data_8RXL
# 
_entry.id   8RXL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8RXL         pdb_00008rxl 10.2210/pdb8rxl/pdb 
WWPDB D_1292136463 ?            ?                   
# 
_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       2025-02-19 
# 
_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                        8RXL 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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              guichou@cbs.cnrs.fr 
_pdbx_contact_author.name_first         jean-francois 
_pdbx_contact_author.name_last          guichou 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7699-3235 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Guichou, J.F.' 1 ? 
'Gelin, M.'     2 ? 
'Allemand, F.'  3 ? 
# 
_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                     'TEAD2 with an inhibitor' 
_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 'Guichou, J.F.' 1 ? 
primary 'Gelin, M.'     2 ? 
primary 'Allemand, F.'  3 ? 
# 
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 'Transcriptional enhancer factor TEF-4'           27455.016 2  ? ? ? ? 
2 non-polymer syn '4-(5-phenylmethoxy-1~{H}-indol-3-yl)butan-2-one' 293.360   2  ? ? ? ? 
3 non-polymer syn GLYCEROL                                          92.094    1  ? ? ? ? 
4 water       nat water                                             18.015    19 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'TEA domain family member 2,TEAD-2' 
# 
_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       
;PAWQARGLGTARLQLVEFSAFVEPPDAVDSYQRHLFVHISQHCPSPGAPPLESVDVRQIYDKFPEKKGGLRELYDRGPPH
AFFLVKFWADLNWGPSGEEAGAGGSISSGGFYGVSSQYESLEHMTLTCSSKVCSFGKQVVEKVETERAQLEDGRFVYRLL
RSPMCEYLVNFLHKLRQLPERYMMNSVLENFTILQVVTNRDTQELLLCTAYVFEVSTSERGAQHHIYRLVRDVEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;PAWQARGLGTARLQLVEFSAFVEPPDAVDSYQRHLFVHISQHCPSPGAPPLESVDVRQIYDKFPEKKGGLRELYDRGPPH
AFFLVKFWADLNWGPSGEEAGAGGSISSGGFYGVSSQYESLEHMTLTCSSKVCSFGKQVVEKVETERAQLEDGRFVYRLL
RSPMCEYLVNFLHKLRQLPERYMMNSVLENFTILQVVTNRDTQELLLCTAYVFEVSTSERGAQHHIYRLVRDVEHHHHHH
;
_entity_poly.pdbx_strand_id                 B,A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '4-(5-phenylmethoxy-1~{H}-indol-3-yl)butan-2-one' A1H3Z 
3 GLYCEROL                                          GOL   
4 water                                             HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PRO n 
1 2   ALA n 
1 3   TRP n 
1 4   GLN n 
1 5   ALA n 
1 6   ARG n 
1 7   GLY n 
1 8   LEU n 
1 9   GLY n 
1 10  THR n 
1 11  ALA n 
1 12  ARG n 
1 13  LEU n 
1 14  GLN n 
1 15  LEU n 
1 16  VAL n 
1 17  GLU n 
1 18  PHE n 
1 19  SER n 
1 20  ALA n 
1 21  PHE n 
1 22  VAL n 
1 23  GLU n 
1 24  PRO n 
1 25  PRO n 
1 26  ASP n 
1 27  ALA n 
1 28  VAL n 
1 29  ASP n 
1 30  SER n 
1 31  TYR n 
1 32  GLN n 
1 33  ARG n 
1 34  HIS n 
1 35  LEU n 
1 36  PHE n 
1 37  VAL n 
1 38  HIS n 
1 39  ILE n 
1 40  SER n 
1 41  GLN n 
1 42  HIS n 
1 43  CYS n 
1 44  PRO n 
1 45  SER n 
1 46  PRO n 
1 47  GLY n 
1 48  ALA n 
1 49  PRO n 
1 50  PRO n 
1 51  LEU n 
1 52  GLU n 
1 53  SER n 
1 54  VAL n 
1 55  ASP n 
1 56  VAL n 
1 57  ARG n 
1 58  GLN n 
1 59  ILE n 
1 60  TYR n 
1 61  ASP n 
1 62  LYS n 
1 63  PHE n 
1 64  PRO n 
1 65  GLU n 
1 66  LYS n 
1 67  LYS n 
1 68  GLY n 
1 69  GLY n 
1 70  LEU n 
1 71  ARG n 
1 72  GLU n 
1 73  LEU n 
1 74  TYR n 
1 75  ASP n 
1 76  ARG n 
1 77  GLY n 
1 78  PRO n 
1 79  PRO n 
1 80  HIS n 
1 81  ALA n 
1 82  PHE n 
1 83  PHE n 
1 84  LEU n 
1 85  VAL n 
1 86  LYS n 
1 87  PHE n 
1 88  TRP n 
1 89  ALA n 
1 90  ASP n 
1 91  LEU n 
1 92  ASN n 
1 93  TRP n 
1 94  GLY n 
1 95  PRO n 
1 96  SER n 
1 97  GLY n 
1 98  GLU n 
1 99  GLU n 
1 100 ALA n 
1 101 GLY n 
1 102 ALA n 
1 103 GLY n 
1 104 GLY n 
1 105 SER n 
1 106 ILE n 
1 107 SER n 
1 108 SER n 
1 109 GLY n 
1 110 GLY n 
1 111 PHE n 
1 112 TYR n 
1 113 GLY n 
1 114 VAL n 
1 115 SER n 
1 116 SER n 
1 117 GLN n 
1 118 TYR n 
1 119 GLU n 
1 120 SER n 
1 121 LEU n 
1 122 GLU n 
1 123 HIS n 
1 124 MET n 
1 125 THR n 
1 126 LEU n 
1 127 THR n 
1 128 CYS n 
1 129 SER n 
1 130 SER n 
1 131 LYS n 
1 132 VAL n 
1 133 CYS n 
1 134 SER n 
1 135 PHE n 
1 136 GLY n 
1 137 LYS n 
1 138 GLN n 
1 139 VAL n 
1 140 VAL n 
1 141 GLU n 
1 142 LYS n 
1 143 VAL n 
1 144 GLU n 
1 145 THR n 
1 146 GLU n 
1 147 ARG n 
1 148 ALA n 
1 149 GLN n 
1 150 LEU n 
1 151 GLU n 
1 152 ASP n 
1 153 GLY n 
1 154 ARG n 
1 155 PHE n 
1 156 VAL n 
1 157 TYR n 
1 158 ARG n 
1 159 LEU n 
1 160 LEU n 
1 161 ARG n 
1 162 SER n 
1 163 PRO n 
1 164 MET n 
1 165 CYS n 
1 166 GLU n 
1 167 TYR n 
1 168 LEU n 
1 169 VAL n 
1 170 ASN n 
1 171 PHE n 
1 172 LEU n 
1 173 HIS n 
1 174 LYS n 
1 175 LEU n 
1 176 ARG n 
1 177 GLN n 
1 178 LEU n 
1 179 PRO n 
1 180 GLU n 
1 181 ARG n 
1 182 TYR n 
1 183 MET n 
1 184 MET n 
1 185 ASN n 
1 186 SER n 
1 187 VAL n 
1 188 LEU n 
1 189 GLU n 
1 190 ASN n 
1 191 PHE n 
1 192 THR n 
1 193 ILE n 
1 194 LEU n 
1 195 GLN n 
1 196 VAL n 
1 197 VAL n 
1 198 THR n 
1 199 ASN n 
1 200 ARG n 
1 201 ASP n 
1 202 THR n 
1 203 GLN n 
1 204 GLU n 
1 205 LEU n 
1 206 LEU n 
1 207 LEU n 
1 208 CYS n 
1 209 THR n 
1 210 ALA n 
1 211 TYR n 
1 212 VAL n 
1 213 PHE n 
1 214 GLU n 
1 215 VAL n 
1 216 SER n 
1 217 THR n 
1 218 SER n 
1 219 GLU n 
1 220 ARG n 
1 221 GLY n 
1 222 ALA n 
1 223 GLN n 
1 224 HIS n 
1 225 HIS n 
1 226 ILE n 
1 227 TYR n 
1 228 ARG n 
1 229 LEU n 
1 230 VAL n 
1 231 ARG n 
1 232 ASP n 
1 233 VAL n 
1 234 GLU n 
1 235 HIS n 
1 236 HIS n 
1 237 HIS n 
1 238 HIS n 
1 239 HIS n 
1 240 HIS 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                   240 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'TEAD2, TEF4' 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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 
A1H3Z non-polymer         . '4-(5-phenylmethoxy-1~{H}-indol-3-yl)butan-2-one' ?                               'C19 H19 N O2'   
293.360 
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 
# 
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   PRO 1   216 216 PRO PRO B . n 
A 1 2   ALA 2   217 217 ALA ALA B . n 
A 1 3   TRP 3   218 218 TRP TRP B . n 
A 1 4   GLN 4   219 219 GLN GLN B . n 
A 1 5   ALA 5   220 220 ALA ALA B . n 
A 1 6   ARG 6   221 221 ARG ARG B . n 
A 1 7   GLY 7   222 222 GLY GLY B . n 
A 1 8   LEU 8   223 223 LEU LEU B . n 
A 1 9   GLY 9   224 224 GLY GLY B . n 
A 1 10  THR 10  225 225 THR THR B . n 
A 1 11  ALA 11  226 226 ALA ALA B . n 
A 1 12  ARG 12  227 227 ARG ARG B . n 
A 1 13  LEU 13  228 228 LEU LEU B . n 
A 1 14  GLN 14  229 229 GLN GLN B . n 
A 1 15  LEU 15  230 230 LEU LEU B . n 
A 1 16  VAL 16  231 231 VAL VAL B . n 
A 1 17  GLU 17  232 232 GLU GLU B . n 
A 1 18  PHE 18  233 233 PHE PHE B . n 
A 1 19  SER 19  234 234 SER SER B . n 
A 1 20  ALA 20  235 235 ALA ALA B . n 
A 1 21  PHE 21  236 236 PHE PHE B . n 
A 1 22  VAL 22  237 237 VAL VAL B . n 
A 1 23  GLU 23  238 238 GLU GLU B . n 
A 1 24  PRO 24  239 239 PRO PRO B . n 
A 1 25  PRO 25  240 240 PRO PRO B . n 
A 1 26  ASP 26  241 241 ASP ASP B . n 
A 1 27  ALA 27  242 242 ALA ALA B . n 
A 1 28  VAL 28  243 243 VAL VAL B . n 
A 1 29  ASP 29  244 244 ASP ASP B . n 
A 1 30  SER 30  245 245 SER SER B . n 
A 1 31  TYR 31  246 246 TYR TYR B . n 
A 1 32  GLN 32  247 247 GLN GLN B . n 
A 1 33  ARG 33  248 248 ARG ARG B . n 
A 1 34  HIS 34  249 249 HIS HIS B . n 
A 1 35  LEU 35  250 250 LEU LEU B . n 
A 1 36  PHE 36  251 251 PHE PHE B . n 
A 1 37  VAL 37  252 252 VAL VAL B . n 
A 1 38  HIS 38  253 253 HIS HIS B . n 
A 1 39  ILE 39  254 254 ILE ILE B . n 
A 1 40  SER 40  255 255 SER SER B . n 
A 1 41  GLN 41  256 256 GLN GLN B . n 
A 1 42  HIS 42  257 257 HIS HIS B . n 
A 1 43  CYS 43  258 ?   ?   ?   B . n 
A 1 44  PRO 44  259 ?   ?   ?   B . n 
A 1 45  SER 45  260 ?   ?   ?   B . n 
A 1 46  PRO 46  261 ?   ?   ?   B . n 
A 1 47  GLY 47  262 ?   ?   ?   B . n 
A 1 48  ALA 48  263 ?   ?   ?   B . n 
A 1 49  PRO 49  264 264 PRO PRO B . n 
A 1 50  PRO 50  265 265 PRO PRO B . n 
A 1 51  LEU 51  266 266 LEU LEU B . n 
A 1 52  GLU 52  267 267 GLU GLU B . n 
A 1 53  SER 53  268 268 SER SER B . n 
A 1 54  VAL 54  269 269 VAL VAL B . n 
A 1 55  ASP 55  270 270 ASP ASP B . n 
A 1 56  VAL 56  271 271 VAL VAL B . n 
A 1 57  ARG 57  272 272 ARG ARG B . n 
A 1 58  GLN 58  273 273 GLN GLN B . n 
A 1 59  ILE 59  274 274 ILE ILE B . n 
A 1 60  TYR 60  275 275 TYR TYR B . n 
A 1 61  ASP 61  276 276 ASP ASP B . n 
A 1 62  LYS 62  277 277 LYS LYS B . n 
A 1 63  PHE 63  278 278 PHE PHE B . n 
A 1 64  PRO 64  279 279 PRO PRO B . n 
A 1 65  GLU 65  280 280 GLU GLU B . n 
A 1 66  LYS 66  281 281 LYS LYS B . n 
A 1 67  LYS 67  282 282 LYS LYS B . n 
A 1 68  GLY 68  283 283 GLY GLY B . n 
A 1 69  GLY 69  284 284 GLY GLY B . n 
A 1 70  LEU 70  285 285 LEU LEU B . n 
A 1 71  ARG 71  286 286 ARG ARG B . n 
A 1 72  GLU 72  287 287 GLU GLU B . n 
A 1 73  LEU 73  288 288 LEU LEU B . n 
A 1 74  TYR 74  289 289 TYR TYR B . n 
A 1 75  ASP 75  290 290 ASP ASP B . n 
A 1 76  ARG 76  291 291 ARG ARG B . n 
A 1 77  GLY 77  292 292 GLY GLY B . n 
A 1 78  PRO 78  293 293 PRO PRO B . n 
A 1 79  PRO 79  294 294 PRO PRO B . n 
A 1 80  HIS 80  295 295 HIS HIS B . n 
A 1 81  ALA 81  296 296 ALA ALA B . n 
A 1 82  PHE 82  297 297 PHE PHE B . n 
A 1 83  PHE 83  298 298 PHE PHE B . n 
A 1 84  LEU 84  299 299 LEU LEU B . n 
A 1 85  VAL 85  300 300 VAL VAL B . n 
A 1 86  LYS 86  301 301 LYS LYS B . n 
A 1 87  PHE 87  302 302 PHE PHE B . n 
A 1 88  TRP 88  303 303 TRP TRP B . n 
A 1 89  ALA 89  304 304 ALA ALA B . n 
A 1 90  ASP 90  305 305 ASP ASP B . n 
A 1 91  LEU 91  306 306 LEU LEU B . n 
A 1 92  ASN 92  307 307 ASN ASN B . n 
A 1 93  TRP 93  308 308 TRP TRP B . n 
A 1 94  GLY 94  309 ?   ?   ?   B . n 
A 1 95  PRO 95  310 ?   ?   ?   B . n 
A 1 96  SER 96  311 ?   ?   ?   B . n 
A 1 97  GLY 97  312 ?   ?   ?   B . n 
A 1 98  GLU 98  313 ?   ?   ?   B . n 
A 1 99  GLU 99  314 ?   ?   ?   B . n 
A 1 100 ALA 100 315 ?   ?   ?   B . n 
A 1 101 GLY 101 316 ?   ?   ?   B . n 
A 1 102 ALA 102 317 ?   ?   ?   B . n 
A 1 103 GLY 103 318 ?   ?   ?   B . n 
A 1 104 GLY 104 319 ?   ?   ?   B . n 
A 1 105 SER 105 320 ?   ?   ?   B . n 
A 1 106 ILE 106 321 ?   ?   ?   B . n 
A 1 107 SER 107 322 ?   ?   ?   B . n 
A 1 108 SER 108 323 ?   ?   ?   B . n 
A 1 109 GLY 109 324 324 GLY GLY B . n 
A 1 110 GLY 110 325 325 GLY GLY B . n 
A 1 111 PHE 111 326 326 PHE PHE B . n 
A 1 112 TYR 112 327 327 TYR TYR B . n 
A 1 113 GLY 113 328 328 GLY GLY B . n 
A 1 114 VAL 114 329 329 VAL VAL B . n 
A 1 115 SER 115 330 330 SER SER B . n 
A 1 116 SER 116 331 331 SER SER B . n 
A 1 117 GLN 117 332 332 GLN GLN B . n 
A 1 118 TYR 118 333 333 TYR TYR B . n 
A 1 119 GLU 119 334 334 GLU GLU B . n 
A 1 120 SER 120 335 335 SER SER B . n 
A 1 121 LEU 121 336 336 LEU LEU B . n 
A 1 122 GLU 122 337 337 GLU GLU B . n 
A 1 123 HIS 123 338 338 HIS HIS B . n 
A 1 124 MET 124 339 339 MET MET B . n 
A 1 125 THR 125 340 340 THR THR B . n 
A 1 126 LEU 126 341 341 LEU LEU B . n 
A 1 127 THR 127 342 342 THR THR B . n 
A 1 128 CYS 128 343 343 CYS CYS B . n 
A 1 129 SER 129 344 344 SER SER B . n 
A 1 130 SER 130 345 345 SER SER B . n 
A 1 131 LYS 131 346 346 LYS LYS B . n 
A 1 132 VAL 132 347 347 VAL VAL B . n 
A 1 133 CYS 133 348 348 CYS CYS B . n 
A 1 134 SER 134 349 349 SER SER B . n 
A 1 135 PHE 135 350 350 PHE PHE B . n 
A 1 136 GLY 136 351 351 GLY GLY B . n 
A 1 137 LYS 137 352 352 LYS LYS B . n 
A 1 138 GLN 138 353 353 GLN GLN B . n 
A 1 139 VAL 139 354 354 VAL VAL B . n 
A 1 140 VAL 140 355 355 VAL VAL B . n 
A 1 141 GLU 141 356 356 GLU GLU B . n 
A 1 142 LYS 142 357 357 LYS LYS B . n 
A 1 143 VAL 143 358 358 VAL VAL B . n 
A 1 144 GLU 144 359 359 GLU GLU B . n 
A 1 145 THR 145 360 360 THR THR B . n 
A 1 146 GLU 146 361 361 GLU GLU B . n 
A 1 147 ARG 147 362 362 ARG ARG B . n 
A 1 148 ALA 148 363 363 ALA ALA B . n 
A 1 149 GLN 149 364 364 GLN GLN B . n 
A 1 150 LEU 150 365 365 LEU LEU B . n 
A 1 151 GLU 151 366 366 GLU GLU B . n 
A 1 152 ASP 152 367 367 ASP ASP B . n 
A 1 153 GLY 153 368 368 GLY GLY B . n 
A 1 154 ARG 154 369 369 ARG ARG B . n 
A 1 155 PHE 155 370 370 PHE PHE B . n 
A 1 156 VAL 156 371 371 VAL VAL B . n 
A 1 157 TYR 157 372 372 TYR TYR B . n 
A 1 158 ARG 158 373 373 ARG ARG B . n 
A 1 159 LEU 159 374 374 LEU LEU B . n 
A 1 160 LEU 160 375 375 LEU LEU B . n 
A 1 161 ARG 161 376 376 ARG ARG B . n 
A 1 162 SER 162 377 377 SER SER B . n 
A 1 163 PRO 163 378 378 PRO PRO B . n 
A 1 164 MET 164 379 379 MET MET B . n 
A 1 165 CYS 165 380 380 CYS CYS B . n 
A 1 166 GLU 166 381 381 GLU GLU B . n 
A 1 167 TYR 167 382 382 TYR TYR B . n 
A 1 168 LEU 168 383 383 LEU LEU B . n 
A 1 169 VAL 169 384 384 VAL VAL B . n 
A 1 170 ASN 170 385 385 ASN ASN B . n 
A 1 171 PHE 171 386 386 PHE PHE B . n 
A 1 172 LEU 172 387 387 LEU LEU B . n 
A 1 173 HIS 173 388 388 HIS HIS B . n 
A 1 174 LYS 174 389 389 LYS LYS B . n 
A 1 175 LEU 175 390 390 LEU LEU B . n 
A 1 176 ARG 176 391 391 ARG ARG B . n 
A 1 177 GLN 177 392 392 GLN GLN B . n 
A 1 178 LEU 178 393 393 LEU LEU B . n 
A 1 179 PRO 179 394 394 PRO PRO B . n 
A 1 180 GLU 180 395 395 GLU GLU B . n 
A 1 181 ARG 181 396 396 ARG ARG B . n 
A 1 182 TYR 182 397 397 TYR TYR B . n 
A 1 183 MET 183 398 398 MET MET B . n 
A 1 184 MET 184 399 399 MET MET B . n 
A 1 185 ASN 185 400 400 ASN ASN B . n 
A 1 186 SER 186 401 401 SER SER B . n 
A 1 187 VAL 187 402 402 VAL VAL B . n 
A 1 188 LEU 188 403 403 LEU LEU B . n 
A 1 189 GLU 189 404 404 GLU GLU B . n 
A 1 190 ASN 190 405 405 ASN ASN B . n 
A 1 191 PHE 191 406 406 PHE PHE B . n 
A 1 192 THR 192 407 407 THR THR B . n 
A 1 193 ILE 193 408 408 ILE ILE B . n 
A 1 194 LEU 194 409 409 LEU LEU B . n 
A 1 195 GLN 195 410 410 GLN GLN B . n 
A 1 196 VAL 196 411 411 VAL VAL B . n 
A 1 197 VAL 197 412 412 VAL VAL B . n 
A 1 198 THR 198 413 413 THR THR B . n 
A 1 199 ASN 199 414 414 ASN ASN B . n 
A 1 200 ARG 200 415 415 ARG ARG B . n 
A 1 201 ASP 201 416 416 ASP ASP B . n 
A 1 202 THR 202 417 417 THR THR B . n 
A 1 203 GLN 203 418 418 GLN GLN B . n 
A 1 204 GLU 204 419 419 GLU GLU B . n 
A 1 205 LEU 205 420 420 LEU LEU B . n 
A 1 206 LEU 206 421 421 LEU LEU B . n 
A 1 207 LEU 207 422 422 LEU LEU B . n 
A 1 208 CYS 208 423 423 CYS CYS B . n 
A 1 209 THR 209 424 424 THR THR B . n 
A 1 210 ALA 210 425 425 ALA ALA B . n 
A 1 211 TYR 211 426 426 TYR TYR B . n 
A 1 212 VAL 212 427 427 VAL VAL B . n 
A 1 213 PHE 213 428 428 PHE PHE B . n 
A 1 214 GLU 214 429 429 GLU GLU B . n 
A 1 215 VAL 215 430 430 VAL VAL B . n 
A 1 216 SER 216 431 431 SER SER B . n 
A 1 217 THR 217 432 432 THR THR B . n 
A 1 218 SER 218 433 433 SER SER B . n 
A 1 219 GLU 219 434 434 GLU GLU B . n 
A 1 220 ARG 220 435 435 ARG ARG B . n 
A 1 221 GLY 221 436 436 GLY GLY B . n 
A 1 222 ALA 222 437 437 ALA ALA B . n 
A 1 223 GLN 223 438 438 GLN GLN B . n 
A 1 224 HIS 224 439 439 HIS HIS B . n 
A 1 225 HIS 225 440 440 HIS HIS B . n 
A 1 226 ILE 226 441 441 ILE ILE B . n 
A 1 227 TYR 227 442 442 TYR TYR B . n 
A 1 228 ARG 228 443 443 ARG ARG B . n 
A 1 229 LEU 229 444 444 LEU LEU B . n 
A 1 230 VAL 230 445 445 VAL VAL B . n 
A 1 231 ARG 231 446 446 ARG ARG B . n 
A 1 232 ASP 232 447 ?   ?   ?   B . n 
A 1 233 VAL 233 448 ?   ?   ?   B . n 
A 1 234 GLU 234 449 ?   ?   ?   B . n 
A 1 235 HIS 235 450 ?   ?   ?   B . n 
A 1 236 HIS 236 451 ?   ?   ?   B . n 
A 1 237 HIS 237 452 ?   ?   ?   B . n 
A 1 238 HIS 238 453 ?   ?   ?   B . n 
A 1 239 HIS 239 454 ?   ?   ?   B . n 
A 1 240 HIS 240 455 ?   ?   ?   B . n 
B 1 1   PRO 1   216 ?   ?   ?   A . n 
B 1 2   ALA 2   217 ?   ?   ?   A . n 
B 1 3   TRP 3   218 ?   ?   ?   A . n 
B 1 4   GLN 4   219 ?   ?   ?   A . n 
B 1 5   ALA 5   220 ?   ?   ?   A . n 
B 1 6   ARG 6   221 ?   ?   ?   A . n 
B 1 7   GLY 7   222 222 GLY GLY A . n 
B 1 8   LEU 8   223 223 LEU LEU A . n 
B 1 9   GLY 9   224 224 GLY GLY A . n 
B 1 10  THR 10  225 225 THR THR A . n 
B 1 11  ALA 11  226 226 ALA ALA A . n 
B 1 12  ARG 12  227 227 ARG ARG A . n 
B 1 13  LEU 13  228 228 LEU LEU A . n 
B 1 14  GLN 14  229 229 GLN GLN A . n 
B 1 15  LEU 15  230 230 LEU LEU A . n 
B 1 16  VAL 16  231 231 VAL VAL A . n 
B 1 17  GLU 17  232 232 GLU GLU A . n 
B 1 18  PHE 18  233 233 PHE PHE A . n 
B 1 19  SER 19  234 234 SER SER A . n 
B 1 20  ALA 20  235 235 ALA ALA A . n 
B 1 21  PHE 21  236 236 PHE PHE A . n 
B 1 22  VAL 22  237 237 VAL VAL A . n 
B 1 23  GLU 23  238 238 GLU GLU A . n 
B 1 24  PRO 24  239 239 PRO PRO A . n 
B 1 25  PRO 25  240 ?   ?   ?   A . n 
B 1 26  ASP 26  241 ?   ?   ?   A . n 
B 1 27  ALA 27  242 ?   ?   ?   A . n 
B 1 28  VAL 28  243 ?   ?   ?   A . n 
B 1 29  ASP 29  244 ?   ?   ?   A . n 
B 1 30  SER 30  245 ?   ?   ?   A . n 
B 1 31  TYR 31  246 ?   ?   ?   A . n 
B 1 32  GLN 32  247 ?   ?   ?   A . n 
B 1 33  ARG 33  248 248 ARG ARG A . n 
B 1 34  HIS 34  249 249 HIS HIS A . n 
B 1 35  LEU 35  250 250 LEU LEU A . n 
B 1 36  PHE 36  251 251 PHE PHE A . n 
B 1 37  VAL 37  252 252 VAL VAL A . n 
B 1 38  HIS 38  253 253 HIS HIS A . n 
B 1 39  ILE 39  254 254 ILE ILE A . n 
B 1 40  SER 40  255 255 SER SER A . n 
B 1 41  GLN 41  256 256 GLN GLN A . n 
B 1 42  HIS 42  257 ?   ?   ?   A . n 
B 1 43  CYS 43  258 ?   ?   ?   A . n 
B 1 44  PRO 44  259 ?   ?   ?   A . n 
B 1 45  SER 45  260 ?   ?   ?   A . n 
B 1 46  PRO 46  261 ?   ?   ?   A . n 
B 1 47  GLY 47  262 ?   ?   ?   A . n 
B 1 48  ALA 48  263 ?   ?   ?   A . n 
B 1 49  PRO 49  264 264 PRO PRO A . n 
B 1 50  PRO 50  265 265 PRO PRO A . n 
B 1 51  LEU 51  266 266 LEU LEU A . n 
B 1 52  GLU 52  267 267 GLU GLU A . n 
B 1 53  SER 53  268 268 SER SER A . n 
B 1 54  VAL 54  269 269 VAL VAL A . n 
B 1 55  ASP 55  270 270 ASP ASP A . n 
B 1 56  VAL 56  271 271 VAL VAL A . n 
B 1 57  ARG 57  272 272 ARG ARG A . n 
B 1 58  GLN 58  273 273 GLN GLN A . n 
B 1 59  ILE 59  274 274 ILE ILE A . n 
B 1 60  TYR 60  275 275 TYR TYR A . n 
B 1 61  ASP 61  276 276 ASP ASP A . n 
B 1 62  LYS 62  277 277 LYS LYS A . n 
B 1 63  PHE 63  278 278 PHE PHE A . n 
B 1 64  PRO 64  279 279 PRO PRO A . n 
B 1 65  GLU 65  280 280 GLU GLU A . n 
B 1 66  LYS 66  281 281 LYS LYS A . n 
B 1 67  LYS 67  282 282 LYS LYS A . n 
B 1 68  GLY 68  283 283 GLY GLY A . n 
B 1 69  GLY 69  284 284 GLY GLY A . n 
B 1 70  LEU 70  285 285 LEU LEU A . n 
B 1 71  ARG 71  286 286 ARG ARG A . n 
B 1 72  GLU 72  287 287 GLU GLU A . n 
B 1 73  LEU 73  288 288 LEU LEU A . n 
B 1 74  TYR 74  289 289 TYR TYR A . n 
B 1 75  ASP 75  290 290 ASP ASP A . n 
B 1 76  ARG 76  291 291 ARG ARG A . n 
B 1 77  GLY 77  292 292 GLY GLY A . n 
B 1 78  PRO 78  293 293 PRO PRO A . n 
B 1 79  PRO 79  294 294 PRO PRO A . n 
B 1 80  HIS 80  295 295 HIS HIS A . n 
B 1 81  ALA 81  296 296 ALA ALA A . n 
B 1 82  PHE 82  297 297 PHE PHE A . n 
B 1 83  PHE 83  298 298 PHE PHE A . n 
B 1 84  LEU 84  299 299 LEU LEU A . n 
B 1 85  VAL 85  300 300 VAL VAL A . n 
B 1 86  LYS 86  301 301 LYS LYS A . n 
B 1 87  PHE 87  302 302 PHE PHE A . n 
B 1 88  TRP 88  303 303 TRP TRP A . n 
B 1 89  ALA 89  304 304 ALA ALA A . n 
B 1 90  ASP 90  305 305 ASP ASP A . n 
B 1 91  LEU 91  306 306 LEU LEU A . n 
B 1 92  ASN 92  307 307 ASN ASN A . n 
B 1 93  TRP 93  308 308 TRP TRP A . n 
B 1 94  GLY 94  309 ?   ?   ?   A . n 
B 1 95  PRO 95  310 ?   ?   ?   A . n 
B 1 96  SER 96  311 ?   ?   ?   A . n 
B 1 97  GLY 97  312 ?   ?   ?   A . n 
B 1 98  GLU 98  313 ?   ?   ?   A . n 
B 1 99  GLU 99  314 ?   ?   ?   A . n 
B 1 100 ALA 100 315 ?   ?   ?   A . n 
B 1 101 GLY 101 316 ?   ?   ?   A . n 
B 1 102 ALA 102 317 ?   ?   ?   A . n 
B 1 103 GLY 103 318 ?   ?   ?   A . n 
B 1 104 GLY 104 319 ?   ?   ?   A . n 
B 1 105 SER 105 320 ?   ?   ?   A . n 
B 1 106 ILE 106 321 ?   ?   ?   A . n 
B 1 107 SER 107 322 ?   ?   ?   A . n 
B 1 108 SER 108 323 ?   ?   ?   A . n 
B 1 109 GLY 109 324 ?   ?   ?   A . n 
B 1 110 GLY 110 325 325 GLY GLY A . n 
B 1 111 PHE 111 326 326 PHE PHE A . n 
B 1 112 TYR 112 327 327 TYR TYR A . n 
B 1 113 GLY 113 328 328 GLY GLY A . n 
B 1 114 VAL 114 329 329 VAL VAL A . n 
B 1 115 SER 115 330 330 SER SER A . n 
B 1 116 SER 116 331 331 SER SER A . n 
B 1 117 GLN 117 332 332 GLN GLN A . n 
B 1 118 TYR 118 333 333 TYR TYR A . n 
B 1 119 GLU 119 334 334 GLU GLU A . n 
B 1 120 SER 120 335 335 SER SER A . n 
B 1 121 LEU 121 336 336 LEU LEU A . n 
B 1 122 GLU 122 337 337 GLU GLU A . n 
B 1 123 HIS 123 338 338 HIS HIS A . n 
B 1 124 MET 124 339 339 MET MET A . n 
B 1 125 THR 125 340 340 THR THR A . n 
B 1 126 LEU 126 341 341 LEU LEU A . n 
B 1 127 THR 127 342 342 THR THR A . n 
B 1 128 CYS 128 343 343 CYS CYS A . n 
B 1 129 SER 129 344 344 SER SER A . n 
B 1 130 SER 130 345 345 SER SER A . n 
B 1 131 LYS 131 346 346 LYS LYS A . n 
B 1 132 VAL 132 347 347 VAL VAL A . n 
B 1 133 CYS 133 348 348 CYS CYS A . n 
B 1 134 SER 134 349 349 SER SER A . n 
B 1 135 PHE 135 350 350 PHE PHE A . n 
B 1 136 GLY 136 351 351 GLY GLY A . n 
B 1 137 LYS 137 352 352 LYS LYS A . n 
B 1 138 GLN 138 353 353 GLN GLN A . n 
B 1 139 VAL 139 354 354 VAL VAL A . n 
B 1 140 VAL 140 355 355 VAL VAL A . n 
B 1 141 GLU 141 356 356 GLU GLU A . n 
B 1 142 LYS 142 357 357 LYS LYS A . n 
B 1 143 VAL 143 358 358 VAL VAL A . n 
B 1 144 GLU 144 359 359 GLU GLU A . n 
B 1 145 THR 145 360 360 THR THR A . n 
B 1 146 GLU 146 361 361 GLU GLU A . n 
B 1 147 ARG 147 362 362 ARG ARG A . n 
B 1 148 ALA 148 363 363 ALA ALA A . n 
B 1 149 GLN 149 364 364 GLN GLN A . n 
B 1 150 LEU 150 365 365 LEU LEU A . n 
B 1 151 GLU 151 366 366 GLU GLU A . n 
B 1 152 ASP 152 367 367 ASP ASP A . n 
B 1 153 GLY 153 368 368 GLY GLY A . n 
B 1 154 ARG 154 369 369 ARG ARG A . n 
B 1 155 PHE 155 370 370 PHE PHE A . n 
B 1 156 VAL 156 371 371 VAL VAL A . n 
B 1 157 TYR 157 372 372 TYR TYR A . n 
B 1 158 ARG 158 373 373 ARG ARG A . n 
B 1 159 LEU 159 374 374 LEU LEU A . n 
B 1 160 LEU 160 375 375 LEU LEU A . n 
B 1 161 ARG 161 376 376 ARG ARG A . n 
B 1 162 SER 162 377 377 SER SER A . n 
B 1 163 PRO 163 378 378 PRO PRO A . n 
B 1 164 MET 164 379 379 MET MET A . n 
B 1 165 CYS 165 380 380 CYS CYS A . n 
B 1 166 GLU 166 381 381 GLU GLU A . n 
B 1 167 TYR 167 382 382 TYR TYR A . n 
B 1 168 LEU 168 383 383 LEU LEU A . n 
B 1 169 VAL 169 384 384 VAL VAL A . n 
B 1 170 ASN 170 385 385 ASN ASN A . n 
B 1 171 PHE 171 386 386 PHE PHE A . n 
B 1 172 LEU 172 387 387 LEU LEU A . n 
B 1 173 HIS 173 388 388 HIS HIS A . n 
B 1 174 LYS 174 389 389 LYS LYS A . n 
B 1 175 LEU 175 390 390 LEU LEU A . n 
B 1 176 ARG 176 391 391 ARG ARG A . n 
B 1 177 GLN 177 392 392 GLN GLN A . n 
B 1 178 LEU 178 393 393 LEU LEU A . n 
B 1 179 PRO 179 394 394 PRO PRO A . n 
B 1 180 GLU 180 395 395 GLU GLU A . n 
B 1 181 ARG 181 396 396 ARG ARG A . n 
B 1 182 TYR 182 397 397 TYR TYR A . n 
B 1 183 MET 183 398 398 MET MET A . n 
B 1 184 MET 184 399 399 MET MET A . n 
B 1 185 ASN 185 400 400 ASN ASN A . n 
B 1 186 SER 186 401 401 SER SER A . n 
B 1 187 VAL 187 402 402 VAL VAL A . n 
B 1 188 LEU 188 403 403 LEU LEU A . n 
B 1 189 GLU 189 404 404 GLU GLU A . n 
B 1 190 ASN 190 405 405 ASN ASN A . n 
B 1 191 PHE 191 406 406 PHE PHE A . n 
B 1 192 THR 192 407 407 THR THR A . n 
B 1 193 ILE 193 408 408 ILE ILE A . n 
B 1 194 LEU 194 409 409 LEU LEU A . n 
B 1 195 GLN 195 410 410 GLN GLN A . n 
B 1 196 VAL 196 411 411 VAL VAL A . n 
B 1 197 VAL 197 412 412 VAL VAL A . n 
B 1 198 THR 198 413 413 THR THR A . n 
B 1 199 ASN 199 414 414 ASN ASN A . n 
B 1 200 ARG 200 415 415 ARG ARG A . n 
B 1 201 ASP 201 416 416 ASP ASP A . n 
B 1 202 THR 202 417 417 THR THR A . n 
B 1 203 GLN 203 418 418 GLN GLN A . n 
B 1 204 GLU 204 419 419 GLU GLU A . n 
B 1 205 LEU 205 420 420 LEU LEU A . n 
B 1 206 LEU 206 421 421 LEU LEU A . n 
B 1 207 LEU 207 422 422 LEU LEU A . n 
B 1 208 CYS 208 423 423 CYS CYS A . n 
B 1 209 THR 209 424 424 THR THR A . n 
B 1 210 ALA 210 425 425 ALA ALA A . n 
B 1 211 TYR 211 426 426 TYR TYR A . n 
B 1 212 VAL 212 427 427 VAL VAL A . n 
B 1 213 PHE 213 428 428 PHE PHE A . n 
B 1 214 GLU 214 429 429 GLU GLU A . n 
B 1 215 VAL 215 430 430 VAL VAL A . n 
B 1 216 SER 216 431 431 SER SER A . n 
B 1 217 THR 217 432 432 THR THR A . n 
B 1 218 SER 218 433 433 SER SER A . n 
B 1 219 GLU 219 434 434 GLU GLU A . n 
B 1 220 ARG 220 435 435 ARG ARG A . n 
B 1 221 GLY 221 436 436 GLY GLY A . n 
B 1 222 ALA 222 437 437 ALA ALA A . n 
B 1 223 GLN 223 438 438 GLN GLN A . n 
B 1 224 HIS 224 439 439 HIS HIS A . n 
B 1 225 HIS 225 440 440 HIS HIS A . n 
B 1 226 ILE 226 441 441 ILE ILE A . n 
B 1 227 TYR 227 442 442 TYR TYR A . n 
B 1 228 ARG 228 443 443 ARG ARG A . n 
B 1 229 LEU 229 444 444 LEU LEU A . n 
B 1 230 VAL 230 445 445 VAL VAL A . n 
B 1 231 ARG 231 446 446 ARG ARG A . n 
B 1 232 ASP 232 447 ?   ?   ?   A . n 
B 1 233 VAL 233 448 ?   ?   ?   A . n 
B 1 234 GLU 234 449 ?   ?   ?   A . n 
B 1 235 HIS 235 450 ?   ?   ?   A . n 
B 1 236 HIS 236 451 ?   ?   ?   A . n 
B 1 237 HIS 237 452 ?   ?   ?   A . n 
B 1 238 HIS 238 453 ?   ?   ?   A . n 
B 1 239 HIS 239 454 ?   ?   ?   A . n 
B 1 240 HIS 240 455 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H3Z 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H3Z 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
C 2 A1H3Z 1  501 501 A1H3Z LIG B . 
D 3 GOL   1  502 601 GOL   GOL B . 
E 2 A1H3Z 1  501 501 A1H3Z LIG A . 
F 4 HOH   1  601 5   HOH   HOH B . 
F 4 HOH   2  602 1   HOH   HOH B . 
F 4 HOH   3  603 15  HOH   HOH B . 
F 4 HOH   4  604 3   HOH   HOH B . 
F 4 HOH   5  605 9   HOH   HOH B . 
F 4 HOH   6  606 11  HOH   HOH B . 
F 4 HOH   7  607 16  HOH   HOH B . 
F 4 HOH   8  608 18  HOH   HOH B . 
F 4 HOH   9  609 12  HOH   HOH B . 
F 4 HOH   10 610 2   HOH   HOH B . 
G 4 HOH   1  601 4   HOH   HOH A . 
G 4 HOH   2  602 23  HOH   HOH A . 
G 4 HOH   3  603 14  HOH   HOH A . 
G 4 HOH   4  604 21  HOH   HOH A . 
G 4 HOH   5  605 22  HOH   HOH A . 
G 4 HOH   6  606 24  HOH   HOH A . 
G 4 HOH   7  607 13  HOH   HOH A . 
G 4 HOH   8  608 20  HOH   HOH A . 
G 4 HOH   9  609 6   HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 B LYS 281 ? CG ? A LYS 66 CG 
2  1 Y 1 B LYS 281 ? CD ? A LYS 66 CD 
3  1 Y 1 B LYS 281 ? CE ? A LYS 66 CE 
4  1 Y 1 B LYS 281 ? NZ ? A LYS 66 NZ 
5  1 Y 1 B LYS 282 ? CD ? A LYS 67 CD 
6  1 Y 1 B LYS 282 ? CE ? A LYS 67 CE 
7  1 Y 1 B LYS 282 ? NZ ? A LYS 67 NZ 
8  1 Y 1 A LYS 281 ? CG ? B LYS 66 CG 
9  1 Y 1 A LYS 281 ? CD ? B LYS 66 CD 
10 1 Y 1 A LYS 281 ? CE ? B LYS 66 CE 
11 1 Y 1 A LYS 281 ? NZ ? B LYS 66 NZ 
12 1 Y 1 A LYS 282 ? CD ? B LYS 67 CD 
13 1 Y 1 A LYS 282 ? CE ? B LYS 67 CE 
14 1 Y 1 A LYS 282 ? NZ ? B LYS 67 NZ 
# 
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    ? ? ? 5.8.0103 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? pointless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   117.51 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RXL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     122.922 
_cell.length_a_esd                 ? 
_cell.length_b                     61.651 
_cell.length_b_esd                 ? 
_cell.length_c                     80.111 
_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                         8RXL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 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                   8RXL 
_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             2.46 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.92 
_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    '2.8M sodium formate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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 PILATUS 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         2021-07-15 
_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   0.9697 
_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                        'ESRF BEAMLINE BM30A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9697 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BM30A 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8RXL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.29 
_reflns.d_resolution_low                               48.45 
_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                                     21606 
_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                           88.09 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.71 
_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                                   0.910 
_reflns.pdbx_CC_star                                   0.976 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    2.29 
_reflns_shell.d_res_low                                     2.37 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1714 
_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                                  0.797 
_reflns_shell.pdbx_CC_star                                  0.942 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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]                            -0.47 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.19 
_refine.aniso_B[2][2]                            0.36 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            0.20 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               67.911 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.930 
_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                                 8RXL 
_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                            2.29 
_refine.ls_d_res_low                             48.45 
_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                     20091 
_refine.ls_number_reflns_R_free                  1058 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    88.13 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.21151 
_refine.ls_R_factor_R_free                       0.27061 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20829 
_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                       0.366 
_refine.pdbx_overall_ESU_R_Free                  0.271 
_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                             14.360 
_refine.overall_SU_ML                            0.306 
_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                       2.29 
_refine_hist.d_res_low                        48.45 
_refine_hist.number_atoms_solvent             19 
_refine_hist.number_atoms_total               3386 
_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        3317 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         50 
_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' ? 0.012  0.019  3460 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  3245 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.596  1.961  4675 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.931  3.000  7419 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.759  5.000  399  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 32.349 22.768 177  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.071 15.000 573  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.360 15.000 31   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.079  0.200  498  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  3864 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  891  ? 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' ? 4.494  6.473  1611 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.496  6.471  1610 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 6.906  9.682  2002 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.904  9.684  2003 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.114  7.131  1849 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 5.112  7.132  1850 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 8.067  10.474 2673 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 11.440 52.609 3624 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 11.437 52.617 3623 ? 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                       2.29 
_refine_ls_shell.d_res_low                        2.35 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             62 
_refine_ls_shell.number_reflns_R_work             1171 
_refine_ls_shell.percent_reflns_obs               70.30 
_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                  0.34 
_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   ? 
_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                  0.349 
# 
_struct.entry_id                     8RXL 
_struct.title                        'TEAD2 with an inhibitor' 
_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        8RXL 
_struct_keywords.text            'inhibitor, complex, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
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 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    TEAD2_HUMAN 
_struct_ref.pdbx_db_accession          Q15562 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;PAWQARGLGTARLQLVEFSAFVEPPDAVDSYQRHLFVHISQHCPSPGAPPLESVDVRQIYDKFPEKKGGLRELYDRGPPH
AFFLVKFWADLNWGPSGEEAGAGGSISSGGFYGVSSQYESLEHMTLTCSSKVCSFGKQVVEKVETERAQLEDGRFVYRLL
RSPMCEYLVNFLHKLRQLPERYMMNSVLENFTILQVVTNRDTQELLLCTAYVFEVSTSERGAQHHIYRLVRD
;
_struct_ref.pdbx_align_begin           216 
# 
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 8RXL B 1 ? 232 ? Q15562 216 ? 447 ? 216 447 
2 1 8RXL A 1 ? 232 ? Q15562 216 ? 447 ? 216 447 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8RXL VAL B 233 ? UNP Q15562 ? ? 'expression tag' 448 1  
1 8RXL GLU B 234 ? UNP Q15562 ? ? 'expression tag' 449 2  
1 8RXL HIS B 235 ? UNP Q15562 ? ? 'expression tag' 450 3  
1 8RXL HIS B 236 ? UNP Q15562 ? ? 'expression tag' 451 4  
1 8RXL HIS B 237 ? UNP Q15562 ? ? 'expression tag' 452 5  
1 8RXL HIS B 238 ? UNP Q15562 ? ? 'expression tag' 453 6  
1 8RXL HIS B 239 ? UNP Q15562 ? ? 'expression tag' 454 7  
1 8RXL HIS B 240 ? UNP Q15562 ? ? 'expression tag' 455 8  
2 8RXL VAL A 233 ? UNP Q15562 ? ? 'expression tag' 448 9  
2 8RXL GLU A 234 ? UNP Q15562 ? ? 'expression tag' 449 10 
2 8RXL HIS A 235 ? UNP Q15562 ? ? 'expression tag' 450 11 
2 8RXL HIS A 236 ? UNP Q15562 ? ? 'expression tag' 451 12 
2 8RXL HIS A 237 ? UNP Q15562 ? ? 'expression tag' 452 13 
2 8RXL HIS A 238 ? UNP Q15562 ? ? 'expression tag' 453 14 
2 8RXL HIS A 239 ? UNP Q15562 ? ? 'expression tag' 454 15 
2 8RXL HIS A 240 ? UNP Q15562 ? ? 'expression tag' 455 16 
# 
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_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,F 
2 1 B,E,G   
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_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 ARG A 57  ? PHE A 63  ? ARG B 272 PHE B 278 5 ? 7  
HELX_P HELX_P2  AA2 GLY A 69  ? GLY A 77  ? GLY B 284 GLY B 292 1 ? 9  
HELX_P HELX_P3  AA3 PRO A 78  ? HIS A 80  ? PRO B 293 HIS B 295 5 ? 3  
HELX_P HELX_P4  AA4 CYS A 165 ? LEU A 178 ? CYS B 380 LEU B 393 1 ? 14 
HELX_P HELX_P5  AA5 GLU A 180 ? ASN A 190 ? GLU B 395 ASN B 405 1 ? 11 
HELX_P HELX_P6  AA6 ARG B 57  ? PHE B 63  ? ARG A 272 PHE A 278 5 ? 7  
HELX_P HELX_P7  AA7 GLY B 69  ? GLY B 77  ? GLY A 284 GLY A 292 1 ? 9  
HELX_P HELX_P8  AA8 PRO B 78  ? HIS B 80  ? PRO A 293 HIS A 295 5 ? 3  
HELX_P HELX_P9  AA9 CYS B 165 ? ARG B 176 ? CYS A 380 ARG A 391 1 ? 12 
HELX_P HELX_P10 AB1 GLU B 180 ? GLU B 189 ? GLU A 395 GLU A 404 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 77 A . ? GLY 292 B PRO 78 A ? PRO 293 B 1 7.55 
2 GLY 77 B . ? GLY 292 A PRO 78 B ? PRO 293 A 1 5.90 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5  ? 
AA2 ? 14 ? 
AA3 ? 5  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? anti-parallel 
AA1 3  4  ? anti-parallel 
AA1 4  5  ? anti-parallel 
AA2 1  2  ? parallel      
AA2 2  3  ? anti-parallel 
AA2 3  4  ? parallel      
AA2 4  5  ? anti-parallel 
AA2 5  6  ? anti-parallel 
AA2 6  7  ? anti-parallel 
AA2 7  8  ? parallel      
AA2 8  9  ? anti-parallel 
AA2 9  10 ? anti-parallel 
AA2 10 11 ? anti-parallel 
AA2 11 12 ? parallel      
AA2 12 13 ? anti-parallel 
AA2 13 14 ? parallel      
AA3 1  2  ? anti-parallel 
AA3 2  3  ? anti-parallel 
AA3 3  4  ? anti-parallel 
AA3 4  5  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  HIS A 34  ? SER A 40  ? HIS B 249 SER B 255 
AA1 2  GLN A 14  ? GLU A 23  ? GLN B 229 GLU B 238 
AA1 3  PHE A 111 ? SER A 120 ? PHE B 326 SER B 335 
AA1 4  PHE A 155 ? PRO A 163 ? PHE B 370 PRO B 378 
AA1 5  GLN A 149 ? LEU A 150 ? GLN B 364 LEU B 365 
AA2 1  GLU A 52  ? ASP A 55  ? GLU B 267 ASP B 270 
AA2 2  GLN A 223 ? VAL A 230 ? GLN B 438 VAL B 445 
AA2 3  PHE A 82  ? ALA A 89  ? PHE B 297 ALA B 304 
AA2 4  LEU A 205 ? VAL A 215 ? LEU B 420 VAL B 430 
AA2 5  PHE A 191 ? ASN A 199 ? PHE B 406 ASN B 414 
AA2 6  THR A 125 ? SER A 134 ? THR B 340 SER B 349 
AA2 7  LYS A 137 ? ARG A 147 ? LYS B 352 ARG B 362 
AA2 8  LYS B 137 ? ARG B 147 ? LYS A 352 ARG A 362 
AA2 9  THR B 125 ? SER B 134 ? THR A 340 SER A 349 
AA2 10 PHE B 191 ? ASN B 199 ? PHE A 406 ASN A 414 
AA2 11 LEU B 205 ? VAL B 215 ? LEU A 420 VAL A 430 
AA2 12 PHE B 82  ? ALA B 89  ? PHE A 297 ALA A 304 
AA2 13 GLN B 223 ? VAL B 230 ? GLN A 438 VAL A 445 
AA2 14 SER B 53  ? ASP B 55  ? SER A 268 ASP A 270 
AA3 1  HIS B 34  ? SER B 40  ? HIS A 249 SER A 255 
AA3 2  GLN B 14  ? GLU B 23  ? GLN A 229 GLU A 238 
AA3 3  PHE B 111 ? SER B 120 ? PHE A 326 SER A 335 
AA3 4  ARG B 154 ? PRO B 163 ? ARG A 369 PRO A 378 
AA3 5  GLN B 149 ? GLU B 151 ? GLN A 364 GLU A 366 
# 
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  O HIS A 34  ? O HIS B 249 N VAL A 22  ? N VAL B 237 
AA1 2  3  N VAL A 16  ? N VAL B 231 O GLN A 117 ? O GLN B 332 
AA1 3  4  N SER A 120 ? N SER B 335 O PHE A 155 ? O PHE B 370 
AA1 4  5  O VAL A 156 ? O VAL B 371 N GLN A 149 ? N GLN B 364 
AA2 1  2  N GLU A 52  ? N GLU B 267 O ARG A 228 ? O ARG B 443 
AA2 2  3  O TYR A 227 ? O TYR B 442 N LEU A 84  ? N LEU B 299 
AA2 3  4  N ALA A 89  ? N ALA B 304 O GLU A 214 ? O GLU B 429 
AA2 4  5  O LEU A 206 ? O LEU B 421 N VAL A 197 ? N VAL B 412 
AA2 5  6  O VAL A 196 ? O VAL B 411 N SER A 129 ? N SER B 344 
AA2 6  7  N CYS A 128 ? N CYS B 343 O GLU A 144 ? O GLU B 359 
AA2 7  8  N VAL A 143 ? N VAL B 358 O GLU B 141 ? O GLU A 356 
AA2 8  9  O GLU B 146 ? O GLU A 361 N LEU B 126 ? N LEU A 341 
AA2 9  10 N CYS B 133 ? N CYS A 348 O THR B 192 ? O THR A 407 
AA2 10 11 N VAL B 197 ? N VAL A 412 O LEU B 207 ? O LEU A 422 
AA2 11 12 O VAL B 212 ? O VAL A 427 N PHE B 87  ? N PHE A 302 
AA2 12 13 N LEU B 84  ? N LEU A 299 O TYR B 227 ? O TYR A 442 
AA2 13 14 O ARG B 228 ? O ARG A 443 N VAL B 54  ? N VAL A 269 
AA3 1  2  O HIS B 34  ? O HIS A 249 N VAL B 22  ? N VAL A 237 
AA3 2  3  N PHE B 21  ? N PHE A 236 O GLY B 113 ? O GLY A 328 
AA3 3  4  N SER B 120 ? N SER A 335 O PHE B 155 ? O PHE A 370 
AA3 4  5  O VAL B 156 ? O VAL A 371 N GLN B 149 ? N GLN A 364 
# 
_pdbx_entry_details.entry_id                   8RXL 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              435 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              435 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              435 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                123.37 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            3.07 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ALA B 217 ? ? -92.85  -148.35 
2  1 LEU B 228 ? ? -165.60 109.60  
3  1 GLU B 280 ? ? -118.57 -162.19 
4  1 LYS B 281 ? ? 65.19   -126.36 
5  1 LYS B 282 ? ? -72.99  -159.21 
6  1 ASP B 367 ? ? -45.74  78.87   
7  1 GLN B 418 ? ? 69.89   -0.72   
8  1 SER B 433 ? ? 41.22   -78.78  
9  1 ASP A 276 ? ? -26.25  -49.87  
10 1 GLU A 280 ? ? -104.26 43.09   
11 1 LYS A 282 ? ? 51.54   -71.59  
# 
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 B CYS 258 ? A CYS 43  
2  1 Y 1 B PRO 259 ? A PRO 44  
3  1 Y 1 B SER 260 ? A SER 45  
4  1 Y 1 B PRO 261 ? A PRO 46  
5  1 Y 1 B GLY 262 ? A GLY 47  
6  1 Y 1 B ALA 263 ? A ALA 48  
7  1 Y 1 B GLY 309 ? A GLY 94  
8  1 Y 1 B PRO 310 ? A PRO 95  
9  1 Y 1 B SER 311 ? A SER 96  
10 1 Y 1 B GLY 312 ? A GLY 97  
11 1 Y 1 B GLU 313 ? A GLU 98  
12 1 Y 1 B GLU 314 ? A GLU 99  
13 1 Y 1 B ALA 315 ? A ALA 100 
14 1 Y 1 B GLY 316 ? A GLY 101 
15 1 Y 1 B ALA 317 ? A ALA 102 
16 1 Y 1 B GLY 318 ? A GLY 103 
17 1 Y 1 B GLY 319 ? A GLY 104 
18 1 Y 1 B SER 320 ? A SER 105 
19 1 Y 1 B ILE 321 ? A ILE 106 
20 1 Y 1 B SER 322 ? A SER 107 
21 1 Y 1 B SER 323 ? A SER 108 
22 1 Y 1 B ASP 447 ? A ASP 232 
23 1 Y 1 B VAL 448 ? A VAL 233 
24 1 Y 1 B GLU 449 ? A GLU 234 
25 1 Y 1 B HIS 450 ? A HIS 235 
26 1 Y 1 B HIS 451 ? A HIS 236 
27 1 Y 1 B HIS 452 ? A HIS 237 
28 1 Y 1 B HIS 453 ? A HIS 238 
29 1 Y 1 B HIS 454 ? A HIS 239 
30 1 Y 1 B HIS 455 ? A HIS 240 
31 1 Y 1 A PRO 216 ? B PRO 1   
32 1 Y 1 A ALA 217 ? B ALA 2   
33 1 Y 1 A TRP 218 ? B TRP 3   
34 1 Y 1 A GLN 219 ? B GLN 4   
35 1 Y 1 A ALA 220 ? B ALA 5   
36 1 Y 1 A ARG 221 ? B ARG 6   
37 1 Y 1 A PRO 240 ? B PRO 25  
38 1 Y 1 A ASP 241 ? B ASP 26  
39 1 Y 1 A ALA 242 ? B ALA 27  
40 1 Y 1 A VAL 243 ? B VAL 28  
41 1 Y 1 A ASP 244 ? B ASP 29  
42 1 Y 1 A SER 245 ? B SER 30  
43 1 Y 1 A TYR 246 ? B TYR 31  
44 1 Y 1 A GLN 247 ? B GLN 32  
45 1 Y 1 A HIS 257 ? B HIS 42  
46 1 Y 1 A CYS 258 ? B CYS 43  
47 1 Y 1 A PRO 259 ? B PRO 44  
48 1 Y 1 A SER 260 ? B SER 45  
49 1 Y 1 A PRO 261 ? B PRO 46  
50 1 Y 1 A GLY 262 ? B GLY 47  
51 1 Y 1 A ALA 263 ? B ALA 48  
52 1 Y 1 A GLY 309 ? B GLY 94  
53 1 Y 1 A PRO 310 ? B PRO 95  
54 1 Y 1 A SER 311 ? B SER 96  
55 1 Y 1 A GLY 312 ? B GLY 97  
56 1 Y 1 A GLU 313 ? B GLU 98  
57 1 Y 1 A GLU 314 ? B GLU 99  
58 1 Y 1 A ALA 315 ? B ALA 100 
59 1 Y 1 A GLY 316 ? B GLY 101 
60 1 Y 1 A ALA 317 ? B ALA 102 
61 1 Y 1 A GLY 318 ? B GLY 103 
62 1 Y 1 A GLY 319 ? B GLY 104 
63 1 Y 1 A SER 320 ? B SER 105 
64 1 Y 1 A ILE 321 ? B ILE 106 
65 1 Y 1 A SER 322 ? B SER 107 
66 1 Y 1 A SER 323 ? B SER 108 
67 1 Y 1 A GLY 324 ? B GLY 109 
68 1 Y 1 A ASP 447 ? B ASP 232 
69 1 Y 1 A VAL 448 ? B VAL 233 
70 1 Y 1 A GLU 449 ? B GLU 234 
71 1 Y 1 A HIS 450 ? B HIS 235 
72 1 Y 1 A HIS 451 ? B HIS 236 
73 1 Y 1 A HIS 452 ? B HIS 237 
74 1 Y 1 A HIS 453 ? B HIS 238 
75 1 Y 1 A HIS 454 ? B HIS 239 
76 1 Y 1 A HIS 455 ? B HIS 240 
# 
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 
A1H3Z C10  C Y N 1   
A1H3Z C15  C Y N 2   
A1H3Z C17  C Y N 3   
A1H3Z C20  C Y N 4   
A1H3Z C21  C Y N 5   
A1H3Z C22  C Y N 6   
A1H3Z C01  C N N 7   
A1H3Z C02  C N N 8   
A1H3Z O03  O N N 9   
A1H3Z C04  C N N 10  
A1H3Z C05  C N N 11  
A1H3Z C06  C Y N 12  
A1H3Z C07  C Y N 13  
A1H3Z N08  N Y N 14  
A1H3Z C09  C Y N 15  
A1H3Z C11  C Y N 16  
A1H3Z C12  C Y N 17  
A1H3Z O13  O N N 18  
A1H3Z C14  C N N 19  
A1H3Z C16  C Y N 20  
A1H3Z C18  C Y N 21  
A1H3Z C19  C Y N 22  
A1H3Z H1   H N N 23  
A1H3Z H2   H N N 24  
A1H3Z H3   H N N 25  
A1H3Z H4   H N N 26  
A1H3Z H5   H N N 27  
A1H3Z H6   H N N 28  
A1H3Z H7   H N N 29  
A1H3Z H8   H N N 30  
A1H3Z H9   H N N 31  
A1H3Z H10  H N N 32  
A1H3Z H11  H N N 33  
A1H3Z H12  H N N 34  
A1H3Z H13  H N N 35  
A1H3Z H14  H N N 36  
A1H3Z H15  H N N 37  
A1H3Z H16  H N N 38  
A1H3Z H17  H N N 39  
A1H3Z H18  H N N 40  
A1H3Z H19  H N N 41  
ALA   N    N N N 42  
ALA   CA   C N S 43  
ALA   C    C N N 44  
ALA   O    O N N 45  
ALA   CB   C N N 46  
ALA   OXT  O N N 47  
ALA   H    H N N 48  
ALA   H2   H N N 49  
ALA   HA   H N N 50  
ALA   HB1  H N N 51  
ALA   HB2  H N N 52  
ALA   HB3  H N N 53  
ALA   HXT  H N N 54  
ARG   N    N N N 55  
ARG   CA   C N S 56  
ARG   C    C N N 57  
ARG   O    O N N 58  
ARG   CB   C N N 59  
ARG   CG   C N N 60  
ARG   CD   C N N 61  
ARG   NE   N N N 62  
ARG   CZ   C N N 63  
ARG   NH1  N N N 64  
ARG   NH2  N N N 65  
ARG   OXT  O N N 66  
ARG   H    H N N 67  
ARG   H2   H N N 68  
ARG   HA   H N N 69  
ARG   HB2  H N N 70  
ARG   HB3  H N N 71  
ARG   HG2  H N N 72  
ARG   HG3  H N N 73  
ARG   HD2  H N N 74  
ARG   HD3  H N N 75  
ARG   HE   H N N 76  
ARG   HH11 H N N 77  
ARG   HH12 H N N 78  
ARG   HH21 H N N 79  
ARG   HH22 H N N 80  
ARG   HXT  H N N 81  
ASN   N    N N N 82  
ASN   CA   C N S 83  
ASN   C    C N N 84  
ASN   O    O N N 85  
ASN   CB   C N N 86  
ASN   CG   C N N 87  
ASN   OD1  O N N 88  
ASN   ND2  N N N 89  
ASN   OXT  O N N 90  
ASN   H    H N N 91  
ASN   H2   H N N 92  
ASN   HA   H N N 93  
ASN   HB2  H N N 94  
ASN   HB3  H N N 95  
ASN   HD21 H N N 96  
ASN   HD22 H N N 97  
ASN   HXT  H N N 98  
ASP   N    N N N 99  
ASP   CA   C N S 100 
ASP   C    C N N 101 
ASP   O    O N N 102 
ASP   CB   C N N 103 
ASP   CG   C N N 104 
ASP   OD1  O N N 105 
ASP   OD2  O N N 106 
ASP   OXT  O N N 107 
ASP   H    H N N 108 
ASP   H2   H N N 109 
ASP   HA   H N N 110 
ASP   HB2  H N N 111 
ASP   HB3  H N N 112 
ASP   HD2  H N N 113 
ASP   HXT  H N N 114 
CYS   N    N N N 115 
CYS   CA   C N R 116 
CYS   C    C N N 117 
CYS   O    O N N 118 
CYS   CB   C N N 119 
CYS   SG   S N N 120 
CYS   OXT  O N N 121 
CYS   H    H N N 122 
CYS   H2   H N N 123 
CYS   HA   H N N 124 
CYS   HB2  H N N 125 
CYS   HB3  H N N 126 
CYS   HG   H N N 127 
CYS   HXT  H N N 128 
GLN   N    N N N 129 
GLN   CA   C N S 130 
GLN   C    C N N 131 
GLN   O    O N N 132 
GLN   CB   C N N 133 
GLN   CG   C N N 134 
GLN   CD   C N N 135 
GLN   OE1  O N N 136 
GLN   NE2  N N N 137 
GLN   OXT  O N N 138 
GLN   H    H N N 139 
GLN   H2   H N N 140 
GLN   HA   H N N 141 
GLN   HB2  H N N 142 
GLN   HB3  H N N 143 
GLN   HG2  H N N 144 
GLN   HG3  H N N 145 
GLN   HE21 H N N 146 
GLN   HE22 H N N 147 
GLN   HXT  H N N 148 
GLU   N    N N N 149 
GLU   CA   C N S 150 
GLU   C    C N N 151 
GLU   O    O N N 152 
GLU   CB   C N N 153 
GLU   CG   C N N 154 
GLU   CD   C N N 155 
GLU   OE1  O N N 156 
GLU   OE2  O N N 157 
GLU   OXT  O N N 158 
GLU   H    H N N 159 
GLU   H2   H N N 160 
GLU   HA   H N N 161 
GLU   HB2  H N N 162 
GLU   HB3  H N N 163 
GLU   HG2  H N N 164 
GLU   HG3  H N N 165 
GLU   HE2  H N N 166 
GLU   HXT  H N N 167 
GLY   N    N N N 168 
GLY   CA   C N N 169 
GLY   C    C N N 170 
GLY   O    O N N 171 
GLY   OXT  O N N 172 
GLY   H    H N N 173 
GLY   H2   H N N 174 
GLY   HA2  H N N 175 
GLY   HA3  H N N 176 
GLY   HXT  H N N 177 
GOL   C1   C N N 178 
GOL   O1   O N N 179 
GOL   C2   C N N 180 
GOL   O2   O N N 181 
GOL   C3   C N N 182 
GOL   O3   O N N 183 
GOL   H11  H N N 184 
GOL   H12  H N N 185 
GOL   HO1  H N N 186 
GOL   H2   H N N 187 
GOL   HO2  H N N 188 
GOL   H31  H N N 189 
GOL   H32  H N N 190 
GOL   HO3  H N N 191 
HIS   N    N N N 192 
HIS   CA   C N S 193 
HIS   C    C N N 194 
HIS   O    O N N 195 
HIS   CB   C N N 196 
HIS   CG   C Y N 197 
HIS   ND1  N Y N 198 
HIS   CD2  C Y N 199 
HIS   CE1  C Y N 200 
HIS   NE2  N Y N 201 
HIS   OXT  O N N 202 
HIS   H    H N N 203 
HIS   H2   H N N 204 
HIS   HA   H N N 205 
HIS   HB2  H N N 206 
HIS   HB3  H N N 207 
HIS   HD1  H N N 208 
HIS   HD2  H N N 209 
HIS   HE1  H N N 210 
HIS   HE2  H N N 211 
HIS   HXT  H N N 212 
HOH   O    O N N 213 
HOH   H1   H N N 214 
HOH   H2   H N N 215 
ILE   N    N N N 216 
ILE   CA   C N S 217 
ILE   C    C N N 218 
ILE   O    O N N 219 
ILE   CB   C N S 220 
ILE   CG1  C N N 221 
ILE   CG2  C N N 222 
ILE   CD1  C N N 223 
ILE   OXT  O N N 224 
ILE   H    H N N 225 
ILE   H2   H N N 226 
ILE   HA   H N N 227 
ILE   HB   H N N 228 
ILE   HG12 H N N 229 
ILE   HG13 H N N 230 
ILE   HG21 H N N 231 
ILE   HG22 H N N 232 
ILE   HG23 H N N 233 
ILE   HD11 H N N 234 
ILE   HD12 H N N 235 
