM   2700 O  OG  . SER   B 1 147 ? 2.644   -10.748 -41.754  1.00 20.42 ? 240 SER   B OG  1 
ATOM   2701 N  N   . SER   B 1 148 ? 4.030   -12.011 -45.909  1.00 22.54 ? 241 SER   B N   1 
ATOM   2702 C  CA  . SER   B 1 148 ? 4.054   -12.899 -47.104  1.00 24.15 ? 241 SER   B CA  1 
ATOM   2703 C  C   . SER   B 1 148 ? 5.471   -13.026 -47.683  1.00 25.07 ? 241 SER   B C   1 
ATOM   2704 O  O   . SER   B 1 148 ? 5.667   -13.879 -48.569  1.00 25.75 ? 241 SER   B O   1 
ATOM   2705 C  CB  . SER   B 1 148 ? 3.100   -12.397 -48.158  1.00 24.17 ? 241 SER   B CB  1 
ATOM   2706 O  OG  . SER   B 1 148 ? 3.553   -11.157 -48.689  1.00 24.83 ? 241 SER   B OG  1 
ATOM   2707 N  N   . CYS   B 1 149 ? 6.422   -12.200 -47.243  1.00 24.60 ? 242 CYS   B N   1 
ATOM   2708 C  CA  . CYS   B 1 149 ? 7.780   -12.128 -47.847  1.00 24.59 ? 242 CYS   B CA  1 
ATOM   2709 C  C   . CYS   B 1 149 ? 8.430   -13.517 -47.862  1.00 25.34 ? 242 CYS   B C   1 
ATOM   2710 O  O   . CYS   B 1 149 ? 8.691   -14.072 -46.785  1.00 23.81 ? 242 CYS   B O   1 
ATOM   2711 C  CB  . CYS   B 1 149 ? 8.674   -11.149 -47.103  1.00 23.25 ? 242 CYS   B CB  1 
ATOM   2712 S  SG  . CYS   B 1 149 ? 8.520   -9.520  -47.736  1.00 22.74 ? 242 CYS   B SG  1 
ATOM   2713 N  N   . MET   B 1 150 ? 8.690   -14.045 -49.059  1.00 28.12 ? 243 MET   B N   1 
ATOM   2714 C  CA  . MET   B 1 150 ? 9.480   -15.286 -49.268  1.00 30.15 ? 243 MET   B CA  1 
ATOM   2715 C  C   . MET   B 1 150 ? 10.924  -15.031 -48.815  1.00 29.45 ? 243 MET   B C   1 
ATOM   2716 O  O   . MET   B 1 150 ? 11.453  -13.944 -49.101  1.00 29.42 ? 243 MET   B O   1 
ATOM   2717 C  CB  . MET   B 1 150 ? 9.437   -15.691 -50.746  1.00 32.59 ? 243 MET   B CB  1 
ATOM   2718 C  CG  . MET   B 1 150 ? 8.068   -16.185 -51.178  1.00 34.47 ? 243 MET   B CG  1 
ATOM   2719 S  SD  . MET   B 1 150 ? 8.013   -16.723 -52.907  1.00 37.44 ? 243 MET   B SD  1 
ATOM   2720 C  CE  . MET   B 1 150 ? 6.378   -16.156 -53.371  1.00 38.31 ? 243 MET   B CE  1 
ATOM   2721 N  N   . GLY   B 1 151 ? 11.526  -15.980 -48.092  1.00 29.88 ? 244 GLY   B N   1 
ATOM   2722 C  CA  . GLY   B 1 151 ? 12.901  -15.854 -47.569  1.00 29.44 ? 244 GLY   B CA  1 
ATOM   2723 C  C   . GLY   B 1 151 ? 12.951  -15.020 -46.299  1.00 28.68 ? 244 GLY   B C   1 
ATOM   2724 O  O   . GLY   B 1 151 ? 14.068  -14.707 -45.845  1.00 28.62 ? 244 GLY   B O   1 
ATOM   2725 N  N   . GLY   B 1 152 ? 11.780  -14.660 -45.760  1.00 27.57 ? 245 GLY   B N   1 
ATOM   2726 C  CA  . GLY   B 1 152 ? 11.599  -14.075 -44.417  1.00 26.77 ? 245 GLY   B CA  1 
ATOM   2727 C  C   . GLY   B 1 152 ? 10.517  -14.822 -43.661  1.00 25.35 ? 245 GLY   B C   1 
ATOM   2728 O  O   . GLY   B 1 152 ? 10.611  -16.059 -43.572  1.00 25.35 ? 245 GLY   B O   1 
ATOM   2729 N  N   . MET   B 1 153 ? 9.490   -14.114 -43.184  1.00 24.41 ? 246 MET   B N   1 
ATOM   2730 C  CA  . MET   B 1 153 ? 8.374   -14.701 -42.394  1.00 23.04 ? 246 MET   B CA  1 
ATOM   2731 C  C   . MET   B 1 153 ? 7.596   -15.706 -43.253  1.00 22.45 ? 246 MET   B C   1 
ATOM   2732 O  O   . MET   B 1 153 ? 7.156   -16.727 -42.699  1.00 21.30 ? 246 MET   B O   1 
ATOM   2733 C  CB  . MET   B 1 153 ? 7.450   -13.601 -41.863  1.00 22.52 ? 246 MET   B CB  1 
ATOM   2734 C  CG  . MET   B 1 153 ? 8.143   -12.727 -40.825  1.00 22.55 ? 246 MET   B CG  1 
ATOM   2735 S  SD  . MET   B 1 153 ? 7.083   -11.429 -40.146  1.00 22.38 ? 246 MET   B SD  1 
ATOM   2736 C  CE  . MET   B 1 153 ? 7.181   -10.205 -41.453  1.00 22.61 ? 246 MET   B CE  1 
ATOM   2737 N  N   . ASN   B 1 154 ? 7.459   -15.442 -44.556  1.00 23.70 ? 247 ASN   B N   1 
ATOM   2738 C  CA  . ASN   B 1 154 ? 6.916   -16.396 -45.561  1.00 23.73 ? 247 ASN   B CA  1 
ATOM   2739 C  C   . ASN   B 1 154 ? 5.558   -16.934 -45.085  1.00 24.25 ? 247 ASN   B C   1 
ATOM   2740 O  O   . ASN   B 1 154 ? 5.388   -18.172 -45.069  1.00 22.80 ? 247 ASN   B O   1 
ATOM   2741 C  CB  . ASN   B 1 154 ? 7.892   -17.547 -45.830  1.00 24.09 ? 247 ASN   B CB  1 
ATOM   2742 C  CG  . ASN   B 1 154 ? 7.516   -18.353 -47.057  1.00 24.42 ? 247 ASN   B CG  1 
ATOM   2743 O  OD1 . ASN   B 1 154 ? 7.261   -17.784 -48.112  1.00 24.36 ? 247 ASN   B OD1 1 
ATOM   2744 N  ND2 . ASN   B 1 154 ? 7.460   -19.670 -46.932  1.00 24.78 ? 247 ASN   B ND2 1 
ATOM   2745 N  N   . ARG   B 1 155 ? 4.655   -16.025 -44.695  1.00 24.65 ? 248 ARG   B N   1 
ATOM   2746 C  CA  . ARG   B 1 155 ? 3.236   -16.278 -44.310  1.00 26.58 ? 248 ARG   B CA  1 
ATOM   2747 C  C   . ARG   B 1 155 ? 3.133   -16.911 -42.914  1.00 25.18 ? 248 ARG   B C   1 
ATOM   2748 O  O   . ARG   B 1 155 ? 2.004   -17.230 -42.509  1.00 26.66 ? 248 ARG   B O   1 
ATOM   2749 C  CB  . ARG   B 1 155 ? 2.531   -17.143 -45.361  1.00 28.23 ? 248 ARG   B CB  1 
ATOM   2750 C  CG  . ARG   B 1 155 ? 2.635   -16.589 -46.774  1.00 31.09 ? 248 ARG   B CG  1 
ATOM   2751 C  CD  . ARG   B 1 155 ? 1.845   -17.388 -47.795  1.00 33.44 ? 248 ARG   B CD  1 
ATOM   2752 N  NE  . ARG   B 1 155 ? 1.949   -16.761 -49.106  1.00 36.44 ? 248 ARG   B NE  1 
ATOM   2753 C  CZ  . ARG   B 1 155 ? 1.288   -15.669 -49.489  1.00 38.19 ? 248 ARG   B CZ  1 
ATOM   2754 N  NH1 . ARG   B 1 155 ? 0.439   -15.067 -48.669  1.00 39.14 ? 248 ARG   B NH1 1 
ATOM   2755 N  NH2 . ARG   B 1 155 ? 1.478   -15.181 -50.704  1.00 40.12 ? 248 ARG   B NH2 1 
ATOM   2756 N  N   . ARG   B 1 156 ? 4.244   -17.079 -42.190  1.00 24.08 ? 249 ARG   B N   1 
ATOM   2757 C  CA  . ARG   B 1 156 ? 4.224   -17.597 -40.798  1.00 22.93 ? 249 ARG   B CA  1 
ATOM   2758 C  C   . ARG   B 1 156 ? 3.818   -16.448 -39.881  1.00 21.77 ? 249 ARG   B C   1 
ATOM   2759 O  O   . ARG   B 1 156 ? 4.396   -15.362 -39.962  1.00 20.79 ? 249 ARG   B O   1 
ATOM   2760 C  CB  . ARG   B 1 156 ? 5.577   -18.189 -40.394  1.00 23.04 ? 249 ARG   B CB  1 
ATOM   2761 C  CG  . ARG   B 1 156 ? 6.004   -19.383 -41.235  1.00 23.41 ? 249 ARG   B CG  1 
ATOM   2762 C  CD  . ARG   B 1 156 ? 7.424   -19.809 -40.927  1.00 23.58 ? 249 ARG   B CD  1 
ATOM   2763 N  NE  . ARG   B 1 156 ? 8.401   -18.822 -41.373  1.00 23.51 ? 249 ARG   B NE  1 
ATOM   2764 C  CZ  . ARG   B 1 156 ? 9.714   -18.921 -41.193  1.00 23.41 ? 249 ARG   B CZ  1 
ATOM   2765 N  NH1 . ARG   B 1 156 ? 10.225  -19.973 -40.576  1.00 23.67 ? 249 ARG   B NH1 1 
ATOM   2766 N  NH2 . ARG   B 1 156 ? 10.515  -17.971 -41.642  1.00 24.07 ? 249 ARG   B NH2 1 
ATOM   2767 N  N   . PRO   B 1 157 ? 2.781   -16.632 -39.031  1.00 21.12 ? 250 PRO   B N   1 
ATOM   2768 C  CA  . PRO   B 1 157 ? 2.339   -15.578 -38.120  1.00 21.06 ? 250 PRO   B CA  1 
ATOM   2769 C  C   . PRO   B 1 157 ? 3.373   -15.292 -37.020  1.00 20.65 ? 250 PRO   B C   1 
ATOM   2770 O  O   . PRO   B 1 157 ? 4.038   -16.219 -36.576  1.00 19.94 ? 250 PRO   B O   1 
ATOM   2771 C  CB  . PRO   B 1 157 ? 1.033   -16.127 -37.523  1.00 21.30 ? 250 PRO   B CB  1 
ATOM   2772 C  CG  . PRO   B 1 157 ? 1.173   -17.632 -37.638  1.00 21.28 ? 250 PRO   B CG  1 
ATOM   2773 C  CD  . PRO   B 1 157 ? 1.954   -17.847 -38.920  1.00 21.25 ? 250 PRO   B CD  1 
ATOM   2774 N  N   . ILE   B 1 158 ? 3.487   -14.020 -36.628  1.00 19.65 ? 251 ILE   B N   1 
ATOM   2775 C  CA  . ILE   B 1 158 ? 4.435   -13.545 -35.578  1.00 19.36 ? 251 ILE   B CA  1 
ATOM   2776 C  C   . ILE   B 1 158 ? 3.643   -12.886 -34.448  1.00 18.87 ? 251 ILE   B C   1 
ATOM   2777 O  O   . ILE   B 1 158 ? 2.506   -12.431 -34.693  1.00 19.40 ? 251 ILE   B O   1 
ATOM   2778 C  CB  . ILE   B 1 158 ? 5.479   -12.570 -36.154  1.00 18.92 ? 251 ILE   B CB  1 
ATOM   2779 C  CG1 . ILE   B 1 158 ? 4.823   -11.337 -36.785  1.00 19.13 ? 251 ILE   B CG1 1 
ATOM   2780 C  CG2 . ILE   B 1 158 ? 6.407   -13.288 -37.121  1.00 18.68 ? 251 ILE   B CG2 1 
ATOM   2781 C  CD1 . ILE   B 1 158 ? 5.731   -10.130 -36.853  1.00 19.56 ? 251 ILE   B CD1 1 
ATOM   2782 N  N   . LEU   B 1 159 ? 4.247   -12.860 -33.262  1.00 18.75 ? 252 LEU   B N   1 
ATOM   2783 C  CA  . LEU   B 1 159 ? 3.833   -12.042 -32.098  1.00 18.74 ? 252 LEU   B CA  1 
ATOM   2784 C  C   . LEU   B 1 159 ? 4.856   -10.922 -31.926  1.00 17.91 ? 252 LEU   B C   1 
ATOM   2785 O  O   . LEU   B 1 159 ? 6.053   -11.176 -32.184  1.00 17.43 ? 252 LEU   B O   1 
ATOM   2786 C  CB  . LEU   B 1 159 ? 3.798   -12.934 -30.852  1.00 20.22 ? 252 LEU   B CB  1 
ATOM   2787 C  CG  . LEU   B 1 159 ? 2.917   -14.177 -30.953  1.00 21.54 ? 252 LEU   B CG  1 
ATOM   2788 C  CD1 . LEU   B 1 159 ? 2.858   -14.905 -29.618  1.00 22.77 ? 252 LEU   B CD1 1 
ATOM   2789 C  CD2 . LEU   B 1 159 ? 1.514   -13.812 -31.422  1.00 21.73 ? 252 LEU   B CD2 1 
ATOM   2790 N  N   . THR   B 1 160 ? 4.403   -9.728  -31.543  1.00 16.75 ? 253 THR   B N   1 
ATOM   2791 C  CA  . THR   B 1 160 ? 5.260   -8.687  -30.926  1.00 16.42 ? 253 THR   B CA  1 
ATOM   2792 C  C   . THR   B 1 160 ? 5.096   -8.805  -29.410  1.00 15.73 ? 253 THR   B C   1 
ATOM   2793 O  O   . THR   B 1 160 ? 3.945   -8.820  -28.944  1.00 14.98 ? 253 THR   B O   1 
ATOM   2794 C  CB  . THR   B 1 160 ? 4.939   -7.281  -31.445  1.00 16.37 ? 253 THR   B CB  1 
ATOM   2795 O  OG1 . THR   B 1 160 ? 5.084   -7.292  -32.866  1.00 16.19 ? 253 THR   B OG1 1 
ATOM   2796 C  CG2 . THR   B 1 160 ? 5.834   -6.217  -30.848  1.00 16.05 ? 253 THR   B CG2 1 
ATOM   2797 N  N   . ILE   B 1 161 ? 6.214   -8.918  -28.695  1.00 15.75 ? 254 ILE   B N   1 
ATOM   2798 C  CA  . ILE   B 1 161 ? 6.283   -8.870  -27.207  1.00 16.44 ? 254 ILE   B CA  1 
ATOM   2799 C  C   . ILE   B 1 161 ? 6.793   -7.483  -26.809  1.00 16.15 ? 254 ILE   B C   1 
ATOM   2800 O  O   . ILE   B 1 161 ? 7.887   -7.095  -27.263  1.00 15.16 ? 254 ILE   B O   1 
ATOM   2801 C  CB  . ILE   B 1 161 ? 7.170   -10.002 -26.654  1.00 17.00 ? 254 ILE   B CB  1 
ATOM   2802 C  CG1 . ILE   B 1 161 ? 6.776   -11.357 -27.250  1.00 17.43 ? 254 ILE   B CG1 1 
ATOM   2803 C  CG2 . ILE   B 1 161 ? 7.133   -10.019 -25.131  1.00 17.38 ? 254 ILE   B CG2 1 
ATOM   2804 C  CD1 . ILE   B 1 161 ? 7.773   -12.462 -26.995  1.00 17.88 ? 254 ILE   B CD1 1 
ATOM   2805 N  N   . ILE   B 1 162 ? 5.993   -6.764  -26.018  1.00 16.19 ? 255 ILE   B N   1 
ATOM   2806 C  CA  . ILE   B 1 162 ? 6.343   -5.443  -25.426  1.00 16.09 ? 255 ILE   B CA  1 
ATOM   2807 C  C   . ILE   B 1 162 ? 6.674   -5.692  -23.952  1.00 16.82 ? 255 ILE   B C   1 
ATOM   2808 O  O   . ILE   B 1 162 ? 5.816   -6.232  -23.240  1.00 16.19 ? 255 ILE   B O   1 
ATOM   2809 C  CB  . ILE   B 1 162 ? 5.195   -4.430  -25.608  1.00 15.93 ? 255 ILE   B CB  1 
ATOM   2810 C  CG1 . ILE   B 1 162 ? 4.686   -4.386  -27.052  1.00 15.73 ? 255 ILE   B CG1 1 
ATOM   2811 C  CG2 . ILE   B 1 162 ? 5.613   -3.049  -25.119  1.00 16.02 ? 255 ILE   B CG2 1 
ATOM   2812 C  CD1 . ILE   B 1 162 ? 5.756   -4.076  -28.082  1.00 15.59 ? 255 ILE   B CD1 1 
ATOM   2813 N  N   . THR   B 1 163 ? 7.889   -5.353  -23.528  1.00 17.16 ? 256 THR   B N   1 
ATOM   2814 C  CA  . THR   B 1 163 ? 8.341   -5.499  -22.125  1.00 17.90 ? 256 THR   B CA  1 
ATOM   2815 C  C   . THR   B 1 163 ? 8.666   -4.118  -21.565  1.00 18.28 ? 256 THR   B C   1 
ATOM   2816 O  O   . THR   B 1 163 ? 9.295   -3.321  -22.278  1.00 17.02 ? 256 THR   B O   1 
ATOM   2817 C  CB  . THR   B 1 163 ? 9.533   -6.452  -22.015  1.00 18.84 ? 256 THR   B CB  1 
ATOM   2818 O  OG1 . THR   B 1 163 ? 10.510  -6.018  -22.957  1.00 19.10 ? 256 THR   B OG1 1 
ATOM   2819 C  CG2 . THR   B 1 163 ? 9.164   -7.890  -22.295  1.00 19.32 ? 256 THR   B CG2 1 
ATOM   2820 N  N   . LEU   B 1 164 ? 8.202   -3.847  -20.346  1.00 18.77 ? 257 LEU   B N   1 
ATOM   2821 C  CA  . LEU   B 1 164 ? 8.585   -2.654  -19.553  1.00 19.26 ? 257 LEU   B CA  1 
ATOM   2822 C  C   . LEU   B 1 164 ? 9.731   -3.089  -18.636  1.00 18.80 ? 257 LEU   B C   1 
ATOM   2823 O  O   . LEU   B 1 164 ? 9.553   -4.103  -17.939  1.00 18.37 ? 257 LEU   B O   1 
ATOM   2824 C  CB  . LEU   B 1 164 ? 7.356   -2.188  -18.768  1.00 20.52 ? 257 LEU   B CB  1 
ATOM   2825 C  CG  . LEU   B 1 164 ? 7.382   -0.758  -18.235  1.00 21.59 ? 257 LEU   B CG  1 
ATOM   2826 C  CD1 . LEU   B 1 164 ? 7.449   0.256   -19.365  1.00 22.18 ? 257 LEU   B CD1 1 
ATOM   2827 C  CD2 . LEU   B 1 164 ? 6.158   -0.498  -17.367  1.00 21.95 ? 257 LEU   B CD2 1 
ATOM   2828 N  N   . GLU   B 1 165 ? 10.882  -2.415  -18.701  1.00 18.73 ? 258 GLU   B N   1 
ATOM   2829 C  CA  . GLU   B 1 165 ? 12.062  -2.726  -17.847  1.00 19.56 ? 258 GLU   B CA  1 
ATOM   2830 C  C   . GLU   B 1 165 ? 12.550  -1.437  -17.184  1.00 19.47 ? 258 GLU   B C   1 
ATOM   2831 O  O   . GLU   B 1 165 ? 12.343  -0.356  -17.763  1.00 19.46 ? 258 GLU   B O   1 
ATOM   2832 C  CB  . GLU   B 1 165 ? 13.195  -3.421  -18.615  1.00 20.41 ? 258 GLU   B CB  1 
ATOM   2833 C  CG  . GLU   B 1 165 ? 13.021  -3.480  -20.121  1.00 21.95 ? 258 GLU   B CG  1 
ATOM   2834 C  CD  . GLU   B 1 165 ? 14.152  -4.165  -20.876  1.00 22.54 ? 258 GLU   B CD  1 
ATOM   2835 O  OE1 . GLU   B 1 165 ? 13.885  -5.191  -21.542  1.00 23.77 ? 258 GLU   B OE1 1 
ATOM   2836 O  OE2 . GLU   B 1 165 ? 15.291  -3.671  -20.812  1.00 23.44 ? 258 GLU   B OE2 1 
ATOM   2837 N  N   . ASP   B 1 166 ? 13.158  -1.555  -16.000  1.00 19.51 ? 259 ASP   B N   1 
ATOM   2838 C  CA  . ASP   B 1 166 ? 13.753  -0.402  -15.277  1.00 20.03 ? 259 ASP   B CA  1 
ATOM   2839 C  C   . ASP   B 1 166 ? 15.127  -0.138  -15.900  1.00 20.39 ? 259 ASP   B C   1 
ATOM   2840 O  O   . ASP   B 1 166 ? 15.526  -0.903  -16.804  1.00 19.71 ? 259 ASP   B O   1 
ATOM   2841 C  CB  . ASP   B 1 166 ? 13.785  -0.623  -13.760  1.00 19.94 ? 259 ASP   B CB  1 
ATOM   2842 C  CG  . ASP   B 1 166 ? 14.770  -1.672  -13.267  1.00 20.26 ? 259 ASP   B CG  1 
ATOM   2843 O  OD1 . ASP   B 1 166 ? 15.553  -2.185  -14.080  1.00 20.22 ? 259 ASP   B OD1 1 
ATOM   2844 O  OD2 . ASP   B 1 166 ? 14.733  -1.979  -12.065  1.00 20.64 ? 259 ASP   B OD2 1 
ATOM   2845 N  N   . SER   B 1 167 ? 15.818  0.903   -15.440  1.00 21.06 ? 260 SER   B N   1 
ATOM   2846 C  CA  . SER   B 1 167 ? 17.119  1.360   -15.995  1.00 21.66 ? 260 SER   B CA  1 
ATOM   2847 C  C   . SER   B 1 167 ? 18.207  0.292   -15.811  1.00 22.11 ? 260 SER   B C   1 
ATOM   2848 O  O   . SER   B 1 167 ? 19.256  0.420   -16.475  1.00 23.63 ? 260 SER   B O   1 
ATOM   2849 C  CB  . SER   B 1 167 ? 17.534  2.659   -15.372  1.00 22.25 ? 260 SER   B CB  1 
ATOM   2850 O  OG  . SER   B 1 167 ? 17.648  2.514   -13.966  1.00 22.33 ? 260 SER   B OG  1 
ATOM   2851 N  N   . SER   B 1 168 ? 17.987  -0.702  -14.940  1.00 21.77 ? 261 SER   B N   1 
ATOM   2852 C  CA  . SER   B 1 168 ? 18.947  -1.797  -14.631  1.00 21.83 ? 261 SER   B CA  1 
ATOM   2853 C  C   . SER   B 1 168 ? 18.574  -3.091  -15.367  1.00 20.73 ? 261 SER   B C   1 
ATOM   2854 O  O   . SER   B 1 168 ? 19.289  -4.094  -15.185  1.00 20.13 ? 261 SER   B O   1 
ATOM   2855 C  CB  . SER   B 1 168 ? 19.033  -2.029  -13.145  1.00 22.67 ? 261 SER   B CB  1 
ATOM   2856 O  OG  . SER   B 1 168 ? 19.474  -0.853  -12.488  1.00 24.23 ? 261 SER   B OG  1 
ATOM   2857 N  N   . GLY   B 1 169 ? 17.509  -3.076  -16.171  1.00 19.98 ? 262 GLY   B N   1 
ATOM   2858 C  CA  . GLY   B 1 169 ? 17.097  -4.219  -17.005  1.00 19.76 ? 262 GLY   B CA  1 
ATOM   2859 C  C   . GLY   B 1 169 ? 16.196  -5.196  -16.270  1.00 19.81 ? 262 GLY   B C   1 
ATOM   2860 O  O   . GLY   B 1 169 ? 15.946  -6.277  -16.822  1.00 20.42 ? 262 GLY   B O   1 
ATOM   2861 N  N   . ASN   B 1 170 ? 15.693  -4.841  -15.083  1.00 19.99 ? 263 ASN   B N   1 
ATOM   2862 C  CA  . ASN   B 1 170 ? 14.734  -5.696  -14.335  1.00 20.10 ? 263 ASN   B CA  1 
ATOM   2863 C  C   . ASN   B 1 170 ? 13.380  -5.647  -15.054  1.00 20.59 ? 263 ASN   B C   1 
ATOM   2864 O  O   . ASN   B 1 170 ? 12.933  -4.543  -15.402  1.00 20.49 ? 263 ASN   B O   1 
ATOM   2865 C  CB  . ASN   B 1 170 ? 14.619  -5.297  -12.861  1.00 19.57 ? 263 ASN   B CB  1 
ATOM   2866 C  CG  . ASN   B 1 170 ? 15.922  -5.438  -12.102  1.00 19.66 ? 263 ASN   B CG  1 
ATOM   2867 O  OD1 . ASN   B 1 170 ? 16.474  -6.533  -12.000  1.00 19.36 ? 263 ASN   B OD1 1 
ATOM   2868 N  ND2 . ASN   B 1 170 ? 16.415  -4.339  -11.557  1.00 19.22 ? 263 ASN   B ND2 1 
ATOM   2869 N  N   . LEU   B 1 171 ? 12.764  -6.811  -15.272  1.00 21.65 ? 264 LEU   B N   1 
ATOM   2870 C  CA  . LEU   B 1 171 ? 11.420  -6.953  -15.894  1.00 21.55 ? 264 LEU   B CA  1 
ATOM   2871 C  C   . LEU   B 1 171 ? 10.356  -6.354  -14.964  1.00 21.02 ? 264 LEU   B C   1 
ATOM   2872 O  O   . LEU   B 1 171 ? 10.277  -6.798  -13.805  1.00 21.36 ? 264 LEU   B O   1 
ATOM   2873 C  CB  . LEU   B 1 171 ? 11.164  -8.441  -16.152  1.00 22.53 ? 264 LEU   B CB  1 
ATOM   2874 C  CG  . LEU   B 1 171 ? 9.840   -8.784  -16.831  1.00 23.47 ? 264 LEU   B CG  1 
ATOM   2875 C  CD1 . LEU   B 1 171 ? 9.771   -8.182  -18.227  1.00 23.70 ? 264 LEU   B CD1 1 
ATOM   2876 C  CD2 . LEU   B 1 171 ? 9.646   -10.295 -16.885  1.00 24.25 ? 264 LEU   B CD2 1 
ATOM   2877 N  N   . LEU   B 1 172 ? 9.575   -5.384  -15.455  1.00 19.90 ? 265 LEU   B N   1 
ATOM   2878 C  CA  . LEU   B 1 172 ? 8.455   -4.742  -14.707  1.00 19.01 ? 265 LEU   B CA  1 
ATOM   2879 C  C   . LEU   B 1 172 ? 7.107   -5.256  -15.220  1.00 18.38 ? 265 LEU   B C   1 
ATOM   2880 O  O   . LEU   B 1 172 ? 6.155   -5.284  -14.423  1.00 17.54 ? 265 LEU   B O   1 
ATOM   2881 C  CB  . LEU   B 1 172 ? 8.514   -3.220  -14.873  1.00 18.87 ? 265 LEU   B CB  1 
ATOM   2882 C  CG  . LEU   B 1 172 ? 9.848   -2.550  -14.554  1.00 19.01 ? 265 LEU   B CG  1 
ATOM   2883 C  CD1 . LEU   B 1 172 ? 9.734   -1.043  -14.729  1.00 19.19 ? 265 LEU   B CD1 1 
ATOM   2884 C  CD2 . LEU   B 1 172 ? 10.316  -2.893  -13.147  1.00 19.59 ? 265 LEU   B CD2 1 
ATOM   2885 N  N   . GLY   B 1 173 ? 7.012   -5.592  -16.510  1.00 17.49 ? 266 GLY   B N   1 
ATOM   2886 C  CA  . GLY   B 1 173 ? 5.727   -5.918  -17.155  1.00 17.51 ? 266 GLY   B CA  1 
ATOM   2887 C  C   . GLY   B 1 173 ? 5.922   -6.467  -18.555  1.00 17.38 ? 266 GLY   B C   1 
ATOM   2888 O  O   . GLY   B 1 173 ? 6.927   -6.111  -19.197  1.00 16.41 ? 266 GLY   B O   1 
ATOM   2889 N  N   . ARG   B 1 174 ? 4.991   -7.308  -19.006  1.00 17.84 ? 267 ARG   B N   1 
ATOM   2890 C  CA  . ARG   B 1 174 ? 5.030   -7.924  -20.356  1.00 18.65 ? 267 ARG   B CA  1 
ATOM   2891 C  C   . ARG   B 1 174 ? 3.614   -8.072  -20.913  1.00 18.21 ? 267 ARG   B C   1 
ATOM   2892 O  O   . ARG   B 1 174 ? 2.707   -8.500  -20.162  1.00 17.36 ? 267 ARG   B O   1 
ATOM   2893 C  CB  . ARG   B 1 174 ? 5.729   -9.284  -20.335  1.00 20.03 ? 267 ARG   B CB  1 
ATOM   2894 C  CG  . ARG   B 1 174 ? 5.982   -9.826  -21.734  1.00 21.31 ? 267 ARG   B CG  1 
ATOM   2895 C  CD  . ARG   B 1 174 ? 6.478   -11.254 -21.774  1.00 23.06 ? 267 ARG   B CD  1 
ATOM   2896 N  NE  . ARG   B 1 174 ? 7.739   -11.457 -21.075  1.00 24.27 ? 267 ARG   B NE  1 
ATOM   2897 C  CZ  . ARG   B 1 174 ? 7.887   -12.053 -19.893  1.00 25.18 ? 267 ARG   B CZ  1 
ATOM   2898 N  NH1 . ARG   B 1 174 ? 6.842   -12.512 -19.222  1.00 25.26 ? 267 ARG   B NH1 1 
ATOM   2899 N  NH2 . ARG   B 1 174 ? 9.098   -12.195 -19.384  1.00 25.91 ? 267 ARG   B NH2 1 
ATOM   2900 N  N   . ASN   B 1 175 ? 3.456   -7.737  -22.195  1.00 17.82 ? 268 ASN   B N   1 
ATOM   2901 C  CA  . ASN   B 1 175 ? 2.210   -7.938  -22.977  1.00 18.47 ? 268 ASN   B CA  1 
ATOM   2902 C  C   . ASN   B 1 175 ? 2.610   -8.324  -24.402  1.00 17.60 ? 268 ASN   B C   1 
ATOM   2903 O  O   . ASN   B 1 175 ? 3.787   -8.108  -24.776  1.00 17.04 ? 268 ASN   B O   1 
ATOM   2904 C  CB  . ASN   B 1 175 ? 1.316   -6.696  -22.939  1.00 19.50 ? 268 ASN   B CB  1 
ATOM   2905 C  CG  . ASN   B 1 175 ? 0.499   -6.574  -21.666  1.00 21.20 ? 268 ASN   B CG  1 
ATOM   2906 O  OD1 . ASN   B 1 175 ? -0.483  -7.293  -21.477  1.00 22.84 ? 268 ASN   B OD1 1 
ATOM   2907 N  ND2 . ASN   B 1 175 ? 0.884   -5.656  -20.791  1.00 20.87 ? 268 ASN   B ND2 1 
ATOM   2908 N  N   . SER   B 1 176 ? 1.675   -8.882  -25.169  1.00 17.10 ? 269 SER   B N   1 
ATOM   2909 C  CA  . SER   B 1 176 ? 1.942   -9.336  -26.554  1.00 16.71 ? 269 SER   B CA  1 
ATOM   2910 C  C   . SER   B 1 176 ? 0.685   -9.210  -27.412  1.00 16.00 ? 269 SER   B C   1 
ATOM   2911 O  O   . SER   B 1 176 ? -0.431  -9.149  -26.865  1.00 15.37 ? 269 SER   B O   1 
ATOM   2912 C  CB  . SER   B 1 176 ? 2.471   -10.744 -26.564  1.00 16.79 ? 269 SER   B CB  1 
ATOM   2913 O  OG  . SER   B 1 176 ? 1.528   -11.624 -25.978  1.00 17.09 ? 269 SER   B OG  1 
ATOM   2914 N  N   . PHE   B 1 177 ? 0.891   -9.168  -28.722  1.00 15.71 ? 270 PHE   B N   1 
ATOM   2915 C  CA  . PHE   B 1 177 ? -0.175  -9.148  -29.748  1.00 16.03 ? 270 PHE   B CA  1 
ATOM   2916 C  C   . PHE   B 1 177 ? 0.380   -9.789  -31.017  1.00 16.46 ? 270 PHE   B C   1 
ATOM   2917 O  O   . PHE   B 1 177 ? 1.581   -9.640  -31.283  1.00 16.36 ? 270 PHE   B O   1 
ATOM   2918 C  CB  . PHE   B 1 177 ? -0.672  -7.719  -29.992  1.00 16.00 ? 270 PHE   B CB  1 
ATOM   2919 C  CG  . PHE   B 1 177 ? 0.384   -6.723  -30.398  1.00 16.10 ? 270 PHE   B CG  1 
ATOM   2920 C  CD1 . PHE   B 1 177 ? 1.111   -6.037  -29.437  1.00 16.13 ? 270 PHE   B CD1 1 
ATOM   2921 C  CD2 . PHE   B 1 177 ? 0.619   -6.431  -31.734  1.00 16.37 ? 270 PHE   B CD2 1 
ATOM   2922 C  CE1 . PHE   B 1 177 ? 2.071   -5.106  -29.804  1.00 16.62 ? 270 PHE   B CE1 1 
ATOM   2923 C  CE2 . PHE   B 1 177 ? 1.581   -5.499  -32.100  1.00 16.37 ? 270 PHE   B CE2 1 
ATOM   2924 C  CZ  . PHE   B 1 177 ? 2.302   -4.836  -31.134  1.00 16.82 ? 270 PHE   B CZ  1 
ATOM   2925 N  N   . GLU   B 1 178 ? -0.477  -10.502 -31.748  1.00 17.38 ? 271 GLU   B N   1 
ATOM   2926 C  CA  . GLU   B 1 178 ? -0.168  -11.046 -33.091  1.00 17.83 ? 271 GLU   B CA  1 
ATOM   2927 C  C   . GLU   B 1 178 ? -0.100  -9.868  -34.063  1.00 17.83 ? 271 GLU   B C   1 
ATOM   2928 O  O   . GLU   B 1 178 ? -0.804  -8.860  -33.824  1.00 16.59 ? 271 GLU   B O   1 
ATOM   2929 C  CB  . GLU   B 1 178 ? -1.214  -12.082 -33.508  1.00 18.53 ? 271 GLU   B CB  1 
ATOM   2930 C  CG  . GLU   B 1 178 ? -0.845  -12.820 -34.783  1.00 19.39 ? 271 GLU   B CG  1 
ATOM   2931 C  CD  . GLU   B 1 178 ? -1.757  -13.983 -35.143  1.00 20.10 ? 271 GLU   B CD  1 
ATOM   2932 O  OE1 . GLU   B 1 178 ? -2.516  -14.442 -34.264  1.00 20.08 ? 271 GLU   B OE1 1 
ATOM   2933 O  OE2 . GLU   B 1 178 ? -1.715  -14.412 -36.309  1.00 21.60 ? 271 GLU   B OE2 1 
ATOM   2934 N  N   . VAL   B 1 179 ? 0.730   -9.986  -35.102  1.00 18.20 ? 272 VAL   B N   1 
ATOM   2935 C  CA  . VAL   B 1 179 ? 0.890   -8.945  -36.158  1.00 19.12 ? 272 VAL   B CA  1 
ATOM   2936 C  C   . VAL   B 1 179 ? 0.821   -9.617  -37.526  1.00 19.45 ? 272 VAL   B C   1 
ATOM   2937 O  O   . VAL   B 1 179 ? 1.455   -10.676 -37.701  1.00 19.14 ? 272 VAL   B O   1 
ATOM   2938 C  CB  . VAL   B 1 179 ? 2.203   -8.157  -36.008  1.00 20.25 ? 272 VAL   B CB  1 
ATOM   2939 C  CG1 . VAL   B 1 179 ? 2.372   -7.143  -37.131  1.00 20.93 ? 272 VAL   B CG1 1 
ATOM   2940 C  CG2 . VAL   B 1 179 ? 2.289   -7.476  -34.655  1.00 20.89 ? 272 VAL   B CG2 1 
ATOM   2941 N  N   . ARG   B 1 180 ? 0.072   -9.010  -38.446  1.00 19.51 ? 273 ARG   B N   1 
ATOM   2942 C  CA  . ARG   B 1 180 ? 0.158   -9.292  -39.898  1.00 19.77 ? 273 ARG   B CA  1 
ATOM   2943 C  C   . ARG   B 1 180 ? 0.553   -7.998  -40.617  1.00 19.39 ? 273 ARG   B C   1 
ATOM   2944 O  O   . ARG   B 1 180 ? -0.188  -6.997  -40.513  1.00 18.63 ? 273 ARG   B O   1 
ATOM   2945 C  CB  . ARG   B 1 180 ? -1.166  -9.865  -40.405  1.00 21.02 ? 273 ARG   B CB  1 
ATOM   2946 C  CG  . ARG   B 1 180 ? -1.200  -10.140 -41.900  1.00 22.65 ? 273 ARG   B CG  1 
ATOM   2947 C  CD  . ARG   B 1 180 ? -2.538  -10.726 -42.302  1.00 23.36 ? 273 ARG   B CD  1 
ATOM   2948 N  NE  . ARG   B 1 180 ? -2.727  -10.754 -43.744  1.00 25.07 ? 273 ARG   B NE  1 
ATOM   2949 C  CZ  . ARG   B 1 180 ? -2.260  -11.688 -44.568  1.00 26.99 ? 273 ARG   B CZ  1 
ATOM   2950 N  NH1 . ARG   B 1 180 ? -1.533  -12.697 -44.111  1.00 28.67 ? 273 ARG   B NH1 1 
ATOM   2951 N  NH2 . ARG   B 1 180 ? -2.525  -11.605 -45.861  1.00 27.65 ? 273 ARG   B NH2 1 
ATOM   2952 N  N   . VAL   B 1 181 ? 1.687   -8.023  -41.321  1.00 18.66 ? 274 VAL   B N   1 
ATOM   2953 C  CA  . VAL   B 1 181 ? 2.155   -6.900  -42.183  1.00 18.70 ? 274 VAL   B CA  1 
ATOM   2954 C  C   . VAL   B 1 181 ? 1.695   -7.211  -43.608  1.00 18.73 ? 274 VAL   B C   1 
ATOM   2955 O  O   . VAL   B 1 181 ? 2.143   -8.241  -44.155  1.00 18.65 ? 274 VAL   B O   1 
ATOM   2956 C  CB  . VAL   B 1 181 ? 3.683   -6.718  -42.096  1.00 18.40 ? 274 VAL   B CB  1 
ATOM   2957 C  CG1 . VAL   B 1 181 ? 4.117   -5.426  -42.772  1.00 18.50 ? 274 VAL   B CG1 1 
ATOM   2958 C  CG2 . VAL   B 1 181 ? 4.177   -6.770  -40.655  1.00 18.36 ? 274 VAL   B CG2 1 
ATOM   2959 N  N   . CYS   B 1 182 ? 0.810   -6.386  -44.171  1.00 19.91 ? 275 CYS   B N   1 
ATOM   2960 C  CA  . CYS   B 1 182 ? 0.060   -6.713  -45.416  1.00 20.19 ? 275 CYS   B CA  1 
ATOM   2961 C  C   . CYS   B 1 182 ? -0.365  -5.436  -46.151  1.00 20.52 ? 275 CYS   B C   1 
ATOM   2962 O  O   . CYS   B 1 182 ? -0.323  -4.350  -45.540  1.00 20.42 ? 275 CYS   B O   1 
ATOM   2963 C  CB  . CYS   B 1 182 ? -1.136  -7.600  -45.087  1.00 20.42 ? 275 CYS   B CB  1 
ATOM   2964 S  SG  . CYS   B 1 182 ? -2.280  -6.876  -43.884  1.00 20.80 ? 275 CYS   B SG  1 
ATOM   2965 N  N   . ALA   B 1 183 ? -0.767  -5.576  -47.418  1.00 20.71 ? 276 ALA   B N   1 
ATOM   2966 C  CA  . ALA   B 1 183 ? -1.067  -4.458  -48.344  1.00 20.86 ? 276 ALA   B CA  1 
ATOM   2967 C  C   . ALA   B 1 183 ? -2.389  -3.769  -47.972  1.00 21.23 ? 276 ALA   B C   1 
ATOM   2968 O  O   . ALA   B 1 183 ? -2.475  -2.541  -48.142  1.00 21.81 ? 276 ALA   B O   1 
ATOM   2969 C  CB  . ALA   B 1 183 ? -1.092  -4.959  -49.766  1.00 20.98 ? 276 ALA   B CB  1 
ATOM   2970 N  N   A CYS   B 1 184 ? -3.371  -4.531  -47.476  0.50 21.13 ? 277 CYS   B N   1 
ATOM   2971 N  N   B CYS   B 1 184 ? -3.384  -4.534  -47.500  0.50 21.41 ? 277 CYS   B N   1 
ATOM   2972 C  CA  A CYS   B 1 184 ? -4.737  -4.041  -47.140  0.50 21.03 ? 277 CYS   B CA  1 
ATOM   2973 C  CA  B CYS   B 1 184 ? -4.749  -4.048  -47.143  0.50 21.46 ? 277 CYS   B CA  1 
ATOM   2974 C  C   A CYS   B 1 184 ? -5.139  -4.512  -45.745  0.50 20.55 ? 277 CYS   B C   1 
ATOM   2975 C  C   B CYS   B 1 184 ? -5.132  -4.520  -45.743  0.50 20.79 ? 277 CYS   B C   1 
ATOM   2976 O  O   A CYS   B 1 184 ? -5.929  -5.444  -45.612  0.50 20.53 ? 277 CYS   B O   1 
ATOM   2977 O  O   B CYS   B 1 184 ? -5.906  -5.465  -45.603  0.50 20.76 ? 277 CYS   B O   1 
ATOM   2978 C  CB  A CYS   B 1 184 ? -5.754  -4.530  -48.163  0.50 21.16 ? 277 CYS   B CB  1 
ATOM   2979 C  CB  B CYS   B 1 184 ? -5.798  -4.557  -48.125  0.50 21.86 ? 277 CYS   B CB  1 
ATOM   2980 S  SG  A CYS   B 1 184 ? -7.146  -3.392  -48.378  0.50 21.26 ? 277 CYS   B SG  1 
ATOM   2981 S  SG  B CYS   B 1 184 ? -5.247  -4.543  -49.850  0.50 22.63 ? 277 CYS   B SG  1 
ATOM   2982 N  N   . PRO   B 1 185 ? -4.612  -3.882  -44.669  1.00 20.32 ? 278 PRO   B N   1 
ATOM   2983 C  CA  . PRO   B 1 185 ? -4.915  -4.305  -43.299  1.00 20.18 ? 278 PRO   B CA  1 
ATOM   2984 C  C   . PRO   B 1 185 ? -6.414  -4.375  -42.964  1.00 19.69 ? 278 PRO   B C   1 
ATOM   2985 O  O   . PRO   B 1 185 ? -6.814  -5.323  -42.309  1.00 18.79 ? 278 PRO   B O   1 
ATOM   2986 C  CB  . PRO   B 1 185 ? -4.259  -3.214  -42.435  1.00 20.30 ? 278 PRO   B CB  1 
ATOM   2987 C  CG  . PRO   B 1 185 ? -3.165  -2.645  -43.303  1.00 20.33 ? 278 PRO   B CG  1 
ATOM   2988 C  CD  . PRO   B 1 185 ? -3.695  -2.731  -44.720  1.00 20.31 ? 278 PRO   B CD  1 
ATOM   2989 N  N   . GLY   B 1 186 ? -7.191  -3.386  -43.421  1.00 19.62 ? 279 GLY   B N   1 
ATOM   2990 C  CA  . GLY   B 1 186 ? -8.649  -3.300  -43.201  1.00 20.03 ? 279 GLY   B CA  1 
ATOM   2991 C  C   . GLY   B 1 186 ? -9.374  -4.539  -43.704  1.00 20.69 ? 279 GLY   B C   1 
ATOM   2992 O  O   . GLY   B 1 186 ? -10.088 -5.175  -42.907  1.00 19.79 ? 279 GLY   B O   1 
ATOM   2993 N  N   . ARG   B 1 187 ? -9.195  -4.870  -44.985  1.00 22.05 ? 280 ARG   B N   1 
ATOM   2994 C  CA  . ARG   B 1 187 ? -9.808  -6.052  -45.644  1.00 23.05 ? 280 ARG   B CA  1 
ATOM   2995 C  C   . ARG   B 1 187 ? -9.360  -7.324  -44.912  1.00 21.50 ? 280 ARG   B C   1 
ATOM   2996 O  O   . ARG   B 1 187 ? -10.212 -8.187  -44.655  1.00 21.40 ? 280 ARG   B O   1 
ATOM   2997 C  CB  . ARG   B 1 187 ? -9.427  -6.073  -47.130  1.00 25.78 ? 280 ARG   B CB  1 
ATOM   2998 C  CG  . ARG   B 1 187 ? -10.062 -7.197  -47.940  1.00 28.46 ? 280 ARG   B CG  1 
ATOM   2999 C  CD  . ARG   B 1 187 ? -9.318  -7.452  -49.241  1.00 31.59 ? 280 ARG   B CD  1 
ATOM   3000 N  NE  . ARG   B 1 187 ? -7.929  -7.840  -48.996  1.00 35.23 ? 280 ARG   B NE  1 
ATOM   3001 C  CZ  . ARG   B 1 187 ? -6.946  -7.818  -49.897  1.00 37.03 ? 280 ARG   B CZ  1 
ATOM   3002 N  NH1 . ARG   B 1 187 ? -7.174  -7.419  -51.139  1.00 38.46 ? 280 ARG   B NH1 1 
ATOM   3003 N  NH2 . ARG   B 1 187 ? -5.726  -8.190  -49.543  1.00 37.54 ? 280 ARG   B NH2 1 
ATOM   3004 N  N   . ASP   B 1 188 ? -8.070  -7.441  -44.591  1.00 20.83 ? 281 ASP   B N   1 
ATOM   3005 C  CA  . ASP   B 1 188 ? -7.487  -8.671  -43.988  1.00 20.50 ? 281 ASP   B CA  1 
ATOM   3006 C  C   . ASP   B 1 188 ? -8.046  -8.866  -42.572  1.00 19.56 ? 281 ASP   B C   1 
ATOM   3007 O  O   . ASP   B 1 188 ? -8.343  -10.018 -42.217  1.00 17.92 ? 281 ASP   B O   1 
ATOM   3008 C  CB  . ASP   B 1 188 ? -5.959  -8.642  -44.051  1.00 21.51 ? 281 ASP   B CB  1 
ATOM   3009 C  CG  . ASP   B 1 188 ? -5.427  -8.910  -45.450  1.00 22.27 ? 281 ASP   B CG  1 
ATOM   3010 O  OD1 . ASP   B 1 188 ? -6.246  -9.193  -46.338  1.00 23.84 ? 281 ASP   B OD1 1 
ATOM   3011 O  OD2 . ASP   B 1 188 ? -4.205  -8.820  -45.644  1.00 23.97 ? 281 ASP   B OD2 1 
ATOM   3012 N  N   . ARG   B 1 189 ? -8.221  -7.788  -41.803  1.00 18.79 ? 282 ARG   B N   1 
ATOM   3013 C  CA  . ARG   B 1 189 ? -8.871  -7.858  -40.467  1.00 19.16 ? 282 ARG   B CA  1 
ATOM   3014 C  C   . ARG   B 1 189 ? -10.306 -8.390  -40.631  1.00 19.52 ? 282 ARG   B C   1 
ATOM   3015 O  O   . ARG   B 1 189 ? -10.673 -9.342  -39.910  1.00 19.51 ? 282 ARG   B O   1 
ATOM   3016 C  CB  . ARG   B 1 189 ? -8.856  -6.497  -39.766  1.00 18.25 ? 282 ARG   B CB  1 
ATOM   3017 C  CG  . ARG   B 1 189 ? -9.643  -6.493  -38.465  1.00 18.12 ? 282 ARG   B CG  1 
ATOM   3018 C  CD  . ARG   B 1 189 ? -9.443  -5.258  -37.616  1.00 17.94 ? 282 ARG   B CD  1 
ATOM   3019 N  NE  . ARG   B 1 189 ? -10.525 -5.173  -36.646  1.00 17.68 ? 282 ARG   B NE  1 
ATOM   3020 C  CZ  . ARG   B 1 189 ? -10.918 -4.071  -36.023  1.00 17.76 ? 282 ARG   B CZ  1 
ATOM   3021 N  NH1 . ARG   B 1 189 ? -10.323 -2.913  -36.258  1.00 17.96 ? 282 ARG   B NH1 1 
ATOM   3022 N  NH2 . ARG   B 1 189 ? -11.921 -4.132  -35.162  1.00 18.02 ? 282 ARG   B NH2 1 
ATOM   3023 N  N   . ARG   B 1 190 ? -11.095 -7.789  -41.526  1.00 20.97 ? 283 ARG   B N   1 
ATOM   3024 C  CA  . ARG   B 1 190 ? -12.501 -8.207  -41.795  1.00 21.36 ? 283 ARG   B CA  1 
ATOM   3025 C  C   . ARG   B 1 190 ? -12.521 -9.706  -42.117  1.00 21.91 ? 283 ARG   B C   1 
ATOM   3026 O  O   . ARG   B 1 190 ? -13.288 -10.444 -41.459  1.00 22.48 ? 283 ARG   B O   1 
ATOM   3027 C  CB  . ARG   B 1 190 ? -13.113 -7.421  -42.957  1.00 21.54 ? 283 ARG   B CB  1 
ATOM   3028 C  CG  . ARG   B 1 190 ? -13.568 -6.014  -42.607  1.00 21.55 ? 283 ARG   B CG  1 
ATOM   3029 C  CD  . ARG   B 1 190 ? -14.180 -5.314  -43.804  1.00 21.23 ? 283 ARG   B CD  1 
ATOM   3030 N  NE  . ARG   B 1 190 ? -14.061 -3.866  -43.707  1.00 21.23 ? 283 ARG   B NE  1 
ATOM   3031 C  CZ  . ARG   B 1 190 ? -14.382 -3.007  -44.670  1.00 21.52 ? 283 ARG   B CZ  1 
ATOM   3032 N  NH1 . ARG   B 1 190 ? -14.851 -3.439  -45.828  1.00 22.15 ? 283 ARG   B NH1 1 
ATOM   3033 N  NH2 . ARG   B 1 190 ? -14.231 -1.710  -44.472  1.00 21.70 ? 283 ARG   B NH2 1 
ATOM   3034 N  N   . THR   B 1 191 ? -11.696 -10.131 -43.081  1.00 22.99 ? 284 THR   B N   1 
ATOM   3035 C  CA  . THR   B 1 191 ? -11.593 -11.539 -43.559  1.00 23.64 ? 284 THR   B CA  1 
ATOM   3036 C  C   . THR   B 1 191 ? -11.291 -12.475 -42.381  1.00 23.98 ? 284 THR   B C   1 
ATOM   3037 O  O   . THR   B 1 191 ? -11.986 -13.493 -42.257  1.00 24.91 ? 284 THR   B O   1 
ATOM   3038 C  CB  . THR   B 1 191 ? -10.538 -11.684 -44.667  1.00 23.99 ? 284 THR   B CB  1 
ATOM   3039 O  OG1 . THR   B 1 191 ? -10.848 -10.781 -45.729  1.00 23.82 ? 284 THR   B OG1 1 
ATOM   3040 C  CG2 . THR   B 1 191 ? -10.453 -13.092 -45.218  1.00 24.56 ? 284 THR   B CG2 1 
ATOM   3041 N  N   . GLU   B 1 192 ? -10.289 -12.156 -41.552  1.00 24.12 ? 285 GLU   B N   1 
ATOM   3042 C  CA  . GLU   B 1 192 ? -9.818  -13.053 -40.458  1.00 24.52 ? 285 GLU   B CA  1 
ATOM   3043 C  C   . GLU   B 1 192 ? -10.840 -13.073 -39.314  1.00 24.70 ? 285 GLU   B C   1 
ATOM   3044 O  O   . GLU   B 1 192 ? -10.844 -14.061 -38.564  1.00 25.63 ? 285 GLU   B O   1 
ATOM   3045 C  CB  . GLU   B 1 192 ? -8.432  -12.641 -39.963  1.00 24.10 ? 285 GLU   B CB  1 
ATOM   3046 C  CG  . GLU   B 1 192 ? -7.335  -12.959 -40.960  1.00 23.60 ? 285 GLU   B CG  1 
ATOM   3047 C  CD  . GLU   B 1 192 ? -5.923  -12.981 -40.407  1.00 23.48 ? 285 GLU   B CD  1 
ATOM   3048 O  OE1 . GLU   B 1 192 ? -5.762  -13.216 -39.199  1.00 23.26 ? 285 GLU   B OE1 1 
ATOM   3049 O  OE2 . GLU   B 1 192 ? -4.985  -12.768 -41.199  1.00 23.71 ? 285 GLU   B OE2 1 
ATOM   3050 N  N   . GLU   B 1 193 ? -11.671 -12.035 -39.188  1.00 24.97 ? 286 GLU   B N   1 
ATOM   3051 C  CA  . GLU   B 1 193 ? -12.749 -11.951 -38.163  1.00 26.04 ? 286 GLU   B CA  1 
ATOM   3052 C  C   . GLU   B 1 193 ? -14.003 -12.688 -38.658  1.00 28.89 ? 286 GLU   B C   1 
ATOM   3053 O  O   . GLU   B 1 193 ? -14.791 -13.148 -37.805  1.00 26.90 ? 286 GLU   B O   1 
ATOM   3054 C  CB  . GLU   B 1 193 ? -13.057 -10.493 -37.828  1.00 24.41 ? 286 GLU   B CB  1 
ATOM   3055 C  CG  . GLU   B 1 193 ? -11.999 -9.846  -36.953  1.00 23.76 ? 286 GLU   B CG  1 
ATOM   3056 C  CD  . GLU   B 1 193 ? -12.248 -8.383  -36.637  1.00 23.83 ? 286 GLU   B CD  1 
ATOM   3057 O  OE1 . GLU   B 1 193 ? -13.152 -7.798  -37.258  1.00 23.63 ? 286 GLU   B OE1 1 
ATOM   3058 O  OE2 . GLU   B 1 193 ? -11.532 -7.829  -35.775  1.00 22.64 ? 286 GLU   B OE2 1 
ATOM   3059 N  N   . GLU   B 1 194 ? -14.183 -12.773 -39.980  1.00 33.55 ? 287 GLU   B N   1 
ATOM   3060 C  CA  . GLU   B 1 194 ? -15.275 -13.534 -40.650  1.00 37.63 ? 287 GLU   B CA  1 
ATOM   3061 C  C   . GLU   B 1 194 ? -15.219 -14.996 -40.188  1.00 40.42 ? 287 GLU   B C   1 
ATOM   3062 O  O   . GLU   B 1 194 ? -16.293 -15.581 -39.970  1.00 41.94 ? 287 GLU   B O   1 
ATOM   3063 C  CB  . GLU   B 1 194 ? -15.137 -13.397 -42.169  1.00 40.18 ? 287 GLU   B CB  1 
ATOM   3064 C  CG  . GLU   B 1 194 ? -16.003 -14.347 -42.982  1.00 42.63 ? 287 GLU   B CG  1 
ATOM   3065 C  CD  . GLU   B 1 194 ? -15.534 -14.559 -44.414  1.00 45.31 ? 287 GLU   B CD  1 
ATOM   3066 O  OE1 . GLU   B 1 194 ? -14.338 -14.311 -44.699  1.00 46.06 ? 287 GLU   B OE1 1 
ATOM   3067 O  OE2 . GLU   B 1 194 ? -16.364 -14.981 -45.247  1.00 47.96 ? 287 GLU   B OE2 1 
ATOM   3068 N  N   . ASN   B 1 195 ? -14.009 -15.542 -40.014  1.00 44.97 ? 288 ASN   B N   1 
ATOM   3069 C  CA  . ASN   B 1 195 ? -13.760 -16.976 -39.700  1.00 49.44 ? 288 ASN   B CA  1 
ATOM   3070 C  C   . ASN   B 1 195 ? -14.146 -17.293 -38.246  1.00 51.62 ? 288 ASN   B C   1 
ATOM   3071 O  O   . ASN   B 1 195 ? -14.156 -18.493 -37.908  1.00 51.77 ? 288 ASN   B O   1 
ATOM   3072 C  CB  . ASN   B 1 195 ? -12.309 -17.366 -39.999  1.00 52.00 ? 288 ASN   B CB  1 
ATOM   3073 C  CG  . ASN   B 1 195 ? -11.986 -17.317 -41.478  1.00 53.99 ? 288 ASN   B CG  1 
ATOM   3074 O  OD1 . ASN   B 1 195 ? -11.109 -16.568 -41.903  1.00 55.84 ? 288 ASN   B OD1 1 
ATOM   3075 N  ND2 . ASN   B 1 195 ? -12.695 -18.103 -42.272  1.00 54.57 ? 288 ASN   B ND2 1 
ATOM   3076 N  N   . LEU   B 1 196 ? -14.441 -16.279 -37.420  1.00 52.80 ? 289 LEU   B N   1 
ATOM   3077 C  CA  . LEU   B 1 196 ? -15.011 -16.455 -36.055  1.00 52.67 ? 289 LEU   B CA  1 
ATOM   3078 C  C   . LEU   B 1 196 ? -16.508 -16.768 -36.177  1.00 53.07 ? 289 LEU   B C   1 
ATOM   3079 O  O   . LEU   B 1 196 ? -17.360 -15.877 -36.111  1.00 51.66 ? 289 LEU   B O   1 
ATOM   3080 C  CB  . LEU   B 1 196 ? -14.786 -15.187 -35.221  1.00 52.85 ? 289 LEU   B CB  1 
ATOM   3081 C  CG  . LEU   B 1 196 ? -13.334 -14.752 -35.032  1.00 52.00 ? 289 LEU   B CG  1 
ATOM   3082 C  CD1 . LEU   B 1 196 ? -13.258 -13.488 -34.187  1.00 51.59 ? 289 LEU   B CD1 1 
ATOM   3083 C  CD2 . LEU   B 1 196 ? -12.505 -15.862 -34.406  1.00 52.05 ? 289 LEU   B CD2 1 
ATOM   3084 N  N   . SER   C 1 3   ? 21.216  -14.152 -93.723  1.00 38.79 ? 96  SER   C N   1 
ATOM   3085 C  CA  . SER   C 1 3   ? 22.208  -14.308 -92.621  1.00 37.55 ? 96  SER   C CA  1 
ATOM   3086 C  C   . SER   C 1 3   ? 23.279  -15.332 -93.024  1.00 36.10 ? 96  SER   C C   1 
ATOM   3087 O  O   . SER   C 1 3   ? 23.140  -15.946 -94.106  1.00 35.77 ? 96  SER   C O   1 
ATOM   3088 C  CB  . SER   C 1 3   ? 21.520  -14.688 -91.333  1.00 38.32 ? 96  SER   C CB  1 
ATOM   3089 O  OG  . SER   C 1 3   ? 21.073  -16.035 -91.374  1.00 39.96 ? 96  SER   C OG  1 
ATOM   3090 N  N   . VAL   C 1 4   ? 24.318  -15.489 -92.197  1.00 33.66 ? 97  VAL   C N   1 
ATOM   3091 C  CA  . VAL   C 1 4   ? 25.461  -16.418 -92.440  1.00 32.30 ? 97  VAL   C CA  1 
ATOM   3092 C  C   . VAL   C 1 4   ? 25.797  -17.120 -91.127  1.00 31.36 ? 97  VAL   C C   1 
ATOM   3093 O  O   . VAL   C 1 4   ? 25.957  -16.467 -90.098  1.00 30.55 ? 97  VAL   C O   1 
ATOM   3094 C  CB  . VAL   C 1 4   ? 26.686  -15.680 -93.017  1.00 33.30 ? 97  VAL   C CB  1 
ATOM   3095 C  CG1 . VAL   C 1 4   ? 27.807  -16.643 -93.380  1.00 32.54 ? 97  VAL   C CG1 1 
ATOM   3096 C  CG2 . VAL   C 1 4   ? 26.313  -14.824 -94.221  1.00 34.58 ? 97  VAL   C CG2 1 
ATOM   3097 N  N   . PRO   C 1 5   ? 25.884  -18.469 -91.110  1.00 29.04 ? 98  PRO   C N   1 
ATOM   3098 C  CA  . PRO   C 1 5   ? 26.328  -19.190 -89.918  1.00 28.01 ? 98  PRO   C CA  1 
ATOM   3099 C  C   . PRO   C 1 5   ? 27.791  -18.839 -89.620  1.00 26.75 ? 98  PRO   C C   1 
ATOM   3100 O  O   . PRO   C 1 5   ? 28.547  -18.662 -90.558  1.00 25.03 ? 98  PRO   C O   1 
ATOM   3101 C  CB  . PRO   C 1 5   ? 26.175  -20.674 -90.281  1.00 28.37 ? 98  PRO   C CB  1 
ATOM   3102 C  CG  . PRO   C 1 5   ? 25.279  -20.682 -91.507  1.00 29.28 ? 98  PRO   C CG  1 
ATOM   3103 C  CD  . PRO   C 1 5   ? 25.552  -19.376 -92.217  1.00 28.61 ? 98  PRO   C CD  1 
ATOM   3104 N  N   . SER   C 1 6   ? 28.144  -18.732 -88.338  1.00 26.54 ? 99  SER   C N   1 
ATOM   3105 C  CA  . SER   C 1 6   ? 29.526  -18.465 -87.861  1.00 26.97 ? 99  SER   C CA  1 
ATOM   3106 C  C   . SER   C 1 6   ? 30.447  -19.627 -88.259  1.00 27.59 ? 99  SER   C C   1 
ATOM   3107 O  O   . SER   C 1 6   ? 30.017  -20.789 -88.121  1.00 26.65 ? 99  SER   C O   1 
ATOM   3108 C  CB  . SER   C 1 6   ? 29.544  -18.235 -86.376  1.00 27.06 ? 99  SER   C CB  1 
ATOM   3109 O  OG  . SER   C 1 6   ? 30.875  -18.079 -85.907  1.00 28.19 ? 99  SER   C OG  1 
ATOM   3110 N  N   . GLN   C 1 7   ? 31.659  -19.318 -88.738  1.00 27.25 ? 100 GLN   C N   1 
ATOM   3111 C  CA  . GLN   C 1 7   ? 32.732  -20.311 -89.025  1.00 27.65 ? 100 GLN   C CA  1 
ATOM   3112 C  C   . GLN   C 1 7   ? 33.885  -20.144 -88.022  1.00 26.92 ? 100 GLN   C C   1 
ATOM   3113 O  O   . GLN   C 1 7   ? 34.966  -20.711 -88.277  1.00 26.20 ? 100 GLN   C O   1 
ATOM   3114 C  CB  . GLN   C 1 7   ? 33.220  -20.183 -90.471  1.00 28.95 ? 100 GLN   C CB  1 
ATOM   3115 C  CG  . GLN   C 1 7   ? 33.731  -18.799 -90.847  1.00 30.22 ? 100 GLN   C CG  1 
ATOM   3116 C  CD  . GLN   C 1 7   ? 34.545  -18.825 -92.119  1.00 30.67 ? 100 GLN   C CD  1 
ATOM   3117 O  OE1 . GLN   C 1 7   ? 34.118  -18.338 -93.162  1.00 31.94 ? 100 GLN   C OE1 1 
ATOM   3118 N  NE2 . GLN   C 1 7   ? 35.732  -19.410 -92.044  1.00 31.85 ? 100 GLN   C NE2 1 
ATOM   3119 N  N   . LYS   C 1 8   ? 33.654  -19.420 -86.919  1.00 25.92 ? 101 LYS   C N   1 
ATOM   3120 C  CA  . LYS   C 1 8   ? 34.639  -19.196 -85.824  1.00 26.13 ? 101 LYS   C CA  1 
ATOM   3121 C  C   . LYS   C 1 8   ? 35.067  -20.528 -85.207  1.00 25.05 ? 101 LYS   C C   1 
ATOM   3122 O  O   . LYS   C 1 8   ? 34.202  -21.218 -84.653  1.00 23.59 ? 101 LYS   C O   1 
ATOM   3123 C  CB  . LYS   C 1 8   ? 34.041  -18.389 -84.667  1.00 27.96 ? 101 LYS   C CB  1 
ATOM   3124 C  CG  . LYS   C 1 8   ? 34.133  -16.881 -84.797  1.00 29.41 ? 101 LYS   C CG  1 
ATOM   3125 C  CD  . LYS   C 1 8   ? 34.399  -16.193 -83.474  1.00 30.58 ? 101 LYS   C CD  1 
ATOM   3126 C  CE  . LYS   C 1 8   ? 35.857  -16.249 -83.073  1.00 31.57 ? 101 LYS   C CE  1 
ATOM   3127 N  NZ  . LYS   C 1 8   ? 36.107  -15.489 -81.827  1.00 32.18 ? 101 LYS   C NZ  1 
ATOM   3128 N  N   . THR   C 1 9   ? 36.360  -20.843 -85.247  1.00 24.65 ? 102 THR   C N   1 
ATOM   3129 C  CA  . THR   C 1 9   ? 36.943  -21.987 -84.503  1.00 24.46 ? 102 THR   C CA  1 
ATOM   3130 C  C   . THR   C 1 9   ? 36.694  -21.755 -83.010  1.00 24.75 ? 102 THR   C C   1 
ATOM   3131 O  O   . THR   C 1 9   ? 36.933  -20.625 -82.532  1.00 23.25 ? 102 THR   C O   1 
ATOM   3132 C  CB  . THR   C 1 9   ? 38.425  -22.177 -84.838  1.00 24.14 ? 102 THR   C CB  1 
ATOM   3133 O  OG1 . THR   C 1 9   ? 38.477  -22.458 -86.236  1.00 24.39 ? 102 THR   C OG1 1 
ATOM   3134 C  CG2 . THR   C 1 9   ? 39.076  -23.288 -84.045  1.00 24.49 ? 102 THR   C CG2 1 
ATOM   3135 N  N   . TYR   C 1 10  ? 36.209  -22.787 -82.323  1.00 24.76 ? 103 TYR   C N   1 
ATOM   3136 C  CA  . TYR   C 1 10  ? 35.848  -22.765 -80.885  1.00 24.78 ? 103 TYR   C CA  1 
ATOM   3137 C  C   . TYR   C 1 10  ? 36.071  -24.166 -80.318  1.00 24.78 ? 103 TYR   C C   1 
ATOM   3138 O  O   . TYR   C 1 10  ? 35.206  -25.032 -80.509  1.00 24.65 ? 103 TYR   C O   1 
ATOM   3139 C  CB  . TYR   C 1 10  ? 34.405  -22.277 -80.729  1.00 25.11 ? 103 TYR   C CB  1 
ATOM   3140 C  CG  . TYR   C 1 10  ? 33.857  -22.323 -79.325  1.00 25.80 ? 103 TYR   C CG  1 
ATOM   3141 C  CD1 . TYR   C 1 10  ? 34.491  -21.665 -78.281  1.00 25.43 ? 103 TYR   C CD1 1 
ATOM   3142 C  CD2 . TYR   C 1 10  ? 32.682  -23.004 -79.046  1.00 25.55 ? 103 TYR   C CD2 1 
ATOM   3143 C  CE1 . TYR   C 1 10  ? 33.983  -21.700 -76.992  1.00 25.84 ? 103 TYR   C CE1 1 
ATOM   3144 C  CE2 . TYR   C 1 10  ? 32.160  -23.045 -77.765  1.00 26.17 ? 103 TYR   C CE2 1 
ATOM   3145 C  CZ  . TYR   C 1 10  ? 32.808  -22.387 -76.735  1.00 26.27 ? 103 TYR   C CZ  1 
ATOM   3146 O  OH  . TYR   C 1 10  ? 32.282  -22.439 -75.477  1.00 26.11 ? 103 TYR   C OH  1 
ATOM   3147 N  N   . GLN   C 1 11  ? 37.213  -24.387 -79.665  1.00 24.61 ? 104 GLN   C N   1 
ATOM   3148 C  CA  . GLN   C 1 11  ? 37.583  -25.712 -79.099  1.00 25.23 ? 104 GLN   C CA  1 
ATOM   3149 C  C   . GLN   C 1 11  ? 36.680  -25.995 -77.892  1.00 24.79 ? 104 GLN   C C   1 
ATOM   3150 O  O   . GLN   C 1 11  ? 36.279  -27.165 -77.721  1.00 22.99 ? 104 GLN   C O   1 
ATOM   3151 C  CB  . GLN   C 1 11  ? 39.079  -25.746 -78.781  1.00 26.29 ? 104 GLN   C CB  1 
ATOM   3152 C  CG  . GLN   C 1 11  ? 39.946  -25.496 -80.012  1.00 27.54 ? 104 GLN   C CG  1 
ATOM   3153 C  CD  . GLN   C 1 11  ? 41.374  -25.948 -79.833  1.00 28.52 ? 104 GLN   C CD  1 
ATOM   3154 O  OE1 . GLN   C 1 11  ? 41.821  -26.226 -78.725  1.00 31.77 ? 104 GLN   C OE1 1 
ATOM   3155 N  NE2 . GLN   C 1 11  ? 42.104  -26.027 -80.933  1.00 29.20 ? 104 GLN   C NE2 1 
ATOM   3156 N  N   . GLY   C 1 12  ? 36.353  -24.953 -77.116  1.00 24.96 ? 105 GLY   C N   1 
ATOM   3157 C  CA  . GLY   C 1 12  ? 35.363  -24.989 -76.023  1.00 25.03 ? 105 GLY   C CA  1 
ATOM   3158 C  C   . GLY   C 1 12  ? 35.818  -25.842 -74.851  1.00 25.49 ? 105 GLY   C C   1 
ATOM   3159 O  O   . GLY   C 1 12  ? 37.021  -26.187 -74.788  1.00 24.66 ? 105 GLY   C O   1 
ATOM   3160 N  N   . SER   C 1 13  ? 34.876  -26.210 -73.977  1.00 24.54 ? 106 SER   C N   1 
ATOM   3161 C  CA  . SER   C 1 13  ? 35.129  -26.871 -72.670  1.00 24.75 ? 106 SER   C CA  1 
ATOM   3162 C  C   . SER   C 1 13  ? 35.799  -28.234 -72.856  1.00 23.36 ? 106 SER   C C   1 
ATOM   3163 O  O   . SER   C 1 13  ? 36.546  -28.630 -71.949  1.00 21.11 ? 106 SER   C O   1 
ATOM   3164 C  CB  . SER   C 1 13  ? 33.859  -27.010 -71.865  1.00 25.42 ? 106 SER   C CB  1 
ATOM   3165 O  OG  . SER   C 1 13  ? 33.453  -25.752 -71.357  1.00 27.09 ? 106 SER   C OG  1 
ATOM   3166 N  N   . TYR   C 1 14  ? 35.534  -28.927 -73.967  1.00 22.80 ? 107 TYR   C N   1 
ATOM   3167 C  CA  . TYR   C 1 14  ? 35.906  -30.353 -74.164  1.00 22.41 ? 107 TYR   C CA  1 
ATOM   3168 C  C   . TYR   C 1 14  ? 37.145  -30.481 -75.054  1.00 20.96 ? 107 TYR   C C   1 
ATOM   3169 O  O   . TYR   C 1 14  ? 37.563  -31.626 -75.288  1.00 19.52 ? 107 TYR   C O   1 
ATOM   3170 C  CB  . TYR   C 1 14  ? 34.702  -31.132 -74.695  1.00 23.30 ? 107 TYR   C CB  1 
ATOM   3171 C  CG  . TYR   C 1 14  ? 33.523  -31.041 -73.763  1.00 24.48 ? 107 TYR   C CG  1 
ATOM   3172 C  CD1 . TYR   C 1 14  ? 33.482  -31.782 -72.593  1.00 24.91 ? 107 TYR   C CD1 1 
ATOM   3173 C  CD2 . TYR   C 1 14  ? 32.492  -30.148 -74.001  1.00 25.44 ? 107 TYR   C CD2 1 
ATOM   3174 C  CE1 . TYR   C 1 14  ? 32.421  -31.680 -71.709  1.00 25.46 ? 107 TYR   C CE1 1 
ATOM   3175 C  CE2 . TYR   C 1 14  ? 31.424  -30.031 -73.126  1.00 25.68 ? 107 TYR   C CE2 1 
ATOM   3176 C  CZ  . TYR   C 1 14  ? 31.390  -30.798 -71.977  1.00 25.72 ? 107 TYR   C CZ  1 
ATOM   3177 O  OH  . TYR   C 1 14  ? 30.344  -30.684 -71.112  1.00 28.08 ? 107 TYR   C OH  1 
ATOM   3178 N  N   . GLY   C 1 15  ? 37.723  -29.358 -75.490  1.00 20.31 ? 108 GLY   C N   1 
ATOM   3179 C  CA  . GLY   C 1 15  ? 38.953  -29.320 -76.301  1.00 20.55 ? 108 GLY   C CA  1 
ATOM   3180 C  C   . GLY   C 1 15  ? 38.727  -29.976 -77.651  1.00 20.40 ? 108 GLY   C C   1 
ATOM   3181 O  O   . GLY   C 1 15  ? 39.457  -30.930 -77.983  1.00 20.62 ? 108 GLY   C O   1 
ATOM   3182 N  N   . PHE   C 1 16  ? 37.723  -29.493 -78.383  1.00 20.35 ? 109 PHE   C N   1 
ATOM   3183 C  CA  . PHE   C 1 16  ? 37.212  -30.104 -79.636  1.00 20.61 ? 109 PHE   C CA  1 
ATOM   3184 C  C   . PHE   C 1 16  ? 38.071  -29.651 -80.816  1.00 20.19 ? 109 PHE   C C   1 
ATOM   3185 O  O   . PHE   C 1 16  ? 38.192  -28.442 -81.042  1.00 20.23 ? 109 PHE   C O   1 
ATOM   3186 C  CB  . PHE   C 1 16  ? 35.744  -29.731 -79.861  1.00 20.99 ? 109 PHE   C CB  1 
ATOM   3187 C  CG  . PHE   C 1 16  ? 35.199  -30.125 -81.211  1.00 21.23 ? 109 PHE   C CG  1 
ATOM   3188 C  CD1 . PHE   C 1 16  ? 35.350  -31.420 -81.682  1.00 21.81 ? 109 PHE   C CD1 1 
ATOM   3189 C  CD2 . PHE   C 1 16  ? 34.530  -29.206 -82.005  1.00 21.19 ? 109 PHE   C CD2 1 
ATOM   3190 C  CE1 . PHE   C 1 16  ? 34.847  -31.787 -82.919  1.00 21.75 ? 109 PHE   C CE1 1 
ATOM   3191 C  CE2 . PHE   C 1 16  ? 34.014  -29.579 -83.236  1.00 21.49 ? 109 PHE   C CE2 1 
ATOM   3192 C  CZ  . PHE   C 1 16  ? 34.177  -30.867 -83.691  1.00 21.72 ? 109 PHE   C CZ  1 
ATOM   3193 N  N   . ARG   C 1 17  ? 38.643  -30.598 -81.559  1.00 20.64 ? 110 ARG   C N   1 
ATOM   3194 C  CA  . ARG   C 1 17  ? 39.296  -30.286 -82.859  1.00 21.05 ? 110 ARG   C CA  1 
ATOM   3195 C  C   . ARG   C 1 17  ? 39.067  -31.439 -83.833  1.00 19.52 ? 110 ARG   C C   1 
ATOM   3196 O  O   . ARG   C 1 17  ? 38.549  -32.494 -83.412  1.00 19.43 ? 110 ARG   C O   1 
