data_8RXQ
# 
_entry.id   8RXQ 
# 
_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   8RXQ         pdb_00008rxq 10.2210/pdb8rxq/pdb 
WWPDB D_1292136475 ?            ?                   
# 
_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                        8RXQ 
_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'                          27489.096 2 ? ? ? ? 
2 non-polymer syn 'ethyl (~{E})-3-(5-phenylmethoxy-1~{H}-indol-3-yl)prop-2-enoate' 321.370   1 ? ? ? ? 
# 
_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       
;MAWQARGLGTARLQLVEFSAFVEPPDAVDSYQRHLFVHISQHCPSPGAPPLESVDVRQIYDKFPEKKGGLRELYDRGPPH
AFFLVKFWADLNWGPSGEEAGAGGSISSGGFYGVSSQYESLEHMTLTCSSKVCSFGKQVVEKVETERAQLEDGRFVYRLL
RSPMCEYLVNFLHKLRQLPERYMMNSVLENFTILQVVTNRDTQELLLCTAYVFEVSTSERGAQHHIYRLVRDVEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAWQARGLGTARLQLVEFSAFVEPPDAVDSYQRHLFVHISQHCPSPGAPPLESVDVRQIYDKFPEKKGGLRELYDRGPPH
AFFLVKFWADLNWGPSGEEAGAGGSISSGGFYGVSSQYESLEHMTLTCSSKVCSFGKQVVEKVETERAQLEDGRFVYRLL
RSPMCEYLVNFLHKLRQLPERYMMNSVLENFTILQVVTNRDTQELLLCTAYVFEVSTSERGAQHHIYRLVRDVEHHHHHH
;
_entity_poly.pdbx_strand_id                 B,A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        'ethyl (~{E})-3-(5-phenylmethoxy-1~{H}-indol-3-yl)prop-2-enoate' 
_pdbx_entity_nonpoly.comp_id     A1H3X 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   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 
A1H3X non-polymer         . 'ethyl (~{E})-3-(5-phenylmethoxy-1~{H}-indol-3-yl)prop-2-enoate' ? 'C20 H19 N O3'   321.370 
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  
HIS   'L-peptide linking' y HISTIDINE                                                        ? 'C6 H10 N3 O2 1' 156.162 
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   MET 1   216 ?   ?   ?   B . n 
A 1 2   ALA 2   217 ?   ?   ?   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 108 323 323 SER SER 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   MET 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  240 240 PRO PRO 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  247 247 GLN GLN 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  257 257 HIS HIS 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 ?   ?   ?   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  309 309 GLY GLY A . n 
B 1 95  PRO 95  310 310 PRO PRO A . n 
B 1 96  SER 96  311 311 SER SER 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 109 324 324 GLY GLY 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        A1H3X 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H3X 
_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        ? 
# 
_pdbx_nonpoly_scheme.asym_id         C 
_pdbx_nonpoly_scheme.entity_id       2 
_pdbx_nonpoly_scheme.mon_id          A1H3X 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     501 
_pdbx_nonpoly_scheme.auth_seq_num    1 
_pdbx_nonpoly_scheme.pdb_mon_id      A1H3X 
_pdbx_nonpoly_scheme.auth_mon_id     LIG 
_pdbx_nonpoly_scheme.pdb_strand_id   B 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
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 A LYS 281 ? CG  ? B LYS 66  CG  
6  1 Y 1 A LYS 281 ? CD  ? B LYS 66  CD  
7  1 Y 1 A LYS 281 ? CE  ? B LYS 66  CE  
8  1 Y 1 A LYS 281 ? NZ  ? B LYS 66  NZ  
9  1 Y 1 A HIS 388 ? ND1 ? B HIS 173 ND1 
10 1 Y 1 A HIS 388 ? CD2 ? B HIS 173 CD2 
11 1 Y 1 A HIS 388 ? CE1 ? B HIS 173 CE1 
12 1 Y 1 A HIS 388 ? NE2 ? B HIS 173 NE2 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? pointless ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   117.42 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RXQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     123.135 
_cell.length_a_esd                 ? 
_cell.length_b                     61.309 
_cell.length_b_esd                 ? 
_cell.length_c                     80.186 
_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                         8RXQ 
_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                   8RXQ 
_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             2.44 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.66 
_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            288 
# 
_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                                       8RXQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.63 
_reflns.d_resolution_low                               54.65 
_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                                     26769 
_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                           94.77 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.68 
_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                                   0.985 
_reflns.pdbx_CC_star                                   0.996 
_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                                    2.63 
_reflns_shell.d_res_low                                     2.72 
_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                             2647 
_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                                  0.586 
_reflns_shell.pdbx_CC_star                                  0.859 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 8RXQ 
_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                            2.63 
_refine.ls_d_res_low                             54.65 
_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                     26769 
_refine.ls_number_reflns_R_free                  1338 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    86.58 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2225 
_refine.ls_R_factor_R_free                       0.2690 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2200 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.34 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 36.03 
_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                             ? 
_refine.overall_SU_ML                            0.54 
_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                         LAST 
_refine_hist.pdbx_number_atoms_protein        3353 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         24 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               3377 
_refine_hist.d_res_high                       2.63 
_refine_hist.d_res_low                        54.65 
# 
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' ? 0.009 ? 3460 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.079 ? 4672 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 9.946 ? 458  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054 ? 499  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009 ? 599  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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 
_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 
'X-RAY DIFFRACTION' 2.63 2.73  . . 138 2430 82.00 . . . . 0.3877 . . . . . . . . . . . 0.4135 
'X-RAY DIFFRACTION' 2.73 2.83  . . 132 2547 87.00 . . . . 0.3607 . . . . . . . . . . . 0.3750 
'X-RAY DIFFRACTION' 2.83 2.96  . . 127 2595 88.00 . . . . 0.3406 . . . . . . . . . . . 0.4448 
'X-RAY DIFFRACTION' 2.96 3.12  . . 157 2671 91.00 . . . . 0.3211 . . . . . . . . . . . 0.3867 
'X-RAY DIFFRACTION' 3.12 3.31  . . 122 2608 89.00 . . . . 0.27   . . . . . . . . . . . 0.2721 
'X-RAY DIFFRACTION' 3.32 3.57  . . 142 2526 86.00 . . . . 0.2234 . . . . . . . . . . . 0.3374 
'X-RAY DIFFRACTION' 3.57 3.93  . . 127 2575 88.00 . . . . 0.2083 . . . . . . . . . . . 0.2454 
'X-RAY DIFFRACTION' 3.93 4.50  . . 144 2526 86.00 . . . . 0.1664 . . . . . . . . . . . 0.2360 
'X-RAY DIFFRACTION' 4.50 5.66  . . 141 2552 87.00 . . . . 0.1649 . . . . . . . . . . . 0.1897 
'X-RAY DIFFRACTION' 5.67 54.65 . . 108 2401 81.00 . . . . 0.1979 . . . . . . . . . . . 0.2631 
# 
_struct.entry_id                     8RXQ 
_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        8RXQ 
_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 ? 
# 
_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   
;AWQARGLGTARLQLVEFSAFVEPPDAVDSYQRHLFVHISQHCPSPGAPPLESVDVRQIYDKFPEKKGGLRELYDRGPPHA
FFLVKFWADLNWGPSGEEAGAGGSISSGGFYGVSSQYESLEHMTLTCSSKVCSFGKQVVEKVETERAQLEDGRFVYRLLR
SPMCEYLVNFLHKLRQLPERYMMNSVLENFTILQVVTNRDTQELLLCTAYVFEVSTSERGAQHHIYRLVRD
;
_struct_ref.pdbx_align_begin           217 
# 
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 8RXQ B 2 ? 232 ? Q15562 217 ? 447 ? 217 447 
2 1 8RXQ A 2 ? 232 ? Q15562 217 ? 447 ? 217 447 
# 
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 8RXQ MET B 1   ? UNP Q15562 ? ? 'initiating methionine' 216 1  
1 8RXQ VAL B 233 ? UNP Q15562 ? ? 'expression tag'        448 2  
1 8RXQ GLU B 234 ? UNP Q15562 ? ? 'expression tag'        449 3  
1 8RXQ HIS B 235 ? UNP Q15562 ? ? 'expression tag'        450 4  
1 8RXQ HIS B 236 ? UNP Q15562 ? ? 'expression tag'        451 5  
1 8RXQ HIS B 237 ? UNP Q15562 ? ? 'expression tag'        452 6  
1 8RXQ HIS B 238 ? UNP Q15562 ? ? 'expression tag'        453 7  
1 8RXQ HIS B 239 ? UNP Q15562 ? ? 'expression tag'        454 8  
1 8RXQ HIS B 240 ? UNP Q15562 ? ? 'expression tag'        455 9  
2 8RXQ MET A 1   ? UNP Q15562 ? ? 'initiating methionine' 216 10 
2 8RXQ VAL A 233 ? UNP Q15562 ? ? 'expression tag'        448 11 
2 8RXQ GLU A 234 ? UNP Q15562 ? ? 'expression tag'        449 12 
2 8RXQ HIS A 235 ? UNP Q15562 ? ? 'expression tag'        450 13 
2 8RXQ HIS A 236 ? UNP Q15562 ? ? 'expression tag'        451 14 
2 8RXQ HIS A 237 ? UNP Q15562 ? ? 'expression tag'        452 15 
2 8RXQ HIS A 238 ? UNP Q15562 ? ? 'expression tag'        453 16 
2 8RXQ HIS A 239 ? UNP Q15562 ? ? 'expression tag'        454 17 
2 8RXQ HIS A 240 ? UNP Q15562 ? ? 'expression tag'        455 18 
# 
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 
2 1 B   
# 
_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 PRO A 24  ? ASP A 29  ? PRO B 239 ASP B 244 5 ? 6  
HELX_P HELX_P2  AA2 ARG A 57  ? PHE A 63  ? ARG B 272 PHE B 278 5 ? 7  
HELX_P HELX_P3  AA3 GLY A 69  ? GLY A 77  ? GLY B 284 GLY B 292 1 ? 9  
HELX_P HELX_P4  AA4 PRO A 78  ? HIS A 80  ? PRO B 293 HIS B 295 5 ? 3  
HELX_P HELX_P5  AA5 CYS A 165 ? LEU A 178 ? CYS B 380 LEU B 393 1 ? 14 
HELX_P HELX_P6  AA6 GLU A 180 ? LEU A 188 ? GLU B 395 LEU B 403 1 ? 9  
HELX_P HELX_P7  AA7 ARG B 57  ? PHE B 63  ? ARG A 272 PHE A 278 5 ? 7  
HELX_P HELX_P8  AA8 GLY B 69  ? GLY B 77  ? GLY A 284 GLY A 292 1 ? 9  
HELX_P HELX_P9  AA9 PRO B 78  ? HIS B 80  ? PRO A 293 HIS A 295 5 ? 3  
HELX_P HELX_P10 AB1 CYS B 165 ? GLN B 177 ? CYS A 380 GLN A 392 1 ? 13 
HELX_P HELX_P11 AB2 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 -3.31 
2 GLY 77 B . ? GLY 292 A PRO 78 B ? PRO 293 A 1 -5.08 
# 
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 TYR A 118 ? N TYR B 333 O TYR A 157 ? O TYR B 372 
AA1 4  5  O VAL A 156 ? O VAL B 371 N GLN A 149 ? N GLN B 364 
AA2 1  2  N VAL A 54  ? N VAL B 269 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 207 ? O LEU B 422 N VAL A 197 ? N VAL B 412 
AA2 5  6  O THR A 192 ? O THR B 407 N CYS A 133 ? N CYS B 348 
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 PHE B 36  ? O PHE A 251 N ALA B 20  ? N ALA A 235 
AA3 2  3  N SER B 19  ? N SER A 234 O SER B 115 ? O SER A 330 
AA3 3  4  N SER B 116 ? N SER A 331 O LEU B 159 ? O LEU A 374 
AA3 4  5  O ARG B 154 ? O ARG A 369 N GLU B 151 ? N GLU A 366 
# 
_pdbx_entry_details.entry_id                   8RXQ 
_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 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP B 241 ? ? -68.59  5.37    
2  1 ASP B 244 ? ? -98.05  -74.74  
3  1 GLN B 247 ? ? -174.14 147.93  
4  1 HIS B 253 ? ? -172.27 105.66  
5  1 GLN B 256 ? ? -116.02 74.27   
6  1 GLN B 273 ? ? -57.71  -2.60   
7  1 GLU B 280 ? ? -115.30 -94.66  
8  1 LYS B 282 ? ? 40.47   108.53  
9  1 GLU B 366 ? ? -123.32 -143.82 
10 1 ASP B 367 ? ? -65.86  83.35   
11 1 LEU B 374 ? ? -118.55 63.16   
12 1 THR B 432 ? ? -51.11  89.63   
13 1 HIS A 253 ? ? -162.70 104.26  
14 1 GLN A 256 ? ? -141.71 28.83   
15 1 ILE A 274 ? ? -142.12 30.11   
16 1 LYS A 281 ? ? 59.64   -57.40  
17 1 LYS A 282 ? ? -50.73  60.21   
18 1 ARG A 291 ? ? -59.95  -9.68   
19 1 PRO A 310 ? ? -66.80  -72.24  
20 1 ASP A 367 ? ? -24.25  73.79   
21 1 LEU A 374 ? ? -111.05 69.51   
22 1 GLU A 404 ? ? -36.92  -33.45  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   SER 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    433 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLU 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    434 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            137.14 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -32.5335 -16.9663 22.8826 0.6077 ? 0.0405  ? 0.0396  ? 0.4251 ? 0.0521  ? 0.5781 ? 5.3468 ? 1.4786 
? 3.6190  ? 3.0668 ? 0.7916  ? 6.2375 ? 0.3218  ? -0.3652 ? -0.5293 ? 0.4222  ? -0.1481 ? -0.2858 ? 0.6656  ? -0.0218 ? -0.2282 ? 
2 'X-RAY DIFFRACTION' ? refined -18.2639 -2.5120  18.6372 0.7936 ? -0.1795 ? -0.1588 ? 1.0517 ? 0.1931  ? 0.9342 ? 4.7882 ? 3.3356 
? -1.7957 ? 2.5599 ? -0.8014 ? 1.5725 ? -0.7888 ? 1.7876  ? 1.1119  ? -1.3581 ? 0.6834  ? 0.0780  ? 0.1810  ? 0.5547  ? 0.0388  ? 
3 'X-RAY DIFFRACTION' ? refined -32.4052 -16.7061 16.7521 0.6975 ? 0.0211  ? 0.0452  ? 0.4409 ? 0.0199  ? 0.5259 ? 3.7704 ? 1.5903 
? 1.3283  ? 2.9684 ? 1.0984  ? 6.4436 ? 0.0060  ? 0.5162  ? 0.0173  ? -0.0066 ? -0.0077 ? -0.0607 ? 0.6345  ? 0.2912  ? -0.2076 ? 
4 'X-RAY DIFFRACTION' ? refined -35.5781 -6.5703  27.6061 0.5073 ? 0.0942  ? 0.0360  ? 0.5432 ? -0.0458 ? 0.5253 ? 4.0678 ? 0.6368 
? 0.7033  ? 2.4314 ? 0.7472  ? 5.8775 ? 0.1526  ? -0.5936 ? 0.3537  ? 0.2831  ? -0.1536 ? 0.0552  ? -0.5980 ? -0.7166 ? 0.0436  ? 
5 'X-RAY DIFFRACTION' ? refined -31.5669 -13.5208 14.0023 0.6083 ? 0.0084  ? 0.0663  ? 0.4305 ? 0.0242  ? 0.6016 ? 3.2187 ? 0.6385 
? 1.5607  ? 1.2151 ? 1.6079  ? 6.3154 ? 0.1526  ? -0.0131 ? -0.1504 ? -0.2219 ? 0.1256  ? -0.2621 ? 0.0473  ? -0.0643 ? -0.1186 ? 
6 'X-RAY DIFFRACTION' ? refined -39.0567 20.9549  22.2864 0.6826 ? 0.1501  ? 0.0886  ? 0.4291 ? 0.0176  ? 0.6149 ? 7.5370 ? 0.9376 
? -1.6288 ? 3.6539 ? -0.5092 ? 6.6886 ? 0.5842  ? 0.0119  ? 0.4016  ? -0.3963 ? -0.1741 ? 0.0545  ? -0.8465 ? 0.1674  ? -0.1127 ? 
7 'X-RAY DIFFRACTION' ? refined -51.7821 8.8159   15.0636 1.0077 ? -0.0940 ? 0.1908  ? 0.9559 ? -0.0394 ? 1.1767 ? 3.1631 ? 
-2.0484 ? 1.1711  ? 1.6752 ? -0.9043 ? 0.4958 ? -0.3425 ? 1.2460  ? -1.3432 ? -1.2509 ? 0.5964  ? 0.1669  ? 0.9600  ? 0.0405  ? 
0.2528  ? 
8 'X-RAY DIFFRACTION' ? refined -36.9157 15.6715  21.1134 0.5876 ? 0.0471  ? -0.0001 ? 0.3774 ? -0.0027 ? 0.5311 ? 4.6523 ? 0.2993 
? -3.6226 ? 1.9976 ? -1.0849 ? 7.5303 ? 0.1338  ? -0.3589 ? 0.2739  ? 0.0161  ? -0.0238 ? 0.0023  ? -0.0770 ? 0.4712  ? -0.1226 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 218 through 277 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 278 through 293 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 294 through 325 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 326 through 380 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 381 through 446 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 222 through 277 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 278 through 293 )
;
8 'X-RAY DIFFRACTION' 8 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 294 through 446 )
;
# 
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 MET 216 ? A MET 1   
2  1 Y 1 B ALA 217 ? A ALA 2   
3  1 Y 1 B CYS 258 ? A CYS 43  
4  1 Y 1 B PRO 259 ? A PRO 44  
5  1 Y 1 B SER 260 ? A SER 45  
6  1 Y 1 B PRO 261 ? A PRO 46  
7  1 Y 1 B GLY 262 ? A GLY 47  
8  1 Y 1 B ALA 263 ? A ALA 48  
9  1 Y 1 B GLY 309 ? A GLY 94  
10 1 Y 1 B PRO 310 ? A PRO 95  
11 1 Y 1 B SER 311 ? A SER 96  
12 1 Y 1 B GLY 312 ? A GLY 97  
13 1 Y 1 B GLU 313 ? A GLU 98  
14 1 Y 1 B GLU 314 ? A GLU 99  
15 1 Y 1 B ALA 315 ? A ALA 100 
16 1 Y 1 B GLY 316 ? A GLY 101 
17 1 Y 1 B ALA 317 ? A ALA 102 
18 1 Y 1 B GLY 318 ? A GLY 103 
19 1 Y 1 B GLY 319 ? A GLY 104 
20 1 Y 1 B SER 320 ? A SER 105 
21 1 Y 1 B ILE 321 ? A ILE 106 
22 1 Y 1 B SER 322 ? A SER 107 
23 1 Y 1 B ASP 447 ? A ASP 232 
24 1 Y 1 B VAL 448 ? A VAL 233 
25 1 Y 1 B GLU 449 ? A GLU 234 
26 1 Y 1 B HIS 450 ? A HIS 235 
27 1 Y 1 B HIS 451 ? A HIS 236 
28 1 Y 1 B HIS 452 ? A HIS 237 
29 1 Y 1 B HIS 453 ? A HIS 238 
30 1 Y 1 B HIS 454 ? A HIS 239 
31 1 Y 1 B HIS 455 ? A HIS 240 
32 1 Y 1 A MET 216 ? B MET 1   
33 1 Y 1 A ALA 217 ? B ALA 2   
34 1 Y 1 A TRP 218 ? B TRP 3   
35 1 Y 1 A GLN 219 ? B GLN 4   
36 1 Y 1 A ALA 220 ? B ALA 5   
37 1 Y 1 A ARG 221 ? B ARG 6   
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 CYS 258 ? B CYS 43  
45 1 Y 1 A PRO 259 ? B PRO 44  
46 1 Y 1 A SER 260 ? B SER 45  
47 1 Y 1 A PRO 261 ? B PRO 46  
48 1 Y 1 A GLY 262 ? B GLY 47  
49 1 Y 1 A ALA 263 ? B ALA 48  
50 1 Y 1 A PRO 264 ? B PRO 49  
51 1 Y 1 A GLY 312 ? B GLY 97  
52 1 Y 1 A GLU 313 ? B GLU 98  
53 1 Y 1 A GLU 314 ? B GLU 99  
54 1 Y 1 A ALA 315 ? B ALA 100 
55 1 Y 1 A GLY 316 ? B GLY 101 
56 1 Y 1 A ALA 317 ? B ALA 102 
57 1 Y 1 A GLY 318 ? B GLY 103 
58 1 Y 1 A GLY 319 ? B GLY 104 
59 1 Y 1 A SER 320 ? B SER 105 
60 1 Y 1 A ILE 321 ? B ILE 106 
61 1 Y 1 A SER 322 ? B SER 107 
62 1 Y 1 A SER 323 ? B SER 108 
63 1 Y 1 A ASP 447 ? B ASP 232 
64 1 Y 1 A VAL 448 ? B VAL 233 
65 1 Y 1 A GLU 449 ? B GLU 234 
66 1 Y 1 A HIS 450 ? B HIS 235 
67 1 Y 1 A HIS 451 ? B HIS 236 
68 1 Y 1 A HIS 452 ? B HIS 237 
69 1 Y 1 A HIS 453 ? B HIS 238 
70 1 Y 1 A HIS 454 ? B HIS 239 
71 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 
A1H3X C13  C Y N 1   
A1H3X C17  C Y N 2   
A1H3X C20  C Y N 3   
A1H3X C21  C Y N 4   
A1H3X C22  C Y N 5   
A1H3X C24  C Y N 6   
A1H3X C01  C N N 7   
A1H3X C02  C N N 8   
A1H3X C04  C N N 9   
A1H3X C06  C N N 10  
A1H3X C07  C N N 11  
A1H3X C08  C Y N 12  
A1H3X C09  C Y N 13  
A1H3X C11  C Y N 14  
A1H3X C12  C Y N 15  
A1H3X C14  C Y N 16  
A1H3X C16  C N N 17  
A1H3X C18  C Y N 18  
A1H3X C19  C Y N 19  
A1H3X C23  C Y N 20  
A1H3X N10  N Y N 21  
A1H3X O03  O N N 22  
A1H3X O05  O N N 23  
A1H3X O15  O N N 24  
A1H3X H1   H N N 25  
A1H3X H2   H N N 26  
A1H3X H3   H N N 27  
A1H3X H4   H N N 28  
A1H3X H5   H N N 29  
A1H3X H6   H N N 30  
A1H3X H7   H N N 31  
A1H3X H8   H N N 32  
A1H3X H9   H N N 33  
A1H3X H10  H N N 34  
A1H3X H11  H N N 35  
A1H3X H12  H N N 36  
A1H3X H13  H N N 37  
A1H3X H14  H N N 38  
A1H3X H15  H N N 39  
A1H3X H16  H N N 40  
A1H3X H17  H N N 41  
A1H3X H18  H N N 42  
A1H3X H19  H N N 43  
ALA   N    N N N 44  
ALA   CA   C N S 45  
ALA   C    C N N 46  
ALA   O    O N N 47  
ALA   CB   C N N 48  
ALA   OXT  O N N 49  
ALA   H    H N N 50  
ALA   H2   H N N 51  
ALA   HA   H N N 52  
ALA   HB1  H N N 53  
ALA   HB2  H N N 54  
ALA   HB3  H N N 55  
ALA   HXT  H N N 56  
ARG   N    N N N 57  
ARG   CA   C N S 58  
ARG   C    C N N 59  
ARG   O    O N N 60  
ARG   CB   C N N 61  
ARG   CG   C N N 62  
ARG   CD   C N N 63  
ARG   NE   N N N 64  
ARG   CZ   C N N 65  
ARG   NH1  N N N 66  
ARG   NH2  N N N 67  
ARG   OXT  O N N 68  
ARG   H    H N N 69  
ARG   H2   H N N 70  
ARG   HA   H N N 71  
ARG   HB2  H N N 72  
ARG   HB3  H N N 73  
ARG   HG2  H N N 74  
ARG   HG3  H N N 75  
ARG   HD2  H N N 76  
ARG   HD3  H N N 77  
ARG   HE   H N N 78  
ARG   HH11 H N N 79  
ARG   HH12 H N N 80  
ARG   HH21 H N N 81  
ARG   HH22 H N N 82  
ARG   HXT  H N N 83  
ASN   N    N N N 84  
ASN   CA   C N S 85  
ASN   C    C N N 86  
ASN   O    O N N 87  
ASN   CB   C N N 88  
ASN   CG   C N N 89  
ASN   OD1  O N N 90  
ASN   ND2  N N N 91  
ASN   OXT  O N N 92  
ASN   H    H N N 93  
ASN   H2   H N N 94  
ASN   HA   H N N 95  
ASN   HB2  H N N 96  
ASN   HB3  H N N 97  
ASN   HD21 H N N 98  
ASN   HD22 H N N 99  
ASN   HXT  H N N 100 
ASP   N    N N N 101 
ASP   CA   C N S 102 
ASP   C    C N N 103 
ASP   O    O N N 104 
ASP   CB   C N N 105 
ASP   CG   C N N 106 
ASP   OD1  O N N 107 
ASP   OD2  O N N 108 
ASP   OXT  O N N 109 
ASP   H    H N N 110 
ASP   H2   H N N 111 
ASP   HA   H N N 112 
ASP   HB2  H N N 113 
ASP   HB3  H N N 114 
ASP   HD2  H N N 115 
ASP   HXT  H N N 116 
CYS   N    N N N 117 
CYS   CA   C N R 118 
CYS   C    C N N 119 
CYS   O    O N N 120 
CYS   CB   C N N 121 
CYS   SG   S N N 122 
CYS   OXT  O N N 123 
CYS   H    H N N 124 
CYS   H2   H N N 125 
CYS   HA   H N N 126 
CYS   HB2  H N N 127 
CYS   HB3  H N N 128 
CYS   HG   H N N 129 
CYS   HXT  H N N 130 
GLN   N    N N N 131 
GLN   CA   C N S 132 
GLN   C    C N N 133 
GLN   O    O N N 134 
GLN   CB   C N N 135 
GLN   CG   C N N 136 
GLN   CD   C N N 137 
GLN   OE1  O N N 138 
GLN   NE2  N N N 139 
GLN   OXT  O N N 140 
GLN   H    H N N 141 
GLN   H2   H N N 142 
GLN   HA   H N N 143 
GLN   HB2  H N N 144 
GLN   HB3  H N N 145 
GLN   HG2  H N N 146 
GLN   HG3  H N N 147 
GLN   HE21 H N N 148 
GLN   HE22 H N N 149 
GLN   HXT  H N N 150 
GLU   N    N N N 151 
GLU   CA   C N S 152 
GLU   C    C N N 153 
GLU   O    O N N 154 
GLU   CB   C N N 155 
GLU   CG   C N N 156 
GLU   CD   C N N 157 
GLU   OE1  O N N 158 
GLU   OE2  O N N 159 
GLU   OXT  O N N 160 
GLU   H    H N N 161 
GLU   H2   H N N 162 
GLU   HA   H N N 163 
GLU   HB2  H N N 164 
GLU   HB3  H N N 165 
GLU   HG2  H N N 166 
GLU   HG3  H N N 167 
GLU   HE2  H N N 168 
GLU   HXT  H N N 169 
GLY   N    N N N 170 
GLY   CA   C N N 171 
GLY   C    C N N 172 
GLY   O    O N N 173 
GLY   OXT  O N N 174 
GLY   H    H N N 175 
GLY   H2   H N N 176 
GLY   HA2  H N N 177 
GLY   HA3  H N N 178 
GLY   HXT  H N N 179 
HIS   N    N N N 180 
HIS   CA   C N S 181 
HIS   C    C N N 182 
HIS   O    O N N 183 
HIS   CB   C N N 184 
HIS   CG   C Y N 185 
HIS   ND1  N Y N 186 
HIS   CD2  C Y N 187 
HIS   CE1  C Y N 188 
HIS   NE2  N Y N 189 
HIS   OXT  O N N 190 
HIS   H    H N N 191 
HIS   H2   H N N 192 
HIS   HA   H N N 193 
HIS   HB2  H N N 194 
HIS   HB3  H N N 195 
HIS   HD1  H N N 196 
HIS   HD2  H N N 197 
HIS   HE1  H N N 198 
HIS   HE2  H N N 199 
HIS   HXT  H N N 200 
ILE   N    N N N 201 
ILE   CA   C N S 202 
ILE   C    C N N 203 
ILE   O    O N N 204 
ILE   CB   C N S 205 
ILE   CG1  C N N 206 
ILE   CG2  C N N 207 
ILE   CD1  C N N 208 
ILE   OXT  O N N 209 
ILE   H    H N N 210 
ILE   H2   H N N 211 
ILE   HA   H N N 212 
ILE   HB   H N N 213 
ILE   HG12 H N N 214 
ILE   HG13 H N N 215 
ILE   HG21 H N N 216 
ILE   HG22 H N N 217 
ILE   HG23 H N N 218 
ILE   HD11 H N N 219 
ILE   HD12 H N N 220 
ILE   HD13 H N N 221 
ILE   HXT  H N N 222 
LEU   N    N N N 223 
LEU   CA   C N S 224 
LEU   C    C N N 225 
LEU   O    O N N 226 
LEU   CB   C N N 227 
LEU   CG   C N N 228 
LEU   CD1  C N N 229 
LEU   CD2  C N N 230 
LEU   OXT  O N N 231 
LEU   H    H N N 232 
LEU   H2   H N N 233 
LEU   HA   H N N 234 
LEU   HB2  H N N 235 
LEU   HB3  H N N 236 
LEU   HG   H N N 237 
LEU   HD11 H N N 238 
LEU   HD12 H N N 239 
LEU   HD13 H N N 240 
LEU   HD21 H N N 241 
LEU   HD22 H N N 242 
LEU   HD23 H N N 243 
LEU   HXT  H N N 244 
LYS   N    N N N 245 
LYS   CA   C N S 246 
LYS   C    C N N 247 
LYS   O    O N N 248 
LYS   CB   C N N 249 
LYS   CG   C N N 250 
LYS   CD   C N N 251 
LYS   CE   C N N 252 
LYS   NZ   N N N 253 
LYS   OXT  O N N 254 
LYS   H    H N N 255 
LYS   H2   H N N 256 
LYS   HA   H N N 257 
LYS   HB2  H N N 258 
LYS   HB3  H N N 259 
LYS   HG2  H N N 260 
LYS   HG3  H N N 261 
LYS   HD2  H N N 262 
LYS   HD3  H N N 263 
LYS   HE2  H N N 264 
LYS   HE3  H N N 265 
LYS   HZ1  H N N 266 
LYS   HZ2  H N N 267 
LYS   HZ3  H N N 268 
LYS   HXT  H N N 269 
MET   N    N N N 270 
MET   CA   C N S 271 
MET   C    C N N 272 
MET   O    O N N 273 
MET   CB   C N N 274 
MET   CG   C N N 275 
MET   SD   S N N 276 
MET   CE   C N N 277 
MET   OXT  O N N 278 
MET   H    H N N 279 
MET   H2   H N N 280 
MET   HA   H N N 281 
MET   HB2  H N N 282 
MET   HB3  H N N 283 
MET   HG2  H N N 284 
MET   HG3  H N N 285 
MET   HE1  H N N 286 
MET   HE2  H N N 287 
MET   HE3  H N N 288 
MET   HXT  H N N 289 
PHE   N    N N N 290 
PHE   CA   C N S 291 
PHE   C    C N N 292 
PHE   O    O N N 293 
PHE   CB   C N N 294 
PHE   CG   C Y N 295 
PHE   CD1  C Y N 296 
PHE   CD2  C Y N 297 
PHE   CE1  C Y N 298 
PHE   CE2  C Y N 299 
PHE   CZ   C Y N 300 
PHE   OXT  O N N 301 
PHE   H    H N N 302 
PHE   H2   H N N 303 
PHE   HA   H N N 304 
PHE   HB2  H N N 305 
PHE   HB3  H N N 306 
PHE   HD1  H N N 307 
PHE   HD2  H N N 308 
PHE   HE1  H N N 309 
PHE   HE2  H N N 310 
PHE   HZ   H N N 311 
PHE   HXT  H N N 312 
PRO   N    N N N 313 
PRO   CA   C N S 314 
PRO   C    C N N 315 
PRO   O    O N N 316 
PRO   CB   C N N 317 
PRO   CG   C N N 318 
PRO   CD   C N N 319 
PRO   OXT  O N N 320 
PRO   H    H N N 321 
PRO   HA   H N N 322 
PRO   HB2  H N N 323 
PRO   HB3  H N N 324 
PRO   HG2  H N N 325 
PRO   HG3  H N N 326 
PRO   HD2  H N N 327 
PRO   HD3  H N N 328 
PRO   HXT  H N N 329 
SER   N    N N N 330 
SER   CA   C N S 331 
SER   C    C N N 332 
SER   O    O N N 333 
SER   CB   C N N 334 
SER   OG   O N N 335 
SER   OXT  O N N 336 
SER   H    H N N 337 
SER   H2   H N N 338 
SER   HA   H N N 339 
SER   HB2  H N N 340 
SER   HB3  H N N 341 
SER   HG   H N N 342 
SER   HXT  H N N 343 
THR   N    N N N 344 
THR   CA   C N S 345 
THR   C    C N N 346 
THR   O    O N N 347 
THR   CB   C N R 348 
THR   OG1  O N N 349 
THR   CG2  C N N 350 
THR   OXT  O N N 351 
THR   H    H N N 352 
THR   H2   H N N 353 
THR   HA   H N N 354 
THR   HB   H N N 355 
THR   HG1  H N N 356 
THR   HG21 H N N 357 
THR   HG22 H N N 358 
THR   HG23 H N N 359 
THR   HXT  H N N 360 
TRP   N    N N N 361 
TRP   CA   C N S 362 
TRP   C    C N N 363 
TRP   O    O N N 364 
TRP   CB   C N N 365 
TRP   CG   C Y N 366 
TRP   CD1  C Y N 367 
TRP   CD2  C Y N 368 
TRP   NE1  N Y N 369 
TRP   CE2  C Y N 370 
TRP   CE3  C Y N 371 
TRP   CZ2  C Y N 372 
TRP   CZ3  C Y N 373 
TRP   CH2  C Y N 374 
TRP   OXT  O N N 375 
TRP   H    H N N 376 
TRP   H2   H N N 377 
TRP   HA   H N N 378 
TRP   HB2  H N N 379 
TRP   HB3  H N N 380 
TRP   HD1  H N N 381 
TRP   HE1  H N N 382 
TRP   HE3  H N N 383 
TRP   HZ2  H N N 384 
TRP   HZ3  H N N 385 
TRP   HH2  H N N 386 
TRP   HXT  H N N 387 
TYR   N    N N N 388 
TYR   CA   C N S 389 
TYR   C    C N N 390 
TYR   O    O N N 391 
TYR   CB   C N N 392 
TYR   CG   C Y N 393 
TYR   CD1  C Y N 394 
TYR   CD2  C Y N 395 
TYR   CE1  C Y N 396 
TYR   CE2  C Y N 397 
TYR   CZ   C Y N 398 
TYR   OH   O N N 399 
TYR   OXT  O N N 400 
TYR   H    H N N 401 
TYR   H2   H N N 402 
TYR   HA   H N N 403 
TYR   HB2  H N N 404 
TYR   HB3  H N N 405 
TYR   HD1  H N N 406 
TYR   HD2  H N N 407 
TYR   HE1  H N N 408 
TYR   HE2  H N N 409 
TYR   HH   H N N 410 
TYR   HXT  H N N 411 
VAL   N    N N N 412 
VAL   CA   C N S 413 
VAL   C    C N N 414 
VAL   O    O N N 415 
VAL   CB   C N N 416 
VAL   CG1  C N N 417 
VAL   CG2  C N N 418 
VAL   OXT  O N N 419 
VAL   H    H N N 420 
VAL   H2   H N N 421 
VAL   HA   H N N 422 
VAL   HB   H N N 423 
VAL   HG11 H N N 424 
VAL   HG12 H N N 425 
VAL   HG13 H N N 426 
VAL   HG21 H N N 427 
VAL   HG22 H N N 428 
VAL   HG23 H N N 429 
VAL   HXT  H N N 430 
# 
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 
A1H3X C20 C21  doub Y N 1   
A1H3X C20 C19  sing Y N 2   
A1H3X C21 C22  sing Y N 3   
A1H3X C19 C18  doub Y N 4   
A1H3X C22 C17  doub Y N 5   
A1H3X C18 C17  sing Y N 6   
A1H3X C17 C16  sing N N 7   
A1H3X C16 O15  sing N N 8   
A1H3X O15 C14  sing N N 9   
A1H3X C14 C23  doub Y N 10  
A1H3X C14 C13  sing Y N 11  
A1H3X C23 C24  sing Y N 12  
A1H3X C13 C12  doub Y N 13  
A1H3X O05 C04  doub N N 14  
A1H3X C04 C06  sing N N 15  
A1H3X C04 O03  sing N N 16  
A1H3X C06 C07  doub N E 17  
A1H3X C24 C11  doub Y N 18  
A1H3X C12 C11  sing Y N 19  
A1H3X C12 C08  sing Y N 20  
A1H3X C11 N10  sing Y N 21  
A1H3X O03 C02  sing N N 22  
A1H3X C07 C08  sing N N 23  
A1H3X C08 C09  doub Y N 24  
A1H3X N10 C09  sing Y N 25  
A1H3X C02 C01  sing N N 26  
A1H3X C13 H1   sing N N 27  
A1H3X C20 H2   sing N N 28  
A1H3X C21 H3   sing N N 29  
A1H3X C22 H4   sing N N 30  
A1H3X C24 H5   sing N N 31  
A1H3X C01 H6   sing N N 32  
A1H3X C01 H7   sing N N 33  
A1H3X C01 H8   sing N N 34  
A1H3X C02 H9   sing N N 35  
A1H3X C02 H10  sing N N 36  
A1H3X C06 H11  sing N N 37  
A1H3X C07 H12  sing N N 38  
A1H3X C09 H13  sing N N 39  
A1H3X C16 H14  sing N N 40  
A1H3X C16 H15  sing N N 41  
A1H3X C18 H16  sing N N 42  
A1H3X C19 H17  sing N N 43  
A1H3X C23 H18  sing N N 44  
A1H3X N10 H19  sing N N 45  
ALA   N   CA   sing N N 46  
ALA   N   H    sing N N 47  
ALA   N   H2   sing N N 48  
ALA   CA  C    sing N N 49  
ALA   CA  CB   sing N N 50  
ALA   CA  HA   sing N N 51  
ALA   C   O    doub N N 52  
ALA   C   OXT  sing N N 53  
ALA   CB  HB1  sing N N 54  
ALA   CB  HB2  sing N N 55  
ALA   CB  HB3  sing N N 56  
ALA   OXT HXT  sing N N 57  
ARG   N   CA   sing N N 58  
ARG   N   H    sing N N 59  
ARG   N   H2   sing N N 60  
ARG   CA  C    sing N N 61  
ARG   CA  CB   sing N N 62  
ARG   CA  HA   sing N N 63  
ARG   C   O    doub N N 64  
ARG   C   OXT  sing N N 65  
ARG   CB  CG   sing N N 66  
ARG   CB  HB2  sing N N 67  
ARG   CB  HB3  sing N N 68  
ARG   CG  CD   sing N N 69  
ARG   CG  HG2  sing N N 70  
ARG   CG  HG3  sing N N 71  
ARG   CD  NE   sing N N 72  
ARG   CD  HD2  sing N N 73  
ARG   CD  HD3  sing N N 74  
ARG   NE  CZ   sing N N 75  
ARG   NE  HE   sing N N 76  
ARG   CZ  NH1  sing N N 77  
ARG   CZ  NH2  doub N N 78  
ARG   NH1 HH11 sing N N 79  
ARG   NH1 HH12 sing N N 80  
ARG   NH2 HH21 sing N N 81  
ARG   NH2 HH22 sing N N 82  
ARG   OXT HXT  sing N N 83  
ASN   N   CA   sing N N 84  
ASN   N   H    sing N N 85  
ASN   N   H2   sing N N 86  
ASN   CA  C    sing N N 87  
ASN   CA  CB   sing N N 88  
ASN   CA  HA   sing N N 89  
ASN   C   O    doub N N 90  
ASN   C   OXT  sing N N 91  
ASN   CB  CG   sing N N 92  
ASN   CB  HB2  sing N N 93  
ASN   CB  HB3  sing N N 94  
ASN   CG  OD1  doub N N 95  
ASN   CG  ND2  sing N N 96  
ASN   ND2 HD21 sing N N 97  
ASN   ND2 HD22 sing N N 98  
ASN   OXT HXT  sing N N 99  
ASP   N   CA   sing N N 100 
ASP   N   H    sing N N 101 
ASP   N   H2   sing N N 102 
ASP   CA  C    sing N N 103 
ASP   CA  CB   sing N N 104 
ASP   CA  HA   sing N N 105 
ASP   C   O    doub N N 106 
ASP   C   OXT  sing N N 107 
ASP   CB  CG   sing N N 108 
ASP   CB  HB2  sing N N 109 
ASP   CB  HB3  sing N N 110 
ASP   CG  OD1  doub N N 111 
ASP   CG  OD2  sing N N 112 
ASP   OD2 HD2  sing N N 113 
ASP   OXT HXT  sing N N 114 