ILE   HD13 H N N 236 
ILE   HXT  H N N 237 
LEU   N    N N N 238 
LEU   CA   C N S 239 
LEU   C    C N N 240 
LEU   O    O N N 241 
LEU   CB   C N N 242 
LEU   CG   C N N 243 
LEU   CD1  C N N 244 
LEU   CD2  C N N 245 
LEU   OXT  O N N 246 
LEU   H    H N N 247 
LEU   H2   H N N 248 
LEU   HA   H N N 249 
LEU   HB2  H N N 250 
LEU   HB3  H N N 251 
LEU   HG   H N N 252 
LEU   HD11 H N N 253 
LEU   HD12 H N N 254 
LEU   HD13 H N N 255 
LEU   HD21 H N N 256 
LEU   HD22 H N N 257 
LEU   HD23 H N N 258 
LEU   HXT  H N N 259 
LYS   N    N N N 260 
LYS   CA   C N S 261 
LYS   C    C N N 262 
LYS   O    O N N 263 
LYS   CB   C N N 264 
LYS   CG   C N N 265 
LYS   CD   C N N 266 
LYS   CE   C N N 267 
LYS   NZ   N N N 268 
LYS   OXT  O N N 269 
LYS   H    H N N 270 
LYS   H2   H N N 271 
LYS   HA   H N N 272 
LYS   HB2  H N N 273 
LYS   HB3  H N N 274 
LYS   HG2  H N N 275 
LYS   HG3  H N N 276 
LYS   HD2  H N N 277 
LYS   HD3  H N N 278 
LYS   HE2  H N N 279 
LYS   HE3  H N N 280 
LYS   HZ1  H N N 281 
LYS   HZ2  H N N 282 
LYS   HZ3  H N N 283 
LYS   HXT  H N N 284 
MET   N    N N N 285 
MET   CA   C N S 286 
MET   C    C N N 287 
MET   O    O N N 288 
MET   CB   C N N 289 
MET   CG   C N N 290 
MET   SD   S N N 291 
MET   CE   C N N 292 
MET   OXT  O N N 293 
MET   H    H N N 294 
MET   H2   H N N 295 
MET   HA   H N N 296 
MET   HB2  H N N 297 
MET   HB3  H N N 298 
MET   HG2  H N N 299 
MET   HG3  H N N 300 
MET   HE1  H N N 301 
MET   HE2  H N N 302 
MET   HE3  H N N 303 
MET   HXT  H N N 304 
PHE   N    N N N 305 
PHE   CA   C N S 306 
PHE   C    C N N 307 
PHE   O    O N N 308 
PHE   CB   C N N 309 
PHE   CG   C Y N 310 
PHE   CD1  C Y N 311 
PHE   CD2  C Y N 312 
PHE   CE1  C Y N 313 
PHE   CE2  C Y N 314 
PHE   CZ   C Y N 315 
PHE   OXT  O N N 316 
PHE   H    H N N 317 
PHE   H2   H N N 318 
PHE   HA   H N N 319 
PHE   HB2  H N N 320 
PHE   HB3  H N N 321 
PHE   HD1  H N N 322 
PHE   HD2  H N N 323 
PHE   HE1  H N N 324 
PHE   HE2  H N N 325 
PHE   HZ   H N N 326 
PHE   HXT  H N N 327 
PRO   N    N N N 328 
PRO   CA   C N S 329 
PRO   C    C N N 330 
PRO   O    O N N 331 
PRO   CB   C N N 332 
PRO   CG   C N N 333 
PRO   CD   C N N 334 
PRO   OXT  O N N 335 
PRO   H    H N N 336 
PRO   HA   H N N 337 
PRO   HB2  H N N 338 
PRO   HB3  H N N 339 
PRO   HG2  H N N 340 
PRO   HG3  H N N 341 
PRO   HD2  H N N 342 
PRO   HD3  H N N 343 
PRO   HXT  H N N 344 
SER   N    N N N 345 
SER   CA   C N S 346 
SER   C    C N N 347 
SER   O    O N N 348 
SER   CB   C N N 349 
SER   OG   O N N 350 
SER   OXT  O N N 351 
SER   H    H N N 352 
SER   H2   H N N 353 
SER   HA   H N N 354 
SER   HB2  H N N 355 
SER   HB3  H N N 356 
SER   HG   H N N 357 
SER   HXT  H N N 358 
THR   N    N N N 359 
THR   CA   C N S 360 
THR   C    C N N 361 
THR   O    O N N 362 
THR   CB   C N R 363 
THR   OG1  O N N 364 
THR   CG2  C N N 365 
THR   OXT  O N N 366 
THR   H    H N N 367 
THR   H2   H N N 368 
THR   HA   H N N 369 
THR   HB   H N N 370 
THR   HG1  H N N 371 
THR   HG21 H N N 372 
THR   HG22 H N N 373 
THR   HG23 H N N 374 
THR   HXT  H N N 375 
TRP   N    N N N 376 
TRP   CA   C N S 377 
TRP   C    C N N 378 
TRP   O    O N N 379 
TRP   CB   C N N 380 
TRP   CG   C Y N 381 
TRP   CD1  C Y N 382 
TRP   CD2  C Y N 383 
TRP   NE1  N Y N 384 
TRP   CE2  C Y N 385 
TRP   CE3  C Y N 386 
TRP   CZ2  C Y N 387 
TRP   CZ3  C Y N 388 
TRP   CH2  C Y N 389 
TRP   OXT  O N N 390 
TRP   H    H N N 391 
TRP   H2   H N N 392 
TRP   HA   H N N 393 
TRP   HB2  H N N 394 
TRP   HB3  H N N 395 
TRP   HD1  H N N 396 
TRP   HE1  H N N 397 
TRP   HE3  H N N 398 
TRP   HZ2  H N N 399 
TRP   HZ3  H N N 400 
TRP   HH2  H N N 401 
TRP   HXT  H N N 402 
TYR   N    N N N 403 
TYR   CA   C N S 404 
TYR   C    C N N 405 
TYR   O    O N N 406 
TYR   CB   C N N 407 
TYR   CG   C Y N 408 
TYR   CD1  C Y N 409 
TYR   CD2  C Y N 410 
TYR   CE1  C Y N 411 
TYR   CE2  C Y N 412 
TYR   CZ   C Y N 413 
TYR   OH   O N N 414 
TYR   OXT  O N N 415 
TYR   H    H N N 416 
TYR   H2   H N N 417 
TYR   HA   H N N 418 
TYR   HB2  H N N 419 
TYR   HB3  H N N 420 
TYR   HD1  H N N 421 
TYR   HD2  H N N 422 
TYR   HE1  H N N 423 
TYR   HE2  H N N 424 
TYR   HH   H N N 425 
TYR   HXT  H N N 426 
VAL   N    N N N 427 
VAL   CA   C N S 428 
VAL   C    C N N 429 
VAL   O    O N N 430 
VAL   CB   C N N 431 
VAL   CG1  C N N 432 
VAL   CG2  C N N 433 
VAL   OXT  O N N 434 
VAL   H    H N N 435 
VAL   H2   H N N 436 
VAL   HA   H N N 437 
VAL   HB   H N N 438 
VAL   HG11 H N N 439 
VAL   HG12 H N N 440 
VAL   HG13 H N N 441 
VAL   HG21 H N N 442 
VAL   HG22 H N N 443 
VAL   HG23 H N N 444 
VAL   HXT  H N N 445 
# 
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 
A1H3Z C18 C19  doub Y N 1   
A1H3Z C18 C17  sing Y N 2   
A1H3Z C19 C20  sing Y N 3   
A1H3Z C17 C16  doub Y N 4   
A1H3Z C20 C15  doub Y N 5   
A1H3Z C16 C15  sing Y N 6   
A1H3Z C15 C14  sing N N 7   
A1H3Z C14 O13  sing N N 8   
A1H3Z O13 C12  sing N N 9   
A1H3Z C21 C12  doub Y N 10  
A1H3Z C21 C22  sing Y N 11  
A1H3Z C12 C11  sing Y N 12  
A1H3Z C22 C09  doub Y N 13  
A1H3Z C11 C10  doub Y N 14  
A1H3Z C01 C02  sing N N 15  
A1H3Z C09 C10  sing Y N 16  
A1H3Z C09 N08  sing Y N 17  
A1H3Z C10 C06  sing Y N 18  
A1H3Z C02 C04  sing N N 19  
A1H3Z C02 O03  doub N N 20  
A1H3Z N08 C07  sing Y N 21  
A1H3Z C04 C05  sing N N 22  
A1H3Z C06 C05  sing N N 23  
A1H3Z C06 C07  doub Y N 24  
A1H3Z C17 H1   sing N N 25  
A1H3Z C20 H2   sing N N 26  
A1H3Z C21 H3   sing N N 27  
A1H3Z C22 H4   sing N N 28  
A1H3Z C01 H5   sing N N 29  
A1H3Z C01 H6   sing N N 30  
A1H3Z C01 H7   sing N N 31  
A1H3Z C04 H8   sing N N 32  
A1H3Z C04 H9   sing N N 33  
A1H3Z C05 H10  sing N N 34  
A1H3Z C05 H11  sing N N 35  
A1H3Z C07 H12  sing N N 36  
A1H3Z N08 H13  sing N N 37  
A1H3Z C11 H14  sing N N 38  
A1H3Z C14 H15  sing N N 39  
A1H3Z C14 H16  sing N N 40  
A1H3Z C16 H17  sing N N 41  
A1H3Z C18 H18  sing N N 42  
A1H3Z C19 H19  sing N N 43  
ALA   N   CA   sing N N 44  
ALA   N   H    sing N N 45  
ALA   N   H2   sing N N 46  
ALA   CA  C    sing N N 47  
ALA   CA  CB   sing N N 48  
ALA   CA  HA   sing N N 49  
ALA   C   O    doub N N 50  
ALA   C   OXT  sing N N 51  
ALA   CB  HB1  sing N N 52  
ALA   CB  HB2  sing N N 53  
ALA   CB  HB3  sing N N 54  
ALA   OXT HXT  sing N N 55  
ARG   N   CA   sing N N 56  
ARG   N   H    sing N N 57  
ARG   N   H2   sing N N 58  
ARG   CA  C    sing N N 59  
ARG   CA  CB   sing N N 60  
ARG   CA  HA   sing N N 61  
ARG   C   O    doub N N 62  
ARG   C   OXT  sing N N 63  
ARG   CB  CG   sing N N 64  
ARG   CB  HB2  sing N N 65  
ARG   CB  HB3  sing N N 66  
ARG   CG  CD   sing N N 67  
ARG   CG  HG2  sing N N 68  
ARG   CG  HG3  sing N N 69  
ARG   CD  NE   sing N N 70  
ARG   CD  HD2  sing N N 71  
ARG   CD  HD3  sing N N 72  
ARG   NE  CZ   sing N N 73  
ARG   NE  HE   sing N N 74  
ARG   CZ  NH1  sing N N 75  
ARG   CZ  NH2  doub N N 76  
ARG   NH1 HH11 sing N N 77  
ARG   NH1 HH12 sing N N 78  
ARG   NH2 HH21 sing N N 79  
ARG   NH2 HH22 sing N N 80  
ARG   OXT HXT  sing N N 81  
ASN   N   CA   sing N N 82  
ASN   N   H    sing N N 83  
ASN   N   H2   sing N N 84  
ASN   CA  C    sing N N 85  
ASN   CA  CB   sing N N 86  
ASN   CA  HA   sing N N 87  
ASN   C   O    doub N N 88  
ASN   C   OXT  sing N N 89  
ASN   CB  CG   sing N N 90  
ASN   CB  HB2  sing N N 91  
ASN   CB  HB3  sing N N 92  
ASN   CG  OD1  doub N N 93  
ASN   CG  ND2  sing N N 94  
ASN   ND2 HD21 sing N N 95  
ASN   ND2 HD22 sing N N 96  
ASN   OXT HXT  sing N N 97  
ASP   N   CA   sing N N 98  
ASP   N   H    sing N N 99  
ASP   N   H2   sing N N 100 
ASP   CA  C    sing N N 101 
ASP   CA  CB   sing N N 102 
ASP   CA  HA   sing N N 103 
ASP   C   O    doub N N 104 
ASP   C   OXT  sing N N 105 
ASP   CB  CG   sing N N 106 
ASP   CB  HB2  sing N N 107 
ASP   CB  HB3  sing N N 108 
ASP   CG  OD1  doub N N 109 
ASP   CG  OD2  sing N N 110 
ASP   OD2 HD2  sing N N 111 
ASP   OXT HXT  sing N N 112 
CYS   N   CA   sing N N 113 
CYS   N   H    sing N N 114 
CYS   N   H2   sing N N 115 
CYS   CA  C    sing N N 116 
CYS   CA  CB   sing N N 117 
CYS   CA  HA   sing N N 118 
CYS   C   O    doub N N 119 
CYS   C   OXT  sing N N 120 
CYS   CB  SG   sing N N 121 
CYS   CB  HB2  sing N N 122 
CYS   CB  HB3  sing N N 123 
CYS   SG  HG   sing N N 124 
CYS   OXT HXT  sing N N 125 
GLN   N   CA   sing N N 126 
GLN   N   H    sing N N 127 
GLN   N   H2   sing N N 128 
GLN   CA  C    sing N N 129 
GLN   CA  CB   sing N N 130 
GLN   CA  HA   sing N N 131 
GLN   C   O    doub N N 132 
GLN   C   OXT  sing N N 133 
GLN   CB  CG   sing N N 134 
GLN   CB  HB2  sing N N 135 
GLN   CB  HB3  sing N N 136 
GLN   CG  CD   sing N N 137 
GLN   CG  HG2  sing N N 138 
GLN   CG  HG3  sing N N 139 
GLN   CD  OE1  doub N N 140 
GLN   CD  NE2  sing N N 141 
GLN   NE2 HE21 sing N N 142 
GLN   NE2 HE22 sing N N 143 
GLN   OXT HXT  sing N N 144 
GLU   N   CA   sing N N 145 
GLU   N   H    sing N N 146 
GLU   N   H2   sing N N 147 
GLU   CA  C    sing N N 148 
GLU   CA  CB   sing N N 149 
GLU   CA  HA   sing N N 150 
GLU   C   O    doub N N 151 
GLU   C   OXT  sing N N 152 
GLU   CB  CG   sing N N 153 
GLU   CB  HB2  sing N N 154 
GLU   CB  HB3  sing N N 155 
GLU   CG  CD   sing N N 156 
GLU   CG  HG2  sing N N 157 
GLU   CG  HG3  sing N N 158 
GLU   CD  OE1  doub N N 159 
GLU   CD  OE2  sing N N 160 
GLU   OE2 HE2  sing N N 161 
GLU   OXT HXT  sing N N 162 
GLY   N   CA   sing N N 163 
GLY   N   H    sing N N 164 
GLY   N   H2   sing N N 165 
GLY   CA  C    sing N N 166 
GLY   CA  HA2  sing N N 167 
GLY   CA  HA3  sing N N 168 
GLY   C   O    doub N N 169 
GLY   C   OXT  sing N N 170 
GLY   OXT HXT  sing N N 171 
GOL   C1  O1   sing N N 172 
GOL   C1  C2   sing N N 173 
GOL   C1  H11  sing N N 174 
GOL   C1  H12  sing N N 175 
GOL   O1  HO1  sing N N 176 
GOL   C2  O2   sing N N 177 
GOL   C2  C3   sing N N 178 
GOL   C2  H2   sing N N 179 
GOL   O2  HO2  sing N N 180 
GOL   C3  O3   sing N N 181 
GOL   C3  H31  sing N N 182 
GOL   C3  H32  sing N N 183 
GOL   O3  HO3  sing N N 184 
HIS   N   CA   sing N N 185 
HIS   N   H    sing N N 186 
HIS   N   H2   sing N N 187 
HIS   CA  C    sing N N 188 
HIS   CA  CB   sing N N 189 
HIS   CA  HA   sing N N 190 
HIS   C   O    doub N N 191 
HIS   C   OXT  sing N N 192 
HIS   CB  CG   sing N N 193 
HIS   CB  HB2  sing N N 194 
HIS   CB  HB3  sing N N 195 
HIS   CG  ND1  sing Y N 196 
HIS   CG  CD2  doub Y N 197 
HIS   ND1 CE1  doub Y N 198 
HIS   ND1 HD1  sing N N 199 
HIS   CD2 NE2  sing Y N 200 
HIS   CD2 HD2  sing N N 201 
HIS   CE1 NE2  sing Y N 202 
HIS   CE1 HE1  sing N N 203 
HIS   NE2 HE2  sing N N 204 
HIS   OXT HXT  sing N N 205 
HOH   O   H1   sing N N 206 
HOH   O   H2   sing N N 207 
ILE   N   CA   sing N N 208 
ILE   N   H    sing N N 209 
ILE   N   H2   sing N N 210 
ILE   CA  C    sing N N 211 
ILE   CA  CB   sing N N 212 
ILE   CA  HA   sing N N 213 
ILE   C   O    doub N N 214 
ILE   C   OXT  sing N N 215 
ILE   CB  CG1  sing N N 216 
ILE   CB  CG2  sing N N 217 
ILE   CB  HB   sing N N 218 
ILE   CG1 CD1  sing N N 219 
ILE   CG1 HG12 sing N N 220 
ILE   CG1 HG13 sing N N 221 
ILE   CG2 HG21 sing N N 222 
ILE   CG2 HG22 sing N N 223 
ILE   CG2 HG23 sing N N 224 
ILE   CD1 HD11 sing N N 225 
ILE   CD1 HD12 sing N N 226 
ILE   CD1 HD13 sing N N 227 
ILE   OXT HXT  sing N N 228 
LEU   N   CA   sing N N 229 
LEU   N   H    sing N N 230 
LEU   N   H2   sing N N 231 
LEU   CA  C    sing N N 232 
LEU   CA  CB   sing N N 233 
LEU   CA  HA   sing N N 234 
LEU   C   O    doub N N 235 
LEU   C   OXT  sing N N 236 
LEU   CB  CG   sing N N 237 
LEU   CB  HB2  sing N N 238 
LEU   CB  HB3  sing N N 239 
LEU   CG  CD1  sing N N 240 
LEU   CG  CD2  sing N N 241 
LEU   CG  HG   sing N N 242 
LEU   CD1 HD11 sing N N 243 
LEU   CD1 HD12 sing N N 244 
LEU   CD1 HD13 sing N N 245 
LEU   CD2 HD21 sing N N 246 
LEU   CD2 HD22 sing N N 247 
LEU   CD2 HD23 sing N N 248 
LEU   OXT HXT  sing N N 249 
LYS   N   CA   sing N N 250 
LYS   N   H    sing N N 251 
LYS   N   H2   sing N N 252 
LYS   CA  C    sing N N 253 
LYS   CA  CB   sing N N 254 
LYS   CA  HA   sing N N 255 
LYS   C   O    doub N N 256 
LYS   C   OXT  sing N N 257 
LYS   CB  CG   sing N N 258 
LYS   CB  HB2  sing N N 259 
LYS   CB  HB3  sing N N 260 
LYS   CG  CD   sing N N 261 
LYS   CG  HG2  sing N N 262 
LYS   CG  HG3  sing N N 263 
LYS   CD  CE   sing N N 264 
LYS   CD  HD2  sing N N 265 
LYS   CD  HD3  sing N N 266 
LYS   CE  NZ   sing N N 267 
LYS   CE  HE2  sing N N 268 
LYS   CE  HE3  sing N N 269 
LYS   NZ  HZ1  sing N N 270 
LYS   NZ  HZ2  sing N N 271 
LYS   NZ  HZ3  sing N N 272 
LYS   OXT HXT  sing N N 273 
MET   N   CA   sing N N 274 
MET   N   H    sing N N 275 
MET   N   H2   sing N N 276 
MET   CA  C    sing N N 277 
MET   CA  CB   sing N N 278 
MET   CA  HA   sing N N 279 
MET   C   O    doub N N 280 
MET   C   OXT  sing N N 281 
MET   CB  CG   sing N N 282 
MET   CB  HB2  sing N N 283 
MET   CB  HB3  sing N N 284 
MET   CG  SD   sing N N 285 
MET   CG  HG2  sing N N 286 
MET   CG  HG3  sing N N 287 
MET   SD  CE   sing N N 288 
MET   CE  HE1  sing N N 289 
MET   CE  HE2  sing N N 290 
MET   CE  HE3  sing N N 291 
MET   OXT HXT  sing N N 292 
PHE   N   CA   sing N N 293 
PHE   N   H    sing N N 294 
PHE   N   H2   sing N N 295 
PHE   CA  C    sing N N 296 
PHE   CA  CB   sing N N 297 
PHE   CA  HA   sing N N 298 
PHE   C   O    doub N N 299 
PHE   C   OXT  sing N N 300 
PHE   CB  CG   sing N N 301 
PHE   CB  HB2  sing N N 302 
PHE   CB  HB3  sing N N 303 
PHE   CG  CD1  doub Y N 304 
PHE   CG  CD2  sing Y N 305 
PHE   CD1 CE1  sing Y N 306 
PHE   CD1 HD1  sing N N 307 
PHE   CD2 CE2  doub Y N 308 
PHE   CD2 HD2  sing N N 309 
PHE   CE1 CZ   doub Y N 310 
PHE   CE1 HE1  sing N N 311 
PHE   CE2 CZ   sing Y N 312 
PHE   CE2 HE2  sing N N 313 
PHE   CZ  HZ   sing N N 314 
PHE   OXT HXT  sing N N 315 
PRO   N   CA   sing N N 316 
PRO   N   CD   sing N N 317 
PRO   N   H    sing N N 318 
PRO   CA  C    sing N N 319 
PRO   CA  CB   sing N N 320 
PRO   CA  HA   sing N N 321 
PRO   C   O    doub N N 322 
PRO   C   OXT  sing N N 323 
PRO   CB  CG   sing N N 324 
PRO   CB  HB2  sing N N 325 
PRO   CB  HB3  sing N N 326 
PRO   CG  CD   sing N N 327 
PRO   CG  HG2  sing N N 328 
PRO   CG  HG3  sing N N 329 
PRO   CD  HD2  sing N N 330 
PRO   CD  HD3  sing N N 331 
PRO   OXT HXT  sing N N 332 
SER   N   CA   sing N N 333 
SER   N   H    sing N N 334 
SER   N   H2   sing N N 335 
SER   CA  C    sing N N 336 
SER   CA  CB   sing N N 337 
SER   CA  HA   sing N N 338 
SER   C   O    doub N N 339 
SER   C   OXT  sing N N 340 
SER   CB  OG   sing N N 341 
SER   CB  HB2  sing N N 342 
SER   CB  HB3  sing N N 343 
SER   OG  HG   sing N N 344 
SER   OXT HXT  sing N N 345 
THR   N   CA   sing N N 346 
THR   N   H    sing N N 347 
THR   N   H2   sing N N 348 
THR   CA  C    sing N N 349 
THR   CA  CB   sing N N 350 
THR   CA  HA   sing N N 351 
THR   C   O    doub N N 352 
THR   C   OXT  sing N N 353 
THR   CB  OG1  sing N N 354 
THR   CB  CG2  sing N N 355 
THR   CB  HB   sing N N 356 
THR   OG1 HG1  sing N N 357 
THR   CG2 HG21 sing N N 358 
THR   CG2 HG22 sing N N 359 
THR   CG2 HG23 sing N N 360 
THR   OXT HXT  sing N N 361 
TRP   N   CA   sing N N 362 
TRP   N   H    sing N N 363 
TRP   N   H2   sing N N 364 
TRP   CA  C    sing N N 365 
TRP   CA  CB   sing N N 366 
TRP   CA  HA   sing N N 367 
TRP   C   O    doub N N 368 
TRP   C   OXT  sing N N 369 
TRP   CB  CG   sing N N 370 
TRP   CB  HB2  sing N N 371 
TRP   CB  HB3  sing N N 372 
TRP   CG  CD1  doub Y N 373 
TRP   CG  CD2  sing Y N 374 
TRP   CD1 NE1  sing Y N 375 
TRP   CD1 HD1  sing N N 376 
TRP   CD2 CE2  doub Y N 377 
TRP   CD2 CE3  sing Y N 378 
TRP   NE1 CE2  sing Y N 379 
TRP   NE1 HE1  sing N N 380 
TRP   CE2 CZ2  sing Y N 381 
TRP   CE3 CZ3  doub Y N 382 
TRP   CE3 HE3  sing N N 383 
TRP   CZ2 CH2  doub Y N 384 
TRP   CZ2 HZ2  sing N N 385 
TRP   CZ3 CH2  sing Y N 386 
TRP   CZ3 HZ3  sing N N 387 
TRP   CH2 HH2  sing N N 388 
TRP   OXT HXT  sing N N 389 
TYR   N   CA   sing N N 390 
TYR   N   H    sing N N 391 
TYR   N   H2   sing N N 392 
TYR   CA  C    sing N N 393 
TYR   CA  CB   sing N N 394 
TYR   CA  HA   sing N N 395 
TYR   C   O    doub N N 396 
TYR   C   OXT  sing N N 397 
TYR   CB  CG   sing N N 398 
TYR   CB  HB2  sing N N 399 
TYR   CB  HB3  sing N N 400 
TYR   CG  CD1  doub Y N 401 
TYR   CG  CD2  sing Y N 402 
TYR   CD1 CE1  sing Y N 403 
TYR   CD1 HD1  sing N N 404 
TYR   CD2 CE2  doub Y N 405 
TYR   CD2 HD2  sing N N 406 
TYR   CE1 CZ   doub Y N 407 
TYR   CE1 HE1  sing N N 408 
TYR   CE2 CZ   sing Y N 409 
TYR   CE2 HE2  sing N N 410 
TYR   CZ  OH   sing N N 411 
TYR   OH  HH   sing N N 412 
TYR   OXT HXT  sing N N 413 
VAL   N   CA   sing N N 414 
VAL   N   H    sing N N 415 
VAL   N   H2   sing N N 416 
VAL   CA  C    sing N N 417 
VAL   CA  CB   sing N N 418 
VAL   CA  HA   sing N N 419 
VAL   C   O    doub N N 420 
VAL   C   OXT  sing N N 421 
VAL   CB  CG1  sing N N 422 
VAL   CB  CG2  sing N N 423 
VAL   CB  HB   sing N N 424 
VAL   CG1 HG11 sing N N 425 
VAL   CG1 HG12 sing N N 426 
VAL   CG1 HG13 sing N N 427 
VAL   CG2 HG21 sing N N 428 
VAL   CG2 HG22 sing N N 429 
VAL   CG2 HG23 sing N N 430 
VAL   OXT HXT  sing N N 431 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_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      PDB 
_pdbx_initial_refinement_model.accession_code   6S60 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8RXL 
_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]   0.008135 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004236 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016220 
_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]   0.014074 
_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 
# 
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   . PRO   A 1 1   ? -8.626  -16.959 30.728 1.00 130.38 ? 216 PRO   B N   1 
ATOM   2    C CA  . PRO   A 1 1   ? -8.629  -17.980 31.756 1.00 133.04 ? 216 PRO   B CA  1 
ATOM   3    C C   . PRO   A 1 1   ? -10.069 -18.520 31.870 1.00 133.84 ? 216 PRO   B C   1 
ATOM   4    O O   . PRO   A 1 1   ? -10.642 -18.894 30.845 1.00 125.41 ? 216 PRO   B O   1 
ATOM   5    C CB  . PRO   A 1 1   ? -8.124  -17.194 32.984 1.00 132.59 ? 216 PRO   B CB  1 
ATOM   6    C CG  . PRO   A 1 1   ? -8.621  -15.789 32.759 1.00 132.72 ? 216 PRO   B CG  1 
ATOM   7    C CD  . PRO   A 1 1   ? -8.983  -15.646 31.299 1.00 132.40 ? 216 PRO   B CD  1 
ATOM   8    N N   . ALA   A 1 2   ? -10.640 -18.592 33.073 1.00 140.98 ? 217 ALA   B N   1 
ATOM   9    C CA  . ALA   A 1 2   ? -12.089 -18.658 33.243 1.00 134.60 ? 217 ALA   B CA  1 
ATOM   10   C C   . ALA   A 1 2   ? -12.607 -17.212 33.430 1.00 133.05 ? 217 ALA   B C   1 
ATOM   11   O O   . ALA   A 1 2   ? -12.021 -16.281 32.853 1.00 128.00 ? 217 ALA   B O   1 
ATOM   12   C CB  . ALA   A 1 2   ? -12.435 -19.556 34.414 1.00 129.76 ? 217 ALA   B CB  1 
ATOM   13   N N   . TRP   A 1 3   ? -13.686 -17.015 34.204 1.00 126.09 ? 218 TRP   B N   1 
ATOM   14   C CA  . TRP   A 1 3   ? -14.401 -15.719 34.297 1.00 118.35 ? 218 TRP   B CA  1 
ATOM   15   C C   . TRP   A 1 3   ? -15.095 -15.274 32.998 1.00 108.49 ? 218 TRP   B C   1 
ATOM   16   O O   . TRP   A 1 3   ? -15.505 -14.113 32.865 1.00 87.04  ? 218 TRP   B O   1 
ATOM   17   C CB  . TRP   A 1 3   ? -13.479 -14.609 34.820 1.00 122.63 ? 218 TRP   B CB  1 
ATOM   18   C CG  . TRP   A 1 3   ? -13.346 -14.617 36.278 1.00 130.86 ? 218 TRP   B CG  1 
ATOM   19   C CD1 . TRP   A 1 3   ? -14.311 -14.283 37.183 1.00 136.67 ? 218 TRP   B CD1 1 
ATOM   20   C CD2 . TRP   A 1 3   ? -12.179 -14.961 37.033 1.00 129.95 ? 218 TRP   B CD2 1 
ATOM   21   N NE1 . TRP   A 1 3   ? -13.822 -14.402 38.459 1.00 133.41 ? 218 TRP   B NE1 1 
ATOM   22   C CE2 . TRP   A 1 3   ? -12.515 -14.815 38.399 1.00 127.35 ? 218 TRP   B CE2 1 
ATOM   23   C CE3 . TRP   A 1 3   ? -10.883 -15.386 36.693 1.00 124.77 ? 218 TRP   B CE3 1 
ATOM   24   C CZ2 . TRP   A 1 3   ? -11.603 -15.075 39.428 1.00 121.35 ? 218 TRP   B CZ2 1 
ATOM   25   C CZ3 . TRP   A 1 3   ? -9.968  -15.639 37.724 1.00 123.54 ? 218 TRP   B CZ3 1 
ATOM   26   C CH2 . TRP   A 1 3   ? -10.339 -15.483 39.076 1.00 120.87 ? 218 TRP   B CH2 1 
ATOM   27   N N   . GLN   A 1 4   ? -15.271 -16.229 32.081 1.00 116.75 ? 219 GLN   B N   1 
ATOM   28   C CA  . GLN   A 1 4   ? -15.834 -16.010 30.748 1.00 111.25 ? 219 GLN   B CA  1 
ATOM   29   C C   . GLN   A 1 4   ? -17.290 -16.377 30.872 1.00 104.96 ? 219 GLN   B C   1 
ATOM   30   O O   . GLN   A 1 4   ? -17.657 -17.230 31.685 1.00 99.27  ? 219 GLN   B O   1 
ATOM   31   C CB  . GLN   A 1 4   ? -15.196 -16.927 29.685 1.00 118.04 ? 219 GLN   B CB  1 
ATOM   32   C CG  . GLN   A 1 4   ? -13.713 -17.250 29.871 1.00 125.06 ? 219 GLN   B CG  1 
ATOM   33   C CD  . GLN   A 1 4   ? -13.104 -17.962 28.669 1.00 126.18 ? 219 GLN   B CD  1 
ATOM   34   O OE1 . GLN   A 1 4   ? -13.656 -18.946 28.164 1.00 126.25 ? 219 GLN   B OE1 1 
ATOM   35   N NE2 . GLN   A 1 4   ? -11.951 -17.472 28.215 1.00 120.16 ? 219 GLN   B NE2 1 
ATOM   36   N N   . ALA   A 1 5   ? -18.120 -15.742 30.059 1.00 102.67 ? 220 ALA   B N   1 
ATOM   37   C CA  . ALA   A 1 5   ? -19.555 -15.894 30.195 1.00 95.26  ? 220 ALA   B CA  1 
ATOM   38   C C   . ALA   A 1 5   ? -20.009 -17.272 29.713 1.00 94.68  ? 220 ALA   B C   1 
ATOM   39   O O   . ALA   A 1 5   ? -19.423 -17.864 28.795 1.00 95.04  ? 220 ALA   B O   1 
ATOM   40   C CB  . ALA   A 1 5   ? -20.283 -14.796 29.440 1.00 95.07  ? 220 ALA   B CB  1 
ATOM   41   N N   . ARG   A 1 6   ? -21.045 -17.762 30.380 1.00 84.79  ? 221 ARG   B N   1 
ATOM   42   C CA  . ARG   A 1 6   ? -21.763 -18.971 29.996 1.00 81.59  ? 221 ARG   B CA  1 
ATOM   43   C C   . ARG   A 1 6   ? -23.139 -18.674 29.339 1.00 77.97  ? 221 ARG   B C   1 
ATOM   44   O O   . ARG   A 1 6   ? -23.696 -19.551 28.685 1.00 84.51  ? 221 ARG   B O   1 
ATOM   45   C CB  . ARG   A 1 6   ? -21.894 -19.944 31.185 1.00 87.43  ? 221 ARG   B CB  1 
ATOM   46   C CG  . ARG   A 1 6   ? -22.006 -19.361 32.605 1.00 106.27 ? 221 ARG   B CG  1 
ATOM   47   C CD  . ARG   A 1 6   ? -23.173 -18.392 32.895 1.00 119.21 ? 221 ARG   B CD  1 
ATOM   48   N NE  . ARG   A 1 6   ? -24.512 -18.800 32.430 1.00 130.24 ? 221 ARG   B NE  1 
ATOM   49   C CZ  . ARG   A 1 6   ? -25.278 -19.758 32.967 1.00 132.89 ? 221 ARG   B CZ  1 
ATOM   50   N NH1 . ARG   A 1 6   ? -24.854 -20.498 33.993 1.00 130.24 ? 221 ARG   B NH1 1 
ATOM   51   N NH2 . ARG   A 1 6   ? -26.484 -20.000 32.447 1.00 138.08 ? 221 ARG   B NH2 1 
ATOM   52   N N   . GLY   A 1 7   ? -23.676 -17.457 29.499 1.00 71.68  ? 222 GLY   B N   1 
ATOM   53   C CA  . GLY   A 1 7   ? -24.908 -17.026 28.813 1.00 62.94  ? 222 GLY   B CA  1 
ATOM   54   C C   . GLY   A 1 7   ? -24.822 -15.571 28.382 1.00 56.95  ? 222 GLY   B C   1 
ATOM   55   O O   . GLY   A 1 7   ? -23.775 -14.950 28.484 1.00 50.58  ? 222 GLY   B O   1 
ATOM   56   N N   . LEU   A 1 8   ? -25.928 -15.026 27.903 1.00 53.30  ? 223 LEU   B N   1 
ATOM   57   C CA  . LEU   A 1 8   ? -25.989 -13.635 27.496 1.00 50.74  ? 223 LEU   B CA  1 
ATOM   58   C C   . LEU   A 1 8   ? -26.234 -12.785 28.731 1.00 49.07  ? 223 LEU   B C   1 
ATOM   59   O O   . LEU   A 1 8   ? -27.365 -12.489 29.109 1.00 46.01  ? 223 LEU   B O   1 
ATOM   60   C CB  . LEU   A 1 8   ? -27.088 -13.429 26.457 1.00 56.21  ? 223 LEU   B CB  1 
ATOM   61   C CG  . LEU   A 1 8   ? -27.105 -12.110 25.678 1.00 59.68  ? 223 LEU   B CG  1 
ATOM   62   C CD1 . LEU   A 1 8   ? -26.761 -12.330 24.223 1.00 61.47  ? 223 LEU   B CD1 1 
ATOM   63   C CD2 . LEU   A 1 8   ? -28.490 -11.504 25.726 1.00 66.68  ? 223 LEU   B CD2 1 
ATOM   64   N N   . GLY   A 1 9   ? -25.144 -12.413 29.380 1.00 46.29  ? 224 GLY   B N   1 
ATOM   65   C CA  . GLY   A 1 9   ? -25.230 -11.628 30.582 1.00 47.57  ? 224 GLY   B CA  1 
ATOM   66   C C   . GLY   A 1 9   ? -23.853 -11.327 31.116 1.00 48.83  ? 224 GLY   B C   1 
ATOM   67   O O   . GLY   A 1 9   ? -22.864 -11.919 30.693 1.00 51.33  ? 224 GLY   B O   1 
ATOM   68   N N   . THR   A 1 10  ? -23.821 -10.378 32.029 1.00 51.74  ? 225 THR   B N   1 
ATOM   69   C CA  . THR   A 1 10  ? -22.659 -10.073 32.839 1.00 59.17  ? 225 THR   B CA  1 
ATOM   70   C C   . THR   A 1 10  ? -23.061 -10.296 34.286 1.00 58.08  ? 225 THR   B C   1 
ATOM   71   O O   . THR   A 1 10  ? -24.210 -10.643 34.545 1.00 62.20  ? 225 THR   B O   1 
ATOM   72   C CB  . THR   A 1 10  ? -22.153 -8.626  32.667 1.00 59.83  ? 225 THR   B CB  1 
ATOM   73   O OG1 . THR   A 1 10  ? -21.090 -8.396  33.596 1.00 71.15  ? 225 THR   B OG1 1 
ATOM   74   C CG2 . THR   A 1 10  ? -23.204 -7.600  32.960 1.00 60.69  ? 225 THR   B CG2 1 
ATOM   75   N N   . ALA   A 1 11  ? -22.114 -10.110 35.204 1.00 51.57  ? 226 ALA   B N   1 
ATOM   76   C CA  . ALA   A 1 11  ? -22.392 -10.157 36.644 1.00 53.84  ? 226 ALA   B CA  1 
ATOM   77   C C   . ALA   A 1 11  ? -23.331 -9.039  37.128 1.00 52.91  ? 226 ALA   B C   1 
ATOM   78   O O   . ALA   A 1 11  ? -24.016 -9.194  38.146 1.00 62.27  ? 226 ALA   B O   1 
ATOM   79   C CB  . ALA   A 1 11  ? -21.086 -10.111 37.425 1.00 54.87  ? 226 ALA   B CB  1 
ATOM   80   N N   . ARG   A 1 12  ? -23.302 -7.896  36.443 1.00 49.52  ? 227 ARG   B N   1 
ATOM   81   C CA  . ARG   A 1 12  ? -24.202 -6.777  36.707 1.00 48.70  ? 227 ARG   B CA  1 
ATOM   82   C C   . ARG   A 1 12  ? -25.546 -6.831  36.000 1.00 51.01  ? 227 ARG   B C   1 
ATOM   83   O O   . ARG   A 1 12  ? -26.452 -6.131  36.400 1.00 51.88  ? 227 ARG   B O   1 
ATOM   84   C CB  . ARG   A 1 12  ? -23.559 -5.453  36.285 1.00 53.80  ? 227 ARG   B CB  1 
ATOM   85   C CG  . ARG   A 1 12  ? -22.211 -5.134  36.916 1.00 54.87  ? 227 ARG   B CG  1 
ATOM   86   C CD  . ARG   A 1 12  ? -21.746 -3.759  36.489 1.00 53.96  ? 227 ARG   B CD  1 
ATOM   87   N NE  . ARG   A 1 12  ? -22.404 -2.712  37.261 1.00 60.56  ? 227 ARG   B NE  1 
ATOM   88   C CZ  . ARG   A 1 12  ? -22.336 -1.405  37.004 1.00 62.62  ? 227 ARG   B CZ  1 
ATOM   89   N NH1 . ARG   A 1 12  ? -21.648 -0.936  35.960 1.00 64.87  ? 227 ARG   B NH1 1 
ATOM   90   N NH2 . ARG   A 1 12  ? -22.986 -0.556  37.793 1.00 59.76  ? 227 ARG   B NH2 1 
ATOM   91   N N   . LEU   A 1 13  ? -25.684 -7.623  34.943 1.00 53.11  ? 228 LEU   B N   1 
ATOM   92   C CA  . LEU   A 1 13  ? -26.895 -7.595  34.148 1.00 48.33  ? 228 LEU   B CA  1 
ATOM   93   C C   . LEU   A 1 13  ? -27.013 -8.787  33.216 1.00 49.01  ? 228 LEU   B C   1 
ATOM   94   O O   . LEU   A 1 13  ? -26.305 -8.904  32.207 1.00 55.28  ? 228 LEU   B O   1 
ATOM   95   C CB  . LEU   A 1 13  ? -27.004 -6.318  33.358 1.00 46.09  ? 228 LEU   B CB  1 
ATOM   96   C CG  . LEU   A 1 13  ? -28.443 -6.088  32.914 1.00 48.14  ? 228 LEU   B CG  1 
ATOM   97   C CD1 . LEU   A 1 13  ? -29.360 -5.641  34.056 1.00 48.64  ? 228 LEU   B CD1 1 
ATOM   98   C CD2 . LEU   A 1 13  ? -28.410 -5.056  31.808 1.00 48.76  ? 228 LEU   B CD2 1 
ATOM   99   N N   . GLN   A 1 14  ? -27.953 -9.645  33.561 1.00 50.50  ? 229 GLN   B N   1 
ATOM   100  C CA  . GLN   A 1 14  ? -28.217 -10.861 32.846 1.00 55.51  ? 229 GLN   B CA  1 
ATOM   101  C C   . GLN   A 1 14  ? -29.506 -10.628 32.072 1.00 53.57  ? 229 GLN   B C   1 
ATOM   102  O O   . GLN   A 1 14  ? -30.414 -9.938  32.558 1.00 45.34  ? 229 GLN   B O   1 
ATOM   103  C CB  . GLN   A 1 14  ? -28.375 -12.020 33.839 1.00 61.59  ? 229 GLN   B CB  1 
ATOM   104  C CG  . GLN   A 1 14  ? -27.204 -12.210 34.828 1.00 71.16  ? 229 GLN   B CG  1 
ATOM   105  C CD  . GLN   A 1 14  ? -27.257 -11.343 36.114 1.00 74.91  ? 229 GLN   B CD  1 
ATOM   106  O OE1 . GLN   A 1 14  ? -28.233 -11.351 36.881 1.00 77.84  ? 229 GLN   B OE1 1 
ATOM   107  N NE2 . GLN   A 1 14  ? -26.176 -10.619 36.363 1.00 79.85  ? 229 GLN   B NE2 1 
ATOM   108  N N   . LEU   A 1 15  ? -29.564 -11.161 30.852 1.00 53.70  ? 230 LEU   B N   1 
ATOM   109  C CA  . LEU   A 1 15  ? -30.823 -11.273 30.136 1.00 52.77  ? 230 LEU   B CA  1 
ATOM   110  C C   . LEU   A 1 15  ? -31.542 -12.469 30.684 1.00 52.19  ? 230 LEU   B C   1 
ATOM   111  O O   . LEU   A 1 15  ? -30.962 -13.530 30.858 1.00 51.26  ? 230 LEU   B O   1 
ATOM   112  C CB  . LEU   A 1 15  ? -30.642 -11.478 28.637 1.00 56.30  ? 230 LEU   B CB  1 
ATOM   113  C CG  . LEU   A 1 15  ? -31.936 -11.561 27.786 1.00 56.17  ? 230 LEU   B CG  1 
ATOM   114  C CD1 . LEU   A 1 15  ? -32.525 -10.194 27.502 1.00 49.90  ? 230 LEU   B CD1 1 
ATOM   115  C CD2 . LEU   A 1 15  ? -31.718 -12.299 26.477 1.00 60.91  ? 230 LEU   B CD2 1 
ATOM   116  N N   . VAL   A 1 16  ? -32.823 -12.283 30.933 1.00 53.62  ? 231 VAL   B N   1 
ATOM   117  C CA  . VAL   A 1 16  ? -33.665 -13.343 31.434 1.00 60.43  ? 231 VAL   B CA  1 
ATOM   118  C C   . VAL   A 1 16  ? -34.394 -13.894 30.236 1.00 56.68  ? 231 VAL   B C   1 
ATOM   119  O O   . VAL   A 1 16  ? -34.358 -15.078 29.969 1.00 55.95  ? 231 VAL   B O   1 
ATOM   120  C CB  . VAL   A 1 16  ? -34.657 -12.799 32.490 1.00 61.33  ? 231 VAL   B CB  1 
ATOM   121  C CG1 . VAL   A 1 16  ? -35.703 -13.838 32.884 1.00 58.66  ? 231 VAL   B CG1 1 
ATOM   122  C CG2 . VAL   A 1 16  ? -33.873 -12.319 33.706 1.00 64.60  ? 231 VAL   B CG2 1 
ATOM   123  N N   . GLU   A 1 17  ? -35.051 -13.003 29.519 1.00 57.86  ? 232 GLU   B N   1 
ATOM   124  C CA  . GLU   A 1 17  ? -35.858 -13.374 28.394 1.00 60.48  ? 232 GLU   B CA  1 
ATOM   125  C C   . GLU   A 1 17  ? -35.923 -12.272 27.338 1.00 57.90  ? 232 GLU   B C   1 
ATOM   126  O O   . GLU   A 1 17  ? -35.919 -11.077 27.644 1.00 59.33  ? 232 GLU   B O   1 
ATOM   127  C CB  . GLU   A 1 17  ? -37.263 -13.727 28.872 1.00 64.34  ? 232 GLU   B CB  1 
ATOM   128  C CG  . GLU   A 1 17  ? -37.561 -15.209 28.867 1.00 75.70  ? 232 GLU   B CG  1 
ATOM   129  C CD  . GLU   A 1 17  ? -38.968 -15.496 28.368 1.00 82.56  ? 232 GLU   B CD  1 
ATOM   130  O OE1 . GLU   A 1 17  ? -39.119 -16.238 27.382 1.00 86.65  ? 232 GLU   B OE1 1 
ATOM   131  O OE2 . GLU   A 1 17  ? -39.923 -14.951 28.948 1.00 84.82  ? 232 GLU   B OE2 1 
ATOM   132  N N   . PHE   A 1 18  ? -35.946 -12.706 26.084 1.00 55.58  ? 233 PHE   B N   1 
ATOM   133  C CA  . PHE   A 1 18  ? -36.245 -11.842 24.964 1.00 52.31  ? 233 PHE   B CA  1 
ATOM   134  C C   . PHE   A 1 18  ? -37.134 -12.601 23.978 1.00 49.48  ? 233 PHE   B C   1 
ATOM   135  O O   . PHE   A 1 18  ? -36.931 -13.787 23.733 1.00 49.95  ? 233 PHE   B O   1 
ATOM   136  C CB  . PHE   A 1 18  ? -34.960 -11.371 24.279 1.00 52.63  ? 233 PHE   B CB  1 
ATOM   137  C CG  . PHE   A 1 18  ? -35.207 -10.679 22.963 1.00 53.92  ? 233 PHE   B CG  1 
ATOM   138  C CD1 . PHE   A 1 18  ? -35.254 -11.407 21.785 1.00 55.76  ? 233 PHE   B CD1 1 
ATOM   139  C CD2 . PHE   A 1 18  ? -35.454 -9.321  22.914 1.00 54.63  ? 233 PHE   B CD2 1 
ATOM   140  C CE1 . PHE   A 1 18  ? -35.519 -10.791 20.585 1.00 57.75  ? 233 PHE   B CE1 1 
ATOM   141  C CE2 . PHE   A 1 18  ? -35.708 -8.695  21.715 1.00 55.62  ? 233 PHE   B CE2 1 
ATOM   142  C CZ  . PHE   A 1 18  ? -35.737 -9.436  20.552 1.00 57.49  ? 233 PHE   B CZ  1 
ATOM   143  N N   . SER   A 1 19  ? -38.123 -11.925 23.415 1.00 48.30  ? 234 SER   B N   1 
ATOM   144  C CA  . SER   A 1 19  ? -38.927 -12.521 22.361 1.00 46.09  ? 234 SER   B CA  1 
ATOM   145  C C   . SER   A 1 19  ? -39.515 -11.435 21.478 1.00 46.49  ? 234 SER   B C   1 
ATOM   146  O O   . SER   A 1 19  ? -39.804 -10.338 21.954 1.00 51.92  ? 234 SER   B O   1 
ATOM   147  C CB  . SER   A 1 19  ? -40.014 -13.377 22.962 1.00 48.17  ? 234 SER   B CB  1 
ATOM   148  O OG  . SER   A 1 19  ? -41.119 -12.590 23.367 1.00 56.70  ? 234 SER   B OG  1 
ATOM   149  N N   . ALA   A 1 20  ? -39.663 -11.732 20.191 1.00 45.86  ? 235 ALA   B N   1 
ATOM   150  C CA  . ALA   A 1 20  ? -40.375 -10.852 19.264 1.00 42.68  ? 235 ALA   B CA  1 
ATOM   151  C C   . ALA   A 1 20  ? -41.472 -11.706 18.688 1.00 38.71  ? 235 ALA   B C   1 
ATOM   152  O O   . ALA   A 1 20  ? -41.235 -12.858 18.372 1.00 38.30  ? 235 ALA   B O   1 
ATOM   153  C CB  . ALA   A 1 20  ? -39.439 -10.332 18.181 1.00 44.36  ? 235 ALA   B CB  1 
ATOM   154  N N   . PHE   A 1 21  ? -42.680 -11.169 18.586 1.00 38.56  ? 236 PHE   B N   1 
ATOM   155  C CA  . PHE   A 1 21  ? -43.817 -12.036 18.340 1.00 39.19  ? 236 PHE   B CA  1 
ATOM   156  C C   . PHE   A 1 21  ? -44.964 -11.352 17.650 1.00 38.18  ? 236 PHE   B C   1 
ATOM   157  O O   . PHE   A 1 21  ? -44.930 -10.151 17.436 1.00 40.08  ? 236 PHE   B O   1 
ATOM   158  C CB  . PHE   A 1 21  ? -44.282 -12.668 19.673 1.00 44.02  ? 236 PHE   B CB  1 
ATOM   159  C CG  . PHE   A 1 21  ? -44.808 -11.685 20.674 1.00 40.83  ? 236 PHE   B CG  1 
ATOM   160  C CD1 . PHE   A 1 21  ? -46.141 -11.288 20.643 1.00 44.57  ? 236 PHE   B CD1 1 
ATOM   161  C CD2 . PHE   A 1 21  ? -43.977 -11.166 21.644 1.00 41.59  ? 236 PHE   B CD2 1 
ATOM   162  C CE1 . PHE   A 1 21  ? -46.628 -10.366 21.564 1.00 50.17  ? 236 PHE   B CE1 1 
ATOM   163  C CE2 . PHE   A 1 21  ? -44.453 -10.246 22.571 1.00 45.70  ? 236 PHE   B CE2 1 
ATOM   164  C CZ  . PHE   A 1 21  ? -45.779 -9.842  22.533 1.00 47.59  ? 236 PHE   B CZ  1 
ATOM   165  N N   . VAL   A 1 22  ? -45.956 -12.143 17.267 1.00 41.55  ? 237 VAL   B N   1 
ATOM   166  C CA  . VAL   A 1 22  ? -47.224 -11.619 16.760 1.00 44.82  ? 237 VAL   B CA  1 
ATOM   167  C C   . VAL   A 1 22  ? -48.386 -12.471 17.259 1.00 49.63  ? 237 VAL   B C   1 
ATOM   168  O O   . VAL   A 1 22  ? -48.307 -13.707 17.268 1.00 48.77  ? 237 VAL   B O   1 
ATOM   169  C CB  . VAL   A 1 22  ? -47.271 -11.514 15.217 1.00 48.17  ? 237 VAL   B CB  1 
ATOM   170  C CG1 . VAL   A 1 22  ? -46.963 -12.841 14.527 1.00 46.84  ? 237 VAL   B CG1 1 
ATOM   171  C CG2 . VAL   A 1 22  ? -48.637 -10.973 14.744 1.00 47.86  ? 237 VAL   B CG2 1 
ATOM   172  N N   . GLU   A 1 23  ? -49.446 -11.797 17.698 1.00 51.83  ? 238 GLU   B N   1 
ATOM   173  C CA  . GLU   A 1 23  ? -50.662 -12.447 18.180 1.00 53.33  ? 238 GLU   B CA  1 
ATOM   174  C C   . GLU   A 1 23  ? -51.694 -12.035 17.165 1.00 56.77  ? 238 GLU   B C   1 
ATOM   175  O O   . GLU   A 1 23  ? -51.877 -10.826 16.960 1.00 59.44  ? 238 GLU   B O   1 
ATOM   176  C CB  . GLU   A 1 23  ? -51.063 -11.890 19.570 1.00 56.95  ? 238 GLU   B CB  1 
ATOM   177  C CG  . GLU   A 1 23  ? -49.987 -11.955 20.677 1.00 52.98  ? 238 GLU   B CG  1 
ATOM   178  C CD  . GLU   A 1 23  ? -50.282 -11.064 21.882 1.00 51.22  ? 238 GLU   B CD  1 
ATOM   179  O OE1 . GLU   A 1 23  ? -50.910 -9.984  21.730 1.00 55.37  ? 238 GLU   B OE1 1 
ATOM   180  O OE2 . GLU   A 1 23  ? -49.866 -11.423 22.999 1.00 48.12  ? 238 GLU   B OE2 1 
ATOM   181  N N   . PRO   A 1 24  ? -52.367 -12.998 16.504 1.00 63.35  ? 239 PRO   B N   1 
ATOM   182  C CA  . PRO   A 1 24  ? -53.271 -12.589 15.425 1.00 63.61  ? 239 PRO   B CA  1 
ATOM   183  C C   . PRO   A 1 24  ? -54.549 -11.987 15.965 1.00 66.95  ? 239 PRO   B C   1 
ATOM   184  O O   . PRO   A 1 24  ? -54.826 -12.138 17.153 1.00 71.94  ? 239 PRO   B O   1 
ATOM   185  C CB  . PRO   A 1 24  ? -53.561 -13.898 14.705 1.00 62.54  ? 239 PRO   B CB  1 
ATOM   186  C CG  . PRO   A 1 24  ? -53.482 -14.910 15.791 1.00 67.49  ? 239 PRO   B CG  1 
ATOM   187  C CD  . PRO   A 1 24  ? -52.336 -14.463 16.649 1.00 65.40  ? 239 PRO   B CD  1 
ATOM   188  N N   . PRO   A 1 25  ? -55.344 -11.328 15.098 1.00 80.42  ? 240 PRO   B N   1 
ATOM   189  C CA  . PRO   A 1 25  ? -56.576 -10.653 15.542 1.00 81.07  ? 240 PRO   B CA  1 
ATOM   190  C C   . PRO   A 1 25  ? -57.614 -11.548 16.238 1.00 87.53  ? 240 PRO   B C   1 
ATOM   191  O O   . PRO   A 1 25  ? -58.444 -11.036 16.990 1.00 93.78  ? 240 PRO   B O   1 
ATOM   192  C CB  . PRO   A 1 25  ? -57.151 -10.076 14.238 1.00 85.82  ? 240 PRO   B CB  1 
ATOM   193  C CG  . PRO   A 1 25  ? -55.994 -9.990  13.304 1.00 83.54  ? 240 PRO   B CG  1 
ATOM   194  C CD  . PRO   A 1 25  ? -55.161 -11.196 13.636 1.00 83.51  ? 240 PRO   B CD  1 
ATOM   195  N N   . ASP   A 1 26  ? -57.555 -12.856 15.982 1.00 88.87  ? 241 ASP   B N   1 
ATOM   196  C CA  . ASP   A 1 26  ? -58.400 -13.859 16.653 1.00 90.66  ? 241 ASP   B CA  1 
ATOM   197  C C   . ASP   A 1 26  ? -57.835 -14.415 17.994 1.00 90.32  ? 241 ASP   B C   1 
ATOM   198  O O   . ASP   A 1 26  ? -58.452 -15.299 18.605 1.00 84.42  ? 241 ASP   B O   1 
ATOM   199  C CB  . ASP   A 1 26  ? -58.691 -15.013 15.667 1.00 90.59  ? 241 ASP   B CB  1 
ATOM   200  C CG  . ASP   A 1 26  ? -57.420 -15.703 15.166 1.00 93.53  ? 241 ASP   B CG  1 
ATOM   201  O OD1 . ASP   A 1 26  ? -56.852 -16.519 15.919 1.00 94.86  ? 241 ASP   B OD1 1 
ATOM   202  O OD2 . ASP   A 1 26  ? -56.986 -15.425 14.021 1.00 98.31  ? 241 ASP   B OD2 1 
ATOM   203  N N   . ALA   A 1 27  ? -56.671 -13.922 18.438 1.00 88.68  ? 242 ALA   B N   1 
ATOM   204  C CA  . ALA   A 1 27  ? -56.072 -14.321 19.730 1.00 82.38  ? 242 ALA   B CA  1 
ATOM   205  C C   . ALA   A 1 27  ? -56.981 -13.937 20.925 1.00 81.50  ? 242 ALA   B C   1 
ATOM   206  O O   . ALA   A 1 27  ? -56.975 -14.579 21.980 1.00 72.33  ? 242 ALA   B O   1 
ATOM   207  C CB  . ALA   A 1 27  ? -54.694 -13.696 19.884 1.00 77.66  ? 242 ALA   B CB  1 
ATOM   208  N N   . VAL   A 1 28  ? -57.730 -12.857 20.740 1.00 77.80  ? 243 VAL   B N   1 
ATOM   209  C CA  . VAL   A 1 28  ? -58.816 -12.465 21.637 1.00 87.83  ? 243 VAL   B CA  1 
ATOM   210  C C   . VAL   A 1 28  ? -59.790 -13.595 22.017 1.00 92.35  ? 243 VAL   B C   1 
ATOM   211  O O   . VAL   A 1 28  ? -60.171 -13.704 23.178 1.00 95.43  ? 243 VAL   B O   1 
ATOM   212  C CB  . VAL   A 1 28  ? -59.650 -11.290 21.053 1.00 89.05  ? 243 VAL   B CB  1 
ATOM   213  C CG1 . VAL   A 1 28  ? -58.853 -9.993  21.071 1.00 86.14  ? 243 VAL   B CG1 1 
ATOM   214  C CG2 . VAL   A 1 28  ? -60.170 -11.598 19.644 1.00 91.57  ? 243 VAL   B CG2 1 
ATOM   215  N N   . ASP   A 1 29  ? -60.176 -14.420 21.043 1.00 96.15  ? 244 ASP   B N   1 
ATOM   216  C CA  . ASP   A 1 29  ? -61.197 -15.462 21.226 1.00 94.39  ? 244 ASP   B CA  1 
ATOM   217  C C   . ASP   A 1 29  ? -60.580 -16.818 21.542 1.00 97.27  ? 244 ASP   B C   1 
ATOM   218  O O   . ASP   A 1 29  ? -61.088 -17.545 22.399 1.00 110.01 ? 244 ASP   B O   1 
ATOM   219  C CB  . ASP   A 1 29  ? -62.105 -15.538 19.994 1.00 91.90  ? 244 ASP   B CB  1 
ATOM   220  C CG  . ASP   A 1 29  ? -62.965 -14.283 19.827 1.00 94.98  ? 244 ASP   B CG  1 
ATOM   221  O OD1 . ASP   A 1 29  ? -62.886 -13.370 20.674 1.00 99.69  ? 244 ASP   B OD1 1 
ATOM   222  O OD2 . ASP   A 1 29  ? -63.735 -14.201 18.853 1.00 96.68  ? 244 ASP   B OD2 1 
ATOM   223  N N   . SER   A 1 30  ? -59.496 -17.162 20.856 1.00 89.34  ? 245 SER   B N   1 
ATOM   224  C CA  . SER   A 1 30  ? -58.613 -18.227 21.332 1.00 93.48  ? 245 SER   B CA  1 
ATOM   225  C C   . SER   A 1 30  ? -57.164 -17.770 21.214 1.00 89.98  ? 245 SER   B C   1 
ATOM   226  O O   . SER   A 1 30  ? -56.708 -17.410 20.126 1.00 87.84  ? 245 SER   B O   1 
ATOM   227  C CB  . SER   A 1 30  ? -58.832 -19.518 20.554 1.00 100.71 ? 245 SER   B CB  1 
ATOM   228  O OG  . SER   A 1 30  ? -58.124 -20.586 21.163 1.00 97.26  ? 245 SER   B OG  1 
ATOM   229  N N   . TYR   A 1 31  ? -56.447 -17.796 22.335 1.00 81.16  ? 246 TYR   B N   1 
ATOM   230  C CA  . TYR   A 1 31  ? -55.140 -17.176 22.405 1.00 77.87  ? 246 TYR   B CA  1 
ATOM   231  C C   . TYR   A 1 31  ? -54.085 -17.974 21.643 1.00 77.82  ? 246 TYR   B C   1 
ATOM   232  O O   . TYR   A 1 31  ? -54.119 -19.193 21.620 1.00 80.51  ? 246 TYR   B O   1 
ATOM   233  C CB  . TYR   A 1 31  ? -54.676 -16.941 23.854 1.00 70.81  ? 246 TYR   B CB  1 
ATOM   234  C CG  . TYR   A 1 31  ? -53.388 -16.149 23.865 1.00 63.89  ? 246 TYR   B CG  1 
ATOM   235  C CD1 . TYR   A 1 31  ? -53.386 -14.817 23.473 1.00 59.97  ? 246 TYR   B CD1 1 
ATOM   236  C CD2 . TYR   A 1 31  ? -52.171 -16.747 24.166 1.00 58.62  ? 246 TYR   B CD2 1 
ATOM   237  C CE1 . TYR   A 1 31  ? -52.215 -14.085 23.422 1.00 57.03  ? 246 TYR   B CE1 1 
ATOM   238  C CE2 . TYR   A 1 31  ? -50.993 -16.019 24.129 1.00 56.69  ? 246 TYR   B CE2 1 
ATOM   239  C CZ  . TYR   A 1 31  ? -51.027 -14.684 23.750 1.00 55.47  ? 246 TYR   B CZ  1 
ATOM   240  O OH  . TYR   A 1 31  ? -49.886 -13.924 23.692 1.00 52.80  ? 246 TYR   B OH  1 
ATOM   241  N N   . GLN   A 1 32  ? -53.155 -17.244 21.032 1.00 77.69  ? 247 GLN   B N   1 
ATOM   242  C CA  . GLN   A 1 32  ? -52.031 -17.809 20.303 1.00 78.17  ? 247 GLN   B CA  1 
ATOM   243  C C   . GLN   A 1 32  ? -51.020 -16.681 20.039 1.00 72.62  ? 247 GLN   B C   1 
ATOM   244  O O   . GLN   A 1 32  ? -51.412 -15.578 19.671 1.00 62.29  ? 247 GLN   B O   1 
ATOM   245  C CB  . GLN   A 1 32  ? -52.560 -18.400 18.995 1.00 82.55  ? 247 GLN   B CB  1 
ATOM   246  C CG  . GLN   A 1 32  ? -51.561 -18.653 17.878 1.00 91.15  ? 247 GLN   B CG  1 
ATOM   247  C CD  . GLN   A 1 32  ? -52.265 -19.096 16.608 1.00 95.64  ? 247 GLN   B CD  1 
ATOM   248  O OE1 . GLN   A 1 32  ? -53.187 -18.427 16.133 1.00 94.56  ? 247 GLN   B OE1 1 
ATOM   249  N NE2 . GLN   A 1 32  ? -51.844 -20.227 16.056 1.00 95.81  ? 247 GLN   B NE2 1 
ATOM   250  N N   . ARG   A 1 33  ? -49.733 -16.932 20.263 1.00 68.24  ? 248 ARG   B N   1 
ATOM   251  C CA  . ARG   A 1 33  ? -48.704 -16.026 19.758 1.00 65.42  ? 248 ARG   B CA  1 
ATOM   252  C C   . ARG   A 1 33  ? -47.750 -16.794 18.847 1.00 58.58  ? 248 ARG   B C   1 
ATOM   253  O O   . ARG   A 1 33  ? -47.507 -17.969 19.052 1.00 52.44  ? 248 ARG   B O   1 
ATOM   254  C CB  . ARG   A 1 33  ? -47.951 -15.334 20.890 1.00 61.06  ? 248 ARG   B CB  1 
ATOM   255  C CG  . ARG   A 1 33  ? -47.140 -16.256 21.750 1.00 66.69  ? 248 ARG   B CG  1 
ATOM   256  C CD  . ARG   A 1 33  ? -46.021 -15.498 22.427 1.00 72.05  ? 248 ARG   B CD  1 
ATOM   257  N NE  . ARG   A 1 33  ? -46.534 -14.536 23.393 1.00 79.16  ? 248 ARG   B NE  1 
ATOM   258  C CZ  . ARG   A 1 33  ? -45.777 -13.869 24.269 1.00 88.51  ? 248 ARG   B CZ  1 
ATOM   259  N NH1 . ARG   A 1 33  ? -44.438 -14.047 24.316 1.00 82.28  ? 248 ARG   B NH1 1 
ATOM   260  N NH2 . ARG   A 1 33  ? -46.365 -13.007 25.108 1.00 82.03  ? 248 ARG   B NH2 1 
ATOM   261  N N   . HIS   A 1 34  ? -47.224 -16.111 17.840 1.00 55.72  ? 249 HIS   B N   1 
ATOM   262  C CA  . HIS   A 1 34  ? -46.199 -16.667 16.981 1.00 49.86  ? 249 HIS   B CA  1 
ATOM   263  C C   . HIS   A 1 34  ? -44.903 -15.974 17.379 1.00 48.66  ? 249 HIS   B C   1 
ATOM   264  O O   . HIS   A 1 34  ? -44.864 -14.749 17.442 1.00 51.15  ? 249 HIS   B O   1 
ATOM   265  C CB  . HIS   A 1 34  ? -46.526 -16.420 15.507 1.00 49.60  ? 249 HIS   B CB  1 
ATOM   266  C CG  . HIS   A 1 34  ? -45.375 -16.700 14.597 1.00 53.10  ? 249 HIS   B CG  1 
ATOM   267  N ND1 . HIS   A 1 34  ? -45.026 -17.977 14.217 1.00 52.12  ? 249 HIS   B ND1 1 
ATOM   268  C CD2 . HIS   A 1 34  ? -44.445 -15.877 14.053 1.00 49.99  ? 249 HIS   B CD2 1 
ATOM   269  C CE1 . HIS   A 1 34  ? -43.941 -17.929 13.459 1.00 49.42  ? 249 HIS   B CE1 1 
ATOM   270  N NE2 . HIS   A 1 34  ? -43.570 -16.668 13.342 1.00 50.36  ? 249 HIS   B NE2 1 
ATOM   271  N N   . LEU   A 1 35  ? -43.862 -16.766 17.629 1.00 43.51  ? 250 LEU   B N   1 
ATOM   272  C CA  . LEU   A 1 35  ? -42.533 -16.279 17.954 1.00 43.43  ? 250 LEU   B CA  1 
ATOM   273  C C   . LEU   A 1 35  ? -41.631 -16.271 16.715 1.00 47.40  ? 250 LEU   B C   1 
ATOM   274  O O   . LEU   A 1 35  ? -41.345 -17.326 16.157 1.00 48.63  ? 250 LEU   B O   1 
ATOM   275  C CB  . LEU   A 1 35  ? -41.917 -17.168 19.032 1.00 43.44  ? 250 LEU   B CB  1 
ATOM   276  C CG  . LEU   A 1 35  ? -42.732 -17.245 20.327 1.00 45.76  ? 250 LEU   B CG  1 
ATOM   277  C CD1 . LEU   A 1 35  ? -42.097 -18.239 21.277 1.00 48.66  ? 250 LEU   B CD1 1 
ATOM   278  C CD2 . LEU   A 1 35  ? -42.843 -15.880 20.976 1.00 44.82  ? 250 LEU   B CD2 1 
ATOM   279  N N   . PHE   A 1 36  ? -41.199 -15.077 16.291 1.00 44.41  ? 251 PHE   B N   1 
ATOM   280  C CA  . PHE   A 1 36  ? -40.192 -14.941 15.251 1.00 44.01  ? 251 PHE   B CA  1 
ATOM   281  C C   . PHE   A 1 36  ? -38.795 -15.348 15.817 1.00 47.80  ? 251 PHE   B C   1 
ATOM   282  O O   . PHE   A 1 36  ? -38.065 -16.107 15.181 1.00 47.21  ? 251 PHE   B O   1 
ATOM   283  C CB  . PHE   A 1 36  ? -40.148 -13.507 14.679 1.00 42.23  ? 251 PHE   B CB  1 
ATOM   284  C CG  . PHE   A 1 36  ? -41.472 -12.989 14.220 1.00 38.58  ? 251 PHE   B CG  1 
ATOM   285  C CD1 . PHE   A 1 36  ? -42.075 -13.496 13.094 1.00 45.10  ? 251 PHE   B CD1 1 
ATOM   286  C CD2 . PHE   A 1 36  ? -42.111 -11.993 14.911 1.00 39.32  ? 251 PHE   B CD2 1 
ATOM   287  C CE1 . PHE   A 1 36  ? -43.308 -13.020 12.646 1.00 43.79  ? 251 PHE   B CE1 1 
ATOM   288  C CE2 . PHE   A 1 36  ? -43.345 -11.524 14.499 1.00 44.48  ? 251 PHE   B CE2 1 
ATOM   289  C CZ  . PHE   A 1 36  ? -43.948 -12.038 13.360 1.00 47.95  ? 251 PHE   B CZ  1 
ATOM   290  N N   . VAL   A 1 37  ? -38.441 -14.839 16.999 1.00 46.04  ? 252 VAL   B N   1 
ATOM   291  C CA  . VAL   A 1 37  ? -37.194 -15.195 17.676 1.00 48.16  ? 252 VAL   B CA  1 
ATOM   292  C C   . VAL   A 1 37  ? -37.463 -15.192 19.141 1.00 50.30  ? 252 VAL   B C   1 
ATOM   293  O O   . VAL   A 1 37  ? -38.418 -14.560 19.578 1.00 51.19  ? 252 VAL   B O   1 
ATOM   294  C CB  . VAL   A 1 37  ? -36.051 -14.220 17.377 1.00 52.97  ? 252 VAL   B CB  1 
ATOM   295  C CG1 . VAL   A 1 37  ? -35.489 -14.492 15.992 1.00 57.50  ? 252 VAL   B CG1 1 
ATOM   296  C CG2 . VAL   A 1 37  ? -36.518 -12.765 17.456 1.00 54.27  ? 252 VAL   B CG2 1 
ATOM   297  N N   . HIS   A 1 38  ? -36.621 -15.890 19.893 1.00 53.70  ? 253 HIS   B N   1 
ATOM   298  C CA  . HIS   A 1 38  ? -36.888 -16.158 21.304 1.00 55.62  ? 253 HIS   B CA  1 
ATOM   299  C C   . HIS   A 1 38  ? -35.587 -16.552 21.974 1.00 52.96  ? 253 HIS   B C   1 
ATOM   300  O O   . HIS   A 1 38  ? -34.868 -17.361 21.444 1.00 55.22  ? 253 HIS   B O   1 
ATOM   301  C CB  . HIS   A 1 38  ? -37.904 -17.299 21.392 1.00 63.65  ? 253 HIS   B CB  1 
ATOM   302  C CG  . HIS   A 1 38  ? -38.334 -17.662 22.785 1.00 74.78  ? 253 HIS   B CG  1 
ATOM   303  N ND1 . HIS   A 1 38  ? -39.256 -16.925 23.499 1.00 85.07  ? 253 HIS   B ND1 1 
ATOM   304  C CD2 . HIS   A 1 38  ? -38.021 -18.722 23.567 1.00 78.25  ? 253 HIS   B CD2 1 
ATOM   305  C CE1 . HIS   A 1 38  ? -39.466 -17.496 24.670 1.00 77.63  ? 253 HIS   B CE1 1 
ATOM   306  N NE2 . HIS   A 1 38  ? -38.727 -18.586 24.738 1.00 78.10  ? 253 HIS   B NE2 1 
ATOM   307  N N   . ILE   A 1 39  ? -35.270 -15.951 23.116 1.00 51.52  ? 254 ILE   B N   1 
ATOM   308  C CA  . ILE   A 1 39  ? -34.185 -16.434 23.985 1.00 54.34  ? 254 ILE   B CA  1 
ATOM   309  C C   . ILE   A 1 39  ? -34.743 -16.581 25.387 1.00 54.98  ? 254 ILE   B C   1 
ATOM   310  O O   . ILE   A 1 39  ? -35.384 -15.660 25.900 1.00 53.70  ? 254 ILE   B O   1 
ATOM   311  C CB  . ILE   A 1 39  ? -32.985 -15.470 24.062 1.00 54.48  ? 254 ILE   B CB  1 
ATOM   312  C CG1 . ILE   A 1 39  ? -32.435 -15.176 22.675 1.00 57.23  ? 254 ILE   B CG1 1 
ATOM   313  C CG2 . ILE   A 1 39  ? -31.888 -16.049 24.957 1.00 54.58  ? 254 ILE   B CG2 1 
ATOM   314  C CD1 . ILE   A 1 39  ? -31.383 -14.084 22.664 1.00 55.66  ? 254 ILE   B CD1 1 
ATOM   315  N N   . SER   A 1 40  ? -34.487 -17.725 26.007 1.00 57.66  ? 255 SER   B N   1 
ATOM   316  C CA  . SER   A 1 40  ? -34.878 -17.947 27.401 1.00 62.36  ? 255 SER   B CA  1 
ATOM   317  C C   . SER   A 1 40  ? -33.679 -18.429 28.214 1.00 62.40  ? 255 SER   B C   1 
ATOM   318  O O   . SER   A 1 40  ? -33.029 -19.409 27.848 1.00 64.94  ? 255 SER   B O   1 
ATOM   319  C CB  . SER   A 1 40  ? -36.013 -18.959 27.478 1.00 63.90  ? 255 SER   B CB  1 