ATOM   3197 C  CB  . ARG   C 1 17  ? 40.776  -29.941 -82.673  1.00 23.49 ? 110 ARG   C CB  1 
ATOM   3198 C  CG  . ARG   C 1 17  ? 41.654  -31.081 -82.192  1.00 25.41 ? 110 ARG   C CG  1 
ATOM   3199 C  CD  . ARG   C 1 17  ? 41.817  -31.098 -80.686  1.00 28.46 ? 110 ARG   C CD  1 
ATOM   3200 N  NE  . ARG   C 1 17  ? 42.837  -32.070 -80.319  1.00 29.56 ? 110 ARG   C NE  1 
ATOM   3201 C  CZ  . ARG   C 1 17  ? 42.830  -32.831 -79.225  1.00 31.28 ? 110 ARG   C CZ  1 
ATOM   3202 N  NH1 . ARG   C 1 17  ? 41.845  -32.754 -78.343  1.00 30.69 ? 110 ARG   C NH1 1 
ATOM   3203 N  NH2 . ARG   C 1 17  ? 43.820  -33.685 -79.027  1.00 31.82 ? 110 ARG   C NH2 1 
ATOM   3204 N  N   . LEU   C 1 18  ? 39.403  -31.213 -85.104  1.00 18.23 ? 111 LEU   C N   1 
ATOM   3205 C  CA  . LEU   C 1 18  ? 39.206  -32.202 -86.189  1.00 17.14 ? 111 LEU   C CA  1 
ATOM   3206 C  C   . LEU   C 1 18  ? 40.553  -32.846 -86.505  1.00 17.07 ? 111 LEU   C C   1 
ATOM   3207 O  O   . LEU   C 1 18  ? 41.594  -32.179 -86.323  1.00 16.42 ? 111 LEU   C O   1 
ATOM   3208 C  CB  . LEU   C 1 18  ? 38.619  -31.512 -87.422  1.00 17.05 ? 111 LEU   C CB  1 
ATOM   3209 C  CG  . LEU   C 1 18  ? 37.218  -30.933 -87.241  1.00 16.81 ? 111 LEU   C CG  1 
ATOM   3210 C  CD1 . LEU   C 1 18  ? 36.746  -30.257 -88.519  1.00 16.85 ? 111 LEU   C CD1 1 
ATOM   3211 C  CD2 . LEU   C 1 18  ? 36.238  -32.014 -86.804  1.00 16.93 ? 111 LEU   C CD2 1 
ATOM   3212 N  N   . GLY   C 1 19  ? 40.505  -34.111 -86.914  1.00 16.58 ? 112 GLY   C N   1 
ATOM   3213 C  CA  . GLY   C 1 19  ? 41.633  -34.856 -87.495  1.00 16.32 ? 112 GLY   C CA  1 
ATOM   3214 C  C   . GLY   C 1 19  ? 41.230  -35.466 -88.821  1.00 16.17 ? 112 GLY   C C   1 
ATOM   3215 O  O   . GLY   C 1 19  ? 40.015  -35.632 -89.074  1.00 16.01 ? 112 GLY   C O   1 
ATOM   3216 N  N   . PHE   C 1 20  ? 42.214  -35.775 -89.654  1.00 16.33 ? 113 PHE   C N   1 
ATOM   3217 C  CA  . PHE   C 1 20  ? 42.016  -36.364 -90.998  1.00 16.33 ? 113 PHE   C CA  1 
ATOM   3218 C  C   . PHE   C 1 20  ? 43.077  -37.456 -91.178  1.00 16.67 ? 113 PHE   C C   1 
ATOM   3219 O  O   . PHE   C 1 20  ? 44.145  -37.381 -90.524  1.00 17.20 ? 113 PHE   C O   1 
ATOM   3220 C  CB  . PHE   C 1 20  ? 42.063  -35.255 -92.055  1.00 15.99 ? 113 PHE   C CB  1 
ATOM   3221 C  CG  . PHE   C 1 20  ? 41.120  -34.101 -91.802  1.00 15.79 ? 113 PHE   C CG  1 
ATOM   3222 C  CD1 . PHE   C 1 20  ? 39.812  -34.140 -92.261  1.00 16.14 ? 113 PHE   C CD1 1 
ATOM   3223 C  CD2 . PHE   C 1 20  ? 41.532  -32.981 -91.091  1.00 16.24 ? 113 PHE   C CD2 1 
ATOM   3224 C  CE1 . PHE   C 1 20  ? 38.937  -33.089 -92.017  1.00 16.04 ? 113 PHE   C CE1 1 
ATOM   3225 C  CE2 . PHE   C 1 20  ? 40.663  -31.925 -90.853  1.00 15.92 ? 113 PHE   C CE2 1 
ATOM   3226 C  CZ  . PHE   C 1 20  ? 39.365  -31.982 -91.318  1.00 16.35 ? 113 PHE   C CZ  1 
ATOM   3227 N  N   . LEU   C 1 21  ? 42.797  -38.455 -92.013  1.00 16.24 ? 114 LEU   C N   1 
ATOM   3228 C  CA  . LEU   C 1 21  ? 43.802  -39.496 -92.341  1.00 16.53 ? 114 LEU   C CA  1 
ATOM   3229 C  C   . LEU   C 1 21  ? 44.963  -38.826 -93.086  1.00 16.37 ? 114 LEU   C C   1 
ATOM   3230 O  O   . LEU   C 1 21  ? 44.732  -37.824 -93.802  1.00 16.26 ? 114 LEU   C O   1 
ATOM   3231 C  CB  . LEU   C 1 21  ? 43.159  -40.606 -93.175  1.00 16.52 ? 114 LEU   C CB  1 
ATOM   3232 C  CG  . LEU   C 1 21  ? 42.034  -41.374 -92.488  1.00 16.81 ? 114 LEU   C CG  1 
ATOM   3233 C  CD1 . LEU   C 1 21  ? 41.377  -42.338 -93.465  1.00 17.04 ? 114 LEU   C CD1 1 
ATOM   3234 C  CD2 . LEU   C 1 21  ? 42.540  -42.108 -91.251  1.00 16.97 ? 114 LEU   C CD2 1 
ATOM   3235 N  N   . HIS   C 1 22  ? 46.173  -39.347 -92.910  1.00 16.17 ? 115 HIS   C N   1 
ATOM   3236 C  CA  . HIS   C 1 22  ? 47.395  -38.851 -93.599  1.00 15.76 ? 115 HIS   C CA  1 
ATOM   3237 C  C   . HIS   C 1 22  ? 47.579  -39.703 -94.856  1.00 15.60 ? 115 HIS   C C   1 
ATOM   3238 O  O   . HIS   C 1 22  ? 48.453  -40.578 -94.856  1.00 15.33 ? 115 HIS   C O   1 
ATOM   3239 C  CB  . HIS   C 1 22  ? 48.571  -38.836 -92.618  1.00 15.86 ? 115 HIS   C CB  1 
ATOM   3240 C  CG  . HIS   C 1 22  ? 48.233  -38.159 -91.333  1.00 16.13 ? 115 HIS   C CG  1 
ATOM   3241 N  ND1 . HIS   C 1 22  ? 48.235  -38.831 -90.122  1.00 16.67 ? 115 HIS   C ND1 1 
ATOM   3242 C  CD2 . HIS   C 1 22  ? 47.817  -36.901 -91.069  1.00 15.94 ? 115 HIS   C CD2 1 
ATOM   3243 C  CE1 . HIS   C 1 22  ? 47.868  -38.005 -89.164  1.00 16.11 ? 115 HIS   C CE1 1 
ATOM   3244 N  NE2 . HIS   C 1 22  ? 47.614  -36.814 -89.716  1.00 16.35 ? 115 HIS   C NE2 1 
ATOM   3245 N  N   . SER   C 1 23  ? 46.740  -39.458 -95.868  1.00 15.75 ? 116 SER   C N   1 
ATOM   3246 C  CA  . SER   C 1 23  ? 46.497  -40.357 -97.025  1.00 16.20 ? 116 SER   C CA  1 
ATOM   3247 C  C   . SER   C 1 23  ? 47.490  -40.107 -98.168  1.00 16.12 ? 116 SER   C C   1 
ATOM   3248 O  O   . SER   C 1 23  ? 47.625  -41.001 -99.015  1.00 15.93 ? 116 SER   C O   1 
ATOM   3249 C  CB  . SER   C 1 23  ? 45.075  -40.216 -97.506  1.00 16.75 ? 116 SER   C CB  1 
ATOM   3250 O  OG  . SER   C 1 23  ? 44.166  -40.554 -96.470  1.00 16.97 ? 116 SER   C OG  1 
ATOM   3251 N  N   . GLY   C 1 24  ? 48.131  -38.937 -98.220  1.00 16.39 ? 117 GLY   C N   1 
ATOM   3252 C  CA  . GLY   C 1 24  ? 49.072  -38.584 -99.301  1.00 16.44 ? 117 GLY   C CA  1 
ATOM   3253 C  C   . GLY   C 1 24  ? 48.343  -38.288 -100.601 1.00 16.65 ? 117 GLY   C C   1 
ATOM   3254 O  O   . GLY   C 1 24  ? 47.104  -38.152 -100.565 1.00 16.81 ? 117 GLY   C O   1 
ATOM   3255 N  N   . THR   C 1 25  ? 49.075  -38.180 -101.714 1.00 17.03 ? 118 THR   C N   1 
ATOM   3256 C  CA  . THR   C 1 25  ? 48.547  -37.659 -103.008 1.00 17.52 ? 118 THR   C CA  1 
ATOM   3257 C  C   . THR   C 1 25  ? 48.760  -38.658 -104.153 1.00 18.22 ? 118 THR   C C   1 
ATOM   3258 O  O   . THR   C 1 25  ? 48.749  -38.214 -105.316 1.00 17.24 ? 118 THR   C O   1 
ATOM   3259 C  CB  . THR   C 1 25  ? 49.177  -36.303 -103.349 1.00 17.35 ? 118 THR   C CB  1 
ATOM   3260 O  OG1 . THR   C 1 25  ? 50.585  -36.481 -103.518 1.00 17.45 ? 118 THR   C OG1 1 
ATOM   3261 C  CG2 . THR   C 1 25  ? 48.899  -35.250 -102.297 1.00 17.19 ? 118 THR   C CG2 1 
ATOM   3262 N  N   . ALA   C 1 26  ? 48.902  -39.955 -103.865 1.00 18.94 ? 119 ALA   C N   1 
ATOM   3263 C  CA  . ALA   C 1 26  ? 48.937  -41.006 -104.909 1.00 20.65 ? 119 ALA   C CA  1 
ATOM   3264 C  C   . ALA   C 1 26  ? 47.657  -40.898 -105.750 1.00 22.18 ? 119 ALA   C C   1 
ATOM   3265 O  O   . ALA   C 1 26  ? 46.609  -40.489 -105.196 1.00 21.20 ? 119 ALA   C O   1 
ATOM   3266 C  CB  . ALA   C 1 26  ? 49.094  -42.373 -104.291 1.00 20.47 ? 119 ALA   C CB  1 
ATOM   3267 N  N   . LYS   C 1 27  ? 47.736  -41.256 -107.034 1.00 25.03 ? 120 LYS   C N   1 
ATOM   3268 C  CA  . LYS   C 1 27  ? 46.617  -41.124 -108.007 1.00 27.69 ? 120 LYS   C CA  1 
ATOM   3269 C  C   . LYS   C 1 27  ? 45.391  -41.893 -107.495 1.00 27.44 ? 120 LYS   C C   1 
ATOM   3270 O  O   . LYS   C 1 27  ? 44.268  -41.440 -107.766 1.00 28.54 ? 120 LYS   C O   1 
ATOM   3271 C  CB  . LYS   C 1 27  ? 47.045  -41.615 -109.396 1.00 30.98 ? 120 LYS   C CB  1 
ATOM   3272 C  CG  . LYS   C 1 27  ? 46.211  -41.075 -110.552 1.00 34.32 ? 120 LYS   C CG  1 
ATOM   3273 C  CD  . LYS   C 1 27  ? 46.745  -41.445 -111.926 1.00 36.42 ? 120 LYS   C CD  1 
ATOM   3274 C  CE  . LYS   C 1 27  ? 47.964  -40.646 -112.346 1.00 38.10 ? 120 LYS   C CE  1 
ATOM   3275 N  NZ  . LYS   C 1 27  ? 47.593  -39.339 -112.940 1.00 38.58 ? 120 LYS   C NZ  1 
ATOM   3276 N  N   . SER   C 1 28  ? 45.604  -42.990 -106.766 1.00 27.97 ? 121 SER   C N   1 
ATOM   3277 C  CA  . SER   C 1 28  ? 44.558  -43.955 -106.329 1.00 29.18 ? 121 SER   C CA  1 
ATOM   3278 C  C   . SER   C 1 28  ? 43.733  -43.426 -105.143 1.00 28.25 ? 121 SER   C C   1 
ATOM   3279 O  O   . SER   C 1 28  ? 42.660  -44.009 -104.883 1.00 29.66 ? 121 SER   C O   1 
ATOM   3280 C  CB  . SER   C 1 28  ? 45.185  -45.288 -105.993 1.00 29.86 ? 121 SER   C CB  1 
ATOM   3281 O  OG  . SER   C 1 28  ? 46.285  -45.120 -105.109 1.00 31.88 ? 121 SER   C OG  1 
ATOM   3282 N  N   . VAL   C 1 29  ? 44.188  -42.388 -104.429 1.00 26.72 ? 122 VAL   C N   1 
ATOM   3283 C  CA  . VAL   C 1 29  ? 43.518  -41.933 -103.171 1.00 25.35 ? 122 VAL   C CA  1 
ATOM   3284 C  C   . VAL   C 1 29  ? 42.145  -41.349 -103.530 1.00 25.35 ? 122 VAL   C C   1 
ATOM   3285 O  O   . VAL   C 1 29  ? 42.057  -40.550 -104.477 1.00 26.70 ? 122 VAL   C O   1 
ATOM   3286 C  CB  . VAL   C 1 29  ? 44.362  -40.942 -102.347 1.00 24.77 ? 122 VAL   C CB  1 
ATOM   3287 C  CG1 . VAL   C 1 29  ? 45.727  -41.516 -102.000 1.00 24.38 ? 122 VAL   C CG1 1 
ATOM   3288 C  CG2 . VAL   C 1 29  ? 44.492  -39.579 -103.015 1.00 24.57 ? 122 VAL   C CG2 1 
ATOM   3289 N  N   . THR   C 1 30  ? 41.108  -41.750 -102.797 1.00 25.20 ? 123 THR   C N   1 
ATOM   3290 C  CA  . THR   C 1 30  ? 39.697  -41.337 -103.022 1.00 24.80 ? 123 THR   C CA  1 
ATOM   3291 C  C   . THR   C 1 30  ? 39.383  -40.101 -102.172 1.00 23.89 ? 123 THR   C C   1 
ATOM   3292 O  O   . THR   C 1 30  ? 38.378  -39.426 -102.452 1.00 22.82 ? 123 THR   C O   1 
ATOM   3293 C  CB  . THR   C 1 30  ? 38.760  -42.511 -102.724 1.00 25.40 ? 123 THR   C CB  1 
ATOM   3294 O  OG1 . THR   C 1 30  ? 38.973  -42.879 -101.365 1.00 24.78 ? 123 THR   C OG1 1 
ATOM   3295 C  CG2 . THR   C 1 30  ? 39.008  -43.702 -103.625 1.00 26.09 ? 123 THR   C CG2 1 
ATOM   3296 N  N   . CYS   C 1 31  ? 40.222  -39.826 -101.171 1.00 23.44 ? 124 CYS   C N   1 
ATOM   3297 C  CA  . CYS   C 1 31  ? 40.036  -38.754 -100.165 1.00 23.34 ? 124 CYS   C CA  1 
ATOM   3298 C  C   . CYS   C 1 31  ? 41.411  -38.391 -99.590  1.00 21.50 ? 124 CYS   C C   1 
ATOM   3299 O  O   . CYS   C 1 31  ? 42.110  -39.309 -99.144  1.00 21.32 ? 124 CYS   C O   1 
ATOM   3300 C  CB  . CYS   C 1 31  ? 39.074  -39.243 -99.084  1.00 25.06 ? 124 CYS   C CB  1 
ATOM   3301 S  SG  . CYS   C 1 31  ? 38.761  -38.044 -97.766  1.00 29.26 ? 124 CYS   C SG  1 
ATOM   3302 N  N   . THR   C 1 32  ? 41.812  -37.118 -99.638  1.00 19.70 ? 125 THR   C N   1 
ATOM   3303 C  CA  . THR   C 1 32  ? 43.088  -36.650 -99.032  1.00 18.80 ? 125 THR   C CA  1 
ATOM   3304 C  C   . THR   C 1 32  ? 42.934  -35.217 -98.523  1.00 17.84 ? 125 THR   C C   1 
ATOM   3305 O  O   . THR   C 1 32  ? 42.370  -34.384 -99.258  1.00 18.22 ? 125 THR   C O   1 
ATOM   3306 C  CB  . THR   C 1 32  ? 44.268  -36.775 -100.002 1.00 18.71 ? 125 THR   C CB  1 
ATOM   3307 O  OG1 . THR   C 1 32  ? 45.440  -36.501 -99.230  1.00 18.07 ? 125 THR   C OG1 1 
ATOM   3308 C  CG2 . THR   C 1 32  ? 44.179  -35.847 -101.196 1.00 18.22 ? 125 THR   C CG2 1 
ATOM   3309 N  N   . TYR   C 1 33  ? 43.447  -34.959 -97.316  1.00 17.24 ? 126 TYR   C N   1 
ATOM   3310 C  CA  . TYR   C 1 33  ? 43.392  -33.646 -96.623  1.00 16.63 ? 126 TYR   C CA  1 
ATOM   3311 C  C   . TYR   C 1 33  ? 44.752  -32.951 -96.733  1.00 15.98 ? 126 TYR   C C   1 
ATOM   3312 O  O   . TYR   C 1 33  ? 45.768  -33.609 -96.485  1.00 15.47 ? 126 TYR   C O   1 
ATOM   3313 C  CB  . TYR   C 1 33  ? 42.986  -33.841 -95.159  1.00 16.66 ? 126 TYR   C CB  1 
ATOM   3314 C  CG  . TYR   C 1 33  ? 43.101  -32.610 -94.298  1.00 16.28 ? 126 TYR   C CG  1 
ATOM   3315 C  CD1 . TYR   C 1 33  ? 42.147  -31.607 -94.350  1.00 16.56 ? 126 TYR   C CD1 1 
ATOM   3316 C  CD2 . TYR   C 1 33  ? 44.156  -32.456 -93.412  1.00 16.81 ? 126 TYR   C CD2 1 
ATOM   3317 C  CE1 . TYR   C 1 33  ? 42.247  -30.473 -93.556  1.00 16.51 ? 126 TYR   C CE1 1 
ATOM   3318 C  CE2 . TYR   C 1 33  ? 44.270  -31.331 -92.610  1.00 16.60 ? 126 TYR   C CE2 1 
ATOM   3319 C  CZ  . TYR   C 1 33  ? 43.312  -30.335 -92.682  1.00 16.79 ? 126 TYR   C CZ  1 
ATOM   3320 O  OH  . TYR   C 1 33  ? 43.425  -29.227 -91.887  1.00 16.50 ? 126 TYR   C OH  1 
ATOM   3321 N  N   . SER   C 1 34  ? 44.741  -31.657 -97.068  1.00 15.78 ? 127 SER   C N   1 
ATOM   3322 C  CA  . SER   C 1 34  ? 45.912  -30.744 -97.082  1.00 15.64 ? 127 SER   C CA  1 
ATOM   3323 C  C   . SER   C 1 34  ? 45.964  -29.950 -95.780  1.00 15.80 ? 127 SER   C C   1 
ATOM   3324 O  O   . SER   C 1 34  ? 45.153  -29.046 -95.582  1.00 16.08 ? 127 SER   C O   1 
ATOM   3325 C  CB  . SER   C 1 34  ? 45.857  -29.811 -98.258  1.00 15.48 ? 127 SER   C CB  1 
ATOM   3326 O  OG  . SER   C 1 34  ? 46.858  -28.811 -98.153  1.00 15.17 ? 127 SER   C OG  1 
ATOM   3327 N  N   . PRO   C 1 35  ? 46.912  -30.255 -94.862  1.00 15.62 ? 128 PRO   C N   1 
ATOM   3328 C  CA  . PRO   C 1 35  ? 47.160  -29.408 -93.696  1.00 16.34 ? 128 PRO   C CA  1 
ATOM   3329 C  C   . PRO   C 1 35  ? 47.487  -27.944 -94.039  1.00 16.50 ? 128 PRO   C C   1 
ATOM   3330 O  O   . PRO   C 1 35  ? 46.973  -27.074 -93.376  1.00 17.10 ? 128 PRO   C O   1 
ATOM   3331 C  CB  . PRO   C 1 35  ? 48.377  -30.061 -93.014  1.00 16.01 ? 128 PRO   C CB  1 
ATOM   3332 C  CG  . PRO   C 1 35  ? 48.347  -31.496 -93.467  1.00 16.00 ? 128 PRO   C CG  1 
ATOM   3333 C  CD  . PRO   C 1 35  ? 47.751  -31.466 -94.861  1.00 15.67 ? 128 PRO   C CD  1 
ATOM   3334 N  N   . ALA   C 1 36  ? 48.331  -27.704 -95.047  1.00 16.91 ? 129 ALA   C N   1 
ATOM   3335 C  CA  . ALA   C 1 36  ? 48.769  -26.346 -95.459  1.00 17.01 ? 129 ALA   C CA  1 
ATOM   3336 C  C   . ALA   C 1 36  ? 47.557  -25.490 -95.856  1.00 17.55 ? 129 ALA   C C   1 
ATOM   3337 O  O   . ALA   C 1 36  ? 47.539  -24.291 -95.505  1.00 18.24 ? 129 ALA   C O   1 
ATOM   3338 C  CB  . ALA   C 1 36  ? 49.774  -26.433 -96.582  1.00 17.31 ? 129 ALA   C CB  1 
ATOM   3339 N  N   . LEU   C 1 37  ? 46.587  -26.076 -96.561  1.00 17.47 ? 130 LEU   C N   1 
ATOM   3340 C  CA  . LEU   C 1 37  ? 45.414  -25.355 -97.126  1.00 17.59 ? 130 LEU   C CA  1 
ATOM   3341 C  C   . LEU   C 1 37  ? 44.183  -25.521 -96.226  1.00 17.63 ? 130 LEU   C C   1 
ATOM   3342 O  O   . LEU   C 1 37  ? 43.158  -24.868 -96.533  1.00 17.34 ? 130 LEU   C O   1 
ATOM   3343 C  CB  . LEU   C 1 37  ? 45.128  -25.903 -98.527  1.00 17.56 ? 130 LEU   C CB  1 
ATOM   3344 C  CG  . LEU   C 1 37  ? 46.221  -25.676 -99.571  1.00 17.96 ? 130 LEU   C CG  1 
ATOM   3345 C  CD1 . LEU   C 1 37  ? 45.934  -26.472 -100.833 1.00 17.94 ? 130 LEU   C CD1 1 
ATOM   3346 C  CD2 . LEU   C 1 37  ? 46.367  -24.195 -99.894  1.00 18.74 ? 130 LEU   C CD2 1 
ATOM   3347 N  N   . ASN   C 1 38  ? 44.265  -26.354 -95.179  1.00 17.24 ? 131 ASN   C N   1 
ATOM   3348 C  CA  . ASN   C 1 38  ? 43.100  -26.819 -94.373  1.00 17.01 ? 131 ASN   C CA  1 
ATOM   3349 C  C   . ASN   C 1 38  ? 41.962  -27.157 -95.344  1.00 16.94 ? 131 ASN   C C   1 
ATOM   3350 O  O   . ASN   C 1 38  ? 40.884  -26.518 -95.268  1.00 16.38 ? 131 ASN   C O   1 
ATOM   3351 C  CB  . ASN   C 1 38  ? 42.665  -25.792 -93.317  1.00 17.06 ? 131 ASN   C CB  1 
ATOM   3352 C  CG  . ASN   C 1 38  ? 41.551  -26.298 -92.418  1.00 17.06 ? 131 ASN   C CG  1 
ATOM   3353 O  OD1 . ASN   C 1 38  ? 41.462  -27.494 -92.142  1.00 16.06 ? 131 ASN   C OD1 1 
ATOM   3354 N  ND2 . ASN   C 1 38  ? 40.688  -25.399 -91.964  1.00 17.04 ? 131 ASN   C ND2 1 
ATOM   3355 N  N   . LYS   C 1 39  ? 42.217  -28.096 -96.257  1.00 17.14 ? 132 LYS   C N   1 
ATOM   3356 C  CA  . LYS   C 1 39  ? 41.323  -28.385 -97.405  1.00 17.60 ? 132 LYS   C CA  1 
ATOM   3357 C  C   . LYS   C 1 39  ? 41.248  -29.894 -97.650  1.00 17.70 ? 132 LYS   C C   1 
ATOM   3358 O  O   . LYS   C 1 39  ? 42.302  -30.515 -97.891  1.00 17.03 ? 132 LYS   C O   1 
ATOM   3359 C  CB  . LYS   C 1 39  ? 41.826  -27.649 -98.648  1.00 18.14 ? 132 LYS   C CB  1 
ATOM   3360 C  CG  . LYS   C 1 39  ? 40.848  -27.617 -99.807  1.00 18.14 ? 132 LYS   C CG  1 
ATOM   3361 C  CD  . LYS   C 1 39  ? 41.246  -26.656 -100.897 1.00 18.32 ? 132 LYS   C CD  1 
ATOM   3362 C  CE  . LYS   C 1 39  ? 40.353  -26.766 -102.114 1.00 18.98 ? 132 LYS   C CE  1 
ATOM   3363 N  NZ  . LYS   C 1 39  ? 40.641  -25.701 -103.100 1.00 19.35 ? 132 LYS   C NZ  1 
ATOM   3364 N  N   . MET   C 1 40  ? 40.034  -30.445 -97.582  1.00 18.50 ? 133 MET   C N   1 
ATOM   3365 C  CA  . MET   C 1 40  ? 39.715  -31.849 -97.942  1.00 19.16 ? 133 MET   C CA  1 
ATOM   3366 C  C   . MET   C 1 40  ? 39.445  -31.914 -99.451  1.00 18.44 ? 133 MET   C C   1 
ATOM   3367 O  O   . MET   C 1 40  ? 38.620  -31.118 -99.938  1.00 18.20 ? 133 MET   C O   1 
ATOM   3368 C  CB  . MET   C 1 40  ? 38.485  -32.339 -97.170  1.00 20.91 ? 133 MET   C CB  1 
ATOM   3369 C  CG  . MET   C 1 40  ? 38.040  -33.743 -97.542  1.00 22.67 ? 133 MET   C CG  1 
ATOM   3370 S  SD  . MET   C 1 40  ? 39.318  -34.993 -97.276  1.00 26.17 ? 133 MET   C SD  1 
ATOM   3371 C  CE  . MET   C 1 40  ? 39.140  -35.280 -95.516  1.00 25.93 ? 133 MET   C CE  1 
ATOM   3372 N  N   . PHE   C 1 41  ? 40.162  -32.791 -100.156 1.00 17.64 ? 134 PHE   C N   1 
ATOM   3373 C  CA  . PHE   C 1 41  ? 39.919  -33.176 -101.569 1.00 17.05 ? 134 PHE   C CA  1 
ATOM   3374 C  C   . PHE   C 1 41  ? 39.295  -34.570 -101.542 1.00 17.43 ? 134 PHE   C C   1 
ATOM   3375 O  O   . PHE   C 1 41  ? 39.910  -35.470 -100.969 1.00 16.39 ? 134 PHE   C O   1 
ATOM   3376 C  CB  . PHE   C 1 41  ? 41.217  -33.142 -102.380 1.00 16.46 ? 134 PHE   C CB  1 
ATOM   3377 C  CG  . PHE   C 1 41  ? 41.917  -31.803 -102.418 1.00 16.22 ? 134 PHE   C CG  1 
ATOM   3378 C  CD1 . PHE   C 1 41  ? 42.632  -31.337 -101.322 1.00 15.47 ? 134 PHE   C CD1 1 
ATOM   3379 C  CD2 . PHE   C 1 41  ? 41.873  -31.008 -103.556 1.00 15.66 ? 134 PHE   C CD2 1 
ATOM   3380 C  CE1 . PHE   C 1 41  ? 43.272  -30.107 -101.363 1.00 15.51 ? 134 PHE   C CE1 1 
ATOM   3381 C  CE2 . PHE   C 1 41  ? 42.511  -29.778 -103.593 1.00 15.67 ? 134 PHE   C CE2 1 
ATOM   3382 C  CZ  . PHE   C 1 41  ? 43.219  -29.333 -102.500 1.00 15.62 ? 134 PHE   C CZ  1 
ATOM   3383 N  N   . CYS   C 1 42  ? 38.091  -34.732 -102.088 1.00 18.12 ? 135 CYS   C N   1 
ATOM   3384 C  CA  . CYS   C 1 42  ? 37.334  -36.007 -102.013 1.00 19.74 ? 135 CYS   C CA  1 
ATOM   3385 C  C   . CYS   C 1 42  ? 36.546  -36.231 -103.302 1.00 20.05 ? 135 CYS   C C   1 
ATOM   3386 O  O   . CYS   C 1 42  ? 36.289  -35.251 -104.013 1.00 20.83 ? 135 CYS   C O   1 
ATOM   3387 C  CB  . CYS   C 1 42  ? 36.408  -36.027 -100.803 1.00 20.03 ? 135 CYS   C CB  1 
ATOM   3388 S  SG  . CYS   C 1 42  ? 35.118  -34.756 -100.830 1.00 21.04 ? 135 CYS   C SG  1 
ATOM   3389 N  N   . GLN   C 1 43  ? 36.188  -37.486 -103.576 1.00 21.28 ? 136 GLN   C N   1 
ATOM   3390 C  CA  . GLN   C 1 43  ? 35.393  -37.882 -104.767 1.00 22.11 ? 136 GLN   C CA  1 
ATOM   3391 C  C   . GLN   C 1 43  ? 33.903  -37.855 -104.418 1.00 21.86 ? 136 GLN   C C   1 
ATOM   3392 O  O   . GLN   C 1 43  ? 33.553  -38.081 -103.224 1.00 19.87 ? 136 GLN   C O   1 
ATOM   3393 C  CB  . GLN   C 1 43  ? 35.810  -39.265 -105.260 1.00 23.59 ? 136 GLN   C CB  1 
ATOM   3394 C  CG  . GLN   C 1 43  ? 37.220  -39.300 -105.830 1.00 25.37 ? 136 GLN   C CG  1 
ATOM   3395 C  CD  . GLN   C 1 43  ? 37.648  -40.698 -106.200 1.00 26.89 ? 136 GLN   C CD  1 
ATOM   3396 O  OE1 . GLN   C 1 43  ? 36.996  -41.681 -105.860 1.00 28.67 ? 136 GLN   C OE1 1 
ATOM   3397 N  NE2 . GLN   C 1 43  ? 38.761  -40.796 -106.906 1.00 29.14 ? 136 GLN   C NE2 1 
ATOM   3398 N  N   . LEU   C 1 44  ? 33.076  -37.598 -105.437 1.00 21.73 ? 137 LEU   C N   1 
ATOM   3399 C  CA  . LEU   C 1 44  ? 31.591  -37.605 -105.376 1.00 22.77 ? 137 LEU   C CA  1 
ATOM   3400 C  C   . LEU   C 1 44  ? 31.116  -38.905 -104.719 1.00 22.38 ? 137 LEU   C C   1 
ATOM   3401 O  O   . LEU   C 1 44  ? 31.550  -39.981 -105.172 1.00 21.30 ? 137 LEU   C O   1 
ATOM   3402 C  CB  . LEU   C 1 44  ? 31.044  -37.480 -106.802 1.00 24.13 ? 137 LEU   C CB  1 
ATOM   3403 C  CG  . LEU   C 1 44  ? 29.524  -37.392 -106.926 1.00 25.07 ? 137 LEU   C CG  1 
ATOM   3404 C  CD1 . LEU   C 1 44  ? 29.028  -36.050 -106.432 1.00 25.35 ? 137 LEU   C CD1 1 
ATOM   3405 C  CD2 . LEU   C 1 44  ? 29.084  -37.618 -108.367 1.00 26.26 ? 137 LEU   C CD2 1 
ATOM   3406 N  N   . ALA   C 1 45  ? 30.304  -38.793 -103.659 1.00 22.13 ? 138 ALA   C N   1 
ATOM   3407 C  CA  . ALA   C 1 45  ? 29.566  -39.897 -102.998 1.00 22.85 ? 138 ALA   C CA  1 
ATOM   3408 C  C   . ALA   C 1 45  ? 30.505  -40.938 -102.365 1.00 23.21 ? 138 ALA   C C   1 
ATOM   3409 O  O   . ALA   C 1 45  ? 29.980  -41.959 -101.888 1.00 25.48 ? 138 ALA   C O   1 
ATOM   3410 C  CB  . ALA   C 1 45  ? 28.628  -40.545 -103.990 1.00 23.26 ? 138 ALA   C CB  1 
ATOM   3411 N  N   . LYS   C 1 46  ? 31.823  -40.712 -102.339 1.00 22.81 ? 139 LYS   C N   1 
ATOM   3412 C  CA  . LYS   C 1 46  ? 32.805  -41.655 -101.735 1.00 22.78 ? 139 LYS   C CA  1 
ATOM   3413 C  C   . LYS   C 1 46  ? 32.996  -41.309 -100.252 1.00 21.35 ? 139 LYS   C C   1 
ATOM   3414 O  O   . LYS   C 1 46  ? 32.730  -40.149 -99.862  1.00 19.03 ? 139 LYS   C O   1 
ATOM   3415 C  CB  . LYS   C 1 46  ? 34.136  -41.616 -102.493 1.00 24.96 ? 139 LYS   C CB  1 
ATOM   3416 C  CG  . LYS   C 1 46  ? 34.092  -42.174 -103.910 1.00 26.80 ? 139 LYS   C CG  1 
ATOM   3417 C  CD  . LYS   C 1 46  ? 33.995  -43.680 -103.980 1.00 28.79 ? 139 LYS   C CD  1 
ATOM   3418 C  CE  . LYS   C 1 46  ? 33.567  -44.170 -105.347 1.00 30.63 ? 139 LYS   C CE  1 
ATOM   3419 N  NZ  . LYS   C 1 46  ? 34.456  -43.662 -106.417 1.00 31.19 ? 139 LYS   C NZ  1 
ATOM   3420 N  N   . THR   C 1 47  ? 33.420  -42.289 -99.450  1.00 20.56 ? 140 THR   C N   1 
ATOM   3421 C  CA  . THR   C 1 47  ? 33.679  -42.131 -97.994  1.00 20.22 ? 140 THR   C CA  1 
ATOM   3422 C  C   . THR   C 1 47  ? 34.690  -41.000 -97.782  1.00 20.08 ? 140 THR   C C   1 
ATOM   3423 O  O   . THR   C 1 47  ? 35.754  -41.015 -98.425  1.00 20.63 ? 140 THR   C O   1 
ATOM   3424 C  CB  . THR   C 1 47  ? 34.186  -43.429 -97.356  1.00 20.03 ? 140 THR   C CB  1 
ATOM   3425 O  OG1 . THR   C 1 47  ? 33.232  -44.453 -97.635  1.00 19.81 ? 140 THR   C OG1 1 
ATOM   3426 C  CG2 . THR   C 1 47  ? 34.376  -43.308 -95.860  1.00 20.03 ? 140 THR   C CG2 1 
ATOM   3427 N  N   A CYS   C 1 48  ? 34.349  -40.062 -96.897  0.50 19.59 ? 141 CYS   C N   1 
ATOM   3428 N  N   B CYS   C 1 48  ? 34.337  -40.023 -96.940  0.50 20.32 ? 141 CYS   C N   1 
ATOM   3429 C  CA  A CYS   C 1 48  ? 35.200  -38.929 -96.455  0.50 19.12 ? 141 CYS   C CA  1 
ATOM   3430 C  CA  B CYS   C 1 48  ? 35.225  -38.931 -96.457  0.50 20.28 ? 141 CYS   C CA  1 
ATOM   3431 C  C   A CYS   C 1 48  ? 35.353  -38.996 -94.939  0.50 19.03 ? 141 CYS   C C   1 
ATOM   3432 C  C   B CYS   C 1 48  ? 35.342  -39.020 -94.940  0.50 19.68 ? 141 CYS   C C   1 
ATOM   3433 O  O   A CYS   C 1 48  ? 34.543  -38.417 -94.218  0.50 18.81 ? 141 CYS   C O   1 
ATOM   3434 O  O   B CYS   C 1 48  ? 34.502  -38.476 -94.226  0.50 19.39 ? 141 CYS   C O   1 
ATOM   3435 C  CB  A CYS   C 1 48  ? 34.569  -37.604 -96.860  0.50 19.10 ? 141 CYS   C CB  1 
ATOM   3436 C  CB  B CYS   C 1 48  ? 34.684  -37.556 -96.818  0.50 21.09 ? 141 CYS   C CB  1 
ATOM   3437 S  SG  A CYS   C 1 48  ? 35.675  -36.183 -96.663  0.50 18.72 ? 141 CYS   C SG  1 
ATOM   3438 S  SG  B CYS   C 1 48  ? 34.440  -37.319 -98.595  0.50 22.55 ? 141 CYS   C SG  1 
ATOM   3439 N  N   . PRO   C 1 49  ? 36.357  -39.730 -94.402  1.00 19.48 ? 142 PRO   C N   1 
ATOM   3440 C  CA  . PRO   C 1 49  ? 36.547  -39.821 -92.955  1.00 19.40 ? 142 PRO   C CA  1 
ATOM   3441 C  C   . PRO   C 1 49  ? 36.913  -38.462 -92.343  1.00 18.87 ? 142 PRO   C C   1 
ATOM   3442 O  O   . PRO   C 1 49  ? 37.827  -37.816 -92.824  1.00 19.61 ? 142 PRO   C O   1 
ATOM   3443 C  CB  . PRO   C 1 49  ? 37.699  -40.829 -92.794  1.00 19.65 ? 142 PRO   C CB  1 
ATOM   3444 C  CG  . PRO   C 1 49  ? 37.737  -41.567 -94.112  1.00 19.60 ? 142 PRO   C CG  1 
ATOM   3445 C  CD  . PRO   C 1 49  ? 37.346  -40.529 -95.144  1.00 19.88 ? 142 PRO   C CD  1 
ATOM   3446 N  N   . VAL   C 1 50  ? 36.155  -38.052 -91.329  1.00 18.05 ? 143 VAL   C N   1 
ATOM   3447 C  CA  . VAL   C 1 50  ? 36.441  -36.844 -90.504  1.00 17.71 ? 143 VAL   C CA  1 
ATOM   3448 C  C   . VAL   C 1 50  ? 36.493  -37.306 -89.046  1.00 16.95 ? 143 VAL   C C   1 
ATOM   3449 O  O   . VAL   C 1 50  ? 35.527  -37.957 -88.591  1.00 15.83 ? 143 VAL   C O   1 
ATOM   3450 C  CB  . VAL   C 1 50  ? 35.410  -35.722 -90.745  1.00 17.68 ? 143 VAL   C CB  1 
ATOM   3451 C  CG1 . VAL   C 1 50  ? 35.700  -34.496 -89.896  1.00 17.95 ? 143 VAL   C CG1 1 
ATOM   3452 C  CG2 . VAL   C 1 50  ? 35.334  -35.332 -92.217  1.00 18.05 ? 143 VAL   C CG2 1 
ATOM   3453 N  N   . GLN   C 1 51  ? 37.607  -37.027 -88.368  1.00 17.04 ? 144 GLN   C N   1 
ATOM   3454 C  CA  . GLN   C 1 51  ? 37.859  -37.450 -86.972  1.00 16.89 ? 144 GLN   C CA  1 
ATOM   3455 C  C   . GLN   C 1 51  ? 37.486  -36.310 -86.022  1.00 16.89 ? 144 GLN   C C   1 
ATOM   3456 O  O   . GLN   C 1 51  ? 37.893  -35.149 -86.279  1.00 16.31 ? 144 GLN   C O   1 
ATOM   3457 C  CB  . GLN   C 1 51  ? 39.325  -37.842 -86.774  1.00 17.52 ? 144 GLN   C CB  1 
ATOM   3458 C  CG  . GLN   C 1 51  ? 39.748  -39.066 -87.571  1.00 17.76 ? 144 GLN   C CG  1 
ATOM   3459 C  CD  . GLN   C 1 51  ? 41.249  -39.192 -87.648  1.00 18.24 ? 144 GLN   C CD  1 
ATOM   3460 O  OE1 . GLN   C 1 51  ? 41.992  -38.358 -87.132  1.00 17.76 ? 144 GLN   C OE1 1 
ATOM   3461 N  NE2 . GLN   C 1 51  ? 41.712  -40.230 -88.324  1.00 19.23 ? 144 GLN   C NE2 1 
ATOM   3462 N  N   . LEU   C 1 52  ? 36.755  -36.644 -84.959  1.00 16.48 ? 145 LEU   C N   1 
ATOM   3463 C  CA  . LEU   C 1 52  ? 36.510  -35.743 -83.808  1.00 17.10 ? 145 LEU   C CA  1 
ATOM   3464 C  C   . LEU   C 1 52  ? 37.500  -36.119 -82.704  1.00 17.63 ? 145 LEU   C C   1 
ATOM   3465 O  O   . LEU   C 1 52  ? 37.515  -37.306 -82.303  1.00 17.74 ? 145 LEU   C O   1 
ATOM   3466 C  CB  . LEU   C 1 52  ? 35.066  -35.893 -83.322  1.00 16.20 ? 145 LEU   C CB  1 
ATOM   3467 C  CG  . LEU   C 1 52  ? 33.983  -35.922 -84.399  1.00 16.12 ? 145 LEU   C CG  1 
ATOM   3468 C  CD1 . LEU   C 1 52  ? 32.609  -36.030 -83.760  1.00 16.03 ? 145 LEU   C CD1 1 
ATOM   3469 C  CD2 . LEU   C 1 52  ? 34.059  -34.702 -85.303  1.00 15.89 ? 145 LEU   C CD2 1 
ATOM   3470 N  N   . TRP   C 1 53  ? 38.307  -35.149 -82.272  1.00 18.75 ? 146 TRP   C N   1 
ATOM   3471 C  CA  . TRP   C 1 53  ? 39.270  -35.258 -81.145  1.00 19.39 ? 146 TRP   C CA  1 
ATOM   3472 C  C   . TRP   C 1 53  ? 38.787  -34.338 -80.023  1.00 19.68 ? 146 TRP   C C   1 
ATOM   3473 O  O   . TRP   C 1 53  ? 38.494  -33.165 -80.323  1.00 19.18 ? 146 TRP   C O   1 
ATOM   3474 C  CB  . TRP   C 1 53  ? 40.687  -34.893 -81.600  1.00 20.02 ? 146 TRP   C CB  1 
ATOM   3475 C  CG  . TRP   C 1 53  ? 41.284  -35.836 -82.599  1.00 20.98 ? 146 TRP   C CG  1 
ATOM   3476 C  CD1 . TRP   C 1 53  ? 40.959  -35.952 -83.920  1.00 21.22 ? 146 TRP   C CD1 1 
ATOM   3477 C  CD2 . TRP   C 1 53  ? 42.327  -36.798 -82.357  1.00 21.29 ? 146 TRP   C CD2 1 
ATOM   3478 N  NE1 . TRP   C 1 53  ? 41.720  -36.924 -84.512  1.00 21.43 ? 146 TRP   C NE1 1 
ATOM   3479 C  CE2 . TRP   C 1 53  ? 42.576  -37.454 -83.582  1.00 21.90 ? 146 TRP   C CE2 1 
ATOM   3480 C  CE3 . TRP   C 1 53  ? 43.079  -37.160 -81.233  1.00 22.17 ? 146 TRP   C CE3 1 
ATOM   3481 C  CZ2 . TRP   C 1 53  ? 43.534  -38.461 -83.706  1.00 22.23 ? 146 TRP   C CZ2 1 
ATOM   3482 C  CZ3 . TRP   C 1 53  ? 44.029  -38.154 -81.357  1.00 22.43 ? 146 TRP   C CZ3 1 
ATOM   3483 C  CH2 . TRP   C 1 53  ? 44.251  -38.793 -82.579  1.00 22.57 ? 146 TRP   C CH2 1 
ATOM   3484 N  N   . VAL   C 1 54  ? 38.670  -34.865 -78.799  1.00 19.98 ? 147 VAL   C N   1 
ATOM   3485 C  CA  . VAL   C 1 54  ? 38.293  -34.095 -77.574  1.00 20.71 ? 147 VAL   C CA  1 
ATOM   3486 C  C   . VAL   C 1 54  ? 39.297  -34.433 -76.467  1.00 21.85 ? 147 VAL   C C   1 
ATOM   3487 O  O   . VAL   C 1 54  ? 39.799  -35.576 -76.466  1.00 21.33 ? 147 VAL   C O   1 
ATOM   3488 C  CB  . VAL   C 1 54  ? 36.846  -34.384 -77.122  1.00 20.26 ? 147 VAL   C CB  1 
ATOM   3489 C  CG1 . VAL   C 1 54  ? 35.823  -33.855 -78.119  1.00 19.88 ? 147 VAL   C CG1 1 
ATOM   3490 C  CG2 . VAL   C 1 54  ? 36.615  -35.863 -76.841  1.00 20.00 ? 147 VAL   C CG2 1 
ATOM   3491 N  N   . ASP   C 1 55  ? 39.560  -33.476 -75.570  1.00 23.03 ? 148 ASP   C N   1 
ATOM   3492 C  CA  . ASP   C 1 55  ? 40.400  -33.652 -74.353  1.00 24.49 ? 148 ASP   C CA  1 
ATOM   3493 C  C   . ASP   C 1 55  ? 39.579  -34.320 -73.243  1.00 25.80 ? 148 ASP   C C   1 
ATOM   3494 O  O   . ASP   C 1 55  ? 40.191  -34.969 -72.375  1.00 25.82 ? 148 ASP   C O   1 
ATOM   3495 C  CB  . ASP   C 1 55  ? 40.954  -32.314 -73.857  1.00 25.36 ? 148 ASP   C CB  1 
ATOM   3496 C  CG  . ASP   C 1 55  ? 41.893  -31.637 -74.835  1.00 25.70 ? 148 ASP   C CG  1 
ATOM   3497 O  OD1 . ASP   C 1 55  ? 42.537  -32.356 -75.618  1.00 27.61 ? 148 ASP   C OD1 1 
ATOM   3498 O  OD2 . ASP   C 1 55  ? 41.969  -30.394 -74.808  1.00 27.44 ? 148 ASP   C OD2 1 
ATOM   3499 N  N   . SER   C 1 56  ? 38.250  -34.159 -73.263  1.00 26.65 ? 149 SER   C N   1 
ATOM   3500 C  CA  . SER   C 1 56  ? 37.311  -34.748 -72.271  1.00 27.13 ? 149 SER   C CA  1 
ATOM   3501 C  C   . SER   C 1 56  ? 35.984  -35.109 -72.947  1.00 27.07 ? 149 SER   C C   1 
ATOM   3502 O  O   . SER   C 1 56  ? 35.582  -34.395 -73.889  1.00 26.44 ? 149 SER   C O   1 
ATOM   3503 C  CB  . SER   C 1 56  ? 37.096  -33.808 -71.123  1.00 27.96 ? 149 SER   C CB  1 
ATOM   3504 O  OG  . SER   C 1 56  ? 36.631  -32.554 -71.599  1.00 29.18 ? 149 SER   C OG  1 
ATOM   3505 N  N   . THR   C 1 57  ? 35.336  -36.177 -72.474  1.00 26.85 ? 150 THR   C N   1 
ATOM   3506 C  CA  . THR   C 1 57  ? 34.103  -36.755 -73.072  1.00 27.18 ? 150 THR   C CA  1 
ATOM   3507 C  C   . THR   C 1 57  ? 32.965  -35.744 -72.950  1.00 26.36 ? 150 THR   C C   1 
ATOM   3508 O  O   . THR   C 1 57  ? 32.634  -35.292 -71.854  1.00 23.85 ? 150 THR   C O   1 
ATOM   3509 C  CB  . THR   C 1 57  ? 33.763  -38.109 -72.440  1.00 27.91 ? 150 THR   C CB  1 
ATOM   3510 O  OG1 . THR   C 1 57  ? 34.975  -38.858 -72.364  1.00 30.22 ? 150 THR   C OG1 1 
ATOM   3511 C  CG2 . THR   C 1 57  ? 32.736  -38.894 -73.226  1.00 28.14 ? 150 THR   C CG2 1 
ATOM   3512 N  N   . PRO   C 1 58  ? 32.362  -35.318 -74.082  1.00 26.36 ? 151 PRO   C N   1 
ATOM   3513 C  CA  . PRO   C 1 58  ? 31.135  -34.528 -74.042  1.00 25.97 ? 151 PRO   C CA  1 
ATOM   3514 C  C   . PRO   C 1 58  ? 30.022  -35.261 -73.298  1.00 25.35 ? 151 PRO   C C   1 
ATOM   3515 O  O   . PRO   C 1 58  ? 30.033  -36.487 -73.185  1.00 25.79 ? 151 PRO   C O   1 
ATOM   3516 C  CB  . PRO   C 1 58  ? 30.766  -34.328 -75.519  1.00 26.51 ? 151 PRO   C CB  1 
ATOM   3517 C  CG  . PRO   C 1 58  ? 32.074  -34.508 -76.263  1.00 27.06 ? 151 PRO   C CG  1 
ATOM   3518 C  CD  . PRO   C 1 58  ? 32.856  -35.518 -75.452  1.00 26.74 ? 151 PRO   C CD  1 
ATOM   3519 N  N   . PRO   C 1 59  ? 29.013  -34.525 -72.791  1.00 24.73 ? 152 PRO   C N   1 
ATOM   3520 C  CA  . PRO   C 1 59  ? 27.948  -35.125 -71.992  1.00 24.57 ? 152 PRO   C CA  1 
ATOM   3521 C  C   . PRO   C 1 59  ? 27.025  -36.016 -72.818  1.00 23.97 ? 152 PRO   C C   1 
ATOM   3522 O  O   . PRO   C 1 59  ? 27.034  -35.955 -74.047  1.00 23.70 ? 152 PRO   C O   1 
ATOM   3523 C  CB  . PRO   C 1 59  ? 27.187  -33.912 -71.441  1.00 24.71 ? 152 PRO   C CB  1 
ATOM   3524 C  CG  . PRO   C 1 59  ? 27.441  -32.814 -72.452  1.00 24.98 ? 152 PRO   C CG  1 
ATOM   3525 C  CD  . PRO   C 1 59  ? 28.829  -33.082 -72.991  1.00 24.94 ? 152 PRO   C CD  1 
ATOM   3526 N  N   . PRO   C 1 60  ? 26.193  -36.859 -72.164  1.00 23.33 ? 153 PRO   C N   1 
ATOM   3527 C  CA  . PRO   C 1 60  ? 25.209  -37.673 -72.869  1.00 22.47 ? 153 PRO   C CA  1 
ATOM   3528 C  C   . PRO   C 1 60  ? 24.295  -36.784 -73.722  1.00 21.86 ? 153 PRO   C C   1 
ATOM   3529 O  O   . PRO   C 1 60  ? 23.967  -35.690 -73.282  1.00 21.74 ? 153 PRO   C O   1 
ATOM   3530 C  CB  . PRO   C 1 60  ? 24.391  -38.359 -71.758  1.00 23.06 ? 153 PRO   C CB  1 
ATOM   3531 C  CG  . PRO   C 1 60  ? 25.264  -38.271 -70.519  1.00 22.93 ? 153 PRO   C CG  1 
ATOM   3532 C  CD  . PRO   C 1 60  ? 26.127  -37.040 -70.704  1.00 23.51 ? 153 PRO   C CD  1 
ATOM   3533 N  N   . GLY   C 1 61  ? 23.921  -37.266 -74.909  1.00 20.70 ? 154 GLY   C N   1 
ATOM   3534 C  CA  . GLY   C 1 61  ? 22.976  -36.585 -75.814  1.00 20.05 ? 154 GLY   C CA  1 
ATOM   3535 C  C   . GLY   C 1 61  ? 23.657  -35.543 -76.686  1.00 18.86 ? 154 GLY   C C   1 
ATOM   3536 O  O   . GLY   C 1 61  ? 22.940  -34.858 -77.437  1.00 19.36 ? 154 GLY   C O   1 
ATOM   3537 N  N   . THR   C 1 62  ? 24.987  -35.416 -76.608  1.00 17.74 ? 155 THR   C N   1 
ATOM   3538 C  CA  . THR   C 1 62  ? 25.775  -34.509 -77.485  1.00 16.76 ? 155 THR   C CA  1 
ATOM   3539 C  C   . THR   C 1 62  ? 25.536  -34.936 -78.937  1.00 15.86 ? 155 THR   C C   1 
ATOM   3540 O  O   . THR   C 1 62  ? 25.374  -36.145 -79.189  1.00 15.32 ? 155 THR   C O   1 
ATOM   3541 C  CB  . THR   C 1 62  ? 27.268  -34.496 -77.127  1.00 16.55 ? 155 THR   C CB  1 
ATOM   3542 O  OG1 . THR   C 1 62  ? 27.402  -33.919 -75.827  1.00 16.59 ? 155 THR   C OG1 1 
ATOM   3543 C  CG2 . THR   C 1 62  ? 28.116  -33.718 -78.112  1.00 16.58 ? 155 THR   C CG2 1 
ATOM   3544 N  N   . ARG   C 1 63  ? 25.477  -33.968 -79.843  1.00 15.40 ? 156 ARG   C N   1 
ATOM   3545 C  CA  . ARG   C 1 63  ? 25.190  -34.205 -81.279  1.00 15.38 ? 156 ARG   C CA  1 
ATOM   3546 C  C   . ARG   C 1 63  ? 26.263  -33.492 -82.098  1.00 15.26 ? 156 ARG   C C   1 
ATOM   3547 O  O   . ARG   C 1 63  ? 26.808  -32.470 -81.613  1.00 15.40 ? 156 ARG   C O   1 
ATOM   3548 C  CB  . ARG   C 1 63  ? 23.765  -33.753 -81.612  1.00 15.71 ? 156 ARG   C CB  1 
ATOM   3549 C  CG  . ARG   C 1 63  ? 22.714  -34.816 -81.318  1.00 16.40 ? 156 ARG   C CG  1 
ATOM   3550 C  CD  . ARG   C 1 63  ? 21.382  -34.256 -80.856  1.00 16.54 ? 156 ARG   C CD  1 
ATOM   3551 N  NE  . ARG   C 1 63  ? 20.754  -33.303 -81.771  1.00 17.02 ? 156 ARG   C NE  1 
ATOM   3552 C  CZ  . ARG   C 1 63  ? 19.950  -33.613 -82.789  1.00 17.25 ? 156 ARG   C CZ  1 
ATOM   3553 N  NH1 . ARG   C 1 63  ? 19.682  -34.874 -83.086  1.00 17.49 ? 156 ARG   C NH1 1 
ATOM   3554 N  NH2 . ARG   C 1 63  ? 19.416  -32.649 -83.520  1.00 17.22 ? 156 ARG   C NH2 1 
ATOM   3555 N  N   . VAL   C 1 64  ? 26.565  -34.048 -83.272  1.00 14.71 ? 157 VAL   C N   1 
ATOM   3556 C  CA  . VAL   C 1 64  ? 27.612  -33.554 -84.206  1.00 14.91 ? 157 VAL   C CA  1 
ATOM   3557 C  C   . VAL   C 1 64  ? 26.906  -33.148 -85.502  1.00 15.01 ? 157 VAL   C C   1 
ATOM   3558 O  O   . VAL   C 1 64  ? 26.348  -34.040 -86.174  1.00 15.63 ? 157 VAL   C O   1 
ATOM   3559 C  CB  . VAL   C 1 64  ? 28.690  -34.626 -84.451  1.00 14.72 ? 157 VAL   C CB  1 
ATOM   3560 C  CG1 . VAL   C 1 64  ? 29.866  -34.062 -85.236  1.00 14.70 ? 157 VAL   C CG1 1 
ATOM   3561 C  CG2 . VAL   C 1 64  ? 29.165  -35.259 -83.150  1.00 14.79 ? 157 VAL   C CG2 1 
ATOM   3562 N  N   . ARG   C 1 65  ? 26.909  -31.853 -85.818  1.00 14.69 ? 158 ARG   C N   1 
ATOM   3563 C  CA  . ARG   C 1 65  ? 26.247  -31.286 -87.019  1.00 14.53 ? 158 ARG   C CA  1 
ATOM   3564 C  C   . ARG   C 1 65  ? 27.303  -30.863 -88.051  1.00 14.44 ? 158 ARG   C C   1 
ATOM   3565 O  O   . ARG   C 1 65  ? 28.344  -30.309 -87.662  1.00 14.34 ? 158 ARG   C O   1 
ATOM   3566 C  CB  . ARG   C 1 65  ? 25.366  -30.103 -86.616  1.00 14.64 ? 158 ARG   C CB  1 
ATOM   3567 C  CG  . ARG   C 1 65  ? 24.543  -29.533 -87.760  1.00 14.80 ? 158 ARG   C CG  1 
ATOM   3568 C  CD  . ARG   C 1 65  ? 23.696  -28.374 -87.286  1.00 14.80 ? 158 ARG   C CD  1 
ATOM   3569 N  NE  . ARG   C 1 65  ? 22.880  -28.802 -86.160  1.00 14.59 ? 158 ARG   C NE  1 
ATOM   3570 C  CZ  . ARG   C 1 65  ? 21.724  -29.450 -86.255  1.00 14.46 ? 158 ARG   C CZ  1 
ATOM   3571 N  NH1 . ARG   C 1 65  ? 21.210  -29.738 -87.439  1.00 14.41 ? 158 ARG   C NH1 1 
ATOM   3572 N  NH2 . ARG   C 1 65  ? 21.069  -29.789 -85.158  1.00 15.00 ? 158 ARG   C NH2 1 
ATOM   3573 N  N   . ALA   C 1 66  ? 27.023  -31.124 -89.326  1.00 14.79 ? 159 ALA   C N   1 
ATOM   3574 C  CA  . ALA   C 1 66  ? 27.818  -30.679 -90.490  1.00 15.13 ? 159 ALA   C CA  1 
ATOM   3575 C  C   . ALA   C 1 66  ? 26.931  -29.804 -91.381  1.00 15.24 ? 159 ALA   C C   1 
ATOM   3576 O  O   . ALA   C 1 66  ? 25.760  -30.165 -91.605  1.00 14.74 ? 159 ALA   C O   1 
ATOM   3577 C  CB  . ALA   C 1 66  ? 28.352  -31.869 -91.245  1.00 15.48 ? 159 ALA   C CB  1 
ATOM   3578 N  N   . MET   C 1 67  ? 27.483  -28.687 -91.844  1.00 15.95 ? 160 MET   C N   1 
ATOM   3579 C  CA  . MET   C 1 67  ? 26.815  -27.700 -92.728  1.00 16.56 ? 160 MET   C CA  1 
ATOM   3580 C  C   . MET   C 1 67  ? 27.862  -27.136 -93.694  1.00 16.48 ? 160 MET   C C   1 
ATOM   3581 O  O   . MET   C 1 67  ? 29.003  -26.895 -93.256  1.00 16.77 ? 160 MET   C O   1 
ATOM   3582 C  CB  . MET   C 1 67  ? 26.208  -26.574 -91.888  1.00 17.24 ? 160 MET   C CB  1 
ATOM   3583 C  CG  . MET   C 1 67  ? 25.463  -25.542 -92.697  1.00 18.02 ? 160 MET   C CG  1 
ATOM   3584 S  SD  . MET   C 1 67  ? 24.879  -24.183 -91.669  1.00 19.20 ? 160 MET   C SD  1 
ATOM   3585 C  CE  . MET   C 1 67  ? 23.613  -25.012 -90.705  1.00 19.01 ? 160 MET   C CE  1 
ATOM   3586 N  N   . ALA   C 1 68  ? 27.495  -26.971 -94.962  1.00 16.86 ? 161 ALA   C N   1 
ATOM   3587 C  CA  . ALA   C 1 68  ? 28.333  -26.343 -96.008  1.00 16.90 ? 161 ALA   C CA  1 
ATOM   3588 C  C   . ALA   C 1 68  ? 27.912  -24.878 -96.151  1.00 17.30 ? 161 ALA   C C   1 
ATOM   3589 O  O   . ALA   C 1 68  ? 26.696  -24.595 -96.071  1.00 17.51 ? 161 ALA   C O   1 
ATOM   3590 C  CB  . ALA   C 1 68  ? 28.198  -27.091 -97.310  1.00 17.10 ? 161 ALA   C CB  1 
ATOM   3591 N  N   . ILE   C 1 69  ? 28.886  -23.985 -96.303  1.00 17.69 ? 162 ILE   C N   1 
ATOM   3592 C  CA  . ILE   C 1 69  ? 28.676  -22.561 -96.696  1.00 18.36 ? 162 ILE   C CA  1 
ATOM   3593 C  C   . ILE   C 1 69  ? 29.662  -22.261 -97.826  1.00 18.76 ? 162 ILE   C C   1 
ATOM   3594 O  O   . ILE   C 1 69  ? 30.670  -22.987 -97.931  1.00 18.36 ? 162 ILE   C O   1 
ATOM   3595 C  CB  . ILE   C 1 69  ? 28.838  -21.614 -95.486  1.00 18.54 ? 162 ILE   C CB  1 
ATOM   3596 C  CG1 . ILE   C 1 69  ? 30.272  -21.606 -94.944  1.00 19.01 ? 162 ILE   C CG1 1 
ATOM   3597 C  CG2 . ILE   C 1 69  ? 27.828  -21.958 -94.395  1.00 18.31 ? 162 ILE   C CG2 1 
ATOM   3598 C  CD1 . ILE   C 1 69  ? 30.623  -20.365 -94.169  1.00 19.31 ? 162 ILE   C CD1 1 
ATOM   3599 N  N   . TYR   C 1 70  ? 29.381  -21.255 -98.656  1.00 19.81 ? 163 TYR   C N   1 
ATOM   3600 C  CA  . TYR   C 1 70  ? 30.340  -20.762 -99.678  1.00 20.68 ? 163 TYR   C CA  1 
ATOM   3601 C  C   . TYR   C 1 70  ? 31.448  -19.981 -98.962  1.00 21.68 ? 163 TYR   C C   1 
ATOM   3602 O  O   . TYR   C 1 70  ? 31.144  -19.226 -98.007  1.00 21.44 ? 163 TYR   C O   1 
ATOM   3603 C  CB  . TYR   C 1 70  ? 29.600  -19.989 -100.771 1.00 20.90 ? 163 TYR   C CB  1 
ATOM   3604 C  CG  . TYR   C 1 70  ? 28.827  -20.891 -101.698 1.00 20.74 ? 163 TYR   C CG  1 
ATOM   3605 C  CD1 . TYR   C 1 70  ? 29.487  -21.816 -102.492 1.00 20.58 ? 163 TYR   C CD1 1 
ATOM   3606 C  CD2 . TYR   C 1 70  ? 27.442  -20.857 -101.760 1.00 20.49 ? 163 TYR   C CD2 1 
ATOM   3607 C  CE1 . TYR   C 1 70  ? 28.797  -22.674 -103.333 1.00 20.69 ? 163 TYR   C CE1 1 
ATOM   3608 C  CE2 . TYR   C 1 70  ? 26.737  -21.698 -102.607 1.00 20.57 ? 163 TYR   C CE2 1 
ATOM   3609 C  CZ  . TYR   C 1 70  ? 27.417  -22.612 -103.394 1.00 20.24 ? 163 TYR   C CZ  1 
ATOM   3610 O  OH  . TYR   C 1 70  ? 26.744  -23.455 -104.230 1.00 19.85 ? 163 TYR   C OH  1 
ATOM   3611 N  N   . LYS   C 1 71  ? 32.701  -20.198 -99.382  1.00 22.82 ? 164 LYS   C N   1 
ATOM   3612 C  CA  . LYS   C 1 71  ? 33.913  -19.599 -98.761  1.00 24.60 ? 164 LYS   C CA  1 
ATOM   3613 C  C   . LYS   C 1 71  ? 34.001  -18.109 -99.126  1.00 25.87 ? 164 LYS   C C   1 
ATOM   3614 O  O   . LYS   C 1 71  ? 34.401  -17.316 -98.258  1.00 26.14 ? 164 LYS   C O   1 
ATOM   3615 C  CB  . LYS   C 1 71  ? 35.173  -20.343 -99.211  1.00 25.05 ? 164 LYS   C CB  1 
ATOM   3616 C  CG  . LYS   C 1 71  ? 36.478  -19.797 -98.644  1.00 25.96 ? 164 LYS   C CG  1 
ATOM   3617 C  CD  . LYS   C 1 71  ? 37.709  -20.371 -99.298  1.00 26.51 ? 164 LYS   C CD  1 
ATOM   3618 C  CE  . LYS   C 1 71  ? 38.984  -19.731 -98.795  1.00 27.38 ? 164 LYS   C CE  1 
ATOM   3619 N  NZ  . LYS   C 1 71  ? 40.171  -20.547 -99.136  1.00 28.70 ? 164 LYS   C NZ  1 
ATOM   3620 N  N   . GLN   C 1 72  ? 33.658  -17.751 -100.366 1.00 27.83 ? 165 GLN   C N   1 
ATOM   3621 C  CA  . GLN   C 1 72  ? 33.780  -16.367 -100.903 1.00 29.63 ? 165 GLN   C CA  1 
ATOM   3622 C  C   . GLN   C 1 72  ? 32.654  -15.497 -100.324 1.00 31.62 ? 165 GLN   C C   1 
ATOM   3623 O  O   . GLN   C 1 72  ? 31.485  -15.939 -100.358 1.00 30.53 ? 165 GLN   C O   1 
ATOM   3624 C  CB  . GLN   C 1 72  ? 33.747  -16.392 -102.431 1.00 30.69 ? 165 GLN   C CB  1 
ATOM   3625 C  CG  . GLN   C 1 72  ? 34.974  -17.042 -103.060 1.00 31.42 ? 165 GLN   C CG  1 
ATOM   3626 C  CD  . GLN   C 1 72  ? 34.741  -17.435 -104.498 1.00 32.14 ? 165 GLN   C CD  1 
ATOM   3627 O  OE1 . GLN   C 1 72  ? 33.801  -18.160 -104.818 1.00 32.16 ? 165 GLN   C OE1 1 
ATOM   3628 N  NE2 . GLN   C 1 72  ? 35.602  -16.963 -105.387 1.00 33.32 ? 165 GLN   C NE2 1 
ATOM   3629 N  N   . SER   C 1 73  ? 33.008  -14.300 -99.837  1.00 33.35 ? 166 SER   C N   1 
ATOM   3630 C  CA  A SER   C 1 73  ? 32.092  -13.342 -99.158  0.15 33.53 ? 166 SER   C CA  1 
ATOM   3631 C  CA  B SER   C 1 73  ? 32.088  -13.345 -99.157  0.85 34.69 ? 166 SER   C CA  1 
ATOM   3632 C  C   . SER   C 1 73  ? 30.835  -13.100 -100.004 1.00 33.77 ? 166 SER   C C   1 
ATOM   3633 O  O   . SER   C 1 73  ? 29.735  -13.115 -99.432  1.00 35.21 ? 166 SER   C O   1 
ATOM   3634 C  CB  A SER   C 1 73  ? 32.801  -12.045 -98.861  0.15 33.43 ? 166 SER   C CB  1 
ATOM   3635 C  CB  B SER   C 1 73  ? 32.784  -12.042 -98.833  0.85 35.08 ? 166 SER   C CB  1 
ATOM   3636 O  OG  A SER   C 1 73  ? 33.348  -11.484 -100.045 0.15 33.26 ? 166 SER   C OG  1 
ATOM   3637 O  OG  B SER   C 1 73  ? 33.082  -11.968 -97.448  0.85 36.81 ? 166 SER   C OG  1 
ATOM   3638 N  N   . GLN   C 1 74  ? 31.013  -12.890 -101.309 1.00 34.19 ? 167 GLN   C N   1 
ATOM   3639 C  CA  . GLN   C 1 74  ? 29.926  -12.494 -102.246 1.00 34.21 ? 167 GLN   C CA  1 
ATOM   3640 C  C   . GLN   C 1 74  ? 28.918  -13.636 -102.457 1.00 32.49 ? 167 GLN   C C   1 
ATOM   3641 O  O   . GLN   C 1 74  ? 27.873  -13.361 -103.071 1.00 31.40 ? 167 GLN   C O   1 
ATOM   3642 C  CB  . GLN   C 1 74  ? 30.506  -12.008 -103.580 1.00 35.42 ? 167 GLN   C CB  1 
ATOM   3643 C  CG  . GLN   C 1 74  ? 31.329  -13.043 -104.337 1.00 36.15 ? 167 GLN   C CG  1 
ATOM   3644 C  CD  . GLN   C 1 74  ? 32.810  -12.905 -104.079 1.00 36.87 ? 167 GLN   C CD  1 
ATOM   3645 O  OE1 . GLN   C 1 74  ? 33.262  -12.866 -102.935 1.00 35.67 ? 167 GLN   C OE1 1 
ATOM   3646 N  NE2 . GLN   C 1 74  ? 33.582  -12.824 -105.152 1.00 37.60 ? 167 GLN   C NE2 1 
ATOM   3647 N  N   . HIS   C 1 75  ? 29.204  -14.855 -101.977 1.00 31.61 ? 168 HIS   C N   1 
ATOM   3648 C  CA  . HIS   C 1 75  ? 28.361  -16.068 -102.179 1.00 30.36 ? 168 HIS   C CA  1 
ATOM   3649 C  C   . HIS   C 1 75  ? 27.876  -16.662 -100.846 1.00 30.45 ? 168 HIS   C C   1 
ATOM   3650 O  O   . HIS   C 1 75  ? 27.093  -17.636 -100.900 1.00 29.14 ? 168 HIS   C O   1 
ATOM   3651 C  CB  . HIS   C 1 75  ? 29.138  -17.118 -102.986 1.00 30.21 ? 168 HIS   C CB  1 
ATOM   3652 C  CG  . HIS   C 1 75  ? 29.523  -16.669 -104.355 1.00 30.32 ? 168 HIS   C CG  1 
ATOM   3653 N  ND1 . HIS   C 1 75  ? 28.587  -16.326 -105.309 1.00 30.14 ? 168 HIS   C ND1 1 
ATOM   3654 C  CD2 . HIS   C 1 75  ? 30.733  -16.517 -104.938 1.00 30.35 ? 168 HIS   C CD2 1 
ATOM   3655 C  CE1 . HIS   C 1 75  ? 29.204  -15.976 -106.421 1.00 30.14 ? 168 HIS   C CE1 1 
ATOM   3656 N  NE2 . HIS   C 1 75  ? 30.520  -16.085 -106.220 1.00 29.63 ? 168 HIS   C NE2 1 
ATOM   3657 N  N   . MET   C 1 76  ? 28.299  -16.102 -99.706  1.00 30.59 ? 169 MET   C N   1 
ATOM   3658 C  CA  . MET   C 1 76  ? 28.107  -16.691 -98.350  1.00 30.71 ? 169 MET   C CA  1 
ATOM   3659 C  C   . MET   C 1 76  ? 26.621  -16.764 -97.972  1.00 29.12 ? 169 MET   C C   1 
ATOM   3660 O  O   . MET   C 1 76  ? 26.268  -17.666 -97.189  1.00 27.15 ? 169 MET   C O   1 
ATOM   3661 C  CB  . MET   C 1 76  ? 28.846  -15.881 -97.281  1.00 32.92 ? 169 MET   C CB  1 
ATOM   3662 C  CG  . MET   C 1 76  ? 30.323  -16.208 -97.194  1.00 35.46 ? 169 MET   C CG  1 
ATOM   3663 S  SD  . MET   C 1 76  ? 31.030  -15.779 -95.588  1.00 38.16 ? 169 MET   C SD  1 
ATOM   3664 C  CE  . MET   C 1 76  ? 32.622  -16.593 -95.697  1.00 38.26 ? 169 MET   C CE  1 
ATOM   3665 N  N   . THR   C 1 77  ? 25.788  -15.846 -98.475  1.00 27.73 ? 170 THR   C N   1 
ATOM   3666 C  CA  . THR   C 1 77  ? 24.345  -15.754 -98.129  1.00 26.53 ? 170 THR   C CA  1 
ATOM   3667 C  C   . THR   C 1 77  ? 23.546  -16.782 -98.939  1.00 25.17 ? 170 THR   C C   1 
ATOM   3668 O  O   . THR   C 1 77  ? 22.392  -17.026 -98.567  1.00 24.27 ? 170 THR   C O   1 
ATOM   3669 C  CB  . THR   C 1 77  ? 23.807  -14.331 -98.325  1.00 26.82 ? 170 THR   C CB  1 
ATOM   3670 O  OG1 . THR   C 1 77  ? 23.937  -14.001 -99.708  1.00 26.56 ? 170 THR   C OG1 1 
ATOM   3671 C  CG2 . THR   C 1 77  ? 24.527  -13.308 -97.474  1.00 27.16 ? 170 THR   C CG2 1 
ATOM   3672 N  N   . GLU   C 1 78  ? 24.130  -17.363 -99.994  1.00 24.20 ? 171 GLU   C N   1 
ATOM   3673 C  CA  . GLU   C 1 78  ? 23.467  -18.391 -100.844 1.00 24.62 ? 171 GLU   C CA  1 
ATOM   3674 C  C   . GLU   C 1 78  ? 23.566  -19.757 -100.153 1.00 23.99 ? 171 GLU   C C   1 
ATOM   3675 O  O   . GLU   C 1 78  ? 24.686  -20.152 -99.775  1.00 23.58 ? 171 GLU   C O   1 
ATOM   3676 C  CB  . GLU   C 1 78  ? 24.094  -18.443 -102.239 1.00 25.62 ? 171 GLU   C CB  1 
ATOM   3677 C  CG  . GLU   C 1 78  ? 23.413  -19.423 -103.181 1.00 26.60 ? 171 GLU   C CG  1 
ATOM   3678 C  CD  . GLU   C 1 78  ? 23.905  -19.378 -104.620 1.00 26.96 ? 171 GLU   C CD  1 
ATOM   3679 O  OE1 . GLU   C 1 78  ? 24.175  -18.270 -105.117 1.00 28.45 ? 171 GLU   C OE1 1 
ATOM   3680 O  OE2 . GLU   C 1 78  ? 24.038  -20.452 -105.237 1.00 27.40 ? 171 GLU   C OE2 1 
ATOM   3681 N  N   . VAL   C 1 79  ? 22.435  -20.446 -99.990  1.00 22.92 ? 172 VAL   C N   1 
ATOM   3682 C  CA  . VAL   C 1 79  ? 22.386  -21.822 -99.413  1.00 22.28 ? 172 VAL   C CA  1 
ATOM   3683 C  C   . VAL   C 1 79  ? 23.138  -22.761 -100.360 1.00 21.64 ? 172 VAL   C C   1 
ATOM   3684 O  O   . VAL   C 1 79  ? 22.835  -22.753 -101.575 1.00 21.19 ? 172 VAL   C O   1 
ATOM   3685 C  CB  . VAL   C 1 79  ? 20.941  -22.303 -99.177  1.00 22.12 ? 172 VAL   C CB  1 
ATOM   3686 C  CG1 . VAL   C 1 79  ? 20.904  -23.769 -98.769  1.00 22.21 ? 172 VAL   C CG1 1 
ATOM   3687 C  CG2 . VAL   C 1 79  ? 20.222  -21.448 -98.144  1.00 22.30 ? 172 VAL   C CG2 1 
ATOM   3688 N  N   . VAL   C 1 80  ? 24.091  -23.530 -99.828  1.00 20.62 ? 173 VAL   C N   1 
ATOM   3689 C  CA  . VAL   C 1 80  ? 24.786  -24.612 -100.585 1.00 20.62 ? 173 VAL   C CA  1 
ATOM   3690 C  C   . VAL   C 1 80  ? 23.814  -25.792 -100.707 1.00 21.02 ? 173 VAL   C C   1 
ATOM   3691 O  O   . VAL   C 1 80  ? 23.379  -26.319 -99.663  1.00 20.61 ? 173 VAL   C O   1 
ATOM   3692 C  CB  . VAL   C 1 80  ? 26.113  -25.035 -99.931  1.00 19.47 ? 173 VAL   C CB  1 