CYS   N   CA   sing N N 115 
CYS   N   H    sing N N 116 
CYS   N   H2   sing N N 117 
CYS   CA  C    sing N N 118 
CYS   CA  CB   sing N N 119 
CYS   CA  HA   sing N N 120 
CYS   C   O    doub N N 121 
CYS   C   OXT  sing N N 122 
CYS   CB  SG   sing N N 123 
CYS   CB  HB2  sing N N 124 
CYS   CB  HB3  sing N N 125 
CYS   SG  HG   sing N N 126 
CYS   OXT HXT  sing N N 127 
GLN   N   CA   sing N N 128 
GLN   N   H    sing N N 129 
GLN   N   H2   sing N N 130 
GLN   CA  C    sing N N 131 
GLN   CA  CB   sing N N 132 
GLN   CA  HA   sing N N 133 
GLN   C   O    doub N N 134 
GLN   C   OXT  sing N N 135 
GLN   CB  CG   sing N N 136 
GLN   CB  HB2  sing N N 137 
GLN   CB  HB3  sing N N 138 
GLN   CG  CD   sing N N 139 
GLN   CG  HG2  sing N N 140 
GLN   CG  HG3  sing N N 141 
GLN   CD  OE1  doub N N 142 
GLN   CD  NE2  sing N N 143 
GLN   NE2 HE21 sing N N 144 
GLN   NE2 HE22 sing N N 145 
GLN   OXT HXT  sing N N 146 
GLU   N   CA   sing N N 147 
GLU   N   H    sing N N 148 
GLU   N   H2   sing N N 149 
GLU   CA  C    sing N N 150 
GLU   CA  CB   sing N N 151 
GLU   CA  HA   sing N N 152 
GLU   C   O    doub N N 153 
GLU   C   OXT  sing N N 154 
GLU   CB  CG   sing N N 155 
GLU   CB  HB2  sing N N 156 
GLU   CB  HB3  sing N N 157 
GLU   CG  CD   sing N N 158 
GLU   CG  HG2  sing N N 159 
GLU   CG  HG3  sing N N 160 
GLU   CD  OE1  doub N N 161 
GLU   CD  OE2  sing N N 162 
GLU   OE2 HE2  sing N N 163 
GLU   OXT HXT  sing N N 164 
GLY   N   CA   sing N N 165 
GLY   N   H    sing N N 166 
GLY   N   H2   sing N N 167 
GLY   CA  C    sing N N 168 
GLY   CA  HA2  sing N N 169 
GLY   CA  HA3  sing N N 170 
GLY   C   O    doub N N 171 
GLY   C   OXT  sing N N 172 
GLY   OXT HXT  sing N N 173 
HIS   N   CA   sing N N 174 
HIS   N   H    sing N N 175 
HIS   N   H2   sing N N 176 
HIS   CA  C    sing N N 177 
HIS   CA  CB   sing N N 178 
HIS   CA  HA   sing N N 179 
HIS   C   O    doub N N 180 
HIS   C   OXT  sing N N 181 
HIS   CB  CG   sing N N 182 
HIS   CB  HB2  sing N N 183 
HIS   CB  HB3  sing N N 184 
HIS   CG  ND1  sing Y N 185 
HIS   CG  CD2  doub Y N 186 
HIS   ND1 CE1  doub Y N 187 
HIS   ND1 HD1  sing N N 188 
HIS   CD2 NE2  sing Y N 189 
HIS   CD2 HD2  sing N N 190 
HIS   CE1 NE2  sing Y N 191 
HIS   CE1 HE1  sing N N 192 
HIS   NE2 HE2  sing N N 193 
HIS   OXT HXT  sing N N 194 
ILE   N   CA   sing N N 195 
ILE   N   H    sing N N 196 
ILE   N   H2   sing N N 197 
ILE   CA  C    sing N N 198 
ILE   CA  CB   sing N N 199 
ILE   CA  HA   sing N N 200 
ILE   C   O    doub N N 201 
ILE   C   OXT  sing N N 202 
ILE   CB  CG1  sing N N 203 
ILE   CB  CG2  sing N N 204 
ILE   CB  HB   sing N N 205 
ILE   CG1 CD1  sing N N 206 
ILE   CG1 HG12 sing N N 207 
ILE   CG1 HG13 sing N N 208 
ILE   CG2 HG21 sing N N 209 
ILE   CG2 HG22 sing N N 210 
ILE   CG2 HG23 sing N N 211 
ILE   CD1 HD11 sing N N 212 
ILE   CD1 HD12 sing N N 213 
ILE   CD1 HD13 sing N N 214 
ILE   OXT HXT  sing N N 215 
LEU   N   CA   sing N N 216 
LEU   N   H    sing N N 217 
LEU   N   H2   sing N N 218 
LEU   CA  C    sing N N 219 
LEU   CA  CB   sing N N 220 
LEU   CA  HA   sing N N 221 
LEU   C   O    doub N N 222 
LEU   C   OXT  sing N N 223 
LEU   CB  CG   sing N N 224 
LEU   CB  HB2  sing N N 225 
LEU   CB  HB3  sing N N 226 
LEU   CG  CD1  sing N N 227 
LEU   CG  CD2  sing N N 228 
LEU   CG  HG   sing N N 229 
LEU   CD1 HD11 sing N N 230 
LEU   CD1 HD12 sing N N 231 
LEU   CD1 HD13 sing N N 232 
LEU   CD2 HD21 sing N N 233 
LEU   CD2 HD22 sing N N 234 
LEU   CD2 HD23 sing N N 235 
LEU   OXT HXT  sing N N 236 
LYS   N   CA   sing N N 237 
LYS   N   H    sing N N 238 
LYS   N   H2   sing N N 239 
LYS   CA  C    sing N N 240 
LYS   CA  CB   sing N N 241 
LYS   CA  HA   sing N N 242 
LYS   C   O    doub N N 243 
LYS   C   OXT  sing N N 244 
LYS   CB  CG   sing N N 245 
LYS   CB  HB2  sing N N 246 
LYS   CB  HB3  sing N N 247 
LYS   CG  CD   sing N N 248 
LYS   CG  HG2  sing N N 249 
LYS   CG  HG3  sing N N 250 
LYS   CD  CE   sing N N 251 
LYS   CD  HD2  sing N N 252 
LYS   CD  HD3  sing N N 253 
LYS   CE  NZ   sing N N 254 
LYS   CE  HE2  sing N N 255 
LYS   CE  HE3  sing N N 256 
LYS   NZ  HZ1  sing N N 257 
LYS   NZ  HZ2  sing N N 258 
LYS   NZ  HZ3  sing N N 259 
LYS   OXT HXT  sing N N 260 
MET   N   CA   sing N N 261 
MET   N   H    sing N N 262 
MET   N   H2   sing N N 263 
MET   CA  C    sing N N 264 
MET   CA  CB   sing N N 265 
MET   CA  HA   sing N N 266 
MET   C   O    doub N N 267 
MET   C   OXT  sing N N 268 
MET   CB  CG   sing N N 269 
MET   CB  HB2  sing N N 270 
MET   CB  HB3  sing N N 271 
MET   CG  SD   sing N N 272 
MET   CG  HG2  sing N N 273 
MET   CG  HG3  sing N N 274 
MET   SD  CE   sing N N 275 
MET   CE  HE1  sing N N 276 
MET   CE  HE2  sing N N 277 
MET   CE  HE3  sing N N 278 
MET   OXT HXT  sing N N 279 
PHE   N   CA   sing N N 280 
PHE   N   H    sing N N 281 
PHE   N   H2   sing N N 282 
PHE   CA  C    sing N N 283 
PHE   CA  CB   sing N N 284 
PHE   CA  HA   sing N N 285 
PHE   C   O    doub N N 286 
PHE   C   OXT  sing N N 287 
PHE   CB  CG   sing N N 288 
PHE   CB  HB2  sing N N 289 
PHE   CB  HB3  sing N N 290 
PHE   CG  CD1  doub Y N 291 
PHE   CG  CD2  sing Y N 292 
PHE   CD1 CE1  sing Y N 293 
PHE   CD1 HD1  sing N N 294 
PHE   CD2 CE2  doub Y N 295 
PHE   CD2 HD2  sing N N 296 
PHE   CE1 CZ   doub Y N 297 
PHE   CE1 HE1  sing N N 298 
PHE   CE2 CZ   sing Y N 299 
PHE   CE2 HE2  sing N N 300 
PHE   CZ  HZ   sing N N 301 
PHE   OXT HXT  sing N N 302 
PRO   N   CA   sing N N 303 
PRO   N   CD   sing N N 304 
PRO   N   H    sing N N 305 
PRO   CA  C    sing N N 306 
PRO   CA  CB   sing N N 307 
PRO   CA  HA   sing N N 308 
PRO   C   O    doub N N 309 
PRO   C   OXT  sing N N 310 
PRO   CB  CG   sing N N 311 
PRO   CB  HB2  sing N N 312 
PRO   CB  HB3  sing N N 313 
PRO   CG  CD   sing N N 314 
PRO   CG  HG2  sing N N 315 
PRO   CG  HG3  sing N N 316 
PRO   CD  HD2  sing N N 317 
PRO   CD  HD3  sing N N 318 
PRO   OXT HXT  sing N N 319 
SER   N   CA   sing N N 320 
SER   N   H    sing N N 321 
SER   N   H2   sing N N 322 
SER   CA  C    sing N N 323 
SER   CA  CB   sing N N 324 
SER   CA  HA   sing N N 325 
SER   C   O    doub N N 326 
SER   C   OXT  sing N N 327 
SER   CB  OG   sing N N 328 
SER   CB  HB2  sing N N 329 
SER   CB  HB3  sing N N 330 
SER   OG  HG   sing N N 331 
SER   OXT HXT  sing N N 332 
THR   N   CA   sing N N 333 
THR   N   H    sing N N 334 
THR   N   H2   sing N N 335 
THR   CA  C    sing N N 336 
THR   CA  CB   sing N N 337 
THR   CA  HA   sing N N 338 
THR   C   O    doub N N 339 
THR   C   OXT  sing N N 340 
THR   CB  OG1  sing N N 341 
THR   CB  CG2  sing N N 342 
THR   CB  HB   sing N N 343 
THR   OG1 HG1  sing N N 344 
THR   CG2 HG21 sing N N 345 
THR   CG2 HG22 sing N N 346 
THR   CG2 HG23 sing N N 347 
THR   OXT HXT  sing N N 348 
TRP   N   CA   sing N N 349 
TRP   N   H    sing N N 350 
TRP   N   H2   sing N N 351 
TRP   CA  C    sing N N 352 
TRP   CA  CB   sing N N 353 
TRP   CA  HA   sing N N 354 
TRP   C   O    doub N N 355 
TRP   C   OXT  sing N N 356 
TRP   CB  CG   sing N N 357 
TRP   CB  HB2  sing N N 358 
TRP   CB  HB3  sing N N 359 
TRP   CG  CD1  doub Y N 360 
TRP   CG  CD2  sing Y N 361 
TRP   CD1 NE1  sing Y N 362 
TRP   CD1 HD1  sing N N 363 
TRP   CD2 CE2  doub Y N 364 
TRP   CD2 CE3  sing Y N 365 
TRP   NE1 CE2  sing Y N 366 
TRP   NE1 HE1  sing N N 367 
TRP   CE2 CZ2  sing Y N 368 
TRP   CE3 CZ3  doub Y N 369 
TRP   CE3 HE3  sing N N 370 
TRP   CZ2 CH2  doub Y N 371 
TRP   CZ2 HZ2  sing N N 372 
TRP   CZ3 CH2  sing Y N 373 
TRP   CZ3 HZ3  sing N N 374 
TRP   CH2 HH2  sing N N 375 
TRP   OXT HXT  sing N N 376 
TYR   N   CA   sing N N 377 
TYR   N   H    sing N N 378 
TYR   N   H2   sing N N 379 
TYR   CA  C    sing N N 380 
TYR   CA  CB   sing N N 381 
TYR   CA  HA   sing N N 382 
TYR   C   O    doub N N 383 
TYR   C   OXT  sing N N 384 
TYR   CB  CG   sing N N 385 
TYR   CB  HB2  sing N N 386 
TYR   CB  HB3  sing N N 387 
TYR   CG  CD1  doub Y N 388 
TYR   CG  CD2  sing Y N 389 
TYR   CD1 CE1  sing Y N 390 
TYR   CD1 HD1  sing N N 391 
TYR   CD2 CE2  doub Y N 392 
TYR   CD2 HD2  sing N N 393 
TYR   CE1 CZ   doub Y N 394 
TYR   CE1 HE1  sing N N 395 
TYR   CE2 CZ   sing Y N 396 
TYR   CE2 HE2  sing N N 397 
TYR   CZ  OH   sing N N 398 
TYR   OH  HH   sing N N 399 
TYR   OXT HXT  sing N N 400 
VAL   N   CA   sing N N 401 
VAL   N   H    sing N N 402 
VAL   N   H2   sing N N 403 
VAL   CA  C    sing N N 404 
VAL   CA  CB   sing N N 405 
VAL   CA  HA   sing N N 406 
VAL   C   O    doub N N 407 
VAL   C   OXT  sing N N 408 
VAL   CB  CG1  sing N N 409 
VAL   CB  CG2  sing N N 410 
VAL   CB  HB   sing N N 411 
VAL   CG1 HG11 sing N N 412 
VAL   CG1 HG12 sing N N 413 
VAL   CG1 HG13 sing N N 414 
VAL   CG2 HG21 sing N N 415 
VAL   CG2 HG22 sing N N 416 
VAL   CG2 HG23 sing N N 417 
VAL   OXT HXT  sing N N 418 
# 
_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                    8RXQ 
_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]   0.008121 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004213 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016311 
_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]   0.014049 
_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   . TRP   A 1 3   ? -12.507 -19.217 33.661 1.00 107.45 ? 218 TRP   B N   1 
ATOM   2    C CA  . TRP   A 1 3   ? -13.854 -18.863 34.101 1.00 107.02 ? 218 TRP   B CA  1 
ATOM   3    C C   . TRP   A 1 3   ? -14.786 -18.675 32.901 1.00 105.88 ? 218 TRP   B C   1 
ATOM   4    O O   . TRP   A 1 3   ? -15.418 -17.625 32.743 1.00 101.47 ? 218 TRP   B O   1 
ATOM   5    C CB  . TRP   A 1 3   ? -13.812 -17.597 34.951 1.00 104.56 ? 218 TRP   B CB  1 
ATOM   6    C CG  . TRP   A 1 3   ? -13.509 -17.861 36.395 1.00 104.65 ? 218 TRP   B CG  1 
ATOM   7    C CD1 . TRP   A 1 3   ? -14.356 -17.705 37.455 1.00 104.71 ? 218 TRP   B CD1 1 
ATOM   8    C CD2 . TRP   A 1 3   ? -12.263 -18.325 36.939 1.00 106.33 ? 218 TRP   B CD2 1 
ATOM   9    N NE1 . TRP   A 1 3   ? -13.716 -18.047 38.625 1.00 106.41 ? 218 TRP   B NE1 1 
ATOM   10   C CE2 . TRP   A 1 3   ? -12.430 -18.425 38.335 1.00 108.09 ? 218 TRP   B CE2 1 
ATOM   11   C CE3 . TRP   A 1 3   ? -11.023 -18.664 36.381 1.00 107.71 ? 218 TRP   B CE3 1 
ATOM   12   C CZ2 . TRP   A 1 3   ? -11.400 -18.848 39.183 1.00 111.17 ? 218 TRP   B CZ2 1 
ATOM   13   C CZ3 . TRP   A 1 3   ? -9.998  -19.079 37.227 1.00 110.82 ? 218 TRP   B CZ3 1 
ATOM   14   C CH2 . TRP   A 1 3   ? -10.196 -19.171 38.614 1.00 112.51 ? 218 TRP   B CH2 1 
ATOM   15   N N   . GLN   A 1 4   ? -14.866 -19.706 32.061 1.00 106.99 ? 219 GLN   B N   1 
ATOM   16   C CA  . GLN   A 1 4   ? -15.599 -19.625 30.802 1.00 101.92 ? 219 GLN   B CA  1 
ATOM   17   C C   . GLN   A 1 4   ? -17.082 -19.932 31.001 1.00 98.47  ? 219 GLN   B C   1 
ATOM   18   O O   . GLN   A 1 4   ? -17.470 -20.730 31.856 1.00 98.45  ? 219 GLN   B O   1 
ATOM   19   C CB  . GLN   A 1 4   ? -14.998 -20.582 29.770 1.00 96.69  ? 219 GLN   B CB  1 
ATOM   20   C CG  . GLN   A 1 4   ? -13.687 -20.093 29.162 1.00 96.55  ? 219 GLN   B CG  1 
ATOM   21   C CD  . GLN   A 1 4   ? -12.911 -21.200 28.467 1.00 97.11  ? 219 GLN   B CD  1 
ATOM   22   O OE1 . GLN   A 1 4   ? -13.451 -22.278 28.193 1.00 97.97  ? 219 GLN   B OE1 1 
ATOM   23   N NE2 . GLN   A 1 4   ? -11.630 -20.949 28.203 1.00 95.56  ? 219 GLN   B NE2 1 
ATOM   24   N N   . ALA   A 1 5   ? -17.913 -19.290 30.187 1.00 99.27  ? 220 ALA   B N   1 
ATOM   25   C CA  . ALA   A 1 5   ? -19.360 -19.384 30.327 1.00 98.14  ? 220 ALA   B CA  1 
ATOM   26   C C   . ALA   A 1 5   ? -19.891 -20.694 29.753 1.00 97.55  ? 220 ALA   B C   1 
ATOM   27   O O   . ALA   A 1 5   ? -19.348 -21.252 28.794 1.00 96.21  ? 220 ALA   B O   1 
ATOM   28   C CB  . ALA   A 1 5   ? -20.046 -18.204 29.633 1.00 91.84  ? 220 ALA   B CB  1 
ATOM   29   N N   . ARG   A 1 6   ? -20.999 -21.139 30.339 1.00 98.94  ? 221 ARG   B N   1 
ATOM   30   C CA  . ARG   A 1 6   ? -21.703 -22.342 29.939 1.00 97.67  ? 221 ARG   B CA  1 
ATOM   31   C C   . ARG   A 1 6   ? -23.066 -22.030 29.363 1.00 93.78  ? 221 ARG   B C   1 
ATOM   32   O O   . ARG   A 1 6   ? -23.612 -22.816 28.628 1.00 94.69  ? 221 ARG   B O   1 
ATOM   33   C CB  . ARG   A 1 6   ? -21.896 -23.277 31.127 1.00 101.67 ? 221 ARG   B CB  1 
ATOM   34   C CG  . ARG   A 1 6   ? -20.688 -23.419 32.025 1.00 110.15 ? 221 ARG   B CG  1 
ATOM   35   C CD  . ARG   A 1 6   ? -19.985 -24.750 31.829 1.00 114.42 ? 221 ARG   B CD  1 
ATOM   36   N NE  . ARG   A 1 6   ? -19.195 -25.090 33.001 1.00 119.69 ? 221 ARG   B NE  1 
ATOM   37   C CZ  . ARG   A 1 6   ? -17.933 -24.733 33.165 1.00 116.11 ? 221 ARG   B CZ  1 
ATOM   38   N NH1 . ARG   A 1 6   ? -17.317 -24.046 32.220 1.00 112.21 ? 221 ARG   B NH1 1 
ATOM   39   N NH2 . ARG   A 1 6   ? -17.290 -25.071 34.268 1.00 114.73 ? 221 ARG   B NH2 1 
ATOM   40   N N   . GLY   A 1 7   ? -23.626 -20.889 29.716 1.00 90.93  ? 222 GLY   B N   1 
ATOM   41   C CA  . GLY   A 1 7   ? -24.877 -20.436 29.151 1.00 82.11  ? 222 GLY   B CA  1 
ATOM   42   C C   . GLY   A 1 7   ? -24.733 -19.029 28.600 1.00 74.18  ? 222 GLY   B C   1 
ATOM   43   O O   . GLY   A 1 7   ? -23.665 -18.420 28.664 1.00 73.03  ? 222 GLY   B O   1 
ATOM   44   N N   . LEU   A 1 8   ? -25.832 -18.537 28.049 1.00 66.09  ? 223 LEU   B N   1 
ATOM   45   C CA  . LEU   A 1 8   ? -25.879 -17.167 27.552 1.00 64.96  ? 223 LEU   B CA  1 
ATOM   46   C C   . LEU   A 1 8   ? -26.120 -16.240 28.743 1.00 65.79  ? 223 LEU   B C   1 
ATOM   47   O O   . LEU   A 1 8   ? -27.257 -15.924 29.099 1.00 61.04  ? 223 LEU   B O   1 
ATOM   48   C CB  . LEU   A 1 8   ? -26.955 -17.033 26.483 1.00 63.44  ? 223 LEU   B CB  1 
ATOM   49   C CG  . LEU   A 1 8   ? -26.798 -15.983 25.381 1.00 56.15  ? 223 LEU   B CG  1 
ATOM   50   C CD1 . LEU   A 1 8   ? -28.046 -16.019 24.545 1.00 54.16  ? 223 LEU   B CD1 1 
ATOM   51   C CD2 . LEU   A 1 8   ? -26.578 -14.591 25.963 1.00 56.33  ? 223 LEU   B CD2 1 
ATOM   52   N N   . GLY   A 1 9   ? -25.033 -15.803 29.368 1.00 67.11  ? 224 GLY   B N   1 
ATOM   53   C CA  . GLY   A 1 9   ? -25.125 -14.926 30.518 1.00 69.08  ? 224 GLY   B CA  1 
ATOM   54   C C   . GLY   A 1 9   ? -23.771 -14.756 31.167 1.00 71.16  ? 224 GLY   B C   1 
ATOM   55   O O   . GLY   A 1 9   ? -22.804 -15.448 30.842 1.00 70.27  ? 224 GLY   B O   1 
ATOM   56   N N   . THR   A 1 10  ? -23.711 -13.793 32.084 1.00 70.94  ? 225 THR   B N   1 
ATOM   57   C CA  . THR   A 1 10  ? -22.543 -13.576 32.928 1.00 70.97  ? 225 THR   B CA  1 
ATOM   58   C C   . THR   A 1 10  ? -22.952 -13.734 34.393 1.00 78.05  ? 225 THR   B C   1 
ATOM   59   O O   . THR   A 1 10  ? -24.095 -14.077 34.711 1.00 79.20  ? 225 THR   B O   1 
ATOM   60   C CB  . THR   A 1 10  ? -21.924 -12.196 32.693 1.00 66.55  ? 225 THR   B CB  1 
ATOM   61   O OG1 . THR   A 1 10  ? -22.809 -11.186 33.168 1.00 65.81  ? 225 THR   B OG1 1 
ATOM   62   C CG2 . THR   A 1 10  ? -21.725 -11.954 31.197 1.00 66.35  ? 225 THR   B CG2 1 
ATOM   63   N N   . ALA   A 1 11  ? -21.996 -13.487 35.295 1.00 79.13  ? 226 ALA   B N   1 
ATOM   64   C CA  . ALA   A 1 11  ? -22.285 -13.551 36.726 1.00 78.46  ? 226 ALA   B CA  1 
ATOM   65   C C   . ALA   A 1 11  ? -23.259 -12.461 37.146 1.00 76.62  ? 226 ALA   B C   1 
ATOM   66   O O   . ALA   A 1 11  ? -23.960 -12.602 38.161 1.00 78.11  ? 226 ALA   B O   1 
ATOM   67   C CB  . ALA   A 1 11  ? -20.991 -13.433 37.532 1.00 78.93  ? 226 ALA   B CB  1 
ATOM   68   N N   . ARG   A 1 12  ? -23.306 -11.373 36.389 1.00 66.40  ? 227 ARG   B N   1 
ATOM   69   C CA  . ARG   A 1 12  ? -24.130 -10.231 36.729 1.00 67.26  ? 227 ARG   B CA  1 
ATOM   70   C C   . ARG   A 1 12  ? -25.523 -10.342 36.137 1.00 68.75  ? 227 ARG   B C   1 
ATOM   71   O O   . ARG   A 1 12  ? -26.499 -9.911  36.759 1.00 75.50  ? 227 ARG   B O   1 
ATOM   72   C CB  . ARG   A 1 12  ? -23.448 -8.934  36.266 1.00 68.73  ? 227 ARG   B CB  1 
ATOM   73   C CG  . ARG   A 1 12  ? -22.025 -8.748  36.821 1.00 70.01  ? 227 ARG   B CG  1 
ATOM   74   C CD  . ARG   A 1 12  ? -21.508 -7.332  36.647 1.00 64.90  ? 227 ARG   B CD  1 
ATOM   75   N NE  . ARG   A 1 12  ? -22.273 -6.395  37.455 1.00 73.16  ? 227 ARG   B NE  1 
ATOM   76   C CZ  . ARG   A 1 12  ? -22.401 -5.104  37.186 1.00 76.99  ? 227 ARG   B CZ  1 
ATOM   77   N NH1 . ARG   A 1 12  ? -21.800 -4.552  36.142 1.00 75.80  ? 227 ARG   B NH1 1 
ATOM   78   N NH2 . ARG   A 1 12  ? -23.164 -4.350  37.978 1.00 75.45  ? 227 ARG   B NH2 1 
ATOM   79   N N   . LEU   A 1 13  ? -25.647 -10.927 34.959 1.00 66.39  ? 228 LEU   B N   1 
ATOM   80   C CA  . LEU   A 1 13  ? -26.927 -10.913 34.279 1.00 67.91  ? 228 LEU   B CA  1 
ATOM   81   C C   . LEU   A 1 13  ? -27.018 -12.161 33.430 1.00 70.62  ? 228 LEU   B C   1 
ATOM   82   O O   . LEU   A 1 13  ? -26.087 -12.468 32.680 1.00 73.29  ? 228 LEU   B O   1 
ATOM   83   C CB  . LEU   A 1 13  ? -27.082 -9.661  33.421 1.00 63.30  ? 228 LEU   B CB  1 
ATOM   84   C CG  . LEU   A 1 13  ? -28.465 -9.497  32.815 1.00 64.13  ? 228 LEU   B CG  1 
ATOM   85   C CD1 . LEU   A 1 13  ? -29.491 -9.462  33.927 1.00 62.42  ? 228 LEU   B CD1 1 
ATOM   86   C CD2 . LEU   A 1 13  ? -28.542 -8.248  31.911 1.00 56.90  ? 228 LEU   B CD2 1 
ATOM   87   N N   . GLN   A 1 14  ? -28.125 -12.876 33.557 1.00 74.55  ? 229 GLN   B N   1 
ATOM   88   C CA  . GLN   A 1 14  ? -28.336 -14.114 32.832 1.00 76.38  ? 229 GLN   B CA  1 
ATOM   89   C C   . GLN   A 1 14  ? -29.633 -14.031 32.050 1.00 71.74  ? 229 GLN   B C   1 
ATOM   90   O O   . GLN   A 1 14  ? -30.613 -13.428 32.504 1.00 69.13  ? 229 GLN   B O   1 
ATOM   91   C CB  . GLN   A 1 14  ? -28.365 -15.321 33.777 1.00 79.39  ? 229 GLN   B CB  1 
ATOM   92   C CG  . GLN   A 1 14  ? -27.113 -15.467 34.619 1.00 83.26  ? 229 GLN   B CG  1 
ATOM   93   C CD  . GLN   A 1 14  ? -27.218 -14.743 35.953 1.00 85.00  ? 229 GLN   B CD  1 
ATOM   94   O OE1 . GLN   A 1 14  ? -28.270 -14.199 36.301 1.00 83.44  ? 229 GLN   B OE1 1 
ATOM   95   N NE2 . GLN   A 1 14  ? -26.127 -14.738 36.711 1.00 86.29  ? 229 GLN   B NE2 1 
ATOM   96   N N   . LEU   A 1 15  ? -29.617 -14.614 30.854 1.00 64.88  ? 230 LEU   B N   1 
ATOM   97   C CA  . LEU   A 1 15  ? -30.842 -14.795 30.100 1.00 62.01  ? 230 LEU   B CA  1 
ATOM   98   C C   . LEU   A 1 15  ? -31.599 -15.973 30.685 1.00 64.64  ? 230 LEU   B C   1 
ATOM   99   O O   . LEU   A 1 15  ? -31.016 -17.033 30.932 1.00 66.60  ? 230 LEU   B O   1 
ATOM   100  C CB  . LEU   A 1 15  ? -30.541 -15.040 28.629 1.00 60.12  ? 230 LEU   B CB  1 
ATOM   101  C CG  . LEU   A 1 15  ? -31.760 -15.101 27.715 1.00 58.61  ? 230 LEU   B CG  1 
ATOM   102  C CD1 . LEU   A 1 15  ? -32.358 -13.728 27.524 1.00 52.94  ? 230 LEU   B CD1 1 
ATOM   103  C CD2 . LEU   A 1 15  ? -31.379 -15.728 26.385 1.00 60.17  ? 230 LEU   B CD2 1 
ATOM   104  N N   . VAL   A 1 16  ? -32.889 -15.789 30.930 1.00 60.51  ? 231 VAL   B N   1 
ATOM   105  C CA  . VAL   A 1 16  ? -33.738 -16.875 31.389 1.00 66.09  ? 231 VAL   B CA  1 
ATOM   106  C C   . VAL   A 1 16  ? -34.619 -17.372 30.276 1.00 66.59  ? 231 VAL   B C   1 
ATOM   107  O O   . VAL   A 1 16  ? -34.709 -18.575 30.030 1.00 71.74  ? 231 VAL   B O   1 
ATOM   108  C CB  . VAL   A 1 16  ? -34.578 -16.443 32.611 1.00 64.04  ? 231 VAL   B CB  1 
ATOM   109  C CG1 . VAL   A 1 16  ? -35.468 -17.585 33.076 1.00 63.95  ? 231 VAL   B CG1 1 
ATOM   110  C CG2 . VAL   A 1 16  ? -33.659 -16.043 33.708 1.00 64.30  ? 231 VAL   B CG2 1 
ATOM   111  N N   . GLU   A 1 17  ? -35.289 -16.459 29.598 1.00 65.44  ? 232 GLU   B N   1 
ATOM   112  C CA  . GLU   A 1 17  ? -36.061 -16.898 28.461 1.00 69.28  ? 232 GLU   B CA  1 
ATOM   113  C C   . GLU   A 1 17  ? -36.126 -15.767 27.444 1.00 67.85  ? 232 GLU   B C   1 
ATOM   114  O O   . GLU   A 1 17  ? -36.115 -14.580 27.791 1.00 66.77  ? 232 GLU   B O   1 
ATOM   115  C CB  . GLU   A 1 17  ? -37.462 -17.386 28.867 1.00 71.26  ? 232 GLU   B CB  1 
ATOM   116  C CG  . GLU   A 1 17  ? -37.922 -18.498 27.933 1.00 74.63  ? 232 GLU   B CG  1 
ATOM   117  C CD  . GLU   A 1 17  ? -39.418 -18.716 27.865 1.00 77.71  ? 232 GLU   B CD  1 
ATOM   118  O OE1 . GLU   A 1 17  ? -39.889 -19.709 28.443 1.00 79.58  ? 232 GLU   B OE1 1 
ATOM   119  O OE2 . GLU   A 1 17  ? -40.114 -17.921 27.192 1.00 83.15  ? 232 GLU   B OE2 1 
ATOM   120  N N   . PHE   A 1 18  ? -36.128 -16.163 26.180 1.00 62.05  ? 233 PHE   B N   1 
ATOM   121  C CA  . PHE   A 1 18  ? -36.384 -15.264 25.080 1.00 59.30  ? 233 PHE   B CA  1 
ATOM   122  C C   . PHE   A 1 18  ? -37.243 -16.005 24.068 1.00 60.82  ? 233 PHE   B C   1 
ATOM   123  O O   . PHE   A 1 18  ? -37.113 -17.220 23.890 1.00 62.36  ? 233 PHE   B O   1 
ATOM   124  C CB  . PHE   A 1 18  ? -35.085 -14.767 24.431 1.00 58.53  ? 233 PHE   B CB  1 
ATOM   125  C CG  . PHE   A 1 18  ? -35.292 -14.177 23.074 1.00 60.59  ? 233 PHE   B CG  1 
ATOM   126  C CD1 . PHE   A 1 18  ? -35.870 -12.931 22.931 1.00 60.09  ? 233 PHE   B CD1 1 
ATOM   127  C CD2 . PHE   A 1 18  ? -34.958 -14.890 21.931 1.00 62.00  ? 233 PHE   B CD2 1 
ATOM   128  C CE1 . PHE   A 1 18  ? -36.073 -12.394 21.675 1.00 61.31  ? 233 PHE   B CE1 1 
ATOM   129  C CE2 . PHE   A 1 18  ? -35.170 -14.354 20.677 1.00 59.10  ? 233 PHE   B CE2 1 
ATOM   130  C CZ  . PHE   A 1 18  ? -35.730 -13.108 20.554 1.00 58.53  ? 233 PHE   B CZ  1 
ATOM   131  N N   . SER   A 1 19  ? -38.132 -15.272 23.410 1.00 58.34  ? 234 SER   B N   1 
ATOM   132  C CA  . SER   A 1 19  ? -38.811 -15.853 22.266 1.00 58.94  ? 234 SER   B CA  1 
ATOM   133  C C   . SER   A 1 19  ? -39.410 -14.742 21.418 1.00 59.25  ? 234 SER   B C   1 
ATOM   134  O O   . SER   A 1 19  ? -39.744 -13.659 21.916 1.00 57.35  ? 234 SER   B O   1 
ATOM   135  C CB  . SER   A 1 19  ? -39.898 -16.838 22.693 1.00 57.58  ? 234 SER   B CB  1 
ATOM   136  O OG  . SER   A 1 19  ? -40.826 -16.166 23.504 1.00 60.66  ? 234 SER   B OG  1 
ATOM   137  N N   . ALA   A 1 20  ? -39.519 -15.028 20.124 1.00 55.55  ? 235 ALA   B N   1 
ATOM   138  C CA  . ALA   A 1 20  ? -40.332 -14.259 19.200 1.00 53.65  ? 235 ALA   B CA  1 
ATOM   139  C C   . ALA   A 1 20  ? -41.445 -15.186 18.756 1.00 47.66  ? 235 ALA   B C   1 
ATOM   140  O O   . ALA   A 1 20  ? -41.200 -16.366 18.526 1.00 52.62  ? 235 ALA   B O   1 
ATOM   141  C CB  . ALA   A 1 20  ? -39.503 -13.772 18.007 1.00 56.54  ? 235 ALA   B CB  1 
ATOM   142  N N   . PHE   A 1 21  ? -42.667 -14.683 18.676 1.00 46.15  ? 236 PHE   B N   1 
ATOM   143  C CA  . PHE   A 1 21  ? -43.797 -15.592 18.499 1.00 50.40  ? 236 PHE   B CA  1 
ATOM   144  C C   . PHE   A 1 21  ? -44.908 -14.850 17.789 1.00 51.44  ? 236 PHE   B C   1 
ATOM   145  O O   . PHE   A 1 21  ? -44.849 -13.629 17.617 1.00 52.61  ? 236 PHE   B O   1 
ATOM   146  C CB  . PHE   A 1 21  ? -44.296 -16.177 19.847 1.00 60.12  ? 236 PHE   B CB  1 
ATOM   147  C CG  . PHE   A 1 21  ? -44.790 -15.141 20.853 1.00 51.50  ? 236 PHE   B CG  1 
ATOM   148  C CD1 . PHE   A 1 21  ? -43.931 -14.572 21.773 1.00 53.77  ? 236 PHE   B CD1 1 
ATOM   149  C CD2 . PHE   A 1 21  ? -46.107 -14.751 20.870 1.00 54.64  ? 236 PHE   B CD2 1 
ATOM   150  C CE1 . PHE   A 1 21  ? -44.388 -13.614 22.709 1.00 58.32  ? 236 PHE   B CE1 1 
ATOM   151  C CE2 . PHE   A 1 21  ? -46.567 -13.799 21.794 1.00 60.96  ? 236 PHE   B CE2 1 
ATOM   152  C CZ  . PHE   A 1 21  ? -45.701 -13.230 22.709 1.00 57.41  ? 236 PHE   B CZ  1 
ATOM   153  N N   . VAL   A 1 22  ? -45.937 -15.598 17.399 1.00 53.83  ? 237 VAL   B N   1 
ATOM   154  C CA  . VAL   A 1 22  ? -47.157 -15.008 16.842 1.00 62.83  ? 237 VAL   B CA  1 
ATOM   155  C C   . VAL   A 1 22  ? -48.358 -15.795 17.370 1.00 63.57  ? 237 VAL   B C   1 
ATOM   156  O O   . VAL   A 1 22  ? -48.306 -17.022 17.510 1.00 62.10  ? 237 VAL   B O   1 
ATOM   157  C CB  . VAL   A 1 22  ? -47.142 -14.983 15.287 1.00 54.24  ? 237 VAL   B CB  1 
ATOM   158  C CG1 . VAL   A 1 22  ? -46.868 -16.367 14.744 1.00 62.55  ? 237 VAL   B CG1 1 
ATOM   159  C CG2 . VAL   A 1 22  ? -48.421 -14.412 14.700 1.00 50.41  ? 237 VAL   B CG2 1 
ATOM   160  N N   . GLU   A 1 23  ? -49.440 -15.088 17.671 1.00 62.41  ? 238 GLU   B N   1 
ATOM   161  C CA  . GLU   A 1 23  ? -50.663 -15.739 18.089 1.00 70.13  ? 238 GLU   B CA  1 
ATOM   162  C C   . GLU   A 1 23  ? -51.747 -15.456 17.056 1.00 72.37  ? 238 GLU   B C   1 
ATOM   163  O O   . GLU   A 1 23  ? -51.971 -14.287 16.714 1.00 75.01  ? 238 GLU   B O   1 
ATOM   164  C CB  . GLU   A 1 23  ? -51.110 -15.240 19.521 1.00 67.31  ? 238 GLU   B CB  1 
ATOM   165  C CG  . GLU   A 1 23  ? -50.033 -15.442 20.614 1.00 63.98  ? 238 GLU   B CG  1 
ATOM   166  C CD  . GLU   A 1 23  ? -50.228 -14.591 21.890 1.00 69.02  ? 238 GLU   B CD  1 
ATOM   167  O OE1 . GLU   A 1 23  ? -50.886 -13.519 21.835 1.00 68.37  ? 238 GLU   B OE1 1 
ATOM   168  O OE2 . GLU   A 1 23  ? -49.713 -15.001 22.965 1.00 67.03  ? 238 GLU   B OE2 1 
ATOM   169  N N   . PRO   A 1 24  ? -52.426 -16.474 16.531 1.00 75.95  ? 239 PRO   B N   1 
ATOM   170  C CA  . PRO   A 1 24  ? -53.454 -16.240 15.502 1.00 82.47  ? 239 PRO   B CA  1 
ATOM   171  C C   . PRO   A 1 24  ? -54.656 -15.542 16.100 1.00 88.80  ? 239 PRO   B C   1 
ATOM   172  O O   . PRO   A 1 24  ? -54.835 -15.539 17.327 1.00 91.29  ? 239 PRO   B O   1 
ATOM   173  C CB  . PRO   A 1 24  ? -53.829 -17.650 15.021 1.00 84.01  ? 239 PRO   B CB  1 
ATOM   174  C CG  . PRO   A 1 24  ? -53.260 -18.584 16.007 1.00 83.69  ? 239 PRO   B CG  1 
ATOM   175  C CD  . PRO   A 1 24  ? -52.386 -17.868 16.986 1.00 78.20  ? 239 PRO   B CD  1 
ATOM   176  N N   . PRO   A 1 25  ? -55.491 -14.923 15.270 1.00 90.29  ? 240 PRO   B N   1 
ATOM   177  C CA  . PRO   A 1 25  ? -56.739 -14.355 15.802 1.00 92.19  ? 240 PRO   B CA  1 
ATOM   178  C C   . PRO   A 1 25  ? -57.565 -15.370 16.567 1.00 95.94  ? 240 PRO   B C   1 
ATOM   179  O O   . PRO   A 1 25  ? -58.097 -15.042 17.638 1.00 97.77  ? 240 PRO   B O   1 
ATOM   180  C CB  . PRO   A 1 25  ? -57.455 -13.856 14.544 1.00 93.96  ? 240 PRO   B CB  1 
ATOM   181  C CG  . PRO   A 1 25  ? -56.340 -13.542 13.605 1.00 95.29  ? 240 PRO   B CG  1 
ATOM   182  C CD  . PRO   A 1 25  ? -55.268 -14.566 13.862 1.00 90.54  ? 240 PRO   B CD  1 
ATOM   183  N N   . ASP   A 1 26  ? -57.644 -16.612 16.075 1.00 98.61  ? 241 ASP   B N   1 
ATOM   184  C CA  . ASP   A 1 26  ? -58.432 -17.642 16.742 1.00 102.88 ? 241 ASP   B CA  1 
ATOM   185  C C   . ASP   A 1 26  ? -57.833 -18.075 18.095 1.00 102.14 ? 241 ASP   B C   1 
ATOM   186  O O   . ASP   A 1 26  ? -58.363 -19.005 18.725 1.00 103.10 ? 241 ASP   B O   1 
ATOM   187  C CB  . ASP   A 1 26  ? -58.599 -18.842 15.799 1.00 102.85 ? 241 ASP   B CB  1 
ATOM   188  C CG  . ASP   A 1 26  ? -57.273 -19.413 15.337 1.00 102.82 ? 241 ASP   B CG  1 
ATOM   189  O OD1 . ASP   A 1 26  ? -56.677 -20.247 16.070 1.00 100.70 ? 241 ASP   B OD1 1 
ATOM   190  O OD2 . ASP   A 1 26  ? -56.832 -19.025 14.227 1.00 102.30 ? 241 ASP   B OD2 1 
ATOM   191  N N   . ALA   A 1 27  ? -56.763 -17.413 18.555 1.00 96.02  ? 242 ALA   B N   1 
ATOM   192  C CA  . ALA   A 1 27  ? -56.214 -17.723 19.866 1.00 94.28  ? 242 ALA   B CA  1 
ATOM   193  C C   . ALA   A 1 27  ? -57.148 -17.283 20.995 1.00 98.82  ? 242 ALA   B C   1 
ATOM   194  O O   . ALA   A 1 27  ? -57.179 -17.921 22.054 1.00 95.75  ? 242 ALA   B O   1 
ATOM   195  C CB  . ALA   A 1 27  ? -54.837 -17.085 20.017 1.00 84.59  ? 242 ALA   B CB  1 
ATOM   196  N N   . VAL   A 1 28  ? -57.939 -16.227 20.788 1.00 102.99 ? 243 VAL   B N   1 
ATOM   197  C CA  . VAL   A 1 28  ? -58.892 -15.805 21.811 1.00 96.95  ? 243 VAL   B CA  1 
ATOM   198  C C   . VAL   A 1 28  ? -59.984 -16.837 22.042 1.00 108.29 ? 243 VAL   B C   1 
ATOM   199  O O   . VAL   A 1 28  ? -60.720 -16.750 23.041 1.00 107.97 ? 243 VAL   B O   1 
ATOM   200  C CB  . VAL   A 1 28  ? -59.534 -14.445 21.464 1.00 89.47  ? 243 VAL   B CB  1 
ATOM   201  C CG1 . VAL   A 1 28  ? -58.487 -13.470 20.951 1.00 93.14  ? 243 VAL   B CG1 1 
ATOM   202  C CG2 . VAL   A 1 28  ? -60.630 -14.621 20.443 1.00 93.60  ? 243 VAL   B CG2 1 
ATOM   203  N N   . ASP   A 1 29  ? -60.110 -17.811 21.142 1.00 121.49 ? 244 ASP   B N   1 
ATOM   204  C CA  . ASP   A 1 29  ? -60.991 -18.948 21.363 1.00 125.35 ? 244 ASP   B CA  1 
ATOM   205  C C   . ASP   A 1 29  ? -60.175 -20.127 21.878 1.00 123.61 ? 244 ASP   B C   1 
ATOM   206  O O   . ASP   A 1 29  ? -60.230 -20.445 23.070 1.00 124.38 ? 244 ASP   B O   1 
ATOM   207  C CB  . ASP   A 1 29  ? -61.750 -19.312 20.087 1.00 125.30 ? 244 ASP   B CB  1 
ATOM   208  C CG  . ASP   A 1 29  ? -62.840 -18.311 19.760 1.00 131.00 ? 244 ASP   B CG  1 
ATOM   209  O OD1 . ASP   A 1 29  ? -62.560 -17.094 19.813 1.00 129.66 ? 244 ASP   B OD1 1 
ATOM   210  O OD2 . ASP   A 1 29  ? -63.980 -18.740 19.467 1.00 138.72 ? 244 ASP   B OD2 1 
ATOM   211  N N   . SER   A 1 30  ? -59.410 -20.780 21.013 1.00 107.99 ? 245 SER   B N   1 
ATOM   212  C CA  . SER   A 1 30  ? -58.517 -21.846 21.446 1.00 102.01 ? 245 SER   B CA  1 
ATOM   213  C C   . SER   A 1 30  ? -57.103 -21.307 21.297 1.00 99.07  ? 245 SER   B C   1 
ATOM   214  O O   . SER   A 1 30  ? -56.635 -21.087 20.174 1.00 96.57  ? 245 SER   B O   1 
ATOM   215  C CB  . SER   A 1 30  ? -58.739 -23.117 20.631 1.00 105.50 ? 245 SER   B CB  1 
ATOM   216  O OG  . SER   A 1 30  ? -58.510 -24.277 21.416 1.00 104.99 ? 245 SER   B OG  1 
ATOM   217  N N   . TYR   A 1 31  ? -56.441 -21.058 22.426 1.00 96.43  ? 246 TYR   B N   1 
ATOM   218  C CA  . TYR   A 1 31  ? -55.134 -20.410 22.392 1.00 87.78  ? 246 TYR   B CA  1 
ATOM   219  C C   . TYR   A 1 31  ? -54.118 -21.301 21.702 1.00 82.60  ? 246 TYR   B C   1 
ATOM   220  O O   . TYR   A 1 31  ? -54.253 -22.522 21.657 1.00 88.64  ? 246 TYR   B O   1 
ATOM   221  C CB  . TYR   A 1 31  ? -54.640 -20.071 23.807 1.00 83.25  ? 246 TYR   B CB  1 
ATOM   222  C CG  . TYR   A 1 31  ? -53.254 -19.446 23.879 1.00 73.52  ? 246 TYR   B CG  1 
ATOM   223  C CD1 . TYR   A 1 31  ? -53.033 -18.145 23.443 1.00 75.14  ? 246 TYR   B CD1 1 
ATOM   224  C CD2 . TYR   A 1 31  ? -52.174 -20.157 24.384 1.00 72.38  ? 246 TYR   B CD2 1 
ATOM   225  C CE1 . TYR   A 1 31  ? -51.758 -17.563 23.490 1.00 70.98  ? 246 TYR   B CE1 1 
ATOM   226  C CE2 . TYR   A 1 31  ? -50.911 -19.590 24.460 1.00 70.36  ? 246 TYR   B CE2 1 
ATOM   227  C CZ  . TYR   A 1 31  ? -50.700 -18.286 24.005 1.00 71.58  ? 246 TYR   B CZ  1 
ATOM   228  O OH  . TYR   A 1 31  ? -49.436 -17.705 24.066 1.00 68.61  ? 246 TYR   B OH  1 
ATOM   229  N N   . GLN   A 1 32  ? -53.108 -20.664 21.137 1.00 79.67  ? 247 GLN   B N   1 
ATOM   230  C CA  . GLN   A 1 32  ? -51.929 -21.316 20.602 1.00 77.87  ? 247 GLN   B CA  1 
ATOM   231  C C   . GLN   A 1 32  ? -50.990 -20.206 20.197 1.00 72.08  ? 247 GLN   B C   1 