ATOM   320  O OG  . SER   A 1 40  ? -36.663 -18.866 28.726 1.00 69.25  ? 255 SER   B OG  1 
ATOM   321  N N   . GLN   A 1 41  ? -33.389 -17.740 29.311 1.00 64.76  ? 256 GLN   B N   1 
ATOM   322  C CA  . GLN   A 1 41  ? -32.296 -18.132 30.198 1.00 74.90  ? 256 GLN   B CA  1 
ATOM   323  C C   . GLN   A 1 41  ? -32.788 -18.236 31.657 1.00 75.97  ? 256 GLN   B C   1 
ATOM   324  O O   . GLN   A 1 41  ? -32.774 -17.258 32.378 1.00 75.22  ? 256 GLN   B O   1 
ATOM   325  C CB  . GLN   A 1 41  ? -31.135 -17.139 30.044 1.00 73.02  ? 256 GLN   B CB  1 
ATOM   326  C CG  . GLN   A 1 41  ? -30.529 -17.118 28.641 1.00 66.36  ? 256 GLN   B CG  1 
ATOM   327  C CD  . GLN   A 1 41  ? -29.324 -16.208 28.531 1.00 63.93  ? 256 GLN   B CD  1 
ATOM   328  O OE1 . GLN   A 1 41  ? -28.358 -16.517 27.829 1.00 55.82  ? 256 GLN   B OE1 1 
ATOM   329  N NE2 . GLN   A 1 41  ? -29.369 -15.075 29.227 1.00 67.88  ? 256 GLN   B NE2 1 
ATOM   330  N N   . HIS   A 1 42  ? -33.206 -19.435 32.071 1.00 88.59  ? 257 HIS   B N   1 
ATOM   331  C CA  . HIS   A 1 42  ? -33.727 -19.681 33.427 1.00 90.24  ? 257 HIS   B CA  1 
ATOM   332  C C   . HIS   A 1 42  ? -32.872 -20.679 34.254 1.00 86.23  ? 257 HIS   B C   1 
ATOM   333  O O   . HIS   A 1 42  ? -33.139 -21.884 34.329 1.00 85.26  ? 257 HIS   B O   1 
ATOM   334  C CB  . HIS   A 1 42  ? -35.189 -20.108 33.311 1.00 91.03  ? 257 HIS   B CB  1 
ATOM   335  C CG  . HIS   A 1 42  ? -36.089 -19.013 32.818 1.00 94.55  ? 257 HIS   B CG  1 
ATOM   336  N ND1 . HIS   A 1 42  ? -36.670 -19.022 31.567 1.00 95.08  ? 257 HIS   B ND1 1 
ATOM   337  C CD2 . HIS   A 1 42  ? -36.495 -17.863 33.410 1.00 94.14  ? 257 HIS   B CD2 1 
ATOM   338  C CE1 . HIS   A 1 42  ? -37.407 -17.934 31.418 1.00 92.78  ? 257 HIS   B CE1 1 
ATOM   339  N NE2 . HIS   A 1 42  ? -37.318 -17.215 32.521 1.00 92.83  ? 257 HIS   B NE2 1 
ATOM   340  N N   . PRO   A 1 49  ? -20.488 -24.535 30.872 1.00 101.89 ? 264 PRO   B N   1 
ATOM   341  C CA  . PRO   A 1 49  ? -19.653 -24.528 29.649 1.00 96.02  ? 264 PRO   B CA  1 
ATOM   342  C C   . PRO   A 1 49  ? -19.525 -23.118 29.044 1.00 94.40  ? 264 PRO   B C   1 
ATOM   343  O O   . PRO   A 1 49  ? -20.556 -22.489 28.821 1.00 85.43  ? 264 PRO   B O   1 
ATOM   344  C CB  . PRO   A 1 49  ? -20.418 -25.460 28.690 1.00 95.98  ? 264 PRO   B CB  1 
ATOM   345  C CG  . PRO   A 1 49  ? -21.834 -25.483 29.194 1.00 99.93  ? 264 PRO   B CG  1 
ATOM   346  C CD  . PRO   A 1 49  ? -21.809 -25.170 30.672 1.00 98.80  ? 264 PRO   B CD  1 
ATOM   347  N N   . PRO   A 1 50  ? -18.288 -22.619 28.767 1.00 96.50  ? 265 PRO   B N   1 
ATOM   348  C CA  . PRO   A 1 50  ? -18.205 -21.255 28.194 1.00 92.01  ? 265 PRO   B CA  1 
ATOM   349  C C   . PRO   A 1 50  ? -18.780 -21.175 26.769 1.00 84.03  ? 265 PRO   B C   1 
ATOM   350  O O   . PRO   A 1 50  ? -18.923 -22.201 26.100 1.00 79.12  ? 265 PRO   B O   1 
ATOM   351  C CB  . PRO   A 1 50  ? -16.691 -20.941 28.193 1.00 90.37  ? 265 PRO   B CB  1 
ATOM   352  C CG  . PRO   A 1 50  ? -16.041 -22.043 28.956 1.00 91.09  ? 265 PRO   B CG  1 
ATOM   353  C CD  . PRO   A 1 50  ? -16.952 -23.234 28.843 1.00 92.99  ? 265 PRO   B CD  1 
ATOM   354  N N   . LEU   A 1 51  ? -19.131 -19.968 26.335 1.00 74.91  ? 266 LEU   B N   1 
ATOM   355  C CA  . LEU   A 1 51  ? -19.677 -19.749 25.001 1.00 65.77  ? 266 LEU   B CA  1 
ATOM   356  C C   . LEU   A 1 51  ? -18.536 -19.587 24.015 1.00 65.40  ? 266 LEU   B C   1 
ATOM   357  O O   . LEU   A 1 51  ? -17.405 -19.284 24.397 1.00 66.35  ? 266 LEU   B O   1 
ATOM   358  C CB  . LEU   A 1 51  ? -20.579 -18.512 24.975 1.00 66.27  ? 266 LEU   B CB  1 
ATOM   359  C CG  . LEU   A 1 51  ? -21.807 -18.486 25.891 1.00 63.80  ? 266 LEU   B CG  1 
ATOM   360  C CD1 . LEU   A 1 51  ? -22.276 -17.060 26.059 1.00 63.03  ? 266 LEU   B CD1 1 
ATOM   361  C CD2 . LEU   A 1 51  ? -22.947 -19.350 25.360 1.00 62.84  ? 266 LEU   B CD2 1 
ATOM   362  N N   . GLU   A 1 52  ? -18.857 -19.772 22.741 1.00 66.48  ? 267 GLU   B N   1 
ATOM   363  C CA  . GLU   A 1 52  ? -17.874 -19.738 21.674 1.00 68.17  ? 267 GLU   B CA  1 
ATOM   364  C C   . GLU   A 1 52  ? -17.688 -18.281 21.436 1.00 67.09  ? 267 GLU   B C   1 
ATOM   365  O O   . GLU   A 1 52  ? -18.580 -17.508 21.771 1.00 70.14  ? 267 GLU   B O   1 
ATOM   366  C CB  . GLU   A 1 52  ? -18.392 -20.408 20.386 1.00 79.49  ? 267 GLU   B CB  1 
ATOM   367  C CG  . GLU   A 1 52  ? -19.165 -21.722 20.568 1.00 92.03  ? 267 GLU   B CG  1 
ATOM   368  C CD  . GLU   A 1 52  ? -19.447 -22.481 19.261 1.00 101.18 ? 267 GLU   B CD  1 
ATOM   369  O OE1 . GLU   A 1 52  ? -19.926 -23.632 19.349 1.00 103.51 ? 267 GLU   B OE1 1 
ATOM   370  O OE2 . GLU   A 1 52  ? -19.200 -21.957 18.147 1.00 109.00 ? 267 GLU   B OE2 1 
ATOM   371  N N   . SER   A 1 53  ? -16.562 -17.889 20.852 1.00 65.91  ? 268 SER   B N   1 
ATOM   372  C CA  . SER   A 1 53  ? -16.307 -16.476 20.576 1.00 65.95  ? 268 SER   B CA  1 
ATOM   373  C C   . SER   A 1 53  ? -16.200 -16.190 19.089 1.00 66.99  ? 268 SER   B C   1 
ATOM   374  O O   . SER   A 1 53  ? -16.011 -17.098 18.281 1.00 73.16  ? 268 SER   B O   1 
ATOM   375  C CB  . SER   A 1 53  ? -15.075 -15.970 21.321 1.00 62.89  ? 268 SER   B CB  1 
ATOM   376  O OG  . SER   A 1 53  ? -13.972 -16.786 21.038 1.00 70.59  ? 268 SER   B OG  1 
ATOM   377  N N   . VAL   A 1 54  ? -16.378 -14.912 18.752 1.00 69.20  ? 269 VAL   B N   1 
ATOM   378  C CA  . VAL   A 1 54  ? -16.316 -14.403 17.386 1.00 66.01  ? 269 VAL   B CA  1 
ATOM   379  C C   . VAL   A 1 54  ? -15.613 -13.057 17.455 1.00 69.95  ? 269 VAL   B C   1 
ATOM   380  O O   . VAL   A 1 54  ? -15.889 -12.265 18.358 1.00 72.60  ? 269 VAL   B O   1 
ATOM   381  C CB  . VAL   A 1 54  ? -17.722 -14.234 16.777 1.00 64.98  ? 269 VAL   B CB  1 
ATOM   382  C CG1 . VAL   A 1 54  ? -17.669 -13.454 15.456 1.00 64.47  ? 269 VAL   B CG1 1 
ATOM   383  C CG2 . VAL   A 1 54  ? -18.382 -15.602 16.601 1.00 62.59  ? 269 VAL   B CG2 1 
ATOM   384  N N   . ASP   A 1 55  ? -14.713 -12.815 16.504 1.00 72.32  ? 270 ASP   B N   1 
ATOM   385  C CA  . ASP   A 1 55  ? -13.923 -11.605 16.477 1.00 79.12  ? 270 ASP   B CA  1 
ATOM   386  C C   . ASP   A 1 55  ? -14.777 -10.465 15.951 1.00 78.68  ? 270 ASP   B C   1 
ATOM   387  O O   . ASP   A 1 55  ? -15.264 -10.503 14.825 1.00 73.25  ? 270 ASP   B O   1 
ATOM   388  C CB  . ASP   A 1 55  ? -12.679 -11.757 15.606 1.00 85.33  ? 270 ASP   B CB  1 
ATOM   389  C CG  . ASP   A 1 55  ? -11.867 -10.475 15.533 1.00 92.86  ? 270 ASP   B CG  1 
ATOM   390  O OD1 . ASP   A 1 55  ? -11.128 -10.161 16.500 1.00 91.87  ? 270 ASP   B OD1 1 
ATOM   391  O OD2 . ASP   A 1 55  ? -12.004 -9.766  14.515 1.00 101.89 ? 270 ASP   B OD2 1 
ATOM   392  N N   . VAL   A 1 56  ? -14.914 -9.444  16.787 1.00 77.89  ? 271 VAL   B N   1 
ATOM   393  C CA  . VAL   A 1 56  ? -15.749 -8.283  16.502 1.00 73.11  ? 271 VAL   B CA  1 
ATOM   394  C C   . VAL   A 1 56  ? -15.301 -7.513  15.263 1.00 73.50  ? 271 VAL   B C   1 
ATOM   395  O O   . VAL   A 1 56  ? -16.133 -6.863  14.612 1.00 64.87  ? 271 VAL   B O   1 
ATOM   396  C CB  . VAL   A 1 56  ? -15.802 -7.344  17.743 1.00 69.80  ? 271 VAL   B CB  1 
ATOM   397  C CG1 . VAL   A 1 56  ? -14.463 -6.649  17.976 1.00 75.84  ? 271 VAL   B CG1 1 
ATOM   398  C CG2 . VAL   A 1 56  ? -16.914 -6.318  17.624 1.00 64.02  ? 271 VAL   B CG2 1 
ATOM   399  N N   . ARG   A 1 57  ? -14.002 -7.575  14.939 1.00 77.56  ? 272 ARG   B N   1 
ATOM   400  C CA  . ARG   A 1 57  ? -13.498 -6.863  13.753 1.00 84.83  ? 272 ARG   B CA  1 
ATOM   401  C C   . ARG   A 1 57  ? -14.181 -7.392  12.509 1.00 79.40  ? 272 ARG   B C   1 
ATOM   402  O O   . ARG   A 1 57  ? -14.477 -6.622  11.617 1.00 79.17  ? 272 ARG   B O   1 
ATOM   403  C CB  . ARG   A 1 57  ? -11.969 -6.906  13.589 1.00 84.65  ? 272 ARG   B CB  1 
ATOM   404  C CG  . ARG   A 1 57  ? -11.187 -6.401  14.789 1.00 87.71  ? 272 ARG   B CG  1 
ATOM   405  C CD  . ARG   A 1 57  ? -9.687  -6.411  14.544 1.00 93.10  ? 272 ARG   B CD  1 
ATOM   406  N NE  . ARG   A 1 57  ? -8.950  -7.011  15.666 1.00 98.80  ? 272 ARG   B NE  1 
ATOM   407  C CZ  . ARG   A 1 57  ? -8.693  -8.317  15.830 1.00 99.01  ? 272 ARG   B CZ  1 
ATOM   408  N NH1 . ARG   A 1 57  ? -9.099  -9.219  14.941 1.00 101.58 ? 272 ARG   B NH1 1 
ATOM   409  N NH2 . ARG   A 1 57  ? -8.014  -8.734  16.905 1.00 103.95 ? 272 ARG   B NH2 1 
ATOM   410  N N   . GLN   A 1 58  ? -14.507 -8.685  12.504 1.00 82.08  ? 273 GLN   B N   1 
ATOM   411  C CA  . GLN   A 1 58  ? -15.194 -9.329  11.370 1.00 86.35  ? 273 GLN   B CA  1 
ATOM   412  C C   . GLN   A 1 58  ? -16.605 -8.776  11.037 1.00 85.32  ? 273 GLN   B C   1 
ATOM   413  O O   . GLN   A 1 58  ? -17.081 -8.959  9.923  1.00 92.04  ? 273 GLN   B O   1 
ATOM   414  C CB  . GLN   A 1 58  ? -15.293 -10.852 11.578 1.00 83.66  ? 273 GLN   B CB  1 
ATOM   415  C CG  . GLN   A 1 58  ? -13.968 -11.569 11.838 1.00 91.99  ? 273 GLN   B CG  1 
ATOM   416  C CD  . GLN   A 1 58  ? -13.199 -11.925 10.575 1.00 97.50  ? 273 GLN   B CD  1 
ATOM   417  O OE1 . GLN   A 1 58  ? -13.019 -11.104 9.670  1.00 90.92  ? 273 GLN   B OE1 1 
ATOM   418  N NE2 . GLN   A 1 58  ? -12.725 -13.162 10.521 1.00 102.50 ? 273 GLN   B NE2 1 
ATOM   419  N N   . ILE   A 1 59  ? -17.273 -8.103  11.971 1.00 85.67  ? 274 ILE   B N   1 
ATOM   420  C CA  . ILE   A 1 59  ? -18.654 -7.649  11.734 1.00 78.33  ? 274 ILE   B CA  1 
ATOM   421  C C   . ILE   A 1 59  ? -18.871 -6.130  11.822 1.00 73.36  ? 274 ILE   B C   1 
ATOM   422  O O   . ILE   A 1 59  ? -19.998 -5.682  11.745 1.00 71.55  ? 274 ILE   B O   1 
ATOM   423  C CB  . ILE   A 1 59  ? -19.634 -8.390  12.671 1.00 80.30  ? 274 ILE   B CB  1 
ATOM   424  C CG1 . ILE   A 1 59  ? -19.432 -7.982  14.136 1.00 79.83  ? 274 ILE   B CG1 1 
ATOM   425  C CG2 . ILE   A 1 59  ? -19.459 -9.897  12.542 1.00 75.05  ? 274 ILE   B CG2 1 
ATOM   426  C CD1 . ILE   A 1 59  ? -20.480 -8.541  15.073 1.00 78.70  ? 274 ILE   B CD1 1 
ATOM   427  N N   . TYR   A 1 60  ? -17.808 -5.340  11.948 1.00 74.82  ? 275 TYR   B N   1 
ATOM   428  C CA  . TYR   A 1 60  ? -17.924 -3.867  11.964 1.00 77.12  ? 275 TYR   B CA  1 
ATOM   429  C C   . TYR   A 1 60  ? -18.760 -3.292  10.832 1.00 74.29  ? 275 TYR   B C   1 
ATOM   430  O O   . TYR   A 1 60  ? -19.592 -2.389  11.042 1.00 70.41  ? 275 TYR   B O   1 
ATOM   431  C CB  . TYR   A 1 60  ? -16.544 -3.219  11.856 1.00 78.01  ? 275 TYR   B CB  1 
ATOM   432  C CG  . TYR   A 1 60  ? -15.653 -3.313  13.065 1.00 80.73  ? 275 TYR   B CG  1 
ATOM   433  C CD1 . TYR   A 1 60  ? -16.171 -3.340  14.362 1.00 81.10  ? 275 TYR   B CD1 1 
ATOM   434  C CD2 . TYR   A 1 60  ? -14.270 -3.313  12.913 1.00 83.67  ? 275 TYR   B CD2 1 
ATOM   435  C CE1 . TYR   A 1 60  ? -15.334 -3.391  15.458 1.00 83.92  ? 275 TYR   B CE1 1 
ATOM   436  C CE2 . TYR   A 1 60  ? -13.427 -3.365  14.008 1.00 82.09  ? 275 TYR   B CE2 1 
ATOM   437  C CZ  . TYR   A 1 60  ? -13.967 -3.400  15.271 1.00 82.34  ? 275 TYR   B CZ  1 
ATOM   438  O OH  . TYR   A 1 60  ? -13.140 -3.440  16.347 1.00 84.17  ? 275 TYR   B OH  1 
ATOM   439  N N   . ASP   A 1 61  ? -18.516 -3.822  9.636  1.00 73.15  ? 276 ASP   B N   1 
ATOM   440  C CA  . ASP   A 1 61  ? -19.147 -3.325  8.410  1.00 79.23  ? 276 ASP   B CA  1 
ATOM   441  C C   . ASP   A 1 61  ? -20.652 -3.596  8.321  1.00 77.52  ? 276 ASP   B C   1 
ATOM   442  O O   . ASP   A 1 61  ? -21.325 -3.033  7.464  1.00 75.28  ? 276 ASP   B O   1 
ATOM   443  C CB  . ASP   A 1 61  ? -18.430 -3.893  7.170  1.00 83.48  ? 276 ASP   B CB  1 
ATOM   444  C CG  . ASP   A 1 61  ? -18.502 -5.426  7.074  1.00 92.24  ? 276 ASP   B CG  1 
ATOM   445  O OD1 . ASP   A 1 61  ? -19.052 -6.092  7.983  1.00 90.78  ? 276 ASP   B OD1 1 
ATOM   446  O OD2 . ASP   A 1 61  ? -17.983 -5.971  6.074  1.00 104.25 ? 276 ASP   B OD2 1 
ATOM   447  N N   . LYS   A 1 62  ? -21.160 -4.488  9.179  1.00 81.44  ? 277 LYS   B N   1 
ATOM   448  C CA  . LYS   A 1 62  ? -22.588 -4.777  9.271  1.00 72.70  ? 277 LYS   B CA  1 
ATOM   449  C C   . LYS   A 1 62  ? -23.310 -3.853  10.223 1.00 66.09  ? 277 LYS   B C   1 
ATOM   450  O O   . LYS   A 1 62  ? -24.536 -3.929  10.295 1.00 68.02  ? 277 LYS   B O   1 
ATOM   451  C CB  . LYS   A 1 62  ? -22.831 -6.217  9.723  1.00 77.12  ? 277 LYS   B CB  1 
ATOM   452  C CG  . LYS   A 1 62  ? -22.053 -7.265  8.951  1.00 76.86  ? 277 LYS   B CG  1 
ATOM   453  C CD  . LYS   A 1 62  ? -22.733 -8.623  8.996  1.00 80.93  ? 277 LYS   B CD  1 
ATOM   454  C CE  . LYS   A 1 62  ? -23.829 -8.733  7.940  1.00 88.36  ? 277 LYS   B CE  1 
ATOM   455  N NZ  . LYS   A 1 62  ? -24.614 -10.003 8.058  1.00 91.39  ? 277 LYS   B NZ  1 
ATOM   456  N N   . PHE   A 1 63  ? -22.582 -2.989  10.942 1.00 71.20  ? 278 PHE   B N   1 
ATOM   457  C CA  . PHE   A 1 63  ? -23.193 -2.008  11.879 1.00 79.40  ? 278 PHE   B CA  1 
ATOM   458  C C   . PHE   A 1 63  ? -22.810 -0.539  11.633 1.00 84.20  ? 278 PHE   B C   1 
ATOM   459  O O   . PHE   A 1 63  ? -21.795 -0.264  10.976 1.00 84.68  ? 278 PHE   B O   1 
ATOM   460  C CB  . PHE   A 1 63  ? -22.877 -2.446  13.308 1.00 75.34  ? 278 PHE   B CB  1 
ATOM   461  C CG  . PHE   A 1 63  ? -23.461 -3.779  13.621 1.00 70.22  ? 278 PHE   B CG  1 
ATOM   462  C CD1 . PHE   A 1 63  ? -24.806 -3.889  13.969 1.00 62.24  ? 278 PHE   B CD1 1 
ATOM   463  C CD2 . PHE   A 1 63  ? -22.716 -4.938  13.447 1.00 66.24  ? 278 PHE   B CD2 1 
ATOM   464  C CE1 . PHE   A 1 63  ? -25.376 -5.124  14.192 1.00 54.28  ? 278 PHE   B CE1 1 
ATOM   465  C CE2 . PHE   A 1 63  ? -23.286 -6.185  13.680 1.00 63.13  ? 278 PHE   B CE2 1 
ATOM   466  C CZ  . PHE   A 1 63  ? -24.619 -6.273  14.056 1.00 56.98  ? 278 PHE   B CZ  1 
ATOM   467  N N   . PRO   A 1 64  ? -23.635 0.414   12.144 1.00 95.81  ? 279 PRO   B N   1 
ATOM   468  C CA  . PRO   A 1 64  ? -23.312 1.830   11.922 1.00 100.71 ? 279 PRO   B CA  1 
ATOM   469  C C   . PRO   A 1 64  ? -21.961 2.177   12.523 1.00 102.13 ? 279 PRO   B C   1 
ATOM   470  O O   . PRO   A 1 64  ? -21.529 1.512   13.472 1.00 105.65 ? 279 PRO   B O   1 
ATOM   471  C CB  . PRO   A 1 64  ? -24.457 2.581   12.626 1.00 96.47  ? 279 PRO   B CB  1 
ATOM   472  C CG  . PRO   A 1 64  ? -25.010 1.608   13.599 1.00 95.51  ? 279 PRO   B CG  1 
ATOM   473  C CD  . PRO   A 1 64  ? -24.878 0.277   12.924 1.00 95.73  ? 279 PRO   B CD  1 
ATOM   474  N N   . GLU   A 1 65  ? -21.292 3.166   11.926 1.00 100.40 ? 280 GLU   B N   1 
ATOM   475  C CA  . GLU   A 1 65  ? -19.964 3.630   12.368 1.00 102.75 ? 280 GLU   B CA  1 
ATOM   476  C C   . GLU   A 1 65  ? -20.079 5.116   12.787 1.00 94.34  ? 280 GLU   B C   1 
ATOM   477  O O   . GLU   A 1 65  ? -21.186 5.585   13.053 1.00 87.05  ? 280 GLU   B O   1 
ATOM   478  C CB  . GLU   A 1 65  ? -18.889 3.330   11.292 1.00 97.12  ? 280 GLU   B CB  1 
ATOM   479  C CG  . GLU   A 1 65  ? -18.995 1.900   10.714 1.00 99.76  ? 280 GLU   B CG  1 
ATOM   480  C CD  . GLU   A 1 65  ? -17.672 1.151   10.530 1.00 102.31 ? 280 GLU   B CD  1 
ATOM   481  O OE1 . GLU   A 1 65  ? -16.626 1.617   11.034 1.00 98.39  ? 280 GLU   B OE1 1 
ATOM   482  O OE2 . GLU   A 1 65  ? -17.687 0.062   9.889  1.00 93.07  ? 280 GLU   B OE2 1 
ATOM   483  N N   . LYS   A 1 66  ? -18.961 5.839   12.875 1.00 98.96  ? 281 LYS   B N   1 
ATOM   484  C CA  . LYS   A 1 66  ? -18.931 7.191   13.471 1.00 99.52  ? 281 LYS   B CA  1 
ATOM   485  C C   . LYS   A 1 66  ? -19.279 7.044   14.975 1.00 104.27 ? 281 LYS   B C   1 
ATOM   486  O O   . LYS   A 1 66  ? -18.650 6.224   15.644 1.00 111.18 ? 281 LYS   B O   1 
ATOM   487  C CB  . LYS   A 1 66  ? -19.822 8.181   12.698 1.00 84.17  ? 281 LYS   B CB  1 
ATOM   488  N N   . LYS   A 1 67  ? -20.273 7.770   15.503 1.00 104.73 ? 282 LYS   B N   1 
ATOM   489  C CA  . LYS   A 1 67  ? -20.692 7.616   16.916 1.00 96.73  ? 282 LYS   B CA  1 
ATOM   490  C C   . LYS   A 1 67  ? -21.457 6.269   17.055 1.00 93.36  ? 282 LYS   B C   1 
ATOM   491  O O   . LYS   A 1 67  ? -21.302 5.392   16.198 1.00 99.14  ? 282 LYS   B O   1 
ATOM   492  C CB  . LYS   A 1 67  ? -21.466 8.873   17.420 1.00 99.37  ? 282 LYS   B CB  1 
ATOM   493  C CG  . LYS   A 1 67  ? -21.220 9.292   18.877 1.00 89.38  ? 282 LYS   B CG  1 
ATOM   494  N N   . GLY   A 1 68  ? -22.275 6.115   18.100 1.00 91.96  ? 283 GLY   B N   1 
ATOM   495  C CA  . GLY   A 1 68  ? -22.722 4.808   18.672 1.00 88.19  ? 283 GLY   B CA  1 
ATOM   496  C C   . GLY   A 1 68  ? -22.758 3.530   17.844 1.00 87.36  ? 283 GLY   B C   1 
ATOM   497  O O   . GLY   A 1 68  ? -23.753 2.785   17.853 1.00 88.58  ? 283 GLY   B O   1 
ATOM   498  N N   . GLY   A 1 69  ? -21.648 3.265   17.163 1.00 78.70  ? 284 GLY   B N   1 
ATOM   499  C CA  . GLY   A 1 69  ? -21.490 2.128   16.286 1.00 74.53  ? 284 GLY   B CA  1 
ATOM   500  C C   . GLY   A 1 69  ? -20.592 1.129   16.990 1.00 71.57  ? 284 GLY   B C   1 
ATOM   501  O O   . GLY   A 1 69  ? -20.020 1.422   18.056 1.00 68.76  ? 284 GLY   B O   1 
ATOM   502  N N   . LEU   A 1 70  ? -20.440 -0.048  16.394 1.00 67.36  ? 285 LEU   B N   1 
ATOM   503  C CA  . LEU   A 1 70  ? -19.750 -1.143  17.086 1.00 66.50  ? 285 LEU   B CA  1 
ATOM   504  C C   . LEU   A 1 70  ? -18.317 -0.848  17.509 1.00 66.67  ? 285 LEU   B C   1 
ATOM   505  O O   . LEU   A 1 70  ? -17.902 -1.217  18.618 1.00 65.39  ? 285 LEU   B O   1 
ATOM   506  C CB  . LEU   A 1 70  ? -19.755 -2.443  16.271 1.00 61.05  ? 285 LEU   B CB  1 
ATOM   507  C CG  . LEU   A 1 70  ? -20.547 -3.633  16.792 1.00 59.30  ? 285 LEU   B CG  1 
ATOM   508  C CD1 . LEU   A 1 70  ? -20.022 -4.872  16.091 1.00 59.84  ? 285 LEU   B CD1 1 
ATOM   509  C CD2 . LEU   A 1 70  ? -20.470 -3.816  18.310 1.00 59.21  ? 285 LEU   B CD2 1 
ATOM   510  N N   . ARG   A 1 71  ? -17.571 -0.201  16.624 1.00 67.85  ? 286 ARG   B N   1 
ATOM   511  C CA  . ARG   A 1 71  ? -16.147 -0.019  16.839 1.00 77.37  ? 286 ARG   B CA  1 
ATOM   512  C C   . ARG   A 1 71  ? -15.917 0.882   18.062 1.00 70.27  ? 286 ARG   B C   1 
ATOM   513  O O   . ARG   A 1 71  ? -15.102 0.553   18.936 1.00 64.97  ? 286 ARG   B O   1 
ATOM   514  C CB  . ARG   A 1 71  ? -15.473 0.538   15.571 1.00 88.00  ? 286 ARG   B CB  1 
ATOM   515  C CG  . ARG   A 1 71  ? -13.961 0.327   15.534 1.00 95.30  ? 286 ARG   B CG  1 
ATOM   516  C CD  . ARG   A 1 71  ? -13.206 1.503   14.928 1.00 106.91 ? 286 ARG   B CD  1 
ATOM   517  N NE  . ARG   A 1 71  ? -12.073 1.882   15.783 1.00 123.47 ? 286 ARG   B NE  1 
ATOM   518  C CZ  . ARG   A 1 71  ? -11.563 3.114   15.923 1.00 128.75 ? 286 ARG   B CZ  1 
ATOM   519  N NH1 . ARG   A 1 71  ? -10.532 3.297   16.747 1.00 130.65 ? 286 ARG   B NH1 1 
ATOM   520  N NH2 . ARG   A 1 71  ? -12.053 4.168   15.264 1.00 126.03 ? 286 ARG   B NH2 1 
ATOM   521  N N   . GLU   A 1 72  ? -16.673 1.978   18.143 1.00 73.64  ? 287 GLU   B N   1 
ATOM   522  C CA  . GLU   A 1 72  ? -16.502 2.942   19.231 1.00 76.94  ? 287 GLU   B CA  1 
ATOM   523  C C   . GLU   A 1 72  ? -17.082 2.454   20.522 1.00 70.30  ? 287 GLU   B C   1 
ATOM   524  O O   . GLU   A 1 72  ? -16.527 2.741   21.567 1.00 77.51  ? 287 GLU   B O   1 
ATOM   525  C CB  . GLU   A 1 72  ? -17.120 4.299   18.910 1.00 87.65  ? 287 GLU   B CB  1 
ATOM   526  C CG  . GLU   A 1 72  ? -16.611 4.956   17.633 1.00 107.10 ? 287 GLU   B CG  1 
ATOM   527  C CD  . GLU   A 1 72  ? -15.110 5.226   17.590 1.00 115.76 ? 287 GLU   B CD  1 
ATOM   528  O OE1 . GLU   A 1 72  ? -14.657 5.726   16.537 1.00 128.07 ? 287 GLU   B OE1 1 
ATOM   529  O OE2 . GLU   A 1 72  ? -14.380 4.952   18.572 1.00 123.90 ? 287 GLU   B OE2 1 
ATOM   530  N N   . LEU   A 1 73  ? -18.194 1.727   20.465 1.00 67.25  ? 288 LEU   B N   1 
ATOM   531  C CA  . LEU   A 1 73  ? -18.700 1.045   21.665 1.00 64.24  ? 288 LEU   B CA  1 
ATOM   532  C C   . LEU   A 1 73  ? -17.675 0.047   22.229 1.00 62.08  ? 288 LEU   B C   1 
ATOM   533  O O   . LEU   A 1 73  ? -17.428 0.047   23.443 1.00 59.82  ? 288 LEU   B O   1 
ATOM   534  C CB  . LEU   A 1 73  ? -20.042 0.360   21.401 1.00 64.63  ? 288 LEU   B CB  1 
ATOM   535  C CG  . LEU   A 1 73  ? -21.245 1.307   21.315 1.00 68.74  ? 288 LEU   B CG  1 
ATOM   536  C CD1 . LEU   A 1 73  ? -22.420 0.637   20.620 1.00 69.38  ? 288 LEU   B CD1 1 
ATOM   537  C CD2 . LEU   A 1 73  ? -21.667 1.827   22.685 1.00 67.99  ? 288 LEU   B CD2 1 
ATOM   538  N N   . TYR   A 1 74  ? -17.052 -0.771  21.370 1.00 63.57  ? 289 TYR   B N   1 
ATOM   539  C CA  . TYR   A 1 74  ? -16.019 -1.722  21.851 1.00 67.93  ? 289 TYR   B CA  1 
ATOM   540  C C   . TYR   A 1 74  ? -14.777 -1.012  22.441 1.00 70.80  ? 289 TYR   B C   1 
ATOM   541  O O   . TYR   A 1 74  ? -14.274 -1.432  23.488 1.00 76.18  ? 289 TYR   B O   1 
ATOM   542  C CB  . TYR   A 1 74  ? -15.613 -2.752  20.778 1.00 67.48  ? 289 TYR   B CB  1 
ATOM   543  C CG  . TYR   A 1 74  ? -15.074 -4.064  21.365 1.00 64.80  ? 289 TYR   B CG  1 
ATOM   544  C CD1 . TYR   A 1 74  ? -13.782 -4.150  21.875 1.00 62.27  ? 289 TYR   B CD1 1 
ATOM   545  C CD2 . TYR   A 1 74  ? -15.859 -5.219  21.406 1.00 63.70  ? 289 TYR   B CD2 1 
ATOM   546  C CE1 . TYR   A 1 74  ? -13.294 -5.335  22.418 1.00 62.98  ? 289 TYR   B CE1 1 
ATOM   547  C CE2 . TYR   A 1 74  ? -15.370 -6.413  21.942 1.00 62.26  ? 289 TYR   B CE2 1 
ATOM   548  C CZ  . TYR   A 1 74  ? -14.084 -6.462  22.454 1.00 62.93  ? 289 TYR   B CZ  1 
ATOM   549  O OH  . TYR   A 1 74  ? -13.574 -7.630  23.005 1.00 68.81  ? 289 TYR   B OH  1 
ATOM   550  N N   . ASP   A 1 75  ? -14.319 0.070   21.806 1.00 74.48  ? 290 ASP   B N   1 
ATOM   551  C CA  . ASP   A 1 75  ? -13.202 0.877   22.342 1.00 75.23  ? 290 ASP   B CA  1 
ATOM   552  C C   . ASP   A 1 75  ? -13.549 1.491   23.705 1.00 72.77  ? 290 ASP   B C   1 
ATOM   553  O O   . ASP   A 1 75  ? -12.744 1.468   24.634 1.00 70.47  ? 290 ASP   B O   1 
ATOM   554  C CB  . ASP   A 1 75  ? -12.789 1.979   21.347 1.00 80.22  ? 290 ASP   B CB  1 
ATOM   555  C CG  . ASP   A 1 75  ? -12.154 1.419   20.054 1.00 85.62  ? 290 ASP   B CG  1 
ATOM   556  O OD1 . ASP   A 1 75  ? -12.061 0.181   19.867 1.00 76.34  ? 290 ASP   B OD1 1 
ATOM   557  O OD2 . ASP   A 1 75  ? -11.753 2.238   19.204 1.00 100.58 ? 290 ASP   B OD2 1 
ATOM   558  N N   . ARG   A 1 76  ? -14.753 2.033   23.806 1.00 70.74  ? 291 ARG   B N   1 
ATOM   559  C CA  . ARG   A 1 76  ? -15.313 2.506   25.079 1.00 80.78  ? 291 ARG   B CA  1 
ATOM   560  C C   . ARG   A 1 76  ? -15.436 1.365   26.116 1.00 80.92  ? 291 ARG   B C   1 
ATOM   561  O O   . ARG   A 1 76  ? -15.119 1.558   27.299 1.00 75.80  ? 291 ARG   B O   1 
ATOM   562  C CB  . ARG   A 1 76  ? -16.666 3.181   24.785 1.00 90.09  ? 291 ARG   B CB  1 
ATOM   563  C CG  . ARG   A 1 76  ? -17.637 3.444   25.928 1.00 97.97  ? 291 ARG   B CG  1 
ATOM   564  C CD  . ARG   A 1 76  ? -18.956 3.932   25.322 1.00 101.69 ? 291 ARG   B CD  1 
ATOM   565  N NE  . ARG   A 1 76  ? -20.060 4.001   26.276 1.00 103.08 ? 291 ARG   B NE  1 
ATOM   566  C CZ  . ARG   A 1 76  ? -21.332 4.246   25.953 1.00 101.12 ? 291 ARG   B CZ  1 
ATOM   567  N NH1 . ARG   A 1 76  ? -21.699 4.456   24.685 1.00 96.77  ? 291 ARG   B NH1 1 
ATOM   568  N NH2 . ARG   A 1 76  ? -22.253 4.285   26.911 1.00 100.15 ? 291 ARG   B NH2 1 
ATOM   569  N N   . GLY   A 1 77  ? -15.895 0.190   25.667 1.00 74.94  ? 292 GLY   B N   1 
ATOM   570  C CA  . GLY   A 1 77  ? -15.953 -1.001  26.512 1.00 68.26  ? 292 GLY   B CA  1 
ATOM   571  C C   . GLY   A 1 77  ? -17.073 -0.957  27.543 1.00 68.37  ? 292 GLY   B C   1 
ATOM   572  O O   . GLY   A 1 77  ? -17.907 -0.046  27.506 1.00 64.22  ? 292 GLY   B O   1 
ATOM   573  N N   . PRO   A 1 78  ? -17.079 -1.917  28.503 1.00 66.29  ? 293 PRO   B N   1 
ATOM   574  C CA  . PRO   A 1 78  ? -16.056 -2.923  28.779 1.00 61.18  ? 293 PRO   B CA  1 
ATOM   575  C C   . PRO   A 1 78  ? -16.198 -4.148  27.884 1.00 56.44  ? 293 PRO   B C   1 
ATOM   576  O O   . PRO   A 1 78  ? -17.319 -4.535  27.594 1.00 59.75  ? 293 PRO   B O   1 
ATOM   577  C CB  . PRO   A 1 78  ? -16.348 -3.293  30.230 1.00 62.59  ? 293 PRO   B CB  1 
ATOM   578  C CG  . PRO   A 1 78  ? -17.832 -3.251  30.286 1.00 67.12  ? 293 PRO   B CG  1 
ATOM   579  C CD  . PRO   A 1 78  ? -18.210 -2.060  29.439 1.00 66.81  ? 293 PRO   B CD  1 
ATOM   580  N N   . PRO   A 1 79  ? -15.075 -4.780  27.484 1.00 54.23  ? 294 PRO   B N   1 
ATOM   581  C CA  . PRO   A 1 79  ? -15.110 -5.821  26.438 1.00 56.90  ? 294 PRO   B CA  1 
ATOM   582  C C   . PRO   A 1 79  ? -15.990 -7.040  26.743 1.00 60.42  ? 294 PRO   B C   1 
ATOM   583  O O   . PRO   A 1 79  ? -16.634 -7.597  25.841 1.00 55.28  ? 294 PRO   B O   1 
ATOM   584  C CB  . PRO   A 1 79  ? -13.642 -6.264  26.301 1.00 53.09  ? 294 PRO   B CB  1 
ATOM   585  C CG  . PRO   A 1 79  ? -12.840 -5.326  27.110 1.00 53.56  ? 294 PRO   B CG  1 
ATOM   586  C CD  . PRO   A 1 79  ? -13.732 -4.640  28.080 1.00 56.19  ? 294 PRO   B CD  1 
ATOM   587  N N   . HIS   A 1 80  ? -16.004 -7.451  28.006 1.00 57.63  ? 295 HIS   B N   1 
ATOM   588  C CA  . HIS   A 1 80  ? -16.791 -8.611  28.403 1.00 57.65  ? 295 HIS   B CA  1 
ATOM   589  C C   . HIS   A 1 80  ? -18.322 -8.417  28.271 1.00 54.38  ? 295 HIS   B C   1 
ATOM   590  O O   . HIS   A 1 80  ? -19.055 -9.377  28.416 1.00 53.21  ? 295 HIS   B O   1 
ATOM   591  C CB  . HIS   A 1 80  ? -16.401 -9.047  29.824 1.00 55.57  ? 295 HIS   B CB  1 
ATOM   592  C CG  . HIS   A 1 80  ? -17.000 -8.204  30.893 1.00 55.57  ? 295 HIS   B CG  1 
ATOM   593  N ND1 . HIS   A 1 80  ? -16.547 -6.935  31.184 1.00 56.93  ? 295 HIS   B ND1 1 
ATOM   594  C CD2 . HIS   A 1 80  ? -18.035 -8.439  31.734 1.00 57.47  ? 295 HIS   B CD2 1 
ATOM   595  C CE1 . HIS   A 1 80  ? -17.295 -6.416  32.143 1.00 53.94  ? 295 HIS   B CE1 1 
ATOM   596  N NE2 . HIS   A 1 80  ? -18.192 -7.314  32.507 1.00 52.97  ? 295 HIS   B NE2 1 
ATOM   597  N N   . ALA   A 1 81  ? -18.801 -7.205  27.983 1.00 53.52  ? 296 ALA   B N   1 
ATOM   598  C CA  . ALA   A 1 81  ? -20.246 -6.957  27.814 1.00 53.38  ? 296 ALA   B CA  1 
ATOM   599  C C   . ALA   A 1 81  ? -20.801 -7.128  26.389 1.00 53.08  ? 296 ALA   B C   1 
ATOM   600  O O   . ALA   A 1 81  ? -21.984 -6.848  26.160 1.00 55.10  ? 296 ALA   B O   1 
ATOM   601  C CB  . ALA   A 1 81  ? -20.600 -5.571  28.345 1.00 56.17  ? 296 ALA   B CB  1 
ATOM   602  N N   . PHE   A 1 82  ? -19.980 -7.613  25.448 1.00 51.77  ? 297 PHE   B N   1 
ATOM   603  C CA  . PHE   A 1 82  ? -20.349 -7.699  24.027 1.00 50.86  ? 297 PHE   B CA  1 
ATOM   604  C C   . PHE   A 1 82  ? -20.668 -9.128  23.539 1.00 51.75  ? 297 PHE   B C   1 
ATOM   605  O O   . PHE   A 1 82  ? -19.837 -10.026 23.633 1.00 50.87  ? 297 PHE   B O   1 
ATOM   606  C CB  . PHE   A 1 82  ? -19.243 -7.078  23.161 1.00 55.24  ? 297 PHE   B CB  1 
ATOM   607  C CG  . PHE   A 1 82  ? -19.142 -5.589  23.322 1.00 57.70  ? 297 PHE   B CG  1 
ATOM   608  C CD1 . PHE   A 1 82  ? -18.587 -5.033  24.480 1.00 59.48  ? 297 PHE   B CD1 1 
ATOM   609  C CD2 . PHE   A 1 82  ? -19.634 -4.736  22.337 1.00 59.05  ? 297 PHE   B CD2 1 
ATOM   610  C CE1 . PHE   A 1 82  ? -18.517 -3.657  24.642 1.00 62.25  ? 297 PHE   B CE1 1 
ATOM   611  C CE2 . PHE   A 1 82  ? -19.573 -3.356  22.496 1.00 59.67  ? 297 PHE   B CE2 1 
ATOM   612  C CZ  . PHE   A 1 82  ? -19.012 -2.822  23.647 1.00 60.54  ? 297 PHE   B CZ  1 
ATOM   613  N N   . PHE   A 1 83  ? -21.866 -9.300  22.972 1.00 47.65  ? 298 PHE   B N   1 
ATOM   614  C CA  . PHE   A 1 83  ? -22.372 -10.582 22.560 1.00 45.09  ? 298 PHE   B CA  1 
ATOM   615  C C   . PHE   A 1 83  ? -22.886 -10.483 21.151 1.00 46.33  ? 298 PHE   B C   1 
ATOM   616  O O   . PHE   A 1 83  ? -23.247 -9.418  20.703 1.00 50.05  ? 298 PHE   B O   1 
ATOM   617  C CB  . PHE   A 1 83  ? -23.482 -11.057 23.516 1.00 46.02  ? 298 PHE   B CB  1 
ATOM   618  C CG  . PHE   A 1 83  ? -22.993 -11.263 24.903 1.00 46.76  ? 298 PHE   B CG  1 
ATOM   619  C CD1 . PHE   A 1 83  ? -22.961 -10.216 25.799 1.00 46.93  ? 298 PHE   B CD1 1 
ATOM   620  C CD2 . PHE   A 1 83  ? -22.473 -12.497 25.289 1.00 53.06  ? 298 PHE   B CD2 1 
ATOM   621  C CE1 . PHE   A 1 83  ? -22.442 -10.393 27.071 1.00 49.55  ? 298 PHE   B CE1 1 
ATOM   622  C CE2 . PHE   A 1 83  ? -21.953 -12.682 26.563 1.00 51.75  ? 298 PHE   B CE2 1 
ATOM   623  C CZ  . PHE   A 1 83  ? -21.942 -11.629 27.456 1.00 49.23  ? 298 PHE   B CZ  1 
ATOM   624  N N   . LEU   A 1 84  ? -22.887 -11.619 20.470 1.00 47.38  ? 299 LEU   B N   1 
ATOM   625  C CA  . LEU   A 1 84  ? -23.434 -11.766 19.155 1.00 46.80  ? 299 LEU   B CA  1 
ATOM   626  C C   . LEU   A 1 84  ? -24.468 -12.875 19.216 1.00 47.05  ? 299 LEU   B C   1 
ATOM   627  O O   . LEU   A 1 84  ? -24.168 -13.970 19.679 1.00 50.10  ? 299 LEU   B O   1 
ATOM   628  C CB  . LEU   A 1 84  ? -22.322 -12.156 18.194 1.00 50.16  ? 299 LEU   B CB  1 
ATOM   629  C CG  . LEU   A 1 84  ? -22.725 -12.658 16.802 1.00 57.90  ? 299 LEU   B CG  1 
ATOM   630  C CD1 . LEU   A 1 84  ? -23.620 -11.668 16.060 1.00 59.27  ? 299 LEU   B CD1 1 
ATOM   631  C CD2 . LEU   A 1 84  ? -21.468 -12.925 15.998 1.00 61.85  ? 299 LEU   B CD2 1 
ATOM   632  N N   . VAL   A 1 85  ? -25.677 -12.599 18.752 1.00 45.67  ? 300 VAL   B N   1 
ATOM   633  C CA  . VAL   A 1 85  ? -26.707 -13.620 18.645 1.00 49.89  ? 300 VAL   B CA  1 
ATOM   634  C C   . VAL   A 1 85  ? -27.003 -13.861 17.191 1.00 51.19  ? 300 VAL   B C   1 
ATOM   635  O O   . VAL   A 1 85  ? -27.366 -12.926 16.476 1.00 54.11  ? 300 VAL   B O   1 
ATOM   636  C CB  . VAL   A 1 85  ? -27.999 -13.179 19.352 1.00 49.51  ? 300 VAL   B CB  1 
ATOM   637  C CG1 . VAL   A 1 85  ? -29.163 -14.150 19.078 1.00 51.65  ? 300 VAL   B CG1 1 
ATOM   638  C CG2 . VAL   A 1 85  ? -27.715 -13.056 20.836 1.00 48.35  ? 300 VAL   B CG2 1 
ATOM   639  N N   . LYS   A 1 86  ? -26.836 -15.102 16.745 1.00 50.67  ? 301 LYS   B N   1 
ATOM   640  C CA  . LYS   A 1 86  ? -27.331 -15.490 15.444 1.00 51.69  ? 301 LYS   B CA  1 
ATOM   641  C C   . LYS   A 1 86  ? -28.727 -16.090 15.657 1.00 50.48  ? 301 LYS   B C   1 
ATOM   642  O O   . LYS   A 1 86  ? -28.938 -16.942 16.525 1.00 49.82  ? 301 LYS   B O   1 
ATOM   643  C CB  . LYS   A 1 86  ? -26.377 -16.469 14.752 1.00 57.42  ? 301 LYS   B CB  1 
ATOM   644  C CG  . LYS   A 1 86  ? -26.756 -16.790 13.313 1.00 65.18  ? 301 LYS   B CG  1 
ATOM   645  C CD  . LYS   A 1 86  ? -25.650 -17.584 12.639 1.00 72.66  ? 301 LYS   B CD  1 
ATOM   646  C CE  . LYS   A 1 86  ? -25.789 -17.634 11.127 1.00 76.35  ? 301 LYS   B CE  1 
ATOM   647  N NZ  . LYS   A 1 86  ? -24.493 -18.101 10.548 1.00 82.36  ? 301 LYS   B NZ  1 
ATOM   648  N N   . PHE   A 1 87  ? -29.676 -15.646 14.853 1.00 48.96  ? 302 PHE   B N   1 
ATOM   649  C CA  . PHE   A 1 87  ? -31.045 -16.122 14.927 1.00 48.42  ? 302 PHE   B CA  1 
ATOM   650  C C   . PHE   A 1 87  ? -31.399 -16.812 13.637 1.00 51.45  ? 302 PHE   B C   1 
ATOM   651  O O   . PHE   A 1 87  ? -31.055 -16.283 12.557 1.00 43.20  ? 302 PHE   B O   1 
ATOM   652  C CB  . PHE   A 1 87  ? -32.027 -14.954 15.048 1.00 45.89  ? 302 PHE   B CB  1 
ATOM   653  C CG  . PHE   A 1 87  ? -32.252 -14.470 16.445 1.00 46.28  ? 302 PHE   B CG  1 
ATOM   654  C CD1 . PHE   A 1 87  ? -32.560 -15.363 17.468 1.00 45.25  ? 302 PHE   B CD1 1 
ATOM   655  C CD2 . PHE   A 1 87  ? -32.267 -13.112 16.719 1.00 47.14  ? 302 PHE   B CD2 1 
ATOM   656  C CE1 . PHE   A 1 87  ? -32.799 -14.914 18.747 1.00 47.66  ? 302 PHE   B CE1 1 
ATOM   657  C CE2 . PHE   A 1 87  ? -32.533 -12.648 18.001 1.00 49.78  ? 302 PHE   B CE2 1 
ATOM   658  C CZ  . PHE   A 1 87  ? -32.787 -13.552 19.017 1.00 51.42  ? 302 PHE   B CZ  1 
ATOM   659  N N   . TRP   A 1 88  ? -32.119 -17.941 13.767 1.00 45.35  ? 303 TRP   B N   1 
ATOM   660  C CA  . TRP   A 1 88  ? -32.879 -18.493 12.690 1.00 44.01  ? 303 TRP   B CA  1 
ATOM   661  C C   . TRP   A 1 88  ? -34.318 -18.181 12.999 1.00 44.17  ? 303 TRP   B C   1 
ATOM   662  O O   . TRP   A 1 88  ? -34.913 -18.750 13.910 1.00 51.11  ? 303 TRP   B O   1 
ATOM   663  C CB  . TRP   A 1 88  ? -32.650 -19.986 12.567 1.00 43.34  ? 303 TRP   B CB  1 
ATOM   664  C CG  . TRP   A 1 88  ? -31.287 -20.286 12.135 1.00 45.73  ? 303 TRP   B CG  1 
ATOM   665  C CD1 . TRP   A 1 88  ? -30.853 -20.448 10.845 1.00 49.61  ? 303 TRP   B CD1 1 
ATOM   666  C CD2 . TRP   A 1 88  ? -30.140 -20.434 12.968 1.00 44.67  ? 303 TRP   B CD2 1 
ATOM   667  N NE1 . TRP   A 1 88  ? -29.494 -20.690 10.832 1.00 47.59  ? 303 TRP   B NE1 1 
ATOM   668  C CE2 . TRP   A 1 88  ? -29.035 -20.689 12.121 1.00 45.34  ? 303 TRP   B CE2 1 
ATOM   669  C CE3 . TRP   A 1 88  ? -29.931 -20.381 14.356 1.00 50.07  ? 303 TRP   B CE3 1 
ATOM   670  C CZ2 . TRP   A 1 88  ? -27.743 -20.905 12.615 1.00 46.56  ? 303 TRP   B CZ2 1 
ATOM   671  C CZ3 . TRP   A 1 88  ? -28.615 -20.579 14.854 1.00 47.77  ? 303 TRP   B CZ3 1 
ATOM   672  C CH2 . TRP   A 1 88  ? -27.556 -20.846 13.984 1.00 47.92  ? 303 TRP   B CH2 1 
ATOM   673  N N   . ALA   A 1 89  ? -34.892 -17.299 12.205 1.00 44.05  ? 304 ALA   B N   1 
ATOM   674  C CA  . ALA   A 1 89  ? -36.196 -16.739 12.503 1.00 42.46  ? 304 ALA   B CA  1 
ATOM   675  C C   . ALA   A 1 89  ? -37.292 -17.524 11.805 1.00 46.18  ? 304 ALA   B C   1 
ATOM   676  O O   . ALA   A 1 89  ? -37.114 -17.960 10.676 1.00 48.11  ? 304 ALA   B O   1 
ATOM   677  C CB  . ALA   A 1 89  ? -36.247 -15.285 12.073 1.00 38.78  ? 304 ALA   B CB  1 
ATOM   678  N N   . ASP   A 1 90  ? -38.420 -17.679 12.491 1.00 49.20  ? 305 ASP   B N   1 
ATOM   679  C CA  . ASP   A 1 90  ? -39.530 -18.439 12.014 1.00 49.14  ? 305 ASP   B CA  1 
ATOM   680  C C   . ASP   A 1 90  ? -40.481 -17.471 11.381 1.00 52.26  ? 305 ASP   B C   1 
ATOM   681  O O   . ASP   A 1 90  ? -41.179 -16.727 12.102 1.00 55.42  ? 305 ASP   B O   1 
ATOM   682  C CB  . ASP   A 1 90  ? -40.180 -19.168 13.181 1.00 50.70  ? 305 ASP   B CB  1 
ATOM   683  C CG  . ASP   A 1 90  ? -41.299 -20.092 12.743 1.00 58.42  ? 305 ASP   B CG  1 
ATOM   684  O OD1 . ASP   A 1 90  ? -41.740 -19.993 11.580 1.00 61.39  ? 305 ASP   B OD1 1 
ATOM   685  O OD2 . ASP   A 1 90  ? -41.767 -20.911 13.570 1.00 63.89  ? 305 ASP   B OD2 1 
ATOM   686  N N   . LEU   A 1 91  ? -40.527 -17.471 10.041 1.00 54.13  ? 306 LEU   B N   1 
ATOM   687  C CA  . LEU   A 1 91  ? -41.374 -16.505 9.279  1.00 59.60  ? 306 LEU   B CA  1 
ATOM   688  C C   . LEU   A 1 91  ? -42.587 -17.157 8.665  1.00 66.49  ? 306 LEU   B C   1 
ATOM   689  O O   . LEU   A 1 91  ? -43.103 -16.676 7.656  1.00 65.83  ? 306 LEU   B O   1 
ATOM   690  C CB  . LEU   A 1 91  ? -40.581 -15.797 8.183  1.00 56.39  ? 306 LEU   B CB  1 
ATOM   691  C CG  . LEU   A 1 91  ? -39.247 -15.217 8.663  1.00 59.68  ? 306 LEU   B CG  1 
ATOM   692  C CD1 . LEU   A 1 91  ? -38.430 -14.663 7.498  1.00 62.97  ? 306 LEU   B CD1 1 
ATOM   693  C CD2 . LEU   A 1 91  ? -39.495 -14.169 9.741  1.00 58.15  ? 306 LEU   B CD2 1 
ATOM   694  N N   . ASN   A 1 92  ? -43.065 -18.208 9.326  1.00 67.69  ? 307 ASN   B N   1 
ATOM   695  C CA  . ASN   A 1 92  ? -44.127 -19.042 8.845  1.00 71.08  ? 307 ASN   B CA  1 
ATOM   696  C C   . ASN   A 1 92  ? -45.290 -18.818 9.784  1.00 63.02  ? 307 ASN   B C   1 
ATOM   697  O O   . ASN   A 1 92  ? -45.399 -19.479 10.798 1.00 60.68  ? 307 ASN   B O   1 
ATOM   698  C CB  . ASN   A 1 92  ? -43.627 -20.515 8.812  1.00 78.93  ? 307 ASN   B CB  1 
ATOM   699  C CG  . ASN   A 1 92  ? -44.751 -21.546 8.821  1.00 86.71  ? 307 ASN   B CG  1 
ATOM   700  O OD1 . ASN   A 1 92  ? -44.750 -22.485 9.635  1.00 97.12  ? 307 ASN   B OD1 1 
ATOM   701  N ND2 . ASN   A 1 92  ? -45.713 -21.379 7.923  1.00 87.36  ? 307 ASN   B ND2 1 
ATOM   702  N N   . TRP   A 1 93  ? -46.138 -17.857 9.452  1.00 63.21  ? 308 TRP   B N   1 
ATOM   703  C CA  . TRP   A 1 93  ? -47.406 -17.679 10.147 1.00 71.57  ? 308 TRP   B CA  1 
ATOM   704  C C   . TRP   A 1 93  ? -48.479 -17.139 9.191  1.00 83.04  ? 308 TRP   B C   1 
ATOM   705  O O   . TRP   A 1 93  ? -49.649 -17.542 9.246  1.00 90.05  ? 308 TRP   B O   1 
ATOM   706  C CB  . TRP   A 1 93  ? -47.222 -16.736 11.339 1.00 72.43  ? 308 TRP   B CB  1 
ATOM   707  C CG  . TRP   A 1 93  ? -47.237 -15.250 10.992 1.00 71.50  ? 308 TRP   B CG  1 
ATOM   708  C CD1 . TRP   A 1 93  ? -48.260 -14.373 11.220 1.00 69.41  ? 308 TRP   B CD1 1 
ATOM   709  C CD2 . TRP   A 1 93  ? -46.185 -14.484 10.350 1.00 71.86  ? 308 TRP   B CD2 1 
ATOM   710  N NE1 . TRP   A 1 93  ? -47.918 -13.109 10.763 1.00 75.65  ? 308 TRP   B NE1 1 
ATOM   711  C CE2 . TRP   A 1 93  ? -46.655 -13.149 10.226 1.00 73.30  ? 308 TRP   B CE2 1 
ATOM   712  C CE3 . TRP   A 1 93  ? -44.906 -14.802 9.853  1.00 70.41  ? 308 TRP   B CE3 1 
ATOM   713  C CZ2 . TRP   A 1 93  ? -45.881 -12.123 9.643  1.00 70.73  ? 308 TRP   B CZ2 1 
ATOM   714  C CZ3 . TRP   A 1 93  ? -44.129 -13.779 9.270  1.00 72.04  ? 308 TRP   B CZ3 1 
ATOM   715  C CH2 . TRP   A 1 93  ? -44.625 -12.455 9.174  1.00 71.33  ? 308 TRP   B CH2 1 
ATOM   716  N N   . GLY   A 1 109 ? -53.147 -7.991  10.194 1.00 72.87  ? 324 GLY   B N   1 
ATOM   717  C CA  . GLY   A 1 109 ? -53.360 -6.839  11.072 1.00 80.14  ? 324 GLY   B CA  1 
ATOM   718  C C   . GLY   A 1 109 ? -53.515 -7.220  12.543 1.00 82.28  ? 324 GLY   B C   1 
ATOM   719  O O   . GLY   A 1 109 ? -54.421 -6.734  13.224 1.00 81.33  ? 324 GLY   B O   1 
ATOM   720  N N   . GLY   A 1 110 ? -52.632 -8.097  13.026 1.00 77.39  ? 325 GLY   B N   1 
ATOM   721  C CA  . GLY   A 1 110 ? -52.597 -8.506  14.433 1.00 66.51  ? 325 GLY   B CA  1 
ATOM   722  C C   . GLY   A 1 110 ? -51.658 -7.599  15.215 1.00 61.92  ? 325 GLY   B C   1 
ATOM   723  O O   . GLY   A 1 110 ? -51.392 -6.488  14.767 1.00 66.20  ? 325 GLY   B O   1 
ATOM   724  N N   . PHE   A 1 111 ? -51.141 -8.079  16.359 1.00 50.12  ? 326 PHE   B N   1 
ATOM   725  C CA  . PHE   A 1 111 ? -50.249 -7.286  17.236 1.00 50.56  ? 326 PHE   B CA  1 
ATOM   726  C C   . PHE   A 1 111 ? -48.814 -7.758  17.186 1.00 44.21  ? 326 PHE   B C   1 
ATOM   727  O O   . PHE   A 1 111 ? -48.527 -8.892  17.526 1.00 44.77  ? 326 PHE   B O   1 
ATOM   728  C CB  . PHE   A 1 111 ? -50.697 -7.313  18.722 1.00 52.32  ? 326 PHE   B CB  1 
ATOM   729  C CG  . PHE   A 1 111 ? -49.750 -6.588  19.649 1.00 48.24  ? 326 PHE   B CG  1 
ATOM   730  C CD1 . PHE   A 1 111 ? -49.586 -5.212  19.555 1.00 46.75  ? 326 PHE   B CD1 1 
ATOM   731  C CD2 . PHE   A 1 111 ? -49.008 -7.280  20.598 1.00 46.87  ? 326 PHE   B CD2 1 
ATOM   732  C CE1 . PHE   A 1 111 ? -48.694 -4.551  20.396 1.00 49.22  ? 326 PHE   B CE1 1 
ATOM   733  C CE2 . PHE   A 1 111 ? -48.120 -6.615  21.441 1.00 45.12  ? 326 PHE   B CE2 1 
ATOM   734  C CZ  . PHE   A 1 111 ? -47.960 -5.253  21.338 1.00 43.60  ? 326 PHE   B CZ  1 
ATOM   735  N N   . TYR   A 1 112 ? -47.917 -6.860  16.805 1.00 44.61  ? 327 TYR   B N   1 
ATOM   736  C CA  . TYR   A 1 112 ? -46.509 -7.157  16.709 1.00 41.84  ? 327 TYR   B CA  1 
ATOM   737  C C   . TYR   A 1 112 ? -45.796 -6.524  17.900 1.00 41.83  ? 327 TYR   B C   1 
ATOM   738  O O   . TYR   A 1 112 ? -45.804 -5.289  18.087 1.00 42.53  ? 327 TYR   B O   1 
ATOM   739  C CB  . TYR   A 1 112 ? -45.986 -6.643  15.366 1.00 43.59  ? 327 TYR   B CB  1 
ATOM   740  C CG  . TYR   A 1 112 ? -46.585 -7.400  14.162 1.00 47.61  ? 327 TYR   B CG  1 
ATOM   741  C CD1 . TYR   A 1 112 ? -47.904 -7.151  13.719 1.00 48.14  ? 327 TYR   B CD1 1 
ATOM   742  C CD2 . TYR   A 1 112 ? -45.829 -8.354  13.452 1.00 48.47  ? 327 TYR   B CD2 1 
ATOM   743  C CE1 . TYR   A 1 112 ? -48.442 -7.813  12.630 1.00 45.54  ? 327 TYR   B CE1 1 
ATOM   744  C CE2 . TYR   A 1 112 ? -46.370 -9.026  12.354 1.00 46.84  ? 327 TYR   B CE2 1 
ATOM   745  C CZ  . TYR   A 1 112 ? -47.672 -8.750  11.956 1.00 48.64  ? 327 TYR   B CZ  1 
ATOM   746  O OH  . TYR   A 1 112 ? -48.218 -9.451  10.910 1.00 51.68  ? 327 TYR   B OH  1 
ATOM   747  N N   . GLY   A 1 113 ? -45.200 -7.371  18.728 1.00 42.45  ? 328 GLY   B N   1 
ATOM   748  C CA  . GLY   A 1 113 ? -44.512 -6.898  19.912 1.00 41.00  ? 328 GLY   B CA  1 
ATOM   749  C C   . GLY   A 1 113 ? -43.167 -7.511  20.171 1.00 39.63  ? 328 GLY   B C   1 
ATOM   750  O O   . GLY   A 1 113 ? -42.768 -8.476  19.526 1.00 41.53  ? 328 GLY   B O   1 
ATOM   751  N N   . VAL   A 1 114 ? -42.494 -6.922  21.153 1.00 42.78  ? 329 VAL   B N   1 
ATOM   752  C CA  . VAL   A 1 114 ? -41.137 -7.255  21.585 1.00 44.55  ? 329 VAL   B CA  1 
ATOM   753  C C   . VAL   A 1 114 ? -41.081 -7.180  23.125 1.00 44.54  ? 329 VAL   B C   1 
ATOM   754  O O   . VAL   A 1 114 ? -41.459 -6.167  23.715 1.00 45.80  ? 329 VAL   B O   1 
ATOM   755  C CB  . VAL   A 1 114 ? -40.129 -6.238  21.012 1.00 46.96  ? 329 VAL   B CB  1 
ATOM   756  C CG1 . VAL   A 1 114 ? -38.686 -6.610  21.366 1.00 47.30  ? 329 VAL   B CG1 1 
ATOM   757  C CG2 . VAL   A 1 114 ? -40.302 -6.148  19.499 1.00 50.17  ? 329 VAL   B CG2 1 
ATOM   758  N N   . SER   A 1 115 ? -40.618 -8.247  23.766 1.00 45.06  ? 330 SER   B N   1 
ATOM   759  C CA  . SER   A 1 115 ? -40.576 -8.314  25.232 1.00 46.00  ? 330 SER   B CA  1 
ATOM   760  C C   . SER   A 1 115 ? -39.164 -8.685  25.649 1.00 45.61  ? 330 SER   B C   1 
ATOM   761  O O   . SER   A 1 115 ? -38.560 -9.614  25.083 1.00 39.74  ? 330 SER   B O   1 
ATOM   762  C CB  . SER   A 1 115 ? -41.607 -9.302  25.783 1.00 46.11  ? 330 SER   B CB  1 
ATOM   763  O OG  . SER   A 1 115 ? -42.949 -8.827  25.602 1.00 48.71  ? 330 SER   B OG  1 
ATOM   764  N N   . SER   A 1 116 ? -38.633 -7.908  26.595 1.00 45.60  ? 331 SER   B N   1 
ATOM   765  C CA  . SER   A 1 116 ? -37.321 -8.136  27.182 1.00 47.57  ? 331 SER   B CA  1 
ATOM   766  C C   . SER   A 1 116 ? -37.452 -8.111  28.699 1.00 49.96  ? 331 SER   B C   1 
ATOM   767  O O   . SER   A 1 116 ? -38.259 -7.376  29.269 1.00 53.07  ? 331 SER   B O   1 
ATOM   768  C CB  . SER   A 1 116 ? -36.348 -7.051  26.768 1.00 51.15  ? 331 SER   B CB  1 
ATOM   769  O OG  . SER   A 1 116 ? -36.181 -7.029  25.367 1.00 63.53  ? 331 SER   B OG  1 
ATOM   770  N N   . GLN   A 1 117 ? -36.634 -8.910  29.352 1.00 53.51  ? 332 GLN   B N   1 
ATOM   771  C CA  . GLN   A 1 117 ? -36.508 -8.859  30.780 1.00 55.27  ? 332 GLN   B CA  1 
ATOM   772  C C   . GLN   A 1 117 ? -35.053 -9.113  31.127 1.00 49.53  ? 332 GLN   B C   1 
ATOM   773  O O   . GLN   A 1 117 ? -34.415 -10.027 30.575 1.00 44.62  ? 332 GLN   B O   1 
ATOM   774  C CB  . GLN   A 1 117 ? -37.446 -9.886  31.425 1.00 61.99  ? 332 GLN   B CB  1 
ATOM   775  C CG  . GLN   A 1 117 ? -37.845 -9.551  32.862 1.00 72.47  ? 332 GLN   B CG  1 
ATOM   776  C CD  . GLN   A 1 117 ? -38.831 -10.550 33.488 1.00 71.00  ? 332 GLN   B CD  1 
ATOM   777  O OE1 . GLN   A 1 117 ? -38.959 -10.622 34.708 1.00 82.17  ? 332 GLN   B OE1 1 
ATOM   778  N NE2 . GLN   A 1 117 ? -39.515 -11.316 32.658 1.00 72.53  ? 332 GLN   B NE2 1 
ATOM   779  N N   . TYR   A 1 118 ? -34.531 -8.297  32.035 1.00 49.80  ? 333 TYR   B N   1 
ATOM   780  C CA  . TYR   A 1 118 ? -33.184 -8.469  32.569 1.00 48.96  ? 333 TYR   B CA  1 
ATOM   781  C C   . TYR   A 1 118 ? -33.207 -8.510  34.118 1.00 52.18  ? 333 TYR   B C   1 
ATOM   782  O O   . TYR   A 1 118 ? -34.190 -8.128  34.745 1.00 57.53  ? 333 TYR   B O   1 
ATOM   783  C CB  . TYR   A 1 118 ? -32.313 -7.294  32.131 1.00 48.70  ? 333 TYR   B CB  1 
ATOM   784  C CG  . TYR   A 1 118 ? -32.318 -6.925  30.662 1.00 48.07  ? 333 TYR   B CG  1 
ATOM   785  C CD1 . TYR   A 1 118 ? -33.349 -6.168  30.117 1.00 48.48  ? 333 TYR   B CD1 1 
ATOM   786  C CD2 . TYR   A 1 118 ? -31.264 -7.263  29.830 1.00 50.95  ? 333 TYR   B CD2 1 
ATOM   787  C CE1 . TYR   A 1 118 ? -33.353 -5.794  28.783 1.00 46.98  ? 333 TYR   B CE1 1 
ATOM   788  C CE2 . TYR   A 1 118 ? -31.269 -6.890  28.479 1.00 53.73  ? 333 TYR   B CE2 1 
ATOM   789  C CZ  . TYR   A 1 118 ? -32.319 -6.156  27.961 1.00 48.54  ? 333 TYR   B CZ  1 
ATOM   790  O OH  . TYR   A 1 118 ? -32.336 -5.764  26.629 1.00 51.55  ? 333 TYR   B OH  1 
ATOM   791  N N   . GLU   A 1 119 ? -32.105 -8.922  34.722 1.00 55.65  ? 334 GLU   B N   1 
ATOM   792  C CA  . GLU   A 1 119 ? -31.986 -8.999  36.169 1.00 60.85  ? 334 GLU   B CA  1 
ATOM   793  C C   . GLU   A 1 119 ? -30.653 -8.448  36.604 1.00 62.78  ? 334 GLU   B C   1 
ATOM   794  O O   . GLU   A 1 119 ? -29.659 -8.629  35.903 1.00 60.46  ? 334 GLU   B O   1 
ATOM   795  C CB  . GLU   A 1 119 ? -32.078 -10.460 36.604 1.00 70.79  ? 334 GLU   B CB  1 
ATOM   796  C CG  . GLU   A 1 119 ? -33.352 -10.817 37.355 1.00 81.61  ? 334 GLU   B CG  1 
ATOM   797  C CD  . GLU   A 1 119 ? -33.527 -12.314 37.565 1.00 83.43  ? 334 GLU   B CD  1 
ATOM   798  O OE1 . GLU   A 1 119 ? -32.574 -13.097 37.352 1.00 79.02  ? 334 GLU   B OE1 1 
ATOM   799  O OE2 . GLU   A 1 119 ? -34.640 -12.705 37.956 1.00 92.00  ? 334 GLU   B OE2 1 
ATOM   800  N N   . SER   A 1 120 ? -30.611 -7.808  37.771 1.00 67.03  ? 335 SER   B N   1 
ATOM   801  C CA  . SER   A 1 120 ? -29.327 -7.468  38.383 1.00 67.51  ? 335 SER   B CA  1 
ATOM   802  C C   . SER   A 1 120 ? -29.331 -7.637  39.875 1.00 72.45  ? 335 SER   B C   1 
ATOM   803  O O   . SER   A 1 120 ? -30.392 -7.667  40.507 1.00 71.39  ? 335 SER   B O   1 
ATOM   804  C CB  . SER   A 1 120 ? -28.940 -6.028  38.111 1.00 66.47  ? 335 SER   B CB  1 
ATOM   805  O OG  . SER   A 1 120 ? -27.653 -5.782  38.684 1.00 69.85  ? 335 SER   B OG  1 
ATOM   806  N N   . LEU   A 1 121 ? -28.114 -7.700  40.416 1.00 71.10  ? 336 LEU   B N   1 
ATOM   807  C CA  . LEU   A 1 121 ? -27.890 -7.563  41.837 1.00 66.10  ? 336 LEU   B CA  1 
ATOM   808  C C   . LEU   A 1 121 ? -28.150 -6.139  42.301 1.00 69.05  ? 336 LEU   B C   1 
ATOM   809  O O   . LEU   A 1 121 ? -28.627 -5.959  43.400 1.00 74.51  ? 336 LEU   B O   1 
ATOM   810  C CB  . LEU   A 1 121 ? -26.466 -7.962  42.220 1.00 69.66  ? 336 LEU   B CB  1 
ATOM   811  C CG  . LEU   A 1 121 ? -26.120 -9.451  42.182 1.00 76.69  ? 336 LEU   B CG  1 
ATOM   812  C CD1 . LEU   A 1 121 ? -24.661 -9.628  42.598 1.00 78.99  ? 336 LEU   B CD1 1 
ATOM   813  C CD2 . LEU   A 1 121 ? -27.052 -10.287 43.060 1.00 74.08  ? 336 LEU   B CD2 1 
ATOM   814  N N   . GLU   A 1 122 ? -27.876 -5.131  41.476 1.00 70.68  ? 337 GLU   B N   1 
ATOM   815  C CA  . GLU   A 1 122 ? -27.993 -3.714  41.900 1.00 67.70  ? 337 GLU   B CA  1 
ATOM   816  C C   . GLU   A 1 122 ? -29.184 -2.984  41.265 1.00 66.80  ? 337 GLU   B C   1 
ATOM   817  O O   . GLU   A 1 122 ? -29.714 -3.406  40.237 1.00 78.93  ? 337 GLU   B O   1 
ATOM   818  C CB  . GLU   A 1 122 ? -26.687 -2.929  41.664 1.00 69.68  ? 337 GLU   B CB  1 
ATOM   819  C CG  . GLU   A 1 122 ? -25.865 -3.382  40.464 1.00 80.97  ? 337 GLU   B CG  1 
ATOM   820  C CD  . GLU   A 1 122 ? -24.611 -2.568  40.251 1.00 82.07  ? 337 GLU   B CD  1 
ATOM   821  O OE1 . GLU   A 1 122 ? -24.531 -1.459  40.812 1.00 79.20  ? 337 GLU   B OE1 1 
ATOM   822  O OE2 . GLU   A 1 122 ? -23.714 -3.053  39.515 1.00 79.17  ? 337 GLU   B OE2 1 
ATOM   823  N N   . HIS   A 1 123 ? -29.597 -1.905  41.928 1.00 63.80  ? 338 HIS   B N   1 
ATOM   824  C CA  . HIS   A 1 123 ? -30.694 -1.010  41.520 1.00 64.94  ? 338 HIS   B CA  1 
ATOM   825  C C   . HIS   A 1 123 ? -30.179 0.087   40.576 1.00 64.09  ? 338 HIS   B C   1 
ATOM   826  O O   . HIS   A 1 123 ? -29.380 0.929   40.979 1.00 64.21  ? 338 HIS   B O   1 
ATOM   827  C CB  . HIS   A 1 123 ? -31.318 -0.333  42.770 1.00 68.43  ? 338 HIS   B CB  1 
ATOM   828  C CG  . HIS   A 1 123 ? -32.373 0.688   42.465 1.00 70.35  ? 338 HIS   B CG  1 
ATOM   829  N ND1 . HIS   A 1 123 ? -33.710 0.372   42.364 1.00 71.83  ? 338 HIS   B ND1 1 
ATOM   830  C CD2 . HIS   A 1 123 ? -32.286 2.022   42.249 1.00 80.88  ? 338 HIS   B CD2 1 
ATOM   831  C CE1 . HIS   A 1 123 ? -34.400 1.462   42.084 1.00 77.43  ? 338 HIS   B CE1 1 
ATOM   832  N NE2 . HIS   A 1 123 ? -33.559 2.477   42.003 1.00 81.38  ? 338 HIS   B NE2 1 