ATOM   3693 C  CG1 . VAL   C 1 80  ? 26.792  -26.145 -100.717 1.00 19.36 ? 173 VAL   C CG1 1 
ATOM   3694 C  CG2 . VAL   C 1 80  ? 27.062  -23.859 -99.748  1.00 19.42 ? 173 VAL   C CG2 1 
ATOM   3695 N  N   . ARG   C 1 81  ? 23.483  -26.174 -101.941 1.00 21.63 ? 174 ARG   C N   1 
ATOM   3696 C  CA  . ARG   C 1 81  ? 22.564  -27.300 -102.250 1.00 23.77 ? 174 ARG   C CA  1 
ATOM   3697 C  C   . ARG   C 1 81  ? 23.073  -28.029 -103.495 1.00 23.12 ? 174 ARG   C C   1 
ATOM   3698 O  O   . ARG   C 1 81  ? 23.953  -27.489 -104.189 1.00 22.85 ? 174 ARG   C O   1 
ATOM   3699 C  CB  . ARG   C 1 81  ? 21.132  -26.790 -102.456 1.00 25.65 ? 174 ARG   C CB  1 
ATOM   3700 C  CG  . ARG   C 1 81  ? 21.011  -25.652 -103.461 1.00 27.79 ? 174 ARG   C CG  1 
ATOM   3701 C  CD  . ARG   C 1 81  ? 19.574  -25.298 -103.805 1.00 30.12 ? 174 ARG   C CD  1 
ATOM   3702 N  NE  . ARG   C 1 81  ? 18.909  -24.572 -102.730 1.00 31.43 ? 174 ARG   C NE  1 
ATOM   3703 C  CZ  . ARG   C 1 81  ? 18.088  -25.105 -101.825 1.00 34.35 ? 174 ARG   C CZ  1 
ATOM   3704 N  NH1 . ARG   C 1 81  ? 17.793  -26.395 -101.849 1.00 36.12 ? 174 ARG   C NH1 1 
ATOM   3705 N  NH2 . ARG   C 1 81  ? 17.550  -24.334 -100.894 1.00 34.57 ? 174 ARG   C NH2 1 
ATOM   3706 N  N   . ARG   C 1 82  ? 22.528  -29.212 -103.773 1.00 23.05 ? 175 ARG   C N   1 
ATOM   3707 C  CA  . ARG   C 1 82  ? 22.883  -29.998 -104.980 1.00 23.36 ? 175 ARG   C CA  1 
ATOM   3708 C  C   . ARG   C 1 82  ? 22.321  -29.303 -106.227 1.00 22.94 ? 175 ARG   C C   1 
ATOM   3709 O  O   . ARG   C 1 82  ? 21.288  -28.609 -106.118 1.00 22.12 ? 175 ARG   C O   1 
ATOM   3710 C  CB  . ARG   C 1 82  ? 22.356  -31.427 -104.866 1.00 23.31 ? 175 ARG   C CB  1 
ATOM   3711 C  CG  . ARG   C 1 82  ? 22.978  -32.222 -103.730 1.00 23.90 ? 175 ARG   C CG  1 
ATOM   3712 C  CD  . ARG   C 1 82  ? 22.293  -33.567 -103.614 1.00 24.60 ? 175 ARG   C CD  1 
ATOM   3713 N  NE  . ARG   C 1 82  ? 22.922  -34.550 -104.470 1.00 25.83 ? 175 ARG   C NE  1 
ATOM   3714 C  CZ  . ARG   C 1 82  ? 22.416  -35.736 -104.776 1.00 25.36 ? 175 ARG   C CZ  1 
ATOM   3715 N  NH1 . ARG   C 1 82  ? 21.235  -36.114 -104.317 1.00 24.91 ? 175 ARG   C NH1 1 
ATOM   3716 N  NH2 . ARG   C 1 82  ? 23.107  -36.541 -105.559 1.00 25.86 ? 175 ARG   C NH2 1 
ATOM   3717 N  N   . CYS   C 1 83  ? 22.999  -29.483 -107.362 1.00 23.35 ? 176 CYS   C N   1 
ATOM   3718 C  CA  . CYS   C 1 83  ? 22.559  -29.032 -108.709 1.00 23.23 ? 176 CYS   C CA  1 
ATOM   3719 C  C   . CYS   C 1 83  ? 21.244  -29.736 -109.052 1.00 23.70 ? 176 CYS   C C   1 
ATOM   3720 O  O   . CYS   C 1 83  ? 20.957  -30.805 -108.519 1.00 24.73 ? 176 CYS   C O   1 
ATOM   3721 C  CB  . CYS   C 1 83  ? 23.649  -29.312 -109.740 1.00 21.61 ? 176 CYS   C CB  1 
ATOM   3722 S  SG  . CYS   C 1 83  ? 23.893  -31.041 -110.058 1.00 21.38 ? 176 CYS   C SG  1 
ATOM   3723 N  N   . PRO   C 1 84  ? 20.376  -29.161 -109.917 1.00 24.60 ? 177 PRO   C N   1 
ATOM   3724 C  CA  . PRO   C 1 84  ? 19.138  -29.837 -110.313 1.00 24.93 ? 177 PRO   C CA  1 
ATOM   3725 C  C   . PRO   C 1 84  ? 19.358  -31.305 -110.719 1.00 24.39 ? 177 PRO   C C   1 
ATOM   3726 O  O   . PRO   C 1 84  ? 18.591  -32.139 -110.296 1.00 24.63 ? 177 PRO   C O   1 
ATOM   3727 C  CB  . PRO   C 1 84  ? 18.646  -28.980 -111.490 1.00 24.65 ? 177 PRO   C CB  1 
ATOM   3728 C  CG  . PRO   C 1 84  ? 19.146  -27.594 -111.152 1.00 24.71 ? 177 PRO   C CG  1 
ATOM   3729 C  CD  . PRO   C 1 84  ? 20.501  -27.821 -110.511 1.00 24.66 ? 177 PRO   C CD  1 
ATOM   3730 N  N   . HIS   C 1 85  ? 20.420  -31.582 -111.484 1.00 23.89 ? 178 HIS   C N   1 
ATOM   3731 C  CA  . HIS   C 1 85  ? 20.792  -32.935 -111.982 1.00 23.31 ? 178 HIS   C CA  1 
ATOM   3732 C  C   . HIS   C 1 85  ? 20.939  -33.937 -110.827 1.00 23.68 ? 178 HIS   C C   1 
ATOM   3733 O  O   . HIS   C 1 85  ? 20.254  -34.986 -110.861 1.00 24.13 ? 178 HIS   C O   1 
ATOM   3734 C  CB  . HIS   C 1 85  ? 22.073  -32.872 -112.826 1.00 22.50 ? 178 HIS   C CB  1 
ATOM   3735 C  CG  . HIS   C 1 85  ? 22.684  -34.210 -113.058 1.00 21.73 ? 178 HIS   C CG  1 
ATOM   3736 N  ND1 . HIS   C 1 85  ? 21.986  -35.239 -113.655 1.00 21.76 ? 178 HIS   C ND1 1 
ATOM   3737 C  CD2 . HIS   C 1 85  ? 23.909  -34.696 -112.770 1.00 22.08 ? 178 HIS   C CD2 1 
ATOM   3738 C  CE1 . HIS   C 1 85  ? 22.753  -36.305 -113.728 1.00 22.31 ? 178 HIS   C CE1 1 
ATOM   3739 N  NE2 . HIS   C 1 85  ? 23.941  -36.000 -113.187 1.00 22.52 ? 178 HIS   C NE2 1 
ATOM   3740 N  N   . HIS   C 1 86  ? 21.823  -33.662 -109.866 1.00 23.99 ? 179 HIS   C N   1 
ATOM   3741 C  CA  . HIS   C 1 86  ? 22.137  -34.594 -108.747 1.00 24.44 ? 179 HIS   C CA  1 
ATOM   3742 C  C   . HIS   C 1 86  ? 20.939  -34.679 -107.791 1.00 26.00 ? 179 HIS   C C   1 
ATOM   3743 O  O   . HIS   C 1 86  ? 20.718  -35.761 -107.229 1.00 27.46 ? 179 HIS   C O   1 
ATOM   3744 C  CB  . HIS   C 1 86  ? 23.444  -34.202 -108.047 1.00 22.85 ? 179 HIS   C CB  1 
ATOM   3745 C  CG  . HIS   C 1 86  ? 24.665  -34.713 -108.738 1.00 21.81 ? 179 HIS   C CG  1 
ATOM   3746 N  ND1 . HIS   C 1 86  ? 25.689  -33.879 -109.140 1.00 19.82 ? 179 HIS   C ND1 1 
ATOM   3747 C  CD2 . HIS   C 1 86  ? 25.020  -35.964 -109.112 1.00 20.90 ? 179 HIS   C CD2 1 
ATOM   3748 C  CE1 . HIS   C 1 86  ? 26.625  -34.598 -109.733 1.00 20.69 ? 179 HIS   C CE1 1 
ATOM   3749 N  NE2 . HIS   C 1 86  ? 26.236  -35.878 -109.732 1.00 20.92 ? 179 HIS   C NE2 1 
ATOM   3750 N  N   . GLU   C 1 87  ? 20.183  -33.593 -107.635 1.00 29.55 ? 180 GLU   C N   1 
ATOM   3751 C  CA  . GLU   C 1 87  ? 18.899  -33.593 -106.883 1.00 33.07 ? 180 GLU   C CA  1 
ATOM   3752 C  C   . GLU   C 1 87  ? 17.979  -34.676 -107.466 1.00 36.29 ? 180 GLU   C C   1 
ATOM   3753 O  O   . GLU   C 1 87  ? 17.329  -35.386 -106.670 1.00 37.55 ? 180 GLU   C O   1 
ATOM   3754 C  CB  . GLU   C 1 87  ? 18.251  -32.207 -106.928 1.00 33.84 ? 180 GLU   C CB  1 
ATOM   3755 C  CG  . GLU   C 1 87  ? 16.876  -32.155 -106.281 1.00 35.12 ? 180 GLU   C CG  1 
ATOM   3756 C  CD  . GLU   C 1 87  ? 16.271  -30.765 -106.176 1.00 36.34 ? 180 GLU   C CD  1 
ATOM   3757 O  OE1 . GLU   C 1 87  ? 17.023  -29.773 -106.290 1.00 35.13 ? 180 GLU   C OE1 1 
ATOM   3758 O  OE2 . GLU   C 1 87  ? 15.045  -30.679 -105.968 1.00 38.75 ? 180 GLU   C OE2 1 
ATOM   3759 N  N   . ARG   C 1 88  ? 17.958  -34.815 -108.797 1.00 38.81 ? 181 ARG   C N   1 
ATOM   3760 C  CA  . ARG   C 1 88  ? 17.004  -35.679 -109.548 1.00 41.30 ? 181 ARG   C CA  1 
ATOM   3761 C  C   . ARG   C 1 88  ? 17.586  -37.076 -109.795 1.00 40.99 ? 181 ARG   C C   1 
ATOM   3762 O  O   . ARG   C 1 88  ? 16.819  -37.938 -110.263 1.00 41.39 ? 181 ARG   C O   1 
ATOM   3763 C  CB  . ARG   C 1 88  ? 16.627  -35.024 -110.880 1.00 42.96 ? 181 ARG   C CB  1 
ATOM   3764 C  CG  . ARG   C 1 88  ? 15.754  -33.787 -110.721 1.00 45.85 ? 181 ARG   C CG  1 
ATOM   3765 C  CD  . ARG   C 1 88  ? 14.750  -33.587 -111.845 1.00 48.52 ? 181 ARG   C CD  1 
ATOM   3766 N  NE  . ARG   C 1 88  ? 15.145  -32.569 -112.812 1.00 50.44 ? 181 ARG   C NE  1 
ATOM   3767 C  CZ  . ARG   C 1 88  ? 15.154  -31.257 -112.583 1.00 51.92 ? 181 ARG   C CZ  1 
ATOM   3768 N  NH1 . ARG   C 1 88  ? 14.813  -30.779 -111.396 1.00 53.65 ? 181 ARG   C NH1 1 
ATOM   3769 N  NH2 . ARG   C 1 88  ? 15.519  -30.423 -113.543 1.00 52.07 ? 181 ARG   C NH2 1 
ATOM   3770 N  N   . CYS   C 1 89  ? 18.874  -37.300 -109.514 1.00 41.19 ? 182 CYS   C N   1 
ATOM   3771 C  CA  . CYS   C 1 89  ? 19.539  -38.623 -109.675 1.00 42.49 ? 182 CYS   C CA  1 
ATOM   3772 C  C   . CYS   C 1 89  ? 18.910  -39.633 -108.709 1.00 43.45 ? 182 CYS   C C   1 
ATOM   3773 O  O   . CYS   C 1 89  ? 18.521  -39.222 -107.595 1.00 44.51 ? 182 CYS   C O   1 
ATOM   3774 C  CB  . CYS   C 1 89  ? 21.041  -38.545 -109.425 1.00 43.04 ? 182 CYS   C CB  1 
ATOM   3775 S  SG  . CYS   C 1 89  ? 21.956  -37.826 -110.814 1.00 43.92 ? 182 CYS   C SG  1 
ATOM   3776 N  N   . SER   C 1 90  ? 18.820  -40.899 -109.126 1.00 42.88 ? 183 SER   C N   1 
ATOM   3777 C  CA  . SER   C 1 90  ? 18.353  -42.039 -108.294 1.00 42.76 ? 183 SER   C CA  1 
ATOM   3778 C  C   . SER   C 1 90  ? 19.539  -42.592 -107.489 1.00 40.57 ? 183 SER   C C   1 
ATOM   3779 O  O   . SER   C 1 90  ? 19.908  -43.769 -107.688 1.00 40.04 ? 183 SER   C O   1 
ATOM   3780 C  CB  . SER   C 1 90  ? 17.692  -43.096 -109.146 1.00 43.97 ? 183 SER   C CB  1 
ATOM   3781 O  OG  . SER   C 1 90  ? 18.583  -43.576 -110.141 1.00 46.36 ? 183 SER   C OG  1 
ATOM   3782 N  N   . ASP   C 1 91  ? 20.106  -41.758 -106.608 1.00 37.99 ? 184 ASP   C N   1 
ATOM   3783 C  CA  . ASP   C 1 91  ? 21.264  -42.095 -105.735 1.00 35.94 ? 184 ASP   C CA  1 
ATOM   3784 C  C   . ASP   C 1 91  ? 20.842  -41.978 -104.264 1.00 35.13 ? 184 ASP   C C   1 
ATOM   3785 O  O   . ASP   C 1 91  ? 21.723  -41.744 -103.420 1.00 33.90 ? 184 ASP   C O   1 
ATOM   3786 C  CB  . ASP   C 1 91  ? 22.470  -41.208 -106.064 1.00 34.93 ? 184 ASP   C CB  1 
ATOM   3787 C  CG  . ASP   C 1 91  ? 22.250  -39.717 -105.845 1.00 34.16 ? 184 ASP   C CG  1 
ATOM   3788 O  OD1 . ASP   C 1 91  ? 21.198  -39.340 -105.287 1.00 33.24 ? 184 ASP   C OD1 1 
ATOM   3789 O  OD2 . ASP   C 1 91  ? 23.138  -38.938 -106.235 1.00 32.79 ? 184 ASP   C OD2 1 
ATOM   3790 N  N   . SER   C 1 92  ? 19.545  -42.151 -103.973 1.00 35.35 ? 185 SER   C N   1 
ATOM   3791 C  CA  . SER   C 1 92  ? 18.941  -42.019 -102.619 1.00 32.98 ? 185 SER   C CA  1 
ATOM   3792 C  C   . SER   C 1 92  ? 19.395  -43.178 -101.722 1.00 32.01 ? 185 SER   C C   1 
ATOM   3793 O  O   . SER   C 1 92  ? 19.524  -44.306 -102.231 1.00 31.58 ? 185 SER   C O   1 
ATOM   3794 C  CB  . SER   C 1 92  ? 17.441  -41.955 -102.709 1.00 33.88 ? 185 SER   C CB  1 
ATOM   3795 O  OG  . SER   C 1 92  ? 16.859  -41.825 -101.422 1.00 34.45 ? 185 SER   C OG  1 
ATOM   3796 N  N   . ASP   C 1 93  ? 19.627  -42.901 -100.433 1.00 29.21 ? 186 ASP   C N   1 
ATOM   3797 C  CA  . ASP   C 1 93  ? 19.922  -43.924 -99.392  1.00 28.51 ? 186 ASP   C CA  1 
ATOM   3798 C  C   . ASP   C 1 93  ? 18.687  -44.121 -98.496  1.00 27.35 ? 186 ASP   C C   1 
ATOM   3799 O  O   . ASP   C 1 93  ? 18.783  -44.905 -97.535  1.00 28.48 ? 186 ASP   C O   1 
ATOM   3800 C  CB  . ASP   C 1 93  ? 21.169  -43.546 -98.587  1.00 28.32 ? 186 ASP   C CB  1 
ATOM   3801 C  CG  . ASP   C 1 93  ? 21.048  -42.251 -97.797  1.00 27.89 ? 186 ASP   C CG  1 
ATOM   3802 O  OD1 . ASP   C 1 93  ? 20.060  -41.520 -98.004  1.00 27.17 ? 186 ASP   C OD1 1 
ATOM   3803 O  OD2 . ASP   C 1 93  ? 21.948  -41.985 -96.982  1.00 27.00 ? 186 ASP   C OD2 1 
ATOM   3804 N  N   . GLY   C 1 94  ? 17.575  -43.438 -98.799  1.00 26.31 ? 187 GLY   C N   1 
ATOM   3805 C  CA  . GLY   C 1 94  ? 16.294  -43.559 -98.074  1.00 26.01 ? 187 GLY   C CA  1 
ATOM   3806 C  C   . GLY   C 1 94  ? 16.246  -42.712 -96.808  1.00 25.38 ? 187 GLY   C C   1 
ATOM   3807 O  O   . GLY   C 1 94  ? 15.229  -42.796 -96.090  1.00 25.58 ? 187 GLY   C O   1 
ATOM   3808 N  N   . LEU   C 1 95  ? 17.288  -41.918 -96.541  1.00 23.63 ? 188 LEU   C N   1 
ATOM   3809 C  CA  . LEU   C 1 95  ? 17.413  -41.087 -95.312  1.00 22.55 ? 188 LEU   C CA  1 
ATOM   3810 C  C   . LEU   C 1 95  ? 17.650  -39.618 -95.680  1.00 21.11 ? 188 LEU   C C   1 
ATOM   3811 O  O   . LEU   C 1 95  ? 16.940  -38.759 -95.132  1.00 20.60 ? 188 LEU   C O   1 
ATOM   3812 C  CB  . LEU   C 1 95  ? 18.556  -41.640 -94.459  1.00 22.61 ? 188 LEU   C CB  1 
ATOM   3813 C  CG  . LEU   C 1 95  ? 18.393  -43.094 -94.014  1.00 22.79 ? 188 LEU   C CG  1 
ATOM   3814 C  CD1 . LEU   C 1 95  ? 19.606  -43.558 -93.225  1.00 23.43 ? 188 LEU   C CD1 1 
ATOM   3815 C  CD2 . LEU   C 1 95  ? 17.128  -43.276 -93.196  1.00 22.80 ? 188 LEU   C CD2 1 
ATOM   3816 N  N   . ALA   C 1 96  ? 18.616  -39.344 -96.561  1.00 20.39 ? 189 ALA   C N   1 
ATOM   3817 C  CA  . ALA   C 1 96  ? 19.056  -37.978 -96.928  1.00 19.53 ? 189 ALA   C CA  1 
ATOM   3818 C  C   . ALA   C 1 96  ? 18.024  -37.331 -97.848  1.00 19.26 ? 189 ALA   C C   1 
ATOM   3819 O  O   . ALA   C 1 96  ? 17.559  -37.953 -98.801  1.00 17.22 ? 189 ALA   C O   1 
ATOM   3820 C  CB  . ALA   C 1 96  ? 20.416  -38.019 -97.578  1.00 19.75 ? 189 ALA   C CB  1 
ATOM   3821 N  N   . PRO   C 1 97  ? 17.627  -36.064 -97.591  1.00 19.10 ? 190 PRO   C N   1 
ATOM   3822 C  CA  . PRO   C 1 97  ? 16.819  -35.316 -98.549  1.00 19.24 ? 190 PRO   C CA  1 
ATOM   3823 C  C   . PRO   C 1 97  ? 17.583  -35.196 -99.864  1.00 19.92 ? 190 PRO   C C   1 
ATOM   3824 O  O   . PRO   C 1 97  ? 18.807  -35.051 -99.856  1.00 19.33 ? 190 PRO   C O   1 
ATOM   3825 C  CB  . PRO   C 1 97  ? 16.611  -33.943 -97.898  1.00 19.11 ? 190 PRO   C CB  1 
ATOM   3826 C  CG  . PRO   C 1 97  ? 16.864  -34.182 -96.424  1.00 19.05 ? 190 PRO   C CG  1 
ATOM   3827 C  CD  . PRO   C 1 97  ? 17.888  -35.297 -96.367  1.00 18.93 ? 190 PRO   C CD  1 
ATOM   3828 N  N   . PRO   C 1 98  ? 16.890  -35.269 -101.023 1.00 19.99 ? 191 PRO   C N   1 
ATOM   3829 C  CA  . PRO   C 1 98  ? 17.565  -35.246 -102.322 1.00 20.18 ? 191 PRO   C CA  1 
ATOM   3830 C  C   . PRO   C 1 98  ? 18.361  -33.963 -102.619 1.00 20.03 ? 191 PRO   C C   1 
ATOM   3831 O  O   . PRO   C 1 98  ? 19.264  -34.048 -103.430 1.00 19.62 ? 191 PRO   C O   1 
ATOM   3832 C  CB  . PRO   C 1 98  ? 16.434  -35.431 -103.355 1.00 20.46 ? 191 PRO   C CB  1 
ATOM   3833 C  CG  . PRO   C 1 98  ? 15.142  -35.163 -102.603 1.00 20.64 ? 191 PRO   C CG  1 
ATOM   3834 C  CD  . PRO   C 1 98  ? 15.433  -35.431 -101.141 1.00 20.60 ? 191 PRO   C CD  1 
ATOM   3835 N  N   . GLN   C 1 99  ? 18.035  -32.833 -101.980 1.00 19.62 ? 192 GLN   C N   1 
ATOM   3836 C  CA  . GLN   C 1 99  ? 18.713  -31.524 -102.215 1.00 20.50 ? 192 GLN   C CA  1 
ATOM   3837 C  C   . GLN   C 1 99  ? 20.011  -31.392 -101.405 1.00 19.30 ? 192 GLN   C C   1 
ATOM   3838 O  O   . GLN   C 1 99  ? 20.807  -30.487 -101.742 1.00 18.76 ? 192 GLN   C O   1 
ATOM   3839 C  CB  . GLN   C 1 99  ? 17.813  -30.355 -101.828 1.00 21.93 ? 192 GLN   C CB  1 
ATOM   3840 C  CG  . GLN   C 1 99  ? 16.649  -30.143 -102.778 1.00 23.84 ? 192 GLN   C CG  1 
ATOM   3841 C  CD  . GLN   C 1 99  ? 15.914  -28.869 -102.448 1.00 25.93 ? 192 GLN   C CD  1 
ATOM   3842 O  OE1 . GLN   C 1 99  ? 15.886  -28.421 -101.303 1.00 28.57 ? 192 GLN   C OE1 1 
ATOM   3843 N  NE2 . GLN   C 1 99  ? 15.326  -28.261 -103.463 1.00 27.98 ? 192 GLN   C NE2 1 
ATOM   3844 N  N   . HIS   C 1 100 ? 20.197  -32.205 -100.360 1.00 18.15 ? 193 HIS   C N   1 
ATOM   3845 C  CA  . HIS   C 1 100 ? 21.313  -32.066 -99.382  1.00 17.39 ? 193 HIS   C CA  1 
ATOM   3846 C  C   . HIS   C 1 100 ? 22.657  -32.475 -100.002 1.00 16.53 ? 193 HIS   C C   1 
ATOM   3847 O  O   . HIS   C 1 100 ? 22.790  -33.638 -100.462 1.00 16.16 ? 193 HIS   C O   1 
ATOM   3848 C  CB  . HIS   C 1 100 ? 21.024  -32.858 -98.100  1.00 17.48 ? 193 HIS   C CB  1 
ATOM   3849 C  CG  . HIS   C 1 100 ? 20.131  -32.134 -97.153  1.00 17.40 ? 193 HIS   C CG  1 
ATOM   3850 N  ND1 . HIS   C 1 100 ? 20.373  -32.100 -95.794  1.00 17.49 ? 193 HIS   C ND1 1 
ATOM   3851 C  CD2 . HIS   C 1 100 ? 19.007  -31.412 -97.358  1.00 17.36 ? 193 HIS   C CD2 1 
ATOM   3852 C  CE1 . HIS   C 1 100 ? 19.438  -31.390 -95.199  1.00 17.50 ? 193 HIS   C CE1 1 
ATOM   3853 N  NE2 . HIS   C 1 100 ? 18.588  -30.955 -96.136  1.00 17.31 ? 193 HIS   C NE2 1 
ATOM   3854 N  N   . LEU   C 1 101 ? 23.643  -31.578 -99.940  1.00 15.65 ? 194 LEU   C N   1 
ATOM   3855 C  CA  . LEU   C 1 101 ? 25.031  -31.861 -100.397 1.00 15.89 ? 194 LEU   C CA  1 
ATOM   3856 C  C   . LEU   C 1 101 ? 25.649  -32.948 -99.515  1.00 15.64 ? 194 LEU   C C   1 
ATOM   3857 O  O   . LEU   C 1 101 ? 26.164  -33.937 -100.066 1.00 15.84 ? 194 LEU   C O   1 
ATOM   3858 C  CB  . LEU   C 1 101 ? 25.881  -30.590 -100.333 1.00 15.94 ? 194 LEU   C CB  1 
ATOM   3859 C  CG  . LEU   C 1 101 ? 27.354  -30.790 -100.696 1.00 16.05 ? 194 LEU   C CG  1 
ATOM   3860 C  CD1 . LEU   C 1 101 ? 27.496  -31.211 -102.149 1.00 16.09 ? 194 LEU   C CD1 1 
ATOM   3861 C  CD2 . LEU   C 1 101 ? 28.153  -29.527 -100.426 1.00 16.46 ? 194 LEU   C CD2 1 
ATOM   3862 N  N   . ILE   C 1 102 ? 25.621  -32.751 -98.197  1.00 16.00 ? 195 ILE   C N   1 
ATOM   3863 C  CA  . ILE   C 1 102 ? 26.384  -33.580 -97.221  1.00 16.17 ? 195 ILE   C CA  1 
ATOM   3864 C  C   . ILE   C 1 102 ? 25.456  -34.659 -96.661  1.00 16.58 ? 195 ILE   C C   1 
ATOM   3865 O  O   . ILE   C 1 102 ? 24.399  -34.293 -96.105  1.00 15.68 ? 195 ILE   C O   1 
ATOM   3866 C  CB  . ILE   C 1 102 ? 26.995  -32.719 -96.098  1.00 16.14 ? 195 ILE   C CB  1 
ATOM   3867 C  CG1 . ILE   C 1 102 ? 27.765  -31.514 -96.652  1.00 16.41 ? 195 ILE   C CG1 1 
ATOM   3868 C  CG2 . ILE   C 1 102 ? 27.868  -33.582 -95.197  1.00 16.55 ? 195 ILE   C CG2 1 
ATOM   3869 C  CD1 . ILE   C 1 102 ? 28.402  -30.640 -95.588  1.00 16.28 ? 195 ILE   C CD1 1 
ATOM   3870 N  N   . ARG   C 1 103 ? 25.860  -35.927 -96.799  1.00 16.77 ? 196 ARG   C N   1 
ATOM   3871 C  CA  . ARG   C 1 103 ? 25.236  -37.091 -96.123  1.00 18.06 ? 196 ARG   C CA  1 
ATOM   3872 C  C   . ARG   C 1 103 ? 26.232  -37.710 -95.140  1.00 17.95 ? 196 ARG   C C   1 
ATOM   3873 O  O   . ARG   C 1 103 ? 27.457  -37.503 -95.301  1.00 17.63 ? 196 ARG   C O   1 
ATOM   3874 C  CB  . ARG   C 1 103 ? 24.832  -38.171 -97.132  1.00 18.94 ? 196 ARG   C CB  1 
ATOM   3875 C  CG  . ARG   C 1 103 ? 23.843  -37.704 -98.186  1.00 19.90 ? 196 ARG   C CG  1 
ATOM   3876 C  CD  . ARG   C 1 103 ? 23.403  -38.845 -99.081  1.00 21.01 ? 196 ARG   C CD  1 
ATOM   3877 N  NE  . ARG   C 1 103 ? 22.517  -38.360 -100.130 1.00 22.47 ? 196 ARG   C NE  1 
ATOM   3878 C  CZ  . ARG   C 1 103 ? 22.123  -39.067 -101.182 1.00 23.17 ? 196 ARG   C CZ  1 
ATOM   3879 N  NH1 . ARG   C 1 103 ? 22.530  -40.316 -101.340 1.00 24.71 ? 196 ARG   C NH1 1 
ATOM   3880 N  NH2 . ARG   C 1 103 ? 21.317  -38.521 -102.074 1.00 23.92 ? 196 ARG   C NH2 1 
ATOM   3881 N  N   . VAL   C 1 104 ? 25.717  -38.459 -94.166  1.00 18.06 ? 197 VAL   C N   1 
ATOM   3882 C  CA  . VAL   C 1 104 ? 26.526  -39.383 -93.323  1.00 18.57 ? 197 VAL   C CA  1 
ATOM   3883 C  C   . VAL   C 1 104 ? 26.186  -40.807 -93.766  1.00 19.54 ? 197 VAL   C C   1 
ATOM   3884 O  O   . VAL   C 1 104 ? 24.982  -41.129 -93.841  1.00 19.14 ? 197 VAL   C O   1 
ATOM   3885 C  CB  . VAL   C 1 104 ? 26.281  -39.167 -91.818  1.00 18.18 ? 197 VAL   C CB  1 
ATOM   3886 C  CG1 . VAL   C 1 104 ? 26.884  -40.294 -90.992  1.00 18.22 ? 197 VAL   C CG1 1 
ATOM   3887 C  CG2 . VAL   C 1 104 ? 26.815  -37.820 -91.355  1.00 17.91 ? 197 VAL   C CG2 1 
ATOM   3888 N  N   . GLU   C 1 105 ? 27.203  -41.610 -94.078  1.00 20.09 ? 198 GLU   C N   1 
ATOM   3889 C  CA  . GLU   C 1 105 ? 27.022  -43.032 -94.467  1.00 21.17 ? 198 GLU   C CA  1 
ATOM   3890 C  C   . GLU   C 1 105 ? 27.234  -43.885 -93.211  1.00 21.03 ? 198 GLU   C C   1 
ATOM   3891 O  O   . GLU   C 1 105 ? 27.961  -43.431 -92.304  1.00 20.02 ? 198 GLU   C O   1 
ATOM   3892 C  CB  . GLU   C 1 105 ? 27.952  -43.395 -95.633  1.00 22.38 ? 198 GLU   C CB  1 
ATOM   3893 C  CG  . GLU   C 1 105 ? 29.230  -44.097 -95.224  1.00 23.07 ? 198 GLU   C CG  1 
ATOM   3894 C  CD  . GLU   C 1 105 ? 30.148  -44.496 -96.368  1.00 23.90 ? 198 GLU   C CD  1 
ATOM   3895 O  OE1 . GLU   C 1 105 ? 30.254  -45.710 -96.636  1.00 25.09 ? 198 GLU   C OE1 1 
ATOM   3896 O  OE2 . GLU   C 1 105 ? 30.771  -43.600 -96.974  1.00 23.05 ? 198 GLU   C OE2 1 
ATOM   3897 N  N   . GLY   C 1 106 ? 26.573  -45.045 -93.152  1.00 21.73 ? 199 GLY   C N   1 
ATOM   3898 C  CA  . GLY   C 1 106 ? 26.775  -46.088 -92.129  1.00 21.44 ? 199 GLY   C CA  1 
ATOM   3899 C  C   . GLY   C 1 106 ? 26.356  -45.644 -90.740  1.00 21.68 ? 199 GLY   C C   1 
ATOM   3900 O  O   . GLY   C 1 106 ? 27.023  -46.060 -89.770  1.00 22.65 ? 199 GLY   C O   1 
ATOM   3901 N  N   . ASN   C 1 107 ? 25.286  -44.848 -90.629  1.00 21.35 ? 200 ASN   C N   1 
ATOM   3902 C  CA  . ASN   C 1 107 ? 24.721  -44.408 -89.324  1.00 20.97 ? 200 ASN   C CA  1 
ATOM   3903 C  C   . ASN   C 1 107 ? 23.201  -44.243 -89.456  1.00 21.19 ? 200 ASN   C C   1 
ATOM   3904 O  O   . ASN   C 1 107 ? 22.748  -43.227 -90.022  1.00 19.75 ? 200 ASN   C O   1 
ATOM   3905 C  CB  . ASN   C 1 107 ? 25.407  -43.140 -88.802  1.00 20.57 ? 200 ASN   C CB  1 
ATOM   3906 C  CG  . ASN   C 1 107 ? 25.080  -42.853 -87.349  1.00 20.41 ? 200 ASN   C CG  1 
ATOM   3907 O  OD1 . ASN   C 1 107 ? 23.979  -43.137 -86.890  1.00 21.01 ? 200 ASN   C OD1 1 
ATOM   3908 N  ND2 . ASN   C 1 107 ? 26.021  -42.286 -86.616  1.00 19.74 ? 200 ASN   C ND2 1 
ATOM   3909 N  N   . LEU   C 1 108 ? 22.444  -45.206 -88.922  1.00 22.85 ? 201 LEU   C N   1 
ATOM   3910 C  CA  . LEU   C 1 108 ? 20.957  -45.240 -88.989  1.00 23.46 ? 201 LEU   C CA  1 
ATOM   3911 C  C   . LEU   C 1 108 ? 20.338  -44.151 -88.101  1.00 22.10 ? 201 LEU   C C   1 
ATOM   3912 O  O   . LEU   C 1 108 ? 19.130  -43.910 -88.257  1.00 22.35 ? 201 LEU   C O   1 
ATOM   3913 C  CB  . LEU   C 1 108 ? 20.460  -46.629 -88.572  1.00 25.31 ? 201 LEU   C CB  1 
ATOM   3914 C  CG  . LEU   C 1 108 ? 20.432  -47.675 -89.684  1.00 27.12 ? 201 LEU   C CG  1 
ATOM   3915 C  CD1 . LEU   C 1 108 ? 19.999  -49.029 -89.138  1.00 28.52 ? 201 LEU   C CD1 1 
ATOM   3916 C  CD2 . LEU   C 1 108 ? 19.514  -47.238 -90.821  1.00 28.14 ? 201 LEU   C CD2 1 
ATOM   3917 N  N   . ARG   C 1 109 ? 21.109  -43.527 -87.206  1.00 20.67 ? 202 ARG   C N   1 
ATOM   3918 C  CA  . ARG   C 1 109 ? 20.604  -42.483 -86.272  1.00 20.44 ? 202 ARG   C CA  1 
ATOM   3919 C  C   . ARG   C 1 109 ? 20.825  -41.087 -86.869  1.00 18.70 ? 202 ARG   C C   1 
ATOM   3920 O  O   . ARG   C 1 109 ? 20.587  -40.102 -86.158  1.00 18.00 ? 202 ARG   C O   1 
ATOM   3921 C  CB  . ARG   C 1 109 ? 21.277  -42.630 -84.905  1.00 22.38 ? 202 ARG   C CB  1 
ATOM   3922 C  CG  . ARG   C 1 109 ? 21.154  -44.029 -84.315  1.00 24.03 ? 202 ARG   C CG  1 
ATOM   3923 C  CD  . ARG   C 1 109 ? 22.344  -44.401 -83.452  1.00 26.06 ? 202 ARG   C CD  1 
ATOM   3924 N  NE  . ARG   C 1 109 ? 22.140  -43.998 -82.070  1.00 27.86 ? 202 ARG   C NE  1 
ATOM   3925 C  CZ  . ARG   C 1 109 ? 23.102  -43.814 -81.175  1.00 28.07 ? 202 ARG   C CZ  1 
ATOM   3926 N  NH1 . ARG   C 1 109 ? 24.375  -43.969 -81.508  1.00 28.39 ? 202 ARG   C NH1 1 
ATOM   3927 N  NH2 . ARG   C 1 109 ? 22.781  -43.452 -79.945  1.00 27.99 ? 202 ARG   C NH2 1 
ATOM   3928 N  N   . VAL   C 1 110 ? 21.249  -41.008 -88.133  1.00 17.09 ? 203 VAL   C N   1 
ATOM   3929 C  CA  . VAL   C 1 110 ? 21.461  -39.726 -88.864  1.00 16.47 ? 203 VAL   C CA  1 
ATOM   3930 C  C   . VAL   C 1 110 ? 20.126  -38.971 -88.936  1.00 16.24 ? 203 VAL   C C   1 
ATOM   3931 O  O   . VAL   C 1 110 ? 19.066  -39.619 -89.138  1.00 15.94 ? 203 VAL   C O   1 
ATOM   3932 C  CB  . VAL   C 1 110 ? 22.058  -39.954 -90.267  1.00 16.84 ? 203 VAL   C CB  1 
ATOM   3933 C  CG1 . VAL   C 1 110 ? 21.103  -40.695 -91.188  1.00 17.05 ? 203 VAL   C CG1 1 
ATOM   3934 C  CG2 . VAL   C 1 110 ? 22.482  -38.641 -90.901  1.00 17.16 ? 203 VAL   C CG2 1 
ATOM   3935 N  N   . GLU   C 1 111 ? 20.185  -37.647 -88.773  1.00 15.09 ? 204 GLU   C N   1 
ATOM   3936 C  CA  . GLU   C 1 111 ? 19.026  -36.722 -88.855  1.00 14.68 ? 204 GLU   C CA  1 
ATOM   3937 C  C   . GLU   C 1 111 ? 19.396  -35.573 -89.799  1.00 14.79 ? 204 GLU   C C   1 
ATOM   3938 O  O   . GLU   C 1 111 ? 20.535  -35.090 -89.711  1.00 14.37 ? 204 GLU   C O   1 
ATOM   3939 C  CB  . GLU   C 1 111 ? 18.674  -36.253 -87.444  1.00 14.35 ? 204 GLU   C CB  1 
ATOM   3940 C  CG  . GLU   C 1 111 ? 17.754  -35.052 -87.388  1.00 14.50 ? 204 GLU   C CG  1 
ATOM   3941 C  CD  . GLU   C 1 111 ? 17.525  -34.535 -85.980  1.00 14.30 ? 204 GLU   C CD  1 
ATOM   3942 O  OE1 . GLU   C 1 111 ? 17.520  -35.361 -85.044  1.00 13.81 ? 204 GLU   C OE1 1 
ATOM   3943 O  OE2 . GLU   C 1 111 ? 17.356  -33.309 -85.826  1.00 14.35 ? 204 GLU   C OE2 1 
ATOM   3944 N  N   . TYR   C 1 112 ? 18.482  -35.189 -90.692  1.00 14.90 ? 205 TYR   C N   1 
ATOM   3945 C  CA  . TYR   C 1 112 ? 18.674  -34.092 -91.675  1.00 15.32 ? 205 TYR   C CA  1 
ATOM   3946 C  C   . TYR   C 1 112 ? 17.721  -32.947 -91.333  1.00 15.60 ? 205 TYR   C C   1 
ATOM   3947 O  O   . TYR   C 1 112 ? 16.568  -33.224 -90.973  1.00 15.93 ? 205 TYR   C O   1 
ATOM   3948 C  CB  . TYR   C 1 112 ? 18.490  -34.622 -93.098  1.00 15.33 ? 205 TYR   C CB  1 
ATOM   3949 C  CG  . TYR   C 1 112 ? 19.573  -35.582 -93.519  1.00 15.15 ? 205 TYR   C CG  1 
ATOM   3950 C  CD1 . TYR   C 1 112 ? 20.729  -35.127 -94.126  1.00 15.54 ? 205 TYR   C CD1 1 
ATOM   3951 C  CD2 . TYR   C 1 112 ? 19.453  -36.944 -93.292  1.00 15.39 ? 205 TYR   C CD2 1 
ATOM   3952 C  CE1 . TYR   C 1 112 ? 21.738  -35.995 -94.512  1.00 15.17 ? 205 TYR   C CE1 1 
ATOM   3953 C  CE2 . TYR   C 1 112 ? 20.454  -37.828 -93.665  1.00 15.37 ? 205 TYR   C CE2 1 
ATOM   3954 C  CZ  . TYR   C 1 112 ? 21.596  -37.352 -94.286  1.00 15.14 ? 205 TYR   C CZ  1 
ATOM   3955 O  OH  . TYR   C 1 112 ? 22.595  -38.201 -94.656  1.00 14.83 ? 205 TYR   C OH  1 
ATOM   3956 N  N   . LEU   C 1 113 ? 18.211  -31.707 -91.413  1.00 16.16 ? 206 LEU   C N   1 
ATOM   3957 C  CA  . LEU   C 1 113 ? 17.430  -30.480 -91.112  1.00 16.68 ? 206 LEU   C CA  1 
ATOM   3958 C  C   . LEU   C 1 113 ? 17.432  -29.552 -92.331  1.00 16.96 ? 206 LEU   C C   1 
ATOM   3959 O  O   . LEU   C 1 113 ? 18.517  -29.286 -92.864  1.00 16.25 ? 206 LEU   C O   1 
ATOM   3960 C  CB  . LEU   C 1 113 ? 18.034  -29.764 -89.900  1.00 16.23 ? 206 LEU   C CB  1 
ATOM   3961 C  CG  . LEU   C 1 113 ? 17.370  -28.433 -89.541  1.00 16.33 ? 206 LEU   C CG  1 
ATOM   3962 C  CD1 . LEU   C 1 113 ? 15.921  -28.643 -89.124  1.00 16.78 ? 206 LEU   C CD1 1 
ATOM   3963 C  CD2 . LEU   C 1 113 ? 18.133  -27.710 -88.443  1.00 16.16 ? 206 LEU   C CD2 1 
ATOM   3964 N  N   . ASP   C 1 114 ? 16.246  -29.089 -92.739  1.00 17.95 ? 207 ASP   C N   1 
ATOM   3965 C  CA  . ASP   C 1 114 ? 16.044  -27.825 -93.496  1.00 19.31 ? 207 ASP   C CA  1 
ATOM   3966 C  C   . ASP   C 1 114 ? 15.649  -26.763 -92.470  1.00 20.00 ? 207 ASP   C C   1 
ATOM   3967 O  O   . ASP   C 1 114 ? 14.563  -26.903 -91.881  1.00 20.19 ? 207 ASP   C O   1 
ATOM   3968 C  CB  . ASP   C 1 114 ? 14.939  -27.940 -94.552  1.00 19.66 ? 207 ASP   C CB  1 
ATOM   3969 C  CG  . ASP   C 1 114 ? 15.237  -28.853 -95.730  1.00 19.94 ? 207 ASP   C CG  1 
ATOM   3970 O  OD1 . ASP   C 1 114 ? 16.361  -29.386 -95.815  1.00 19.75 ? 207 ASP   C OD1 1 
ATOM   3971 O  OD2 . ASP   C 1 114 ? 14.335  -29.016 -96.560  1.00 19.87 ? 207 ASP   C OD2 1 
ATOM   3972 N  N   . ASP   C 1 115 ? 16.512  -25.781 -92.216  1.00 21.05 ? 208 ASP   C N   1 
ATOM   3973 C  CA  . ASP   C 1 115 ? 16.244  -24.716 -91.217  1.00 21.13 ? 208 ASP   C CA  1 
ATOM   3974 C  C   . ASP   C 1 115 ? 15.003  -23.937 -91.669  1.00 21.46 ? 208 ASP   C C   1 
ATOM   3975 O  O   . ASP   C 1 115 ? 14.986  -23.477 -92.817  1.00 20.80 ? 208 ASP   C O   1 
ATOM   3976 C  CB  . ASP   C 1 115 ? 17.454  -23.804 -91.027  1.00 21.01 ? 208 ASP   C CB  1 
ATOM   3977 C  CG  . ASP   C 1 115 ? 17.323  -22.928 -89.796  1.00 21.20 ? 208 ASP   C CG  1 
ATOM   3978 O  OD1 . ASP   C 1 115 ? 16.582  -21.931 -89.865  1.00 21.56 ? 208 ASP   C OD1 1 
ATOM   3979 O  OD2 . ASP   C 1 115 ? 17.930  -23.272 -88.767  1.00 21.34 ? 208 ASP   C OD2 1 
ATOM   3980 N  N   . ARG   C 1 116 ? 14.000  -23.819 -90.796  1.00 24.08 ? 209 ARG   C N   1 
ATOM   3981 C  CA  . ARG   C 1 116 ? 12.687  -23.199 -91.119  1.00 27.08 ? 209 ARG   C CA  1 
ATOM   3982 C  C   . ARG   C 1 116 ? 12.856  -21.693 -91.385  1.00 27.09 ? 209 ARG   C C   1 
ATOM   3983 O  O   . ARG   C 1 116 ? 11.984  -21.135 -92.079  1.00 27.07 ? 209 ARG   C O   1 
ATOM   3984 C  CB  . ARG   C 1 116 ? 11.678  -23.487 -90.001  1.00 29.65 ? 209 ARG   C CB  1 
ATOM   3985 C  CG  . ARG   C 1 116 ? 11.967  -22.788 -88.681  1.00 31.85 ? 209 ARG   C CG  1 
ATOM   3986 C  CD  . ARG   C 1 116 ? 11.180  -23.393 -87.534  1.00 34.14 ? 209 ARG   C CD  1 
ATOM   3987 N  NE  . ARG   C 1 116 ? 11.112  -22.488 -86.392  1.00 35.71 ? 209 ARG   C NE  1 
ATOM   3988 C  CZ  . ARG   C 1 116 ? 12.080  -22.299 -85.496  1.00 37.04 ? 209 ARG   C CZ  1 
ATOM   3989 N  NH1 . ARG   C 1 116 ? 13.226  -22.955 -85.586  1.00 38.56 ? 209 ARG   C NH1 1 
ATOM   3990 N  NH2 . ARG   C 1 116 ? 11.893  -21.444 -84.504  1.00 37.42 ? 209 ARG   C NH2 1 
ATOM   3991 N  N   . ASN   C 1 117 ? 13.927  -21.070 -90.871  1.00 27.06 ? 210 ASN   C N   1 
ATOM   3992 C  CA  . ASN   C 1 117 ? 14.191  -19.608 -90.975  1.00 27.56 ? 210 ASN   C CA  1 
ATOM   3993 C  C   . ASN   C 1 117 ? 15.286  -19.326 -92.016  1.00 27.74 ? 210 ASN   C C   1 
ATOM   3994 O  O   . ASN   C 1 117 ? 15.048  -18.476 -92.899  1.00 27.57 ? 210 ASN   C O   1 
ATOM   3995 C  CB  . ASN   C 1 117 ? 14.539  -19.016 -89.608  1.00 28.49 ? 210 ASN   C CB  1 
ATOM   3996 C  CG  . ASN   C 1 117 ? 13.355  -19.006 -88.665  1.00 29.82 ? 210 ASN   C CG  1 
ATOM   3997 O  OD1 . ASN   C 1 117 ? 13.463  -19.434 -87.518  1.00 31.06 ? 210 ASN   C OD1 1 
ATOM   3998 N  ND2 . ASN   C 1 117 ? 12.213  -18.540 -89.145  1.00 29.82 ? 210 ASN   C ND2 1 
ATOM   3999 N  N   . THR   C 1 118 ? 16.436  -20.006 -91.933  1.00 26.18 ? 211 THR   C N   1 
ATOM   4000 C  CA  . THR   C 1 118 ? 17.635  -19.729 -92.773  1.00 25.49 ? 211 THR   C CA  1 
ATOM   4001 C  C   . THR   C 1 118 ? 17.574  -20.537 -94.078  1.00 24.12 ? 211 THR   C C   1 
ATOM   4002 O  O   . THR   C 1 118 ? 18.277  -20.150 -95.025  1.00 24.45 ? 211 THR   C O   1 
ATOM   4003 C  CB  . THR   C 1 118 ? 18.932  -19.997 -91.994  1.00 25.93 ? 211 THR   C CB  1 
ATOM   4004 O  OG1 . THR   C 1 118 ? 19.091  -21.406 -91.822  1.00 26.55 ? 211 THR   C OG1 1 
ATOM   4005 C  CG2 . THR   C 1 118 ? 18.961  -19.320 -90.640  1.00 26.02 ? 211 THR   C CG2 1 
ATOM   4006 N  N   . PHE   C 1 119 ? 16.787  -21.622 -94.112  1.00 22.28 ? 212 PHE   C N   1 
ATOM   4007 C  CA  . PHE   C 1 119 ? 16.661  -22.593 -95.237  1.00 22.04 ? 212 PHE   C CA  1 
ATOM   4008 C  C   . PHE   C 1 119 ? 17.986  -23.337 -95.464  1.00 20.01 ? 212 PHE   C C   1 
ATOM   4009 O  O   . PHE   C 1 119 ? 18.127  -23.998 -96.508  1.00 18.99 ? 212 PHE   C O   1 
ATOM   4010 C  CB  . PHE   C 1 119 ? 16.176  -21.905 -96.517  1.00 23.28 ? 212 PHE   C CB  1 
ATOM   4011 C  CG  . PHE   C 1 119 ? 15.005  -20.979 -96.312  1.00 24.58 ? 212 PHE   C CG  1 
ATOM   4012 C  CD1 . PHE   C 1 119 ? 13.846  -21.430 -95.698  1.00 25.23 ? 212 PHE   C CD1 1 
ATOM   4013 C  CD2 . PHE   C 1 119 ? 15.071  -19.652 -96.707  1.00 25.88 ? 212 PHE   C CD2 1 
ATOM   4014 C  CE1 . PHE   C 1 119 ? 12.769  -20.579 -95.501  1.00 25.69 ? 212 PHE   C CE1 1 
ATOM   4015 C  CE2 . PHE   C 1 119 ? 13.993  -18.801 -96.508  1.00 26.37 ? 212 PHE   C CE2 1 
ATOM   4016 C  CZ  . PHE   C 1 119 ? 12.847  -19.264 -95.899  1.00 26.34 ? 212 PHE   C CZ  1 
ATOM   4017 N  N   . ARG   C 1 120 ? 18.918  -23.252 -94.512  1.00 19.16 ? 213 ARG   C N   1 
ATOM   4018 C  CA  . ARG   C 1 120 ? 20.228  -23.950 -94.573  1.00 19.23 ? 213 ARG   C CA  1 
ATOM   4019 C  C   . ARG   C 1 120 ? 19.981  -25.445 -94.366  1.00 18.20 ? 213 ARG   C C   1 
ATOM   4020 O  O   . ARG   C 1 120 ? 19.090  -25.792 -93.555  1.00 16.93 ? 213 ARG   C O   1 
ATOM   4021 C  CB  . ARG   C 1 120 ? 21.182  -23.419 -93.500  1.00 19.90 ? 213 ARG   C CB  1 
ATOM   4022 C  CG  . ARG   C 1 120 ? 21.515  -21.939 -93.640  1.00 20.28 ? 213 ARG   C CG  1 
ATOM   4023 C  CD  . ARG   C 1 120 ? 22.746  -21.713 -94.487  1.00 20.61 ? 213 ARG   C CD  1 
ATOM   4024 N  NE  . ARG   C 1 120 ? 23.084  -20.301 -94.628  1.00 20.70 ? 213 ARG   C NE  1 
ATOM   4025 C  CZ  . ARG   C 1 120 ? 24.006  -19.829 -95.463  1.00 21.41 ? 213 ARG   C CZ  1 
ATOM   4026 N  NH1 . ARG   C 1 120 ? 24.690  -20.654 -96.239  1.00 21.52 ? 213 ARG   C NH1 1 
ATOM   4027 N  NH2 . ARG   C 1 120 ? 24.248  -18.531 -95.519  1.00 21.90 ? 213 ARG   C NH2 1 
ATOM   4028 N  N   . HIS   C 1 121 ? 20.740  -26.287 -95.071  1.00 17.62 ? 214 HIS   C N   1 
ATOM   4029 C  CA  . HIS   C 1 121 ? 20.745  -27.763 -94.896  1.00 16.67 ? 214 HIS   C CA  1 
ATOM   4030 C  C   . HIS   C 1 121 ? 21.826  -28.135 -93.883  1.00 16.29 ? 214 HIS   C C   1 
ATOM   4031 O  O   . HIS   C 1 121 ? 22.920  -27.549 -93.940  1.00 16.06 ? 214 HIS   C O   1 
ATOM   4032 C  CB  . HIS   C 1 121 ? 20.991  -28.484 -96.224  1.00 16.83 ? 214 HIS   C CB  1 
ATOM   4033 C  CG  . HIS   C 1 121 ? 20.013  -28.122 -97.288  1.00 16.96 ? 214 HIS   C CG  1 
ATOM   4034 N  ND1 . HIS   C 1 121 ? 20.281  -28.320 -98.623  1.00 17.57 ? 214 HIS   C ND1 1 
ATOM   4035 C  CD2 . HIS   C 1 121 ? 18.785  -27.567 -97.221  1.00 17.18 ? 214 HIS   C CD2 1 
ATOM   4036 C  CE1 . HIS   C 1 121 ? 19.253  -27.910 -99.339  1.00 17.74 ? 214 HIS   C CE1 1 
ATOM   4037 N  NE2 . HIS   C 1 121 ? 18.322  -27.443 -98.501  1.00 17.19 ? 214 HIS   C NE2 1 
ATOM   4038 N  N   . SER   C 1 122 ? 21.548  -29.098 -93.007  1.00 15.50 ? 215 SER   C N   1 
ATOM   4039 C  CA  . SER   C 1 122 ? 22.588  -29.693 -92.133  1.00 14.94 ? 215 SER   C CA  1 
ATOM   4040 C  C   . SER   C 1 122 ? 22.263  -31.161 -91.864  1.00 14.52 ? 215 SER   C C   1 
ATOM   4041 O  O   . SER   C 1 122 ? 21.099  -31.572 -92.055  1.00 14.45 ? 215 SER   C O   1 
ATOM   4042 C  CB  . SER   C 1 122 ? 22.786  -28.889 -90.868  1.00 14.90 ? 215 SER   C CB  1 
ATOM   4043 O  OG  . SER   C 1 122 ? 21.597  -28.802 -90.101  1.00 14.83 ? 215 SER   C OG  1 
ATOM   4044 N  N   . VAL   C 1 123 ? 23.289  -31.918 -91.483  1.00 14.26 ? 216 VAL   C N   1 
ATOM   4045 C  CA  . VAL   C 1 123 ? 23.193  -33.362 -91.142  1.00 14.01 ? 216 VAL   C CA  1 
ATOM   4046 C  C   . VAL   C 1 123 ? 23.834  -33.542 -89.765  1.00 14.03 ? 216 VAL   C C   1 
ATOM   4047 O  O   . VAL   C 1 123 ? 24.937  -33.003 -89.541  1.00 12.97 ? 216 VAL   C O   1 
ATOM   4048 C  CB  . VAL   C 1 123 ? 23.837  -34.252 -92.219  1.00 13.71 ? 216 VAL   C CB  1 
ATOM   4049 C  CG1 . VAL   C 1 123 ? 25.275  -33.858 -92.529  1.00 13.58 ? 216 VAL   C CG1 1 
ATOM   4050 C  CG2 . VAL   C 1 123 ? 23.740  -35.724 -91.849  1.00 13.94 ? 216 VAL   C CG2 1 
ATOM   4051 N  N   . VAL   C 1 124 ? 23.136  -34.241 -88.875  1.00 14.54 ? 217 VAL   C N   1 
ATOM   4052 C  CA  . VAL   C 1 124 ? 23.517  -34.367 -87.442  1.00 15.80 ? 217 VAL   C CA  1 
ATOM   4053 C  C   . VAL   C 1 124 ? 23.437  -35.848 -87.066  1.00 16.31 ? 217 VAL   C C   1 
ATOM   4054 O  O   . VAL   C 1 124 ? 22.515  -36.542 -87.538  1.00 16.13 ? 217 VAL   C O   1 
ATOM   4055 C  CB  . VAL   C 1 124 ? 22.652  -33.450 -86.546  1.00 16.03 ? 217 VAL   C CB  1 
ATOM   4056 C  CG1 . VAL   C 1 124 ? 21.174  -33.798 -86.594  1.00 16.25 ? 217 VAL   C CG1 1 
ATOM   4057 C  CG2 . VAL   C 1 124 ? 23.140  -33.417 -85.107  1.00 16.13 ? 217 VAL   C CG2 1 
ATOM   4058 N  N   . VAL   C 1 125 ? 24.420  -36.309 -86.295  1.00 16.97 ? 218 VAL   C N   1 
ATOM   4059 C  CA  . VAL   C 1 125 ? 24.477  -37.680 -85.716  1.00 17.10 ? 218 VAL   C CA  1 
ATOM   4060 C  C   . VAL   C 1 125 ? 24.707  -37.542 -84.216  1.00 17.14 ? 218 VAL   C C   1 
ATOM   4061 O  O   . VAL   C 1 125 ? 25.301  -36.565 -83.761  1.00 16.59 ? 218 VAL   C O   1 
ATOM   4062 C  CB  . VAL   C 1 125 ? 25.581  -38.531 -86.371  1.00 17.20 ? 218 VAL   C CB  1 
ATOM   4063 C  CG1 . VAL   C 1 125 ? 25.281  -38.810 -87.836  1.00 17.67 ? 218 VAL   C CG1 1 
ATOM   4064 C  CG2 . VAL   C 1 125 ? 26.960  -37.907 -86.207  1.00 17.46 ? 218 VAL   C CG2 1 
ATOM   4065 N  N   . PRO   C 1 126 ? 24.260  -38.524 -83.405  1.00 17.65 ? 219 PRO   C N   1 
ATOM   4066 C  CA  . PRO   C 1 126 ? 24.657  -38.586 -82.002  1.00 17.84 ? 219 PRO   C CA  1 
ATOM   4067 C  C   . PRO   C 1 126 ? 26.188  -38.678 -81.914  1.00 18.57 ? 219 PRO   C C   1 
ATOM   4068 O  O   . PRO   C 1 126 ? 26.787  -39.419 -82.677  1.00 18.57 ? 219 PRO   C O   1 
ATOM   4069 C  CB  . PRO   C 1 126 ? 23.977  -39.862 -81.470  1.00 18.02 ? 219 PRO   C CB  1 
ATOM   4070 C  CG  . PRO   C 1 126 ? 22.868  -40.157 -82.464  1.00 17.91 ? 219 PRO   C CG  1 
ATOM   4071 C  CD  . PRO   C 1 126 ? 23.364  -39.625 -83.793  1.00 17.87 ? 219 PRO   C CD  1 
ATOM   4072 N  N   . TYR   C 1 127 ? 26.800  -37.907 -81.016  1.00 19.51 ? 220 TYR   C N   1 
ATOM   4073 C  CA  . TYR   C 1 127 ? 28.229  -38.073 -80.654  1.00 19.83 ? 220 TYR   C CA  1 
ATOM   4074 C  C   . TYR   C 1 127 ? 28.404  -39.424 -79.961  1.00 21.11 ? 220 TYR   C C   1 
ATOM   4075 O  O   . TYR   C 1 127 ? 27.646  -39.704 -79.027  1.00 21.50 ? 220 TYR   C O   1 
ATOM   4076 C  CB  . TYR   C 1 127 ? 28.734  -36.956 -79.741  1.00 19.22 ? 220 TYR   C CB  1 
ATOM   4077 C  CG  . TYR   C 1 127 ? 30.139  -37.203 -79.261  1.00 18.52 ? 220 TYR   C CG  1 
ATOM   4078 C  CD1 . TYR   C 1 127 ? 31.226  -36.924 -80.074  1.00 18.05 ? 220 TYR   C CD1 1 
ATOM   4079 C  CD2 . TYR   C 1 127 ? 30.382  -37.754 -78.012  1.00 18.24 ? 220 TYR   C CD2 1 
ATOM   4080 C  CE1 . TYR   C 1 127 ? 32.522  -37.165 -79.653  1.00 17.86 ? 220 TYR   C CE1 1 
ATOM   4081 C  CE2 . TYR   C 1 127 ? 31.675  -38.004 -77.578  1.00 18.28 ? 220 TYR   C CE2 1 
ATOM   4082 C  CZ  . TYR   C 1 127 ? 32.748  -37.701 -78.398  1.00 18.41 ? 220 TYR   C CZ  1 
ATOM   4083 O  OH  . TYR   C 1 127 ? 34.025  -37.946 -77.982  1.00 19.27 ? 220 TYR   C OH  1 
ATOM   4084 N  N   . GLU   C 1 128 ? 29.362  -40.230 -80.427  1.00 24.16 ? 221 GLU   C N   1 
ATOM   4085 C  CA  . GLU   C 1 128 ? 29.810  -41.485 -79.764  1.00 26.57 ? 221 GLU   C CA  1 
ATOM   4086 C  C   . GLU   C 1 128 ? 31.248  -41.279 -79.301  1.00 27.21 ? 221 GLU   C C   1 
ATOM   4087 O  O   . GLU   C 1 128 ? 32.079  -40.812 -80.080  1.00 25.71 ? 221 GLU   C O   1 
ATOM   4088 C  CB  . GLU   C 1 128 ? 29.745  -42.683 -80.714  1.00 29.00 ? 221 GLU   C CB  1 
ATOM   4089 C  CG  . GLU   C 1 128 ? 28.372  -42.934 -81.311  1.00 31.14 ? 221 GLU   C CG  1 
ATOM   4090 C  CD  . GLU   C 1 128 ? 28.376  -43.881 -82.500  1.00 32.91 ? 221 GLU   C CD  1 
ATOM   4091 O  OE1 . GLU   C 1 128 ? 27.311  -44.046 -83.129  1.00 36.05 ? 221 GLU   C OE1 1 
ATOM   4092 O  OE2 . GLU   C 1 128 ? 29.446  -44.445 -82.804  1.00 35.34 ? 221 GLU   C OE2 1 
ATOM   4093 N  N   . PRO   C 1 129 ? 31.588  -41.609 -78.032  1.00 28.55 ? 222 PRO   C N   1 
ATOM   4094 C  CA  . PRO   C 1 129 ? 32.973  -41.531 -77.570  1.00 29.12 ? 222 PRO   C CA  1 
ATOM   4095 C  C   . PRO   C 1 129 ? 33.829  -42.495 -78.390  1.00 29.89 ? 222 PRO   C C   1 
ATOM   4096 O  O   . PRO   C 1 129 ? 33.298  -43.443 -78.965  1.00 30.51 ? 222 PRO   C O   1 
ATOM   4097 C  CB  . PRO   C 1 129 ? 32.928  -41.933 -76.085  1.00 29.22 ? 222 PRO   C CB  1 
ATOM   4098 C  CG  . PRO   C 1 129 ? 31.454  -41.933 -75.702  1.00 29.34 ? 222 PRO   C CG  1 
ATOM   4099 C  CD  . PRO   C 1 129 ? 30.672  -42.102 -76.990  1.00 28.82 ? 222 PRO   C CD  1 
ATOM   4100 N  N   . PRO   C 1 130 ? 35.164  -42.289 -78.492  1.00 31.35 ? 223 PRO   C N   1 
ATOM   4101 C  CA  . PRO   C 1 130 ? 36.020  -43.200 -79.254  1.00 32.97 ? 223 PRO   C CA  1 
ATOM   4102 C  C   . PRO   C 1 130 ? 35.832  -44.669 -78.841  1.00 35.22 ? 223 PRO   C C   1 
ATOM   4103 O  O   . PRO   C 1 130 ? 35.569  -44.941 -77.682  1.00 33.49 ? 223 PRO   C O   1 
ATOM   4104 C  CB  . PRO   C 1 130 ? 37.446  -42.724 -78.938  1.00 32.49 ? 223 PRO   C CB  1 
ATOM   4105 C  CG  . PRO   C 1 130 ? 37.279  -41.266 -78.562  1.00 31.80 ? 223 PRO   C CG  1 
ATOM   4106 C  CD  . PRO   C 1 130 ? 35.921  -41.179 -77.893  1.00 31.25 ? 223 PRO   C CD  1 
ATOM   4107 N  N   . GLU   C 1 131 ? 35.970  -45.578 -79.807  1.00 38.90 ? 224 GLU   C N   1 
ATOM   4108 C  CA  . GLU   C 1 131 ? 35.792  -47.039 -79.610  1.00 41.78 ? 224 GLU   C CA  1 
ATOM   4109 C  C   . GLU   C 1 131 ? 36.940  -47.576 -78.748  1.00 41.64 ? 224 GLU   C C   1 
ATOM   4110 O  O   . GLU   C 1 131 ? 38.060  -47.072 -78.816  1.00 42.27 ? 224 GLU   C O   1 
ATOM   4111 C  CB  . GLU   C 1 131 ? 35.739  -47.752 -80.961  1.00 43.56 ? 224 GLU   C CB  1 
ATOM   4112 C  CG  . GLU   C 1 131 ? 34.837  -48.968 -80.957  1.00 45.47 ? 224 GLU   C CG  1 
ATOM   4113 C  CD  . GLU   C 1 131 ? 33.348  -48.669 -80.990  1.00 45.64 ? 224 GLU   C CD  1 
ATOM   4114 O  OE1 . GLU   C 1 131 ? 32.606  -49.300 -80.215  1.00 47.28 ? 224 GLU   C OE1 1 
ATOM   4115 O  OE2 . GLU   C 1 131 ? 32.932  -47.811 -81.796  1.00 47.69 ? 224 GLU   C OE2 1 
ATOM   4116 N  N   . SER   C 1 134 ? 40.984  -46.584 -79.379  1.00 39.96 ? 227 SER   C N   1 
ATOM   4117 C  CA  . SER   C 1 134 ? 40.976  -45.454 -80.354  1.00 39.65 ? 227 SER   C CA  1 
ATOM   4118 C  C   . SER   C 1 134 ? 41.117  -44.123 -79.606  1.00 38.66 ? 227 SER   C C   1 
ATOM   4119 O  O   . SER   C 1 134 ? 40.732  -44.068 -78.420  1.00 38.23 ? 227 SER   C O   1 
ATOM   4120 C  CB  . SER   C 1 134 ? 39.730  -45.480 -81.204  1.00 40.51 ? 227 SER   C CB  1 
ATOM   4121 O  OG  . SER   C 1 134 ? 39.725  -44.407 -82.135  1.00 42.37 ? 227 SER   C OG  1 
ATOM   4122 N  N   . ASP   C 1 135 ? 41.654  -43.097 -80.276  1.00 36.39 ? 228 ASP   C N   1 
ATOM   4123 C  CA  . ASP   C 1 135 ? 41.909  -41.750 -79.694  1.00 34.67 ? 228 ASP   C CA  1 
ATOM   4124 C  C   . ASP   C 1 135 ? 40.962  -40.705 -80.303  1.00 31.10 ? 228 ASP   C C   1 
ATOM   4125 O  O   . ASP   C 1 135 ? 41.063  -39.530 -79.899  1.00 29.01 ? 228 ASP   C O   1 
ATOM   4126 C  CB  . ASP   C 1 135 ? 43.371  -41.343 -79.890  1.00 37.99 ? 228 ASP   C CB  1 
ATOM   4127 C  CG  . ASP   C 1 135 ? 44.337  -42.121 -79.012  1.00 41.28 ? 228 ASP   C CG  1 
ATOM   4128 O  OD1 . ASP   C 1 135 ? 44.072  -42.217 -77.790  1.00 43.23 ? 228 ASP   C OD1 1 
ATOM   4129 O  OD2 . ASP   C 1 135 ? 45.342  -42.630 -79.557  1.00 43.84 ? 228 ASP   C OD2 1 
ATOM   4130 N  N   . CYS   C 1 136 ? 40.078  -41.099 -81.228  1.00 27.85 ? 229 CYS   C N   1 
ATOM   4131 C  CA  . CYS   C 1 136 ? 39.122  -40.175 -81.899  1.00 26.09 ? 229 CYS   C CA  1 
ATOM   4132 C  C   . CYS   C 1 136 ? 37.863  -40.914 -82.361  1.00 25.05 ? 229 CYS   C C   1 
ATOM   4133 O  O   . CYS   C 1 136 ? 37.889  -42.157 -82.467  1.00 24.45 ? 229 CYS   C O   1 
ATOM   4134 C  CB  . CYS   C 1 136 ? 39.771  -39.479 -83.089  1.00 25.37 ? 229 CYS   C CB  1 
ATOM   4135 S  SG  . CYS   C 1 136 ? 40.395  -40.613 -84.354  1.00 23.67 ? 229 CYS   C SG  1 
ATOM   4136 N  N   . THR   C 1 137 ? 36.800  -40.151 -82.614  1.00 23.49 ? 230 THR   C N   1 
ATOM   4137 C  CA  . THR   C 1 137 ? 35.539  -40.627 -83.232  1.00 22.45 ? 230 THR   C CA  1 
ATOM   4138 C  C   . THR   C 1 137 ? 35.563  -40.259 -84.716  1.00 21.66 ? 230 THR   C C   1 
ATOM   4139 O  O   . THR   C 1 137 ? 35.725  -39.057 -85.021  1.00 21.67 ? 230 THR   C O   1 
ATOM   4140 C  CB  . THR   C 1 137 ? 34.306  -40.018 -82.558  1.00 23.05 ? 230 THR   C CB  1 
ATOM   4141 O  OG1 . THR   C 1 137 ? 34.327  -40.363 -81.171  1.00 24.06 ? 230 THR   C OG1 1 
ATOM   4142 C  CG2 . THR   C 1 137 ? 33.016  -40.492 -83.191  1.00 23.11 ? 230 THR   C CG2 1 
ATOM   4143 N  N   . THR   C 1 138 ? 35.371  -41.242 -85.595  1.00 19.94 ? 231 THR   C N   1 
ATOM   4144 C  CA  . THR   C 1 138 ? 35.348  -41.046 -87.065  1.00 19.45 ? 231 THR   C CA  1 
ATOM   4145 C  C   . THR   C 1 138 ? 33.896  -41.019 -87.541  1.00 18.97 ? 231 THR   C C   1 
ATOM   4146 O  O   . THR   C 1 138 ? 33.138  -41.940 -87.185  1.00 18.78 ? 231 THR   C O   1 
ATOM   4147 C  CB  . THR   C 1 138 ? 36.171  -42.119 -87.778  1.00 19.26 ? 231 THR   C CB  1 
ATOM   4148 O  OG1 . THR   C 1 138 ? 37.496  -41.992 -87.267  1.00 20.08 ? 231 THR   C OG1 1 
ATOM   4149 C  CG2 . THR   C 1 138 ? 36.172  -41.967 -89.284  1.00 19.22 ? 231 THR   C CG2 1 
ATOM   4150 N  N   . ILE   C 1 139 ? 33.536  -39.978 -88.288  1.00 18.14 ? 232 ILE   C N   1 
ATOM   4151 C  CA  . ILE   C 1 139 ? 32.257  -39.892 -89.048  1.00 18.31 ? 232 ILE   C CA  1 
ATOM   4152 C  C   . ILE   C 1 139 ? 32.614  -40.047 -90.523  1.00 18.02 ? 232 ILE   C C   1 
ATOM   4153 O  O   . ILE   C 1 139 ? 33.618  -39.439 -90.949  1.00 17.22 ? 232 ILE   C O   1 
ATOM   4154 C  CB  . ILE   C 1 139 ? 31.511  -38.579 -88.747  1.00 18.33 ? 232 ILE   C CB  1 
ATOM   4155 C  CG1 . ILE   C 1 139 ? 31.219  -38.445 -87.250  1.00 18.64 ? 232 ILE   C CG1 1 
ATOM   4156 C  CG2 . ILE   C 1 139 ? 30.246  -38.475 -89.592  1.00 18.64 ? 232 ILE   C CG2 1 
ATOM   4157 C  CD1 . ILE   C 1 139 ? 30.473  -37.189 -86.873  1.00 19.03 ? 232 ILE   C CD1 1 
ATOM   4158 N  N   . HIS   C 1 140 ? 31.859  -40.877 -91.245  1.00 17.96 ? 233 HIS   C N   1 
ATOM   4159 C  CA  . HIS   C 1 140 ? 31.991  -41.065 -92.712  1.00 18.40 ? 233 HIS   C CA  1 
ATOM   4160 C  C   . HIS   C 1 140 ? 30.976  -40.174 -93.421  1.00 17.89 ? 233 HIS   C C   1 
ATOM   4161 O  O   . HIS   C 1 140 ? 29.792  -40.556 -93.483  1.00 17.08 ? 233 HIS   C O   1 
ATOM   4162 C  CB  . HIS   C 1 140 ? 31.827  -42.535 -93.109  1.00 19.28 ? 233 HIS   C CB  1 
ATOM   4163 C  CG  . HIS   C 1 140 ? 32.990  -43.386 -92.728  1.00 19.98 ? 233 HIS   C CG  1 
ATOM   4164 N  ND1 . HIS   C 1 140 ? 32.963  -44.762 -92.846  1.00 20.94 ? 233 HIS   C ND1 1 
ATOM   4165 C  CD2 . HIS   C 1 140 ? 34.211  -43.069 -92.245  1.00 20.37 ? 233 HIS   C CD2 1 
ATOM   4166 C  CE1 . HIS   C 1 140 ? 34.118  -45.255 -92.442  1.00 21.56 ? 233 HIS   C CE1 1 
ATOM   4167 N  NE2 . HIS   C 1 140 ? 34.897  -44.238 -92.068  1.00 20.84 ? 233 HIS   C NE2 1 
ATOM   4168 N  N   . TYR   C 1 141 ? 31.443  -39.037 -93.940  1.00 17.37 ? 234 TYR   C N   1 
ATOM   4169 C  CA  . TYR   C 1 141 ? 30.636  -38.099 -94.754  1.00 17.13 ? 234 TYR   C CA  1 
ATOM   4170 C  C   . TYR   C 1 141 ? 30.735  -38.499 -96.226  1.00 17.37 ? 234 TYR   C C   1 
ATOM   4171 O  O   . TYR   C 1 141 ? 31.753  -39.107 -96.632  1.00 17.22 ? 234 TYR   C O   1 
ATOM   4172 C  CB  . TYR   C 1 141 ? 31.089  -36.653 -94.550  1.00 16.92 ? 234 TYR   C CB  1 
ATOM   4173 C  CG  . TYR   C 1 141 ? 30.767  -36.101 -93.187  1.00 16.83 ? 234 TYR   C CG  1 
ATOM   4174 C  CD1 . TYR   C 1 141 ? 29.469  -35.773 -92.835  1.00 16.33 ? 234 TYR   C CD1 1 
ATOM   4175 C  CD2 . TYR   C 1 141 ? 31.760  -35.922 -92.240  1.00 16.76 ? 234 TYR   C CD2 1 
ATOM   4176 C  CE1 . TYR   C 1 141 ? 29.166  -35.274 -91.577  1.00 16.67 ? 234 TYR   C CE1 1 
ATOM   4177 C  CE2 . TYR   C 1 141 ? 31.476  -35.417 -90.981  1.00 16.57 ? 234 TYR   C CE2 1 
ATOM   4178 C  CZ  . TYR   C 1 141 ? 30.177  -35.088 -90.649  1.00 16.56 ? 234 TYR   C CZ  1 
ATOM   4179 O  OH  . TYR   C 1 141 ? 29.910  -34.608 -89.402  1.00 16.57 ? 234 TYR   C OH  1 
ATOM   4180 N  N   . ASN   C 1 142 ? 29.677  -38.183 -96.974  1.00 16.74 ? 235 ASN   C N   1 
ATOM   4181 C  CA  . ASN   C 1 142 ? 29.604  -38.261 -98.454  1.00 16.83 ? 235 ASN   C CA  1 
ATOM   4182 C  C   . ASN   C 1 142 ? 29.179  -36.882 -98.967  1.00 16.66 ? 235 ASN   C C   1 
ATOM   4183 O  O   . ASN   C 1 142 ? 28.211  -36.321 -98.430  1.00 15.81 ? 235 ASN   C O   1 
ATOM   4184 C  CB  . ASN   C 1 142 ? 28.606  -39.311 -98.955  1.00 17.33 ? 235 ASN   C CB  1 
ATOM   4185 C  CG  . ASN   C 1 142 ? 28.890  -40.735 -98.523  1.00 18.04 ? 235 ASN   C CG  1 
ATOM   4186 O  OD1 . ASN   C 1 142 ? 27.989  -41.568 -98.544  1.00 19.19 ? 235 ASN   C OD1 1 
ATOM   4187 N  ND2 . ASN   C 1 142 ? 30.121  -41.047 -98.156  1.00 18.27 ? 235 ASN   C ND2 1 
ATOM   4188 N  N   . TYR   C 1 143 ? 29.894  -36.361 -99.959  1.00 16.74 ? 236 TYR   C N   1 
ATOM   4189 C  CA  . TYR   C 1 143 ? 29.544  -35.125 -100.699 1.00 16.72 ? 236 TYR   C CA  1 