ATOM   232  O O   . GLN   A 1 32  ? -51.444 -19.139 19.786 1.00 73.10  ? 247 GLN   B O   1 
ATOM   233  C CB  . GLN   A 1 32  ? -52.254 -22.210 19.403 1.00 81.70  ? 247 GLN   B CB  1 
ATOM   234  C CG  . GLN   A 1 32  ? -53.065 -21.542 18.310 1.00 84.55  ? 247 GLN   B CG  1 
ATOM   235  C CD  . GLN   A 1 32  ? -53.058 -22.362 17.035 1.00 91.64  ? 247 GLN   B CD  1 
ATOM   236  O OE1 . GLN   A 1 32  ? -53.076 -23.596 17.076 1.00 96.34  ? 247 GLN   B OE1 1 
ATOM   237  N NE2 . GLN   A 1 32  ? -53.001 -21.686 15.896 1.00 91.62  ? 247 GLN   B NE2 1 
ATOM   238  N N   . ARG   A 1 33  ? -49.711 -20.456 20.303 1.00 73.01  ? 248 ARG   B N   1 
ATOM   239  C CA  . ARG   A 1 33  ? -48.787 -19.516 19.773 1.00 71.99  ? 248 ARG   B CA  1 
ATOM   240  C C   . ARG   A 1 33  ? -47.751 -20.249 18.996 1.00 72.95  ? 248 ARG   B C   1 
ATOM   241  O O   . ARG   A 1 33  ? -47.401 -21.369 19.303 1.00 75.41  ? 248 ARG   B O   1 
ATOM   242  C CB  . ARG   A 1 33  ? -48.174 -18.670 20.865 1.00 72.65  ? 248 ARG   B CB  1 
ATOM   243  C CG  . ARG   A 1 33  ? -46.952 -19.232 21.534 1.00 72.26  ? 248 ARG   B CG  1 
ATOM   244  C CD  . ARG   A 1 33  ? -46.718 -18.438 22.776 1.00 69.89  ? 248 ARG   B CD  1 
ATOM   245  N NE  . ARG   A 1 33  ? -45.351 -18.522 23.222 1.00 77.75  ? 248 ARG   B NE  1 
ATOM   246  C CZ  . ARG   A 1 33  ? -44.841 -17.696 24.111 1.00 79.89  ? 248 ARG   B CZ  1 
ATOM   247  N NH1 . ARG   A 1 33  ? -43.590 -17.818 24.501 1.00 74.93  ? 248 ARG   B NH1 1 
ATOM   248  N NH2 . ARG   A 1 33  ? -45.608 -16.752 24.612 1.00 83.86  ? 248 ARG   B NH2 1 
ATOM   249  N N   . HIS   A 1 34  ? -47.278 -19.584 17.969 1.00 69.98  ? 249 HIS   B N   1 
ATOM   250  C CA  . HIS   A 1 34  ? -46.227 -20.121 17.121 1.00 62.08  ? 249 HIS   B CA  1 
ATOM   251  C C   . HIS   A 1 34  ? -44.929 -19.405 17.440 1.00 57.69  ? 249 HIS   B C   1 
ATOM   252  O O   . HIS   A 1 34  ? -44.881 -18.173 17.397 1.00 59.43  ? 249 HIS   B O   1 
ATOM   253  C CB  . HIS   A 1 34  ? -46.559 -19.950 15.643 1.00 64.08  ? 249 HIS   B CB  1 
ATOM   254  C CG  . HIS   A 1 34  ? -45.486 -20.475 14.741 1.00 69.59  ? 249 HIS   B CG  1 
ATOM   255  N ND1 . HIS   A 1 34  ? -44.628 -19.650 14.046 1.00 66.53  ? 249 HIS   B ND1 1 
ATOM   256  C CD2 . HIS   A 1 34  ? -45.109 -21.741 14.450 1.00 68.63  ? 249 HIS   B CD2 1 
ATOM   257  C CE1 . HIS   A 1 34  ? -43.776 -20.384 13.359 1.00 67.30  ? 249 HIS   B CE1 1 
ATOM   258  N NE2 . HIS   A 1 34  ? -44.044 -21.656 13.589 1.00 69.57  ? 249 HIS   B NE2 1 
ATOM   259  N N   . LEU   A 1 35  ? -43.887 -20.176 17.754 1.00 53.94  ? 250 LEU   B N   1 
ATOM   260  C CA  . LEU   A 1 35  ? -42.568 -19.641 18.092 1.00 54.97  ? 250 LEU   B CA  1 
ATOM   261  C C   . LEU   A 1 35  ? -41.681 -19.605 16.849 1.00 61.58  ? 250 LEU   B C   1 
ATOM   262  O O   . LEU   A 1 35  ? -41.316 -20.657 16.301 1.00 62.55  ? 250 LEU   B O   1 
ATOM   263  C CB  . LEU   A 1 35  ? -41.896 -20.488 19.164 1.00 56.70  ? 250 LEU   B CB  1 
ATOM   264  C CG  . LEU   A 1 35  ? -42.553 -20.621 20.515 1.00 60.48  ? 250 LEU   B CG  1 
ATOM   265  C CD1 . LEU   A 1 35  ? -41.665 -21.516 21.298 1.00 60.44  ? 250 LEU   B CD1 1 
ATOM   266  C CD2 . LEU   A 1 35  ? -42.653 -19.261 21.157 1.00 61.14  ? 250 LEU   B CD2 1 
ATOM   267  N N   . PHE   A 1 36  ? -41.314 -18.396 16.417 1.00 58.02  ? 251 PHE   B N   1 
ATOM   268  C CA  . PHE   A 1 36  ? -40.303 -18.250 15.377 1.00 58.91  ? 251 PHE   B CA  1 
ATOM   269  C C   . PHE   A 1 36  ? -38.936 -18.712 15.885 1.00 59.95  ? 251 PHE   B C   1 
ATOM   270  O O   . PHE   A 1 36  ? -38.282 -19.565 15.266 1.00 55.30  ? 251 PHE   B O   1 
ATOM   271  C CB  . PHE   A 1 36  ? -40.251 -16.789 14.916 1.00 59.83  ? 251 PHE   B CB  1 
ATOM   272  C CG  . PHE   A 1 36  ? -41.552 -16.266 14.352 1.00 57.30  ? 251 PHE   B CG  1 
ATOM   273  C CD1 . PHE   A 1 36  ? -42.049 -16.740 13.148 1.00 60.42  ? 251 PHE   B CD1 1 
ATOM   274  C CD2 . PHE   A 1 36  ? -42.266 -15.291 15.018 1.00 51.87  ? 251 PHE   B CD2 1 
ATOM   275  C CE1 . PHE   A 1 36  ? -43.242 -16.258 12.622 1.00 58.95  ? 251 PHE   B CE1 1 
ATOM   276  C CE2 . PHE   A 1 36  ? -43.455 -14.799 14.483 1.00 55.26  ? 251 PHE   B CE2 1 
ATOM   277  C CZ  . PHE   A 1 36  ? -43.937 -15.294 13.278 1.00 59.53  ? 251 PHE   B CZ  1 
ATOM   278  N N   . VAL   A 1 37  ? -38.484 -18.135 17.012 1.00 58.05  ? 252 VAL   B N   1 
ATOM   279  C CA  . VAL   A 1 37  ? -37.275 -18.554 17.717 1.00 57.23  ? 252 VAL   B CA  1 
ATOM   280  C C   . VAL   A 1 37  ? -37.563 -18.489 19.206 1.00 56.60  ? 252 VAL   B C   1 
ATOM   281  O O   . VAL   A 1 37  ? -38.508 -17.831 19.646 1.00 58.22  ? 252 VAL   B O   1 
ATOM   282  C CB  . VAL   A 1 37  ? -36.050 -17.688 17.389 1.00 57.06  ? 252 VAL   B CB  1 
ATOM   283  C CG1 . VAL   A 1 37  ? -35.721 -17.797 15.903 1.00 57.77  ? 252 VAL   B CG1 1 
ATOM   284  C CG2 . VAL   A 1 37  ? -36.301 -16.245 17.800 1.00 56.21  ? 252 VAL   B CG2 1 
ATOM   285  N N   . HIS   A 1 38  ? -36.720 -19.165 19.989 1.00 56.49  ? 253 HIS   B N   1 
ATOM   286  C CA  . HIS   A 1 38  ? -37.040 -19.362 21.401 1.00 58.68  ? 253 HIS   B CA  1 
ATOM   287  C C   . HIS   A 1 38  ? -35.895 -19.985 22.187 1.00 56.43  ? 253 HIS   B C   1 
ATOM   288  O O   . HIS   A 1 38  ? -35.649 -21.183 22.067 1.00 61.89  ? 253 HIS   B O   1 
ATOM   289  C CB  . HIS   A 1 38  ? -38.293 -20.245 21.513 1.00 57.73  ? 253 HIS   B CB  1 
ATOM   290  C CG  . HIS   A 1 38  ? -38.603 -20.711 22.904 1.00 66.50  ? 253 HIS   B CG  1 
ATOM   291  N ND1 . HIS   A 1 38  ? -38.347 -21.996 23.335 1.00 68.33  ? 253 HIS   B ND1 1 
ATOM   292  C CD2 . HIS   A 1 38  ? -39.165 -20.067 23.959 1.00 66.79  ? 253 HIS   B CD2 1 
ATOM   293  C CE1 . HIS   A 1 38  ? -38.735 -22.123 24.592 1.00 62.48  ? 253 HIS   B CE1 1 
ATOM   294  N NE2 . HIS   A 1 38  ? -39.233 -20.967 24.994 1.00 65.59  ? 253 HIS   B NE2 1 
ATOM   295  N N   . ILE   A 1 39  ? -35.205 -19.209 23.002 1.00 58.29  ? 254 ILE   B N   1 
ATOM   296  C CA  . ILE   A 1 39  ? -34.193 -19.741 23.914 1.00 61.36  ? 254 ILE   B CA  1 
ATOM   297  C C   . ILE   A 1 39  ? -34.807 -19.925 25.300 1.00 63.54  ? 254 ILE   B C   1 
ATOM   298  O O   . ILE   A 1 39  ? -35.690 -19.165 25.708 1.00 65.85  ? 254 ILE   B O   1 
ATOM   299  C CB  . ILE   A 1 39  ? -32.965 -18.818 23.971 1.00 60.74  ? 254 ILE   B CB  1 
ATOM   300  C CG1 . ILE   A 1 39  ? -32.455 -18.531 22.556 1.00 58.98  ? 254 ILE   B CG1 1 
ATOM   301  C CG2 . ILE   A 1 39  ? -31.885 -19.432 24.848 1.00 61.21  ? 254 ILE   B CG2 1 
ATOM   302  C CD1 . ILE   A 1 39  ? -31.210 -17.668 22.506 1.00 50.74  ? 254 ILE   B CD1 1 
ATOM   303  N N   . SER   A 1 40  ? -34.356 -20.937 26.033 1.00 65.74  ? 255 SER   B N   1 
ATOM   304  C CA  . SER   A 1 40  ? -34.946 -21.231 27.340 1.00 71.24  ? 255 SER   B CA  1 
ATOM   305  C C   . SER   A 1 40  ? -33.885 -21.870 28.223 1.00 73.17  ? 255 SER   B C   1 
ATOM   306  O O   . SER   A 1 40  ? -33.520 -23.024 27.988 1.00 78.54  ? 255 SER   B O   1 
ATOM   307  C CB  . SER   A 1 40  ? -36.154 -22.150 27.189 1.00 70.77  ? 255 SER   B CB  1 
ATOM   308  O OG  . SER   A 1 40  ? -36.805 -22.346 28.427 1.00 80.31  ? 255 SER   B OG  1 
ATOM   309  N N   . GLN   A 1 41  ? -33.402 -21.148 29.234 1.00 75.43  ? 256 GLN   B N   1 
ATOM   310  C CA  . GLN   A 1 41  ? -32.348 -21.654 30.120 1.00 79.02  ? 256 GLN   B CA  1 
ATOM   311  C C   . GLN   A 1 41  ? -32.887 -21.790 31.540 1.00 84.06  ? 256 GLN   B C   1 
ATOM   312  O O   . GLN   A 1 41  ? -32.559 -20.997 32.417 1.00 83.98  ? 256 GLN   B O   1 
ATOM   313  C CB  . GLN   A 1 41  ? -31.122 -20.726 30.091 1.00 71.68  ? 256 GLN   B CB  1 
ATOM   314  C CG  . GLN   A 1 41  ? -30.891 -20.048 28.750 1.00 72.35  ? 256 GLN   B CG  1 
ATOM   315  C CD  . GLN   A 1 41  ? -29.431 -19.719 28.472 1.00 69.24  ? 256 GLN   B CD  1 
ATOM   316  O OE1 . GLN   A 1 41  ? -28.816 -18.929 29.181 1.00 70.26  ? 256 GLN   B OE1 1 
ATOM   317  N NE2 . GLN   A 1 41  ? -28.877 -20.321 27.426 1.00 67.08  ? 256 GLN   B NE2 1 
ATOM   318  N N   . HIS   A 1 42  ? -33.713 -22.815 31.765 1.00 100.83 ? 257 HIS   B N   1 
ATOM   319  C CA  . HIS   A 1 42  ? -34.277 -23.082 33.102 1.00 103.49 ? 257 HIS   B CA  1 
ATOM   320  C C   . HIS   A 1 42  ? -33.441 -24.090 33.903 1.00 100.76 ? 257 HIS   B C   1 
ATOM   321  O O   . HIS   A 1 42  ? -33.906 -25.192 34.222 1.00 103.09 ? 257 HIS   B O   1 
ATOM   322  C CB  . HIS   A 1 42  ? -35.717 -23.593 32.993 1.00 105.65 ? 257 HIS   B CB  1 
ATOM   323  C CG  . HIS   A 1 42  ? -36.662 -22.612 32.373 1.00 106.43 ? 257 HIS   B CG  1 
ATOM   324  N ND1 . HIS   A 1 42  ? -37.975 -22.924 32.088 1.00 109.28 ? 257 HIS   B ND1 1 
ATOM   325  C CD2 . HIS   A 1 42  ? -36.485 -21.327 31.980 1.00 102.97 ? 257 HIS   B CD2 1 
ATOM   326  C CE1 . HIS   A 1 42  ? -38.568 -21.872 31.549 1.00 107.11 ? 257 HIS   B CE1 1 
ATOM   327  N NE2 . HIS   A 1 42  ? -37.684 -20.891 31.471 1.00 104.14 ? 257 HIS   B NE2 1 
ATOM   328  N N   . PRO   A 1 49  ? -20.601 -27.929 30.689 1.00 109.67 ? 264 PRO   B N   1 
ATOM   329  C CA  . PRO   A 1 49  ? -19.636 -27.732 29.600 1.00 107.61 ? 264 PRO   B CA  1 
ATOM   330  C C   . PRO   A 1 49  ? -19.640 -26.325 28.989 1.00 106.51 ? 264 PRO   B C   1 
ATOM   331  O O   . PRO   A 1 49  ? -20.712 -25.768 28.704 1.00 100.18 ? 264 PRO   B O   1 
ATOM   332  C CB  . PRO   A 1 49  ? -20.065 -28.767 28.552 1.00 105.00 ? 264 PRO   B CB  1 
ATOM   333  C CG  . PRO   A 1 49  ? -21.513 -29.061 28.858 1.00 110.80 ? 264 PRO   B CG  1 
ATOM   334  C CD  . PRO   A 1 49  ? -21.869 -28.493 30.205 1.00 107.71 ? 264 PRO   B CD  1 
ATOM   335  N N   . PRO   A 1 50  ? -18.440 -25.766 28.803 1.00 105.40 ? 265 PRO   B N   1 
ATOM   336  C CA  . PRO   A 1 50  ? -18.324 -24.433 28.198 1.00 100.67 ? 265 PRO   B CA  1 
ATOM   337  C C   . PRO   A 1 50  ? -18.802 -24.419 26.754 1.00 92.72  ? 265 PRO   B C   1 
ATOM   338  O O   . PRO   A 1 50  ? -18.543 -25.348 25.981 1.00 92.16  ? 265 PRO   B O   1 
ATOM   339  C CB  . PRO   A 1 50  ? -16.820 -24.134 28.296 1.00 98.76  ? 265 PRO   B CB  1 
ATOM   340  C CG  . PRO   A 1 50  ? -16.176 -25.493 28.422 1.00 102.59 ? 265 PRO   B CG  1 
ATOM   341  C CD  . PRO   A 1 50  ? -17.139 -26.236 29.308 1.00 104.80 ? 265 PRO   B CD  1 
ATOM   342  N N   . LEU   A 1 51  ? -19.502 -23.346 26.396 1.00 89.78  ? 266 LEU   B N   1 
ATOM   343  C CA  . LEU   A 1 51  ? -20.019 -23.224 25.048 1.00 86.26  ? 266 LEU   B CA  1 
ATOM   344  C C   . LEU   A 1 51  ? -18.869 -23.033 24.071 1.00 88.27  ? 266 LEU   B C   1 
ATOM   345  O O   . LEU   A 1 51  ? -17.746 -22.692 24.451 1.00 88.46  ? 266 LEU   B O   1 
ATOM   346  C CB  . LEU   A 1 51  ? -20.997 -22.059 24.937 1.00 82.10  ? 266 LEU   B CB  1 
ATOM   347  C CG  . LEU   A 1 51  ? -22.235 -22.075 25.829 1.00 80.76  ? 266 LEU   B CG  1 
ATOM   348  C CD1 . LEU   A 1 51  ? -22.633 -20.654 26.177 1.00 77.33  ? 266 LEU   B CD1 1 
ATOM   349  C CD2 . LEU   A 1 51  ? -23.403 -22.837 25.196 1.00 74.66  ? 266 LEU   B CD2 1 
ATOM   350  N N   . GLU   A 1 52  ? -19.160 -23.267 22.798 1.00 90.45  ? 267 GLU   B N   1 
ATOM   351  C CA  . GLU   A 1 52  ? -18.139 -23.170 21.771 1.00 91.73  ? 267 GLU   B CA  1 
ATOM   352  C C   . GLU   A 1 52  ? -17.910 -21.723 21.385 1.00 91.64  ? 267 GLU   B C   1 
ATOM   353  O O   . GLU   A 1 52  ? -18.850 -20.940 21.248 1.00 91.04  ? 267 GLU   B O   1 
ATOM   354  C CB  . GLU   A 1 52  ? -18.532 -23.977 20.541 1.00 93.51  ? 267 GLU   B CB  1 
ATOM   355  C CG  . GLU   A 1 52  ? -18.442 -25.470 20.737 1.00 97.05  ? 267 GLU   B CG  1 
ATOM   356  C CD  . GLU   A 1 52  ? -19.233 -26.221 19.688 1.00 104.25 ? 267 GLU   B CD  1 
ATOM   357  O OE1 . GLU   A 1 52  ? -19.295 -25.732 18.535 1.00 103.26 ? 267 GLU   B OE1 1 
ATOM   358  O OE2 . GLU   A 1 52  ? -19.771 -27.304 20.012 1.00 107.23 ? 267 GLU   B OE2 1 
ATOM   359  N N   . SER   A 1 53  ? -16.653 -21.377 21.192 1.00 81.52  ? 268 SER   B N   1 
ATOM   360  C CA  . SER   A 1 53  ? -16.286 -20.016 20.861 1.00 80.76  ? 268 SER   B CA  1 
ATOM   361  C C   . SER   A 1 53  ? -16.305 -19.785 19.355 1.00 80.82  ? 268 SER   B C   1 
ATOM   362  O O   . SER   A 1 53  ? -16.126 -20.704 18.553 1.00 83.77  ? 268 SER   B O   1 
ATOM   363  C CB  . SER   A 1 53  ? -14.903 -19.704 21.411 1.00 82.00  ? 268 SER   B CB  1 
ATOM   364  O OG  . SER   A 1 53  ? -13.998 -20.705 20.993 1.00 88.71  ? 268 SER   B OG  1 
ATOM   365  N N   . VAL   A 1 54  ? -16.519 -18.530 18.980 1.00 79.30  ? 269 VAL   B N   1 
ATOM   366  C CA  . VAL   A 1 54  ? -16.517 -18.099 17.592 1.00 76.19  ? 269 VAL   B CA  1 
ATOM   367  C C   . VAL   A 1 54  ? -15.840 -16.741 17.562 1.00 80.59  ? 269 VAL   B C   1 
ATOM   368  O O   . VAL   A 1 54  ? -16.292 -15.814 18.243 1.00 79.79  ? 269 VAL   B O   1 
ATOM   369  C CB  . VAL   A 1 54  ? -17.939 -18.012 17.022 1.00 75.02  ? 269 VAL   B CB  1 
ATOM   370  C CG1 . VAL   A 1 54  ? -18.009 -17.022 15.858 1.00 74.55  ? 269 VAL   B CG1 1 
ATOM   371  C CG2 . VAL   A 1 54  ? -18.410 -19.389 16.627 1.00 69.54  ? 269 VAL   B CG2 1 
ATOM   372  N N   . ASP   A 1 55  ? -14.747 -16.623 16.799 1.00 84.81  ? 270 ASP   B N   1 
ATOM   373  C CA  . ASP   A 1 55  ? -13.976 -15.383 16.777 1.00 87.34  ? 270 ASP   B CA  1 
ATOM   374  C C   . ASP   A 1 55  ? -14.827 -14.240 16.243 1.00 88.99  ? 270 ASP   B C   1 
ATOM   375  O O   . ASP   A 1 55  ? -15.388 -14.335 15.148 1.00 89.14  ? 270 ASP   B O   1 
ATOM   376  C CB  . ASP   A 1 55  ? -12.722 -15.550 15.932 1.00 89.37  ? 270 ASP   B CB  1 
ATOM   377  C CG  . ASP   A 1 55  ? -11.860 -14.301 15.923 1.00 94.46  ? 270 ASP   B CG  1 
ATOM   378  O OD1 . ASP   A 1 55  ? -12.358 -13.261 15.444 1.00 92.67  ? 270 ASP   B OD1 1 
ATOM   379  O OD2 . ASP   A 1 55  ? -10.694 -14.353 16.394 1.00 96.03  ? 270 ASP   B OD2 1 
ATOM   380  N N   . VAL   A 1 56  ? -14.910 -13.153 17.019 1.00 90.96  ? 271 VAL   B N   1 
ATOM   381  C CA  . VAL   A 1 56  ? -15.848 -12.081 16.708 1.00 88.12  ? 271 VAL   B CA  1 
ATOM   382  C C   . VAL   A 1 56  ? -15.524 -11.455 15.359 1.00 93.04  ? 271 VAL   B C   1 
ATOM   383  O O   . VAL   A 1 56  ? -16.417 -10.934 14.679 1.00 92.81  ? 271 VAL   B O   1 
ATOM   384  C CB  . VAL   A 1 56  ? -15.853 -11.043 17.851 1.00 81.11  ? 271 VAL   B CB  1 
ATOM   385  C CG1 . VAL   A 1 56  ? -14.500 -10.364 17.981 1.00 84.46  ? 271 VAL   B CG1 1 
ATOM   386  C CG2 . VAL   A 1 56  ? -16.941 -10.033 17.642 1.00 80.36  ? 271 VAL   B CG2 1 
ATOM   387  N N   . ARG   A 1 57  ? -14.257 -11.533 14.928 1.00 91.10  ? 272 ARG   B N   1 
ATOM   388  C CA  . ARG   A 1 57  ? -13.854 -10.898 13.674 1.00 92.43  ? 272 ARG   B CA  1 
ATOM   389  C C   . ARG   A 1 57  ? -14.605 -11.482 12.481 1.00 92.05  ? 272 ARG   B C   1 
ATOM   390  O O   . ARG   A 1 57  ? -15.026 -10.742 11.585 1.00 92.61  ? 272 ARG   B O   1 
ATOM   391  C CB  . ARG   A 1 57  ? -12.347 -11.042 13.478 1.00 92.63  ? 272 ARG   B CB  1 
ATOM   392  C CG  . ARG   A 1 57  ? -11.475 -10.191 14.394 1.00 92.56  ? 272 ARG   B CG  1 
ATOM   393  C CD  . ARG   A 1 57  ? -10.044 -10.708 14.352 1.00 94.28  ? 272 ARG   B CD  1 
ATOM   394  N NE  . ARG   A 1 57  ? -9.245  -10.374 15.527 1.00 98.86  ? 272 ARG   B NE  1 
ATOM   395  C CZ  . ARG   A 1 57  ? -8.417  -11.216 16.138 1.00 101.16 ? 272 ARG   B CZ  1 
ATOM   396  N NH1 . ARG   A 1 57  ? -8.325  -12.485 15.771 1.00 101.45 ? 272 ARG   B NH1 1 
ATOM   397  N NH2 . ARG   A 1 57  ? -7.654  -10.770 17.137 1.00 98.92  ? 272 ARG   B NH2 1 
ATOM   398  N N   . GLN   A 1 58  ? -14.810 -12.800 12.463 1.00 90.71  ? 273 GLN   B N   1 
ATOM   399  C CA  . GLN   A 1 58  ? -15.542 -13.473 11.394 1.00 89.45  ? 273 GLN   B CA  1 
ATOM   400  C C   . GLN   A 1 58  ? -16.974 -12.969 11.177 1.00 90.70  ? 273 GLN   B C   1 
ATOM   401  O O   . GLN   A 1 58  ? -17.661 -13.454 10.273 1.00 89.10  ? 273 GLN   B O   1 
ATOM   402  C CB  . GLN   A 1 58  ? -15.584 -14.985 11.662 1.00 87.59  ? 273 GLN   B CB  1 
ATOM   403  C CG  . GLN   A 1 58  ? -14.232 -15.637 11.922 1.00 89.89  ? 273 GLN   B CG  1 
ATOM   404  C CD  . GLN   A 1 58  ? -13.555 -16.157 10.647 1.00 98.32  ? 273 GLN   B CD  1 
ATOM   405  O OE1 . GLN   A 1 58  ? -13.149 -15.380 9.776  1.00 99.46  ? 273 GLN   B OE1 1 
ATOM   406  N NE2 . GLN   A 1 58  ? -13.433 -17.478 10.538 1.00 98.48  ? 273 GLN   B NE2 1 
ATOM   407  N N   . ILE   A 1 59  ? -17.458 -12.022 11.984 1.00 94.15  ? 274 ILE   B N   1 
ATOM   408  C CA  . ILE   A 1 59  ? -18.824 -11.528 11.801 1.00 94.69  ? 274 ILE   B CA  1 
ATOM   409  C C   . ILE   A 1 59  ? -18.874 -10.002 11.831 1.00 97.96  ? 274 ILE   B C   1 
ATOM   410  O O   . ILE   A 1 59  ? -19.959 -9.413  11.911 1.00 97.36  ? 274 ILE   B O   1 
ATOM   411  C CB  . ILE   A 1 59  ? -19.777 -12.120 12.858 1.00 89.06  ? 274 ILE   B CB  1 
ATOM   412  C CG1 . ILE   A 1 59  ? -19.218 -11.896 14.258 1.00 88.46  ? 274 ILE   B CG1 1 
ATOM   413  C CG2 . ILE   A 1 59  ? -19.979 -13.596 12.636 1.00 86.06  ? 274 ILE   B CG2 1 
ATOM   414  C CD1 . ILE   A 1 59  ? -20.057 -12.481 15.343 1.00 79.14  ? 274 ILE   B CD1 1 
ATOM   415  N N   . TYR   A 1 60  ? -17.705 -9.355  11.745 1.00 100.51 ? 275 TYR   B N   1 
ATOM   416  C CA  . TYR   A 1 60  ? -17.616 -7.897  11.868 1.00 102.03 ? 275 TYR   B CA  1 
ATOM   417  C C   . TYR   A 1 60  ? -18.490 -7.189  10.844 1.00 104.27 ? 275 TYR   B C   1 
ATOM   418  O O   . TYR   A 1 60  ? -19.317 -6.336  11.193 1.00 104.95 ? 275 TYR   B O   1 
ATOM   419  C CB  . TYR   A 1 60  ? -16.155 -7.467  11.708 1.00 102.27 ? 275 TYR   B CB  1 
ATOM   420  C CG  . TYR   A 1 60  ? -15.364 -7.491  12.989 1.00 102.32 ? 275 TYR   B CG  1 
ATOM   421  C CD1 . TYR   A 1 60  ? -14.094 -6.919  13.066 1.00 104.19 ? 275 TYR   B CD1 1 
ATOM   422  C CD2 . TYR   A 1 60  ? -15.927 -8.002  14.150 1.00 99.74  ? 275 TYR   B CD2 1 
ATOM   423  C CE1 . TYR   A 1 60  ? -13.379 -6.939  14.265 1.00 103.31 ? 275 TYR   B CE1 1 
ATOM   424  C CE2 . TYR   A 1 60  ? -15.243 -8.015  15.327 1.00 99.68  ? 275 TYR   B CE2 1 
ATOM   425  C CZ  . TYR   A 1 60  ? -13.982 -7.488  15.393 1.00 100.08 ? 275 TYR   B CZ  1 
ATOM   426  O OH  . TYR   A 1 60  ? -13.360 -7.541  16.619 1.00 101.20 ? 275 TYR   B OH  1 
ATOM   427  N N   . ASP   A 1 61  ? -18.315 -7.533  9.569  1.00 106.55 ? 276 ASP   B N   1 
ATOM   428  C CA  . ASP   A 1 61  ? -18.983 -6.857  8.468  1.00 108.93 ? 276 ASP   B CA  1 
ATOM   429  C C   . ASP   A 1 61  ? -20.460 -7.201  8.364  1.00 108.92 ? 276 ASP   B C   1 
ATOM   430  O O   . ASP   A 1 61  ? -21.141 -6.636  7.502  1.00 108.68 ? 276 ASP   B O   1 
ATOM   431  C CB  . ASP   A 1 61  ? -18.271 -7.190  7.157  1.00 115.09 ? 276 ASP   B CB  1 
ATOM   432  C CG  . ASP   A 1 61  ? -18.096 -8.689  6.948  1.00 117.82 ? 276 ASP   B CG  1 
ATOM   433  O OD1 . ASP   A 1 61  ? -18.683 -9.472  7.736  1.00 107.20 ? 276 ASP   B OD1 1 
ATOM   434  O OD2 . ASP   A 1 61  ? -17.372 -9.074  5.991  1.00 118.00 ? 276 ASP   B OD2 1 
ATOM   435  N N   . LYS   A 1 62  ? -20.969 -8.104  9.206  1.00 110.56 ? 277 LYS   B N   1 
ATOM   436  C CA  . LYS   A 1 62  ? -22.397 -8.383  9.263  1.00 102.75 ? 277 LYS   B CA  1 
ATOM   437  C C   . LYS   A 1 62  ? -23.136 -7.471  10.234 1.00 98.32  ? 277 LYS   B C   1 
ATOM   438  O O   . LYS   A 1 62  ? -24.352 -7.615  10.377 1.00 92.45  ? 277 LYS   B O   1 
ATOM   439  C CB  . LYS   A 1 62  ? -22.649 -9.859  9.632  1.00 94.59  ? 277 LYS   B CB  1 
ATOM   440  C CG  . LYS   A 1 62  ? -23.086 -10.705 8.423  1.00 91.62  ? 277 LYS   B CG  1 
ATOM   441  C CD  . LYS   A 1 62  ? -22.833 -12.227 8.543  1.00 87.55  ? 277 LYS   B CD  1 
ATOM   442  C CE  . LYS   A 1 62  ? -23.921 -12.950 9.373  1.00 87.42  ? 277 LYS   B CE  1 
ATOM   443  N NZ  . LYS   A 1 62  ? -23.997 -14.455 9.153  1.00 75.00  ? 277 LYS   B NZ  1 
ATOM   444  N N   . PHE   A 1 63  ? -22.444 -6.509  10.874 1.00 106.68 ? 278 PHE   B N   1 
ATOM   445  C CA  . PHE   A 1 63  ? -23.045 -5.673  11.918 1.00 117.28 ? 278 PHE   B CA  1 
ATOM   446  C C   . PHE   A 1 63  ? -22.691 -4.190  11.757 1.00 136.37 ? 278 PHE   B C   1 
ATOM   447  O O   . PHE   A 1 63  ? -21.928 -3.845  10.843 1.00 130.62 ? 278 PHE   B O   1 
ATOM   448  C CB  . PHE   A 1 63  ? -22.627 -6.226  13.287 1.00 111.73 ? 278 PHE   B CB  1 
ATOM   449  C CG  . PHE   A 1 63  ? -23.352 -7.487  13.645 1.00 99.07  ? 278 PHE   B CG  1 
ATOM   450  C CD1 . PHE   A 1 63  ? -24.619 -7.442  14.204 1.00 85.90  ? 278 PHE   B CD1 1 
ATOM   451  C CD2 . PHE   A 1 63  ? -22.802 -8.720  13.353 1.00 92.68  ? 278 PHE   B CD2 1 
ATOM   452  C CE1 . PHE   A 1 63  ? -25.300 -8.601  14.492 1.00 80.26  ? 278 PHE   B CE1 1 
ATOM   453  C CE2 . PHE   A 1 63  ? -23.487 -9.877  13.637 1.00 88.04  ? 278 PHE   B CE2 1 
ATOM   454  C CZ  . PHE   A 1 63  ? -24.735 -9.815  14.201 1.00 80.88  ? 278 PHE   B CZ  1 
ATOM   455  N N   . PRO   A 1 64  ? -23.250 -3.276  12.571 1.00 177.13 ? 279 PRO   B N   1 
ATOM   456  C CA  . PRO   A 1 64  ? -22.913 -1.853  12.411 1.00 178.62 ? 279 PRO   B CA  1 
ATOM   457  C C   . PRO   A 1 64  ? -21.421 -1.601  12.567 1.00 178.98 ? 279 PRO   B C   1 
ATOM   458  O O   . PRO   A 1 64  ? -20.647 -2.454  13.016 1.00 179.12 ? 279 PRO   B O   1 
ATOM   459  C CB  . PRO   A 1 64  ? -23.720 -1.155  13.515 1.00 177.60 ? 279 PRO   B CB  1 
ATOM   460  C CG  . PRO   A 1 64  ? -24.862 -2.048  13.789 1.00 171.54 ? 279 PRO   B CG  1 
ATOM   461  C CD  . PRO   A 1 64  ? -24.354 -3.454  13.543 1.00 171.98 ? 279 PRO   B CD  1 
ATOM   462  N N   . GLU   A 1 65  ? -21.020 -0.385  12.178 1.00 144.25 ? 280 GLU   B N   1 
ATOM   463  C CA  . GLU   A 1 65  ? -19.620 -0.013  12.183 1.00 132.87 ? 280 GLU   B CA  1 
ATOM   464  C C   . GLU   A 1 65  ? -19.435 1.100   13.200 1.00 129.86 ? 280 GLU   B C   1 
ATOM   465  O O   . GLU   A 1 65  ? -19.235 0.815   14.399 1.00 125.62 ? 280 GLU   B O   1 
ATOM   466  C CB  . GLU   A 1 65  ? -19.159 0.352   10.767 1.00 123.02 ? 280 GLU   B CB  1 
ATOM   467  C CG  . GLU   A 1 65  ? -18.416 -0.758  10.035 1.00 118.92 ? 280 GLU   B CG  1 
ATOM   468  C CD  . GLU   A 1 65  ? -17.260 -1.351  10.839 1.00 114.87 ? 280 GLU   B CD  1 
ATOM   469  O OE1 . GLU   A 1 65  ? -16.660 -0.628  11.665 1.00 113.62 ? 280 GLU   B OE1 1 
ATOM   470  O OE2 . GLU   A 1 65  ? -16.931 -2.542  10.634 1.00 110.66 ? 280 GLU   B OE2 1 
ATOM   471  N N   . LYS   A 1 66  ? -19.469 2.372   12.796 1.00 125.50 ? 281 LYS   B N   1 
ATOM   472  C CA  . LYS   A 1 66  ? -19.242 3.459   13.744 1.00 121.07 ? 281 LYS   B CA  1 
ATOM   473  C C   . LYS   A 1 66  ? -20.263 3.410   14.878 1.00 120.36 ? 281 LYS   B C   1 
ATOM   474  O O   . LYS   A 1 66  ? -21.452 3.169   14.650 1.00 121.88 ? 281 LYS   B O   1 
ATOM   475  C CB  . LYS   A 1 66  ? -19.308 4.814   13.027 1.00 116.40 ? 281 LYS   B CB  1 
ATOM   476  N N   . LYS   A 1 67  ? -19.771 3.611   16.108 1.00 117.76 ? 282 LYS   B N   1 
ATOM   477  C CA  . LYS   A 1 67  ? -20.535 3.667   17.358 1.00 115.06 ? 282 LYS   B CA  1 
ATOM   478  C C   . LYS   A 1 67  ? -21.658 2.637   17.473 1.00 111.81 ? 282 LYS   B C   1 
ATOM   479  O O   . LYS   A 1 67  ? -22.704 2.763   16.827 1.00 108.31 ? 282 LYS   B O   1 
ATOM   480  C CB  . LYS   A 1 67  ? -21.108 5.078   17.567 1.00 111.07 ? 282 LYS   B CB  1 
ATOM   481  C CG  . LYS   A 1 67  ? -20.225 6.010   18.418 1.00 102.56 ? 282 LYS   B CG  1 
ATOM   482  C CD  . LYS   A 1 67  ? -19.464 7.002   17.541 1.00 98.43  ? 282 LYS   B CD  1 
ATOM   483  C CE  . LYS   A 1 67  ? -18.719 8.056   18.357 1.00 94.31  ? 282 LYS   B CE  1 
ATOM   484  N NZ  . LYS   A 1 67  ? -17.391 7.578   18.846 1.00 89.42  ? 282 LYS   B NZ  1 
ATOM   485  N N   . GLY   A 1 68  ? -21.473 1.636   18.330 1.00 113.27 ? 283 GLY   B N   1 
ATOM   486  C CA  . GLY   A 1 68  ? -22.510 0.654   18.581 1.00 106.62 ? 283 GLY   B CA  1 
ATOM   487  C C   . GLY   A 1 68  ? -22.511 -0.526  17.641 1.00 110.21 ? 283 GLY   B C   1 
ATOM   488  O O   . GLY   A 1 68  ? -23.469 -1.311  17.653 1.00 106.78 ? 283 GLY   B O   1 
ATOM   489  N N   . GLY   A 1 69  ? -21.490 -0.658  16.801 1.00 118.07 ? 284 GLY   B N   1 
ATOM   490  C CA  . GLY   A 1 69  ? -21.298 -1.866  16.040 1.00 117.16 ? 284 GLY   B CA  1 
ATOM   491  C C   . GLY   A 1 69  ? -20.576 -2.905  16.864 1.00 97.56  ? 284 GLY   B C   1 
ATOM   492  O O   . GLY   A 1 69  ? -20.178 -2.673  18.004 1.00 92.45  ? 284 GLY   B O   1 
ATOM   493  N N   . LEU   A 1 70  ? -20.385 -4.072  16.251 1.00 99.05  ? 285 LEU   B N   1 
ATOM   494  C CA  . LEU   A 1 70  ? -19.834 -5.210  16.980 1.00 89.97  ? 285 LEU   B CA  1 
ATOM   495  C C   . LEU   A 1 70  ? -18.420 -4.941  17.480 1.00 88.70  ? 285 LEU   B C   1 
ATOM   496  O O   . LEU   A 1 70  ? -18.104 -5.213  18.643 1.00 85.65  ? 285 LEU   B O   1 
ATOM   497  C CB  . LEU   A 1 70  ? -19.856 -6.455  16.107 1.00 80.75  ? 285 LEU   B CB  1 
ATOM   498  C CG  . LEU   A 1 70  ? -19.705 -7.708  16.963 1.00 83.33  ? 285 LEU   B CG  1 
ATOM   499  C CD1 . LEU   A 1 70  ? -20.483 -7.594  18.297 1.00 73.10  ? 285 LEU   B CD1 1 
ATOM   500  C CD2 . LEU   A 1 70  ? -20.138 -8.915  16.168 1.00 85.53  ? 285 LEU   B CD2 1 
ATOM   501  N N   . ARG   A 1 71  ? -17.541 -4.436  16.614 1.00 91.62  ? 286 ARG   B N   1 
ATOM   502  C CA  . ARG   A 1 71  ? -16.163 -4.234  17.044 1.00 93.84  ? 286 ARG   B CA  1 
ATOM   503  C C   . ARG   A 1 71  ? -16.083 -3.173  18.133 1.00 92.18  ? 286 ARG   B C   1 
ATOM   504  O O   . ARG   A 1 71  ? -15.535 -3.426  19.207 1.00 91.54  ? 286 ARG   B O   1 
ATOM   505  C CB  . ARG   A 1 71  ? -15.272 -3.864  15.860 1.00 94.33  ? 286 ARG   B CB  1 
ATOM   506  C CG  . ARG   A 1 71  ? -13.792 -3.731  16.222 1.00 93.88  ? 286 ARG   B CG  1 
ATOM   507  C CD  . ARG   A 1 71  ? -12.968 -3.358  15.022 1.00 94.77  ? 286 ARG   B CD  1 
ATOM   508  N NE  . ARG   A 1 71  ? -13.839 -2.941  13.930 1.00 99.92  ? 286 ARG   B NE  1 
ATOM   509  C CZ  . ARG   A 1 71  ? -13.771 -3.403  12.689 1.00 97.80  ? 286 ARG   B CZ  1 
ATOM   510  N NH1 . ARG   A 1 71  ? -12.786 -4.197  12.298 1.00 95.57  ? 286 ARG   B NH1 1 
ATOM   511  N NH2 . ARG   A 1 71  ? -14.715 -3.056  11.818 1.00 97.47  ? 286 ARG   B NH2 1 
ATOM   512  N N   . GLU   A 1 72  ? -16.658 -1.990  17.890 1.00 107.47 ? 287 GLU   B N   1 
ATOM   513  C CA  . GLU   A 1 72  ? -16.505 -0.882  18.835 1.00 105.57 ? 287 GLU   B CA  1 
ATOM   514  C C   . GLU   A 1 72  ? -17.090 -1.204  20.204 1.00 101.72 ? 287 GLU   B C   1 
ATOM   515  O O   . GLU   A 1 72  ? -16.672 -0.608  21.201 1.00 99.77  ? 287 GLU   B O   1 
ATOM   516  C CB  . GLU   A 1 72  ? -17.149 0.395   18.285 1.00 111.38 ? 287 GLU   B CB  1 
ATOM   517  C CG  . GLU   A 1 72  ? -16.615 0.849   16.923 1.00 119.90 ? 287 GLU   B CG  1 
ATOM   518  C CD  . GLU   A 1 72  ? -16.679 2.363   16.741 1.00 122.78 ? 287 GLU   B CD  1 
ATOM   519  O OE1 . GLU   A 1 72  ? -17.234 3.045   17.635 1.00 123.94 ? 287 GLU   B OE1 1 
ATOM   520  O OE2 . GLU   A 1 72  ? -16.179 2.868   15.708 1.00 117.12 ? 287 GLU   B OE2 1 
ATOM   521  N N   . LEU   A 1 73  ? -18.061 -2.123  20.273 1.00 95.78  ? 288 LEU   B N   1 
ATOM   522  C CA  . LEU   A 1 73  ? -18.588 -2.597  21.550 1.00 87.81  ? 288 LEU   B CA  1 
ATOM   523  C C   . LEU   A 1 73  ? -17.626 -3.572  22.214 1.00 86.22  ? 288 LEU   B C   1 
ATOM   524  O O   . LEU   A 1 73  ? -17.334 -3.459  23.408 1.00 88.26  ? 288 LEU   B O   1 
ATOM   525  C CB  . LEU   A 1 73  ? -19.947 -3.259  21.339 1.00 81.80  ? 288 LEU   B CB  1 
ATOM   526  C CG  . LEU   A 1 73  ? -21.119 -2.301  21.487 1.00 81.13  ? 288 LEU   B CG  1 
ATOM   527  C CD1 . LEU   A 1 73  ? -22.429 -2.955  21.133 1.00 74.16  ? 288 LEU   B CD1 1 
ATOM   528  C CD2 . LEU   A 1 73  ? -21.134 -1.822  22.903 1.00 81.51  ? 288 LEU   B CD2 1 
ATOM   529  N N   . TYR   A 1 74  ? -17.132 -4.543  21.448 1.00 82.09  ? 289 TYR   B N   1 
ATOM   530  C CA  . TYR   A 1 74  ? -16.142 -5.481  21.952 1.00 78.18  ? 289 TYR   B CA  1 
ATOM   531  C C   . TYR   A 1 74  ? -14.870 -4.799  22.439 1.00 86.51  ? 289 TYR   B C   1 
ATOM   532  O O   . TYR   A 1 74  ? -14.135 -5.393  23.236 1.00 90.47  ? 289 TYR   B O   1 
ATOM   533  C CB  . TYR   A 1 74  ? -15.793 -6.490  20.869 1.00 77.45  ? 289 TYR   B CB  1 
ATOM   534  C CG  . TYR   A 1 74  ? -15.316 -7.805  21.408 1.00 76.49  ? 289 TYR   B CG  1 
ATOM   535  C CD1 . TYR   A 1 74  ? -13.990 -7.986  21.791 1.00 78.73  ? 289 TYR   B CD1 1 
ATOM   536  C CD2 . TYR   A 1 74  ? -16.183 -8.872  21.516 1.00 72.85  ? 289 TYR   B CD2 1 
ATOM   537  C CE1 . TYR   A 1 74  ? -13.552 -9.191  22.281 1.00 78.96  ? 289 TYR   B CE1 1 
ATOM   538  C CE2 . TYR   A 1 74  ? -15.757 -10.082 22.002 1.00 72.70  ? 289 TYR   B CE2 1 
ATOM   539  C CZ  . TYR   A 1 74  ? -14.443 -10.237 22.387 1.00 76.07  ? 289 TYR   B CZ  1 
ATOM   540  O OH  . TYR   A 1 74  ? -14.032 -11.451 22.883 1.00 79.42  ? 289 TYR   B OH  1 
ATOM   541  N N   . ASP   A 1 75  ? -14.573 -3.581  21.976 1.00 90.02  ? 290 ASP   B N   1 
ATOM   542  C CA  . ASP   A 1 75  ? -13.389 -2.893  22.482 1.00 90.95  ? 290 ASP   B CA  1 
ATOM   543  C C   . ASP   A 1 75  ? -13.652 -2.195  23.808 1.00 90.20  ? 290 ASP   B C   1 
ATOM   544  O O   . ASP   A 1 75  ? -12.708 -1.953  24.565 1.00 88.48  ? 290 ASP   B O   1 
ATOM   545  C CB  . ASP   A 1 75  ? -12.853 -1.874  21.471 1.00 98.14  ? 290 ASP   B CB  1 
ATOM   546  C CG  . ASP   A 1 75  ? -12.565 -2.483  20.107 1.00 98.70  ? 290 ASP   B CG  1 
ATOM   547  O OD1 . ASP   A 1 75  ? -13.365 -2.264  19.181 1.00 101.41 ? 290 ASP   B OD1 1 
ATOM   548  O OD2 . ASP   A 1 75  ? -11.544 -3.189  19.963 1.00 101.52 ? 290 ASP   B OD2 1 
ATOM   549  N N   . ARG   A 1 76  ? -14.908 -1.852  24.110 1.00 99.88  ? 291 ARG   B N   1 
ATOM   550  C CA  . ARG   A 1 76  ? -15.237 -1.380  25.452 1.00 97.27  ? 291 ARG   B CA  1 
ATOM   551  C C   . ARG   A 1 76  ? -15.265 -2.519  26.465 1.00 93.00  ? 291 ARG   B C   1 
ATOM   552  O O   . ARG   A 1 76  ? -15.080 -2.277  27.662 1.00 89.05  ? 291 ARG   B O   1 
ATOM   553  C CB  . ARG   A 1 76  ? -16.583 -0.651  25.438 1.00 98.21  ? 291 ARG   B CB  1 
ATOM   554  C CG  . ARG   A 1 76  ? -16.899 -0.044  24.087 1.00 103.36 ? 291 ARG   B CG  1 
ATOM   555  C CD  . ARG   A 1 76  ? -17.703 1.255   24.124 1.00 111.18 ? 291 ARG   B CD  1 
ATOM   556  N NE  . ARG   A 1 76  ? -18.089 1.648   22.769 1.00 117.44 ? 291 ARG   B NE  1 
ATOM   557  C CZ  . ARG   A 1 76  ? -19.063 2.499   22.464 1.00 121.00 ? 291 ARG   B CZ  1 
ATOM   558  N NH1 . ARG   A 1 76  ? -19.792 3.082   23.402 1.00 127.08 ? 291 ARG   B NH1 1 
ATOM   559  N NH2 . ARG   A 1 76  ? -19.305 2.776   21.183 1.00 119.44 ? 291 ARG   B NH2 1 
ATOM   560  N N   . GLY   A 1 77  ? -15.461 -3.754  26.007 1.00 85.20  ? 292 GLY   B N   1 
ATOM   561  C CA  . GLY   A 1 77  ? -15.563 -4.882  26.892 1.00 77.93  ? 292 GLY   B CA  1 
ATOM   562  C C   . GLY   A 1 77  ? -16.866 -4.827  27.652 1.00 76.44  ? 292 GLY   B C   1 