ATOM   833  N N   . MET   A 1 124 ? -30.655 0.082   39.332 1.00 61.90  ? 339 MET   B N   1 
ATOM   834  C CA  . MET   A 1 124 ? -30.251 1.056   38.325 1.00 56.29  ? 339 MET   B CA  1 
ATOM   835  C C   . MET   A 1 124 ? -31.489 1.482   37.591 1.00 53.42  ? 339 MET   B C   1 
ATOM   836  O O   . MET   A 1 124 ? -32.534 0.862   37.703 1.00 58.25  ? 339 MET   B O   1 
ATOM   837  C CB  . MET   A 1 124 ? -29.273 0.409   37.341 1.00 59.18  ? 339 MET   B CB  1 
ATOM   838  C CG  . MET   A 1 124 ? -27.996 -0.127  37.991 1.00 61.88  ? 339 MET   B CG  1 
ATOM   839  S SD  . MET   A 1 124 ? -26.922 -1.109  36.914 1.00 69.88  ? 339 MET   B SD  1 
ATOM   840  C CE  . MET   A 1 124 ? -27.867 -2.627  36.761 1.00 65.39  ? 339 MET   B CE  1 
ATOM   841  N N   . THR   A 1 125 ? -31.389 2.577   36.878 1.00 54.35  ? 340 THR   B N   1 
ATOM   842  C CA  . THR   A 1 125 ? -32.338 2.857   35.837 1.00 61.44  ? 340 THR   B CA  1 
ATOM   843  C C   . THR   A 1 125 ? -31.547 2.531   34.586 1.00 57.01  ? 340 THR   B C   1 
ATOM   844  O O   . THR   A 1 125 ? -30.392 2.927   34.452 1.00 56.56  ? 340 THR   B O   1 
ATOM   845  C CB  . THR   A 1 125 ? -32.830 4.312   35.835 1.00 66.86  ? 340 THR   B CB  1 
ATOM   846  O OG1 . THR   A 1 125 ? -31.708 5.187   35.956 1.00 94.94  ? 340 THR   B OG1 1 
ATOM   847  C CG2 . THR   A 1 125 ? -33.790 4.581   36.993 1.00 66.15  ? 340 THR   B CG2 1 
ATOM   848  N N   . LEU   A 1 126 ? -32.165 1.754   33.708 1.00 55.83  ? 341 LEU   B N   1 
ATOM   849  C CA  . LEU   A 1 126 ? -31.563 1.341   32.449 1.00 50.71  ? 341 LEU   B CA  1 
ATOM   850  C C   . LEU   A 1 126 ? -32.051 2.189   31.313 1.00 49.65  ? 341 LEU   B C   1 
ATOM   851  O O   . LEU   A 1 126 ? -33.224 2.571   31.306 1.00 49.14  ? 341 LEU   B O   1 
ATOM   852  C CB  . LEU   A 1 126 ? -31.966 -0.088  32.129 1.00 49.37  ? 341 LEU   B CB  1 
ATOM   853  C CG  . LEU   A 1 126 ? -31.545 -1.126  33.161 1.00 47.98  ? 341 LEU   B CG  1 
ATOM   854  C CD1 . LEU   A 1 126 ? -32.008 -2.480  32.669 1.00 49.71  ? 341 LEU   B CD1 1 
ATOM   855  C CD2 . LEU   A 1 126 ? -30.038 -1.108  33.358 1.00 46.88  ? 341 LEU   B CD2 1 
ATOM   856  N N   . THR   A 1 127 ? -31.161 2.452   30.357 1.00 43.32  ? 342 THR   B N   1 
ATOM   857  C CA  . THR   A 1 127 ? -31.564 2.858   29.029 1.00 46.05  ? 342 THR   B CA  1 
ATOM   858  C C   . THR   A 1 127 ? -31.305 1.706   28.042 1.00 47.21  ? 342 THR   B C   1 
ATOM   859  O O   . THR   A 1 127 ? -30.205 1.174   27.984 1.00 44.98  ? 342 THR   B O   1 
ATOM   860  C CB  . THR   A 1 127 ? -30.806 4.116   28.592 1.00 49.93  ? 342 THR   B CB  1 
ATOM   861  O OG1 . THR   A 1 127 ? -30.907 5.101   29.627 1.00 49.89  ? 342 THR   B OG1 1 
ATOM   862  C CG2 . THR   A 1 127 ? -31.396 4.683   27.281 1.00 48.82  ? 342 THR   B CG2 1 
ATOM   863  N N   . CYS   A 1 128 ? -32.330 1.339   27.278 1.00 45.87  ? 343 CYS   B N   1 
ATOM   864  C CA  . CYS   A 1 128 ? -32.251 0.280   26.325 1.00 48.19  ? 343 CYS   B CA  1 
ATOM   865  C C   . CYS   A 1 128 ? -32.486 0.880   25.006 1.00 46.70  ? 343 CYS   B C   1 
ATOM   866  O O   . CYS   A 1 128 ? -33.591 1.322   24.754 1.00 46.06  ? 343 CYS   B O   1 
ATOM   867  C CB  . CYS   A 1 128 ? -33.357 -0.734  26.571 1.00 56.63  ? 343 CYS   B CB  1 
ATOM   868  S SG  . CYS   A 1 128 ? -33.331 -1.437  28.235 1.00 62.64  ? 343 CYS   B SG  1 
ATOM   869  N N   . SER   A 1 129 ? -31.469 0.852   24.157 1.00 44.74  ? 344 SER   B N   1 
ATOM   870  C CA  . SER   A 1 129 ? -31.581 1.306   22.782 1.00 47.73  ? 344 SER   B CA  1 
ATOM   871  C C   . SER   A 1 129 ? -31.541 0.126   21.805 1.00 48.96  ? 344 SER   B C   1 
ATOM   872  O O   . SER   A 1 129 ? -30.627 -0.671  21.862 1.00 53.53  ? 344 SER   B O   1 
ATOM   873  C CB  . SER   A 1 129 ? -30.417 2.248   22.457 1.00 48.62  ? 344 SER   B CB  1 
ATOM   874  O OG  . SER   A 1 129 ? -30.148 2.220   21.066 1.00 54.24  ? 344 SER   B OG  1 
ATOM   875  N N   . SER   A 1 130 ? -32.499 0.043   20.894 1.00 49.38  ? 345 SER   B N   1 
ATOM   876  C CA  . SER   A 1 130 ? -32.483 -0.920  19.804 1.00 50.66  ? 345 SER   B CA  1 
ATOM   877  C C   . SER   A 1 130 ? -32.403 -0.214  18.434 1.00 55.15  ? 345 SER   B C   1 
ATOM   878  O O   . SER   A 1 130 ? -33.366 0.447   18.018 1.00 53.73  ? 345 SER   B O   1 
ATOM   879  C CB  . SER   A 1 130 ? -33.749 -1.764  19.888 1.00 52.47  ? 345 SER   B CB  1 
ATOM   880  O OG  . SER   A 1 130 ? -33.814 -2.387  21.157 1.00 58.74  ? 345 SER   B OG  1 
ATOM   881  N N   . LYS   A 1 131 ? -31.270 -0.369  17.741 1.00 53.64  ? 346 LYS   B N   1 
ATOM   882  C CA  . LYS   A 1 131 ? -31.005 0.292   16.448 1.00 53.77  ? 346 LYS   B CA  1 
ATOM   883  C C   . LYS   A 1 131 ? -31.117 -0.702  15.288 1.00 50.13  ? 346 LYS   B C   1 
ATOM   884  O O   . LYS   A 1 131 ? -30.224 -1.495  15.085 1.00 49.83  ? 346 LYS   B O   1 
ATOM   885  C CB  . LYS   A 1 131 ? -29.581 0.865   16.410 1.00 59.96  ? 346 LYS   B CB  1 
ATOM   886  C CG  . LYS   A 1 131 ? -29.295 2.014   17.367 1.00 76.08  ? 346 LYS   B CG  1 
ATOM   887  C CD  . LYS   A 1 131 ? -27.798 2.311   17.564 1.00 84.29  ? 346 LYS   B CD  1 
ATOM   888  C CE  . LYS   A 1 131 ? -27.058 2.529   16.247 1.00 92.10  ? 346 LYS   B CE  1 
ATOM   889  N NZ  . LYS   A 1 131 ? -26.107 3.678   16.301 1.00 101.19 ? 346 LYS   B NZ  1 
ATOM   890  N N   . VAL   A 1 132 ? -32.195 -0.638  14.515 1.00 48.91  ? 347 VAL   B N   1 
ATOM   891  C CA  . VAL   A 1 132 ? -32.319 -1.416  13.271 1.00 47.80  ? 347 VAL   B CA  1 
ATOM   892  C C   . VAL   A 1 132 ? -31.405 -0.833  12.171 1.00 47.83  ? 347 VAL   B C   1 
ATOM   893  O O   . VAL   A 1 132 ? -31.331 0.377   11.987 1.00 46.64  ? 347 VAL   B O   1 
ATOM   894  C CB  . VAL   A 1 132 ? -33.794 -1.474  12.791 1.00 47.71  ? 347 VAL   B CB  1 
ATOM   895  C CG1 . VAL   A 1 132 ? -33.937 -2.288  11.511 1.00 46.70  ? 347 VAL   B CG1 1 
ATOM   896  C CG2 . VAL   A 1 132 ? -34.679 -2.068  13.889 1.00 49.42  ? 347 VAL   B CG2 1 
ATOM   897  N N   . CYS   A 1 133 ? -30.704 -1.699  11.446 1.00 51.44  ? 348 CYS   B N   1 
ATOM   898  C CA  . CYS   A 1 133 ? -29.753 -1.275  10.413 1.00 54.24  ? 348 CYS   B CA  1 
ATOM   899  C C   . CYS   A 1 133 ? -29.933 -2.054  9.120  1.00 55.36  ? 348 CYS   B C   1 
ATOM   900  O O   . CYS   A 1 133 ? -30.169 -3.250  9.132  1.00 56.60  ? 348 CYS   B O   1 
ATOM   901  C CB  . CYS   A 1 133 ? -28.323 -1.436  10.908 1.00 54.96  ? 348 CYS   B CB  1 
ATOM   902  S SG  . CYS   A 1 133 ? -28.055 -0.676  12.517 1.00 60.48  ? 348 CYS   B SG  1 
ATOM   903  N N   . SER   A 1 134 ? -29.815 -1.358  8.000  1.00 58.37  ? 349 SER   B N   1 
ATOM   904  C CA  . SER   A 1 134 ? -29.892 -1.967  6.673  1.00 58.02  ? 349 SER   B CA  1 
ATOM   905  C C   . SER   A 1 134 ? -28.608 -1.612  5.925  1.00 55.73  ? 349 SER   B C   1 
ATOM   906  O O   . SER   A 1 134 ? -28.293 -0.438  5.778  1.00 60.14  ? 349 SER   B O   1 
ATOM   907  C CB  . SER   A 1 134 ? -31.124 -1.459  5.922  1.00 57.61  ? 349 SER   B CB  1 
ATOM   908  O OG  . SER   A 1 134 ? -31.179 -1.974  4.597  1.00 60.63  ? 349 SER   B OG  1 
ATOM   909  N N   . PHE   A 1 135 ? -27.872 -2.628  5.470  1.00 56.04  ? 350 PHE   B N   1 
ATOM   910  C CA  . PHE   A 1 135 ? -26.541 -2.461  4.863  1.00 66.68  ? 350 PHE   B CA  1 
ATOM   911  C C   . PHE   A 1 135 ? -25.624 -1.673  5.811  1.00 70.82  ? 350 PHE   B C   1 
ATOM   912  O O   . PHE   A 1 135 ? -24.984 -0.701  5.407  1.00 72.88  ? 350 PHE   B O   1 
ATOM   913  C CB  . PHE   A 1 135 ? -26.630 -1.796  3.464  1.00 65.98  ? 350 PHE   B CB  1 
ATOM   914  C CG  . PHE   A 1 135 ? -27.512 -2.540  2.481  1.00 66.84  ? 350 PHE   B CG  1 
ATOM   915  C CD1 . PHE   A 1 135 ? -28.882 -2.262  2.397  1.00 59.43  ? 350 PHE   B CD1 1 
ATOM   916  C CD2 . PHE   A 1 135 ? -26.970 -3.521  1.623  1.00 64.44  ? 350 PHE   B CD2 1 
ATOM   917  C CE1 . PHE   A 1 135 ? -29.698 -2.963  1.502  1.00 57.87  ? 350 PHE   B CE1 1 
ATOM   918  C CE2 . PHE   A 1 135 ? -27.783 -4.215  0.724  1.00 61.12  ? 350 PHE   B CE2 1 
ATOM   919  C CZ  . PHE   A 1 135 ? -29.149 -3.939  0.664  1.00 58.80  ? 350 PHE   B CZ  1 
ATOM   920  N N   . GLY   A 1 136 ? -25.607 -2.075  7.082  1.00 71.20  ? 351 GLY   B N   1 
ATOM   921  C CA  . GLY   A 1 136 ? -24.798 -1.409  8.102  1.00 73.18  ? 351 GLY   B CA  1 
ATOM   922  C C   . GLY   A 1 136 ? -25.149 0.021   8.491  1.00 74.70  ? 351 GLY   B C   1 
ATOM   923  O O   . GLY   A 1 136 ? -24.371 0.656   9.196  1.00 83.28  ? 351 GLY   B O   1 
ATOM   924  N N   . LYS   A 1 137 ? -26.309 0.528   8.070  1.00 73.34  ? 352 LYS   B N   1 
ATOM   925  C CA  . LYS   A 1 137 ? -26.670 1.928   8.297  1.00 75.08  ? 352 LYS   B CA  1 
ATOM   926  C C   . LYS   A 1 137 ? -28.022 1.995   9.001  1.00 75.16  ? 352 LYS   B C   1 
ATOM   927  O O   . LYS   A 1 137 ? -28.996 1.374   8.565  1.00 68.77  ? 352 LYS   B O   1 
ATOM   928  C CB  . LYS   A 1 137 ? -26.679 2.728   6.975  1.00 72.92  ? 352 LYS   B CB  1 
ATOM   929  C CG  . LYS   A 1 137 ? -27.195 4.171   7.081  1.00 91.06  ? 352 LYS   B CG  1 
ATOM   930  C CD  . LYS   A 1 137 ? -26.462 5.050   8.123  1.00 101.26 ? 352 LYS   B CD  1 
ATOM   931  C CE  . LYS   A 1 137 ? -27.383 5.958   8.956  1.00 99.51  ? 352 LYS   B CE  1 
ATOM   932  N NZ  . LYS   A 1 137 ? -27.948 7.112   8.199  1.00 98.46  ? 352 LYS   B NZ  1 
ATOM   933  N N   . GLN   A 1 138 ? -28.076 2.778   10.081 1.00 79.88  ? 353 GLN   B N   1 
ATOM   934  C CA  . GLN   A 1 138 ? -29.278 2.872   10.909 1.00 72.53  ? 353 GLN   B CA  1 
ATOM   935  C C   . GLN   A 1 138 ? -30.489 3.392   10.128 1.00 65.84  ? 353 GLN   B C   1 
ATOM   936  O O   . GLN   A 1 138 ? -30.401 4.369   9.397  1.00 72.71  ? 353 GLN   B O   1 
ATOM   937  C CB  . GLN   A 1 138 ? -29.036 3.760   12.130 1.00 72.49  ? 353 GLN   B CB  1 
ATOM   938  C CG  . GLN   A 1 138 ? -30.313 4.013   12.913 1.00 76.20  ? 353 GLN   B CG  1 
ATOM   939  C CD  . GLN   A 1 138 ? -30.100 4.872   14.125 1.00 72.43  ? 353 GLN   B CD  1 
ATOM   940  O OE1 . GLN   A 1 138 ? -29.097 4.738   14.814 1.00 71.01  ? 353 GLN   B OE1 1 
ATOM   941  N NE2 . GLN   A 1 138 ? -31.057 5.744   14.409 1.00 66.99  ? 353 GLN   B NE2 1 
ATOM   942  N N   . VAL   A 1 139 ? -31.623 2.738   10.330 1.00 60.93  ? 354 VAL   B N   1 
ATOM   943  C CA  . VAL   A 1 139 ? -32.882 3.098   9.695  1.00 57.06  ? 354 VAL   B CA  1 
ATOM   944  C C   . VAL   A 1 139 ? -33.892 3.535   10.749 1.00 57.19  ? 354 VAL   B C   1 
ATOM   945  O O   . VAL   A 1 139 ? -34.456 4.606   10.629 1.00 60.47  ? 354 VAL   B O   1 
ATOM   946  C CB  . VAL   A 1 139 ? -33.400 1.902   8.867  1.00 58.98  ? 354 VAL   B CB  1 
ATOM   947  C CG1 . VAL   A 1 139 ? -34.815 2.132   8.346  1.00 59.82  ? 354 VAL   B CG1 1 
ATOM   948  C CG2 . VAL   A 1 139 ? -32.429 1.637   7.729  1.00 57.50  ? 354 VAL   B CG2 1 
ATOM   949  N N   . VAL   A 1 140 ? -34.138 2.692   11.755 1.00 59.66  ? 355 VAL   B N   1 
ATOM   950  C CA  . VAL   A 1 140 ? -34.891 3.086   12.944 1.00 58.71  ? 355 VAL   B CA  1 
ATOM   951  C C   . VAL   A 1 140 ? -34.129 2.786   14.235 1.00 59.09  ? 355 VAL   B C   1 
ATOM   952  O O   . VAL   A 1 140 ? -33.169 2.018   14.261 1.00 55.44  ? 355 VAL   B O   1 
ATOM   953  C CB  . VAL   A 1 140 ? -36.296 2.467   12.985 1.00 62.69  ? 355 VAL   B CB  1 
ATOM   954  C CG1 . VAL   A 1 140 ? -37.100 2.896   11.770 1.00 62.09  ? 355 VAL   B CG1 1 
ATOM   955  C CG2 . VAL   A 1 140 ? -36.249 0.952   13.047 1.00 66.42  ? 355 VAL   B CG2 1 
ATOM   956  N N   . GLU   A 1 141 ? -34.563 3.450   15.298 1.00 55.35  ? 356 GLU   B N   1 
ATOM   957  C CA  . GLU   A 1 141 ? -33.939 3.341   16.611 1.00 56.12  ? 356 GLU   B CA  1 
ATOM   958  C C   . GLU   A 1 141 ? -34.997 3.576   17.664 1.00 53.67  ? 356 GLU   B C   1 
ATOM   959  O O   . GLU   A 1 141 ? -35.705 4.563   17.581 1.00 55.36  ? 356 GLU   B O   1 
ATOM   960  C CB  . GLU   A 1 141 ? -32.795 4.345   16.772 1.00 53.20  ? 356 GLU   B CB  1 
ATOM   961  C CG  . GLU   A 1 141 ? -32.222 4.342   18.175 1.00 59.46  ? 356 GLU   B CG  1 
ATOM   962  C CD  . GLU   A 1 141 ? -31.019 5.242   18.385 1.00 62.65  ? 356 GLU   B CD  1 
ATOM   963  O OE1 . GLU   A 1 141 ? -30.827 6.265   17.673 1.00 67.46  ? 356 GLU   B OE1 1 
ATOM   964  O OE2 . GLU   A 1 141 ? -30.282 4.921   19.336 1.00 70.87  ? 356 GLU   B OE2 1 
ATOM   965  N N   . LYS   A 1 142 ? -35.147 2.663   18.620 1.00 52.41  ? 357 LYS   B N   1 
ATOM   966  C CA  . LYS   A 1 142 ? -36.034 2.898   19.763 1.00 52.44  ? 357 LYS   B CA  1 
ATOM   967  C C   . LYS   A 1 142 ? -35.229 2.937   21.036 1.00 52.06  ? 357 LYS   B C   1 
ATOM   968  O O   . LYS   A 1 142 ? -34.358 2.117   21.238 1.00 52.35  ? 357 LYS   B O   1 
ATOM   969  C CB  . LYS   A 1 142 ? -37.149 1.876   19.886 1.00 58.34  ? 357 LYS   B CB  1 
ATOM   970  C CG  . LYS   A 1 142 ? -38.022 2.161   21.107 1.00 70.40  ? 357 LYS   B CG  1 
ATOM   971  C CD  . LYS   A 1 142 ? -39.481 1.756   20.941 1.00 81.25  ? 357 LYS   B CD  1 
ATOM   972  C CE  . LYS   A 1 142 ? -40.390 2.471   21.952 1.00 86.05  ? 357 LYS   B CE  1 
ATOM   973  N NZ  . LYS   A 1 142 ? -41.547 1.631   22.385 1.00 87.83  ? 357 LYS   B NZ  1 
ATOM   974  N N   . VAL   A 1 143 ? -35.516 3.914   21.890 1.00 53.21  ? 358 VAL   B N   1 
ATOM   975  C CA  . VAL   A 1 143 ? -34.798 4.067   23.137 1.00 54.31  ? 358 VAL   B CA  1 
ATOM   976  C C   . VAL   A 1 143 ? -35.834 4.161   24.244 1.00 57.75  ? 358 VAL   B C   1 
ATOM   977  O O   . VAL   A 1 143 ? -36.638 5.057   24.214 1.00 64.44  ? 358 VAL   B O   1 
ATOM   978  C CB  . VAL   A 1 143 ? -33.912 5.307   23.136 1.00 50.97  ? 358 VAL   B CB  1 
ATOM   979  C CG1 . VAL   A 1 143 ? -32.976 5.283   24.330 1.00 55.55  ? 358 VAL   B CG1 1 
ATOM   980  C CG2 . VAL   A 1 143 ? -33.126 5.406   21.840 1.00 52.55  ? 358 VAL   B CG2 1 
ATOM   981  N N   . GLU   A 1 144 ? -35.831 3.214   25.181 1.00 56.87  ? 359 GLU   B N   1 
ATOM   982  C CA  . GLU   A 1 144 ? -36.727 3.213   26.335 1.00 57.96  ? 359 GLU   B CA  1 
ATOM   983  C C   . GLU   A 1 144 ? -35.890 3.202   27.590 1.00 55.88  ? 359 GLU   B C   1 
ATOM   984  O O   . GLU   A 1 144 ? -34.725 2.818   27.553 1.00 57.57  ? 359 GLU   B O   1 
ATOM   985  C CB  . GLU   A 1 144 ? -37.642 1.976   26.305 1.00 65.98  ? 359 GLU   B CB  1 
ATOM   986  C CG  . GLU   A 1 144 ? -38.861 2.140   25.404 1.00 73.57  ? 359 GLU   B CG  1 
ATOM   987  C CD  . GLU   A 1 144 ? -39.725 0.885   25.268 1.00 81.80  ? 359 GLU   B CD  1 
ATOM   988  O OE1 . GLU   A 1 144 ? -40.969 1.011   25.288 1.00 84.74  ? 359 GLU   B OE1 1 
ATOM   989  O OE2 . GLU   A 1 144 ? -39.182 -0.227  25.104 1.00 87.65  ? 359 GLU   B OE2 1 
ATOM   990  N N   . THR   A 1 145 ? -36.466 3.646   28.706 1.00 53.87  ? 360 THR   B N   1 
ATOM   991  C CA  . THR   A 1 145 ? -35.785 3.507   29.983 1.00 51.72  ? 360 THR   B CA  1 
ATOM   992  C C   . THR   A 1 145 ? -36.662 2.676   30.892 1.00 50.87  ? 360 THR   B C   1 
ATOM   993  O O   . THR   A 1 145 ? -37.862 2.554   30.679 1.00 57.77  ? 360 THR   B O   1 
ATOM   994  C CB  . THR   A 1 145 ? -35.433 4.839   30.650 1.00 52.08  ? 360 THR   B CB  1 
ATOM   995  O OG1 . THR   A 1 145 ? -36.639 5.469   31.042 1.00 67.53  ? 360 THR   B OG1 1 
ATOM   996  C CG2 . THR   A 1 145 ? -34.687 5.756   29.720 1.00 53.56  ? 360 THR   B CG2 1 
ATOM   997  N N   . GLU   A 1 146 ? -36.032 2.040   31.862 1.00 52.43  ? 361 GLU   B N   1 
ATOM   998  C CA  . GLU   A 1 146 ? -36.727 1.209   32.833 1.00 53.72  ? 361 GLU   B CA  1 
ATOM   999  C C   . GLU   A 1 146 ? -36.013 1.286   34.183 1.00 58.63  ? 361 GLU   B C   1 
ATOM   1000 O O   . GLU   A 1 146 ? -34.828 0.920   34.309 1.00 55.08  ? 361 GLU   B O   1 
ATOM   1001 C CB  . GLU   A 1 146 ? -36.764 -0.229  32.349 1.00 56.68  ? 361 GLU   B CB  1 
ATOM   1002 C CG  . GLU   A 1 146 ? -37.511 -1.186  33.256 1.00 59.43  ? 361 GLU   B CG  1 
ATOM   1003 C CD  . GLU   A 1 146 ? -38.998 -0.911  33.349 1.00 61.42  ? 361 GLU   B CD  1 
ATOM   1004 O OE1 . GLU   A 1 146 ? -39.546 -0.237  32.447 1.00 64.90  ? 361 GLU   B OE1 1 
ATOM   1005 O OE2 . GLU   A 1 146 ? -39.618 -1.397  34.328 1.00 72.40  ? 361 GLU   B OE2 1 
ATOM   1006 N N   . ARG   A 1 147 ? -36.746 1.766   35.181 1.00 64.88  ? 362 ARG   B N   1 
ATOM   1007 C CA  . ARG   A 1 147 ? -36.313 1.724   36.569 1.00 74.45  ? 362 ARG   B CA  1 
ATOM   1008 C C   . ARG   A 1 147 ? -36.466 0.282   37.089 1.00 67.37  ? 362 ARG   B C   1 
ATOM   1009 O O   . ARG   A 1 147 ? -37.385 -0.431  36.692 1.00 64.66  ? 362 ARG   B O   1 
ATOM   1010 C CB  . ARG   A 1 147 ? -37.144 2.718   37.421 1.00 86.34  ? 362 ARG   B CB  1 
ATOM   1011 C CG  . ARG   A 1 147 ? -36.529 3.126   38.767 1.00 97.82  ? 362 ARG   B CG  1 
ATOM   1012 C CD  . ARG   A 1 147 ? -37.086 4.450   39.311 1.00 106.57 ? 362 ARG   B CD  1 
ATOM   1013 N NE  . ARG   A 1 147 ? -38.469 4.335   39.815 1.00 112.47 ? 362 ARG   B NE  1 
ATOM   1014 C CZ  . ARG   A 1 147 ? -39.573 4.891   39.288 1.00 114.69 ? 362 ARG   B CZ  1 
ATOM   1015 N NH1 . ARG   A 1 147 ? -39.540 5.661   38.196 1.00 112.07 ? 362 ARG   B NH1 1 
ATOM   1016 N NH2 . ARG   A 1 147 ? -40.752 4.678   39.878 1.00 119.53 ? 362 ARG   B NH2 1 
ATOM   1017 N N   . ALA   A 1 148 ? -35.564 -0.116  37.986 1.00 66.43  ? 363 ALA   B N   1 
ATOM   1018 C CA  . ALA   A 1 148 ? -35.613 -1.432  38.662 1.00 72.77  ? 363 ALA   B CA  1 
ATOM   1019 C C   . ALA   A 1 148 ? -36.849 -1.675  39.573 1.00 72.41  ? 363 ALA   B C   1 
ATOM   1020 O O   . ALA   A 1 148 ? -37.402 -0.735  40.147 1.00 74.53  ? 363 ALA   B O   1 
ATOM   1021 C CB  . ALA   A 1 148 ? -34.337 -1.618  39.481 1.00 71.61  ? 363 ALA   B CB  1 
ATOM   1022 N N   . GLN   A 1 149 ? -37.258 -2.936  39.711 1.00 68.94  ? 364 GLN   B N   1 
ATOM   1023 C CA  . GLN   A 1 149 ? -38.244 -3.351  40.711 1.00 71.38  ? 364 GLN   B CA  1 
ATOM   1024 C C   . GLN   A 1 149 ? -37.668 -4.503  41.493 1.00 73.05  ? 364 GLN   B C   1 
ATOM   1025 O O   . GLN   A 1 149 ? -37.450 -5.578  40.940 1.00 76.86  ? 364 GLN   B O   1 
ATOM   1026 C CB  . GLN   A 1 149 ? -39.553 -3.772  40.056 1.00 78.53  ? 364 GLN   B CB  1 
ATOM   1027 C CG  . GLN   A 1 149 ? -40.346 -2.590  39.511 1.00 87.99  ? 364 GLN   B CG  1 
ATOM   1028 C CD  . GLN   A 1 149 ? -41.172 -2.938  38.280 1.00 101.88 ? 364 GLN   B CD  1 
ATOM   1029 O OE1 . GLN   A 1 149 ? -42.379 -2.681  38.246 1.00 96.74  ? 364 GLN   B OE1 1 
ATOM   1030 N NE2 . GLN   A 1 149 ? -40.521 -3.518  37.251 1.00 111.63 ? 364 GLN   B NE2 1 
ATOM   1031 N N   . LEU   A 1 150 ? -37.401 -4.269  42.777 1.00 78.65  ? 365 LEU   B N   1 
ATOM   1032 C CA  . LEU   A 1 150 ? -36.775 -5.267  43.636 1.00 80.27  ? 365 LEU   B CA  1 
ATOM   1033 C C   . LEU   A 1 150 ? -37.765 -6.374  43.859 1.00 79.39  ? 365 LEU   B C   1 
ATOM   1034 O O   . LEU   A 1 150 ? -38.897 -6.117  44.256 1.00 72.83  ? 365 LEU   B O   1 
ATOM   1035 C CB  . LEU   A 1 150 ? -36.377 -4.664  44.986 1.00 85.63  ? 365 LEU   B CB  1 
ATOM   1036 C CG  . LEU   A 1 150 ? -35.800 -5.535  46.132 1.00 87.58  ? 365 LEU   B CG  1 
ATOM   1037 C CD1 . LEU   A 1 150 ? -34.699 -6.515  45.734 1.00 85.79  ? 365 LEU   B CD1 1 
ATOM   1038 C CD2 . LEU   A 1 150 ? -35.293 -4.623  47.249 1.00 85.74  ? 365 LEU   B CD2 1 
ATOM   1039 N N   . GLU   A 1 151 ? -37.336 -7.592  43.552 1.00 83.24  ? 366 GLU   B N   1 
ATOM   1040 C CA  . GLU   A 1 151 ? -38.095 -8.804  43.814 1.00 86.36  ? 366 GLU   B CA  1 
ATOM   1041 C C   . GLU   A 1 151 ? -37.192 -9.750  44.610 1.00 92.44  ? 366 GLU   B C   1 
ATOM   1042 O O   . GLU   A 1 151 ? -36.148 -9.315  45.075 1.00 102.45 ? 366 GLU   B O   1 
ATOM   1043 C CB  . GLU   A 1 151 ? -38.592 -9.378  42.494 1.00 89.37  ? 366 GLU   B CB  1 
ATOM   1044 C CG  . GLU   A 1 151 ? -39.406 -8.342  41.709 1.00 92.47  ? 366 GLU   B CG  1 
ATOM   1045 C CD  . GLU   A 1 151 ? -40.471 -8.944  40.802 1.00 90.22  ? 366 GLU   B CD  1 
ATOM   1046 O OE1 . GLU   A 1 151 ? -41.518 -8.275  40.593 1.00 85.26  ? 366 GLU   B OE1 1 
ATOM   1047 O OE2 . GLU   A 1 151 ? -40.252 -10.073 40.298 1.00 84.58  ? 366 GLU   B OE2 1 
ATOM   1048 N N   . ASP   A 1 152 ? -37.599 -11.008 44.799 1.00 102.33 ? 367 ASP   B N   1 
ATOM   1049 C CA  . ASP   A 1 152 ? -36.954 -11.961 45.750 1.00 100.48 ? 367 ASP   B CA  1 
ATOM   1050 C C   . ASP   A 1 152 ? -35.404 -12.020 45.715 1.00 97.89  ? 367 ASP   B C   1 
ATOM   1051 O O   . ASP   A 1 152 ? -34.833 -12.951 45.154 1.00 108.37 ? 367 ASP   B O   1 
ATOM   1052 C CB  . ASP   A 1 152 ? -37.532 -13.376 45.520 1.00 103.69 ? 367 ASP   B CB  1 
ATOM   1053 C CG  . ASP   A 1 152 ? -37.259 -14.330 46.681 1.00 112.28 ? 367 ASP   B CG  1 
ATOM   1054 O OD1 . ASP   A 1 152 ? -37.710 -14.051 47.818 1.00 113.58 ? 367 ASP   B OD1 1 
ATOM   1055 O OD2 . ASP   A 1 152 ? -36.610 -15.373 46.447 1.00 114.26 ? 367 ASP   B OD2 1 
ATOM   1056 N N   . GLY   A 1 153 ? -34.737 -11.045 46.343 1.00 91.95  ? 368 GLY   B N   1 
ATOM   1057 C CA  . GLY   A 1 153 ? -33.272 -10.864 46.222 1.00 96.26  ? 368 GLY   B CA  1 
ATOM   1058 C C   . GLY   A 1 153 ? -32.867 -9.911  45.087 1.00 99.25  ? 368 GLY   B C   1 
ATOM   1059 O O   . GLY   A 1 153 ? -32.446 -8.778  45.356 1.00 85.36  ? 368 GLY   B O   1 
ATOM   1060 N N   . ARG   A 1 154 ? -33.048 -10.368 43.833 1.00 94.57  ? 369 ARG   B N   1 
ATOM   1061 C CA  . ARG   A 1 154 ? -32.613 -9.662  42.609 1.00 87.91  ? 369 ARG   B CA  1 
ATOM   1062 C C   . ARG   A 1 154 ? -33.497 -8.466  42.314 1.00 83.22  ? 369 ARG   B C   1 
ATOM   1063 O O   . ARG   A 1 154 ? -34.641 -8.386  42.750 1.00 82.35  ? 369 ARG   B O   1 
ATOM   1064 C CB  . ARG   A 1 154 ? -32.657 -10.560 41.350 1.00 91.32  ? 369 ARG   B CB  1 
ATOM   1065 C CG  . ARG   A 1 154 ? -31.505 -11.530 41.172 1.00 101.65 ? 369 ARG   B CG  1 
ATOM   1066 C CD  . ARG   A 1 154 ? -31.519 -12.519 42.316 1.00 117.59 ? 369 ARG   B CD  1 
ATOM   1067 N NE  . ARG   A 1 154 ? -30.867 -13.806 42.064 1.00 128.90 ? 369 ARG   B NE  1 
ATOM   1068 C CZ  . ARG   A 1 154 ? -29.917 -14.370 42.824 1.00 132.97 ? 369 ARG   B CZ  1 
ATOM   1069 N NH1 . ARG   A 1 154 ? -29.454 -15.562 42.486 1.00 130.40 ? 369 ARG   B NH1 1 
ATOM   1070 N NH2 . ARG   A 1 154 ? -29.414 -13.779 43.913 1.00 133.94 ? 369 ARG   B NH2 1 
ATOM   1071 N N   . PHE   A 1 155 ? -32.945 -7.545  41.539 1.00 75.75  ? 370 PHE   B N   1 
ATOM   1072 C CA  . PHE   A 1 155 ? -33.734 -6.536  40.880 1.00 68.86  ? 370 PHE   B CA  1 
ATOM   1073 C C   . PHE   A 1 155 ? -34.194 -7.084  39.557 1.00 65.58  ? 370 PHE   B C   1 
ATOM   1074 O O   . PHE   A 1 155 ? -33.593 -8.018  39.021 1.00 66.70  ? 370 PHE   B O   1 
ATOM   1075 C CB  . PHE   A 1 155 ? -32.907 -5.300  40.673 1.00 71.82  ? 370 PHE   B CB  1 
ATOM   1076 C CG  . PHE   A 1 155 ? -32.608 -4.606  41.944 1.00 72.85  ? 370 PHE   B CG  1 
ATOM   1077 C CD1 . PHE   A 1 155 ? -33.587 -3.825  42.558 1.00 76.32  ? 370 PHE   B CD1 1 
ATOM   1078 C CD2 . PHE   A 1 155 ? -31.391 -4.780  42.567 1.00 68.57  ? 370 PHE   B CD2 1 
ATOM   1079 C CE1 . PHE   A 1 155 ? -33.328 -3.189  43.764 1.00 78.23  ? 370 PHE   B CE1 1 
ATOM   1080 C CE2 . PHE   A 1 155 ? -31.117 -4.147  43.767 1.00 73.11  ? 370 PHE   B CE2 1 
ATOM   1081 C CZ  . PHE   A 1 155 ? -32.091 -3.355  44.375 1.00 75.83  ? 370 PHE   B CZ  1 
ATOM   1082 N N   . VAL   A 1 156 ? -35.277 -6.520  39.046 1.00 55.69  ? 371 VAL   B N   1 
ATOM   1083 C CA  . VAL   A 1 156 ? -35.810 -6.967  37.770 1.00 62.55  ? 371 VAL   B CA  1 
ATOM   1084 C C   . VAL   A 1 156 ? -36.248 -5.786  36.910 1.00 56.16  ? 371 VAL   B C   1 
ATOM   1085 O O   . VAL   A 1 156 ? -36.737 -4.780  37.395 1.00 55.36  ? 371 VAL   B O   1 
ATOM   1086 C CB  . VAL   A 1 156 ? -36.957 -7.988  37.947 1.00 72.58  ? 371 VAL   B CB  1 
ATOM   1087 C CG1 . VAL   A 1 156 ? -38.258 -7.298  38.346 1.00 78.73  ? 371 VAL   B CG1 1 
ATOM   1088 C CG2 . VAL   A 1 156 ? -37.167 -8.803  36.671 1.00 72.42  ? 371 VAL   B CG2 1 
ATOM   1089 N N   . TYR   A 1 157 ? -36.049 -5.932  35.615 1.00 52.76  ? 372 TYR   B N   1 
ATOM   1090 C CA  . TYR   A 1 157 ? -36.297 -4.873  34.665 1.00 48.70  ? 372 TYR   B CA  1 
ATOM   1091 C C   . TYR   A 1 157 ? -37.207 -5.414  33.571 1.00 48.39  ? 372 TYR   B C   1 
ATOM   1092 O O   . TYR   A 1 157 ? -36.830 -6.331  32.856 1.00 52.08  ? 372 TYR   B O   1 
ATOM   1093 C CB  . TYR   A 1 157 ? -34.948 -4.464  34.113 1.00 47.92  ? 372 TYR   B CB  1 
ATOM   1094 C CG  . TYR   A 1 157 ? -33.969 -3.912  35.148 1.00 47.32  ? 372 TYR   B CG  1 
ATOM   1095 C CD1 . TYR   A 1 157 ? -33.928 -2.549  35.436 1.00 48.88  ? 372 TYR   B CD1 1 
ATOM   1096 C CD2 . TYR   A 1 157 ? -33.070 -4.744  35.818 1.00 46.40  ? 372 TYR   B CD2 1 
ATOM   1097 C CE1 . TYR   A 1 157 ? -33.017 -2.041  36.357 1.00 50.51  ? 372 TYR   B CE1 1 
ATOM   1098 C CE2 . TYR   A 1 157 ? -32.156 -4.239  36.737 1.00 45.37  ? 372 TYR   B CE2 1 
ATOM   1099 C CZ  . TYR   A 1 157 ? -32.134 -2.892  36.997 1.00 48.41  ? 372 TYR   B CZ  1 
ATOM   1100 O OH  . TYR   A 1 157 ? -31.258 -2.376  37.908 1.00 52.45  ? 372 TYR   B OH  1 
ATOM   1101 N N   . ARG   A 1 158 ? -38.419 -4.896  33.469 1.00 52.93  ? 373 ARG   B N   1 
ATOM   1102 C CA  . ARG   A 1 158 ? -39.422 -5.464  32.540 1.00 58.41  ? 373 ARG   B CA  1 
ATOM   1103 C C   . ARG   A 1 158 ? -39.724 -4.506  31.426 1.00 54.45  ? 373 ARG   B C   1 
ATOM   1104 O O   . ARG   A 1 158 ? -40.192 -3.410  31.697 1.00 60.78  ? 373 ARG   B O   1 
ATOM   1105 C CB  . ARG   A 1 158 ? -40.736 -5.789  33.276 1.00 64.34  ? 373 ARG   B CB  1 
ATOM   1106 C CG  . ARG   A 1 158 ? -40.694 -7.109  34.040 1.00 67.96  ? 373 ARG   B CG  1 
ATOM   1107 C CD  . ARG   A 1 158 ? -42.071 -7.582  34.494 1.00 72.61  ? 373 ARG   B CD  1 
ATOM   1108 N NE  . ARG   A 1 158 ? -41.905 -8.767  35.312 1.00 79.65  ? 373 ARG   B NE  1 
ATOM   1109 C CZ  . ARG   A 1 158 ? -41.508 -8.745  36.587 1.00 88.73  ? 373 ARG   B CZ  1 
ATOM   1110 N NH1 . ARG   A 1 158 ? -41.350 -9.890  37.241 1.00 91.59  ? 373 ARG   B NH1 1 
ATOM   1111 N NH2 . ARG   A 1 158 ? -41.274 -7.593  37.226 1.00 88.54  ? 373 ARG   B NH2 1 
ATOM   1112 N N   . LEU   A 1 159 ? -39.462 -4.904  30.178 1.00 52.18  ? 374 LEU   B N   1 
ATOM   1113 C CA  . LEU   A 1 159 ? -39.880 -4.104  29.009 1.00 50.19  ? 374 LEU   B CA  1 
ATOM   1114 C C   . LEU   A 1 159 ? -40.726 -5.002  28.135 1.00 49.55  ? 374 LEU   B C   1 
ATOM   1115 O O   . LEU   A 1 159 ? -40.278 -5.497  27.108 1.00 56.93  ? 374 LEU   B O   1 
ATOM   1116 C CB  . LEU   A 1 159 ? -38.687 -3.534  28.242 1.00 48.85  ? 374 LEU   B CB  1 
ATOM   1117 C CG  . LEU   A 1 159 ? -37.774 -2.547  28.984 1.00 51.17  ? 374 LEU   B CG  1 
ATOM   1118 C CD1 . LEU   A 1 159 ? -36.616 -3.254  29.689 1.00 54.19  ? 374 LEU   B CD1 1 
ATOM   1119 C CD2 . LEU   A 1 159 ? -37.207 -1.506  28.054 1.00 51.38  ? 374 LEU   B CD2 1 
ATOM   1120 N N   . LEU   A 1 160 ? -41.945 -5.237  28.581 1.00 46.76  ? 375 LEU   B N   1 
ATOM   1121 C CA  . LEU   A 1 160 ? -42.791 -6.254  27.984 1.00 51.50  ? 375 LEU   B CA  1 
ATOM   1122 C C   . LEU   A 1 160 ? -43.732 -5.635  26.998 1.00 48.73  ? 375 LEU   B C   1 
ATOM   1123 O O   . LEU   A 1 160 ? -44.176 -4.501  27.179 1.00 45.74  ? 375 LEU   B O   1 
ATOM   1124 C CB  . LEU   A 1 160 ? -43.589 -7.015  29.045 1.00 50.51  ? 375 LEU   B CB  1 
ATOM   1125 C CG  . LEU   A 1 160 ? -42.745 -7.529  30.202 1.00 52.00  ? 375 LEU   B CG  1 
ATOM   1126 C CD1 . LEU   A 1 160 ? -43.658 -8.176  31.227 1.00 53.05  ? 375 LEU   B CD1 1 
ATOM   1127 C CD2 . LEU   A 1 160 ? -41.680 -8.484  29.689 1.00 53.94  ? 375 LEU   B CD2 1 
ATOM   1128 N N   . ARG   A 1 161 ? -44.004 -6.391  25.937 1.00 50.05  ? 376 ARG   B N   1 
ATOM   1129 C CA  . ARG   A 1 161 ? -44.958 -6.000  24.911 1.00 50.04  ? 376 ARG   B CA  1 
ATOM   1130 C C   . ARG   A 1 161 ? -44.753 -4.616  24.324 1.00 47.33  ? 376 ARG   B C   1 
ATOM   1131 O O   . ARG   A 1 161 ? -45.729 -3.950  24.022 1.00 45.19  ? 376 ARG   B O   1 
ATOM   1132 C CB  . ARG   A 1 161 ? -46.379 -6.106  25.469 1.00 49.07  ? 376 ARG   B CB  1 
ATOM   1133 C CG  . ARG   A 1 161 ? -46.744 -7.477  26.013 1.00 49.60  ? 376 ARG   B CG  1 
ATOM   1134 C CD  . ARG   A 1 161 ? -48.148 -7.416  26.592 1.00 53.71  ? 376 ARG   B CD  1 
ATOM   1135 N NE  . ARG   A 1 161 ? -49.206 -7.172  25.593 1.00 51.66  ? 376 ARG   B NE  1 
ATOM   1136 C CZ  . ARG   A 1 161 ? -49.709 -8.096  24.771 1.00 51.96  ? 376 ARG   B CZ  1 
ATOM   1137 N NH1 . ARG   A 1 161 ? -49.243 -9.347  24.790 1.00 50.54  ? 376 ARG   B NH1 1 
ATOM   1138 N NH2 . ARG   A 1 161 ? -50.697 -7.777  23.924 1.00 51.81  ? 376 ARG   B NH2 1 
ATOM   1139 N N   . SER   A 1 162 ? -43.506 -4.170  24.163 1.00 51.26  ? 377 SER   B N   1 
ATOM   1140 C CA  . SER   A 1 162 ? -43.254 -2.922  23.408 1.00 54.69  ? 377 SER   B CA  1 
ATOM   1141 C C   . SER   A 1 162 ? -43.764 -3.144  21.993 1.00 50.89  ? 377 SER   B C   1 
ATOM   1142 O O   . SER   A 1 162 ? -43.463 -4.168  21.389 1.00 56.50  ? 377 SER   B O   1 
ATOM   1143 C CB  . SER   A 1 162 ? -41.770 -2.574  23.313 1.00 57.82  ? 377 SER   B CB  1 
ATOM   1144 O OG  . SER   A 1 162 ? -41.123 -2.659  24.555 1.00 64.60  ? 377 SER   B OG  1 
ATOM   1145 N N   . PRO   A 1 163 ? -44.565 -2.224  21.460 1.00 53.07  ? 378 PRO   B N   1 
ATOM   1146 C CA  . PRO   A 1 163 ? -44.970 -2.429  20.042 1.00 53.11  ? 378 PRO   B CA  1 
ATOM   1147 C C   . PRO   A 1 163 ? -43.782 -2.421  19.070 1.00 47.46  ? 378 PRO   B C   1 
ATOM   1148 O O   . PRO   A 1 163 ? -42.842 -1.664  19.248 1.00 45.61  ? 378 PRO   B O   1 
ATOM   1149 C CB  . PRO   A 1 163 ? -45.902 -1.245  19.787 1.00 52.87  ? 378 PRO   B CB  1 
ATOM   1150 C CG  . PRO   A 1 163 ? -46.503 -0.976  21.141 1.00 50.76  ? 378 PRO   B CG  1 
ATOM   1151 C CD  . PRO   A 1 163 ? -45.335 -1.135  22.086 1.00 51.28  ? 378 PRO   B CD  1 
ATOM   1152 N N   . MET   A 1 164 ? -43.799 -3.309  18.091 1.00 45.19  ? 379 MET   B N   1 
ATOM   1153 C CA  . MET   A 1 164 ? -42.730 -3.359  17.099 1.00 46.10  ? 379 MET   B CA  1 
ATOM   1154 C C   . MET   A 1 164 ? -42.787 -2.100  16.193 1.00 46.38  ? 379 MET   B C   1 
ATOM   1155 O O   . MET   A 1 164 ? -43.892 -1.694  15.776 1.00 47.08  ? 379 MET   B O   1 
ATOM   1156 C CB  . MET   A 1 164 ? -42.918 -4.638  16.289 1.00 47.52  ? 379 MET   B CB  1 
ATOM   1157 C CG  . MET   A 1 164 ? -41.720 -5.110  15.514 1.00 50.53  ? 379 MET   B CG  1 
ATOM   1158 S SD  . MET   A 1 164 ? -42.045 -6.715  14.753 1.00 49.95  ? 379 MET   B SD  1 
ATOM   1159 C CE  . MET   A 1 164 ? -41.511 -7.803  16.058 1.00 51.05  ? 379 MET   B CE  1 
ATOM   1160 N N   . CYS   A 1 165 ? -41.641 -1.468  15.904 1.00 45.67  ? 380 CYS   B N   1 
ATOM   1161 C CA  . CYS   A 1 165 ? -41.587 -0.391  14.867 1.00 52.79  ? 380 CYS   B CA  1 
ATOM   1162 C C   . CYS   A 1 165 ? -42.282 -0.819  13.582 1.00 53.22  ? 380 CYS   B C   1 
ATOM   1163 O O   . CYS   A 1 165 ? -41.995 -1.910  13.057 1.00 51.33  ? 380 CYS   B O   1 
ATOM   1164 C CB  . CYS   A 1 165 ? -40.162 -0.058  14.447 1.00 55.34  ? 380 CYS   B CB  1 
ATOM   1165 S SG  . CYS   A 1 165 ? -39.006 0.296   15.771 1.00 79.27  ? 380 CYS   B SG  1 
ATOM   1166 N N   . GLU   A 1 166 ? -43.147 0.039   13.050 1.00 52.21  ? 381 GLU   B N   1 
ATOM   1167 C CA  . GLU   A 1 166 ? -43.773 -0.216  11.756 1.00 59.16  ? 381 GLU   B CA  1 
ATOM   1168 C C   . GLU   A 1 166 ? -42.760 -0.563  10.646 1.00 52.61  ? 381 GLU   B C   1 
ATOM   1169 O O   . GLU   A 1 166 ? -43.105 -1.303  9.739  1.00 48.81  ? 381 GLU   B O   1 
ATOM   1170 C CB  . GLU   A 1 166 ? -44.682 0.938   11.340 1.00 68.45  ? 381 GLU   B CB  1 
ATOM   1171 C CG  . GLU   A 1 166 ? -45.947 1.017   12.188 1.00 81.29  ? 381 GLU   B CG  1 
ATOM   1172 C CD  . GLU   A 1 166 ? -47.015 1.970   11.636 1.00 101.69 ? 381 GLU   B CD  1 
ATOM   1173 O OE1 . GLU   A 1 166 ? -48.174 1.867   12.108 1.00 101.50 ? 381 GLU   B OE1 1 
ATOM   1174 O OE2 . GLU   A 1 166 ? -46.714 2.821   10.752 1.00 105.83 ? 381 GLU   B OE2 1 
ATOM   1175 N N   . TYR   A 1 167 ? -41.521 -0.072  10.753 1.00 49.38  ? 382 TYR   B N   1 
ATOM   1176 C CA  . TYR   A 1 167 ? -40.437 -0.510  9.867  1.00 55.23  ? 382 TYR   B CA  1 
ATOM   1177 C C   . TYR   A 1 167 ? -40.275 -2.028  9.860  1.00 52.96  ? 382 TYR   B C   1 
ATOM   1178 O O   . TYR   A 1 167 ? -40.357 -2.644  8.777  1.00 53.49  ? 382 TYR   B O   1 
ATOM   1179 C CB  . TYR   A 1 167 ? -39.070 0.139   10.178 1.00 55.65  ? 382 TYR   B CB  1 
ATOM   1180 C CG  . TYR   A 1 167 ? -38.045 -0.252  9.134  1.00 57.00  ? 382 TYR   B CG  1 
ATOM   1181 C CD1 . TYR   A 1 167 ? -38.048 0.342   7.872  1.00 58.71  ? 382 TYR   B CD1 1 
ATOM   1182 C CD2 . TYR   A 1 167 ? -37.133 -1.289  9.365  1.00 55.86  ? 382 TYR   B CD2 1 
ATOM   1183 C CE1 . TYR   A 1 167 ? -37.136 -0.047  6.886  1.00 58.26  ? 382 TYR   B CE1 1 
ATOM   1184 C CE2 . TYR   A 1 167 ? -36.219 -1.684  8.388  1.00 51.27  ? 382 TYR   B CE2 1 
ATOM   1185 C CZ  . TYR   A 1 167 ? -36.217 -1.051  7.159  1.00 55.99  ? 382 TYR   B CZ  1 
ATOM   1186 O OH  . TYR   A 1 167 ? -35.324 -1.422  6.186  1.00 58.47  ? 382 TYR   B OH  1 
ATOM   1187 N N   . LEU   A 1 168 ? -40.046 -2.617  11.038 1.00 46.37  ? 383 LEU   B N   1 
ATOM   1188 C CA  . LEU   A 1 168 ? -39.908 -4.061  11.133 1.00 48.08  ? 383 LEU   B CA  1 
ATOM   1189 C C   . LEU   A 1 168 ? -41.176 -4.750  10.694 1.00 43.53  ? 383 LEU   B C   1 
ATOM   1190 O O   . LEU   A 1 168 ? -41.136 -5.712  9.941  1.00 42.16  ? 383 LEU   B O   1 
ATOM   1191 C CB  . LEU   A 1 168 ? -39.572 -4.537  12.539 1.00 56.79  ? 383 LEU   B CB  1 
ATOM   1192 C CG  . LEU   A 1 168 ? -38.186 -4.309  13.148 1.00 66.42  ? 383 LEU   B CG  1 
ATOM   1193 C CD1 . LEU   A 1 168 ? -37.910 -5.420  14.147 1.00 66.69  ? 383 LEU   B CD1 1 
ATOM   1194 C CD2 . LEU   A 1 168 ? -37.072 -4.270  12.119 1.00 74.82  ? 383 LEU   B CD2 1 
ATOM   1195 N N   . VAL   A 1 169 ? -42.319 -4.268  11.141 1.00 43.08  ? 384 VAL   B N   1 
ATOM   1196 C CA  . VAL   A 1 169 ? -43.562 -4.952  10.774 1.00 43.92  ? 384 VAL   B CA  1 
ATOM   1197 C C   . VAL   A 1 169 ? -43.686 -5.040  9.243  1.00 43.30  ? 384 VAL   B C   1 
ATOM   1198 O O   . VAL   A 1 169 ? -43.961 -6.102  8.708  1.00 38.74  ? 384 VAL   B O   1 
ATOM   1199 C CB  . VAL   A 1 169 ? -44.792 -4.295  11.387 1.00 42.82  ? 384 VAL   B CB  1 
ATOM   1200 C CG1 . VAL   A 1 169 ? -46.044 -4.999  10.924 1.00 42.77  ? 384 VAL   B CG1 1 
ATOM   1201 C CG2 . VAL   A 1 169 ? -44.704 -4.361  12.906 1.00 46.74  ? 384 VAL   B CG2 1 
ATOM   1202 N N   . ASN   A 1 170 ? -43.439 -3.929  8.559  1.00 45.94  ? 385 ASN   B N   1 
ATOM   1203 C CA  . ASN   A 1 170 ? -43.457 -3.920  7.105  1.00 50.04  ? 385 ASN   B CA  1 
ATOM   1204 C C   . ASN   A 1 170 ? -42.353 -4.772  6.468  1.00 50.56  ? 385 ASN   B C   1 
ATOM   1205 O O   . ASN   A 1 170 ? -42.613 -5.488  5.490  1.00 49.63  ? 385 ASN   B O   1 
ATOM   1206 C CB  . ASN   A 1 170 ? -43.483 -2.485  6.583  1.00 53.73  ? 385 ASN   B CB  1 
ATOM   1207 C CG  . ASN   A 1 170 ? -44.810 -1.808  6.889  1.00 58.23  ? 385 ASN   B CG  1 
ATOM   1208 O OD1 . ASN   A 1 170 ? -45.842 -2.482  6.983  1.00 63.71  ? 385 ASN   B OD1 1 
ATOM   1209 N ND2 . ASN   A 1 170 ? -44.796 -0.488  7.066  1.00 57.78  ? 385 ASN   B ND2 1 
ATOM   1210 N N   . PHE   A 1 171 ? -41.154 -4.733  7.050  1.00 45.60  ? 386 PHE   B N   1 
ATOM   1211 C CA  . PHE   A 1 171 ? -40.094 -5.616  6.627  1.00 45.80  ? 386 PHE   B CA  1 
ATOM   1212 C C   . PHE   A 1 171 ? -40.562 -7.071  6.670  1.00 47.79  ? 386 PHE   B C   1 
ATOM   1213 O O   . PHE   A 1 171 ? -40.439 -7.804  5.682  1.00 48.26  ? 386 PHE   B O   1 
ATOM   1214 C CB  . PHE   A 1 171 ? -38.853 -5.403  7.494  1.00 51.74  ? 386 PHE   B CB  1 
ATOM   1215 C CG  . PHE   A 1 171 ? -37.640 -6.152  7.015  1.00 54.79  ? 386 PHE   B CG  1 
ATOM   1216 C CD1 . PHE   A 1 171 ? -37.056 -5.840  5.790  1.00 53.14  ? 386 PHE   B CD1 1 
ATOM   1217 C CD2 . PHE   A 1 171 ? -37.071 -7.161  7.790  1.00 52.15  ? 386 PHE   B CD2 1 
ATOM   1218 C CE1 . PHE   A 1 171 ? -35.943 -6.541  5.332  1.00 50.64  ? 386 PHE   B CE1 1 
ATOM   1219 C CE2 . PHE   A 1 171 ? -35.942 -7.843  7.346  1.00 52.62  ? 386 PHE   B CE2 1 
ATOM   1220 C CZ  . PHE   A 1 171 ? -35.375 -7.533  6.112  1.00 50.27  ? 386 PHE   B CZ  1 
ATOM   1221 N N   . LEU   A 1 172 ? -41.140 -7.479  7.801  1.00 48.73  ? 387 LEU   B N   1 
ATOM   1222 C CA  . LEU   A 1 172 ? -41.556 -8.872  7.984  1.00 47.10  ? 387 LEU   B CA  1 
ATOM   1223 C C   . LEU   A 1 172 ? -42.547 -9.287  6.932  1.00 45.72  ? 387 LEU   B C   1 
ATOM   1224 O O   . LEU   A 1 172 ? -42.352 -10.303 6.326  1.00 45.34  ? 387 LEU   B O   1 
ATOM   1225 C CB  . LEU   A 1 172 ? -42.111 -9.148  9.397  1.00 47.85  ? 387 LEU   B CB  1 
ATOM   1226 C CG  . LEU   A 1 172 ? -41.051 -9.014  10.515 1.00 50.21  ? 387 LEU   B CG  1 
ATOM   1227 C CD1 . LEU   A 1 172 ? -41.680 -8.815  11.897 1.00 47.74  ? 387 LEU   B CD1 1 
ATOM   1228 C CD2 . LEU   A 1 172 ? -40.097 -10.195 10.519 1.00 51.17  ? 387 LEU   B CD2 1 
ATOM   1229 N N   . HIS   A 1 173 ? -43.587 -8.501  6.701  1.00 49.68  ? 388 HIS   B N   1 
ATOM   1230 C CA  . HIS   A 1 173 ? -44.587 -8.835  5.683  1.00 58.08  ? 388 HIS   B CA  1 
ATOM   1231 C C   . HIS   A 1 173 ? -43.996 -8.988  4.285  1.00 58.79  ? 388 HIS   B C   1 
ATOM   1232 O O   . HIS   A 1 173 ? -44.410 -9.865  3.507  1.00 57.86  ? 388 HIS   B O   1 
ATOM   1233 C CB  . HIS   A 1 173 ? -45.705 -7.787  5.654  1.00 65.06  ? 388 HIS   B CB  1 
ATOM   1234 C CG  . HIS   A 1 173 ? -46.670 -7.929  6.782  1.00 82.38  ? 388 HIS   B CG  1 
ATOM   1235 N ND1 . HIS   A 1 173 ? -47.511 -9.015  6.901  1.00 94.77  ? 388 HIS   B ND1 1 
ATOM   1236 C CD2 . HIS   A 1 173 ? -46.914 -7.143  7.858  1.00 91.04  ? 388 HIS   B CD2 1 
ATOM   1237 C CE1 . HIS   A 1 173 ? -48.243 -8.884  7.992  1.00 96.44  ? 388 HIS   B CE1 1 
ATOM   1238 N NE2 . HIS   A 1 173 ? -47.901 -7.756  8.590  1.00 92.05  ? 388 HIS   B NE2 1 
ATOM   1239 N N   . LYS   A 1 174 ? -43.045 -8.117  3.978  1.00 58.74  ? 389 LYS   B N   1 
ATOM   1240 C CA  . LYS   A 1 174 ? -42.331 -8.182  2.700  1.00 66.26  ? 389 LYS   B CA  1 
ATOM   1241 C C   . LYS   A 1 174 ? -41.457 -9.424  2.603  1.00 61.46  ? 389 LYS   B C   1 
ATOM   1242 O O   . LYS   A 1 174 ? -41.512 -10.141 1.618  1.00 63.28  ? 389 LYS   B O   1 
ATOM   1243 C CB  . LYS   A 1 174 ? -41.480 -6.935  2.494  1.00 61.71  ? 389 LYS   B CB  1 
ATOM   1244 C CG  . LYS   A 1 174 ? -42.310 -5.694  2.201  1.00 59.27  ? 389 LYS   B CG  1 
ATOM   1245 C CD  . LYS   A 1 174 ? -41.491 -4.455  2.476  1.00 57.77  ? 389 LYS   B CD  1 
ATOM   1246 C CE  . LYS   A 1 174 ? -42.212 -3.188  2.084  1.00 56.67  ? 389 LYS   B CE  1 
ATOM   1247 N NZ  . LYS   A 1 174 ? -41.297 -2.049  2.398  1.00 57.89  ? 389 LYS   B NZ  1 
ATOM   1248 N N   . LEU   A 1 175 ? -40.679 -9.669  3.649  1.00 59.80  ? 390 LEU   B N   1 
ATOM   1249 C CA  . LEU   A 1 175 ? -39.793 -10.832 3.720  1.00 55.50  ? 390 LEU   B CA  1 
ATOM   1250 C C   . LEU   A 1 175 ? -40.589 -12.137 3.572  1.00 55.45  ? 390 LEU   B C   1 
ATOM   1251 O O   . LEU   A 1 175 ? -40.278 -12.977 2.747  1.00 62.40  ? 390 LEU   B O   1 
ATOM   1252 C CB  . LEU   A 1 175 ? -39.036 -10.783 5.039  1.00 51.40  ? 390 LEU   B CB  1 
ATOM   1253 C CG  . LEU   A 1 175 ? -37.656 -11.355 5.079  1.00 54.02  ? 390 LEU   B CG  1 
ATOM   1254 C CD1 . LEU   A 1 175 ? -36.737 -10.590 4.140  1.00 52.95  ? 390 LEU   B CD1 1 
ATOM   1255 C CD2 . LEU   A 1 175 ? -37.151 -11.269 6.515  1.00 54.18  ? 390 LEU   B CD2 1 
ATOM   1256 N N   . ARG   A 1 176 ? -41.641 -12.273 4.361  1.00 61.08  ? 391 ARG   B N   1 
ATOM   1257 C CA  . ARG   A 1 176 ? -42.613 -13.398 4.295  1.00 65.73  ? 391 ARG   B CA  1 
ATOM   1258 C C   . ARG   A 1 176 ? -43.059 -13.781 2.863  1.00 65.48  ? 391 ARG   B C   1 
ATOM   1259 O O   . ARG   A 1 176 ? -43.208 -14.956 2.542  1.00 63.77  ? 391 ARG   B O   1 
ATOM   1260 C CB  . ARG   A 1 176 ? -43.815 -13.059 5.221  1.00 70.60  ? 391 ARG   B CB  1 
ATOM   1261 C CG  . ARG   A 1 176 ? -45.187 -13.665 4.934  1.00 80.72  ? 391 ARG   B CG  1 
ATOM   1262 C CD  . ARG   A 1 176 ? -46.091 -13.569 6.175  1.00 82.15  ? 391 ARG   B CD  1 
ATOM   1263 N NE  . ARG   A 1 176 ? -47.197 -14.527 6.184  1.00 94.67  ? 391 ARG   B NE  1 
ATOM   1264 C CZ  . ARG   A 1 176 ? -47.084 -15.860 6.290  1.00 100.36 ? 391 ARG   B CZ  1 
ATOM   1265 N NH1 . ARG   A 1 176 ? -45.902 -16.468 6.382  1.00 92.01  ? 391 ARG   B NH1 1 
ATOM   1266 N NH2 . ARG   A 1 176 ? -48.183 -16.611 6.280  1.00 110.99 ? 391 ARG   B NH2 1 
ATOM   1267 N N   . GLN   A 1 177 ? -43.233 -12.791 2.003  1.00 66.19  ? 392 GLN   B N   1 
ATOM   1268 C CA  . GLN   A 1 177 ? -43.755 -13.021 0.664  1.00 70.02  ? 392 GLN   B CA  1 
ATOM   1269 C C   . GLN   A 1 177 ? -42.745 -13.476 -0.407 1.00 67.63  ? 392 GLN   B C   1 
ATOM   1270 O O   . GLN   A 1 177 ? -43.174 -13.891 -1.480 1.00 69.83  ? 392 GLN   B O   1 
ATOM   1271 C CB  . GLN   A 1 177 ? -44.448 -11.758 0.195  1.00 80.56  ? 392 GLN   B CB  1 
ATOM   1272 C CG  . GLN   A 1 177 ? -45.712 -11.478 0.984  1.00 91.95  ? 392 GLN   B CG  1 
ATOM   1273 C CD  . GLN   A 1 177 ? -46.293 -10.121 0.660  1.00 102.11 ? 392 GLN   B CD  1 
ATOM   1274 O OE1 . GLN   A 1 177 ? -45.561 -9.167  0.367  1.00 102.10 ? 392 GLN   B OE1 1 
ATOM   1275 N NE2 . GLN   A 1 177 ? -47.619 -10.026 0.698  1.00 105.89 ? 392 GLN   B NE2 1 
ATOM   1276 N N   . LEU   A 1 178 ? -41.437 -13.396 -0.124 1.00 59.26  ? 393 LEU   B N   1 
ATOM   1277 C CA  . LEU   A 1 178 ? -40.405 -13.790 -1.063 1.00 51.91  ? 393 LEU   B CA  1 
ATOM   1278 C C   . LEU   A 1 178 ? -40.513 -15.266 -1.336 1.00 61.79  ? 393 LEU   B C   1 
ATOM   1279 O O   . LEU   A 1 178 ? -40.772 -16.047 -0.403 1.00 66.50  ? 393 LEU   B O   1 
ATOM   1280 C CB  . LEU   A 1 178 ? -39.013 -13.528 -0.526 1.00 51.21  ? 393 LEU   B CB  1 
ATOM   1281 C CG  . LEU   A 1 178 ? -38.651 -12.103 -0.091 1.00 53.60  ? 393 LEU   B CG  1 
ATOM   1282 C CD1 . LEU   A 1 178 ? -37.144 -11.960 0.049  1.00 52.83  ? 393 LEU   B CD1 1 
ATOM   1283 C CD2 . LEU   A 1 178 ? -39.186 -11.063 -1.059 1.00 54.39  ? 393 LEU   B CD2 1 
ATOM   1284 N N   . PRO   A 1 179 ? -40.284 -15.673 -2.602 1.00 64.20  ? 394 PRO   B N   1 
ATOM   1285 C CA  . PRO   A 1 179 ? -40.610 -17.047 -2.992 1.00 63.20  ? 394 PRO   B CA  1 
ATOM   1286 C C   . PRO   A 1 179 ? -39.560 -18.095 -2.654 1.00 56.23  ? 394 PRO   B C   1 
ATOM   1287 O O   . PRO   A 1 179 ? -39.827 -19.261 -2.857 1.00 61.57  ? 394 PRO   B O   1 
ATOM   1288 C CB  . PRO   A 1 179 ? -40.797 -16.946 -4.514 1.00 68.92  ? 394 PRO   B CB  1 
ATOM   1289 C CG  . PRO   A 1 179 ? -40.184 -15.633 -4.922 1.00 67.26  ? 394 PRO   B CG  1 
ATOM   1290 C CD  . PRO   A 1 179 ? -39.597 -14.982 -3.702 1.00 68.49  ? 394 PRO   B CD  1 
ATOM   1291 N N   . GLU   A 1 180 ? -38.416 -17.712 -2.097 1.00 55.86  ? 395 GLU   B N   1 
ATOM   1292 C CA  . GLU   A 1 180 ? -37.338 -18.655 -1.880 1.00 56.63  ? 395 GLU   B CA  1 
ATOM   1293 C C   . GLU   A 1 180 ? -36.608 -18.313 -0.611 1.00 56.92  ? 395 GLU   B C   1 
ATOM   1294 O O   . GLU   A 1 180 ? -36.151 -17.189 -0.438 1.00 54.20  ? 395 GLU   B O   1 
ATOM   1295 C CB  . GLU   A 1 180 ? -36.324 -18.537 -3.019 1.00 64.78  ? 395 GLU   B CB  1 
ATOM   1296 C CG  . GLU   A 1 180 ? -36.808 -18.963 -4.395 1.00 67.66  ? 395 GLU   B CG  1 
ATOM   1297 C CD  . GLU   A 1 180 ? -36.919 -20.467 -4.551 1.00 75.07  ? 395 GLU   B CD  1 
ATOM   1298 O OE1 . GLU   A 1 180 ? -36.175 -21.208 -3.867 1.00 74.05  ? 395 GLU   B OE1 1 
ATOM   1299 O OE2 . GLU   A 1 180 ? -37.746 -20.908 -5.386 1.00 83.07  ? 395 GLU   B OE2 1 
ATOM   1300 N N   . ARG   A 1 181 ? -36.426 -19.298 0.247  1.00 58.54  ? 396 ARG   B N   1 
ATOM   1301 C CA  . ARG   A 1 181 ? -35.595 -19.112 1.418  1.00 61.69  ? 396 ARG   B CA  1 
ATOM   1302 C C   . ARG   A 1 181 ? -34.237 -18.495 1.116  1.00 52.80  ? 396 ARG   B C   1 
ATOM   1303 O O   . ARG   A 1 181 ? -33.716 -17.698 1.895  1.00 60.10  ? 396 ARG   B O   1 
ATOM   1304 C CB  . ARG   A 1 181 ? -35.384 -20.439 2.166  1.00 67.92  ? 396 ARG   B CB  1 
ATOM   1305 C CG  . ARG   A 1 181 ? -36.521 -20.806 3.117  1.00 76.97  ? 396 ARG   B CG  1 
ATOM   1306 C CD  . ARG   A 1 181 ? -36.188 -21.996 4.019  1.00 83.71  ? 396 ARG   B CD  1 
ATOM   1307 N NE  . ARG   A 1 181 ? -34.878 -21.852 4.673  1.00 93.73  ? 396 ARG   B NE  1 
ATOM   1308 C CZ  . ARG   A 1 181 ? -33.732 -22.447 4.309  1.00 107.44 ? 396 ARG   B CZ  1 
ATOM   1309 N NH1 . ARG   A 1 181 ? -33.663 -23.291 3.266  1.00 111.12 ? 396 ARG   B NH1 1 
ATOM   1310 N NH2 . ARG   A 1 181 ? -32.621 -22.193 5.011  1.00 106.27 ? 396 ARG   B NH2 1 
ATOM   1311 N N   . TYR   A 1 182 ? -33.628 -18.857 0.013  1.00 51.19  ? 397 TYR   B N   1 
ATOM   1312 C CA  . TYR   A 1 182 ? -32.294 -18.326 -0.222 1.00 52.14  ? 397 TYR   B CA  1 
ATOM   1313 C C   . TYR   A 1 182 ? -32.385 -16.816 -0.472 1.00 47.63  ? 397 TYR   B C   1 
ATOM   1314 O O   . TYR   A 1 182 ? -31.475 -16.074 -0.087 1.00 47.07  ? 397 TYR   B O   1 
ATOM   1315 C CB  . TYR   A 1 182 ? -31.559 -19.107 -1.329 1.00 53.09  ? 397 TYR   B CB  1 
ATOM   1316 C CG  . TYR   A 1 182 ? -31.929 -18.736 -2.731 1.00 54.95  ? 397 TYR   B CG  1 
ATOM   1317 C CD1 . TYR   A 1 182 ? -32.961 -19.392 -3.412 1.00 59.74  ? 397 TYR   B CD1 1 
ATOM   1318 C CD2 . TYR   A 1 182 ? -31.209 -17.755 -3.400 1.00 57.48  ? 397 TYR   B CD2 1 
ATOM   1319 C CE1 . TYR   A 1 182 ? -33.273 -19.060 -4.730 1.00 60.84  ? 397 TYR   B CE1 1 
ATOM   1320 C CE2 . TYR   A 1 182 ? -31.515 -17.396 -4.697 1.00 58.86  ? 397 TYR   B CE2 1 
ATOM   1321 C CZ  . TYR   A 1 182 ? -32.544 -18.035 -5.363 1.00 64.14  ? 397 TYR   B CZ  1 
ATOM   1322 O OH  . TYR   A 1 182 ? -32.792 -17.622 -6.659 1.00 66.84  ? 397 TYR   B OH  1 
ATOM   1323 N N   . MET   A 1 183 ? -33.486 -16.354 -1.069 1.00 47.27  ? 398 MET   B N   1 
ATOM   1324 C CA  . MET   A 1 183 ? -33.703 -14.893 -1.241 1.00 52.24  ? 398 MET   B CA  1 
ATOM   1325 C C   . MET   A 1 183 ? -33.919 -14.175 0.113  1.00 50.04  ? 398 MET   B C   1 
ATOM   1326 O O   . MET   A 1 183 ? -33.293 -13.141 0.415  1.00 43.04  ? 398 MET   B O   1 
ATOM   1327 C CB  . MET   A 1 183 ? -34.882 -14.614 -2.183 1.00 55.67  ? 398 MET   B CB  1 
ATOM   1328 C CG  . MET   A 1 183 ? -34.628 -15.004 -3.640 1.00 56.43  ? 398 MET   B CG  1 
ATOM   1329 S SD  . MET   A 1 183 ? -36.053 -14.683 -4.736 1.00 59.56  ? 398 MET   B SD  1 
ATOM   1330 C CE  . MET   A 1 183 ? -35.246 -14.853 -6.313 1.00 58.92  ? 398 MET   B CE  1 
ATOM   1331 N N   . MET   A 1 184 ? -34.766 -14.760 0.951  1.00 46.33  ? 399 MET   B N   1 
ATOM   1332 C CA  . MET   A 1 184 ? -34.891 -14.296 2.322  1.00 45.56  ? 399 MET   B CA  1 
ATOM   1333 C C   . MET   A 1 184 ? -33.551 -14.186 2.985  1.00 45.70  ? 399 MET   B C   1 
ATOM   1334 O O   . MET   A 1 184 ? -33.248 -13.159 3.583  1.00 53.84  ? 399 MET   B O   1 
ATOM   1335 C CB  . MET   A 1 184 ? -35.748 -15.240 3.115  1.00 49.43  ? 399 MET   B CB  1 
ATOM   1336 C CG  . MET   A 1 184 ? -37.189 -15.134 2.703  1.00 49.01  ? 399 MET   B CG  1 
ATOM   1337 S SD  . MET   A 1 184 ? -38.076 -16.467 3.464  1.00 51.35  ? 399 MET   B SD  1 
ATOM   1338 C CE  . MET   A 1 184 ? -39.709 -16.182 2.753  1.00 49.12  ? 399 MET   B CE  1 
ATOM   1339 N N   . ASN   A 1 185 ? -32.715 -15.205 2.861  1.00 43.25  ? 400 ASN   B N   1 
ATOM   1340 C CA  . ASN   A 1 185 ? -31.371 -15.097 3.473  1.00 45.77  ? 400 ASN   B CA  1 
ATOM   1341 C C   . ASN   A 1 185 ? -30.412 -14.120 2.840  1.00 48.33  ? 400 ASN   B C   1 
ATOM   1342 O O   . ASN   A 1 185 ? -29.513 -13.630 3.540  1.00 51.37  ? 400 ASN   B O   1 
ATOM   1343 C CB  . ASN   A 1 185 ? -30.705 -16.458 3.553  1.00 43.61  ? 400 ASN   B CB  1 
ATOM   1344 C CG  . ASN   A 1 185 ? -31.381 -17.353 4.560  1.00 47.91  ? 400 ASN   B CG  1 