ATOM   4190 C  C   . TYR   C 1 143 ? 28.914  -35.549 -102.029 1.00 17.70 ? 236 TYR   C C   1 
ATOM   4191 O  O   . TYR   C 1 143 ? 29.560  -36.288 -102.789 1.00 17.41 ? 236 TYR   C O   1 
ATOM   4192 C  CB  . TYR   C 1 143 ? 30.787  -34.249 -100.844 1.00 16.69 ? 236 TYR   C CB  1 
ATOM   4193 C  CG  . TYR   C 1 143 ? 31.269  -33.672 -99.538  1.00 16.17 ? 236 TYR   C CG  1 
ATOM   4194 C  CD1 . TYR   C 1 143 ? 32.096  -34.391 -98.693  1.00 16.29 ? 236 TYR   C CD1 1 
ATOM   4195 C  CD2 . TYR   C 1 143 ? 30.877  -32.406 -99.139  1.00 16.13 ? 236 TYR   C CD2 1 
ATOM   4196 C  CE1 . TYR   C 1 143 ? 32.529  -33.866 -97.487  1.00 16.09 ? 236 TYR   C CE1 1 
ATOM   4197 C  CE2 . TYR   C 1 143 ? 31.300  -31.865 -97.937  1.00 16.00 ? 236 TYR   C CE2 1 
ATOM   4198 C  CZ  . TYR   C 1 143 ? 32.125  -32.598 -97.105  1.00 16.13 ? 236 TYR   C CZ  1 
ATOM   4199 O  OH  . TYR   C 1 143 ? 32.534  -32.057 -95.920  1.00 15.84 ? 236 TYR   C OH  1 
ATOM   4200 N  N   . MET   C 1 144 ? 27.677  -35.116 -102.281 1.00 18.55 ? 237 MET   C N   1 
ATOM   4201 C  CA  . MET   C 1 144 ? 26.780  -35.730 -103.299 1.00 19.26 ? 237 MET   C CA  1 
ATOM   4202 C  C   . MET   C 1 144 ? 26.685  -34.855 -104.556 1.00 19.69 ? 237 MET   C C   1 
ATOM   4203 O  O   . MET   C 1 144 ? 25.872  -35.183 -105.442 1.00 20.29 ? 237 MET   C O   1 
ATOM   4204 C  CB  . MET   C 1 144 ? 25.391  -35.948 -102.695 1.00 19.82 ? 237 MET   C CB  1 
ATOM   4205 C  CG  . MET   C 1 144 ? 25.400  -36.900 -101.510 1.00 20.48 ? 237 MET   C CG  1 
ATOM   4206 S  SD  . MET   C 1 144 ? 26.238  -38.478 -101.823 1.00 21.14 ? 237 MET   C SD  1 
ATOM   4207 C  CE  . MET   C 1 144 ? 25.324  -39.085 -103.243 1.00 21.67 ? 237 MET   C CE  1 
ATOM   4208 N  N   . CYS   C 1 145 ? 27.507  -33.807 -104.638 1.00 20.34 ? 238 CYS   C N   1 
ATOM   4209 C  CA  . CYS   C 1 145 ? 27.771  -33.001 -105.863 1.00 21.78 ? 238 CYS   C CA  1 
ATOM   4210 C  C   . CYS   C 1 145 ? 29.277  -32.773 -105.996 1.00 22.53 ? 238 CYS   C C   1 
ATOM   4211 O  O   . CYS   C 1 145 ? 29.967  -32.772 -104.957 1.00 21.24 ? 238 CYS   C O   1 
ATOM   4212 C  CB  . CYS   C 1 145 ? 27.092  -31.638 -105.813 1.00 22.24 ? 238 CYS   C CB  1 
ATOM   4213 S  SG  . CYS   C 1 145 ? 25.525  -31.641 -106.595 1.00 23.39 ? 238 CYS   C SG  1 
ATOM   4214 N  N   . ASN   C 1 146 ? 29.749  -32.590 -107.232 1.00 23.77 ? 239 ASN   C N   1 
ATOM   4215 C  CA  . ASN   C 1 146 ? 31.145  -32.201 -107.557 1.00 23.84 ? 239 ASN   C CA  1 
ATOM   4216 C  C   . ASN   C 1 146 ? 31.234  -30.675 -107.459 1.00 22.80 ? 239 ASN   C C   1 
ATOM   4217 O  O   . ASN   C 1 146 ? 30.209  -29.996 -107.694 1.00 21.82 ? 239 ASN   C O   1 
ATOM   4218 C  CB  . ASN   C 1 146 ? 31.581  -32.727 -108.930 1.00 25.16 ? 239 ASN   C CB  1 
ATOM   4219 C  CG  . ASN   C 1 146 ? 32.083  -34.157 -108.892 1.00 27.09 ? 239 ASN   C CG  1 
ATOM   4220 O  OD1 . ASN   C 1 146 ? 32.946  -34.497 -108.081 1.00 29.24 ? 239 ASN   C OD1 1 
ATOM   4221 N  ND2 . ASN   C 1 146 ? 31.577  -34.997 -109.782 1.00 27.11 ? 239 ASN   C ND2 1 
ATOM   4222 N  N   . SER   C 1 147 ? 32.411  -30.154 -107.110 1.00 22.04 ? 240 SER   C N   1 
ATOM   4223 C  CA  . SER   C 1 147 ? 32.686  -28.696 -107.040 1.00 22.30 ? 240 SER   C CA  1 
ATOM   4224 C  C   . SER   C 1 147 ? 32.410  -28.051 -108.404 1.00 23.27 ? 240 SER   C C   1 
ATOM   4225 O  O   . SER   C 1 147 ? 32.024  -26.870 -108.419 1.00 25.27 ? 240 SER   C O   1 
ATOM   4226 C  CB  . SER   C 1 147 ? 34.094  -28.426 -106.562 1.00 21.91 ? 240 SER   C CB  1 
ATOM   4227 O  OG  . SER   C 1 147 ? 34.220  -28.740 -105.183 1.00 20.52 ? 240 SER   C OG  1 
ATOM   4228 N  N   . SER   C 1 148 ? 32.572  -28.808 -109.495 1.00 23.83 ? 241 SER   C N   1 
ATOM   4229 C  CA  . SER   C 1 148 ? 32.453  -28.335 -110.901 1.00 24.48 ? 241 SER   C CA  1 
ATOM   4230 C  C   . SER   C 1 148 ? 31.024  -28.492 -111.448 1.00 25.15 ? 241 SER   C C   1 
ATOM   4231 O  O   . SER   C 1 148 ? 30.815  -28.126 -112.615 1.00 26.85 ? 241 SER   C O   1 
ATOM   4232 C  CB  . SER   C 1 148 ? 33.424  -29.070 -111.775 1.00 23.96 ? 241 SER   C CB  1 
ATOM   4233 O  OG  . SER   C 1 148 ? 33.100  -30.455 -111.804 1.00 24.58 ? 241 SER   C OG  1 
ATOM   4234 N  N   . CYS   C 1 149 ? 30.079  -29.027 -110.669 1.00 25.27 ? 242 CYS   C N   1 
ATOM   4235 C  CA  . CYS   C 1 149 ? 28.667  -29.239 -111.100 1.00 25.43 ? 242 CYS   C CA  1 
ATOM   4236 C  C   . CYS   C 1 149 ? 28.055  -27.921 -111.595 1.00 26.63 ? 242 CYS   C C   1 
ATOM   4237 O  O   . CYS   C 1 149 ? 27.989  -26.963 -110.798 1.00 27.23 ? 242 CYS   C O   1 
ATOM   4238 C  CB  . CYS   C 1 149 ? 27.802  -29.785 -109.971 1.00 23.45 ? 242 CYS   C CB  1 
ATOM   4239 S  SG  . CYS   C 1 149 ? 27.809  -31.544 -109.866 1.00 22.43 ? 242 CYS   C SG  1 
ATOM   4240 N  N   . MET   C 1 150 ? 27.605  -27.884 -112.856 1.00 28.39 ? 243 MET   C N   1 
ATOM   4241 C  CA  . MET   C 1 150 ? 26.861  -26.734 -113.438 1.00 28.49 ? 243 MET   C CA  1 
ATOM   4242 C  C   . MET   C 1 150 ? 25.504  -26.629 -112.730 1.00 27.48 ? 243 MET   C C   1 
ATOM   4243 O  O   . MET   C 1 150 ? 24.854  -27.671 -112.564 1.00 26.78 ? 243 MET   C O   1 
ATOM   4244 C  CB  . MET   C 1 150 ? 26.621  -26.916 -114.941 1.00 30.06 ? 243 MET   C CB  1 
ATOM   4245 C  CG  . MET   C 1 150 ? 27.867  -27.247 -115.755 1.00 30.40 ? 243 MET   C CG  1 
ATOM   4246 S  SD  . MET   C 1 150 ? 27.490  -27.357 -117.532 1.00 31.73 ? 243 MET   C SD  1 
ATOM   4247 C  CE  . MET   C 1 150 ? 27.269  -25.615 -117.897 1.00 33.11 ? 243 MET   C CE  1 
ATOM   4248 N  N   . GLY   C 1 151 ? 25.103  -25.421 -112.324 1.00 28.42 ? 244 GLY   C N   1 
ATOM   4249 C  CA  . GLY   C 1 151 ? 23.808  -25.158 -111.664 1.00 28.57 ? 244 GLY   C CA  1 
ATOM   4250 C  C   . GLY   C 1 151 ? 23.794  -25.602 -110.209 1.00 29.58 ? 244 GLY   C C   1 
ATOM   4251 O  O   . GLY   C 1 151 ? 22.697  -25.628 -109.616 1.00 29.88 ? 244 GLY   C O   1 
ATOM   4252 N  N   . GLY   C 1 152 ? 24.962  -25.946 -109.652 1.00 29.36 ? 245 GLY   C N   1 
ATOM   4253 C  CA  . GLY   C 1 152 ? 25.157  -26.229 -108.217 1.00 29.14 ? 245 GLY   C CA  1 
ATOM   4254 C  C   . GLY   C 1 152 ? 26.202  -25.297 -107.634 1.00 29.21 ? 245 GLY   C C   1 
ATOM   4255 O  O   . GLY   C 1 152 ? 26.022  -24.065 -107.736 1.00 28.72 ? 245 GLY   C O   1 
ATOM   4256 N  N   . MET   C 1 153 ? 27.277  -25.854 -107.071 1.00 28.24 ? 246 MET   C N   1 
ATOM   4257 C  CA  . MET   C 1 153 ? 28.425  -25.071 -106.542 1.00 27.51 ? 246 MET   C CA  1 
ATOM   4258 C  C   . MET   C 1 153 ? 29.118  -24.338 -107.698 1.00 28.62 ? 246 MET   C C   1 
ATOM   4259 O  O   . MET   C 1 153 ? 29.523  -23.177 -107.495 1.00 28.86 ? 246 MET   C O   1 
ATOM   4260 C  CB  . MET   C 1 153 ? 29.402  -25.990 -105.804 1.00 26.31 ? 246 MET   C CB  1 
ATOM   4261 C  CG  . MET   C 1 153 ? 28.801  -26.544 -104.522 1.00 25.24 ? 246 MET   C CG  1 
ATOM   4262 S  SD  . MET   C 1 153 ? 29.959  -27.559 -103.589 1.00 23.94 ? 246 MET   C SD  1 
ATOM   4263 C  CE  . MET   C 1 153 ? 29.798  -29.122 -104.451 1.00 23.98 ? 246 MET   C CE  1 
ATOM   4264 N  N   . ASN   C 1 154 ? 29.227  -24.983 -108.863 1.00 30.09 ? 247 ASN   C N   1 
ATOM   4265 C  CA  . ASN   C 1 154 ? 29.659  -24.352 -110.140 1.00 31.71 ? 247 ASN   C CA  1 
ATOM   4266 C  C   . ASN   C 1 154 ? 31.066  -23.765 -109.974 1.00 32.09 ? 247 ASN   C C   1 
ATOM   4267 O  O   . ASN   C 1 154 ? 31.264  -22.595 -110.344 1.00 31.24 ? 247 ASN   C O   1 
ATOM   4268 C  CB  . ASN   C 1 154 ? 28.652  -23.291 -110.596 1.00 32.81 ? 247 ASN   C CB  1 
ATOM   4269 C  CG  . ASN   C 1 154 ? 28.876  -22.823 -112.020 1.00 33.54 ? 247 ASN   C CG  1 
ATOM   4270 O  OD1 . ASN   C 1 154 ? 29.478  -23.529 -112.828 1.00 34.41 ? 247 ASN   C OD1 1 
ATOM   4271 N  ND2 . ASN   C 1 154 ? 28.398  -21.630 -112.334 1.00 33.60 ? 247 ASN   C ND2 1 
ATOM   4272 N  N   . ARG   C 1 155 ? 31.985  -24.555 -109.406 1.00 32.53 ? 248 ARG   C N   1 
ATOM   4273 C  CA  . ARG   C 1 155 ? 33.436  -24.256 -109.237 1.00 32.73 ? 248 ARG   C CA  1 
ATOM   4274 C  C   . ARG   C 1 155 ? 33.674  -23.337 -108.031 1.00 30.55 ? 248 ARG   C C   1 
ATOM   4275 O  O   . ARG   C 1 155 ? 34.850  -23.056 -107.749 1.00 30.42 ? 248 ARG   C O   1 
ATOM   4276 C  CB  . ARG   C 1 155 ? 34.031  -23.666 -110.522 1.00 34.47 ? 248 ARG   C CB  1 
ATOM   4277 C  CG  . ARG   C 1 155 ? 33.857  -24.560 -111.742 1.00 37.15 ? 248 ARG   C CG  1 
ATOM   4278 C  CD  . ARG   C 1 155 ? 34.773  -24.196 -112.898 1.00 39.51 ? 248 ARG   C CD  1 
ATOM   4279 N  NE  . ARG   C 1 155 ? 34.874  -25.285 -113.864 1.00 41.91 ? 248 ARG   C NE  1 
ATOM   4280 C  CZ  . ARG   C 1 155 ? 35.590  -26.397 -113.693 1.00 43.07 ? 248 ARG   C CZ  1 
ATOM   4281 N  NH1 . ARG   C 1 155 ? 36.287  -26.588 -112.583 1.00 43.38 ? 248 ARG   C NH1 1 
ATOM   4282 N  NH2 . ARG   C 1 155 ? 35.605  -27.323 -114.638 1.00 44.19 ? 248 ARG   C NH2 1 
ATOM   4283 N  N   . ARG   C 1 156 ? 32.624  -22.911 -107.320 1.00 29.25 ? 249 ARG   C N   1 
ATOM   4284 C  CA  . ARG   C 1 156 ? 32.758  -22.025 -106.134 1.00 27.93 ? 249 ARG   C CA  1 
ATOM   4285 C  C   . ARG   C 1 156 ? 33.217  -22.867 -104.947 1.00 26.53 ? 249 ARG   C C   1 
ATOM   4286 O  O   . ARG   C 1 156 ? 32.592  -23.879 -104.632 1.00 26.14 ? 249 ARG   C O   1 
ATOM   4287 C  CB  . ARG   C 1 156 ? 31.445  -21.303 -105.818 1.00 28.33 ? 249 ARG   C CB  1 
ATOM   4288 C  CG  . ARG   C 1 156 ? 30.975  -20.359 -106.917 1.00 28.62 ? 249 ARG   C CG  1 
ATOM   4289 C  CD  . ARG   C 1 156 ? 29.603  -19.787 -106.623 1.00 28.68 ? 249 ARG   C CD  1 
ATOM   4290 N  NE  . ARG   C 1 156 ? 28.550  -20.785 -106.743 1.00 28.18 ? 249 ARG   C NE  1 
ATOM   4291 C  CZ  . ARG   C 1 156 ? 27.255  -20.552 -106.550 1.00 28.19 ? 249 ARG   C CZ  1 
ATOM   4292 N  NH1 . ARG   C 1 156 ? 26.840  -19.341 -106.218 1.00 28.52 ? 249 ARG   C NH1 1 
ATOM   4293 N  NH2 . ARG   C 1 156 ? 26.376  -21.532 -106.688 1.00 27.77 ? 249 ARG   C NH2 1 
ATOM   4294 N  N   . PRO   C 1 157 ? 34.330  -22.499 -104.270 1.00 24.59 ? 250 PRO   C N   1 
ATOM   4295 C  CA  . PRO   C 1 157 ? 34.770  -23.211 -103.069 1.00 24.04 ? 250 PRO   C CA  1 
ATOM   4296 C  C   . PRO   C 1 157 ? 33.750  -23.126 -101.923 1.00 22.00 ? 250 PRO   C C   1 
ATOM   4297 O  O   . PRO   C 1 157 ? 33.077  -22.121 -101.805 1.00 20.44 ? 250 PRO   C O   1 
ATOM   4298 C  CB  . PRO   C 1 157 ? 36.078  -22.509 -102.668 1.00 24.11 ? 250 PRO   C CB  1 
ATOM   4299 C  CG  . PRO   C 1 157 ? 36.001  -21.156 -103.335 1.00 24.96 ? 250 PRO   C CG  1 
ATOM   4300 C  CD  . PRO   C 1 157 ? 35.228  -21.387 -104.616 1.00 25.04 ? 250 PRO   C CD  1 
ATOM   4301 N  N   . ILE   C 1 158 ? 33.670  -24.186 -101.115 1.00 21.08 ? 251 ILE   C N   1 
ATOM   4302 C  CA  . ILE   C 1 158 ? 32.781  -24.280 -99.919  1.00 20.37 ? 251 ILE   C CA  1 
ATOM   4303 C  C   . ILE   C 1 158 ? 33.638  -24.587 -98.689  1.00 19.91 ? 251 ILE   C C   1 
ATOM   4304 O  O   . ILE   C 1 158 ? 34.726  -25.159 -98.848  1.00 18.36 ? 251 ILE   C O   1 
ATOM   4305 C  CB  . ILE   C 1 158 ? 31.681  -25.345 -100.110 1.00 19.95 ? 251 ILE   C CB  1 
ATOM   4306 C  CG1 . ILE   C 1 158 ? 32.265  -26.732 -100.398 1.00 20.06 ? 251 ILE   C CG1 1 
ATOM   4307 C  CG2 . ILE   C 1 158 ? 30.700  -24.909 -101.189 1.00 20.48 ? 251 ILE   C CG2 1 
ATOM   4308 C  CD1 . ILE   C 1 158 ? 31.277  -27.861 -100.235 1.00 19.92 ? 251 ILE   C CD1 1 
ATOM   4309 N  N   . LEU   C 1 159 ? 33.145  -24.208 -97.511  1.00 19.94 ? 252 LEU   C N   1 
ATOM   4310 C  CA  . LEU   C 1 159 ? 33.625  -24.723 -96.207  1.00 20.08 ? 252 LEU   C CA  1 
ATOM   4311 C  C   . LEU   C 1 159 ? 32.588  -25.720 -95.698  1.00 19.14 ? 252 LEU   C C   1 
ATOM   4312 O  O   . LEU   C 1 159 ? 31.384  -25.494 -95.946  1.00 19.13 ? 252 LEU   C O   1 
ATOM   4313 C  CB  . LEU   C 1 159 ? 33.790  -23.563 -95.222  1.00 21.11 ? 252 LEU   C CB  1 
ATOM   4314 C  CG  . LEU   C 1 159 ? 34.672  -22.418 -95.707  1.00 22.57 ? 252 LEU   C CG  1 
ATOM   4315 C  CD1 . LEU   C 1 159 ? 34.848  -21.376 -94.612  1.00 23.31 ? 252 LEU   C CD1 1 
ATOM   4316 C  CD2 . LEU   C 1 159 ? 36.024  -22.936 -96.180  1.00 22.64 ? 252 LEU   C CD2 1 
ATOM   4317 N  N   . THR   C 1 160 ? 33.043  -26.788 -95.048  1.00 17.26 ? 253 THR   C N   1 
ATOM   4318 C  CA  . THR   C 1 160 ? 32.216  -27.604 -94.127  1.00 16.87 ? 253 THR   C CA  1 
ATOM   4319 C  C   . THR   C 1 160 ? 32.444  -27.076 -92.711  1.00 16.05 ? 253 THR   C C   1 
ATOM   4320 O  O   . THR   C 1 160 ? 33.613  -26.950 -92.319  1.00 15.57 ? 253 THR   C O   1 
ATOM   4321 C  CB  . THR   C 1 160 ? 32.543  -29.095 -94.254  1.00 16.87 ? 253 THR   C CB  1 
ATOM   4322 O  OG1 . THR   C 1 160 ? 32.321  -29.466 -95.615  1.00 17.09 ? 253 THR   C OG1 1 
ATOM   4323 C  CG2 . THR   C 1 160 ? 31.709  -29.955 -93.330  1.00 16.76 ? 253 THR   C CG2 1 
ATOM   4324 N  N   . ILE   C 1 161 ? 31.367  -26.775 -91.985  1.00 15.80 ? 254 ILE   C N   1 
ATOM   4325 C  CA  . ILE   C 1 161 ? 31.399  -26.351 -90.555  1.00 15.93 ? 254 ILE   C CA  1 
ATOM   4326 C  C   . ILE   C 1 161 ? 30.909  -27.528 -89.707  1.00 15.53 ? 254 ILE   C C   1 
ATOM   4327 O  O   . ILE   C 1 161 ? 29.773  -27.974 -89.932  1.00 15.24 ? 254 ILE   C O   1 
ATOM   4328 C  CB  . ILE   C 1 161 ? 30.557  -25.075 -90.339  1.00 16.39 ? 254 ILE   C CB  1 
ATOM   4329 C  CG1 . ILE   C 1 161 ? 30.993  -23.953 -91.284  1.00 16.85 ? 254 ILE   C CG1 1 
ATOM   4330 C  CG2 . ILE   C 1 161 ? 30.608  -24.632 -88.882  1.00 16.73 ? 254 ILE   C CG2 1 
ATOM   4331 C  CD1 . ILE   C 1 161 ? 30.091  -22.742 -91.276  1.00 17.52 ? 254 ILE   C CD1 1 
ATOM   4332 N  N   . ILE   C 1 162 ? 31.758  -28.029 -88.804  1.00 15.68 ? 255 ILE   C N   1 
ATOM   4333 C  CA  . ILE   C 1 162 ? 31.420  -29.124 -87.846  1.00 16.03 ? 255 ILE   C CA  1 
ATOM   4334 C  C   . ILE   C 1 162 ? 31.183  -28.476 -86.484  1.00 16.50 ? 255 ILE   C C   1 
ATOM   4335 O  O   . ILE   C 1 162 ? 32.127  -27.878 -85.953  1.00 16.72 ? 255 ILE   C O   1 
ATOM   4336 C  CB  . ILE   C 1 162 ? 32.516  -30.211 -87.772  1.00 15.69 ? 255 ILE   C CB  1 
ATOM   4337 C  CG1 . ILE   C 1 162 ? 32.969  -30.687 -89.156  1.00 15.76 ? 255 ILE   C CG1 1 
ATOM   4338 C  CG2 . ILE   C 1 162 ? 32.055  -31.376 -86.903  1.00 15.47 ? 255 ILE   C CG2 1 
ATOM   4339 C  CD1 . ILE   C 1 162 ? 31.907  -31.396 -89.954  1.00 15.97 ? 255 ILE   C CD1 1 
ATOM   4340 N  N   . THR   C 1 163 ? 29.963  -28.578 -85.956  1.00 17.30 ? 256 THR   C N   1 
ATOM   4341 C  CA  . THR   C 1 163 ? 29.601  -28.082 -84.605  1.00 17.95 ? 256 THR   C CA  1 
ATOM   4342 C  C   . THR   C 1 163 ? 29.288  -29.278 -83.704  1.00 18.31 ? 256 THR   C C   1 
ATOM   4343 O  O   . THR   C 1 163 ? 28.651  -30.245 -84.169  1.00 18.09 ? 256 THR   C O   1 
ATOM   4344 C  CB  . THR   C 1 163 ? 28.456  -27.063 -84.658  1.00 18.31 ? 256 THR   C CB  1 
ATOM   4345 O  OG1 . THR   C 1 163 ? 27.345  -27.659 -85.324  1.00 19.40 ? 256 THR   C OG1 1 
ATOM   4346 C  CG2 . THR   C 1 163 ? 28.841  -25.783 -85.366  1.00 18.51 ? 256 THR   C CG2 1 
ATOM   4347 N  N   . LEU   C 1 164 ? 29.773  -29.211 -82.470  1.00 19.00 ? 257 LEU   C N   1 
ATOM   4348 C  CA  . LEU   C 1 164 ? 29.342  -30.057 -81.335  1.00 19.94 ? 257 LEU   C CA  1 
ATOM   4349 C  C   . LEU   C 1 164 ? 28.238  -29.286 -80.602  1.00 19.54 ? 257 LEU   C C   1 
ATOM   4350 O  O   . LEU   C 1 164 ? 28.459  -28.100 -80.315  1.00 19.07 ? 257 LEU   C O   1 
ATOM   4351 C  CB  . LEU   C 1 164 ? 30.566  -30.286 -80.444  1.00 21.20 ? 257 LEU   C CB  1 
ATOM   4352 C  CG  . LEU   C 1 164 ? 30.601  -31.573 -79.628  1.00 22.88 ? 257 LEU   C CG  1 
ATOM   4353 C  CD1 . LEU   C 1 164 ? 30.493  -32.801 -80.522  1.00 23.69 ? 257 LEU   C CD1 1 
ATOM   4354 C  CD2 . LEU   C 1 164 ? 31.883  -31.621 -78.808  1.00 23.06 ? 257 LEU   C CD2 1 
ATOM   4355 N  N   . GLU   C 1 165 ? 27.078  -29.903 -80.370  1.00 19.12 ? 258 GLU   C N   1 
ATOM   4356 C  CA  . GLU   C 1 165 ? 25.968  -29.263 -79.615  1.00 19.97 ? 258 GLU   C CA  1 
ATOM   4357 C  C   . GLU   C 1 165 ? 25.413  -30.258 -78.593  1.00 19.42 ? 258 GLU   C C   1 
ATOM   4358 O  O   . GLU   C 1 165 ? 25.504  -31.475 -78.826  1.00 20.29 ? 258 GLU   C O   1 
ATOM   4359 C  CB  . GLU   C 1 165 ? 24.881  -28.707 -80.544  1.00 20.41 ? 258 GLU   C CB  1 
ATOM   4360 C  CG  . GLU   C 1 165 ? 24.670  -29.483 -81.828  1.00 20.96 ? 258 GLU   C CG  1 
ATOM   4361 C  CD  . GLU   C 1 165 ? 23.488  -29.009 -82.661  1.00 20.78 ? 258 GLU   C CD  1 
ATOM   4362 O  OE1 . GLU   C 1 165 ? 23.697  -28.168 -83.547  1.00 21.84 ? 258 GLU   C OE1 1 
ATOM   4363 O  OE2 . GLU   C 1 165 ? 22.360  -29.486 -82.424  1.00 20.49 ? 258 GLU   C OE2 1 
ATOM   4364 N  N   . ASP   C 1 166 ? 24.890  -29.743 -77.483  1.00 19.87 ? 259 ASP   C N   1 
ATOM   4365 C  CA  . ASP   C 1 166 ? 24.263  -30.567 -76.421  1.00 20.22 ? 259 ASP   C CA  1 
ATOM   4366 C  C   . ASP   C 1 166 ? 22.861  -30.942 -76.909  1.00 19.86 ? 259 ASP   C C   1 
ATOM   4367 O  O   . ASP   C 1 166 ? 22.484  -30.509 -78.026  1.00 19.48 ? 259 ASP   C O   1 
ATOM   4368 C  CB  . ASP   C 1 166 ? 24.287  -29.846 -75.070  1.00 20.79 ? 259 ASP   C CB  1 
ATOM   4369 C  CG  . ASP   C 1 166 ? 23.395  -28.618 -74.970  1.00 21.10 ? 259 ASP   C CG  1 
ATOM   4370 O  OD1 . ASP   C 1 166 ? 22.554  -28.413 -75.867  1.00 21.01 ? 259 ASP   C OD1 1 
ATOM   4371 O  OD2 . ASP   C 1 166 ? 23.538  -27.885 -73.975  1.00 21.66 ? 259 ASP   C OD2 1 
ATOM   4372 N  N   . SER   C 1 167 ? 22.120  -31.716 -76.114  1.00 19.89 ? 260 SER   C N   1 
ATOM   4373 C  CA  . SER   C 1 167 ? 20.777  -32.243 -76.470  1.00 19.79 ? 260 SER   C CA  1 
ATOM   4374 C  C   . SER   C 1 167 ? 19.797  -31.092 -76.755  1.00 20.77 ? 260 SER   C C   1 
ATOM   4375 O  O   . SER   C 1 167 ? 18.803  -31.349 -77.448  1.00 20.87 ? 260 SER   C O   1 
ATOM   4376 C  CB  . SER   C 1 167 ? 20.264  -33.179 -75.398  1.00 19.93 ? 260 SER   C CB  1 
ATOM   4377 O  OG  . SER   C 1 167 ? 20.263  -32.546 -74.126  1.00 20.01 ? 260 SER   C OG  1 
ATOM   4378 N  N   . SER   C 1 168 ? 20.070  -29.873 -76.262  1.00 21.59 ? 261 SER   C N   1 
ATOM   4379 C  CA  . SER   C 1 168 ? 19.189  -28.678 -76.390  1.00 22.03 ? 261 SER   C CA  1 
ATOM   4380 C  C   . SER   C 1 168 ? 19.596  -27.799 -77.581  1.00 21.94 ? 261 SER   C C   1 
ATOM   4381 O  O   . SER   C 1 168 ? 18.869  -26.835 -77.857  1.00 22.25 ? 261 SER   C O   1 
ATOM   4382 C  CB  . SER   C 1 168 ? 19.185  -27.870 -75.115  1.00 22.51 ? 261 SER   C CB  1 
ATOM   4383 O  OG  . SER   C 1 168 ? 18.571  -28.594 -74.059  1.00 23.12 ? 261 SER   C OG  1 
ATOM   4384 N  N   . GLY   C 1 169 ? 20.715  -28.104 -78.245  1.00 22.20 ? 262 GLY   C N   1 
ATOM   4385 C  CA  . GLY   C 1 169 ? 21.221  -27.354 -79.412  1.00 21.88 ? 262 GLY   C CA  1 
ATOM   4386 C  C   . GLY   C 1 169 ? 22.235  -26.284 -79.033  1.00 22.19 ? 262 GLY   C C   1 
ATOM   4387 O  O   . GLY   C 1 169 ? 22.661  -25.548 -79.935  1.00 21.88 ? 262 GLY   C O   1 
ATOM   4388 N  N   . ASN   C 1 170 ? 22.635  -26.208 -77.757  1.00 22.26 ? 263 ASN   C N   1 
ATOM   4389 C  CA  . ASN   C 1 170 ? 23.636  -25.224 -77.263  1.00 22.08 ? 263 ASN   C CA  1 
ATOM   4390 C  C   . ASN   C 1 170 ? 25.014  -25.590 -77.831  1.00 21.86 ? 263 ASN   C C   1 
ATOM   4391 O  O   . ASN   C 1 170 ? 25.395  -26.779 -77.759  1.00 21.12 ? 263 ASN   C O   1 
ATOM   4392 C  CB  . ASN   C 1 170 ? 23.677  -25.163 -75.734  1.00 22.30 ? 263 ASN   C CB  1 
ATOM   4393 C  CG  . ASN   C 1 170 ? 22.343  -24.788 -75.122  1.00 22.96 ? 263 ASN   C CG  1 
ATOM   4394 O  OD1 . ASN   C 1 170 ? 21.746  -23.787 -75.507  1.00 23.90 ? 263 ASN   C OD1 1 
ATOM   4395 N  ND2 . ASN   C 1 170 ? 21.865  -25.578 -74.174  1.00 23.28 ? 263 ASN   C ND2 1 
ATOM   4396 N  N   . LEU   C 1 171 ? 25.737  -24.598 -78.352  1.00 21.59 ? 264 LEU   C N   1 
ATOM   4397 C  CA  . LEU   C 1 171 ? 27.089  -24.762 -78.951  1.00 21.41 ? 264 LEU   C CA  1 
ATOM   4398 C  C   . LEU   C 1 171 ? 28.072  -25.252 -77.881  1.00 20.31 ? 264 LEU   C C   1 
ATOM   4399 O  O   . LEU   C 1 171 ? 28.152  -24.603 -76.822  1.00 20.97 ? 264 LEU   C O   1 
ATOM   4400 C  CB  . LEU   C 1 171 ? 27.531  -23.412 -79.521  1.00 22.30 ? 264 LEU   C CB  1 
ATOM   4401 C  CG  . LEU   C 1 171 ? 28.894  -23.387 -80.208  1.00 23.25 ? 264 LEU   C CG  1 
ATOM   4402 C  CD1 . LEU   C 1 171 ? 28.862  -24.173 -81.513  1.00 23.76 ? 264 LEU   C CD1 1 
ATOM   4403 C  CD2 . LEU   C 1 171 ? 29.324  -21.953 -80.460  1.00 23.99 ? 264 LEU   C CD2 1 
ATOM   4404 N  N   . LEU   C 1 172 ? 28.784  -26.351 -78.151  1.00 18.53 ? 265 LEU   C N   1 
ATOM   4405 C  CA  . LEU   C 1 172 ? 29.883  -26.877 -77.294  1.00 18.07 ? 265 LEU   C CA  1 
ATOM   4406 C  C   . LEU   C 1 172 ? 31.236  -26.682 -77.991  1.00 18.27 ? 265 LEU   C C   1 
ATOM   4407 O  O   . LEU   C 1 172 ? 32.261  -26.588 -77.282  1.00 18.54 ? 265 LEU   C O   1 
ATOM   4408 C  CB  . LEU   C 1 172 ? 29.640  -28.362 -77.007  1.00 17.84 ? 265 LEU   C CB  1 
ATOM   4409 C  CG  . LEU   C 1 172 ? 28.340  -28.707 -76.280  1.00 17.88 ? 265 LEU   C CG  1 
ATOM   4410 C  CD1 . LEU   C 1 172 ? 28.220  -30.210 -76.069  1.00 17.38 ? 265 LEU   C CD1 1 
ATOM   4411 C  CD2 . LEU   C 1 172 ? 28.237  -27.976 -74.948  1.00 17.96 ? 265 LEU   C CD2 1 
ATOM   4412 N  N   . GLY   C 1 173 ? 31.251  -26.649 -79.326  1.00 17.93 ? 266 GLY   C N   1 
ATOM   4413 C  CA  . GLY   C 1 173 ? 32.494  -26.595 -80.116  1.00 17.98 ? 266 GLY   C CA  1 
ATOM   4414 C  C   . GLY   C 1 173 ? 32.225  -26.383 -81.590  1.00 17.96 ? 266 GLY   C C   1 
ATOM   4415 O  O   . GLY   C 1 173 ? 31.136  -26.758 -82.063  1.00 18.09 ? 266 GLY   C O   1 
ATOM   4416 N  N   . ARG   C 1 174 ? 33.181  -25.783 -82.297  1.00 18.00 ? 267 ARG   C N   1 
ATOM   4417 C  CA  . ARG   C 1 174 ? 33.077  -25.549 -83.757  1.00 18.67 ? 267 ARG   C CA  1 
ATOM   4418 C  C   . ARG   C 1 174 ? 34.466  -25.661 -84.384  1.00 18.68 ? 267 ARG   C C   1 
ATOM   4419 O  O   . ARG   C 1 174 ? 35.444  -25.187 -83.778  1.00 18.80 ? 267 ARG   C O   1 
ATOM   4420 C  CB  . ARG   C 1 174 ? 32.455  -24.183 -84.066  1.00 19.64 ? 267 ARG   C CB  1 
ATOM   4421 C  CG  . ARG   C 1 174 ? 32.148  -23.973 -85.541  1.00 19.66 ? 267 ARG   C CG  1 
ATOM   4422 C  CD  . ARG   C 1 174 ? 31.675  -22.577 -85.891  1.00 20.57 ? 267 ARG   C CD  1 
ATOM   4423 N  NE  . ARG   C 1 174 ? 30.503  -22.158 -85.136  1.00 20.94 ? 267 ARG   C NE  1 
ATOM   4424 C  CZ  . ARG   C 1 174 ? 30.489  -21.277 -84.136  1.00 21.51 ? 267 ARG   C CZ  1 
ATOM   4425 N  NH1 . ARG   C 1 174 ? 31.602  -20.688 -83.724  1.00 22.29 ? 267 ARG   C NH1 1 
ATOM   4426 N  NH2 . ARG   C 1 174 ? 29.343  -20.981 -83.547  1.00 21.54 ? 267 ARG   C NH2 1 
ATOM   4427 N  N   . ASN   C 1 175 ? 34.525  -26.285 -85.557  1.00 18.08 ? 268 ASN   C N   1 
ATOM   4428 C  CA  . ASN   C 1 175 ? 35.726  -26.323 -86.424  1.00 18.70 ? 268 ASN   C CA  1 
ATOM   4429 C  C   . ASN   C 1 175 ? 35.239  -26.324 -87.873  1.00 17.86 ? 268 ASN   C C   1 
ATOM   4430 O  O   . ASN   C 1 175 ? 34.031  -26.511 -88.098  1.00 18.12 ? 268 ASN   C O   1 
ATOM   4431 C  CB  . ASN   C 1 175 ? 36.623  -27.518 -86.095  1.00 19.14 ? 268 ASN   C CB  1 
ATOM   4432 C  CG  . ASN   C 1 175 ? 37.502  -27.278 -84.886  1.00 20.00 ? 268 ASN   C CG  1 
ATOM   4433 O  OD1 . ASN   C 1 175 ? 38.491  -26.553 -84.965  1.00 21.05 ? 268 ASN   C OD1 1 
ATOM   4434 N  ND2 . ASN   C 1 175 ? 37.156  -27.887 -83.764  1.00 20.53 ? 268 ASN   C ND2 1 
ATOM   4435 N  N   . SER   C 1 176 ? 36.150  -26.128 -88.818  1.00 17.54 ? 269 SER   C N   1 
ATOM   4436 C  CA  . SER   C 1 176 ? 35.810  -25.996 -90.254  1.00 16.84 ? 269 SER   C CA  1 
ATOM   4437 C  C   . SER   C 1 176 ? 37.028  -26.339 -91.108  1.00 16.18 ? 269 SER   C C   1 
ATOM   4438 O  O   . SER   C 1 176 ? 38.159  -26.237 -90.612  1.00 15.60 ? 269 SER   C O   1 
ATOM   4439 C  CB  . SER   C 1 176 ? 35.307  -24.612 -90.554  1.00 17.21 ? 269 SER   C CB  1 
ATOM   4440 O  OG  . SER   C 1 176 ? 36.265  -23.646 -90.159  1.00 17.17 ? 269 SER   C OG  1 
ATOM   4441 N  N   . PHE   C 1 177 ? 36.768  -26.738 -92.350  1.00 16.02 ? 270 PHE   C N   1 
ATOM   4442 C  CA  . PHE   C 1 177 ? 37.787  -27.056 -93.377  1.00 15.52 ? 270 PHE   C CA  1 
ATOM   4443 C  C   . PHE   C 1 177 ? 37.168  -26.741 -94.738  1.00 16.06 ? 270 PHE   C C   1 
ATOM   4444 O  O   . PHE   C 1 177 ? 35.930  -26.862 -94.872  1.00 15.96 ? 270 PHE   C O   1 
ATOM   4445 C  CB  . PHE   C 1 177 ? 38.249  -28.511 -93.243  1.00 15.18 ? 270 PHE   C CB  1 
ATOM   4446 C  CG  . PHE   C 1 177 ? 37.142  -29.539 -93.276  1.00 15.21 ? 270 PHE   C CG  1 
ATOM   4447 C  CD1 . PHE   C 1 177 ? 36.418  -29.836 -92.131  1.00 14.92 ? 270 PHE   C CD1 1 
ATOM   4448 C  CD2 . PHE   C 1 177 ? 36.806  -30.188 -94.456  1.00 15.12 ? 270 PHE   C CD2 1 
ATOM   4449 C  CE1 . PHE   C 1 177 ? 35.400  -30.777 -92.160  1.00 14.89 ? 270 PHE   C CE1 1 
ATOM   4450 C  CE2 . PHE   C 1 177 ? 35.783  -31.123 -94.484  1.00 14.94 ? 270 PHE   C CE2 1 
ATOM   4451 C  CZ  . PHE   C 1 177 ? 35.079  -31.412 -93.336  1.00 14.99 ? 270 PHE   C CZ  1 
ATOM   4452 N  N   . GLU   C 1 178 ? 37.983  -26.307 -95.698  1.00 16.22 ? 271 GLU   C N   1 
ATOM   4453 C  CA  . GLU   C 1 178 ? 37.547  -26.155 -97.107  1.00 17.06 ? 271 GLU   C CA  1 
ATOM   4454 C  C   . GLU   C 1 178 ? 37.372  -27.554 -97.710  1.00 16.97 ? 271 GLU   C C   1 
ATOM   4455 O  O   . GLU   C 1 178 ? 38.037  -28.496 -97.240  1.00 15.67 ? 271 GLU   C O   1 
ATOM   4456 C  CB  . GLU   C 1 178 ? 38.543  -25.310 -97.898  1.00 17.72 ? 271 GLU   C CB  1 
ATOM   4457 C  CG  . GLU   C 1 178 ? 38.113  -25.072 -99.332  1.00 18.28 ? 271 GLU   C CG  1 
ATOM   4458 C  CD  . GLU   C 1 178 ? 38.988  -24.101 -100.098 1.00 18.78 ? 271 GLU   C CD  1 
ATOM   4459 O  OE1 . GLU   C 1 178 ? 39.882  -23.485 -99.468  1.00 19.69 ? 271 GLU   C OE1 1 
ATOM   4460 O  OE2 . GLU   C 1 178 ? 38.773  -23.966 -101.320 1.00 19.14 ? 271 GLU   C OE2 1 
ATOM   4461 N  N   . VAL   C 1 179 ? 36.494  -27.687 -98.705  1.00 17.52 ? 272 VAL   C N   1 
ATOM   4462 C  CA  . VAL   C 1 179 ? 36.280  -28.967 -99.437  1.00 17.89 ? 272 VAL   C CA  1 
ATOM   4463 C  C   . VAL   C 1 179 ? 36.287  -28.680 -100.937 1.00 18.32 ? 272 VAL   C C   1 
ATOM   4464 O  O   . VAL   C 1 179 ? 35.630  -27.710 -101.366 1.00 18.76 ? 272 VAL   C O   1 
ATOM   4465 C  CB  . VAL   C 1 179 ? 34.974  -29.671 -99.019  1.00 18.08 ? 272 VAL   C CB  1 
ATOM   4466 C  CG1 . VAL   C 1 179 ? 34.794  -30.995 -99.753  1.00 18.34 ? 272 VAL   C CG1 1 
ATOM   4467 C  CG2 . VAL   C 1 179 ? 34.916  -29.880 -97.520  1.00 18.20 ? 272 VAL   C CG2 1 
ATOM   4468 N  N   . ARG   C 1 180 ? 37.018  -29.502 -101.687 1.00 17.97 ? 273 ARG   C N   1 
ATOM   4469 C  CA  . ARG   C 1 180 ? 36.887  -29.623 -103.156 1.00 18.82 ? 273 ARG   C CA  1 
ATOM   4470 C  C   . ARG   C 1 180 ? 36.459  -31.060 -103.456 1.00 18.33 ? 273 ARG   C C   1 
ATOM   4471 O  O   . ARG   C 1 180 ? 37.207  -31.998 -103.089 1.00 17.85 ? 273 ARG   C O   1 
ATOM   4472 C  CB  . ARG   C 1 180 ? 38.198  -29.228 -103.837 1.00 20.01 ? 273 ARG   C CB  1 
ATOM   4473 C  CG  . ARG   C 1 180 ? 38.211  -29.448 -105.340 1.00 21.54 ? 273 ARG   C CG  1 
ATOM   4474 C  CD  . ARG   C 1 180 ? 39.570  -29.084 -105.889 1.00 22.52 ? 273 ARG   C CD  1 
ATOM   4475 N  NE  . ARG   C 1 180 ? 39.762  -29.504 -107.265 1.00 25.07 ? 273 ARG   C NE  1 
ATOM   4476 C  CZ  . ARG   C 1 180 ? 39.268  -28.885 -108.331 1.00 26.67 ? 273 ARG   C CZ  1 
ATOM   4477 N  NH1 . ARG   C 1 180 ? 38.505  -27.811 -108.193 1.00 28.23 ? 273 ARG   C NH1 1 
ATOM   4478 N  NH2 . ARG   C 1 180 ? 39.531  -29.356 -109.538 1.00 27.19 ? 273 ARG   C NH2 1 
ATOM   4479 N  N   . VAL   C 1 181 ? 35.268  -31.226 -104.032 1.00 17.74 ? 274 VAL   C N   1 
ATOM   4480 C  CA  . VAL   C 1 181 ? 34.778  -32.539 -104.534 1.00 18.17 ? 274 VAL   C CA  1 
ATOM   4481 C  C   . VAL   C 1 181 ? 35.229  -32.630 -105.995 1.00 18.64 ? 274 VAL   C C   1 
ATOM   4482 O  O   . VAL   C 1 181 ? 34.769  -31.796 -106.799 1.00 17.94 ? 274 VAL   C O   1 
ATOM   4483 C  CB  . VAL   C 1 181 ? 33.251  -32.698 -104.374 1.00 18.06 ? 274 VAL   C CB  1 
ATOM   4484 C  CG1 . VAL   C 1 181 ? 32.828  -34.140 -104.594 1.00 18.24 ? 274 VAL   C CG1 1 
ATOM   4485 C  CG2 . VAL   C 1 181 ? 32.752  -32.202 -103.024 1.00 17.91 ? 274 VAL   C CG2 1 
ATOM   4486 N  N   . CYS   C 1 182 ? 36.135  -33.564 -106.306 1.00 19.63 ? 275 CYS   C N   1 
ATOM   4487 C  CA  . CYS   C 1 182 ? 36.805  -33.669 -107.631 1.00 20.44 ? 275 CYS   C CA  1 
ATOM   4488 C  C   . CYS   C 1 182 ? 37.072  -35.135 -107.994 1.00 21.49 ? 275 CYS   C C   1 
ATOM   4489 O  O   . CYS   C 1 182 ? 36.939  -36.007 -107.116 1.00 21.39 ? 275 CYS   C O   1 
ATOM   4490 C  CB  . CYS   C 1 182 ? 38.110  -32.887 -107.628 1.00 21.04 ? 275 CYS   C CB  1 
ATOM   4491 S  SG  . CYS   C 1 182 ? 39.166  -33.276 -106.208 1.00 21.16 ? 275 CYS   C SG  1 
ATOM   4492 N  N   . ALA   C 1 183 ? 37.452  -35.383 -109.250 1.00 21.94 ? 276 ALA   C N   1 
ATOM   4493 C  CA  . ALA   C 1 183 ? 37.632  -36.736 -109.825 1.00 21.87 ? 276 ALA   C CA  1 
ATOM   4494 C  C   . ALA   C 1 183 ? 38.927  -37.369 -109.300 1.00 21.81 ? 276 ALA   C C   1 
ATOM   4495 O  O   . ALA   C 1 183 ? 38.927  -38.588 -109.045 1.00 22.10 ? 276 ALA   C O   1 
ATOM   4496 C  CB  . ALA   C 1 183 ? 37.625  -36.656 -111.331 1.00 22.54 ? 276 ALA   C CB  1 
ATOM   4497 N  N   A CYS   C 1 184 ? 39.992  -36.572 -109.154 0.50 22.20 ? 277 CYS   C N   1 
ATOM   4498 N  N   B CYS   C 1 184 ? 39.986  -36.565 -109.139 0.50 21.95 ? 277 CYS   C N   1 
ATOM   4499 C  CA  A CYS   C 1 184 ? 41.342  -37.031 -108.725 0.50 22.80 ? 277 CYS   C CA  1 
ATOM   4500 C  CA  B CYS   C 1 184 ? 41.355  -37.006 -108.746 0.50 22.40 ? 277 CYS   C CA  1 
ATOM   4501 C  C   A CYS   C 1 184 ? 41.840  -36.179 -107.561 0.50 22.16 ? 277 CYS   C C   1 
ATOM   4502 C  C   B CYS   C 1 184 ? 41.852  -36.181 -107.560 0.50 21.93 ? 277 CYS   C C   1 
ATOM   4503 O  O   A CYS   C 1 184 ? 42.643  -35.269 -107.753 0.50 22.53 ? 277 CYS   C O   1 
ATOM   4504 O  O   B CYS   C 1 184 ? 42.674  -35.285 -107.735 0.50 22.27 ? 277 CYS   C O   1 
ATOM   4505 C  CB  A CYS   C 1 184 ? 42.346  -36.970 -109.870 0.50 23.41 ? 277 CYS   C CB  1 
ATOM   4506 C  CB  B CYS   C 1 184 ? 42.332  -36.865 -109.909 0.50 22.76 ? 277 CYS   C CB  1 
ATOM   4507 S  SG  A CYS   C 1 184 ? 43.820  -37.973 -109.552 0.50 24.96 ? 277 CYS   C SG  1 
ATOM   4508 S  SG  B CYS   C 1 184 ? 41.880  -37.837 -111.370 0.50 23.69 ? 277 CYS   C SG  1 
ATOM   4509 N  N   . PRO   C 1 185 ? 41.383  -36.456 -106.320 1.00 21.60 ? 278 PRO   C N   1 
ATOM   4510 C  CA  . PRO   C 1 185 ? 41.817  -35.691 -105.146 1.00 20.76 ? 278 PRO   C CA  1 
ATOM   4511 C  C   . PRO   C 1 185 ? 43.341  -35.587 -104.968 1.00 20.42 ? 278 PRO   C C   1 
ATOM   4512 O  O   . PRO   C 1 185 ? 43.820  -34.507 -104.669 1.00 19.18 ? 278 PRO   C O   1 
ATOM   4513 C  CB  . PRO   C 1 185 ? 41.220  -36.489 -103.979 1.00 20.88 ? 278 PRO   C CB  1 
ATOM   4514 C  CG  . PRO   C 1 185 ? 40.004  -37.157 -104.568 1.00 21.31 ? 278 PRO   C CG  1 
ATOM   4515 C  CD  . PRO   C 1 185 ? 40.402  -37.502 -105.989 1.00 21.36 ? 278 PRO   C CD  1 
ATOM   4516 N  N   . GLY   C 1 186 ? 44.051  -36.704 -105.158 1.00 20.64 ? 279 GLY   C N   1 
ATOM   4517 C  CA  . GLY   C 1 186 ? 45.522  -36.783 -105.060 1.00 20.78 ? 279 GLY   C CA  1 
ATOM   4518 C  C   . GLY   C 1 186 ? 46.197  -35.754 -105.947 1.00 21.26 ? 279 GLY   C C   1 
ATOM   4519 O  O   . GLY   C 1 186 ? 46.928  -34.892 -105.414 1.00 20.98 ? 279 GLY   C O   1 
ATOM   4520 N  N   . ARG   C 1 187 ? 45.953  -35.837 -107.257 1.00 21.79 ? 280 ARG   C N   1 
ATOM   4521 C  CA  . ARG   C 1 187 ? 46.539  -34.934 -108.281 1.00 23.15 ? 280 ARG   C CA  1 
ATOM   4522 C  C   . ARG   C 1 187 ? 46.132  -33.489 -107.973 1.00 21.88 ? 280 ARG   C C   1 
ATOM   4523 O  O   . ARG   C 1 187 ? 47.011  -32.615 -108.012 1.00 21.85 ? 280 ARG   C O   1 
ATOM   4524 C  CB  . ARG   C 1 187 ? 46.084  -35.361 -109.680 1.00 25.41 ? 280 ARG   C CB  1 
ATOM   4525 C  CG  . ARG   C 1 187 ? 46.630  -34.505 -110.813 1.00 28.27 ? 280 ARG   C CG  1 
ATOM   4526 C  CD  . ARG   C 1 187 ? 45.790  -34.668 -112.066 1.00 31.63 ? 280 ARG   C CD  1 
ATOM   4527 N  NE  . ARG   C 1 187 ? 44.449  -34.127 -111.863 1.00 34.49 ? 280 ARG   C NE  1 
ATOM   4528 C  CZ  . ARG   C 1 187 ? 43.412  -34.306 -112.682 1.00 35.83 ? 280 ARG   C CZ  1 
ATOM   4529 N  NH1 . ARG   C 1 187 ? 43.540  -35.026 -113.785 1.00 37.19 ? 280 ARG   C NH1 1 
ATOM   4530 N  NH2 . ARG   C 1 187 ? 42.243  -33.759 -112.389 1.00 36.18 ? 280 ARG   C NH2 1 
ATOM   4531 N  N   . ASP   C 1 188 ? 44.855  -33.245 -107.670 1.00 21.50 ? 281 ASP   C N   1 
ATOM   4532 C  CA  . ASP   C 1 188 ? 44.335  -31.874 -107.415 1.00 20.88 ? 281 ASP   C CA  1 
ATOM   4533 C  C   . ASP   C 1 188 ? 45.013  -31.299 -106.166 1.00 19.39 ? 281 ASP   C C   1 
ATOM   4534 O  O   . ASP   C 1 188 ? 45.387  -30.116 -106.201 1.00 19.45 ? 281 ASP   C O   1 
ATOM   4535 C  CB  . ASP   C 1 188 ? 42.809  -31.861 -107.317 1.00 22.36 ? 281 ASP   C CB  1 
ATOM   4536 C  CG  . ASP   C 1 188 ? 42.113  -32.116 -108.646 1.00 23.79 ? 281 ASP   C CG  1 
ATOM   4537 O  OD1 . ASP   C 1 188 ? 42.816  -32.339 -109.653 1.00 24.36 ? 281 ASP   C OD1 1 
ATOM   4538 O  OD2 . ASP   C 1 188 ? 40.877  -32.083 -108.663 1.00 25.28 ? 281 ASP   C OD2 1 
ATOM   4539 N  N   . ARG   C 1 189 ? 45.189  -32.098 -105.107 1.00 18.24 ? 282 ARG   C N   1 
ATOM   4540 C  CA  . ARG   C 1 189 ? 45.877  -31.636 -103.871 1.00 18.05 ? 282 ARG   C CA  1 
ATOM   4541 C  C   . ARG   C 1 189 ? 47.322  -31.259 -104.217 1.00 18.04 ? 282 ARG   C C   1 
ATOM   4542 O  O   . ARG   C 1 189 ? 47.741  -30.131 -103.874 1.00 18.08 ? 282 ARG   C O   1 
ATOM   4543 C  CB  . ARG   C 1 189 ? 45.864  -32.685 -102.753 1.00 17.59 ? 282 ARG   C CB  1 
ATOM   4544 C  CG  . ARG   C 1 189 ? 46.670  -32.248 -101.536 1.00 17.30 ? 282 ARG   C CG  1 
ATOM   4545 C  CD  . ARG   C 1 189 ? 46.489  -33.086 -100.288 1.00 17.26 ? 282 ARG   C CD  1 
ATOM   4546 N  NE  . ARG   C 1 189 ? 47.641  -32.894 -99.419  1.00 17.05 ? 282 ARG   C NE  1 
ATOM   4547 C  CZ  . ARG   C 1 189 ? 48.136  -33.788 -98.572  1.00 17.26 ? 282 ARG   C CZ  1 
ATOM   4548 N  NH1 . ARG   C 1 189 ? 47.575  -34.978 -98.432  1.00 17.21 ? 282 ARG   C NH1 1 
ATOM   4549 N  NH2 . ARG   C 1 189 ? 49.209  -33.481 -97.864  1.00 17.34 ? 282 ARG   C NH2 1 
ATOM   4550 N  N   . ARG   C 1 190 ? 48.055  -32.163 -104.872 1.00 18.92 ? 283 ARG   C N   1 
ATOM   4551 C  CA  . ARG   C 1 190 ? 49.496  -31.961 -105.193 1.00 19.60 ? 283 ARG   C CA  1 
ATOM   4552 C  C   . ARG   C 1 190 ? 49.659  -30.692 -106.039 1.00 21.05 ? 283 ARG   C C   1 
ATOM   4553 O  O   . ARG   C 1 190 ? 50.607  -29.925 -105.765 1.00 22.40 ? 283 ARG   C O   1 
ATOM   4554 C  CB  . ARG   C 1 190 ? 50.092  -33.177 -105.904 1.00 19.20 ? 283 ARG   C CB  1 
ATOM   4555 C  CG  . ARG   C 1 190 ? 51.614  -33.214 -105.855 1.00 18.94 ? 283 ARG   C CG  1 
ATOM   4556 C  CD  . ARG   C 1 190 ? 52.191  -34.392 -106.609 1.00 19.11 ? 283 ARG   C CD  1 
ATOM   4557 N  NE  . ARG   C 1 190 ? 51.836  -35.676 -106.020 1.00 19.07 ? 283 ARG   C NE  1 
ATOM   4558 C  CZ  . ARG   C 1 190 ? 52.199  -36.860 -106.506 1.00 19.89 ? 283 ARG   C CZ  1 
ATOM   4559 N  NH1 . ARG   C 1 190 ? 52.943  -36.937 -107.597 1.00 19.85 ? 283 ARG   C NH1 1 
ATOM   4560 N  NH2 . ARG   C 1 190 ? 51.817  -37.970 -105.897 1.00 20.10 ? 283 ARG   C NH2 1 
ATOM   4561 N  N   . THR   C 1 191 ? 48.768  -30.474 -107.012 1.00 22.65 ? 284 THR   C N   1 
ATOM   4562 C  CA  . THR   C 1 191 ? 48.773  -29.295 -107.922 1.00 23.92 ? 284 THR   C CA  1 
ATOM   4563 C  C   . THR   C 1 191 ? 48.504  -28.012 -107.121 1.00 25.19 ? 284 THR   C C   1 
ATOM   4564 O  O   . THR   C 1 191 ? 49.250  -27.040 -107.319 1.00 25.32 ? 284 THR   C O   1 
ATOM   4565 C  CB  . THR   C 1 191 ? 47.776  -29.488 -109.074 1.00 24.43 ? 284 THR   C CB  1 
ATOM   4566 O  OG1 . THR   C 1 191 ? 48.192  -30.649 -109.795 1.00 23.85 ? 284 THR   C OG1 1 
ATOM   4567 C  CG2 . THR   C 1 191 ? 47.687  -28.297 -110.004 1.00 24.38 ? 284 THR   C CG2 1 
ATOM   4568 N  N   . GLU   C 1 192 ? 47.489  -28.002 -106.248 1.00 26.33 ? 285 GLU   C N   1 
ATOM   4569 C  CA  . GLU   C 1 192 ? 47.120  -26.807 -105.436 1.00 27.73 ? 285 GLU   C CA  1 
ATOM   4570 C  C   . GLU   C 1 192 ? 48.242  -26.460 -104.448 1.00 28.67 ? 285 GLU   C C   1 
ATOM   4571 O  O   . GLU   C 1 192 ? 48.387  -25.269 -104.137 1.00 31.20 ? 285 GLU   C O   1 
ATOM   4572 C  CB  . GLU   C 1 192 ? 45.800  -27.019 -104.695 1.00 28.06 ? 285 GLU   C CB  1 
ATOM   4573 C  CG  . GLU   C 1 192 ? 44.584  -26.915 -105.599 1.00 28.58 ? 285 GLU   C CG  1 
ATOM   4574 C  CD  . GLU   C 1 192 ? 43.286  -26.569 -104.890 1.00 29.08 ? 285 GLU   C CD  1 
ATOM   4575 O  OE1 . GLU   C 1 192 ? 43.352  -26.087 -103.743 1.00 29.24 ? 285 GLU   C OE1 1 
ATOM   4576 O  OE2 . GLU   C 1 192 ? 42.212  -26.780 -105.491 1.00 28.87 ? 285 GLU   C OE2 1 
ATOM   4577 N  N   . GLU   C 1 193 ? 49.005  -27.449 -103.972 1.00 28.68 ? 286 GLU   C N   1 
ATOM   4578 C  CA  . GLU   C 1 193 ? 50.121  -27.230 -103.012 1.00 29.83 ? 286 GLU   C CA  1 
ATOM   4579 C  C   . GLU   C 1 193 ? 51.380  -26.764 -103.758 1.00 32.79 ? 286 GLU   C C   1 
ATOM   4580 O  O   . GLU   C 1 193 ? 52.265  -26.191 -103.091 1.00 31.30 ? 286 GLU   C O   1 
ATOM   4581 C  CB  . GLU   C 1 193 ? 50.382  -28.498 -102.197 1.00 28.66 ? 286 GLU   C CB  1 
ATOM   4582 C  CG  . GLU   C 1 193 ? 49.320  -28.738 -101.137 1.00 27.68 ? 286 GLU   C CG  1 
ATOM   4583 C  CD  . GLU   C 1 193 ? 49.419  -30.056 -100.393 1.00 26.72 ? 286 GLU   C CD  1 
ATOM   4584 O  OE1 . GLU   C 1 193 ? 50.274  -30.884 -100.757 1.00 27.51 ? 286 GLU   C OE1 1 
ATOM   4585 O  OE2 . GLU   C 1 193 ? 48.639  -30.250 -99.445  1.00 24.16 ? 286 GLU   C OE2 1 
ATOM   4586 N  N   . GLU   C 1 194 ? 51.448  -26.992 -105.076 1.00 36.35 ? 287 GLU   C N   1 
ATOM   4587 C  CA  . GLU   C 1 194 ? 52.641  -26.731 -105.934 1.00 41.23 ? 287 GLU   C CA  1 
ATOM   4588 C  C   . GLU   C 1 194 ? 53.052  -25.257 -105.858 1.00 42.59 ? 287 GLU   C C   1 
ATOM   4589 O  O   . GLU   C 1 194 ? 54.266  -24.987 -105.777 1.00 44.11 ? 287 GLU   C O   1 
ATOM   4590 C  CB  . GLU   C 1 194 ? 52.351  -27.106 -107.390 1.00 44.32 ? 287 GLU   C CB  1 
ATOM   4591 C  CG  . GLU   C 1 194 ? 53.437  -26.674 -108.364 1.00 47.30 ? 287 GLU   C CG  1 
ATOM   4592 C  CD  . GLU   C 1 194 ? 53.115  -26.927 -109.826 1.00 49.50 ? 287 GLU   C CD  1 
ATOM   4593 O  OE1 . GLU   C 1 194 ? 54.017  -26.726 -110.668 1.00 51.80 ? 287 GLU   C OE1 1 
ATOM   4594 O  OE2 . GLU   C 1 194 ? 51.964  -27.319 -110.119 1.00 48.92 ? 287 GLU   C OE2 1 
ATOM   4595 N  N   . ASN   C 1 195 ? 52.077  -24.348 -105.907 1.00 45.11 ? 288 ASN   C N   1 
ATOM   4596 C  CA  . ASN   C 1 195 ? 52.301  -22.880 -105.995 1.00 47.17 ? 288 ASN   C CA  1 
ATOM   4597 C  C   . ASN   C 1 195 ? 52.835  -22.351 -104.655 1.00 47.52 ? 288 ASN   C C   1 
ATOM   4598 O  O   . ASN   C 1 195 ? 53.477  -21.288 -104.675 1.00 48.49 ? 288 ASN   C O   1 
ATOM   4599 C  CB  . ASN   C 1 195 ? 51.036  -22.144 -106.455 1.00 49.04 ? 288 ASN   C CB  1 
ATOM   4600 C  CG  . ASN   C 1 195 ? 49.826  -22.409 -105.583 1.00 50.36 ? 288 ASN   C CG  1 
ATOM   4601 O  OD1 . ASN   C 1 195 ? 48.856  -23.014 -106.033 1.00 52.77 ? 288 ASN   C OD1 1 
ATOM   4602 N  ND2 . ASN   C 1 195 ? 49.871  -21.960 -104.340 1.00 50.74 ? 288 ASN   C ND2 1 
ATOM   4603 N  N   . LEU   C 1 196 ? 52.586  -23.059 -103.544 1.00 47.16 ? 289 LEU   C N   1 
ATOM   4604 C  CA  . LEU   C 1 196 ? 52.998  -22.638 -102.175 1.00 46.35 ? 289 LEU   C CA  1 
ATOM   4605 C  C   . LEU   C 1 196 ? 54.523  -22.482 -102.139 1.00 45.75 ? 289 LEU   C C   1 
ATOM   4606 O  O   . LEU   C 1 196 ? 55.020  -21.382 -101.907 1.00 48.53 ? 289 LEU   C O   1 
ATOM   4607 C  CB  . LEU   C 1 196 ? 52.535  -23.668 -101.136 1.00 44.67 ? 289 LEU   C CB  1 
ATOM   4608 C  CG  . LEU   C 1 196 ? 51.027  -23.900 -101.025 1.00 44.49 ? 289 LEU   C CG  1 
ATOM   4609 C  CD1 . LEU   C 1 196 ? 50.733  -25.065 -100.091 1.00 43.67 ? 289 LEU   C CD1 1 
ATOM   4610 C  CD2 . LEU   C 1 196 ? 50.306  -22.646 -100.551 1.00 44.46 ? 289 LEU   C CD2 1 
ATOM   4611 N  N   . SER   D 1 3   ? 17.346  -15.292 -46.055  1.00 58.06 ? 96  SER   D N   1 
ATOM   4612 C  CA  . SER   D 1 3   ? 18.344  -15.757 -45.055  1.00 57.14 ? 96  SER   D CA  1 
ATOM   4613 C  C   . SER   D 1 3   ? 19.583  -16.313 -45.764  1.00 56.19 ? 96  SER   D C   1 
ATOM   4614 O  O   . SER   D 1 3   ? 19.552  -16.454 -47.008  1.00 59.20 ? 96  SER   D O   1 
ATOM   4615 C  CB  . SER   D 1 3   ? 17.747  -16.788 -44.130  1.00 57.97 ? 96  SER   D CB  1 
ATOM   4616 O  OG  . SER   D 1 3   ? 18.761  -17.472 -43.408  1.00 59.44 ? 96  SER   D OG  1 
ATOM   4617 N  N   . VAL   D 1 4   ? 20.628  -16.602 -44.983  1.00 52.44 ? 97  VAL   D N   1 
ATOM   4618 C  CA  . VAL   D 1 4   ? 21.842  -17.357 -45.411  1.00 49.05 ? 97  VAL   D CA  1 
ATOM   4619 C  C   . VAL   D 1 4   ? 22.136  -18.404 -44.341  1.00 46.27 ? 97  VAL   D C   1 
ATOM   4620 O  O   . VAL   D 1 4   ? 22.322  -18.049 -43.179  1.00 43.12 ? 97  VAL   D O   1 
ATOM   4621 C  CB  . VAL   D 1 4   ? 23.045  -16.420 -45.624  1.00 49.15 ? 97  VAL   D CB  1 
ATOM   4622 C  CG1 . VAL   D 1 4   ? 24.285  -17.187 -46.053  1.00 48.94 ? 97  VAL   D CG1 1 
ATOM   4623 C  CG2 . VAL   D 1 4   ? 22.731  -15.317 -46.622  1.00 49.79 ? 97  VAL   D CG2 1 
ATOM   4624 N  N   . PRO   D 1 5   ? 22.171  -19.715 -44.684  1.00 43.88 ? 98  PRO   D N   1 
ATOM   4625 C  CA  . PRO   D 1 5   ? 22.535  -20.749 -43.717  1.00 42.60 ? 98  PRO   D CA  1 
ATOM   4626 C  C   . PRO   D 1 5   ? 23.970  -20.522 -43.220  1.00 41.57 ? 98  PRO   D C   1 
ATOM   4627 O  O   . PRO   D 1 5   ? 24.805  -20.137 -44.023  1.00 40.68 ? 98  PRO   D O   1 
ATOM   4628 C  CB  . PRO   D 1 5   ? 22.430  -22.078 -44.486  1.00 42.86 ? 98  PRO   D CB  1 
ATOM   4629 C  CG  . PRO   D 1 5   ? 21.656  -21.746 -45.752  1.00 43.66 ? 98  PRO   D CG  1 
ATOM   4630 C  CD  . PRO   D 1 5   ? 21.878  -20.270 -46.014  1.00 44.09 ? 98  PRO   D CD  1 
ATOM   4631 N  N   . SER   D 1 6   ? 24.218  -20.745 -41.926  1.00 39.98 ? 99  SER   D N   1 
ATOM   4632 C  CA  . SER   D 1 6   ? 25.562  -20.639 -41.301  1.00 38.71 ? 99  SER   D CA  1 
ATOM   4633 C  C   . SER   D 1 6   ? 26.517  -21.601 -42.013  1.00 38.21 ? 99  SER   D C   1 
ATOM   4634 O  O   . SER   D 1 6   ? 26.091  -22.738 -42.293  1.00 37.16 ? 99  SER   D O   1 
ATOM   4635 C  CB  . SER   D 1 6   ? 25.510  -20.926 -39.824  1.00 38.01 ? 99  SER   D CB  1 
ATOM   4636 O  OG  . SER   D 1 6   ? 24.371  -20.326 -39.230  1.00 38.11 ? 99  SER   D OG  1 
ATOM   4637 N  N   . GLN   D 1 7   ? 27.745  -21.153 -42.301  1.00 37.98 ? 100 GLN   D N   1 
ATOM   4638 C  CA  . GLN   D 1 7   ? 28.830  -21.998 -42.871  1.00 38.63 ? 100 GLN   D CA  1 
ATOM   4639 C  C   . GLN   D 1 7   ? 30.018  -22.054 -41.901  1.00 36.49 ? 100 GLN   D C   1 
ATOM   4640 O  O   . GLN   D 1 7   ? 31.051  -22.623 -42.287  1.00 36.04 ? 100 GLN   D O   1 
ATOM   4641 C  CB  . GLN   D 1 7   ? 29.236  -21.504 -44.263  1.00 41.54 ? 100 GLN   D CB  1 
ATOM   4642 C  CG  . GLN   D 1 7   ? 29.691  -20.052 -44.325  1.00 44.70 ? 100 GLN   D CG  1 
ATOM   4643 C  CD  . GLN   D 1 7   ? 29.876  -19.598 -45.753  1.00 48.00 ? 100 GLN   D CD  1 
ATOM   4644 O  OE1 . GLN   D 1 7   ? 29.004  -19.785 -46.593  1.00 50.03 ? 100 GLN   D OE1 1 
ATOM   4645 N  NE2 . GLN   D 1 7   ? 31.017  -18.996 -46.048  1.00 50.20 ? 100 GLN   D NE2 1 
ATOM   4646 N  N   . LYS   D 1 8   ? 29.866  -21.533 -40.678  1.00 35.07 ? 101 LYS   D N   1 
ATOM   4647 C  CA  . LYS   D 1 8   ? 30.916  -21.570 -39.625  1.00 34.58 ? 101 LYS   D CA  1 
ATOM   4648 C  C   . LYS   D 1 8   ? 31.264  -23.027 -39.304  1.00 32.07 ? 101 LYS   D C   1 
ATOM   4649 O  O   . LYS   D 1 8   ? 30.342  -23.795 -38.952  1.00 30.95 ? 101 LYS   D O   1 
ATOM   4650 C  CB  . LYS   D 1 8   ? 30.449  -20.863 -38.350  1.00 36.56 ? 101 LYS   D CB  1 
ATOM   4651 C  CG  . LYS   D 1 8   ? 30.264  -19.359 -38.475  1.00 38.52 ? 101 LYS   D CG  1 
ATOM   4652 C  CD  . LYS   D 1 8   ? 30.507  -18.609 -37.182  1.00 39.70 ? 101 LYS   D CD  1 
ATOM   4653 C  CE  . LYS   D 1 8   ? 30.443  -17.106 -37.357  1.00 40.34 ? 101 LYS   D CE  1 
ATOM   4654 N  NZ  . LYS   D 1 8   ? 30.546  -16.398 -36.059  1.00 41.19 ? 101 LYS   D NZ  1 
ATOM   4655 N  N   . THR   D 1 9   ? 32.543  -23.385 -39.418  1.00 30.03 ? 102 THR   D N   1 
ATOM   4656 C  CA  . THR   D 1 9   ? 33.091  -24.698 -38.991  1.00 30.09 ? 102 THR   D CA  1 
ATOM   4657 C  C   . THR   D 1 9   ? 32.812  -24.881 -37.495  1.00 29.91 ? 102 THR   D C   1 
ATOM   4658 O  O   . THR   D 1 9   ? 33.066  -23.932 -36.721  1.00 29.31 ? 102 THR   D O   1 
ATOM   4659 C  CB  . THR   D 1 9   ? 34.585  -24.814 -39.318  1.00 30.12 ? 102 THR   D CB  1 
ATOM   4660 O  OG1 . THR   D 1 9   ? 34.709  -24.653 -40.732  1.00 31.17 ? 102 THR   D OG1 1 
ATOM   4661 C  CG2 . THR   D 1 9   ? 35.190  -26.132 -38.884  1.00 29.91 ? 102 THR   D CG2 1 
ATOM   4662 N  N   . TYR   D 1 10  ? 32.268  -26.042 -37.128  1.00 29.11 ? 103 TYR   D N   1 
ATOM   4663 C  CA  . TYR   D 1 10  ? 32.077  -26.507 -35.731  1.00 29.80 ? 103 TYR   D CA  1 
ATOM   4664 C  C   . TYR   D 1 10  ? 32.265  -28.025 -35.695  1.00 27.65 ? 103 TYR   D C   1 
ATOM   4665 O  O   . TYR   D 1 10  ? 31.418  -28.742 -36.259  1.00 26.40 ? 103 TYR   D O   1 
ATOM   4666 C  CB  . TYR   D 1 10  ? 30.693  -26.115 -35.211  1.00 32.89 ? 103 TYR   D CB  1 
ATOM   4667 C  CG  . TYR   D 1 10  ? 30.545  -24.665 -34.824  1.00 35.39 ? 103 TYR   D CG  1 
ATOM   4668 C  CD1 . TYR   D 1 10  ? 31.119  -24.173 -33.662  1.00 36.61 ? 103 TYR   D CD1 1 
ATOM   4669 C  CD2 . TYR   D 1 10  ? 29.817  -23.785 -35.609  1.00 36.93 ? 103 TYR   D CD2 1 
ATOM   4670 C  CE1 . TYR   D 1 10  ? 30.982  -22.844 -33.295  1.00 37.39 ? 103 TYR   D CE1 1 
ATOM   4671 C  CE2 . TYR   D 1 10  ? 29.669  -22.453 -35.257  1.00 37.98 ? 103 TYR   D CE2 1 
ATOM   4672 C  CZ  . TYR   D 1 10  ? 30.252  -21.981 -34.094  1.00 38.95 ? 103 TYR   D CZ  1 
ATOM   4673 O  OH  . TYR   D 1 10  ? 30.105  -20.668 -33.745  1.00 38.86 ? 103 TYR   D OH  1 
ATOM   4674 N  N   . GLN   D 1 11  ? 33.345  -28.498 -35.069  1.00 26.30 ? 104 GLN   D N   1 
ATOM   4675 C  CA  . GLN   D 1 11  ? 33.614  -29.948 -34.886  1.00 26.51 ? 104 GLN   D CA  1 
ATOM   4676 C  C   . GLN   D 1 11  ? 32.641  -30.511 -33.839  1.00 25.68 ? 104 GLN   D C   1 
ATOM   4677 O  O   . GLN   D 1 11  ? 32.265  -31.691 -33.960  1.00 24.52 ? 104 GLN   D O   1 
ATOM   4678 C  CB  . GLN   D 1 11  ? 35.084  -30.174 -34.525  1.00 27.81 ? 104 GLN   D CB  1 
ATOM   4679 C  CG  . GLN   D 1 11  ? 36.040  -29.752 -35.636  1.00 29.05 ? 104 GLN   D CG  1 
ATOM   4680 C  CD  . GLN   D 1 11  ? 37.423  -30.347 -35.510  1.00 31.37 ? 104 GLN   D CD  1 
ATOM   4681 O  OE1 . GLN   D 1 11  ? 37.744  -31.035 -34.543  1.00 32.73 ? 104 GLN   D OE1 1 
ATOM   4682 N  NE2 . GLN   D 1 11  ? 38.265  -30.080 -36.498  1.00 32.38 ? 104 GLN   D NE2 1 
ATOM   4683 N  N   . GLY   D 1 12  ? 32.243  -29.690 -32.862  1.00 25.73 ? 105 GLY   D N   1 
ATOM   4684 C  CA  . GLY   D 1 12  ? 31.222  -30.023 -31.847  1.00 26.69 ? 105 GLY   D CA  1 
ATOM   4685 C  C   . GLY   D 1 12  ? 31.583  -31.246 -31.017  1.00 27.23 ? 105 GLY   D C   1 
ATOM   4686 O  O   . GLY   D 1 12  ? 32.782  -31.595 -30.951  1.00 28.02 ? 105 GLY   D O   1 