ATOM   563  O O   . GLY   A 1 77  ? -17.729 -3.984  27.379 1.00 76.51  ? 292 GLY   B O   1 
ATOM   564  N N   . PRO   A 1 78  ? -17.047 -5.737  28.622 1.00 76.36  ? 293 PRO   B N   1 
ATOM   565  C CA  . PRO   A 1 78  ? -16.151 -6.836  28.998 1.00 71.20  ? 293 PRO   B CA  1 
ATOM   566  C C   . PRO   A 1 78  ? -16.234 -7.925  27.958 1.00 66.78  ? 293 PRO   B C   1 
ATOM   567  O O   . PRO   A 1 78  ? -17.340 -8.272  27.563 1.00 68.76  ? 293 PRO   B O   1 
ATOM   568  C CB  . PRO   A 1 78  ? -16.717 -7.289  30.350 1.00 72.60  ? 293 PRO   B CB  1 
ATOM   569  C CG  . PRO   A 1 78  ? -18.201 -7.042  30.217 1.00 66.57  ? 293 PRO   B CG  1 
ATOM   570  C CD  . PRO   A 1 78  ? -18.310 -5.775  29.392 1.00 70.75  ? 293 PRO   B CD  1 
ATOM   571  N N   . PRO   A 1 79  ? -15.113 -8.478  27.493 1.00 67.57  ? 294 PRO   B N   1 
ATOM   572  C CA  . PRO   A 1 79  ? -15.190 -9.471  26.402 1.00 68.49  ? 294 PRO   B CA  1 
ATOM   573  C C   . PRO   A 1 79  ? -16.095 -10.653 26.727 1.00 66.49  ? 294 PRO   B C   1 
ATOM   574  O O   . PRO   A 1 79  ? -16.791 -11.159 25.835 1.00 65.90  ? 294 PRO   B O   1 
ATOM   575  C CB  . PRO   A 1 79  ? -13.727 -9.904  26.212 1.00 68.25  ? 294 PRO   B CB  1 
ATOM   576  C CG  . PRO   A 1 79  ? -12.908 -8.804  26.864 1.00 70.55  ? 294 PRO   B CG  1 
ATOM   577  C CD  . PRO   A 1 79  ? -13.740 -8.298  27.994 1.00 71.63  ? 294 PRO   B CD  1 
ATOM   578  N N   . HIS   A 1 80  ? -16.139 -11.077 27.993 1.00 64.16  ? 295 HIS   B N   1 
ATOM   579  C CA  . HIS   A 1 80  ? -16.913 -12.239 28.404 1.00 61.23  ? 295 HIS   B CA  1 
ATOM   580  C C   . HIS   A 1 80  ? -18.419 -12.018 28.328 1.00 61.26  ? 295 HIS   B C   1 
ATOM   581  O O   . HIS   A 1 80  ? -19.173 -12.979 28.512 1.00 60.45  ? 295 HIS   B O   1 
ATOM   582  C CB  . HIS   A 1 80  ? -16.516 -12.625 29.822 1.00 64.28  ? 295 HIS   B CB  1 
ATOM   583  C CG  . HIS   A 1 80  ? -17.127 -11.748 30.872 1.00 69.10  ? 295 HIS   B CG  1 
ATOM   584  N ND1 . HIS   A 1 80  ? -16.450 -10.691 31.440 1.00 71.13  ? 295 HIS   B ND1 1 
ATOM   585  C CD2 . HIS   A 1 80  ? -18.343 -11.779 31.468 1.00 66.03  ? 295 HIS   B CD2 1 
ATOM   586  C CE1 . HIS   A 1 80  ? -17.232 -10.095 32.322 1.00 68.45  ? 295 HIS   B CE1 1 
ATOM   587  N NE2 . HIS   A 1 80  ? -18.385 -10.736 32.358 1.00 66.61  ? 295 HIS   B NE2 1 
ATOM   588  N N   . ALA   A 1 81  ? -18.878 -10.795 28.065 1.00 60.57  ? 296 ALA   B N   1 
ATOM   589  C CA  . ALA   A 1 81  ? -20.302 -10.521 27.954 1.00 59.27  ? 296 ALA   B CA  1 
ATOM   590  C C   . ALA   A 1 81  ? -20.855 -10.725 26.544 1.00 59.47  ? 296 ALA   B C   1 
ATOM   591  O O   . ALA   A 1 81  ? -22.044 -10.477 26.327 1.00 55.94  ? 296 ALA   B O   1 
ATOM   592  C CB  . ALA   A 1 81  ? -20.593 -9.092  28.419 1.00 62.06  ? 296 ALA   B CB  1 
ATOM   593  N N   . PHE   A 1 82  ? -20.035 -11.184 25.591 1.00 62.98  ? 297 PHE   B N   1 
ATOM   594  C CA  . PHE   A 1 82  ? -20.402 -11.252 24.178 1.00 58.80  ? 297 PHE   B CA  1 
ATOM   595  C C   . PHE   A 1 82  ? -20.710 -12.689 23.752 1.00 57.92  ? 297 PHE   B C   1 
ATOM   596  O O   . PHE   A 1 82  ? -19.947 -13.617 24.053 1.00 57.90  ? 297 PHE   B O   1 
ATOM   597  C CB  . PHE   A 1 82  ? -19.286 -10.642 23.324 1.00 58.45  ? 297 PHE   B CB  1 
ATOM   598  C CG  . PHE   A 1 82  ? -19.194 -9.153  23.458 1.00 61.08  ? 297 PHE   B CG  1 
ATOM   599  C CD1 . PHE   A 1 82  ? -18.606 -8.586  24.576 1.00 64.49  ? 297 PHE   B CD1 1 
ATOM   600  C CD2 . PHE   A 1 82  ? -19.721 -8.310  22.491 1.00 63.07  ? 297 PHE   B CD2 1 
ATOM   601  C CE1 . PHE   A 1 82  ? -18.541 -7.205  24.724 1.00 67.33  ? 297 PHE   B CE1 1 
ATOM   602  C CE2 . PHE   A 1 82  ? -19.646 -6.936  22.630 1.00 64.00  ? 297 PHE   B CE2 1 
ATOM   603  C CZ  . PHE   A 1 82  ? -19.062 -6.387  23.747 1.00 67.94  ? 297 PHE   B CZ  1 
ATOM   604  N N   . PHE   A 1 83  ? -21.836 -12.861 23.052 1.00 54.20  ? 298 PHE   B N   1 
ATOM   605  C CA  . PHE   A 1 83  ? -22.338 -14.162 22.632 1.00 56.30  ? 298 PHE   B CA  1 
ATOM   606  C C   . PHE   A 1 83  ? -22.870 -14.084 21.214 1.00 56.98  ? 298 PHE   B C   1 
ATOM   607  O O   . PHE   A 1 83  ? -23.449 -13.078 20.801 1.00 55.49  ? 298 PHE   B O   1 
ATOM   608  C CB  . PHE   A 1 83  ? -23.474 -14.687 23.540 1.00 57.06  ? 298 PHE   B CB  1 
ATOM   609  C CG  . PHE   A 1 83  ? -23.042 -14.906 24.940 1.00 57.60  ? 298 PHE   B CG  1 
ATOM   610  C CD1 . PHE   A 1 83  ? -23.105 -13.864 25.858 1.00 56.85  ? 298 PHE   B CD1 1 
ATOM   611  C CD2 . PHE   A 1 83  ? -22.518 -16.115 25.324 1.00 55.15  ? 298 PHE   B CD2 1 
ATOM   612  C CE1 . PHE   A 1 83  ? -22.660 -14.024 27.129 1.00 56.16  ? 298 PHE   B CE1 1 
ATOM   613  C CE2 . PHE   A 1 83  ? -22.079 -16.291 26.594 1.00 61.71  ? 298 PHE   B CE2 1 
ATOM   614  C CZ  . PHE   A 1 83  ? -22.155 -15.237 27.512 1.00 62.71  ? 298 PHE   B CZ  1 
ATOM   615  N N   . LEU   A 1 84  ? -22.692 -15.170 20.477 1.00 57.40  ? 299 LEU   B N   1 
ATOM   616  C CA  . LEU   A 1 84  ? -23.348 -15.349 19.194 1.00 56.74  ? 299 LEU   B CA  1 
ATOM   617  C C   . LEU   A 1 84  ? -24.407 -16.429 19.352 1.00 56.93  ? 299 LEU   B C   1 
ATOM   618  O O   . LEU   A 1 84  ? -24.135 -17.498 19.922 1.00 55.24  ? 299 LEU   B O   1 
ATOM   619  C CB  . LEU   A 1 84  ? -22.337 -15.707 18.101 1.00 57.36  ? 299 LEU   B CB  1 
ATOM   620  C CG  . LEU   A 1 84  ? -22.810 -16.309 16.775 1.00 59.15  ? 299 LEU   B CG  1 
ATOM   621  C CD1 . LEU   A 1 84  ? -23.606 -15.322 15.933 1.00 56.76  ? 299 LEU   B CD1 1 
ATOM   622  C CD2 . LEU   A 1 84  ? -21.598 -16.780 16.001 1.00 62.68  ? 299 LEU   B CD2 1 
ATOM   623  N N   . VAL   A 1 85  ? -25.623 -16.123 18.904 1.00 55.19  ? 300 VAL   B N   1 
ATOM   624  C CA  . VAL   A 1 85  ? -26.728 -17.074 18.890 1.00 58.77  ? 300 VAL   B CA  1 
ATOM   625  C C   . VAL   A 1 85  ? -27.142 -17.263 17.445 1.00 58.45  ? 300 VAL   B C   1 
ATOM   626  O O   . VAL   A 1 85  ? -27.612 -16.322 16.791 1.00 56.94  ? 300 VAL   B O   1 
ATOM   627  C CB  . VAL   A 1 85  ? -27.922 -16.612 19.741 1.00 56.51  ? 300 VAL   B CB  1 
ATOM   628  C CG1 . VAL   A 1 85  ? -29.197 -17.411 19.372 1.00 51.65  ? 300 VAL   B CG1 1 
ATOM   629  C CG2 . VAL   A 1 85  ? -27.583 -16.768 21.179 1.00 52.89  ? 300 VAL   B CG2 1 
ATOM   630  N N   . LYS   A 1 86  ? -26.959 -18.472 16.946 1.00 61.37  ? 301 LYS   B N   1 
ATOM   631  C CA  . LYS   A 1 86  ? -27.395 -18.821 15.611 1.00 59.82  ? 301 LYS   B CA  1 
ATOM   632  C C   . LYS   A 1 86  ? -28.766 -19.466 15.715 1.00 58.78  ? 301 LYS   B C   1 
ATOM   633  O O   . LYS   A 1 86  ? -28.955 -20.408 16.488 1.00 59.03  ? 301 LYS   B O   1 
ATOM   634  C CB  . LYS   A 1 86  ? -26.390 -19.759 14.962 1.00 62.95  ? 301 LYS   B CB  1 
ATOM   635  C CG  . LYS   A 1 86  ? -26.941 -20.495 13.804 1.00 64.04  ? 301 LYS   B CG  1 
ATOM   636  C CD  . LYS   A 1 86  ? -25.836 -20.818 12.841 1.00 71.59  ? 301 LYS   B CD  1 
ATOM   637  C CE  . LYS   A 1 86  ? -26.417 -21.165 11.486 1.00 71.05  ? 301 LYS   B CE  1 
ATOM   638  N NZ  . LYS   A 1 86  ? -27.793 -20.582 11.340 1.00 68.90  ? 301 LYS   B NZ  1 
ATOM   639  N N   . PHE   A 1 87  ? -29.720 -18.945 14.959 1.00 57.62  ? 302 PHE   B N   1 
ATOM   640  C CA  . PHE   A 1 87  ? -31.094 -19.421 14.993 1.00 59.93  ? 302 PHE   B CA  1 
ATOM   641  C C   . PHE   A 1 87  ? -31.433 -20.205 13.721 1.00 60.66  ? 302 PHE   B C   1 
ATOM   642  O O   . PHE   A 1 87  ? -30.995 -19.853 12.620 1.00 54.81  ? 302 PHE   B O   1 
ATOM   643  C CB  . PHE   A 1 87  ? -32.066 -18.242 15.146 1.00 56.19  ? 302 PHE   B CB  1 
ATOM   644  C CG  . PHE   A 1 87  ? -32.366 -17.876 16.566 1.00 57.52  ? 302 PHE   B CG  1 
ATOM   645  C CD1 . PHE   A 1 87  ? -32.646 -18.855 17.512 1.00 61.10  ? 302 PHE   B CD1 1 
ATOM   646  C CD2 . PHE   A 1 87  ? -32.385 -16.549 16.960 1.00 57.19  ? 302 PHE   B CD2 1 
ATOM   647  C CE1 . PHE   A 1 87  ? -32.936 -18.512 18.825 1.00 57.22  ? 302 PHE   B CE1 1 
ATOM   648  C CE2 . PHE   A 1 87  ? -32.676 -16.202 18.264 1.00 57.71  ? 302 PHE   B CE2 1 
ATOM   649  C CZ  . PHE   A 1 87  ? -32.951 -17.183 19.195 1.00 57.61  ? 302 PHE   B CZ  1 
ATOM   650  N N   . TRP   A 1 88  ? -32.225 -21.263 13.880 1.00 59.39  ? 303 TRP   B N   1 
ATOM   651  C CA  . TRP   A 1 88  ? -32.977 -21.869 12.788 1.00 58.79  ? 303 TRP   B CA  1 
ATOM   652  C C   . TRP   A 1 88  ? -34.445 -21.512 12.989 1.00 55.98  ? 303 TRP   B C   1 
ATOM   653  O O   . TRP   A 1 88  ? -35.128 -22.092 13.833 1.00 58.98  ? 303 TRP   B O   1 
ATOM   654  C CB  . TRP   A 1 88  ? -32.753 -23.375 12.750 1.00 63.62  ? 303 TRP   B CB  1 
ATOM   655  C CG  . TRP   A 1 88  ? -31.408 -23.671 12.251 1.00 67.56  ? 303 TRP   B CG  1 
ATOM   656  C CD1 . TRP   A 1 88  ? -31.027 -23.802 10.947 1.00 61.36  ? 303 TRP   B CD1 1 
ATOM   657  C CD2 . TRP   A 1 88  ? -30.218 -23.799 13.036 1.00 67.48  ? 303 TRP   B CD2 1 
ATOM   658  N NE1 . TRP   A 1 88  ? -29.679 -24.027 10.877 1.00 60.41  ? 303 TRP   B NE1 1 
ATOM   659  C CE2 . TRP   A 1 88  ? -29.156 -24.042 12.142 1.00 64.76  ? 303 TRP   B CE2 1 
ATOM   660  C CE3 . TRP   A 1 88  ? -29.952 -23.752 14.407 1.00 62.20  ? 303 TRP   B CE3 1 
ATOM   661  C CZ2 . TRP   A 1 88  ? -27.846 -24.239 12.572 1.00 67.06  ? 303 TRP   B CZ2 1 
ATOM   662  C CZ3 . TRP   A 1 88  ? -28.652 -23.945 14.836 1.00 65.08  ? 303 TRP   B CZ3 1 
ATOM   663  C CH2 . TRP   A 1 88  ? -27.613 -24.187 13.916 1.00 73.61  ? 303 TRP   B CH2 1 
ATOM   664  N N   . ALA   A 1 89  ? -34.938 -20.569 12.213 1.00 51.39  ? 304 ALA   B N   1 
ATOM   665  C CA  . ALA   A 1 89  ? -36.273 -20.058 12.455 1.00 60.02  ? 304 ALA   B CA  1 
ATOM   666  C C   . ALA   A 1 89  ? -37.339 -21.033 11.952 1.00 60.54  ? 304 ALA   B C   1 
ATOM   667  O O   . ALA   A 1 89  ? -37.231 -21.573 10.854 1.00 62.66  ? 304 ALA   B O   1 
ATOM   668  C CB  . ALA   A 1 89  ? -36.424 -18.680 11.807 1.00 60.40  ? 304 ALA   B CB  1 
ATOM   669  N N   . ASP   A 1 90  ? -38.367 -21.276 12.763 1.00 63.07  ? 305 ASP   B N   1 
ATOM   670  C CA  . ASP   A 1 90  ? -39.554 -21.972 12.270 1.00 65.63  ? 305 ASP   B CA  1 
ATOM   671  C C   . ASP   A 1 90  ? -40.430 -20.936 11.588 1.00 66.28  ? 305 ASP   B C   1 
ATOM   672  O O   . ASP   A 1 90  ? -40.999 -20.065 12.255 1.00 63.41  ? 305 ASP   B O   1 
ATOM   673  C CB  . ASP   A 1 90  ? -40.297 -22.676 13.405 1.00 66.04  ? 305 ASP   B CB  1 
ATOM   674  C CG  . ASP   A 1 90  ? -41.489 -23.513 12.923 1.00 72.36  ? 305 ASP   B CG  1 
ATOM   675  O OD1 . ASP   A 1 90  ? -42.104 -23.181 11.880 1.00 73.22  ? 305 ASP   B OD1 1 
ATOM   676  O OD2 . ASP   A 1 90  ? -41.807 -24.527 13.596 1.00 74.89  ? 305 ASP   B OD2 1 
ATOM   677  N N   . LEU   A 1 91  ? -40.524 -21.008 10.257 1.00 69.65  ? 306 LEU   B N   1 
ATOM   678  C CA  . LEU   A 1 91  ? -41.327 -20.067 9.481  1.00 73.67  ? 306 LEU   B CA  1 
ATOM   679  C C   . LEU   A 1 91  ? -42.566 -20.689 8.843  1.00 80.38  ? 306 LEU   B C   1 
ATOM   680  O O   . LEU   A 1 91  ? -43.008 -20.222 7.790  1.00 79.64  ? 306 LEU   B O   1 
ATOM   681  C CB  . LEU   A 1 91  ? -40.523 -19.395 8.374  1.00 70.06  ? 306 LEU   B CB  1 
ATOM   682  C CG  . LEU   A 1 91  ? -39.182 -18.721 8.552  1.00 69.32  ? 306 LEU   B CG  1 
ATOM   683  C CD1 . LEU   A 1 91  ? -38.971 -17.992 7.255  1.00 73.25  ? 306 LEU   B CD1 1 
ATOM   684  C CD2 . LEU   A 1 91  ? -39.240 -17.753 9.697  1.00 67.87  ? 306 LEU   B CD2 1 
ATOM   685  N N   . ASN   A 1 92  ? -43.163 -21.703 9.459  1.00 82.31  ? 307 ASN   B N   1 
ATOM   686  C CA  . ASN   A 1 92  ? -44.364 -22.319 8.903  1.00 86.94  ? 307 ASN   B CA  1 
ATOM   687  C C   . ASN   A 1 92  ? -45.471 -22.218 9.949  1.00 84.20  ? 307 ASN   B C   1 
ATOM   688  O O   . ASN   A 1 92  ? -45.675 -23.146 10.736 1.00 83.52  ? 307 ASN   B O   1 
ATOM   689  C CB  . ASN   A 1 92  ? -44.086 -23.749 8.493  1.00 95.91  ? 307 ASN   B CB  1 
ATOM   690  C CG  . ASN   A 1 92  ? -45.191 -24.346 7.636  1.00 99.51  ? 307 ASN   B CG  1 
ATOM   691  O OD1 . ASN   A 1 92  ? -45.668 -23.720 6.683  1.00 95.72  ? 307 ASN   B OD1 1 
ATOM   692  N ND2 . ASN   A 1 92  ? -45.602 -25.570 7.973  1.00 99.54  ? 307 ASN   B ND2 1 
ATOM   693  N N   . TRP   A 1 93  ? -46.178 -21.087 9.949  1.00 86.59  ? 308 TRP   B N   1 
ATOM   694  C CA  . TRP   A 1 93  ? -47.236 -20.829 10.929 1.00 88.09  ? 308 TRP   B CA  1 
ATOM   695  C C   . TRP   A 1 93  ? -48.584 -20.603 10.251 1.00 91.04  ? 308 TRP   B C   1 
ATOM   696  O O   . TRP   A 1 93  ? -49.026 -21.412 9.435  1.00 93.19  ? 308 TRP   B O   1 
ATOM   697  C CB  . TRP   A 1 93  ? -46.900 -19.617 11.823 1.00 85.55  ? 308 TRP   B CB  1 
ATOM   698  C CG  . TRP   A 1 93  ? -46.695 -18.275 11.123 1.00 85.45  ? 308 TRP   B CG  1 
ATOM   699  C CD1 . TRP   A 1 93  ? -47.612 -17.264 11.017 1.00 85.46  ? 308 TRP   B CD1 1 
ATOM   700  C CD2 . TRP   A 1 93  ? -45.490 -17.791 10.472 1.00 86.77  ? 308 TRP   B CD2 1 
ATOM   701  N NE1 . TRP   A 1 93  ? -47.062 -16.195 10.329 1.00 88.19  ? 308 TRP   B NE1 1 
ATOM   702  C CE2 . TRP   A 1 93  ? -45.766 -16.491 9.986  1.00 87.85  ? 308 TRP   B CE2 1 
ATOM   703  C CE3 . TRP   A 1 93  ? -44.220 -18.332 10.243 1.00 85.17  ? 308 TRP   B CE3 1 
ATOM   704  C CZ2 . TRP   A 1 93  ? -44.809 -15.721 9.284  1.00 85.30  ? 308 TRP   B CZ2 1 
ATOM   705  C CZ3 . TRP   A 1 93  ? -43.268 -17.552 9.541  1.00 84.79  ? 308 TRP   B CZ3 1 
ATOM   706  C CH2 . TRP   A 1 93  ? -43.574 -16.272 9.077  1.00 83.46  ? 308 TRP   B CH2 1 
ATOM   707  N N   . SER   A 1 108 ? -51.755 -12.342 7.911  1.00 114.87 ? 323 SER   B N   1 
ATOM   708  C CA  . SER   A 1 108 ? -52.894 -13.136 8.363  1.00 116.80 ? 323 SER   B CA  1 
ATOM   709  C C   . SER   A 1 108 ? -53.592 -12.489 9.564  1.00 116.58 ? 323 SER   B C   1 
ATOM   710  O O   . SER   A 1 108 ? -54.548 -13.050 10.101 1.00 116.73 ? 323 SER   B O   1 
ATOM   711  C CB  . SER   A 1 108 ? -52.453 -14.564 8.710  1.00 121.93 ? 323 SER   B CB  1 
ATOM   712  O OG  . SER   A 1 108 ? -51.824 -15.198 7.605  1.00 119.93 ? 323 SER   B OG  1 
ATOM   713  N N   . GLY   A 1 109 ? -53.095 -11.320 9.982  1.00 106.92 ? 324 GLY   B N   1 
ATOM   714  C CA  . GLY   A 1 109 ? -53.776 -10.453 10.932 1.00 97.50  ? 324 GLY   B CA  1 
ATOM   715  C C   . GLY   A 1 109 ? -53.804 -10.892 12.388 1.00 98.41  ? 324 GLY   B C   1 
ATOM   716  O O   . GLY   A 1 109 ? -54.866 -10.844 13.025 1.00 95.76  ? 324 GLY   B O   1 
ATOM   717  N N   . GLY   A 1 110 ? -52.648 -11.303 12.928 1.00 89.89  ? 325 GLY   B N   1 
ATOM   718  C CA  . GLY   A 1 110 ? -52.541 -11.722 14.313 1.00 77.58  ? 325 GLY   B CA  1 
ATOM   719  C C   . GLY   A 1 110 ? -51.457 -10.946 15.046 1.00 71.45  ? 325 GLY   B C   1 
ATOM   720  O O   . GLY   A 1 110 ? -50.791 -10.085 14.469 1.00 76.85  ? 325 GLY   B O   1 
ATOM   721  N N   . PHE   A 1 111 ? -51.287 -11.279 16.332 1.00 65.58  ? 326 PHE   B N   1 
ATOM   722  C CA  . PHE   A 1 111 ? -50.398 -10.519 17.211 1.00 61.47  ? 326 PHE   B CA  1 
ATOM   723  C C   . PHE   A 1 111 ? -48.997 -11.114 17.210 1.00 56.63  ? 326 PHE   B C   1 
ATOM   724  O O   . PHE   A 1 111 ? -48.805 -12.267 17.619 1.00 57.78  ? 326 PHE   B O   1 
ATOM   725  C CB  . PHE   A 1 111 ? -50.912 -10.458 18.658 1.00 60.73  ? 326 PHE   B CB  1 
ATOM   726  C CG  . PHE   A 1 111 ? -49.855 -9.981  19.632 1.00 57.90  ? 326 PHE   B CG  1 
ATOM   727  C CD1 . PHE   A 1 111 ? -49.515 -8.638  19.700 1.00 57.98  ? 326 PHE   B CD1 1 
ATOM   728  C CD2 . PHE   A 1 111 ? -49.147 -10.885 20.416 1.00 56.40  ? 326 PHE   B CD2 1 
ATOM   729  C CE1 . PHE   A 1 111 ? -48.509 -8.210  20.539 1.00 56.09  ? 326 PHE   B CE1 1 
ATOM   730  C CE2 . PHE   A 1 111 ? -48.141 -10.458 21.269 1.00 54.57  ? 326 PHE   B CE2 1 
ATOM   731  C CZ  . PHE   A 1 111 ? -47.827 -9.120  21.336 1.00 55.02  ? 326 PHE   B CZ  1 
ATOM   732  N N   . TYR   A 1 112 ? -48.016 -10.303 16.820 1.00 56.34  ? 327 TYR   B N   1 
ATOM   733  C CA  . TYR   A 1 112 ? -46.613 -10.706 16.784 1.00 56.91  ? 327 TYR   B CA  1 
ATOM   734  C C   . TYR   A 1 112 ? -45.901 -10.123 17.993 1.00 54.19  ? 327 TYR   B C   1 
ATOM   735  O O   . TYR   A 1 112 ? -46.065 -8.934  18.285 1.00 55.77  ? 327 TYR   B O   1 
ATOM   736  C CB  . TYR   A 1 112 ? -45.933 -10.219 15.498 1.00 54.71  ? 327 TYR   B CB  1 
ATOM   737  C CG  . TYR   A 1 112 ? -46.377 -10.977 14.285 1.00 56.35  ? 327 TYR   B CG  1 
ATOM   738  C CD1 . TYR   A 1 112 ? -47.632 -10.750 13.721 1.00 55.56  ? 327 TYR   B CD1 1 
ATOM   739  C CD2 . TYR   A 1 112 ? -45.550 -11.951 13.710 1.00 54.15  ? 327 TYR   B CD2 1 
ATOM   740  C CE1 . TYR   A 1 112 ? -48.045 -11.469 12.613 1.00 58.74  ? 327 TYR   B CE1 1 
ATOM   741  C CE2 . TYR   A 1 112 ? -45.952 -12.662 12.608 1.00 52.35  ? 327 TYR   B CE2 1 
ATOM   742  C CZ  . TYR   A 1 112 ? -47.199 -12.417 12.063 1.00 57.28  ? 327 TYR   B CZ  1 
ATOM   743  O OH  . TYR   A 1 112 ? -47.628 -13.137 10.977 1.00 66.31  ? 327 TYR   B OH  1 
ATOM   744  N N   . GLY   A 1 113 ? -45.089 -10.933 18.670 1.00 48.46  ? 328 GLY   B N   1 
ATOM   745  C CA  . GLY   A 1 113 ? -44.495 -10.462 19.906 1.00 49.26  ? 328 GLY   B CA  1 
ATOM   746  C C   . GLY   A 1 113 ? -43.130 -11.036 20.195 1.00 51.13  ? 328 GLY   B C   1 
ATOM   747  O O   . GLY   A 1 113 ? -42.733 -12.075 19.658 1.00 54.76  ? 328 GLY   B O   1 
ATOM   748  N N   . VAL   A 1 114 ? -42.412 -10.322 21.064 1.00 52.34  ? 329 VAL   B N   1 
ATOM   749  C CA  . VAL   A 1 114 ? -41.110 -10.707 21.605 1.00 55.13  ? 329 VAL   B CA  1 
ATOM   750  C C   . VAL   A 1 114 ? -41.173 -10.632 23.136 1.00 59.51  ? 329 VAL   B C   1 
ATOM   751  O O   . VAL   A 1 114 ? -41.785 -9.712  23.700 1.00 58.52  ? 329 VAL   B O   1 
ATOM   752  C CB  . VAL   A 1 114 ? -39.986 -9.791  21.065 1.00 56.19  ? 329 VAL   B CB  1 
ATOM   753  C CG1 . VAL   A 1 114 ? -38.635 -10.379 21.344 1.00 56.18  ? 329 VAL   B CG1 1 
ATOM   754  C CG2 . VAL   A 1 114 ? -40.152 -9.525  19.572 1.00 57.58  ? 329 VAL   B CG2 1 
ATOM   755  N N   . SER   A 1 115 ? -40.546 -11.604 23.809 1.00 57.75  ? 330 SER   B N   1 
ATOM   756  C CA  . SER   A 1 115 ? -40.460 -11.638 25.269 1.00 60.37  ? 330 SER   B CA  1 
ATOM   757  C C   . SER   A 1 115 ? -39.025 -11.903 25.694 1.00 61.02  ? 330 SER   B C   1 
ATOM   758  O O   . SER   A 1 115 ? -38.396 -12.833 25.188 1.00 61.64  ? 330 SER   B O   1 
ATOM   759  C CB  . SER   A 1 115 ? -41.364 -12.720 25.875 1.00 57.77  ? 330 SER   B CB  1 
ATOM   760  O OG  . SER   A 1 115 ? -42.732 -12.370 25.840 1.00 56.68  ? 330 SER   B OG  1 
ATOM   761  N N   . SER   A 1 116 ? -38.512 -11.106 26.625 1.00 64.53  ? 331 SER   B N   1 
ATOM   762  C CA  . SER   A 1 116 ? -37.193 -11.343 27.190 1.00 64.64  ? 331 SER   B CA  1 
ATOM   763  C C   . SER   A 1 116 ? -37.307 -11.404 28.706 1.00 68.13  ? 331 SER   B C   1 
ATOM   764  O O   . SER   A 1 116 ? -38.150 -10.727 29.312 1.00 70.92  ? 331 SER   B O   1 
ATOM   765  C CB  . SER   A 1 116 ? -36.196 -10.250 26.807 1.00 65.54  ? 331 SER   B CB  1 
ATOM   766  O OG  . SER   A 1 116 ? -36.043 -10.119 25.395 1.00 70.24  ? 331 SER   B OG  1 
ATOM   767  N N   . GLN   A 1 117 ? -36.446 -12.210 29.324 1.00 63.96  ? 332 GLN   B N   1 
ATOM   768  C CA  . GLN   A 1 117 ? -36.404 -12.283 30.773 1.00 59.83  ? 332 GLN   B CA  1 
ATOM   769  C C   . GLN   A 1 117 ? -34.971 -12.485 31.234 1.00 58.37  ? 332 GLN   B C   1 
ATOM   770  O O   . GLN   A 1 117 ? -34.257 -13.343 30.704 1.00 58.37  ? 332 GLN   B O   1 
ATOM   771  C CB  . GLN   A 1 117 ? -37.311 -13.405 31.272 1.00 64.25  ? 332 GLN   B CB  1 
ATOM   772  C CG  . GLN   A 1 117 ? -37.537 -13.428 32.764 1.00 64.37  ? 332 GLN   B CG  1 
ATOM   773  C CD  . GLN   A 1 117 ? -38.916 -13.945 33.096 1.00 69.32  ? 332 GLN   B CD  1 
ATOM   774  O OE1 . GLN   A 1 117 ? -39.691 -14.285 32.197 1.00 73.68  ? 332 GLN   B OE1 1 
ATOM   775  N NE2 . GLN   A 1 117 ? -39.238 -14.001 34.382 1.00 70.40  ? 332 GLN   B NE2 1 
ATOM   776  N N   . TYR   A 1 118 ? -34.557 -11.695 32.220 1.00 56.65  ? 333 TYR   B N   1 
ATOM   777  C CA  . TYR   A 1 118 ? -33.214 -11.761 32.774 1.00 60.83  ? 333 TYR   B CA  1 
ATOM   778  C C   . TYR   A 1 118 ? -33.282 -11.843 34.297 1.00 63.50  ? 333 TYR   B C   1 
ATOM   779  O O   . TYR   A 1 118 ? -34.248 -11.400 34.916 1.00 63.75  ? 333 TYR   B O   1 
ATOM   780  C CB  . TYR   A 1 118 ? -32.372 -10.542 32.349 1.00 58.56  ? 333 TYR   B CB  1 
ATOM   781  C CG  . TYR   A 1 118 ? -32.377 -10.259 30.850 1.00 63.26  ? 333 TYR   B CG  1 
ATOM   782  C CD1 . TYR   A 1 118 ? -33.415 -9.541  30.257 1.00 63.50  ? 333 TYR   B CD1 1 
ATOM   783  C CD2 . TYR   A 1 118 ? -31.340 -10.698 30.025 1.00 60.12  ? 333 TYR   B CD2 1 
ATOM   784  C CE1 . TYR   A 1 118 ? -33.433 -9.292  28.890 1.00 59.42  ? 333 TYR   B CE1 1 
ATOM   785  C CE2 . TYR   A 1 118 ? -31.353 -10.433 28.660 1.00 60.04  ? 333 TYR   B CE2 1 
ATOM   786  C CZ  . TYR   A 1 118 ? -32.403 -9.728  28.105 1.00 58.71  ? 333 TYR   B CZ  1 
ATOM   787  O OH  . TYR   A 1 118 ? -32.433 -9.449  26.759 1.00 61.94  ? 333 TYR   B OH  1 
ATOM   788  N N   . GLU   A 1 119 ? -32.242 -12.407 34.894 1.00 63.85  ? 334 GLU   B N   1 
ATOM   789  C CA  . GLU   A 1 119 ? -32.085 -12.453 36.332 1.00 66.06  ? 334 GLU   B CA  1 
ATOM   790  C C   . GLU   A 1 119 ? -30.754 -11.846 36.739 1.00 69.10  ? 334 GLU   B C   1 
ATOM   791  O O   . GLU   A 1 119 ? -29.797 -11.814 35.968 1.00 67.15  ? 334 GLU   B O   1 
ATOM   792  C CB  . GLU   A 1 119 ? -32.141 -13.877 36.845 1.00 73.16  ? 334 GLU   B CB  1 
ATOM   793  C CG  . GLU   A 1 119 ? -33.473 -14.511 36.698 1.00 79.15  ? 334 GLU   B CG  1 
ATOM   794  C CD  . GLU   A 1 119 ? -33.639 -15.635 37.671 1.00 88.57  ? 334 GLU   B CD  1 
ATOM   795  O OE1 . GLU   A 1 119 ? -32.894 -15.623 38.673 1.00 90.89  ? 334 GLU   B OE1 1 
ATOM   796  O OE2 . GLU   A 1 119 ? -34.477 -16.531 37.419 1.00 88.89  ? 334 GLU   B OE2 1 
ATOM   797  N N   . SER   A 1 120 ? -30.686 -11.395 37.982 1.00 71.26  ? 335 SER   B N   1 
ATOM   798  C CA  . SER   A 1 120 ? -29.445 -10.833 38.474 1.00 69.91  ? 335 SER   B CA  1 
ATOM   799  C C   . SER   A 1 120 ? -29.284 -11.160 39.948 1.00 77.33  ? 335 SER   B C   1 
ATOM   800  O O   . SER   A 1 120 ? -30.245 -11.495 40.648 1.00 79.41  ? 335 SER   B O   1 
ATOM   801  C CB  . SER   A 1 120 ? -29.400 -9.324  38.271 1.00 69.02  ? 335 SER   B CB  1 
ATOM   802  O OG  . SER   A 1 120 ? -28.277 -8.792  38.939 1.00 74.53  ? 335 SER   B OG  1 
ATOM   803  N N   . LEU   A 1 121 ? -28.047 -11.059 40.416 1.00 77.74  ? 336 LEU   B N   1 
ATOM   804  C CA  . LEU   A 1 121 ? -27.871 -11.079 41.857 1.00 75.49  ? 336 LEU   B CA  1 
ATOM   805  C C   . LEU   A 1 121 ? -28.051 -9.687  42.443 1.00 74.49  ? 336 LEU   B C   1 
ATOM   806  O O   . LEU   A 1 121 ? -28.659 -9.534  43.503 1.00 81.40  ? 336 LEU   B O   1 
ATOM   807  C CB  . LEU   A 1 121 ? -26.498 -11.648 42.215 1.00 75.53  ? 336 LEU   B CB  1 
ATOM   808  C CG  . LEU   A 1 121 ? -26.450 -13.177 42.283 1.00 76.87  ? 336 LEU   B CG  1 
ATOM   809  C CD1 . LEU   A 1 121 ? -25.336 -13.647 43.222 1.00 74.50  ? 336 LEU   B CD1 1 
ATOM   810  C CD2 . LEU   A 1 121 ? -27.816 -13.784 42.666 1.00 73.01  ? 336 LEU   B CD2 1 
ATOM   811  N N   . GLU   A 1 122 ? -27.564 -8.666  41.753 1.00 76.26  ? 337 GLU   B N   1 
ATOM   812  C CA  . GLU   A 1 122 ? -27.723 -7.293  42.190 1.00 76.99  ? 337 GLU   B CA  1 
ATOM   813  C C   . GLU   A 1 122 ? -28.908 -6.636  41.485 1.00 77.44  ? 337 GLU   B C   1 
ATOM   814  O O   . GLU   A 1 122 ? -29.447 -7.133  40.493 1.00 77.46  ? 337 GLU   B O   1 
ATOM   815  C CB  . GLU   A 1 122 ? -26.444 -6.504  41.934 1.00 75.75  ? 337 GLU   B CB  1 
ATOM   816  C CG  . GLU   A 1 122 ? -25.723 -6.975  40.701 1.00 81.25  ? 337 GLU   B CG  1 
ATOM   817  C CD  . GLU   A 1 122 ? -24.499 -6.154  40.411 1.00 83.50  ? 337 GLU   B CD  1 
ATOM   818  O OE1 . GLU   A 1 122 ? -24.345 -5.094  41.078 1.00 80.92  ? 337 GLU   B OE1 1 
ATOM   819  O OE2 . GLU   A 1 122 ? -23.727 -6.561  39.500 1.00 78.33  ? 337 GLU   B OE2 1 
ATOM   820  N N   . HIS   A 1 123 ? -29.303 -5.495  42.024 1.00 76.86  ? 338 HIS   B N   1 
ATOM   821  C CA  . HIS   A 1 123 ? -30.505 -4.777  41.627 1.00 75.35  ? 338 HIS   B CA  1 
ATOM   822  C C   . HIS   A 1 123 ? -30.110 -3.637  40.695 1.00 74.11  ? 338 HIS   B C   1 
ATOM   823  O O   . HIS   A 1 123 ? -29.427 -2.690  41.105 1.00 75.90  ? 338 HIS   B O   1 
ATOM   824  C CB  . HIS   A 1 123 ? -31.219 -4.256  42.872 1.00 74.78  ? 338 HIS   B CB  1 
ATOM   825  C CG  . HIS   A 1 123 ? -32.251 -3.219  42.587 1.00 75.54  ? 338 HIS   B CG  1 
ATOM   826  N ND1 . HIS   A 1 123 ? -33.557 -3.538  42.289 1.00 79.93  ? 338 HIS   B ND1 1 
ATOM   827  C CD2 . HIS   A 1 123 ? -32.182 -1.869  42.582 1.00 76.20  ? 338 HIS   B CD2 1 
ATOM   828  C CE1 . HIS   A 1 123 ? -34.245 -2.430  42.088 1.00 79.11  ? 338 HIS   B CE1 1 
ATOM   829  N NE2 . HIS   A 1 123 ? -33.434 -1.403  42.261 1.00 81.46  ? 338 HIS   B NE2 1 
ATOM   830  N N   . MET   A 1 124 ? -30.519 -3.723  39.443 1.00 70.28  ? 339 MET   B N   1 
ATOM   831  C CA  . MET   A 1 124 ? -30.166 -2.675  38.506 1.00 71.78  ? 339 MET   B CA  1 
ATOM   832  C C   . MET   A 1 124 ? -31.378 -2.268  37.685 1.00 68.24  ? 339 MET   B C   1 
ATOM   833  O O   . MET   A 1 124 ? -32.462 -2.849  37.785 1.00 68.42  ? 339 MET   B O   1 
ATOM   834  C CB  . MET   A 1 124 ? -28.974 -3.094  37.626 1.00 73.37  ? 339 MET   B CB  1 
ATOM   835  C CG  . MET   A 1 124 ? -28.030 -4.097  38.309 1.00 75.88  ? 339 MET   B CG  1 
ATOM   836  S SD  . MET   A 1 124 ? -26.842 -4.937  37.238 1.00 70.88  ? 339 MET   B SD  1 
ATOM   837  C CE  . MET   A 1 124 ? -27.933 -5.990  36.291 1.00 66.14  ? 339 MET   B CE  1 
ATOM   838  N N   . THR   A 1 125 ? -31.199 -1.185  36.946 1.00 68.65  ? 340 THR   B N   1 
ATOM   839  C CA  . THR   A 1 125 ? -32.153 -0.751  35.940 1.00 70.72  ? 340 THR   B CA  1 
ATOM   840  C C   . THR   A 1 125 ? -31.479 -1.045  34.612 1.00 71.79  ? 340 THR   B C   1 
ATOM   841  O O   . THR   A 1 125 ? -30.444 -0.447  34.300 1.00 72.95  ? 340 THR   B O   1 
ATOM   842  C CB  . THR   A 1 125 ? -32.505 0.732   36.060 1.00 75.47  ? 340 THR   B CB  1 
ATOM   843  O OG1 . THR   A 1 125 ? -32.476 1.138   37.427 1.00 80.61  ? 340 THR   B OG1 1 
ATOM   844  C CG2 . THR   A 1 125 ? -33.908 0.976   35.538 1.00 76.62  ? 340 THR   B CG2 1 
ATOM   845  N N   . LEU   A 1 126 ? -32.041 -1.987  33.858 1.00 70.55  ? 341 LEU   B N   1 
ATOM   846  C CA  . LEU   A 1 126 ? -31.475 -2.390  32.577 1.00 66.24  ? 341 LEU   B CA  1 
ATOM   847  C C   . LEU   A 1 126 ? -31.948 -1.470  31.458 1.00 66.67  ? 341 LEU   B C   1 
ATOM   848  O O   . LEU   A 1 126 ? -33.083 -0.985  31.468 1.00 66.95  ? 341 LEU   B O   1 
ATOM   849  C CB  . LEU   A 1 126 ? -31.878 -3.826  32.255 1.00 62.58  ? 341 LEU   B CB  1 
ATOM   850  C CG  . LEU   A 1 126 ? -31.505 -4.862  33.306 1.00 56.71  ? 341 LEU   B CG  1 
ATOM   851  C CD1 . LEU   A 1 126 ? -31.791 -6.273  32.811 1.00 52.51  ? 341 LEU   B CD1 1 
ATOM   852  C CD2 . LEU   A 1 126 ? -30.054 -4.696  33.703 1.00 59.09  ? 341 LEU   B CD2 1 
ATOM   853  N N   . THR   A 1 127 ? -31.068 -1.221  30.494 1.00 66.46  ? 342 THR   B N   1 
ATOM   854  C CA  . THR   A 1 127 ? -31.476 -0.688  29.202 1.00 63.44  ? 342 THR   B CA  1 
ATOM   855  C C   . THR   A 1 127 ? -31.176 -1.726  28.141 1.00 60.39  ? 342 THR   B C   1 
ATOM   856  O O   . THR   A 1 127 ? -30.105 -2.338  28.138 1.00 59.80  ? 342 THR   B O   1 
ATOM   857  C CB  . THR   A 1 127 ? -30.811 0.641   28.857 1.00 64.17  ? 342 THR   B CB  1 
ATOM   858  O OG1 . THR   A 1 127 ? -30.778 1.491   30.010 1.00 69.07  ? 342 THR   B OG1 1 
ATOM   859  C CG2 . THR   A 1 127 ? -31.592 1.315   27.763 1.00 62.85  ? 342 THR   B CG2 1 
ATOM   860  N N   . CYS   A 1 128 ? -32.134 -1.933  27.258 1.00 59.54  ? 343 CYS   B N   1 
ATOM   861  C CA  . CYS   A 1 128 ? -32.146 -3.096  26.394 1.00 57.77  ? 343 CYS   B CA  1 
ATOM   862  C C   . CYS   A 1 128 ? -32.336 -2.604  24.971 1.00 62.20  ? 343 CYS   B C   1 
ATOM   863  O O   . CYS   A 1 128 ? -33.418 -2.108  24.638 1.00 62.09  ? 343 CYS   B O   1 
ATOM   864  C CB  . CYS   A 1 128 ? -33.273 -4.020  26.812 1.00 61.68  ? 343 CYS   B CB  1 
ATOM   865  S SG  . CYS   A 1 128 ? -32.852 -4.992  28.242 1.00 67.03  ? 343 CYS   B SG  1 
ATOM   866  N N   . SER   A 1 129 ? -31.292 -2.716  24.143 1.00 58.05  ? 344 SER   B N   1 
ATOM   867  C CA  . SER   A 1 129 ? -31.331 -2.221  22.772 1.00 60.99  ? 344 SER   B CA  1 
ATOM   868  C C   . SER   A 1 129 ? -31.407 -3.382  21.798 1.00 57.26  ? 344 SER   B C   1 
ATOM   869  O O   . SER   A 1 129 ? -30.610 -4.316  21.878 1.00 61.39  ? 344 SER   B O   1 
ATOM   870  C CB  . SER   A 1 129 ? -30.111 -1.356  22.439 1.00 62.42  ? 344 SER   B CB  1 
ATOM   871  O OG  . SER   A 1 129 ? -29.270 -2.004  21.488 1.00 66.45  ? 344 SER   B OG  1 
ATOM   872  N N   . SER   A 1 130 ? -32.333 -3.296  20.862 1.00 58.36  ? 345 SER   B N   1 
ATOM   873  C CA  . SER   A 1 130 ? -32.450 -4.252  19.771 1.00 62.98  ? 345 SER   B CA  1 
ATOM   874  C C   . SER   A 1 130 ? -32.244 -3.555  18.428 1.00 60.11  ? 345 SER   B C   1 
ATOM   875  O O   . SER   A 1 130 ? -33.194 -3.018  17.856 1.00 61.19  ? 345 SER   B O   1 
ATOM   876  C CB  . SER   A 1 130 ? -33.807 -4.931  19.828 1.00 62.30  ? 345 SER   B CB  1 
ATOM   877  O OG  . SER   A 1 130 ? -33.745 -6.000  20.732 1.00 63.30  ? 345 SER   B OG  1 
ATOM   878  N N   . LYS   A 1 131 ? -31.017 -3.586  17.910 1.00 61.46  ? 346 LYS   B N   1 
ATOM   879  C CA  . LYS   A 1 131 ? -30.728 -3.106  16.556 1.00 63.91  ? 346 LYS   B CA  1 
ATOM   880  C C   . LYS   A 1 131 ? -30.901 -4.233  15.538 1.00 60.02  ? 346 LYS   B C   1 
ATOM   881  O O   . LYS   A 1 131 ? -30.159 -5.218  15.568 1.00 56.75  ? 346 LYS   B O   1 
ATOM   882  C CB  . LYS   A 1 131 ? -29.312 -2.541  16.466 1.00 66.81  ? 346 LYS   B CB  1 
ATOM   883  C CG  . LYS   A 1 131 ? -28.919 -1.622  17.615 1.00 75.05  ? 346 LYS   B CG  1 
ATOM   884  C CD  . LYS   A 1 131 ? -27.686 -0.793  17.243 1.00 83.29  ? 346 LYS   B CD  1 
ATOM   885  C CE  . LYS   A 1 131 ? -27.529 0.404   18.181 1.00 87.57  ? 346 LYS   B CE  1 
ATOM   886  N NZ  . LYS   A 1 131 ? -26.663 0.089   19.363 1.00 88.40  ? 346 LYS   B NZ  1 
ATOM   887  N N   . VAL   A 1 132 ? -31.872 -4.083  14.639 1.00 61.00  ? 347 VAL   B N   1 
ATOM   888  C CA  . VAL   A 1 132 ? -32.037 -4.978  13.497 1.00 63.97  ? 347 VAL   B CA  1 
ATOM   889  C C   . VAL   A 1 132 ? -31.272 -4.418  12.305 1.00 65.81  ? 347 VAL   B C   1 
ATOM   890  O O   . VAL   A 1 132 ? -31.490 -3.272  11.906 1.00 64.30  ? 347 VAL   B O   1 
ATOM   891  C CB  . VAL   A 1 132 ? -33.519 -5.148  13.139 1.00 64.99  ? 347 VAL   B CB  1 
ATOM   892  C CG1 . VAL   A 1 132 ? -33.651 -5.991  11.841 1.00 64.97  ? 347 VAL   B CG1 1 