ATOM   1345 O OD1 . ASN   A 1 185 ? -31.930 -16.876 5.577  1.00 42.19  ? 400 ASN   B OD1 1 
ATOM   1346 N ND2 . ASN   A 1 185 ? -31.367 -18.653 4.292  1.00 47.10  ? 400 ASN   B ND2 1 
ATOM   1347 N N   . SER   A 1 186 ? -30.577 -13.848 1.535  1.00 45.65  ? 401 SER   B N   1 
ATOM   1348 C CA  . SER   A 1 186 ? -29.744 -12.844 0.880  1.00 45.57  ? 401 SER   B CA  1 
ATOM   1349 C C   . SER   A 1 186 ? -30.130 -11.490 1.442  1.00 47.33  ? 401 SER   B C   1 
ATOM   1350 O O   . SER   A 1 186 ? -29.256 -10.721 1.866  1.00 44.68  ? 401 SER   B O   1 
ATOM   1351 C CB  . SER   A 1 186 ? -29.932 -12.821 -0.638 1.00 47.47  ? 401 SER   B CB  1 
ATOM   1352 O OG  . SER   A 1 186 ? -29.611 -14.065 -1.223 1.00 59.11  ? 401 SER   B OG  1 
ATOM   1353 N N   . VAL   A 1 187 ? -31.440 -11.227 1.474  1.00 43.03  ? 402 VAL   B N   1 
ATOM   1354 C CA  . VAL   A 1 187 ? -31.964 -9.987  2.027  1.00 43.01  ? 402 VAL   B CA  1 
ATOM   1355 C C   . VAL   A 1 187 ? -31.565 -9.820  3.480  1.00 43.68  ? 402 VAL   B C   1 
ATOM   1356 O O   . VAL   A 1 187 ? -31.113 -8.722  3.868  1.00 40.67  ? 402 VAL   B O   1 
ATOM   1357 C CB  . VAL   A 1 187 ? -33.493 -9.893  1.955  1.00 41.21  ? 402 VAL   B CB  1 
ATOM   1358 C CG1 . VAL   A 1 187 ? -33.988 -8.697  2.765  1.00 42.64  ? 402 VAL   B CG1 1 
ATOM   1359 C CG2 . VAL   A 1 187 ? -33.936 -9.753  0.511  1.00 40.79  ? 402 VAL   B CG2 1 
ATOM   1360 N N   . LEU   A 1 188 ? -31.704 -10.882 4.277  1.00 41.70  ? 403 LEU   B N   1 
ATOM   1361 C CA  . LEU   A 1 188 ? -31.312 -10.783 5.703  1.00 44.49  ? 403 LEU   B CA  1 
ATOM   1362 C C   . LEU   A 1 188 ? -29.823 -10.633 5.907  1.00 48.00  ? 403 LEU   B C   1 
ATOM   1363 O O   . LEU   A 1 188 ? -29.394 -10.228 6.978  1.00 43.70  ? 403 LEU   B O   1 
ATOM   1364 C CB  . LEU   A 1 188 ? -31.751 -11.996 6.498  1.00 44.15  ? 403 LEU   B CB  1 
ATOM   1365 C CG  . LEU   A 1 188 ? -33.247 -12.121 6.670  1.00 45.06  ? 403 LEU   B CG  1 
ATOM   1366 C CD1 . LEU   A 1 188 ? -33.531 -13.531 7.168  1.00 45.77  ? 403 LEU   B CD1 1 
ATOM   1367 C CD2 . LEU   A 1 188 ? -33.741 -11.029 7.616  1.00 46.42  ? 403 LEU   B CD2 1 
ATOM   1368 N N   . GLU   A 1 189 ? -29.019 -10.973 4.908  1.00 53.39  ? 404 GLU   B N   1 
ATOM   1369 C CA  . GLU   A 1 189 ? -27.568 -10.841 5.050  1.00 57.92  ? 404 GLU   B CA  1 
ATOM   1370 C C   . GLU   A 1 189 ? -27.193 -9.404  5.365  1.00 55.06  ? 404 GLU   B C   1 
ATOM   1371 O O   . GLU   A 1 189 ? -26.175 -9.149  6.011  1.00 55.57  ? 404 GLU   B O   1 
ATOM   1372 C CB  . GLU   A 1 189 ? -26.846 -11.298 3.784  1.00 60.91  ? 404 GLU   B CB  1 
ATOM   1373 C CG  . GLU   A 1 189 ? -25.382 -11.624 4.020  1.00 74.02  ? 404 GLU   B CG  1 
ATOM   1374 C CD  . GLU   A 1 189 ? -24.542 -11.499 2.751  1.00 93.92  ? 404 GLU   B CD  1 
ATOM   1375 O OE1 . GLU   A 1 189 ? -24.916 -12.101 1.709  1.00 104.45 ? 404 GLU   B OE1 1 
ATOM   1376 O OE2 . GLU   A 1 189 ? -23.502 -10.793 2.793  1.00 103.33 ? 404 GLU   B OE2 1 
ATOM   1377 N N   . ASN   A 1 190 ? -28.023 -8.467  4.900  1.00 54.28  ? 405 ASN   B N   1 
ATOM   1378 C CA  . ASN   A 1 190 ? -27.789 -7.027  5.069  1.00 53.93  ? 405 ASN   B CA  1 
ATOM   1379 C C   . ASN   A 1 190 ? -28.607 -6.356  6.209  1.00 58.51  ? 405 ASN   B C   1 
ATOM   1380 O O   . ASN   A 1 190 ? -28.622 -5.131  6.329  1.00 58.47  ? 405 ASN   B O   1 
ATOM   1381 C CB  . ASN   A 1 190 ? -28.086 -6.349  3.721  1.00 55.39  ? 405 ASN   B CB  1 
ATOM   1382 C CG  . ASN   A 1 190 ? -27.206 -6.883  2.597  1.00 56.79  ? 405 ASN   B CG  1 
ATOM   1383 O OD1 . ASN   A 1 190 ? -25.976 -6.839  2.694  1.00 55.50  ? 405 ASN   B OD1 1 
ATOM   1384 N ND2 . ASN   A 1 190 ? -27.827 -7.385  1.521  1.00 57.09  ? 405 ASN   B ND2 1 
ATOM   1385 N N   . PHE   A 1 191 ? -29.249 -7.156  7.067  1.00 55.99  ? 406 PHE   B N   1 
ATOM   1386 C CA  . PHE   A 1 191 ? -30.191 -6.650  8.049  1.00 51.47  ? 406 PHE   B CA  1 
ATOM   1387 C C   . PHE   A 1 191 ? -29.750 -7.004  9.434  1.00 44.69  ? 406 PHE   B C   1 
ATOM   1388 O O   . PHE   A 1 191 ? -29.654 -8.169  9.773  1.00 54.30  ? 406 PHE   B O   1 
ATOM   1389 C CB  . PHE   A 1 191 ? -31.560 -7.237  7.780  1.00 49.60  ? 406 PHE   B CB  1 
ATOM   1390 C CG  . PHE   A 1 191 ? -32.547 -6.849  8.787  1.00 49.48  ? 406 PHE   B CG  1 
ATOM   1391 C CD1 . PHE   A 1 191 ? -33.253 -5.645  8.664  1.00 52.92  ? 406 PHE   B CD1 1 
ATOM   1392 C CD2 . PHE   A 1 191 ? -32.759 -7.658  9.905  1.00 51.01  ? 406 PHE   B CD2 1 
ATOM   1393 C CE1 . PHE   A 1 191 ? -34.175 -5.272  9.638  1.00 56.33  ? 406 PHE   B CE1 1 
ATOM   1394 C CE2 . PHE   A 1 191 ? -33.670 -7.281  10.888 1.00 49.86  ? 406 PHE   B CE2 1 
ATOM   1395 C CZ  . PHE   A 1 191 ? -34.376 -6.098  10.763 1.00 52.45  ? 406 PHE   B CZ  1 
ATOM   1396 N N   . THR   A 1 192 ? -29.490 -6.003  10.248 1.00 45.81  ? 407 THR   B N   1 
ATOM   1397 C CA  . THR   A 1 192 ? -28.909 -6.225  11.570 1.00 48.91  ? 407 THR   B CA  1 
ATOM   1398 C C   . THR   A 1 192 ? -29.548 -5.341  12.653 1.00 49.72  ? 407 THR   B C   1 
ATOM   1399 O O   . THR   A 1 192 ? -30.226 -4.366  12.346 1.00 52.34  ? 407 THR   B O   1 
ATOM   1400 C CB  . THR   A 1 192 ? -27.374 -6.055  11.560 1.00 47.83  ? 407 THR   B CB  1 
ATOM   1401 O OG1 . THR   A 1 192 ? -27.029 -4.723  11.181 1.00 50.83  ? 407 THR   B OG1 1 
ATOM   1402 C CG2 . THR   A 1 192 ? -26.718 -7.047  10.573 1.00 51.27  ? 407 THR   B CG2 1 
ATOM   1403 N N   . ILE   A 1 193 ? -29.379 -5.748  13.913 1.00 44.23  ? 408 ILE   B N   1 
ATOM   1404 C CA  . ILE   A 1 193 ? -29.914 -5.041  15.047 1.00 42.41  ? 408 ILE   B CA  1 
ATOM   1405 C C   . ILE   A 1 193 ? -28.831 -4.959  16.113 1.00 43.08  ? 408 ILE   B C   1 
ATOM   1406 O O   . ILE   A 1 193 ? -28.159 -5.923  16.379 1.00 43.77  ? 408 ILE   B O   1 
ATOM   1407 C CB  . ILE   A 1 193 ? -31.189 -5.721  15.556 1.00 42.08  ? 408 ILE   B CB  1 
ATOM   1408 C CG1 . ILE   A 1 193 ? -32.345 -5.440  14.583 1.00 42.49  ? 408 ILE   B CG1 1 
ATOM   1409 C CG2 . ILE   A 1 193 ? -31.598 -5.177  16.921 1.00 42.96  ? 408 ILE   B CG2 1 
ATOM   1410 C CD1 . ILE   A 1 193 ? -33.641 -6.104  14.989 1.00 43.28  ? 408 ILE   B CD1 1 
ATOM   1411 N N   . LEU   A 1 194 ? -28.653 -3.786  16.703 1.00 47.36  ? 409 LEU   B N   1 
ATOM   1412 C CA  . LEU   A 1 194 ? -27.750 -3.609  17.840 1.00 48.66  ? 409 LEU   B CA  1 
ATOM   1413 C C   . LEU   A 1 194 ? -28.549 -3.113  19.062 1.00 46.62  ? 409 LEU   B C   1 
ATOM   1414 O O   . LEU   A 1 194 ? -29.295 -2.127  18.965 1.00 46.97  ? 409 LEU   B O   1 
ATOM   1415 C CB  . LEU   A 1 194 ? -26.652 -2.634  17.446 1.00 49.15  ? 409 LEU   B CB  1 
ATOM   1416 C CG  . LEU   A 1 194 ? -25.465 -2.400  18.380 1.00 48.72  ? 409 LEU   B CG  1 
ATOM   1417 C CD1 . LEU   A 1 194 ? -24.541 -3.596  18.404 1.00 48.09  ? 409 LEU   B CD1 1 
ATOM   1418 C CD2 . LEU   A 1 194 ? -24.689 -1.186  17.915 1.00 50.22  ? 409 LEU   B CD2 1 
ATOM   1419 N N   . GLN   A 1 195 ? -28.450 -3.854  20.162 1.00 45.79  ? 410 GLN   B N   1 
ATOM   1420 C CA  . GLN   A 1 195 ? -29.040 -3.485  21.440 1.00 49.67  ? 410 GLN   B CA  1 
ATOM   1421 C C   . GLN   A 1 195 ? -27.956 -3.041  22.371 1.00 51.11  ? 410 GLN   B C   1 
ATOM   1422 O O   . GLN   A 1 195 ? -27.018 -3.785  22.640 1.00 49.89  ? 410 GLN   B O   1 
ATOM   1423 C CB  . GLN   A 1 195 ? -29.785 -4.641  22.091 1.00 57.33  ? 410 GLN   B CB  1 
ATOM   1424 C CG  . GLN   A 1 195 ? -31.200 -4.772  21.555 1.00 69.27  ? 410 GLN   B CG  1 
ATOM   1425 C CD  . GLN   A 1 195 ? -32.219 -5.108  22.623 1.00 73.04  ? 410 GLN   B CD  1 
ATOM   1426 O OE1 . GLN   A 1 195 ? -32.828 -6.187  22.590 1.00 73.12  ? 410 GLN   B OE1 1 
ATOM   1427 N NE2 . GLN   A 1 195 ? -32.415 -4.187  23.577 1.00 76.20  ? 410 GLN   B NE2 1 
ATOM   1428 N N   . VAL   A 1 196 ? -28.110 -1.823  22.868 1.00 54.51  ? 411 VAL   B N   1 
ATOM   1429 C CA  . VAL   A 1 196 ? -27.214 -1.222  23.852 1.00 52.39  ? 411 VAL   B CA  1 
ATOM   1430 C C   . VAL   A 1 196 ? -28.045 -0.839  25.098 1.00 53.87  ? 411 VAL   B C   1 
ATOM   1431 O O   . VAL   A 1 196 ? -29.049 -0.072  25.043 1.00 55.58  ? 411 VAL   B O   1 
ATOM   1432 C CB  . VAL   A 1 196 ? -26.494 0.012   23.274 1.00 50.93  ? 411 VAL   B CB  1 
ATOM   1433 C CG1 . VAL   A 1 196 ? -25.516 0.579   24.289 1.00 52.30  ? 411 VAL   B CG1 1 
ATOM   1434 C CG2 . VAL   A 1 196 ? -25.763 -0.352  21.979 1.00 50.22  ? 411 VAL   B CG2 1 
ATOM   1435 N N   . VAL   A 1 197 ? -27.615 -1.400  26.215 1.00 50.80  ? 412 VAL   B N   1 
ATOM   1436 C CA  . VAL   A 1 197 ? -28.214 -1.172  27.503 1.00 45.62  ? 412 VAL   B CA  1 
ATOM   1437 C C   . VAL   A 1 197 ? -27.164 -0.473  28.354 1.00 48.42  ? 412 VAL   B C   1 
ATOM   1438 O O   . VAL   A 1 197 ? -26.034 -0.953  28.504 1.00 49.34  ? 412 VAL   B O   1 
ATOM   1439 C CB  . VAL   A 1 197 ? -28.611 -2.502  28.145 1.00 48.58  ? 412 VAL   B CB  1 
ATOM   1440 C CG1 . VAL   A 1 197 ? -29.269 -2.259  29.509 1.00 49.09  ? 412 VAL   B CG1 1 
ATOM   1441 C CG2 . VAL   A 1 197 ? -29.499 -3.320  27.194 1.00 45.90  ? 412 VAL   B CG2 1 
ATOM   1442 N N   . THR   A 1 198 ? -27.511 0.678   28.906 1.00 50.74  ? 413 THR   B N   1 
ATOM   1443 C CA  . THR   A 1 198 ? -26.572 1.422   29.729 1.00 52.45  ? 413 THR   B CA  1 
ATOM   1444 C C   . THR   A 1 198 ? -27.244 1.818   31.014 1.00 53.06  ? 413 THR   B C   1 
ATOM   1445 O O   . THR   A 1 198 ? -28.458 1.975   31.046 1.00 49.18  ? 413 THR   B O   1 
ATOM   1446 C CB  . THR   A 1 198 ? -26.129 2.707   29.027 1.00 54.18  ? 413 THR   B CB  1 
ATOM   1447 O OG1 . THR   A 1 198 ? -27.275 3.521   28.812 1.00 61.17  ? 413 THR   B OG1 1 
ATOM   1448 C CG2 . THR   A 1 198 ? -25.499 2.404   27.681 1.00 54.11  ? 413 THR   B CG2 1 
ATOM   1449 N N   . ASN   A 1 199 ? -26.448 1.990   32.063 1.00 57.29  ? 414 ASN   B N   1 
ATOM   1450 C CA  . ASN   A 1 199 ? -26.918 2.617   33.291 1.00 59.13  ? 414 ASN   B CA  1 
ATOM   1451 C C   . ASN   A 1 199 ? -27.190 4.071   32.933 1.00 59.30  ? 414 ASN   B C   1 
ATOM   1452 O O   . ASN   A 1 199 ? -26.252 4.830   32.693 1.00 66.36  ? 414 ASN   B O   1 
ATOM   1453 C CB  . ASN   A 1 199 ? -25.837 2.495   34.357 1.00 61.56  ? 414 ASN   B CB  1 
ATOM   1454 C CG  . ASN   A 1 199 ? -26.240 3.069   35.709 1.00 60.48  ? 414 ASN   B CG  1 
ATOM   1455 O OD1 . ASN   A 1 199 ? -26.843 4.124   35.813 1.00 74.15  ? 414 ASN   B OD1 1 
ATOM   1456 N ND2 . ASN   A 1 199 ? -25.848 2.391   36.756 1.00 64.42  ? 414 ASN   B ND2 1 
ATOM   1457 N N   . ARG   A 1 200 ? -28.471 4.433   32.861 1.00 57.63  ? 415 ARG   B N   1 
ATOM   1458 C CA  . ARG   A 1 200 ? -28.897 5.790   32.540 1.00 65.52  ? 415 ARG   B CA  1 
ATOM   1459 C C   . ARG   A 1 200 ? -28.259 6.874   33.440 1.00 71.12  ? 415 ARG   B C   1 
ATOM   1460 O O   . ARG   A 1 200 ? -28.009 7.986   32.977 1.00 74.57  ? 415 ARG   B O   1 
ATOM   1461 C CB  . ARG   A 1 200 ? -30.421 5.894   32.627 1.00 73.50  ? 415 ARG   B CB  1 
ATOM   1462 C CG  . ARG   A 1 200 ? -31.017 7.182   32.052 1.00 80.87  ? 415 ARG   B CG  1 
ATOM   1463 C CD  . ARG   A 1 200 ? -32.326 7.554   32.740 1.00 91.50  ? 415 ARG   B CD  1 
ATOM   1464 N NE  . ARG   A 1 200 ? -32.138 7.853   34.171 1.00 98.84  ? 415 ARG   B NE  1 
ATOM   1465 C CZ  . ARG   A 1 200 ? -33.100 8.236   35.017 1.00 105.51 ? 415 ARG   B CZ  1 
ATOM   1466 N NH1 . ARG   A 1 200 ? -34.363 8.398   34.601 1.00 108.16 ? 415 ARG   B NH1 1 
ATOM   1467 N NH2 . ARG   A 1 200 ? -32.798 8.461   36.296 1.00 99.11  ? 415 ARG   B NH2 1 
ATOM   1468 N N   . ASP   A 1 201 ? -27.992 6.569   34.706 1.00 66.08  ? 416 ASP   B N   1 
ATOM   1469 C CA  . ASP   A 1 201 ? -27.414 7.577   35.604 1.00 75.27  ? 416 ASP   B CA  1 
ATOM   1470 C C   . ASP   A 1 201 ? -25.913 7.716   35.359 1.00 77.34  ? 416 ASP   B C   1 
ATOM   1471 O O   . ASP   A 1 201 ? -25.438 8.787   35.002 1.00 79.33  ? 416 ASP   B O   1 
ATOM   1472 C CB  . ASP   A 1 201 ? -27.720 7.256   37.070 1.00 72.59  ? 416 ASP   B CB  1 
ATOM   1473 C CG  . ASP   A 1 201 ? -29.217 7.047   37.321 1.00 76.93  ? 416 ASP   B CG  1 
ATOM   1474 O OD1 . ASP   A 1 201 ? -30.048 7.870   36.874 1.00 76.77  ? 416 ASP   B OD1 1 
ATOM   1475 O OD2 . ASP   A 1 201 ? -29.572 6.029   37.945 1.00 84.54  ? 416 ASP   B OD2 1 
ATOM   1476 N N   . THR   A 1 202 ? -25.177 6.626   35.513 1.00 75.54  ? 417 THR   B N   1 
ATOM   1477 C CA  . THR   A 1 202 ? -23.731 6.656   35.301 1.00 76.29  ? 417 THR   B CA  1 
ATOM   1478 C C   . THR   A 1 202 ? -23.281 6.746   33.838 1.00 77.41  ? 417 THR   B C   1 
ATOM   1479 O O   . THR   A 1 202 ? -22.129 7.093   33.588 1.00 80.72  ? 417 THR   B O   1 
ATOM   1480 C CB  . THR   A 1 202 ? -23.029 5.404   35.844 1.00 75.59  ? 417 THR   B CB  1 
ATOM   1481 O OG1 . THR   A 1 202 ? -23.352 4.287   35.005 1.00 80.17  ? 417 THR   B OG1 1 
ATOM   1482 C CG2 . THR   A 1 202 ? -23.408 5.130   37.295 1.00 68.23  ? 417 THR   B CG2 1 
ATOM   1483 N N   . GLN   A 1 203 ? -24.150 6.404   32.886 1.00 78.22  ? 418 GLN   B N   1 
ATOM   1484 C CA  . GLN   A 1 203 ? -23.756 6.211   31.469 1.00 78.29  ? 418 GLN   B CA  1 
ATOM   1485 C C   . GLN   A 1 203 ? -22.887 4.962   31.187 1.00 78.25  ? 418 GLN   B C   1 
ATOM   1486 O O   . GLN   A 1 203 ? -22.529 4.731   30.029 1.00 76.84  ? 418 GLN   B O   1 
ATOM   1487 C CB  . GLN   A 1 203 ? -23.025 7.434   30.869 1.00 76.07  ? 418 GLN   B CB  1 
ATOM   1488 C CG  . GLN   A 1 203 ? -23.540 8.802   31.260 1.00 86.60  ? 418 GLN   B CG  1 
ATOM   1489 C CD  . GLN   A 1 203 ? -24.973 9.022   30.845 1.00 95.07  ? 418 GLN   B CD  1 
ATOM   1490 O OE1 . GLN   A 1 203 ? -25.556 8.217   30.123 1.00 97.88  ? 418 GLN   B OE1 1 
ATOM   1491 N NE2 . GLN   A 1 203 ? -25.552 10.130  31.297 1.00 102.51 ? 418 GLN   B NE2 1 
ATOM   1492 N N   . GLU   A 1 204 ? -22.543 4.168   32.204 1.00 76.42  ? 419 GLU   B N   1 
ATOM   1493 C CA  . GLU   A 1 204 ? -21.748 2.967   31.990 1.00 74.67  ? 419 GLU   B CA  1 
ATOM   1494 C C   . GLU   A 1 204 ? -22.541 2.039   31.074 1.00 68.80  ? 419 GLU   B C   1 
ATOM   1495 O O   . GLU   A 1 204 ? -23.767 1.920   31.226 1.00 61.18  ? 419 GLU   B O   1 
ATOM   1496 C CB  . GLU   A 1 204 ? -21.472 2.232   33.310 1.00 86.86  ? 419 GLU   B CB  1 
ATOM   1497 C CG  . GLU   A 1 204 ? -20.597 2.972   34.324 1.00 93.27  ? 419 GLU   B CG  1 
ATOM   1498 C CD  . GLU   A 1 204 ? -20.760 2.428   35.743 1.00 95.12  ? 419 GLU   B CD  1 
ATOM   1499 O OE1 . GLU   A 1 204 ? -21.895 2.446   36.274 1.00 88.63  ? 419 GLU   B OE1 1 
ATOM   1500 O OE2 . GLU   A 1 204 ? -19.756 1.967   36.330 1.00 96.80  ? 419 GLU   B OE2 1 
ATOM   1501 N N   . LEU   A 1 205 ? -21.836 1.414   30.125 1.00 62.80  ? 420 LEU   B N   1 
ATOM   1502 C CA  . LEU   A 1 205 ? -22.399 0.397   29.240 1.00 58.74  ? 420 LEU   B CA  1 
ATOM   1503 C C   . LEU   A 1 205 ? -22.489 -0.921  29.984 1.00 55.19  ? 420 LEU   B C   1 
ATOM   1504 O O   . LEU   A 1 205 ? -21.505 -1.338  30.616 1.00 55.95  ? 420 LEU   B O   1 
ATOM   1505 C CB  . LEU   A 1 205 ? -21.529 0.234   28.002 1.00 59.36  ? 420 LEU   B CB  1 
ATOM   1506 C CG  . LEU   A 1 205 ? -22.173 -0.565  26.864 1.00 60.54  ? 420 LEU   B CG  1 
ATOM   1507 C CD1 . LEU   A 1 205 ? -21.728 -0.010  25.522 1.00 69.73  ? 420 LEU   B CD1 1 
ATOM   1508 C CD2 . LEU   A 1 205 ? -21.842 -2.031  26.960 1.00 59.37  ? 420 LEU   B CD2 1 
ATOM   1509 N N   . LEU   A 1 206 ? -23.661 -1.563  29.931 1.00 49.51  ? 421 LEU   B N   1 
ATOM   1510 C CA  . LEU   A 1 206 ? -23.901 -2.817  30.682 1.00 49.06  ? 421 LEU   B CA  1 
ATOM   1511 C C   . LEU   A 1 206 ? -23.983 -4.071  29.816 1.00 51.79  ? 421 LEU   B C   1 
ATOM   1512 O O   . LEU   A 1 206 ? -23.595 -5.162  30.257 1.00 58.59  ? 421 LEU   B O   1 
ATOM   1513 C CB  . LEU   A 1 206 ? -25.172 -2.717  31.539 1.00 50.36  ? 421 LEU   B CB  1 
ATOM   1514 C CG  . LEU   A 1 206 ? -25.193 -1.777  32.761 1.00 48.46  ? 421 LEU   B CG  1 
ATOM   1515 C CD1 . LEU   A 1 206 ? -26.586 -1.679  33.357 1.00 46.87  ? 421 LEU   B CD1 1 
ATOM   1516 C CD2 . LEU   A 1 206 ? -24.217 -2.226  33.833 1.00 49.10  ? 421 LEU   B CD2 1 
ATOM   1517 N N   . LEU   A 1 207 ? -24.489 -3.934  28.597 1.00 53.42  ? 422 LEU   B N   1 
ATOM   1518 C CA  . LEU   A 1 207 ? -24.702 -5.078  27.710 1.00 52.43  ? 422 LEU   B CA  1 
ATOM   1519 C C   . LEU   A 1 207 ? -24.787 -4.535  26.299 1.00 48.92  ? 422 LEU   B C   1 
ATOM   1520 O O   . LEU   A 1 207 ? -25.465 -3.547  26.041 1.00 43.96  ? 422 LEU   B O   1 
ATOM   1521 C CB  . LEU   A 1 207 ? -26.012 -5.780  28.082 1.00 54.32  ? 422 LEU   B CB  1 
ATOM   1522 C CG  . LEU   A 1 207 ? -26.156 -7.297  27.975 1.00 56.17  ? 422 LEU   B CG  1 
ATOM   1523 C CD1 . LEU   A 1 207 ? -25.075 -8.033  28.762 1.00 55.39  ? 422 LEU   B CD1 1 
ATOM   1524 C CD2 . LEU   A 1 207 ? -27.547 -7.688  28.478 1.00 56.79  ? 422 LEU   B CD2 1 
ATOM   1525 N N   . CYS   A 1 208 ? -24.063 -5.145  25.393 1.00 48.07  ? 423 CYS   B N   1 
ATOM   1526 C CA  . CYS   A 1 208 ? -24.171 -4.778  23.999 1.00 47.91  ? 423 CYS   B CA  1 
ATOM   1527 C C   . CYS   A 1 208 ? -24.323 -6.052  23.195 1.00 47.48  ? 423 CYS   B C   1 
ATOM   1528 O O   . CYS   A 1 208 ? -23.453 -6.936  23.270 1.00 45.51  ? 423 CYS   B O   1 
ATOM   1529 C CB  . CYS   A 1 208 ? -22.935 -4.029  23.524 1.00 46.32  ? 423 CYS   B CB  1 
ATOM   1530 S SG  . CYS   A 1 208 ? -23.169 -3.502  21.811 1.00 51.31  ? 423 CYS   B SG  1 
ATOM   1531 N N   . THR   A 1 209 ? -25.403 -6.131  22.422 1.00 44.66  ? 424 THR   B N   1 
ATOM   1532 C CA  . THR   A 1 209 ? -25.729 -7.323  21.692 1.00 46.52  ? 424 THR   B CA  1 
ATOM   1533 C C   . THR   A 1 209 ? -25.984 -7.046  20.219 1.00 46.20  ? 424 THR   B C   1 
ATOM   1534 O O   . THR   A 1 209 ? -26.966 -6.396  19.868 1.00 46.80  ? 424 THR   B O   1 
ATOM   1535 C CB  . THR   A 1 209 ? -26.934 -7.995  22.341 1.00 47.95  ? 424 THR   B CB  1 
ATOM   1536 O OG1 . THR   A 1 209 ? -26.567 -8.340  23.669 1.00 40.59  ? 424 THR   B OG1 1 
ATOM   1537 C CG2 . THR   A 1 209 ? -27.331 -9.269  21.604 1.00 50.33  ? 424 THR   B CG2 1 
ATOM   1538 N N   . ALA   A 1 210 ? -25.106 -7.578  19.367 1.00 46.05  ? 425 ALA   B N   1 
ATOM   1539 C CA  . ALA   A 1 210 ? -25.331 -7.604  17.911 1.00 48.46  ? 425 ALA   B CA  1 
ATOM   1540 C C   . ALA   A 1 210 ? -26.174 -8.833  17.485 1.00 50.49  ? 425 ALA   B C   1 
ATOM   1541 O O   . ALA   A 1 210 ? -25.892 -9.957  17.893 1.00 48.55  ? 425 ALA   B O   1 
ATOM   1542 C CB  . ALA   A 1 210 ? -23.994 -7.596  17.169 1.00 47.87  ? 425 ALA   B CB  1 
ATOM   1543 N N   . TYR   A 1 211 ? -27.191 -8.593  16.657 1.00 49.78  ? 426 TYR   B N   1 
ATOM   1544 C CA  . TYR   A 1 211 ? -28.022 -9.643  16.080 1.00 50.40  ? 426 TYR   B CA  1 
ATOM   1545 C C   . TYR   A 1 211 ? -27.845 -9.757  14.563 1.00 52.83  ? 426 TYR   B C   1 
ATOM   1546 O O   . TYR   A 1 211 ? -27.976 -8.766  13.847 1.00 49.02  ? 426 TYR   B O   1 
ATOM   1547 C CB  . TYR   A 1 211 ? -29.472 -9.347  16.331 1.00 49.80  ? 426 TYR   B CB  1 
ATOM   1548 C CG  . TYR   A 1 211 ? -29.822 -9.305  17.779 1.00 53.07  ? 426 TYR   B CG  1 
ATOM   1549 C CD1 . TYR   A 1 211 ? -30.177 -10.450 18.441 1.00 55.63  ? 426 TYR   B CD1 1 
ATOM   1550 C CD2 . TYR   A 1 211 ? -29.830 -8.118  18.488 1.00 55.76  ? 426 TYR   B CD2 1 
ATOM   1551 C CE1 . TYR   A 1 211 ? -30.522 -10.436 19.781 1.00 56.71  ? 426 TYR   B CE1 1 
ATOM   1552 C CE2 . TYR   A 1 211 ? -30.189 -8.097  19.823 1.00 58.36  ? 426 TYR   B CE2 1 
ATOM   1553 C CZ  . TYR   A 1 211 ? -30.543 -9.268  20.460 1.00 52.99  ? 426 TYR   B CZ  1 
ATOM   1554 O OH  . TYR   A 1 211 ? -30.901 -9.277  21.778 1.00 49.56  ? 426 TYR   B OH  1 
ATOM   1555 N N   . VAL   A 1 212 ? -27.568 -10.974 14.084 1.00 49.90  ? 427 VAL   B N   1 
ATOM   1556 C CA  . VAL   A 1 212 ? -27.563 -11.255 12.650 1.00 44.35  ? 427 VAL   B CA  1 
ATOM   1557 C C   . VAL   A 1 212 ? -28.583 -12.332 12.436 1.00 42.57  ? 427 VAL   B C   1 
ATOM   1558 O O   . VAL   A 1 212 ? -28.913 -13.054 13.370 1.00 42.06  ? 427 VAL   B O   1 
ATOM   1559 C CB  . VAL   A 1 212 ? -26.178 -11.611 12.133 1.00 42.16  ? 427 VAL   B CB  1 
ATOM   1560 C CG1 . VAL   A 1 212 ? -25.250 -10.438 12.365 1.00 44.94  ? 427 VAL   B CG1 1 
ATOM   1561 C CG2 . VAL   A 1 212 ? -25.588 -12.842 12.808 1.00 45.78  ? 427 VAL   B CG2 1 
ATOM   1562 N N   . PHE   A 1 213 ? -29.119 -12.407 11.232 1.00 44.12  ? 428 PHE   B N   1 
ATOM   1563 C CA  . PHE   A 1 213 ? -30.355 -13.144 11.009 1.00 47.97  ? 428 PHE   B CA  1 
ATOM   1564 C C   . PHE   A 1 213 ? -30.322 -14.086 9.801  1.00 49.90  ? 428 PHE   B C   1 
ATOM   1565 O O   . PHE   A 1 213 ? -29.793 -13.751 8.777  1.00 57.37  ? 428 PHE   B O   1 
ATOM   1566 C CB  . PHE   A 1 213 ? -31.519 -12.168 10.828 1.00 46.27  ? 428 PHE   B CB  1 
ATOM   1567 C CG  . PHE   A 1 213 ? -31.816 -11.316 12.047 1.00 47.06  ? 428 PHE   B CG  1 
ATOM   1568 C CD1 . PHE   A 1 213 ? -31.140 -10.117 12.258 1.00 47.52  ? 428 PHE   B CD1 1 
ATOM   1569 C CD2 . PHE   A 1 213 ? -32.793 -11.695 12.957 1.00 45.59  ? 428 PHE   B CD2 1 
ATOM   1570 C CE1 . PHE   A 1 213 ? -31.422 -9.334  13.362 1.00 48.72  ? 428 PHE   B CE1 1 
ATOM   1571 C CE2 . PHE   A 1 213 ? -33.078 -10.906 14.062 1.00 48.12  ? 428 PHE   B CE2 1 
ATOM   1572 C CZ  . PHE   A 1 213 ? -32.388 -9.731  14.267 1.00 45.36  ? 428 PHE   B CZ  1 
ATOM   1573 N N   . GLU   A 1 214 ? -30.898 -15.269 9.960  1.00 53.88  ? 429 GLU   B N   1 
ATOM   1574 C CA  . GLU   A 1 214 ? -31.313 -16.132 8.859  1.00 53.50  ? 429 GLU   B CA  1 
ATOM   1575 C C   . GLU   A 1 214 ? -32.749 -16.515 9.091  1.00 48.28  ? 429 GLU   B C   1 
ATOM   1576 O O   . GLU   A 1 214 ? -33.285 -16.298 10.176 1.00 48.71  ? 429 GLU   B O   1 
ATOM   1577 C CB  . GLU   A 1 214 ? -30.479 -17.407 8.845  1.00 59.26  ? 429 GLU   B CB  1 
ATOM   1578 C CG  . GLU   A 1 214 ? -29.204 -17.237 8.046  1.00 67.30  ? 429 GLU   B CG  1 
ATOM   1579 C CD  . GLU   A 1 214 ? -28.347 -18.492 8.036  1.00 73.24  ? 429 GLU   B CD  1 
ATOM   1580 O OE1 . GLU   A 1 214 ? -28.884 -19.633 7.803  1.00 59.46  ? 429 GLU   B OE1 1 
ATOM   1581 O OE2 . GLU   A 1 214 ? -27.132 -18.303 8.267  1.00 67.67  ? 429 GLU   B OE2 1 
ATOM   1582 N N   . VAL   A 1 215 ? -33.364 -17.099 8.079  1.00 48.44  ? 430 VAL   B N   1 
ATOM   1583 C CA  . VAL   A 1 215 ? -34.692 -17.674 8.225  1.00 54.96  ? 430 VAL   B CA  1 
ATOM   1584 C C   . VAL   A 1 215 ? -34.523 -19.170 8.496  1.00 58.98  ? 430 VAL   B C   1 
ATOM   1585 O O   . VAL   A 1 215 ? -33.668 -19.799 7.891  1.00 64.36  ? 430 VAL   B O   1 
ATOM   1586 C CB  . VAL   A 1 215 ? -35.586 -17.367 7.015  1.00 54.60  ? 430 VAL   B CB  1 
ATOM   1587 C CG1 . VAL   A 1 215 ? -34.952 -17.806 5.699  1.00 62.15  ? 430 VAL   B CG1 1 
ATOM   1588 C CG2 . VAL   A 1 215 ? -36.950 -18.004 7.177  1.00 55.88  ? 430 VAL   B CG2 1 
ATOM   1589 N N   . SER   A 1 216 ? -35.274 -19.725 9.450  1.00 58.97  ? 431 SER   B N   1 
ATOM   1590 C CA  . SER   A 1 216 ? -35.338 -21.186 9.592  1.00 63.72  ? 431 SER   B CA  1 
ATOM   1591 C C   . SER   A 1 216 ? -36.463 -21.766 8.684  1.00 67.09  ? 431 SER   B C   1 
ATOM   1592 O O   . SER   A 1 216 ? -37.276 -21.026 8.132  1.00 68.31  ? 431 SER   B O   1 
ATOM   1593 C CB  . SER   A 1 216 ? -35.484 -21.607 11.057 1.00 57.83  ? 431 SER   B CB  1 
ATOM   1594 O OG  . SER   A 1 216 ? -36.771 -22.046 11.386 1.00 62.07  ? 431 SER   B OG  1 
ATOM   1595 N N   . THR   A 1 217 ? -36.498 -23.090 8.557  1.00 74.21  ? 432 THR   B N   1 
ATOM   1596 C CA  . THR   A 1 217 ? -37.398 -23.797 7.627  1.00 73.25  ? 432 THR   B CA  1 
ATOM   1597 C C   . THR   A 1 217 ? -38.770 -24.120 8.239  1.00 81.24  ? 432 THR   B C   1 
ATOM   1598 O O   . THR   A 1 217 ? -38.878 -25.040 9.049  1.00 92.32  ? 432 THR   B O   1 
ATOM   1599 C CB  . THR   A 1 217 ? -36.756 -25.141 7.183  1.00 68.07  ? 432 THR   B CB  1 
ATOM   1600 O OG1 . THR   A 1 217 ? -36.571 -26.006 8.323  1.00 66.88  ? 432 THR   B OG1 1 
ATOM   1601 C CG2 . THR   A 1 217 ? -35.409 -24.910 6.538  1.00 65.10  ? 432 THR   B CG2 1 
ATOM   1602 N N   . SER   A 1 218 ? -39.797 -23.360 7.868  1.00 85.26  ? 433 SER   B N   1 
ATOM   1603 C CA  . SER   A 1 218 ? -41.205 -23.757 8.034  1.00 94.29  ? 433 SER   B CA  1 
ATOM   1604 C C   . SER   A 1 218 ? -41.551 -24.452 9.366  1.00 96.40  ? 433 SER   B C   1 
ATOM   1605 O O   . SER   A 1 218 ? -42.076 -23.808 10.290 1.00 95.47  ? 433 SER   B O   1 
ATOM   1606 C CB  . SER   A 1 218 ? -41.617 -24.628 6.828  1.00 96.21  ? 433 SER   B CB  1 
ATOM   1607 O OG  . SER   A 1 218 ? -42.644 -25.544 7.161  1.00 102.76 ? 433 SER   B OG  1 
ATOM   1608 N N   . GLU   A 1 219 ? -41.214 -25.753 9.443  1.00 98.67  ? 434 GLU   B N   1 
ATOM   1609 C CA  . GLU   A 1 219 ? -41.523 -26.649 10.589 1.00 92.81  ? 434 GLU   B CA  1 
ATOM   1610 C C   . GLU   A 1 219 ? -40.427 -26.772 11.669 1.00 78.16  ? 434 GLU   B C   1 
ATOM   1611 O O   . GLU   A 1 219 ? -40.691 -27.313 12.749 1.00 76.19  ? 434 GLU   B O   1 
ATOM   1612 C CB  . GLU   A 1 219 ? -41.899 -28.061 10.082 1.00 96.97  ? 434 GLU   B CB  1 
ATOM   1613 C CG  . GLU   A 1 219 ? -40.749 -29.068 9.908  1.00 98.99  ? 434 GLU   B CG  1 
ATOM   1614 C CD  . GLU   A 1 219 ? -40.211 -29.168 8.484  1.00 98.71  ? 434 GLU   B CD  1 
ATOM   1615 O OE1 . GLU   A 1 219 ? -40.398 -30.250 7.885  1.00 85.88  ? 434 GLU   B OE1 1 
ATOM   1616 O OE2 . GLU   A 1 219 ? -39.606 -28.192 7.968  1.00 98.05  ? 434 GLU   B OE2 1 
ATOM   1617 N N   . ARG   A 1 220 ? -39.193 -26.355 11.364 1.00 64.70  ? 435 ARG   B N   1 
ATOM   1618 C CA  . ARG   A 1 220 ? -38.286 -25.914 12.426 1.00 58.73  ? 435 ARG   B CA  1 
ATOM   1619 C C   . ARG   A 1 220 ? -38.728 -24.483 12.774 1.00 63.75  ? 435 ARG   B C   1 
ATOM   1620 O O   . ARG   A 1 220 ? -38.993 -23.637 11.889 1.00 68.42  ? 435 ARG   B O   1 
ATOM   1621 C CB  . ARG   A 1 220 ? -36.833 -25.894 12.012 1.00 54.89  ? 435 ARG   B CB  1 
ATOM   1622 C CG  . ARG   A 1 220 ? -36.303 -27.191 11.489 1.00 53.86  ? 435 ARG   B CG  1 
ATOM   1623 C CD  . ARG   A 1 220 ? -34.785 -27.139 11.293 1.00 54.50  ? 435 ARG   B CD  1 
ATOM   1624 N NE  . ARG   A 1 220 ? -34.009 -27.226 12.545 1.00 52.60  ? 435 ARG   B NE  1 
ATOM   1625 C CZ  . ARG   A 1 220 ? -32.678 -27.425 12.625 1.00 55.54  ? 435 ARG   B CZ  1 
ATOM   1626 N NH1 . ARG   A 1 220 ? -31.937 -27.576 11.520 1.00 61.70  ? 435 ARG   B NH1 1 
ATOM   1627 N NH2 . ARG   A 1 220 ? -32.066 -27.466 13.820 1.00 49.55  ? 435 ARG   B NH2 1 
ATOM   1628 N N   . GLY   A 1 221 ? -38.843 -24.225 14.060 1.00 57.92  ? 436 GLY   B N   1 
ATOM   1629 C CA  . GLY   A 1 221 ? -39.205 -22.908 14.527 1.00 57.58  ? 436 GLY   B CA  1 
ATOM   1630 C C   . GLY   A 1 221 ? -37.944 -22.110 14.769 1.00 54.99  ? 436 GLY   B C   1 
ATOM   1631 O O   . GLY   A 1 221 ? -36.844 -22.450 14.293 1.00 57.27  ? 436 GLY   B O   1 
ATOM   1632 N N   . ALA   A 1 222 ? -38.099 -21.070 15.566 1.00 51.76  ? 437 ALA   B N   1 
ATOM   1633 C CA  . ALA   A 1 222 ? -37.014 -20.163 15.853 1.00 51.68  ? 437 ALA   B CA  1 
ATOM   1634 C C   . ALA   A 1 222 ? -35.918 -20.865 16.623 1.00 49.52  ? 437 ALA   B C   1 
ATOM   1635 O O   . ALA   A 1 222 ? -36.208 -21.586 17.549 1.00 58.10  ? 437 ALA   B O   1 
ATOM   1636 C CB  . ALA   A 1 222 ? -37.530 -18.981 16.645 1.00 50.50  ? 437 ALA   B CB  1 
ATOM   1637 N N   . GLN   A 1 223 ? -34.668 -20.664 16.230 1.00 50.24  ? 438 GLN   B N   1 
ATOM   1638 C CA  . GLN   A 1 223 ? -33.514 -21.073 17.043 1.00 50.73  ? 438 GLN   B CA  1 
ATOM   1639 C C   . GLN   A 1 223 ? -32.518 -19.912 17.058 1.00 45.20  ? 438 GLN   B C   1 
ATOM   1640 O O   . GLN   A 1 223 ? -32.654 -18.939 16.294 1.00 41.23  ? 438 GLN   B O   1 
ATOM   1641 C CB  . GLN   A 1 223 ? -32.846 -22.346 16.487 1.00 60.75  ? 438 GLN   B CB  1 
ATOM   1642 C CG  . GLN   A 1 223 ? -33.591 -23.667 16.772 1.00 71.14  ? 438 GLN   B CG  1 
ATOM   1643 C CD  . GLN   A 1 223 ? -32.684 -24.929 16.751 1.00 79.26  ? 438 GLN   B CD  1 
ATOM   1644 O OE1 . GLN   A 1 223 ? -32.319 -25.442 15.686 1.00 72.55  ? 438 GLN   B OE1 1 
ATOM   1645 N NE2 . GLN   A 1 223 ? -32.339 -25.439 17.938 1.00 80.05  ? 438 GLN   B NE2 1 
ATOM   1646 N N   . HIS   A 1 224 ? -31.530 -20.037 17.934 1.00 43.04  ? 439 HIS   B N   1 
ATOM   1647 C CA  . HIS   A 1 224 ? -30.458 -19.075 18.097 1.00 44.62  ? 439 HIS   B CA  1 
ATOM   1648 C C   . HIS   A 1 224 ? -29.172 -19.699 18.623 1.00 43.73  ? 439 HIS   B C   1 
ATOM   1649 O O   . HIS   A 1 224 ? -29.180 -20.803 19.096 1.00 41.81  ? 439 HIS   B O   1 
ATOM   1650 C CB  . HIS   A 1 224 ? -30.885 -17.990 19.084 1.00 49.04  ? 439 HIS   B CB  1 
ATOM   1651 C CG  . HIS   A 1 224 ? -31.067 -18.479 20.472 1.00 50.69  ? 439 HIS   B CG  1 
ATOM   1652 N ND1 . HIS   A 1 224 ? -30.028 -18.563 21.374 1.00 57.16  ? 439 HIS   B ND1 1 
ATOM   1653 C CD2 . HIS   A 1 224 ? -32.170 -18.913 21.121 1.00 56.31  ? 439 HIS   B CD2 1 
ATOM   1654 C CE1 . HIS   A 1 224 ? -30.485 -19.027 22.524 1.00 57.44  ? 439 HIS   B CE1 1 
ATOM   1655 N NE2 . HIS   A 1 224 ? -31.783 -19.245 22.397 1.00 58.97  ? 439 HIS   B NE2 1 
ATOM   1656 N N   . HIS   A 1 225 ? -28.086 -18.946 18.555 1.00 45.98  ? 440 HIS   B N   1 
ATOM   1657 C CA  . HIS   A 1 225 ? -26.786 -19.357 19.053 1.00 52.07  ? 440 HIS   B CA  1 
ATOM   1658 C C   . HIS   A 1 225 ? -26.098 -18.050 19.475 1.00 54.55  ? 440 HIS   B C   1 
ATOM   1659 O O   . HIS   A 1 225 ? -26.045 -17.088 18.694 1.00 52.89  ? 440 HIS   B O   1 
ATOM   1660 C CB  . HIS   A 1 225 ? -25.987 -20.054 17.941 1.00 60.36  ? 440 HIS   B CB  1 
ATOM   1661 C CG  . HIS   A 1 225 ? -24.752 -20.761 18.415 1.00 72.62  ? 440 HIS   B CG  1 
ATOM   1662 N ND1 . HIS   A 1 225 ? -23.697 -20.113 19.023 1.00 79.35  ? 440 HIS   B ND1 1 
ATOM   1663 C CD2 . HIS   A 1 225 ? -24.396 -22.066 18.350 1.00 80.38  ? 440 HIS   B CD2 1 
ATOM   1664 C CE1 . HIS   A 1 225 ? -22.756 -20.989 19.328 1.00 81.77  ? 440 HIS   B CE1 1 
ATOM   1665 N NE2 . HIS   A 1 225 ? -23.151 -22.180 18.920 1.00 80.79  ? 440 HIS   B NE2 1 
ATOM   1666 N N   . ILE   A 1 226 ? -25.567 -18.050 20.696 1.00 48.70  ? 441 ILE   B N   1 
ATOM   1667 C CA  . ILE   A 1 226 ? -25.013 -16.897 21.338 1.00 48.87  ? 441 ILE   B CA  1 
ATOM   1668 C C   . ILE   A 1 226 ? -23.488 -17.023 21.351 1.00 54.39  ? 441 ILE   B C   1 
ATOM   1669 O O   . ILE   A 1 226 ? -22.963 -18.047 21.777 1.00 51.64  ? 441 ILE   B O   1 
ATOM   1670 C CB  . ILE   A 1 226 ? -25.529 -16.809 22.783 1.00 49.35  ? 441 ILE   B CB  1 
ATOM   1671 C CG1 . ILE   A 1 226 ? -27.061 -16.921 22.840 1.00 51.52  ? 441 ILE   B CG1 1 
ATOM   1672 C CG2 . ILE   A 1 226 ? -25.133 -15.491 23.405 1.00 53.00  ? 441 ILE   B CG2 1 
ATOM   1673 C CD1 . ILE   A 1 226 ? -27.676 -16.832 24.240 1.00 50.75  ? 441 ILE   B CD1 1 
ATOM   1674 N N   . TYR   A 1 227 ? -22.783 -15.989 20.876 1.00 55.94  ? 442 TYR   B N   1 
ATOM   1675 C CA  . TYR   A 1 227 ? -21.314 -15.923 20.931 1.00 53.36  ? 442 TYR   B CA  1 
ATOM   1676 C C   . TYR   A 1 227 ? -20.852 -14.746 21.799 1.00 54.51  ? 442 TYR   B C   1 
ATOM   1677 O O   . TYR   A 1 227 ? -21.541 -13.748 21.889 1.00 55.21  ? 442 TYR   B O   1 
ATOM   1678 C CB  . TYR   A 1 227 ? -20.744 -15.748 19.522 1.00 53.70  ? 442 TYR   B CB  1 
ATOM   1679 C CG  . TYR   A 1 227 ? -21.155 -16.832 18.566 1.00 55.65  ? 442 TYR   B CG  1 
ATOM   1680 C CD1 . TYR   A 1 227 ? -22.348 -16.758 17.862 1.00 57.03  ? 442 TYR   B CD1 1 
ATOM   1681 C CD2 . TYR   A 1 227 ? -20.344 -17.945 18.371 1.00 60.53  ? 442 TYR   B CD2 1 
ATOM   1682 C CE1 . TYR   A 1 227 ? -22.733 -17.775 17.003 1.00 62.26  ? 442 TYR   B CE1 1 
ATOM   1683 C CE2 . TYR   A 1 227 ? -20.716 -18.964 17.522 1.00 61.11  ? 442 TYR   B CE2 1 
ATOM   1684 C CZ  . TYR   A 1 227 ? -21.907 -18.880 16.838 1.00 64.83  ? 442 TYR   B CZ  1 
ATOM   1685 O OH  . TYR   A 1 227 ? -22.266 -19.914 16.006 1.00 73.18  ? 442 TYR   B OH  1 
ATOM   1686 N N   . ARG   A 1 228 ? -19.687 -14.867 22.432 1.00 59.15  ? 443 ARG   B N   1 
ATOM   1687 C CA  . ARG   A 1 228 ? -18.958 -13.713 22.982 1.00 59.06  ? 443 ARG   B CA  1 
ATOM   1688 C C   . ARG   A 1 228 ? -18.242 -12.965 21.853 1.00 60.94  ? 443 ARG   B C   1 
ATOM   1689 O O   . ARG   A 1 228 ? -17.695 -13.609 20.961 1.00 60.28  ? 443 ARG   B O   1 
ATOM   1690 C CB  . ARG   A 1 228 ? -17.909 -14.156 24.014 1.00 62.66  ? 443 ARG   B CB  1 
ATOM   1691 C CG  . ARG   A 1 228 ? -18.486 -14.831 25.256 1.00 73.40  ? 443 ARG   B CG  1 
ATOM   1692 C CD  . ARG   A 1 228 ? -17.443 -15.323 26.285 1.00 79.51  ? 443 ARG   B CD  1 
ATOM   1693 N NE  . ARG   A 1 228 ? -16.557 -16.378 25.762 1.00 83.88  ? 443 ARG   B NE  1 
ATOM   1694 C CZ  . ARG   A 1 228 ? -15.290 -16.224 25.347 1.00 85.60  ? 443 ARG   B CZ  1 
ATOM   1695 N NH1 . ARG   A 1 228 ? -14.661 -15.045 25.396 1.00 87.50  ? 443 ARG   B NH1 1 
ATOM   1696 N NH2 . ARG   A 1 228 ? -14.630 -17.279 24.872 1.00 87.42  ? 443 ARG   B NH2 1 
ATOM   1697 N N   . LEU   A 1 229 ? -18.243 -11.624 21.896 1.00 58.78  ? 444 LEU   B N   1 
ATOM   1698 C CA  . LEU   A 1 229 ? -17.434 -10.791 20.985 1.00 55.54  ? 444 LEU   B CA  1 
ATOM   1699 C C   . LEU   A 1 229 ? -16.089 -10.371 21.610 1.00 60.29  ? 444 LEU   B C   1 
ATOM   1700 O O   . LEU   A 1 229 ? -16.044 -9.750  22.691 1.00 51.78  ? 444 LEU   B O   1 
ATOM   1701 C CB  . LEU   A 1 229 ? -18.213 -9.569  20.513 1.00 54.68  ? 444 LEU   B CB  1 
ATOM   1702 C CG  . LEU   A 1 229 ? -19.304 -9.870  19.480 1.00 53.87  ? 444 LEU   B CG  1 
ATOM   1703 C CD1 . LEU   A 1 229 ? -20.237 -8.685  19.296 1.00 52.83  ? 444 LEU   B CD1 1 
ATOM   1704 C CD2 . LEU   A 1 229 ? -18.704 -10.278 18.143 1.00 55.47  ? 444 LEU   B CD2 1 
ATOM   1705 N N   . VAL   A 1 230 ? -14.998 -10.706 20.906 1.00 67.47  ? 445 VAL   B N   1 
ATOM   1706 C CA  . VAL   A 1 230 ? -13.618 -10.565 21.436 1.00 69.52  ? 445 VAL   B CA  1 
ATOM   1707 C C   . VAL   A 1 230 ? -12.691 -9.892  20.438 1.00 71.14  ? 445 VAL   B C   1 
ATOM   1708 O O   . VAL   A 1 230 ? -13.083 -9.621  19.299 1.00 73.38  ? 445 VAL   B O   1 
ATOM   1709 C CB  . VAL   A 1 230 ? -13.006 -11.923 21.835 1.00 66.08  ? 445 VAL   B CB  1 
ATOM   1710 C CG1 . VAL   A 1 230 ? -13.923 -12.658 22.803 1.00 67.15  ? 445 VAL   B CG1 1 
ATOM   1711 C CG2 . VAL   A 1 230 ? -12.702 -12.770 20.608 1.00 62.92  ? 445 VAL   B CG2 1 
ATOM   1712 N N   . ARG   A 1 231 ? -11.468 -9.620  20.888 1.00 78.16  ? 446 ARG   B N   1 
ATOM   1713 C CA  . ARG   A 1 231 ? -10.471 -8.947  20.074 1.00 80.13  ? 446 ARG   B CA  1 
ATOM   1714 C C   . ARG   A 1 231 ? -9.082  -9.139  20.668 1.00 75.56  ? 446 ARG   B C   1 
ATOM   1715 O O   . ARG   A 1 231 ? -8.247  -9.808  20.069 1.00 76.21  ? 446 ARG   B O   1 
ATOM   1716 C CB  . ARG   A 1 231 ? -10.819 -7.462  19.980 1.00 83.36  ? 446 ARG   B CB  1 
ATOM   1717 C CG  . ARG   A 1 231 ? -9.868  -6.651  19.122 1.00 90.61  ? 446 ARG   B CG  1 
ATOM   1718 C CD  . ARG   A 1 231 ? -10.532 -5.405  18.558 1.00 92.07  ? 446 ARG   B CD  1 
ATOM   1719 N NE  . ARG   A 1 231 ? -10.761 -4.380  19.579 1.00 99.54  ? 446 ARG   B NE  1 
ATOM   1720 C CZ  . ARG   A 1 231 ? -11.322 -3.185  19.357 1.00 105.99 ? 446 ARG   B CZ  1 
ATOM   1721 N NH1 . ARG   A 1 231 ? -11.738 -2.835  18.144 1.00 117.76 ? 446 ARG   B NH1 1 
ATOM   1722 N NH2 . ARG   A 1 231 ? -11.473 -2.320  20.357 1.00 103.81 ? 446 ARG   B NH2 1 
ATOM   1723 N N   . GLY   B 1 7   ? -47.270 31.631  26.676 1.00 84.60  ? 222 GLY   A N   1 
ATOM   1724 C CA  . GLY   B 1 7   ? -46.130 30.658  26.730 1.00 82.22  ? 222 GLY   A CA  1 
ATOM   1725 C C   . GLY   B 1 7   ? -46.426 29.332  26.040 1.00 77.56  ? 222 GLY   A C   1 
ATOM   1726 O O   . GLY   B 1 7   ? -47.542 29.100  25.566 1.00 74.67  ? 222 GLY   A O   1 
ATOM   1727 N N   . LEU   B 1 8   ? -45.417 28.470  25.960 1.00 74.34  ? 223 LEU   A N   1 
ATOM   1728 C CA  . LEU   B 1 8   ? -45.632 27.071  25.570 1.00 69.19  ? 223 LEU   A CA  1 
ATOM   1729 C C   . LEU   B 1 8   ? -46.155 26.275  26.774 1.00 63.31  ? 223 LEU   A C   1 
ATOM   1730 O O   . LEU   B 1 8   ? -45.393 25.964  27.700 1.00 56.91  ? 223 LEU   A O   1 
ATOM   1731 C CB  . LEU   B 1 8   ? -44.340 26.446  25.029 1.00 70.38  ? 223 LEU   A CB  1 
ATOM   1732 C CG  . LEU   B 1 8   ? -44.519 25.261  24.069 1.00 73.79  ? 223 LEU   A CG  1 
ATOM   1733 C CD1 . LEU   B 1 8   ? -43.172 24.899  23.470 1.00 76.66  ? 223 LEU   A CD1 1 
ATOM   1734 C CD2 . LEU   B 1 8   ? -45.163 24.054  24.732 1.00 76.36  ? 223 LEU   A CD2 1 
ATOM   1735 N N   . GLY   B 1 9   ? -47.450 25.954  26.745 1.00 62.64  ? 224 GLY   A N   1 
ATOM   1736 C CA  . GLY   B 1 9   ? -48.094 25.231  27.830 1.00 65.20  ? 224 GLY   A CA  1 
ATOM   1737 C C   . GLY   B 1 9   ? -49.610 25.285  27.869 1.00 66.48  ? 224 GLY   A C   1 
ATOM   1738 O O   . GLY   B 1 9   ? -50.244 25.882  27.012 1.00 67.67  ? 224 GLY   A O   1 
ATOM   1739 N N   . THR   B 1 10  ? -50.173 24.618  28.874 1.00 66.14  ? 225 THR   A N   1 
ATOM   1740 C CA  . THR   B 1 10  ? -51.577 24.727  29.247 1.00 64.17  ? 225 THR   A CA  1 
ATOM   1741 C C   . THR   B 1 10  ? -51.668 25.014  30.757 1.00 66.60  ? 225 THR   A C   1 
ATOM   1742 O O   . THR   B 1 10  ? -50.626 25.207  31.433 1.00 65.89  ? 225 THR   A O   1 
ATOM   1743 C CB  . THR   B 1 10  ? -52.302 23.420  28.944 1.00 65.28  ? 225 THR   A CB  1 
ATOM   1744 O OG1 . THR   B 1 10  ? -51.875 22.417  29.872 1.00 65.34  ? 225 THR   A OG1 1 
ATOM   1745 C CG2 . THR   B 1 10  ? -52.006 22.960  27.528 1.00 64.66  ? 225 THR   A CG2 1 
ATOM   1746 N N   . ALA   B 1 11  ? -52.894 25.035  31.287 1.00 62.82  ? 226 ALA   A N   1 
ATOM   1747 C CA  . ALA   B 1 11  ? -53.130 25.062  32.755 1.00 64.43  ? 226 ALA   A CA  1 
ATOM   1748 C C   . ALA   B 1 11  ? -52.403 23.915  33.460 1.00 67.38  ? 226 ALA   A C   1 
ATOM   1749 O O   . ALA   B 1 11  ? -51.740 24.108  34.488 1.00 71.07  ? 226 ALA   A O   1 
ATOM   1750 C CB  . ALA   B 1 11  ? -54.617 24.954  33.055 1.00 64.79  ? 226 ALA   A CB  1 
ATOM   1751 N N   . ARG   B 1 12  ? -52.516 22.728  32.870 1.00 60.42  ? 227 ARG   A N   1 
ATOM   1752 C CA  . ARG   B 1 12  ? -51.999 21.513  33.478 1.00 60.41  ? 227 ARG   A CA  1 
ATOM   1753 C C   . ARG   B 1 12  ? -50.484 21.367  33.468 1.00 54.80  ? 227 ARG   A C   1 
ATOM   1754 O O   . ARG   B 1 12  ? -49.933 20.840  34.422 1.00 55.32  ? 227 ARG   A O   1 
ATOM   1755 C CB  . ARG   B 1 12  ? -52.638 20.287  32.828 1.00 63.53  ? 227 ARG   A CB  1 
ATOM   1756 C CG  . ARG   B 1 12  ? -54.162 20.209  32.977 1.00 64.12  ? 227 ARG   A CG  1 
ATOM   1757 C CD  . ARG   B 1 12  ? -54.687 18.802  32.673 1.00 62.51  ? 227 ARG   A CD  1 
ATOM   1758 N NE  . ARG   B 1 12  ? -54.473 17.799  33.731 1.00 56.95  ? 227 ARG   A NE  1 
ATOM   1759 C CZ  . ARG   B 1 12  ? -54.796 16.508  33.626 1.00 60.62  ? 227 ARG   A CZ  1 
ATOM   1760 N NH1 . ARG   B 1 12  ? -55.333 16.029  32.504 1.00 60.95  ? 227 ARG   A NH1 1 
ATOM   1761 N NH2 . ARG   B 1 12  ? -54.584 15.676  34.647 1.00 63.66  ? 227 ARG   A NH2 1 
ATOM   1762 N N   . LEU   B 1 13  ? -49.820 21.800  32.388 1.00 58.53  ? 228 LEU   A N   1 
ATOM   1763 C CA  . LEU   B 1 13  ? -48.357 21.664  32.238 1.00 47.37  ? 228 LEU   A CA  1 
ATOM   1764 C C   . LEU   B 1 13  ? -47.791 22.761  31.363 1.00 51.11  ? 228 LEU   A C   1 
ATOM   1765 O O   . LEU   B 1 13  ? -48.343 23.072  30.313 1.00 51.09  ? 228 LEU   A O   1 
ATOM   1766 C CB  . LEU   B 1 13  ? -48.035 20.332  31.598 1.00 46.66  ? 228 LEU   A CB  1 
ATOM   1767 C CG  . LEU   B 1 13  ? -46.551 19.918  31.628 1.00 47.85  ? 228 LEU   A CG  1 
ATOM   1768 C CD1 . LEU   B 1 13  ? -46.056 19.585  33.026 1.00 44.73  ? 228 LEU   A CD1 1 
ATOM   1769 C CD2 . LEU   B 1 13  ? -46.356 18.732  30.699 1.00 47.36  ? 228 LEU   A CD2 1 
ATOM   1770 N N   . GLN   B 1 14  ? -46.689 23.349  31.798 1.00 53.33  ? 229 GLN   A N   1 
ATOM   1771 C CA  . GLN   B 1 14  ? -46.028 24.394  31.062 1.00 56.14  ? 229 GLN   A CA  1 
ATOM   1772 C C   . GLN   B 1 14  ? -44.583 23.981  30.917 1.00 62.60  ? 229 GLN   A C   1 
ATOM   1773 O O   . GLN   B 1 14  ? -44.006 23.383  31.849 1.00 54.37  ? 229 GLN   A O   1 
ATOM   1774 C CB  . GLN   B 1 14  ? -46.065 25.733  31.819 1.00 63.41  ? 229 GLN   A CB  1 
ATOM   1775 C CG  . GLN   B 1 14  ? -47.455 26.233  32.226 1.00 73.10  ? 229 GLN   A CG  1 
ATOM   1776 C CD  . GLN   B 1 14  ? -47.864 25.820  33.642 1.00 78.81  ? 229 GLN   A CD  1 
ATOM   1777 O OE1 . GLN   B 1 14  ? -47.070 25.929  34.584 1.00 84.04  ? 229 GLN   A OE1 1 
ATOM   1778 N NE2 . GLN   B 1 14  ? -49.110 25.342  33.797 1.00 74.69  ? 229 GLN   A NE2 1 
ATOM   1779 N N   . LEU   B 1 15  ? -43.998 24.317  29.761 1.00 61.76  ? 230 LEU   A N   1 
ATOM   1780 C CA  . LEU   B 1 15  ? -42.561 24.223  29.582 1.00 62.31  ? 230 LEU   A CA  1 
ATOM   1781 C C   . LEU   B 1 15  ? -41.937 25.415  30.235 1.00 57.87  ? 230 LEU   A C   1 
ATOM   1782 O O   . LEU   B 1 15  ? -42.431 26.498  30.041 1.00 60.40  ? 230 LEU   A O   1 
ATOM   1783 C CB  . LEU   B 1 15  ? -42.202 24.235  28.112 1.00 69.75  ? 230 LEU   A CB  1 
ATOM   1784 C CG  . LEU   B 1 15  ? -40.751 23.805  27.839 1.00 80.21  ? 230 LEU   A CG  1 
ATOM   1785 C CD1 . LEU   B 1 15  ? -40.681 22.861  26.639 1.00 88.77  ? 230 LEU   A CD1 1 
ATOM   1786 C CD2 . LEU   B 1 15  ? -39.832 25.002  27.642 1.00 84.74  ? 230 LEU   A CD2 1 
ATOM   1787 N N   . VAL   B 1 16  ? -40.851 25.217  30.985 1.00 62.16  ? 231 VAL   A N   1 
ATOM   1788 C CA  . VAL   B 1 16  ? -40.123 26.300  31.686 1.00 64.10  ? 231 VAL   A CA  1 
ATOM   1789 C C   . VAL   B 1 16  ? -38.802 26.631  30.976 1.00 68.15  ? 231 VAL   A C   1 
ATOM   1790 O O   . VAL   B 1 16  ? -38.482 27.813  30.778 1.00 74.82  ? 231 VAL   A O   1 
ATOM   1791 C CB  . VAL   B 1 16  ? -39.823 25.983  33.188 1.00 69.12  ? 231 VAL   A CB  1 
ATOM   1792 C CG1 . VAL   B 1 16  ? -39.667 27.276  33.982 1.00 75.19  ? 231 VAL   A CG1 1 
ATOM   1793 C CG2 . VAL   B 1 16  ? -40.923 25.154  33.839 1.00 71.45  ? 231 VAL   A CG2 1 
ATOM   1794 N N   . GLU   B 1 17  ? -38.033 25.592  30.631 1.00 70.04  ? 232 GLU   A N   1 
ATOM   1795 C CA  . GLU   B 1 17  ? -36.798 25.723  29.847 1.00 67.71  ? 232 GLU   A CA  1 
ATOM   1796 C C   . GLU   B 1 17  ? -36.533 24.496  28.993 1.00 63.30  ? 232 GLU   A C   1 
ATOM   1797 O O   . GLU   B 1 17  ? -36.746 23.381  29.428 1.00 58.41  ? 232 GLU   A O   1 
ATOM   1798 C CB  . GLU   B 1 17  ? -35.580 25.956  30.759 1.00 71.37  ? 232 GLU   A CB  1 
ATOM   1799 C CG  . GLU   B 1 17  ? -34.750 27.162  30.338 1.00 78.74  ? 232 GLU   A CG  1 
ATOM   1800 C CD  . GLU   B 1 17  ? -33.881 27.690  31.451 1.00 88.59  ? 232 GLU   A CD  1 
ATOM   1801 O OE1 . GLU   B 1 17  ? -34.437 28.284  32.416 1.00 96.43  ? 232 GLU   A OE1 1 
ATOM   1802 O OE2 . GLU   B 1 17  ? -32.648 27.525  31.342 1.00 85.62  ? 232 GLU   A OE2 1 
ATOM   1803 N N   . PHE   B 1 18  ? -36.043 24.721  27.777 1.00 64.94  ? 233 PHE   A N   1 
ATOM   1804 C CA  . PHE   B 1 18  ? -35.604 23.643  26.897 1.00 62.98  ? 233 PHE   A CA  1 
ATOM   1805 C C   . PHE   B 1 18  ? -34.277 24.013  26.237 1.00 65.07  ? 233 PHE   A C   1 
ATOM   1806 O O   . PHE   B 1 18  ? -34.126 25.106  25.699 1.00 60.83  ? 233 PHE   A O   1 
ATOM   1807 C CB  . PHE   B 1 18  ? -36.653 23.319  25.820 1.00 60.13  ? 233 PHE   A CB  1 
ATOM   1808 C CG  . PHE   B 1 18  ? -36.159 22.336  24.812 1.00 61.38  ? 233 PHE   A CG  1 
ATOM   1809 C CD1 . PHE   B 1 18  ? -36.063 20.997  25.147 1.00 60.50  ? 233 PHE   A CD1 1 
ATOM   1810 C CD2 . PHE   B 1 18  ? -35.709 22.755  23.551 1.00 61.00  ? 233 PHE   A CD2 1 
ATOM   1811 C CE1 . PHE   B 1 18  ? -35.568 20.077  24.233 1.00 64.90  ? 233 PHE   A CE1 1 
ATOM   1812 C CE2 . PHE   B 1 18  ? -35.212 21.837  22.638 1.00 60.30  ? 233 PHE   A CE2 1 
ATOM   1813 C CZ  . PHE   B 1 18  ? -35.137 20.501  22.978 1.00 60.28  ? 233 PHE   A CZ  1 
ATOM   1814 N N   . SER   B 1 19  ? -33.359 23.054  26.214 1.00 64.17  ? 234 SER   A N   1 
ATOM   1815 C CA  . SER   B 1 19  ? -32.003 23.283  25.772 1.00 67.23  ? 234 SER   A CA  1 
ATOM   1816 C C   . SER   B 1 19  ? -31.450 22.055  24.994 1.00 61.95  ? 234 SER   A C   1 
ATOM   1817 O O   . SER   B 1 19  ? -31.627 20.905  25.414 1.00 49.15  ? 234 SER   A O   1 
ATOM   1818 C CB  . SER   B 1 19  ? -31.159 23.562  27.025 1.00 69.84  ? 234 SER   A CB  1 
ATOM   1819 O OG  . SER   B 1 19  ? -30.087 24.430  26.752 1.00 75.46  ? 234 SER   A OG  1 
ATOM   1820 N N   . ALA   B 1 20  ? -30.778 22.301  23.874 1.00 57.15  ? 235 ALA   A N   1 
ATOM   1821 C CA  . ALA   B 1 20  ? -29.982 21.251  23.224 1.00 56.21  ? 235 ALA   A CA  1 
ATOM   1822 C C   . ALA   B 1 20  ? -28.609 21.830  23.077 1.00 50.66  ? 235 ALA   A C   1 
ATOM   1823 O O   . ALA   B 1 20  ? -28.467 22.956  22.583 1.00 47.19  ? 235 ALA   A O   1 
ATOM   1824 C CB  . ALA   B 1 20  ? -30.571 20.873  21.879 1.00 55.05  ? 235 ALA   A CB  1 
ATOM   1825 N N   . PHE   B 1 21  ? -27.606 21.081  23.511 1.00 48.70  ? 236 PHE   A N   1 
ATOM   1826 C CA  . PHE   B 1 21  ? -26.282 21.672  23.707 1.00 55.76  ? 236 PHE   A CA  1 
ATOM   1827 C C   . PHE   B 1 21  ? -25.139 20.701  23.532 1.00 55.23  ? 236 PHE   A C   1 
ATOM   1828 O O   . PHE   B 1 21  ? -25.339 19.475  23.479 1.00 60.25  ? 236 PHE   A O   1 
ATOM   1829 C CB  . PHE   B 1 21  ? -26.188 22.290  25.113 1.00 59.65  ? 236 PHE   A CB  1 
ATOM   1830 C CG  . PHE   B 1 21  ? -26.445 21.308  26.201 1.00 62.50  ? 236 PHE   A CG  1 
ATOM   1831 C CD1 . PHE   B 1 21  ? -25.425 20.532  26.704 1.00 66.19  ? 236 PHE   A CD1 1 
ATOM   1832 C CD2 . PHE   B 1 21  ? -27.730 21.121  26.684 1.00 70.07  ? 236 PHE   A CD2 1 
ATOM   1833 C CE1 . PHE   B 1 21  ? -25.679 19.597  27.687 1.00 71.21  ? 236 PHE   A CE1 1 
ATOM   1834 C CE2 . PHE   B 1 21  ? -27.991 20.185  27.670 1.00 65.69  ? 236 PHE   A CE2 1 
ATOM   1835 C CZ  . PHE   B 1 21  ? -26.964 19.430  28.174 1.00 66.72  ? 236 PHE   A CZ  1 
ATOM   1836 N N   . VAL   B 1 22  ? -23.940 21.267  23.454 1.00 54.89  ? 237 VAL   A N   1 
ATOM   1837 C CA  . VAL   B 1 22  ? -22.688 20.491  23.515 1.00 62.83  ? 237 VAL   A CA  1 
ATOM   1838 C C   . VAL   B 1 22  ? -21.671 21.204  24.397 1.00 64.52  ? 237 VAL   A C   1 
ATOM   1839 O O   . VAL   B 1 22  ? -21.666 22.445  24.490 1.00 67.26  ? 237 VAL   A O   1 
ATOM   1840 C CB  . VAL   B 1 22  ? -22.084 20.195  22.095 1.00 62.69  ? 237 VAL   A CB  1 
ATOM   1841 C CG1 . VAL   B 1 22  ? -21.670 21.459  21.346 1.00 58.75  ? 237 VAL   A CG1 1 
ATOM   1842 C CG2 . VAL   B 1 22  ? -20.884 19.246  22.185 1.00 65.40  ? 237 VAL   A CG2 1 
ATOM   1843 N N   . GLU   B 1 23  ? -20.797 20.429  25.023 1.00 75.06  ? 238 GLU   A N   1 
ATOM   1844 C CA  . GLU   B 1 23  ? -19.762 20.998  25.893 1.00 92.40  ? 238 GLU   A CA  1 
ATOM   1845 C C   . GLU   B 1 23  ? -18.489 20.141  25.895 1.00 98.13  ? 238 GLU   A C   1 
ATOM   1846 O O   . GLU   B 1 23  ? -18.573 18.916  25.750 1.00 99.49  ? 238 GLU   A O   1 
ATOM   1847 C CB  . GLU   B 1 23  ? -20.323 21.127  27.305 1.00 97.37  ? 238 GLU   A CB  1 
ATOM   1848 C CG  . GLU   B 1 23  ? -21.014 19.847  27.752 1.00 100.19 ? 238 GLU   A CG  1 
ATOM   1849 C CD  . GLU   B 1 23  ? -21.618 19.935  29.124 1.00 97.39  ? 238 GLU   A CD  1 
ATOM   1850 O OE1 . GLU   B 1 23  ? -21.636 18.887  29.794 1.00 88.87  ? 238 GLU   A OE1 1 
ATOM   1851 O OE2 . GLU   B 1 23  ? -22.097 21.023  29.523 1.00 100.57 ? 238 GLU   A OE2 1 
ATOM   1852 N N   . PRO   B 1 24  ? -17.312 20.778  26.075 1.00 103.33 ? 239 PRO   A N   1 
ATOM   1853 C CA  . PRO   B 1 24  ? -16.044 20.051  25.960 1.00 103.70 ? 239 PRO   A CA  1 
ATOM   1854 C C   . PRO   B 1 24  ? -15.764 19.124  27.149 1.00 97.33  ? 239 PRO   A C   1 
ATOM   1855 O O   . PRO   B 1 24  ? -15.381 17.971  26.951 1.00 86.94  ? 239 PRO   A O   1 
ATOM   1856 C CB  . PRO   B 1 24  ? -15.013 21.180  25.889 1.00 108.42 ? 239 PRO   A CB  1 