ATOM   4687 N  N   . SER   D 1 13  ? 30.570  -31.890 -30.426  1.00 27.53 ? 106 SER   D N   1 
ATOM   4688 C  CA  . SER   D 1 13  ? 30.705  -32.943 -29.385  1.00 27.87 ? 106 SER   D CA  1 
ATOM   4689 C  C   . SER   D 1 13  ? 31.471  -34.154 -29.923  1.00 27.30 ? 106 SER   D C   1 
ATOM   4690 O  O   . SER   D 1 13  ? 32.253  -34.728 -29.154  1.00 26.58 ? 106 SER   D O   1 
ATOM   4691 C  CB  . SER   D 1 13  ? 29.358  -33.360 -28.849  1.00 27.68 ? 106 SER   D CB  1 
ATOM   4692 O  OG  . SER   D 1 13  ? 29.494  -34.397 -27.884  1.00 28.49 ? 106 SER   D OG  1 
ATOM   4693 N  N   . TYR   D 1 14  ? 31.240  -34.538 -31.181  1.00 27.26 ? 107 TYR   D N   1 
ATOM   4694 C  CA  . TYR   D 1 14  ? 31.733  -35.813 -31.769  1.00 27.24 ? 107 TYR   D CA  1 
ATOM   4695 C  C   . TYR   D 1 14  ? 33.032  -35.595 -32.559  1.00 26.68 ? 107 TYR   D C   1 
ATOM   4696 O  O   . TYR   D 1 14  ? 33.479  -36.547 -33.226  1.00 26.41 ? 107 TYR   D O   1 
ATOM   4697 C  CB  . TYR   D 1 14  ? 30.620  -36.452 -32.606  1.00 27.91 ? 107 TYR   D CB  1 
ATOM   4698 C  CG  . TYR   D 1 14  ? 29.399  -36.798 -31.792  1.00 28.17 ? 107 TYR   D CG  1 
ATOM   4699 C  CD1 . TYR   D 1 14  ? 29.383  -37.920 -30.980  1.00 29.17 ? 107 TYR   D CD1 1 
ATOM   4700 C  CD2 . TYR   D 1 14  ? 28.276  -35.987 -31.794  1.00 28.39 ? 107 TYR   D CD2 1 
ATOM   4701 C  CE1 . TYR   D 1 14  ? 28.282  -38.239 -30.204  1.00 28.84 ? 107 TYR   D CE1 1 
ATOM   4702 C  CE2 . TYR   D 1 14  ? 27.161  -36.296 -31.030  1.00 28.53 ? 107 TYR   D CE2 1 
ATOM   4703 C  CZ  . TYR   D 1 14  ? 27.166  -37.426 -30.230  1.00 28.66 ? 107 TYR   D CZ  1 
ATOM   4704 O  OH  . TYR   D 1 14  ? 26.088  -37.753 -29.461  1.00 29.32 ? 107 TYR   D OH  1 
ATOM   4705 N  N   . GLY   D 1 15  ? 33.637  -34.404 -32.466  1.00 26.80 ? 108 GLY   D N   1 
ATOM   4706 C  CA  . GLY   D 1 15  ? 34.897  -34.068 -33.161  1.00 26.90 ? 108 GLY   D CA  1 
ATOM   4707 C  C   . GLY   D 1 15  ? 34.775  -34.323 -34.654  1.00 27.21 ? 108 GLY   D C   1 
ATOM   4708 O  O   . GLY   D 1 15  ? 35.640  -35.028 -35.223  1.00 26.48 ? 108 GLY   D O   1 
ATOM   4709 N  N   . PHE   D 1 16  ? 33.712  -33.789 -35.255  1.00 26.03 ? 109 PHE   D N   1 
ATOM   4710 C  CA  . PHE   D 1 16  ? 33.316  -34.022 -36.667  1.00 25.55 ? 109 PHE   D CA  1 
ATOM   4711 C  C   . PHE   D 1 16  ? 34.217  -33.197 -37.588  1.00 25.23 ? 109 PHE   D C   1 
ATOM   4712 O  O   . PHE   D 1 16  ? 34.255  -31.955 -37.441  1.00 23.71 ? 109 PHE   D O   1 
ATOM   4713 C  CB  . PHE   D 1 16  ? 31.840  -33.671 -36.868  1.00 25.44 ? 109 PHE   D CB  1 
ATOM   4714 C  CG  . PHE   D 1 16  ? 31.368  -33.689 -38.300  1.00 25.70 ? 109 PHE   D CG  1 
ATOM   4715 C  CD1 . PHE   D 1 16  ? 31.567  -34.804 -39.100  1.00 26.58 ? 109 PHE   D CD1 1 
ATOM   4716 C  CD2 . PHE   D 1 16  ? 30.703  -32.600 -38.842  1.00 25.55 ? 109 PHE   D CD2 1 
ATOM   4717 C  CE1 . PHE   D 1 16  ? 31.123  -34.824 -40.415  1.00 26.68 ? 109 PHE   D CE1 1 
ATOM   4718 C  CE2 . PHE   D 1 16  ? 30.260  -32.620 -40.157  1.00 26.17 ? 109 PHE   D CE2 1 
ATOM   4719 C  CZ  . PHE   D 1 16  ? 30.472  -33.731 -40.942  1.00 25.86 ? 109 PHE   D CZ  1 
ATOM   4720 N  N   . ARG   D 1 17  ? 34.916  -33.869 -38.508  1.00 26.13 ? 110 ARG   D N   1 
ATOM   4721 C  CA  . ARG   D 1 17  ? 35.626  -33.206 -39.636  1.00 27.06 ? 110 ARG   D CA  1 
ATOM   4722 C  C   . ARG   D 1 17  ? 35.503  -34.066 -40.903  1.00 25.15 ? 110 ARG   D C   1 
ATOM   4723 O  O   . ARG   D 1 17  ? 35.088  -35.242 -40.809  1.00 24.14 ? 110 ARG   D O   1 
ATOM   4724 C  CB  . ARG   D 1 17  ? 37.083  -32.882 -39.278  1.00 29.06 ? 110 ARG   D CB  1 
ATOM   4725 C  CG  . ARG   D 1 17  ? 37.995  -34.086 -39.102  1.00 31.71 ? 110 ARG   D CG  1 
ATOM   4726 C  CD  . ARG   D 1 17  ? 38.107  -34.550 -37.663  1.00 33.87 ? 110 ARG   D CD  1 
ATOM   4727 N  NE  . ARG   D 1 17  ? 39.138  -35.577 -37.530  1.00 36.34 ? 110 ARG   D NE  1 
ATOM   4728 C  CZ  . ARG   D 1 17  ? 39.120  -36.583 -36.656  1.00 36.70 ? 110 ARG   D CZ  1 
ATOM   4729 N  NH1 . ARG   D 1 17  ? 38.116  -36.727 -35.804  1.00 36.64 ? 110 ARG   D NH1 1 
ATOM   4730 N  NH2 . ARG   D 1 17  ? 40.115  -37.453 -36.645  1.00 37.44 ? 110 ARG   D NH2 1 
ATOM   4731 N  N   . LEU   D 1 18  ? 35.833  -33.467 -42.047  1.00 24.27 ? 111 LEU   D N   1 
ATOM   4732 C  CA  . LEU   D 1 18  ? 35.735  -34.098 -43.387  1.00 23.14 ? 111 LEU   D CA  1 
ATOM   4733 C  C   . LEU   D 1 18  ? 37.121  -34.578 -43.814  1.00 22.76 ? 111 LEU   D C   1 
ATOM   4734 O  O   . LEU   D 1 18  ? 38.111  -33.906 -43.470  1.00 23.42 ? 111 LEU   D O   1 
ATOM   4735 C  CB  . LEU   D 1 18  ? 35.170  -33.080 -44.382  1.00 22.98 ? 111 LEU   D CB  1 
ATOM   4736 C  CG  . LEU   D 1 18  ? 33.774  -32.556 -44.057  1.00 22.30 ? 111 LEU   D CG  1 
ATOM   4737 C  CD1 . LEU   D 1 18  ? 33.303  -31.581 -45.123  1.00 22.35 ? 111 LEU   D CD1 1 
ATOM   4738 C  CD2 . LEU   D 1 18  ? 32.788  -33.703 -43.898  1.00 22.44 ? 111 LEU   D CD2 1 
ATOM   4739 N  N   . GLY   D 1 19  ? 37.162  -35.708 -44.520  1.00 21.99 ? 112 GLY   D N   1 
ATOM   4740 C  CA  . GLY   D 1 19  ? 38.351  -36.217 -45.224  1.00 21.93 ? 112 GLY   D CA  1 
ATOM   4741 C  C   . GLY   D 1 19  ? 38.050  -36.448 -46.691  1.00 21.01 ? 112 GLY   D C   1 
ATOM   4742 O  O   . GLY   D 1 19  ? 36.870  -36.639 -47.035  1.00 20.14 ? 112 GLY   D O   1 
ATOM   4743 N  N   . PHE   D 1 20  ? 39.084  -36.416 -47.530  1.00 20.06 ? 113 PHE   D N   1 
ATOM   4744 C  CA  . PHE   D 1 20  ? 38.992  -36.644 -48.994  1.00 20.16 ? 113 PHE   D CA  1 
ATOM   4745 C  C   . PHE   D 1 20  ? 40.104  -37.618 -49.385  1.00 19.59 ? 113 PHE   D C   1 
ATOM   4746 O  O   . PHE   D 1 20  ? 41.186  -37.581 -48.758  1.00 19.70 ? 113 PHE   D O   1 
ATOM   4747 C  CB  . PHE   D 1 20  ? 39.057  -35.306 -49.734  1.00 19.75 ? 113 PHE   D CB  1 
ATOM   4748 C  CG  . PHE   D 1 20  ? 38.074  -34.281 -49.226  1.00 19.79 ? 113 PHE   D CG  1 
ATOM   4749 C  CD1 . PHE   D 1 20  ? 38.391  -33.468 -48.148  1.00 19.18 ? 113 PHE   D CD1 1 
ATOM   4750 C  CD2 . PHE   D 1 20  ? 36.823  -34.134 -49.814  1.00 19.43 ? 113 PHE   D CD2 1 
ATOM   4751 C  CE1 . PHE   D 1 20  ? 37.483  -32.537 -47.667  1.00 19.00 ? 113 PHE   D CE1 1 
ATOM   4752 C  CE2 . PHE   D 1 20  ? 35.920  -33.195 -49.336  1.00 18.76 ? 113 PHE   D CE2 1 
ATOM   4753 C  CZ  . PHE   D 1 20  ? 36.252  -32.398 -48.264  1.00 19.00 ? 113 PHE   D CZ  1 
ATOM   4754 N  N   . LEU   D 1 21  ? 39.837  -38.493 -50.354  1.00 19.77 ? 114 LEU   D N   1 
ATOM   4755 C  CA  . LEU   D 1 21  ? 40.860  -39.423 -50.897  1.00 19.59 ? 114 LEU   D CA  1 
ATOM   4756 C  C   . LEU   D 1 21  ? 42.023  -38.582 -51.439  1.00 19.50 ? 114 LEU   D C   1 
ATOM   4757 O  O   . LEU   D 1 21  ? 41.763  -37.469 -51.959  1.00 19.75 ? 114 LEU   D O   1 
ATOM   4758 C  CB  . LEU   D 1 21  ? 40.244  -40.306 -51.986  1.00 19.70 ? 114 LEU   D CB  1 
ATOM   4759 C  CG  . LEU   D 1 21  ? 39.228  -41.347 -51.510  1.00 19.67 ? 114 LEU   D CG  1 
ATOM   4760 C  CD1 . LEU   D 1 21  ? 38.549  -42.016 -52.696  1.00 19.68 ? 114 LEU   D CD1 1 
ATOM   4761 C  CD2 . LEU   D 1 21  ? 39.888  -42.393 -50.624  1.00 19.77 ? 114 LEU   D CD2 1 
ATOM   4762 N  N   . HIS   D 1 22  ? 43.257  -39.069 -51.268  1.00 18.76 ? 115 HIS   D N   1 
ATOM   4763 C  CA  . HIS   D 1 22  ? 44.487  -38.462 -51.843  1.00 18.17 ? 115 HIS   D CA  1 
ATOM   4764 C  C   . HIS   D 1 22  ? 44.621  -38.979 -53.274  1.00 18.09 ? 115 HIS   D C   1 
ATOM   4765 O  O   . HIS   D 1 22  ? 45.465  -39.857 -53.512  1.00 17.67 ? 115 HIS   D O   1 
ATOM   4766 C  CB  . HIS   D 1 22  ? 45.686  -38.748 -50.936  1.00 17.83 ? 115 HIS   D CB  1 
ATOM   4767 C  CG  . HIS   D 1 22  ? 45.424  -38.320 -49.537  1.00 17.44 ? 115 HIS   D CG  1 
ATOM   4768 N  ND1 . HIS   D 1 22  ? 45.424  -39.206 -48.482  1.00 17.29 ? 115 HIS   D ND1 1 
ATOM   4769 C  CD2 . HIS   D 1 22  ? 45.081  -37.119 -49.030  1.00 17.39 ? 115 HIS   D CD2 1 
ATOM   4770 C  CE1 . HIS   D 1 22  ? 45.126  -38.558 -47.376  1.00 17.49 ? 115 HIS   D CE1 1 
ATOM   4771 N  NE2 . HIS   D 1 22  ? 44.918  -37.275 -47.683  1.00 17.68 ? 115 HIS   D NE2 1 
ATOM   4772 N  N   . SER   D 1 23  ? 43.773  -38.457 -54.166  1.00 18.05 ? 116 SER   D N   1 
ATOM   4773 C  CA  . SER   D 1 23  ? 43.467  -39.023 -55.505  1.00 18.07 ? 116 SER   D CA  1 
ATOM   4774 C  C   . SER   D 1 23  ? 44.500  -38.596 -56.555  1.00 17.90 ? 116 SER   D C   1 
ATOM   4775 O  O   . SER   D 1 23  ? 44.586  -39.289 -57.585  1.00 17.42 ? 116 SER   D O   1 
ATOM   4776 C  CB  . SER   D 1 23  ? 42.081  -38.633 -55.931  1.00 18.88 ? 116 SER   D CB  1 
ATOM   4777 O  OG  . SER   D 1 23  ? 41.117  -39.173 -55.040  1.00 19.97 ? 116 SER   D OG  1 
ATOM   4778 N  N   . GLY   D 1 24  ? 45.225  -37.494 -56.323  1.00 17.54 ? 117 GLY   D N   1 
ATOM   4779 C  CA  . GLY   D 1 24  ? 46.131  -36.883 -57.315  1.00 17.73 ? 117 GLY   D CA  1 
ATOM   4780 C  C   . GLY   D 1 24  ? 45.350  -36.248 -58.457  1.00 17.64 ? 117 GLY   D C   1 
ATOM   4781 O  O   . GLY   D 1 24  ? 44.126  -36.079 -58.311  1.00 17.55 ? 117 GLY   D O   1 
ATOM   4782 N  N   . THR   D 1 25  ? 46.019  -35.916 -59.565  1.00 17.64 ? 118 THR   D N   1 
ATOM   4783 C  CA  . THR   D 1 25  ? 45.468  -35.052 -60.647  1.00 17.97 ? 118 THR   D CA  1 
ATOM   4784 C  C   . THR   D 1 25  ? 45.671  -35.695 -62.027  1.00 19.07 ? 118 THR   D C   1 
ATOM   4785 O  O   . THR   D 1 25  ? 45.656  -34.943 -63.014  1.00 18.60 ? 118 THR   D O   1 
ATOM   4786 C  CB  . THR   D 1 25  ? 46.069  -33.638 -60.582  1.00 17.20 ? 118 THR   D CB  1 
ATOM   4787 O  OG1 . THR   D 1 25  ? 47.490  -33.687 -60.729  1.00 16.47 ? 118 THR   D OG1 1 
ATOM   4788 C  CG2 . THR   D 1 25  ? 45.737  -32.921 -59.291  1.00 17.18 ? 118 THR   D CG2 1 
ATOM   4789 N  N   . ALA   D 1 26  ? 45.810  -37.024 -62.115  1.00 20.61 ? 119 ALA   D N   1 
ATOM   4790 C  CA  . ALA   D 1 26  ? 45.869  -37.755 -63.407  1.00 22.41 ? 119 ALA   D CA  1 
ATOM   4791 C  C   . ALA   D 1 26  ? 44.571  -37.481 -64.173  1.00 24.40 ? 119 ALA   D C   1 
ATOM   4792 O  O   . ALA   D 1 26  ? 43.544  -37.226 -63.517  1.00 25.08 ? 119 ALA   D O   1 
ATOM   4793 C  CB  . ALA   D 1 26  ? 46.092  -39.234 -63.187  1.00 21.98 ? 119 ALA   D CB  1 
ATOM   4794 N  N   . LYS   D 1 27  ? 44.607  -37.511 -65.508  1.00 27.11 ? 120 LYS   D N   1 
ATOM   4795 C  CA  . LYS   D 1 27  ? 43.461  -37.075 -66.354  1.00 29.32 ? 120 LYS   D CA  1 
ATOM   4796 C  C   . LYS   D 1 27  ? 42.259  -37.994 -66.095  1.00 29.21 ? 120 LYS   D C   1 
ATOM   4797 O  O   . LYS   D 1 27  ? 41.117  -37.517 -66.234  1.00 32.06 ? 120 LYS   D O   1 
ATOM   4798 C  CB  . LYS   D 1 27  ? 43.847  -37.021 -67.837  1.00 31.82 ? 120 LYS   D CB  1 
ATOM   4799 C  CG  . LYS   D 1 27  ? 42.984  -36.084 -68.682  1.00 34.01 ? 120 LYS   D CG  1 
ATOM   4800 C  CD  . LYS   D 1 27  ? 43.747  -35.271 -69.720  1.00 35.96 ? 120 LYS   D CD  1 
ATOM   4801 C  CE  . LYS   D 1 27  ? 43.210  -33.861 -69.867  1.00 37.58 ? 120 LYS   D CE  1 
ATOM   4802 N  NZ  . LYS   D 1 27  ? 43.790  -33.147 -71.030  1.00 39.47 ? 120 LYS   D NZ  1 
ATOM   4803 N  N   . SER   D 1 28  ? 42.501  -39.242 -65.681  1.00 28.25 ? 121 SER   D N   1 
ATOM   4804 C  CA  . SER   D 1 28  ? 41.451  -40.256 -65.393  1.00 28.35 ? 121 SER   D CA  1 
ATOM   4805 C  C   . SER   D 1 28  ? 40.648  -39.931 -64.119  1.00 27.08 ? 121 SER   D C   1 
ATOM   4806 O  O   . SER   D 1 28  ? 39.531  -40.472 -63.973  1.00 27.02 ? 121 SER   D O   1 
ATOM   4807 C  CB  . SER   D 1 28  ? 42.050  -41.634 -65.312  1.00 29.49 ? 121 SER   D CB  1 
ATOM   4808 O  OG  . SER   D 1 28  ? 42.967  -41.732 -64.231  1.00 31.27 ? 121 SER   D OG  1 
ATOM   4809 N  N   A VAL   D 1 29  ? 41.186  -39.096 -63.219  0.50 26.31 ? 122 VAL   D N   1 
ATOM   4810 N  N   B VAL   D 1 29  ? 41.178  -39.076 -63.237  0.50 26.41 ? 122 VAL   D N   1 
ATOM   4811 C  CA  A VAL   D 1 29  ? 40.557  -38.819 -61.892  0.50 25.69 ? 122 VAL   D CA  1 
ATOM   4812 C  CA  B VAL   D 1 29  ? 40.575  -38.784 -61.901  0.50 25.83 ? 122 VAL   D CA  1 
ATOM   4813 C  C   A VAL   D 1 29  ? 39.246  -38.060 -62.116  0.50 25.84 ? 122 VAL   D C   1 
ATOM   4814 C  C   B VAL   D 1 29  ? 39.251  -38.033 -62.096  0.50 25.93 ? 122 VAL   D C   1 
ATOM   4815 O  O   A VAL   D 1 29  ? 39.238  -37.077 -62.885  0.50 25.95 ? 122 VAL   D O   1 
ATOM   4816 O  O   B VAL   D 1 29  ? 39.236  -37.023 -62.829  0.50 26.05 ? 122 VAL   D O   1 
ATOM   4817 C  CB  A VAL   D 1 29  ? 41.481  -38.058 -60.922  0.50 25.29 ? 122 VAL   D CB  1 
ATOM   4818 C  CB  B VAL   D 1 29  ? 41.547  -38.008 -60.994  0.50 25.53 ? 122 VAL   D CB  1 
ATOM   4819 C  CG1 A VAL   D 1 29  ? 42.817  -38.760 -60.747  0.50 25.33 ? 122 VAL   D CG1 1 
ATOM   4820 C  CG1 B VAL   D 1 29  ? 40.907  -37.643 -59.666  0.50 25.18 ? 122 VAL   D CG1 1 
ATOM   4821 C  CG2 A VAL   D 1 29  ? 41.668  -36.605 -61.333  0.50 24.84 ? 122 VAL   D CG2 1 
ATOM   4822 C  CG2 B VAL   D 1 29  ? 42.831  -38.785 -60.761  0.50 25.61 ? 122 VAL   D CG2 1 
ATOM   4823 N  N   . THR   D 1 30  ? 38.193  -38.524 -61.445  1.00 25.04 ? 123 THR   D N   1 
ATOM   4824 C  CA  . THR   D 1 30  ? 36.792  -38.048 -61.575  1.00 25.92 ? 123 THR   D CA  1 
ATOM   4825 C  C   . THR   D 1 30  ? 36.528  -36.961 -60.525  1.00 24.09 ? 123 THR   D C   1 
ATOM   4826 O  O   . THR   D 1 30  ? 35.659  -36.096 -60.753  1.00 24.12 ? 123 THR   D O   1 
ATOM   4827 C  CB  . THR   D 1 30  ? 35.880  -39.275 -61.440  1.00 27.17 ? 123 THR   D CB  1 
ATOM   4828 O  OG1 . THR   D 1 30  ? 35.540  -39.691 -62.763  1.00 30.81 ? 123 THR   D OG1 1 
ATOM   4829 C  CG2 . THR   D 1 30  ? 34.635  -39.021 -60.626  1.00 28.61 ? 123 THR   D CG2 1 
ATOM   4830 N  N   . CYS   D 1 31  ? 37.248  -37.043 -59.405  1.00 22.15 ? 124 CYS   D N   1 
ATOM   4831 C  CA  . CYS   D 1 31  ? 37.112  -36.195 -58.197  1.00 21.64 ? 124 CYS   D CA  1 
ATOM   4832 C  C   . CYS   D 1 31  ? 38.497  -36.086 -57.553  1.00 20.48 ? 124 CYS   D C   1 
ATOM   4833 O  O   . CYS   D 1 31  ? 39.086  -37.150 -57.261  1.00 19.51 ? 124 CYS   D O   1 
ATOM   4834 C  CB  . CYS   D 1 31  ? 36.116  -36.818 -57.224  1.00 21.76 ? 124 CYS   D CB  1 
ATOM   4835 S  SG  . CYS   D 1 31  ? 35.953  -35.926 -55.656  1.00 23.96 ? 124 CYS   D SG  1 
ATOM   4836 N  N   . THR   D 1 32  ? 39.012  -34.866 -57.390  1.00 18.79 ? 125 THR   D N   1 
ATOM   4837 C  CA  . THR   D 1 32  ? 40.311  -34.596 -56.720  1.00 18.82 ? 125 THR   D CA  1 
ATOM   4838 C  C   . THR   D 1 32  ? 40.147  -33.384 -55.802  1.00 18.77 ? 125 THR   D C   1 
ATOM   4839 O  O   . THR   D 1 32  ? 39.570  -32.373 -56.237  1.00 18.99 ? 125 THR   D O   1 
ATOM   4840 C  CB  . THR   D 1 32  ? 41.451  -34.424 -57.732  1.00 18.40 ? 125 THR   D CB  1 
ATOM   4841 O  OG1 . THR   D 1 32  ? 42.670  -34.373 -56.989  1.00 18.32 ? 125 THR   D OG1 1 
ATOM   4842 C  CG2 . THR   D 1 32  ? 41.319  -33.190 -58.600  1.00 18.26 ? 125 THR   D CG2 1 
ATOM   4843 N  N   . TYR   D 1 33  ? 40.632  -33.502 -54.570  1.00 18.61 ? 126 TYR   D N   1 
ATOM   4844 C  CA  . TYR   D 1 33  ? 40.532  -32.456 -53.527  1.00 18.26 ? 126 TYR   D CA  1 
ATOM   4845 C  C   . TYR   D 1 33  ? 41.898  -31.794 -53.338  1.00 18.02 ? 126 TYR   D C   1 
ATOM   4846 O  O   . TYR   D 1 33  ? 42.909  -32.510 -53.214  1.00 17.44 ? 126 TYR   D O   1 
ATOM   4847 C  CB  . TYR   D 1 33  ? 39.994  -33.068 -52.235  1.00 18.49 ? 126 TYR   D CB  1 
ATOM   4848 C  CG  . TYR   D 1 33  ? 40.099  -32.157 -51.044  1.00 18.13 ? 126 TYR   D CG  1 
ATOM   4849 C  CD1 . TYR   D 1 33  ? 39.159  -31.165 -50.828  1.00 17.90 ? 126 TYR   D CD1 1 
ATOM   4850 C  CD2 . TYR   D 1 33  ? 41.153  -32.271 -50.151  1.00 17.76 ? 126 TYR   D CD2 1 
ATOM   4851 C  CE1 . TYR   D 1 33  ? 39.248  -30.318 -49.738  1.00 18.43 ? 126 TYR   D CE1 1 
ATOM   4852 C  CE2 . TYR   D 1 33  ? 41.251  -31.438 -49.051  1.00 18.07 ? 126 TYR   D CE2 1 
ATOM   4853 C  CZ  . TYR   D 1 33  ? 40.293  -30.461 -48.844  1.00 18.02 ? 126 TYR   D CZ  1 
ATOM   4854 O  OH  . TYR   D 1 33  ? 40.375  -29.627 -47.774  1.00 18.01 ? 126 TYR   D OH  1 
ATOM   4855 N  N   . SER   D 1 34  ? 41.910  -30.460 -53.310  1.00 17.84 ? 127 SER   D N   1 
ATOM   4856 C  CA  . SER   D 1 34  ? 43.098  -29.611 -53.041  1.00 17.91 ? 127 SER   D CA  1 
ATOM   4857 C  C   . SER   D 1 34  ? 43.112  -29.181 -51.576  1.00 18.55 ? 127 SER   D C   1 
ATOM   4858 O  O   . SER   D 1 34  ? 42.350  -28.292 -51.194  1.00 17.98 ? 127 SER   D O   1 
ATOM   4859 C  CB  . SER   D 1 34  ? 43.102  -28.411 -53.940  1.00 18.20 ? 127 SER   D CB  1 
ATOM   4860 O  OG  . SER   D 1 34  ? 44.075  -27.470 -53.515  1.00 18.14 ? 127 SER   D OG  1 
ATOM   4861 N  N   . PRO   D 1 35  ? 43.971  -29.785 -50.719  1.00 18.65 ? 128 PRO   D N   1 
ATOM   4862 C  CA  . PRO   D 1 35  ? 44.154  -29.311 -49.347  1.00 19.45 ? 128 PRO   D CA  1 
ATOM   4863 C  C   . PRO   D 1 35  ? 44.500  -27.816 -49.253  1.00 19.43 ? 128 PRO   D C   1 
ATOM   4864 O  O   . PRO   D 1 35  ? 44.020  -27.171 -48.345  1.00 19.98 ? 128 PRO   D O   1 
ATOM   4865 C  CB  . PRO   D 1 35  ? 45.348  -30.123 -48.809  1.00 19.59 ? 128 PRO   D CB  1 
ATOM   4866 C  CG  . PRO   D 1 35  ? 45.434  -31.350 -49.701  1.00 19.44 ? 128 PRO   D CG  1 
ATOM   4867 C  CD  . PRO   D 1 35  ? 44.797  -30.965 -51.019  1.00 19.27 ? 128 PRO   D CD  1 
ATOM   4868 N  N   . ALA   D 1 36  ? 45.347  -27.312 -50.161  1.00 19.27 ? 129 ALA   D N   1 
ATOM   4869 C  CA  . ALA   D 1 36  ? 45.834  -25.911 -50.163  1.00 19.22 ? 129 ALA   D CA  1 
ATOM   4870 C  C   . ALA   D 1 36  ? 44.652  -24.950 -50.349  1.00 19.50 ? 129 ALA   D C   1 
ATOM   4871 O  O   . ALA   D 1 36  ? 44.657  -23.886 -49.709  1.00 19.78 ? 129 ALA   D O   1 
ATOM   4872 C  CB  . ALA   D 1 36  ? 46.892  -25.713 -51.222  1.00 18.82 ? 129 ALA   D CB  1 
ATOM   4873 N  N   . LEU   D 1 37  ? 43.669  -25.330 -51.170  1.00 19.36 ? 130 LEU   D N   1 
ATOM   4874 C  CA  . LEU   D 1 37  ? 42.506  -24.478 -51.537  1.00 19.14 ? 130 LEU   D CA  1 
ATOM   4875 C  C   . LEU   D 1 37  ? 41.261  -24.869 -50.731  1.00 19.04 ? 130 LEU   D C   1 
ATOM   4876 O  O   . LEU   D 1 37  ? 40.281  -24.110 -50.797  1.00 19.54 ? 130 LEU   D O   1 
ATOM   4877 C  CB  . LEU   D 1 37  ? 42.248  -24.637 -53.037  1.00 19.10 ? 130 LEU   D CB  1 
ATOM   4878 C  CG  . LEU   D 1 37  ? 43.372  -24.153 -53.950  1.00 19.13 ? 130 LEU   D CG  1 
ATOM   4879 C  CD1 . LEU   D 1 37  ? 43.103  -24.543 -55.396  1.00 19.16 ? 130 LEU   D CD1 1 
ATOM   4880 C  CD2 . LEU   D 1 37  ? 43.563  -22.649 -53.825  1.00 19.71 ? 130 LEU   D CD2 1 
ATOM   4881 N  N   . ASN   D 1 38  ? 41.289  -26.003 -50.019  1.00 18.74 ? 131 ASN   D N   1 
ATOM   4882 C  CA  . ASN   D 1 38  ? 40.089  -26.647 -49.412  1.00 18.76 ? 131 ASN   D CA  1 
ATOM   4883 C  C   . ASN   D 1 38  ? 38.987  -26.704 -50.473  1.00 18.15 ? 131 ASN   D C   1 
ATOM   4884 O  O   . ASN   D 1 38  ? 37.866  -26.209 -50.212  1.00 18.00 ? 131 ASN   D O   1 
ATOM   4885 C  CB  . ASN   D 1 38  ? 39.601  -25.925 -48.153  1.00 18.90 ? 131 ASN   D CB  1 
ATOM   4886 C  CG  . ASN   D 1 38  ? 38.457  -26.646 -47.468  1.00 19.45 ? 131 ASN   D CG  1 
ATOM   4887 O  OD1 . ASN   D 1 38  ? 38.383  -27.874 -47.497  1.00 19.56 ? 131 ASN   D OD1 1 
ATOM   4888 N  ND2 . ASN   D 1 38  ? 37.560  -25.899 -46.845  1.00 20.01 ? 131 ASN   D ND2 1 
ATOM   4889 N  N   . LYS   D 1 39  ? 39.313  -27.253 -51.643  1.00 18.31 ? 132 LYS   D N   1 
ATOM   4890 C  CA  . LYS   D 1 39  ? 38.453  -27.178 -52.852  1.00 18.10 ? 132 LYS   D CA  1 
ATOM   4891 C  C   . LYS   D 1 39  ? 38.420  -28.536 -53.550  1.00 17.73 ? 132 LYS   D C   1 
ATOM   4892 O  O   . LYS   D 1 39  ? 39.501  -29.104 -53.814  1.00 16.96 ? 132 LYS   D O   1 
ATOM   4893 C  CB  . LYS   D 1 39  ? 38.947  -26.079 -53.797  1.00 18.75 ? 132 LYS   D CB  1 
ATOM   4894 C  CG  . LYS   D 1 39  ? 38.054  -25.808 -55.002  1.00 19.34 ? 132 LYS   D CG  1 
ATOM   4895 C  CD  . LYS   D 1 39  ? 38.413  -24.514 -55.717  1.00 19.73 ? 132 LYS   D CD  1 
ATOM   4896 C  CE  . LYS   D 1 39  ? 37.514  -24.201 -56.893  1.00 20.31 ? 132 LYS   D CE  1 
ATOM   4897 N  NZ  . LYS   D 1 39  ? 37.726  -22.816 -57.380  1.00 21.04 ? 132 LYS   D NZ  1 
ATOM   4898 N  N   . MET   D 1 40  ? 37.211  -29.023 -53.829  1.00 17.68 ? 133 MET   D N   1 
ATOM   4899 C  CA  . MET   D 1 40  ? 36.962  -30.272 -54.588  1.00 18.23 ? 133 MET   D CA  1 
ATOM   4900 C  C   . MET   D 1 40  ? 36.762  -29.908 -56.061  1.00 18.10 ? 133 MET   D C   1 
ATOM   4901 O  O   . MET   D 1 40  ? 35.971  -28.987 -56.350  1.00 17.97 ? 133 MET   D O   1 
ATOM   4902 C  CB  . MET   D 1 40  ? 35.730  -31.019 -54.072  1.00 18.89 ? 133 MET   D CB  1 
ATOM   4903 C  CG  . MET   D 1 40  ? 35.350  -32.190 -54.953  1.00 20.23 ? 133 MET   D CG  1 
ATOM   4904 S  SD  . MET   D 1 40  ? 33.812  -32.963 -54.453  1.00 23.54 ? 133 MET   D SD  1 
ATOM   4905 C  CE  . MET   D 1 40  ? 34.373  -33.864 -53.010  1.00 24.05 ? 133 MET   D CE  1 
ATOM   4906 N  N   . PHE   D 1 41  ? 37.503  -30.576 -56.942  1.00 18.12 ? 134 PHE   D N   1 
ATOM   4907 C  CA  . PHE   D 1 41  ? 37.363  -30.505 -58.416  1.00 18.12 ? 134 PHE   D CA  1 
ATOM   4908 C  C   . PHE   D 1 41  ? 36.760  -31.835 -58.867  1.00 18.09 ? 134 PHE   D C   1 
ATOM   4909 O  O   . PHE   D 1 41  ? 37.334  -32.890 -58.552  1.00 17.32 ? 134 PHE   D O   1 
ATOM   4910 C  CB  . PHE   D 1 41  ? 38.721  -30.213 -59.059  1.00 18.59 ? 134 PHE   D CB  1 
ATOM   4911 C  CG  . PHE   D 1 41  ? 39.321  -28.887 -58.664  1.00 18.09 ? 134 PHE   D CG  1 
ATOM   4912 C  CD1 . PHE   D 1 41  ? 39.974  -28.738 -57.450  1.00 18.38 ? 134 PHE   D CD1 1 
ATOM   4913 C  CD2 . PHE   D 1 41  ? 39.229  -27.788 -59.504  1.00 18.40 ? 134 PHE   D CD2 1 
ATOM   4914 C  CE1 . PHE   D 1 41  ? 40.527  -27.520 -57.084  1.00 18.06 ? 134 PHE   D CE1 1 
ATOM   4915 C  CE2 . PHE   D 1 41  ? 39.780  -26.570 -59.137  1.00 18.28 ? 134 PHE   D CE2 1 
ATOM   4916 C  CZ  . PHE   D 1 41  ? 40.430  -26.439 -57.930  1.00 18.18 ? 134 PHE   D CZ  1 
ATOM   4917 N  N   . CYS   D 1 42  ? 35.611  -31.805 -59.540  1.00 18.79 ? 135 CYS   D N   1 
ATOM   4918 C  CA  . CYS   D 1 42  ? 34.883  -33.043 -59.915  1.00 18.99 ? 135 CYS   D CA  1 
ATOM   4919 C  C   . CYS   D 1 42  ? 34.149  -32.871 -61.245  1.00 19.25 ? 135 CYS   D C   1 
ATOM   4920 O  O   . CYS   D 1 42  ? 33.808  -31.738 -61.598  1.00 18.70 ? 135 CYS   D O   1 
ATOM   4921 C  CB  . CYS   D 1 42  ? 33.903  -33.445 -58.823  1.00 19.28 ? 135 CYS   D CB  1 
ATOM   4922 S  SG  . CYS   D 1 42  ? 32.631  -32.199 -58.512  1.00 19.47 ? 135 CYS   D SG  1 
ATOM   4923 N  N   . GLN   D 1 43  ? 33.942  -33.985 -61.944  1.00 20.63 ? 136 GLN   D N   1 
ATOM   4924 C  CA  . GLN   D 1 43  ? 33.190  -34.052 -63.220  1.00 21.42 ? 136 GLN   D CA  1 
ATOM   4925 C  C   . GLN   D 1 43  ? 31.696  -34.165 -62.917  1.00 21.56 ? 136 GLN   D C   1 
ATOM   4926 O  O   . GLN   D 1 43  ? 31.331  -34.784 -61.899  1.00 21.11 ? 136 GLN   D O   1 
ATOM   4927 C  CB  . GLN   D 1 43  ? 33.654  -35.237 -64.066  1.00 23.17 ? 136 GLN   D CB  1 
ATOM   4928 C  CG  . GLN   D 1 43  ? 34.989  -35.000 -64.751  1.00 24.95 ? 136 GLN   D CG  1 
ATOM   4929 C  CD  . GLN   D 1 43  ? 35.408  -36.170 -65.607  1.00 26.62 ? 136 GLN   D CD  1 
ATOM   4930 O  OE1 . GLN   D 1 43  ? 34.728  -37.189 -65.681  1.00 27.73 ? 136 GLN   D OE1 1 
ATOM   4931 N  NE2 . GLN   D 1 43  ? 36.543  -36.025 -66.272  1.00 29.14 ? 136 GLN   D NE2 1 
ATOM   4932 N  N   . LEU   D 1 44  ? 30.887  -33.560 -63.787  1.00 21.78 ? 137 LEU   D N   1 
ATOM   4933 C  CA  . LEU   D 1 44  ? 29.407  -33.652 -63.819  1.00 22.45 ? 137 LEU   D CA  1 
ATOM   4934 C  C   . LEU   D 1 44  ? 28.988  -35.120 -63.654  1.00 21.74 ? 137 LEU   D C   1 
ATOM   4935 O  O   . LEU   D 1 44  ? 29.484  -35.967 -64.420  1.00 20.11 ? 137 LEU   D O   1 
ATOM   4936 C  CB  . LEU   D 1 44  ? 28.956  -33.070 -65.166  1.00 24.21 ? 137 LEU   D CB  1 
ATOM   4937 C  CG  . LEU   D 1 44  ? 27.455  -33.046 -65.440  1.00 25.57 ? 137 LEU   D CG  1 
ATOM   4938 C  CD1 . LEU   D 1 44  ? 26.772  -31.992 -64.591  1.00 25.23 ? 137 LEU   D CD1 1 
ATOM   4939 C  CD2 . LEU   D 1 44  ? 27.190  -32.786 -66.918  1.00 26.30 ? 137 LEU   D CD2 1 
ATOM   4940 N  N   . ALA   D 1 45  ? 28.156  -35.405 -62.648  1.00 21.92 ? 138 ALA   D N   1 
ATOM   4941 C  CA  . ALA   D 1 45  ? 27.404  -36.671 -62.457  1.00 22.79 ? 138 ALA   D CA  1 
ATOM   4942 C  C   . ALA   D 1 45  ? 28.328  -37.833 -62.070  1.00 23.30 ? 138 ALA   D C   1 
ATOM   4943 O  O   . ALA   D 1 45  ? 27.842  -38.974 -62.075  1.00 25.93 ? 138 ALA   D O   1 
ATOM   4944 C  CB  . ALA   D 1 45  ? 26.610  -36.999 -63.703  1.00 22.80 ? 138 ALA   D CB  1 
ATOM   4945 N  N   . LYS   D 1 46  ? 29.582  -37.572 -61.699  1.00 23.29 ? 139 LYS   D N   1 
ATOM   4946 C  CA  . LYS   D 1 46  ? 30.550  -38.640 -61.333  1.00 23.14 ? 139 LYS   D CA  1 
ATOM   4947 C  C   . LYS   D 1 46  ? 30.696  -38.723 -59.806  1.00 22.28 ? 139 LYS   D C   1 
ATOM   4948 O  O   . LYS   D 1 46  ? 30.370  -37.734 -59.114  1.00 21.09 ? 139 LYS   D O   1 
ATOM   4949 C  CB  . LYS   D 1 46  ? 31.890  -38.396 -62.030  1.00 23.97 ? 139 LYS   D CB  1 
ATOM   4950 C  CG  . LYS   D 1 46  ? 31.850  -38.476 -63.548  1.00 25.23 ? 139 LYS   D CG  1 
ATOM   4951 C  CD  . LYS   D 1 46  ? 31.618  -39.883 -64.070  1.00 25.94 ? 139 LYS   D CD  1 
ATOM   4952 C  CE  . LYS   D 1 46  ? 31.557  -39.951 -65.583  1.00 27.25 ? 139 LYS   D CE  1 
ATOM   4953 N  NZ  . LYS   D 1 46  ? 32.671  -39.196 -66.202  1.00 28.61 ? 139 LYS   D NZ  1 
ATOM   4954 N  N   . THR   D 1 47  ? 31.167  -39.877 -59.316  1.00 21.73 ? 140 THR   D N   1 
ATOM   4955 C  CA  . THR   D 1 47  ? 31.307  -40.226 -57.876  1.00 21.36 ? 140 THR   D CA  1 
ATOM   4956 C  C   . THR   D 1 47  ? 32.273  -39.248 -57.198  1.00 21.13 ? 140 THR   D C   1 
ATOM   4957 O  O   . THR   D 1 47  ? 33.425  -39.135 -57.658  1.00 21.49 ? 140 THR   D O   1 
ATOM   4958 C  CB  . THR   D 1 47  ? 31.783  -41.674 -57.692  1.00 21.35 ? 140 THR   D CB  1 
ATOM   4959 O  OG1 . THR   D 1 47  ? 30.930  -42.544 -58.437  1.00 20.90 ? 140 THR   D OG1 1 
ATOM   4960 C  CG2 . THR   D 1 47  ? 31.791  -42.112 -56.245  1.00 21.65 ? 140 THR   D CG2 1 
ATOM   4961 N  N   . CYS   D 1 48  ? 31.813  -38.574 -56.142  1.00 20.36 ? 141 CYS   D N   1 
ATOM   4962 C  CA  . CYS   D 1 48  ? 32.618  -37.677 -55.275  1.00 20.49 ? 141 CYS   D CA  1 
ATOM   4963 C  C   . CYS   D 1 48  ? 32.630  -38.241 -53.861  1.00 20.01 ? 141 CYS   D C   1 
ATOM   4964 O  O   . CYS   D 1 48  ? 31.703  -37.983 -53.097  1.00 19.91 ? 141 CYS   D O   1 
ATOM   4965 C  CB  . CYS   D 1 48  ? 32.042  -36.269 -55.245  1.00 21.15 ? 141 CYS   D CB  1 
ATOM   4966 S  SG  . CYS   D 1 48  ? 32.069  -35.461 -56.860  1.00 21.62 ? 141 CYS   D SG  1 
ATOM   4967 N  N   . PRO   D 1 49  ? 33.635  -39.069 -53.494  1.00 19.93 ? 142 PRO   D N   1 
ATOM   4968 C  CA  . PRO   D 1 49  ? 33.733  -39.602 -52.139  1.00 20.19 ? 142 PRO   D CA  1 
ATOM   4969 C  C   . PRO   D 1 49  ? 34.089  -38.491 -51.141  1.00 20.34 ? 142 PRO   D C   1 
ATOM   4970 O  O   . PRO   D 1 49  ? 35.088  -37.829 -51.338  1.00 20.19 ? 142 PRO   D O   1 
ATOM   4971 C  CB  . PRO   D 1 49  ? 34.853  -40.653 -52.208  1.00 20.22 ? 142 PRO   D CB  1 
ATOM   4972 C  CG  . PRO   D 1 49  ? 35.090  -40.875 -53.690  1.00 20.39 ? 142 PRO   D CG  1 
ATOM   4973 C  CD  . PRO   D 1 49  ? 34.713  -39.570 -54.361  1.00 20.12 ? 142 PRO   D CD  1 
ATOM   4974 N  N   . VAL   D 1 50  ? 33.248  -38.320 -50.118  1.00 20.22 ? 143 VAL   D N   1 
ATOM   4975 C  CA  . VAL   D 1 50  ? 33.459  -37.392 -48.968  1.00 20.07 ? 143 VAL   D CA  1 
ATOM   4976 C  C   . VAL   D 1 50  ? 33.466  -38.258 -47.707  1.00 20.41 ? 143 VAL   D C   1 
ATOM   4977 O  O   . VAL   D 1 50  ? 32.500  -39.021 -47.514  1.00 20.13 ? 143 VAL   D O   1 
ATOM   4978 C  CB  . VAL   D 1 50  ? 32.374  -36.295 -48.906  1.00 19.92 ? 143 VAL   D CB  1 
ATOM   4979 C  CG1 . VAL   D 1 50  ? 32.502  -35.424 -47.664  1.00 20.16 ? 143 VAL   D CG1 1 
ATOM   4980 C  CG2 . VAL   D 1 50  ? 32.377  -35.424 -50.150  1.00 20.18 ? 143 VAL   D CG2 1 
ATOM   4981 N  N   . GLN   D 1 51  ? 34.535  -38.172 -46.914  1.00 20.51 ? 144 GLN   D N   1 
ATOM   4982 C  CA  . GLN   D 1 51  ? 34.721  -38.976 -45.680  1.00 20.71 ? 144 GLN   D CA  1 
ATOM   4983 C  C   . GLN   D 1 51  ? 34.236  -38.166 -44.475  1.00 20.35 ? 144 GLN   D C   1 
ATOM   4984 O  O   . GLN   D 1 51  ? 34.509  -36.951 -44.423  1.00 20.08 ? 144 GLN   D O   1 
ATOM   4985 C  CB  . GLN   D 1 51  ? 36.188  -39.374 -45.501  1.00 20.62 ? 144 GLN   D CB  1 
ATOM   4986 C  CG  . GLN   D 1 51  ? 36.775  -40.099 -46.699  1.00 20.82 ? 144 GLN   D CG  1 
ATOM   4987 C  CD  . GLN   D 1 51  ? 38.272  -40.250 -46.587  1.00 20.89 ? 144 GLN   D CD  1 
ATOM   4988 O  OE1 . GLN   D 1 51  ? 38.935  -39.554 -45.819  1.00 19.54 ? 144 GLN   D OE1 1 
ATOM   4989 N  NE2 . GLN   D 1 51  ? 38.817  -41.173 -47.360  1.00 21.97 ? 144 GLN   D NE2 1 
ATOM   4990 N  N   . LEU   D 1 52  ? 33.531  -38.827 -43.555  1.00 21.17 ? 145 LEU   D N   1 
ATOM   4991 C  CA  . LEU   D 1 52  ? 33.132  -38.280 -42.233  1.00 21.12 ? 145 LEU   D CA  1 
ATOM   4992 C  C   . LEU   D 1 52  ? 34.049  -38.887 -41.168  1.00 21.94 ? 145 LEU   D C   1 
ATOM   4993 O  O   . LEU   D 1 52  ? 34.028  -40.125 -41.013  1.00 22.52 ? 145 LEU   D O   1 
ATOM   4994 C  CB  . LEU   D 1 52  ? 31.666  -38.638 -41.960  1.00 20.73 ? 145 LEU   D CB  1 
ATOM   4995 C  CG  . LEU   D 1 52  ? 30.680  -38.368 -43.098  1.00 20.08 ? 145 LEU   D CG  1 
ATOM   4996 C  CD1 . LEU   D 1 52  ? 29.257  -38.618 -42.636  1.00 20.25 ? 145 LEU   D CD1 1 
ATOM   4997 C  CD2 . LEU   D 1 52  ? 30.816  -36.949 -43.629  1.00 19.56 ? 145 LEU   D CD2 1 
ATOM   4998 N  N   . TRP   D 1 53  ? 34.832  -38.051 -40.486  1.00 23.85 ? 146 TRP   D N   1 
ATOM   4999 C  CA  . TRP   D 1 53  ? 35.744  -38.453 -39.383  1.00 25.71 ? 146 TRP   D CA  1 
ATOM   5000 C  C   . TRP   D 1 53  ? 35.155  -37.959 -38.060  1.00 25.44 ? 146 TRP   D C   1 
ATOM   5001 O  O   . TRP   D 1 53  ? 34.814  -36.762 -37.981  1.00 24.76 ? 146 TRP   D O   1 
ATOM   5002 C  CB  . TRP   D 1 53  ? 37.155  -37.900 -39.618  1.00 27.22 ? 146 TRP   D CB  1 
ATOM   5003 C  CG  . TRP   D 1 53  ? 37.846  -38.509 -40.798  1.00 29.10 ? 146 TRP   D CG  1 
ATOM   5004 C  CD1 . TRP   D 1 53  ? 37.658  -38.180 -42.109  1.00 30.12 ? 146 TRP   D CD1 1 
ATOM   5005 C  CD2 . TRP   D 1 53  ? 38.835  -39.556 -40.786  1.00 30.65 ? 146 TRP   D CD2 1 
ATOM   5006 N  NE1 . TRP   D 1 53  ? 38.454  -38.951 -42.912  1.00 30.09 ? 146 TRP   D NE1 1 
ATOM   5007 C  CE2 . TRP   D 1 53  ? 39.192  -39.802 -42.131  1.00 31.07 ? 146 TRP   D CE2 1 
ATOM   5008 C  CE3 . TRP   D 1 53  ? 39.455  -40.311 -39.782  1.00 31.59 ? 146 TRP   D CE3 1 
ATOM   5009 C  CZ2 . TRP   D 1 53  ? 40.136  -40.765 -42.493  1.00 31.19 ? 146 TRP   D CZ2 1 
ATOM   5010 C  CZ3 . TRP   D 1 53  ? 40.386  -41.263 -40.140  1.00 31.63 ? 146 TRP   D CZ3 1 
ATOM   5011 C  CH2 . TRP   D 1 53  ? 40.718  -41.488 -41.477  1.00 31.99 ? 146 TRP   D CH2 1 
ATOM   5012 N  N   . VAL   D 1 54  ? 35.031  -38.851 -37.073  1.00 25.74 ? 147 VAL   D N   1 
ATOM   5013 C  CA  . VAL   D 1 54  ? 34.498  -38.522 -35.718  1.00 26.34 ? 147 VAL   D CA  1 
ATOM   5014 C  C   . VAL   D 1 54  ? 35.434  -39.107 -34.657  1.00 26.78 ? 147 VAL   D C   1 
ATOM   5015 O  O   . VAL   D 1 54  ? 35.961  -40.205 -34.887  1.00 26.09 ? 147 VAL   D O   1 
ATOM   5016 C  CB  . VAL   D 1 54  ? 33.049  -39.020 -35.552  1.00 25.28 ? 147 VAL   D CB  1 
ATOM   5017 C  CG1 . VAL   D 1 54  ? 32.103  -38.257 -36.465  1.00 25.54 ? 147 VAL   D CG1 1 
ATOM   5018 C  CG2 . VAL   D 1 54  ? 32.917  -40.520 -35.771  1.00 24.85 ? 147 VAL   D CG2 1 
ATOM   5019 N  N   . ASP   D 1 55  ? 35.627  -38.379 -33.552  1.00 29.18 ? 148 ASP   D N   1 
ATOM   5020 C  CA  . ASP   D 1 55  ? 36.399  -38.823 -32.356  1.00 30.21 ? 148 ASP   D CA  1 
ATOM   5021 C  C   . ASP   D 1 55  ? 35.540  -39.787 -31.529  1.00 31.01 ? 148 ASP   D C   1 
ATOM   5022 O  O   . ASP   D 1 55  ? 36.116  -40.595 -30.781  1.00 31.50 ? 148 ASP   D O   1 
ATOM   5023 C  CB  . ASP   D 1 55  ? 36.843  -37.635 -31.497  1.00 31.54 ? 148 ASP   D CB  1 
ATOM   5024 C  CG  . ASP   D 1 55  ? 37.828  -36.688 -32.166  1.00 33.09 ? 148 ASP   D CG  1 
ATOM   5025 O  OD1 . ASP   D 1 55  ? 38.510  -37.114 -33.122  1.00 35.52 ? 148 ASP   D OD1 1 
ATOM   5026 O  OD2 . ASP   D 1 55  ? 37.904  -35.527 -31.725  1.00 34.01 ? 148 ASP   D OD2 1 
ATOM   5027 N  N   . SER   D 1 56  ? 34.211  -39.704 -31.650  1.00 31.11 ? 149 SER   D N   1 
ATOM   5028 C  CA  . SER   D 1 56  ? 33.246  -40.603 -30.964  1.00 31.49 ? 149 SER   D CA  1 
ATOM   5029 C  C   . SER   D 1 56  ? 32.017  -40.832 -31.851  1.00 33.04 ? 149 SER   D C   1 
ATOM   5030 O  O   . SER   D 1 56  ? 31.605  -39.887 -32.554  1.00 34.18 ? 149 SER   D O   1 
ATOM   5031 C  CB  . SER   D 1 56  ? 32.861  -40.047 -29.622  1.00 31.25 ? 149 SER   D CB  1 
ATOM   5032 O  OG  . SER   D 1 56  ? 32.335  -38.738 -29.756  1.00 30.52 ? 149 SER   D OG  1 
ATOM   5033 N  N   . THR   D 1 57  ? 31.460  -42.045 -31.809  1.00 33.91 ? 150 THR   D N   1 
ATOM   5034 C  CA  . THR   D 1 57  ? 30.320  -42.485 -32.654  1.00 35.42 ? 150 THR   D CA  1 
ATOM   5035 C  C   . THR   D 1 57  ? 29.084  -41.684 -32.256  1.00 34.90 ? 150 THR   D C   1 
ATOM   5036 O  O   . THR   D 1 57  ? 28.725  -41.642 -31.081  1.00 34.24 ? 150 THR   D O   1 
ATOM   5037 C  CB  . THR   D 1 57  ? 30.109  -44.001 -32.548  1.00 36.57 ? 150 THR   D CB  1 
ATOM   5038 O  OG1 . THR   D 1 57  ? 31.372  -44.627 -32.765  1.00 38.45 ? 150 THR   D OG1 1 
ATOM   5039 C  CG2 . THR   D 1 57  ? 29.114  -44.539 -33.552  1.00 37.32 ? 150 THR   D CG2 1 
ATOM   5040 N  N   . PRO   D 1 58  ? 28.433  -40.970 -33.206  1.00 34.48 ? 151 PRO   D N   1 
ATOM   5041 C  CA  . PRO   D 1 58  ? 27.137  -40.347 -32.943  1.00 34.44 ? 151 PRO   D CA  1 
ATOM   5042 C  C   . PRO   D 1 58  ? 26.089  -41.427 -32.696  1.00 32.59 ? 151 PRO   D C   1 
ATOM   5043 O  O   . PRO   D 1 58  ? 26.239  -42.549 -33.174  1.00 31.44 ? 151 PRO   D O   1 
ATOM   5044 C  CB  . PRO   D 1 58  ? 26.823  -39.542 -34.216  1.00 35.61 ? 151 PRO   D CB  1 
ATOM   5045 C  CG  . PRO   D 1 58  ? 28.150  -39.437 -34.948  1.00 36.09 ? 151 PRO   D CG  1 
ATOM   5046 C  CD  . PRO   D 1 58  ? 28.925  -40.678 -34.561  1.00 35.61 ? 151 PRO   D CD  1 
ATOM   5047 N  N   . PRO   D 1 59  ? 24.994  -41.123 -31.964  1.00 32.77 ? 152 PRO   D N   1 
ATOM   5048 C  CA  . PRO   D 1 59  ? 23.995  -42.134 -31.621  1.00 32.55 ? 152 PRO   D CA  1 
ATOM   5049 C  C   . PRO   D 1 59  ? 23.193  -42.598 -32.836  1.00 33.54 ? 152 PRO   D C   1 
ATOM   5050 O  O   . PRO   D 1 59  ? 23.263  -41.988 -33.904  1.00 32.82 ? 152 PRO   D O   1 
ATOM   5051 C  CB  . PRO   D 1 59  ? 23.102  -41.417 -30.597  1.00 32.90 ? 152 PRO   D CB  1 
ATOM   5052 C  CG  . PRO   D 1 59  ? 23.224  -39.950 -30.960  1.00 33.40 ? 152 PRO   D CG  1 
ATOM   5053 C  CD  . PRO   D 1 59  ? 24.649  -39.791 -31.447  1.00 32.85 ? 152 PRO   D CD  1 
ATOM   5054 N  N   . PRO   D 1 60  ? 22.414  -43.697 -32.712  1.00 33.66 ? 153 PRO   D N   1 
ATOM   5055 C  CA  . PRO   D 1 60  ? 21.543  -44.153 -33.796  1.00 33.17 ? 153 PRO   D CA  1 
ATOM   5056 C  C   . PRO   D 1 60  ? 20.561  -43.050 -34.220  1.00 30.96 ? 153 PRO   D C   1 
ATOM   5057 O  O   . PRO   D 1 60  ? 20.112  -42.312 -33.362  1.00 30.76 ? 153 PRO   D O   1 
ATOM   5058 C  CB  . PRO   D 1 60  ? 20.778  -45.345 -33.197  1.00 33.91 ? 153 PRO   D CB  1 
ATOM   5059 C  CG  . PRO   D 1 60  ? 21.634  -45.802 -32.034  1.00 34.58 ? 153 PRO   D CG  1 
ATOM   5060 C  CD  . PRO   D 1 60  ? 22.326  -44.556 -31.522  1.00 34.46 ? 153 PRO   D CD  1 
ATOM   5061 N  N   . GLY   D 1 61  ? 20.271  -42.957 -35.520  1.00 29.00 ? 154 GLY   D N   1 
ATOM   5062 C  CA  . GLY   D 1 61  ? 19.313  -41.988 -36.086  1.00 27.92 ? 154 GLY   D CA  1 
ATOM   5063 C  C   . GLY   D 1 61  ? 19.965  -40.658 -36.431  1.00 26.59 ? 154 GLY   D C   1 
ATOM   5064 O  O   . GLY   D 1 61  ? 19.244  -39.754 -36.885  1.00 26.64 ? 154 GLY   D O   1 
ATOM   5065 N  N   . THR   D 1 62  ? 21.282  -40.531 -36.242  1.00 25.18 ? 155 THR   D N   1 
ATOM   5066 C  CA  . THR   D 1 62  ? 22.070  -39.336 -36.649  1.00 23.10 ? 155 THR   D CA  1 
ATOM   5067 C  C   . THR   D 1 62  ? 22.002  -39.216 -38.175  1.00 21.10 ? 155 THR   D C   1 
ATOM   5068 O  O   . THR   D 1 62  ? 22.002  -40.266 -38.847  1.00 19.18 ? 155 THR   D O   1 
ATOM   5069 C  CB  . THR   D 1 62  ? 23.513  -39.427 -36.136  1.00 23.84 ? 155 THR   D CB  1 
ATOM   5070 O  OG1 . THR   D 1 62  ? 23.440  -39.429 -34.710  1.00 23.75 ? 155 THR   D OG1 1 
ATOM   5071 C  CG2 . THR   D 1 62  ? 24.391  -38.294 -36.622  1.00 23.55 ? 155 THR   D CG2 1 
ATOM   5072 N  N   . ARG   D 1 63  ? 21.943  -37.989 -38.699  1.00 20.02 ? 156 ARG   D N   1 
ATOM   5073 C  CA  . ARG   D 1 63  ? 21.772  -37.738 -40.155  1.00 19.14 ? 156 ARG   D CA  1 
ATOM   5074 C  C   . ARG   D 1 63  ? 22.868  -36.797 -40.668  1.00 18.17 ? 156 ARG   D C   1 
ATOM   5075 O  O   . ARG   D 1 63  ? 23.374  -35.970 -39.899  1.00 17.86 ? 156 ARG   D O   1 
ATOM   5076 C  CB  . ARG   D 1 63  ? 20.360  -37.210 -40.420  1.00 18.93 ? 156 ARG   D CB  1 
ATOM   5077 C  CG  . ARG   D 1 63  ? 19.312  -38.313 -40.488  1.00 19.05 ? 156 ARG   D CG  1 
ATOM   5078 C  CD  . ARG   D 1 63  ? 17.981  -37.898 -39.897  1.00 18.61 ? 156 ARG   D CD  1 
ATOM   5079 N  NE  . ARG   D 1 63  ? 17.378  -36.753 -40.565  1.00 18.73 ? 156 ARG   D NE  1 
ATOM   5080 C  CZ  . ARG   D 1 63  ? 16.657  -36.805 -41.685  1.00 18.74 ? 156 ARG   D CZ  1 
ATOM   5081 N  NH1 . ARG   D 1 63  ? 16.453  -37.954 -42.309  1.00 18.60 ? 156 ARG   D NH1 1 
ATOM   5082 N  NH2 . ARG   D 1 63  ? 16.149  -35.694 -42.183  1.00 18.83 ? 156 ARG   D NH2 1 
ATOM   5083 N  N   . VAL   D 1 64  ? 23.213  -36.943 -41.945  1.00 17.14 ? 157 VAL   D N   1 
ATOM   5084 C  CA  . VAL   D 1 64  ? 24.285  -36.166 -42.627  1.00 16.60 ? 157 VAL   D CA  1 
ATOM   5085 C  C   . VAL   D 1 64  ? 23.635  -35.434 -43.798  1.00 16.23 ? 157 VAL   D C   1 
ATOM   5086 O  O   . VAL   D 1 64  ? 23.120  -36.123 -44.694  1.00 15.53 ? 157 VAL   D O   1 
ATOM   5087 C  CB  . VAL   D 1 64  ? 25.429  -37.074 -43.104  1.00 16.71 ? 157 VAL   D CB  1 
ATOM   5088 C  CG1 . VAL   D 1 64  ? 26.612  -36.251 -43.593  1.00 16.62 ? 157 VAL   D CG1 1 
ATOM   5089 C  CG2 . VAL   D 1 64  ? 25.858  -38.066 -42.032  1.00 16.87 ? 157 VAL   D CG2 1 
ATOM   5090 N  N   . ARG   D 1 65  ? 23.643  -34.100 -43.754  1.00 16.17 ? 158 ARG   D N   1 
ATOM   5091 C  CA  . ARG   D 1 65  ? 22.989  -33.217 -44.752  1.00 16.14 ? 158 ARG   D CA  1 
ATOM   5092 C  C   . ARG   D 1 65  ? 24.080  -32.517 -45.557  1.00 15.78 ? 158 ARG   D C   1 
ATOM   5093 O  O   . ARG   D 1 65  ? 25.057  -32.075 -44.943  1.00 16.65 ? 158 ARG   D O   1 
ATOM   5094 C  CB  . ARG   D 1 65  ? 22.071  -32.200 -44.062  1.00 16.09 ? 158 ARG   D CB  1 
ATOM   5095 C  CG  . ARG   D 1 65  ? 21.289  -31.300 -45.011  1.00 16.20 ? 158 ARG   D CG  1 
ATOM   5096 C  CD  . ARG   D 1 65  ? 20.362  -30.344 -44.281  1.00 16.44 ? 158 ARG   D CD  1 
ATOM   5097 N  NE  . ARG   D 1 65  ? 19.494  -31.062 -43.352  1.00 16.66 ? 158 ARG   D NE  1 
ATOM   5098 C  CZ  . ARG   D 1 65  ? 18.369  -31.693 -43.682  1.00 16.83 ? 158 ARG   D CZ  1 
ATOM   5099 N  NH1 . ARG   D 1 65  ? 17.926  -31.684 -44.931  1.00 16.68 ? 158 ARG   D NH1 1 
ATOM   5100 N  NH2 . ARG   D 1 65  ? 17.681  -32.335 -42.755  1.00 17.05 ? 158 ARG   D NH2 1 
ATOM   5101 N  N   . ALA   D 1 66  ? 23.896  -32.422 -46.876  1.00 15.98 ? 159 ALA   D N   1 
ATOM   5102 C  CA  . ALA   D 1 66  ? 24.726  -31.614 -47.795  1.00 15.96 ? 159 ALA   D CA  1 
ATOM   5103 C  C   . ALA   D 1 66  ? 23.860  -30.508 -48.400  1.00 16.01 ? 159 ALA   D C   1 
ATOM   5104 O  O   . ALA   D 1 66  ? 22.700  -30.777 -48.751  1.00 15.99 ? 159 ALA   D O   1 
ATOM   5105 C  CB  . ALA   D 1 66  ? 25.329  -32.490 -48.860  1.00 15.98 ? 159 ALA   D CB  1 
ATOM   5106 N  N   . MET   D 1 67  ? 24.420  -29.307 -48.517  1.00 16.38 ? 160 MET   D N   1 
ATOM   5107 C  CA  . MET   D 1 67  ? 23.754  -28.122 -49.107  1.00 16.97 ? 160 MET   D CA  1 
ATOM   5108 C  C   . MET   D 1 67  ? 24.812  -27.273 -49.815  1.00 17.01 ? 160 MET   D C   1 
ATOM   5109 O  O   . MET   D 1 67  ? 25.890  -27.056 -49.218  1.00 17.13 ? 160 MET   D O   1 
ATOM   5110 C  CB  . MET   D 1 67  ? 23.061  -27.290 -48.023  1.00 17.71 ? 160 MET   D CB  1 
ATOM   5111 C  CG  . MET   D 1 67  ? 22.404  -26.023 -48.547  1.00 18.12 ? 160 MET   D CG  1 
ATOM   5112 S  SD  . MET   D 1 67  ? 21.616  -25.057 -47.233  1.00 18.71 ? 160 MET   D SD  1 
ATOM   5113 C  CE  . MET   D 1 67  ? 20.293  -26.159 -46.738  1.00 18.53 ? 160 MET   D CE  1 
ATOM   5114 N  N   . ALA   D 1 68  ? 24.517  -26.825 -51.037  1.00 17.24 ? 161 ALA   D N   1 
ATOM   5115 C  CA  . ALA   D 1 68  ? 25.370  -25.904 -51.823  1.00 17.80 ? 161 ALA   D CA  1 
ATOM   5116 C  C   . ALA   D 1 68  ? 24.949  -24.463 -51.520  1.00 18.10 ? 161 ALA   D C   1 
ATOM   5117 O  O   . ALA   D 1 68  ? 23.732  -24.214 -51.446  1.00 17.55 ? 161 ALA   D O   1 
ATOM   5118 C  CB  . ALA   D 1 68  ? 25.255  -26.211 -53.298  1.00 18.13 ? 161 ALA   D CB  1 
ATOM   5119 N  N   . ILE   D 1 69  ? 25.915  -23.563 -51.321  1.00 18.76 ? 162 ILE   D N   1 
ATOM   5120 C  CA  . ILE   D 1 69  ? 25.668  -22.089 -51.247  1.00 20.07 ? 162 ILE   D CA  1 
ATOM   5121 C  C   . ILE   D 1 69  ? 26.744  -21.369 -52.068  1.00 20.09 ? 162 ILE   D C   1 
ATOM   5122 O  O   . ILE   D 1 69  ? 27.883  -21.865 -52.121  1.00 19.57 ? 162 ILE   D O   1 
ATOM   5123 C  CB  . ILE   D 1 69  ? 25.622  -21.598 -49.783  1.00 20.76 ? 162 ILE   D CB  1 
ATOM   5124 C  CG1 . ILE   D 1 69  ? 26.979  -21.726 -49.090  1.00 21.47 ? 162 ILE   D CG1 1 
ATOM   5125 C  CG2 . ILE   D 1 69  ? 24.527  -22.311 -49.000  1.00 21.03 ? 162 ILE   D CG2 1 
ATOM   5126 C  CD1 . ILE   D 1 69  ? 27.036  -21.042 -47.745  1.00 22.75 ? 162 ILE   D CD1 1 
ATOM   5127 N  N   . TYR   D 1 70  ? 26.404  -20.239 -52.691  1.00 20.21 ? 163 TYR   D N   1 
ATOM   5128 C  CA  . TYR   D 1 70  ? 27.389  -19.382 -53.401  1.00 20.47 ? 163 TYR   D CA  1 
ATOM   5129 C  C   . TYR   D 1 70  ? 28.399  -18.849 -52.376  1.00 21.14 ? 163 TYR   D C   1 
ATOM   5130 O  O   . TYR   D 1 70  ? 28.001  -18.479 -51.255  1.00 20.79 ? 163 TYR   D O   1 
ATOM   5131 C  CB  . TYR   D 1 70  ? 26.680  -18.296 -54.211  1.00 20.09 ? 163 TYR   D CB  1 
ATOM   5132 C  CG  . TYR   D 1 70  ? 25.994  -18.839 -55.436  1.00 19.35 ? 163 TYR   D CG  1 
ATOM   5133 C  CD1 . TYR   D 1 70  ? 26.735  -19.375 -56.475  1.00 18.95 ? 163 TYR   D CD1 1 
ATOM   5134 C  CD2 . TYR   D 1 70  ? 24.613  -18.863 -55.541  1.00 18.94 ? 163 TYR   D CD2 1 
ATOM   5135 C  CE1 . TYR   D 1 70  ? 26.127  -19.893 -57.605  1.00 18.40 ? 163 TYR   D CE1 1 
ATOM   5136 C  CE2 . TYR   D 1 70  ? 23.985  -19.381 -56.661  1.00 18.09 ? 163 TYR   D CE2 1 
ATOM   5137 C  CZ  . TYR   D 1 70  ? 24.747  -19.903 -57.692  1.00 18.06 ? 163 TYR   D CZ  1 
ATOM   5138 O  OH  . TYR   D 1 70  ? 24.154  -20.416 -58.799  1.00 17.24 ? 163 TYR   D OH  1 
ATOM   5139 N  N   . LYS   D 1 71  ? 29.681  -18.873 -52.738  1.00 21.86 ? 164 LYS   D N   1 
ATOM   5140 C  CA  . LYS   D 1 71  ? 30.806  -18.508 -51.840  1.00 23.53 ? 164 LYS   D CA  1 
ATOM   5141 C  C   . LYS   D 1 71  ? 30.826  -16.988 -51.638  1.00 23.97 ? 164 LYS   D C   1 
ATOM   5142 O  O   . LYS   D 1 71  ? 31.077  -16.556 -50.505  1.00 23.32 ? 164 LYS   D O   1 
ATOM   5143 C  CB  . LYS   D 1 71  ? 32.142  -18.992 -52.413  1.00 23.98 ? 164 LYS   D CB  1 
ATOM   5144 C  CG  . LYS   D 1 71  ? 33.346  -18.725 -51.519  1.00 24.20 ? 164 LYS   D CG  1 
ATOM   5145 C  CD  . LYS   D 1 71  ? 34.671  -19.086 -52.139  1.00 25.22 ? 164 LYS   D CD  1 
ATOM   5146 C  CE  . LYS   D 1 71  ? 35.830  -18.816 -51.201  1.00 26.11 ? 164 LYS   D CE  1 
ATOM   5147 N  NZ  . LYS   D 1 71  ? 37.133  -18.871 -51.904  1.00 26.94 ? 164 LYS   D NZ  1 
ATOM   5148 N  N   . GLN   D 1 72  ? 30.576  -16.227 -52.707  1.00 26.36 ? 165 GLN   D N   1 
ATOM   5149 C  CA  . GLN   D 1 72  ? 30.687  -14.742 -52.750  1.00 27.88 ? 165 GLN   D CA  1 
ATOM   5150 C  C   . GLN   D 1 72  ? 29.489  -14.114 -52.025  1.00 29.37 ? 165 GLN   D C   1 
ATOM   5151 O  O   . GLN   D 1 72  ? 28.346  -14.579 -52.257  1.00 27.35 ? 165 GLN   D O   1 
ATOM   5152 C  CB  . GLN   D 1 72  ? 30.770  -14.263 -54.202  1.00 28.30 ? 165 GLN   D CB  1 
ATOM   5153 C  CG  . GLN   D 1 72  ? 32.016  -14.743 -54.935  1.00 29.25 ? 165 GLN   D CG  1 
ATOM   5154 C  CD  . GLN   D 1 72  ? 31.899  -14.590 -56.432  1.00 30.16 ? 165 GLN   D CD  1 
ATOM   5155 O  OE1 . GLN   D 1 72  ? 31.008  -15.152 -57.068  1.00 29.41 ? 165 GLN   D OE1 1 
ATOM   5156 N  NE2 . GLN   D 1 72  ? 32.810  -13.827 -57.016  1.00 31.03 ? 165 GLN   D NE2 1 
ATOM   5157 N  N   . SER   D 1 73  ? 29.756  -13.081 -51.214  1.00 30.37 ? 166 SER   D N   1 
ATOM   5158 C  CA  A SER   D 1 73  ? 28.759  -12.358 -50.378  0.15 31.25 ? 166 SER   D CA  1 
ATOM   5159 C  CA  B SER   D 1 73  ? 28.759  -12.353 -50.379  0.85 32.31 ? 166 SER   D CA  1 
ATOM   5160 C  C   . SER   D 1 73  ? 27.592  -11.852 -51.236  1.00 32.01 ? 166 SER   D C   1 
ATOM   5161 O  O   . SER   D 1 73  ? 26.438  -11.964 -50.775  1.00 34.14 ? 166 SER   D O   1 
ATOM   5162 C  CB  A SER   D 1 73  ? 29.412  -11.223 -49.629  0.15 30.95 ? 166 SER   D CB  1 
ATOM   5163 C  CB  B SER   D 1 73  ? 29.406  -11.207 -49.643  0.85 33.00 ? 166 SER   D CB  1 
ATOM   5164 O  OG  A SER   D 1 73  ? 30.097  -10.356 -50.521  0.15 30.40 ? 166 SER   D OG  1 
ATOM   5165 O  OG  B SER   D 1 73  ? 30.547  -11.651 -48.926  0.85 34.96 ? 166 SER   D OG  1 
ATOM   5166 N  N   . GLN   D 1 74  ? 27.891  -11.318 -52.424  1.00 33.59 ? 167 GLN   D N   1 
ATOM   5167 C  CA  . GLN   D 1 74  ? 26.891  -10.654 -53.307  1.00 34.71 ? 167 GLN   D CA  1 
ATOM   5168 C  C   . GLN   D 1 74  ? 25.920  -11.678 -53.912  1.00 33.21 ? 167 GLN   D C   1 
ATOM   5169 O  O   . GLN   D 1 74  ? 24.880  -11.231 -54.439  1.00 33.57 ? 167 GLN   D O   1 
ATOM   5170 C  CB  . GLN   D 1 74  ? 27.564  -9.830  -54.411  1.00 36.98 ? 167 GLN   D CB  1 
ATOM   5171 C  CG  . GLN   D 1 74  ? 28.464  -10.626 -55.345  1.00 39.05 ? 167 GLN   D CG  1 
ATOM   5172 C  CD  . GLN   D 1 74  ? 29.925  -10.518 -54.982  1.00 41.22 ? 167 GLN   D CD  1 
ATOM   5173 O  OE1 . GLN   D 1 74  ? 30.291  -10.362 -53.818  1.00 41.44 ? 167 GLN   D OE1 1 
ATOM   5174 N  NE2 . GLN   D 1 74  ? 30.780  -10.600 -55.990  1.00 43.61 ? 167 GLN   D NE2 1 
ATOM   5175 N  N   . HIS   D 1 75  ? 26.232  -12.980 -53.851  1.00 31.25 ? 168 HIS   D N   1 
ATOM   5176 C  CA  . HIS   D 1 75  ? 25.410  -14.073 -54.444  1.00 29.55 ? 168 HIS   D CA  1 
ATOM   5177 C  C   . HIS   D 1 75  ? 24.884  -15.042 -53.371  1.00 28.79 ? 168 HIS   D C   1 
ATOM   5178 O  O   . HIS   D 1 75  ? 24.152  -15.968 -53.755  1.00 28.36 ? 168 HIS   D O   1 
ATOM   5179 C  CB  . HIS   D 1 75  ? 26.219  -14.834 -55.505  1.00 29.96 ? 168 HIS   D CB  1 
ATOM   5180 C  CG  . HIS   D 1 75  ? 26.713  -13.985 -56.629  1.00 30.48 ? 168 HIS   D CG  1 
ATOM   5181 N  ND1 . HIS   D 1 75  ? 25.860  -13.325 -57.493  1.00 30.58 ? 168 HIS   D ND1 1 
ATOM   5182 C  CD2 . HIS   D 1 75  ? 27.967  -13.704 -57.048  1.00 30.95 ? 168 HIS   D CD2 1 