ATOM   893  C CG2 . VAL   A 1 132 ? -34.271 -5.762  14.297 1.00 60.00  ? 347 VAL   B CG2 1 
ATOM   894  N N   . CYS   A 1 133 ? -30.396 -5.231  11.714 1.00 66.70  ? 348 CYS   B N   1 
ATOM   895  C CA  . CYS   A 1 133 ? -29.548 -4.782  10.618 1.00 71.08  ? 348 CYS   B CA  1 
ATOM   896  C C   . CYS   A 1 133 ? -29.806 -5.604  9.361  1.00 71.82  ? 348 CYS   B C   1 
ATOM   897  O O   . CYS   A 1 133 ? -29.887 -6.832  9.414  1.00 66.84  ? 348 CYS   B O   1 
ATOM   898  C CB  . CYS   A 1 133 ? -28.070 -4.875  10.983 1.00 75.25  ? 348 CYS   B CB  1 
ATOM   899  S SG  . CYS   A 1 133 ? -27.632 -4.226  12.597 1.00 72.85  ? 348 CYS   B SG  1 
ATOM   900  N N   . SER   A 1 134 ? -29.919 -4.920  8.225  1.00 79.20  ? 349 SER   B N   1 
ATOM   901  C CA  . SER   A 1 134 ? -29.973 -5.558  6.915  1.00 81.18  ? 349 SER   B CA  1 
ATOM   902  C C   . SER   A 1 134 ? -28.716 -5.200  6.135  1.00 84.97  ? 349 SER   B C   1 
ATOM   903  O O   . SER   A 1 134 ? -28.500 -4.026  5.807  1.00 87.11  ? 349 SER   B O   1 
ATOM   904  C CB  . SER   A 1 134 ? -31.208 -5.127  6.133  1.00 82.88  ? 349 SER   B CB  1 
ATOM   905  O OG  . SER   A 1 134 ? -30.903 -5.086  4.747  1.00 89.10  ? 349 SER   B OG  1 
ATOM   906  N N   . PHE   A 1 135 ? -27.913 -6.214  5.807  1.00 79.05  ? 350 PHE   B N   1 
ATOM   907  C CA  . PHE   A 1 135 ? -26.592 -6.012  5.212  1.00 81.27  ? 350 PHE   B CA  1 
ATOM   908  C C   . PHE   A 1 135 ? -25.667 -5.232  6.146  1.00 87.76  ? 350 PHE   B C   1 
ATOM   909  O O   . PHE   A 1 135 ? -24.779 -4.511  5.689  1.00 93.59  ? 350 PHE   B O   1 
ATOM   910  C CB  . PHE   A 1 135 ? -26.668 -5.289  3.861  1.00 82.54  ? 350 PHE   B CB  1 
ATOM   911  C CG  . PHE   A 1 135 ? -27.181 -6.132  2.729  1.00 79.69  ? 350 PHE   B CG  1 
ATOM   912  C CD1 . PHE   A 1 135 ? -28.544 -6.234  2.479  1.00 79.72  ? 350 PHE   B CD1 1 
ATOM   913  C CD2 . PHE   A 1 135 ? -26.294 -6.804  1.896  1.00 76.82  ? 350 PHE   B CD2 1 
ATOM   914  C CE1 . PHE   A 1 135 ? -29.015 -7.006  1.418  1.00 76.88  ? 350 PHE   B CE1 1 
ATOM   915  C CE2 . PHE   A 1 135 ? -26.754 -7.581  0.843  1.00 75.24  ? 350 PHE   B CE2 1 
ATOM   916  C CZ  . PHE   A 1 135 ? -28.119 -7.683  0.602  1.00 74.20  ? 350 PHE   B CZ  1 
ATOM   917  N N   . GLY   A 1 136 ? -25.869 -5.338  7.456  1.00 86.45  ? 351 GLY   B N   1 
ATOM   918  C CA  . GLY   A 1 136 ? -25.038 -4.598  8.384  1.00 94.01  ? 351 GLY   B CA  1 
ATOM   919  C C   . GLY   A 1 136 ? -25.409 -3.140  8.594  1.00 97.31  ? 351 GLY   B C   1 
ATOM   920  O O   . GLY   A 1 136 ? -24.805 -2.487  9.458  1.00 106.73 ? 351 GLY   B O   1 
ATOM   921  N N   . LYS   A 1 137 ? -26.361 -2.601  7.832  1.00 89.22  ? 352 LYS   B N   1 
ATOM   922  C CA  . LYS   A 1 137 ? -26.869 -1.259  8.073  1.00 85.68  ? 352 LYS   B CA  1 
ATOM   923  C C   . LYS   A 1 137 ? -27.945 -1.337  9.151  1.00 83.41  ? 352 LYS   B C   1 
ATOM   924  O O   . LYS   A 1 137 ? -28.835 -2.193  9.084  1.00 79.63  ? 352 LYS   B O   1 
ATOM   925  C CB  . LYS   A 1 137 ? -27.413 -0.644  6.780  1.00 82.15  ? 352 LYS   B CB  1 
ATOM   926  C CG  . LYS   A 1 137 ? -28.923 -0.796  6.559  1.00 83.36  ? 352 LYS   B CG  1 
ATOM   927  C CD  . LYS   A 1 137 ? -29.320 -0.791  5.080  1.00 90.10  ? 352 LYS   B CD  1 
ATOM   928  C CE  . LYS   A 1 137 ? -30.646 -0.039  4.829  1.00 92.02  ? 352 LYS   B CE  1 
ATOM   929  N NZ  . LYS   A 1 137 ? -30.503 1.448   4.664  1.00 92.29  ? 352 LYS   B NZ  1 
ATOM   930  N N   . GLN   A 1 138 ? -27.827 -0.484  10.176 1.00 86.34  ? 353 GLN   B N   1 
ATOM   931  C CA  . GLN   A 1 138 ? -28.838 -0.417  11.231 1.00 82.71  ? 353 GLN   B CA  1 
ATOM   932  C C   . GLN   A 1 138 ? -30.147 0.075   10.630 1.00 82.09  ? 353 GLN   B C   1 
ATOM   933  O O   . GLN   A 1 138 ? -30.223 1.215   10.159 1.00 88.24  ? 353 GLN   B O   1 
ATOM   934  C CB  . GLN   A 1 138 ? -28.383 0.507   12.360 1.00 83.20  ? 353 GLN   B CB  1 
ATOM   935  C CG  . GLN   A 1 138 ? -29.040 0.219   13.694 1.00 83.03  ? 353 GLN   B CG  1 
ATOM   936  C CD  . GLN   A 1 138 ? -29.882 1.378   14.199 1.00 84.05  ? 353 GLN   B CD  1 
ATOM   937  O OE1 . GLN   A 1 138 ? -29.501 2.067   15.151 1.00 85.91  ? 353 GLN   B OE1 1 
ATOM   938  N NE2 . GLN   A 1 138 ? -31.037 1.596   13.569 1.00 80.57  ? 353 GLN   B NE2 1 
ATOM   939  N N   . VAL   A 1 139 ? -31.163 -0.781  10.618 1.00 71.22  ? 354 VAL   B N   1 
ATOM   940  C CA  . VAL   A 1 139 ? -32.413 -0.519  9.908  1.00 68.27  ? 354 VAL   B CA  1 
ATOM   941  C C   . VAL   A 1 139 ? -33.492 -0.052  10.854 1.00 67.85  ? 354 VAL   B C   1 
ATOM   942  O O   . VAL   A 1 139 ? -34.206 0.908   10.579 1.00 66.82  ? 354 VAL   B O   1 
ATOM   943  C CB  . VAL   A 1 139 ? -32.863 -1.784  9.142  1.00 68.00  ? 354 VAL   B CB  1 
ATOM   944  C CG1 . VAL   A 1 139 ? -34.285 -1.636  8.612  1.00 59.75  ? 354 VAL   B CG1 1 
ATOM   945  C CG2 . VAL   A 1 139 ? -31.898 -2.105  8.034  1.00 75.76  ? 354 VAL   B CG2 1 
ATOM   946  N N   . VAL   A 1 140 ? -33.618 -0.737  11.975 1.00 69.51  ? 355 VAL   B N   1 
ATOM   947  C CA  . VAL   A 1 140 ? -34.649 -0.495  12.969 1.00 66.99  ? 355 VAL   B CA  1 
ATOM   948  C C   . VAL   A 1 140 ? -34.045 -0.771  14.343 1.00 66.53  ? 355 VAL   B C   1 
ATOM   949  O O   . VAL   A 1 140 ? -33.240 -1.694  14.514 1.00 62.26  ? 355 VAL   B O   1 
ATOM   950  C CB  . VAL   A 1 140 ? -35.898 -1.353  12.680 1.00 64.73  ? 355 VAL   B CB  1 
ATOM   951  C CG1 . VAL   A 1 140 ? -36.644 -1.656  13.948 1.00 67.52  ? 355 VAL   B CG1 1 
ATOM   952  C CG2 . VAL   A 1 140 ? -36.823 -0.595  11.738 1.00 67.11  ? 355 VAL   B CG2 1 
ATOM   953  N N   . GLU   A 1 141 ? -34.386 0.078   15.306 1.00 67.95  ? 356 GLU   B N   1 
ATOM   954  C CA  . GLU   A 1 141 ? -33.874 -0.039  16.659 1.00 66.24  ? 356 GLU   B CA  1 
ATOM   955  C C   . GLU   A 1 141 ? -35.021 0.135   17.645 1.00 62.35  ? 356 GLU   B C   1 
ATOM   956  O O   . GLU   A 1 141 ? -35.909 0.964   17.438 1.00 63.26  ? 356 GLU   B O   1 
ATOM   957  C CB  . GLU   A 1 141 ? -32.769 1.002   16.913 1.00 68.94  ? 356 GLU   B CB  1 
ATOM   958  C CG  . GLU   A 1 141 ? -31.954 0.762   18.165 1.00 67.17  ? 356 GLU   B CG  1 
ATOM   959  C CD  . GLU   A 1 141 ? -30.961 1.868   18.435 1.00 75.65  ? 356 GLU   B CD  1 
ATOM   960  O OE1 . GLU   A 1 141 ? -30.921 2.861   17.673 1.00 77.62  ? 356 GLU   B OE1 1 
ATOM   961  O OE2 . GLU   A 1 141 ? -30.216 1.751   19.428 1.00 79.54  ? 356 GLU   B OE2 1 
ATOM   962  N N   . LYS   A 1 142 ? -35.014 -0.667  18.699 1.00 64.14  ? 357 LYS   B N   1 
ATOM   963  C CA  . LYS   A 1 142 ? -35.907 -0.465  19.830 1.00 65.49  ? 357 LYS   B CA  1 
ATOM   964  C C   . LYS   A 1 142 ? -35.070 -0.429  21.098 1.00 62.06  ? 357 LYS   B C   1 
ATOM   965  O O   . LYS   A 1 142 ? -34.142 -1.223  21.254 1.00 59.85  ? 357 LYS   B O   1 
ATOM   966  C CB  . LYS   A 1 142 ? -36.975 -1.553  19.915 1.00 61.87  ? 357 LYS   B CB  1 
ATOM   967  C CG  . LYS   A 1 142 ? -37.756 -1.531  21.221 1.00 72.95  ? 357 LYS   B CG  1 
ATOM   968  C CD  . LYS   A 1 142 ? -39.222 -1.190  20.988 1.00 79.54  ? 357 LYS   B CD  1 
ATOM   969  C CE  . LYS   A 1 142 ? -40.010 -1.145  22.290 1.00 81.99  ? 357 LYS   B CE  1 
ATOM   970  N NZ  . LYS   A 1 142 ? -41.486 -1.095  22.063 1.00 88.23  ? 357 LYS   B NZ  1 
ATOM   971  N N   . VAL   A 1 143 ? -35.357 0.534   21.972 1.00 65.61  ? 358 VAL   B N   1 
ATOM   972  C CA  . VAL   A 1 143 ? -34.660 0.659   23.244 1.00 65.35  ? 358 VAL   B CA  1 
ATOM   973  C C   . VAL   A 1 143 ? -35.702 0.690   24.345 1.00 66.29  ? 358 VAL   B C   1 
ATOM   974  O O   . VAL   A 1 143 ? -36.616 1.520   24.315 1.00 66.29  ? 358 VAL   B O   1 
ATOM   975  C CB  . VAL   A 1 143 ? -33.770 1.911   23.319 1.00 61.66  ? 358 VAL   B CB  1 
ATOM   976  C CG1 . VAL   A 1 143 ? -32.876 1.817   24.526 1.00 62.85  ? 358 VAL   B CG1 1 
ATOM   977  C CG2 . VAL   A 1 143 ? -32.935 2.044   22.092 1.00 63.54  ? 358 VAL   B CG2 1 
ATOM   978  N N   . GLU   A 1 144 ? -35.565 -0.213  25.308 1.00 72.58  ? 359 GLU   B N   1 
ATOM   979  C CA  . GLU   A 1 144 ? -36.453 -0.291  26.457 1.00 73.43  ? 359 GLU   B CA  1 
ATOM   980  C C   . GLU   A 1 144 ? -35.620 -0.271  27.722 1.00 71.44  ? 359 GLU   B C   1 
ATOM   981  O O   . GLU   A 1 144 ? -34.431 -0.593  27.712 1.00 72.95  ? 359 GLU   B O   1 
ATOM   982  C CB  . GLU   A 1 144 ? -37.314 -1.560  26.423 1.00 73.31  ? 359 GLU   B CB  1 
ATOM   983  C CG  . GLU   A 1 144 ? -38.385 -1.504  25.360 1.00 79.08  ? 359 GLU   B CG  1 
ATOM   984  C CD  . GLU   A 1 144 ? -39.310 -2.698  25.373 1.00 84.36  ? 359 GLU   B CD  1 
ATOM   985  O OE1 . GLU   A 1 144 ? -39.005 -3.710  24.686 1.00 81.89  ? 359 GLU   B OE1 1 
ATOM   986  O OE2 . GLU   A 1 144 ? -40.352 -2.605  26.065 1.00 87.69  ? 359 GLU   B OE2 1 
ATOM   987  N N   . THR   A 1 145 ? -36.256 0.115   28.813 1.00 64.91  ? 360 THR   B N   1 
ATOM   988  C CA  . THR   A 1 145 ? -35.653 0.004   30.126 1.00 66.19  ? 360 THR   B CA  1 
ATOM   989  C C   . THR   A 1 145 ? -36.536 -0.865  31.013 1.00 67.89  ? 360 THR   B C   1 
ATOM   990  O O   . THR   A 1 145 ? -37.755 -0.930  30.835 1.00 70.25  ? 360 THR   B O   1 
ATOM   991  C CB  . THR   A 1 145 ? -35.443 1.373   30.730 1.00 63.36  ? 360 THR   B CB  1 
ATOM   992  O OG1 . THR   A 1 145 ? -36.715 2.027   30.810 1.00 68.82  ? 360 THR   B OG1 1 
ATOM   993  C CG2 . THR   A 1 145 ? -34.474 2.191   29.882 1.00 63.29  ? 360 THR   B CG2 1 
ATOM   994  N N   . GLU   A 1 146 ? -35.916 -1.577  31.945 1.00 66.34  ? 361 GLU   B N   1 
ATOM   995  C CA  . GLU   A 1 146 ? -36.686 -2.398  32.870 1.00 69.82  ? 361 GLU   B CA  1 
ATOM   996  C C   . GLU   A 1 146 ? -36.038 -2.342  34.243 1.00 74.15  ? 361 GLU   B C   1 
ATOM   997  O O   . GLU   A 1 146 ? -34.852 -2.664  34.394 1.00 71.48  ? 361 GLU   B O   1 
ATOM   998  C CB  . GLU   A 1 146 ? -36.810 -3.843  32.382 1.00 65.86  ? 361 GLU   B CB  1 
ATOM   999  C CG  . GLU   A 1 146 ? -37.544 -4.777  33.342 1.00 66.58  ? 361 GLU   B CG  1 
ATOM   1000 C CD  . GLU   A 1 146 ? -39.042 -4.481  33.458 1.00 68.51  ? 361 GLU   B CD  1 
ATOM   1001 O OE1 . GLU   A 1 146 ? -39.606 -3.819  32.555 1.00 70.61  ? 361 GLU   B OE1 1 
ATOM   1002 O OE2 . GLU   A 1 146 ? -39.660 -4.944  34.446 1.00 68.29  ? 361 GLU   B OE2 1 
ATOM   1003 N N   . ARG   A 1 147 ? -36.825 -1.910  35.227 1.00 72.33  ? 362 ARG   B N   1 
ATOM   1004 C CA  . ARG   A 1 147 ? -36.413 -1.913  36.618 1.00 72.05  ? 362 ARG   B CA  1 
ATOM   1005 C C   . ARG   A 1 147 ? -36.485 -3.330  37.174 1.00 71.26  ? 362 ARG   B C   1 
ATOM   1006 O O   . ARG   A 1 147 ? -37.389 -4.095  36.830 1.00 72.74  ? 362 ARG   B O   1 
ATOM   1007 C CB  . ARG   A 1 147 ? -37.324 -0.975  37.415 1.00 77.79  ? 362 ARG   B CB  1 
ATOM   1008 C CG  . ARG   A 1 147 ? -36.643 -0.119  38.446 1.00 78.17  ? 362 ARG   B CG  1 
ATOM   1009 C CD  . ARG   A 1 147 ? -36.929 -0.683  39.808 1.00 86.03  ? 362 ARG   B CD  1 
ATOM   1010 N NE  . ARG   A 1 147 ? -36.735 0.300   40.867 1.00 96.22  ? 362 ARG   B NE  1 
ATOM   1011 C CZ  . ARG   A 1 147 ? -36.760 0.011   42.162 1.00 92.76  ? 362 ARG   B CZ  1 
ATOM   1012 N NH1 . ARG   A 1 147 ? -37.046 -1.214  42.591 1.00 89.37  ? 362 ARG   B NH1 1 
ATOM   1013 N NH2 . ARG   A 1 147 ? -36.491 0.971   43.046 1.00 93.28  ? 362 ARG   B NH2 1 
ATOM   1014 N N   . ALA   A 1 148 ? -35.522 -3.682  38.025 1.00 66.97  ? 363 ALA   B N   1 
ATOM   1015 C CA  . ALA   A 1 148 ? -35.546 -4.980  38.696 1.00 71.51  ? 363 ALA   B CA  1 
ATOM   1016 C C   . ALA   A 1 148 ? -36.790 -5.130  39.578 1.00 77.40  ? 363 ALA   B C   1 
ATOM   1017 O O   . ALA   A 1 148 ? -37.289 -4.166  40.164 1.00 78.21  ? 363 ALA   B O   1 
ATOM   1018 C CB  . ALA   A 1 148 ? -34.283 -5.159  39.547 1.00 69.37  ? 363 ALA   B CB  1 
ATOM   1019 N N   . GLN   A 1 149 ? -37.300 -6.355  39.670 1.00 74.12  ? 364 GLN   B N   1 
ATOM   1020 C CA  . GLN   A 1 149 ? -38.300 -6.703  40.673 1.00 74.76  ? 364 GLN   B CA  1 
ATOM   1021 C C   . GLN   A 1 149 ? -37.778 -7.880  41.476 1.00 77.39  ? 364 GLN   B C   1 
ATOM   1022 O O   . GLN   A 1 149 ? -37.426 -8.918  40.906 1.00 76.01  ? 364 GLN   B O   1 
ATOM   1023 C CB  . GLN   A 1 149 ? -39.670 -7.025  40.070 1.00 75.03  ? 364 GLN   B CB  1 
ATOM   1024 C CG  . GLN   A 1 149 ? -40.187 -5.975  39.095 1.00 73.98  ? 364 GLN   B CG  1 
ATOM   1025 C CD  . GLN   A 1 149 ? -41.333 -6.501  38.216 1.00 81.43  ? 364 GLN   B CD  1 
ATOM   1026 O OE1 . GLN   A 1 149 ? -41.131 -7.053  37.095 1.00 72.25  ? 364 GLN   B OE1 1 
ATOM   1027 N NE2 . GLN   A 1 149 ? -42.559 -6.328  38.732 1.00 71.47  ? 364 GLN   B NE2 1 
ATOM   1028 N N   . LEU   A 1 150 ? -37.718 -7.695  42.798 1.00 86.48  ? 365 LEU   B N   1 
ATOM   1029 C CA  . LEU   A 1 150 ? -37.158 -8.677  43.717 1.00 85.89  ? 365 LEU   B CA  1 
ATOM   1030 C C   . LEU   A 1 150 ? -38.072 -9.886  43.792 1.00 87.61  ? 365 LEU   B C   1 
ATOM   1031 O O   . LEU   A 1 150 ? -39.263 -9.752  44.079 1.00 83.62  ? 365 LEU   B O   1 
ATOM   1032 C CB  . LEU   A 1 150 ? -36.981 -8.054  45.097 1.00 82.13  ? 365 LEU   B CB  1 
ATOM   1033 C CG  . LEU   A 1 150 ? -36.095 -8.769  46.119 1.00 86.92  ? 365 LEU   B CG  1 
ATOM   1034 C CD1 . LEU   A 1 150 ? -34.934 -9.481  45.434 1.00 88.05  ? 365 LEU   B CD1 1 
ATOM   1035 C CD2 . LEU   A 1 150 ? -35.593 -7.788  47.205 1.00 80.07  ? 365 LEU   B CD2 1 
ATOM   1036 N N   . GLU   A 1 151 ? -37.524 -11.062 43.503 1.00 96.94  ? 366 GLU   B N   1 
ATOM   1037 C CA  . GLU   A 1 151 ? -38.273 -12.296 43.683 1.00 96.76  ? 366 GLU   B CA  1 
ATOM   1038 C C   . GLU   A 1 151 ? -37.487 -13.207 44.613 1.00 102.71 ? 366 GLU   B C   1 
ATOM   1039 O O   . GLU   A 1 151 ? -36.849 -12.712 45.547 1.00 105.77 ? 366 GLU   B O   1 
ATOM   1040 C CB  . GLU   A 1 151 ? -38.584 -12.930 42.333 1.00 95.23  ? 366 GLU   B CB  1 
ATOM   1041 C CG  . GLU   A 1 151 ? -39.172 -11.893 41.395 1.00 97.27  ? 366 GLU   B CG  1 
ATOM   1042 C CD  . GLU   A 1 151 ? -40.470 -12.315 40.754 1.00 101.04 ? 366 GLU   B CD  1 
ATOM   1043 O OE1 . GLU   A 1 151 ? -40.494 -13.377 40.087 1.00 100.10 ? 366 GLU   B OE1 1 
ATOM   1044 O OE2 . GLU   A 1 151 ? -41.469 -11.577 40.931 1.00 100.86 ? 366 GLU   B OE2 1 
ATOM   1045 N N   . ASP   A 1 152 ? -37.512 -14.519 44.386 1.00 108.71 ? 367 ASP   B N   1 
ATOM   1046 C CA  . ASP   A 1 152 ? -37.066 -15.473 45.407 1.00 112.84 ? 367 ASP   B CA  1 
ATOM   1047 C C   . ASP   A 1 152 ? -35.567 -15.322 45.670 1.00 115.91 ? 367 ASP   B C   1 
ATOM   1048 O O   . ASP   A 1 152 ? -34.730 -16.058 45.142 1.00 118.63 ? 367 ASP   B O   1 
ATOM   1049 C CB  . ASP   A 1 152 ? -37.415 -16.898 44.994 1.00 111.43 ? 367 ASP   B CB  1 
ATOM   1050 C CG  . ASP   A 1 152 ? -37.108 -17.915 46.086 1.00 119.73 ? 367 ASP   B CG  1 
ATOM   1051 O OD1 . ASP   A 1 152 ? -37.393 -17.638 47.282 1.00 114.16 ? 367 ASP   B OD1 1 
ATOM   1052 O OD2 . ASP   A 1 152 ? -36.593 -19.002 45.745 1.00 123.99 ? 367 ASP   B OD2 1 
ATOM   1053 N N   . GLY   A 1 153 ? -35.226 -14.355 46.530 1.00 111.44 ? 368 GLY   B N   1 
ATOM   1054 C CA  . GLY   A 1 153 ? -33.846 -14.050 46.885 1.00 111.11 ? 368 GLY   B CA  1 
ATOM   1055 C C   . GLY   A 1 153 ? -33.023 -13.351 45.818 1.00 111.99 ? 368 GLY   B C   1 
ATOM   1056 O O   . GLY   A 1 153 ? -31.886 -12.939 46.105 1.00 109.75 ? 368 GLY   B O   1 
ATOM   1057 N N   . ARG   A 1 154 ? -33.558 -13.192 44.607 1.00 105.31 ? 369 ARG   B N   1 
ATOM   1058 C CA  . ARG   A 1 154 ? -32.841 -12.673 43.461 1.00 97.26  ? 369 ARG   B CA  1 
ATOM   1059 C C   . ARG   A 1 154 ? -33.729 -11.661 42.756 1.00 94.94  ? 369 ARG   B C   1 
ATOM   1060 O O   . ARG   A 1 154 ? -34.938 -11.595 42.987 1.00 94.95  ? 369 ARG   B O   1 
ATOM   1061 C CB  . ARG   A 1 154 ? -32.449 -13.809 42.503 1.00 100.63 ? 369 ARG   B CB  1 
ATOM   1062 C CG  . ARG   A 1 154 ? -33.626 -14.711 42.101 1.00 101.76 ? 369 ARG   B CG  1 
ATOM   1063 C CD  . ARG   A 1 154 ? -33.166 -16.089 41.612 1.00 105.01 ? 369 ARG   B CD  1 
ATOM   1064 N NE  . ARG   A 1 154 ? -34.246 -16.824 40.955 1.00 107.43 ? 369 ARG   B NE  1 
ATOM   1065 C CZ  . ARG   A 1 154 ? -34.086 -17.924 40.222 1.00 106.32 ? 369 ARG   B CZ  1 
ATOM   1066 N NH1 . ARG   A 1 154 ? -32.892 -18.478 40.053 1.00 103.16 ? 369 ARG   B NH1 1 
ATOM   1067 N NH2 . ARG   A 1 154 ? -35.149 -18.477 39.637 1.00 103.78 ? 369 ARG   B NH2 1 
ATOM   1068 N N   . PHE   A 1 155 ? -33.115 -10.881 41.876 1.00 86.51  ? 370 PHE   B N   1 
ATOM   1069 C CA  . PHE   A 1 155 ? -33.815 -9.871  41.101 1.00 81.51  ? 370 PHE   B CA  1 
ATOM   1070 C C   . PHE   A 1 155 ? -34.182 -10.423 39.734 1.00 75.80  ? 370 PHE   B C   1 
ATOM   1071 O O   . PHE   A 1 155 ? -33.487 -11.279 39.185 1.00 76.33  ? 370 PHE   B O   1 
ATOM   1072 C CB  . PHE   A 1 155 ? -32.956 -8.620  40.956 1.00 78.10  ? 370 PHE   B CB  1 
ATOM   1073 C CG  . PHE   A 1 155 ? -32.607 -8.008  42.256 1.00 79.96  ? 370 PHE   B CG  1 
ATOM   1074 C CD1 . PHE   A 1 155 ? -33.551 -7.275  42.960 1.00 81.70  ? 370 PHE   B CD1 1 
ATOM   1075 C CD2 . PHE   A 1 155 ? -31.358 -8.203  42.812 1.00 79.15  ? 370 PHE   B CD2 1 
ATOM   1076 C CE1 . PHE   A 1 155 ? -33.242 -6.720  44.193 1.00 78.73  ? 370 PHE   B CE1 1 
ATOM   1077 C CE2 . PHE   A 1 155 ? -31.042 -7.651  44.042 1.00 78.31  ? 370 PHE   B CE2 1 
ATOM   1078 C CZ  . PHE   A 1 155 ? -31.988 -6.915  44.736 1.00 74.98  ? 370 PHE   B CZ  1 
ATOM   1079 N N   . VAL   A 1 156 ? -35.286 -9.926  39.188 1.00 70.84  ? 371 VAL   B N   1 
ATOM   1080 C CA  . VAL   A 1 156 ? -35.847 -10.460 37.956 1.00 68.55  ? 371 VAL   B CA  1 
ATOM   1081 C C   . VAL   A 1 156 ? -36.260 -9.302  37.058 1.00 67.42  ? 371 VAL   B C   1 
ATOM   1082 O O   . VAL   A 1 156 ? -36.809 -8.298  37.532 1.00 68.22  ? 371 VAL   B O   1 
ATOM   1083 C CB  . VAL   A 1 156 ? -37.043 -11.383 38.245 1.00 75.10  ? 371 VAL   B CB  1 
ATOM   1084 C CG1 . VAL   A 1 156 ? -37.938 -11.496 37.010 1.00 72.32  ? 371 VAL   B CG1 1 
ATOM   1085 C CG2 . VAL   A 1 156 ? -36.548 -12.740 38.713 1.00 79.15  ? 371 VAL   B CG2 1 
ATOM   1086 N N   . TYR   A 1 157 ? -35.994 -9.446  35.756 1.00 63.68  ? 372 TYR   B N   1 
ATOM   1087 C CA  . TYR   A 1 157 ? -36.281 -8.405  34.777 1.00 62.26  ? 372 TYR   B CA  1 
ATOM   1088 C C   . TYR   A 1 157 ? -37.117 -8.994  33.653 1.00 59.29  ? 372 TYR   B C   1 
ATOM   1089 O O   . TYR   A 1 157 ? -36.728 -9.991  33.050 1.00 62.53  ? 372 TYR   B O   1 
ATOM   1090 C CB  . TYR   A 1 157 ? -34.998 -7.810  34.236 1.00 57.92  ? 372 TYR   B CB  1 
ATOM   1091 C CG  . TYR   A 1 157 ? -33.955 -7.467  35.270 1.00 57.34  ? 372 TYR   B CG  1 
ATOM   1092 C CD1 . TYR   A 1 157 ? -33.175 -8.457  35.854 1.00 60.32  ? 372 TYR   B CD1 1 
ATOM   1093 C CD2 . TYR   A 1 157 ? -33.701 -6.145  35.614 1.00 54.87  ? 372 TYR   B CD2 1 
ATOM   1094 C CE1 . TYR   A 1 157 ? -32.197 -8.145  36.771 1.00 62.45  ? 372 TYR   B CE1 1 
ATOM   1095 C CE2 . TYR   A 1 157 ? -32.710 -5.821  36.512 1.00 56.13  ? 372 TYR   B CE2 1 
ATOM   1096 C CZ  . TYR   A 1 157 ? -31.968 -6.821  37.095 1.00 62.68  ? 372 TYR   B CZ  1 
ATOM   1097 O OH  . TYR   A 1 157 ? -30.992 -6.500  38.006 1.00 68.12  ? 372 TYR   B OH  1 
ATOM   1098 N N   . ARG   A 1 158 ? -38.258 -8.376  33.370 1.00 59.09  ? 373 ARG   B N   1 
ATOM   1099 C CA  . ARG   A 1 158 ? -39.304 -8.990  32.565 1.00 60.00  ? 373 ARG   B CA  1 
ATOM   1100 C C   . ARG   A 1 158 ? -39.749 -8.002  31.502 1.00 62.22  ? 373 ARG   B C   1 
ATOM   1101 O O   . ARG   A 1 158 ? -40.386 -6.991  31.817 1.00 62.09  ? 373 ARG   B O   1 
ATOM   1102 C CB  . ARG   A 1 158 ? -40.491 -9.418  33.425 1.00 60.50  ? 373 ARG   B CB  1 
ATOM   1103 C CG  . ARG   A 1 158 ? -40.402 -10.834 33.960 1.00 64.05  ? 373 ARG   B CG  1 
ATOM   1104 C CD  . ARG   A 1 158 ? -41.754 -11.294 34.495 1.00 70.27  ? 373 ARG   B CD  1 
ATOM   1105 N NE  . ARG   A 1 158 ? -41.623 -12.204 35.625 1.00 74.69  ? 373 ARG   B NE  1 
ATOM   1106 C CZ  . ARG   A 1 158 ? -41.332 -11.821 36.863 1.00 77.86  ? 373 ARG   B CZ  1 
ATOM   1107 N NH1 . ARG   A 1 158 ? -41.158 -10.547 37.170 1.00 79.01  ? 373 ARG   B NH1 1 
ATOM   1108 N NH2 . ARG   A 1 158 ? -41.199 -12.741 37.815 1.00 81.83  ? 373 ARG   B NH2 1 
ATOM   1109 N N   . LEU   A 1 159 ? -39.441 -8.319  30.249 1.00 61.56  ? 374 LEU   B N   1 
ATOM   1110 C CA  . LEU   A 1 159 ? -39.865 -7.536  29.094 1.00 61.93  ? 374 LEU   B CA  1 
ATOM   1111 C C   . LEU   A 1 159 ? -40.743 -8.422  28.205 1.00 59.47  ? 374 LEU   B C   1 
ATOM   1112 O O   . LEU   A 1 159 ? -40.408 -8.725  27.058 1.00 65.58  ? 374 LEU   B O   1 
ATOM   1113 C CB  . LEU   A 1 159 ? -38.633 -6.987  28.352 1.00 63.56  ? 374 LEU   B CB  1 
ATOM   1114 C CG  . LEU   A 1 159 ? -37.659 -6.205  29.243 1.00 63.54  ? 374 LEU   B CG  1 
ATOM   1115 C CD1 . LEU   A 1 159 ? -36.514 -7.079  29.753 1.00 58.83  ? 374 LEU   B CD1 1 
ATOM   1116 C CD2 . LEU   A 1 159 ? -37.131 -4.968  28.530 1.00 65.65  ? 374 LEU   B CD2 1 
ATOM   1117 N N   . LEU   A 1 160 ? -41.875 -8.847  28.743 1.00 60.16  ? 375 LEU   B N   1 
ATOM   1118 C CA  . LEU   A 1 160 ? -42.696 -9.841  28.072 1.00 61.35  ? 375 LEU   B CA  1 
ATOM   1119 C C   . LEU   A 1 160 ? -43.594 -9.196  27.034 1.00 57.75  ? 375 LEU   B C   1 
ATOM   1120 O O   . LEU   A 1 160 ? -44.130 -8.106  27.242 1.00 56.34  ? 375 LEU   B O   1 
ATOM   1121 C CB  . LEU   A 1 160 ? -43.563 -10.607 29.076 1.00 59.94  ? 375 LEU   B CB  1 
ATOM   1122 C CG  . LEU   A 1 160 ? -42.764 -11.159 30.243 1.00 60.32  ? 375 LEU   B CG  1 
ATOM   1123 C CD1 . LEU   A 1 160 ? -43.606 -11.154 31.526 1.00 63.61  ? 375 LEU   B CD1 1 
ATOM   1124 C CD2 . LEU   A 1 160 ? -42.208 -12.524 29.891 1.00 57.33  ? 375 LEU   B CD2 1 
ATOM   1125 N N   . ARG   A 1 161 ? -43.747 -9.883  25.908 1.00 59.03  ? 376 ARG   B N   1 
ATOM   1126 C CA  . ARG   A 1 161 ? -44.822 -9.618  24.960 1.00 58.76  ? 376 ARG   B CA  1 
ATOM   1127 C C   . ARG   A 1 161 ? -44.699 -8.254  24.298 1.00 57.76  ? 376 ARG   B C   1 
ATOM   1128 O O   . ARG   A 1 161 ? -45.717 -7.670  23.905 1.00 57.28  ? 376 ARG   B O   1 
ATOM   1129 C CB  . ARG   A 1 161 ? -46.196 -9.763  25.631 1.00 52.66  ? 376 ARG   B CB  1 
ATOM   1130 C CG  . ARG   A 1 161 ? -46.554 -11.180 25.970 1.00 52.96  ? 376 ARG   B CG  1 
ATOM   1131 C CD  . ARG   A 1 161 ? -47.930 -11.300 26.514 1.00 56.42  ? 376 ARG   B CD  1 
ATOM   1132 N NE  . ARG   A 1 161 ? -48.948 -10.660 25.695 1.00 58.33  ? 376 ARG   B NE  1 
ATOM   1133 C CZ  . ARG   A 1 161 ? -49.612 -11.271 24.724 1.00 59.16  ? 376 ARG   B CZ  1 
ATOM   1134 N NH1 . ARG   A 1 161 ? -49.327 -12.510 24.378 1.00 60.82  ? 376 ARG   B NH1 1 
ATOM   1135 N NH2 . ARG   A 1 161 ? -50.595 -10.624 24.094 1.00 61.33  ? 376 ARG   B NH2 1 
ATOM   1136 N N   . SER   A 1 162 ? -43.472 -7.726  24.183 1.00 58.51  ? 377 SER   B N   1 
ATOM   1137 C CA  . SER   A 1 162 ? -43.296 -6.488  23.429 1.00 57.28  ? 377 SER   B CA  1 
ATOM   1138 C C   . SER   A 1 162 ? -43.831 -6.725  22.025 1.00 57.40  ? 377 SER   B C   1 
ATOM   1139 O O   . SER   A 1 162 ? -43.556 -7.774  21.435 1.00 59.98  ? 377 SER   B O   1 
ATOM   1140 C CB  . SER   A 1 162 ? -41.828 -6.041  23.341 1.00 58.97  ? 377 SER   B CB  1 
ATOM   1141 O OG  . SER   A 1 162 ? -41.072 -6.241  24.525 1.00 58.07  ? 377 SER   B OG  1 
ATOM   1142 N N   . PRO   A 1 163 ? -44.623 -5.814  21.475 1.00 55.04  ? 378 PRO   B N   1 
ATOM   1143 C CA  . PRO   A 1 163 ? -45.093 -6.000  20.091 1.00 57.40  ? 378 PRO   B CA  1 
ATOM   1144 C C   . PRO   A 1 163 ? -43.937 -5.854  19.107 1.00 58.16  ? 378 PRO   B C   1 
ATOM   1145 O O   . PRO   A 1 163 ? -43.158 -4.902  19.195 1.00 60.31  ? 378 PRO   B O   1 
ATOM   1146 C CB  . PRO   A 1 163 ? -46.133 -4.891  19.918 1.00 58.08  ? 378 PRO   B CB  1 
ATOM   1147 C CG  . PRO   A 1 163 ? -46.368 -4.349  21.358 1.00 56.16  ? 378 PRO   B CG  1 
ATOM   1148 C CD  . PRO   A 1 163 ? -45.063 -4.535  22.035 1.00 55.18  ? 378 PRO   B CD  1 
ATOM   1149 N N   . MET   A 1 164 ? -43.804 -6.833  18.200 1.00 60.04  ? 379 MET   B N   1 
ATOM   1150 C CA  . MET   A 1 164 ? -42.788 -6.785  17.151 1.00 56.19  ? 379 MET   B CA  1 
ATOM   1151 C C   . MET   A 1 164 ? -42.940 -5.513  16.330 1.00 57.60  ? 379 MET   B C   1 
ATOM   1152 O O   . MET   A 1 164 ? -44.062 -5.095  16.018 1.00 59.94  ? 379 MET   B O   1 
ATOM   1153 C CB  . MET   A 1 164 ? -42.915 -8.005  16.247 1.00 54.60  ? 379 MET   B CB  1 
ATOM   1154 C CG  . MET   A 1 164 ? -41.589 -8.536  15.811 1.00 61.29  ? 379 MET   B CG  1 
ATOM   1155 S SD  . MET   A 1 164 ? -41.680 -10.292 15.376 1.00 60.21  ? 379 MET   B SD  1 
ATOM   1156 C CE  . MET   A 1 164 ? -42.762 -10.293 14.002 1.00 53.74  ? 379 MET   B CE  1 
ATOM   1157 N N   . CYS   A 1 165 ? -41.808 -4.873  16.005 1.00 60.43  ? 380 CYS   B N   1 
ATOM   1158 C CA  . CYS   A 1 165 ? -41.858 -3.696  15.133 1.00 65.52  ? 380 CYS   B CA  1 
ATOM   1159 C C   . CYS   A 1 165 ? -42.284 -4.099  13.731 1.00 60.25  ? 380 CYS   B C   1 
ATOM   1160 O O   . CYS   A 1 165 ? -41.893 -5.155  13.231 1.00 57.48  ? 380 CYS   B O   1 
ATOM   1161 C CB  . CYS   A 1 165 ? -40.517 -2.977  15.054 1.00 63.04  ? 380 CYS   B CB  1 
ATOM   1162 S SG  . CYS   A 1 165 ? -39.142 -4.039  15.225 1.00 69.56  ? 380 CYS   B SG  1 
ATOM   1163 N N   . GLU   A 1 166 ? -43.091 -3.238  13.103 1.00 61.64  ? 381 GLU   B N   1 
ATOM   1164 C CA  . GLU   A 1 166 ? -43.799 -3.594  11.886 1.00 64.55  ? 381 GLU   B CA  1 
ATOM   1165 C C   . GLU   A 1 166 ? -42.844 -3.975  10.747 1.00 66.69  ? 381 GLU   B C   1 
ATOM   1166 O O   . GLU   A 1 166 ? -43.231 -4.725  9.842  1.00 64.74  ? 381 GLU   B O   1 
ATOM   1167 C CB  . GLU   A 1 166 ? -44.721 -2.434  11.530 1.00 70.26  ? 381 GLU   B CB  1 
ATOM   1168 C CG  . GLU   A 1 166 ? -45.899 -2.815  10.658 1.00 81.48  ? 381 GLU   B CG  1 
ATOM   1169 C CD  . GLU   A 1 166 ? -46.092 -1.881  9.450  1.00 90.68  ? 381 GLU   B CD  1 
ATOM   1170 O OE1 . GLU   A 1 166 ? -45.246 -0.978  9.237  1.00 93.69  ? 381 GLU   B OE1 1 
ATOM   1171 O OE2 . GLU   A 1 166 ? -47.084 -2.064  8.697  1.00 94.50  ? 381 GLU   B OE2 1 
ATOM   1172 N N   . TYR   A 1 167 ? -41.587 -3.530  10.813 1.00 65.88  ? 382 TYR   B N   1 
ATOM   1173 C CA  . TYR   A 1 167 ? -40.583 -3.959  9.850  1.00 60.71  ? 382 TYR   B CA  1 
ATOM   1174 C C   . TYR   A 1 167 ? -40.325 -5.450  9.956  1.00 61.71  ? 382 TYR   B C   1 
ATOM   1175 O O   . TYR   A 1 167 ? -40.236 -6.154  8.940  1.00 65.31  ? 382 TYR   B O   1 
ATOM   1176 C CB  . TYR   A 1 167 ? -39.275 -3.196  10.061 1.00 63.39  ? 382 TYR   B CB  1 
ATOM   1177 C CG  . TYR   A 1 167 ? -38.203 -3.646  9.095  1.00 68.89  ? 382 TYR   B CG  1 
ATOM   1178 C CD1 . TYR   A 1 167 ? -38.276 -3.324  7.737  1.00 68.90  ? 382 TYR   B CD1 1 
ATOM   1179 C CD2 . TYR   A 1 167 ? -37.152 -4.452  9.516  1.00 71.94  ? 382 TYR   B CD2 1 
ATOM   1180 C CE1 . TYR   A 1 167 ? -37.314 -3.757  6.845  1.00 65.08  ? 382 TYR   B CE1 1 
ATOM   1181 C CE2 . TYR   A 1 167 ? -36.186 -4.894  8.620  1.00 65.79  ? 382 TYR   B CE2 1 
ATOM   1182 C CZ  . TYR   A 1 167 ? -36.274 -4.535  7.302  1.00 64.03  ? 382 TYR   B CZ  1 
ATOM   1183 O OH  . TYR   A 1 167 ? -35.315 -4.967  6.431  1.00 70.13  ? 382 TYR   B OH  1 
ATOM   1184 N N   . LEU   A 1 168 ? -40.154 -5.946  11.177 1.00 61.26  ? 383 LEU   B N   1 
ATOM   1185 C CA  . LEU   A 1 168 ? -39.955 -7.381  11.356 1.00 61.08  ? 383 LEU   B CA  1 
ATOM   1186 C C   . LEU   A 1 168 ? -41.189 -8.180  10.956 1.00 58.51  ? 383 LEU   B C   1 
ATOM   1187 O O   . LEU   A 1 168 ? -41.071 -9.227  10.315 1.00 56.60  ? 383 LEU   B O   1 
ATOM   1188 C CB  . LEU   A 1 168 ? -39.576 -7.688  12.797 1.00 64.40  ? 383 LEU   B CB  1 
ATOM   1189 C CG  . LEU   A 1 168 ? -38.071 -7.822  12.933 1.00 67.30  ? 383 LEU   B CG  1 
ATOM   1190 C CD1 . LEU   A 1 168 ? -37.714 -8.388  14.317 1.00 63.06  ? 383 LEU   B CD1 1 
ATOM   1191 C CD2 . LEU   A 1 168 ? -37.558 -8.690  11.787 1.00 68.09  ? 383 LEU   B CD2 1 
ATOM   1192 N N   . VAL   A 1 169 ? -42.383 -7.721  11.333 1.00 62.03  ? 384 VAL   B N   1 
ATOM   1193 C CA  . VAL   A 1 169 ? -43.585 -8.461  10.951 1.00 63.74  ? 384 VAL   B CA  1 
ATOM   1194 C C   . VAL   A 1 169 ? -43.675 -8.571  9.438  1.00 62.82  ? 384 VAL   B C   1 
ATOM   1195 O O   . VAL   A 1 169 ? -43.957 -9.643  8.898  1.00 62.69  ? 384 VAL   B O   1 
ATOM   1196 C CB  . VAL   A 1 169 ? -44.852 -7.811  11.533 1.00 57.77  ? 384 VAL   B CB  1 
ATOM   1197 C CG1 . VAL   A 1 169 ? -46.064 -8.597  11.094 1.00 55.09  ? 384 VAL   B CG1 1 
ATOM   1198 C CG2 . VAL   A 1 169 ? -44.779 -7.760  13.031 1.00 54.82  ? 384 VAL   B CG2 1 
ATOM   1199 N N   . ASN   A 1 170 ? -43.443 -7.453  8.736  1.00 72.09  ? 385 ASN   B N   1 
ATOM   1200 C CA  . ASN   A 1 170 ? -43.566 -7.434  7.280  1.00 73.79  ? 385 ASN   B CA  1 
ATOM   1201 C C   . ASN   A 1 170 ? -42.466 -8.258  6.627  1.00 74.65  ? 385 ASN   B C   1 
ATOM   1202 O O   . ASN   A 1 170 ? -42.730 -9.023  5.691  1.00 77.59  ? 385 ASN   B O   1 
ATOM   1203 C CB  . ASN   A 1 170 ? -43.528 -5.996  6.762  1.00 76.43  ? 385 ASN   B CB  1 
ATOM   1204 C CG  . ASN   A 1 170 ? -44.871 -5.295  6.909  1.00 84.53  ? 385 ASN   B CG  1 
ATOM   1205 O OD1 . ASN   A 1 170 ? -45.910 -5.954  7.030  1.00 86.77  ? 385 ASN   B OD1 1 
ATOM   1206 N ND2 . ASN   A 1 170 ? -44.862 -3.952  6.898  1.00 84.50  ? 385 ASN   B ND2 1 
ATOM   1207 N N   . PHE   A 1 171 ? -41.232 -8.125  7.120  1.00 62.63  ? 386 PHE   B N   1 
ATOM   1208 C CA  . PHE   A 1 171 ? -40.138 -8.976  6.662  1.00 60.74  ? 386 PHE   B CA  1 
ATOM   1209 C C   . PHE   A 1 171 ? -40.493 -10.448 6.714  1.00 61.48  ? 386 PHE   B C   1 
ATOM   1210 O O   . PHE   A 1 171 ? -40.005 -11.225 5.898  1.00 63.40  ? 386 PHE   B O   1 
ATOM   1211 C CB  . PHE   A 1 171 ? -38.895 -8.717  7.510  1.00 63.32  ? 386 PHE   B CB  1 
ATOM   1212 C CG  . PHE   A 1 171 ? -37.723 -9.610  7.182  1.00 61.42  ? 386 PHE   B CG  1 
ATOM   1213 C CD1 . PHE   A 1 171 ? -36.933 -9.365  6.066  1.00 65.28  ? 386 PHE   B CD1 1 
ATOM   1214 C CD2 . PHE   A 1 171 ? -37.375 -10.653 8.015  1.00 61.98  ? 386 PHE   B CD2 1 
ATOM   1215 C CE1 . PHE   A 1 171 ? -35.835 -10.161 5.768  1.00 63.93  ? 386 PHE   B CE1 1 
ATOM   1216 C CE2 . PHE   A 1 171 ? -36.274 -11.458 7.728  1.00 63.74  ? 386 PHE   B CE2 1 
ATOM   1217 C CZ  . PHE   A 1 171 ? -35.503 -11.204 6.595  1.00 63.74  ? 386 PHE   B CZ  1 
ATOM   1218 N N   . LEU   A 1 172 ? -41.344 -10.851 7.655  1.00 65.00  ? 387 LEU   B N   1 
ATOM   1219 C CA  . LEU   A 1 172 ? -41.627 -12.266 7.851  1.00 64.53  ? 387 LEU   B CA  1 
ATOM   1220 C C   . LEU   A 1 172 ? -42.677 -12.775 6.870  1.00 64.60  ? 387 LEU   B C   1 
ATOM   1221 O O   . LEU   A 1 172 ? -42.587 -13.917 6.415  1.00 66.48  ? 387 LEU   B O   1 
ATOM   1222 C CB  . LEU   A 1 172 ? -42.077 -12.518 9.298  1.00 67.73  ? 387 LEU   B CB  1 
ATOM   1223 C CG  . LEU   A 1 172 ? -41.042 -12.489 10.433 1.00 63.32  ? 387 LEU   B CG  1 