ATOM   1857 C CG  . PRO   B 1 24  ? -15.623 22.295  26.677 1.00 106.84 ? 239 PRO   A CG  1 
ATOM   1858 C CD  . PRO   B 1 24  ? -17.108 22.189  26.472 1.00 104.40 ? 239 PRO   A CD  1 
ATOM   1859 N N   . ARG   B 1 33  ? -20.352 25.140  27.450 1.00 81.82  ? 248 ARG   A N   1 
ATOM   1860 C CA  . ARG   B 1 33  ? -21.708 24.935  26.939 1.00 83.87  ? 248 ARG   A CA  1 
ATOM   1861 C C   . ARG   B 1 33  ? -22.009 25.759  25.685 1.00 85.39  ? 248 ARG   A C   1 
ATOM   1862 O O   . ARG   B 1 33  ? -22.099 26.991  25.756 1.00 77.48  ? 248 ARG   A O   1 
ATOM   1863 C CB  . ARG   B 1 33  ? -22.766 25.283  28.000 1.00 87.73  ? 248 ARG   A CB  1 
ATOM   1864 C CG  . ARG   B 1 33  ? -23.305 24.089  28.765 1.00 96.69  ? 248 ARG   A CG  1 
ATOM   1865 C CD  . ARG   B 1 33  ? -24.805 24.195  29.007 1.00 99.53  ? 248 ARG   A CD  1 
ATOM   1866 N NE  . ARG   B 1 33  ? -25.299 23.042  29.774 1.00 106.88 ? 248 ARG   A NE  1 
ATOM   1867 C CZ  . ARG   B 1 33  ? -26.586 22.756  30.018 1.00 111.45 ? 248 ARG   A CZ  1 
ATOM   1868 N NH1 . ARG   B 1 33  ? -27.572 23.533  29.557 1.00 111.44 ? 248 ARG   A NH1 1 
ATOM   1869 N NH2 . ARG   B 1 33  ? -26.896 21.672  30.735 1.00 109.38 ? 248 ARG   A NH2 1 
ATOM   1870 N N   . HIS   B 1 34  ? -22.185 25.076  24.548 1.00 75.68  ? 249 HIS   A N   1 
ATOM   1871 C CA  . HIS   B 1 34  ? -22.753 25.700  23.350 1.00 77.32  ? 249 HIS   A CA  1 
ATOM   1872 C C   . HIS   B 1 34  ? -24.196 25.224  23.166 1.00 72.67  ? 249 HIS   A C   1 
ATOM   1873 O O   . HIS   B 1 34  ? -24.473 24.039  23.198 1.00 74.10  ? 249 HIS   A O   1 
ATOM   1874 C CB  . HIS   B 1 34  ? -21.945 25.377  22.079 1.00 80.83  ? 249 HIS   A CB  1 
ATOM   1875 C CG  . HIS   B 1 34  ? -22.484 26.050  20.854 1.00 75.91  ? 249 HIS   A CG  1 
ATOM   1876 N ND1 . HIS   B 1 34  ? -23.472 25.488  20.077 1.00 72.21  ? 249 HIS   A ND1 1 
ATOM   1877 C CD2 . HIS   B 1 34  ? -22.221 27.264  20.313 1.00 76.67  ? 249 HIS   A CD2 1 
ATOM   1878 C CE1 . HIS   B 1 34  ? -23.775 26.319  19.095 1.00 72.05  ? 249 HIS   A CE1 1 
ATOM   1879 N NE2 . HIS   B 1 34  ? -23.032 27.404  19.213 1.00 71.45  ? 249 HIS   A NE2 1 
ATOM   1880 N N   . LEU   B 1 35  ? -25.089 26.166  22.922 1.00 64.16  ? 250 LEU   A N   1 
ATOM   1881 C CA  . LEU   B 1 35  ? -26.503 25.904  22.812 1.00 60.39  ? 250 LEU   A CA  1 
ATOM   1882 C C   . LEU   B 1 35  ? -26.870 25.940  21.348 1.00 56.00  ? 250 LEU   A C   1 
ATOM   1883 O O   . LEU   B 1 35  ? -26.673 26.951  20.677 1.00 55.32  ? 250 LEU   A O   1 
ATOM   1884 C CB  . LEU   B 1 35  ? -27.292 26.968  23.591 1.00 59.06  ? 250 LEU   A CB  1 
ATOM   1885 C CG  . LEU   B 1 35  ? -26.796 27.190  25.036 1.00 59.43  ? 250 LEU   A CG  1 
ATOM   1886 C CD1 . LEU   B 1 35  ? -27.496 28.396  25.657 1.00 60.86  ? 250 LEU   A CD1 1 
ATOM   1887 C CD2 . LEU   B 1 35  ? -26.945 25.934  25.879 1.00 57.74  ? 250 LEU   A CD2 1 
ATOM   1888 N N   . PHE   B 1 36  ? -27.385 24.837  20.828 1.00 52.70  ? 251 PHE   A N   1 
ATOM   1889 C CA  . PHE   B 1 36  ? -27.811 24.823  19.427 1.00 52.52  ? 251 PHE   A CA  1 
ATOM   1890 C C   . PHE   B 1 36  ? -29.140 25.496  19.371 1.00 54.40  ? 251 PHE   A C   1 
ATOM   1891 O O   . PHE   B 1 36  ? -29.392 26.297  18.473 1.00 56.08  ? 251 PHE   A O   1 
ATOM   1892 C CB  . PHE   B 1 36  ? -27.953 23.422  18.879 1.00 55.01  ? 251 PHE   A CB  1 
ATOM   1893 C CG  . PHE   B 1 36  ? -26.736 22.573  19.074 1.00 55.53  ? 251 PHE   A CG  1 
ATOM   1894 C CD1 . PHE   B 1 36  ? -25.561 22.875  18.415 1.00 54.15  ? 251 PHE   A CD1 1 
ATOM   1895 C CD2 . PHE   B 1 36  ? -26.769 21.476  19.908 1.00 51.62  ? 251 PHE   A CD2 1 
ATOM   1896 C CE1 . PHE   B 1 36  ? -24.436 22.086  18.584 1.00 55.13  ? 251 PHE   A CE1 1 
ATOM   1897 C CE2 . PHE   B 1 36  ? -25.645 20.691  20.091 1.00 56.75  ? 251 PHE   A CE2 1 
ATOM   1898 C CZ  . PHE   B 1 36  ? -24.473 20.996  19.422 1.00 58.01  ? 251 PHE   A CZ  1 
ATOM   1899 N N   . VAL   B 1 37  ? -29.988 25.146  20.342 1.00 57.78  ? 252 VAL   A N   1 
ATOM   1900 C CA  . VAL   B 1 37  ? -31.223 25.877  20.614 1.00 60.52  ? 252 VAL   A CA  1 
ATOM   1901 C C   . VAL   B 1 37  ? -31.474 26.033  22.129 1.00 58.69  ? 252 VAL   A C   1 
ATOM   1902 O O   . VAL   B 1 37  ? -30.931 25.292  22.951 1.00 58.71  ? 252 VAL   A O   1 
ATOM   1903 C CB  . VAL   B 1 37  ? -32.441 25.225  19.907 1.00 61.47  ? 252 VAL   A CB  1 
ATOM   1904 C CG1 . VAL   B 1 37  ? -32.236 25.176  18.396 1.00 63.31  ? 252 VAL   A CG1 1 
ATOM   1905 C CG2 . VAL   B 1 37  ? -32.734 23.840  20.453 1.00 57.79  ? 252 VAL   A CG2 1 
ATOM   1906 N N   . HIS   B 1 38  ? -32.321 27.000  22.463 1.00 62.25  ? 253 HIS   A N   1 
ATOM   1907 C CA  . HIS   B 1 38  ? -32.577 27.403  23.848 1.00 66.22  ? 253 HIS   A CA  1 
ATOM   1908 C C   . HIS   B 1 38  ? -33.930 28.124  23.908 1.00 64.10  ? 253 HIS   A C   1 
ATOM   1909 O O   . HIS   B 1 38  ? -34.140 29.117  23.218 1.00 63.69  ? 253 HIS   A O   1 
ATOM   1910 C CB  . HIS   B 1 38  ? -31.427 28.302  24.365 1.00 69.58  ? 253 HIS   A CB  1 
ATOM   1911 C CG  . HIS   B 1 38  ? -31.545 28.714  25.807 1.00 81.00  ? 253 HIS   A CG  1 
ATOM   1912 N ND1 . HIS   B 1 38  ? -32.006 27.871  26.799 1.00 85.74  ? 253 HIS   A ND1 1 
ATOM   1913 C CD2 . HIS   B 1 38  ? -31.218 29.874  26.427 1.00 86.25  ? 253 HIS   A CD2 1 
ATOM   1914 C CE1 . HIS   B 1 38  ? -31.984 28.499  27.960 1.00 83.46  ? 253 HIS   A CE1 1 
ATOM   1915 N NE2 . HIS   B 1 38  ? -31.509 29.716  27.761 1.00 89.72  ? 253 HIS   A NE2 1 
ATOM   1916 N N   . ILE   B 1 39  ? -34.860 27.576  24.685 1.00 60.75  ? 254 ILE   A N   1 
ATOM   1917 C CA  . ILE   B 1 39  ? -36.028 28.322  25.129 1.00 63.94  ? 254 ILE   A CA  1 
ATOM   1918 C C   . ILE   B 1 39  ? -35.921 28.558  26.637 1.00 70.04  ? 254 ILE   A C   1 
ATOM   1919 O O   . ILE   B 1 39  ? -35.702 27.603  27.390 1.00 69.46  ? 254 ILE   A O   1 
ATOM   1920 C CB  . ILE   B 1 39  ? -37.326 27.569  24.853 1.00 54.92  ? 254 ILE   A CB  1 
ATOM   1921 C CG1 . ILE   B 1 39  ? -37.523 27.398  23.349 1.00 50.72  ? 254 ILE   A CG1 1 
ATOM   1922 C CG2 . ILE   B 1 39  ? -38.502 28.317  25.496 1.00 56.82  ? 254 ILE   A CG2 1 
ATOM   1923 C CD1 . ILE   B 1 39  ? -38.577 26.365  22.983 1.00 47.34  ? 254 ILE   A CD1 1 
ATOM   1924 N N   . SER   B 1 40  ? -36.055 29.819  27.066 1.00 76.85  ? 255 SER   A N   1 
ATOM   1925 C CA  . SER   B 1 40  ? -36.224 30.147  28.494 1.00 80.66  ? 255 SER   A CA  1 
ATOM   1926 C C   . SER   B 1 40  ? -37.435 31.019  28.681 1.00 80.42  ? 255 SER   A C   1 
ATOM   1927 O O   . SER   B 1 40  ? -37.728 31.859  27.840 1.00 85.67  ? 255 SER   A O   1 
ATOM   1928 C CB  . SER   B 1 40  ? -34.997 30.830  29.087 1.00 84.65  ? 255 SER   A CB  1 
ATOM   1929 O OG  . SER   B 1 40  ? -35.034 30.720  30.503 1.00 87.23  ? 255 SER   A OG  1 
ATOM   1930 N N   . GLN   B 1 41  ? -38.146 30.804  29.783 1.00 91.83  ? 256 GLN   A N   1 
ATOM   1931 C CA  . GLN   B 1 41  ? -39.433 31.464  30.026 1.00 98.21  ? 256 GLN   A CA  1 
ATOM   1932 C C   . GLN   B 1 41  ? -39.574 31.867  31.496 1.00 91.47  ? 256 GLN   A C   1 
ATOM   1933 O O   . GLN   B 1 41  ? -39.605 31.011  32.379 1.00 88.48  ? 256 GLN   A O   1 
ATOM   1934 C CB  . GLN   B 1 41  ? -40.595 30.543  29.569 1.00 89.97  ? 256 GLN   A CB  1 
ATOM   1935 C CG  . GLN   B 1 41  ? -40.437 29.988  28.145 1.00 81.54  ? 256 GLN   A CG  1 
ATOM   1936 C CD  . GLN   B 1 41  ? -41.747 29.749  27.392 1.00 77.40  ? 256 GLN   A CD  1 
ATOM   1937 O OE1 . GLN   B 1 41  ? -41.952 30.286  26.306 1.00 76.59  ? 256 GLN   A OE1 1 
ATOM   1938 N NE2 . GLN   B 1 41  ? -42.616 28.935  27.948 1.00 75.38  ? 256 GLN   A NE2 1 
ATOM   1939 N N   . PRO   B 1 49  ? -48.020 39.071  25.036 1.00 110.89 ? 264 PRO   A N   1 
ATOM   1940 C CA  . PRO   B 1 49  ? -48.920 39.011  23.863 1.00 117.02 ? 264 PRO   A CA  1 
ATOM   1941 C C   . PRO   B 1 49  ? -49.385 37.572  23.500 1.00 121.47 ? 264 PRO   A C   1 
ATOM   1942 O O   . PRO   B 1 49  ? -48.620 36.635  23.724 1.00 124.44 ? 264 PRO   A O   1 
ATOM   1943 C CB  . PRO   B 1 49  ? -48.057 39.605  22.742 1.00 114.33 ? 264 PRO   A CB  1 
ATOM   1944 C CG  . PRO   B 1 49  ? -46.642 39.320  23.153 1.00 111.08 ? 264 PRO   A CG  1 
ATOM   1945 C CD  . PRO   B 1 49  ? -46.611 39.298  24.658 1.00 111.50 ? 264 PRO   A CD  1 
ATOM   1946 N N   . PRO   B 1 50  ? -50.615 37.392  22.934 1.00 121.22 ? 265 PRO   A N   1 
ATOM   1947 C CA  . PRO   B 1 50  ? -51.081 36.024  22.595 1.00 120.24 ? 265 PRO   A CA  1 
ATOM   1948 C C   . PRO   B 1 50  ? -50.337 35.411  21.399 1.00 119.87 ? 265 PRO   A C   1 
ATOM   1949 O O   . PRO   B 1 50  ? -50.033 36.132  20.449 1.00 128.78 ? 265 PRO   A O   1 
ATOM   1950 C CB  . PRO   B 1 50  ? -52.574 36.214  22.253 1.00 119.15 ? 265 PRO   A CB  1 
ATOM   1951 C CG  . PRO   B 1 50  ? -52.885 37.655  22.490 1.00 121.70 ? 265 PRO   A CG  1 
ATOM   1952 C CD  . PRO   B 1 50  ? -51.587 38.406  22.490 1.00 122.41 ? 265 PRO   A CD  1 
ATOM   1953 N N   . LEU   B 1 51  ? -50.068 34.102  21.447 1.00 111.78 ? 266 LEU   A N   1 
ATOM   1954 C CA  . LEU   B 1 51  ? -49.264 33.411  20.413 1.00 106.11 ? 266 LEU   A CA  1 
ATOM   1955 C C   . LEU   B 1 51  ? -49.953 33.327  19.054 1.00 100.36 ? 266 LEU   A C   1 
ATOM   1956 O O   . LEU   B 1 51  ? -51.147 33.014  18.987 1.00 93.61  ? 266 LEU   A O   1 
ATOM   1957 C CB  . LEU   B 1 51  ? -48.932 31.974  20.833 1.00 100.68 ? 266 LEU   A CB  1 
ATOM   1958 C CG  . LEU   B 1 51  ? -48.061 31.778  22.066 1.00 97.89  ? 266 LEU   A CG  1 
ATOM   1959 C CD1 . LEU   B 1 51  ? -48.061 30.298  22.418 1.00 96.04  ? 266 LEU   A CD1 1 
ATOM   1960 C CD2 . LEU   B 1 51  ? -46.652 32.322  21.858 1.00 94.02  ? 266 LEU   A CD2 1 
ATOM   1961 N N   . GLU   B 1 52  ? -49.184 33.569  17.985 1.00 94.96  ? 267 GLU   A N   1 
ATOM   1962 C CA  . GLU   B 1 52  ? -49.694 33.458  16.618 1.00 87.76  ? 267 GLU   A CA  1 
ATOM   1963 C C   . GLU   B 1 52  ? -50.159 32.027  16.376 1.00 81.56  ? 267 GLU   A C   1 
ATOM   1964 O O   . GLU   B 1 52  ? -49.465 31.089  16.723 1.00 82.17  ? 267 GLU   A O   1 
ATOM   1965 C CB  . GLU   B 1 52  ? -48.631 33.838  15.581 1.00 89.39  ? 267 GLU   A CB  1 
ATOM   1966 C CG  . GLU   B 1 52  ? -48.271 35.325  15.518 1.00 90.44  ? 267 GLU   A CG  1 
ATOM   1967 C CD  . GLU   B 1 52  ? -47.394 35.668  14.319 1.00 91.64  ? 267 GLU   A CD  1 
ATOM   1968 O OE1 . GLU   B 1 52  ? -47.419 34.925  13.306 1.00 80.50  ? 267 GLU   A OE1 1 
ATOM   1969 O OE2 . GLU   B 1 52  ? -46.671 36.685  14.388 1.00 98.13  ? 267 GLU   A OE2 1 
ATOM   1970 N N   . SER   B 1 53  ? -51.354 31.884  15.818 1.00 74.56  ? 268 SER   A N   1 
ATOM   1971 C CA  . SER   B 1 53  ? -51.900 30.612  15.413 1.00 68.58  ? 268 SER   A CA  1 
ATOM   1972 C C   . SER   B 1 53  ? -51.163 30.059  14.180 1.00 74.69  ? 268 SER   A C   1 
ATOM   1973 O O   . SER   B 1 53  ? -50.535 30.813  13.452 1.00 76.63  ? 268 SER   A O   1 
ATOM   1974 C CB  . SER   B 1 53  ? -53.384 30.802  15.092 1.00 74.12  ? 268 SER   A CB  1 
ATOM   1975 O OG  . SER   B 1 53  ? -53.982 29.592  14.669 1.00 82.25  ? 268 SER   A OG  1 
ATOM   1976 N N   . VAL   B 1 54  ? -51.219 28.738  13.976 1.00 76.10  ? 269 VAL   A N   1 
ATOM   1977 C CA  . VAL   B 1 54  ? -50.801 28.079  12.721 1.00 72.31  ? 269 VAL   A CA  1 
ATOM   1978 C C   . VAL   B 1 54  ? -51.689 26.853  12.504 1.00 82.11  ? 269 VAL   A C   1 
ATOM   1979 O O   . VAL   B 1 54  ? -52.014 26.128  13.460 1.00 78.52  ? 269 VAL   A O   1 
ATOM   1980 C CB  . VAL   B 1 54  ? -49.318 27.620  12.717 1.00 69.24  ? 269 VAL   A CB  1 
ATOM   1981 C CG1 . VAL   B 1 54  ? -49.042 26.673  11.551 1.00 67.30  ? 269 VAL   A CG1 1 
ATOM   1982 C CG2 . VAL   B 1 54  ? -48.356 28.809  12.639 1.00 68.47  ? 269 VAL   A CG2 1 
ATOM   1983 N N   . ASP   B 1 55  ? -52.070 26.620  11.247 1.00 86.48  ? 270 ASP   A N   1 
ATOM   1984 C CA  . ASP   B 1 55  ? -52.991 25.537  10.929 1.00 88.54  ? 270 ASP   A CA  1 
ATOM   1985 C C   . ASP   B 1 55  ? -52.269 24.199  10.839 1.00 84.06  ? 270 ASP   A C   1 
ATOM   1986 O O   . ASP   B 1 55  ? -51.291 24.053  10.113 1.00 87.25  ? 270 ASP   A O   1 
ATOM   1987 C CB  . ASP   B 1 55  ? -53.737 25.805  9.632  1.00 92.61  ? 270 ASP   A CB  1 
ATOM   1988 C CG  . ASP   B 1 55  ? -54.726 24.715  9.316  1.00 96.93  ? 270 ASP   A CG  1 
ATOM   1989 O OD1 . ASP   B 1 55  ? -54.305 23.728  8.696  1.00 101.89 ? 270 ASP   A OD1 1 
ATOM   1990 O OD2 . ASP   B 1 55  ? -55.907 24.824  9.711  1.00 101.14 ? 270 ASP   A OD2 1 
ATOM   1991 N N   . VAL   B 1 56  ? -52.786 23.223  11.566 1.00 72.92  ? 271 VAL   A N   1 
ATOM   1992 C CA  . VAL   B 1 56  ? -52.187 21.915  11.613 1.00 71.57  ? 271 VAL   A CA  1 
ATOM   1993 C C   . VAL   B 1 56  ? -52.170 21.219  10.229 1.00 83.22  ? 271 VAL   A C   1 
ATOM   1994 O O   . VAL   B 1 56  ? -51.183 20.555  9.908  1.00 92.34  ? 271 VAL   A O   1 
ATOM   1995 C CB  . VAL   B 1 56  ? -52.833 21.051  12.737 1.00 67.55  ? 271 VAL   A CB  1 
ATOM   1996 C CG1 . VAL   B 1 56  ? -54.240 20.611  12.385 1.00 68.33  ? 271 VAL   A CG1 1 
ATOM   1997 C CG2 . VAL   B 1 56  ? -51.977 19.840  13.056 1.00 67.30  ? 271 VAL   A CG2 1 
ATOM   1998 N N   . ARG   B 1 57  ? -53.203 21.394  9.393  1.00 93.57  ? 272 ARG   A N   1 
ATOM   1999 C CA  . ARG   B 1 57  ? -53.208 20.785  8.024  1.00 96.13  ? 272 ARG   A CA  1 
ATOM   2000 C C   . ARG   B 1 57  ? -51.897 21.094  7.313  1.00 92.21  ? 272 ARG   A C   1 
ATOM   2001 O O   . ARG   B 1 57  ? -51.316 20.242  6.646  1.00 92.52  ? 272 ARG   A O   1 
ATOM   2002 C CB  . ARG   B 1 57  ? -54.361 21.279  7.131  1.00 97.47  ? 272 ARG   A CB  1 
ATOM   2003 C CG  . ARG   B 1 57  ? -55.782 21.041  7.648  1.00 106.09 ? 272 ARG   A CG  1 
ATOM   2004 C CD  . ARG   B 1 57  ? -56.807 21.962  6.975  1.00 112.47 ? 272 ARG   A CD  1 
ATOM   2005 N NE  . ARG   B 1 57  ? -57.244 23.060  7.855  1.00 116.14 ? 272 ARG   A NE  1 
ATOM   2006 C CZ  . ARG   B 1 57  ? -58.348 23.068  8.619  1.00 117.20 ? 272 ARG   A CZ  1 
ATOM   2007 N NH1 . ARG   B 1 57  ? -59.200 22.039  8.643  1.00 120.62 ? 272 ARG   A NH1 1 
ATOM   2008 N NH2 . ARG   B 1 57  ? -58.610 24.130  9.385  1.00 108.80 ? 272 ARG   A NH2 1 
ATOM   2009 N N   . GLN   B 1 58  ? -51.424 22.317  7.510  1.00 95.94  ? 273 GLN   A N   1 
ATOM   2010 C CA  . GLN   B 1 58  ? -50.173 22.793  6.934  1.00 102.47 ? 273 GLN   A CA  1 
ATOM   2011 C C   . GLN   B 1 58  ? -48.872 21.982  7.197  1.00 103.15 ? 273 GLN   A C   1 
ATOM   2012 O O   . GLN   B 1 58  ? -47.875 22.233  6.524  1.00 106.42 ? 273 GLN   A O   1 
ATOM   2013 C CB  . GLN   B 1 58  ? -49.956 24.241  7.372  1.00 100.65 ? 273 GLN   A CB  1 
ATOM   2014 C CG  . GLN   B 1 58  ? -48.864 24.948  6.603  1.00 107.07 ? 273 GLN   A CG  1 
ATOM   2015 C CD  . GLN   B 1 58  ? -49.089 26.422  6.492  1.00 101.26 ? 273 GLN   A CD  1 
ATOM   2016 O OE1 . GLN   B 1 58  ? -50.224 26.892  6.523  1.00 100.43 ? 273 GLN   A OE1 1 
ATOM   2017 N NE2 . GLN   B 1 58  ? -48.004 27.166  6.345  1.00 102.83 ? 273 GLN   A NE2 1 
ATOM   2018 N N   . ILE   B 1 59  ? -48.848 21.042  8.147  1.00 95.41  ? 274 ILE   A N   1 
ATOM   2019 C CA  . ILE   B 1 59  ? -47.621 20.260  8.404  1.00 91.42  ? 274 ILE   A CA  1 
ATOM   2020 C C   . ILE   B 1 59  ? -47.811 18.737  8.584  1.00 93.46  ? 274 ILE   A C   1 
ATOM   2021 O O   . ILE   B 1 59  ? -46.936 18.098  9.173  1.00 89.74  ? 274 ILE   A O   1 
ATOM   2022 C CB  . ILE   B 1 59  ? -46.844 20.843  9.619  1.00 88.57  ? 274 ILE   A CB  1 
ATOM   2023 C CG1 . ILE   B 1 59  ? -47.670 20.702  10.912 1.00 86.28  ? 274 ILE   A CG1 1 
ATOM   2024 C CG2 . ILE   B 1 59  ? -46.461 22.297  9.369  1.00 80.64  ? 274 ILE   A CG2 1 
ATOM   2025 C CD1 . ILE   B 1 59  ? -46.970 21.194  12.156 1.00 85.40  ? 274 ILE   A CD1 1 
ATOM   2026 N N   . TYR   B 1 60  ? -48.920 18.166  8.078  1.00 103.69 ? 275 TYR   A N   1 
ATOM   2027 C CA  . TYR   B 1 60  ? -49.155 16.683  8.047  1.00 113.27 ? 275 TYR   A CA  1 
ATOM   2028 C C   . TYR   B 1 60  ? -48.046 15.984  7.257  1.00 117.70 ? 275 TYR   A C   1 
ATOM   2029 O O   . TYR   B 1 60  ? -47.529 14.926  7.653  1.00 106.81 ? 275 TYR   A O   1 
ATOM   2030 C CB  . TYR   B 1 60  ? -50.493 16.339  7.358  1.00 119.58 ? 275 TYR   A CB  1 
ATOM   2031 C CG  . TYR   B 1 60  ? -51.769 16.530  8.159  1.00 118.63 ? 275 TYR   A CG  1 
ATOM   2032 C CD1 . TYR   B 1 60  ? -51.831 17.408  9.252  1.00 113.57 ? 275 TYR   A CD1 1 
ATOM   2033 C CD2 . TYR   B 1 60  ? -52.941 15.847  7.795  1.00 116.43 ? 275 TYR   A CD2 1 
ATOM   2034 C CE1 . TYR   B 1 60  ? -53.008 17.580  9.965  1.00 108.44 ? 275 TYR   A CE1 1 
ATOM   2035 C CE2 . TYR   B 1 60  ? -54.123 16.025  8.503  1.00 112.90 ? 275 TYR   A CE2 1 
ATOM   2036 C CZ  . TYR   B 1 60  ? -54.147 16.890  9.588  1.00 108.63 ? 275 TYR   A CZ  1 
ATOM   2037 O OH  . TYR   B 1 60  ? -55.299 17.077  10.305 1.00 96.35  ? 275 TYR   A OH  1 
ATOM   2038 N N   . ASP   B 1 61  ? -47.762 16.594  6.102  1.00 119.78 ? 276 ASP   A N   1 
ATOM   2039 C CA  . ASP   B 1 61  ? -46.549 16.423  5.291  1.00 117.65 ? 276 ASP   A CA  1 
ATOM   2040 C C   . ASP   B 1 61  ? -45.285 15.983  6.063  1.00 114.00 ? 276 ASP   A C   1 
ATOM   2041 O O   . ASP   B 1 61  ? -44.635 15.008  5.677  1.00 113.79 ? 276 ASP   A O   1 
ATOM   2042 C CB  . ASP   B 1 61  ? -46.295 17.767  4.563  1.00 116.78 ? 276 ASP   A CB  1 
ATOM   2043 C CG  . ASP   B 1 61  ? -45.065 17.755  3.679  1.00 124.08 ? 276 ASP   A CG  1 
ATOM   2044 O OD1 . ASP   B 1 61  ? -44.870 16.783  2.921  1.00 130.61 ? 276 ASP   A OD1 1 
ATOM   2045 O OD2 . ASP   B 1 61  ? -44.300 18.742  3.728  1.00 128.05 ? 276 ASP   A OD2 1 
ATOM   2046 N N   . LYS   B 1 62  ? -44.974 16.678  7.161  1.00 104.91 ? 277 LYS   A N   1 
ATOM   2047 C CA  . LYS   B 1 62  ? -43.645 16.634  7.790  1.00 91.72  ? 277 LYS   A CA  1 
ATOM   2048 C C   . LYS   B 1 62  ? -43.405 15.540  8.844  1.00 89.79  ? 277 LYS   A C   1 
ATOM   2049 O O   . LYS   B 1 62  ? -42.259 15.366  9.272  1.00 89.99  ? 277 LYS   A O   1 
ATOM   2050 C CB  . LYS   B 1 62  ? -43.323 18.004  8.406  1.00 95.51  ? 277 LYS   A CB  1 
ATOM   2051 C CG  . LYS   B 1 62  ? -43.650 19.187  7.505  1.00 99.37  ? 277 LYS   A CG  1 
ATOM   2052 C CD  . LYS   B 1 62  ? -42.641 20.324  7.585  1.00 100.33 ? 277 LYS   A CD  1 
ATOM   2053 C CE  . LYS   B 1 62  ? -42.572 21.035  6.242  1.00 104.63 ? 277 LYS   A CE  1 
ATOM   2054 N NZ  . LYS   B 1 62  ? -41.781 22.289  6.299  1.00 111.55 ? 277 LYS   A NZ  1 
ATOM   2055 N N   . PHE   B 1 63  ? -44.457 14.818  9.261  1.00 87.67  ? 278 PHE   A N   1 
ATOM   2056 C CA  . PHE   B 1 63  ? -44.371 13.776  10.319 1.00 84.62  ? 278 PHE   A CA  1 
ATOM   2057 C C   . PHE   B 1 63  ? -45.112 12.528  9.826  1.00 87.43  ? 278 PHE   A C   1 
ATOM   2058 O O   . PHE   B 1 63  ? -45.971 12.645  8.952  1.00 88.46  ? 278 PHE   A O   1 
ATOM   2059 C CB  . PHE   B 1 63  ? -44.979 14.297  11.650 1.00 84.15  ? 278 PHE   A CB  1 
ATOM   2060 C CG  . PHE   B 1 63  ? -44.424 15.634  12.089 1.00 71.81  ? 278 PHE   A CG  1 
ATOM   2061 C CD1 . PHE   B 1 63  ? -44.924 16.826  11.556 1.00 69.51  ? 278 PHE   A CD1 1 
ATOM   2062 C CD2 . PHE   B 1 63  ? -43.381 15.703  12.997 1.00 70.91  ? 278 PHE   A CD2 1 
ATOM   2063 C CE1 . PHE   B 1 63  ? -44.377 18.056  11.900 1.00 65.25  ? 278 PHE   A CE1 1 
ATOM   2064 C CE2 . PHE   B 1 63  ? -42.852 16.931  13.371 1.00 67.93  ? 278 PHE   A CE2 1 
ATOM   2065 C CZ  . PHE   B 1 63  ? -43.340 18.106  12.810 1.00 63.87  ? 278 PHE   A CZ  1 
ATOM   2066 N N   . PRO   B 1 64  ? -44.804 11.336  10.381 1.00 99.85  ? 279 PRO   A N   1 
ATOM   2067 C CA  . PRO   B 1 64  ? -45.462 10.141  9.841  1.00 108.17 ? 279 PRO   A CA  1 
ATOM   2068 C C   . PRO   B 1 64  ? -46.982 10.162  10.003 1.00 113.11 ? 279 PRO   A C   1 
ATOM   2069 O O   . PRO   B 1 64  ? -47.522 10.953  10.788 1.00 123.60 ? 279 PRO   A O   1 
ATOM   2070 C CB  . PRO   B 1 64  ? -44.824 8.981   10.643 1.00 108.84 ? 279 PRO   A CB  1 
ATOM   2071 C CG  . PRO   B 1 64  ? -44.296 9.607   11.886 1.00 108.00 ? 279 PRO   A CG  1 
ATOM   2072 C CD  . PRO   B 1 64  ? -43.866 10.987  11.467 1.00 110.23 ? 279 PRO   A CD  1 
ATOM   2073 N N   . GLU   B 1 65  ? -47.654 9.321   9.221  1.00 107.50 ? 280 GLU   A N   1 
ATOM   2074 C CA  . GLU   B 1 65  ? -49.059 9.009   9.433  1.00 108.65 ? 280 GLU   A CA  1 
ATOM   2075 C C   . GLU   B 1 65  ? -49.113 7.602   10.063 1.00 114.70 ? 280 GLU   A C   1 
ATOM   2076 O O   . GLU   B 1 65  ? -49.968 6.778   9.707  1.00 108.25 ? 280 GLU   A O   1 
ATOM   2077 C CB  . GLU   B 1 65  ? -49.826 9.106   8.107  1.00 104.75 ? 280 GLU   A CB  1 
ATOM   2078 C CG  . GLU   B 1 65  ? -49.724 10.471  7.419  1.00 107.88 ? 280 GLU   A CG  1 
ATOM   2079 C CD  . GLU   B 1 65  ? -50.505 11.577  8.131  1.00 118.67 ? 280 GLU   A CD  1 
ATOM   2080 O OE1 . GLU   B 1 65  ? -51.759 11.506  8.138  1.00 112.55 ? 280 GLU   A OE1 1 
ATOM   2081 O OE2 . GLU   B 1 65  ? -49.874 12.528  8.663  1.00 114.56 ? 280 GLU   A OE2 1 
ATOM   2082 N N   . LYS   B 1 66  ? -48.210 7.367   11.029 1.00 112.76 ? 281 LYS   A N   1 
ATOM   2083 C CA  . LYS   B 1 66  ? -47.915 6.041   11.577 1.00 104.24 ? 281 LYS   A CA  1 
ATOM   2084 C C   . LYS   B 1 66  ? -48.568 5.942   12.939 1.00 101.10 ? 281 LYS   A C   1 
ATOM   2085 O O   . LYS   B 1 66  ? -47.948 6.278   13.951 1.00 89.92  ? 281 LYS   A O   1 
ATOM   2086 C CB  . LYS   B 1 66  ? -46.398 5.816   11.706 1.00 97.66  ? 281 LYS   A CB  1 
ATOM   2087 N N   . LYS   B 1 67  ? -49.826 5.497   12.941 1.00 106.69 ? 282 LYS   A N   1 
ATOM   2088 C CA  . LYS   B 1 67  ? -50.637 5.268   14.155 1.00 111.40 ? 282 LYS   A CA  1 
ATOM   2089 C C   . LYS   B 1 67  ? -50.639 6.498   15.074 1.00 116.62 ? 282 LYS   A C   1 
ATOM   2090 O O   . LYS   B 1 67  ? -51.651 7.204   15.153 1.00 111.14 ? 282 LYS   A O   1 
ATOM   2091 C CB  . LYS   B 1 67  ? -50.206 3.973   14.885 1.00 108.08 ? 282 LYS   A CB  1 
ATOM   2092 C CG  . LYS   B 1 67  ? -51.097 3.549   16.054 1.00 97.13  ? 282 LYS   A CG  1 
ATOM   2093 N N   . GLY   B 1 68  ? -49.501 6.765   15.728 1.00 120.99 ? 283 GLY   A N   1 
ATOM   2094 C CA  . GLY   B 1 68  ? -49.265 8.006   16.472 1.00 120.59 ? 283 GLY   A CA  1 
ATOM   2095 C C   . GLY   B 1 68  ? -48.618 9.078   15.606 1.00 123.16 ? 283 GLY   A C   1 
ATOM   2096 O O   . GLY   B 1 68  ? -47.601 9.657   15.984 1.00 117.91 ? 283 GLY   A O   1 
ATOM   2097 N N   . GLY   B 1 69  ? -49.207 9.328   14.437 1.00 127.54 ? 284 GLY   A N   1 
ATOM   2098 C CA  . GLY   B 1 69  ? -48.818 10.431  13.573 1.00 122.38 ? 284 GLY   A CA  1 
ATOM   2099 C C   . GLY   B 1 69  ? -49.627 11.645  13.976 1.00 119.19 ? 284 GLY   A C   1 
ATOM   2100 O O   . GLY   B 1 69  ? -50.765 11.509  14.435 1.00 114.02 ? 284 GLY   A O   1 
ATOM   2101 N N   . LEU   B 1 70  ? -49.040 12.827  13.795 1.00 110.57 ? 285 LEU   A N   1 
ATOM   2102 C CA  . LEU   B 1 70  ? -49.662 14.113  14.165 1.00 98.57  ? 285 LEU   A CA  1 
ATOM   2103 C C   . LEU   B 1 70  ? -51.158 14.219  13.854 1.00 96.87  ? 285 LEU   A C   1 
ATOM   2104 O O   . LEU   B 1 70  ? -51.925 14.775  14.641 1.00 89.96  ? 285 LEU   A O   1 
ATOM   2105 C CB  . LEU   B 1 70  ? -48.956 15.272  13.456 1.00 97.32  ? 285 LEU   A CB  1 
ATOM   2106 C CG  . LEU   B 1 70  ? -48.571 16.476  14.307 1.00 91.16  ? 285 LEU   A CG  1 
ATOM   2107 C CD1 . LEU   B 1 70  ? -48.167 17.590  13.357 1.00 93.47  ? 285 LEU   A CD1 1 
ATOM   2108 C CD2 . LEU   B 1 70  ? -49.680 16.933  15.243 1.00 89.53  ? 285 LEU   A CD2 1 
ATOM   2109 N N   . ARG   B 1 71  ? -51.543 13.700  12.689 1.00 99.12  ? 286 ARG   A N   1 
ATOM   2110 C CA  . ARG   B 1 71  ? -52.946 13.642  12.253 1.00 103.66 ? 286 ARG   A CA  1 
ATOM   2111 C C   . ARG   B 1 71  ? -53.857 12.935  13.276 1.00 100.33 ? 286 ARG   A C   1 
ATOM   2112 O O   . ARG   B 1 71  ? -54.842 13.514  13.736 1.00 92.17  ? 286 ARG   A O   1 
ATOM   2113 C CB  . ARG   B 1 71  ? -53.030 12.923  10.902 1.00 108.29 ? 286 ARG   A CB  1 
ATOM   2114 C CG  . ARG   B 1 71  ? -54.341 13.114  10.162 1.00 108.09 ? 286 ARG   A CG  1 
ATOM   2115 C CD  . ARG   B 1 71  ? -55.031 11.793  9.859  1.00 109.77 ? 286 ARG   A CD  1 
ATOM   2116 N NE  . ARG   B 1 71  ? -56.002 11.933  8.774  1.00 108.41 ? 286 ARG   A NE  1 
ATOM   2117 C CZ  . ARG   B 1 71  ? -57.167 12.586  8.851  1.00 103.82 ? 286 ARG   A CZ  1 
ATOM   2118 N NH1 . ARG   B 1 71  ? -57.962 12.630  7.784  1.00 99.20  ? 286 ARG   A NH1 1 
ATOM   2119 N NH2 . ARG   B 1 71  ? -57.560 13.192  9.974  1.00 104.28 ? 286 ARG   A NH2 1 
ATOM   2120 N N   . GLU   B 1 72  ? -53.509 11.696  13.629 1.00 103.53 ? 287 GLU   A N   1 
ATOM   2121 C CA  . GLU   B 1 72  ? -54.253 10.929  14.635 1.00 104.56 ? 287 GLU   A CA  1 
ATOM   2122 C C   . GLU   B 1 72  ? -54.293 11.640  15.992 1.00 93.99  ? 287 GLU   A C   1 
ATOM   2123 O O   . GLU   B 1 72  ? -55.364 11.761  16.574 1.00 102.12 ? 287 GLU   A O   1 
ATOM   2124 C CB  . GLU   B 1 72  ? -53.680 9.510   14.811 1.00 114.62 ? 287 GLU   A CB  1 
ATOM   2125 C CG  . GLU   B 1 72  ? -54.209 8.455   13.832 1.00 121.77 ? 287 GLU   A CG  1 
ATOM   2126 C CD  . GLU   B 1 72  ? -53.473 8.403   12.497 1.00 125.86 ? 287 GLU   A CD  1 
ATOM   2127 O OE1 . GLU   B 1 72  ? -54.151 8.215   11.469 1.00 116.53 ? 287 GLU   A OE1 1 
ATOM   2128 O OE2 . GLU   B 1 72  ? -52.227 8.533   12.461 1.00 137.91 ? 287 GLU   A OE2 1 
ATOM   2129 N N   . LEU   B 1 73  ? -53.147 12.119  16.481 1.00 80.03  ? 288 LEU   A N   1 
ATOM   2130 C CA  . LEU   B 1 73  ? -53.094 12.782  17.797 1.00 78.70  ? 288 LEU   A CA  1 
ATOM   2131 C C   . LEU   B 1 73  ? -54.025 13.999  17.911 1.00 74.94  ? 288 LEU   A C   1 
ATOM   2132 O O   . LEU   B 1 73  ? -54.726 14.144  18.908 1.00 79.42  ? 288 LEU   A O   1 
ATOM   2133 C CB  . LEU   B 1 73  ? -51.659 13.178  18.191 1.00 75.13  ? 288 LEU   A CB  1 
ATOM   2134 C CG  . LEU   B 1 73  ? -50.703 12.054  18.637 1.00 72.24  ? 288 LEU   A CG  1 
ATOM   2135 C CD1 . LEU   B 1 73  ? -49.748 11.665  17.522 1.00 74.11  ? 288 LEU   A CD1 1 
ATOM   2136 C CD2 . LEU   B 1 73  ? -49.888 12.449  19.849 1.00 75.10  ? 288 LEU   A CD2 1 
ATOM   2137 N N   . TYR   B 1 74  ? -54.034 14.860  16.898 1.00 77.50  ? 289 TYR   A N   1 
ATOM   2138 C CA  . TYR   B 1 74  ? -54.888 16.058  16.909 1.00 79.28  ? 289 TYR   A CA  1 
ATOM   2139 C C   . TYR   B 1 74  ? -56.379 15.679  16.916 1.00 89.90  ? 289 TYR   A C   1 
ATOM   2140 O O   . TYR   B 1 74  ? -57.164 16.296  17.660 1.00 88.73  ? 289 TYR   A O   1 
ATOM   2141 C CB  . TYR   B 1 74  ? -54.567 17.014  15.733 1.00 76.45  ? 289 TYR   A CB  1 
ATOM   2142 C CG  . TYR   B 1 74  ? -54.944 18.465  16.021 1.00 73.96  ? 289 TYR   A CG  1 
ATOM   2143 C CD1 . TYR   B 1 74  ? -54.119 19.266  16.797 1.00 76.49  ? 289 TYR   A CD1 1 
ATOM   2144 C CD2 . TYR   B 1 74  ? -56.127 19.029  15.546 1.00 72.01  ? 289 TYR   A CD2 1 
ATOM   2145 C CE1 . TYR   B 1 74  ? -54.452 20.581  17.093 1.00 73.93  ? 289 TYR   A CE1 1 
ATOM   2146 C CE2 . TYR   B 1 74  ? -56.463 20.353  15.840 1.00 68.84  ? 289 TYR   A CE2 1 
ATOM   2147 C CZ  . TYR   B 1 74  ? -55.622 21.116  16.617 1.00 68.15  ? 289 TYR   A CZ  1 
ATOM   2148 O OH  . TYR   B 1 74  ? -55.909 22.416  16.949 1.00 70.00  ? 289 TYR   A OH  1 
ATOM   2149 N N   . ASP   B 1 75  ? -56.746 14.661  16.115 1.00 98.10  ? 290 ASP   A N   1 
ATOM   2150 C CA  . ASP   B 1 75  ? -58.125 14.099  16.085 1.00 100.90 ? 290 ASP   A CA  1 
ATOM   2151 C C   . ASP   B 1 75  ? -58.645 13.740  17.464 1.00 102.31 ? 290 ASP   A C   1 
ATOM   2152 O O   . ASP   B 1 75  ? -59.765 14.117  17.823 1.00 115.02 ? 290 ASP   A O   1 
ATOM   2153 C CB  . ASP   B 1 75  ? -58.213 12.838  15.213 1.00 97.08  ? 290 ASP   A CB  1 
ATOM   2154 C CG  . ASP   B 1 75  ? -58.019 13.125  13.745 1.00 105.15 ? 290 ASP   A CG  1 
ATOM   2155 O OD1 . ASP   B 1 75  ? -57.903 14.319  13.383 1.00 106.41 ? 290 ASP   A OD1 1 
ATOM   2156 O OD2 . ASP   B 1 75  ? -57.977 12.150  12.955 1.00 99.16  ? 290 ASP   A OD2 1 
ATOM   2157 N N   . ARG   B 1 76  ? -57.831 13.002  18.220 1.00 101.20 ? 291 ARG   A N   1 
ATOM   2158 C CA  . ARG   B 1 76  ? -58.127 12.699  19.629 1.00 104.29 ? 291 ARG   A CA  1 
ATOM   2159 C C   . ARG   B 1 76  ? -58.237 14.006  20.398 1.00 98.91  ? 291 ARG   A C   1 
ATOM   2160 O O   . ARG   B 1 76  ? -59.200 14.239  21.135 1.00 99.28  ? 291 ARG   A O   1 
ATOM   2161 C CB  . ARG   B 1 76  ? -57.022 11.858  20.280 1.00 108.83 ? 291 ARG   A CB  1 
ATOM   2162 C CG  . ARG   B 1 76  ? -56.723 10.508  19.626 1.00 117.81 ? 291 ARG   A CG  1 
ATOM   2163 C CD  . ARG   B 1 76  ? -55.912 9.586   20.537 1.00 118.66 ? 291 ARG   A CD  1 
ATOM   2164 N NE  . ARG   B 1 76  ? -54.887 10.301  21.311 1.00 122.74 ? 291 ARG   A NE  1 
ATOM   2165 C CZ  . ARG   B 1 76  ? -54.160 9.765   22.290 1.00 121.01 ? 291 ARG   A CZ  1 
ATOM   2166 N NH1 . ARG   B 1 76  ? -54.303 8.481   22.623 1.00 132.53 ? 291 ARG   A NH1 1 
ATOM   2167 N NH2 . ARG   B 1 76  ? -53.267 10.516  22.933 1.00 108.18 ? 291 ARG   A NH2 1 
ATOM   2168 N N   . GLY   B 1 77  ? -57.236 14.857  20.198 1.00 92.94  ? 292 GLY   A N   1 
ATOM   2169 C CA  . GLY   B 1 77  ? -57.146 16.111  20.906 1.00 92.11  ? 292 GLY   A CA  1 
ATOM   2170 C C   . GLY   B 1 77  ? -56.550 15.818  22.269 1.00 84.23  ? 292 GLY   A C   1 
ATOM   2171 O O   . GLY   B 1 77  ? -56.060 14.708  22.503 1.00 88.98  ? 292 GLY   A O   1 
ATOM   2172 N N   . PRO   B 1 78  ? -56.605 16.794  23.190 1.00 76.02  ? 293 PRO   A N   1 
ATOM   2173 C CA  . PRO   B 1 78  ? -57.294 18.096  23.065 1.00 75.98  ? 293 PRO   A CA  1 
ATOM   2174 C C   . PRO   B 1 78  ? -56.537 19.141  22.205 1.00 72.16  ? 293 PRO   A C   1 
ATOM   2175 O O   . PRO   B 1 78  ? -55.346 19.375  22.460 1.00 72.07  ? 293 PRO   A O   1 
ATOM   2176 C CB  . PRO   B 1 78  ? -57.404 18.580  24.524 1.00 74.39  ? 293 PRO   A CB  1 
ATOM   2177 C CG  . PRO   B 1 78  ? -56.323 17.861  25.273 1.00 73.00  ? 293 PRO   A CG  1 
ATOM   2178 C CD  . PRO   B 1 78  ? -55.885 16.660  24.472 1.00 72.42  ? 293 PRO   A CD  1 
ATOM   2179 N N   . PRO   B 1 79  ? -57.219 19.776  21.220 1.00 68.25  ? 294 PRO   A N   1 
ATOM   2180 C CA  . PRO   B 1 79  ? -56.649 20.829  20.328 1.00 65.01  ? 294 PRO   A CA  1 
ATOM   2181 C C   . PRO   B 1 79  ? -55.678 21.854  20.940 1.00 59.71  ? 294 PRO   A C   1 
ATOM   2182 O O   . PRO   B 1 79  ? -54.674 22.181  20.323 1.00 58.04  ? 294 PRO   A O   1 
ATOM   2183 C CB  . PRO   B 1 79  ? -57.894 21.580  19.837 1.00 67.90  ? 294 PRO   A CB  1 
ATOM   2184 C CG  . PRO   B 1 79  ? -59.030 20.608  19.971 1.00 69.72  ? 294 PRO   A CG  1 
ATOM   2185 C CD  . PRO   B 1 79  ? -58.620 19.465  20.857 1.00 66.40  ? 294 PRO   A CD  1 
ATOM   2186 N N   . HIS   B 1 80  ? -55.992 22.365  22.132 1.00 56.81  ? 295 HIS   A N   1 
ATOM   2187 C CA  . HIS   B 1 80  ? -55.188 23.420  22.813 1.00 55.90  ? 295 HIS   A CA  1 
ATOM   2188 C C   . HIS   B 1 80  ? -53.841 22.933  23.395 1.00 54.94  ? 295 HIS   A C   1 
ATOM   2189 O O   . HIS   B 1 80  ? -53.053 23.751  23.892 1.00 50.82  ? 295 HIS   A O   1 
ATOM   2190 C CB  . HIS   B 1 80  ? -55.996 24.051  23.961 1.00 60.67  ? 295 HIS   A CB  1 
ATOM   2191 C CG  . HIS   B 1 80  ? -55.974 23.240  25.229 1.00 71.10  ? 295 HIS   A CG  1 
ATOM   2192 N ND1 . HIS   B 1 80  ? -56.768 22.122  25.422 1.00 69.29  ? 295 HIS   A ND1 1 
ATOM   2193 C CD2 . HIS   B 1 80  ? -55.210 23.358  26.345 1.00 74.87  ? 295 HIS   A CD2 1 
ATOM   2194 C CE1 . HIS   B 1 80  ? -56.496 21.597  26.604 1.00 75.65  ? 295 HIS   A CE1 1 
ATOM   2195 N NE2 . HIS   B 1 80  ? -55.552 22.324  27.182 1.00 77.67  ? 295 HIS   A NE2 1 
ATOM   2196 N N   . ALA   B 1 81  ? -53.608 21.614  23.396 1.00 52.38  ? 296 ALA   A N   1 
ATOM   2197 C CA  . ALA   B 1 81  ? -52.340 21.056  23.865 1.00 54.01  ? 296 ALA   A CA  1 
ATOM   2198 C C   . ALA   B 1 81  ? -51.229 21.037  22.810 1.00 56.36  ? 296 ALA   A C   1 
ATOM   2199 O O   . ALA   B 1 81  ? -50.096 20.727  23.165 1.00 56.47  ? 296 ALA   A O   1 
ATOM   2200 C CB  . ALA   B 1 81  ? -52.557 19.658  24.400 1.00 54.91  ? 296 ALA   A CB  1 
ATOM   2201 N N   . PHE   B 1 82  ? -51.544 21.401  21.559 1.00 48.80  ? 297 PHE   A N   1 
ATOM   2202 C CA  . PHE   B 1 82  ? -50.645 21.263  20.420 1.00 49.91  ? 297 PHE   A CA  1 
ATOM   2203 C C   . PHE   B 1 82  ? -49.974 22.568  19.976 1.00 53.85  ? 297 PHE   A C   1 
ATOM   2204 O O   . PHE   B 1 82  ? -50.653 23.510  19.583 1.00 61.58  ? 297 PHE   A O   1 
ATOM   2205 C CB  . PHE   B 1 82  ? -51.431 20.693  19.253 1.00 52.51  ? 297 PHE   A CB  1 
ATOM   2206 C CG  . PHE   B 1 82  ? -51.778 19.239  19.418 1.00 51.33  ? 297 PHE   A CG  1 
ATOM   2207 C CD1 . PHE   B 1 82  ? -52.799 18.854  20.264 1.00 53.67  ? 297 PHE   A CD1 1 
ATOM   2208 C CD2 . PHE   B 1 82  ? -51.069 18.250  18.734 1.00 53.08  ? 297 PHE   A CD2 1 
ATOM   2209 C CE1 . PHE   B 1 82  ? -53.126 17.514  20.431 1.00 53.13  ? 297 PHE   A CE1 1 
ATOM   2210 C CE2 . PHE   B 1 82  ? -51.386 16.908  18.894 1.00 52.95  ? 297 PHE   A CE2 1 
ATOM   2211 C CZ  . PHE   B 1 82  ? -52.421 16.546  19.744 1.00 55.66  ? 297 PHE   A CZ  1 
ATOM   2212 N N   . PHE   B 1 83  ? -48.635 22.577  19.988 1.00 56.46  ? 298 PHE   A N   1 
ATOM   2213 C CA  . PHE   B 1 83  ? -47.783 23.742  19.725 1.00 54.33  ? 298 PHE   A CA  1 
ATOM   2214 C C   . PHE   B 1 83  ? -46.761 23.468  18.609 1.00 54.67  ? 298 PHE   A C   1 
ATOM   2215 O O   . PHE   B 1 83  ? -46.424 22.333  18.381 1.00 51.28  ? 298 PHE   A O   1 
ATOM   2216 C CB  . PHE   B 1 83  ? -47.068 24.133  21.010 1.00 56.71  ? 298 PHE   A CB  1 
ATOM   2217 C CG  . PHE   B 1 83  ? -47.999 24.649  22.046 1.00 65.80  ? 298 PHE   A CG  1 
ATOM   2218 C CD1 . PHE   B 1 83  ? -48.815 23.767  22.763 1.00 69.20  ? 298 PHE   A CD1 1 
ATOM   2219 C CD2 . PHE   B 1 83  ? -48.132 26.014  22.261 1.00 64.03  ? 298 PHE   A CD2 1 
ATOM   2220 C CE1 . PHE   B 1 83  ? -49.730 24.236  23.694 1.00 72.60  ? 298 PHE   A CE1 1 
ATOM   2221 C CE2 . PHE   B 1 83  ? -49.040 26.487  23.199 1.00 73.55  ? 298 PHE   A CE2 1 
ATOM   2222 C CZ  . PHE   B 1 83  ? -49.843 25.600  23.912 1.00 70.24  ? 298 PHE   A CZ  1 
ATOM   2223 N N   . LEU   B 1 84  ? -46.330 24.518  17.898 1.00 53.81  ? 299 LEU   A N   1 
ATOM   2224 C CA  . LEU   B 1 84  ? -45.261 24.461  16.904 1.00 52.02  ? 299 LEU   A CA  1 
ATOM   2225 C C   . LEU   B 1 84  ? -44.148 25.433  17.332 1.00 51.84  ? 299 LEU   A C   1 
ATOM   2226 O O   . LEU   B 1 84  ? -44.425 26.594  17.555 1.00 54.47  ? 299 LEU   A O   1 
ATOM   2227 C CB  . LEU   B 1 84  ? -45.771 24.834  15.521 1.00 52.13  ? 299 LEU   A CB  1 
ATOM   2228 C CG  . LEU   B 1 84  ? -44.760 24.868  14.355 1.00 54.24  ? 299 LEU   A CG  1 
ATOM   2229 C CD1 . LEU   B 1 84  ? -44.623 23.531  13.647 1.00 52.73  ? 299 LEU   A CD1 1 
ATOM   2230 C CD2 . LEU   B 1 84  ? -45.214 25.889  13.330 1.00 58.58  ? 299 LEU   A CD2 1 
ATOM   2231 N N   . VAL   B 1 85  ? -42.914 24.936  17.477 1.00 46.59  ? 300 VAL   A N   1 
ATOM   2232 C CA  . VAL   B 1 85  ? -41.725 25.758  17.596 1.00 47.55  ? 300 VAL   A CA  1 
ATOM   2233 C C   . VAL   B 1 85  ? -40.945 25.720  16.277 1.00 50.94  ? 300 VAL   A C   1 
ATOM   2234 O O   . VAL   B 1 85  ? -40.662 24.645  15.764 1.00 49.70  ? 300 VAL   A O   1 
ATOM   2235 C CB  . VAL   B 1 85  ? -40.847 25.265  18.739 1.00 47.58  ? 300 VAL   A CB  1 
ATOM   2236 C CG1 . VAL   B 1 85  ? -39.550 26.070  18.848 1.00 52.31  ? 300 VAL   A CG1 1 
ATOM   2237 C CG2 . VAL   B 1 85  ? -41.629 25.357  20.038 1.00 53.82  ? 300 VAL   A CG2 1 
ATOM   2238 N N   . LYS   B 1 86  ? -40.635 26.882  15.705 1.00 52.58  ? 301 LYS   A N   1 
ATOM   2239 C CA  . LYS   B 1 86  ? -39.637 26.937  14.630 1.00 53.61  ? 301 LYS   A CA  1 
ATOM   2240 C C   . LYS   B 1 86  ? -38.321 27.356  15.259 1.00 49.92  ? 301 LYS   A C   1 
ATOM   2241 O O   . LYS   B 1 86  ? -38.288 28.354  15.991 1.00 42.42  ? 301 LYS   A O   1 
ATOM   2242 C CB  . LYS   B 1 86  ? -40.044 27.902  13.524 1.00 59.33  ? 301 LYS   A CB  1 
ATOM   2243 C CG  . LYS   B 1 86  ? -39.069 27.894  12.332 1.00 68.66  ? 301 LYS   A CG  1 
ATOM   2244 C CD  . LYS   B 1 86  ? -39.708 28.384  11.028 1.00 72.82  ? 301 LYS   A CD  1 
ATOM   2245 C CE  . LYS   B 1 86  ? -39.348 27.515  9.818  1.00 76.78  ? 301 LYS   A CE  1 
ATOM   2246 N NZ  . LYS   B 1 86  ? -39.109 28.332  8.591  1.00 74.02  ? 301 LYS   A NZ  1 
ATOM   2247 N N   . PHE   B 1 87  ? -37.258 26.590  15.012 1.00 48.15  ? 302 PHE   A N   1 
ATOM   2248 C CA  . PHE   B 1 87  ? -35.932 26.923  15.528 1.00 51.59  ? 302 PHE   A CA  1 
ATOM   2249 C C   . PHE   B 1 87  ? -35.023 27.433  14.420 1.00 56.13  ? 302 PHE   A C   1 
ATOM   2250 O O   . PHE   B 1 87  ? -35.027 26.872  13.316 1.00 56.78  ? 302 PHE   A O   1 
ATOM   2251 C CB  . PHE   B 1 87  ? -35.263 25.721  16.160 1.00 54.27  ? 302 PHE   A CB  1 
ATOM   2252 C CG  . PHE   B 1 87  ? -35.658 25.470  17.583 1.00 61.39  ? 302 PHE   A CG  1 
ATOM   2253 C CD1 . PHE   B 1 87  ? -35.525 26.461  18.546 1.00 60.34  ? 302 PHE   A CD1 1 
ATOM   2254 C CD2 . PHE   B 1 87  ? -36.108 24.215  17.983 1.00 63.15  ? 302 PHE   A CD2 1 
ATOM   2255 C CE1 . PHE   B 1 87  ? -35.881 26.228  19.869 1.00 65.48  ? 302 PHE   A CE1 1 
ATOM   2256 C CE2 . PHE   B 1 87  ? -36.454 23.984  19.311 1.00 64.36  ? 302 PHE   A CE2 1 
ATOM   2257 C CZ  . PHE   B 1 87  ? -36.341 24.987  20.254 1.00 62.22  ? 302 PHE   A CZ  1 
ATOM   2258 N N   . TRP   B 1 88  ? -34.271 28.502  14.719 1.00 52.37  ? 303 TRP   A N   1 
ATOM   2259 C CA  . TRP   B 1 88  ? -33.134 28.935  13.897 1.00 54.69  ? 303 TRP   A CA  1 
ATOM   2260 C C   . TRP   B 1 88  ? -31.934 28.606  14.706 1.00 54.87  ? 303 TRP   A C   1 
ATOM   2261 O O   . TRP   B 1 88  ? -31.619 29.321  15.635 1.00 54.84  ? 303 TRP   A O   1 
ATOM   2262 C CB  . TRP   B 1 88  ? -33.185 30.425  13.596 1.00 53.15  ? 303 TRP   A CB  1 
ATOM   2263 C CG  . TRP   B 1 88  ? -34.184 30.673  12.581 1.00 50.90  ? 303 TRP   A CG  1 
ATOM   2264 C CD1 . TRP   B 1 88  ? -33.985 30.658  11.256 1.00 51.61  ? 303 TRP   A CD1 1 
ATOM   2265 C CD2 . TRP   B 1 88  ? -35.583 30.897  12.786 1.00 50.86  ? 303 TRP   A CD2 1 
ATOM   2266 N NE1 . TRP   B 1 88  ? -35.167 30.877  10.598 1.00 53.40  ? 303 TRP   A NE1 1 
ATOM   2267 C CE2 . TRP   B 1 88  ? -36.168 31.030  11.515 1.00 49.29  ? 303 TRP   A CE2 1 
ATOM   2268 C CE3 . TRP   B 1 88  ? -36.397 31.010  13.922 1.00 53.64  ? 303 TRP   A CE3 1 
ATOM   2269 C CZ2 . TRP   B 1 88  ? -37.533 31.277  11.334 1.00 52.77  ? 303 TRP   A CZ2 1 
ATOM   2270 C CZ3 . TRP   B 1 88  ? -37.769 31.270  13.751 1.00 53.67  ? 303 TRP   A CZ3 1 
ATOM   2271 C CH2 . TRP   B 1 88  ? -38.318 31.396  12.464 1.00 55.97  ? 303 TRP   A CH2 1 
ATOM   2272 N N   . ALA   B 1 89  ? -31.291 27.496  14.366 1.00 53.26  ? 304 ALA   A N   1 
ATOM   2273 C CA  . ALA   B 1 89  ? -30.292 26.879  15.210 1.00 51.81  ? 304 ALA   A CA  1 
ATOM   2274 C C   . ALA   B 1 89  ? -28.906 27.482  15.056 1.00 58.51  ? 304 ALA   A C   1 
ATOM   2275 O O   . ALA   B 1 89  ? -28.541 27.971  13.984 1.00 69.86  ? 304 ALA   A O   1 
ATOM   2276 C CB  . ALA   B 1 89  ? -30.240 25.397  14.904 1.00 52.52  ? 304 ALA   A CB  1 
ATOM   2277 N N   . ASP   B 1 90  ? -28.129 27.420  16.129 1.00 61.80  ? 305 ASP   A N   1 
ATOM   2278 C CA  . ASP   B 1 90  ? -26.749 27.875  16.123 1.00 67.99  ? 305 ASP   A CA  1 
ATOM   2279 C C   . ASP   B 1 90  ? -25.842 26.667  15.973 1.00 66.51  ? 305 ASP   A C   1 
ATOM   2280 O O   . ASP   B 1 90  ? -25.757 25.880  16.900 1.00 68.00  ? 305 ASP   A O   1 
ATOM   2281 C CB  . ASP   B 1 90  ? -26.451 28.604  17.439 1.00 73.06  ? 305 ASP   A CB  1 
ATOM   2282 C CG  . ASP   B 1 90  ? -25.198 29.475  17.369 1.00 70.13  ? 305 ASP   A CG  1 
ATOM   2283 O OD1 . ASP   B 1 90  ? -24.130 28.974  16.966 1.00 72.12  ? 305 ASP   A OD1 1 
ATOM   2284 O OD2 . ASP   B 1 90  ? -25.292 30.655  17.757 1.00 71.65  ? 305 ASP   A OD2 1 
ATOM   2285 N N   . LEU   B 1 91  ? -25.165 26.515  14.827 1.00 65.72  ? 306 LEU   A N   1 
ATOM   2286 C CA  . LEU   B 1 91  ? -24.253 25.366  14.598 1.00 71.23  ? 306 LEU   A CA  1 
ATOM   2287 C C   . LEU   B 1 91  ? -22.734 25.667  14.585 1.00 81.31  ? 306 LEU   A C   1 
ATOM   2288 O O   . LEU   B 1 91  ? -21.948 24.774  14.249 1.00 89.81  ? 306 LEU   A O   1 
ATOM   2289 C CB  . LEU   B 1 91  ? -24.643 24.616  13.316 1.00 68.96  ? 306 LEU   A CB  1 
ATOM   2290 C CG  . LEU   B 1 91  ? -26.120 24.240  13.127 1.00 73.21  ? 306 LEU   A CG  1 
ATOM   2291 C CD1 . LEU   B 1 91  ? -26.390 23.452  11.851 1.00 76.88  ? 306 LEU   A CD1 1 
ATOM   2292 C CD2 . LEU   B 1 91  ? -26.611 23.420  14.294 1.00 74.60  ? 306 LEU   A CD2 1 
ATOM   2293 N N   . ASN   B 1 92  ? -22.309 26.877  14.977 1.00 87.46  ? 307 ASN   A N   1 
ATOM   2294 C CA  . ASN   B 1 92  ? -20.876 27.226  14.990 1.00 93.48  ? 307 ASN   A CA  1 
ATOM   2295 C C   . ASN   B 1 92  ? -20.298 27.183  16.400 1.00 88.87  ? 307 ASN   A C   1 
ATOM   2296 O O   . ASN   B 1 92  ? -20.694 27.984  17.245 1.00 88.66  ? 307 ASN   A O   1 
ATOM   2297 C CB  . ASN   B 1 92  ? -20.660 28.620  14.377 1.00 106.48 ? 307 ASN   A CB  1 
ATOM   2298 C CG  . ASN   B 1 92  ? -19.175 28.967  14.128 1.00 120.72 ? 307 ASN   A CG  1 
ATOM   2299 O OD1 . ASN   B 1 92  ? -18.274 28.114  14.208 1.00 119.24 ? 307 ASN   A OD1 1 
ATOM   2300 N ND2 . ASN   B 1 92  ? -18.922 30.245  13.815 1.00 121.96 ? 307 ASN   A ND2 1 
ATOM   2301 N N   . TRP   B 1 93  ? -19.357 26.263  16.641 1.00 89.05  ? 308 TRP   A N   1 
ATOM   2302 C CA  . TRP   B 1 93  ? -18.595 26.258  17.889 1.00 95.18  ? 308 TRP   A CA  1 
ATOM   2303 C C   . TRP   B 1 93  ? -17.095 25.992  17.719 1.00 101.99 ? 308 TRP   A C   1 
ATOM   2304 O O   . TRP   B 1 93  ? -16.677 24.919  17.299 1.00 106.95 ? 308 TRP   A O   1 
ATOM   2305 C CB  . TRP   B 1 93  ? -19.232 25.289  18.876 1.00 93.29  ? 308 TRP   A CB  1 
ATOM   2306 C CG  . TRP   B 1 93  ? -19.246 23.834  18.502 1.00 90.96  ? 308 TRP   A CG  1 
ATOM   2307 C CD1 . TRP   B 1 93  ? -18.378 22.879  18.946 1.00 93.40  ? 308 TRP   A CD1 1 
ATOM   2308 C CD2 . TRP   B 1 93  ? -20.205 23.150  17.673 1.00 85.02  ? 308 TRP   A CD2 1 
ATOM   2309 N NE1 . TRP   B 1 93  ? -18.721 21.644  18.438 1.00 93.00  ? 308 TRP   A NE1 1 
ATOM   2310 C CE2 . TRP   B 1 93  ? -19.842 21.777  17.661 1.00 85.42  ? 308 TRP   A CE2 1 
ATOM   2311 C CE3 . TRP   B 1 93  ? -21.333 23.559  16.943 1.00 79.23  ? 308 TRP   A CE3 1 
ATOM   2312 C CZ2 . TRP   B 1 93  ? -20.559 20.806  16.931 1.00 76.04  ? 308 TRP   A CZ2 1 
ATOM   2313 C CZ3 . TRP   B 1 93  ? -22.049 22.592  16.209 1.00 77.14  ? 308 TRP   A CZ3 1 
ATOM   2314 C CH2 . TRP   B 1 93  ? -21.658 21.229  16.218 1.00 75.74  ? 308 TRP   A CH2 1 
ATOM   2315 N N   . GLY   B 1 110 ? -17.486 16.137  22.449 1.00 91.92  ? 325 GLY   A N   1 
ATOM   2316 C CA  . GLY   B 1 110 ? -18.084 16.687  23.668 1.00 92.72  ? 325 GLY   A CA  1 
ATOM   2317 C C   . GLY   B 1 110 ? -19.115 15.752  24.287 1.00 92.90  ? 325 GLY   A C   1 
ATOM   2318 O O   . GLY   B 1 110 ? -19.150 14.555  23.971 1.00 88.73  ? 325 GLY   A O   1 
ATOM   2319 N N   . PHE   B 1 111 ? -19.928 16.289  25.200 1.00 86.38  ? 326 PHE   A N   1 
ATOM   2320 C CA  . PHE   B 1 111 ? -21.183 15.634  25.593 1.00 81.89  ? 326 PHE   A CA  1 
ATOM   2321 C C   . PHE   B 1 111 ? -22.294 16.394  24.892 1.00 71.88  ? 326 PHE   A C   1 
ATOM   2322 O O   . PHE   B 1 111 ? -22.308 17.630  24.871 1.00 68.64  ? 326 PHE   A O   1 
ATOM   2323 C CB  . PHE   B 1 111 ? -21.414 15.618  27.113 1.00 81.20  ? 326 PHE   A CB  1 
ATOM   2324 C CG  . PHE   B 1 111 ? -22.736 15.000  27.517 1.00 76.63  ? 326 PHE   A CG  1 
ATOM   2325 C CD1 . PHE   B 1 111 ? -22.974 13.652  27.307 1.00 75.74  ? 326 PHE   A CD1 1 
ATOM   2326 C CD2 . PHE   B 1 111 ? -23.748 15.772  28.085 1.00 78.33  ? 326 PHE   A CD2 1 
ATOM   2327 C CE1 . PHE   B 1 111 ? -24.186 13.071  27.666 1.00 80.97  ? 326 PHE   A CE1 1 
ATOM   2328 C CE2 . PHE   B 1 111 ? -24.967 15.197  28.446 1.00 77.40  ? 326 PHE   A CE2 1 
ATOM   2329 C CZ  . PHE   B 1 111 ? -25.186 13.844  28.241 1.00 77.41  ? 326 PHE   A CZ  1 
ATOM   2330 N N   . TYR   B 1 112 ? -23.206 15.637  24.301 1.00 71.86  ? 327 TYR   A N   1 
ATOM   2331 C CA  . TYR   B 1 112 ? -24.319 16.191  23.555 1.00 69.54  ? 327 TYR   A CA  1 
ATOM   2332 C C   . TYR   B 1 112 ? -25.520 15.854  24.389 1.00 68.83  ? 327 TYR   A C   1 
ATOM   2333 O O   . TYR   B 1 112 ? -25.859 14.676  24.552 1.00 59.88  ? 327 TYR   A O   1 
ATOM   2334 C CB  . TYR   B 1 112 ? -24.414 15.571  22.164 1.00 70.36  ? 327 TYR   A CB  1 
ATOM   2335 C CG  . TYR   B 1 112 ? -23.314 16.065  21.253 1.00 77.07  ? 327 TYR   A CG  1 
ATOM   2336 C CD1 . TYR   B 1 112 ? -22.001 15.596  21.395 1.00 75.86  ? 327 TYR   A CD1 1 
ATOM   2337 C CD2 . TYR   B 1 112 ? -23.571 17.036  20.262 1.00 81.04  ? 327 TYR   A CD2 1 
ATOM   2338 C CE1 . TYR   B 1 112 ? -20.983 16.067  20.573 1.00 81.44  ? 327 TYR   A CE1 1 
ATOM   2339 C CE2 . TYR   B 1 112 ? -22.555 17.508  19.428 1.00 79.24  ? 327 TYR   A CE2 1 
ATOM   2340 C CZ  . TYR   B 1 112 ? -21.265 17.020  19.586 1.00 79.61  ? 327 TYR   A CZ  1 
ATOM   2341 O OH  . TYR   B 1 112 ? -20.246 17.475  18.774 1.00 86.23  ? 327 TYR   A OH  1 
ATOM   2342 N N   . GLY   B 1 113 ? -26.117 16.898  24.956 1.00 66.45  ? 328 GLY   A N   1 
ATOM   2343 C CA  . GLY   B 1 113 ? -27.208 16.759  25.882 1.00 65.19  ? 328 GLY   A CA  1 
ATOM   2344 C C   . GLY   B 1 113 ? -28.426 17.545  25.454 1.00 62.67  ? 328 GLY   A C   1 
ATOM   2345 O O   . GLY   B 1 113 ? -28.340 18.530  24.695 1.00 54.04  ? 328 GLY   A O   1 
ATOM   2346 N N   . VAL   B 1 114 ? -29.561 17.076  25.963 1.00 65.25  ? 329 VAL   A N   1 
ATOM   2347 C CA  . VAL   B 1 114 ? -30.845 17.749  25.869 1.00 64.03  ? 329 VAL   A CA  1 
ATOM   2348 C C   . VAL   B 1 114 ? -31.414 17.932  27.296 1.00 62.13  ? 329 VAL   A C   1 
ATOM   2349 O O   . VAL   B 1 114 ? -31.674 16.952  27.994 1.00 58.39  ? 329 VAL   A O   1 
ATOM   2350 C CB  . VAL   B 1 114 ? -31.821 16.940  24.980 1.00 60.54  ? 329 VAL   A CB  1 
ATOM   2351 C CG1 . VAL   B 1 114 ? -33.210 17.560  24.999 1.00 62.61  ? 329 VAL   A CG1 1 
ATOM   2352 C CG2 . VAL   B 1 114 ? -31.296 16.878  23.551 1.00 62.84  ? 329 VAL   A CG2 1 
ATOM   2353 N N   . SER   B 1 115 ? -31.606 19.182  27.719 1.00 64.82  ? 330 SER   A N   1 
ATOM   2354 C CA  . SER   B 1 115 ? -32.249 19.486  29.015 1.00 63.41  ? 330 SER   A CA  1 
ATOM   2355 C C   . SER   B 1 115 ? -33.669 20.021  28.820 1.00 61.47  ? 330 SER   A C   1 
ATOM   2356 O O   . SER   B 1 115 ? -33.833 21.057  28.191 1.00 68.46  ? 330 SER   A O   1 
ATOM   2357 C CB  . SER   B 1 115 ? -31.406 20.490  29.803 1.00 61.19  ? 330 SER   A CB  1 
ATOM   2358 O OG  . SER   B 1 115 ? -30.290 19.835  30.400 1.00 64.02  ? 330 SER   A OG  1 
ATOM   2359 N N   . SER   B 1 116 ? -34.677 19.294  29.328 1.00 60.84  ? 331 SER   A N   1 
ATOM   2360 C CA  . SER   B 1 116 ? -36.063 19.789  29.475 1.00 62.19  ? 331 SER   A CA  1 
ATOM   2361 C C   . SER   B 1 116 ? -36.425 20.020  30.961 1.00 64.30  ? 331 SER   A C   1 
ATOM   2362 O O   . SER   B 1 116 ? -35.984 19.276  31.845 1.00 64.07  ? 331 SER   A O   1 
ATOM   2363 C CB  . SER   B 1 116 ? -37.063 18.799  28.888 1.00 63.05  ? 331 SER   A CB  1 
ATOM   2364 O OG  . SER   B 1 116 ? -37.152 18.919  27.488 1.00 68.91  ? 331 SER   A OG  1 
ATOM   2365 N N   . GLN   B 1 117 ? -37.232 21.037  31.232 1.00 59.85  ? 332 GLN   A N   1 
ATOM   2366 C CA  . GLN   B 1 117 ? -37.785 21.250  32.576 1.00 67.30  ? 332 GLN   A CA  1 
ATOM   2367 C C   . GLN   B 1 117 ? -39.229 21.697  32.417 1.00 62.89  ? 332 GLN   A C   1 
ATOM   2368 O O   . GLN   B 1 117 ? -39.478 22.653  31.700 1.00 61.57  ? 332 GLN   A O   1 