ATOM   5183 C  CE1 . HIS   D 1 75  ? 26.567  -12.671 -58.392  1.00 30.52 ? 168 HIS   D CE1 1 
ATOM   5184 N  NE2 . HIS   D 1 75  ? 27.864  -12.887 -58.140  1.00 29.55 ? 168 HIS   D NE2 1 
ATOM   5185 N  N   . MET   D 1 76  ? 25.222  -14.841 -52.091  1.00 28.00 ? 169 MET   D N   1 
ATOM   5186 C  CA  . MET   D 1 76  ? 24.989  -15.824 -50.991  1.00 28.89 ? 169 MET   D CA  1 
ATOM   5187 C  C   . MET   D 1 76  ? 23.494  -16.122 -50.808  1.00 26.74 ? 169 MET   D C   1 
ATOM   5188 O  O   . MET   D 1 76  ? 23.165  -17.286 -50.487  1.00 24.13 ? 169 MET   D O   1 
ATOM   5189 C  CB  . MET   D 1 76  ? 25.540  -15.315 -49.656  1.00 31.24 ? 169 MET   D CB  1 
ATOM   5190 C  CG  . MET   D 1 76  ? 27.004  -15.628 -49.442  1.00 33.44 ? 169 MET   D CG  1 
ATOM   5191 S  SD  . MET   D 1 76  ? 27.424  -15.680 -47.682  1.00 36.38 ? 169 MET   D SD  1 
ATOM   5192 C  CE  . MET   D 1 76  ? 27.152  -17.419 -47.354  1.00 37.16 ? 169 MET   D CE  1 
ATOM   5193 N  N   . THR   D 1 77  ? 22.628  -15.116 -50.977  1.00 25.19 ? 170 THR   D N   1 
ATOM   5194 C  CA  . THR   D 1 77  ? 21.162  -15.220 -50.737  1.00 25.23 ? 170 THR   D CA  1 
ATOM   5195 C  C   . THR   D 1 77  ? 20.462  -15.902 -51.920  1.00 24.90 ? 170 THR   D C   1 
ATOM   5196 O  O   . THR   D 1 77  ? 19.261  -16.204 -51.773  1.00 25.62 ? 170 THR   D O   1 
ATOM   5197 C  CB  . THR   D 1 77  ? 20.531  -13.851 -50.454  1.00 24.61 ? 170 THR   D CB  1 
ATOM   5198 O  OG1 . THR   D 1 77  ? 20.618  -13.061 -51.638  1.00 24.86 ? 170 THR   D OG1 1 
ATOM   5199 C  CG2 . THR   D 1 77  ? 21.193  -13.123 -49.305  1.00 25.67 ? 170 THR   D CG2 1 
ATOM   5200 N  N   . GLU   D 1 78  ? 21.155  -16.122 -53.045  1.00 23.96 ? 171 GLU   D N   1 
ATOM   5201 C  CA  . GLU   D 1 78  ? 20.583  -16.817 -54.231  1.00 23.84 ? 171 GLU   D CA  1 
ATOM   5202 C  C   . GLU   D 1 78  ? 20.665  -18.334 -54.017  1.00 23.21 ? 171 GLU   D C   1 
ATOM   5203 O  O   . GLU   D 1 78  ? 21.766  -18.831 -53.703  1.00 22.17 ? 171 GLU   D O   1 
ATOM   5204 C  CB  . GLU   D 1 78  ? 21.294  -16.403 -55.521  1.00 24.43 ? 171 GLU   D CB  1 
ATOM   5205 C  CG  . GLU   D 1 78  ? 20.654  -16.982 -56.768  1.00 25.27 ? 171 GLU   D CG  1 
ATOM   5206 C  CD  . GLU   D 1 78  ? 21.332  -16.600 -58.070  1.00 26.33 ? 171 GLU   D CD  1 
ATOM   5207 O  OE1 . GLU   D 1 78  ? 21.819  -15.454 -58.168  1.00 27.75 ? 171 GLU   D OE1 1 
ATOM   5208 O  OE2 . GLU   D 1 78  ? 21.372  -17.448 -58.985  1.00 27.67 ? 171 GLU   D OE2 1 
ATOM   5209 N  N   . VAL   D 1 79  ? 19.542  -19.038 -54.202  1.00 22.32 ? 172 VAL   D N   1 
ATOM   5210 C  CA  . VAL   D 1 79  ? 19.443  -20.522 -54.061  1.00 21.92 ? 172 VAL   D CA  1 
ATOM   5211 C  C   . VAL   D 1 79  ? 20.283  -21.158 -55.176  1.00 21.11 ? 172 VAL   D C   1 
ATOM   5212 O  O   . VAL   D 1 79  ? 20.062  -20.818 -56.359  1.00 21.81 ? 172 VAL   D O   1 
ATOM   5213 C  CB  . VAL   D 1 79  ? 17.982  -21.011 -54.108  1.00 22.23 ? 172 VAL   D CB  1 
ATOM   5214 C  CG1 . VAL   D 1 79  ? 17.898  -22.531 -54.074  1.00 22.75 ? 172 VAL   D CG1 1 
ATOM   5215 C  CG2 . VAL   D 1 79  ? 17.141  -20.409 -52.990  1.00 22.36 ? 172 VAL   D CG2 1 
ATOM   5216 N  N   . VAL   D 1 80  ? 21.223  -22.030 -54.811  1.00 20.29 ? 173 VAL   D N   1 
ATOM   5217 C  CA  . VAL   D 1 80  ? 22.029  -22.831 -55.779  1.00 19.86 ? 173 VAL   D CA  1 
ATOM   5218 C  C   . VAL   D 1 80  ? 21.126  -23.930 -56.347  1.00 19.69 ? 173 VAL   D C   1 
ATOM   5219 O  O   . VAL   D 1 80  ? 20.625  -24.753 -55.562  1.00 18.78 ? 173 VAL   D O   1 
ATOM   5220 C  CB  . VAL   D 1 80  ? 23.294  -23.432 -55.139  1.00 20.00 ? 173 VAL   D CB  1 
ATOM   5221 C  CG1 . VAL   D 1 80  ? 24.098  -24.234 -56.154  1.00 19.93 ? 173 VAL   D CG1 1 
ATOM   5222 C  CG2 . VAL   D 1 80  ? 24.167  -22.368 -54.489  1.00 20.09 ? 173 VAL   D CG2 1 
ATOM   5223 N  N   . ARG   D 1 81  ? 20.932  -23.937 -57.666  1.00 20.08 ? 174 ARG   D N   1 
ATOM   5224 C  CA  . ARG   D 1 81  ? 20.097  -24.942 -58.373  1.00 21.15 ? 174 ARG   D CA  1 
ATOM   5225 C  C   . ARG   D 1 81  ? 20.735  -25.257 -59.724  1.00 20.49 ? 174 ARG   D C   1 
ATOM   5226 O  O   . ARG   D 1 81  ? 21.612  -24.487 -60.175  1.00 19.31 ? 174 ARG   D O   1 
ATOM   5227 C  CB  . ARG   D 1 81  ? 18.660  -24.440 -58.553  1.00 22.77 ? 174 ARG   D CB  1 
ATOM   5228 C  CG  . ARG   D 1 81  ? 18.557  -23.079 -59.226  1.00 25.02 ? 174 ARG   D CG  1 
ATOM   5229 C  CD  . ARG   D 1 81  ? 17.126  -22.644 -59.497  1.00 26.93 ? 174 ARG   D CD  1 
ATOM   5230 N  NE  . ARG   D 1 81  ? 16.409  -22.339 -58.266  1.00 28.38 ? 174 ARG   D NE  1 
ATOM   5231 C  CZ  . ARG   D 1 81  ? 15.496  -23.122 -57.687  1.00 29.81 ? 174 ARG   D CZ  1 
ATOM   5232 N  NH1 . ARG   D 1 81  ? 15.156  -24.285 -58.223  1.00 31.16 ? 174 ARG   D NH1 1 
ATOM   5233 N  NH2 . ARG   D 1 81  ? 14.921  -22.730 -56.564  1.00 29.64 ? 174 ARG   D NH2 1 
ATOM   5234 N  N   . ARG   D 1 82  ? 20.298  -26.352 -60.343  1.00 19.80 ? 175 ARG   D N   1 
ATOM   5235 C  CA  . ARG   D 1 82  ? 20.722  -26.739 -61.709  1.00 19.76 ? 175 ARG   D CA  1 
ATOM   5236 C  C   . ARG   D 1 82  ? 20.181  -25.709 -62.701  1.00 19.78 ? 175 ARG   D C   1 
ATOM   5237 O  O   . ARG   D 1 82  ? 19.094  -25.135 -62.430  1.00 19.70 ? 175 ARG   D O   1 
ATOM   5238 C  CB  . ARG   D 1 82  ? 20.203  -28.131 -62.067  1.00 19.91 ? 175 ARG   D CB  1 
ATOM   5239 C  CG  . ARG   D 1 82  ? 20.720  -29.235 -61.159  1.00 20.13 ? 175 ARG   D CG  1 
ATOM   5240 C  CD  . ARG   D 1 82  ? 20.079  -30.543 -61.548  1.00 20.42 ? 175 ARG   D CD  1 
ATOM   5241 N  NE  . ARG   D 1 82  ? 20.787  -31.205 -62.624  1.00 21.06 ? 175 ARG   D NE  1 
ATOM   5242 C  CZ  . ARG   D 1 82  ? 20.306  -32.203 -63.350  1.00 20.57 ? 175 ARG   D CZ  1 
ATOM   5243 N  NH1 . ARG   D 1 82  ? 19.072  -32.643 -63.167  1.00 19.77 ? 175 ARG   D NH1 1 
ATOM   5244 N  NH2 . ARG   D 1 82  ? 21.068  -32.748 -64.282  1.00 21.26 ? 175 ARG   D NH2 1 
ATOM   5245 N  N   . CYS   D 1 83  ? 20.911  -25.490 -63.796  1.00 19.46 ? 176 CYS   D N   1 
ATOM   5246 C  CA  . CYS   D 1 83  ? 20.491  -24.616 -64.924  1.00 19.97 ? 176 CYS   D CA  1 
ATOM   5247 C  C   . CYS   D 1 83  ? 19.236  -25.205 -65.572  1.00 20.38 ? 176 CYS   D C   1 
ATOM   5248 O  O   . CYS   D 1 83  ? 18.919  -26.378 -65.375  1.00 20.08 ? 176 CYS   D O   1 
ATOM   5249 C  CB  . CYS   D 1 83  ? 21.630  -24.432 -65.928  1.00 19.50 ? 176 CYS   D CB  1 
ATOM   5250 S  SG  . CYS   D 1 83  ? 22.012  -25.852 -66.899  1.00 19.67 ? 176 CYS   D SG  1 
ATOM   5251 N  N   . PRO   D 1 84  ? 18.450  -24.404 -66.328  1.00 22.10 ? 177 PRO   D N   1 
ATOM   5252 C  CA  . PRO   D 1 84  ? 17.282  -24.924 -67.043  1.00 22.81 ? 177 PRO   D CA  1 
ATOM   5253 C  C   . PRO   D 1 84  ? 17.582  -26.181 -67.873  1.00 22.72 ? 177 PRO   D C   1 
ATOM   5254 O  O   . PRO   D 1 84  ? 16.800  -27.117 -67.822  1.00 22.74 ? 177 PRO   D O   1 
ATOM   5255 C  CB  . PRO   D 1 84  ? 16.885  -23.758 -67.959  1.00 23.13 ? 177 PRO   D CB  1 
ATOM   5256 C  CG  . PRO   D 1 84  ? 17.325  -22.533 -67.188  1.00 22.82 ? 177 PRO   D CG  1 
ATOM   5257 C  CD  . PRO   D 1 84  ? 18.606  -22.952 -66.496  1.00 22.59 ? 177 PRO   D CD  1 
ATOM   5258 N  N   . HIS   D 1 85  ? 18.700  -26.180 -68.607  1.00 22.63 ? 178 HIS   D N   1 
ATOM   5259 C  CA  . HIS   D 1 85  ? 19.109  -27.296 -69.502  1.00 23.13 ? 178 HIS   D CA  1 
ATOM   5260 C  C   . HIS   D 1 85  ? 19.227  -28.596 -68.700  1.00 22.81 ? 178 HIS   D C   1 
ATOM   5261 O  O   . HIS   D 1 85  ? 18.564  -29.580 -69.075  1.00 23.71 ? 178 HIS   D O   1 
ATOM   5262 C  CB  . HIS   D 1 85  ? 20.421  -26.985 -70.239  1.00 23.39 ? 178 HIS   D CB  1 
ATOM   5263 C  CG  . HIS   D 1 85  ? 21.028  -28.202 -70.850  1.00 23.49 ? 178 HIS   D CG  1 
ATOM   5264 N  ND1 . HIS   D 1 85  ? 20.521  -28.777 -71.995  1.00 23.64 ? 178 HIS   D ND1 1 
ATOM   5265 C  CD2 . HIS   D 1 85  ? 22.064  -28.975 -70.460  1.00 23.58 ? 178 HIS   D CD2 1 
ATOM   5266 C  CE1 . HIS   D 1 85  ? 21.230  -29.844 -72.299  1.00 24.44 ? 178 HIS   D CE1 1 
ATOM   5267 N  NE2 . HIS   D 1 85  ? 22.182  -29.991 -71.370  1.00 24.54 ? 178 HIS   D NE2 1 
ATOM   5268 N  N   . HIS   D 1 86  ? 20.059  -28.603 -67.653  1.00 22.54 ? 179 HIS   D N   1 
ATOM   5269 C  CA  . HIS   D 1 86  ? 20.385  -29.816 -66.852  1.00 22.32 ? 179 HIS   D CA  1 
ATOM   5270 C  C   . HIS   D 1 86  ? 19.147  -30.289 -66.081  1.00 22.79 ? 179 HIS   D C   1 
ATOM   5271 O  O   . HIS   D 1 86  ? 18.967  -31.511 -65.950  1.00 22.78 ? 179 HIS   D O   1 
ATOM   5272 C  CB  . HIS   D 1 86  ? 21.615  -29.565 -65.965  1.00 20.97 ? 179 HIS   D CB  1 
ATOM   5273 C  CG  . HIS   D 1 86  ? 22.895  -29.754 -66.706  1.00 19.58 ? 179 HIS   D CG  1 
ATOM   5274 N  ND1 . HIS   D 1 86  ? 23.898  -28.796 -66.750  1.00 18.58 ? 179 HIS   D ND1 1 
ATOM   5275 C  CD2 . HIS   D 1 86  ? 23.330  -30.795 -67.451  1.00 19.11 ? 179 HIS   D CD2 1 
ATOM   5276 C  CE1 . HIS   D 1 86  ? 24.895  -29.251 -67.491  1.00 18.85 ? 179 HIS   D CE1 1 
ATOM   5277 N  NE2 . HIS   D 1 86  ? 24.569  -30.474 -67.933  1.00 18.60 ? 179 HIS   D NE2 1 
ATOM   5278 N  N   . GLU   D 1 87  ? 18.308  -29.361 -65.624  1.00 24.39 ? 180 GLU   D N   1 
ATOM   5279 C  CA  . GLU   D 1 87  ? 17.033  -29.678 -64.925  1.00 25.73 ? 180 GLU   D CA  1 
ATOM   5280 C  C   . GLU   D 1 87  ? 16.149  -30.541 -65.838  1.00 27.04 ? 180 GLU   D C   1 
ATOM   5281 O  O   . GLU   D 1 87  ? 15.434  -31.409 -65.301  1.00 25.76 ? 180 GLU   D O   1 
ATOM   5282 C  CB  . GLU   D 1 87  ? 16.340  -28.382 -64.506  1.00 26.55 ? 180 GLU   D CB  1 
ATOM   5283 C  CG  . GLU   D 1 87  ? 14.985  -28.585 -63.862  1.00 27.99 ? 180 GLU   D CG  1 
ATOM   5284 C  CD  . GLU   D 1 87  ? 14.257  -27.290 -63.551  1.00 28.96 ? 180 GLU   D CD  1 
ATOM   5285 O  OE1 . GLU   D 1 87  ? 14.936  -26.263 -63.354  1.00 29.60 ? 180 GLU   D OE1 1 
ATOM   5286 O  OE2 . GLU   D 1 87  ? 13.013  -27.314 -63.504  1.00 31.34 ? 180 GLU   D OE2 1 
ATOM   5287 N  N   . ARG   D 1 88  ? 16.212  -30.315 -67.158  1.00 28.69 ? 181 ARG   D N   1 
ATOM   5288 C  CA  . ARG   D 1 88  ? 15.352  -30.975 -68.179  1.00 29.62 ? 181 ARG   D CA  1 
ATOM   5289 C  C   . ARG   D 1 88  ? 16.025  -32.249 -68.709  1.00 28.77 ? 181 ARG   D C   1 
ATOM   5290 O  O   . ARG   D 1 88  ? 15.337  -33.010 -69.413  1.00 28.56 ? 181 ARG   D O   1 
ATOM   5291 C  CB  . ARG   D 1 88  ? 15.047  -30.006 -69.326  1.00 31.76 ? 181 ARG   D CB  1 
ATOM   5292 C  CG  . ARG   D 1 88  ? 14.144  -28.837 -68.949  1.00 33.82 ? 181 ARG   D CG  1 
ATOM   5293 C  CD  . ARG   D 1 88  ? 13.718  -28.012 -70.155  1.00 36.52 ? 181 ARG   D CD  1 
ATOM   5294 N  NE  . ARG   D 1 88  ? 14.778  -27.882 -71.159  1.00 39.65 ? 181 ARG   D NE  1 
ATOM   5295 C  CZ  . ARG   D 1 88  ? 15.459  -26.769 -71.447  1.00 41.01 ? 181 ARG   D CZ  1 
ATOM   5296 N  NH1 . ARG   D 1 88  ? 15.209  -25.627 -70.824  1.00 41.59 ? 181 ARG   D NH1 1 
ATOM   5297 N  NH2 . ARG   D 1 88  ? 16.396  -26.805 -72.381  1.00 41.10 ? 181 ARG   D NH2 1 
ATOM   5298 N  N   . CYS   D 1 89  ? 17.307  -32.480 -68.402  1.00 28.55 ? 182 CYS   D N   1 
ATOM   5299 C  CA  . CYS   D 1 89  ? 18.047  -33.706 -68.815  1.00 28.95 ? 182 CYS   D CA  1 
ATOM   5300 C  C   . CYS   D 1 89  ? 17.311  -34.934 -68.262  1.00 29.82 ? 182 CYS   D C   1 
ATOM   5301 O  O   . CYS   D 1 89  ? 16.747  -34.845 -67.163  1.00 28.94 ? 182 CYS   D O   1 
ATOM   5302 C  CB  . CYS   D 1 89  ? 19.503  -33.687 -68.359  1.00 28.70 ? 182 CYS   D CB  1 
ATOM   5303 S  SG  . CYS   D 1 89  ? 20.596  -32.741 -69.455  1.00 29.43 ? 182 CYS   D SG  1 
ATOM   5304 N  N   . SER   D 1 90  ? 17.275  -36.026 -69.026  1.00 31.97 ? 183 SER   D N   1 
ATOM   5305 C  CA  . SER   D 1 90  ? 16.633  -37.306 -68.629  1.00 32.66 ? 183 SER   D CA  1 
ATOM   5306 C  C   . SER   D 1 90  ? 17.657  -38.161 -67.874  1.00 32.80 ? 183 SER   D C   1 
ATOM   5307 O  O   . SER   D 1 90  ? 18.102  -39.190 -68.424  1.00 34.30 ? 183 SER   D O   1 
ATOM   5308 C  CB  . SER   D 1 90  ? 16.064  -38.019 -69.832  1.00 33.71 ? 183 SER   D CB  1 
ATOM   5309 O  OG  . SER   D 1 90  ? 17.075  -38.268 -70.798  1.00 34.89 ? 183 SER   D OG  1 
ATOM   5310 N  N   . ASP   D 1 91  ? 18.032  -37.726 -66.665  1.00 31.70 ? 184 ASP   D N   1 
ATOM   5311 C  CA  . ASP   D 1 91  ? 19.080  -38.365 -65.823  1.00 29.81 ? 184 ASP   D CA  1 
ATOM   5312 C  C   . ASP   D 1 91  ? 18.506  -38.673 -64.434  1.00 29.73 ? 184 ASP   D C   1 
ATOM   5313 O  O   . ASP   D 1 91  ? 19.301  -38.836 -63.489  1.00 28.16 ? 184 ASP   D O   1 
ATOM   5314 C  CB  . ASP   D 1 91  ? 20.332  -37.483 -65.750  1.00 29.74 ? 184 ASP   D CB  1 
ATOM   5315 C  CG  . ASP   D 1 91  ? 20.112  -36.106 -65.141  1.00 28.90 ? 184 ASP   D CG  1 
ATOM   5316 O  OD1 . ASP   D 1 91  ? 19.039  -35.882 -64.542  1.00 27.97 ? 184 ASP   D OD1 1 
ATOM   5317 O  OD2 . ASP   D 1 91  ? 21.023  -35.266 -65.267  1.00 28.72 ? 184 ASP   D OD2 1 
ATOM   5318 N  N   . SER   D 1 92  ? 17.178  -38.756 -64.316  1.00 29.75 ? 185 SER   D N   1 
ATOM   5319 C  CA  . SER   D 1 92  ? 16.467  -39.013 -63.036  1.00 29.24 ? 185 SER   D CA  1 
ATOM   5320 C  C   . SER   D 1 92  ? 16.872  -40.388 -62.493  1.00 28.27 ? 185 SER   D C   1 
ATOM   5321 O  O   . SER   D 1 92  ? 17.033  -41.326 -63.300  1.00 26.95 ? 185 SER   D O   1 
ATOM   5322 C  CB  . SER   D 1 92  ? 14.974  -38.910 -63.200  1.00 29.87 ? 185 SER   D CB  1 
ATOM   5323 O  OG  . SER   D 1 92  ? 14.322  -39.123 -61.958  1.00 31.37 ? 185 SER   D OG  1 
ATOM   5324 N  N   . ASP   D 1 93  ? 17.048  -40.487 -61.173  1.00 26.78 ? 186 ASP   D N   1 
ATOM   5325 C  CA  . ASP   D 1 93  ? 17.298  -41.764 -60.456  1.00 26.25 ? 186 ASP   D CA  1 
ATOM   5326 C  C   . ASP   D 1 93  ? 16.013  -42.200 -59.741  1.00 25.47 ? 186 ASP   D C   1 
ATOM   5327 O  O   . ASP   D 1 93  ? 16.064  -43.219 -59.040  1.00 26.35 ? 186 ASP   D O   1 
ATOM   5328 C  CB  . ASP   D 1 93  ? 18.497  -41.639 -59.509  1.00 26.25 ? 186 ASP   D CB  1 
ATOM   5329 C  CG  . ASP   D 1 93  ? 18.331  -40.648 -58.367  1.00 25.80 ? 186 ASP   D CG  1 
ATOM   5330 O  OD1 . ASP   D 1 93  ? 17.302  -39.934 -58.329  1.00 24.04 ? 186 ASP   D OD1 1 
ATOM   5331 O  OD2 . ASP   D 1 93  ? 19.239  -40.600 -57.520  1.00 25.61 ? 186 ASP   D OD2 1 
ATOM   5332 N  N   . GLY   D 1 94  ? 14.918  -41.447 -59.908  1.00 24.47 ? 187 GLY   D N   1 
ATOM   5333 C  CA  . GLY   D 1 94  ? 13.601  -41.723 -59.299  1.00 24.02 ? 187 GLY   D CA  1 
ATOM   5334 C  C   . GLY   D 1 94  ? 13.457  -41.153 -57.893  1.00 23.31 ? 187 GLY   D C   1 
ATOM   5335 O  O   . GLY   D 1 94  ? 12.342  -41.239 -57.337  1.00 23.51 ? 187 GLY   D O   1 
ATOM   5336 N  N   . LEU   D 1 95  ? 14.523  -40.579 -57.326  1.00 22.08 ? 188 LEU   D N   1 
ATOM   5337 C  CA  . LEU   D 1 95  ? 14.546  -40.096 -55.916  1.00 21.16 ? 188 LEU   D CA  1 
ATOM   5338 C  C   . LEU   D 1 95  ? 14.856  -38.596 -55.873  1.00 20.00 ? 188 LEU   D C   1 
ATOM   5339 O  O   . LEU   D 1 95  ? 14.098  -37.866 -55.211  1.00 20.38 ? 188 LEU   D O   1 
ATOM   5340 C  CB  . LEU   D 1 95  ? 15.580  -40.902 -55.127  1.00 21.42 ? 188 LEU   D CB  1 
ATOM   5341 C  CG  . LEU   D 1 95  ? 15.375  -42.415 -55.122  1.00 21.32 ? 188 LEU   D CG  1 
ATOM   5342 C  CD1 . LEU   D 1 95  ? 16.561  -43.112 -54.471  1.00 21.50 ? 188 LEU   D CD1 1 
ATOM   5343 C  CD2 . LEU   D 1 95  ? 14.080  -42.785 -54.414  1.00 21.50 ? 188 LEU   D CD2 1 
ATOM   5344 N  N   . ALA   D 1 96  ? 15.912  -38.150 -56.557  1.00 19.16 ? 189 ALA   D N   1 
ATOM   5345 C  CA  . ALA   D 1 96  ? 16.363  -36.735 -56.576  1.00 18.80 ? 189 ALA   D CA  1 
ATOM   5346 C  C   . ALA   D 1 96  ? 15.357  -35.859 -57.321  1.00 18.24 ? 189 ALA   D C   1 
ATOM   5347 O  O   . ALA   D 1 96  ? 14.930  -36.197 -58.426  1.00 18.33 ? 189 ALA   D O   1 
ATOM   5348 C  CB  . ALA   D 1 96  ? 17.727  -36.634 -57.218  1.00 18.68 ? 189 ALA   D CB  1 
ATOM   5349 N  N   . PRO   D 1 97  ? 14.956  -34.694 -56.760  1.00 17.94 ? 190 PRO   D N   1 
ATOM   5350 C  CA  . PRO   D 1 97  ? 14.279  -33.665 -57.547  1.00 17.90 ? 190 PRO   D CA  1 
ATOM   5351 C  C   . PRO   D 1 97  ? 15.167  -33.225 -58.708  1.00 17.94 ? 190 PRO   D C   1 
ATOM   5352 O  O   . PRO   D 1 97  ? 16.380  -33.080 -58.541  1.00 17.59 ? 190 PRO   D O   1 
ATOM   5353 C  CB  . PRO   D 1 97  ? 14.062  -32.503 -56.567  1.00 17.47 ? 190 PRO   D CB  1 
ATOM   5354 C  CG  . PRO   D 1 97  ? 14.149  -33.141 -55.194  1.00 17.82 ? 190 PRO   D CG  1 
ATOM   5355 C  CD  . PRO   D 1 97  ? 15.107  -34.307 -55.348  1.00 17.91 ? 190 PRO   D CD  1 
ATOM   5356 N  N   . PRO   D 1 98  ? 14.602  -32.990 -59.916  1.00 18.16 ? 191 PRO   D N   1 
ATOM   5357 C  CA  . PRO   D 1 98  ? 15.413  -32.625 -61.080  1.00 18.48 ? 191 PRO   D CA  1 
ATOM   5358 C  C   . PRO   D 1 98  ? 16.162  -31.287 -60.950  1.00 18.62 ? 191 PRO   D C   1 
ATOM   5359 O  O   . PRO   D 1 98  ? 17.099  -31.100 -61.692  1.00 18.39 ? 191 PRO   D O   1 
ATOM   5360 C  CB  . PRO   D 1 98  ? 14.406  -32.566 -62.241  1.00 18.65 ? 191 PRO   D CB  1 
ATOM   5361 C  CG  . PRO   D 1 98  ? 13.053  -32.389 -61.575  1.00 18.88 ? 191 PRO   D CG  1 
ATOM   5362 C  CD  . PRO   D 1 98  ? 13.168  -33.075 -60.228  1.00 18.59 ? 191 PRO   D CD  1 
ATOM   5363 N  N   . GLN   D 1 99  ? 15.754  -30.415 -60.018  1.00 18.90 ? 192 GLN   D N   1 
ATOM   5364 C  CA  . GLN   D 1 99  ? 16.358  -29.072 -59.787  1.00 19.74 ? 192 GLN   D CA  1 
ATOM   5365 C  C   . GLN   D 1 99  ? 17.609  -29.164 -58.901  1.00 18.44 ? 192 GLN   D C   1 
ATOM   5366 O  O   . GLN   D 1 99  ? 18.409  -28.206 -58.933  1.00 18.50 ? 192 GLN   D O   1 
ATOM   5367 C  CB  . GLN   D 1 99  ? 15.373  -28.124 -59.097  1.00 21.41 ? 192 GLN   D CB  1 
ATOM   5368 C  CG  . GLN   D 1 99  ? 14.054  -27.934 -59.832  1.00 22.52 ? 192 GLN   D CG  1 
ATOM   5369 C  CD  . GLN   D 1 99  ? 13.064  -29.052 -59.610  1.00 23.88 ? 192 GLN   D CD  1 
ATOM   5370 O  OE1 . GLN   D 1 99  ? 13.232  -29.909 -58.740  1.00 23.64 ? 192 GLN   D OE1 1 
ATOM   5371 N  NE2 . GLN   D 1 99  ? 12.015  -29.055 -60.418  1.00 24.84 ? 192 GLN   D NE2 1 
ATOM   5372 N  N   . HIS   D 1 100 ? 17.770  -30.244 -58.125  1.00 17.43 ? 193 HIS   D N   1 
ATOM   5373 C  CA  . HIS   D 1 100 ? 18.815  -30.376 -57.069  1.00 16.30 ? 193 HIS   D CA  1 
ATOM   5374 C  C   . HIS   D 1 100 ? 20.198  -30.586 -57.691  1.00 15.94 ? 193 HIS   D C   1 
ATOM   5375 O  O   . HIS   D 1 100 ? 20.366  -31.552 -58.447  1.00 15.33 ? 193 HIS   D O   1 
ATOM   5376 C  CB  . HIS   D 1 100 ? 18.486  -31.515 -56.097  1.00 15.88 ? 193 HIS   D CB  1 
ATOM   5377 C  CG  . HIS   D 1 100 ? 17.476  -31.146 -55.065  1.00 15.49 ? 193 HIS   D CG  1 
ATOM   5378 N  ND1 . HIS   D 1 100 ? 17.599  -31.532 -53.742  1.00 14.97 ? 193 HIS   D ND1 1 
ATOM   5379 C  CD2 . HIS   D 1 100 ? 16.350  -30.407 -55.149  1.00 14.86 ? 193 HIS   D CD2 1 
ATOM   5380 C  CE1 . HIS   D 1 100 ? 16.572  -31.066 -53.063  1.00 15.42 ? 193 HIS   D CE1 1 
ATOM   5381 N  NE2 . HIS   D 1 100 ? 15.795  -30.364 -53.903  1.00 14.71 ? 193 HIS   D NE2 1 
ATOM   5382 N  N   . LEU   D 1 101 ? 21.155  -29.724 -57.341  1.00 15.98 ? 194 LEU   D N   1 
ATOM   5383 C  CA  . LEU   D 1 101 ? 22.574  -29.833 -57.772  1.00 15.50 ? 194 LEU   D CA  1 
ATOM   5384 C  C   . LEU   D 1 101 ? 23.204  -31.108 -57.194  1.00 15.41 ? 194 LEU   D C   1 
ATOM   5385 O  O   . LEU   D 1 101 ? 23.822  -31.866 -57.962  1.00 15.46 ? 194 LEU   D O   1 
ATOM   5386 C  CB  . LEU   D 1 101 ? 23.335  -28.593 -57.300  1.00 15.63 ? 194 LEU   D CB  1 
ATOM   5387 C  CG  . LEU   D 1 101 ? 24.824  -28.584 -57.637  1.00 15.27 ? 194 LEU   D CG  1 
ATOM   5388 C  CD1 . LEU   D 1 101 ? 25.022  -28.538 -59.142  1.00 15.32 ? 194 LEU   D CD1 1 
ATOM   5389 C  CD2 . LEU   D 1 101 ? 25.528  -27.413 -56.963  1.00 15.30 ? 194 LEU   D CD2 1 
ATOM   5390 N  N   . ILE   D 1 102 ? 23.073  -31.328 -55.886  1.00 15.25 ? 195 ILE   D N   1 
ATOM   5391 C  CA  . ILE   D 1 102 ? 23.792  -32.415 -55.157  1.00 15.24 ? 195 ILE   D CA  1 
ATOM   5392 C  C   . ILE   D 1 102 ? 22.857  -33.613 -54.972  1.00 15.16 ? 195 ILE   D C   1 
ATOM   5393 O  O   . ILE   D 1 102 ? 21.777  -33.445 -54.386  1.00 14.96 ? 195 ILE   D O   1 
ATOM   5394 C  CB  . ILE   D 1 102 ? 24.349  -31.909 -53.810  1.00 14.84 ? 195 ILE   D CB  1 
ATOM   5395 C  CG1 . ILE   D 1 102 ? 25.086  -30.576 -53.972  1.00 14.82 ? 195 ILE   D CG1 1 
ATOM   5396 C  CG2 . ILE   D 1 102 ? 25.235  -32.968 -53.175  1.00 14.86 ? 195 ILE   D CG2 1 
ATOM   5397 C  CD1 . ILE   D 1 102 ? 25.646  -30.013 -52.692  1.00 14.65 ? 195 ILE   D CD1 1 
ATOM   5398 N  N   . ARG   D 1 103 ? 23.284  -34.786 -55.444  1.00 15.78 ? 196 ARG   D N   1 
ATOM   5399 C  CA  . ARG   D 1 103 ? 22.627  -36.087 -55.173  1.00 16.24 ? 196 ARG   D CA  1 
ATOM   5400 C  C   . ARG   D 1 103 ? 23.576  -36.955 -54.350  1.00 16.68 ? 196 ARG   D C   1 
ATOM   5401 O  O   . ARG   D 1 103 ? 24.799  -36.671 -54.358  1.00 17.29 ? 196 ARG   D O   1 
ATOM   5402 C  CB  . ARG   D 1 103 ? 22.282  -36.819 -56.472  1.00 16.48 ? 196 ARG   D CB  1 
ATOM   5403 C  CG  . ARG   D 1 103 ? 21.306  -36.068 -57.361  1.00 16.95 ? 196 ARG   D CG  1 
ATOM   5404 C  CD  . ARG   D 1 103 ? 20.980  -36.850 -58.618  1.00 16.91 ? 196 ARG   D CD  1 
ATOM   5405 N  NE  . ARG   D 1 103 ? 20.176  -36.053 -59.535  1.00 17.58 ? 196 ARG   D NE  1 
ATOM   5406 C  CZ  . ARG   D 1 103 ? 19.759  -36.468 -60.727  1.00 17.84 ? 196 ARG   D CZ  1 
ATOM   5407 N  NH1 . ARG   D 1 103 ? 20.069  -37.684 -61.147  1.00 18.03 ? 196 ARG   D NH1 1 
ATOM   5408 N  NH2 . ARG   D 1 103 ? 19.041  -35.665 -61.496  1.00 17.28 ? 196 ARG   D NH2 1 
ATOM   5409 N  N   . VAL   D 1 104 ? 23.031  -37.972 -53.678  1.00 16.37 ? 197 VAL   D N   1 
ATOM   5410 C  CA  . VAL   D 1 104 ? 23.813  -39.110 -53.119  1.00 17.17 ? 197 VAL   D CA  1 
ATOM   5411 C  C   . VAL   D 1 104 ? 23.539  -40.322 -54.009  1.00 18.06 ? 197 VAL   D C   1 
ATOM   5412 O  O   . VAL   D 1 104 ? 22.354  -40.562 -54.317  1.00 19.20 ? 197 VAL   D O   1 
ATOM   5413 C  CB  . VAL   D 1 104 ? 23.460  -39.393 -51.647  1.00 16.62 ? 197 VAL   D CB  1 
ATOM   5414 C  CG1 . VAL   D 1 104 ? 24.188  -40.629 -51.130  1.00 16.64 ? 197 VAL   D CG1 1 
ATOM   5415 C  CG2 . VAL   D 1 104 ? 23.760  -38.192 -50.764  1.00 16.06 ? 197 VAL   D CG2 1 
ATOM   5416 N  N   . GLU   D 1 105 ? 24.589  -41.028 -54.433  1.00 19.69 ? 198 GLU   D N   1 
ATOM   5417 C  CA  . GLU   D 1 105 ? 24.478  -42.264 -55.254  1.00 21.24 ? 198 GLU   D CA  1 
ATOM   5418 C  C   . GLU   D 1 105 ? 24.683  -43.481 -54.339  1.00 22.00 ? 198 GLU   D C   1 
ATOM   5419 O  O   . GLU   D 1 105 ? 25.437  -43.368 -53.347  1.00 22.98 ? 198 GLU   D O   1 
ATOM   5420 C  CB  . GLU   D 1 105 ? 25.456  -42.194 -56.433  1.00 22.53 ? 198 GLU   D CB  1 
ATOM   5421 C  CG  . GLU   D 1 105 ? 26.732  -42.986 -56.250  1.00 23.19 ? 198 GLU   D CG  1 
ATOM   5422 C  CD  . GLU   D 1 105 ? 27.690  -42.905 -57.425  1.00 24.24 ? 198 GLU   D CD  1 
ATOM   5423 O  OE1 . GLU   D 1 105 ? 27.825  -43.912 -58.145  1.00 27.08 ? 198 GLU   D OE1 1 
ATOM   5424 O  OE2 . GLU   D 1 105 ? 28.308  -41.841 -57.610  1.00 24.46 ? 198 GLU   D OE2 1 
ATOM   5425 N  N   . GLY   D 1 106 ? 23.997  -44.588 -54.639  1.00 22.89 ? 199 GLY   D N   1 
ATOM   5426 C  CA  . GLY   D 1 106 ? 24.169  -45.891 -53.965  1.00 23.13 ? 199 GLY   D CA  1 
ATOM   5427 C  C   . GLY   D 1 106 ? 23.644  -45.911 -52.537  1.00 23.54 ? 199 GLY   D C   1 
ATOM   5428 O  O   . GLY   D 1 106 ? 24.207  -46.671 -51.728  1.00 23.68 ? 199 GLY   D O   1 
ATOM   5429 N  N   . ASN   D 1 107 ? 22.594  -45.139 -52.227  1.00 23.65 ? 200 ASN   D N   1 
ATOM   5430 C  CA  . ASN   D 1 107 ? 21.936  -45.138 -50.891  1.00 23.56 ? 200 ASN   D CA  1 
ATOM   5431 C  C   . ASN   D 1 107 ? 20.417  -44.995 -51.066  1.00 24.53 ? 200 ASN   D C   1 
ATOM   5432 O  O   . ASN   D 1 107 ? 19.954  -43.874 -51.337  1.00 23.29 ? 200 ASN   D O   1 
ATOM   5433 C  CB  . ASN   D 1 107 ? 22.517  -44.044 -49.992  1.00 23.69 ? 200 ASN   D CB  1 
ATOM   5434 C  CG  . ASN   D 1 107 ? 22.155  -44.216 -48.532  1.00 23.30 ? 200 ASN   D CG  1 
ATOM   5435 O  OD1 . ASN   D 1 107 ? 21.059  -44.668 -48.202  1.00 23.55 ? 200 ASN   D OD1 1 
ATOM   5436 N  ND2 . ASN   D 1 107 ? 23.070  -43.854 -47.649  1.00 22.73 ? 200 ASN   D ND2 1 
ATOM   5437 N  N   . LEU   D 1 108 ? 19.671  -46.090 -50.880  1.00 25.78 ? 201 LEU   D N   1 
ATOM   5438 C  CA  . LEU   D 1 108 ? 18.190  -46.133 -51.051  1.00 27.21 ? 201 LEU   D CA  1 
ATOM   5439 C  C   . LEU   D 1 108 ? 17.473  -45.375 -49.926  1.00 25.87 ? 201 LEU   D C   1 
ATOM   5440 O  O   . LEU   D 1 108 ? 16.241  -45.193 -50.059  1.00 25.92 ? 201 LEU   D O   1 
ATOM   5441 C  CB  . LEU   D 1 108 ? 17.707  -47.589 -51.097  1.00 28.82 ? 201 LEU   D CB  1 
ATOM   5442 C  CG  . LEU   D 1 108 ? 17.566  -48.208 -52.489  1.00 31.35 ? 201 LEU   D CG  1 
ATOM   5443 C  CD1 . LEU   D 1 108 ? 16.827  -49.539 -52.406  1.00 31.70 ? 201 LEU   D CD1 1 
ATOM   5444 C  CD2 . LEU   D 1 108 ? 16.852  -47.263 -53.453  1.00 32.10 ? 201 LEU   D CD2 1 
ATOM   5445 N  N   . ARG   D 1 109 ? 18.182  -44.966 -48.864  1.00 24.03 ? 202 ARG   D N   1 
ATOM   5446 C  CA  . ARG   D 1 109 ? 17.592  -44.255 -47.694  1.00 23.83 ? 202 ARG   D CA  1 
ATOM   5447 C  C   . ARG   D 1 109 ? 17.828  -42.746 -47.825  1.00 21.15 ? 202 ARG   D C   1 
ATOM   5448 O  O   . ARG   D 1 109 ? 17.551  -42.021 -46.857  1.00 19.58 ? 202 ARG   D O   1 
ATOM   5449 C  CB  . ARG   D 1 109 ? 18.181  -44.787 -46.381  1.00 25.51 ? 202 ARG   D CB  1 
ATOM   5450 C  CG  . ARG   D 1 109 ? 18.023  -46.288 -46.188  1.00 27.85 ? 202 ARG   D CG  1 
ATOM   5451 C  CD  . ARG   D 1 109 ? 18.680  -46.776 -44.907  1.00 29.74 ? 202 ARG   D CD  1 
ATOM   5452 N  NE  . ARG   D 1 109 ? 18.024  -46.248 -43.717  1.00 32.01 ? 202 ARG   D NE  1 
ATOM   5453 C  CZ  . ARG   D 1 109 ? 18.484  -46.363 -42.472  1.00 33.95 ? 202 ARG   D CZ  1 
ATOM   5454 N  NH1 . ARG   D 1 109 ? 19.626  -46.986 -42.229  1.00 34.78 ? 202 ARG   D NH1 1 
ATOM   5455 N  NH2 . ARG   D 1 109 ? 17.800  -45.841 -41.468  1.00 35.43 ? 202 ARG   D NH2 1 
ATOM   5456 N  N   . VAL   D 1 110 ? 18.332  -42.293 -48.976  1.00 19.51 ? 203 VAL   D N   1 
ATOM   5457 C  CA  . VAL   D 1 110 ? 18.566  -40.849 -49.273  1.00 18.33 ? 203 VAL   D CA  1 
ATOM   5458 C  C   . VAL   D 1 110 ? 17.225  -40.107 -49.170  1.00 17.31 ? 203 VAL   D C   1 
ATOM   5459 O  O   . VAL   D 1 110 ? 16.179  -40.686 -49.552  1.00 16.67 ? 203 VAL   D O   1 
ATOM   5460 C  CB  . VAL   D 1 110 ? 19.242  -40.644 -50.646  1.00 18.35 ? 203 VAL   D CB  1 
ATOM   5461 C  CG1 . VAL   D 1 110 ? 18.376  -41.128 -51.802  1.00 18.42 ? 203 VAL   D CG1 1 
ATOM   5462 C  CG2 . VAL   D 1 110 ? 19.643  -39.195 -50.853  1.00 18.25 ? 203 VAL   D CG2 1 
ATOM   5463 N  N   . GLU   D 1 111 ? 17.274  -38.875 -48.662  1.00 16.50 ? 204 GLU   D N   1 
ATOM   5464 C  CA  . GLU   D 1 111 ? 16.109  -37.974 -48.464  1.00 15.85 ? 204 GLU   D CA  1 
ATOM   5465 C  C   . GLU   D 1 111 ? 16.455  -36.597 -49.036  1.00 15.78 ? 204 GLU   D C   1 
ATOM   5466 O  O   . GLU   D 1 111 ? 17.574  -36.092 -48.765  1.00 15.82 ? 204 GLU   D O   1 
ATOM   5467 C  CB  . GLU   D 1 111 ? 15.765  -37.903 -46.976  1.00 15.73 ? 204 GLU   D CB  1 
ATOM   5468 C  CG  . GLU   D 1 111 ? 14.789  -36.804 -46.607  1.00 15.82 ? 204 GLU   D CG  1 
ATOM   5469 C  CD  . GLU   D 1 111 ? 14.525  -36.691 -45.115  1.00 15.96 ? 204 GLU   D CD  1 
ATOM   5470 O  OE1 . GLU   D 1 111 ? 14.489  -37.747 -44.436  1.00 16.73 ? 204 GLU   D OE1 1 
ATOM   5471 O  OE2 . GLU   D 1 111 ? 14.383  -35.549 -44.627  1.00 15.73 ? 204 GLU   D OE2 1 
ATOM   5472 N  N   . TYR   D 1 112 ? 15.534  -36.018 -49.804  1.00 15.58 ? 205 TYR   D N   1 
ATOM   5473 C  CA  . TYR   D 1 112 ? 15.705  -34.713 -50.490  1.00 15.72 ? 205 TYR   D CA  1 
ATOM   5474 C  C   . TYR   D 1 112 ? 14.721  -33.716 -49.882  1.00 16.05 ? 205 TYR   D C   1 
ATOM   5475 O  O   . TYR   D 1 112 ? 13.547  -34.079 -49.661  1.00 16.59 ? 205 TYR   D O   1 
ATOM   5476 C  CB  . TYR   D 1 112 ? 15.540  -34.889 -52.002  1.00 15.48 ? 205 TYR   D CB  1 
ATOM   5477 C  CG  . TYR   D 1 112 ? 16.693  -35.621 -52.634  1.00 15.43 ? 205 TYR   D CG  1 
ATOM   5478 C  CD1 . TYR   D 1 112 ? 17.837  -34.947 -53.032  1.00 15.07 ? 205 TYR   D CD1 1 
ATOM   5479 C  CD2 . TYR   D 1 112 ? 16.661  -36.999 -52.795  1.00 15.45 ? 205 TYR   D CD2 1 
ATOM   5480 C  CE1 . TYR   D 1 112 ? 18.912  -35.617 -53.593  1.00 15.12 ? 205 TYR   D CE1 1 
ATOM   5481 C  CE2 . TYR   D 1 112 ? 17.729  -37.684 -53.354  1.00 15.20 ? 205 TYR   D CE2 1 
ATOM   5482 C  CZ  . TYR   D 1 112 ? 18.859  -36.991 -53.757  1.00 15.23 ? 205 TYR   D CZ  1 
ATOM   5483 O  OH  . TYR   D 1 112 ? 19.918  -37.665 -54.297  1.00 14.75 ? 205 TYR   D OH  1 
ATOM   5484 N  N   . LEU   D 1 113 ? 15.204  -32.507 -49.599  1.00 16.12 ? 206 LEU   D N   1 
ATOM   5485 C  CA  . LEU   D 1 113 ? 14.415  -31.408 -48.993  1.00 16.13 ? 206 LEU   D CA  1 
ATOM   5486 C  C   . LEU   D 1 113 ? 14.449  -30.188 -49.918  1.00 16.60 ? 206 LEU   D C   1 
ATOM   5487 O  O   . LEU   D 1 113 ? 15.556  -29.756 -50.320  1.00 16.56 ? 206 LEU   D O   1 
ATOM   5488 C  CB  . LEU   D 1 113 ? 14.986  -31.062 -47.613  1.00 15.82 ? 206 LEU   D CB  1 
ATOM   5489 C  CG  . LEU   D 1 113 ? 14.307  -29.892 -46.905  1.00 15.50 ? 206 LEU   D CG  1 
ATOM   5490 C  CD1 . LEU   D 1 113 ? 12.874  -30.245 -46.540  1.00 15.48 ? 206 LEU   D CD1 1 
ATOM   5491 C  CD2 . LEU   D 1 113 ? 15.086  -29.476 -45.667  1.00 15.55 ? 206 LEU   D CD2 1 
ATOM   5492 N  N   . ASP   D 1 114 ? 13.264  -29.695 -50.270  1.00 16.23 ? 207 ASP   D N   1 
ATOM   5493 C  CA  . ASP   D 1 114 ? 13.011  -28.275 -50.618  1.00 17.17 ? 207 ASP   D CA  1 
ATOM   5494 C  C   . ASP   D 1 114 ? 12.528  -27.598 -49.333  1.00 17.87 ? 207 ASP   D C   1 
ATOM   5495 O  O   . ASP   D 1 114 ? 11.410  -27.919 -48.894  1.00 17.44 ? 207 ASP   D O   1 
ATOM   5496 C  CB  . ASP   D 1 114 ? 11.942  -28.128 -51.704  1.00 16.98 ? 207 ASP   D CB  1 
ATOM   5497 C  CG  . ASP   D 1 114 ? 12.310  -28.668 -53.072  1.00 17.31 ? 207 ASP   D CG  1 
ATOM   5498 O  OD1 . ASP   D 1 114 ? 13.509  -28.844 -53.345  1.00 17.72 ? 207 ASP   D OD1 1 
ATOM   5499 O  OD2 . ASP   D 1 114 ? 11.381  -28.888 -53.865  1.00 17.99 ? 207 ASP   D OD2 1 
ATOM   5500 N  N   . ASP   D 1 115 ? 13.347  -26.746 -48.717  1.00 18.96 ? 208 ASP   D N   1 
ATOM   5501 C  CA  . ASP   D 1 115 ? 12.961  -26.022 -47.478  1.00 20.17 ? 208 ASP   D CA  1 
ATOM   5502 C  C   . ASP   D 1 115 ? 11.740  -25.152 -47.797  1.00 20.92 ? 208 ASP   D C   1 
ATOM   5503 O  O   . ASP   D 1 115 ? 11.799  -24.379 -48.767  1.00 19.49 ? 208 ASP   D O   1 
ATOM   5504 C  CB  . ASP   D 1 115 ? 14.119  -25.196 -46.921  1.00 20.89 ? 208 ASP   D CB  1 
ATOM   5505 C  CG  . ASP   D 1 115 ? 13.910  -24.783 -45.476  1.00 21.75 ? 208 ASP   D CG  1 
ATOM   5506 O  OD1 . ASP   D 1 115 ? 13.095  -23.868 -45.239  1.00 22.26 ? 208 ASP   D OD1 1 
ATOM   5507 O  OD2 . ASP   D 1 115 ? 14.548  -25.395 -44.597  1.00 22.51 ? 208 ASP   D OD2 1 
ATOM   5508 N  N   . ARG   D 1 116 ? 10.659  -25.282 -47.025  1.00 23.23 ? 209 ARG   D N   1 
ATOM   5509 C  CA  . ARG   D 1 116 ? 9.376   -24.598 -47.338  1.00 25.41 ? 209 ARG   D CA  1 
ATOM   5510 C  C   . ARG   D 1 116 ? 9.538   -23.078 -47.175  1.00 24.96 ? 209 ARG   D C   1 
ATOM   5511 O  O   . ARG   D 1 116 ? 8.802   -22.346 -47.853  1.00 23.37 ? 209 ARG   D O   1 
ATOM   5512 C  CB  . ARG   D 1 116 ? 8.227   -25.183 -46.509  1.00 28.15 ? 209 ARG   D CB  1 
ATOM   5513 C  CG  . ARG   D 1 116 ? 8.250   -24.848 -45.025  1.00 31.58 ? 209 ARG   D CG  1 
ATOM   5514 C  CD  . ARG   D 1 116 ? 7.074   -25.503 -44.318  1.00 35.09 ? 209 ARG   D CD  1 
ATOM   5515 N  NE  . ARG   D 1 116 ? 5.799   -24.976 -44.796  1.00 37.43 ? 209 ARG   D NE  1 
ATOM   5516 C  CZ  . ARG   D 1 116 ? 4.608   -25.531 -44.583  1.00 39.99 ? 209 ARG   D CZ  1 
ATOM   5517 N  NH1 . ARG   D 1 116 ? 3.521   -24.952 -45.065  1.00 42.77 ? 209 ARG   D NH1 1 
ATOM   5518 N  NH2 . ARG   D 1 116 ? 4.497   -26.659 -43.900  1.00 41.37 ? 209 ARG   D NH2 1 
ATOM   5519 N  N   . ASN   D 1 117 ? 10.499  -22.622 -46.361  1.00 25.38 ? 210 ASN   D N   1 
ATOM   5520 C  CA  . ASN   D 1 117 ? 10.658  -21.191 -45.979  1.00 26.58 ? 210 ASN   D CA  1 
ATOM   5521 C  C   . ASN   D 1 117 ? 11.851  -20.555 -46.715  1.00 26.85 ? 210 ASN   D C   1 
ATOM   5522 O  O   . ASN   D 1 117 ? 11.673  -19.431 -47.228  1.00 28.21 ? 210 ASN   D O   1 
ATOM   5523 C  CB  . ASN   D 1 117 ? 10.723  -21.059 -44.455  1.00 26.79 ? 210 ASN   D CB  1 
ATOM   5524 C  CG  . ASN   D 1 117 ? 9.462   -21.580 -43.795  1.00 26.98 ? 210 ASN   D CG  1 
ATOM   5525 O  OD1 . ASN   D 1 117 ? 9.504   -22.491 -42.974  1.00 28.23 ? 210 ASN   D OD1 1 
ATOM   5526 N  ND2 . ASN   D 1 117 ? 8.323   -21.030 -44.177  1.00 26.96 ? 210 ASN   D ND2 1 
ATOM   5527 N  N   . THR   D 1 118 ? 13.006  -21.234 -46.790  1.00 26.61 ? 211 THR   D N   1 
ATOM   5528 C  CA  . THR   D 1 118 ? 14.253  -20.705 -47.419  1.00 25.34 ? 211 THR   D CA  1 
ATOM   5529 C  C   . THR   D 1 118 ? 14.335  -21.093 -48.903  1.00 25.53 ? 211 THR   D C   1 
ATOM   5530 O  O   . THR   D 1 118 ? 15.123  -20.447 -49.617  1.00 25.05 ? 211 THR   D O   1 
ATOM   5531 C  CB  . THR   D 1 118 ? 15.520  -21.184 -46.698  1.00 25.30 ? 211 THR   D CB  1 
ATOM   5532 O  OG1 . THR   D 1 118 ? 15.728  -22.568 -46.993  1.00 24.90 ? 211 THR   D OG1 1 
ATOM   5533 C  CG2 . THR   D 1 118 ? 15.468  -20.968 -45.201  1.00 25.05 ? 211 THR   D CG2 1 
ATOM   5534 N  N   . PHE   D 1 119 ? 13.600  -22.130 -49.331  1.00 24.50 ? 212 PHE   D N   1 
ATOM   5535 C  CA  . PHE   D 1 119 ? 13.574  -22.672 -50.720  1.00 24.37 ? 212 PHE   D CA  1 
ATOM   5536 C  C   . PHE   D 1 119 ? 14.917  -23.328 -51.070  1.00 22.88 ? 212 PHE   D C   1 
ATOM   5537 O  O   . PHE   D 1 119 ? 15.105  -23.712 -52.242  1.00 21.18 ? 212 PHE   D O   1 
ATOM   5538 C  CB  . PHE   D 1 119 ? 13.203  -21.580 -51.727  1.00 26.27 ? 212 PHE   D CB  1 
ATOM   5539 C  CG  . PHE   D 1 119 ? 11.963  -20.814 -51.344  1.00 28.52 ? 212 PHE   D CG  1 
ATOM   5540 C  CD1 . PHE   D 1 119 ? 10.727  -21.440 -51.307  1.00 29.10 ? 212 PHE   D CD1 1 
ATOM   5541 C  CD2 . PHE   D 1 119 ? 12.037  -19.480 -50.981  1.00 30.43 ? 212 PHE   D CD2 1 
ATOM   5542 C  CE1 . PHE   D 1 119 ? 9.587   -20.742 -50.935  1.00 29.80 ? 212 PHE   D CE1 1 
ATOM   5543 C  CE2 . PHE   D 1 119 ? 10.897  -18.785 -50.609  1.00 31.10 ? 212 PHE   D CE2 1 
ATOM   5544 C  CZ  . PHE   D 1 119 ? 9.675   -19.416 -50.585  1.00 30.20 ? 212 PHE   D CZ  1 
ATOM   5545 N  N   . ARG   D 1 120 ? 15.800  -23.489 -50.080  1.00 20.76 ? 213 ARG   D N   1 
ATOM   5546 C  CA  . ARG   D 1 120 ? 17.137  -24.112 -50.244  1.00 20.70 ? 213 ARG   D CA  1 
ATOM   5547 C  C   . ARG   D 1 120 ? 16.963  -25.618 -50.457  1.00 18.54 ? 213 ARG   D C   1 
ATOM   5548 O  O   . ARG   D 1 120 ? 16.060  -26.212 -49.826  1.00 16.97 ? 213 ARG   D O   1 
ATOM   5549 C  CB  . ARG   D 1 120 ? 18.007  -23.863 -49.010  1.00 21.97 ? 213 ARG   D CB  1 
ATOM   5550 C  CG  . ARG   D 1 120 ? 18.232  -22.392 -48.686  1.00 23.30 ? 213 ARG   D CG  1 
ATOM   5551 C  CD  . ARG   D 1 120 ? 19.543  -21.895 -49.245  1.00 23.96 ? 213 ARG   D CD  1 
ATOM   5552 N  NE  . ARG   D 1 120 ? 19.782  -20.489 -48.956  1.00 23.87 ? 213 ARG   D NE  1 
ATOM   5553 C  CZ  . ARG   D 1 120 ? 20.721  -19.748 -49.540  1.00 24.75 ? 213 ARG   D CZ  1 
ATOM   5554 N  NH1 . ARG   D 1 120 ? 21.531  -20.280 -50.443  1.00 24.55 ? 213 ARG   D NH1 1 
ATOM   5555 N  NH2 . ARG   D 1 120 ? 20.850  -18.471 -49.221  1.00 24.27 ? 213 ARG   D NH2 1 
ATOM   5556 N  N   . HIS   D 1 121 ? 17.806  -26.194 -51.317  1.00 17.26 ? 214 HIS   D N   1 
ATOM   5557 C  CA  . HIS   D 1 121 ? 17.876  -27.647 -51.611  1.00 16.49 ? 214 HIS   D CA  1 
ATOM   5558 C  C   . HIS   D 1 121 ? 18.920  -28.279 -50.691  1.00 16.21 ? 214 HIS   D C   1 
ATOM   5559 O  O   . HIS   D 1 121 ? 19.997  -27.680 -50.504  1.00 16.79 ? 214 HIS   D O   1 
ATOM   5560 C  CB  . HIS   D 1 121 ? 18.215  -27.901 -53.086  1.00 16.16 ? 214 HIS   D CB  1 
ATOM   5561 C  CG  . HIS   D 1 121 ? 17.282  -27.245 -54.051  1.00 16.38 ? 214 HIS   D CG  1 
ATOM   5562 N  ND1 . HIS   D 1 121 ? 17.584  -27.115 -55.390  1.00 16.15 ? 214 HIS   D ND1 1 
ATOM   5563 C  CD2 . HIS   D 1 121 ? 16.068  -26.677 -53.881  1.00 16.42 ? 214 HIS   D CD2 1 
ATOM   5564 C  CE1 . HIS   D 1 121 ? 16.587  -26.517 -56.010  1.00 16.32 ? 214 HIS   D CE1 1 
ATOM   5565 N  NE2 . HIS   D 1 121 ? 15.646  -26.229 -55.104  1.00 16.36 ? 214 HIS   D NE2 1 
ATOM   5566 N  N   . SER   D 1 122 ? 18.622  -29.455 -50.153  1.00 15.70 ? 215 SER   D N   1 
ATOM   5567 C  CA  . SER   D 1 122 ? 19.606  -30.267 -49.404  1.00 15.18 ? 215 SER   D CA  1 
ATOM   5568 C  C   . SER   D 1 122 ? 19.285  -31.747 -49.582  1.00 15.19 ? 215 SER   D C   1 
ATOM   5569 O  O   . SER   D 1 122 ? 18.136  -32.088 -49.935  1.00 14.86 ? 215 SER   D O   1 
ATOM   5570 C  CB  . SER   D 1 122 ? 19.668  -29.856 -47.952  1.00 14.93 ? 215 SER   D CB  1 
ATOM   5571 O  OG  . SER   D 1 122 ? 18.449  -30.131 -47.289  1.00 14.66 ? 215 SER   D OG  1 
ATOM   5572 N  N   . VAL   D 1 123 ? 20.295  -32.586 -49.371  1.00 15.37 ? 216 VAL   D N   1 
ATOM   5573 C  CA  . VAL   D 1 123 ? 20.196  -34.066 -49.487  1.00 15.29 ? 216 VAL   D CA  1 
ATOM   5574 C  C   . VAL   D 1 123 ? 20.780  -34.642 -48.201  1.00 15.98 ? 216 VAL   D C   1 
ATOM   5575 O  O   . VAL   D 1 123 ? 21.867  -34.188 -47.768  1.00 14.85 ? 216 VAL   D O   1 
ATOM   5576 C  CB  . VAL   D 1 123 ? 20.898  -34.602 -50.749  1.00 15.26 ? 216 VAL   D CB  1 
ATOM   5577 C  CG1 . VAL   D 1 123 ? 22.345  -34.131 -50.854  1.00 15.11 ? 216 VAL   D CG1 1 
ATOM   5578 C  CG2 . VAL   D 1 123 ? 20.811  -36.118 -50.825  1.00 15.38 ? 216 VAL   D CG2 1 
ATOM   5579 N  N   . VAL   D 1 124 ? 20.056  -35.567 -47.589  1.00 16.55 ? 217 VAL   D N   1 
ATOM   5580 C  CA  . VAL   D 1 124 ? 20.410  -36.096 -46.243  1.00 17.41 ? 217 VAL   D CA  1 
ATOM   5581 C  C   . VAL   D 1 124 ? 20.381  -37.622 -46.319  1.00 17.79 ? 217 VAL   D C   1 
ATOM   5582 O  O   . VAL   D 1 124 ? 19.558  -38.175 -47.090  1.00 17.73 ? 217 VAL   D O   1 
ATOM   5583 C  CB  . VAL   D 1 124 ? 19.501  -35.504 -45.144  1.00 18.05 ? 217 VAL   D CB  1 
ATOM   5584 C  CG1 . VAL   D 1 124 ? 18.025  -35.757 -45.392  1.00 18.94 ? 217 VAL   D CG1 1 
ATOM   5585 C  CG2 . VAL   D 1 124 ? 19.895  -35.990 -43.762  1.00 18.19 ? 217 VAL   D CG2 1 
ATOM   5586 N  N   . VAL   D 1 125 ? 21.304  -38.272 -45.605  1.00 18.41 ? 218 VAL   D N   1 
ATOM   5587 C  CA  . VAL   D 1 125 ? 21.361  -39.758 -45.476  1.00 18.70 ? 218 VAL   D CA  1 
ATOM   5588 C  C   . VAL   D 1 125 ? 21.522  -40.089 -43.999  1.00 19.35 ? 218 VAL   D C   1 
ATOM   5589 O  O   . VAL   D 1 125 ? 21.981  -39.254 -43.221  1.00 18.58 ? 218 VAL   D O   1 
ATOM   5590 C  CB  . VAL   D 1 125 ? 22.499  -40.387 -46.302  1.00 19.61 ? 218 VAL   D CB  1 
ATOM   5591 C  CG1 . VAL   D 1 125 ? 22.252  -40.256 -47.798  1.00 19.59 ? 218 VAL   D CG1 1 
ATOM   5592 C  CG2 . VAL   D 1 125 ? 23.864  -39.827 -45.918  1.00 19.64 ? 218 VAL   D CG2 1 
ATOM   5593 N  N   . PRO   D 1 126 ? 21.137  -41.313 -43.579  1.00 20.76 ? 219 PRO   D N   1 
ATOM   5594 C  CA  . PRO   D 1 126 ? 21.464  -41.808 -42.246  1.00 21.58 ? 219 PRO   D CA  1 
ATOM   5595 C  C   . PRO   D 1 126 ? 22.987  -41.899 -42.083  1.00 23.00 ? 219 PRO   D C   1 
ATOM   5596 O  O   . PRO   D 1 126 ? 23.650  -42.384 -42.987  1.00 22.13 ? 219 PRO   D O   1 
ATOM   5597 C  CB  . PRO   D 1 126 ? 20.829  -43.207 -42.190  1.00 21.26 ? 219 PRO   D CB  1 
ATOM   5598 C  CG  . PRO   D 1 126 ? 19.791  -43.196 -43.284  1.00 21.50 ? 219 PRO   D CG  1 
ATOM   5599 C  CD  . PRO   D 1 126 ? 20.342  -42.277 -44.355  1.00 21.34 ? 219 PRO   D CD  1 
ATOM   5600 N  N   . TYR   D 1 127 ? 23.510  -41.411 -40.960  1.00 23.87 ? 220 TYR   D N   1 
ATOM   5601 C  CA  . TYR   D 1 127 ? 24.914  -41.662 -40.562  1.00 25.08 ? 220 TYR   D CA  1 
ATOM   5602 C  C   . TYR   D 1 127 ? 25.050  -43.149 -40.222  1.00 26.90 ? 220 TYR   D C   1 
ATOM   5603 O  O   . TYR   D 1 127 ? 24.254  -43.649 -39.401  1.00 25.82 ? 220 TYR   D O   1 
ATOM   5604 C  CB  . TYR   D 1 127 ? 25.342  -40.802 -39.375  1.00 25.03 ? 220 TYR   D CB  1 
ATOM   5605 C  CG  . TYR   D 1 127 ? 26.707  -41.185 -38.866  1.00 24.99 ? 220 TYR   D CG  1 
ATOM   5606 C  CD1 . TYR   D 1 127 ? 27.852  -40.653 -39.436  1.00 24.96 ? 220 TYR   D CD1 1 
ATOM   5607 C  CD2 . TYR   D 1 127 ? 26.853  -42.136 -37.869  1.00 24.88 ? 220 TYR   D CD2 1 
ATOM   5608 C  CE1 . TYR   D 1 127 ? 29.112  -41.024 -38.997  1.00 26.09 ? 220 TYR   D CE1 1 
ATOM   5609 C  CE2 . TYR   D 1 127 ? 28.104  -42.521 -37.421  1.00 26.00 ? 220 TYR   D CE2 1 
ATOM   5610 C  CZ  . TYR   D 1 127 ? 29.238  -41.957 -37.982  1.00 26.64 ? 220 TYR   D CZ  1 
ATOM   5611 O  OH  . TYR   D 1 127 ? 30.472  -42.329 -37.542  1.00 27.31 ? 220 TYR   D OH  1 
ATOM   5612 N  N   . GLU   D 1 128 ? 26.006  -43.832 -40.859  1.00 28.56 ? 221 GLU   D N   1 
ATOM   5613 C  CA  . GLU   D 1 128 ? 26.397  -45.231 -40.539  1.00 31.23 ? 221 GLU   D CA  1 
ATOM   5614 C  C   . GLU   D 1 128 ? 27.833  -45.199 -40.029  1.00 31.54 ? 221 GLU   D C   1 
ATOM   5615 O  O   . GLU   D 1 128 ? 28.675  -44.527 -40.622  1.00 30.12 ? 221 GLU   D O   1 
ATOM   5616 C  CB  . GLU   D 1 128 ? 26.279  -46.138 -41.766  1.00 34.11 ? 221 GLU   D CB  1 
ATOM   5617 C  CG  . GLU   D 1 128 ? 24.866  -46.249 -42.318  1.00 36.84 ? 221 GLU   D CG  1 
ATOM   5618 C  CD  . GLU   D 1 128 ? 24.711  -47.139 -43.542  1.00 39.60 ? 221 GLU   D CD  1 
ATOM   5619 O  OE1 . GLU   D 1 128 ? 25.731  -47.436 -44.200  1.00 42.16 ? 221 GLU   D OE1 1 
ATOM   5620 O  OE2 . GLU   D 1 128 ? 23.565  -47.537 -43.836  1.00 42.02 ? 221 GLU   D OE2 1 
ATOM   5621 N  N   . PRO   D 1 129 ? 28.158  -45.886 -38.908  1.00 32.34 ? 222 PRO   D N   1 
ATOM   5622 C  CA  . PRO   D 1 129 ? 29.541  -45.964 -38.441  1.00 32.83 ? 222 PRO   D CA  1 
ATOM   5623 C  C   . PRO   D 1 129 ? 30.438  -46.579 -39.511  1.00 33.18 ? 222 PRO   D C   1 
ATOM   5624 O  O   . PRO   D 1 129 ? 29.959  -47.324 -40.363  1.00 31.59 ? 222 PRO   D O   1 
ATOM   5625 C  CB  . PRO   D 1 129 ? 29.481  -46.878 -37.206  1.00 33.03 ? 222 PRO   D CB  1 
ATOM   5626 C  CG  . PRO   D 1 129 ? 28.033  -46.819 -36.760  1.00 33.57 ? 222 PRO   D CG  1 
ATOM   5627 C  CD  . PRO   D 1 129 ? 27.229  -46.613 -38.028  1.00 32.92 ? 222 PRO   D CD  1 
ATOM   5628 N  N   . PRO   D 1 130 ? 31.763  -46.309 -39.496  1.00 35.46 ? 223 PRO   D N   1 
ATOM   5629 C  CA  . PRO   D 1 130 ? 32.679  -46.972 -40.422  1.00 37.05 ? 223 PRO   D CA  1 
ATOM   5630 C  C   . PRO   D 1 130 ? 32.505  -48.493 -40.299  1.00 38.92 ? 223 PRO   D C   1 
ATOM   5631 O  O   . PRO   D 1 130 ? 32.357  -48.969 -39.188  1.00 38.57 ? 223 PRO   D O   1 
ATOM   5632 C  CB  . PRO   D 1 130 ? 34.075  -46.518 -39.970  1.00 36.46 ? 223 PRO   D CB  1 
ATOM   5633 C  CG  . PRO   D 1 130 ? 33.830  -45.235 -39.200  1.00 35.99 ? 223 PRO   D CG  1 
ATOM   5634 C  CD  . PRO   D 1 130 ? 32.454  -45.385 -38.583  1.00 35.56 ? 223 PRO   D CD  1 
ATOM   5635 N  N   . GLU   D 1 131 ? 32.477  -49.207 -41.427  1.00 41.77 ? 224 GLU   D N   1 
ATOM   5636 C  CA  . GLU   D 1 131 ? 32.389  -50.692 -41.452  1.00 44.68 ? 224 GLU   D CA  1 
ATOM   5637 C  C   . GLU   D 1 131 ? 33.725  -51.276 -40.975  1.00 45.08 ? 224 GLU   D C   1 
ATOM   5638 O  O   . GLU   D 1 131 ? 34.742  -50.557 -41.016  1.00 44.90 ? 224 GLU   D O   1 
ATOM   5639 C  CB  . GLU   D 1 131 ? 31.999  -51.200 -42.841  1.00 46.32 ? 224 GLU   D CB  1 
ATOM   5640 C  CG  . GLU   D 1 131 ? 30.496  -51.232 -43.057  1.00 47.15 ? 224 GLU   D CG  1 
ATOM   5641 C  CD  . GLU   D 1 131 ? 30.064  -51.617 -44.460  1.00 48.20 ? 224 GLU   D CD  1 
ATOM   5642 O  OE1 . GLU   D 1 131 ? 29.590  -52.757 -44.635  1.00 49.38 ? 224 GLU   D OE1 1 
ATOM   5643 O  OE2 . GLU   D 1 131 ? 30.194  -50.775 -45.370  1.00 49.80 ? 224 GLU   D OE2 1 
ATOM   5644 N  N   . VAL   D 1 132 ? 33.704  -52.534 -40.532  1.00 46.69 ? 225 VAL   D N   1 
ATOM   5645 C  CA  . VAL   D 1 132 ? 34.873  -53.258 -39.947  1.00 46.86 ? 225 VAL   D CA  1 
ATOM   5646 C  C   . VAL   D 1 132 ? 36.016  -53.262 -40.973  1.00 45.63 ? 225 VAL   D C   1 
ATOM   5647 O  O   . VAL   D 1 132 ? 35.864  -53.902 -42.029  1.00 43.84 ? 225 VAL   D O   1 
ATOM   5648 C  CB  . VAL   D 1 132 ? 34.456  -54.674 -39.497  1.00 47.97 ? 225 VAL   D CB  1 
ATOM   5649 C  CG1 . VAL   D 1 132 ? 35.638  -55.596 -39.238  1.00 48.28 ? 225 VAL   D CG1 1 
ATOM   5650 C  CG2 . VAL   D 1 132 ? 33.553  -54.607 -38.272  1.00 48.90 ? 225 VAL   D CG2 1 
ATOM   5651 N  N   . GLY   D 1 133 ? 37.101  -52.542 -40.669  1.00 46.29 ? 226 GLY   D N   1 
ATOM   5652 C  CA  . GLY   D 1 133 ? 38.287  -52.387 -41.534  1.00 47.08 ? 226 GLY   D CA  1 
ATOM   5653 C  C   . GLY   D 1 133 ? 38.348  -51.012 -42.181  1.00 46.69 ? 226 GLY   D C   1 
ATOM   5654 O  O   . GLY   D 1 133 ? 39.111  -50.857 -43.155  1.00 46.65 ? 226 GLY   D O   1 
ATOM   5655 N  N   . SER   D 1 134 ? 37.579  -50.048 -41.659  1.00 46.58 ? 227 SER   D N   1 
ATOM   5656 C  CA  . SER   D 1 134 ? 37.541  -48.633 -42.118  1.00 44.99 ? 227 SER   D CA  1 
ATOM   5657 C  C   . SER   D 1 134 ? 37.553  -47.705 -40.899  1.00 41.86 ? 227 SER   D C   1 
ATOM   5658 O  O   . SER   D 1 134 ? 36.998  -48.101 -39.855  1.00 41.05 ? 227 SER   D O   1 
ATOM   5659 C  CB  . SER   D 1 134 ? 36.343  -48.388 -42.999  1.00 47.02 ? 227 SER   D CB  1 
ATOM   5660 O  OG  . SER   D 1 134 ? 36.433  -47.124 -43.641  1.00 49.82 ? 227 SER   D OG  1 
ATOM   5661 N  N   . ASP   D 1 135 ? 38.178  -46.529 -41.033  1.00 40.82 ? 228 ASP   D N   1 
ATOM   5662 C  CA  . ASP   D 1 135 ? 38.377  -45.534 -39.943  1.00 39.84 ? 228 ASP   D CA  1 
ATOM   5663 C  C   . ASP   D 1 135 ? 37.420  -44.342 -40.117  1.00 37.22 ? 228 ASP   D C   1 
ATOM   5664 O  O   . ASP   D 1 135 ? 37.370  -43.495 -39.204  1.00 38.26 ? 228 ASP   D O   1 
ATOM   5665 C  CB  . ASP   D 1 135 ? 39.835  -45.061 -39.890  1.00 42.26 ? 228 ASP   D CB  1 
ATOM   5666 C  CG  . ASP   D 1 135 ? 40.778  -45.993 -39.139  1.00 44.85 ? 228 ASP   D CG  1 
ATOM   5667 O  OD1 . ASP   D 1 135 ? 40.300  -46.730 -38.246  1.00 46.19 ? 228 ASP   D OD1 1 
ATOM   5668 O  OD2 . ASP   D 1 135 ? 41.990  -45.969 -39.443  1.00 45.67 ? 228 ASP   D OD2 1 
ATOM   5669 N  N   . CYS   D 1 136 ? 36.686  -44.270 -41.230  1.00 33.97 ? 229 CYS   D N   1 
ATOM   5670 C  CA  . CYS   D 1 136 ? 35.747  -43.155 -41.535  1.00 31.22 ? 229 CYS   D CA  1 
ATOM   5671 C  C   . CYS   D 1 136 ? 34.542  -43.671 -42.326  1.00 29.59 ? 229 CYS   D C   1 
ATOM   5672 O  O   . CYS   D 1 136 ? 34.624  -44.781 -42.890  1.00 29.41 ? 229 CYS   D O   1 
ATOM   5673 C  CB  . CYS   D 1 136 ? 36.449  -42.056 -42.321  1.00 30.88 ? 229 CYS   D CB  1 
ATOM   5674 S  SG  . CYS   D 1 136 ? 37.101  -42.627 -43.911  1.00 29.30 ? 229 CYS   D SG  1 
ATOM   5675 N  N   . THR   D 1 137 ? 33.467  -42.880 -42.340  1.00 27.96 ? 230 THR   D N   1 
ATOM   5676 C  CA  . THR   D 1 137 ? 32.236  -43.097 -43.141  1.00 27.18 ? 230 THR   D CA  1 
ATOM   5677 C  C   . THR   D 1 137 ? 32.376  -42.334 -44.461  1.00 25.27 ? 230 THR   D C   1 
ATOM   5678 O  O   . THR   D 1 137 ? 32.691  -41.132 -44.414  1.00 26.36 ? 230 THR   D O   1 
ATOM   5679 C  CB  . THR   D 1 137 ? 30.997  -42.638 -42.362  1.00 27.71 ? 230 THR   D CB  1 