ATOM   1224 C CD1 . LEU   A 1 172 ? -41.660 -12.992 11.717 1.00 57.43  ? 387 LEU   B CD1 1 
ATOM   1225 C CD2 . LEU   A 1 172 ? -39.761 -13.253 10.128 1.00 58.69  ? 387 LEU   B CD2 1 
ATOM   1226 N N   . HIS   A 1 173 ? -43.692 -11.963 6.554  1.00 61.72  ? 388 HIS   B N   1 
ATOM   1227 C CA  . HIS   A 1 173 ? -44.677 -12.379 5.558  1.00 69.45  ? 388 HIS   B CA  1 
ATOM   1228 C C   . HIS   A 1 173 ? -44.057 -12.449 4.173  1.00 72.64  ? 388 HIS   B C   1 
ATOM   1229 O O   . HIS   A 1 173 ? -44.454 -13.275 3.342  1.00 71.26  ? 388 HIS   B O   1 
ATOM   1230 C CB  . HIS   A 1 173 ? -45.854 -11.413 5.497  1.00 69.69  ? 388 HIS   B CB  1 
ATOM   1231 C CG  . HIS   A 1 173 ? -46.754 -11.465 6.682  1.00 74.85  ? 388 HIS   B CG  1 
ATOM   1232 N ND1 . HIS   A 1 173 ? -46.280 -11.484 7.978  1.00 71.95  ? 388 HIS   B ND1 1 
ATOM   1233 C CD2 . HIS   A 1 173 ? -48.106 -11.485 6.772  1.00 79.87  ? 388 HIS   B CD2 1 
ATOM   1234 C CE1 . HIS   A 1 173 ? -47.302 -11.497 8.814  1.00 72.01  ? 388 HIS   B CE1 1 
ATOM   1235 N NE2 . HIS   A 1 173 ? -48.421 -11.506 8.110  1.00 78.73  ? 388 HIS   B NE2 1 
ATOM   1236 N N   . LYS   A 1 174 ? -43.139 -11.533 3.887  1.00 68.53  ? 389 LYS   B N   1 
ATOM   1237 C CA  . LYS   A 1 174 ? -42.410 -11.608 2.640  1.00 69.65  ? 389 LYS   B CA  1 
ATOM   1238 C C   . LYS   A 1 174 ? -41.506 -12.827 2.632  1.00 73.58  ? 389 LYS   B C   1 
ATOM   1239 O O   . LYS   A 1 174 ? -41.575 -13.661 1.719  1.00 76.83  ? 389 LYS   B O   1 
ATOM   1240 C CB  . LYS   A 1 174 ? -41.615 -10.330 2.439  1.00 64.96  ? 389 LYS   B CB  1 
ATOM   1241 C CG  . LYS   A 1 174 ? -42.459 -9.083  2.332  1.00 56.88  ? 389 LYS   B CG  1 
ATOM   1242 C CD  . LYS   A 1 174 ? -41.524 -7.949  2.076  1.00 61.34  ? 389 LYS   B CD  1 
ATOM   1243 C CE  . LYS   A 1 174 ? -41.920 -6.671  2.748  1.00 58.30  ? 389 LYS   B CE  1 
ATOM   1244 N NZ  . LYS   A 1 174 ? -40.673 -5.929  3.077  1.00 62.02  ? 389 LYS   B NZ  1 
ATOM   1245 N N   . LEU   A 1 175 ? -40.686 -12.977 3.676  1.00 69.75  ? 390 LEU   B N   1 
ATOM   1246 C CA  . LEU   A 1 175 ? -39.750 -14.094 3.748  1.00 70.14  ? 390 LEU   B CA  1 
ATOM   1247 C C   . LEU   A 1 175 ? -40.452 -15.439 3.856  1.00 72.35  ? 390 LEU   B C   1 
ATOM   1248 O O   . LEU   A 1 175 ? -39.827 -16.472 3.606  1.00 71.65  ? 390 LEU   B O   1 
ATOM   1249 C CB  . LEU   A 1 175 ? -38.784 -13.875 4.916  1.00 65.14  ? 390 LEU   B CB  1 
ATOM   1250 C CG  . LEU   A 1 175 ? -37.763 -14.924 5.366  1.00 68.54  ? 390 LEU   B CG  1 
ATOM   1251 C CD1 . LEU   A 1 175 ? -36.449 -14.720 4.639  1.00 68.16  ? 390 LEU   B CD1 1 
ATOM   1252 C CD2 . LEU   A 1 175 ? -37.527 -14.813 6.869  1.00 66.12  ? 390 LEU   B CD2 1 
ATOM   1253 N N   . ARG   A 1 176 ? -41.739 -15.451 4.178  1.00 91.16  ? 391 ARG   B N   1 
ATOM   1254 C CA  . ARG   A 1 176 ? -42.485 -16.701 4.223  1.00 91.75  ? 391 ARG   B CA  1 
ATOM   1255 C C   . ARG   A 1 176 ? -42.975 -17.113 2.844  1.00 91.73  ? 391 ARG   B C   1 
ATOM   1256 O O   . ARG   A 1 176 ? -43.101 -18.313 2.564  1.00 92.31  ? 391 ARG   B O   1 
ATOM   1257 C CB  . ARG   A 1 176 ? -43.643 -16.560 5.216  1.00 91.47  ? 391 ARG   B CB  1 
ATOM   1258 C CG  . ARG   A 1 176 ? -45.014 -16.396 4.585  1.00 92.59  ? 391 ARG   B CG  1 
ATOM   1259 C CD  . ARG   A 1 176 ? -46.120 -16.310 5.631  1.00 94.95  ? 391 ARG   B CD  1 
ATOM   1260 N NE  . ARG   A 1 176 ? -46.185 -17.525 6.436  1.00 97.00  ? 391 ARG   B NE  1 
ATOM   1261 C CZ  . ARG   A 1 176 ? -47.174 -17.839 7.261  1.00 98.33  ? 391 ARG   B CZ  1 
ATOM   1262 N NH1 . ARG   A 1 176 ? -48.218 -17.041 7.427  1.00 99.90  ? 391 ARG   B NH1 1 
ATOM   1263 N NH2 . ARG   A 1 176 ? -47.116 -18.987 7.934  1.00 98.76  ? 391 ARG   B NH2 1 
ATOM   1264 N N   . GLN   A 1 177 ? -43.220 -16.148 1.968  1.00 79.06  ? 392 GLN   B N   1 
ATOM   1265 C CA  . GLN   A 1 177 ? -43.813 -16.443 0.677  1.00 82.23  ? 392 GLN   B CA  1 
ATOM   1266 C C   . GLN   A 1 177 ? -42.785 -16.845 -0.387 1.00 82.40  ? 392 GLN   B C   1 
ATOM   1267 O O   . GLN   A 1 177 ? -43.180 -17.325 -1.461 1.00 81.80  ? 392 GLN   B O   1 
ATOM   1268 C CB  . GLN   A 1 177 ? -44.654 -15.234 0.239  1.00 84.27  ? 392 GLN   B CB  1 
ATOM   1269 C CG  . GLN   A 1 177 ? -43.897 -14.123 -0.483 1.00 86.01  ? 392 GLN   B CG  1 
ATOM   1270 C CD  . GLN   A 1 177 ? -44.826 -13.046 -1.030 1.00 89.24  ? 392 GLN   B CD  1 
ATOM   1271 O OE1 . GLN   A 1 177 ? -45.792 -12.650 -0.368 1.00 94.77  ? 392 GLN   B OE1 1 
ATOM   1272 N NE2 . GLN   A 1 177 ? -44.551 -12.583 -2.256 1.00 91.89  ? 392 GLN   B NE2 1 
ATOM   1273 N N   . LEU   A 1 178 ? -41.471 -16.688 -0.100 1.00 78.10  ? 393 LEU   B N   1 
ATOM   1274 C CA  . LEU   A 1 178 ? -40.389 -17.113 -0.983 1.00 69.61  ? 393 LEU   B CA  1 
ATOM   1275 C C   . LEU   A 1 178 ? -40.620 -18.560 -1.358 1.00 70.72  ? 393 LEU   B C   1 
ATOM   1276 O O   . LEU   A 1 178 ? -41.158 -19.323 -0.545 1.00 72.06  ? 393 LEU   B O   1 
ATOM   1277 C CB  . LEU   A 1 178 ? -39.019 -16.976 -0.319 1.00 68.06  ? 393 LEU   B CB  1 
ATOM   1278 C CG  . LEU   A 1 178 ? -38.573 -15.593 0.159  1.00 70.70  ? 393 LEU   B CG  1 
ATOM   1279 C CD1 . LEU   A 1 178 ? -37.105 -15.595 0.600  1.00 67.60  ? 393 LEU   B CD1 1 
ATOM   1280 C CD2 . LEU   A 1 178 ? -38.811 -14.555 -0.916 1.00 64.95  ? 393 LEU   B CD2 1 
ATOM   1281 N N   . PRO   A 1 179 ? -40.238 -18.975 -2.571 1.00 72.05  ? 394 PRO   B N   1 
ATOM   1282 C CA  . PRO   A 1 179 ? -40.558 -20.332 -3.038 1.00 64.41  ? 394 PRO   B CA  1 
ATOM   1283 C C   . PRO   A 1 179 ? -39.553 -21.420 -2.680 1.00 62.85  ? 394 PRO   B C   1 
ATOM   1284 O O   . PRO   A 1 179 ? -39.840 -22.594 -2.938 1.00 69.23  ? 394 PRO   B O   1 
ATOM   1285 C CB  . PRO   A 1 179 ? -40.636 -20.157 -4.565 1.00 70.34  ? 394 PRO   B CB  1 
ATOM   1286 C CG  . PRO   A 1 179 ? -40.406 -18.667 -4.839 1.00 72.99  ? 394 PRO   B CG  1 
ATOM   1287 C CD  . PRO   A 1 179 ? -39.716 -18.123 -3.650 1.00 71.13  ? 394 PRO   B CD  1 
ATOM   1288 N N   . GLU   A 1 180 ? -38.409 -21.098 -2.089 1.00 61.19  ? 395 GLU   B N   1 
ATOM   1289 C CA  . GLU   A 1 180 ? -37.374 -22.082 -1.815 1.00 59.60  ? 395 GLU   B CA  1 
ATOM   1290 C C   . GLU   A 1 180 ? -36.647 -21.731 -0.524 1.00 63.34  ? 395 GLU   B C   1 
ATOM   1291 O O   . GLU   A 1 180 ? -36.426 -20.559 -0.211 1.00 66.39  ? 395 GLU   B O   1 
ATOM   1292 C CB  . GLU   A 1 180 ? -36.360 -22.146 -2.955 1.00 67.72  ? 395 GLU   B CB  1 
ATOM   1293 C CG  . GLU   A 1 180 ? -36.914 -22.667 -4.270 1.00 67.95  ? 395 GLU   B CG  1 
ATOM   1294 C CD  . GLU   A 1 180 ? -37.007 -24.173 -4.262 1.00 70.48  ? 395 GLU   B CD  1 
ATOM   1295 O OE1 . GLU   A 1 180 ? -36.566 -24.776 -3.256 1.00 71.43  ? 395 GLU   B OE1 1 
ATOM   1296 O OE2 . GLU   A 1 180 ? -37.518 -24.754 -5.244 1.00 74.55  ? 395 GLU   B OE2 1 
ATOM   1297 N N   . ARG   A 1 181 ? -36.270 -22.759 0.226  1.00 67.78  ? 396 ARG   B N   1 
ATOM   1298 C CA  . ARG   A 1 181 ? -35.547 -22.535 1.472  1.00 61.88  ? 396 ARG   B CA  1 
ATOM   1299 C C   . ARG   A 1 181 ? -34.184 -21.911 1.209  1.00 60.68  ? 396 ARG   B C   1 
ATOM   1300 O O   . ARG   A 1 181 ? -33.735 -21.064 1.983  1.00 59.95  ? 396 ARG   B O   1 
ATOM   1301 C CB  . ARG   A 1 181 ? -35.404 -23.864 2.236  1.00 62.85  ? 396 ARG   B CB  1 
ATOM   1302 C CG  . ARG   A 1 181 ? -35.769 -23.803 3.720  1.00 66.44  ? 396 ARG   B CG  1 
ATOM   1303 C CD  . ARG   A 1 181 ? -35.844 -25.175 4.425  1.00 73.06  ? 396 ARG   B CD  1 
ATOM   1304 N NE  . ARG   A 1 181 ? -34.597 -25.936 4.360  1.00 75.62  ? 396 ARG   B NE  1 
ATOM   1305 C CZ  . ARG   A 1 181 ? -33.484 -25.668 5.041  1.00 76.64  ? 396 ARG   B CZ  1 
ATOM   1306 N NH1 . ARG   A 1 181 ? -33.392 -24.615 5.846  1.00 72.31  ? 396 ARG   B NH1 1 
ATOM   1307 N NH2 . ARG   A 1 181 ? -32.423 -26.461 4.888  1.00 71.49  ? 396 ARG   B NH2 1 
ATOM   1308 N N   . TYR   A 1 182 ? -33.515 -22.301 0.118  1.00 62.86  ? 397 TYR   B N   1 
ATOM   1309 C CA  . TYR   A 1 182 ? -32.177 -21.779 -0.116 1.00 59.57  ? 397 TYR   B CA  1 
ATOM   1310 C C   . TYR   A 1 182 ? -32.238 -20.293 -0.397 1.00 61.47  ? 397 TYR   B C   1 
ATOM   1311 O O   . TYR   A 1 182 ? -31.346 -19.553 0.023  1.00 61.73  ? 397 TYR   B O   1 
ATOM   1312 C CB  . TYR   A 1 182 ? -31.479 -22.552 -1.248 1.00 63.87  ? 397 TYR   B CB  1 
ATOM   1313 C CG  . TYR   A 1 182 ? -31.890 -22.157 -2.636 1.00 63.94  ? 397 TYR   B CG  1 
ATOM   1314 C CD1 . TYR   A 1 182 ? -31.316 -21.050 -3.251 1.00 65.69  ? 397 TYR   B CD1 1 
ATOM   1315 C CD2 . TYR   A 1 182 ? -32.832 -22.898 -3.348 1.00 64.85  ? 397 TYR   B CD2 1 
ATOM   1316 C CE1 . TYR   A 1 182 ? -31.683 -20.661 -4.516 1.00 66.05  ? 397 TYR   B CE1 1 
ATOM   1317 C CE2 . TYR   A 1 182 ? -33.209 -22.522 -4.631 1.00 64.13  ? 397 TYR   B CE2 1 
ATOM   1318 C CZ  . TYR   A 1 182 ? -32.626 -21.391 -5.202 1.00 67.21  ? 397 TYR   B CZ  1 
ATOM   1319 O OH  . TYR   A 1 182 ? -32.964 -20.970 -6.463 1.00 67.03  ? 397 TYR   B OH  1 
ATOM   1320 N N   . MET   A 1 183 ? -33.299 -19.841 -1.073 1.00 69.53  ? 398 MET   B N   1 
ATOM   1321 C CA  . MET   A 1 183 ? -33.552 -18.407 -1.209 1.00 68.35  ? 398 MET   B CA  1 
ATOM   1322 C C   . MET   A 1 183 ? -33.821 -17.765 0.152  1.00 66.94  ? 398 MET   B C   1 
ATOM   1323 O O   . MET   A 1 183 ? -33.306 -16.678 0.457  1.00 65.43  ? 398 MET   B O   1 
ATOM   1324 C CB  . MET   A 1 183 ? -34.732 -18.190 -2.157 1.00 66.74  ? 398 MET   B CB  1 
ATOM   1325 C CG  . MET   A 1 183 ? -34.432 -18.563 -3.599 1.00 66.00  ? 398 MET   B CG  1 
ATOM   1326 S SD  . MET   A 1 183 ? -35.939 -18.616 -4.606 1.00 75.49  ? 398 MET   B SD  1 
ATOM   1327 C CE  . MET   A 1 183 ? -35.348 -18.004 -6.181 1.00 66.39  ? 398 MET   B CE  1 
ATOM   1328 N N   . MET   A 1 184 ? -34.608 -18.442 0.995  1.00 65.38  ? 399 MET   B N   1 
ATOM   1329 C CA  . MET   A 1 184 ? -34.876 -17.935 2.336  1.00 58.91  ? 399 MET   B CA  1 
ATOM   1330 C C   . MET   A 1 184 ? -33.586 -17.722 3.105  1.00 58.11  ? 399 MET   B C   1 
ATOM   1331 O O   . MET   A 1 184 ? -33.353 -16.641 3.654  1.00 62.60  ? 399 MET   B O   1 
ATOM   1332 C CB  . MET   A 1 184 ? -35.788 -18.893 3.087  1.00 59.02  ? 399 MET   B CB  1 
ATOM   1333 C CG  . MET   A 1 184 ? -37.231 -18.444 3.117  1.00 58.39  ? 399 MET   B CG  1 
ATOM   1334 S SD  . MET   A 1 184 ? -38.276 -19.865 3.426  1.00 57.86  ? 399 MET   B SD  1 
ATOM   1335 C CE  . MET   A 1 184 ? -39.706 -19.550 2.382  1.00 63.54  ? 399 MET   B CE  1 
ATOM   1336 N N   . ASN   A 1 185 ? -32.721 -18.730 3.134  1.00 56.31  ? 400 ASN   B N   1 
ATOM   1337 C CA  . ASN   A 1 185 ? -31.465 -18.576 3.848  1.00 56.80  ? 400 ASN   B CA  1 
ATOM   1338 C C   . ASN   A 1 185 ? -30.525 -17.589 3.180  1.00 58.23  ? 400 ASN   B C   1 
ATOM   1339 O O   . ASN   A 1 185 ? -29.642 -17.070 3.867  1.00 59.75  ? 400 ASN   B O   1 
ATOM   1340 C CB  . ASN   A 1 185 ? -30.780 -19.928 4.013  1.00 61.09  ? 400 ASN   B CB  1 
ATOM   1341 C CG  . ASN   A 1 185 ? -31.443 -20.781 5.082  1.00 63.46  ? 400 ASN   B CG  1 
ATOM   1342 O OD1 . ASN   A 1 185 ? -32.022 -20.252 6.026  1.00 63.48  ? 400 ASN   B OD1 1 
ATOM   1343 N ND2 . ASN   A 1 185 ? -31.367 -22.101 4.939  1.00 64.99  ? 400 ASN   B ND2 1 
ATOM   1344 N N   . SER   A 1 186 ? -30.700 -17.309 1.877  1.00 56.72  ? 401 SER   B N   1 
ATOM   1345 C CA  . SER   A 1 186 ? -29.847 -16.335 1.193  1.00 58.22  ? 401 SER   B CA  1 
ATOM   1346 C C   . SER   A 1 186 ? -30.149 -14.925 1.665  1.00 61.82  ? 401 SER   B C   1 
ATOM   1347 O O   . SER   A 1 186 ? -29.236 -14.168 2.017  1.00 62.45  ? 401 SER   B O   1 
ATOM   1348 C CB  . SER   A 1 186 ? -30.041 -16.401 -0.316 1.00 59.43  ? 401 SER   B CB  1 
ATOM   1349 O OG  . SER   A 1 186 ? -29.997 -17.735 -0.778 1.00 69.93  ? 401 SER   B OG  1 
ATOM   1350 N N   . VAL   A 1 187 ? -31.430 -14.546 1.624  1.00 60.39  ? 402 VAL   B N   1 
ATOM   1351 C CA  . VAL   A 1 187 ? -31.887 -13.306 2.244  1.00 58.62  ? 402 VAL   B CA  1 
ATOM   1352 C C   . VAL   A 1 187 ? -31.340 -13.192 3.654  1.00 58.20  ? 402 VAL   B C   1 
ATOM   1353 O O   . VAL   A 1 187 ? -30.547 -12.297 3.962  1.00 55.79  ? 402 VAL   B O   1 
ATOM   1354 C CB  . VAL   A 1 187 ? -33.418 -13.255 2.250  1.00 59.14  ? 402 VAL   B CB  1 
ATOM   1355 C CG1 . VAL   A 1 187 ? -33.889 -11.932 2.831  1.00 49.41  ? 402 VAL   B CG1 1 
ATOM   1356 C CG2 . VAL   A 1 187 ? -33.943 -13.518 0.830  1.00 57.69  ? 402 VAL   B CG2 1 
ATOM   1357 N N   . LEU   A 1 188 ? -31.731 -14.142 4.513  1.00 59.90  ? 403 LEU   B N   1 
ATOM   1358 C CA  . LEU   A 1 188 ? -31.381 -14.174 5.931  1.00 58.90  ? 403 LEU   B CA  1 
ATOM   1359 C C   . LEU   A 1 188 ? -29.885 -14.072 6.197  1.00 60.27  ? 403 LEU   B C   1 
ATOM   1360 O O   . LEU   A 1 188 ? -29.497 -13.861 7.352  1.00 59.70  ? 403 LEU   B O   1 
ATOM   1361 C CB  . LEU   A 1 188 ? -31.896 -15.460 6.554  1.00 58.68  ? 403 LEU   B CB  1 
ATOM   1362 C CG  . LEU   A 1 188 ? -33.404 -15.645 6.655  1.00 59.85  ? 403 LEU   B CG  1 
ATOM   1363 C CD1 . LEU   A 1 188 ? -33.616 -16.949 7.331  1.00 60.74  ? 403 LEU   B CD1 1 
ATOM   1364 C CD2 . LEU   A 1 188 ? -34.055 -14.535 7.442  1.00 56.78  ? 403 LEU   B CD2 1 
ATOM   1365 N N   . GLU   A 1 189 ? -29.041 -14.235 5.177  1.00 62.02  ? 404 GLU   B N   1 
ATOM   1366 C CA  . GLU   A 1 189 ? -27.601 -14.129 5.381  1.00 65.50  ? 404 GLU   B CA  1 
ATOM   1367 C C   . GLU   A 1 189 ? -27.178 -12.693 5.581  1.00 66.08  ? 404 GLU   B C   1 
ATOM   1368 O O   . GLU   A 1 189 ? -26.086 -12.436 6.103  1.00 70.69  ? 404 GLU   B O   1 
ATOM   1369 C CB  . GLU   A 1 189 ? -26.832 -14.722 4.193  1.00 65.44  ? 404 GLU   B CB  1 
ATOM   1370 C CG  . GLU   A 1 189 ? -25.453 -15.249 4.557  1.00 70.06  ? 404 GLU   B CG  1 
ATOM   1371 C CD  . GLU   A 1 189 ? -24.891 -16.200 3.501  1.00 92.48  ? 404 GLU   B CD  1 
ATOM   1372 O OE1 . GLU   A 1 189 ? -25.069 -15.921 2.286  1.00 95.79  ? 404 GLU   B OE1 1 
ATOM   1373 O OE2 . GLU   A 1 189 ? -24.264 -17.224 3.876  1.00 96.29  ? 404 GLU   B OE2 1 
ATOM   1374 N N   . ASN   A 1 190 ? -28.018 -11.759 5.160  1.00 60.66  ? 405 ASN   B N   1 
ATOM   1375 C CA  . ASN   A 1 190 ? -27.761 -10.336 5.297  1.00 65.63  ? 405 ASN   B CA  1 
ATOM   1376 C C   . ASN   A 1 190 ? -28.638 -9.706  6.367  1.00 62.49  ? 405 ASN   B C   1 
ATOM   1377 O O   . ASN   A 1 190 ? -28.764 -8.480  6.436  1.00 66.27  ? 405 ASN   B O   1 
ATOM   1378 C CB  . ASN   A 1 190 ? -27.964 -9.666  3.941  1.00 68.85  ? 405 ASN   B CB  1 
ATOM   1379 C CG  . ASN   A 1 190 ? -27.129 -10.312 2.873  1.00 67.52  ? 405 ASN   B CG  1 
ATOM   1380 O OD1 . ASN   A 1 190 ? -25.893 -10.306 2.954  1.00 62.19  ? 405 ASN   B OD1 1 
ATOM   1381 N ND2 . ASN   A 1 190 ? -27.788 -10.909 1.881  1.00 67.51  ? 405 ASN   B ND2 1 
ATOM   1382 N N   . PHE   A 1 191 ? -29.256 -10.535 7.189  1.00 57.91  ? 406 PHE   B N   1 
ATOM   1383 C CA  . PHE   A 1 191 ? -30.219 -10.112 8.184  1.00 59.99  ? 406 PHE   B CA  1 
ATOM   1384 C C   . PHE   A 1 191 ? -29.648 -10.522 9.529  1.00 58.81  ? 406 PHE   B C   1 
ATOM   1385 O O   . PHE   A 1 191 ? -29.480 -11.715 9.787  1.00 64.39  ? 406 PHE   B O   1 
ATOM   1386 C CB  . PHE   A 1 191 ? -31.565 -10.762 7.910  1.00 56.82  ? 406 PHE   B CB  1 
ATOM   1387 C CG  . PHE   A 1 191 ? -32.597 -10.427 8.917  1.00 63.72  ? 406 PHE   B CG  1 
ATOM   1388 C CD1 . PHE   A 1 191 ? -32.775 -11.234 10.044 1.00 62.80  ? 406 PHE   B CD1 1 
ATOM   1389 C CD2 . PHE   A 1 191 ? -33.398 -9.301  8.751  1.00 63.52  ? 406 PHE   B CD2 1 
ATOM   1390 C CE1 . PHE   A 1 191 ? -33.729 -10.920 10.991 1.00 58.96  ? 406 PHE   B CE1 1 
ATOM   1391 C CE2 . PHE   A 1 191 ? -34.369 -8.977  9.693  1.00 64.12  ? 406 PHE   B CE2 1 
ATOM   1392 C CZ  . PHE   A 1 191 ? -34.532 -9.790  10.816 1.00 63.25  ? 406 PHE   B CZ  1 
ATOM   1393 N N   . THR   A 1 192 ? -29.275 -9.547  10.356 1.00 58.26  ? 407 THR   B N   1 
ATOM   1394 C CA  . THR   A 1 192 ? -28.790 -9.840  11.699 1.00 65.59  ? 407 THR   B CA  1 
ATOM   1395 C C   . THR   A 1 192 ? -29.388 -8.875  12.730 1.00 64.50  ? 407 THR   B C   1 
ATOM   1396 O O   . THR   A 1 192 ? -29.974 -7.833  12.412 1.00 62.41  ? 407 THR   B O   1 
ATOM   1397 C CB  . THR   A 1 192 ? -27.258 -9.801  11.804 1.00 64.61  ? 407 THR   B CB  1 
ATOM   1398 O OG1 . THR   A 1 192 ? -26.827 -8.450  11.881 1.00 69.09  ? 407 THR   B OG1 1 
ATOM   1399 C CG2 . THR   A 1 192 ? -26.584 -10.502 10.645 1.00 68.08  ? 407 THR   B CG2 1 
ATOM   1400 N N   . ILE   A 1 193 ? -29.230 -9.250  13.990 1.00 62.65  ? 408 ILE   B N   1 
ATOM   1401 C CA  . ILE   A 1 193 ? -29.763 -8.494  15.114 1.00 62.01  ? 408 ILE   B CA  1 
ATOM   1402 C C   . ILE   A 1 193 ? -28.675 -8.387  16.170 1.00 59.36  ? 408 ILE   B C   1 
ATOM   1403 O O   . ILE   A 1 193 ? -28.049 -9.391  16.523 1.00 58.24  ? 408 ILE   B O   1 
ATOM   1404 C CB  . ILE   A 1 193 ? -31.021 -9.164  15.696 1.00 58.35  ? 408 ILE   B CB  1 
ATOM   1405 C CG1 . ILE   A 1 193 ? -32.238 -8.850  14.830 1.00 58.69  ? 408 ILE   B CG1 1 
ATOM   1406 C CG2 . ILE   A 1 193 ? -31.267 -8.667  17.078 1.00 62.01  ? 408 ILE   B CG2 1 
ATOM   1407 C CD1 . ILE   A 1 193 ? -33.469 -9.592  15.260 1.00 55.54  ? 408 ILE   B CD1 1 
ATOM   1408 N N   . LEU   A 1 194 ? -28.430 -7.177  16.655 1.00 58.81  ? 409 LEU   B N   1 
ATOM   1409 C CA  . LEU   A 1 194 ? -27.542 -6.953  17.784 1.00 62.93  ? 409 LEU   B CA  1 
ATOM   1410 C C   . LEU   A 1 194 ? -28.383 -6.556  19.002 1.00 63.28  ? 409 LEU   B C   1 
ATOM   1411 O O   . LEU   A 1 194 ? -29.258 -5.688  18.916 1.00 62.76  ? 409 LEU   B O   1 
ATOM   1412 C CB  . LEU   A 1 194 ? -26.490 -5.889  17.450 1.00 61.60  ? 409 LEU   B CB  1 
ATOM   1413 C CG  . LEU   A 1 194 ? -25.265 -5.806  18.368 1.00 63.37  ? 409 LEU   B CG  1 
ATOM   1414 C CD1 . LEU   A 1 194 ? -24.652 -7.149  18.550 1.00 58.99  ? 409 LEU   B CD1 1 
ATOM   1415 C CD2 . LEU   A 1 194 ? -24.237 -4.864  17.832 1.00 72.39  ? 409 LEU   B CD2 1 
ATOM   1416 N N   . GLN   A 1 195 ? -28.134 -7.207  20.130 1.00 69.17  ? 410 GLN   B N   1 
ATOM   1417 C CA  . GLN   A 1 195 ? -28.901 -6.986  21.349 1.00 68.39  ? 410 GLN   B CA  1 
ATOM   1418 C C   . GLN   A 1 195 ? -27.940 -6.606  22.458 1.00 69.08  ? 410 GLN   B C   1 
ATOM   1419 O O   . GLN   A 1 195 ? -27.091 -7.415  22.848 1.00 69.06  ? 410 GLN   B O   1 
ATOM   1420 C CB  . GLN   A 1 195 ? -29.673 -8.234  21.720 1.00 68.39  ? 410 GLN   B CB  1 
ATOM   1421 C CG  . GLN   A 1 195 ? -30.337 -8.152  23.015 1.00 71.71  ? 410 GLN   B CG  1 
ATOM   1422 C CD  . GLN   A 1 195 ? -31.616 -8.925  22.981 1.00 80.57  ? 410 GLN   B CD  1 
ATOM   1423 O OE1 . GLN   A 1 195 ? -32.606 -8.463  22.411 1.00 83.15  ? 410 GLN   B OE1 1 
ATOM   1424 N NE2 . GLN   A 1 195 ? -31.604 -10.135 23.555 1.00 82.31  ? 410 GLN   B NE2 1 
ATOM   1425 N N   . VAL   A 1 196 ? -28.064 -5.381  22.955 1.00 59.70  ? 411 VAL   B N   1 
ATOM   1426 C CA  . VAL   A 1 196 ? -27.129 -4.826  23.928 1.00 62.21  ? 411 VAL   B CA  1 
ATOM   1427 C C   . VAL   A 1 196 ? -27.902 -4.452  25.181 1.00 59.83  ? 411 VAL   B C   1 
ATOM   1428 O O   . VAL   A 1 196 ? -28.743 -3.542  25.154 1.00 58.64  ? 411 VAL   B O   1 
ATOM   1429 C CB  . VAL   A 1 196 ? -26.372 -3.614  23.375 1.00 62.03  ? 411 VAL   B CB  1 
ATOM   1430 C CG1 . VAL   A 1 196 ? -25.375 -3.109  24.403 1.00 56.93  ? 411 VAL   B CG1 1 
ATOM   1431 C CG2 . VAL   A 1 196 ? -25.675 -3.988  22.080 1.00 64.09  ? 411 VAL   B CG2 1 
ATOM   1432 N N   . VAL   A 1 197 ? -27.612 -5.146  26.280 1.00 59.97  ? 412 VAL   B N   1 
ATOM   1433 C CA  . VAL   A 1 197 ? -28.165 -4.827  27.589 1.00 59.98  ? 412 VAL   B CA  1 
ATOM   1434 C C   . VAL   A 1 197 ? -27.077 -4.147  28.405 1.00 60.10  ? 412 VAL   B C   1 
ATOM   1435 O O   . VAL   A 1 197 ? -25.952 -4.653  28.505 1.00 60.29  ? 412 VAL   B O   1 
ATOM   1436 C CB  . VAL   A 1 197 ? -28.690 -6.082  28.306 1.00 58.61  ? 412 VAL   B CB  1 
ATOM   1437 C CG1 . VAL   A 1 197 ? -29.655 -5.677  29.429 1.00 60.21  ? 412 VAL   B CG1 1 
ATOM   1438 C CG2 . VAL   A 1 197 ? -29.365 -7.032  27.331 1.00 55.90  ? 412 VAL   B CG2 1 
ATOM   1439 N N   . THR   A 1 198 ? -27.403 -2.993  28.978 1.00 61.82  ? 413 THR   B N   1 
ATOM   1440 C CA  . THR   A 1 198 ? -26.460 -2.214  29.764 1.00 62.86  ? 413 THR   B CA  1 
ATOM   1441 C C   . THR   A 1 198 ? -27.144 -1.707  31.016 1.00 65.75  ? 413 THR   B C   1 
ATOM   1442 O O   . THR   A 1 198 ? -28.357 -1.487  31.029 1.00 65.58  ? 413 THR   B O   1 
ATOM   1443 C CB  . THR   A 1 198 ? -25.935 -1.018  28.983 1.00 66.69  ? 413 THR   B CB  1 
ATOM   1444 O OG1 . THR   A 1 198 ? -27.000 -0.507  28.178 1.00 68.95  ? 413 THR   B OG1 1 
ATOM   1445 C CG2 . THR   A 1 198 ? -24.786 -1.415  28.077 1.00 66.31  ? 413 THR   B CG2 1 
ATOM   1446 N N   . ASN   A 1 199 ? -26.349 -1.517  32.065 1.00 69.50  ? 414 ASN   B N   1 
ATOM   1447 C CA  . ASN   A 1 199 ? -26.788 -0.812  33.259 1.00 71.76  ? 414 ASN   B CA  1 
ATOM   1448 C C   . ASN   A 1 199 ? -27.173 0.621   32.897 1.00 76.97  ? 414 ASN   B C   1 
ATOM   1449 O O   . ASN   A 1 199 ? -26.304 1.412   32.512 1.00 81.86  ? 414 ASN   B O   1 
ATOM   1450 C CB  . ASN   A 1 199 ? -25.667 -0.839  34.302 1.00 76.14  ? 414 ASN   B CB  1 
ATOM   1451 C CG  . ASN   A 1 199 ? -26.133 -0.443  35.710 1.00 82.72  ? 414 ASN   B CG  1 
ATOM   1452 O OD1 . ASN   A 1 199 ? -27.221 0.111   35.915 1.00 80.78  ? 414 ASN   B OD1 1 
ATOM   1453 N ND2 . ASN   A 1 199 ? -25.286 -0.724  36.688 1.00 83.18  ? 414 ASN   B ND2 1 
ATOM   1454 N N   . ARG   A 1 200 ? -28.462 0.973   33.017 1.00 73.40  ? 415 ARG   B N   1 
ATOM   1455 C CA  . ARG   A 1 200 ? -28.900 2.334   32.692 1.00 77.08  ? 415 ARG   B CA  1 
ATOM   1456 C C   . ARG   A 1 200 ? -28.173 3.387   33.525 1.00 82.25  ? 415 ARG   B C   1 
ATOM   1457 O O   . ARG   A 1 200 ? -27.872 4.474   33.024 1.00 86.37  ? 415 ARG   B O   1 
ATOM   1458 C CB  . ARG   A 1 200 ? -30.411 2.487   32.885 1.00 76.66  ? 415 ARG   B CB  1 
ATOM   1459 C CG  . ARG   A 1 200 ? -30.919 3.901   32.569 1.00 79.80  ? 415 ARG   B CG  1 
ATOM   1460 C CD  . ARG   A 1 200 ? -32.326 4.146   33.066 1.00 79.09  ? 415 ARG   B CD  1 
ATOM   1461 N NE  . ARG   A 1 200 ? -32.341 4.467   34.489 1.00 84.21  ? 415 ARG   B NE  1 
ATOM   1462 C CZ  . ARG   A 1 200 ? -33.442 4.626   35.214 1.00 86.08  ? 415 ARG   B CZ  1 
ATOM   1463 N NH1 . ARG   A 1 200 ? -34.645 4.571   34.664 1.00 88.16  ? 415 ARG   B NH1 1 
ATOM   1464 N NH2 . ARG   A 1 200 ? -33.333 4.830   36.526 1.00 88.34  ? 415 ARG   B NH2 1 
ATOM   1465 N N   . ASP   A 1 201 ? -27.900 3.099   34.801 1.00 86.66  ? 416 ASP   B N   1 
ATOM   1466 C CA  . ASP   A 1 201 ? -27.246 4.096   35.649 1.00 88.86  ? 416 ASP   B CA  1 
ATOM   1467 C C   . ASP   A 1 201 ? -25.763 4.225   35.309 1.00 88.54  ? 416 ASP   B C   1 
ATOM   1468 O O   . ASP   A 1 201 ? -25.271 5.329   35.037 1.00 91.77  ? 416 ASP   B O   1 
ATOM   1469 C CB  . ASP   A 1 201 ? -27.402 3.755   37.140 1.00 90.94  ? 416 ASP   B CB  1 
ATOM   1470 C CG  . ASP   A 1 201 ? -28.837 3.424   37.550 1.00 92.46  ? 416 ASP   B CG  1 
ATOM   1471 O OD1 . ASP   A 1 201 ? -29.795 4.079   37.065 1.00 86.32  ? 416 ASP   B OD1 1 
ATOM   1472 O OD2 . ASP   A 1 201 ? -28.985 2.502   38.394 1.00 94.04  ? 416 ASP   B OD2 1 
ATOM   1473 N N   . THR   A 1 202 ? -25.028 3.107   35.337 1.00 84.10  ? 417 THR   B N   1 
ATOM   1474 C CA  . THR   A 1 202 ? -23.571 3.136   35.252 1.00 86.11  ? 417 THR   B CA  1 
ATOM   1475 C C   . THR   A 1 202 ? -23.038 3.071   33.829 1.00 85.31  ? 417 THR   B C   1 
ATOM   1476 O O   . THR   A 1 202 ? -21.826 3.225   33.639 1.00 84.10  ? 417 THR   B O   1 
ATOM   1477 C CB  . THR   A 1 202 ? -22.937 1.979   36.047 1.00 86.47  ? 417 THR   B CB  1 
ATOM   1478 O OG1 . THR   A 1 202 ? -23.122 0.742   35.343 1.00 84.93  ? 417 THR   B OG1 1 
ATOM   1479 C CG2 . THR   A 1 202 ? -23.529 1.874   37.444 1.00 85.14  ? 417 THR   B CG2 1 
ATOM   1480 N N   . GLN   A 1 203 ? -23.897 2.830   32.839 1.00 83.33  ? 418 GLN   B N   1 
ATOM   1481 C CA  . GLN   A 1 203 ? -23.531 2.740   31.427 1.00 85.98  ? 418 GLN   B CA  1 
ATOM   1482 C C   . GLN   A 1 203 ? -22.666 1.527   31.096 1.00 77.90  ? 418 GLN   B C   1 
ATOM   1483 O O   . GLN   A 1 203 ? -22.207 1.410   29.961 1.00 80.50  ? 418 GLN   B O   1 
ATOM   1484 C CB  . GLN   A 1 203 ? -22.811 4.008   30.927 1.00 85.79  ? 418 GLN   B CB  1 
ATOM   1485 C CG  . GLN   A 1 203 ? -23.694 5.242   30.787 1.00 83.82  ? 418 GLN   B CG  1 
ATOM   1486 C CD  . GLN   A 1 203 ? -24.987 4.944   30.039 1.00 85.24  ? 418 GLN   B CD  1 
ATOM   1487 O OE1 . GLN   A 1 203 ? -26.080 5.244   30.520 1.00 86.94  ? 418 GLN   B OE1 1 
ATOM   1488 N NE2 . GLN   A 1 203 ? -24.867 4.339   28.859 1.00 82.16  ? 418 GLN   B NE2 1 
ATOM   1489 N N   . GLU   A 1 204 ? -22.425 0.619   32.033 1.00 76.16  ? 419 GLU   B N   1 
ATOM   1490 C CA  . GLU   A 1 204 ? -21.563 -0.503  31.707 1.00 75.25  ? 419 GLU   B CA  1 
ATOM   1491 C C   . GLU   A 1 204 ? -22.355 -1.612  31.030 1.00 74.74  ? 419 GLU   B C   1 
ATOM   1492 O O   . GLU   A 1 204 ? -23.550 -1.792  31.278 1.00 75.75  ? 419 GLU   B O   1 
ATOM   1493 C CB  . GLU   A 1 204 ? -20.858 -1.048  32.950 1.00 80.58  ? 419 GLU   B CB  1 
ATOM   1494 C CG  . GLU   A 1 204 ? -21.765 -1.569  34.037 1.00 82.75  ? 419 GLU   B CG  1 
ATOM   1495 C CD  . GLU   A 1 204 ? -21.053 -1.659  35.378 1.00 85.66  ? 419 GLU   B CD  1 
ATOM   1496 O OE1 . GLU   A 1 204 ? -19.866 -2.071  35.387 1.00 84.22  ? 419 GLU   B OE1 1 
ATOM   1497 O OE2 . GLU   A 1 204 ? -21.672 -1.285  36.410 1.00 83.42  ? 419 GLU   B OE2 1 
ATOM   1498 N N   . LEU   A 1 205 ? -21.664 -2.362  30.169 1.00 71.65  ? 420 LEU   B N   1 
ATOM   1499 C CA  . LEU   A 1 205 ? -22.293 -3.407  29.375 1.00 65.53  ? 420 LEU   B CA  1 
ATOM   1500 C C   . LEU   A 1 205 ? -22.404 -4.711  30.169 1.00 60.86  ? 420 LEU   B C   1 
ATOM   1501 O O   . LEU   A 1 205 ? -21.452 -5.142  30.833 1.00 57.88  ? 420 LEU   B O   1 
ATOM   1502 C CB  . LEU   A 1 205 ? -21.499 -3.617  28.079 1.00 65.69  ? 420 LEU   B CB  1 
ATOM   1503 C CG  . LEU   A 1 205 ? -22.016 -4.652  27.067 1.00 62.33  ? 420 LEU   B CG  1 
ATOM   1504 C CD1 . LEU   A 1 205 ? -22.231 -3.993  25.730 1.00 62.82  ? 420 LEU   B CD1 1 
ATOM   1505 C CD2 . LEU   A 1 205 ? -21.062 -5.803  26.925 1.00 63.25  ? 420 LEU   B CD2 1 
ATOM   1506 N N   . LEU   A 1 206 ? -23.581 -5.336  30.108 1.00 56.57  ? 421 LEU   B N   1 
ATOM   1507 C CA  . LEU   A 1 206 ? -23.805 -6.601  30.801 1.00 59.66  ? 421 LEU   B CA  1 
ATOM   1508 C C   . LEU   A 1 206 ? -24.014 -7.787  29.871 1.00 62.07  ? 421 LEU   B C   1 
ATOM   1509 O O   . LEU   A 1 206 ? -23.586 -8.895  30.205 1.00 66.62  ? 421 LEU   B O   1 
ATOM   1510 C CB  . LEU   A 1 206 ? -25.006 -6.492  31.755 1.00 64.69  ? 421 LEU   B CB  1 
ATOM   1511 C CG  . LEU   A 1 206 ? -25.101 -5.258  32.664 1.00 59.54  ? 421 LEU   B CG  1 
ATOM   1512 C CD1 . LEU   A 1 206 ? -26.549 -4.971  33.028 1.00 57.99  ? 421 LEU   B CD1 1 
ATOM   1513 C CD2 . LEU   A 1 206 ? -24.220 -5.394  33.901 1.00 59.67  ? 421 LEU   B CD2 1 
ATOM   1514 N N   . LEU   A 1 207 ? -24.652 -7.601  28.709 1.00 61.37  ? 422 LEU   B N   1 
ATOM   1515 C CA  . LEU   A 1 207 ? -24.869 -8.697  27.763 1.00 60.02  ? 422 LEU   B CA  1 
ATOM   1516 C C   . LEU   A 1 207 ? -25.018 -8.164  26.344 1.00 60.56  ? 422 LEU   B C   1 
ATOM   1517 O O   . LEU   A 1 207 ? -25.860 -7.298  26.086 1.00 61.96  ? 422 LEU   B O   1 
ATOM   1518 C CB  . LEU   A 1 207 ? -26.113 -9.487  28.142 1.00 60.43  ? 422 LEU   B CB  1 
ATOM   1519 C CG  . LEU   A 1 207 ? -26.061 -10.996 28.099 1.00 58.91  ? 422 LEU   B CG  1 
ATOM   1520 C CD1 . LEU   A 1 207 ? -24.876 -11.500 28.908 1.00 58.41  ? 422 LEU   B CD1 1 
ATOM   1521 C CD2 . LEU   A 1 207 ? -27.371 -11.459 28.710 1.00 63.78  ? 422 LEU   B CD2 1 
ATOM   1522 N N   . CYS   A 1 208 ? -24.217 -8.701  25.426 1.00 63.37  ? 423 CYS   B N   1 
ATOM   1523 C CA  . CYS   A 1 208 ? -24.258 -8.339  24.010 1.00 59.58  ? 423 CYS   B CA  1 
ATOM   1524 C C   . CYS   A 1 208 ? -24.386 -9.619  23.190 1.00 57.54  ? 423 CYS   B C   1 
ATOM   1525 O O   . CYS   A 1 208 ? -23.537 -10.509 23.297 1.00 56.98  ? 423 CYS   B O   1 
ATOM   1526 C CB  . CYS   A 1 208 ? -22.998 -7.564  23.621 1.00 58.40  ? 423 CYS   B CB  1 
ATOM   1527 S SG  . CYS   A 1 208 ? -22.957 -7.008  21.913 1.00 63.06  ? 423 CYS   B SG  1 
ATOM   1528 N N   . THR   A 1 209 ? -25.440 -9.726  22.383 1.00 56.77  ? 424 THR   B N   1 
ATOM   1529 C CA  . THR   A 1 209 ? -25.725 -10.974 21.678 1.00 59.13  ? 424 THR   B CA  1 
ATOM   1530 C C   . THR   A 1 209 ? -26.008 -10.717 20.202 1.00 57.30  ? 424 THR   B C   1 
ATOM   1531 O O   . THR   A 1 209 ? -27.088 -10.239 19.847 1.00 56.21  ? 424 THR   B O   1 
ATOM   1532 C CB  . THR   A 1 209 ? -26.894 -11.705 22.321 1.00 56.70  ? 424 THR   B CB  1 
ATOM   1533 O OG1 . THR   A 1 209 ? -26.780 -11.585 23.739 1.00 60.04  ? 424 THR   B OG1 1 
ATOM   1534 C CG2 . THR   A 1 209 ? -26.857 -13.159 21.950 1.00 55.10  ? 424 THR   B CG2 1 
ATOM   1535 N N   . ALA   A 1 210 ? -25.051 -11.077 19.348 1.00 53.68  ? 425 ALA   B N   1 
ATOM   1536 C CA  . ALA   A 1 210 ? -25.244 -11.071 17.906 1.00 58.25  ? 425 ALA   B CA  1 
ATOM   1537 C C   . ALA   A 1 210 ? -26.085 -12.277 17.492 1.00 56.97  ? 425 ALA   B C   1 
ATOM   1538 O O   . ALA   A 1 210 ? -25.784 -13.409 17.876 1.00 57.35  ? 425 ALA   B O   1 
ATOM   1539 C CB  . ALA   A 1 210 ? -23.883 -11.091 17.198 1.00 59.82  ? 425 ALA   B CB  1 
ATOM   1540 N N   . TYR   A 1 211 ? -27.148 -12.039 16.729 1.00 56.44  ? 426 TYR   B N   1 
ATOM   1541 C CA  . TYR   A 1 211 ? -28.037 -13.096 16.260 1.00 55.37  ? 426 TYR   B CA  1 
ATOM   1542 C C   . TYR   A 1 211 ? -27.880 -13.234 14.751 1.00 60.76  ? 426 TYR   B C   1 
ATOM   1543 O O   . TYR   A 1 211 ? -28.110 -12.268 14.009 1.00 60.35  ? 426 TYR   B O   1 
ATOM   1544 C CB  . TYR   A 1 211 ? -29.496 -12.787 16.596 1.00 54.76  ? 426 TYR   B CB  1 
ATOM   1545 C CG  . TYR   A 1 211 ? -29.874 -12.811 18.071 1.00 60.71  ? 426 TYR   B CG  1 
ATOM   1546 C CD1 . TYR   A 1 211 ? -30.201 -14.003 18.713 1.00 58.14  ? 426 TYR   B CD1 1 
ATOM   1547 C CD2 . TYR   A 1 211 ? -29.923 -11.627 18.818 1.00 59.77  ? 426 TYR   B CD2 1 
ATOM   1548 C CE1 . TYR   A 1 211 ? -30.562 -14.016 20.046 1.00 60.55  ? 426 TYR   B CE1 1 
ATOM   1549 C CE2 . TYR   A 1 211 ? -30.278 -11.640 20.154 1.00 63.48  ? 426 TYR   B CE2 1 
ATOM   1550 C CZ  . TYR   A 1 211 ? -30.599 -12.837 20.758 1.00 62.63  ? 426 TYR   B CZ  1 
ATOM   1551 O OH  . TYR   A 1 211 ? -30.952 -12.856 22.077 1.00 60.18  ? 426 TYR   B OH  1 
ATOM   1552 N N   . VAL   A 1 212 ? -27.500 -14.425 14.293 1.00 59.37  ? 427 VAL   B N   1 
ATOM   1553 C CA  . VAL   A 1 212 ? -27.515 -14.726 12.867 1.00 58.10  ? 427 VAL   B CA  1 
ATOM   1554 C C   . VAL   A 1 212 ? -28.600 -15.757 12.637 1.00 56.29  ? 427 VAL   B C   1 