ATOM   2369 C CB  . GLN   B 1 117 ? -36.969 22.279  33.357 1.00 70.04  ? 332 GLN   A CB  1 
ATOM   2370 C CG  . GLN   B 1 117 ? -37.482 22.514  34.772 1.00 86.83  ? 332 GLN   A CG  1 
ATOM   2371 C CD  . GLN   B 1 117 ? -36.462 23.170  35.704 1.00 97.61  ? 332 GLN   A CD  1 
ATOM   2372 O OE1 . GLN   B 1 117 ? -36.490 22.952  36.922 1.00 104.51 ? 332 GLN   A OE1 1 
ATOM   2373 N NE2 . GLN   B 1 117 ? -35.562 23.971  35.140 1.00 102.95 ? 332 GLN   A NE2 1 
ATOM   2374 N N   . TYR   B 1 118 ? -40.173 20.986  33.033 1.00 55.84  ? 333 TYR   A N   1 
ATOM   2375 C CA  . TYR   B 1 118 ? -41.580 21.378  32.991 1.00 58.12  ? 333 TYR   A CA  1 
ATOM   2376 C C   . TYR   B 1 118 ? -42.040 21.774  34.382 1.00 59.52  ? 333 TYR   A C   1 
ATOM   2377 O O   . TYR   B 1 118 ? -41.280 21.689  35.353 1.00 54.21  ? 333 TYR   A O   1 
ATOM   2378 C CB  . TYR   B 1 118 ? -42.459 20.248  32.451 1.00 61.64  ? 333 TYR   A CB  1 
ATOM   2379 C CG  . TYR   B 1 118 ? -42.116 19.767  31.056 1.00 64.75  ? 333 TYR   A CG  1 
ATOM   2380 C CD1 . TYR   B 1 118 ? -41.128 18.809  30.842 1.00 66.36  ? 333 TYR   A CD1 1 
ATOM   2381 C CD2 . TYR   B 1 118 ? -42.801 20.249  29.951 1.00 63.93  ? 333 TYR   A CD2 1 
ATOM   2382 C CE1 . TYR   B 1 118 ? -40.822 18.370  29.556 1.00 73.01  ? 333 TYR   A CE1 1 
ATOM   2383 C CE2 . TYR   B 1 118 ? -42.514 19.810  28.668 1.00 63.05  ? 333 TYR   A CE2 1 
ATOM   2384 C CZ  . TYR   B 1 118 ? -41.528 18.875  28.458 1.00 69.63  ? 333 TYR   A CZ  1 
ATOM   2385 O OH  . TYR   B 1 118 ? -41.265 18.457  27.156 1.00 73.39  ? 333 TYR   A OH  1 
ATOM   2386 N N   . GLU   B 1 119 ? -43.279 22.249  34.468 1.00 64.89  ? 334 GLU   A N   1 
ATOM   2387 C CA  . GLU   B 1 119 ? -43.895 22.518  35.756 1.00 64.55  ? 334 GLU   A CA  1 
ATOM   2388 C C   . GLU   B 1 119 ? -45.432 22.414  35.756 1.00 63.01  ? 334 GLU   A C   1 
ATOM   2389 O O   . GLU   B 1 119 ? -46.094 22.527  34.705 1.00 56.30  ? 334 GLU   A O   1 
ATOM   2390 C CB  . GLU   B 1 119 ? -43.399 23.867  36.313 1.00 66.60  ? 334 GLU   A CB  1 
ATOM   2391 C CG  . GLU   B 1 119 ? -44.117 25.110  35.805 1.00 69.36  ? 334 GLU   A CG  1 
ATOM   2392 C CD  . GLU   B 1 119 ? -43.497 26.406  36.290 1.00 71.94  ? 334 GLU   A CD  1 
ATOM   2393 O OE1 . GLU   B 1 119 ? -42.527 26.367  37.090 1.00 76.72  ? 334 GLU   A OE1 1 
ATOM   2394 O OE2 . GLU   B 1 119 ? -43.971 27.472  35.830 1.00 76.36  ? 334 GLU   A OE2 1 
ATOM   2395 N N   . SER   B 1 120 ? -45.970 22.183  36.953 1.00 61.23  ? 335 SER   A N   1 
ATOM   2396 C CA  . SER   B 1 120 ? -47.408 22.051  37.154 1.00 66.42  ? 335 SER   A CA  1 
ATOM   2397 C C   . SER   B 1 120 ? -47.826 22.279  38.606 1.00 62.41  ? 335 SER   A C   1 
ATOM   2398 O O   . SER   B 1 120 ? -47.000 22.294  39.511 1.00 57.16  ? 335 SER   A O   1 
ATOM   2399 C CB  . SER   B 1 120 ? -47.860 20.652  36.771 1.00 70.38  ? 335 SER   A CB  1 
ATOM   2400 O OG  . SER   B 1 120 ? -47.346 19.718  37.715 1.00 78.90  ? 335 SER   A OG  1 
ATOM   2401 N N   . LEU   B 1 121 ? -49.137 22.406  38.792 1.00 62.86  ? 336 LEU   A N   1 
ATOM   2402 C CA  . LEU   B 1 121 ? -49.764 22.455  40.110 1.00 62.79  ? 336 LEU   A CA  1 
ATOM   2403 C C   . LEU   B 1 121 ? -50.230 21.097  40.590 1.00 63.37  ? 336 LEU   A C   1 
ATOM   2404 O O   . LEU   B 1 121 ? -50.452 20.933  41.776 1.00 72.28  ? 336 LEU   A O   1 
ATOM   2405 C CB  . LEU   B 1 121 ? -50.941 23.422  40.098 1.00 60.57  ? 336 LEU   A CB  1 
ATOM   2406 C CG  . LEU   B 1 121 ? -50.513 24.874  39.756 1.00 62.07  ? 336 LEU   A CG  1 
ATOM   2407 C CD1 . LEU   B 1 121 ? -51.708 25.790  39.588 1.00 60.09  ? 336 LEU   A CD1 1 
ATOM   2408 C CD2 . LEU   B 1 121 ? -49.542 25.452  40.785 1.00 59.75  ? 336 LEU   A CD2 1 
ATOM   2409 N N   . GLU   B 1 122 ? -50.381 20.128  39.694 1.00 61.19  ? 337 GLU   A N   1 
ATOM   2410 C CA  . GLU   B 1 122 ? -50.766 18.782  40.083 1.00 59.60  ? 337 GLU   A CA  1 
ATOM   2411 C C   . GLU   B 1 122 ? -49.527 17.915  40.215 1.00 61.60  ? 337 GLU   A C   1 
ATOM   2412 O O   . GLU   B 1 122 ? -48.514 18.140  39.547 1.00 55.17  ? 337 GLU   A O   1 
ATOM   2413 C CB  . GLU   B 1 122 ? -51.726 18.166  39.078 1.00 64.19  ? 337 GLU   A CB  1 
ATOM   2414 C CG  . GLU   B 1 122 ? -53.004 18.964  38.885 1.00 71.70  ? 337 GLU   A CG  1 
ATOM   2415 C CD  . GLU   B 1 122 ? -53.615 18.769  37.511 1.00 81.79  ? 337 GLU   A CD  1 
ATOM   2416 O OE1 . GLU   B 1 122 ? -53.944 17.605  37.176 1.00 85.30  ? 337 GLU   A OE1 1 
ATOM   2417 O OE2 . GLU   B 1 122 ? -53.755 19.778  36.773 1.00 82.90  ? 337 GLU   A OE2 1 
ATOM   2418 N N   . HIS   B 1 123 ? -49.612 16.943  41.121 1.00 62.90  ? 338 HIS   A N   1 
ATOM   2419 C CA  . HIS   B 1 123 ? -48.614 15.917  41.240 1.00 60.72  ? 338 HIS   A CA  1 
ATOM   2420 C C   . HIS   B 1 123 ? -48.926 14.891  40.171 1.00 61.79  ? 338 HIS   A C   1 
ATOM   2421 O O   . HIS   B 1 123 ? -50.014 14.317  40.159 1.00 61.96  ? 338 HIS   A O   1 
ATOM   2422 C CB  . HIS   B 1 123 ? -48.631 15.260  42.613 1.00 60.86  ? 338 HIS   A CB  1 
ATOM   2423 C CG  . HIS   B 1 123 ? -47.453 14.373  42.841 1.00 60.79  ? 338 HIS   A CG  1 
ATOM   2424 N ND1 . HIS   B 1 123 ? -47.394 13.085  42.358 1.00 65.41  ? 338 HIS   A ND1 1 
ATOM   2425 C CD2 . HIS   B 1 123 ? -46.261 14.611  43.434 1.00 60.75  ? 338 HIS   A CD2 1 
ATOM   2426 C CE1 . HIS   B 1 123 ? -46.227 12.554  42.676 1.00 65.46  ? 338 HIS   A CE1 1 
ATOM   2427 N NE2 . HIS   B 1 123 ? -45.524 13.459  43.336 1.00 64.00  ? 338 HIS   A NE2 1 
ATOM   2428 N N   . MET   B 1 124 ? -47.977 14.701  39.260 1.00 57.57  ? 339 MET   A N   1 
ATOM   2429 C CA  . MET   B 1 124 ? -48.109 13.730  38.184 1.00 55.64  ? 339 MET   A CA  1 
ATOM   2430 C C   . MET   B 1 124 ? -46.799 12.980  37.965 1.00 53.26  ? 339 MET   A C   1 
ATOM   2431 O O   . MET   B 1 124 ? -45.744 13.338  38.491 1.00 55.50  ? 339 MET   A O   1 
ATOM   2432 C CB  . MET   B 1 124 ? -48.497 14.463  36.901 1.00 56.07  ? 339 MET   A CB  1 
ATOM   2433 C CG  . MET   B 1 124 ? -49.898 15.048  36.933 1.00 54.90  ? 339 MET   A CG  1 
ATOM   2434 S SD  . MET   B 1 124 ? -50.362 15.763  35.348 1.00 52.31  ? 339 MET   A SD  1 
ATOM   2435 C CE  . MET   B 1 124 ? -49.250 17.155  35.305 1.00 55.40  ? 339 MET   A CE  1 
ATOM   2436 N N   . THR   B 1 125 ? -46.881 11.911  37.201 1.00 55.11  ? 340 THR   A N   1 
ATOM   2437 C CA  . THR   B 1 125 ? -45.699 11.286  36.620 1.00 61.38  ? 340 THR   A CA  1 
ATOM   2438 C C   . THR   B 1 125 ? -45.798 11.415  35.078 1.00 55.82  ? 340 THR   A C   1 
ATOM   2439 O O   . THR   B 1 125 ? -46.843 11.126  34.480 1.00 53.50  ? 340 THR   A O   1 
ATOM   2440 C CB  . THR   B 1 125 ? -45.550 9.839   37.123 1.00 67.19  ? 340 THR   A CB  1 
ATOM   2441 O OG1 . THR   B 1 125 ? -46.826 9.202   37.156 1.00 84.26  ? 340 THR   A OG1 1 
ATOM   2442 C CG2 . THR   B 1 125 ? -45.030 9.830   38.537 1.00 69.20  ? 340 THR   A CG2 1 
ATOM   2443 N N   . LEU   B 1 126 ? -44.746 11.925  34.445 1.00 55.01  ? 341 LEU   A N   1 
ATOM   2444 C CA  . LEU   B 1 126 ? -44.821 12.219  33.004 1.00 58.01  ? 341 LEU   A CA  1 
ATOM   2445 C C   . LEU   B 1 126 ? -44.175 11.138  32.146 1.00 56.60  ? 341 LEU   A C   1 
ATOM   2446 O O   . LEU   B 1 126 ? -43.144 10.569  32.513 1.00 52.21  ? 341 LEU   A O   1 
ATOM   2447 C CB  . LEU   B 1 126 ? -44.155 13.551  32.684 1.00 57.47  ? 341 LEU   A CB  1 
ATOM   2448 C CG  . LEU   B 1 126 ? -44.675 14.803  33.384 1.00 58.75  ? 341 LEU   A CG  1 
ATOM   2449 C CD1 . LEU   B 1 126 ? -43.829 15.991  32.921 1.00 59.74  ? 341 LEU   A CD1 1 
ATOM   2450 C CD2 . LEU   B 1 126 ? -46.160 15.045  33.144 1.00 58.58  ? 341 LEU   A CD2 1 
ATOM   2451 N N   . THR   B 1 127 ? -44.793 10.876  30.998 1.00 56.25  ? 342 THR   A N   1 
ATOM   2452 C CA  . THR   B 1 127 ? -44.162 10.118  29.905 1.00 53.15  ? 342 THR   A CA  1 
ATOM   2453 C C   . THR   B 1 127 ? -43.850 11.087  28.784 1.00 50.52  ? 342 THR   A C   1 
ATOM   2454 O O   . THR   B 1 127 ? -44.747 11.745  28.296 1.00 55.37  ? 342 THR   A O   1 
ATOM   2455 C CB  . THR   B 1 127 ? -45.107 9.047   29.376 1.00 48.23  ? 342 THR   A CB  1 
ATOM   2456 O OG1 . THR   B 1 127 ? -45.483 8.195   30.459 1.00 48.26  ? 342 THR   A OG1 1 
ATOM   2457 C CG2 . THR   B 1 127 ? -44.446 8.226   28.279 1.00 50.90  ? 342 THR   A CG2 1 
ATOM   2458 N N   . CYS   B 1 128 ? -42.586 11.194  28.400 1.00 55.92  ? 343 CYS   A N   1 
ATOM   2459 C CA  . CYS   B 1 128 ? -42.161 12.147  27.361 1.00 56.58  ? 343 CYS   A CA  1 
ATOM   2460 C C   . CYS   B 1 128 ? -41.558 11.347  26.221 1.00 57.39  ? 343 CYS   A C   1 
ATOM   2461 O O   . CYS   B 1 128 ? -40.469 10.778  26.371 1.00 56.36  ? 343 CYS   A O   1 
ATOM   2462 C CB  . CYS   B 1 128 ? -41.131 13.134  27.919 1.00 62.86  ? 343 CYS   A CB  1 
ATOM   2463 S SG  . CYS   B 1 128 ? -41.573 13.958  29.494 1.00 72.03  ? 343 CYS   A SG  1 
ATOM   2464 N N   . SER   B 1 129 ? -42.271 11.251  25.104 1.00 52.36  ? 344 SER   A N   1 
ATOM   2465 C CA  . SER   B 1 129 ? -41.678 10.672  23.891 1.00 57.67  ? 344 SER   A CA  1 
ATOM   2466 C C   . SER   B 1 129 ? -41.130 11.761  22.947 1.00 50.93  ? 344 SER   A C   1 
ATOM   2467 O O   . SER   B 1 129 ? -41.651 12.845  22.873 1.00 48.19  ? 344 SER   A O   1 
ATOM   2468 C CB  . SER   B 1 129 ? -42.661 9.748   23.167 1.00 58.53  ? 344 SER   A CB  1 
ATOM   2469 O OG  . SER   B 1 129 ? -43.959 10.262  23.240 1.00 69.95  ? 344 SER   A OG  1 
ATOM   2470 N N   . SER   B 1 130 ? -40.039 11.469  22.265 1.00 49.95  ? 345 SER   A N   1 
ATOM   2471 C CA  . SER   B 1 130 ? -39.479 12.373  21.280 1.00 52.66  ? 345 SER   A CA  1 
ATOM   2472 C C   . SER   B 1 130 ? -39.349 11.506  20.055 1.00 56.40  ? 345 SER   A C   1 
ATOM   2473 O O   . SER   B 1 130 ? -38.717 10.460  20.146 1.00 60.19  ? 345 SER   A O   1 
ATOM   2474 C CB  . SER   B 1 130 ? -38.102 12.860  21.728 1.00 52.54  ? 345 SER   A CB  1 
ATOM   2475 O OG  . SER   B 1 130 ? -38.176 13.642  22.898 1.00 61.97  ? 345 SER   A OG  1 
ATOM   2476 N N   . LYS   B 1 131 ? -39.957 11.893  18.936 1.00 52.56  ? 346 LYS   A N   1 
ATOM   2477 C CA  . LYS   B 1 131 ? -39.778 11.169  17.687 1.00 51.34  ? 346 LYS   A CA  1 
ATOM   2478 C C   . LYS   B 1 131 ? -39.077 12.055  16.661 1.00 52.92  ? 346 LYS   A C   1 
ATOM   2479 O O   . LYS   B 1 131 ? -39.665 13.021  16.153 1.00 50.21  ? 346 LYS   A O   1 
ATOM   2480 C CB  . LYS   B 1 131 ? -41.119 10.690  17.138 1.00 58.70  ? 346 LYS   A CB  1 
ATOM   2481 C CG  . LYS   B 1 131 ? -42.063 10.050  18.154 1.00 65.09  ? 346 LYS   A CG  1 
ATOM   2482 C CD  . LYS   B 1 131 ? -43.238 9.286   17.520 1.00 73.08  ? 346 LYS   A CD  1 
ATOM   2483 C CE  . LYS   B 1 131 ? -43.812 9.979   16.274 1.00 87.63  ? 346 LYS   A CE  1 
ATOM   2484 N NZ  . LYS   B 1 131 ? -44.932 9.295   15.564 1.00 94.43  ? 346 LYS   A NZ  1 
ATOM   2485 N N   . VAL   B 1 132 ? -37.826 11.732  16.346 1.00 49.96  ? 347 VAL   A N   1 
ATOM   2486 C CA  . VAL   B 1 132 ? -37.116 12.395  15.242 1.00 49.37  ? 347 VAL   A CA  1 
ATOM   2487 C C   . VAL   B 1 132 ? -37.540 11.809  13.890 1.00 51.48  ? 347 VAL   A C   1 
ATOM   2488 O O   . VAL   B 1 132 ? -37.398 10.604  13.691 1.00 55.45  ? 347 VAL   A O   1 
ATOM   2489 C CB  . VAL   B 1 132 ? -35.601 12.213  15.382 1.00 49.05  ? 347 VAL   A CB  1 
ATOM   2490 C CG1 . VAL   B 1 132 ? -34.875 12.859  14.196 1.00 48.93  ? 347 VAL   A CG1 1 
ATOM   2491 C CG2 . VAL   B 1 132 ? -35.132 12.743  16.738 1.00 48.69  ? 347 VAL   A CG2 1 
ATOM   2492 N N   . CYS   B 1 133 ? -38.050 12.639  12.975 1.00 48.55  ? 348 CYS   A N   1 
ATOM   2493 C CA  . CYS   B 1 133 ? -38.460 12.175  11.660 1.00 49.21  ? 348 CYS   A CA  1 
ATOM   2494 C C   . CYS   B 1 133 ? -37.535 12.701  10.580 1.00 51.58  ? 348 CYS   A C   1 
ATOM   2495 O O   . CYS   B 1 133 ? -36.951 13.759  10.688 1.00 49.58  ? 348 CYS   A O   1 
ATOM   2496 C CB  . CYS   B 1 133 ? -39.911 12.529  11.342 1.00 51.13  ? 348 CYS   A CB  1 
ATOM   2497 S SG  . CYS   B 1 133 ? -41.081 12.081  12.629 1.00 61.43  ? 348 CYS   A SG  1 
ATOM   2498 N N   . SER   B 1 134 ? -37.387 11.910  9.536  1.00 58.81  ? 349 SER   A N   1 
ATOM   2499 C CA  . SER   B 1 134 ? -36.561 12.267  8.401  1.00 57.05  ? 349 SER   A CA  1 
ATOM   2500 C C   . SER   B 1 134 ? -37.347 11.883  7.160  1.00 56.13  ? 349 SER   A C   1 
ATOM   2501 O O   . SER   B 1 134 ? -37.756 10.724  7.008  1.00 53.43  ? 349 SER   A O   1 
ATOM   2502 C CB  . SER   B 1 134 ? -35.245 11.534  8.453  1.00 54.74  ? 349 SER   A CB  1 
ATOM   2503 O OG  . SER   B 1 134 ? -34.484 11.954  7.377  1.00 52.91  ? 349 SER   A OG  1 
ATOM   2504 N N   . PHE   B 1 135 ? -37.607 12.883  6.318  1.00 56.65  ? 350 PHE   A N   1 
ATOM   2505 C CA  . PHE   B 1 135 ? -38.486 12.745  5.154  1.00 61.89  ? 350 PHE   A CA  1 
ATOM   2506 C C   . PHE   B 1 135 ? -39.868 12.175  5.507  1.00 66.37  ? 350 PHE   A C   1 
ATOM   2507 O O   . PHE   B 1 135 ? -40.393 11.355  4.788  1.00 72.01  ? 350 PHE   A O   1 
ATOM   2508 C CB  . PHE   B 1 135 ? -37.772 11.924  4.067  1.00 54.86  ? 350 PHE   A CB  1 
ATOM   2509 C CG  . PHE   B 1 135 ? -36.464 12.532  3.627  1.00 55.76  ? 350 PHE   A CG  1 
ATOM   2510 C CD1 . PHE   B 1 135 ? -35.270 12.244  4.306  1.00 57.94  ? 350 PHE   A CD1 1 
ATOM   2511 C CD2 . PHE   B 1 135 ? -36.417 13.419  2.547  1.00 56.52  ? 350 PHE   A CD2 1 
ATOM   2512 C CE1 . PHE   B 1 135 ? -34.057 12.821  3.916  1.00 57.35  ? 350 PHE   A CE1 1 
ATOM   2513 C CE2 . PHE   B 1 135 ? -35.203 13.989  2.141  1.00 56.79  ? 350 PHE   A CE2 1 
ATOM   2514 C CZ  . PHE   B 1 135 ? -34.022 13.694  2.825  1.00 56.80  ? 350 PHE   A CZ  1 
ATOM   2515 N N   . GLY   B 1 136 ? -40.445 12.597  6.634  1.00 82.67  ? 351 GLY   A N   1 
ATOM   2516 C CA  . GLY   B 1 136 ? -41.753 12.076  7.096  1.00 86.89  ? 351 GLY   A CA  1 
ATOM   2517 C C   . GLY   B 1 136 ? -41.733 10.704  7.781  1.00 89.87  ? 351 GLY   A C   1 
ATOM   2518 O O   . GLY   B 1 136 ? -42.686 10.330  8.465  1.00 91.31  ? 351 GLY   A O   1 
ATOM   2519 N N   . LYS   B 1 137 ? -40.652 9.951   7.598  1.00 81.61  ? 352 LYS   A N   1 
ATOM   2520 C CA  . LYS   B 1 137 ? -40.502 8.656   8.209  1.00 79.69  ? 352 LYS   A CA  1 
ATOM   2521 C C   . LYS   B 1 137 ? -39.808 8.859   9.543  1.00 66.02  ? 352 LYS   A C   1 
ATOM   2522 O O   . LYS   B 1 137 ? -38.819 9.587   9.642  1.00 57.11  ? 352 LYS   A O   1 
ATOM   2523 C CB  . LYS   B 1 137 ? -39.673 7.739   7.294  1.00 91.99  ? 352 LYS   A CB  1 
ATOM   2524 C CG  . LYS   B 1 137 ? -39.432 6.356   7.873  1.00 104.12 ? 352 LYS   A CG  1 
ATOM   2525 C CD  . LYS   B 1 137 ? -38.603 5.445   6.968  1.00 107.78 ? 352 LYS   A CD  1 
ATOM   2526 C CE  . LYS   B 1 137 ? -38.801 3.977   7.336  1.00 98.86  ? 352 LYS   A CE  1 
ATOM   2527 N NZ  . LYS   B 1 137 ? -38.808 3.745   8.812  1.00 96.52  ? 352 LYS   A NZ  1 
ATOM   2528 N N   . GLN   B 1 138 ? -40.319 8.194   10.566 1.00 60.53  ? 353 GLN   A N   1 
ATOM   2529 C CA  . GLN   B 1 138 ? -39.670 8.184   11.873 1.00 61.08  ? 353 GLN   A CA  1 
ATOM   2530 C C   . GLN   B 1 138 ? -38.364 7.401   11.838 1.00 57.70  ? 353 GLN   A C   1 
ATOM   2531 O O   . GLN   B 1 138 ? -38.280 6.355   11.238 1.00 68.64  ? 353 GLN   A O   1 
ATOM   2532 C CB  . GLN   B 1 138 ? -40.596 7.570   12.902 1.00 60.42  ? 353 GLN   A CB  1 
ATOM   2533 C CG  . GLN   B 1 138 ? -40.107 7.694   14.319 1.00 63.59  ? 353 GLN   A CG  1 
ATOM   2534 C CD  . GLN   B 1 138 ? -40.912 6.792   15.211 1.00 69.88  ? 353 GLN   A CD  1 
ATOM   2535 O OE1 . GLN   B 1 138 ? -42.071 7.087   15.486 1.00 65.03  ? 353 GLN   A OE1 1 
ATOM   2536 N NE2 . GLN   B 1 138 ? -40.324 5.651   15.625 1.00 65.60  ? 353 GLN   A NE2 1 
ATOM   2537 N N   . VAL   B 1 139 ? -37.350 7.944   12.471 1.00 52.14  ? 354 VAL   A N   1 
ATOM   2538 C CA  . VAL   B 1 139 ? -36.043 7.358   12.508 1.00 50.71  ? 354 VAL   A CA  1 
ATOM   2539 C C   . VAL   B 1 139 ? -35.538 7.163   13.941 1.00 53.80  ? 354 VAL   A C   1 
ATOM   2540 O O   . VAL   B 1 139 ? -34.667 6.318   14.145 1.00 56.08  ? 354 VAL   A O   1 
ATOM   2541 C CB  . VAL   B 1 139 ? -35.069 8.237   11.699 1.00 59.19  ? 354 VAL   A CB  1 
ATOM   2542 C CG1 . VAL   B 1 139 ? -33.621 7.897   11.985 1.00 65.00  ? 354 VAL   A CG1 1 
ATOM   2543 C CG2 . VAL   B 1 139 ? -35.325 8.067   10.197 1.00 60.24  ? 354 VAL   A CG2 1 
ATOM   2544 N N   . VAL   B 1 140 ? -36.005 7.965   14.909 1.00 50.25  ? 355 VAL   A N   1 
ATOM   2545 C CA  . VAL   B 1 140 ? -35.698 7.752   16.317 1.00 50.73  ? 355 VAL   A CA  1 
ATOM   2546 C C   . VAL   B 1 140 ? -36.951 7.918   17.166 1.00 53.10  ? 355 VAL   A C   1 
ATOM   2547 O O   . VAL   B 1 140 ? -37.810 8.692   16.815 1.00 56.20  ? 355 VAL   A O   1 
ATOM   2548 C CB  . VAL   B 1 140 ? -34.582 8.667   16.834 1.00 52.20  ? 355 VAL   A CB  1 
ATOM   2549 C CG1 . VAL   B 1 140 ? -34.056 8.160   18.175 1.00 53.71  ? 355 VAL   A CG1 1 
ATOM   2550 C CG2 . VAL   B 1 140 ? -33.426 8.723   15.836 1.00 55.41  ? 355 VAL   A CG2 1 
ATOM   2551 N N   . GLU   B 1 141 ? -37.096 7.078   18.201 1.00 55.08  ? 356 GLU   A N   1 
ATOM   2552 C CA  . GLU   B 1 141 ? -38.039 7.292   19.287 1.00 53.09  ? 356 GLU   A CA  1 
ATOM   2553 C C   . GLU   B 1 141 ? -37.384 7.046   20.634 1.00 49.86  ? 356 GLU   A C   1 
ATOM   2554 O O   . GLU   B 1 141 ? -37.061 5.921   20.943 1.00 53.71  ? 356 GLU   A O   1 
ATOM   2555 C CB  . GLU   B 1 141 ? -39.286 6.450   19.186 1.00 55.95  ? 356 GLU   A CB  1 
ATOM   2556 C CG  . GLU   B 1 141 ? -40.160 6.650   20.427 1.00 65.77  ? 356 GLU   A CG  1 
ATOM   2557 C CD  . GLU   B 1 141 ? -41.627 6.376   20.201 1.00 73.85  ? 356 GLU   A CD  1 
ATOM   2558 O OE1 . GLU   B 1 141 ? -41.926 5.434   19.449 1.00 83.60  ? 356 GLU   A OE1 1 
ATOM   2559 O OE2 . GLU   B 1 141 ? -42.475 7.091   20.788 1.00 77.52  ? 356 GLU   A OE2 1 
ATOM   2560 N N   . LYS   B 1 142 ? -37.222 8.122   21.408 1.00 50.97  ? 357 LYS   A N   1 
ATOM   2561 C CA  . LYS   B 1 142 ? -36.703 8.128   22.757 1.00 53.12  ? 357 LYS   A CA  1 
ATOM   2562 C C   . LYS   B 1 142 ? -37.904 8.288   23.689 1.00 56.46  ? 357 LYS   A C   1 
ATOM   2563 O O   . LYS   B 1 142 ? -38.695 9.193   23.485 1.00 60.39  ? 357 LYS   A O   1 
ATOM   2564 C CB  . LYS   B 1 142 ? -35.725 9.293   22.910 1.00 60.70  ? 357 LYS   A CB  1 
ATOM   2565 C CG  . LYS   B 1 142 ? -34.756 9.210   24.082 1.00 71.27  ? 357 LYS   A CG  1 
ATOM   2566 C CD  . LYS   B 1 142 ? -33.670 10.285  23.959 1.00 81.67  ? 357 LYS   A CD  1 
ATOM   2567 C CE  . LYS   B 1 142 ? -32.608 10.190  25.059 1.00 91.24  ? 357 LYS   A CE  1 
ATOM   2568 N NZ  . LYS   B 1 142 ? -31.499 9.215   24.798 1.00 92.63  ? 357 LYS   A NZ  1 
ATOM   2569 N N   . VAL   B 1 143 ? -38.053 7.399   24.680 1.00 59.00  ? 358 VAL   A N   1 
ATOM   2570 C CA  . VAL   B 1 143 ? -39.179 7.408   25.644 1.00 60.75  ? 358 VAL   A CA  1 
ATOM   2571 C C   . VAL   B 1 143 ? -38.684 7.451   27.098 1.00 63.86  ? 358 VAL   A C   1 
ATOM   2572 O O   . VAL   B 1 143 ? -37.982 6.540   27.537 1.00 64.86  ? 358 VAL   A O   1 
ATOM   2573 C CB  . VAL   B 1 143 ? -40.113 6.202   25.453 1.00 56.41  ? 358 VAL   A CB  1 
ATOM   2574 C CG1 . VAL   B 1 143 ? -41.156 6.137   26.558 1.00 54.28  ? 358 VAL   A CG1 1 
ATOM   2575 C CG2 . VAL   B 1 143 ? -40.793 6.296   24.090 1.00 59.12  ? 358 VAL   A CG2 1 
ATOM   2576 N N   . GLU   B 1 144 ? -39.086 8.506   27.821 1.00 64.60  ? 359 GLU   A N   1 
ATOM   2577 C CA  . GLU   B 1 144 ? -38.627 8.798   29.185 1.00 64.70  ? 359 GLU   A CA  1 
ATOM   2578 C C   . GLU   B 1 144 ? -39.763 9.032   30.173 1.00 63.71  ? 359 GLU   A C   1 
ATOM   2579 O O   . GLU   B 1 144 ? -40.916 9.298   29.798 1.00 61.62  ? 359 GLU   A O   1 
ATOM   2580 C CB  . GLU   B 1 144 ? -37.764 10.043  29.214 1.00 64.76  ? 359 GLU   A CB  1 
ATOM   2581 C CG  . GLU   B 1 144 ? -36.636 10.022  28.227 1.00 75.03  ? 359 GLU   A CG  1 
ATOM   2582 C CD  . GLU   B 1 144 ? -35.345 10.330  28.906 1.00 80.77  ? 359 GLU   A CD  1 
ATOM   2583 O OE1 . GLU   B 1 144 ? -34.845 11.458  28.721 1.00 82.96  ? 359 GLU   A OE1 1 
ATOM   2584 O OE2 . GLU   B 1 144 ? -34.871 9.434   29.646 1.00 80.22  ? 359 GLU   A OE2 1 
ATOM   2585 N N   . THR   B 1 145 ? -39.392 8.936   31.447 1.00 63.79  ? 360 THR   A N   1 
ATOM   2586 C CA  . THR   B 1 145 ? -40.292 9.164   32.559 1.00 64.79  ? 360 THR   A CA  1 
ATOM   2587 C C   . THR   B 1 145 ? -39.652 10.100  33.576 1.00 65.67  ? 360 THR   A C   1 
ATOM   2588 O O   . THR   B 1 145 ? -38.423 10.082  33.806 1.00 59.64  ? 360 THR   A O   1 
ATOM   2589 C CB  . THR   B 1 145 ? -40.708 7.847   33.205 1.00 61.70  ? 360 THR   A CB  1 
ATOM   2590 O OG1 . THR   B 1 145 ? -41.142 6.977   32.173 1.00 61.46  ? 360 THR   A OG1 1 
ATOM   2591 C CG2 . THR   B 1 145 ? -41.897 8.024   34.145 1.00 66.65  ? 360 THR   A CG2 1 
ATOM   2592 N N   . GLU   B 1 146 ? -40.502 10.962  34.133 1.00 66.02  ? 361 GLU   A N   1 
ATOM   2593 C CA  . GLU   B 1 146 ? -40.131 11.858  35.229 1.00 64.40  ? 361 GLU   A CA  1 
ATOM   2594 C C   . GLU   B 1 146 ? -41.333 12.056  36.155 1.00 64.75  ? 361 GLU   A C   1 
ATOM   2595 O O   . GLU   B 1 146 ? -42.454 12.414  35.708 1.00 52.84  ? 361 GLU   A O   1 
ATOM   2596 C CB  . GLU   B 1 146 ? -39.634 13.196  34.703 1.00 64.57  ? 361 GLU   A CB  1 
ATOM   2597 C CG  . GLU   B 1 146 ? -38.876 14.002  35.752 1.00 73.84  ? 361 GLU   A CG  1 
ATOM   2598 C CD  . GLU   B 1 146 ? -37.506 13.435  36.113 1.00 74.32  ? 361 GLU   A CD  1 
ATOM   2599 O OE1 . GLU   B 1 146 ? -36.918 13.934  37.088 1.00 75.45  ? 361 GLU   A OE1 1 
ATOM   2600 O OE2 . GLU   B 1 146 ? -37.002 12.515  35.437 1.00 75.52  ? 361 GLU   A OE2 1 
ATOM   2601 N N   . ARG   B 1 147 ? -41.085 11.773  37.433 1.00 68.23  ? 362 ARG   A N   1 
ATOM   2602 C CA  . ARG   B 1 147 ? -42.081 11.888  38.496 1.00 69.77  ? 362 ARG   A CA  1 
ATOM   2603 C C   . ARG   B 1 147 ? -41.937 13.305  39.043 1.00 59.10  ? 362 ARG   A C   1 
ATOM   2604 O O   . ARG   B 1 147 ? -40.833 13.834  39.109 1.00 62.73  ? 362 ARG   A O   1 
ATOM   2605 C CB  . ARG   B 1 147 ? -41.817 10.814  39.562 1.00 75.10  ? 362 ARG   A CB  1 
ATOM   2606 C CG  . ARG   B 1 147 ? -42.723 10.836  40.789 1.00 85.04  ? 362 ARG   A CG  1 
ATOM   2607 C CD  . ARG   B 1 147 ? -42.424 9.650   41.706 1.00 89.86  ? 362 ARG   A CD  1 
ATOM   2608 N NE  . ARG   B 1 147 ? -43.511 9.339   42.640 1.00 93.45  ? 362 ARG   A NE  1 
ATOM   2609 C CZ  . ARG   B 1 147 ? -43.865 10.070  43.710 1.00 101.37 ? 362 ARG   A CZ  1 
ATOM   2610 N NH1 . ARG   B 1 147 ? -43.241 11.216  44.019 1.00 100.69 ? 362 ARG   A NH1 1 
ATOM   2611 N NH2 . ARG   B 1 147 ? -44.873 9.658   44.487 1.00 98.30  ? 362 ARG   A NH2 1 
ATOM   2612 N N   . ALA   B 1 148 ? -43.043 13.937  39.408 1.00 55.61  ? 363 ALA   A N   1 
ATOM   2613 C CA  . ALA   B 1 148 ? -42.997 15.311  39.923 1.00 50.46  ? 363 ALA   A CA  1 
ATOM   2614 C C   . ALA   B 1 148 ? -42.081 15.386  41.107 1.00 48.59  ? 363 ALA   A C   1 
ATOM   2615 O O   . ALA   B 1 148 ? -42.002 14.442  41.883 1.00 48.27  ? 363 ALA   A O   1 
ATOM   2616 C CB  . ALA   B 1 148 ? -44.375 15.762  40.351 1.00 49.35  ? 363 ALA   A CB  1 
ATOM   2617 N N   . GLN   B 1 149 ? -41.431 16.527  41.251 1.00 54.37  ? 364 GLN   A N   1 
ATOM   2618 C CA  . GLN   B 1 149 ? -40.630 16.886  42.415 1.00 60.43  ? 364 GLN   A CA  1 
ATOM   2619 C C   . GLN   B 1 149 ? -41.195 18.222  43.003 1.00 65.73  ? 364 GLN   A C   1 
ATOM   2620 O O   . GLN   B 1 149 ? -41.414 19.190  42.248 1.00 60.51  ? 364 GLN   A O   1 
ATOM   2621 C CB  . GLN   B 1 149 ? -39.188 17.077  41.927 1.00 68.11  ? 364 GLN   A CB  1 
ATOM   2622 C CG  . GLN   B 1 149 ? -38.084 16.645  42.880 1.00 76.80  ? 364 GLN   A CG  1 
ATOM   2623 C CD  . GLN   B 1 149 ? -37.697 17.756  43.836 1.00 81.80  ? 364 GLN   A CD  1 
ATOM   2624 O OE1 . GLN   B 1 149 ? -37.419 18.895  43.416 1.00 81.71  ? 364 GLN   A OE1 1 
ATOM   2625 N NE2 . GLN   B 1 149 ? -37.699 17.443  45.133 1.00 76.50  ? 364 GLN   A NE2 1 
ATOM   2626 N N   . LEU   B 1 150 ? -41.421 18.290  44.329 1.00 73.41  ? 365 LEU   A N   1 
ATOM   2627 C CA  . LEU   B 1 150 ? -41.912 19.543  45.011 1.00 66.35  ? 365 LEU   A CA  1 
ATOM   2628 C C   . LEU   B 1 150 ? -40.820 20.624  45.221 1.00 62.42  ? 365 LEU   A C   1 
ATOM   2629 O O   . LEU   B 1 150 ? -39.722 20.339  45.679 1.00 63.96  ? 365 LEU   A O   1 
ATOM   2630 C CB  . LEU   B 1 150 ? -42.608 19.228  46.353 1.00 64.28  ? 365 LEU   A CB  1 
ATOM   2631 C CG  . LEU   B 1 150 ? -43.248 20.398  47.162 1.00 66.81  ? 365 LEU   A CG  1 
ATOM   2632 C CD1 . LEU   B 1 150 ? -44.383 21.120  46.448 1.00 62.28  ? 365 LEU   A CD1 1 
ATOM   2633 C CD2 . LEU   B 1 150 ? -43.755 19.914  48.514 1.00 71.54  ? 365 LEU   A CD2 1 
ATOM   2634 N N   . GLU   B 1 151 ? -41.156 21.867  44.892 1.00 65.59  ? 366 GLU   A N   1 
ATOM   2635 C CA  . GLU   B 1 151 ? -40.228 22.998  44.975 1.00 71.19  ? 366 GLU   A CA  1 
ATOM   2636 C C   . GLU   B 1 151 ? -40.990 24.325  44.803 1.00 75.44  ? 366 GLU   A C   1 
ATOM   2637 O O   . GLU   B 1 151 ? -41.610 24.550  43.754 1.00 75.92  ? 366 GLU   A O   1 
ATOM   2638 C CB  . GLU   B 1 151 ? -39.164 22.882  43.883 1.00 71.12  ? 366 GLU   A CB  1 
ATOM   2639 C CG  . GLU   B 1 151 ? -38.288 24.115  43.706 1.00 76.29  ? 366 GLU   A CG  1 
ATOM   2640 C CD  . GLU   B 1 151 ? -37.259 23.939  42.609 1.00 77.59  ? 366 GLU   A CD  1 
ATOM   2641 O OE1 . GLU   B 1 151 ? -37.268 24.724  41.637 1.00 84.31  ? 366 GLU   A OE1 1 
ATOM   2642 O OE2 . GLU   B 1 151 ? -36.450 23.000  42.710 1.00 71.62  ? 366 GLU   A OE2 1 
ATOM   2643 N N   . ASP   B 1 152 ? -40.912 25.195  45.813 1.00 74.31  ? 367 ASP   A N   1 
ATOM   2644 C CA  . ASP   B 1 152 ? -41.556 26.525  45.800 1.00 77.11  ? 367 ASP   A CA  1 
ATOM   2645 C C   . ASP   B 1 152 ? -43.079 26.472  45.579 1.00 71.71  ? 367 ASP   A C   1 
ATOM   2646 O O   . ASP   B 1 152 ? -43.600 27.242  44.781 1.00 71.30  ? 367 ASP   A O   1 
ATOM   2647 C CB  . ASP   B 1 152 ? -40.916 27.467  44.742 1.00 84.88  ? 367 ASP   A CB  1 
ATOM   2648 C CG  . ASP   B 1 152 ? -39.406 27.673  44.934 1.00 93.91  ? 367 ASP   A CG  1 
ATOM   2649 O OD1 . ASP   B 1 152 ? -38.827 27.138  45.911 1.00 97.23  ? 367 ASP   A OD1 1 
ATOM   2650 O OD2 . ASP   B 1 152 ? -38.799 28.383  44.091 1.00 89.27  ? 367 ASP   A OD2 1 
ATOM   2651 N N   . GLY   B 1 153 ? -43.788 25.575  46.269 1.00 65.65  ? 368 GLY   A N   1 
ATOM   2652 C CA  . GLY   B 1 153 ? -45.254 25.494  46.155 1.00 66.86  ? 368 GLY   A CA  1 
ATOM   2653 C C   . GLY   B 1 153 ? -45.824 25.104  44.791 1.00 71.55  ? 368 GLY   A C   1 
ATOM   2654 O O   . GLY   B 1 153 ? -46.975 25.422  44.473 1.00 76.78  ? 368 GLY   A O   1 
ATOM   2655 N N   . ARG   B 1 154 ? -45.016 24.410  43.991 1.00 71.69  ? 369 ARG   A N   1 
ATOM   2656 C CA  . ARG   B 1 154 ? -45.432 23.868  42.705 1.00 69.75  ? 369 ARG   A CA  1 
ATOM   2657 C C   . ARG   B 1 154 ? -44.575 22.642  42.334 1.00 64.05  ? 369 ARG   A C   1 
ATOM   2658 O O   . ARG   B 1 154 ? -43.542 22.380  42.948 1.00 56.49  ? 369 ARG   A O   1 
ATOM   2659 C CB  . ARG   B 1 154 ? -45.382 24.952  41.621 1.00 79.29  ? 369 ARG   A CB  1 
ATOM   2660 C CG  . ARG   B 1 154 ? -44.068 25.729  41.482 1.00 88.45  ? 369 ARG   A CG  1 
ATOM   2661 C CD  . ARG   B 1 154 ? -43.035 25.035  40.597 1.00 96.06  ? 369 ARG   A CD  1 
ATOM   2662 N NE  . ARG   B 1 154 ? -42.297 25.975  39.740 1.00 101.60 ? 369 ARG   A NE  1 
ATOM   2663 C CZ  . ARG   B 1 154 ? -40.984 26.233  39.777 1.00 107.49 ? 369 ARG   A CZ  1 
ATOM   2664 N NH1 . ARG   B 1 154 ? -40.489 27.106  38.902 1.00 110.79 ? 369 ARG   A NH1 1 
ATOM   2665 N NH2 . ARG   B 1 154 ? -40.153 25.641  40.648 1.00 106.25 ? 369 ARG   A NH2 1 
ATOM   2666 N N   . PHE   B 1 155 ? -45.031 21.877  41.355 1.00 61.10  ? 370 PHE   A N   1 
ATOM   2667 C CA  . PHE   B 1 155 ? -44.340 20.657  40.946 1.00 64.10  ? 370 PHE   A CA  1 
ATOM   2668 C C   . PHE   B 1 155 ? -43.491 20.885  39.710 1.00 59.49  ? 370 PHE   A C   1 
ATOM   2669 O O   . PHE   B 1 155 ? -43.948 21.428  38.710 1.00 56.82  ? 370 PHE   A O   1 
ATOM   2670 C CB  . PHE   B 1 155 ? -45.336 19.538  40.729 1.00 64.47  ? 370 PHE   A CB  1 
ATOM   2671 C CG  . PHE   B 1 155 ? -46.055 19.160  41.981 1.00 65.56  ? 370 PHE   A CG  1 
ATOM   2672 C CD1 . PHE   B 1 155 ? -45.414 18.429  42.966 1.00 67.13  ? 370 PHE   A CD1 1 
ATOM   2673 C CD2 . PHE   B 1 155 ? -47.361 19.587  42.205 1.00 69.42  ? 370 PHE   A CD2 1 
ATOM   2674 C CE1 . PHE   B 1 155 ? -46.087 18.094  44.132 1.00 71.48  ? 370 PHE   A CE1 1 
ATOM   2675 C CE2 . PHE   B 1 155 ? -48.039 19.253  43.370 1.00 62.73  ? 370 PHE   A CE2 1 
ATOM   2676 C CZ  . PHE   B 1 155 ? -47.405 18.508  44.331 1.00 64.87  ? 370 PHE   A CZ  1 
ATOM   2677 N N   . VAL   B 1 156 ? -42.235 20.488  39.826 1.00 55.28  ? 371 VAL   A N   1 
ATOM   2678 C CA  . VAL   B 1 156 ? -41.265 20.661  38.779 1.00 56.75  ? 371 VAL   A CA  1 
ATOM   2679 C C   . VAL   B 1 156 ? -40.877 19.249  38.262 1.00 58.05  ? 371 VAL   A C   1 
ATOM   2680 O O   . VAL   B 1 156 ? -40.859 18.256  39.020 1.00 56.70  ? 371 VAL   A O   1 
ATOM   2681 C CB  . VAL   B 1 156 ? -40.089 21.547  39.293 1.00 59.81  ? 371 VAL   A CB  1 
ATOM   2682 C CG1 . VAL   B 1 156 ? -39.052 20.747  40.095 1.00 58.31  ? 371 VAL   A CG1 1 
ATOM   2683 C CG2 . VAL   B 1 156 ? -39.418 22.271  38.143 1.00 66.27  ? 371 VAL   A CG2 1 
ATOM   2684 N N   . TYR   B 1 157 ? -40.631 19.152  36.956 1.00 55.90  ? 372 TYR   A N   1 
ATOM   2685 C CA  . TYR   B 1 157 ? -40.249 17.895  36.307 1.00 56.93  ? 372 TYR   A CA  1 
ATOM   2686 C C   . TYR   B 1 157 ? -38.980 18.186  35.497 1.00 62.13  ? 372 TYR   A C   1 
ATOM   2687 O O   . TYR   B 1 157 ? -39.060 18.714  34.387 1.00 67.17  ? 372 TYR   A O   1 
ATOM   2688 C CB  . TYR   B 1 157 ? -41.374 17.378  35.390 1.00 56.23  ? 372 TYR   A CB  1 
ATOM   2689 C CG  . TYR   B 1 157 ? -42.719 17.274  36.062 1.00 58.77  ? 372 TYR   A CG  1 
ATOM   2690 C CD1 . TYR   B 1 157 ? -43.451 18.418  36.371 1.00 59.70  ? 372 TYR   A CD1 1 
ATOM   2691 C CD2 . TYR   B 1 157 ? -43.280 16.033  36.389 1.00 55.86  ? 372 TYR   A CD2 1 
ATOM   2692 C CE1 . TYR   B 1 157 ? -44.685 18.330  37.001 1.00 57.71  ? 372 TYR   A CE1 1 
ATOM   2693 C CE2 . TYR   B 1 157 ? -44.526 15.946  36.996 1.00 54.29  ? 372 TYR   A CE2 1 
ATOM   2694 C CZ  . TYR   B 1 157 ? -45.219 17.099  37.306 1.00 53.70  ? 372 TYR   A CZ  1 
ATOM   2695 O OH  . TYR   B 1 157 ? -46.434 17.035  37.923 1.00 56.81  ? 372 TYR   A OH  1 
ATOM   2696 N N   . ARG   B 1 158 ? -37.825 17.847  36.062 1.00 58.61  ? 373 ARG   A N   1 
ATOM   2697 C CA  . ARG   B 1 158 ? -36.537 18.114  35.466 1.00 57.45  ? 373 ARG   A CA  1 
ATOM   2698 C C   . ARG   B 1 158 ? -36.014 16.890  34.711 1.00 65.24  ? 373 ARG   A C   1 
ATOM   2699 O O   . ARG   B 1 158 ? -35.766 15.870  35.337 1.00 68.73  ? 373 ARG   A O   1 
ATOM   2700 C CB  . ARG   B 1 158 ? -35.565 18.479  36.579 1.00 67.89  ? 373 ARG   A CB  1 
ATOM   2701 C CG  . ARG   B 1 158 ? -35.753 19.900  37.085 1.00 75.71  ? 373 ARG   A CG  1 
ATOM   2702 C CD  . ARG   B 1 158 ? -34.528 20.429  37.817 1.00 79.33  ? 373 ARG   A CD  1 
ATOM   2703 N NE  . ARG   B 1 158 ? -34.776 20.480  39.250 1.00 85.61  ? 373 ARG   A NE  1 
ATOM   2704 C CZ  . ARG   B 1 158 ? -35.185 21.551  39.933 1.00 83.42  ? 373 ARG   A CZ  1 
ATOM   2705 N NH1 . ARG   B 1 158 ? -35.403 22.741  39.356 1.00 72.46  ? 373 ARG   A NH1 1 
ATOM   2706 N NH2 . ARG   B 1 158 ? -35.379 21.418  41.237 1.00 91.57  ? 373 ARG   A NH2 1 
ATOM   2707 N N   . LEU   B 1 159 ? -35.863 16.980  33.377 1.00 68.10  ? 374 LEU   A N   1 
ATOM   2708 C CA  . LEU   B 1 159 ? -35.201 15.921  32.552 1.00 66.51  ? 374 LEU   A CA  1 
ATOM   2709 C C   . LEU   B 1 159 ? -33.924 16.518  31.943 1.00 63.87  ? 374 LEU   A C   1 
ATOM   2710 O O   . LEU   B 1 159 ? -33.887 16.979  30.795 1.00 67.48  ? 374 LEU   A O   1 
ATOM   2711 C CB  . LEU   B 1 159 ? -36.126 15.334  31.470 1.00 66.62  ? 374 LEU   A CB  1 
ATOM   2712 C CG  . LEU   B 1 159 ? -37.455 14.713  31.934 1.00 65.18  ? 374 LEU   A CG  1 
ATOM   2713 C CD1 . LEU   B 1 159 ? -38.552 15.766  32.057 1.00 64.15  ? 374 LEU   A CD1 1 
ATOM   2714 C CD2 . LEU   B 1 159 ? -37.910 13.630  30.974 1.00 64.24  ? 374 LEU   A CD2 1 
ATOM   2715 N N   . LEU   B 1 160 ? -32.881 16.497  32.755 1.00 65.27  ? 375 LEU   A N   1 
ATOM   2716 C CA  . LEU   B 1 160 ? -31.694 17.296  32.550 1.00 70.83  ? 375 LEU   A CA  1 
ATOM   2717 C C   . LEU   B 1 160 ? -30.644 16.390  31.960 1.00 69.63  ? 375 LEU   A C   1 
ATOM   2718 O O   . LEU   B 1 160 ? -30.639 15.197  32.262 1.00 63.62  ? 375 LEU   A O   1 
ATOM   2719 C CB  . LEU   B 1 160 ? -31.224 17.904  33.881 1.00 72.00  ? 375 LEU   A CB  1 
ATOM   2720 C CG  . LEU   B 1 160 ? -31.819 19.280  34.218 1.00 77.35  ? 375 LEU   A CG  1 
ATOM   2721 C CD1 . LEU   B 1 160 ? -33.331 19.343  34.008 1.00 77.71  ? 375 LEU   A CD1 1 
ATOM   2722 C CD2 . LEU   B 1 160 ? -31.442 19.676  35.642 1.00 79.72  ? 375 LEU   A CD2 1 
ATOM   2723 N N   . ARG   B 1 161 ? -29.823 16.965  31.073 1.00 71.46  ? 376 ARG   A N   1 
ATOM   2724 C CA  . ARG   B 1 161 ? -28.663 16.316  30.429 1.00 67.80  ? 376 ARG   A CA  1 
ATOM   2725 C C   . ARG   B 1 161 ? -28.868 14.884  29.978 1.00 60.61  ? 376 ARG   A C   1 
ATOM   2726 O O   . ARG   B 1 161 ? -28.005 14.024  30.205 1.00 63.72  ? 376 ARG   A O   1 
ATOM   2727 C CB  . ARG   B 1 161 ? -27.448 16.394  31.352 1.00 71.85  ? 376 ARG   A CB  1 
ATOM   2728 C CG  . ARG   B 1 161 ? -27.113 17.813  31.792 1.00 82.13  ? 376 ARG   A CG  1 
ATOM   2729 C CD  . ARG   B 1 161 ? -26.018 17.803  32.835 1.00 86.97  ? 376 ARG   A CD  1 
ATOM   2730 N NE  . ARG   B 1 161 ? -24.854 17.082  32.333 1.00 90.57  ? 376 ARG   A NE  1 
ATOM   2731 C CZ  . ARG   B 1 161 ? -23.981 17.570  31.457 1.00 97.01  ? 376 ARG   A CZ  1 
ATOM   2732 N NH1 . ARG   B 1 161 ? -24.113 18.812  30.974 1.00 101.48 ? 376 ARG   A NH1 1 
ATOM   2733 N NH2 . ARG   B 1 161 ? -22.960 16.808  31.061 1.00 96.08  ? 376 ARG   A NH2 1 
ATOM   2734 N N   . SER   B 1 162 ? -30.021 14.617  29.377 1.00 54.24  ? 377 SER   A N   1 
ATOM   2735 C CA  . SER   B 1 162 ? -30.245 13.358  28.655 1.00 59.62  ? 377 SER   A CA  1 
ATOM   2736 C C   . SER   B 1 162 ? -29.243 13.345  27.455 1.00 63.26  ? 377 SER   A C   1 
ATOM   2737 O O   . SER   B 1 162 ? -29.142 14.347  26.726 1.00 60.59  ? 377 SER   A O   1 
ATOM   2738 C CB  . SER   B 1 162 ? -31.722 13.319  28.184 1.00 61.59  ? 377 SER   A CB  1 
ATOM   2739 O OG  . SER   B 1 162 ? -31.976 12.266  27.271 1.00 67.40  ? 377 SER   A OG  1 
ATOM   2740 N N   . PRO   B 1 163 ? -28.455 12.267  27.274 1.00 65.42  ? 378 PRO   A N   1 
ATOM   2741 C CA  . PRO   B 1 163 ? -27.567 12.245  26.095 1.00 65.85  ? 378 PRO   A CA  1 
ATOM   2742 C C   . PRO   B 1 163 ? -28.361 12.213  24.809 1.00 59.08  ? 378 PRO   A C   1 
ATOM   2743 O O   . PRO   B 1 163 ? -29.161 11.311  24.579 1.00 60.62  ? 378 PRO   A O   1 
ATOM   2744 C CB  . PRO   B 1 163 ? -26.774 10.941  26.240 1.00 71.60  ? 378 PRO   A CB  1 
ATOM   2745 C CG  . PRO   B 1 163 ? -26.974 10.530  27.658 1.00 74.80  ? 378 PRO   A CG  1 
ATOM   2746 C CD  . PRO   B 1 163 ? -28.339 11.025  28.045 1.00 74.06  ? 378 PRO   A CD  1 
ATOM   2747 N N   . MET   B 1 164 ? -28.166 13.238  24.009 1.00 55.67  ? 379 MET   A N   1 
ATOM   2748 C CA  . MET   B 1 164 ? -28.740 13.313  22.705 1.00 57.77  ? 379 MET   A CA  1 
ATOM   2749 C C   . MET   B 1 164 ? -28.367 12.045  21.989 1.00 56.80  ? 379 MET   A C   1 
ATOM   2750 O O   . MET   B 1 164 ? -27.223 11.593  22.104 1.00 58.71  ? 379 MET   A O   1 
ATOM   2751 C CB  . MET   B 1 164 ? -28.136 14.501  21.987 1.00 62.47  ? 379 MET   A CB  1 
ATOM   2752 C CG  . MET   B 1 164 ? -28.638 14.715  20.573 1.00 67.71  ? 379 MET   A CG  1 
ATOM   2753 S SD  . MET   B 1 164 ? -27.885 16.206  19.893 1.00 68.31  ? 379 MET   A SD  1 
ATOM   2754 C CE  . MET   B 1 164 ? -28.602 17.479  20.936 1.00 67.65  ? 379 MET   A CE  1 
ATOM   2755 N N   . CYS   B 1 165 ? -29.333 11.471  21.275 1.00 54.54  ? 380 CYS   A N   1 
ATOM   2756 C CA  . CYS   B 1 165 ? -29.121 10.214  20.576 1.00 58.50  ? 380 CYS   A CA  1 
ATOM   2757 C C   . CYS   B 1 165 ? -28.044 10.350  19.497 1.00 59.76  ? 380 CYS   A C   1 
ATOM   2758 O O   . CYS   B 1 165 ? -27.788 11.429  18.969 1.00 52.58  ? 380 CYS   A O   1 
ATOM   2759 C CB  . CYS   B 1 165 ? -30.424 9.688   19.979 1.00 62.63  ? 380 CYS   A CB  1 
ATOM   2760 S SG  . CYS   B 1 165 ? -30.851 10.408  18.384 1.00 71.90  ? 380 CYS   A SG  1 
ATOM   2761 N N   . GLU   B 1 166 ? -27.406 9.235   19.194 1.00 66.90  ? 381 GLU   A N   1 
ATOM   2762 C CA  . GLU   B 1 166 ? -26.177 9.255   18.416 1.00 72.99  ? 381 GLU   A CA  1 
ATOM   2763 C C   . GLU   B 1 166 ? -26.475 9.487   16.939 1.00 66.76  ? 381 GLU   A C   1 
ATOM   2764 O O   . GLU   B 1 166 ? -25.605 9.915   16.200 1.00 66.14  ? 381 GLU   A O   1 
ATOM   2765 C CB  . GLU   B 1 166 ? -25.374 7.968   18.645 1.00 82.62  ? 381 GLU   A CB  1 
ATOM   2766 C CG  . GLU   B 1 166 ? -24.844 7.823   20.085 1.00 90.58  ? 381 GLU   A CG  1 
ATOM   2767 C CD  . GLU   B 1 166 ? -25.805 7.150   21.074 1.00 95.08  ? 381 GLU   A CD  1 
ATOM   2768 O OE1 . GLU   B 1 166 ? -26.987 6.896   20.747 1.00 99.81  ? 381 GLU   A OE1 1 
ATOM   2769 O OE2 . GLU   B 1 166 ? -25.368 6.877   22.210 1.00 99.07  ? 381 GLU   A OE2 1 
ATOM   2770 N N   . TYR   B 1 167 ? -27.714 9.227   16.524 1.00 65.22  ? 382 TYR   A N   1 
ATOM   2771 C CA  . TYR   B 1 167 ? -28.177 9.579   15.197 1.00 59.39  ? 382 TYR   A CA  1 
ATOM   2772 C C   . TYR   B 1 167 ? -28.017 11.092  15.008 1.00 62.34  ? 382 TYR   A C   1 
ATOM   2773 O O   . TYR   B 1 167 ? -27.353 11.555  14.072 1.00 58.82  ? 382 TYR   A O   1 
ATOM   2774 C CB  . TYR   B 1 167 ? -29.639 9.141   14.996 1.00 61.15  ? 382 TYR   A CB  1 
ATOM   2775 C CG  . TYR   B 1 167 ? -30.190 9.555   13.653 1.00 64.21  ? 382 TYR   A CG  1 
ATOM   2776 C CD1 . TYR   B 1 167 ? -30.757 10.808  13.476 1.00 68.65  ? 382 TYR   A CD1 1 
ATOM   2777 C CD2 . TYR   B 1 167 ? -30.091 8.717   12.537 1.00 69.77  ? 382 TYR   A CD2 1 
ATOM   2778 C CE1 . TYR   B 1 167 ? -31.227 11.221  12.232 1.00 75.30  ? 382 TYR   A CE1 1 
ATOM   2779 C CE2 . TYR   B 1 167 ? -30.563 9.117   11.289 1.00 70.33  ? 382 TYR   A CE2 1 
ATOM   2780 C CZ  . TYR   B 1 167 ? -31.135 10.373  11.142 1.00 73.04  ? 382 TYR   A CZ  1 
ATOM   2781 O OH  . TYR   B 1 167 ? -31.633 10.806  9.930  1.00 76.67  ? 382 TYR   A OH  1 
ATOM   2782 N N   . LEU   B 1 168 ? -28.614 11.859  15.918 1.00 62.00  ? 383 LEU   A N   1 
ATOM   2783 C CA  . LEU   B 1 168 ? -28.519 13.308  15.867 1.00 59.19  ? 383 LEU   A CA  1 
ATOM   2784 C C   . LEU   B 1 168 ? -27.099 13.808  15.981 1.00 57.69  ? 383 LEU   A C   1 
ATOM   2785 O O   . LEU   B 1 168 ? -26.775 14.809  15.366 1.00 64.85  ? 383 LEU   A O   1 
ATOM   2786 C CB  . LEU   B 1 168 ? -29.351 13.978  16.970 1.00 61.10  ? 383 LEU   A CB  1 
ATOM   2787 C CG  . LEU   B 1 168 ? -30.861 14.043  16.822 1.00 67.83  ? 383 LEU   A CG  1 
ATOM   2788 C CD1 . LEU   B 1 168 ? -31.473 14.786  17.997 1.00 72.93  ? 383 LEU   A CD1 1 
ATOM   2789 C CD2 . LEU   B 1 168 ? -31.284 14.729  15.540 1.00 71.98  ? 383 LEU   A CD2 1 
ATOM   2790 N N   . VAL   B 1 169 ? -26.267 13.163  16.795 1.00 55.99  ? 384 VAL   A N   1 
ATOM   2791 C CA  . VAL   B 1 169 ? -24.895 13.636  16.997 1.00 52.71  ? 384 VAL   A CA  1 
ATOM   2792 C C   . VAL   B 1 169 ? -24.131 13.544  15.668 1.00 53.52  ? 384 VAL   A C   1 
ATOM   2793 O O   . VAL   B 1 169 ? -23.420 14.471  15.292 1.00 47.64  ? 384 VAL   A O   1 
ATOM   2794 C CB  . VAL   B 1 169 ? -24.153 12.851  18.091 1.00 52.70  ? 384 VAL   A CB  1 
ATOM   2795 C CG1 . VAL   B 1 169 ? -22.704 13.315  18.181 1.00 53.62  ? 384 VAL   A CG1 1 
ATOM   2796 C CG2 . VAL   B 1 169 ? -24.829 13.028  19.454 1.00 56.12  ? 384 VAL   A CG2 1 
ATOM   2797 N N   . ASN   B 1 170 ? -24.305 12.439  14.951 1.00 52.62  ? 385 ASN   A N   1 
ATOM   2798 C CA  . ASN   B 1 170 ? -23.635 12.270  13.656 1.00 58.85  ? 385 ASN   A CA  1 
ATOM   2799 C C   . ASN   B 1 170 ? -24.167 13.230  12.589 1.00 58.22  ? 385 ASN   A C   1 
ATOM   2800 O O   . ASN   B 1 170 ? -23.380 13.917  11.931 1.00 57.81  ? 385 ASN   A O   1 
ATOM   2801 C CB  . ASN   B 1 170 ? -23.727 10.816  13.194 1.00 63.00  ? 385 ASN   A CB  1 
ATOM   2802 C CG  . ASN   B 1 170 ? -22.932 9.877   14.098 1.00 68.65  ? 385 ASN   A CG  1 
ATOM   2803 O OD1 . ASN   B 1 170 ? -21.814 10.200  14.535 1.00 70.17  ? 385 ASN   A OD1 1 
ATOM   2804 N ND2 . ASN   B 1 170 ? -23.507 8.718   14.398 1.00 70.61  ? 385 ASN   A ND2 1 
ATOM   2805 N N   . PHE   B 1 171 ? -25.498 13.281  12.473 1.00 53.17  ? 386 PHE   A N   1 
ATOM   2806 C CA  . PHE   B 1 171 ? -26.228 14.266  11.676 1.00 52.39  ? 386 PHE   A CA  1 
ATOM   2807 C C   . PHE   B 1 171 ? -25.741 15.712  11.897 1.00 58.53  ? 386 PHE   A C   1 
ATOM   2808 O O   . PHE   B 1 171 ? -25.617 16.453  10.913 1.00 59.08  ? 386 PHE   A O   1 
ATOM   2809 C CB  . PHE   B 1 171 ? -27.742 14.146  11.938 1.00 50.67  ? 386 PHE   A CB  1 
ATOM   2810 C CG  . PHE   B 1 171 ? -28.584 15.112  11.158 1.00 50.72  ? 386 PHE   A CG  1 
ATOM   2811 C CD1 . PHE   B 1 171 ? -28.899 14.856  9.833  1.00 53.55  ? 386 PHE   A CD1 1 
ATOM   2812 C CD2 . PHE   B 1 171 ? -29.069 16.275  11.747 1.00 48.67  ? 386 PHE   A CD2 1 
ATOM   2813 C CE1 . PHE   B 1 171 ? -29.673 15.740  9.093  1.00 56.45  ? 386 PHE   A CE1 1 
ATOM   2814 C CE2 . PHE   B 1 171 ? -29.850 17.157  11.020 1.00 51.60  ? 386 PHE   A CE2 1 
ATOM   2815 C CZ  . PHE   B 1 171 ? -30.148 16.895  9.684  1.00 54.70  ? 386 PHE   A CZ  1 
ATOM   2816 N N   . LEU   B 1 172 ? -25.435 16.089  13.147 1.00 55.50  ? 387 LEU   A N   1 
ATOM   2817 C CA  . LEU   B 1 172 ? -24.908 17.436  13.458 1.00 55.78  ? 387 LEU   A CA  1 
ATOM   2818 C C   . LEU   B 1 172 ? -23.455 17.616  13.065 1.00 55.10  ? 387 LEU   A C   1 
ATOM   2819 O O   . LEU   B 1 172 ? -23.074 18.698  12.622 1.00 53.83  ? 387 LEU   A O   1 
ATOM   2820 C CB  . LEU   B 1 172 ? -25.022 17.776  14.940 1.00 54.57  ? 387 LEU   A CB  1 
ATOM   2821 C CG  . LEU   B 1 172 ? -26.418 18.047  15.511 1.00 62.15  ? 387 LEU   A CG  1 
ATOM   2822 C CD1 . LEU   B 1 172 ? -26.406 18.070  17.047 1.00 62.26  ? 387 LEU   A CD1 1 
ATOM   2823 C CD2 . LEU   B 1 172 ? -27.000 19.338  14.968 1.00 60.70  ? 387 LEU   A CD2 1 
ATOM   2824 N N   . HIS   B 1 173 ? -22.640 16.591  13.275 1.00 57.56  ? 388 HIS   A N   1 
ATOM   2825 C CA  A HIS   B 1 173 ? -21.234 16.667  12.873 0.50 62.30  ? 388 HIS   A CA  1 
ATOM   2826 C CA  B HIS   B 1 173 ? -21.228 16.608  12.863 0.50 61.10  ? 388 HIS   A CA  1 
ATOM   2827 C C   . HIS   B 1 173 ? -21.124 16.864  11.355 1.00 62.55  ? 388 HIS   A C   1 
ATOM   2828 O O   . HIS   B 1 173 ? -20.311 17.679  10.882 1.00 64.85  ? 388 HIS   A O   1 
ATOM   2829 C CB  A HIS   B 1 173 ? -20.443 15.446  13.346 0.50 62.91  ? 388 HIS   A CB  1 
ATOM   2830 C CB  B HIS   B 1 173 ? -20.568 15.268  13.208 0.50 60.41  ? 388 HIS   A CB  1 
ATOM   2831 C CG  A HIS   B 1 173 ? -19.821 15.624  14.697 0.50 67.40  ? 388 HIS   A CG  1 
ATOM   2832 C CG  B HIS   B 1 173 ? -19.072 15.309  13.241 0.50 61.92  ? 388 HIS   A CG  1 
ATOM   2833 N ND1 A HIS   B 1 173 ? -18.465 15.799  14.870 0.50 74.06  ? 388 HIS   A ND1 1 
ATOM   2834 N ND1 B HIS   B 1 173 ? -18.371 16.125  14.103 0.50 67.84  ? 388 HIS   A ND1 1 
ATOM   2835 C CD2 A HIS   B 1 173 ? -20.364 15.659  15.937 0.50 65.18  ? 388 HIS   A CD2 1 
ATOM   2836 C CD2 B HIS   B 1 173 ? -18.143 14.596  12.559 0.50 60.82  ? 388 HIS   A CD2 1 
ATOM   2837 C CE1 A HIS   B 1 173 ? -18.197 15.928  16.157 0.50 70.80  ? 388 HIS   A CE1 1 
ATOM   2838 C CE1 B HIS   B 1 173 ? -17.074 15.934  13.931 0.50 65.65  ? 388 HIS   A CE1 1 
ATOM   2839 N NE2 A HIS   B 1 173 ? -19.332 15.849  16.825 0.50 67.27  ? 388 HIS   A NE2 1 
ATOM   2840 N NE2 B HIS   B 1 173 ? -16.910 15.007  13.004 0.50 61.07  ? 388 HIS   A NE2 1 
ATOM   2841 N N   . LYS   B 1 174 ? -21.965 16.161  10.609 1.00 59.47  ? 389 LYS   A N   1 
ATOM   2842 C CA  . LYS   B 1 174 ? -22.013 16.286  9.164  1.00 62.03  ? 389 LYS   A CA  1 
ATOM   2843 C C   . LYS   B 1 174 ? -22.608 17.639  8.759  1.00 60.22  ? 389 LYS   A C   1 
ATOM   2844 O O   . LYS   B 1 174 ? -21.992 18.395  7.980  1.00 60.98  ? 389 LYS   A O   1 
ATOM   2845 C CB  . LYS   B 1 174 ? -22.764 15.089  8.547  1.00 61.86  ? 389 LYS   A CB  1 
ATOM   2846 C CG  . LYS   B 1 174 ? -21.993 13.781  8.748  1.00 65.17  ? 389 LYS   A CG  1 
ATOM   2847 C CD  . LYS   B 1 174 ? -22.624 12.544  8.098  1.00 72.09  ? 389 LYS   A CD  1 
ATOM   2848 C CE  . LYS   B 1 174 ? -23.970 12.178  8.703  1.00 75.34  ? 389 LYS   A CE  1 
ATOM   2849 N NZ  . LYS   B 1 174 ? -24.504 10.914  8.126  1.00 76.46  ? 389 LYS   A NZ  1 
ATOM   2850 N N   . LEU   B 1 175 ? -23.763 17.969  9.330  1.00 56.54  ? 390 LEU   A N   1 
ATOM   2851 C CA  . LEU   B 1 175 ? -24.456 19.209  8.999  1.00 52.51  ? 390 LEU   A CA  1 
ATOM   2852 C C   . LEU   B 1 175 ? -23.554 20.423  9.146  1.00 59.36  ? 390 LEU   A C   1 
ATOM   2853 O O   . LEU   B 1 175 ? -23.538 21.291  8.275  1.00 60.04  ? 390 LEU   A O   1 
ATOM   2854 C CB  . LEU   B 1 175 ? -25.697 19.373  9.838  1.00 53.59  ? 390 LEU   A CB  1 
ATOM   2855 C CG  . LEU   B 1 175 ? -26.743 20.369  9.397  1.00 53.30  ? 390 LEU   A CG  1 
ATOM   2856 C CD1 . LEU   B 1 175 ? -27.295 20.026  8.048  1.00 55.42  ? 390 LEU   A CD1 1 
ATOM   2857 C CD2 . LEU   B 1 175 ? -27.873 20.340  10.409 1.00 57.92  ? 390 LEU   A CD2 1 
ATOM   2858 N N   . ARG   B 1 176 ? -22.739 20.458  10.193 1.00 65.67  ? 391 ARG   A N   1 
ATOM   2859 C CA  . ARG   B 1 176 ? -21.910 21.631  10.425 1.00 72.76  ? 391 ARG   A CA  1 
ATOM   2860 C C   . ARG   B 1 176 ? -20.808 21.857  9.383  1.00 75.90  ? 391 ARG   A C   1 
ATOM   2861 O O   . ARG   B 1 176 ? -20.317 22.975  9.274  1.00 82.64  ? 391 ARG   A O   1 
ATOM   2862 C CB  . ARG   B 1 176 ? -21.343 21.649  11.847 1.00 78.68  ? 391 ARG   A CB  1 
ATOM   2863 C CG  . ARG   B 1 176 ? -20.235 20.647  12.157 1.00 89.72  ? 391 ARG   A CG  1 
ATOM   2864 C CD  . ARG   B 1 176 ? -19.364 21.185  13.286 1.00 100.30 ? 391 ARG   A CD  1 
ATOM   2865 N NE  . ARG   B 1 176 ? -18.579 20.148  13.955 1.00 111.13 ? 391 ARG   A NE  1 
ATOM   2866 C CZ  . ARG   B 1 176 ? -17.748 20.366  14.975 1.00 120.11 ? 391 ARG   A CZ  1 
ATOM   2867 N NH1 . ARG   B 1 176 ? -17.571 21.597  15.464 1.00 120.61 ? 391 ARG   A NH1 1 
ATOM   2868 N NH2 . ARG   B 1 176 ? -17.081 19.343  15.512 1.00 134.12 ? 391 ARG   A NH2 1 
ATOM   2869 N N   . GLN   B 1 177 ? -20.432 20.821  8.627  1.00 74.47  ? 392 GLN   A N   1 
ATOM   2870 C CA  . GLN   B 1 177 ? -19.357 20.935  7.616  1.00 77.75  ? 392 GLN   A CA  1 
ATOM   2871 C C   . GLN   B 1 177 ? -19.777 21.564  6.285  1.00 69.22  ? 392 GLN   A C   1 
ATOM   2872 O O   . GLN   B 1 177 ? -18.928 21.994  5.515  1.00 79.64  ? 392 GLN   A O   1 
ATOM   2873 C CB  . GLN   B 1 177 ? -18.731 19.570  7.347  1.00 81.55  ? 392 GLN   A CB  1 
ATOM   2874 C CG  . GLN   B 1 177 ? -17.783 19.129  8.448  1.00 90.28  ? 392 GLN   A CG  1 
ATOM   2875 C CD  . GLN   B 1 177 ? -17.650 17.622  8.537  1.00 100.97 ? 392 GLN   A CD  1 
ATOM   2876 O OE1 . GLN   B 1 177 ? -17.356 17.092  9.610  1.00 104.17 ? 392 GLN   A OE1 1 
ATOM   2877 N NE2 . GLN   B 1 177 ? -17.881 16.918  7.414  1.00 101.29 ? 392 GLN   A NE2 1 
ATOM   2878 N N   . LEU   B 1 178 ? -21.076 21.603  6.030  1.00 59.57  ? 393 LEU   A N   1 
ATOM   2879 C CA  . LEU   B 1 178 ? -21.621 22.194  4.827  1.00 56.31  ? 393 LEU   A CA  1 
ATOM   2880 C C   . LEU   B 1 178 ? -21.175 23.638  4.664  1.00 56.15  ? 393 LEU   A C   1 
ATOM   2881 O O   . LEU   B 1 178 ? -21.134 24.389  5.633  1.00 63.49  ? 393 LEU   A O   1 