ATOM   5680 O  OG1 . THR   D 1 137 ? 30.968  -43.367 -41.135  1.00 29.54 ? 230 THR   D OG1 1 
ATOM   5681 C  CG2 . THR   D 1 137 ? 29.703  -42.839 -43.118  1.00 27.86 ? 230 THR   D CG2 1 
ATOM   5682 N  N   . THR   D 1 138 ? 32.155  -43.000 -45.592  1.00 23.52 ? 231 THR   D N   1 
ATOM   5683 C  CA  . THR   D 1 138 ? 32.219  -42.370 -46.935  1.00 23.01 ? 231 THR   D CA  1 
ATOM   5684 C  C   . THR   D 1 138 ? 30.799  -42.211 -47.487  1.00 22.40 ? 231 THR   D C   1 
ATOM   5685 O  O   . THR   D 1 138 ? 30.027  -43.185 -47.444  1.00 22.47 ? 231 THR   D O   1 
ATOM   5686 C  CB  . THR   D 1 138 ? 33.137  -43.153 -47.880  1.00 22.42 ? 231 THR   D CB  1 
ATOM   5687 O  OG1 . THR   D 1 138 ? 34.444  -43.102 -47.309  1.00 21.65 ? 231 THR   D OG1 1 
ATOM   5688 C  CG2 . THR   D 1 138 ? 33.167  -42.583 -49.282  1.00 22.14 ? 231 THR   D CG2 1 
ATOM   5689 N  N   . ILE   D 1 139 ? 30.483  -41.015 -47.984  1.00 21.54 ? 232 ILE   D N   1 
ATOM   5690 C  CA  . ILE   D 1 139 ? 29.260  -40.746 -48.792  1.00 21.30 ? 232 ILE   D CA  1 
ATOM   5691 C  C   . ILE   D 1 139 ? 29.717  -40.447 -50.222  1.00 21.21 ? 232 ILE   D C   1 
ATOM   5692 O  O   . ILE   D 1 139 ? 30.711  -39.704 -50.387  1.00 20.95 ? 232 ILE   D O   1 
ATOM   5693 C  CB  . ILE   D 1 139 ? 28.423  -39.609 -48.172  1.00 21.08 ? 232 ILE   D CB  1 
ATOM   5694 C  CG1 . ILE   D 1 139 ? 27.982  -39.961 -46.748  1.00 21.14 ? 232 ILE   D CG1 1 
ATOM   5695 C  CG2 . ILE   D 1 139 ? 27.233  -39.262 -49.064  1.00 20.92 ? 232 ILE   D CG2 1 
ATOM   5696 C  CD1 . ILE   D 1 139 ? 27.397  -38.806 -45.976  1.00 21.32 ? 232 ILE   D CD1 1 
ATOM   5697 N  N   . HIS   D 1 140 ? 29.040  -41.042 -51.206  1.00 21.22 ? 233 HIS   D N   1 
ATOM   5698 C  CA  . HIS   D 1 140 ? 29.270  -40.804 -52.653  1.00 20.84 ? 233 HIS   D CA  1 
ATOM   5699 C  C   . HIS   D 1 140 ? 28.271  -39.749 -53.144  1.00 19.93 ? 233 HIS   D C   1 
ATOM   5700 O  O   . HIS   D 1 140 ? 27.087  -40.091 -53.347  1.00 19.55 ? 233 HIS   D O   1 
ATOM   5701 C  CB  . HIS   D 1 140 ? 29.198  -42.122 -53.434  1.00 21.69 ? 233 HIS   D CB  1 
ATOM   5702 C  CG  . HIS   D 1 140 ? 30.373  -43.021 -53.226  1.00 22.00 ? 233 HIS   D CG  1 
ATOM   5703 N  ND1 . HIS   D 1 140 ? 30.340  -44.363 -53.554  1.00 22.84 ? 233 HIS   D ND1 1 
ATOM   5704 C  CD2 . HIS   D 1 140 ? 31.613  -42.782 -52.746  1.00 22.69 ? 233 HIS   D CD2 1 
ATOM   5705 C  CE1 . HIS   D 1 140 ? 31.509  -44.911 -53.280  1.00 23.15 ? 233 HIS   D CE1 1 
ATOM   5706 N  NE2 . HIS   D 1 140 ? 32.307  -43.960 -52.783  1.00 22.44 ? 233 HIS   D NE2 1 
ATOM   5707 N  N   . TYR   D 1 141 ? 28.737  -38.506 -53.285  1.00 18.50 ? 234 TYR   D N   1 
ATOM   5708 C  CA  . TYR   D 1 141 ? 27.959  -37.363 -53.827  1.00 17.84 ? 234 TYR   D CA  1 
ATOM   5709 C  C   . TYR   D 1 141 ? 28.128  -37.307 -55.350  1.00 18.05 ? 234 TYR   D C   1 
ATOM   5710 O  O   . TYR   D 1 141 ? 29.171  -37.775 -55.876  1.00 17.72 ? 234 TYR   D O   1 
ATOM   5711 C  CB  . TYR   D 1 141 ? 28.376  -36.053 -53.153  1.00 16.91 ? 234 TYR   D CB  1 
ATOM   5712 C  CG  . TYR   D 1 141 ? 27.955  -35.939 -51.711  1.00 16.41 ? 234 TYR   D CG  1 
ATOM   5713 C  CD1 . TYR   D 1 141 ? 26.625  -35.755 -51.364  1.00 16.13 ? 234 TYR   D CD1 1 
ATOM   5714 C  CD2 . TYR   D 1 141 ? 28.883  -36.022 -50.683  1.00 16.35 ? 234 TYR   D CD2 1 
ATOM   5715 C  CE1 . TYR   D 1 141 ? 26.227  -35.654 -50.038  1.00 15.83 ? 234 TYR   D CE1 1 
ATOM   5716 C  CE2 . TYR   D 1 141 ? 28.503  -35.923 -49.354  1.00 15.78 ? 234 TYR   D CE2 1 
ATOM   5717 C  CZ  . TYR   D 1 141 ? 27.170  -35.734 -49.027  1.00 16.15 ? 234 TYR   D CZ  1 
ATOM   5718 O  OH  . TYR   D 1 141 ? 26.792  -35.639 -47.713  1.00 14.79 ? 234 TYR   D OH  1 
ATOM   5719 N  N   . ASN   D 1 142 ? 27.104  -36.778 -56.031  1.00 18.58 ? 235 ASN   D N   1 
ATOM   5720 C  CA  . ASN   D 1 142 ? 27.124  -36.401 -57.470  1.00 19.25 ? 235 ASN   D CA  1 
ATOM   5721 C  C   . ASN   D 1 142 ? 26.680  -34.942 -57.594  1.00 18.88 ? 235 ASN   D C   1 
ATOM   5722 O  O   . ASN   D 1 142 ? 25.661  -34.582 -56.973  1.00 18.70 ? 235 ASN   D O   1 
ATOM   5723 C  CB  . ASN   D 1 142 ? 26.190  -37.251 -58.336  1.00 20.48 ? 235 ASN   D CB  1 
ATOM   5724 C  CG  . ASN   D 1 142 ? 26.422  -38.743 -58.243  1.00 21.99 ? 235 ASN   D CG  1 
ATOM   5725 O  OD1 . ASN   D 1 142 ? 25.511  -39.521 -58.523  1.00 24.56 ? 235 ASN   D OD1 1 
ATOM   5726 N  ND2 . ASN   D 1 142 ? 27.627  -39.157 -57.885  1.00 22.06 ? 235 ASN   D ND2 1 
ATOM   5727 N  N   . TYR   D 1 143 ? 27.423  -34.142 -58.356  1.00 18.19 ? 236 TYR   D N   1 
ATOM   5728 C  CA  . TYR   D 1 143 ? 27.067  -32.753 -58.737  1.00 18.00 ? 236 TYR   D CA  1 
ATOM   5729 C  C   . TYR   D 1 143 ? 26.576  -32.765 -60.192  1.00 17.92 ? 236 TYR   D C   1 
ATOM   5730 O  O   . TYR   D 1 143 ? 27.307  -33.247 -61.081  1.00 18.14 ? 236 TYR   D O   1 
ATOM   5731 C  CB  . TYR   D 1 143 ? 28.261  -31.827 -58.503  1.00 17.40 ? 236 TYR   D CB  1 
ATOM   5732 C  CG  . TYR   D 1 143 ? 28.675  -31.704 -57.058  1.00 17.34 ? 236 TYR   D CG  1 
ATOM   5733 C  CD1 . TYR   D 1 143 ? 29.447  -32.680 -56.446  1.00 17.32 ? 236 TYR   D CD1 1 
ATOM   5734 C  CD2 . TYR   D 1 143 ? 28.310  -30.600 -56.305  1.00 17.16 ? 236 TYR   D CD2 1 
ATOM   5735 C  CE1 . TYR   D 1 143 ? 29.841  -32.565 -55.121  1.00 17.53 ? 236 TYR   D CE1 1 
ATOM   5736 C  CE2 . TYR   D 1 143 ? 28.689  -30.472 -54.978  1.00 17.60 ? 236 TYR   D CE2 1 
ATOM   5737 C  CZ  . TYR   D 1 143 ? 29.460  -31.456 -54.383  1.00 17.63 ? 236 TYR   D CZ  1 
ATOM   5738 O  OH  . TYR   D 1 143 ? 29.836  -31.319 -53.079  1.00 17.87 ? 236 TYR   D OH  1 
ATOM   5739 N  N   . MET   D 1 144 ? 25.364  -32.258 -60.420  1.00 18.06 ? 237 MET   D N   1 
ATOM   5740 C  CA  . MET   D 1 144 ? 24.541  -32.557 -61.625  1.00 18.34 ? 237 MET   D CA  1 
ATOM   5741 C  C   . MET   D 1 144 ? 24.428  -31.328 -62.535  1.00 18.58 ? 237 MET   D C   1 
ATOM   5742 O  O   . MET   D 1 144 ? 23.498  -31.281 -63.373  1.00 18.92 ? 237 MET   D O   1 
ATOM   5743 C  CB  . MET   D 1 144 ? 23.146  -33.009 -61.189  1.00 18.29 ? 237 MET   D CB  1 
ATOM   5744 C  CG  . MET   D 1 144 ? 23.172  -34.178 -60.218  1.00 18.14 ? 237 MET   D CG  1 
ATOM   5745 S  SD  . MET   D 1 144 ? 24.029  -35.633 -60.873  1.00 18.69 ? 237 MET   D SD  1 
ATOM   5746 C  CE  . MET   D 1 144 ? 23.188  -35.809 -62.448  1.00 18.55 ? 237 MET   D CE  1 
ATOM   5747 N  N   . CYS   D 1 145 ? 25.346  -30.376 -62.393  1.00 18.99 ? 238 CYS   D N   1 
ATOM   5748 C  CA  . CYS   D 1 145 ? 25.414  -29.134 -63.205  1.00 19.22 ? 238 CYS   D CA  1 
ATOM   5749 C  C   . CYS   D 1 145 ? 26.850  -28.608 -63.118  1.00 18.72 ? 238 CYS   D C   1 
ATOM   5750 O  O   . CYS   D 1 145 ? 27.474  -28.784 -62.047  1.00 17.88 ? 238 CYS   D O   1 
ATOM   5751 C  CB  . CYS   D 1 145 ? 24.388  -28.135 -62.687  1.00 20.39 ? 238 CYS   D CB  1 
ATOM   5752 S  SG  . CYS   D 1 145 ? 24.039  -26.722 -63.685  1.00 21.99 ? 238 CYS   D SG  1 
ATOM   5753 N  N   . ASN   D 1 146 ? 27.372  -28.033 -64.204  1.00 18.20 ? 239 ASN   D N   1 
ATOM   5754 C  CA  . ASN   D 1 146 ? 28.768  -27.521 -64.271  1.00 18.36 ? 239 ASN   D CA  1 
ATOM   5755 C  C   . ASN   D 1 146 ? 28.834  -26.123 -63.659  1.00 18.07 ? 239 ASN   D C   1 
ATOM   5756 O  O   . ASN   D 1 146 ? 27.836  -25.395 -63.759  1.00 17.60 ? 239 ASN   D O   1 
ATOM   5757 C  CB  . ASN   D 1 146 ? 29.301  -27.511 -65.704  1.00 18.60 ? 239 ASN   D CB  1 
ATOM   5758 C  CG  . ASN   D 1 146 ? 29.558  -28.911 -66.208  1.00 19.05 ? 239 ASN   D CG  1 
ATOM   5759 O  OD1 . ASN   D 1 146 ? 30.146  -29.720 -65.495  1.00 19.88 ? 239 ASN   D OD1 1 
ATOM   5760 N  ND2 . ASN   D 1 146 ? 29.116  -29.207 -67.418  1.00 18.89 ? 239 ASN   D ND2 1 
ATOM   5761 N  N   . SER   D 1 147 ? 29.966  -25.778 -63.037  1.00 17.91 ? 240 SER   D N   1 
ATOM   5762 C  CA  . SER   D 1 147 ? 30.256  -24.421 -62.504  1.00 18.39 ? 240 SER   D CA  1 
ATOM   5763 C  C   . SER   D 1 147 ? 30.026  -23.370 -63.601  1.00 19.36 ? 240 SER   D C   1 
ATOM   5764 O  O   . SER   D 1 147 ? 29.509  -22.292 -63.275  1.00 19.30 ? 240 SER   D O   1 
ATOM   5765 C  CB  . SER   D 1 147 ? 31.661  -24.335 -61.954  1.00 18.47 ? 240 SER   D CB  1 
ATOM   5766 O  OG  . SER   D 1 147 ? 31.783  -25.093 -60.764  1.00 17.89 ? 240 SER   D OG  1 
ATOM   5767 N  N   . SER   D 1 148 ? 30.373  -23.689 -64.854  1.00 20.71 ? 241 SER   D N   1 
ATOM   5768 C  CA  . SER   D 1 148 ? 30.387  -22.743 -66.004  1.00 22.21 ? 241 SER   D CA  1 
ATOM   5769 C  C   . SER   D 1 148 ? 28.980  -22.533 -66.583  1.00 23.00 ? 241 SER   D C   1 
ATOM   5770 O  O   . SER   D 1 148 ? 28.821  -21.614 -67.411  1.00 24.23 ? 241 SER   D O   1 
ATOM   5771 C  CB  . SER   D 1 148 ? 31.333  -23.225 -67.071  1.00 22.51 ? 241 SER   D CB  1 
ATOM   5772 O  OG  . SER   D 1 148 ? 30.895  -24.464 -67.601  1.00 22.07 ? 241 SER   D OG  1 
ATOM   5773 N  N   . CYS   D 1 149 ? 28.003  -23.353 -66.192  1.00 23.34 ? 242 CYS   D N   1 
ATOM   5774 C  CA  . CYS   D 1 149 ? 26.657  -23.402 -66.823  1.00 24.38 ? 242 CYS   D CA  1 
ATOM   5775 C  C   . CYS   D 1 149 ? 26.011  -22.011 -66.811  1.00 25.77 ? 242 CYS   D C   1 
ATOM   5776 O  O   . CYS   D 1 149 ? 25.695  -21.502 -65.713  1.00 24.94 ? 242 CYS   D O   1 
ATOM   5777 C  CB  . CYS   D 1 149 ? 25.739  -24.394 -66.122  1.00 22.94 ? 242 CYS   D CB  1 
ATOM   5778 S  SG  . CYS   D 1 149 ? 25.863  -26.013 -66.796  1.00 23.06 ? 242 CYS   D SG  1 
ATOM   5779 N  N   . MET   D 1 150 ? 25.841  -21.418 -67.994  1.00 29.07 ? 243 MET   D N   1 
ATOM   5780 C  CA  . MET   D 1 150 ? 24.958  -20.244 -68.193  1.00 32.61 ? 243 MET   D CA  1 
ATOM   5781 C  C   . MET   D 1 150 ? 23.531  -20.676 -67.836  1.00 32.31 ? 243 MET   D C   1 
ATOM   5782 O  O   . MET   D 1 150 ? 23.123  -21.784 -68.254  1.00 35.70 ? 243 MET   D O   1 
ATOM   5783 C  CB  . MET   D 1 150 ? 24.992  -19.732 -69.637  1.00 35.47 ? 243 MET   D CB  1 
ATOM   5784 C  CG  . MET   D 1 150 ? 26.115  -18.756 -69.909  1.00 38.22 ? 243 MET   D CG  1 
ATOM   5785 S  SD  . MET   D 1 150 ? 26.143  -18.206 -71.638  1.00 42.91 ? 243 MET   D SD  1 
ATOM   5786 C  CE  . MET   D 1 150 ? 24.651  -17.212 -71.687  1.00 41.53 ? 243 MET   D CE  1 
ATOM   5787 N  N   . GLY   D 1 151 ? 22.819  -19.843 -67.077  1.00 31.11 ? 244 GLY   D N   1 
ATOM   5788 C  CA  . GLY   D 1 151 ? 21.461  -20.128 -66.579  1.00 29.67 ? 244 GLY   D CA  1 
ATOM   5789 C  C   . GLY   D 1 151 ? 21.473  -20.707 -65.175  1.00 28.11 ? 244 GLY   D C   1 
ATOM   5790 O  O   . GLY   D 1 151 ? 20.378  -20.820 -64.587  1.00 27.55 ? 244 GLY   D O   1 
ATOM   5791 N  N   . GLY   D 1 152 ? 22.658  -21.051 -64.651  1.00 26.52 ? 245 GLY   D N   1 
ATOM   5792 C  CA  . GLY   D 1 152 ? 22.840  -21.613 -63.297  1.00 25.91 ? 245 GLY   D CA  1 
ATOM   5793 C  C   . GLY   D 1 152 ? 23.954  -20.918 -62.534  1.00 24.95 ? 245 GLY   D C   1 
ATOM   5794 O  O   . GLY   D 1 152 ? 23.891  -19.684 -62.384  1.00 24.97 ? 245 GLY   D O   1 
ATOM   5795 N  N   . MET   D 1 153 ? 24.947  -21.679 -62.067  1.00 24.09 ? 246 MET   D N   1 
ATOM   5796 C  CA  . MET   D 1 153 ? 26.084  -21.153 -61.263  1.00 23.44 ? 246 MET   D CA  1 
ATOM   5797 C  C   . MET   D 1 153 ? 26.871  -20.121 -62.084  1.00 22.93 ? 246 MET   D C   1 
ATOM   5798 O  O   . MET   D 1 153 ? 27.313  -19.130 -61.487  1.00 22.52 ? 246 MET   D O   1 
ATOM   5799 C  CB  . MET   D 1 153 ? 26.999  -22.288 -60.793  1.00 22.45 ? 246 MET   D CB  1 
ATOM   5800 C  CG  . MET   D 1 153 ? 26.371  -23.112 -59.681  1.00 22.30 ? 246 MET   D CG  1 
ATOM   5801 S  SD  . MET   D 1 153 ? 27.374  -24.526 -59.157  1.00 21.34 ? 246 MET   D SD  1 
ATOM   5802 C  CE  . MET   D 1 153 ? 27.087  -25.650 -60.522  1.00 21.59 ? 246 MET   D CE  1 
ATOM   5803 N  N   . ASN   D 1 154 ? 27.018  -20.333 -63.397  1.00 24.35 ? 247 ASN   D N   1 
ATOM   5804 C  CA  . ASN   D 1 154 ? 27.561  -19.328 -64.355  1.00 25.34 ? 247 ASN   D CA  1 
ATOM   5805 C  C   . ASN   D 1 154 ? 28.935  -18.841 -63.875  1.00 25.02 ? 247 ASN   D C   1 
ATOM   5806 O  O   . ASN   D 1 154 ? 29.133  -17.613 -63.797  1.00 23.19 ? 247 ASN   D O   1 
ATOM   5807 C  CB  . ASN   D 1 154 ? 26.587  -18.158 -64.537  1.00 26.82 ? 247 ASN   D CB  1 
ATOM   5808 C  CG  . ASN   D 1 154 ? 26.955  -17.242 -65.687  1.00 27.59 ? 247 ASN   D CG  1 
ATOM   5809 O  OD1 . ASN   D 1 154 ? 27.525  -17.677 -66.683  1.00 29.42 ? 247 ASN   D OD1 1 
ATOM   5810 N  ND2 . ASN   D 1 154 ? 26.633  -15.967 -65.558  1.00 28.84 ? 247 ASN   D ND2 1 
ATOM   5811 N  N   . ARG   D 1 155 ? 29.818  -19.785 -63.527  1.00 25.09 ? 248 ARG   D N   1 
ATOM   5812 C  CA  . ARG   D 1 155 ? 31.245  -19.581 -63.145  1.00 26.52 ? 248 ARG   D CA  1 
ATOM   5813 C  C   . ARG   D 1 155 ? 31.368  -19.011 -61.724  1.00 25.87 ? 248 ARG   D C   1 
ATOM   5814 O  O   . ARG   D 1 155 ? 32.513  -18.754 -61.298  1.00 26.52 ? 248 ARG   D O   1 
ATOM   5815 C  CB  . ARG   D 1 155 ? 31.960  -18.685 -64.163  1.00 27.97 ? 248 ARG   D CB  1 
ATOM   5816 C  CG  . ARG   D 1 155 ? 31.837  -19.186 -65.595  1.00 29.75 ? 248 ARG   D CG  1 
ATOM   5817 C  CD  . ARG   D 1 155 ? 32.609  -18.366 -66.615  1.00 32.10 ? 248 ARG   D CD  1 
ATOM   5818 N  NE  . ARG   D 1 155 ? 32.475  -18.951 -67.945  1.00 33.54 ? 248 ARG   D NE  1 
ATOM   5819 C  CZ  . ARG   D 1 155 ? 33.121  -20.033 -68.380  1.00 35.22 ? 248 ARG   D CZ  1 
ATOM   5820 N  NH1 . ARG   D 1 155 ? 33.977  -20.674 -67.601  1.00 36.11 ? 248 ARG   D NH1 1 
ATOM   5821 N  NH2 . ARG   D 1 155 ? 32.910  -20.472 -69.609  1.00 37.40 ? 248 ARG   D NH2 1 
ATOM   5822 N  N   . ARG   D 1 156 ? 30.262  -18.834 -60.995  1.00 24.60 ? 249 ARG   D N   1 
ATOM   5823 C  CA  . ARG   D 1 156 ? 30.318  -18.359 -59.587  1.00 24.04 ? 249 ARG   D CA  1 
ATOM   5824 C  C   . ARG   D 1 156 ? 30.723  -19.535 -58.703  1.00 22.83 ? 249 ARG   D C   1 
ATOM   5825 O  O   . ARG   D 1 156 ? 30.127  -20.607 -58.799  1.00 23.35 ? 249 ARG   D O   1 
ATOM   5826 C  CB  . ARG   D 1 156 ? 28.981  -17.748 -59.156  1.00 24.72 ? 249 ARG   D CB  1 
ATOM   5827 C  CG  . ARG   D 1 156 ? 28.590  -16.505 -59.943  1.00 25.19 ? 249 ARG   D CG  1 
ATOM   5828 C  CD  . ARG   D 1 156 ? 27.182  -16.051 -59.618  1.00 26.23 ? 249 ARG   D CD  1 
ATOM   5829 N  NE  . ARG   D 1 156 ? 26.168  -16.959 -60.139  1.00 26.34 ? 249 ARG   D NE  1 
ATOM   5830 C  CZ  . ARG   D 1 156 ? 24.858  -16.797 -59.986  1.00 26.51 ? 249 ARG   D CZ  1 
ATOM   5831 N  NH1 . ARG   D 1 156 ? 24.392  -15.755 -59.317  1.00 26.82 ? 249 ARG   D NH1 1 
ATOM   5832 N  NH2 . ARG   D 1 156 ? 24.018  -17.677 -60.504  1.00 26.69 ? 249 ARG   D NH2 1 
ATOM   5833 N  N   . PRO   D 1 157 ? 31.752  -19.385 -57.835  1.00 22.42 ? 250 PRO   D N   1 
ATOM   5834 C  CA  . PRO   D 1 157 ? 32.163  -20.465 -56.937  1.00 21.68 ? 250 PRO   D CA  1 
ATOM   5835 C  C   . PRO   D 1 157 ? 31.100  -20.787 -55.875  1.00 20.59 ? 250 PRO   D C   1 
ATOM   5836 O  O   . PRO   D 1 157 ? 30.406  -19.884 -55.438  1.00 19.66 ? 250 PRO   D O   1 
ATOM   5837 C  CB  . PRO   D 1 157 ? 33.457  -19.952 -56.283  1.00 22.28 ? 250 PRO   D CB  1 
ATOM   5838 C  CG  . PRO   D 1 157 ? 33.400  -18.443 -56.436  1.00 22.52 ? 250 PRO   D CG  1 
ATOM   5839 C  CD  . PRO   D 1 157 ? 32.592  -18.184 -57.691  1.00 22.43 ? 250 PRO   D CD  1 
ATOM   5840 N  N   . ILE   D 1 158 ? 30.998  -22.065 -55.499  1.00 19.80 ? 251 ILE   D N   1 
ATOM   5841 C  CA  . ILE   D 1 158 ? 30.043  -22.561 -54.464  1.00 19.62 ? 251 ILE   D CA  1 
ATOM   5842 C  C   . ILE   D 1 158 ? 30.820  -23.287 -53.365  1.00 19.16 ? 251 ILE   D C   1 
ATOM   5843 O  O   . ILE   D 1 158 ? 31.924  -23.804 -53.639  1.00 18.55 ? 251 ILE   D O   1 
ATOM   5844 C  CB  . ILE   D 1 158 ? 28.961  -23.470 -55.078  1.00 19.46 ? 251 ILE   D CB  1 
ATOM   5845 C  CG1 . ILE   D 1 158 ? 29.569  -24.704 -55.756  1.00 20.38 ? 251 ILE   D CG1 1 
ATOM   5846 C  CG2 . ILE   D 1 158 ? 28.075  -22.673 -56.025  1.00 19.33 ? 251 ILE   D CG2 1 
ATOM   5847 C  CD1 . ILE   D 1 158 ? 28.619  -25.874 -55.873  1.00 20.96 ? 251 ILE   D CD1 1 
ATOM   5848 N  N   . LEU   D 1 159 ? 30.256  -23.281 -52.159  1.00 18.88 ? 252 LEU   D N   1 
ATOM   5849 C  CA  . LEU   D 1 159 ? 30.651  -24.171 -51.045  1.00 18.95 ? 252 LEU   D CA  1 
ATOM   5850 C  C   . LEU   D 1 159 ? 29.586  -25.258 -50.937  1.00 18.33 ? 252 LEU   D C   1 
ATOM   5851 O  O   . LEU   D 1 159 ? 28.404  -24.961 -51.235  1.00 18.36 ? 252 LEU   D O   1 
ATOM   5852 C  CB  . LEU   D 1 159 ? 30.739  -23.380 -49.737  1.00 19.64 ? 252 LEU   D CB  1 
ATOM   5853 C  CG  . LEU   D 1 159 ? 31.577  -22.104 -49.765  1.00 19.83 ? 252 LEU   D CG  1 
ATOM   5854 C  CD1 . LEU   D 1 159 ? 31.697  -21.533 -48.363  1.00 20.07 ? 252 LEU   D CD1 1 
ATOM   5855 C  CD2 . LEU   D 1 159 ? 32.957  -22.353 -50.357  1.00 20.09 ? 252 LEU   D CD2 1 
ATOM   5856 N  N   . THR   D 1 160 ? 30.010  -26.472 -50.594  1.00 17.77 ? 253 THR   D N   1 
ATOM   5857 C  CA  . THR   D 1 160 ? 29.160  -27.541 -50.019  1.00 17.52 ? 253 THR   D CA  1 
ATOM   5858 C  C   . THR   D 1 160 ? 29.315  -27.472 -48.499  1.00 17.88 ? 253 THR   D C   1 
ATOM   5859 O  O   . THR   D 1 160 ? 30.466  -27.571 -48.028  1.00 17.31 ? 253 THR   D O   1 
ATOM   5860 C  CB  . THR   D 1 160 ? 29.544  -28.917 -50.572  1.00 17.29 ? 253 THR   D CB  1 
ATOM   5861 O  OG1 . THR   D 1 160 ? 29.404  -28.856 -51.991  1.00 17.51 ? 253 THR   D OG1 1 
ATOM   5862 C  CG2 . THR   D 1 160 ? 28.697  -30.038 -50.011  1.00 17.13 ? 253 THR   D CG2 1 
ATOM   5863 N  N   . ILE   D 1 161 ? 28.210  -27.274 -47.776  1.00 18.15 ? 254 ILE   D N   1 
ATOM   5864 C  CA  . ILE   D 1 161 ? 28.148  -27.356 -46.287  1.00 18.17 ? 254 ILE   D CA  1 
ATOM   5865 C  C   . ILE   D 1 161 ? 27.691  -28.770 -45.932  1.00 18.48 ? 254 ILE   D C   1 
ATOM   5866 O  O   . ILE   D 1 161 ? 26.607  -29.179 -46.415  1.00 17.70 ? 254 ILE   D O   1 
ATOM   5867 C  CB  . ILE   D 1 161 ? 27.209  -26.290 -45.690  1.00 19.12 ? 254 ILE   D CB  1 
ATOM   5868 C  CG1 . ILE   D 1 161 ? 27.459  -24.908 -46.297  1.00 20.10 ? 254 ILE   D CG1 1 
ATOM   5869 C  CG2 . ILE   D 1 161 ? 27.319  -26.272 -44.170  1.00 19.11 ? 254 ILE   D CG2 1 
ATOM   5870 C  CD1 . ILE   D 1 161 ? 26.452  -23.870 -45.875  1.00 20.92 ? 254 ILE   D CD1 1 
ATOM   5871 N  N   . ILE   D 1 162 ? 28.505  -29.492 -45.156  1.00 18.58 ? 255 ILE   D N   1 
ATOM   5872 C  CA  . ILE   D 1 162 ? 28.141  -30.814 -44.570  1.00 18.94 ? 255 ILE   D CA  1 
ATOM   5873 C  C   . ILE   D 1 162 ? 27.833  -30.600 -43.083  1.00 19.73 ? 255 ILE   D C   1 
ATOM   5874 O  O   . ILE   D 1 162 ? 28.714  -30.104 -42.352  1.00 19.37 ? 255 ILE   D O   1 
ATOM   5875 C  CB  . ILE   D 1 162 ? 29.244  -31.864 -44.794  1.00 18.89 ? 255 ILE   D CB  1 
ATOM   5876 C  CG1 . ILE   D 1 162 ? 29.715  -31.902 -46.251  1.00 19.18 ? 255 ILE   D CG1 1 
ATOM   5877 C  CG2 . ILE   D 1 162 ? 28.778  -33.232 -44.311  1.00 18.90 ? 255 ILE   D CG2 1 
ATOM   5878 C  CD1 . ILE   D 1 162 ? 28.653  -32.325 -47.239  1.00 19.32 ? 255 ILE   D CD1 1 
ATOM   5879 N  N   . THR   D 1 163 ? 26.608  -30.927 -42.670  1.00 19.78 ? 256 THR   D N   1 
ATOM   5880 C  CA  . THR   D 1 163 ? 26.127  -30.791 -41.273  1.00 20.09 ? 256 THR   D CA  1 
ATOM   5881 C  C   . THR   D 1 163 ? 25.765  -32.181 -40.744  1.00 20.00 ? 256 THR   D C   1 
ATOM   5882 O  O   . THR   D 1 163 ? 25.156  -32.968 -41.493  1.00 19.13 ? 256 THR   D O   1 
ATOM   5883 C  CB  . THR   D 1 163 ? 24.952  -29.812 -41.172  1.00 20.43 ? 256 THR   D CB  1 
ATOM   5884 O  OG1 . THR   D 1 163 ? 23.964  -30.226 -42.113  1.00 20.93 ? 256 THR   D OG1 1 
ATOM   5885 C  CG2 . THR   D 1 163 ? 25.344  -28.379 -41.453  1.00 21.16 ? 256 THR   D CG2 1 
ATOM   5886 N  N   . LEU   D 1 164 ? 26.174  -32.471 -39.510  1.00 20.07 ? 257 LEU   D N   1 
ATOM   5887 C  CA  . LEU   D 1 164 ? 25.753  -33.667 -38.742  1.00 20.64 ? 257 LEU   D CA  1 
ATOM   5888 C  C   . LEU   D 1 164 ? 24.606  -33.218 -37.829  1.00 20.79 ? 257 LEU   D C   1 
ATOM   5889 O  O   . LEU   D 1 164 ? 24.792  -32.206 -37.116  1.00 20.30 ? 257 LEU   D O   1 
ATOM   5890 C  CB  . LEU   D 1 164 ? 26.966  -34.183 -37.961  1.00 21.98 ? 257 LEU   D CB  1 
ATOM   5891 C  CG  . LEU   D 1 164 ? 26.896  -35.628 -37.473  1.00 22.78 ? 257 LEU   D CG  1 
ATOM   5892 C  CD1 . LEU   D 1 164 ? 27.058  -36.604 -38.625  1.00 23.15 ? 257 LEU   D CD1 1 
ATOM   5893 C  CD2 . LEU   D 1 164 ? 27.954  -35.885 -36.409  1.00 23.47 ? 257 LEU   D CD2 1 
ATOM   5894 N  N   . GLU   D 1 165 ? 23.443  -33.871 -37.925  1.00 21.27 ? 258 GLU   D N   1 
ATOM   5895 C  CA  . GLU   D 1 165 ? 22.244  -33.578 -37.090  1.00 22.54 ? 258 GLU   D CA  1 
ATOM   5896 C  C   . GLU   D 1 165 ? 21.788  -34.874 -36.411  1.00 22.11 ? 258 GLU   D C   1 
ATOM   5897 O  O   . GLU   D 1 165 ? 21.934  -35.940 -37.033  1.00 21.67 ? 258 GLU   D O   1 
ATOM   5898 C  CB  . GLU   D 1 165 ? 21.066  -33.026 -37.903  1.00 23.54 ? 258 GLU   D CB  1 
ATOM   5899 C  CG  . GLU   D 1 165 ? 21.431  -32.320 -39.195  1.00 24.89 ? 258 GLU   D CG  1 
ATOM   5900 C  CD  . GLU   D 1 165 ? 20.232  -31.876 -40.025  1.00 25.01 ? 258 GLU   D CD  1 
ATOM   5901 O  OE1 . GLU   D 1 165 ? 20.367  -30.889 -40.769  1.00 26.82 ? 258 GLU   D OE1 1 
ATOM   5902 O  OE2 . GLU   D 1 165 ? 19.172  -32.519 -39.938  1.00 24.05 ? 258 GLU   D OE2 1 
ATOM   5903 N  N   . ASP   D 1 166 ? 21.230  -34.790 -35.198  1.00 23.06 ? 259 ASP   D N   1 
ATOM   5904 C  CA  . ASP   D 1 166 ? 20.599  -35.958 -34.526  1.00 23.52 ? 259 ASP   D CA  1 
ATOM   5905 C  C   . ASP   D 1 166 ? 19.218  -36.179 -35.157  1.00 24.03 ? 259 ASP   D C   1 
ATOM   5906 O  O   . ASP   D 1 166 ? 18.824  -35.377 -36.026  1.00 23.18 ? 259 ASP   D O   1 
ATOM   5907 C  CB  . ASP   D 1 166 ? 20.549  -35.798 -33.003  1.00 23.62 ? 259 ASP   D CB  1 
ATOM   5908 C  CG  . ASP   D 1 166 ? 19.609  -34.723 -32.484  1.00 24.24 ? 259 ASP   D CG  1 
ATOM   5909 O  OD1 . ASP   D 1 166 ? 18.852  -34.143 -33.289  1.00 24.35 ? 259 ASP   D OD1 1 
ATOM   5910 O  OD2 . ASP   D 1 166 ? 19.645  -34.470 -31.266  1.00 24.61 ? 259 ASP   D OD2 1 
ATOM   5911 N  N   . SER   D 1 167 ? 18.511  -37.227 -34.729  1.00 24.03 ? 260 SER   D N   1 
ATOM   5912 C  CA  . SER   D 1 167 ? 17.187  -37.643 -35.261  1.00 24.36 ? 260 SER   D CA  1 
ATOM   5913 C  C   . SER   D 1 167 ? 16.127  -36.552 -35.039  1.00 24.02 ? 260 SER   D C   1 
ATOM   5914 O  O   . SER   D 1 167 ? 15.073  -36.644 -35.691  1.00 24.84 ? 260 SER   D O   1 
ATOM   5915 C  CB  . SER   D 1 167 ? 16.757  -38.948 -34.648  1.00 24.74 ? 260 SER   D CB  1 
ATOM   5916 O  OG  . SER   D 1 167 ? 16.659  -38.823 -33.237  1.00 25.36 ? 260 SER   D OG  1 
ATOM   5917 N  N   . SER   D 1 168 ? 16.377  -35.572 -34.159  1.00 23.30 ? 261 SER   D N   1 
ATOM   5918 C  CA  . SER   D 1 168 ? 15.430  -34.476 -33.814  1.00 23.44 ? 261 SER   D CA  1 
ATOM   5919 C  C   . SER   D 1 168 ? 15.792  -33.174 -34.542  1.00 23.33 ? 261 SER   D C   1 
ATOM   5920 O  O   . SER   D 1 168 ? 15.089  -32.174 -34.324  1.00 24.18 ? 261 SER   D O   1 
ATOM   5921 C  CB  . SER   D 1 168 ? 15.365  -34.265 -32.318  1.00 23.86 ? 261 SER   D CB  1 
ATOM   5922 O  OG  . SER   D 1 168 ? 14.873  -35.428 -31.665  1.00 24.39 ? 261 SER   D OG  1 
ATOM   5923 N  N   . GLY   D 1 169 ? 16.837  -33.174 -35.377  1.00 23.19 ? 262 GLY   D N   1 
ATOM   5924 C  CA  . GLY   D 1 169 ? 17.258  -31.990 -36.155  1.00 22.68 ? 262 GLY   D CA  1 
ATOM   5925 C  C   . GLY   D 1 169 ? 18.234  -31.091 -35.408  1.00 22.91 ? 262 GLY   D C   1 
ATOM   5926 O  O   . GLY   D 1 169 ? 18.579  -30.022 -35.957  1.00 23.30 ? 262 GLY   D O   1 
ATOM   5927 N  N   . ASN   D 1 170 ? 18.688  -31.486 -34.212  1.00 22.21 ? 263 ASN   D N   1 
ATOM   5928 C  CA  . ASN   D 1 170 ? 19.691  -30.708 -33.436  1.00 22.38 ? 263 ASN   D CA  1 
ATOM   5929 C  C   . ASN   D 1 170 ? 21.033  -30.759 -34.171  1.00 22.24 ? 263 ASN   D C   1 
ATOM   5930 O  O   . ASN   D 1 170 ? 21.495  -31.865 -34.476  1.00 21.71 ? 263 ASN   D O   1 
ATOM   5931 C  CB  . ASN   D 1 170 ? 19.849  -31.207 -31.997  1.00 21.80 ? 263 ASN   D CB  1 
ATOM   5932 C  CG  . ASN   D 1 170 ? 18.570  -31.085 -31.200  1.00 21.31 ? 263 ASN   D CG  1 
ATOM   5933 O  OD1 . ASN   D 1 170 ? 18.029  -29.991 -31.061  1.00 21.50 ? 263 ASN   D OD1 1 
ATOM   5934 N  ND2 . ASN   D 1 170 ? 18.078  -32.202 -30.691  1.00 20.69 ? 263 ASN   D ND2 1 
ATOM   5935 N  N   . LEU   D 1 171 ? 21.616  -29.592 -34.438  1.00 23.82 ? 264 LEU   D N   1 
ATOM   5936 C  CA  . LEU   D 1 171 ? 22.943  -29.438 -35.090  1.00 25.13 ? 264 LEU   D CA  1 
ATOM   5937 C  C   . LEU   D 1 171 ? 24.034  -30.005 -34.173  1.00 25.37 ? 264 LEU   D C   1 
ATOM   5938 O  O   . LEU   D 1 171 ? 24.154  -29.521 -33.028  1.00 25.64 ? 264 LEU   D O   1 
ATOM   5939 C  CB  . LEU   D 1 171 ? 23.166  -27.949 -35.369  1.00 26.25 ? 264 LEU   D CB  1 
ATOM   5940 C  CG  . LEU   D 1 171 ? 24.461  -27.590 -36.092  1.00 28.11 ? 264 LEU   D CG  1 
ATOM   5941 C  CD1 . LEU   D 1 171 ? 24.497  -28.184 -37.493  1.00 28.75 ? 264 LEU   D CD1 1 
ATOM   5942 C  CD2 . LEU   D 1 171 ? 24.629  -26.080 -36.151  1.00 29.04 ? 264 LEU   D CD2 1 
ATOM   5943 N  N   . LEU   D 1 172 ? 24.798  -30.988 -34.665  1.00 24.40 ? 265 LEU   D N   1 
ATOM   5944 C  CA  . LEU   D 1 172 ? 25.909  -31.645 -33.924  1.00 23.24 ? 265 LEU   D CA  1 
ATOM   5945 C  C   . LEU   D 1 172 ? 27.253  -31.062 -34.374  1.00 23.36 ? 265 LEU   D C   1 
ATOM   5946 O  O   . LEU   D 1 172 ? 28.090  -30.782 -33.496  1.00 22.74 ? 265 LEU   D O   1 
ATOM   5947 C  CB  . LEU   D 1 172 ? 25.850  -33.158 -34.158  1.00 23.23 ? 265 LEU   D CB  1 
ATOM   5948 C  CG  . LEU   D 1 172 ? 24.519  -33.821 -33.805  1.00 23.04 ? 265 LEU   D CG  1 
ATOM   5949 C  CD1 . LEU   D 1 172 ? 24.580  -35.326 -34.022  1.00 22.87 ? 265 LEU   D CD1 1 
ATOM   5950 C  CD2 . LEU   D 1 172 ? 24.117  -33.506 -32.373  1.00 22.75 ? 265 LEU   D CD2 1 
ATOM   5951 N  N   . GLY   D 1 173 ? 27.452  -30.894 -35.686  1.00 22.64 ? 266 GLY   D N   1 
ATOM   5952 C  CA  . GLY   D 1 173 ? 28.726  -30.435 -36.275  1.00 22.28 ? 266 GLY   D CA  1 
ATOM   5953 C  C   . GLY   D 1 173 ? 28.532  -29.883 -37.676  1.00 22.09 ? 266 GLY   D C   1 
ATOM   5954 O  O   . GLY   D 1 173 ? 27.528  -30.248 -38.321  1.00 21.22 ? 266 GLY   D O   1 
ATOM   5955 N  N   . ARG   D 1 174 ? 29.449  -29.024 -38.129  1.00 21.89 ? 267 ARG   D N   1 
ATOM   5956 C  CA  . ARG   D 1 174 ? 29.394  -28.413 -39.482  1.00 22.31 ? 267 ARG   D CA  1 
ATOM   5957 C  C   . ARG   D 1 174 ? 30.805  -28.225 -40.044  1.00 21.87 ? 267 ARG   D C   1 
ATOM   5958 O  O   . ARG   D 1 174 ? 31.667  -27.668 -39.338  1.00 21.31 ? 267 ARG   D O   1 
ATOM   5959 C  CB  . ARG   D 1 174 ? 28.669  -27.066 -39.458  1.00 23.32 ? 267 ARG   D CB  1 
ATOM   5960 C  CG  . ARG   D 1 174 ? 28.445  -26.489 -40.847  1.00 23.96 ? 267 ARG   D CG  1 
ATOM   5961 C  CD  . ARG   D 1 174 ? 27.970  -25.051 -40.851  1.00 25.87 ? 267 ARG   D CD  1 
ATOM   5962 N  NE  . ARG   D 1 174 ? 26.710  -24.861 -40.151  1.00 27.20 ? 267 ARG   D NE  1 
ATOM   5963 C  CZ  . ARG   D 1 174 ? 26.555  -24.282 -38.962  1.00 27.91 ? 267 ARG   D CZ  1 
ATOM   5964 N  NH1 . ARG   D 1 174 ? 27.592  -23.811 -38.288  1.00 28.48 ? 267 ARG   D NH1 1 
ATOM   5965 N  NH2 . ARG   D 1 174 ? 25.342  -24.170 -38.449  1.00 28.74 ? 267 ARG   D NH2 1 
ATOM   5966 N  N   . ASN   D 1 175 ? 30.998  -28.637 -41.297  1.00 21.37 ? 268 ASN   D N   1 
ATOM   5967 C  CA  . ASN   D 1 175 ? 32.231  -28.389 -42.084  1.00 21.19 ? 268 ASN   D CA  1 
ATOM   5968 C  C   . ASN   D 1 175 ? 31.823  -27.963 -43.492  1.00 20.12 ? 268 ASN   D C   1 
ATOM   5969 O  O   . ASN   D 1 175 ? 30.641  -28.116 -43.844  1.00 19.28 ? 268 ASN   D O   1 
ATOM   5970 C  CB  . ASN   D 1 175 ? 33.131  -29.624 -42.113  1.00 22.65 ? 268 ASN   D CB  1 
ATOM   5971 C  CG  . ASN   D 1 175 ? 33.821  -29.863 -40.790  1.00 23.94 ? 268 ASN   D CG  1 
ATOM   5972 O  OD1 . ASN   D 1 175 ? 34.801  -29.201 -40.472  1.00 24.96 ? 268 ASN   D OD1 1 
ATOM   5973 N  ND2 . ASN   D 1 175 ? 33.313  -30.804 -40.013  1.00 24.82 ? 268 ASN   D ND2 1 
ATOM   5974 N  N   . SER   D 1 176 ? 32.772  -27.446 -44.266  1.00 19.04 ? 269 SER   D N   1 
ATOM   5975 C  CA  . SER   D 1 176 ? 32.521  -26.984 -45.651  1.00 17.78 ? 269 SER   D CA  1 
ATOM   5976 C  C   . SER   D 1 176 ? 33.778  -27.151 -46.506  1.00 17.61 ? 269 SER   D C   1 
ATOM   5977 O  O   . SER   D 1 176 ? 34.895  -27.198 -45.948  1.00 16.41 ? 269 SER   D O   1 
ATOM   5978 C  CB  . SER   D 1 176 ? 32.037  -25.567 -45.653  1.00 17.91 ? 269 SER   D CB  1 
ATOM   5979 O  OG  . SER   D 1 176 ? 32.993  -24.714 -45.043  1.00 18.73 ? 269 SER   D OG  1 
ATOM   5980 N  N   . PHE   D 1 177 ? 33.576  -27.222 -47.819  1.00 17.10 ? 270 PHE   D N   1 
ATOM   5981 C  CA  . PHE   D 1 177 ? 34.648  -27.170 -48.844  1.00 17.09 ? 270 PHE   D CA  1 
ATOM   5982 C  C   . PHE   D 1 177 ? 34.100  -26.477 -50.089  1.00 17.32 ? 270 PHE   D C   1 
ATOM   5983 O  O   . PHE   D 1 177 ? 32.888  -26.579 -50.363  1.00 17.78 ? 270 PHE   D O   1 
ATOM   5984 C  CB  . PHE   D 1 177 ? 35.171  -28.572 -49.153  1.00 16.71 ? 270 PHE   D CB  1 
ATOM   5985 C  CG  . PHE   D 1 177 ? 34.111  -29.557 -49.561  1.00 16.74 ? 270 PHE   D CG  1 
ATOM   5986 C  CD1 . PHE   D 1 177 ? 33.390  -30.257 -48.603  1.00 16.55 ? 270 PHE   D CD1 1 
ATOM   5987 C  CD2 . PHE   D 1 177 ? 33.849  -29.807 -50.901  1.00 16.79 ? 270 PHE   D CD2 1 
ATOM   5988 C  CE1 . PHE   D 1 177 ? 32.426  -31.181 -48.974  1.00 16.75 ? 270 PHE   D CE1 1 
ATOM   5989 C  CE2 . PHE   D 1 177 ? 32.875  -30.725 -51.268  1.00 16.80 ? 270 PHE   D CE2 1 
ATOM   5990 C  CZ  . PHE   D 1 177 ? 32.164  -31.403 -50.306  1.00 16.85 ? 270 PHE   D CZ  1 
ATOM   5991 N  N   . GLU   D 1 178 ? 34.974  -25.771 -50.807  1.00 17.77 ? 271 GLU   D N   1 
ATOM   5992 C  CA  . GLU   D 1 178 ? 34.647  -25.165 -52.118  1.00 17.61 ? 271 GLU   D CA  1 
ATOM   5993 C  C   . GLU   D 1 178 ? 34.510  -26.297 -53.137  1.00 17.67 ? 271 GLU   D C   1 
ATOM   5994 O  O   . GLU   D 1 178 ? 35.178  -27.335 -52.960  1.00 17.02 ? 271 GLU   D O   1 
ATOM   5995 C  CB  . GLU   D 1 178 ? 35.718  -24.156 -52.530  1.00 18.10 ? 271 GLU   D CB  1 
ATOM   5996 C  CG  . GLU   D 1 178 ? 35.370  -23.410 -53.804  1.00 18.18 ? 271 GLU   D CG  1 
ATOM   5997 C  CD  . GLU   D 1 178 ? 36.236  -22.202 -54.118  1.00 18.81 ? 271 GLU   D CD  1 
ATOM   5998 O  OE1 . GLU   D 1 178 ? 37.023  -21.786 -53.244  1.00 18.67 ? 271 GLU   D OE1 1 
ATOM   5999 O  OE2 . GLU   D 1 178 ? 36.124  -21.688 -55.251  1.00 18.97 ? 271 GLU   D OE2 1 
ATOM   6000 N  N   . VAL   D 1 179 ? 33.669  -26.111 -54.156  1.00 17.34 ? 272 VAL   D N   1 
ATOM   6001 C  CA  . VAL   D 1 179 ? 33.490  -27.109 -55.246  1.00 18.41 ? 272 VAL   D CA  1 
ATOM   6002 C  C   . VAL   D 1 179 ? 33.522  -26.404 -56.599  1.00 18.57 ? 272 VAL   D C   1 
ATOM   6003 O  O   . VAL   D 1 179 ? 32.892  -25.336 -56.746  1.00 18.59 ? 272 VAL   D O   1 
ATOM   6004 C  CB  . VAL   D 1 179 ? 32.193  -27.927 -55.109  1.00 19.29 ? 272 VAL   D CB  1 
ATOM   6005 C  CG1 . VAL   D 1 179 ? 32.055  -28.918 -56.257  1.00 19.70 ? 272 VAL   D CG1 1 
ATOM   6006 C  CG2 . VAL   D 1 179 ? 32.120  -28.649 -53.776  1.00 19.74 ? 272 VAL   D CG2 1 
ATOM   6007 N  N   A ARG   D 1 180 ? 34.251  -26.999 -57.546  0.50 19.22 ? 273 ARG   D N   1 
ATOM   6008 N  N   B ARG   D 1 180 ? 34.245  -26.998 -57.552  0.50 18.64 ? 273 ARG   D N   1 
ATOM   6009 C  CA  A ARG   D 1 180 ? 34.225  -26.658 -58.989  0.50 19.49 ? 273 ARG   D CA  1 
ATOM   6010 C  CA  B ARG   D 1 180 ? 34.212  -26.642 -58.992  0.50 18.56 ? 273 ARG   D CA  1 
ATOM   6011 C  C   A ARG   D 1 180 ? 33.845  -27.923 -59.762  0.50 19.37 ? 273 ARG   D C   1 
ATOM   6012 C  C   B ARG   D 1 180 ? 33.856  -27.905 -59.781  0.50 18.85 ? 273 ARG   D C   1 
ATOM   6013 O  O   A ARG   D 1 180 ? 34.602  -28.918 -59.685  0.50 19.02 ? 273 ARG   D O   1 
ATOM   6014 O  O   B ARG   D 1 180 ? 34.644  -28.877 -59.738  0.50 18.64 ? 273 ARG   D O   1 
ATOM   6015 C  CB  A ARG   D 1 180 ? 35.579  -26.109 -59.447  0.50 20.54 ? 273 ARG   D CB  1 
ATOM   6016 C  CB  B ARG   D 1 180 ? 35.549  -26.053 -59.451  0.50 18.82 ? 273 ARG   D CB  1 
ATOM   6017 C  CG  A ARG   D 1 180 ? 35.646  -25.788 -60.933  0.50 21.20 ? 273 ARG   D CG  1 
ATOM   6018 C  CG  B ARG   D 1 180 ? 35.551  -25.588 -60.901  0.50 18.73 ? 273 ARG   D CG  1 
ATOM   6019 C  CD  A ARG   D 1 180 ? 37.012  -25.261 -61.334  0.50 21.79 ? 273 ARG   D CD  1 
ATOM   6020 C  CD  B ARG   D 1 180 ? 36.923  -25.127 -61.363  0.50 18.65 ? 273 ARG   D CD  1 
ATOM   6021 N  NE  A ARG   D 1 180 ? 37.206  -25.256 -62.777  0.50 22.74 ? 273 ARG   D NE  1 
ATOM   6022 N  NE  B ARG   D 1 180 ? 36.929  -24.749 -62.770  0.50 18.75 ? 273 ARG   D NE  1 
ATOM   6023 C  CZ  A ARG   D 1 180 ? 36.920  -24.230 -63.569  0.50 23.37 ? 273 ARG   D CZ  1 
ATOM   6024 C  CZ  B ARG   D 1 180 ? 37.943  -24.152 -63.389  0.50 18.65 ? 273 ARG   D CZ  1 
ATOM   6025 N  NH1 A ARG   D 1 180 ? 36.409  -23.122 -63.058  0.50 23.88 ? 273 ARG   D NH1 1 
ATOM   6026 N  NH1 B ARG   D 1 180 ? 39.047  -23.855 -62.725  0.50 18.60 ? 273 ARG   D NH1 1 
ATOM   6027 N  NH2 A ARG   D 1 180 ? 37.130  -24.319 -64.871  0.50 23.52 ? 273 ARG   D NH2 1 
ATOM   6028 N  NH2 B ARG   D 1 180 ? 37.849  -23.853 -64.672  0.50 18.96 ? 273 ARG   D NH2 1 
ATOM   6029 N  N   . VAL   D 1 181 ? 32.693  -27.895 -60.436  1.00 18.81 ? 274 VAL   D N   1 
ATOM   6030 C  CA  . VAL   D 1 181 ? 32.221  -28.997 -61.318  1.00 18.85 ? 274 VAL   D CA  1 
ATOM   6031 C  C   . VAL   D 1 181 ? 32.669  -28.624 -62.734  1.00 18.57 ? 274 VAL   D C   1 
ATOM   6032 O  O   . VAL   D 1 181 ? 32.221  -27.572 -63.237  1.00 18.41 ? 274 VAL   D O   1 
ATOM   6033 C  CB  . VAL   D 1 181 ? 30.698  -29.208 -61.214  1.00 18.57 ? 274 VAL   D CB  1 
ATOM   6034 C  CG1 . VAL   D 1 181 ? 30.265  -30.478 -61.927  1.00 18.57 ? 274 VAL   D CG1 1 
ATOM   6035 C  CG2 . VAL   D 1 181 ? 30.223  -29.229 -59.768  1.00 19.09 ? 274 VAL   D CG2 1 
ATOM   6036 N  N   . CYS   D 1 182 ? 33.564  -29.416 -63.325  1.00 19.20 ? 275 CYS   D N   1 
ATOM   6037 C  CA  . CYS   D 1 182 ? 34.315  -29.039 -64.553  1.00 19.76 ? 275 CYS   D CA  1 
ATOM   6038 C  C   . CYS   D 1 182 ? 34.712  -30.289 -65.345  1.00 20.54 ? 275 CYS   D C   1 
ATOM   6039 O  O   . CYS   D 1 182 ? 34.677  -31.393 -64.776  1.00 20.20 ? 275 CYS   D O   1 
ATOM   6040 C  CB  . CYS   D 1 182 ? 35.535  -28.197 -64.196  1.00 19.79 ? 275 CYS   D CB  1 
ATOM   6041 S  SG  . CYS   D 1 182 ? 36.676  -28.993 -63.033  1.00 20.10 ? 275 CYS   D SG  1 
ATOM   6042 N  N   . ALA   D 1 183 ? 35.078  -30.105 -66.616  1.00 21.47 ? 276 ALA   D N   1 
ATOM   6043 C  CA  . ALA   D 1 183 ? 35.390  -31.192 -67.574  1.00 21.67 ? 276 ALA   D CA  1 
ATOM   6044 C  C   . ALA   D 1 183 ? 36.690  -31.922 -67.194  1.00 21.65 ? 276 ALA   D C   1 
ATOM   6045 O  O   . ALA   D 1 183 ? 36.732  -33.157 -67.337  1.00 21.78 ? 276 ALA   D O   1 
ATOM   6046 C  CB  . ALA   D 1 183 ? 35.464  -30.629 -68.974  1.00 22.44 ? 276 ALA   D CB  1 
ATOM   6047 N  N   A CYS   D 1 184 ? 37.711  -31.195 -66.725  0.50 21.54 ? 277 CYS   D N   1 
ATOM   6048 N  N   B CYS   D 1 184 ? 37.714  -31.189 -66.738  0.50 22.04 ? 277 CYS   D N   1 
ATOM   6049 C  CA  A CYS   D 1 184 ? 39.060  -31.746 -66.410  0.50 21.57 ? 277 CYS   D CA  1 
ATOM   6050 C  CA  B CYS   D 1 184 ? 39.061  -31.730 -66.398  0.50 22.37 ? 277 CYS   D CA  1 
ATOM   6051 C  C   A CYS   D 1 184 ? 39.481  -31.349 -64.996  0.50 21.49 ? 277 CYS   D C   1 
ATOM   6052 C  C   B CYS   D 1 184 ? 39.461  -31.323 -64.985  0.50 21.95 ? 277 CYS   D C   1 
ATOM   6053 O  O   A CYS   D 1 184 ? 40.284  -30.434 -64.823  0.50 21.65 ? 277 CYS   D O   1 
ATOM   6054 O  O   B CYS   D 1 184 ? 40.224  -30.376 -64.802  0.50 22.09 ? 277 CYS   D O   1 
ATOM   6055 C  CB  A CYS   D 1 184 ? 40.089  -31.264 -67.425  0.50 21.88 ? 277 CYS   D CB  1 
ATOM   6056 C  CB  B CYS   D 1 184 ? 40.115  -31.239 -67.379  0.50 23.25 ? 277 CYS   D CB  1 
ATOM   6057 S  SG  A CYS   D 1 184 ? 41.485  -32.400 -67.629  0.50 22.06 ? 277 CYS   D SG  1 
ATOM   6058 S  SG  B CYS   D 1 184 ? 39.788  -31.774 -69.075  0.50 24.68 ? 277 CYS   D SG  1 
ATOM   6059 N  N   . PRO   D 1 185 ? 38.955  -32.030 -63.949  1.00 21.26 ? 278 PRO   D N   1 
ATOM   6060 C  CA  . PRO   D 1 185 ? 39.294  -31.715 -62.559  1.00 21.04 ? 278 PRO   D CA  1 
ATOM   6061 C  C   . PRO   D 1 185 ? 40.796  -31.675 -62.233  1.00 20.13 ? 278 PRO   D C   1 
ATOM   6062 O  O   . PRO   D 1 185 ? 41.205  -30.791 -61.512  1.00 19.58 ? 278 PRO   D O   1 
ATOM   6063 C  CB  . PRO   D 1 185 ? 38.665  -32.875 -61.767  1.00 21.18 ? 278 PRO   D CB  1 
ATOM   6064 C  CG  . PRO   D 1 185 ? 37.547  -33.382 -62.641  1.00 21.05 ? 278 PRO   D CG  1 
ATOM   6065 C  CD  . PRO   D 1 185 ? 38.004  -33.146 -64.063  1.00 21.21 ? 278 PRO   D CD  1 
ATOM   6066 N  N   . GLY   D 1 186 ? 41.565  -32.635 -62.755  1.00 20.76 ? 279 GLY   D N   1 
ATOM   6067 C  CA  . GLY   D 1 186 ? 43.018  -32.751 -62.514  1.00 20.79 ? 279 GLY   D CA  1 
ATOM   6068 C  C   . GLY   D 1 186 ? 43.766  -31.521 -63.003  1.00 21.01 ? 279 GLY   D C   1 
ATOM   6069 O  O   . GLY   D 1 186 ? 44.506  -30.909 -62.203  1.00 19.71 ? 279 GLY   D O   1 
ATOM   6070 N  N   . ARG   D 1 187 ? 43.564  -31.154 -64.270  1.00 22.65 ? 280 ARG   D N   1 
ATOM   6071 C  CA  . ARG   D 1 187 ? 44.201  -29.969 -64.904  1.00 23.79 ? 280 ARG   D CA  1 
ATOM   6072 C  C   . ARG   D 1 187 ? 43.771  -28.702 -64.154  1.00 22.44 ? 280 ARG   D C   1 
ATOM   6073 O  O   . ARG   D 1 187 ? 44.637  -27.848 -63.893  1.00 22.76 ? 280 ARG   D O   1 
ATOM   6074 C  CB  . ARG   D 1 187 ? 43.838  -29.908 -66.392  1.00 26.52 ? 280 ARG   D CB  1 
ATOM   6075 C  CG  . ARG   D 1 187 ? 44.496  -28.768 -67.158  1.00 29.84 ? 280 ARG   D CG  1 
ATOM   6076 C  CD  . ARG   D 1 187 ? 43.720  -28.402 -68.413  1.00 32.25 ? 280 ARG   D CD  1 
ATOM   6077 N  NE  . ARG   D 1 187 ? 42.352  -27.982 -68.109  1.00 34.33 ? 280 ARG   D NE  1 
ATOM   6078 C  CZ  . ARG   D 1 187 ? 41.343  -27.962 -68.977  1.00 35.87 ? 280 ARG   D CZ  1 
ATOM   6079 N  NH1 . ARG   D 1 187 ? 41.524  -28.348 -70.231  1.00 37.50 ? 280 ARG   D NH1 1 
ATOM   6080 N  NH2 . ARG   D 1 187 ? 40.145  -27.563 -68.583  1.00 36.68 ? 280 ARG   D NH2 1 
ATOM   6081 N  N   . ASP   D 1 188 ? 42.486  -28.575 -63.815  1.00 21.41 ? 281 ASP   D N   1 
ATOM   6082 C  CA  . ASP   D 1 188 ? 41.934  -27.342 -63.188  1.00 20.72 ? 281 ASP   D CA  1 
ATOM   6083 C  C   . ASP   D 1 188 ? 42.512  -27.183 -61.777  1.00 19.20 ? 281 ASP   D C   1 
ATOM   6084 O  O   . ASP   D 1 188 ? 42.834  -26.047 -61.418  1.00 17.15 ? 281 ASP   D O   1 
ATOM   6085 C  CB  . ASP   D 1 188 ? 40.404  -27.330 -63.213  1.00 22.10 ? 281 ASP   D CB  1 
ATOM   6086 C  CG  . ASP   D 1 188 ? 39.842  -27.151 -64.614  1.00 23.44 ? 281 ASP   D CG  1 
ATOM   6087 O  OD1 . ASP   D 1 188 ? 40.612  -26.738 -65.506  1.00 24.48 ? 281 ASP   D OD1 1 
ATOM   6088 O  OD2 . ASP   D 1 188 ? 38.651  -27.446 -64.810  1.00 25.64 ? 281 ASP   D OD2 1 
ATOM   6089 N  N   . ARG   D 1 189 ? 42.660  -28.273 -61.015  1.00 18.94 ? 282 ARG   D N   1 
ATOM   6090 C  CA  . ARG   D 1 189 ? 43.307  -28.231 -59.675  1.00 18.91 ? 282 ARG   D CA  1 
ATOM   6091 C  C   . ARG   D 1 189 ? 44.754  -27.733 -59.833  1.00 19.36 ? 282 ARG   D C   1 
ATOM   6092 O  O   . ARG   D 1 189 ? 45.128  -26.788 -59.117  1.00 19.43 ? 282 ARG   D O   1 
ATOM   6093 C  CB  . ARG   D 1 189 ? 43.265  -29.593 -58.976  1.00 18.64 ? 282 ARG   D CB  1 
ATOM   6094 C  CG  . ARG   D 1 189 ? 44.059  -29.623 -57.678  1.00 18.31 ? 282 ARG   D CG  1 
ATOM   6095 C  CD  . ARG   D 1 189 ? 43.882  -30.904 -56.889  1.00 18.08 ? 282 ARG   D CD  1 
ATOM   6096 N  NE  . ARG   D 1 189 ? 44.922  -31.021 -55.873  1.00 17.60 ? 282 ARG   D NE  1 
ATOM   6097 C  CZ  . ARG   D 1 189 ? 45.302  -32.152 -55.287  1.00 17.57 ? 282 ARG   D CZ  1 
ATOM   6098 N  NH1 . ARG   D 1 189 ? 44.721  -33.299 -55.595  1.00 17.17 ? 282 ARG   D NH1 1 
ATOM   6099 N  NH2 . ARG   D 1 189 ? 46.264  -32.131 -54.377  1.00 17.79 ? 282 ARG   D NH2 1 
ATOM   6100 N  N   . ARG   D 1 190 ? 45.540  -28.346 -60.728  1.00 19.70 ? 283 ARG   D N   1 
ATOM   6101 C  CA  . ARG   D 1 190 ? 46.949  -27.939 -60.999  1.00 20.00 ? 283 ARG   D CA  1 
ATOM   6102 C  C   . ARG   D 1 190 ? 46.995  -26.432 -61.292  1.00 20.50 ? 283 ARG   D C   1 
ATOM   6103 O  O   . ARG   D 1 190 ? 47.852  -25.738 -60.710  1.00 20.04 ? 283 ARG   D O   1 
ATOM   6104 C  CB  . ARG   D 1 190 ? 47.548  -28.721 -62.174  1.00 19.89 ? 283 ARG   D CB  1 
ATOM   6105 C  CG  . ARG   D 1 190 ? 47.895  -30.170 -61.868  1.00 19.72 ? 283 ARG   D CG  1 
ATOM   6106 C  CD  . ARG   D 1 190 ? 48.499  -30.872 -63.073  1.00 19.80 ? 283 ARG   D CD  1 
ATOM   6107 N  NE  . ARG   D 1 190 ? 48.393  -32.325 -62.990  1.00 20.07 ? 283 ARG   D NE  1 
ATOM   6108 C  CZ  . ARG   D 1 190 ? 48.740  -33.174 -63.955  1.00 20.16 ? 283 ARG   D CZ  1 
ATOM   6109 N  NH1 . ARG   D 1 190 ? 49.227  -32.723 -65.100  1.00 20.88 ? 283 ARG   D NH1 1 
ATOM   6110 N  NH2 . ARG   D 1 190 ? 48.600  -34.476 -63.773  1.00 19.81 ? 283 ARG   D NH2 1 
ATOM   6111 N  N   . THR   D 1 191 ? 46.101  -25.946 -62.156  1.00 21.60 ? 284 THR   D N   1 
ATOM   6112 C  CA  . THR   D 1 191 ? 46.051  -24.526 -62.603  1.00 22.50 ? 284 THR   D CA  1 
ATOM   6113 C  C   . THR   D 1 191 ? 45.772  -23.619 -61.398  1.00 23.01 ? 284 THR   D C   1 
ATOM   6114 O  O   . THR   D 1 191 ? 46.495  -22.622 -61.234  1.00 22.48 ? 284 THR   D O   1 
ATOM   6115 C  CB  . THR   D 1 191 ? 45.031  -24.343 -63.733  1.00 22.97 ? 284 THR   D CB  1 
ATOM   6116 O  OG1 . THR   D 1 191 ? 45.463  -25.176 -64.808  1.00 22.58 ? 284 THR   D OG1 1 
ATOM   6117 C  CG2 . THR   D 1 191 ? 44.907  -22.911 -64.209  1.00 23.56 ? 284 THR   D CG2 1 
ATOM   6118 N  N   . GLU   D 1 192 ? 44.776  -23.955 -60.574  1.00 23.27 ? 285 GLU   D N   1 
ATOM   6119 C  CA  . GLU   D 1 192 ? 44.344  -23.086 -59.447  1.00 24.05 ? 285 GLU   D CA  1 
ATOM   6120 C  C   . GLU   D 1 192 ? 45.422  -23.079 -58.357  1.00 23.97 ? 285 GLU   D C   1 
ATOM   6121 O  O   . GLU   D 1 192 ? 45.579  -22.032 -57.710  1.00 24.01 ? 285 GLU   D O   1 
ATOM   6122 C  CB  . GLU   D 1 192 ? 42.962  -23.497 -58.939  1.00 24.41 ? 285 GLU   D CB  1 
ATOM   6123 C  CG  . GLU   D 1 192 ? 41.863  -23.177 -59.938  1.00 25.06 ? 285 GLU   D CG  1 
ATOM   6124 C  CD  . GLU   D 1 192 ? 40.463  -23.031 -59.370  1.00 25.88 ? 285 GLU   D CD  1 
ATOM   6125 O  OE1 . GLU   D 1 192 ? 40.327  -22.918 -58.134  1.00 26.56 ? 285 GLU   D OE1 1 
ATOM   6126 O  OE2 . GLU   D 1 192 ? 39.510  -23.024 -60.173  1.00 26.96 ? 285 GLU   D OE2 1 
ATOM   6127 N  N   . GLU   D 1 193 ? 46.164  -24.178 -58.189  1.00 24.10 ? 286 GLU   D N   1 
ATOM   6128 C  CA  . GLU   D 1 193 ? 47.266  -24.274 -57.191  1.00 24.80 ? 286 GLU   D CA  1 
ATOM   6129 C  C   . GLU   D 1 193 ? 48.498  -23.497 -57.679  1.00 27.32 ? 286 GLU   D C   1 
ATOM   6130 O  O   . GLU   D 1 193 ? 49.289  -23.053 -56.818  1.00 26.86 ? 286 GLU   D O   1 
ATOM   6131 C  CB  . GLU   D 1 193 ? 47.597  -25.735 -56.901  1.00 23.77 ? 286 GLU   D CB  1 
ATOM   6132 C  CG  . GLU   D 1 193 ? 46.527  -26.408 -56.065  1.00 23.52 ? 286 GLU   D CG  1 
ATOM   6133 C  CD  . GLU   D 1 193 ? 46.758  -27.877 -55.769  1.00 23.00 ? 286 GLU   D CD  1 
ATOM   6134 O  OE1 . GLU   D 1 193 ? 47.692  -28.451 -56.344  1.00 22.74 ? 286 GLU   D OE1 1 
ATOM   6135 O  OE2 . GLU   D 1 193 ? 46.000  -28.437 -54.955  1.00 22.26 ? 286 GLU   D OE2 1 
ATOM   6136 N  N   . GLU   D 1 194 ? 48.657  -23.344 -58.999  1.00 30.80 ? 287 GLU   D N   1 
ATOM   6137 C  CA  . GLU   D 1 194 ? 49.783  -22.601 -59.627  1.00 35.04 ? 287 GLU   D CA  1 
ATOM   6138 C  C   . GLU   D 1 194 ? 49.692  -21.119 -59.243  1.00 37.09 ? 287 GLU   D C   1 
ATOM   6139 O  O   . GLU   D 1 194 ? 50.746  -20.481 -59.102  1.00 37.62 ? 287 GLU   D O   1 
ATOM   6140 C  CB  . GLU   D 1 194 ? 49.768  -22.783 -61.148  1.00 36.54 ? 287 GLU   D CB  1 
ATOM   6141 C  CG  . GLU   D 1 194 ? 50.896  -22.053 -61.863  1.00 38.78 ? 287 GLU   D CG  1 
ATOM   6142 C  CD  . GLU   D 1 194 ? 51.106  -22.461 -63.312  1.00 40.02 ? 287 GLU   D CD  1 
ATOM   6143 O  OE1 . GLU   D 1 194 ? 50.150  -22.981 -63.926  1.00 41.09 ? 287 GLU   D OE1 1 
ATOM   6144 O  OE2 . GLU   D 1 194 ? 52.227  -22.255 -63.826  1.00 41.63 ? 287 GLU   D OE2 1 
ATOM   6145 N  N   . ASN   D 1 195 ? 48.474  -20.605 -59.054  1.00 41.72 ? 288 ASN   D N   1 
ATOM   6146 C  CA  . ASN   D 1 195 ? 48.196  -19.164 -58.810  1.00 46.81 ? 288 ASN   D CA  1 
ATOM   6147 C  C   . ASN   D 1 195 ? 48.508  -18.784 -57.355  1.00 49.20 ? 288 ASN   D C   1 
ATOM   6148 O  O   . ASN   D 1 195 ? 48.456  -17.577 -57.057  1.00 50.23 ? 288 ASN   D O   1 
ATOM   6149 C  CB  . ASN   D 1 195 ? 46.755  -18.819 -59.191  1.00 48.88 ? 288 ASN   D CB  1 
ATOM   6150 C  CG  . ASN   D 1 195 ? 46.475  -19.085 -60.655  1.00 51.06 ? 288 ASN   D CG  1 
ATOM   6151 O  OD1 . ASN   D 1 195 ? 45.608  -19.888 -60.989  1.00 53.02 ? 288 ASN   D OD1 1 
ATOM   6152 N  ND2 . ASN   D 1 195 ? 47.221  -18.436 -61.535  1.00 52.30 ? 288 ASN   D ND2 1 
ATOM   6153 N  N   . LEU   D 1 196 ? 48.822  -19.759 -56.491  1.00 52.27 ? 289 LEU   D N   1 
ATOM   6154 C  CA  . LEU   D 1 196 ? 49.287  -19.529 -55.094  1.00 53.00 ? 289 LEU   D CA  1 
ATOM   6155 C  C   . LEU   D 1 196 ? 50.750  -19.069 -55.121  1.00 53.46 ? 289 LEU   D C   1 
ATOM   6156 O  O   . LEU   D 1 196 ? 51.634  -19.795 -55.572  1.00 52.34 ? 289 LEU   D O   1 
ATOM   6157 C  CB  . LEU   D 1 196 ? 49.132  -20.819 -54.280  1.00 54.65 ? 289 LEU   D CB  1 
ATOM   6158 C  CG  . LEU   D 1 196 ? 47.729  -21.427 -54.247  1.00 55.05 ? 289 LEU   D CG  1 
ATOM   6159 C  CD1 . LEU   D 1 196 ? 47.650  -22.548 -53.219  1.00 55.53 ? 289 LEU   D CD1 1 
ATOM   6160 C  CD2 . LEU   D 1 196 ? 46.677  -20.366 -53.960  1.00 55.75 ? 289 LEU   D CD2 1 
HETATM 6161 ZN ZN  . ZN    E 2 .   ? 8.543   -4.530  -89.731  0.80 17.68 ? 301 ZN    A ZN  1 
HETATM 6162 C  C1  . GOL   F 3 .   ? -11.373 -2.321  -63.188  1.00 46.91 ? 302 GOL   A C1  1 
HETATM 6163 O  O1  . GOL   F 3 .   ? -10.257 -3.196  -63.060  1.00 46.35 ? 302 GOL   A O1  1 
HETATM 6164 C  C2  . GOL   F 3 .   ? -11.073 -1.187  -64.143  1.00 46.49 ? 302 GOL   A C2  1 
HETATM 6165 O  O2  . GOL   F 3 .   ? -11.969 -0.105  -63.896  1.00 49.07 ? 302 GOL   A O2  1 
HETATM 6166 C  C3  . GOL   F 3 .   ? -11.151 -1.605  -65.596  1.00 46.15 ? 302 GOL   A C3  1 
HETATM 6167 O  O3  . GOL   F 3 .   ? -10.239 -2.661  -65.884  1.00 45.03 ? 302 GOL   A O3  1 
HETATM 6168 C  C4  . A1LUZ G 4 .   ? 13.015  -2.201  -51.672  1.00 36.33 ? 301 A1LUZ B C4  1 
HETATM 6169 C  C5  . A1LUZ G 4 .   ? 13.753  -1.024  -52.294  1.00 36.91 ? 301 A1LUZ B C5  1 
HETATM 6170 C  C1  . A1LUZ G 4 .   ? 10.412  -2.456  -50.994  1.00 35.62 ? 301 A1LUZ B C1  1 
HETATM 6171 N  N   . A1LUZ G 4 .   ? 9.613   -2.014  -50.099  1.00 35.81 ? 301 A1LUZ B N   1 
HETATM 6172 C  C2  . A1LUZ G 4 .   ? 9.933   -0.991  -49.285  1.00 37.03 ? 301 A1LUZ B C2  1 
HETATM 6173 S  S   . A1LUZ G 4 .   ? 11.472  -0.288  -49.851  1.00 37.00 ? 301 A1LUZ B S   1 
HETATM 6174 C  C3  . A1LUZ G 4 .   ? 11.781  -1.818  -50.799  1.00 36.79 ? 301 A1LUZ B C3  1 
HETATM 6175 O  O1  . A1LUZ G 4 .   ? 10.144  -3.455  -51.851  1.00 35.08 ? 301 A1LUZ B O1  1 