ATOM   1555 O O   . VAL   A 1 212 ? -29.003 -16.469 13.554 1.00 59.93  ? 427 VAL   B O   1 
ATOM   1556 C CB  . VAL   A 1 212 ? -26.160 -15.220 12.362 1.00 56.33  ? 427 VAL   B CB  1 
ATOM   1557 C CG1 . VAL   A 1 212 ? -25.108 -14.137 12.561 1.00 60.29  ? 427 VAL   B CG1 1 
ATOM   1558 C CG2 . VAL   A 1 212 ? -25.787 -16.478 13.069 1.00 60.98  ? 427 VAL   B CG2 1 
ATOM   1559 N N   . PHE   A 1 213 ? -29.114 -15.809 11.411 1.00 58.35  ? 428 PHE   B N   1 
ATOM   1560 C CA  . PHE   A 1 213 ? -30.359 -16.524 11.150 1.00 57.51  ? 428 PHE   B CA  1 
ATOM   1561 C C   . PHE   A 1 213 ? -30.284 -17.435 9.931  1.00 60.24  ? 428 PHE   B C   1 
ATOM   1562 O O   . PHE   A 1 213 ? -29.632 -17.131 8.931  1.00 66.20  ? 428 PHE   B O   1 
ATOM   1563 C CB  . PHE   A 1 213 ? -31.508 -15.560 10.952 1.00 57.95  ? 428 PHE   B CB  1 
ATOM   1564 C CG  . PHE   A 1 213 ? -31.863 -14.807 12.186 1.00 61.30  ? 428 PHE   B CG  1 
ATOM   1565 C CD1 . PHE   A 1 213 ? -31.085 -13.745 12.608 1.00 60.11  ? 428 PHE   B CD1 1 
ATOM   1566 C CD2 . PHE   A 1 213 ? -32.968 -15.158 12.925 1.00 55.59  ? 428 PHE   B CD2 1 
ATOM   1567 C CE1 . PHE   A 1 213 ? -31.405 -13.064 13.742 1.00 58.89  ? 428 PHE   B CE1 1 
ATOM   1568 C CE2 . PHE   A 1 213 ? -33.281 -14.469 14.048 1.00 55.68  ? 428 PHE   B CE2 1 
ATOM   1569 C CZ  . PHE   A 1 213 ? -32.508 -13.423 14.459 1.00 54.50  ? 428 PHE   B CZ  1 
ATOM   1570 N N   . GLU   A 1 214 ? -30.984 -18.558 10.040 1.00 60.12  ? 429 GLU   B N   1 
ATOM   1571 C CA  . GLU   A 1 214 ? -31.316 -19.438 8.937  1.00 59.20  ? 429 GLU   B CA  1 
ATOM   1572 C C   . GLU   A 1 214 ? -32.755 -19.883 9.122  1.00 61.00  ? 429 GLU   B C   1 
ATOM   1573 O O   . GLU   A 1 214 ? -33.409 -19.524 10.106 1.00 58.76  ? 429 GLU   B O   1 
ATOM   1574 C CB  . GLU   A 1 214 ? -30.403 -20.652 8.896  1.00 57.99  ? 429 GLU   B CB  1 
ATOM   1575 C CG  . GLU   A 1 214 ? -29.145 -20.420 8.160  1.00 61.64  ? 429 GLU   B CG  1 
ATOM   1576 C CD  . GLU   A 1 214 ? -28.327 -21.681 8.074  1.00 69.37  ? 429 GLU   B CD  1 
ATOM   1577 O OE1 . GLU   A 1 214 ? -28.771 -22.657 7.405  1.00 68.52  ? 429 GLU   B OE1 1 
ATOM   1578 O OE2 . GLU   A 1 214 ? -27.257 -21.706 8.720  1.00 68.53  ? 429 GLU   B OE2 1 
ATOM   1579 N N   . VAL   A 1 215 ? -33.256 -20.695 8.196  1.00 65.63  ? 430 VAL   B N   1 
ATOM   1580 C CA  . VAL   A 1 215 ? -34.602 -21.223 8.364  1.00 66.54  ? 430 VAL   B CA  1 
ATOM   1581 C C   . VAL   A 1 215 ? -34.522 -22.718 8.571  1.00 67.00  ? 430 VAL   B C   1 
ATOM   1582 O O   . VAL   A 1 215 ? -33.575 -23.376 8.131  1.00 70.13  ? 430 VAL   B O   1 
ATOM   1583 C CB  . VAL   A 1 215 ? -35.548 -20.890 7.201  1.00 65.53  ? 430 VAL   B CB  1 
ATOM   1584 C CG1 . VAL   A 1 215 ? -35.988 -19.458 7.351  1.00 65.72  ? 430 VAL   B CG1 1 
ATOM   1585 C CG2 . VAL   A 1 215 ? -34.892 -21.147 5.857  1.00 65.05  ? 430 VAL   B CG2 1 
ATOM   1586 N N   . SER   A 1 216 ? -35.540 -23.239 9.252  1.00 68.47  ? 431 SER   B N   1 
ATOM   1587 C CA  . SER   A 1 216 ? -35.623 -24.608 9.734  1.00 76.47  ? 431 SER   B CA  1 
ATOM   1588 C C   . SER   A 1 216 ? -36.646 -25.367 8.892  1.00 86.56  ? 431 SER   B C   1 
ATOM   1589 O O   . SER   A 1 216 ? -37.803 -24.945 8.793  1.00 89.39  ? 431 SER   B O   1 
ATOM   1590 C CB  . SER   A 1 216 ? -36.018 -24.599 11.213 1.00 73.71  ? 431 SER   B CB  1 
ATOM   1591 O OG  . SER   A 1 216 ? -35.860 -25.855 11.850 1.00 78.97  ? 431 SER   B OG  1 
ATOM   1592 N N   . THR   A 1 217 ? -36.214 -26.470 8.273  1.00 97.03  ? 432 THR   B N   1 
ATOM   1593 C CA  . THR   A 1 217 ? -37.103 -27.388 7.561  1.00 99.92  ? 432 THR   B CA  1 
ATOM   1594 C C   . THR   A 1 217 ? -38.283 -27.799 8.435  1.00 103.09 ? 432 THR   B C   1 
ATOM   1595 O O   . THR   A 1 217 ? -38.206 -28.820 9.126  1.00 106.98 ? 432 THR   B O   1 
ATOM   1596 C CB  . THR   A 1 217 ? -36.342 -28.648 7.126  1.00 101.94 ? 432 THR   B CB  1 
ATOM   1597 O OG1 . THR   A 1 217 ? -35.727 -29.247 8.274  1.00 107.86 ? 432 THR   B OG1 1 
ATOM   1598 C CG2 . THR   A 1 217 ? -35.273 -28.356 6.095  1.00 98.29  ? 432 THR   B CG2 1 
ATOM   1599 N N   . SER   A 1 218 ? -39.388 -27.051 8.397  1.00 121.30 ? 433 SER   B N   1 
ATOM   1600 C CA  . SER   A 1 218 ? -40.348 -27.060 9.506  1.00 124.90 ? 433 SER   B CA  1 
ATOM   1601 C C   . SER   A 1 218 ? -41.203 -28.332 9.550  1.00 127.71 ? 433 SER   B C   1 
ATOM   1602 O O   . SER   A 1 218 ? -42.433 -28.300 9.522  1.00 130.78 ? 433 SER   B O   1 
ATOM   1603 C CB  . SER   A 1 218 ? -41.244 -25.833 9.457  1.00 126.34 ? 433 SER   B CB  1 
ATOM   1604 O OG  . SER   A 1 218 ? -42.553 -26.223 9.075  1.00 127.35 ? 433 SER   B OG  1 
ATOM   1605 N N   . GLU   A 1 219 ? -40.520 -29.469 9.596  1.00 113.77 ? 434 GLU   B N   1 
ATOM   1606 C CA  . GLU   A 1 219 ? -40.948 -30.529 10.494 1.00 104.93 ? 434 GLU   B CA  1 
ATOM   1607 C C   . GLU   A 1 219 ? -40.270 -30.349 11.834 1.00 100.32 ? 434 GLU   B C   1 
ATOM   1608 O O   . GLU   A 1 219 ? -40.859 -30.636 12.879 1.00 101.87 ? 434 GLU   B O   1 
ATOM   1609 C CB  . GLU   A 1 219 ? -40.607 -31.913 9.928  1.00 108.30 ? 434 GLU   B CB  1 
ATOM   1610 C CG  . GLU   A 1 219 ? -40.963 -32.160 8.465  1.00 106.86 ? 434 GLU   B CG  1 
ATOM   1611 C CD  . GLU   A 1 219 ? -40.976 -33.645 8.142  1.00 109.75 ? 434 GLU   B CD  1 
ATOM   1612 O OE1 . GLU   A 1 219 ? -40.357 -34.416 8.904  1.00 105.94 ? 434 GLU   B OE1 1 
ATOM   1613 O OE2 . GLU   A 1 219 ? -41.617 -34.050 7.145  1.00 112.73 ? 434 GLU   B OE2 1 
ATOM   1614 N N   . ARG   A 1 220 ? -39.033 -29.872 11.795 1.00 92.71  ? 435 ARG   B N   1 
ATOM   1615 C CA  . ARG   A 1 220 ? -38.348 -29.362 12.967 1.00 90.01  ? 435 ARG   B CA  1 
ATOM   1616 C C   . ARG   A 1 220 ? -38.813 -27.943 13.238 1.00 91.13  ? 435 ARG   B C   1 
ATOM   1617 O O   . ARG   A 1 220 ? -38.826 -27.099 12.333 1.00 89.91  ? 435 ARG   B O   1 
ATOM   1618 C CB  . ARG   A 1 220 ? -36.838 -29.378 12.746 1.00 83.82  ? 435 ARG   B CB  1 
ATOM   1619 C CG  . ARG   A 1 220 ? -36.382 -30.404 11.739 1.00 82.06  ? 435 ARG   B CG  1 
ATOM   1620 C CD  . ARG   A 1 220 ? -34.905 -30.252 11.402 1.00 81.54  ? 435 ARG   B CD  1 
ATOM   1621 N NE  . ARG   A 1 220 ? -34.037 -30.233 12.576 1.00 80.00  ? 435 ARG   B NE  1 
ATOM   1622 C CZ  . ARG   A 1 220 ? -32.808 -30.736 12.605 1.00 78.86  ? 435 ARG   B CZ  1 
ATOM   1623 N NH1 . ARG   A 1 220 ? -32.269 -31.305 11.535 1.00 78.45  ? 435 ARG   B NH1 1 
ATOM   1624 N NH2 . ARG   A 1 220 ? -32.103 -30.670 13.734 1.00 77.94  ? 435 ARG   B NH2 1 
ATOM   1625 N N   . GLY   A 1 221 ? -39.197 -27.674 14.479 1.00 80.78  ? 436 GLY   B N   1 
ATOM   1626 C CA  . GLY   A 1 221 ? -39.514 -26.309 14.839 1.00 75.49  ? 436 GLY   B CA  1 
ATOM   1627 C C   . GLY   A 1 221 ? -38.233 -25.524 15.004 1.00 71.58  ? 436 GLY   B C   1 
ATOM   1628 O O   . GLY   A 1 221 ? -37.190 -25.953 14.497 1.00 74.75  ? 436 GLY   B O   1 
ATOM   1629 N N   . ALA   A 1 222 ? -38.272 -24.401 15.722 1.00 68.18  ? 437 ALA   B N   1 
ATOM   1630 C CA  . ALA   A 1 222 ? -37.062 -23.608 15.850 1.00 62.13  ? 437 ALA   B CA  1 
ATOM   1631 C C   . ALA   A 1 222 ? -35.994 -24.404 16.590 1.00 64.49  ? 437 ALA   B C   1 
ATOM   1632 O O   . ALA   A 1 222 ? -36.232 -25.502 17.100 1.00 70.55  ? 437 ALA   B O   1 
ATOM   1633 C CB  . ALA   A 1 222 ? -37.343 -22.283 16.553 1.00 60.20  ? 437 ALA   B CB  1 
ATOM   1634 N N   . GLN   A 1 223 ? -34.794 -23.843 16.618 1.00 60.44  ? 438 GLN   B N   1 
ATOM   1635 C CA  . GLN   A 1 223 ? -33.621 -24.476 17.209 1.00 61.54  ? 438 GLN   B CA  1 
ATOM   1636 C C   . GLN   A 1 223 ? -32.555 -23.392 17.242 1.00 58.25  ? 438 GLN   B C   1 
ATOM   1637 O O   . GLN   A 1 223 ? -32.719 -22.340 16.617 1.00 56.65  ? 438 GLN   B O   1 
ATOM   1638 C CB  . GLN   A 1 223 ? -33.178 -25.701 16.402 1.00 68.67  ? 438 GLN   B CB  1 
ATOM   1639 C CG  . GLN   A 1 223 ? -33.195 -27.003 17.174 1.00 75.84  ? 438 GLN   B CG  1 
ATOM   1640 C CD  . GLN   A 1 223 ? -32.674 -28.166 16.342 1.00 81.16  ? 438 GLN   B CD  1 
ATOM   1641 O OE1 . GLN   A 1 223 ? -32.663 -28.086 15.104 1.00 82.23  ? 438 GLN   B OE1 1 
ATOM   1642 N NE2 . GLN   A 1 223 ? -32.262 -29.265 17.010 1.00 73.74  ? 438 GLN   B NE2 1 
ATOM   1643 N N   . HIS   A 1 224 ? -31.472 -23.635 17.984 1.00 54.19  ? 439 HIS   B N   1 
ATOM   1644 C CA  . HIS   A 1 224 ? -30.495 -22.562 18.167 1.00 56.63  ? 439 HIS   B CA  1 
ATOM   1645 C C   . HIS   A 1 224 ? -29.188 -23.132 18.702 1.00 56.94  ? 439 HIS   B C   1 
ATOM   1646 O O   . HIS   A 1 224 ? -29.148 -24.216 19.288 1.00 56.03  ? 439 HIS   B O   1 
ATOM   1647 C CB  . HIS   A 1 224 ? -31.029 -21.457 19.110 1.00 56.57  ? 439 HIS   B CB  1 
ATOM   1648 C CG  . HIS   A 1 224 ? -31.201 -21.923 20.517 1.00 61.64  ? 439 HIS   B CG  1 
ATOM   1649 N ND1 . HIS   A 1 224 ? -30.253 -21.705 21.497 1.00 61.79  ? 439 HIS   B ND1 1 
ATOM   1650 C CD2 . HIS   A 1 224 ? -32.167 -22.682 21.088 1.00 56.75  ? 439 HIS   B CD2 1 
ATOM   1651 C CE1 . HIS   A 1 224 ? -30.645 -22.281 22.618 1.00 57.74  ? 439 HIS   B CE1 1 
ATOM   1652 N NE2 . HIS   A 1 224 ? -31.797 -22.888 22.392 1.00 59.94  ? 439 HIS   B NE2 1 
ATOM   1653 N N   . HIS   A 1 225 ? -28.113 -22.377 18.481 1.00 60.44  ? 440 HIS   B N   1 
ATOM   1654 C CA  . HIS   A 1 225 ? -26.790 -22.668 19.021 1.00 63.14  ? 440 HIS   B CA  1 
ATOM   1655 C C   . HIS   A 1 225 ? -26.244 -21.379 19.626 1.00 61.50  ? 440 HIS   B C   1 
ATOM   1656 O O   . HIS   A 1 225 ? -26.345 -20.313 19.009 1.00 59.36  ? 440 HIS   B O   1 
ATOM   1657 C CB  . HIS   A 1 225 ? -25.848 -23.209 17.929 1.00 66.13  ? 440 HIS   B CB  1 
ATOM   1658 C CG  . HIS   A 1 225 ? -24.775 -24.122 18.439 1.00 69.85  ? 440 HIS   B CG  1 
ATOM   1659 N ND1 . HIS   A 1 225 ? -24.060 -23.867 19.590 1.00 69.52  ? 440 HIS   B ND1 1 
ATOM   1660 C CD2 . HIS   A 1 225 ? -24.268 -25.272 17.934 1.00 79.61  ? 440 HIS   B CD2 1 
ATOM   1661 C CE1 . HIS   A 1 225 ? -23.174 -24.829 19.783 1.00 74.93  ? 440 HIS   B CE1 1 
ATOM   1662 N NE2 . HIS   A 1 225 ? -23.274 -25.690 18.787 1.00 79.62  ? 440 HIS   B NE2 1 
ATOM   1663 N N   . ILE   A 1 226 ? -25.692 -21.471 20.835 1.00 57.89  ? 441 ILE   B N   1 
ATOM   1664 C CA  . ILE   A 1 226 ? -25.137 -20.325 21.541 1.00 60.96  ? 441 ILE   B CA  1 
ATOM   1665 C C   . ILE   A 1 226 ? -23.623 -20.466 21.554 1.00 64.56  ? 441 ILE   B C   1 
ATOM   1666 O O   . ILE   A 1 226 ? -23.099 -21.546 21.850 1.00 63.99  ? 441 ILE   B O   1 
ATOM   1667 C CB  . ILE   A 1 226 ? -25.690 -20.213 22.974 1.00 62.71  ? 441 ILE   B CB  1 
ATOM   1668 C CG1 . ILE   A 1 226 ? -27.198 -19.950 22.965 1.00 59.15  ? 441 ILE   B CG1 1 
ATOM   1669 C CG2 . ILE   A 1 226 ? -24.967 -19.120 23.751 1.00 60.30  ? 441 ILE   B CG2 1 
ATOM   1670 C CD1 . ILE   A 1 226 ? -27.909 -20.486 24.191 1.00 52.79  ? 441 ILE   B CD1 1 
ATOM   1671 N N   . TYR   A 1 227 ? -22.921 -19.380 21.219 1.00 63.01  ? 442 TYR   B N   1 
ATOM   1672 C CA  . TYR   A 1 227 ? -21.467 -19.372 21.171 1.00 67.18  ? 442 TYR   B CA  1 
ATOM   1673 C C   . TYR   A 1 227 ? -20.955 -18.217 22.004 1.00 64.13  ? 442 TYR   B C   1 
ATOM   1674 O O   . TYR   A 1 227 ? -21.621 -17.191 22.124 1.00 59.86  ? 442 TYR   B O   1 
ATOM   1675 C CB  . TYR   A 1 227 ? -20.903 -19.213 19.726 1.00 69.93  ? 442 TYR   B CB  1 
ATOM   1676 C CG  . TYR   A 1 227 ? -21.212 -20.344 18.785 1.00 67.30  ? 442 TYR   B CG  1 
ATOM   1677 C CD1 . TYR   A 1 227 ? -22.373 -20.337 18.032 1.00 63.37  ? 442 TYR   B CD1 1 
ATOM   1678 C CD2 . TYR   A 1 227 ? -20.337 -21.412 18.644 1.00 74.70  ? 442 TYR   B CD2 1 
ATOM   1679 C CE1 . TYR   A 1 227 ? -22.671 -21.369 17.179 1.00 70.30  ? 442 TYR   B CE1 1 
ATOM   1680 C CE2 . TYR   A 1 227 ? -20.618 -22.455 17.783 1.00 76.03  ? 442 TYR   B CE2 1 
ATOM   1681 C CZ  . TYR   A 1 227 ? -21.788 -22.426 17.049 1.00 76.30  ? 442 TYR   B CZ  1 
ATOM   1682 O OH  . TYR   A 1 227 ? -22.083 -23.457 16.188 1.00 82.97  ? 442 TYR   B OH  1 
ATOM   1683 N N   . ARG   A 1 228 ? -19.753 -18.386 22.549 1.00 68.92  ? 443 ARG   B N   1 
ATOM   1684 C CA  . ARG   A 1 228 ? -19.006 -17.286 23.148 1.00 68.86  ? 443 ARG   B CA  1 
ATOM   1685 C C   . ARG   A 1 228 ? -18.220 -16.554 22.065 1.00 68.69  ? 443 ARG   B C   1 
ATOM   1686 O O   . ARG   A 1 228 ? -17.411 -17.170 21.373 1.00 72.95  ? 443 ARG   B O   1 
ATOM   1687 C CB  . ARG   A 1 228 ? -18.046 -17.816 24.209 1.00 75.05  ? 443 ARG   B CB  1 
ATOM   1688 C CG  . ARG   A 1 228 ? -18.717 -18.316 25.480 1.00 77.28  ? 443 ARG   B CG  1 
ATOM   1689 C CD  . ARG   A 1 228 ? -17.926 -19.442 26.146 1.00 80.51  ? 443 ARG   B CD  1 
ATOM   1690 N NE  . ARG   A 1 228 ? -16.489 -19.194 26.172 1.00 84.36  ? 443 ARG   B NE  1 
ATOM   1691 C CZ  . ARG   A 1 228 ? -15.563 -20.115 25.930 1.00 89.30  ? 443 ARG   B CZ  1 
ATOM   1692 N NH1 . ARG   A 1 228 ? -15.886 -21.367 25.639 1.00 87.04  ? 443 ARG   B NH1 1 
ATOM   1693 N NH2 . ARG   A 1 228 ? -14.277 -19.775 25.991 1.00 88.76  ? 443 ARG   B NH2 1 
ATOM   1694 N N   . LEU   A 1 229 ? -18.441 -15.250 21.923 1.00 67.46  ? 444 LEU   B N   1 
ATOM   1695 C CA  . LEU   A 1 229 ? -17.630 -14.433 21.028 1.00 67.31  ? 444 LEU   B CA  1 
ATOM   1696 C C   . LEU   A 1 229 ? -16.287 -14.113 21.680 1.00 72.92  ? 444 LEU   B C   1 
ATOM   1697 O O   . LEU   A 1 229 ? -16.237 -13.571 22.793 1.00 71.09  ? 444 LEU   B O   1 
ATOM   1698 C CB  . LEU   A 1 229 ? -18.365 -13.142 20.670 1.00 66.24  ? 444 LEU   B CB  1 
ATOM   1699 C CG  . LEU   A 1 229 ? -19.538 -13.320 19.708 1.00 64.34  ? 444 LEU   B CG  1 
ATOM   1700 C CD1 . LEU   A 1 229 ? -20.160 -11.986 19.290 1.00 57.42  ? 444 LEU   B CD1 1 
ATOM   1701 C CD2 . LEU   A 1 229 ? -19.049 -14.085 18.506 1.00 69.26  ? 444 LEU   B CD2 1 
ATOM   1702 N N   . VAL   A 1 230 ? -15.196 -14.429 20.973 1.00 77.33  ? 445 VAL   B N   1 
ATOM   1703 C CA  . VAL   A 1 230 ? -13.840 -14.338 21.505 1.00 78.78  ? 445 VAL   B CA  1 
ATOM   1704 C C   . VAL   A 1 230 ? -12.932 -13.645 20.488 1.00 81.29  ? 445 VAL   B C   1 
ATOM   1705 O O   . VAL   A 1 230 ? -13.367 -13.214 19.420 1.00 81.15  ? 445 VAL   B O   1 
ATOM   1706 C CB  . VAL   A 1 230 ? -13.271 -15.718 21.885 1.00 77.63  ? 445 VAL   B CB  1 
ATOM   1707 C CG1 . VAL   A 1 230 ? -14.040 -16.307 23.073 1.00 73.53  ? 445 VAL   B CG1 1 
ATOM   1708 C CG2 . VAL   A 1 230 ? -13.312 -16.634 20.684 1.00 74.42  ? 445 VAL   B CG2 1 
ATOM   1709 N N   . ARG   A 1 231 ? -11.651 -13.552 20.842 1.00 81.83  ? 446 ARG   B N   1 
ATOM   1710 C CA  . ARG   A 1 231 ? -10.677 -12.753 20.102 1.00 85.31  ? 446 ARG   B CA  1 
ATOM   1711 C C   . ARG   A 1 231 ? -9.281  -12.925 20.700 1.00 82.88  ? 446 ARG   B C   1 
ATOM   1712 O O   . ARG   A 1 231 ? -8.310  -13.151 19.981 1.00 90.79  ? 446 ARG   B O   1 
ATOM   1713 C CB  . ARG   A 1 231 ? -11.082 -11.267 20.111 1.00 87.13  ? 446 ARG   B CB  1 
ATOM   1714 C CG  . ARG   A 1 231 ? -10.412 -10.394 19.037 1.00 91.41  ? 446 ARG   B CG  1 
ATOM   1715 C CD  . ARG   A 1 231 ? -11.225 -9.127  18.760 1.00 88.46  ? 446 ARG   B CD  1 
ATOM   1716 N NE  . ARG   A 1 231 ? -10.824 -8.011  19.611 1.00 92.32  ? 446 ARG   B NE  1 
ATOM   1717 C CZ  . ARG   A 1 231 ? -11.330 -6.784  19.542 1.00 93.58  ? 446 ARG   B CZ  1 
ATOM   1718 N NH1 . ARG   A 1 231 ? -12.264 -6.467  18.658 1.00 92.52  ? 446 ARG   B NH1 1 
ATOM   1719 N NH2 . ARG   A 1 231 ? -10.910 -5.860  20.402 1.00 94.12  ? 446 ARG   B NH2 1 
ATOM   1720 N N   . GLY   B 1 7   ? -47.629 27.902  26.411 1.00 91.77  ? 222 GLY   A N   1 
ATOM   1721 C CA  . GLY   B 1 7   ? -46.587 26.949  26.766 1.00 91.11  ? 222 GLY   A CA  1 
ATOM   1722 C C   . GLY   B 1 7   ? -46.725 25.580  26.116 1.00 95.31  ? 222 GLY   A C   1 
ATOM   1723 O O   . GLY   B 1 7   ? -47.789 25.221  25.610 1.00 99.22  ? 222 GLY   A O   1 
ATOM   1724 N N   . LEU   B 1 8   ? -45.640 24.807  26.126 1.00 78.40  ? 223 LEU   A N   1 
ATOM   1725 C CA  . LEU   B 1 8   ? -45.652 23.433  25.621 1.00 75.62  ? 223 LEU   A CA  1 
ATOM   1726 C C   . LEU   B 1 8   ? -46.088 22.485  26.746 1.00 76.74  ? 223 LEU   A C   1 
ATOM   1727 O O   . LEU   B 1 8   ? -45.274 21.841  27.411 1.00 74.75  ? 223 LEU   A O   1 
ATOM   1728 C CB  . LEU   B 1 8   ? -44.276 23.082  25.066 1.00 71.73  ? 223 LEU   A CB  1 
ATOM   1729 C CG  . LEU   B 1 8   ? -43.928 21.704  24.497 1.00 68.88  ? 223 LEU   A CG  1 
ATOM   1730 C CD1 . LEU   B 1 8   ? -45.103 21.061  23.814 1.00 68.11  ? 223 LEU   A CD1 1 
ATOM   1731 C CD2 . LEU   B 1 8   ? -42.734 21.807  23.543 1.00 68.03  ? 223 LEU   A CD2 1 
ATOM   1732 N N   . GLY   B 1 9   ? -47.402 22.399  26.961 1.00 72.74  ? 224 GLY   A N   1 
ATOM   1733 C CA  . GLY   B 1 9   ? -47.928 21.539  28.013 1.00 72.34  ? 224 GLY   A CA  1 
ATOM   1734 C C   . GLY   B 1 9   ? -49.445 21.506  28.014 1.00 69.35  ? 224 GLY   A C   1 
ATOM   1735 O O   . GLY   B 1 9   ? -50.106 22.130  27.182 1.00 73.71  ? 224 GLY   A O   1 
ATOM   1736 N N   . THR   B 1 10  ? -49.997 20.755  28.961 1.00 67.54  ? 225 THR   A N   1 
ATOM   1737 C CA  . THR   B 1 10  ? -51.438 20.741  29.205 1.00 68.84  ? 225 THR   A CA  1 
ATOM   1738 C C   . THR   B 1 10  ? -51.730 21.257  30.617 1.00 69.99  ? 225 THR   A C   1 
ATOM   1739 O O   . THR   B 1 10  ? -50.850 21.775  31.313 1.00 69.67  ? 225 THR   A O   1 
ATOM   1740 C CB  . THR   B 1 10  ? -52.016 19.339  29.026 1.00 67.60  ? 225 THR   A CB  1 
ATOM   1741 O OG1 . THR   B 1 10  ? -51.356 18.429  29.925 1.00 64.92  ? 225 THR   A OG1 1 
ATOM   1742 C CG2 . THR   B 1 10  ? -51.846 18.876  27.602 1.00 66.86  ? 225 THR   A CG2 1 
ATOM   1743 N N   . ALA   B 1 11  ? -52.987 21.108  31.043 1.00 70.51  ? 226 ALA   A N   1 
ATOM   1744 C CA  . ALA   B 1 11  ? -53.296 21.305  32.457 1.00 69.01  ? 226 ALA   A CA  1 
ATOM   1745 C C   . ALA   B 1 11  ? -52.618 20.251  33.323 1.00 67.91  ? 226 ALA   A C   1 
ATOM   1746 O O   . ALA   B 1 11  ? -52.256 20.534  34.468 1.00 68.06  ? 226 ALA   A O   1 
ATOM   1747 C CB  . ALA   B 1 11  ? -54.805 21.272  32.687 1.00 66.53  ? 226 ALA   A CB  1 
ATOM   1748 N N   . ARG   B 1 12  ? -52.412 19.050  32.784 1.00 64.68  ? 227 ARG   A N   1 
ATOM   1749 C CA  . ARG   B 1 12  ? -51.958 17.911  33.558 1.00 60.81  ? 227 ARG   A CA  1 
ATOM   1750 C C   . ARG   B 1 12  ? -50.459 17.691  33.511 1.00 63.77  ? 227 ARG   A C   1 
ATOM   1751 O O   . ARG   B 1 12  ? -49.902 17.117  34.448 1.00 65.00  ? 227 ARG   A O   1 
ATOM   1752 C CB  . ARG   B 1 12  ? -52.660 16.647  33.067 1.00 68.61  ? 227 ARG   A CB  1 
ATOM   1753 C CG  . ARG   B 1 12  ? -54.168 16.682  33.228 1.00 73.10  ? 227 ARG   A CG  1 
ATOM   1754 C CD  . ARG   B 1 12  ? -54.765 15.326  32.908 1.00 76.32  ? 227 ARG   A CD  1 
ATOM   1755 N NE  . ARG   B 1 12  ? -54.154 14.243  33.670 1.00 73.92  ? 227 ARG   A NE  1 
ATOM   1756 C CZ  . ARG   B 1 12  ? -54.404 12.961  33.454 1.00 75.53  ? 227 ARG   A CZ  1 
ATOM   1757 N NH1 . ARG   B 1 12  ? -55.241 12.573  32.506 1.00 76.95  ? 227 ARG   A NH1 1 
ATOM   1758 N NH2 . ARG   B 1 12  ? -53.810 12.047  34.216 1.00 75.65  ? 227 ARG   A NH2 1 
ATOM   1759 N N   . LEU   B 1 13  ? -49.790 18.106  32.442 1.00 68.91  ? 228 LEU   A N   1 
ATOM   1760 C CA  . LEU   B 1 13  ? -48.353 17.926  32.327 1.00 64.73  ? 228 LEU   A CA  1 
ATOM   1761 C C   . LEU   B 1 13  ? -47.790 19.097  31.536 1.00 68.40  ? 228 LEU   A C   1 
ATOM   1762 O O   . LEU   B 1 13  ? -48.454 19.630  30.642 1.00 67.80  ? 228 LEU   A O   1 
ATOM   1763 C CB  . LEU   B 1 13  ? -48.022 16.596  31.658 1.00 58.98  ? 228 LEU   A CB  1 
ATOM   1764 C CG  . LEU   B 1 13  ? -46.561 16.167  31.605 1.00 64.06  ? 228 LEU   A CG  1 
ATOM   1765 C CD1 . LEU   B 1 13  ? -46.003 15.835  32.971 1.00 63.16  ? 228 LEU   A CD1 1 
ATOM   1766 C CD2 . LEU   B 1 13  ? -46.424 14.976  30.662 1.00 68.31  ? 228 LEU   A CD2 1 
ATOM   1767 N N   . GLN   B 1 14  ? -46.581 19.519  31.896 1.00 67.30  ? 229 GLN   A N   1 
ATOM   1768 C CA  . GLN   B 1 14  ? -45.917 20.616  31.213 1.00 66.24  ? 229 GLN   A CA  1 
ATOM   1769 C C   . GLN   B 1 14  ? -44.437 20.318  31.130 1.00 68.70  ? 229 GLN   A C   1 
ATOM   1770 O O   . GLN   B 1 14  ? -43.824 19.896  32.120 1.00 68.21  ? 229 GLN   A O   1 
ATOM   1771 C CB  . GLN   B 1 14  ? -46.106 21.964  31.922 1.00 65.02  ? 229 GLN   A CB  1 
ATOM   1772 C CG  . GLN   B 1 14  ? -47.535 22.396  31.974 1.00 69.66  ? 229 GLN   A CG  1 
ATOM   1773 C CD  . GLN   B 1 14  ? -48.089 22.313  33.387 1.00 74.25  ? 229 GLN   A CD  1 
ATOM   1774 O OE1 . GLN   B 1 14  ? -47.334 22.261  34.376 1.00 74.48  ? 229 GLN   A OE1 1 
ATOM   1775 N NE2 . GLN   B 1 14  ? -49.411 22.196  33.486 1.00 72.11  ? 229 GLN   A NE2 1 
ATOM   1776 N N   . LEU   B 1 15  ? -43.874 20.563  29.944 1.00 67.73  ? 230 LEU   A N   1 
ATOM   1777 C CA  . LEU   B 1 15  ? -42.445 20.412  29.723 1.00 71.39  ? 230 LEU   A CA  1 
ATOM   1778 C C   . LEU   B 1 15  ? -41.736 21.656  30.219 1.00 71.49  ? 230 LEU   A C   1 
ATOM   1779 O O   . LEU   B 1 15  ? -42.123 22.780  29.891 1.00 69.70  ? 230 LEU   A O   1 
ATOM   1780 C CB  . LEU   B 1 15  ? -42.132 20.167  28.243 1.00 73.26  ? 230 LEU   A CB  1 
ATOM   1781 C CG  . LEU   B 1 15  ? -40.759 20.542  27.664 1.00 69.02  ? 230 LEU   A CG  1 
ATOM   1782 C CD1 . LEU   B 1 15  ? -39.620 19.710  28.219 1.00 67.83  ? 230 LEU   A CD1 1 
ATOM   1783 C CD2 . LEU   B 1 15  ? -40.830 20.389  26.175 1.00 69.22  ? 230 LEU   A CD2 1 
ATOM   1784 N N   . VAL   B 1 16  ? -40.698 21.440  31.017 1.00 73.96  ? 231 VAL   A N   1 
ATOM   1785 C CA  . VAL   B 1 16  ? -39.966 22.507  31.675 1.00 77.58  ? 231 VAL   A CA  1 
ATOM   1786 C C   . VAL   B 1 16  ? -38.642 22.786  30.975 1.00 80.21  ? 231 VAL   A C   1 
ATOM   1787 O O   . VAL   B 1 16  ? -38.281 23.946  30.757 1.00 85.40  ? 231 VAL   A O   1 
ATOM   1788 C CB  . VAL   B 1 16  ? -39.763 22.129  33.163 1.00 82.12  ? 231 VAL   A CB  1 
ATOM   1789 C CG1 . VAL   B 1 16  ? -38.839 23.097  33.862 1.00 90.90  ? 231 VAL   A CG1 1 
ATOM   1790 C CG2 . VAL   B 1 16  ? -41.112 22.047  33.882 1.00 71.57  ? 231 VAL   A CG2 1 
ATOM   1791 N N   . GLU   B 1 17  ? -37.942 21.722  30.583 1.00 78.26  ? 232 GLU   A N   1 
ATOM   1792 C CA  . GLU   B 1 17  ? -36.637 21.811  29.945 1.00 76.47  ? 232 GLU   A CA  1 
ATOM   1793 C C   . GLU   B 1 17  ? -36.465 20.632  29.003 1.00 73.39  ? 232 GLU   A C   1 
ATOM   1794 O O   . GLU   B 1 17  ? -36.571 19.480  29.430 1.00 73.11  ? 232 GLU   A O   1 
ATOM   1795 C CB  . GLU   B 1 17  ? -35.529 21.806  30.989 1.00 82.77  ? 232 GLU   A CB  1 
ATOM   1796 C CG  . GLU   B 1 17  ? -34.196 22.194  30.428 1.00 82.91  ? 232 GLU   A CG  1 
ATOM   1797 C CD  . GLU   B 1 17  ? -33.837 23.591  30.823 1.00 91.16  ? 232 GLU   A CD  1 
ATOM   1798 O OE1 . GLU   B 1 17  ? -34.707 24.275  31.410 1.00 96.41  ? 232 GLU   A OE1 1 
ATOM   1799 O OE2 . GLU   B 1 17  ? -32.701 24.014  30.541 1.00 92.97  ? 232 GLU   A OE2 1 
ATOM   1800 N N   . PHE   B 1 18  ? -36.184 20.908  27.738 1.00 75.99  ? 233 PHE   A N   1 
ATOM   1801 C CA  . PHE   B 1 18  ? -35.676 19.889  26.826 1.00 73.01  ? 233 PHE   A CA  1 
ATOM   1802 C C   . PHE   B 1 18  ? -34.355 20.350  26.220 1.00 72.00  ? 233 PHE   A C   1 
ATOM   1803 O O   . PHE   B 1 18  ? -34.176 21.534  25.928 1.00 71.18  ? 233 PHE   A O   1 
ATOM   1804 C CB  . PHE   B 1 18  ? -36.651 19.557  25.693 1.00 67.12  ? 233 PHE   A CB  1 
ATOM   1805 C CG  . PHE   B 1 18  ? -36.114 18.540  24.770 1.00 70.21  ? 233 PHE   A CG  1 
ATOM   1806 C CD1 . PHE   B 1 18  ? -36.046 17.213  25.162 1.00 70.75  ? 233 PHE   A CD1 1 
ATOM   1807 C CD2 . PHE   B 1 18  ? -35.574 18.906  23.545 1.00 74.11  ? 233 PHE   A CD2 1 
ATOM   1808 C CE1 . PHE   B 1 18  ? -35.499 16.254  24.324 1.00 70.95  ? 233 PHE   A CE1 1 
ATOM   1809 C CE2 . PHE   B 1 18  ? -35.019 17.949  22.693 1.00 68.82  ? 233 PHE   A CE2 1 
ATOM   1810 C CZ  . PHE   B 1 18  ? -34.984 16.626  23.083 1.00 69.24  ? 233 PHE   A CZ  1 
ATOM   1811 N N   . SER   B 1 19  ? -33.435 19.408  26.020 1.00 77.51  ? 234 SER   A N   1 
ATOM   1812 C CA  . SER   B 1 19  ? -32.138 19.713  25.430 1.00 75.39  ? 234 SER   A CA  1 
ATOM   1813 C C   . SER   B 1 19  ? -31.466 18.431  24.939 1.00 73.61  ? 234 SER   A C   1 
ATOM   1814 O O   . SER   B 1 19  ? -31.450 17.411  25.643 1.00 72.69  ? 234 SER   A O   1 
ATOM   1815 C CB  . SER   B 1 19  ? -31.226 20.436  26.434 1.00 75.61  ? 234 SER   A CB  1 
ATOM   1816 O OG  . SER   B 1 19  ? -30.748 19.569  27.445 1.00 76.93  ? 234 SER   A OG  1 
ATOM   1817 N N   . ALA   B 1 20  ? -30.913 18.495  23.731 1.00 71.48  ? 235 ALA   A N   1 
ATOM   1818 C CA  . ALA   B 1 20  ? -30.019 17.468  23.219 1.00 68.14  ? 235 ALA   A CA  1 
ATOM   1819 C C   . ALA   B 1 20  ? -28.666 18.123  23.041 1.00 64.06  ? 235 ALA   A C   1 
ATOM   1820 O O   . ALA   B 1 20  ? -28.587 19.251  22.550 1.00 64.13  ? 235 ALA   A O   1 
ATOM   1821 C CB  . ALA   B 1 20  ? -30.527 16.869  21.908 1.00 64.55  ? 235 ALA   A CB  1 
ATOM   1822 N N   . PHE   B 1 21  ? -27.612 17.428  23.463 1.00 59.74  ? 236 PHE   A N   1 
ATOM   1823 C CA  . PHE   B 1 21  ? -26.333 18.079  23.688 1.00 64.79  ? 236 PHE   A CA  1 
ATOM   1824 C C   . PHE   B 1 21  ? -25.209 17.072  23.541 1.00 71.64  ? 236 PHE   A C   1 
ATOM   1825 O O   . PHE   B 1 21  ? -25.426 15.861  23.612 1.00 75.29  ? 236 PHE   A O   1 
ATOM   1826 C CB  . PHE   B 1 21  ? -26.275 18.721  25.077 1.00 77.45  ? 236 PHE   A CB  1 
ATOM   1827 C CG  . PHE   B 1 21  ? -26.349 17.723  26.209 1.00 81.76  ? 236 PHE   A CG  1 
ATOM   1828 C CD1 . PHE   B 1 21  ? -27.571 17.225  26.638 1.00 75.46  ? 236 PHE   A CD1 1 
ATOM   1829 C CD2 . PHE   B 1 21  ? -25.195 17.279  26.837 1.00 85.33  ? 236 PHE   A CD2 1 
ATOM   1830 C CE1 . PHE   B 1 21  ? -27.634 16.309  27.640 1.00 73.51  ? 236 PHE   A CE1 1 
ATOM   1831 C CE2 . PHE   B 1 21  ? -25.264 16.364  27.854 1.00 84.97  ? 236 PHE   A CE2 1 
ATOM   1832 C CZ  . PHE   B 1 21  ? -26.486 15.881  28.252 1.00 81.03  ? 236 PHE   A CZ  1 
ATOM   1833 N N   . VAL   B 1 22  ? -24.001 17.588  23.324 1.00 72.97  ? 237 VAL   A N   1 
ATOM   1834 C CA  . VAL   B 1 22  ? -22.775 16.802  23.404 1.00 79.63  ? 237 VAL   A CA  1 
ATOM   1835 C C   . VAL   B 1 22  ? -21.837 17.503  24.380 1.00 84.98  ? 237 VAL   A C   1 
ATOM   1836 O O   . VAL   B 1 22  ? -21.654 18.723  24.308 1.00 84.49  ? 237 VAL   A O   1 
ATOM   1837 C CB  . VAL   B 1 22  ? -22.095 16.594  22.026 1.00 81.00  ? 237 VAL   A CB  1 
ATOM   1838 C CG1 . VAL   B 1 22  ? -21.834 17.921  21.273 1.00 73.76  ? 237 VAL   A CG1 1 
ATOM   1839 C CG2 . VAL   B 1 22  ? -20.806 15.802  22.177 1.00 77.62  ? 237 VAL   A CG2 1 
ATOM   1840 N N   . GLU   B 1 23  ? -21.283 16.742  25.316 1.00 94.27  ? 238 GLU   A N   1 
ATOM   1841 C CA  . GLU   B 1 23  ? -20.273 17.206  26.255 1.00 97.08  ? 238 GLU   A CA  1 
ATOM   1842 C C   . GLU   B 1 23  ? -18.909 16.725  25.813 1.00 101.24 ? 238 GLU   A C   1 
ATOM   1843 O O   . GLU   B 1 23  ? -18.787 15.594  25.331 1.00 103.45 ? 238 GLU   A O   1 
ATOM   1844 C CB  . GLU   B 1 23  ? -20.542 16.685  27.663 1.00 97.41  ? 238 GLU   A CB  1 
ATOM   1845 C CG  . GLU   B 1 23  ? -21.724 17.316  28.344 1.00 98.06  ? 238 GLU   A CG  1 
ATOM   1846 C CD  . GLU   B 1 23  ? -22.086 16.597  29.625 1.00 96.53  ? 238 GLU   A CD  1 
ATOM   1847 O OE1 . GLU   B 1 23  ? -22.255 17.273  30.666 1.00 99.12  ? 238 GLU   A OE1 1 
ATOM   1848 O OE2 . GLU   B 1 23  ? -22.194 15.353  29.589 1.00 92.32  ? 238 GLU   A OE2 1 
ATOM   1849 N N   . PRO   B 1 24  ? -17.874 17.545  25.972 1.00 106.07 ? 239 PRO   A N   1 
ATOM   1850 C CA  . PRO   B 1 24  ? -16.573 17.188  25.420 1.00 109.64 ? 239 PRO   A CA  1 
ATOM   1851 C C   . PRO   B 1 24  ? -16.066 15.894  26.025 1.00 112.69 ? 239 PRO   A C   1 
ATOM   1852 O O   . PRO   B 1 24  ? -16.446 15.522  27.154 1.00 109.78 ? 239 PRO   A O   1 
ATOM   1853 C CB  . PRO   B 1 24  ? -15.687 18.382  25.803 1.00 111.97 ? 239 PRO   A CB  1 
ATOM   1854 C CG  . PRO   B 1 24  ? -16.399 19.022  26.979 1.00 106.54 ? 239 PRO   A CG  1 
ATOM   1855 C CD  . PRO   B 1 24  ? -17.845 18.861  26.635 1.00 104.74 ? 239 PRO   A CD  1 
ATOM   1856 N N   . PRO   B 1 25  ? -15.220 15.148  25.291 1.00 116.44 ? 240 PRO   A N   1 
ATOM   1857 C CA  . PRO   B 1 25  ? -14.542 13.940  25.772 1.00 119.71 ? 240 PRO   A CA  1 
ATOM   1858 C C   . PRO   B 1 25  ? -13.773 14.156  27.077 1.00 121.18 ? 240 PRO   A C   1 
ATOM   1859 O O   . PRO   B 1 25  ? -13.733 13.249  27.911 1.00 118.66 ? 240 PRO   A O   1 
ATOM   1860 C CB  . PRO   B 1 25  ? -13.579 13.610  24.624 1.00 117.80 ? 240 PRO   A CB  1 
ATOM   1861 C CG  . PRO   B 1 25  ? -14.292 14.087  23.415 1.00 116.48 ? 240 PRO   A CG  1 
ATOM   1862 C CD  . PRO   B 1 25  ? -14.936 15.386  23.863 1.00 118.61 ? 240 PRO   A CD  1 
ATOM   1863 N N   . GLN   B 1 32  ? -17.426 23.314  28.969 1.00 124.15 ? 247 GLN   A N   1 
ATOM   1864 C CA  . GLN   B 1 32  ? -18.882 23.303  29.088 1.00 125.49 ? 247 GLN   A CA  1 
ATOM   1865 C C   . GLN   B 1 32  ? -19.514 22.205  28.236 1.00 121.72 ? 247 GLN   A C   1 
ATOM   1866 O O   . GLN   B 1 32  ? -19.125 21.046  28.334 1.00 120.06 ? 247 GLN   A O   1 
ATOM   1867 C CB  . GLN   B 1 32  ? -19.457 24.663  28.703 1.00 125.21 ? 247 GLN   A CB  1 
ATOM   1868 C CG  . GLN   B 1 32  ? -19.706 25.561  29.892 1.00 129.25 ? 247 GLN   A CG  1 
ATOM   1869 C CD  . GLN   B 1 32  ? -20.812 26.553  29.641 1.00 128.09 ? 247 GLN   A CD  1 
ATOM   1870 O OE1 . GLN   B 1 32  ? -20.648 27.748  29.879 1.00 124.97 ? 247 GLN   A OE1 1 
ATOM   1871 N NE2 . GLN   B 1 32  ? -21.948 26.065  29.148 1.00 124.46 ? 247 GLN   A NE2 1 
ATOM   1872 N N   . ARG   B 1 33  ? -20.488 22.572  27.406 1.00 120.41 ? 248 ARG   A N   1 
ATOM   1873 C CA  . ARG   B 1 33  ? -21.197 21.599  26.584 1.00 112.68 ? 248 ARG   A CA  1 
ATOM   1874 C C   . ARG   B 1 33  ? -21.899 22.332  25.453 1.00 110.09 ? 248 ARG   A C   1 
ATOM   1875 O O   . ARG   B 1 33  ? -22.213 23.521  25.562 1.00 112.44 ? 248 ARG   A O   1 
ATOM   1876 C CB  . ARG   B 1 33  ? -22.215 20.795  27.402 1.00 109.55 ? 248 ARG   A CB  1 
ATOM   1877 C CG  . ARG   B 1 33  ? -23.445 21.590  27.816 1.00 106.01 ? 248 ARG   A CG  1 
ATOM   1878 C CD  . ARG   B 1 33  ? -24.664 20.690  28.014 1.00 105.50 ? 248 ARG   A CD  1 
ATOM   1879 N NE  . ARG   B 1 33  ? -24.499 19.694  29.068 1.00 106.48 ? 248 ARG   A NE  1 
ATOM   1880 C CZ  . ARG   B 1 33  ? -25.505 19.133  29.734 1.00 108.52 ? 248 ARG   A CZ  1 
ATOM   1881 N NH1 . ARG   B 1 33  ? -26.768 19.441  29.475 1.00 108.58 ? 248 ARG   A NH1 1 
ATOM   1882 N NH2 . ARG   B 1 33  ? -25.238 18.241  30.687 1.00 108.69 ? 248 ARG   A NH2 1 
ATOM   1883 N N   . HIS   B 1 34  ? -22.156 21.599  24.370 1.00 88.00  ? 249 HIS   A N   1 
ATOM   1884 C CA  . HIS   B 1 34  ? -22.794 22.144  23.178 1.00 84.41  ? 249 HIS   A CA  1 
ATOM   1885 C C   . HIS   B 1 34  ? -24.225 21.641  23.084 1.00 78.07  ? 249 HIS   A C   1 