ATOM   2882 C CB  . LEU   B 1 178 ? -23.140 22.147  4.849  1.00 50.97  ? 393 LEU   A CB  1 
ATOM   2883 C CG  . LEU   B 1 178 ? -23.713 20.842  4.341  1.00 49.17  ? 393 LEU   A CG  1 
ATOM   2884 C CD1 . LEU   B 1 178 ? -23.189 19.638  5.065  1.00 52.80  ? 393 LEU   A CD1 1 
ATOM   2885 C CD2 . LEU   B 1 178 ? -25.218 20.879  4.435  1.00 55.22  ? 393 LEU   A CD2 1 
ATOM   2886 N N   . PRO   B 1 179 ? -20.853 24.039  3.435  1.00 54.95  ? 394 PRO   A N   1 
ATOM   2887 C CA  . PRO   B 1 179 ? -20.184 25.317  3.274  1.00 52.98  ? 394 PRO   A CA  1 
ATOM   2888 C C   . PRO   B 1 179 ? -21.094 26.513  3.275  1.00 50.21  ? 394 PRO   A C   1 
ATOM   2889 O O   . PRO   B 1 179 ? -20.580 27.619  3.320  1.00 51.75  ? 394 PRO   A O   1 
ATOM   2890 C CB  . PRO   B 1 179 ? -19.518 25.196  1.885  1.00 54.82  ? 394 PRO   A CB  1 
ATOM   2891 C CG  . PRO   B 1 179 ? -19.980 23.904  1.313  1.00 58.25  ? 394 PRO   A CG  1 
ATOM   2892 C CD  . PRO   B 1 179 ? -21.141 23.442  2.127  1.00 59.41  ? 394 PRO   A CD  1 
ATOM   2893 N N   . GLU   B 1 180 ? -22.410 26.304  3.179  1.00 48.80  ? 395 GLU   A N   1 
ATOM   2894 C CA  . GLU   B 1 180 ? -23.377 27.367  3.108  1.00 45.34  ? 395 GLU   A CA  1 
ATOM   2895 C C   . GLU   B 1 180 ? -24.546 27.078  3.999  1.00 46.16  ? 395 GLU   A C   1 
ATOM   2896 O O   . GLU   B 1 180 ? -25.060 25.977  3.998  1.00 45.14  ? 395 GLU   A O   1 
ATOM   2897 C CB  . GLU   B 1 180 ? -23.921 27.486  1.701  1.00 51.03  ? 395 GLU   A CB  1 
ATOM   2898 C CG  . GLU   B 1 180 ? -22.874 27.785  0.649  1.00 59.87  ? 395 GLU   A CG  1 
ATOM   2899 C CD  . GLU   B 1 180 ? -22.246 29.154  0.786  1.00 62.71  ? 395 GLU   A CD  1 
ATOM   2900 O OE1 . GLU   B 1 180 ? -23.003 30.122  1.025  1.00 63.44  ? 395 GLU   A OE1 1 
ATOM   2901 O OE2 . GLU   B 1 180 ? -20.998 29.244  0.638  1.00 60.85  ? 395 GLU   A OE2 1 
ATOM   2902 N N   . ARG   B 1 181 ? -24.976 28.090  4.742  1.00 51.04  ? 396 ARG   A N   1 
ATOM   2903 C CA  . ARG   B 1 181 ? -26.238 28.064  5.470  1.00 54.50  ? 396 ARG   A CA  1 
ATOM   2904 C C   . ARG   B 1 181 ? -27.414 27.576  4.604  1.00 50.66  ? 396 ARG   A C   1 
ATOM   2905 O O   . ARG   B 1 181 ? -28.202 26.761  5.065  1.00 50.81  ? 396 ARG   A O   1 
ATOM   2906 C CB  . ARG   B 1 181 ? -26.582 29.468  6.020  1.00 60.83  ? 396 ARG   A CB  1 
ATOM   2907 C CG  . ARG   B 1 181 ? -26.204 29.732  7.476  1.00 67.08  ? 396 ARG   A CG  1 
ATOM   2908 C CD  . ARG   B 1 181 ? -26.588 31.154  7.930  1.00 72.42  ? 396 ARG   A CD  1 
ATOM   2909 N NE  . ARG   B 1 181 ? -27.877 31.611  7.361  1.00 77.57  ? 396 ARG   A NE  1 
ATOM   2910 C CZ  . ARG   B 1 181 ? -28.037 32.457  6.322  1.00 85.87  ? 396 ARG   A CZ  1 
ATOM   2911 N NH1 . ARG   B 1 181 ? -26.992 33.034  5.700  1.00 82.84  ? 396 ARG   A NH1 1 
ATOM   2912 N NH2 . ARG   B 1 181 ? -29.276 32.753  5.902  1.00 81.28  ? 396 ARG   A NH2 1 
ATOM   2913 N N   . TYR   B 1 182 ? -27.543 28.071  3.371  1.00 48.60  ? 397 TYR   A N   1 
ATOM   2914 C CA  . TYR   B 1 182 ? -28.708 27.702  2.529  1.00 47.86  ? 397 TYR   A CA  1 
ATOM   2915 C C   . TYR   B 1 182 ? -28.733 26.204  2.219  1.00 46.05  ? 397 TYR   A C   1 
ATOM   2916 O O   . TYR   B 1 182 ? -29.798 25.657  1.956  1.00 45.25  ? 397 TYR   A O   1 
ATOM   2917 C CB  . TYR   B 1 182 ? -28.830 28.533  1.230  1.00 44.46  ? 397 TYR   A CB  1 
ATOM   2918 C CG  . TYR   B 1 182 ? -27.847 28.193  0.082  1.00 52.57  ? 397 TYR   A CG  1 
ATOM   2919 C CD1 . TYR   B 1 182 ? -28.174 27.249  -0.898 1.00 51.75  ? 397 TYR   A CD1 1 
ATOM   2920 C CD2 . TYR   B 1 182 ? -26.603 28.859  -0.038 1.00 54.37  ? 397 TYR   A CD2 1 
ATOM   2921 C CE1 . TYR   B 1 182 ? -27.296 26.962  -1.940 1.00 59.24  ? 397 TYR   A CE1 1 
ATOM   2922 C CE2 . TYR   B 1 182 ? -25.728 28.592  -1.085 1.00 51.69  ? 397 TYR   A CE2 1 
ATOM   2923 C CZ  . TYR   B 1 182 ? -26.063 27.639  -2.039 1.00 58.08  ? 397 TYR   A CZ  1 
ATOM   2924 O OH  . TYR   B 1 182 ? -25.168 27.327  -3.079 1.00 56.65  ? 397 TYR   A OH  1 
ATOM   2925 N N   . MET   B 1 183 ? -27.572 25.555  2.258  1.00 43.66  ? 398 MET   A N   1 
ATOM   2926 C CA  . MET   B 1 183 ? -27.516 24.095  2.121  1.00 49.27  ? 398 MET   A CA  1 
ATOM   2927 C C   . MET   B 1 183 ? -27.995 23.381  3.388  1.00 47.34  ? 398 MET   A C   1 
ATOM   2928 O O   . MET   B 1 183 ? -28.788 22.452  3.307  1.00 45.49  ? 398 MET   A O   1 
ATOM   2929 C CB  . MET   B 1 183 ? -26.108 23.637  1.725  1.00 50.42  ? 398 MET   A CB  1 
ATOM   2930 C CG  . MET   B 1 183 ? -25.705 24.150  0.341  1.00 52.73  ? 398 MET   A CG  1 
ATOM   2931 S SD  . MET   B 1 183 ? -24.041 23.674  -0.160 1.00 56.56  ? 398 MET   A SD  1 
ATOM   2932 C CE  . MET   B 1 183 ? -24.106 24.247  -1.853 1.00 67.32  ? 398 MET   A CE  1 
ATOM   2933 N N   . MET   B 1 184 ? -27.542 23.862  4.542  1.00 48.00  ? 399 MET   A N   1 
ATOM   2934 C CA  . MET   B 1 184 ? -28.020 23.405  5.842  1.00 44.05  ? 399 MET   A CA  1 
ATOM   2935 C C   . MET   B 1 184 ? -29.532 23.513  5.932  1.00 44.27  ? 399 MET   A C   1 
ATOM   2936 O O   . MET   B 1 184 ? -30.176 22.589  6.392  1.00 52.48  ? 399 MET   A O   1 
ATOM   2937 C CB  . MET   B 1 184 ? -27.373 24.176  6.968  1.00 44.72  ? 399 MET   A CB  1 
ATOM   2938 C CG  . MET   B 1 184 ? -25.878 23.932  7.097  1.00 45.49  ? 399 MET   A CG  1 
ATOM   2939 S SD  . MET   B 1 184 ? -25.178 25.235  8.119  1.00 51.03  ? 399 MET   A SD  1 
ATOM   2940 C CE  . MET   B 1 184 ? -23.445 24.794  8.146  1.00 44.03  ? 399 MET   A CE  1 
ATOM   2941 N N   . ASN   B 1 185 ? -30.111 24.591  5.442  1.00 44.79  ? 400 ASN   A N   1 
ATOM   2942 C CA  . ASN   B 1 185 ? -31.577 24.726  5.429  1.00 46.87  ? 400 ASN   A CA  1 
ATOM   2943 C C   . ASN   B 1 185 ? -32.291 23.815  4.473  1.00 43.42  ? 400 ASN   A C   1 
ATOM   2944 O O   . ASN   B 1 185 ? -33.397 23.370  4.748  1.00 49.91  ? 400 ASN   A O   1 
ATOM   2945 C CB  . ASN   B 1 185 ? -31.997 26.177  5.134  1.00 49.00  ? 400 ASN   A CB  1 
ATOM   2946 C CG  . ASN   B 1 185 ? -31.544 27.154  6.231  1.00 51.26  ? 400 ASN   A CG  1 
ATOM   2947 O OD1 . ASN   B 1 185 ? -31.250 26.774  7.357  1.00 45.05  ? 400 ASN   A OD1 1 
ATOM   2948 N ND2 . ASN   B 1 185 ? -31.441 28.411  5.869  1.00 55.20  ? 400 ASN   A ND2 1 
ATOM   2949 N N   . SER   B 1 186 ? -31.685 23.563  3.329  1.00 44.81  ? 401 SER   A N   1 
ATOM   2950 C CA  . SER   B 1 186 ? -32.230 22.595  2.403  1.00 45.42  ? 401 SER   A CA  1 
ATOM   2951 C C   . SER   B 1 186 ? -32.292 21.214  3.052  1.00 42.30  ? 401 SER   A C   1 
ATOM   2952 O O   . SER   B 1 186 ? -33.313 20.524  2.979  1.00 40.15  ? 401 SER   A O   1 
ATOM   2953 C CB  . SER   B 1 186 ? -31.363 22.525  1.147  1.00 50.94  ? 401 SER   A CB  1 
ATOM   2954 O OG  . SER   B 1 186 ? -31.257 23.805  0.530  1.00 57.03  ? 401 SER   A OG  1 
ATOM   2955 N N   . VAL   B 1 187 ? -31.182 20.833  3.676  1.00 40.04  ? 402 VAL   A N   1 
ATOM   2956 C CA  . VAL   B 1 187 ? -31.051 19.557  4.356  1.00 42.93  ? 402 VAL   A CA  1 
ATOM   2957 C C   . VAL   B 1 187 ? -32.066 19.497  5.503  1.00 47.22  ? 402 VAL   A C   1 
ATOM   2958 O O   . VAL   B 1 187 ? -32.722 18.486  5.665  1.00 48.72  ? 402 VAL   A O   1 
ATOM   2959 C CB  . VAL   B 1 187 ? -29.618 19.305  4.931  1.00 42.05  ? 402 VAL   A CB  1 
ATOM   2960 C CG1 . VAL   B 1 187 ? -29.594 18.014  5.765  1.00 41.61  ? 402 VAL   A CG1 1 
ATOM   2961 C CG2 . VAL   B 1 187 ? -28.593 19.197  3.823  1.00 41.32  ? 402 VAL   A CG2 1 
ATOM   2962 N N   . LEU   B 1 188 ? -32.195 20.585  6.262  1.00 46.26  ? 403 LEU   A N   1 
ATOM   2963 C CA  . LEU   B 1 188 ? -33.101 20.628  7.399  1.00 45.42  ? 403 LEU   A CA  1 
ATOM   2964 C C   . LEU   B 1 188 ? -34.574 20.742  7.014  1.00 45.27  ? 403 LEU   A C   1 
ATOM   2965 O O   . LEU   B 1 188 ? -35.415 20.461  7.825  1.00 48.97  ? 403 LEU   A O   1 
ATOM   2966 C CB  . LEU   B 1 188 ? -32.702 21.729  8.359  1.00 45.99  ? 403 LEU   A CB  1 
ATOM   2967 C CG  . LEU   B 1 188 ? -31.335 21.585  9.076  1.00 48.97  ? 403 LEU   A CG  1 
ATOM   2968 C CD1 . LEU   B 1 188 ? -30.926 22.918  9.688  1.00 50.67  ? 403 LEU   A CD1 1 
ATOM   2969 C CD2 . LEU   B 1 188 ? -31.327 20.507  10.149 1.00 46.39  ? 403 LEU   A CD2 1 
ATOM   2970 N N   . GLU   B 1 189 ? -34.904 21.073  5.782  1.00 50.25  ? 404 GLU   A N   1 
ATOM   2971 C CA  . GLU   B 1 189 ? -36.319 21.090  5.327  1.00 56.65  ? 404 GLU   A CA  1 
ATOM   2972 C C   . GLU   B 1 189 ? -37.028 19.760  5.616  1.00 58.26  ? 404 GLU   A C   1 
ATOM   2973 O O   . GLU   B 1 189 ? -38.191 19.754  5.942  1.00 60.25  ? 404 GLU   A O   1 
ATOM   2974 C CB  . GLU   B 1 189 ? -36.389 21.410  3.808  1.00 67.05  ? 404 GLU   A CB  1 
ATOM   2975 C CG  . GLU   B 1 189 ? -37.727 21.957  3.301  1.00 77.28  ? 404 GLU   A CG  1 
ATOM   2976 C CD  . GLU   B 1 189 ? -37.680 22.480  1.853  1.00 82.04  ? 404 GLU   A CD  1 
ATOM   2977 O OE1 . GLU   B 1 189 ? -36.589 22.671  1.266  1.00 74.41  ? 404 GLU   A OE1 1 
ATOM   2978 O OE2 . GLU   B 1 189 ? -38.769 22.713  1.288  1.00 92.80  ? 404 GLU   A OE2 1 
ATOM   2979 N N   . ASN   B 1 190 ? -36.313 18.635  5.520  1.00 61.81  ? 405 ASN   A N   1 
ATOM   2980 C CA  . ASN   B 1 190 ? -36.929 17.299  5.606  1.00 60.84  ? 405 ASN   A CA  1 
ATOM   2981 C C   . ASN   B 1 190 ? -36.837 16.637  6.994  1.00 63.50  ? 405 ASN   A C   1 
ATOM   2982 O O   . ASN   B 1 190 ? -37.176 15.458  7.154  1.00 59.23  ? 405 ASN   A O   1 
ATOM   2983 C CB  . ASN   B 1 190 ? -36.287 16.393  4.563  1.00 55.85  ? 405 ASN   A CB  1 
ATOM   2984 C CG  . ASN   B 1 190 ? -36.157 17.072  3.209  1.00 57.44  ? 405 ASN   A CG  1 
ATOM   2985 O OD1 . ASN   B 1 190 ? -37.150 17.238  2.483  1.00 59.87  ? 405 ASN   A OD1 1 
ATOM   2986 N ND2 . ASN   B 1 190 ? -34.932 17.494  2.871  1.00 51.80  ? 405 ASN   A ND2 1 
ATOM   2987 N N   . PHE   B 1 191 ? -36.430 17.406  8.000  1.00 56.04  ? 406 PHE   A N   1 
ATOM   2988 C CA  . PHE   B 1 191 ? -36.042 16.856  9.267  1.00 58.50  ? 406 PHE   A CA  1 
ATOM   2989 C C   . PHE   B 1 191 ? -36.882 17.512  10.365 1.00 57.15  ? 406 PHE   A C   1 
ATOM   2990 O O   . PHE   B 1 191 ? -36.898 18.736  10.464 1.00 60.39  ? 406 PHE   A O   1 
ATOM   2991 C CB  . PHE   B 1 191 ? -34.552 17.098  9.446  1.00 59.61  ? 406 PHE   A CB  1 
ATOM   2992 C CG  . PHE   B 1 191 ? -34.073 16.880  10.830 1.00 63.16  ? 406 PHE   A CG  1 
ATOM   2993 C CD1 . PHE   B 1 191 ? -34.202 17.886  11.789 1.00 68.54  ? 406 PHE   A CD1 1 
ATOM   2994 C CD2 . PHE   B 1 191 ? -33.477 15.693  11.194 1.00 70.37  ? 406 PHE   A CD2 1 
ATOM   2995 C CE1 . PHE   B 1 191 ? -33.752 17.715  13.090 1.00 68.10  ? 406 PHE   A CE1 1 
ATOM   2996 C CE2 . PHE   B 1 191 ? -33.027 15.517  12.506 1.00 76.32  ? 406 PHE   A CE2 1 
ATOM   2997 C CZ  . PHE   B 1 191 ? -33.159 16.539  13.450 1.00 69.32  ? 406 PHE   A CZ  1 
ATOM   2998 N N   . THR   B 1 192 ? -37.578 16.715  11.185 1.00 49.16  ? 407 THR   A N   1 
ATOM   2999 C CA  . THR   B 1 192 ? -38.478 17.275  12.198 1.00 50.33  ? 407 THR   A CA  1 
ATOM   3000 C C   . THR   B 1 192 ? -38.492 16.463  13.463 1.00 48.61  ? 407 THR   A C   1 
ATOM   3001 O O   . THR   B 1 192 ? -38.066 15.342  13.464 1.00 52.17  ? 407 THR   A O   1 
ATOM   3002 C CB  . THR   B 1 192 ? -39.926 17.411  11.674 1.00 48.28  ? 407 THR   A CB  1 
ATOM   3003 O OG1 . THR   B 1 192 ? -40.430 16.131  11.306 1.00 46.17  ? 407 THR   A OG1 1 
ATOM   3004 C CG2 . THR   B 1 192 ? -39.973 18.337  10.470 1.00 47.71  ? 407 THR   A CG2 1 
ATOM   3005 N N   . ILE   B 1 193 ? -38.952 17.064  14.553 1.00 48.16  ? 408 ILE   A N   1 
ATOM   3006 C CA  . ILE   B 1 193 ? -39.054 16.382  15.821 1.00 44.63  ? 408 ILE   A CA  1 
ATOM   3007 C C   . ILE   B 1 193 ? -40.447 16.561  16.356 1.00 47.02  ? 408 ILE   A C   1 
ATOM   3008 O O   . ILE   B 1 193 ? -40.992 17.636  16.253 1.00 49.93  ? 408 ILE   A O   1 
ATOM   3009 C CB  . ILE   B 1 193 ? -38.044 16.884  16.842 1.00 41.32  ? 408 ILE   A CB  1 
ATOM   3010 C CG1 . ILE   B 1 193 ? -36.648 16.560  16.340 1.00 47.58  ? 408 ILE   A CG1 1 
ATOM   3011 C CG2 . ILE   B 1 193 ? -38.281 16.162  18.158 1.00 43.71  ? 408 ILE   A CG2 1 
ATOM   3012 C CD1 . ILE   B 1 193 ? -35.504 16.969  17.244 1.00 49.20  ? 408 ILE   A CD1 1 
ATOM   3013 N N   . LEU   B 1 194 ? -41.018 15.505  16.934 1.00 49.32  ? 409 LEU   A N   1 
ATOM   3014 C CA  . LEU   B 1 194 ? -42.366 15.550  17.534 1.00 48.09  ? 409 LEU   A CA  1 
ATOM   3015 C C   . LEU   B 1 194 ? -42.219 15.097  18.949 1.00 50.05  ? 409 LEU   A C   1 
ATOM   3016 O O   . LEU   B 1 194 ? -41.589 14.071  19.192 1.00 54.38  ? 409 LEU   A O   1 
ATOM   3017 C CB  . LEU   B 1 194 ? -43.294 14.650  16.761 1.00 48.73  ? 409 LEU   A CB  1 
ATOM   3018 C CG  . LEU   B 1 194 ? -44.759 14.589  17.156 1.00 56.31  ? 409 LEU   A CG  1 
ATOM   3019 C CD1 . LEU   B 1 194 ? -45.400 15.959  17.281 1.00 59.02  ? 409 LEU   A CD1 1 
ATOM   3020 C CD2 . LEU   B 1 194 ? -45.475 13.761  16.092 1.00 59.29  ? 409 LEU   A CD2 1 
ATOM   3021 N N   . GLN   B 1 195 ? -42.730 15.881  19.901 1.00 56.08  ? 410 GLN   A N   1 
ATOM   3022 C CA  . GLN   B 1 195 ? -42.453 15.646  21.324 1.00 54.57  ? 410 GLN   A CA  1 
ATOM   3023 C C   . GLN   B 1 195 ? -43.740 15.622  22.116 1.00 51.59  ? 410 GLN   A C   1 
ATOM   3024 O O   . GLN   B 1 195 ? -44.368 16.646  22.283 1.00 58.94  ? 410 GLN   A O   1 
ATOM   3025 C CB  . GLN   B 1 195 ? -41.501 16.696  21.849 1.00 59.71  ? 410 GLN   A CB  1 
ATOM   3026 C CG  . GLN   B 1 195 ? -41.159 16.562  23.308 1.00 69.18  ? 410 GLN   A CG  1 
ATOM   3027 C CD  . GLN   B 1 195 ? -40.019 17.479  23.675 1.00 82.39  ? 410 GLN   A CD  1 
ATOM   3028 O OE1 . GLN   B 1 195 ? -40.234 18.598  24.172 1.00 103.63 ? 410 GLN   A OE1 1 
ATOM   3029 N NE2 . GLN   B 1 195 ? -38.792 17.028  23.410 1.00 83.43  ? 410 GLN   A NE2 1 
ATOM   3030 N N   . VAL   B 1 196 ? -44.112 14.435  22.605 1.00 52.55  ? 411 VAL   A N   1 
ATOM   3031 C CA  . VAL   B 1 196 ? -45.413 14.177  23.230 1.00 52.82  ? 411 VAL   A CA  1 
ATOM   3032 C C   . VAL   B 1 196 ? -45.245 13.872  24.713 1.00 51.51  ? 411 VAL   A C   1 
ATOM   3033 O O   . VAL   B 1 196 ? -44.547 12.926  25.068 1.00 49.21  ? 411 VAL   A O   1 
ATOM   3034 C CB  . VAL   B 1 196 ? -46.127 12.982  22.567 1.00 54.56  ? 411 VAL   A CB  1 
ATOM   3035 C CG1 . VAL   B 1 196 ? -47.554 12.831  23.097 1.00 53.15  ? 411 VAL   A CG1 1 
ATOM   3036 C CG2 . VAL   B 1 196 ? -46.130 13.147  21.050 1.00 58.61  ? 411 VAL   A CG2 1 
ATOM   3037 N N   . VAL   B 1 197 ? -45.891 14.686  25.554 1.00 52.15  ? 412 VAL   A N   1 
ATOM   3038 C CA  . VAL   B 1 197 ? -45.916 14.510  26.996 1.00 51.14  ? 412 VAL   A CA  1 
ATOM   3039 C C   . VAL   B 1 197 ? -47.319 14.106  27.411 1.00 54.77  ? 412 VAL   A C   1 
ATOM   3040 O O   . VAL   B 1 197 ? -48.311 14.769  27.074 1.00 54.10  ? 412 VAL   A O   1 
ATOM   3041 C CB  . VAL   B 1 197 ? -45.479 15.773  27.744 1.00 53.33  ? 412 VAL   A CB  1 
ATOM   3042 C CG1 . VAL   B 1 197 ? -45.237 15.467  29.209 1.00 54.09  ? 412 VAL   A CG1 1 
ATOM   3043 C CG2 . VAL   B 1 197 ? -44.197 16.318  27.138 1.00 54.46  ? 412 VAL   A CG2 1 
ATOM   3044 N N   . THR   B 1 198 ? -47.391 12.974  28.105 1.00 56.93  ? 413 THR   A N   1 
ATOM   3045 C CA  . THR   B 1 198 ? -48.647 12.421  28.581 1.00 57.24  ? 413 THR   A CA  1 
ATOM   3046 C C   . THR   B 1 198 ? -48.558 12.162  30.070 1.00 54.72  ? 413 THR   A C   1 
ATOM   3047 O O   . THR   B 1 198 ? -47.476 11.988  30.637 1.00 52.22  ? 413 THR   A O   1 
ATOM   3048 C CB  . THR   B 1 198 ? -48.933 11.083  27.946 1.00 52.89  ? 413 THR   A CB  1 
ATOM   3049 O OG1 . THR   B 1 198 ? -47.768 10.301  28.137 1.00 57.82  ? 413 THR   A OG1 1 
ATOM   3050 C CG2 . THR   B 1 198 ? -49.183 11.216  26.471 1.00 55.77  ? 413 THR   A CG2 1 
ATOM   3051 N N   . ASN   B 1 199 ? -49.729 12.133  30.688 1.00 58.17  ? 414 ASN   A N   1 
ATOM   3052 C CA  . ASN   B 1 199 ? -49.863 11.701  32.067 1.00 59.73  ? 414 ASN   A CA  1 
ATOM   3053 C C   . ASN   B 1 199 ? -49.703 10.195  32.034 1.00 57.45  ? 414 ASN   A C   1 
ATOM   3054 O O   . ASN   B 1 199 ? -50.563 9.484   31.498 1.00 55.76  ? 414 ASN   A O   1 
ATOM   3055 C CB  . ASN   B 1 199 ? -51.232 12.101  32.611 1.00 59.34  ? 414 ASN   A CB  1 
ATOM   3056 C CG  . ASN   B 1 199 ? -51.333 11.958  34.110 1.00 56.19  ? 414 ASN   A CG  1 
ATOM   3057 O OD1 . ASN   B 1 199 ? -50.998 10.926  34.672 1.00 59.83  ? 414 ASN   A OD1 1 
ATOM   3058 N ND2 . ASN   B 1 199 ? -51.802 12.999  34.767 1.00 56.65  ? 414 ASN   A ND2 1 
ATOM   3059 N N   . ARG   B 1 200 ? -48.590 9.713   32.574 1.00 58.34  ? 415 ARG   A N   1 
ATOM   3060 C CA  . ARG   B 1 200 ? -48.352 8.275   32.592 1.00 63.66  ? 415 ARG   A CA  1 
ATOM   3061 C C   . ARG   B 1 200 ? -49.529 7.541   33.239 1.00 60.04  ? 415 ARG   A C   1 
ATOM   3062 O O   . ARG   B 1 200 ? -50.022 6.579   32.675 1.00 60.89  ? 415 ARG   A O   1 
ATOM   3063 C CB  . ARG   B 1 200 ? -47.037 7.904   33.290 1.00 64.61  ? 415 ARG   A CB  1 
ATOM   3064 C CG  . ARG   B 1 200 ? -46.625 6.456   32.992 1.00 69.99  ? 415 ARG   A CG  1 
ATOM   3065 C CD  . ARG   B 1 200 ? -46.092 5.699   34.194 1.00 75.29  ? 415 ARG   A CD  1 
ATOM   3066 N NE  . ARG   B 1 200 ? -46.809 6.042   35.425 1.00 78.26  ? 415 ARG   A NE  1 
ATOM   3067 C CZ  . ARG   B 1 200 ? -46.304 5.958   36.655 1.00 80.86  ? 415 ARG   A CZ  1 
ATOM   3068 N NH1 . ARG   B 1 200 ? -45.067 5.498   36.880 1.00 81.11  ? 415 ARG   A NH1 1 
ATOM   3069 N NH2 . ARG   B 1 200 ? -47.046 6.333   37.687 1.00 84.06  ? 415 ARG   A NH2 1 
ATOM   3070 N N   . ASP   B 1 201 ? -50.001 8.031   34.380 1.00 58.56  ? 416 ASP   A N   1 
ATOM   3071 C CA  . ASP   B 1 201 ? -51.091 7.366   35.117 1.00 70.90  ? 416 ASP   A CA  1 
ATOM   3072 C C   . ASP   B 1 201 ? -52.439 7.338   34.398 1.00 72.17  ? 416 ASP   A C   1 
ATOM   3073 O O   . ASP   B 1 201 ? -53.124 6.341   34.490 1.00 84.40  ? 416 ASP   A O   1 
ATOM   3074 C CB  . ASP   B 1 201 ? -51.268 7.942   36.542 1.00 70.70  ? 416 ASP   A CB  1 
ATOM   3075 C CG  . ASP   B 1 201 ? -50.090 7.623   37.450 1.00 72.66  ? 416 ASP   A CG  1 
ATOM   3076 O OD1 . ASP   B 1 201 ? -49.470 6.551   37.272 1.00 76.31  ? 416 ASP   A OD1 1 
ATOM   3077 O OD2 . ASP   B 1 201 ? -49.746 8.440   38.332 1.00 73.14  ? 416 ASP   A OD2 1 
ATOM   3078 N N   . THR   B 1 202 ? -52.823 8.392   33.688 1.00 70.83  ? 417 THR   A N   1 
ATOM   3079 C CA  . THR   B 1 202 ? -54.103 8.393   32.966 1.00 68.75  ? 417 THR   A CA  1 
ATOM   3080 C C   . THR   B 1 202 ? -53.976 8.160   31.455 1.00 69.35  ? 417 THR   A C   1 
ATOM   3081 O O   . THR   B 1 202 ? -54.983 7.934   30.789 1.00 68.61  ? 417 THR   A O   1 
ATOM   3082 C CB  . THR   B 1 202 ? -54.878 9.694   33.218 1.00 73.83  ? 417 THR   A CB  1 
ATOM   3083 O OG1 . THR   B 1 202 ? -54.092 10.820  32.809 1.00 79.26  ? 417 THR   A OG1 1 
ATOM   3084 C CG2 . THR   B 1 202 ? -55.194 9.838   34.699 1.00 76.80  ? 417 THR   A CG2 1 
ATOM   3085 N N   . GLN   B 1 203 ? -52.759 8.215   30.912 1.00 72.51  ? 418 GLN   A N   1 
ATOM   3086 C CA  . GLN   B 1 203 ? -52.541 8.213   29.447 1.00 77.40  ? 418 GLN   A CA  1 
ATOM   3087 C C   . GLN   B 1 203 ? -53.106 9.444   28.710 1.00 74.17  ? 418 GLN   A C   1 
ATOM   3088 O O   . GLN   B 1 203 ? -53.143 9.458   27.483 1.00 78.74  ? 418 GLN   A O   1 
ATOM   3089 C CB  . GLN   B 1 203 ? -53.063 6.905   28.783 1.00 80.81  ? 418 GLN   A CB  1 
ATOM   3090 C CG  . GLN   B 1 203 ? -52.365 5.634   29.234 1.00 87.98  ? 418 GLN   A CG  1 
ATOM   3091 C CD  . GLN   B 1 203 ? -50.850 5.771   29.156 1.00 97.43  ? 418 GLN   A CD  1 
ATOM   3092 O OE1 . GLN   B 1 203 ? -50.309 6.220   28.145 1.00 106.44 ? 418 GLN   A OE1 1 
ATOM   3093 N NE2 . GLN   B 1 203 ? -50.166 5.426   30.236 1.00 96.50  ? 418 GLN   A NE2 1 
ATOM   3094 N N   . GLU   B 1 204 ? -53.513 10.475  29.450 1.00 68.09  ? 419 GLU   A N   1 
ATOM   3095 C CA  . GLU   B 1 204 ? -54.006 11.706  28.864 1.00 66.11  ? 419 GLU   A CA  1 
ATOM   3096 C C   . GLU   B 1 204 ? -52.858 12.478  28.254 1.00 64.74  ? 419 GLU   A C   1 
ATOM   3097 O O   . GLU   B 1 204 ? -51.765 12.537  28.831 1.00 60.78  ? 419 GLU   A O   1 
ATOM   3098 C CB  . GLU   B 1 204 ? -54.597 12.606  29.933 1.00 75.02  ? 419 GLU   A CB  1 
ATOM   3099 C CG  . GLU   B 1 204 ? -55.849 12.090  30.622 1.00 82.15  ? 419 GLU   A CG  1 
ATOM   3100 C CD  . GLU   B 1 204 ? -56.225 12.996  31.773 1.00 87.23  ? 419 GLU   A CD  1 
ATOM   3101 O OE1 . GLU   B 1 204 ? -57.313 13.593  31.718 1.00 87.85  ? 419 GLU   A OE1 1 
ATOM   3102 O OE2 . GLU   B 1 204 ? -55.397 13.185  32.699 1.00 94.03  ? 419 GLU   A OE2 1 
ATOM   3103 N N   . LEU   B 1 205 ? -53.112 13.108  27.112 1.00 62.03  ? 420 LEU   A N   1 
ATOM   3104 C CA  . LEU   B 1 205 ? -52.100 13.956  26.480 1.00 63.40  ? 420 LEU   A CA  1 
ATOM   3105 C C   . LEU   B 1 205 ? -52.073 15.262  27.198 1.00 56.80  ? 420 LEU   A C   1 
ATOM   3106 O O   . LEU   B 1 205 ? -53.120 15.830  27.446 1.00 59.00  ? 420 LEU   A O   1 
ATOM   3107 C CB  . LEU   B 1 205 ? -52.377 14.180  24.988 1.00 68.58  ? 420 LEU   A CB  1 
ATOM   3108 C CG  . LEU   B 1 205 ? -51.192 14.804  24.226 1.00 68.55  ? 420 LEU   A CG  1 
ATOM   3109 C CD1 . LEU   B 1 205 ? -50.933 14.082  22.916 1.00 70.35  ? 420 LEU   A CD1 1 
ATOM   3110 C CD2 . LEU   B 1 205 ? -51.416 16.284  23.981 1.00 69.60  ? 420 LEU   A CD2 1 
ATOM   3111 N N   . LEU   B 1 206 ? -50.880 15.702  27.575 1.00 58.07  ? 421 LEU   A N   1 
ATOM   3112 C CA  . LEU   B 1 206 ? -50.678 17.004  28.227 1.00 56.43  ? 421 LEU   A CA  1 
ATOM   3113 C C   . LEU   B 1 206 ? -50.070 18.045  27.290 1.00 57.91  ? 421 LEU   A C   1 
ATOM   3114 O O   . LEU   B 1 206 ? -50.352 19.235  27.417 1.00 58.56  ? 421 LEU   A O   1 
ATOM   3115 C CB  . LEU   B 1 206 ? -49.736 16.863  29.425 1.00 56.55  ? 421 LEU   A CB  1 
ATOM   3116 C CG  . LEU   B 1 206 ? -50.181 15.988  30.595 1.00 56.66  ? 421 LEU   A CG  1 
ATOM   3117 C CD1 . LEU   B 1 206 ? -49.009 15.698  31.510 1.00 57.14  ? 421 LEU   A CD1 1 
ATOM   3118 C CD2 . LEU   B 1 206 ? -51.267 16.674  31.393 1.00 59.55  ? 421 LEU   A CD2 1 
ATOM   3119 N N   . LEU   B 1 207 ? -49.209 17.612  26.368 1.00 62.06  ? 422 LEU   A N   1 
ATOM   3120 C CA  . LEU   B 1 207 ? -48.381 18.544  25.607 1.00 57.19  ? 422 LEU   A CA  1 
ATOM   3121 C C   . LEU   B 1 207 ? -47.832 17.836  24.392 1.00 54.94  ? 422 LEU   A C   1 
ATOM   3122 O O   . LEU   B 1 207 ? -47.174 16.803  24.525 1.00 53.25  ? 422 LEU   A O   1 
ATOM   3123 C CB  . LEU   B 1 207 ? -47.247 19.075  26.513 1.00 55.90  ? 422 LEU   A CB  1 
ATOM   3124 C CG  . LEU   B 1 207 ? -46.689 20.480  26.321 1.00 57.12  ? 422 LEU   A CG  1 
ATOM   3125 C CD1 . LEU   B 1 207 ? -47.788 21.533  26.230 1.00 60.72  ? 422 LEU   A CD1 1 
ATOM   3126 C CD2 . LEU   B 1 207 ? -45.772 20.817  27.484 1.00 55.95  ? 422 LEU   A CD2 1 
ATOM   3127 N N   . CYS   B 1 208 ? -48.114 18.383  23.213 1.00 53.72  ? 423 CYS   A N   1 
ATOM   3128 C CA  . CYS   B 1 208 ? -47.594 17.837  21.976 1.00 52.01  ? 423 CYS   A CA  1 
ATOM   3129 C C   . CYS   B 1 208 ? -46.993 18.928  21.129 1.00 50.86  ? 423 CYS   A C   1 
ATOM   3130 O O   . CYS   B 1 208 ? -47.719 19.749  20.627 1.00 52.81  ? 423 CYS   A O   1 
ATOM   3131 C CB  . CYS   B 1 208 ? -48.687 17.147  21.190 1.00 53.10  ? 423 CYS   A CB  1 
ATOM   3132 S SG  . CYS   B 1 208 ? -48.032 16.568  19.606 1.00 52.89  ? 423 CYS   A SG  1 
ATOM   3133 N N   . THR   B 1 209 ? -45.679 18.880  20.932 1.00 49.95  ? 424 THR   A N   1 
ATOM   3134 C CA  . THR   B 1 209 ? -44.932 19.914  20.282 1.00 49.54  ? 424 THR   A CA  1 
ATOM   3135 C C   . THR   B 1 209 ? -44.233 19.445  19.020 1.00 50.50  ? 424 THR   A C   1 
ATOM   3136 O O   . THR   B 1 209 ? -43.392 18.552  19.055 1.00 55.94  ? 424 THR   A O   1 
ATOM   3137 C CB  . THR   B 1 209 ? -43.858 20.445  21.229 1.00 60.39  ? 424 THR   A CB  1 
ATOM   3138 O OG1 . THR   B 1 209 ? -44.414 20.577  22.548 1.00 67.62  ? 424 THR   A OG1 1 
ATOM   3139 C CG2 . THR   B 1 209 ? -43.308 21.813  20.718 1.00 61.98  ? 424 THR   A CG2 1 
ATOM   3140 N N   . ALA   B 1 210 ? -44.558 20.085  17.904 1.00 52.15  ? 425 ALA   A N   1 
ATOM   3141 C CA  . ALA   B 1 210 ? -43.795 19.950  16.641 1.00 52.40  ? 425 ALA   A CA  1 
ATOM   3142 C C   . ALA   B 1 210 ? -42.640 20.942  16.573 1.00 51.49  ? 425 ALA   A C   1 
ATOM   3143 O O   . ALA   B 1 210 ? -42.817 22.113  16.890 1.00 55.38  ? 425 ALA   A O   1 
ATOM   3144 C CB  . ALA   B 1 210 ? -44.714 20.137  15.438 1.00 52.35  ? 425 ALA   A CB  1 
ATOM   3145 N N   . TYR   B 1 211 ? -41.457 20.461  16.202 1.00 49.87  ? 426 TYR   A N   1 
ATOM   3146 C CA  . TYR   B 1 211 ? -40.275 21.298  15.998 1.00 50.97  ? 426 TYR   A CA  1 
ATOM   3147 C C   . TYR   B 1 211 ? -39.794 21.266  14.540 1.00 54.76  ? 426 TYR   A C   1 
ATOM   3148 O O   . TYR   B 1 211 ? -39.483 20.178  13.996 1.00 56.66  ? 426 TYR   A O   1 
ATOM   3149 C CB  . TYR   B 1 211 ? -39.130 20.810  16.846 1.00 46.88  ? 426 TYR   A CB  1 
ATOM   3150 C CG  . TYR   B 1 211 ? -39.355 20.836  18.313 1.00 54.70  ? 426 TYR   A CG  1 
ATOM   3151 C CD1 . TYR   B 1 211 ? -39.029 21.944  19.051 1.00 59.26  ? 426 TYR   A CD1 1 
ATOM   3152 C CD2 . TYR   B 1 211 ? -39.827 19.725  18.988 1.00 59.64  ? 426 TYR   A CD2 1 
ATOM   3153 C CE1 . TYR   B 1 211 ? -39.177 21.965  20.426 1.00 62.21  ? 426 TYR   A CE1 1 
ATOM   3154 C CE2 . TYR   B 1 211 ? -39.999 19.744  20.356 1.00 61.86  ? 426 TYR   A CE2 1 
ATOM   3155 C CZ  . TYR   B 1 211 ? -39.663 20.861  21.081 1.00 60.56  ? 426 TYR   A CZ  1 
ATOM   3156 O OH  . TYR   B 1 211 ? -39.810 20.877  22.464 1.00 67.94  ? 426 TYR   A OH  1 
ATOM   3157 N N   . VAL   B 1 212 ? -39.696 22.449  13.926 1.00 51.47  ? 427 VAL   A N   1 
ATOM   3158 C CA  . VAL   B 1 212 ? -39.018 22.600  12.615 1.00 48.13  ? 427 VAL   A CA  1 
ATOM   3159 C C   . VAL   B 1 212 ? -37.755 23.436  12.793 1.00 47.50  ? 427 VAL   A C   1 
ATOM   3160 O O   . VAL   B 1 212 ? -37.604 24.143  13.805 1.00 46.57  ? 427 VAL   A O   1 
ATOM   3161 C CB  . VAL   B 1 212 ? -39.915 23.190  11.513 1.00 45.20  ? 427 VAL   A CB  1 
ATOM   3162 C CG1 . VAL   B 1 212 ? -41.116 22.283  11.223 1.00 44.67  ? 427 VAL   A CG1 1 
ATOM   3163 C CG2 . VAL   B 1 212 ? -40.365 24.593  11.873 1.00 50.56  ? 427 VAL   A CG2 1 
ATOM   3164 N N   . PHE   B 1 213 ? -36.857 23.346  11.810 1.00 43.46  ? 428 PHE   A N   1 
ATOM   3165 C CA  . PHE   B 1 213 ? -35.477 23.839  11.932 1.00 46.26  ? 428 PHE   A CA  1 
ATOM   3166 C C   . PHE   B 1 213 ? -34.957 24.606  10.703 1.00 46.76  ? 428 PHE   A C   1 
ATOM   3167 O O   . PHE   B 1 213 ? -35.232 24.245  9.571  1.00 49.09  ? 428 PHE   A O   1 
ATOM   3168 C CB  . PHE   B 1 213 ? -34.545 22.659  12.201 1.00 45.80  ? 428 PHE   A CB  1 
ATOM   3169 C CG  . PHE   B 1 213 ? -34.829 21.949  13.488 1.00 45.52  ? 428 PHE   A CG  1 
ATOM   3170 C CD1 . PHE   B 1 213 ? -35.821 20.953  13.543 1.00 43.69  ? 428 PHE   A CD1 1 
ATOM   3171 C CD2 . PHE   B 1 213 ? -34.112 22.254  14.650 1.00 43.17  ? 428 PHE   A CD2 1 
ATOM   3172 C CE1 . PHE   B 1 213 ? -36.108 20.297  14.736 1.00 43.61  ? 428 PHE   A CE1 1 
ATOM   3173 C CE2 . PHE   B 1 213 ? -34.405 21.591  15.841 1.00 44.73  ? 428 PHE   A CE2 1 
ATOM   3174 C CZ  . PHE   B 1 213 ? -35.393 20.603  15.881 1.00 41.64  ? 428 PHE   A CZ  1 
ATOM   3175 N N   . GLU   B 1 214 ? -34.241 25.692  10.954 1.00 47.88  ? 429 GLU   A N   1 
ATOM   3176 C CA  . GLU   B 1 214 ? -33.334 26.299  9.968  1.00 47.89  ? 429 GLU   A CA  1 
ATOM   3177 C C   . GLU   B 1 214 ? -32.082 26.623  10.735 1.00 46.18  ? 429 GLU   A C   1 
ATOM   3178 O O   . GLU   B 1 214 ? -31.965 26.292  11.913 1.00 49.42  ? 429 GLU   A O   1 
ATOM   3179 C CB  . GLU   B 1 214 ? -33.904 27.567  9.368  1.00 45.81  ? 429 GLU   A CB  1 
ATOM   3180 C CG  . GLU   B 1 214 ? -35.234 27.403  8.669  1.00 50.67  ? 429 GLU   A CG  1 
ATOM   3181 C CD  . GLU   B 1 214 ? -35.577 28.608  7.799  1.00 50.90  ? 429 GLU   A CD  1 
ATOM   3182 O OE1 . GLU   B 1 214 ? -34.859 29.637  7.868  1.00 50.04  ? 429 GLU   A OE1 1 
ATOM   3183 O OE2 . GLU   B 1 214 ? -36.567 28.509  7.053  1.00 49.68  ? 429 GLU   A OE2 1 
ATOM   3184 N N   . VAL   B 1 215 ? -31.148 27.261  10.076 1.00 49.73  ? 430 VAL   A N   1 
ATOM   3185 C CA  . VAL   B 1 215 ? -29.927 27.690  10.715 1.00 58.53  ? 430 VAL   A CA  1 
ATOM   3186 C C   . VAL   B 1 215 ? -29.908 29.212  10.727 1.00 61.95  ? 430 VAL   A C   1 
ATOM   3187 O O   . VAL   B 1 215 ? -30.279 29.852  9.742  1.00 66.67  ? 430 VAL   A O   1 
ATOM   3188 C CB  . VAL   B 1 215 ? -28.741 27.094  9.977  1.00 56.57  ? 430 VAL   A CB  1 
ATOM   3189 C CG1 . VAL   B 1 215 ? -27.428 27.577  10.565 1.00 63.19  ? 430 VAL   A CG1 1 
ATOM   3190 C CG2 . VAL   B 1 215 ? -28.860 25.587  10.068 1.00 57.99  ? 430 VAL   A CG2 1 
ATOM   3191 N N   . SER   B 1 216 ? -29.560 29.763  11.888 1.00 68.67  ? 431 SER   A N   1 
ATOM   3192 C CA  . SER   B 1 216 ? -29.297 31.192  12.072 1.00 74.36  ? 431 SER   A CA  1 
ATOM   3193 C C   . SER   B 1 216 ? -27.816 31.403  11.826 1.00 73.41  ? 431 SER   A C   1 
ATOM   3194 O O   . SER   B 1 216 ? -27.019 30.456  11.911 1.00 71.65  ? 431 SER   A O   1 
ATOM   3195 C CB  . SER   B 1 216 ? -29.612 31.633  13.522 1.00 74.56  ? 431 SER   A CB  1 
ATOM   3196 O OG  . SER   B 1 216 ? -29.704 33.045  13.650 1.00 68.73  ? 431 SER   A OG  1 
ATOM   3197 N N   . THR   B 1 217 ? -27.448 32.656  11.588 1.00 71.61  ? 432 THR   A N   1 
ATOM   3198 C CA  . THR   B 1 217 ? -26.047 33.021  11.424 1.00 73.97  ? 432 THR   A CA  1 
ATOM   3199 C C   . THR   B 1 217 ? -25.393 33.099  12.811 1.00 79.32  ? 432 THR   A C   1 
ATOM   3200 O O   . THR   B 1 217 ? -26.080 33.221  13.854 1.00 69.56  ? 432 THR   A O   1 
ATOM   3201 C CB  . THR   B 1 217 ? -25.877 34.355  10.661 1.00 73.01  ? 432 THR   A CB  1 
ATOM   3202 O OG1 . THR   B 1 217 ? -26.360 35.450  11.458 1.00 80.26  ? 432 THR   A OG1 1 
ATOM   3203 C CG2 . THR   B 1 217 ? -26.640 34.339  9.329  1.00 69.34  ? 432 THR   A CG2 1 
ATOM   3204 N N   . SER   B 1 218 ? -24.067 32.974  12.820 1.00 90.41  ? 433 SER   A N   1 
ATOM   3205 C CA  . SER   B 1 218 ? -23.274 33.271  14.016 1.00 98.55  ? 433 SER   A CA  1 
ATOM   3206 C C   . SER   B 1 218 ? -23.264 34.762  14.171 1.00 107.61 ? 433 SER   A C   1 
ATOM   3207 O O   . SER   B 1 218 ? -23.398 35.487  13.180 1.00 116.68 ? 433 SER   A O   1 
ATOM   3208 C CB  . SER   B 1 218 ? -21.846 32.771  13.896 1.00 92.51  ? 433 SER   A CB  1 
ATOM   3209 O OG  . SER   B 1 218 ? -21.830 31.400  14.196 1.00 94.51  ? 433 SER   A OG  1 
ATOM   3210 N N   . GLU   B 1 219 ? -23.147 35.216  15.415 1.00 107.34 ? 434 GLU   A N   1 
ATOM   3211 C CA  . GLU   B 1 219 ? -23.238 36.637  15.732 1.00 114.94 ? 434 GLU   A CA  1 
ATOM   3212 C C   . GLU   B 1 219 ? -24.679 37.213  15.528 1.00 107.96 ? 434 GLU   A C   1 
ATOM   3213 O O   . GLU   B 1 219 ? -24.882 38.419  15.685 1.00 118.80 ? 434 GLU   A O   1 
ATOM   3214 C CB  . GLU   B 1 219 ? -22.170 37.462  14.950 1.00 124.36 ? 434 GLU   A CB  1 
ATOM   3215 C CG  . GLU   B 1 219 ? -20.733 36.901  14.971 1.00 124.95 ? 434 GLU   A CG  1 
ATOM   3216 C CD  . GLU   B 1 219 ? -19.955 37.126  13.671 1.00 124.26 ? 434 GLU   A CD  1 
ATOM   3217 O OE1 . GLU   B 1 219 ? -19.297 36.173  13.205 1.00 116.46 ? 434 GLU   A OE1 1 
ATOM   3218 O OE2 . GLU   B 1 219 ? -19.991 38.246  13.113 1.00 120.94 ? 434 GLU   A OE2 1 
ATOM   3219 N N   . ARG   B 1 220 ? -25.656 36.372  15.155 1.00 91.65  ? 435 ARG   A N   1 
ATOM   3220 C CA  . ARG   B 1 220 ? -27.097 36.720  15.185 1.00 72.33  ? 435 ARG   A CA  1 
ATOM   3221 C C   . ARG   B 1 220 ? -27.893 35.765  16.074 1.00 68.84  ? 435 ARG   A C   1 
ATOM   3222 O O   . ARG   B 1 220 ? -29.021 36.084  16.453 1.00 69.82  ? 435 ARG   A O   1 
ATOM   3223 C CB  . ARG   B 1 220 ? -27.699 36.708  13.788 1.00 67.27  ? 435 ARG   A CB  1 
ATOM   3224 C CG  . ARG   B 1 220 ? -29.054 37.422  13.630 1.00 66.11  ? 435 ARG   A CG  1 
ATOM   3225 C CD  . ARG   B 1 220 ? -29.822 36.798  12.477 1.00 66.86  ? 435 ARG   A CD  1 
ATOM   3226 N NE  . ARG   B 1 220 ? -30.983 37.506  11.923 1.00 67.56  ? 435 ARG   A NE  1 
ATOM   3227 C CZ  . ARG   B 1 220 ? -32.133 37.793  12.558 1.00 72.90  ? 435 ARG   A CZ  1 
ATOM   3228 N NH1 . ARG   B 1 220 ? -32.326 37.576  13.857 1.00 66.00  ? 435 ARG   A NH1 1 
ATOM   3229 N NH2 . ARG   B 1 220 ? -33.113 38.366  11.881 1.00 74.58  ? 435 ARG   A NH2 1 
ATOM   3230 N N   . GLY   B 1 221 ? -27.332 34.588  16.362 1.00 63.96  ? 436 GLY   A N   1 
ATOM   3231 C CA  . GLY   B 1 221 ? -27.745 33.805  17.499 1.00 63.64  ? 436 GLY   A CA  1 
ATOM   3232 C C   . GLY   B 1 221 ? -29.003 32.969  17.286 1.00 62.11  ? 436 GLY   A C   1 
ATOM   3233 O O   . GLY   B 1 221 ? -29.881 33.274  16.449 1.00 52.76  ? 436 GLY   A O   1 
ATOM   3234 N N   . ALA   B 1 222 ? -29.084 31.916  18.091 1.00 57.65  ? 437 ALA   A N   1 
ATOM   3235 C CA  . ALA   B 1 222 ? -30.252 31.057  18.134 1.00 58.65  ? 437 ALA   A CA  1 
ATOM   3236 C C   . ALA   B 1 222 ? -31.554 31.817  18.457 1.00 55.50  ? 437 ALA   A C   1 
ATOM   3237 O O   . ALA   B 1 222 ? -31.555 32.727  19.276 1.00 56.93  ? 437 ALA   A O   1 
ATOM   3238 C CB  . ALA   B 1 222 ? -30.013 29.925  19.121 1.00 60.69  ? 437 ALA   A CB  1 
ATOM   3239 N N   . GLN   B 1 223 ? -32.636 31.440  17.777 1.00 54.17  ? 438 GLN   A N   1 
ATOM   3240 C CA  . GLN   B 1 223 ? -33.939 32.065  17.907 1.00 58.63  ? 438 GLN   A CA  1 
ATOM   3241 C C   . GLN   B 1 223 ? -35.039 31.042  17.651 1.00 57.11  ? 438 GLN   A C   1 
ATOM   3242 O O   . GLN   B 1 223 ? -34.893 30.169  16.808 1.00 54.80  ? 438 GLN   A O   1 
ATOM   3243 C CB  . GLN   B 1 223 ? -34.105 33.238  16.911 1.00 69.84  ? 438 GLN   A CB  1 
ATOM   3244 C CG  . GLN   B 1 223 ? -35.390 34.093  17.096 1.00 75.17  ? 438 GLN   A CG  1 
ATOM   3245 C CD  . GLN   B 1 223 ? -35.645 35.133  15.985 1.00 82.01  ? 438 GLN   A CD  1 
ATOM   3246 O OE1 . GLN   B 1 223 ? -34.987 35.133  14.939 1.00 87.60  ? 438 GLN   A OE1 1 
ATOM   3247 N NE2 . GLN   B 1 223 ? -36.620 36.020  16.212 1.00 78.27  ? 438 GLN   A NE2 1 
ATOM   3248 N N   . HIS   B 1 224 ? -36.160 31.203  18.351 1.00 56.65  ? 439 HIS   A N   1 
ATOM   3249 C CA  . HIS   B 1 224 ? -37.352 30.386  18.137 1.00 58.35  ? 439 HIS   A CA  1 
ATOM   3250 C C   . HIS   B 1 224 ? -38.547 31.274  18.036 1.00 53.20  ? 439 HIS   A C   1 
ATOM   3251 O O   . HIS   B 1 224 ? -38.513 32.387  18.484 1.00 65.20  ? 439 HIS   A O   1 
ATOM   3252 C CB  . HIS   B 1 224 ? -37.572 29.390  19.290 1.00 61.83  ? 439 HIS   A CB  1 
ATOM   3253 C CG  . HIS   B 1 224 ? -37.544 30.021  20.644 1.00 65.66  ? 439 HIS   A CG  1 
ATOM   3254 N ND1 . HIS   B 1 224 ? -38.689 30.416  21.306 1.00 62.85  ? 439 HIS   A ND1 1 
ATOM   3255 C CD2 . HIS   B 1 224 ? -36.504 30.350  21.449 1.00 64.01  ? 439 HIS   A CD2 1 
ATOM   3256 C CE1 . HIS   B 1 224 ? -38.355 30.951  22.465 1.00 65.70  ? 439 HIS   A CE1 1 
ATOM   3257 N NE2 . HIS   B 1 224 ? -37.037 30.924  22.575 1.00 67.43  ? 439 HIS   A NE2 1 
ATOM   3258 N N   . HIS   B 1 225 ? -39.599 30.764  17.440 1.00 54.99  ? 440 HIS   A N   1 
ATOM   3259 C CA  . HIS   B 1 225 ? -40.893 31.399  17.468 1.00 63.35  ? 440 HIS   A CA  1 
ATOM   3260 C C   . HIS   B 1 225 ? -41.919 30.306  17.688 1.00 60.17  ? 440 HIS   A C   1 
ATOM   3261 O O   . HIS   B 1 225 ? -41.923 29.298  16.957 1.00 55.40  ? 440 HIS   A O   1 
ATOM   3262 C CB  . HIS   B 1 225 ? -41.166 32.256  16.203 1.00 70.34  ? 440 HIS   A CB  1 
ATOM   3263 C CG  . HIS   B 1 225 ? -40.877 33.717  16.411 1.00 87.19  ? 440 HIS   A CG  1 
ATOM   3264 N ND1 . HIS   B 1 225 ? -41.680 34.532  17.189 1.00 101.86 ? 440 HIS   A ND1 1 
ATOM   3265 C CD2 . HIS   B 1 225 ? -39.848 34.495  16.000 1.00 94.80  ? 440 HIS   A CD2 1 
ATOM   3266 C CE1 . HIS   B 1 225 ? -41.173 35.751  17.227 1.00 98.58  ? 440 HIS   A CE1 1 
ATOM   3267 N NE2 . HIS   B 1 225 ? -40.060 35.755  16.515 1.00 103.16 ? 440 HIS   A NE2 1 
ATOM   3268 N N   . ILE   B 1 226 ? -42.765 30.507  18.708 1.00 58.29  ? 441 ILE   A N   1 
ATOM   3269 C CA  . ILE   B 1 226 ? -43.718 29.500  19.167 1.00 55.59  ? 441 ILE   A CA  1 
ATOM   3270 C C   . ILE   B 1 226 ? -45.092 29.847  18.642 1.00 56.79  ? 441 ILE   A C   1 
ATOM   3271 O O   . ILE   B 1 226 ? -45.494 30.992  18.736 1.00 67.91  ? 441 ILE   A O   1 
ATOM   3272 C CB  . ILE   B 1 226 ? -43.740 29.455  20.694 1.00 56.50  ? 441 ILE   A CB  1 
ATOM   3273 C CG1 . ILE   B 1 226 ? -42.300 29.308  21.211 1.00 56.59  ? 441 ILE   A CG1 1 
ATOM   3274 C CG2 . ILE   B 1 226 ? -44.667 28.349  21.178 1.00 57.25  ? 441 ILE   A CG2 1 
ATOM   3275 C CD1 . ILE   B 1 226 ? -42.174 29.267  22.708 1.00 59.48  ? 441 ILE   A CD1 1 
ATOM   3276 N N   . TYR   B 1 227 ? -45.804 28.850  18.119 1.00 60.89  ? 442 TYR   A N   1 
ATOM   3277 C CA  . TYR   B 1 227 ? -47.148 28.990  17.524 1.00 64.66  ? 442 TYR   A CA  1 
ATOM   3278 C C   . TYR   B 1 227 ? -48.147 27.977  18.121 1.00 67.75  ? 442 TYR   A C   1 
ATOM   3279 O O   . TYR   B 1 227 ? -47.754 26.998  18.739 1.00 70.11  ? 442 TYR   A O   1 
ATOM   3280 C CB  . TYR   B 1 227 ? -47.089 28.776  15.999 1.00 65.14  ? 442 TYR   A CB  1 
ATOM   3281 C CG  . TYR   B 1 227 ? -46.075 29.658  15.264 1.00 74.58  ? 442 TYR   A CG  1 
ATOM   3282 C CD1 . TYR   B 1 227 ? -44.709 29.344  15.256 1.00 72.75  ? 442 TYR   A CD1 1 
ATOM   3283 C CD2 . TYR   B 1 227 ? -46.485 30.807  14.569 1.00 75.60  ? 442 TYR   A CD2 1 
ATOM   3284 C CE1 . TYR   B 1 227 ? -43.788 30.153  14.589 1.00 83.12  ? 442 TYR   A CE1 1 
ATOM   3285 C CE2 . TYR   B 1 227 ? -45.573 31.621  13.901 1.00 82.59  ? 442 TYR   A CE2 1 
ATOM   3286 C CZ  . TYR   B 1 227 ? -44.221 31.303  13.908 1.00 86.80  ? 442 TYR   A CZ  1 
ATOM   3287 O OH  . TYR   B 1 227 ? -43.306 32.115  13.238 1.00 75.51  ? 442 TYR   A OH  1 
ATOM   3288 N N   . ARG   B 1 228 ? -49.434 28.223  17.919 1.00 67.70  ? 443 ARG   A N   1 
ATOM   3289 C CA  . ARG   B 1 228 ? -50.483 27.303  18.305 1.00 69.51  ? 443 ARG   A CA  1 
ATOM   3290 C C   . ARG   B 1 228 ? -50.877 26.526  17.075 1.00 68.00  ? 443 ARG   A C   1 
ATOM   3291 O O   . ARG   B 1 228 ? -50.949 27.071  15.984 1.00 62.88  ? 443 ARG   A O   1 
ATOM   3292 C CB  . ARG   B 1 228 ? -51.729 28.034  18.836 1.00 78.44  ? 443 ARG   A CB  1 
ATOM   3293 C CG  . ARG   B 1 228 ? -51.594 28.670  20.221 1.00 87.57  ? 443 ARG   A CG  1 
ATOM   3294 C CD  . ARG   B 1 228 ? -52.940 28.783  20.963 1.00 98.42  ? 443 ARG   A CD  1 
ATOM   3295 N NE  . ARG   B 1 228 ? -53.233 27.635  21.854 1.00 106.79 ? 443 ARG   A NE  1 
ATOM   3296 C CZ  . ARG   B 1 228 ? -53.017 27.574  23.181 1.00 110.24 ? 443 ARG   A CZ  1 
ATOM   3297 N NH1 . ARG   B 1 228 ? -52.488 28.601  23.871 1.00 108.08 ? 443 ARG   A NH1 1 
ATOM   3298 N NH2 . ARG   B 1 228 ? -53.333 26.453  23.838 1.00 106.97 ? 443 ARG   A NH2 1 
ATOM   3299 N N   . LEU   B 1 229 ? -51.150 25.250  17.252 1.00 63.66  ? 444 LEU   A N   1 
ATOM   3300 C CA  . LEU   B 1 229 ? -51.719 24.487  16.197 1.00 66.19  ? 444 LEU   A CA  1 
ATOM   3301 C C   . LEU   B 1 229 ? -53.228 24.569  16.357 1.00 73.19  ? 444 LEU   A C   1 
ATOM   3302 O O   . LEU   B 1 229 ? -53.751 24.414  17.475 1.00 80.68  ? 444 LEU   A O   1 
ATOM   3303 C CB  . LEU   B 1 229 ? -51.202 23.053  16.234 1.00 73.36  ? 444 LEU   A CB  1 
ATOM   3304 C CG  . LEU   B 1 229 ? -49.753 22.935  15.736 1.00 76.12  ? 444 LEU   A CG  1 
ATOM   3305 C CD1 . LEU   B 1 229 ? -49.080 21.671  16.243 1.00 80.40  ? 444 LEU   A CD1 1 
ATOM   3306 C CD2 . LEU   B 1 229 ? -49.669 22.968  14.219 1.00 76.33  ? 444 LEU   A CD2 1 
ATOM   3307 N N   . VAL   B 1 230 ? -53.913 24.846  15.244 1.00 71.63  ? 445 VAL   A N   1 
ATOM   3308 C CA  . VAL   B 1 230 ? -55.367 25.057  15.222 1.00 73.75  ? 445 VAL   A CA  1 
ATOM   3309 C C   . VAL   B 1 230 ? -55.901 24.380  13.971 1.00 75.29  ? 445 VAL   A C   1 
ATOM   3310 O O   . VAL   B 1 230 ? -55.122 23.978  13.113 1.00 69.65  ? 445 VAL   A O   1 
ATOM   3311 C CB  . VAL   B 1 230 ? -55.757 26.566  15.284 1.00 76.86  ? 445 VAL   A CB  1 
ATOM   3312 C CG1 . VAL   B 1 230 ? -57.259 26.748  15.511 1.00 85.56  ? 445 VAL   A CG1 1 
ATOM   3313 C CG2 . VAL   B 1 230 ? -55.013 27.279  16.410 1.00 73.87  ? 445 VAL   A CG2 1 
ATOM   3314 N N   . ARG   B 1 231 ? -57.215 24.180  13.916 1.00 85.45  ? 446 ARG   A N   1 
ATOM   3315 C CA  . ARG   B 1 231 ? -57.876 23.560  12.776 1.00 92.19  ? 446 ARG   A CA  1 
ATOM   3316 C C   . ARG   B 1 231 ? -59.372 23.883  12.785 1.00 92.97  ? 446 ARG   A C   1 
ATOM   3317 O O   . ARG   B 1 231 ? -59.889 24.502  11.859 1.00 93.77  ? 446 ARG   A O   1 
ATOM   3318 C CB  . ARG   B 1 231 ? -57.672 22.043  12.831 1.00 92.68  ? 446 ARG   A CB  1 
ATOM   3319 C CG  . ARG   B 1 231 ? -58.129 21.339  11.572 1.00 100.50 ? 446 ARG   A CG  1 
ATOM   3320 C CD  . ARG   B 1 231 ? -57.684 19.885  11.439 1.00 100.39 ? 446 ARG   A CD  1 
ATOM   3321 N NE  . ARG   B 1 231 ? -58.213 18.984  12.468 1.00 99.65  ? 446 ARG   A NE  1 
ATOM   3322 C CZ  . ARG   B 1 231 ? -58.259 17.649  12.377 1.00 100.45 ? 446 ARG   A CZ  1 
ATOM   3323 N NH1 . ARG   B 1 231 ? -57.827 17.008  11.290 1.00 99.86  ? 446 ARG   A NH1 1 
ATOM   3324 N NH2 . ARG   B 1 231 ? -58.749 16.933  13.389 1.00 101.95 ? 446 ARG   A NH2 1 
HETATM 3325 C C10 . A1H3Z C 2 .   ? -35.758 -6.502  17.917 1.00 74.90  ? 501 A1H3Z B C10 1 
HETATM 3326 C C15 . A1H3Z C 2 .   ? -36.622 -10.377 13.517 1.00 76.42  ? 501 A1H3Z B C15 1 
HETATM 3327 C C17 . A1H3Z C 2 .   ? -36.346 -9.424  11.351 1.00 81.95  ? 501 A1H3Z B C17 1 
HETATM 3328 C C20 . A1H3Z C 2 .   ? -36.915 -11.599 12.930 1.00 81.57  ? 501 A1H3Z B C20 1 
HETATM 3329 C C21 . A1H3Z C 2 .   ? -34.843 -8.985  17.045 1.00 71.57  ? 501 A1H3Z B C21 1 
HETATM 3330 C C22 . A1H3Z C 2 .   ? -34.152 -8.307  18.059 1.00 72.88  ? 501 A1H3Z B C22 1 
HETATM 3331 C C01 . A1H3Z C 2 .   ? -39.504 -1.712  19.492 1.00 77.01  ? 501 A1H3Z B C01 1 
HETATM 3332 C C02 . A1H3Z C 2 .   ? -38.535 -2.317  18.466 1.00 78.76  ? 501 A1H3Z B C02 1 
HETATM 3333 O O03 . A1H3Z C 2 .   ? -38.737 -2.236  17.295 1.00 72.41  ? 501 A1H3Z B O03 1 
HETATM 3334 C C04 . A1H3Z C 2 .   ? -37.299 -3.066  18.957 1.00 78.31  ? 501 A1H3Z B C04 1 
HETATM 3335 C C05 . A1H3Z C 2 .   ? -37.126 -4.340  18.142 1.00 70.72  ? 501 A1H3Z B C05 1 
HETATM 3336 C C06 . A1H3Z C 2 .   ? -35.989 -5.262  18.536 1.00 74.82  ? 501 A1H3Z B C06 1 
HETATM 3337 C C07 . A1H3Z C 2 .   ? -34.991 -5.088  19.485 1.00 81.20  ? 501 A1H3Z B C07 1 
HETATM 3338 N N08 . A1H3Z C 2 .   ? -34.183 -6.163  19.463 1.00 76.48  ? 501 A1H3Z B N08 1 
HETATM 3339 C C09 . A1H3Z C 2 .   ? -34.629 -7.040  18.503 1.00 76.31  ? 501 A1H3Z B C09 1 
HETATM 3340 C C11 . A1H3Z C 2 .   ? -36.449 -7.187  16.896 1.00 68.26  ? 501 A1H3Z B C11 1 
HETATM 3341 C C12 . A1H3Z C 2 .   ? -36.002 -8.422  16.458 1.00 70.97  ? 501 A1H3Z B C12 1 
HETATM 3342 O O13 . A1H3Z C 2 .   ? -36.775 -8.986  15.428 1.00 72.49  ? 501 A1H3Z B O13 1 
HETATM 3343 C C14 . A1H3Z C 2 .   ? -36.645 -10.315 15.039 1.00 72.33  ? 501 A1H3Z B C14 1 
HETATM 3344 C C16 . A1H3Z C 2 .   ? -36.333 -9.281  12.726 1.00 74.29  ? 501 A1H3Z B C16 1 
HETATM 3345 C C18 . A1H3Z C 2 .   ? -36.631 -10.653 10.762 1.00 82.92  ? 501 A1H3Z B C18 1 
HETATM 3346 C C19 . A1H3Z C 2 .   ? -36.916 -11.744 11.557 1.00 81.15  ? 501 A1H3Z B C19 1 
HETATM 3347 C C1  . GOL   D 3 .   ? -38.147 -3.876  23.812 1.00 84.50  ? 502 GOL   B C1  1 
HETATM 3348 O O1  . GOL   D 3 .   ? -38.162 -5.112  24.583 1.00 72.72  ? 502 GOL   B O1  1 
HETATM 3349 C C2  . GOL   D 3 .   ? -36.760 -3.251  23.540 1.00 87.85  ? 502 GOL   B C2  1 
HETATM 3350 O O2  . GOL   D 3 .   ? -35.781 -3.748  24.485 1.00 90.98  ? 502 GOL   B O2  1 
HETATM 3351 C C3  . GOL   D 3 .   ? -36.868 -1.707  23.608 1.00 91.18  ? 502 GOL   B C3  1 
HETATM 3352 O O3  . GOL   D 3 .   ? -35.764 -0.955  23.052 1.00 84.09  ? 502 GOL   B O3  1 
HETATM 3353 C C10 . A1H3Z E 2 .   ? -34.082 17.048  20.657 1.00 93.99  ? 501 A1H3Z A C10 1 
HETATM 3354 C C15 . A1H3Z E 2 .   ? -30.931 20.419  17.025 1.00 80.21  ? 501 A1H3Z A C15 1 
HETATM 3355 C C17 . A1H3Z E 2 .   ? -29.847 21.536  15.181 1.00 88.46  ? 501 A1H3Z A C17 1 
HETATM 3356 C C20 . A1H3Z E 2 .   ? -31.832 19.858  16.123 1.00 85.51  ? 501 A1H3Z A C20 1 
HETATM 3357 C C21 . A1H3Z E 2 .   ? -33.883 19.559  19.342 1.00 81.15  ? 501 A1H3Z A C21 1 
HETATM 3358 C C22 . A1H3Z E 2 .   ? -35.080 19.165  19.957 1.00 86.93  ? 501 A1H3Z A C22 1 
HETATM 3359 C C01 . A1H3Z E 2 .   ? -33.700 11.055  20.318 1.00 99.30  ? 501 A1H3Z A C01 1 
HETATM 3360 C C02 . A1H3Z E 2 .   ? -33.219 12.244  21.147 1.00 92.70  ? 501 A1H3Z A C02 1 
HETATM 3361 O O03 . A1H3Z E 2 .   ? -32.129 12.292  21.617 1.00 84.00  ? 501 A1H3Z A O03 1 
HETATM 3362 C C04 . A1H3Z E 2 .   ? -34.226 13.363  21.348 1.00 92.92  ? 501 A1H3Z A C04 1 
HETATM 3363 C C05 . A1H3Z E 2 .   ? -33.562 14.684  21.656 1.00 92.44  ? 501 A1H3Z A C05 1 
HETATM 3364 C C06 . A1H3Z E 2 .   ? -34.460 15.880  21.360 1.00 95.28  ? 501 A1H3Z A C06 1 
HETATM 3365 C C07 . A1H3Z E 2 .   ? -35.775 16.044  21.744 1.00 105.49 ? 501 A1H3Z A C07 1 
HETATM 3366 N N08 . A1H3Z E 2 .   ? -36.182 17.245  21.301 1.00 111.14 ? 501 A1H3Z A N08 1 
HETATM 3367 C C09 . A1H3Z E 2 .   ? -35.169 17.889  20.623 1.00 98.55  ? 501 A1H3Z A C09 1 
HETATM 3368 C C11 . A1H3Z E 2 .   ? -32.878 17.459  20.034 1.00 90.99  ? 501 A1H3Z A C11 1 
HETATM 3369 C C12 . A1H3Z E 2 .   ? -32.766 18.695  19.390 1.00 86.25  ? 501 A1H3Z A C12 1 
HETATM 3370 O O13 . A1H3Z E 2 .   ? -31.494 18.920  18.809 1.00 86.01  ? 501 A1H3Z A O13 1 
HETATM 3371 C C14 . A1H3Z E 2 .   ? -30.984 20.182  18.533 1.00 80.22  ? 501 A1H3Z A C14 1 
HETATM 3372 C C16 . A1H3Z E 2 .   ? -29.941 21.260  16.540 1.00 82.71  ? 501 A1H3Z A C16 1 
HETATM 3373 C C18 . A1H3Z E 2 .   ? -30.737 20.978  14.278 1.00 88.29  ? 501 A1H3Z A C18 1 
HETATM 3374 C C19 . A1H3Z E 2 .   ? -31.723 20.137  14.757 1.00 87.92  ? 501 A1H3Z A C19 1 
HETATM 3375 O O   . HOH   F 4 .   ? -31.272 -20.550 6.758  1.00 47.32  ? 601 HOH   B O   1 
HETATM 3376 O O   . HOH   F 4 .   ? -38.953 -2.531  3.775  1.00 46.61  ? 602 HOH   B O   1 
HETATM 3377 O O   . HOH   F 4 .   ? -44.484 -10.767 26.828 1.00 63.79  ? 603 HOH   B O   1 
HETATM 3378 O O   . HOH   F 4 .   ? -53.055 -8.258  21.145 1.00 55.85  ? 604 HOH   B O   1 
HETATM 3379 O O   . HOH   F 4 .   ? -11.350 -9.177  23.918 1.00 68.84  ? 605 HOH   B O   1 
HETATM 3380 O O   . HOH   F 4 .   ? -48.127 -4.010  16.482 1.00 53.15  ? 606 HOH   B O   1 
HETATM 3381 O O   . HOH   F 4 .   ? -34.009 -20.196 24.459 1.00 51.87  ? 607 HOH   B O   1 
HETATM 3382 O O   . HOH   F 4 .   ? -44.151 -22.784 12.697 1.00 77.49  ? 608 HOH   B O   1 
HETATM 3383 O O   . HOH   F 4 .   ? -41.074 -0.554  29.475 1.00 64.09  ? 609 HOH   B O   1 
HETATM 3384 O O   . HOH   F 4 .   ? -40.536 -1.217  5.624  1.00 60.21  ? 610 HOH   B O   1 
HETATM 3385 O O   . HOH   G 4 .   ? -46.780 6.126   29.867 1.00 61.50  ? 601 HOH   A O   1 
HETATM 3386 O O   . HOH   G 4 .   ? -35.165 11.804  33.725 1.00 61.66  ? 602 HOH   A O   1 
HETATM 3387 O O   . HOH   G 4 .   ? -42.704 32.958  20.088 1.00 51.91  ? 603 HOH   A O   1 
HETATM 3388 O O   . HOH   G 4 .   ? -37.484 34.153  25.946 1.00 57.62  ? 604 HOH   A O   1 
HETATM 3389 O O   . HOH   G 4 .   ? -45.282 34.109  19.059 1.00 64.93  ? 605 HOH   A O   1 
HETATM 3390 O O   . HOH   G 4 .   ? -29.401 6.903   23.021 1.00 70.37  ? 606 HOH   A O   1 
HETATM 3391 O O   . HOH   G 4 .   ? -57.208 8.054   28.039 1.00 64.18  ? 607 HOH   A O   1 
HETATM 3392 O O   . HOH   G 4 .   ? -50.245 31.902  24.689 1.00 62.49  ? 608 HOH   A O   1 
HETATM 3393 O O   . HOH   G 4 .   ? -49.716 29.279  33.072 1.00 72.17  ? 609 HOH   A O   1 
# 