HETATM 6176 O  O2  . A1LUZ G 4 .   ? 13.618  0.241   -51.861  1.00 35.65 ? 301 A1LUZ B O2  1 
HETATM 6177 O  O3  . A1LUZ G 4 .   ? 14.499  -1.232  -53.219  1.00 36.48 ? 301 A1LUZ B O3  1 
HETATM 6178 O  O4  . A1LUZ G 4 .   ? 9.242   -0.547  -48.388  1.00 39.83 ? 301 A1LUZ B O4  1 
HETATM 6179 ZN ZN  . ZN    H 2 .   ? 10.533  -8.692  -46.964  0.80 19.32 ? 302 ZN    B ZN  1 
HETATM 6180 ZN ZN  . ZN    I 2 .   ? 25.728  -31.964 -108.902 0.80 18.62 ? 301 ZN    C ZN  1 
HETATM 6181 C  C1  . GOL   J 3 .   ? 24.506  -25.797 -70.484  1.00 35.58 ? 302 GOL   C C1  1 
HETATM 6182 O  O1  . GOL   J 3 .   ? 25.120  -24.705 -69.807  1.00 33.16 ? 302 GOL   C O1  1 
HETATM 6183 C  C2  . GOL   J 3 .   ? 24.973  -25.900 -71.922  1.00 37.05 ? 302 GOL   C C2  1 
HETATM 6184 O  O2  . GOL   J 3 .   ? 25.492  -24.646 -72.367  1.00 38.02 ? 302 GOL   C O2  1 
HETATM 6185 C  C3  . GOL   J 3 .   ? 26.007  -26.985 -72.138  1.00 37.32 ? 302 GOL   C C3  1 
HETATM 6186 O  O3  . GOL   J 3 .   ? 25.458  -28.286 -71.933  1.00 38.35 ? 302 GOL   C O3  1 
HETATM 6187 C  C4  . A1LUZ K 4 .   ? 21.193  -33.385 -70.837  1.00 34.58 ? 301 A1LUZ D C4  1 
HETATM 6188 C  C5  . A1LUZ K 4 .   ? 20.419  -34.574 -71.379  1.00 35.98 ? 301 A1LUZ D C5  1 
HETATM 6189 C  C1  . A1LUZ K 4 .   ? 23.796  -33.069 -70.249  1.00 34.19 ? 301 A1LUZ D C1  1 
HETATM 6190 N  N   . A1LUZ K 4 .   ? 24.612  -33.461 -69.349  1.00 34.66 ? 301 A1LUZ D N   1 
HETATM 6191 C  C2  . A1LUZ K 4 .   ? 24.336  -34.492 -68.529  1.00 35.22 ? 301 A1LUZ D C2  1 
HETATM 6192 S  S   . A1LUZ K 4 .   ? 22.856  -35.297 -69.125  1.00 34.25 ? 301 A1LUZ D S   1 
HETATM 6193 C  C3  . A1LUZ K 4 .   ? 22.461  -33.753 -70.018  1.00 34.99 ? 301 A1LUZ D C3  1 
HETATM 6194 O  O1  . A1LUZ K 4 .   ? 24.004  -32.076 -71.125  1.00 34.85 ? 301 A1LUZ D O1  1 
HETATM 6195 O  O2  . A1LUZ K 4 .   ? 20.604  -35.827 -70.933  1.00 36.53 ? 301 A1LUZ D O2  1 
HETATM 6196 O  O3  . A1LUZ K 4 .   ? 19.602  -34.378 -72.246  1.00 35.98 ? 301 A1LUZ D O3  1 
HETATM 6197 O  O4  . A1LUZ K 4 .   ? 25.036  -34.890 -67.621  1.00 37.65 ? 301 A1LUZ D O4  1 
HETATM 6198 ZN ZN  . ZN    L 2 .   ? 23.885  -26.974 -66.007  0.80 17.48 ? 302 ZN    D ZN  1 
HETATM 6199 C  C1  . GOL   M 3 .   ? 35.713  -22.799 -46.456  1.00 40.88 ? 303 GOL   D C1  1 
HETATM 6200 O  O1  . GOL   M 3 .   ? 35.191  -24.072 -46.090  1.00 39.34 ? 303 GOL   D O1  1 
HETATM 6201 C  C2  . GOL   M 3 .   ? 36.572  -22.876 -47.701  1.00 41.87 ? 303 GOL   D C2  1 
HETATM 6202 O  O2  . GOL   M 3 .   ? 37.933  -23.092 -47.332  1.00 40.36 ? 303 GOL   D O2  1 
HETATM 6203 C  C3  . GOL   M 3 .   ? 36.479  -21.640 -48.570  1.00 43.65 ? 303 GOL   D C3  1 
HETATM 6204 O  O3  . GOL   M 3 .   ? 36.848  -21.920 -49.919  1.00 46.07 ? 303 GOL   D O3  1 
HETATM 6205 O  O   . HOH   N 5 .   ? -7.477  -7.901  -88.131  1.00 32.27 ? 401 HOH   A O   1 
HETATM 6206 O  O   . HOH   N 5 .   ? 9.512   7.534   -62.607  1.00 36.50 ? 402 HOH   A O   1 
HETATM 6207 O  O   . HOH   N 5 .   ? 13.675  -0.087  -58.753  1.00 13.61 ? 403 HOH   A O   1 
HETATM 6208 O  O   . HOH   N 5 .   ? 13.583  -12.565 -90.538  1.00 35.08 ? 404 HOH   A O   1 
HETATM 6209 O  O   . HOH   N 5 .   ? -16.963 -4.056  -79.500  1.00 27.67 ? 405 HOH   A O   1 
HETATM 6210 O  O   . HOH   N 5 .   ? 2.869   -10.554 -94.587  1.00 35.00 ? 406 HOH   A O   1 
HETATM 6211 O  O   . HOH   N 5 .   ? -11.208 -8.739  -72.158  1.00 25.28 ? 407 HOH   A O   1 
HETATM 6212 O  O   . HOH   N 5 .   ? 17.638  -11.026 -78.944  1.00 24.00 ? 408 HOH   A O   1 
HETATM 6213 O  O   . HOH   N 5 .   ? -1.426  2.427   -60.775  1.00 19.97 ? 409 HOH   A O   1 
HETATM 6214 O  O   . HOH   N 5 .   ? 12.841  -5.175  -61.305  1.00 18.63 ? 410 HOH   A O   1 
HETATM 6215 O  O   . HOH   N 5 .   ? -0.045  -7.178  -57.237  1.00 22.76 ? 411 HOH   A O   1 
HETATM 6216 O  O   . HOH   N 5 .   ? 2.096   1.759   -81.684  1.00 18.85 ? 412 HOH   A O   1 
HETATM 6217 O  O   . HOH   N 5 .   ? 2.385   -13.314 -94.523  1.00 37.80 ? 413 HOH   A O   1 
HETATM 6218 O  O   . HOH   N 5 .   ? -1.987  -12.709 -68.349  1.00 17.56 ? 414 HOH   A O   1 
HETATM 6219 O  O   . HOH   N 5 .   ? -3.910  -17.172 -63.138  1.00 26.64 ? 415 HOH   A O   1 
HETATM 6220 O  O   . HOH   N 5 .   ? 12.102  4.684   -75.559  1.00 14.69 ? 416 HOH   A O   1 
HETATM 6221 O  O   . HOH   N 5 .   ? 7.503   -15.969 -78.417  1.00 17.47 ? 417 HOH   A O   1 
HETATM 6222 O  O   . HOH   N 5 .   ? 2.117   -10.482 -55.454  1.00 35.04 ? 418 HOH   A O   1 
HETATM 6223 O  O   . HOH   N 5 .   ? 8.945   -7.727  -52.709  1.00 34.36 ? 419 HOH   A O   1 
HETATM 6224 O  O   . HOH   N 5 .   ? -10.112 7.084   -76.817  1.00 30.70 ? 420 HOH   A O   1 
HETATM 6225 O  O   . HOH   N 5 .   ? -2.928  -8.398  -50.602  1.00 32.45 ? 421 HOH   A O   1 
HETATM 6226 O  O   . HOH   N 5 .   ? 5.137   2.920   -55.569  1.00 27.00 ? 422 HOH   A O   1 
HETATM 6227 O  O   . HOH   N 5 .   ? -10.097 1.882   -68.738  1.00 20.31 ? 423 HOH   A O   1 
HETATM 6228 O  O   . HOH   N 5 .   ? -12.480 7.555   -79.661  1.00 20.48 ? 424 HOH   A O   1 
HETATM 6229 O  O   . HOH   N 5 .   ? 19.998  -1.745  -70.814  1.00 16.78 ? 425 HOH   A O   1 
HETATM 6230 O  O   . HOH   N 5 .   ? 9.670   -10.215 -65.056  1.00 33.43 ? 426 HOH   A O   1 
HETATM 6231 O  O   . HOH   N 5 .   ? 7.135   -1.248  -69.523  1.00 12.19 ? 427 HOH   A O   1 
HETATM 6232 O  O   . HOH   N 5 .   ? 14.896  3.424   -64.701  1.00 20.59 ? 428 HOH   A O   1 
HETATM 6233 O  O   . HOH   N 5 .   ? -12.212 -0.409  -75.684  1.00 19.50 ? 429 HOH   A O   1 
HETATM 6234 O  O   . HOH   N 5 .   ? -4.403  -12.610 -72.117  1.00 35.89 ? 430 HOH   A O   1 
HETATM 6235 O  O   . HOH   N 5 .   ? 9.850   -12.609 -77.520  1.00 13.71 ? 431 HOH   A O   1 
HETATM 6236 O  O   . HOH   N 5 .   ? -8.752  3.236   -87.302  1.00 25.57 ? 432 HOH   A O   1 
HETATM 6237 O  O   . HOH   N 5 .   ? 1.247   -9.661  -84.961  1.00 26.32 ? 433 HOH   A O   1 
HETATM 6238 O  O   . HOH   N 5 .   ? 1.723   -16.778 -83.209  1.00 19.42 ? 434 HOH   A O   1 
HETATM 6239 O  O   . HOH   N 5 .   ? -5.440  -15.452 -82.306  1.00 36.74 ? 435 HOH   A O   1 
HETATM 6240 O  O   . HOH   N 5 .   ? 13.053  -0.258  -81.565  1.00 17.23 ? 436 HOH   A O   1 
HETATM 6241 O  O   . HOH   N 5 .   ? 10.558  7.291   -73.422  1.00 18.66 ? 437 HOH   A O   1 
HETATM 6242 O  O   . HOH   N 5 .   ? -17.210 -3.171  -82.985  1.00 16.72 ? 438 HOH   A O   1 
HETATM 6243 O  O   . HOH   N 5 .   ? 0.041   0.451   -88.571  1.00 26.68 ? 439 HOH   A O   1 
HETATM 6244 O  O   . HOH   N 5 .   ? 6.292   -12.524 -65.956  1.00 31.43 ? 440 HOH   A O   1 
HETATM 6245 O  O   . HOH   N 5 .   ? 10.289  -12.061 -84.697  1.00 21.31 ? 441 HOH   A O   1 
HETATM 6246 O  O   . HOH   N 5 .   ? -14.517 5.585   -82.251  1.00 20.08 ? 442 HOH   A O   1 
HETATM 6247 O  O   . HOH   N 5 .   ? 13.798  -9.455  -71.829  1.00 14.78 ? 443 HOH   A O   1 
HETATM 6248 O  O   . HOH   N 5 .   ? 12.660  -6.692  -93.943  1.00 22.95 ? 444 HOH   A O   1 
HETATM 6249 O  O   . HOH   N 5 .   ? 9.427   -8.298  -76.520  1.00 11.86 ? 445 HOH   A O   1 
HETATM 6250 O  O   . HOH   N 5 .   ? 8.246   -7.954  -86.459  1.00 35.84 ? 446 HOH   A O   1 
HETATM 6251 O  O   . HOH   N 5 .   ? 6.432   -13.503 -68.256  1.00 22.34 ? 447 HOH   A O   1 
HETATM 6252 O  O   . HOH   N 5 .   ? 5.809   5.815   -68.676  1.00 17.36 ? 448 HOH   A O   1 
HETATM 6253 O  O   . HOH   N 5 .   ? 11.186  -7.124  -79.682  1.00 16.52 ? 449 HOH   A O   1 
HETATM 6254 O  O   . HOH   N 5 .   ? 15.669  -5.109  -67.350  1.00 16.93 ? 450 HOH   A O   1 
HETATM 6255 O  O   . HOH   N 5 .   ? -6.948  -6.944  -66.445  1.00 28.64 ? 451 HOH   A O   1 
HETATM 6256 O  O   . HOH   N 5 .   ? 13.001  -13.822 -70.861  1.00 20.84 ? 452 HOH   A O   1 
HETATM 6257 O  O   . HOH   N 5 .   ? 3.267   -18.370 -72.286  1.00 34.68 ? 453 HOH   A O   1 
HETATM 6258 O  O   . HOH   N 5 .   ? -0.786  -18.028 -75.998  1.00 39.59 ? 454 HOH   A O   1 
HETATM 6259 O  O   . HOH   N 5 .   ? 8.226   6.049   -64.755  1.00 24.65 ? 455 HOH   A O   1 
HETATM 6260 O  O   . HOH   N 5 .   ? -6.082  2.278   -74.510  1.00 20.50 ? 456 HOH   A O   1 
HETATM 6261 O  O   . HOH   N 5 .   ? 11.127  -4.072  -75.930  1.00 12.12 ? 457 HOH   A O   1 
HETATM 6262 O  O   . HOH   N 5 .   ? 13.535  1.478   -63.168  1.00 17.62 ? 458 HOH   A O   1 
HETATM 6263 O  O   . HOH   N 5 .   ? -6.435  -13.198 -73.806  1.00 25.23 ? 459 HOH   A O   1 
HETATM 6264 O  O   . HOH   N 5 .   ? 11.155  -10.224 -77.589  1.00 13.16 ? 460 HOH   A O   1 
HETATM 6265 O  O   . HOH   N 5 .   ? 13.838  -11.208 -69.878  1.00 20.41 ? 461 HOH   A O   1 
HETATM 6266 O  O   . HOH   N 5 .   ? 10.748  -2.727  -54.812  1.00 18.51 ? 462 HOH   A O   1 
HETATM 6267 O  O   . HOH   N 5 .   ? 4.685   6.715   -71.244  1.00 15.80 ? 463 HOH   A O   1 
HETATM 6268 O  O   . HOH   N 5 .   ? 6.715   -8.676  -69.085  1.00 16.88 ? 464 HOH   A O   1 
HETATM 6269 O  O   . HOH   N 5 .   ? 22.699  -6.634  -76.396  1.00 18.43 ? 465 HOH   A O   1 
HETATM 6270 O  O   . HOH   N 5 .   ? -18.835 -6.307  -85.675  1.00 23.97 ? 466 HOH   A O   1 
HETATM 6271 O  O   . HOH   N 5 .   ? -4.346  2.381   -59.842  1.00 20.40 ? 467 HOH   A O   1 
HETATM 6272 O  O   . HOH   N 5 .   ? 13.083  -19.760 -76.613  1.00 36.08 ? 468 HOH   A O   1 
HETATM 6273 O  O   . HOH   N 5 .   ? 18.173  0.786   -71.930  1.00 13.71 ? 469 HOH   A O   1 
HETATM 6274 O  O   . HOH   N 5 .   ? 2.140   -8.683  -54.978  1.00 29.40 ? 470 HOH   A O   1 
HETATM 6275 O  O   . HOH   N 5 .   ? -5.853  -7.524  -70.558  1.00 21.20 ? 471 HOH   A O   1 
HETATM 6276 O  O   . HOH   N 5 .   ? 15.656  -5.869  -63.536  1.00 21.76 ? 472 HOH   A O   1 
HETATM 6277 O  O   . HOH   N 5 .   ? 11.135  -20.102 -75.269  1.00 31.34 ? 473 HOH   A O   1 
HETATM 6278 O  O   . HOH   N 5 .   ? 18.215  -6.101  -79.477  1.00 22.37 ? 474 HOH   A O   1 
HETATM 6279 O  O   . HOH   N 5 .   ? 10.580  2.648   -59.312  1.00 27.54 ? 475 HOH   A O   1 
HETATM 6280 O  O   . HOH   N 5 .   ? 2.051   -19.309 -69.016  1.00 20.02 ? 476 HOH   A O   1 
HETATM 6281 O  O   . HOH   N 5 .   ? 14.215  -16.740 -81.892  1.00 23.10 ? 477 HOH   A O   1 
HETATM 6282 O  O   . HOH   N 5 .   ? -16.199 -1.967  -76.187  1.00 11.77 ? 478 HOH   A O   1 
HETATM 6283 O  O   . HOH   N 5 .   ? 4.741   3.704   -64.315  1.00 17.96 ? 479 HOH   A O   1 
HETATM 6284 O  O   . HOH   N 5 .   ? 14.595  4.020   -60.099  1.00 36.09 ? 480 HOH   A O   1 
HETATM 6285 O  O   . HOH   N 5 .   ? -3.963  -16.754 -67.066  1.00 28.23 ? 481 HOH   A O   1 
HETATM 6286 O  O   . HOH   N 5 .   ? -6.514  -12.842 -76.891  1.00 39.84 ? 482 HOH   A O   1 
HETATM 6287 O  O   . HOH   N 5 .   ? -0.574  8.083   -65.319  1.00 27.26 ? 483 HOH   A O   1 
HETATM 6288 O  O   . HOH   N 5 .   ? -15.599 -6.312  -77.519  1.00 17.17 ? 484 HOH   A O   1 
HETATM 6289 O  O   . HOH   N 5 .   ? -2.494  9.329   -63.889  1.00 26.44 ? 485 HOH   A O   1 
HETATM 6290 O  O   . HOH   N 5 .   ? 17.168  3.262   -72.315  1.00 25.28 ? 486 HOH   A O   1 
HETATM 6291 O  O   . HOH   N 5 .   ? -16.076 5.732   -89.021  1.00 27.26 ? 487 HOH   A O   1 
HETATM 6292 O  O   . HOH   N 5 .   ? 7.269   2.267   -57.264  1.00 25.72 ? 488 HOH   A O   1 
HETATM 6293 O  O   . HOH   N 5 .   ? 19.861  -10.788 -68.607  1.00 25.62 ? 489 HOH   A O   1 
HETATM 6294 O  O   . HOH   N 5 .   ? -10.419 4.904   -69.434  1.00 19.93 ? 490 HOH   A O   1 
HETATM 6295 O  O   . HOH   N 5 .   ? 18.796  -4.067  -81.140  1.00 16.99 ? 491 HOH   A O   1 
HETATM 6296 O  O   . HOH   N 5 .   ? -12.216 1.241   -67.320  1.00 30.73 ? 492 HOH   A O   1 
HETATM 6297 O  O   . HOH   N 5 .   ? -10.558 -1.645  -69.857  1.00 21.35 ? 493 HOH   A O   1 
HETATM 6298 O  O   . HOH   N 5 .   ? 10.024  -5.816  -77.664  1.00 16.49 ? 494 HOH   A O   1 
HETATM 6299 O  O   . HOH   N 5 .   ? -7.415  6.483   -80.538  1.00 34.32 ? 495 HOH   A O   1 
HETATM 6300 O  O   . HOH   N 5 .   ? 3.767   -17.768 -63.171  1.00 9.83  ? 496 HOH   A O   1 
HETATM 6301 O  O   . HOH   N 5 .   ? 6.336   9.647   -67.754  1.00 44.18 ? 497 HOH   A O   1 
HETATM 6302 O  O   . HOH   N 5 .   ? -5.374  -12.136 -69.721  1.00 30.97 ? 498 HOH   A O   1 
HETATM 6303 O  O   . HOH   N 5 .   ? 10.357  11.992  -68.884  1.00 32.49 ? 499 HOH   A O   1 
HETATM 6304 O  O   . HOH   N 5 .   ? 14.694  1.268   -94.136  1.00 41.90 ? 500 HOH   A O   1 
HETATM 6305 O  O   . HOH   N 5 .   ? 11.430  11.120  -72.966  1.00 40.49 ? 501 HOH   A O   1 
HETATM 6306 O  O   . HOH   N 5 .   ? 18.820  -4.581  -57.666  1.00 37.59 ? 502 HOH   A O   1 
HETATM 6307 O  O   . HOH   N 5 .   ? 1.455   -16.502 -55.416  1.00 48.16 ? 503 HOH   A O   1 
HETATM 6308 O  O   . HOH   N 5 .   ? 12.544  -10.496 -67.954  1.00 32.62 ? 504 HOH   A O   1 
HETATM 6309 O  O   . HOH   N 5 .   ? -13.431 2.936   -65.532  1.00 20.58 ? 505 HOH   A O   1 
HETATM 6310 O  O   . HOH   N 5 .   ? -17.125 5.598   -82.345  1.00 20.23 ? 506 HOH   A O   1 
HETATM 6311 O  O   . HOH   N 5 .   ? -7.661  -7.113  -69.025  1.00 32.51 ? 507 HOH   A O   1 
HETATM 6312 O  O   . HOH   N 5 .   ? 13.005  2.157   -60.460  1.00 18.73 ? 508 HOH   A O   1 
HETATM 6313 O  O   . HOH   N 5 .   ? 10.204  12.920  -71.383  1.00 43.99 ? 509 HOH   A O   1 
HETATM 6314 O  O   . HOH   N 5 .   ? 23.222  -8.887  -75.022  1.00 24.31 ? 510 HOH   A O   1 
HETATM 6315 O  O   . HOH   N 5 .   ? -20.024 -5.395  -88.056  1.00 31.60 ? 511 HOH   A O   1 
HETATM 6316 O  O   . HOH   N 5 .   ? 19.157  -20.790 -69.623  1.00 33.93 ? 512 HOH   A O   1 
HETATM 6317 O  O   . HOH   N 5 .   ? 9.577   -9.809  -50.874  1.00 37.66 ? 513 HOH   A O   1 
HETATM 6318 O  O   . HOH   N 5 .   ? 21.127  -4.061  -82.571  1.00 20.72 ? 514 HOH   A O   1 
HETATM 6319 O  O   . HOH   N 5 .   ? 7.445   -11.357 -69.581  1.00 17.49 ? 515 HOH   A O   1 
HETATM 6320 O  O   . HOH   O 5 .   ? -12.301 -0.756  -48.151  1.00 35.92 ? 401 HOH   B O   1 
HETATM 6321 O  O   . HOH   O 5 .   ? 6.438   -5.532  -11.693  1.00 20.33 ? 402 HOH   B O   1 
HETATM 6322 O  O   . HOH   O 5 .   ? -4.950  -10.224 -48.373  1.00 46.52 ? 403 HOH   B O   1 
HETATM 6323 O  O   . HOH   O 5 .   ? 11.555  -11.755 -50.265  1.00 29.36 ? 404 HOH   B O   1 
HETATM 6324 O  O   . HOH   O 5 .   ? 14.796  3.950   -35.776  1.00 19.13 ? 405 HOH   B O   1 
HETATM 6325 O  O   . HOH   O 5 .   ? 4.510   -0.579  -40.197  1.00 18.69 ? 406 HOH   B O   1 
HETATM 6326 O  O   . HOH   O 5 .   ? 16.808  -12.752 -26.673  1.00 28.85 ? 407 HOH   B O   1 
HETATM 6327 O  O   . HOH   O 5 .   ? 2.013   -11.436 -23.299  1.00 21.98 ? 408 HOH   B O   1 
HETATM 6328 O  O   . HOH   O 5 .   ? -5.622  0.354   -34.268  1.00 23.44 ? 409 HOH   B O   1 
HETATM 6329 O  O   . HOH   O 5 .   ? -0.395  8.707   -26.256  1.00 20.04 ? 410 HOH   B O   1 
HETATM 6330 O  O   . HOH   O 5 .   ? 17.245  4.391   -18.472  1.00 22.29 ? 411 HOH   B O   1 
HETATM 6331 O  O   . HOH   O 5 .   ? -14.102 -5.878  -35.840  1.00 21.11 ? 412 HOH   B O   1 
HETATM 6332 O  O   . HOH   O 5 .   ? 12.564  -8.806  -33.121  1.00 14.14 ? 413 HOH   B O   1 
HETATM 6333 O  O   . HOH   O 5 .   ? 12.894  -14.884 -39.898  1.00 20.74 ? 414 HOH   B O   1 
HETATM 6334 O  O   . HOH   O 5 .   ? -2.569  6.771   -28.922  1.00 26.27 ? 415 HOH   B O   1 
HETATM 6335 O  O   . HOH   O 5 .   ? 10.989  7.963   -25.415  1.00 19.96 ? 416 HOH   B O   1 
HETATM 6336 O  O   . HOH   O 5 .   ? 10.118  -11.732 -23.419  1.00 19.85 ? 417 HOH   B O   1 
HETATM 6337 O  O   . HOH   O 5 .   ? -3.396  -7.544  -47.773  1.00 24.55 ? 418 HOH   B O   1 
HETATM 6338 O  O   . HOH   O 5 .   ? 10.778  -16.764 -33.148  1.00 16.23 ? 419 HOH   B O   1 
HETATM 6339 O  O   . HOH   O 5 .   ? -11.401 2.975   -40.629  1.00 22.94 ? 420 HOH   B O   1 
HETATM 6340 O  O   . HOH   O 5 .   ? 17.251  -8.482  -28.592  1.00 19.60 ? 421 HOH   B O   1 
HETATM 6341 O  O   . HOH   O 5 .   ? -7.190  2.556   -27.010  1.00 20.32 ? 422 HOH   B O   1 
HETATM 6342 O  O   . HOH   O 5 .   ? 4.344   10.369  -23.759  1.00 27.47 ? 423 HOH   B O   1 
HETATM 6343 O  O   . HOH   O 5 .   ? -2.497  -6.848  -19.812  1.00 30.64 ? 424 HOH   B O   1 
HETATM 6344 O  O   . HOH   O 5 .   ? 10.311  -0.257  -27.960  1.00 13.91 ? 425 HOH   B O   1 
HETATM 6345 O  O   . HOH   O 5 .   ? 5.390   12.896  -21.406  1.00 23.72 ? 426 HOH   B O   1 
HETATM 6346 O  O   . HOH   O 5 .   ? 15.502  -8.987  -12.351  1.00 32.77 ? 427 HOH   B O   1 
HETATM 6347 O  O   . HOH   O 5 .   ? -8.974  5.415   -38.407  1.00 16.09 ? 428 HOH   B O   1 
HETATM 6348 O  O   . HOH   O 5 .   ? -4.095  2.553   -35.533  1.00 27.59 ? 429 HOH   B O   1 
HETATM 6349 O  O   . HOH   O 5 .   ? 14.154  -8.562  -36.560  1.00 16.04 ? 430 HOH   B O   1 
HETATM 6350 O  O   . HOH   O 5 .   ? 1.782   5.320   -19.907  1.00 22.75 ? 431 HOH   B O   1 
HETATM 6351 O  O   . HOH   O 5 .   ? 1.835   -9.856  -46.264  1.00 18.89 ? 432 HOH   B O   1 
HETATM 6352 O  O   . HOH   O 5 .   ? 13.032  -13.230 -33.060  1.00 17.04 ? 433 HOH   B O   1 
HETATM 6353 O  O   . HOH   O 5 .   ? 18.159  5.736   -25.140  1.00 17.46 ? 434 HOH   B O   1 
HETATM 6354 O  O   . HOH   O 5 .   ? 0.396   -13.118 -38.084  1.00 28.24 ? 435 HOH   B O   1 
HETATM 6355 O  O   . HOH   O 5 .   ? 15.539  -2.301  -40.198  1.00 18.36 ? 436 HOH   B O   1 
HETATM 6356 O  O   . HOH   O 5 .   ? -9.141  -1.239  -33.148  1.00 18.07 ? 437 HOH   B O   1 
HETATM 6357 O  O   . HOH   O 5 .   ? 15.874  -17.347 -27.750  1.00 28.41 ? 438 HOH   B O   1 
HETATM 6358 O  O   . HOH   O 5 .   ? 19.202  6.803   -31.306  1.00 22.77 ? 439 HOH   B O   1 
HETATM 6359 O  O   . HOH   O 5 .   ? -7.824  -8.100  -27.199  1.00 28.01 ? 440 HOH   B O   1 
HETATM 6360 O  O   . HOH   O 5 .   ? 2.342   -3.851  -46.583  1.00 25.92 ? 441 HOH   B O   1 
HETATM 6361 O  O   . HOH   O 5 .   ? -3.170  1.832   -32.914  1.00 23.42 ? 442 HOH   B O   1 
HETATM 6362 O  O   . HOH   O 5 .   ? 13.402  6.957   -34.279  1.00 24.68 ? 443 HOH   B O   1 
HETATM 6363 O  O   . HOH   O 5 .   ? 23.728  -5.038  -39.227  1.00 31.99 ? 444 HOH   B O   1 
HETATM 6364 O  O   . HOH   O 5 .   ? 4.645   -18.904 -36.832  1.00 18.75 ? 445 HOH   B O   1 
HETATM 6365 O  O   . HOH   O 5 .   ? 4.078   -12.653 -40.158  1.00 25.04 ? 446 HOH   B O   1 
HETATM 6366 O  O   . HOH   O 5 .   ? 20.425  4.315   -25.383  1.00 20.90 ? 447 HOH   B O   1 
HETATM 6367 O  O   . HOH   O 5 .   ? 4.335   -3.163  -14.381  1.00 18.61 ? 448 HOH   B O   1 
HETATM 6368 O  O   . HOH   O 5 .   ? 1.384   -9.090  -12.631  1.00 29.51 ? 449 HOH   B O   1 
HETATM 6369 O  O   . HOH   O 5 .   ? 14.183  -9.118  -14.709  1.00 31.72 ? 450 HOH   B O   1 
HETATM 6370 O  O   . HOH   O 5 .   ? 25.578  -7.514  -30.237  1.00 35.24 ? 451 HOH   B O   1 
HETATM 6371 O  O   . HOH   O 5 .   ? -0.645  -9.057  -23.663  1.00 27.22 ? 452 HOH   B O   1 
HETATM 6372 O  O   . HOH   O 5 .   ? 14.241  -10.885 -33.835  1.00 14.73 ? 453 HOH   B O   1 
HETATM 6373 O  O   . HOH   O 5 .   ? 8.166   -5.233  -51.049  1.00 30.69 ? 454 HOH   B O   1 
HETATM 6374 O  O   . HOH   O 5 .   ? 23.052  -0.660  -29.623  1.00 12.10 ? 455 HOH   B O   1 
HETATM 6375 O  O   . HOH   O 5 .   ? 16.838  4.339   -23.057  1.00 20.61 ? 456 HOH   B O   1 
HETATM 6376 O  O   . HOH   O 5 .   ? -7.220  5.627   -36.149  1.00 30.34 ? 457 HOH   B O   1 
HETATM 6377 O  O   . HOH   O 5 .   ? -12.531 -7.364  -33.206  1.00 13.03 ? 458 HOH   B O   1 
HETATM 6378 O  O   . HOH   O 5 .   ? 18.854  -3.138  -25.282  1.00 17.55 ? 459 HOH   B O   1 
HETATM 6379 O  O   . HOH   O 5 .   ? 6.785   7.362   -27.038  1.00 26.44 ? 460 HOH   B O   1 
HETATM 6380 O  O   . HOH   O 5 .   ? 25.509  -6.703  -33.794  1.00 17.09 ? 461 HOH   B O   1 
HETATM 6381 O  O   . HOH   O 5 .   ? 14.011  -4.578  -33.658  1.00 12.17 ? 462 HOH   B O   1 
HETATM 6382 O  O   . HOH   O 5 .   ? 21.023  -11.643 -35.435  1.00 28.72 ? 463 HOH   B O   1 
HETATM 6383 O  O   . HOH   O 5 .   ? -3.274  -13.243 -28.329  1.00 27.85 ? 464 HOH   B O   1 
HETATM 6384 O  O   . HOH   O 5 .   ? 16.603  -1.611  -19.337  1.00 23.17 ? 465 HOH   B O   1 
HETATM 6385 O  O   . HOH   O 5 .   ? 21.011  -7.224  -37.089  1.00 21.16 ? 466 HOH   B O   1 
HETATM 6386 O  O   . HOH   O 5 .   ? 2.747   6.035   -41.860  1.00 32.38 ? 467 HOH   B O   1 
HETATM 6387 O  O   . HOH   O 5 .   ? 2.342   9.421   -25.744  1.00 26.63 ? 468 HOH   B O   1 
HETATM 6388 O  O   . HOH   O 5 .   ? 7.494   6.745   -31.487  1.00 19.48 ? 469 HOH   B O   1 
HETATM 6389 O  O   . HOH   O 5 .   ? 19.202  -2.857  -21.505  1.00 23.43 ? 470 HOH   B O   1 
HETATM 6390 O  O   . HOH   O 5 .   ? 8.681   6.542   -29.049  1.00 20.56 ? 471 HOH   B O   1 
HETATM 6391 O  O   . HOH   O 5 .   ? 12.784  4.078   -40.753  1.00 27.61 ? 472 HOH   B O   1 
HETATM 6392 O  O   . HOH   O 5 .   ? -15.840 -9.436  -40.536  1.00 25.70 ? 473 HOH   B O   1 
HETATM 6393 O  O   . HOH   O 5 .   ? 13.477  6.708   -19.489  1.00 29.94 ? 474 HOH   B O   1 
HETATM 6394 O  O   . HOH   O 5 .   ? 13.478  12.404  -30.480  1.00 36.26 ? 475 HOH   B O   1 
HETATM 6395 O  O   . HOH   O 5 .   ? -3.071  -5.434  -22.495  1.00 26.21 ? 476 HOH   B O   1 
HETATM 6396 O  O   . HOH   O 5 .   ? 10.213  -7.433  -25.538  1.00 14.94 ? 477 HOH   B O   1 
HETATM 6397 O  O   . HOH   O 5 .   ? 10.601  -11.271 -42.994  1.00 25.62 ? 478 HOH   B O   1 
HETATM 6398 O  O   . HOH   O 5 .   ? 22.064  -0.359  -16.242  1.00 27.29 ? 479 HOH   B O   1 
HETATM 6399 O  O   . HOH   O 5 .   ? -7.414  4.977   -28.303  1.00 21.39 ? 480 HOH   B O   1 
HETATM 6400 O  O   . HOH   O 5 .   ? -0.997  5.178   -18.705  1.00 21.72 ? 481 HOH   B O   1 
HETATM 6401 O  O   . HOH   O 5 .   ? 0.090   -15.031 -21.040  1.00 28.18 ? 482 HOH   B O   1 
HETATM 6402 O  O   . HOH   O 5 .   ? 16.773  -16.263 -38.765  1.00 26.02 ? 483 HOH   B O   1 
HETATM 6403 O  O   . HOH   O 5 .   ? -13.256 -2.746  -32.946  1.00 12.91 ? 484 HOH   B O   1 
HETATM 6404 O  O   . HOH   O 5 .   ? -1.576  -6.657  -24.144  1.00 45.16 ? 485 HOH   B O   1 
HETATM 6405 O  O   . HOH   O 5 .   ? 14.171  2.811   -13.891  1.00 26.51 ? 486 HOH   B O   1 
HETATM 6406 O  O   . HOH   O 5 .   ? 17.225  -10.061 -26.377  1.00 23.98 ? 487 HOH   B O   1 
HETATM 6407 O  O   . HOH   O 5 .   ? 7.703   5.960   -24.167  1.00 22.05 ? 488 HOH   B O   1 
HETATM 6408 O  O   . HOH   O 5 .   ? 12.750  -6.599  -34.874  1.00 10.87 ? 489 HOH   B O   1 
HETATM 6409 O  O   . HOH   O 5 .   ? -0.300  -8.442  -48.209  1.00 32.19 ? 490 HOH   B O   1 
HETATM 6410 O  O   . HOH   O 5 .   ? 23.392  -8.685  -25.766  1.00 27.41 ? 491 HOH   B O   1 
HETATM 6411 O  O   . HOH   O 5 .   ? -7.039  -1.516  -27.220  1.00 26.76 ? 492 HOH   B O   1 
HETATM 6412 O  O   . HOH   O 5 .   ? -0.828  -10.005 -14.981  1.00 30.78 ? 493 HOH   B O   1 
HETATM 6413 O  O   . HOH   O 5 .   ? 14.194  -11.819 -50.651  1.00 25.08 ? 494 HOH   B O   1 
HETATM 6414 O  O   . HOH   O 5 .   ? 23.011  1.030   -37.158  1.00 32.15 ? 495 HOH   B O   1 
HETATM 6415 O  O   . HOH   O 5 .   ? 13.702  2.072   -54.318  1.00 33.45 ? 496 HOH   B O   1 
HETATM 6416 O  O   . HOH   O 5 .   ? 6.366   9.808   -35.542  1.00 36.21 ? 497 HOH   B O   1 
HETATM 6417 O  O   . HOH   O 5 .   ? 8.244   -12.061 -51.404  1.00 34.14 ? 498 HOH   B O   1 
HETATM 6418 O  O   . HOH   O 5 .   ? 20.377  3.633   -32.309  1.00 20.11 ? 499 HOH   B O   1 
HETATM 6419 O  O   . HOH   O 5 .   ? 4.182   -23.399 -41.186  1.00 30.59 ? 500 HOH   B O   1 
HETATM 6420 O  O   . HOH   O 5 .   ? 18.198  -0.170  -43.750  1.00 39.81 ? 501 HOH   B O   1 
HETATM 6421 O  O   . HOH   O 5 .   ? 3.790   9.226   -30.426  1.00 42.01 ? 502 HOH   B O   1 
HETATM 6422 O  O   . HOH   O 5 .   ? 22.175  0.287   -33.662  1.00 32.13 ? 503 HOH   B O   1 
HETATM 6423 O  O   . HOH   O 5 .   ? 16.057  -8.536  -24.533  1.00 26.51 ? 504 HOH   B O   1 
HETATM 6424 O  O   . HOH   O 5 .   ? 23.057  -0.192  -39.212  1.00 44.41 ? 505 HOH   B O   1 
HETATM 6425 O  O   . HOH   O 5 .   ? 14.369  7.900   -36.552  1.00 35.40 ? 506 HOH   B O   1 
HETATM 6426 O  O   . HOH   O 5 .   ? 22.785  -14.883 -36.926  1.00 39.44 ? 507 HOH   B O   1 
HETATM 6427 O  O   . HOH   O 5 .   ? 20.458  -4.239  -23.479  1.00 22.77 ? 508 HOH   B O   1 
HETATM 6428 O  O   . HOH   O 5 .   ? -13.959 3.021   -40.908  1.00 17.66 ? 509 HOH   B O   1 
HETATM 6429 O  O   . HOH   O 5 .   ? 14.328  10.179  -35.448  1.00 44.90 ? 510 HOH   B O   1 
HETATM 6430 O  O   . HOH   O 5 .   ? 25.947  -9.141  -31.994  1.00 35.36 ? 511 HOH   B O   1 
HETATM 6431 O  O   . HOH   O 5 .   ? 6.074   8.859   -30.987  1.00 34.46 ? 512 HOH   B O   1 
HETATM 6432 O  O   . HOH   O 5 .   ? 11.229  10.607  -15.672  1.00 49.30 ? 513 HOH   B O   1 
HETATM 6433 O  O   . HOH   O 5 .   ? 15.137  0.824   -56.601  1.00 33.69 ? 514 HOH   B O   1 
HETATM 6434 O  O   . HOH   O 5 .   ? -5.111  -8.513  -24.592  1.00 31.50 ? 515 HOH   B O   1 
HETATM 6435 O  O   . HOH   O 5 .   ? 16.463  5.715   -20.652  1.00 27.93 ? 516 HOH   B O   1 
HETATM 6436 O  O   . HOH   O 5 .   ? 18.348  6.050   -16.597  1.00 34.25 ? 517 HOH   B O   1 
HETATM 6437 O  O   . HOH   O 5 .   ? -3.098  4.951   -37.249  1.00 28.66 ? 518 HOH   B O   1 
HETATM 6438 O  O   . HOH   O 5 .   ? -4.265  -9.630  -21.304  1.00 36.41 ? 519 HOH   B O   1 
HETATM 6439 O  O   . HOH   O 5 .   ? 7.265   10.534  -14.436  1.00 33.41 ? 520 HOH   B O   1 
HETATM 6440 O  O   . HOH   O 5 .   ? -4.204  -13.481 -20.981  1.00 38.64 ? 521 HOH   B O   1 
HETATM 6441 O  O   . HOH   O 5 .   ? 13.137  6.388   -41.949  1.00 41.35 ? 522 HOH   B O   1 
HETATM 6442 O  O   . HOH   O 5 .   ? 11.044  -9.846  -25.433  1.00 20.03 ? 523 HOH   B O   1 
HETATM 6443 O  O   . HOH   O 5 .   ? 13.338  -9.488  -23.897  1.00 30.93 ? 524 HOH   B O   1 
HETATM 6444 O  O   . HOH   O 5 .   ? -5.659  -13.902 -17.977  1.00 33.54 ? 525 HOH   B O   1 
HETATM 6445 O  O   . HOH   P 5 .   ? 25.148  -26.472 -84.067  1.00 29.51 ? 401 HOH   C O   1 
HETATM 6446 O  O   . HOH   P 5 .   ? 51.366  -31.454 -98.749  1.00 34.95 ? 402 HOH   C O   1 
HETATM 6447 O  O   . HOH   P 5 .   ? 17.992  -42.272 -89.575  1.00 34.18 ? 403 HOH   C O   1 
HETATM 6448 O  O   . HOH   P 5 .   ? 22.329  -40.599 -94.740  1.00 14.30 ? 404 HOH   C O   1 
HETATM 6449 O  O   . HOH   P 5 .   ? 36.131  -23.096 -87.743  1.00 20.71 ? 405 HOH   C O   1 
HETATM 6450 O  O   . HOH   P 5 .   ? 43.174  -39.317 -106.399 1.00 25.01 ? 406 HOH   C O   1 
HETATM 6451 O  O   . HOH   P 5 .   ? 35.846  -38.155 -79.762  1.00 18.81 ? 407 HOH   C O   1 
HETATM 6452 O  O   . HOH   P 5 .   ? 40.737  -26.764 -83.740  1.00 29.84 ? 408 HOH   C O   1 
HETATM 6453 O  O   . HOH   P 5 .   ? 20.469  -26.725 -91.113  1.00 12.69 ? 409 HOH   C O   1 
HETATM 6454 O  O   . HOH   P 5 .   ? 26.256  -41.806 -83.843  1.00 21.69 ? 410 HOH   C O   1 
HETATM 6455 O  O   . HOH   P 5 .   ? 32.375  -37.730 -100.695 1.00 17.54 ? 411 HOH   C O   1 
HETATM 6456 O  O   . HOH   P 5 .   ? 21.165  -30.730 -80.497  1.00 22.81 ? 412 HOH   C O   1 
HETATM 6457 O  O   . HOH   P 5 .   ? 33.080  -26.685 -104.103 1.00 25.29 ? 413 HOH   C O   1 
HETATM 6458 O  O   . HOH   P 5 .   ? 26.670  -20.221 -98.116  1.00 18.77 ? 414 HOH   C O   1 
HETATM 6459 O  O   . HOH   P 5 .   ? 34.235  -28.276 -76.584  1.00 18.51 ? 415 HOH   C O   1 
HETATM 6460 O  O   . HOH   P 5 .   ? 37.971  -43.292 -85.064  1.00 22.92 ? 416 HOH   C O   1 
HETATM 6461 O  O   . HOH   P 5 .   ? 45.686  -26.822 -91.122  1.00 27.21 ? 417 HOH   C O   1 
HETATM 6462 O  O   . HOH   P 5 .   ? 24.741  -27.744 -95.806  1.00 12.06 ? 418 HOH   C O   1 
HETATM 6463 O  O   . HOH   P 5 .   ? 53.011  -29.721 -104.753 1.00 21.72 ? 419 HOH   C O   1 
HETATM 6464 O  O   . HOH   P 5 .   ? 23.735  -43.279 -92.474  1.00 15.79 ? 420 HOH   C O   1 
HETATM 6465 O  O   . HOH   P 5 .   ? 44.481  -37.853 -87.911  1.00 18.15 ? 421 HOH   C O   1 
HETATM 6466 O  O   . HOH   P 5 .   ? 28.092  -22.402 -87.254  1.00 29.29 ? 422 HOH   C O   1 
HETATM 6467 O  O   . HOH   P 5 .   ? 20.532  -35.941 -77.854  1.00 13.38 ? 423 HOH   C O   1 
HETATM 6468 O  O   . HOH   P 5 .   ? 24.486  -30.163 -113.462 1.00 30.29 ? 424 HOH   C O   1 
HETATM 6469 O  O   . HOH   P 5 .   ? 48.244  -45.372 -106.913 1.00 34.83 ? 425 HOH   C O   1 
HETATM 6470 O  O   . HOH   P 5 .   ? 24.461  -23.501 -97.059  1.00 15.22 ? 426 HOH   C O   1 
HETATM 6471 O  O   . HOH   P 5 .   ? 46.681  -43.486 -98.686  1.00 18.47 ? 427 HOH   C O   1 
HETATM 6472 O  O   . HOH   P 5 .   ? 23.773  -38.178 -78.496  1.00 21.23 ? 428 HOH   C O   1 
HETATM 6473 O  O   . HOH   P 5 .   ? 13.519  -27.276 -98.433  1.00 29.00 ? 429 HOH   C O   1 
HETATM 6474 O  O   . HOH   P 5 .   ? 14.187  -34.033 -90.005  1.00 18.59 ? 430 HOH   C O   1 
HETATM 6475 O  O   . HOH   P 5 .   ? 40.384  -38.110 -93.622  1.00 21.30 ? 431 HOH   C O   1 
HETATM 6476 O  O   . HOH   P 5 .   ? 46.584  -35.632 -94.900  1.00 21.96 ? 432 HOH   C O   1 
HETATM 6477 O  O   . HOH   P 5 .   ? 19.489  -39.242 -83.840  1.00 16.96 ? 433 HOH   C O   1 
HETATM 6478 O  O   . HOH   P 5 .   ? 24.075  -23.813 -103.904 1.00 22.44 ? 434 HOH   C O   1 
HETATM 6479 O  O   . HOH   P 5 .   ? 29.205  -38.543 -74.752  1.00 29.13 ? 435 HOH   C O   1 
HETATM 6480 O  O   . HOH   P 5 .   ? 38.723  -25.660 -87.521  1.00 23.91 ? 436 HOH   C O   1 
HETATM 6481 O  O   . HOH   P 5 .   ? 27.217  -34.681 -88.669  1.00 15.01 ? 437 HOH   C O   1 
HETATM 6482 O  O   . HOH   P 5 .   ? 49.041  -41.659 -101.245 1.00 17.10 ? 438 HOH   C O   1 
HETATM 6483 O  O   . HOH   P 5 .   ? 21.600  -29.700 -113.067 1.00 32.06 ? 439 HOH   C O   1 
HETATM 6484 O  O   . HOH   P 5 .   ? 51.640  -32.806 -102.132 1.00 18.40 ? 440 HOH   C O   1 
HETATM 6485 O  O   . HOH   P 5 .   ? 32.703  -19.560 -102.736 1.00 20.85 ? 441 HOH   C O   1 
HETATM 6486 O  O   . HOH   P 5 .   ? 38.562  -23.243 -91.622  1.00 32.95 ? 442 HOH   C O   1 
HETATM 6487 O  O   . HOH   P 5 .   ? 32.206  -25.313 -74.839  1.00 21.50 ? 443 HOH   C O   1 
HETATM 6488 O  O   . HOH   P 5 .   ? 22.983  -29.080 -98.959  1.00 13.62 ? 444 HOH   C O   1 
HETATM 6489 O  O   . HOH   P 5 .   ? 23.186  -25.791 -96.951  1.00 16.56 ? 445 HOH   C O   1 
HETATM 6490 O  O   . HOH   P 5 .   ? 11.800  -29.362 -95.493  1.00 15.97 ? 446 HOH   C O   1 
HETATM 6491 O  O   . HOH   P 5 .   ? 28.433  -41.532 -87.761  1.00 21.38 ? 447 HOH   C O   1 
HETATM 6492 O  O   . HOH   P 5 .   ? 20.336  -24.571 -89.293  1.00 20.01 ? 448 HOH   C O   1 
HETATM 6493 O  O   . HOH   P 5 .   ? 21.231  -35.987 -100.864 1.00 24.20 ? 449 HOH   C O   1 
HETATM 6494 O  O   . HOH   P 5 .   ? 42.689  -37.629 -95.690  1.00 33.14 ? 450 HOH   C O   1 
HETATM 6495 O  O   . HOH   P 5 .   ? 27.857  -44.303 -99.119  1.00 28.88 ? 451 HOH   C O   1 
HETATM 6496 O  O   . HOH   P 5 .   ? 23.569  -32.974 -73.828  1.00 18.96 ? 452 HOH   C O   1 
HETATM 6497 O  O   . HOH   P 5 .   ? 27.591  -27.202 -88.348  1.00 13.45 ? 453 HOH   C O   1 
HETATM 6498 O  O   . HOH   P 5 .   ? 29.632  -42.533 -90.220  1.00 16.16 ? 454 HOH   C O   1 
HETATM 6499 O  O   . HOH   P 5 .   ? 17.662  -31.498 -74.408  1.00 38.29 ? 455 HOH   C O   1 
HETATM 6500 O  O   . HOH   P 5 .   ? 20.694  -37.375 -82.253  1.00 17.36 ? 456 HOH   C O   1 
HETATM 6501 O  O   . HOH   P 5 .   ? 23.184  -31.942 -95.080  1.00 13.97 ? 457 HOH   C O   1 
HETATM 6502 O  O   . HOH   P 5 .   ? 18.592  -29.998 -82.918  1.00 21.59 ? 458 HOH   C O   1 
HETATM 6503 O  O   . HOH   P 5 .   ? 40.089  -28.327 -89.780  1.00 24.85 ? 459 HOH   C O   1 
HETATM 6504 O  O   . HOH   P 5 .   ? 22.326  -18.371 -92.484  1.00 36.65 ? 460 HOH   C O   1 
HETATM 6505 O  O   . HOH   P 5 .   ? 20.043  -19.499 -101.279 1.00 23.06 ? 461 HOH   C O   1 
HETATM 6506 O  O   . HOH   P 5 .   ? 18.656  -30.841 -86.533  1.00 16.93 ? 462 HOH   C O   1 
HETATM 6507 O  O   . HOH   P 5 .   ? 33.993  -34.682 -69.381  1.00 34.48 ? 463 HOH   C O   1 
HETATM 6508 O  O   . HOH   P 5 .   ? 24.196  -14.168 -89.610  1.00 34.76 ? 464 HOH   C O   1 
HETATM 6509 O  O   . HOH   P 5 .   ? 38.301  -19.342 -86.823  1.00 26.59 ? 465 HOH   C O   1 
HETATM 6510 O  O   . HOH   P 5 .   ? 52.530  -40.767 -106.416 1.00 25.20 ? 466 HOH   C O   1 
HETATM 6511 O  O   . HOH   P 5 .   ? 34.832  -43.895 -84.459  1.00 22.97 ? 467 HOH   C O   1 
HETATM 6512 O  O   . HOH   P 5 .   ? 21.448  -22.210 -90.254  1.00 26.97 ? 468 HOH   C O   1 
HETATM 6513 O  O   . HOH   P 5 .   ? 50.640  -32.186 -109.190 1.00 38.33 ? 469 HOH   C O   1 
HETATM 6514 O  O   . HOH   P 5 .   ? 29.666  -39.433 -83.361  1.00 16.01 ? 470 HOH   C O   1 
HETATM 6515 O  O   . HOH   P 5 .   ? 16.231  -30.111 -98.684  1.00 24.09 ? 471 HOH   C O   1 
HETATM 6516 O  O   . HOH   P 5 .   ? 30.639  -46.441 -93.623  1.00 46.74 ? 472 HOH   C O   1 
HETATM 6517 O  O   . HOH   P 5 .   ? 15.553  -32.179 -100.475 1.00 21.26 ? 473 HOH   C O   1 
HETATM 6518 O  O   . HOH   P 5 .   ? 44.021  -33.403 -85.070  1.00 32.62 ? 474 HOH   C O   1 
HETATM 6519 O  O   . HOH   P 5 .   ? 49.861  -29.680 -96.696  1.00 20.60 ? 475 HOH   C O   1 
HETATM 6520 O  O   . HOH   P 5 .   ? 35.714  -39.262 -101.084 1.00 29.64 ? 476 HOH   C O   1 
HETATM 6521 O  O   . HOH   P 5 .   ? 38.723  -37.915 -78.942  1.00 22.11 ? 477 HOH   C O   1 
HETATM 6522 O  O   . HOH   P 5 .   ? 25.034  -21.689 -77.918  1.00 40.26 ? 478 HOH   C O   1 
HETATM 6523 O  O   . HOH   P 5 .   ? 41.278  -39.603 -96.243  1.00 32.17 ? 479 HOH   C O   1 
HETATM 6524 O  O   . HOH   P 5 .   ? 24.850  -40.109 -75.444  1.00 39.49 ? 480 HOH   C O   1 
HETATM 6525 O  O   . HOH   P 5 .   ? 22.393  -18.208 -89.677  1.00 42.44 ? 481 HOH   C O   1 
HETATM 6526 O  O   . HOH   P 5 .   ? 17.124  -39.328 -91.485  1.00 20.95 ? 482 HOH   C O   1 
HETATM 6527 O  O   . HOH   P 5 .   ? 44.781  -34.222 -88.938  1.00 18.95 ? 483 HOH   C O   1 
HETATM 6528 O  O   . HOH   P 5 .   ? 50.618  -41.554 -108.133 1.00 24.49 ? 484 HOH   C O   1 
HETATM 6529 O  O   . HOH   P 5 .   ? 27.057  -38.069 -76.457  1.00 26.13 ? 485 HOH   C O   1 
HETATM 6530 O  O   . HOH   P 5 .   ? 41.288  -28.810 -85.682  1.00 28.04 ? 486 HOH   C O   1 
HETATM 6531 O  O   . HOH   P 5 .   ? 37.143  -32.810 -111.004 1.00 35.45 ? 487 HOH   C O   1 
HETATM 6532 O  O   . HOH   P 5 .   ? 30.572  -41.472 -85.394  1.00 30.85 ? 488 HOH   C O   1 
HETATM 6533 O  O   . HOH   P 5 .   ? 24.253  -30.194 -96.866  1.00 11.26 ? 489 HOH   C O   1 
HETATM 6534 O  O   . HOH   P 5 .   ? 14.360  -25.152 -87.882  1.00 26.39 ? 490 HOH   C O   1 
HETATM 6535 O  O   . HOH   P 5 .   ? 44.853  -40.944 -88.569  1.00 28.57 ? 491 HOH   C O   1 
HETATM 6536 O  O   . HOH   P 5 .   ? 40.409  -22.352 -93.241  1.00 32.96 ? 492 HOH   C O   1 
HETATM 6537 O  O   . HOH   P 5 .   ? 46.628  -37.233 -86.484  1.00 26.42 ? 493 HOH   C O   1 
HETATM 6538 O  O   . HOH   P 5 .   ? 52.632  -30.440 -108.932 1.00 32.83 ? 494 HOH   C O   1 
HETATM 6539 O  O   . HOH   P 5 .   ? 39.725  -23.392 -89.264  1.00 29.01 ? 495 HOH   C O   1 
HETATM 6540 O  O   . HOH   P 5 .   ? 21.812  -25.702 -87.446  1.00 33.63 ? 496 HOH   C O   1 
HETATM 6541 O  O   . HOH   P 5 .   ? 19.195  -24.052 -80.023  1.00 36.45 ? 497 HOH   C O   1 
HETATM 6542 O  O   . HOH   P 5 .   ? 57.370  -23.615 -104.609 1.00 43.50 ? 498 HOH   C O   1 
HETATM 6543 O  O   . HOH   P 5 .   ? 14.274  -24.918 -102.318 1.00 37.58 ? 499 HOH   C O   1 
HETATM 6544 O  O   . HOH   P 5 .   ? 41.794  -28.700 -88.264  1.00 37.49 ? 500 HOH   C O   1 
HETATM 6545 O  O   . HOH   P 5 .   ? 51.589  -41.671 -101.421 1.00 22.05 ? 501 HOH   C O   1 
HETATM 6546 O  O   . HOH   P 5 .   ? 30.772  -44.655 -89.335  1.00 41.22 ? 502 HOH   C O   1 
HETATM 6547 O  O   . HOH   P 5 .   ? 11.345  -27.172 -94.396  1.00 26.55 ? 503 HOH   C O   1 
HETATM 6548 O  O   . HOH   P 5 .   ? 43.747  -22.664 -91.941  1.00 48.08 ? 504 HOH   C O   1 
HETATM 6549 O  O   . HOH   P 5 .   ? 24.334  -24.966 -86.691  1.00 33.08 ? 505 HOH   C O   1 
HETATM 6550 O  O   . HOH   P 5 .   ? 26.199  -32.111 -112.860 1.00 26.26 ? 506 HOH   C O   1 
HETATM 6551 O  O   . HOH   P 5 .   ? 21.164  -37.909 -79.629  1.00 17.38 ? 507 HOH   C O   1 
HETATM 6552 O  O   . HOH   P 5 .   ? 31.953  -19.029 -79.906  1.00 43.05 ? 508 HOH   C O   1 
HETATM 6553 O  O   . HOH   P 5 .   ? 44.346  -24.897 -89.984  1.00 43.00 ? 509 HOH   C O   1 
HETATM 6554 O  O   . HOH   P 5 .   ? 42.280  -24.621 -85.275  1.00 36.53 ? 510 HOH   C O   1 
HETATM 6555 O  O   . HOH   P 5 .   ? 43.687  -26.736 -88.415  1.00 36.35 ? 511 HOH   C O   1 
HETATM 6556 O  O   . HOH   P 5 .   ? 26.793  -24.466 -88.852  1.00 19.86 ? 512 HOH   C O   1 
HETATM 6557 O  O   . HOH   P 5 .   ? 45.834  -34.627 -83.950  1.00 34.42 ? 513 HOH   C O   1 
HETATM 6558 O  O   . HOH   Q 5 .   ? 24.186  -18.053 -66.555  1.00 32.36 ? 401 HOH   D O   1 
HETATM 6559 O  O   . HOH   Q 5 .   ? 18.812  -27.775 -31.606  1.00 25.78 ? 402 HOH   D O   1 
HETATM 6560 O  O   . HOH   Q 5 .   ? 19.710  -40.047 -55.215  1.00 18.61 ? 403 HOH   D O   1 
HETATM 6561 O  O   . HOH   Q 5 .   ? 14.931  -43.179 -50.362  1.00 23.19 ? 404 HOH   D O   1 
HETATM 6562 O  O   . HOH   Q 5 .   ? 37.154  -19.519 -55.634  1.00 26.91 ? 405 HOH   D O   1 
HETATM 6563 O  O   . HOH   Q 5 .   ? 37.799  -28.144 -67.022  1.00 24.75 ? 406 HOH   D O   1 
HETATM 6564 O  O   . HOH   Q 5 .   ? 48.450  -30.505 -55.109  1.00 18.29 ? 407 HOH   D O   1 
HETATM 6565 O  O   . HOH   Q 5 .   ? 29.303  -19.062 -48.982  1.00 43.27 ? 408 HOH   D O   1 
HETATM 6566 O  O   . HOH   Q 5 .   ? 21.828  -27.369 -52.219  1.00 13.24 ? 409 HOH   D O   1 
HETATM 6567 O  O   . HOH   Q 5 .   ? 37.392  -51.407 -38.409  1.00 33.28 ? 410 HOH   D O   1 
HETATM 6568 O  O   . HOH   Q 5 .   ? 20.554  -38.142 -69.874  1.00 37.70 ? 411 HOH   D O   1 
HETATM 6569 O  O   . HOH   Q 5 .   ? 34.883  -45.065 -45.743  1.00 27.57 ? 412 HOH   D O   1 
HETATM 6570 O  O   . HOH   Q 5 .   ? 16.998  -40.706 -37.671  1.00 22.30 ? 413 HOH   D O   1 
HETATM 6571 O  O   . HOH   Q 5 .   ? 30.484  -23.134 -59.039  1.00 18.09 ? 414 HOH   D O   1 
HETATM 6572 O  O   . HOH   Q 5 .   ? 23.580  -19.413 -51.975  1.00 19.32 ? 415 HOH   D O   1 
HETATM 6573 O  O   . HOH   Q 5 .   ? 24.417  -24.682 -42.517  1.00 21.73 ? 416 HOH   D O   1 
HETATM 6574 O  O   . HOH   Q 5 .   ? 31.520  -17.816 -48.282  1.00 31.35 ? 417 HOH   D O   1 
HETATM 6575 O  O   . HOH   Q 5 .   ? 43.766  -34.861 -52.602  1.00 23.46 ? 418 HOH   D O   1 
HETATM 6576 O  O   . HOH   Q 5 .   ? 17.472  -16.199 -49.912  1.00 39.81 ? 419 HOH   D O   1 
HETATM 6577 O  O   . HOH   Q 5 .   ? 27.870  -30.611 -30.922  1.00 32.00 ? 420 HOH   D O   1 
HETATM 6578 O  O   . HOH   Q 5 .   ? 32.413  -41.898 -39.203  1.00 27.48 ? 421 HOH   D O   1 
HETATM 6579 O  O   . HOH   Q 5 .   ? 23.434  -36.083 -65.872  1.00 28.81 ? 422 HOH   D O   1 
HETATM 6580 O  O   . HOH   Q 5 .   ? 30.077  -33.106 -33.605  1.00 26.59 ? 423 HOH   D O   1 
HETATM 6581 O  O   . HOH   Q 5 .   ? 26.118  -30.720 -70.333  1.00 24.76 ? 424 HOH   D O   1 
HETATM 6582 O  O   . HOH   Q 5 .   ? 45.706  -39.250 -59.972  1.00 18.85 ? 425 HOH   D O   1 
HETATM 6583 O  O   . HOH   Q 5 .   ? 43.428  -41.642 -57.886  1.00 20.78 ? 426 HOH   D O   1 
HETATM 6584 O  O   . HOH   Q 5 .   ? 12.813  -31.598 -65.564  1.00 27.08 ? 427 HOH   D O   1 
HETATM 6585 O  O   . HOH   Q 5 .   ? 37.573  -37.907 -52.239  1.00 19.37 ? 428 HOH   D O   1 
HETATM 6586 O  O   . HOH   Q 5 .   ? 18.940  -33.546 -59.439  1.00 15.51 ? 429 HOH   D O   1 
HETATM 6587 O  O   . HOH   Q 5 .   ? 31.969  -31.615 -65.857  1.00 28.41 ? 430 HOH   D O   1 
HETATM 6588 O  O   . HOH   Q 5 .   ? 20.342  -27.396 -55.670  1.00 13.60 ? 431 HOH   D O   1 
HETATM 6589 O  O   . HOH   Q 5 .   ? 41.465  -38.773 -46.088  1.00 25.38 ? 432 HOH   D O   1 
HETATM 6590 O  O   . HOH   Q 5 .   ? 40.006  -36.553 -53.745  1.00 29.58 ? 433 HOH   D O   1 
HETATM 6591 O  O   . HOH   Q 5 .   ? 26.626  -42.876 -51.010  1.00 19.15 ? 434 HOH   D O   1 
HETATM 6592 O  O   . HOH   Q 5 .   ? 21.547  -20.985 -58.768  1.00 18.35 ? 435 HOH   D O   1 
HETATM 6593 O  O   . HOH   Q 5 .   ? 20.184  -25.239 -52.975  1.00 16.45 ? 436 HOH   D O   1 
HETATM 6594 O  O   . HOH   Q 5 .   ? 11.328  -35.388 -48.960  1.00 13.89 ? 437 HOH   D O   1 
HETATM 6595 O  O   . HOH   Q 5 .   ? 21.210  -42.852 -53.542  1.00 22.55 ? 438 HOH   D O   1 
HETATM 6596 O  O   . HOH   Q 5 .   ? 29.921  -35.123 -59.513  1.00 17.29 ? 439 HOH   D O   1 
HETATM 6597 O  O   . HOH   Q 5 .   ? 41.262  -20.968 -56.546  1.00 29.64 ? 440 HOH   D O   1 
HETATM 6598 O  O   . HOH   Q 5 .   ? 16.976  -26.183 -45.438  1.00 22.80 ? 441 HOH   D O   1 
HETATM 6599 O  O   . HOH   Q 5 .   ? 8.876   -29.380 -53.018  1.00 15.50 ? 442 HOH   D O   1 
HETATM 6600 O  O   . HOH   Q 5 .   ? 36.722  -42.776 -48.702  1.00 25.85 ? 443 HOH   D O   1 
HETATM 6601 O  O   . HOH   Q 5 .   ? 10.257  -24.915 -50.913  1.00 28.80 ? 444 HOH   D O   1 
HETATM 6602 O  O   . HOH   Q 5 .   ? 8.813   -28.435 -49.449  1.00 24.89 ? 445 HOH   D O   1 
HETATM 6603 O  O   . HOH   Q 5 .   ? 38.519  -38.427 -54.904  1.00 28.99 ? 446 HOH   D O   1 
HETATM 6604 O  O   . HOH   Q 5 .   ? 49.328  -36.913 -64.705  1.00 20.69 ? 447 HOH   D O   1 
HETATM 6605 O  O   . HOH   Q 5 .   ? 16.794  -25.935 -61.242  1.00 24.49 ? 448 HOH   D O   1 
HETATM 6606 O  O   . HOH   Q 5 .   ? 17.312  -27.485 -47.776  1.00 18.02 ? 449 HOH   D O   1 
HETATM 6607 O  O   . HOH   Q 5 .   ? 32.479  -25.911 -65.376  1.00 21.98 ? 450 HOH   D O   1 
HETATM 6608 O  O   . HOH   Q 5 .   ? 18.665  -18.933 -65.544  1.00 32.48 ? 451 HOH   D O   1 
HETATM 6609 O  O   . HOH   Q 5 .   ? 43.923  -20.031 -56.877  1.00 30.54 ? 452 HOH   D O   1 
HETATM 6610 O  O   . HOH   Q 5 .   ? 24.074  -35.960 -47.248  1.00 13.59 ? 453 HOH   D O   1 
HETATM 6611 O  O   . HOH   Q 5 .   ? 15.583  -33.054 -44.616  1.00 17.03 ? 454 HOH   D O   1 
HETATM 6612 O  O   . HOH   Q 5 .   ? 17.304  -36.608 -31.253  1.00 29.67 ? 455 HOH   D O   1 
HETATM 6613 O  O   . HOH   Q 5 .   ? 18.214  -31.048 -71.358  1.00 33.95 ? 456 HOH   D O   1 
HETATM 6614 O  O   . HOH   Q 5 .   ? 17.215  -35.722 -72.157  1.00 35.01 ? 457 HOH   D O   1 
HETATM 6615 O  O   . HOH   Q 5 .   ? 17.488  -40.505 -42.334  1.00 20.63 ? 458 HOH   D O   1 
HETATM 6616 O  O   . HOH   Q 5 .   ? 17.821  -23.660 -45.570  1.00 24.81 ? 459 HOH   D O   1 
HETATM 6617 O  O   . HOH   Q 5 .   ? 16.089  -41.971 -44.502  1.00 25.19 ? 460 HOH   D O   1 
HETATM 6618 O  O   . HOH   Q 5 .   ? 29.780  -17.146 -55.567  1.00 21.14 ? 461 HOH   D O   1 
HETATM 6619 O  O   . HOH   Q 5 .   ? 21.417  -22.762 -51.989  1.00 16.84 ? 462 HOH   D O   1 
HETATM 6620 O  O   . HOH   Q 5 .   ? 23.046  -13.200 -57.075  1.00 32.15 ? 463 HOH   D O   1 
HETATM 6621 O  O   . HOH   Q 5 .   ? 20.961  -48.497 -50.302  1.00 38.35 ? 464 HOH   D O   1 
HETATM 6622 O  O   . HOH   Q 5 .   ? 38.362  -40.046 -59.111  1.00 33.40 ? 465 HOH   D O   1 
HETATM 6623 O  O   . HOH   Q 5 .   ? 34.236  -22.945 -57.313  1.00 29.89 ? 466 HOH   D O   1 
HETATM 6624 O  O   . HOH   Q 5 .   ? 50.253  -26.736 -59.640  1.00 22.95 ? 467 HOH   D O   1 
HETATM 6625 O  O   . HOH   Q 5 .   ? 13.804  -40.476 -44.548  1.00 21.89 ? 468 HOH   D O   1 
HETATM 6626 O  O   . HOH   Q 5 .   ? 25.527  -42.726 -48.456  1.00 23.90 ? 469 HOH   D O   1 
HETATM 6627 O  O   . HOH   Q 5 .   ? 20.370  -31.521 -52.874  1.00 12.41 ? 470 HOH   D O   1 
HETATM 6628 O  O   . HOH   Q 5 .   ? 47.677  -33.395 -52.279  1.00 14.35 ? 471 HOH   D O   1 
HETATM 6629 O  O   . HOH   Q 5 .   ? 13.486  -28.666 -56.169  1.00 26.41 ? 472 HOH   D O   1 
HETATM 6630 O  O   . HOH   Q 5 .   ? 15.292  -39.518 -66.290  1.00 38.61 ? 473 HOH   D O   1 
HETATM 6631 O  O   . HOH   Q 5 .   ? 24.176  -28.907 -44.618  1.00 17.30 ? 474 HOH   D O   1 
HETATM 6632 O  O   . HOH   Q 5 .   ? 17.783  -19.620 -57.566  1.00 31.42 ? 475 HOH   D O   1 
HETATM 6633 O  O   . HOH   Q 5 .   ? 20.416  -37.605 -73.153  1.00 40.21 ? 476 HOH   D O   1 
HETATM 6634 O  O   . HOH   Q 5 .   ? 35.204  -26.910 -42.406  1.00 38.64 ? 477 HOH   D O   1 
HETATM 6635 O  O   . HOH   Q 5 .   ? 27.568  -43.289 -45.980  1.00 28.95 ? 478 HOH   D O   1 
HETATM 6636 O  O   . HOH   Q 5 .   ? 41.674  -41.042 -47.606  1.00 27.06 ? 479 HOH   D O   1 
HETATM 6637 O  O   . HOH   Q 5 .   ? 23.991  -24.460 -61.798  1.00 33.25 ? 480 HOH   D O   1 
HETATM 6638 O  O   . HOH   Q 5 .   ? 20.425  -27.068 -33.716  1.00 30.37 ? 481 HOH   D O   1 
HETATM 6639 O  O   . HOH   Q 5 .   ? 17.268  -17.422 -55.003  1.00 30.27 ? 482 HOH   D O   1 
HETATM 6640 O  O   . HOH   Q 5 .   ? 10.814  -27.320 -44.949  1.00 23.87 ? 483 HOH   D O   1 
HETATM 6641 O  O   . HOH   Q 5 .   ? 34.209  -24.436 -64.575  1.00 32.50 ? 484 HOH   D O   1 
HETATM 6642 O  O   . HOH   Q 5 .   ? 47.002  -28.888 -52.210  1.00 18.22 ? 485 HOH   D O   1 
HETATM 6643 O  O   . HOH   Q 5 .   ? 28.077  -27.052 -69.180  1.00 30.25 ? 486 HOH   D O   1 
HETATM 6644 O  O   . HOH   Q 5 .   ? 26.573  -42.356 -43.552  1.00 20.92 ? 487 HOH   D O   1 
HETATM 6645 O  O   . HOH   Q 5 .   ? 13.215  -26.156 -56.947  1.00 32.87 ? 488 HOH   D O   1 
HETATM 6646 O  O   . HOH   Q 5 .   ? 41.292  -34.900 -46.193  1.00 34.00 ? 489 HOH   D O   1 
HETATM 6647 O  O   . HOH   Q 5 .   ? 21.580  -29.463 -54.081  1.00 13.22 ? 490 HOH   D O   1 
HETATM 6648 O  O   . HOH   Q 5 .   ? 41.666  -42.073 -55.554  1.00 27.78 ? 491 HOH   D O   1 
HETATM 6649 O  O   . HOH   Q 5 .   ? 14.070  -39.915 -51.597  1.00 22.89 ? 492 HOH   D O   1 
HETATM 6650 O  O   . HOH   Q 5 .   ? 35.461  -22.417 -59.378  1.00 34.33 ? 493 HOH   D O   1 
HETATM 6651 O  O   . HOH   Q 5 .   ? 33.922  -21.489 -61.186  1.00 39.52 ? 494 HOH   D O   1 
HETATM 6652 O  O   . HOH   Q 5 .   ? 4.721   -27.877 -46.836  1.00 28.32 ? 495 HOH   D O   1 
HETATM 6653 O  O   . HOH   Q 5 .   ? 33.661  -21.951 -64.282  1.00 31.73 ? 496 HOH   D O   1 
HETATM 6654 O  O   . HOH   Q 5 .   ? 16.034  -35.640 -62.800  1.00 30.80 ? 497 HOH   D O   1 
HETATM 6655 O  O   . HOH   Q 5 .   ? 22.190  -46.759 -40.173  1.00 47.39 ? 498 HOH   D O   1 
HETATM 6656 O  O   . HOH   Q 5 .   ? 44.150  -37.554 -44.489  1.00 46.63 ? 499 HOH   D O   1 
HETATM 6657 O  O   . HOH   Q 5 .   ? 40.325  -32.255 -45.302  1.00 39.99 ? 500 HOH   D O   1 
HETATM 6658 O  O   . HOH   Q 5 .   ? 49.440  -26.246 -64.275  1.00 28.88 ? 501 HOH   D O   1 
HETATM 6659 O  O   . HOH   Q 5 .   ? 12.512  -27.675 -43.106  1.00 44.74 ? 502 HOH   D O   1 
HETATM 6660 O  O   . HOH   Q 5 .   ? 0.666   -23.658 -43.390  1.00 44.16 ? 503 HOH   D O   1 
HETATM 6661 O  O   . HOH   Q 5 .   ? 9.930   -31.268 -58.443  1.00 38.59 ? 504 HOH   D O   1 
HETATM 6662 O  O   . HOH   Q 5 .   ? 18.096  -27.765 -43.799  1.00 28.04 ? 505 HOH   D O   1 
HETATM 6663 O  O   . HOH   Q 5 .   ? 29.803  -45.967 -50.040  1.00 42.27 ? 506 HOH   D O   1 
HETATM 6664 O  O   . HOH   Q 5 .   ? 8.505   -27.194 -51.259  1.00 24.42 ? 507 HOH   D O   1 
HETATM 6665 O  O   . HOH   Q 5 .   ? 17.856  -41.978 -39.930  1.00 28.67 ? 508 HOH   D O   1 
HETATM 6666 O  O   . HOH   Q 5 .   ? 37.422  -40.867 -56.460  1.00 21.09 ? 509 HOH   D O   1 
HETATM 6667 O  O   . HOH   Q 5 .   ? 15.485  -14.270 -50.935  1.00 39.06 ? 510 HOH   D O   1 
HETATM 6668 O  O   . HOH   Q 5 .   ? 19.390  -37.118 -75.740  1.00 30.65 ? 511 HOH   D O   1 
HETATM 6669 O  O   . HOH   Q 5 .   ? 21.051  -26.918 -42.869  1.00 30.67 ? 512 HOH   D O   1 
HETATM 6670 O  O   . HOH   Q 5 .   ? 23.237  -26.320 -44.428  1.00 21.18 ? 513 HOH   D O   1 
HETATM 6671 O  O   . HOH   Q 5 .   ? 15.053  -17.889 -53.527  1.00 33.19 ? 514 HOH   D O   1 
HETATM 6672 O  O   . HOH   Q 5 .   ? 17.894  -51.739 -54.816  1.00 38.16 ? 515 HOH   D O   1 
# 