ATOM   1886 O O   . HIS   B 1 34  ? -24.460 20.435  23.126 1.00 79.89  ? 249 HIS   A O   1 
ATOM   1887 C CB  . HIS   B 1 34  ? -22.031 21.767  21.897 1.00 82.97  ? 249 HIS   A CB  1 
ATOM   1888 C CG  . HIS   B 1 34  ? -22.673 22.279  20.639 1.00 77.79  ? 249 HIS   A CG  1 
ATOM   1889 N ND1 . HIS   B 1 34  ? -22.414 23.532  20.128 1.00 78.27  ? 249 HIS   A ND1 1 
ATOM   1890 C CD2 . HIS   B 1 34  ? -23.580 21.716  19.805 1.00 75.00  ? 249 HIS   A CD2 1 
ATOM   1891 C CE1 . HIS   B 1 34  ? -23.125 23.717  19.031 1.00 78.49  ? 249 HIS   A CE1 1 
ATOM   1892 N NE2 . HIS   B 1 34  ? -23.849 22.634  18.819 1.00 75.03  ? 249 HIS   A NE2 1 
ATOM   1893 N N   . LEU   B 1 35  ? -25.165 22.563  22.912 1.00 74.45  ? 250 LEU   A N   1 
ATOM   1894 C CA  . LEU   B 1 35  ? -26.588 22.261  22.797 1.00 70.89  ? 250 LEU   A CA  1 
ATOM   1895 C C   . LEU   B 1 35  ? -26.957 22.194  21.316 1.00 71.31  ? 250 LEU   A C   1 
ATOM   1896 O O   . LEU   B 1 35  ? -26.780 23.178  20.595 1.00 74.72  ? 250 LEU   A O   1 
ATOM   1897 C CB  . LEU   B 1 35  ? -27.400 23.357  23.485 1.00 70.98  ? 250 LEU   A CB  1 
ATOM   1898 C CG  . LEU   B 1 35  ? -27.656 23.425  24.992 1.00 71.02  ? 250 LEU   A CG  1 
ATOM   1899 C CD1 . LEU   B 1 35  ? -28.877 22.620  25.316 1.00 72.09  ? 250 LEU   A CD1 1 
ATOM   1900 C CD2 . LEU   B 1 35  ? -26.455 22.936  25.784 1.00 73.05  ? 250 LEU   A CD2 1 
ATOM   1901 N N   . PHE   B 1 36  ? -27.476 21.056  20.856 1.00 69.34  ? 251 PHE   A N   1 
ATOM   1902 C CA  . PHE   B 1 36  ? -28.035 21.017  19.503 1.00 66.56  ? 251 PHE   A CA  1 
ATOM   1903 C C   . PHE   B 1 36  ? -29.385 21.725  19.456 1.00 67.00  ? 251 PHE   A C   1 
ATOM   1904 O O   . PHE   B 1 36  ? -29.593 22.643  18.657 1.00 62.04  ? 251 PHE   A O   1 
ATOM   1905 C CB  . PHE   B 1 36  ? -28.174 19.568  19.021 1.00 68.02  ? 251 PHE   A CB  1 
ATOM   1906 C CG  . PHE   B 1 36  ? -26.899 18.786  19.064 1.00 63.99  ? 251 PHE   A CG  1 
ATOM   1907 C CD1 . PHE   B 1 36  ? -25.821 19.138  18.259 1.00 65.55  ? 251 PHE   A CD1 1 
ATOM   1908 C CD2 . PHE   B 1 36  ? -26.771 17.710  19.925 1.00 58.97  ? 251 PHE   A CD2 1 
ATOM   1909 C CE1 . PHE   B 1 36  ? -24.638 18.419  18.304 1.00 68.59  ? 251 PHE   A CE1 1 
ATOM   1910 C CE2 . PHE   B 1 36  ? -25.597 16.985  19.988 1.00 67.17  ? 251 PHE   A CE2 1 
ATOM   1911 C CZ  . PHE   B 1 36  ? -24.520 17.340  19.165 1.00 73.57  ? 251 PHE   A CZ  1 
ATOM   1912 N N   . VAL   B 1 37  ? -30.319 21.307  20.321 1.00 76.24  ? 252 VAL   A N   1 
ATOM   1913 C CA  . VAL   B 1 37  ? -31.600 21.979  20.513 1.00 74.81  ? 252 VAL   A CA  1 
ATOM   1914 C C   . VAL   B 1 37  ? -31.830 22.214  22.004 1.00 73.10  ? 252 VAL   A C   1 
ATOM   1915 O O   . VAL   B 1 37  ? -31.254 21.541  22.859 1.00 75.03  ? 252 VAL   A O   1 
ATOM   1916 C CB  . VAL   B 1 37  ? -32.761 21.179  19.898 1.00 72.49  ? 252 VAL   A CB  1 
ATOM   1917 C CG1 . VAL   B 1 37  ? -32.623 21.164  18.367 1.00 68.45  ? 252 VAL   A CG1 1 
ATOM   1918 C CG2 . VAL   B 1 37  ? -32.775 19.779  20.477 1.00 68.94  ? 252 VAL   A CG2 1 
ATOM   1919 N N   . HIS   B 1 38  ? -32.686 23.187  22.317 1.00 63.97  ? 253 HIS   A N   1 
ATOM   1920 C CA  . HIS   B 1 38  ? -32.823 23.622  23.704 1.00 69.64  ? 253 HIS   A CA  1 
ATOM   1921 C C   . HIS   B 1 38  ? -34.130 24.405  23.853 1.00 70.50  ? 253 HIS   A C   1 
ATOM   1922 O O   . HIS   B 1 38  ? -34.208 25.560  23.435 1.00 73.34  ? 253 HIS   A O   1 
ATOM   1923 C CB  . HIS   B 1 38  ? -31.614 24.448  24.130 1.00 67.16  ? 253 HIS   A CB  1 
ATOM   1924 C CG  . HIS   B 1 38  ? -31.628 24.848  25.571 1.00 74.37  ? 253 HIS   A CG  1 
ATOM   1925 N ND1 . HIS   B 1 38  ? -31.791 23.936  26.595 1.00 78.21  ? 253 HIS   A ND1 1 
ATOM   1926 C CD2 . HIS   B 1 38  ? -31.474 26.055  26.168 1.00 80.74  ? 253 HIS   A CD2 1 
ATOM   1927 C CE1 . HIS   B 1 38  ? -31.756 24.564  27.758 1.00 77.07  ? 253 HIS   A CE1 1 
ATOM   1928 N NE2 . HIS   B 1 38  ? -31.563 25.851  27.528 1.00 80.46  ? 253 HIS   A NE2 1 
ATOM   1929 N N   . ILE   B 1 39  ? -35.138 23.770  24.448 1.00 70.88  ? 254 ILE   A N   1 
ATOM   1930 C CA  . ILE   B 1 39  ? -36.368 24.435  24.870 1.00 71.70  ? 254 ILE   A CA  1 
ATOM   1931 C C   . ILE   B 1 39  ? -36.282 24.662  26.371 1.00 74.78  ? 254 ILE   A C   1 
ATOM   1932 O O   . ILE   B 1 39  ? -36.191 23.702  27.146 1.00 71.89  ? 254 ILE   A O   1 
ATOM   1933 C CB  . ILE   B 1 39  ? -37.613 23.603  24.532 1.00 72.89  ? 254 ILE   A CB  1 
ATOM   1934 C CG1 . ILE   B 1 39  ? -37.741 23.391  23.031 1.00 69.66  ? 254 ILE   A CG1 1 
ATOM   1935 C CG2 . ILE   B 1 39  ? -38.871 24.268  25.092 1.00 70.60  ? 254 ILE   A CG2 1 
ATOM   1936 C CD1 . ILE   B 1 39  ? -38.717 22.297  22.696 1.00 65.49  ? 254 ILE   A CD1 1 
ATOM   1937 N N   . SER   B 1 40  ? -36.311 25.925  26.786 1.00 77.11  ? 255 SER   A N   1 
ATOM   1938 C CA  . SER   B 1 40  ? -36.321 26.282  28.197 1.00 82.42  ? 255 SER   A CA  1 
ATOM   1939 C C   . SER   B 1 40  ? -37.610 27.026  28.510 1.00 82.80  ? 255 SER   A C   1 
ATOM   1940 O O   . SER   B 1 40  ? -38.045 27.883  27.740 1.00 82.92  ? 255 SER   A O   1 
ATOM   1941 C CB  . SER   B 1 40  ? -35.107 27.135  28.565 1.00 81.70  ? 255 SER   A CB  1 
ATOM   1942 O OG  . SER   B 1 40  ? -34.906 27.139  29.964 1.00 90.59  ? 255 SER   A OG  1 
ATOM   1943 N N   . GLN   B 1 41  ? -38.241 26.684  29.629 1.00 88.68  ? 256 GLN   A N   1 
ATOM   1944 C CA  . GLN   B 1 41  ? -39.514 27.321  29.940 1.00 98.49  ? 256 GLN   A CA  1 
ATOM   1945 C C   . GLN   B 1 41  ? -39.655 27.611  31.432 1.00 109.86 ? 256 GLN   A C   1 
ATOM   1946 O O   . GLN   B 1 41  ? -40.773 27.663  31.957 1.00 108.56 ? 256 GLN   A O   1 
ATOM   1947 C CB  . GLN   B 1 41  ? -40.681 26.457  29.451 1.00 90.21  ? 256 GLN   A CB  1 
ATOM   1948 C CG  . GLN   B 1 41  ? -40.752 26.271  27.936 1.00 79.05  ? 256 GLN   A CG  1 
ATOM   1949 C CD  . GLN   B 1 41  ? -42.092 25.723  27.472 1.00 75.62  ? 256 GLN   A CD  1 
ATOM   1950 O OE1 . GLN   B 1 41  ? -42.482 25.890  26.325 1.00 75.77  ? 256 GLN   A OE1 1 
ATOM   1951 N NE2 . GLN   B 1 41  ? -42.803 25.069  28.369 1.00 80.30  ? 256 GLN   A NE2 1 
ATOM   1952 N N   . HIS   B 1 42  ? -38.538 27.830  32.117 1.00 134.25 ? 257 HIS   A N   1 
ATOM   1953 C CA  . HIS   B 1 42  ? -38.501 27.853  33.578 1.00 138.66 ? 257 HIS   A CA  1 
ATOM   1954 C C   . HIS   B 1 42  ? -39.267 29.016  34.221 1.00 139.60 ? 257 HIS   A C   1 
ATOM   1955 O O   . HIS   B 1 42  ? -39.109 30.176  33.842 1.00 143.25 ? 257 HIS   A O   1 
ATOM   1956 C CB  . HIS   B 1 42  ? -37.039 27.867  34.027 1.00 139.72 ? 257 HIS   A CB  1 
ATOM   1957 C CG  . HIS   B 1 42  ? -36.479 26.501  34.283 1.00 138.36 ? 257 HIS   A CG  1 
ATOM   1958 N ND1 . HIS   B 1 42  ? -35.257 26.090  33.792 1.00 137.82 ? 257 HIS   A ND1 1 
ATOM   1959 C CD2 . HIS   B 1 42  ? -36.950 25.472  35.025 1.00 135.65 ? 257 HIS   A CD2 1 
ATOM   1960 C CE1 . HIS   B 1 42  ? -35.018 24.852  34.190 1.00 134.36 ? 257 HIS   A CE1 1 
ATOM   1961 N NE2 . HIS   B 1 42  ? -36.031 24.453  34.937 1.00 132.05 ? 257 HIS   A NE2 1 
ATOM   1962 N N   . PRO   B 1 50  ? -49.899 33.747  22.750 1.00 102.42 ? 265 PRO   A N   1 
ATOM   1963 C CA  . PRO   B 1 50  ? -50.638 32.511  22.501 1.00 96.31  ? 265 PRO   A CA  1 
ATOM   1964 C C   . PRO   B 1 50  ? -50.048 31.653  21.371 1.00 97.02  ? 265 PRO   A C   1 
ATOM   1965 O O   . PRO   B 1 50  ? -49.856 32.216  20.282 1.00 99.76  ? 265 PRO   A O   1 
ATOM   1966 C CB  . PRO   B 1 50  ? -52.039 33.013  22.132 1.00 98.62  ? 265 PRO   A CB  1 
ATOM   1967 C CG  . PRO   B 1 50  ? -51.824 34.495  21.696 1.00 102.50 ? 265 PRO   A CG  1 
ATOM   1968 C CD  . PRO   B 1 50  ? -50.355 34.800  21.840 1.00 101.05 ? 265 PRO   A CD  1 
ATOM   1969 N N   . LEU   B 1 51  ? -49.787 30.346  21.593 1.00 89.78  ? 266 LEU   A N   1 
ATOM   1970 C CA  . LEU   B 1 51  ? -49.104 29.556  20.569 1.00 90.50  ? 266 LEU   A CA  1 
ATOM   1971 C C   . LEU   B 1 51  ? -49.880 29.615  19.263 1.00 95.84  ? 266 LEU   A C   1 
ATOM   1972 O O   . LEU   B 1 51  ? -51.109 29.474  19.253 1.00 96.12  ? 266 LEU   A O   1 
ATOM   1973 C CB  . LEU   B 1 51  ? -48.921 28.095  20.993 1.00 84.23  ? 266 LEU   A CB  1 
ATOM   1974 C CG  . LEU   B 1 51  ? -47.999 27.727  22.155 1.00 83.04  ? 266 LEU   A CG  1 
ATOM   1975 C CD1 . LEU   B 1 51  ? -47.904 26.208  22.267 1.00 78.83  ? 266 LEU   A CD1 1 
ATOM   1976 C CD2 . LEU   B 1 51  ? -46.626 28.351  22.006 1.00 76.47  ? 266 LEU   A CD2 1 
ATOM   1977 N N   . GLU   B 1 52  ? -49.154 29.906  18.182 1.00 91.66  ? 267 GLU   A N   1 
ATOM   1978 C CA  . GLU   B 1 52  ? -49.669 29.751  16.833 1.00 89.91  ? 267 GLU   A CA  1 
ATOM   1979 C C   . GLU   B 1 52  ? -50.103 28.309  16.621 1.00 86.62  ? 267 GLU   A C   1 
ATOM   1980 O O   . GLU   B 1 52  ? -49.554 27.383  17.217 1.00 87.01  ? 267 GLU   A O   1 
ATOM   1981 C CB  . GLU   B 1 52  ? -48.590 30.108  15.814 1.00 95.05  ? 267 GLU   A CB  1 
ATOM   1982 C CG  . GLU   B 1 52  ? -48.792 31.397  15.045 1.00 99.57  ? 267 GLU   A CG  1 
ATOM   1983 C CD  . GLU   B 1 52  ? -47.654 31.639  14.057 1.00 104.70 ? 267 GLU   A CD  1 
ATOM   1984 O OE1 . GLU   B 1 52  ? -47.574 30.903  13.047 1.00 102.81 ? 267 GLU   A OE1 1 
ATOM   1985 O OE2 . GLU   B 1 52  ? -46.833 32.556  14.295 1.00 111.08 ? 267 GLU   A OE2 1 
ATOM   1986 N N   . SER   B 1 53  ? -51.094 28.113  15.765 1.00 87.60  ? 268 SER   A N   1 
ATOM   1987 C CA  . SER   B 1 53  ? -51.582 26.773  15.501 1.00 86.63  ? 268 SER   A CA  1 
ATOM   1988 C C   . SER   B 1 53  ? -51.142 26.316  14.118 1.00 91.74  ? 268 SER   A C   1 
ATOM   1989 O O   . SER   B 1 53  ? -50.826 27.122  13.241 1.00 96.17  ? 268 SER   A O   1 
ATOM   1990 C CB  . SER   B 1 53  ? -53.104 26.698  15.611 1.00 91.38  ? 268 SER   A CB  1 
ATOM   1991 O OG  . SER   B 1 53  ? -53.713 27.035  14.378 1.00 98.00  ? 268 SER   A OG  1 
ATOM   1992 N N   . VAL   B 1 54  ? -51.123 24.996  13.944 1.00 94.27  ? 269 VAL   A N   1 
ATOM   1993 C CA  . VAL   B 1 54  ? -50.698 24.334  12.710 1.00 95.95  ? 269 VAL   A CA  1 
ATOM   1994 C C   . VAL   B 1 54  ? -51.591 23.122  12.492 1.00 97.20  ? 269 VAL   A C   1 
ATOM   1995 O O   . VAL   B 1 54  ? -51.832 22.357  13.430 1.00 94.82  ? 269 VAL   A O   1 
ATOM   1996 C CB  . VAL   B 1 54  ? -49.221 23.903  12.776 1.00 90.40  ? 269 VAL   A CB  1 
ATOM   1997 C CG1 . VAL   B 1 54  ? -48.973 22.717  11.856 1.00 92.00  ? 269 VAL   A CG1 1 
ATOM   1998 C CG2 . VAL   B 1 54  ? -48.351 25.060  12.374 1.00 88.22  ? 269 VAL   A CG2 1 
ATOM   1999 N N   . ASP   B 1 55  ? -52.105 22.942  11.277 1.00 99.07  ? 270 ASP   A N   1 
ATOM   2000 C CA  . ASP   B 1 55  ? -53.052 21.854  11.103 1.00 99.81  ? 270 ASP   A CA  1 
ATOM   2001 C C   . ASP   B 1 55  ? -52.279 20.552  10.947 1.00 100.68 ? 270 ASP   A C   1 
ATOM   2002 O O   . ASP   B 1 55  ? -51.285 20.486  10.219 1.00 102.93 ? 270 ASP   A O   1 
ATOM   2003 C CB  . ASP   B 1 55  ? -54.000 22.092  9.926  1.00 107.07 ? 270 ASP   A CB  1 
ATOM   2004 C CG  . ASP   B 1 55  ? -55.029 20.967  9.778  1.00 110.45 ? 270 ASP   A CG  1 
ATOM   2005 O OD1 . ASP   B 1 55  ? -56.241 21.262  9.648  1.00 113.21 ? 270 ASP   A OD1 1 
ATOM   2006 O OD2 . ASP   B 1 55  ? -54.626 19.785  9.793  1.00 115.00 ? 270 ASP   A OD2 1 
ATOM   2007 N N   . VAL   B 1 56  ? -52.742 19.523  11.657 1.00 105.08 ? 271 VAL   A N   1 
ATOM   2008 C CA  . VAL   B 1 56  ? -52.060 18.247  11.701 1.00 102.87 ? 271 VAL   A CA  1 
ATOM   2009 C C   . VAL   B 1 56  ? -52.185 17.506  10.375 1.00 113.88 ? 271 VAL   A C   1 
ATOM   2010 O O   . VAL   B 1 56  ? -51.360 16.629  10.101 1.00 116.13 ? 271 VAL   A O   1 
ATOM   2011 C CB  . VAL   B 1 56  ? -52.588 17.434  12.909 1.00 96.99  ? 271 VAL   A CB  1 
ATOM   2012 C CG1 . VAL   B 1 56  ? -54.053 17.073  12.741 1.00 101.44 ? 271 VAL   A CG1 1 
ATOM   2013 C CG2 . VAL   B 1 56  ? -51.754 16.184  13.156 1.00 95.97  ? 271 VAL   A CG2 1 
ATOM   2014 N N   . ARG   B 1 57  ? -53.175 17.838  9.527  1.00 124.29 ? 272 ARG   A N   1 
ATOM   2015 C CA  . ARG   B 1 57  ? -53.183 17.267  8.176  1.00 125.89 ? 272 ARG   A CA  1 
ATOM   2016 C C   . ARG   B 1 57  ? -51.868 17.554  7.466  1.00 125.98 ? 272 ARG   A C   1 
ATOM   2017 O O   . ARG   B 1 57  ? -51.356 16.718  6.712  1.00 130.48 ? 272 ARG   A O   1 
ATOM   2018 C CB  . ARG   B 1 57  ? -54.325 17.814  7.303  1.00 127.53 ? 272 ARG   A CB  1 
ATOM   2019 C CG  . ARG   B 1 57  ? -55.721 17.977  7.883  1.00 128.68 ? 272 ARG   A CG  1 
ATOM   2020 C CD  . ARG   B 1 57  ? -56.501 19.107  7.156  1.00 130.16 ? 272 ARG   A CD  1 
ATOM   2021 N NE  . ARG   B 1 57  ? -55.740 20.337  6.898  1.00 132.82 ? 272 ARG   A NE  1 
ATOM   2022 C CZ  . ARG   B 1 57  ? -55.070 20.638  5.786  1.00 128.95 ? 272 ARG   A CZ  1 
ATOM   2023 N NH1 . ARG   B 1 57  ? -55.046 19.823  4.742  1.00 132.42 ? 272 ARG   A NH1 1 
ATOM   2024 N NH2 . ARG   B 1 57  ? -54.414 21.797  5.719  1.00 123.50 ? 272 ARG   A NH2 1 
ATOM   2025 N N   . GLN   B 1 58  ? -51.305 18.738  7.706  1.00 117.26 ? 273 GLN   A N   1 
ATOM   2026 C CA  . GLN   B 1 58  ? -50.154 19.240  6.973  1.00 111.93 ? 273 GLN   A CA  1 
ATOM   2027 C C   . GLN   B 1 58  ? -48.869 18.500  7.277  1.00 110.14 ? 273 GLN   A C   1 
ATOM   2028 O O   . GLN   B 1 58  ? -47.848 18.835  6.671  1.00 110.85 ? 273 GLN   A O   1 
ATOM   2029 C CB  . GLN   B 1 58  ? -49.974 20.721  7.276  1.00 107.85 ? 273 GLN   A CB  1 
ATOM   2030 C CG  . GLN   B 1 58  ? -51.267 21.471  7.126  1.00 109.31 ? 273 GLN   A CG  1 
ATOM   2031 C CD  . GLN   B 1 58  ? -51.101 22.721  6.320  1.00 107.15 ? 273 GLN   A CD  1 
ATOM   2032 O OE1 . GLN   B 1 58  ? -50.340 22.746  5.356  1.00 106.01 ? 273 GLN   A OE1 1 
ATOM   2033 N NE2 . GLN   B 1 58  ? -51.845 23.763  6.679  1.00 107.58 ? 273 GLN   A NE2 1 
ATOM   2034 N N   . ILE   B 1 59  ? -48.871 17.523  8.183  1.00 110.09 ? 274 ILE   A N   1 
ATOM   2035 C CA  . ILE   B 1 59  ? -47.648 16.786  8.482  1.00 108.95 ? 274 ILE   A CA  1 
ATOM   2036 C C   . ILE   B 1 59  ? -47.933 15.304  8.723  1.00 113.34 ? 274 ILE   A C   1 
ATOM   2037 O O   . ILE   B 1 59  ? -47.208 14.647  9.480  1.00 112.28 ? 274 ILE   A O   1 
ATOM   2038 C CB  . ILE   B 1 59  ? -46.917 17.404  9.690  1.00 104.31 ? 274 ILE   A CB  1 
ATOM   2039 C CG1 . ILE   B 1 59  ? -47.821 17.426  10.920 1.00 102.16 ? 274 ILE   A CG1 1 
ATOM   2040 C CG2 . ILE   B 1 59  ? -46.439 18.823  9.396  1.00 99.87  ? 274 ILE   A CG2 1 
ATOM   2041 C CD1 . ILE   B 1 59  ? -47.063 17.719  12.163 1.00 88.35  ? 274 ILE   A CD1 1 
ATOM   2042 N N   . TYR   B 1 60  ? -48.975 14.757  8.077  1.00 119.40 ? 275 TYR   A N   1 
ATOM   2043 C CA  . TYR   B 1 60  ? -49.286 13.329  8.218  1.00 123.13 ? 275 TYR   A CA  1 
ATOM   2044 C C   . TYR   B 1 60  ? -48.330 12.444  7.423  1.00 123.56 ? 275 TYR   A C   1 
ATOM   2045 O O   . TYR   B 1 60  ? -48.229 11.241  7.701  1.00 124.30 ? 275 TYR   A O   1 
ATOM   2046 C CB  . TYR   B 1 60  ? -50.722 13.035  7.763  1.00 125.55 ? 275 TYR   A CB  1 
ATOM   2047 C CG  . TYR   B 1 60  ? -51.830 13.333  8.766  1.00 122.86 ? 275 TYR   A CG  1 
ATOM   2048 C CD1 . TYR   B 1 60  ? -51.581 13.382  10.135 1.00 120.53 ? 275 TYR   A CD1 1 
ATOM   2049 C CD2 . TYR   B 1 60  ? -53.137 13.545  8.333  1.00 123.40 ? 275 TYR   A CD2 1 
ATOM   2050 C CE1 . TYR   B 1 60  ? -52.604 13.646  11.039 1.00 120.07 ? 275 TYR   A CE1 1 
ATOM   2051 C CE2 . TYR   B 1 60  ? -54.159 13.811  9.228  1.00 122.66 ? 275 TYR   A CE2 1 
ATOM   2052 C CZ  . TYR   B 1 60  ? -53.889 13.860  10.580 1.00 120.53 ? 275 TYR   A CZ  1 
ATOM   2053 O OH  . TYR   B 1 60  ? -54.907 14.123  11.472 1.00 118.17 ? 275 TYR   A OH  1 
ATOM   2054 N N   . ASP   B 1 61  ? -47.645 13.019  6.432  1.00 122.49 ? 276 ASP   A N   1 
ATOM   2055 C CA  . ASP   B 1 61  ? -46.707 12.308  5.572  1.00 121.71 ? 276 ASP   A CA  1 
ATOM   2056 C C   . ASP   B 1 61  ? -45.370 12.026  6.243  1.00 120.44 ? 276 ASP   A C   1 
ATOM   2057 O O   . ASP   B 1 61  ? -44.636 11.144  5.780  1.00 118.18 ? 276 ASP   A O   1 
ATOM   2058 C CB  . ASP   B 1 61  ? -46.457 13.135  4.311  1.00 121.23 ? 276 ASP   A CB  1 
ATOM   2059 C CG  . ASP   B 1 61  ? -46.161 14.594  4.628  1.00 118.74 ? 276 ASP   A CG  1 
ATOM   2060 O OD1 . ASP   B 1 61  ? -46.663 15.101  5.654  1.00 114.91 ? 276 ASP   A OD1 1 
ATOM   2061 O OD2 . ASP   B 1 61  ? -45.426 15.238  3.856  1.00 123.44 ? 276 ASP   A OD2 1 
ATOM   2062 N N   . LYS   B 1 62  ? -45.039 12.760  7.310  1.00 116.86 ? 277 LYS   A N   1 
ATOM   2063 C CA  . LYS   B 1 62  ? -43.701 12.786  7.885  1.00 108.35 ? 277 LYS   A CA  1 
ATOM   2064 C C   . LYS   B 1 62  ? -43.555 11.866  9.090  1.00 105.67 ? 277 LYS   A C   1 
ATOM   2065 O O   . LYS   B 1 62  ? -42.603 12.026  9.861  1.00 100.87 ? 277 LYS   A O   1 
ATOM   2066 C CB  . LYS   B 1 62  ? -43.334 14.219  8.283  1.00 99.02  ? 277 LYS   A CB  1 
ATOM   2067 C CG  . LYS   B 1 62  ? -43.752 15.284  7.275  1.00 104.23 ? 277 LYS   A CG  1 
ATOM   2068 C CD  . LYS   B 1 62  ? -43.278 16.681  7.693  1.00 101.22 ? 277 LYS   A CD  1 
ATOM   2069 C CE  . LYS   B 1 62  ? -41.747 16.792  7.743  1.00 95.18  ? 277 LYS   A CE  1 
ATOM   2070 N NZ  . LYS   B 1 62  ? -41.238 18.204  7.638  1.00 83.16  ? 277 LYS   A NZ  1 
ATOM   2071 N N   . PHE   B 1 63  ? -44.470 10.921  9.277  1.00 116.63 ? 278 PHE   A N   1 
ATOM   2072 C CA  . PHE   B 1 63  ? -44.550 10.176  10.526 1.00 123.57 ? 278 PHE   A CA  1 
ATOM   2073 C C   . PHE   B 1 63  ? -45.064 8.781   10.220 1.00 137.75 ? 278 PHE   A C   1 
ATOM   2074 O O   . PHE   B 1 63  ? -45.566 8.524   9.116  1.00 133.79 ? 278 PHE   A O   1 
ATOM   2075 C CB  . PHE   B 1 63  ? -45.440 10.913  11.548 1.00 115.36 ? 278 PHE   A CB  1 
ATOM   2076 C CG  . PHE   B 1 63  ? -44.845 12.220  12.006 1.00 97.94  ? 278 PHE   A CG  1 
ATOM   2077 C CD1 . PHE   B 1 63  ? -43.880 12.246  13.003 1.00 85.79  ? 278 PHE   A CD1 1 
ATOM   2078 C CD2 . PHE   B 1 63  ? -45.189 13.407  11.381 1.00 93.61  ? 278 PHE   A CD2 1 
ATOM   2079 C CE1 . PHE   B 1 63  ? -43.295 13.439  13.392 1.00 79.15  ? 278 PHE   A CE1 1 
ATOM   2080 C CE2 . PHE   B 1 63  ? -44.606 14.601  11.756 1.00 89.60  ? 278 PHE   A CE2 1 
ATOM   2081 C CZ  . PHE   B 1 63  ? -43.656 14.619  12.763 1.00 78.75  ? 278 PHE   A CZ  1 
ATOM   2082 N N   . PRO   B 1 64  ? -44.930 7.840   11.163 1.00 175.85 ? 279 PRO   A N   1 
ATOM   2083 C CA  . PRO   B 1 64  ? -45.403 6.478   10.898 1.00 176.41 ? 279 PRO   A CA  1 
ATOM   2084 C C   . PRO   B 1 64  ? -46.910 6.459   10.712 1.00 176.76 ? 279 PRO   A C   1 
ATOM   2085 O O   . PRO   B 1 64  ? -47.619 7.432   10.979 1.00 179.50 ? 279 PRO   A O   1 
ATOM   2086 C CB  . PRO   B 1 64  ? -44.974 5.690   12.143 1.00 171.92 ? 279 PRO   A CB  1 
ATOM   2087 C CG  . PRO   B 1 64  ? -44.886 6.707   13.220 1.00 168.67 ? 279 PRO   A CG  1 
ATOM   2088 C CD  . PRO   B 1 64  ? -44.434 7.976   12.551 1.00 169.33 ? 279 PRO   A CD  1 
ATOM   2089 N N   . GLU   B 1 65  ? -47.400 5.330   10.218 1.00 151.41 ? 280 GLU   A N   1 
ATOM   2090 C CA  . GLU   B 1 65  ? -48.828 5.142   10.029 1.00 149.19 ? 280 GLU   A CA  1 
ATOM   2091 C C   . GLU   B 1 65  ? -49.252 3.877   10.749 1.00 145.80 ? 280 GLU   A C   1 
ATOM   2092 O O   . GLU   B 1 65  ? -48.531 2.875   10.735 1.00 147.64 ? 280 GLU   A O   1 
ATOM   2093 C CB  . GLU   B 1 65  ? -49.200 5.081   8.548  1.00 143.45 ? 280 GLU   A CB  1 
ATOM   2094 C CG  . GLU   B 1 65  ? -48.648 6.243   7.741  1.00 143.89 ? 280 GLU   A CG  1 
ATOM   2095 C CD  . GLU   B 1 65  ? -49.589 7.438   7.698  1.00 146.93 ? 280 GLU   A CD  1 
ATOM   2096 O OE1 . GLU   B 1 65  ? -50.599 7.450   8.441  1.00 144.75 ? 280 GLU   A OE1 1 
ATOM   2097 O OE2 . GLU   B 1 65  ? -49.312 8.376   6.921  1.00 144.57 ? 280 GLU   A OE2 1 
ATOM   2098 N N   . LYS   B 1 66  ? -50.418 3.944   11.397 1.00 140.73 ? 281 LYS   A N   1 
ATOM   2099 C CA  . LYS   B 1 66  ? -50.901 2.904   12.299 1.00 136.83 ? 281 LYS   A CA  1 
ATOM   2100 C C   . LYS   B 1 66  ? -49.918 2.704   13.448 1.00 135.59 ? 281 LYS   A C   1 
ATOM   2101 O O   . LYS   B 1 66  ? -50.290 2.852   14.617 1.00 132.89 ? 281 LYS   A O   1 
ATOM   2102 C CB  . LYS   B 1 66  ? -51.144 1.593   11.544 1.00 139.91 ? 281 LYS   A CB  1 
ATOM   2103 N N   . LYS   B 1 67  ? -48.660 2.388   13.120 1.00 135.93 ? 282 LYS   A N   1 
ATOM   2104 C CA  . LYS   B 1 67  ? -47.563 2.184   14.066 1.00 134.01 ? 282 LYS   A CA  1 
ATOM   2105 C C   . LYS   B 1 67  ? -47.462 3.353   15.042 1.00 130.62 ? 282 LYS   A C   1 
ATOM   2106 O O   . LYS   B 1 67  ? -46.429 4.027   15.104 1.00 127.69 ? 282 LYS   A O   1 
ATOM   2107 C CB  . LYS   B 1 67  ? -46.251 1.989   13.278 1.00 131.70 ? 282 LYS   A CB  1 
ATOM   2108 C CG  . LYS   B 1 67  ? -44.986 1.568   14.054 1.00 120.59 ? 282 LYS   A CG  1 
ATOM   2109 C CD  . LYS   B 1 67  ? -44.019 0.731   13.181 1.00 108.25 ? 282 LYS   A CD  1 
ATOM   2110 C CE  . LYS   B 1 67  ? -43.187 -0.201  14.040 1.00 108.08 ? 282 LYS   A CE  1 
ATOM   2111 N NZ  . LYS   B 1 67  ? -43.911 -0.494  15.313 1.00 105.54 ? 282 LYS   A NZ  1 
ATOM   2112 N N   . GLY   B 1 68  ? -48.528 3.590   15.805 1.00 127.93 ? 283 GLY   A N   1 
ATOM   2113 C CA  . GLY   B 1 68  ? -48.624 4.760   16.665 1.00 118.94 ? 283 GLY   A CA  1 
ATOM   2114 C C   . GLY   B 1 68  ? -48.416 6.057   15.917 1.00 119.25 ? 283 GLY   A C   1 
ATOM   2115 O O   . GLY   B 1 68  ? -47.798 6.985   16.449 1.00 112.95 ? 283 GLY   A O   1 
ATOM   2116 N N   . GLY   B 1 69  ? -48.901 6.136   14.681 1.00 124.10 ? 284 GLY   A N   1 
ATOM   2117 C CA  . GLY   B 1 69  ? -48.644 7.290   13.847 1.00 124.84 ? 284 GLY   A CA  1 
ATOM   2118 C C   . GLY   B 1 69  ? -49.314 8.552   14.351 1.00 108.37 ? 284 GLY   A C   1 
ATOM   2119 O O   . GLY   B 1 69  ? -50.060 8.554   15.329 1.00 101.99 ? 284 GLY   A O   1 
ATOM   2120 N N   . LEU   B 1 70  ? -49.023 9.653   13.650 1.00 105.87 ? 285 LEU   A N   1 
ATOM   2121 C CA  . LEU   B 1 70  ? -49.614 10.936  14.006 1.00 98.16  ? 285 LEU   A CA  1 
ATOM   2122 C C   . LEU   B 1 70  ? -51.113 10.961  13.740 1.00 104.93 ? 285 LEU   A C   1 
ATOM   2123 O O   . LEU   B 1 70  ? -51.887 11.467  14.563 1.00 101.65 ? 285 LEU   A O   1 
ATOM   2124 C CB  . LEU   B 1 70  ? -48.931 12.063  13.243 1.00 95.56  ? 285 LEU   A CB  1 
ATOM   2125 C CG  . LEU   B 1 70  ? -49.019 13.376  14.010 1.00 86.21  ? 285 LEU   A CG  1 
ATOM   2126 C CD1 . LEU   B 1 70  ? -48.876 13.090  15.486 1.00 75.20  ? 285 LEU   A CD1 1 
ATOM   2127 C CD2 . LEU   B 1 70  ? -47.979 14.377  13.540 1.00 85.05  ? 285 LEU   A CD2 1 
ATOM   2128 N N   . ARG   B 1 71  ? -51.543 10.445  12.588 1.00 102.29 ? 286 ARG   A N   1 
ATOM   2129 C CA  . ARG   B 1 71  ? -52.973 10.368  12.327 1.00 107.38 ? 286 ARG   A CA  1 
ATOM   2130 C C   . ARG   B 1 71  ? -53.646 9.430   13.323 1.00 109.78 ? 286 ARG   A C   1 
ATOM   2131 O O   . ARG   B 1 71  ? -54.748 9.714   13.806 1.00 109.55 ? 286 ARG   A O   1 
ATOM   2132 C CB  . ARG   B 1 71  ? -53.218 9.930   10.878 1.00 109.40 ? 286 ARG   A CB  1 
ATOM   2133 C CG  . ARG   B 1 71  ? -54.597 10.278  10.290 1.00 110.72 ? 286 ARG   A CG  1 
ATOM   2134 C CD  . ARG   B 1 71  ? -55.696 9.378   10.852 1.00 115.67 ? 286 ARG   A CD  1 
ATOM   2135 N NE  . ARG   B 1 71  ? -56.979 9.491   10.165 1.00 118.74 ? 286 ARG   A NE  1 
ATOM   2136 C CZ  . ARG   B 1 71  ? -57.289 8.879   9.027  1.00 118.48 ? 286 ARG   A CZ  1 
ATOM   2137 N NH1 . ARG   B 1 71  ? -56.404 8.142   8.369  1.00 112.75 ? 286 ARG   A NH1 1 
ATOM   2138 N NH2 . ARG   B 1 71  ? -58.524 8.995   8.542  1.00 115.95 ? 286 ARG   A NH2 1 
ATOM   2139 N N   . GLU   B 1 72  ? -52.978 8.330   13.679 1.00 116.10 ? 287 GLU   A N   1 
ATOM   2140 C CA  . GLU   B 1 72  ? -53.562 7.381   14.623 1.00 116.19 ? 287 GLU   A CA  1 
ATOM   2141 C C   . GLU   B 1 72  ? -53.689 7.984   16.021 1.00 112.27 ? 287 GLU   A C   1 
ATOM   2142 O O   . GLU   B 1 72  ? -54.751 7.900   16.649 1.00 111.50 ? 287 GLU   A O   1 
ATOM   2143 C CB  . GLU   B 1 72  ? -52.728 6.098   14.661 1.00 119.44 ? 287 GLU   A CB  1 
ATOM   2144 C CG  . GLU   B 1 72  ? -53.543 4.833   14.460 1.00 124.81 ? 287 GLU   A CG  1 
ATOM   2145 C CD  . GLU   B 1 72  ? -54.253 4.828   13.120 1.00 127.95 ? 287 GLU   A CD  1 
ATOM   2146 O OE1 . GLU   B 1 72  ? -55.428 4.406   13.055 1.00 126.43 ? 287 GLU   A OE1 1 
ATOM   2147 O OE2 . GLU   B 1 72  ? -53.633 5.274   12.132 1.00 130.52 ? 287 GLU   A OE2 1 
ATOM   2148 N N   . LEU   B 1 73  ? -52.614 8.588   16.533 1.00 108.63 ? 288 LEU   A N   1 
ATOM   2149 C CA  . LEU   B 1 73  ? -52.650 9.127   17.889 1.00 100.46 ? 288 LEU   A CA  1 
ATOM   2150 C C   . LEU   B 1 73  ? -53.665 10.254  18.010 1.00 97.86  ? 288 LEU   A C   1 
ATOM   2151 O O   . LEU   B 1 73  ? -54.437 10.296  18.973 1.00 97.21  ? 288 LEU   A O   1 
ATOM   2152 C CB  . LEU   B 1 73  ? -51.260 9.613   18.291 1.00 94.12  ? 288 LEU   A CB  1 
ATOM   2153 C CG  . LEU   B 1 73  ? -50.317 8.499   18.727 1.00 94.50  ? 288 LEU   A CG  1 
ATOM   2154 C CD1 . LEU   B 1 73  ? -48.895 8.997   18.733 1.00 88.33  ? 288 LEU   A CD1 1 
ATOM   2155 C CD2 . LEU   B 1 73  ? -50.724 7.990   20.095 1.00 89.35  ? 288 LEU   A CD2 1 
ATOM   2156 N N   . TYR   B 1 74  ? -53.685 11.169  17.034 1.00 96.89  ? 289 TYR   A N   1 
ATOM   2157 C CA  . TYR   B 1 74  ? -54.521 12.363  17.130 1.00 95.07  ? 289 TYR   A CA  1 
ATOM   2158 C C   . TYR   B 1 74  ? -56.003 12.015  17.235 1.00 102.99 ? 289 TYR   A C   1 
ATOM   2159 O O   . TYR   B 1 74  ? -56.779 12.777  17.828 1.00 101.44 ? 289 TYR   A O   1 
ATOM   2160 C CB  . TYR   B 1 74  ? -54.270 13.282  15.929 1.00 93.15  ? 289 TYR   A CB  1 
ATOM   2161 C CG  . TYR   B 1 74  ? -54.727 14.710  16.153 1.00 89.17  ? 289 TYR   A CG  1 
ATOM   2162 C CD1 . TYR   B 1 74  ? -56.050 15.077  15.942 1.00 95.27  ? 289 TYR   A CD1 1 
ATOM   2163 C CD2 . TYR   B 1 74  ? -53.840 15.692  16.571 1.00 84.10  ? 289 TYR   A CD2 1 
ATOM   2164 C CE1 . TYR   B 1 74  ? -56.484 16.376  16.153 1.00 90.59  ? 289 TYR   A CE1 1 
ATOM   2165 C CE2 . TYR   B 1 74  ? -54.268 17.003  16.781 1.00 82.06  ? 289 TYR   A CE2 1 
ATOM   2166 C CZ  . TYR   B 1 74  ? -55.593 17.331  16.569 1.00 83.17  ? 289 TYR   A CZ  1 
ATOM   2167 O OH  . TYR   B 1 74  ? -56.040 18.610  16.779 1.00 80.20  ? 289 TYR   A OH  1 
ATOM   2168 N N   . ASP   B 1 75  ? -56.415 10.873  16.680 1.00 114.86 ? 290 ASP   A N   1 
ATOM   2169 C CA  . ASP   B 1 75  ? -57.813 10.461  16.790 1.00 114.12 ? 290 ASP   A CA  1 
ATOM   2170 C C   . ASP   B 1 75  ? -58.135 9.951   18.191 1.00 112.74 ? 290 ASP   A C   1 
ATOM   2171 O O   . ASP   B 1 75  ? -59.190 10.279  18.748 1.00 109.00 ? 290 ASP   A O   1 
ATOM   2172 C CB  . ASP   B 1 75  ? -58.130 9.387   15.749 1.00 117.81 ? 290 ASP   A CB  1 
ATOM   2173 C CG  . ASP   B 1 75  ? -58.067 9.912   14.332 1.00 118.56 ? 290 ASP   A CG  1 
ATOM   2174 O OD1 . ASP   B 1 75  ? -58.113 11.149  14.161 1.00 117.70 ? 290 ASP   A OD1 1 
ATOM   2175 O OD2 . ASP   B 1 75  ? -57.972 9.088   13.395 1.00 121.97 ? 290 ASP   A OD2 1 
ATOM   2176 N N   . ARG   B 1 76  ? -57.244 9.144   18.776 1.00 103.96 ? 291 ARG   A N   1 
ATOM   2177 C CA  . ARG   B 1 76  ? -57.411 8.725   20.163 1.00 98.02  ? 291 ARG   A CA  1 
ATOM   2178 C C   . ARG   B 1 76  ? -57.436 9.901   21.118 1.00 95.31  ? 291 ARG   A C   1 
ATOM   2179 O O   . ARG   B 1 76  ? -57.735 9.709   22.300 1.00 95.85  ? 291 ARG   A O   1 
ATOM   2180 C CB  . ARG   B 1 76  ? -56.290 7.776   20.586 1.00 98.86  ? 291 ARG   A CB  1 
ATOM   2181 C CG  . ARG   B 1 76  ? -56.260 6.451   19.845 1.00 99.95  ? 291 ARG   A CG  1 
ATOM   2182 C CD  . ARG   B 1 76  ? -55.887 5.322   20.780 1.00 97.07  ? 291 ARG   A CD  1 
ATOM   2183 N NE  . ARG   B 1 76  ? -54.451 5.067   20.777 1.00 99.61  ? 291 ARG   A NE  1 
ATOM   2184 C CZ  . ARG   B 1 76  ? -53.782 4.521   19.771 1.00 104.12 ? 291 ARG   A CZ  1 
ATOM   2185 N NH1 . ARG   B 1 76  ? -54.392 4.141   18.657 1.00 107.93 ? 291 ARG   A NH1 1 
ATOM   2186 N NH2 . ARG   B 1 76  ? -52.466 4.347   19.886 1.00 101.91 ? 291 ARG   A NH2 1 
ATOM   2187 N N   . GLY   B 1 77  ? -57.115 11.099  20.640 1.00 93.06  ? 292 GLY   A N   1 
ATOM   2188 C CA  . GLY   B 1 77  ? -57.162 12.291  21.445 1.00 88.50  ? 292 GLY   A CA  1 
ATOM   2189 C C   . GLY   B 1 77  ? -56.156 12.254  22.571 1.00 85.70  ? 292 GLY   A C   1 
ATOM   2190 O O   . GLY   B 1 77  ? -55.314 11.358  22.667 1.00 87.70  ? 292 GLY   A O   1 
ATOM   2191 N N   . PRO   B 1 78  ? -56.217 13.244  23.439 1.00 78.12  ? 293 PRO   A N   1 
ATOM   2192 C CA  . PRO   B 1 78  ? -57.086 14.413  23.357 1.00 77.67  ? 293 PRO   A CA  1 
ATOM   2193 C C   . PRO   B 1 78  ? -56.424 15.479  22.499 1.00 72.79  ? 293 PRO   A C   1 
ATOM   2194 O O   . PRO   B 1 78  ? -55.243 15.762  22.676 1.00 74.87  ? 293 PRO   A O   1 
ATOM   2195 C CB  . PRO   B 1 78  ? -57.239 14.819  24.822 1.00 82.03  ? 293 PRO   A CB  1 
ATOM   2196 C CG  . PRO   B 1 78  ? -55.947 14.372  25.483 1.00 76.82  ? 293 PRO   A CG  1 
ATOM   2197 C CD  . PRO   B 1 78  ? -55.451 13.188  24.698 1.00 76.05  ? 293 PRO   A CD  1 
ATOM   2198 N N   . PRO   B 1 79  ? -57.176 16.088  21.581 1.00 70.71  ? 294 PRO   A N   1 
ATOM   2199 C CA  . PRO   B 1 79  ? -56.559 16.963  20.558 1.00 71.19  ? 294 PRO   A CA  1 
ATOM   2200 C C   . PRO   B 1 79  ? -55.671 18.069  21.102 1.00 68.70  ? 294 PRO   A C   1 
ATOM   2201 O O   . PRO   B 1 79  ? -54.749 18.497  20.401 1.00 73.60  ? 294 PRO   A O   1 
ATOM   2202 C CB  . PRO   B 1 79  ? -57.769 17.561  19.827 1.00 72.26  ? 294 PRO   A CB  1 
ATOM   2203 C CG  . PRO   B 1 79  ? -58.917 16.669  20.150 1.00 75.54  ? 294 PRO   A CG  1 
ATOM   2204 C CD  . PRO   B 1 79  ? -58.640 16.008  21.465 1.00 73.21  ? 294 PRO   A CD  1 
ATOM   2205 N N   . HIS   B 1 80  ? -55.934 18.557  22.317 1.00 70.49  ? 295 HIS   A N   1 
ATOM   2206 C CA  . HIS   B 1 80  ? -55.226 19.663  22.962 1.00 70.14  ? 295 HIS   A CA  1 
ATOM   2207 C C   . HIS   B 1 80  ? -53.872 19.259  23.519 1.00 67.15  ? 295 HIS   A C   1 
ATOM   2208 O O   . HIS   B 1 80  ? -53.154 20.123  24.037 1.00 63.45  ? 295 HIS   A O   1 
ATOM   2209 C CB  . HIS   B 1 80  ? -56.063 20.232  24.115 1.00 74.16  ? 295 HIS   A CB  1 
ATOM   2210 C CG  . HIS   B 1 80  ? -56.291 19.245  25.229 1.00 73.97  ? 295 HIS   A CG  1 
ATOM   2211 N ND1 . HIS   B 1 80  ? -55.361 19.007  26.220 1.00 70.00  ? 295 HIS   A ND1 1 
ATOM   2212 C CD2 . HIS   B 1 80  ? -57.329 18.416  25.485 1.00 72.96  ? 295 HIS   A CD2 1 
ATOM   2213 C CE1 . HIS   B 1 80  ? -55.815 18.083  27.041 1.00 71.77  ? 295 HIS   A CE1 1 
ATOM   2214 N NE2 . HIS   B 1 80  ? -57.010 17.712  26.620 1.00 80.88  ? 295 HIS   A NE2 1 
ATOM   2215 N N   . ALA   B 1 81  ? -53.528 17.977  23.450 1.00 65.38  ? 296 ALA   A N   1 
ATOM   2216 C CA  . ALA   B 1 81  ? -52.270 17.476  23.974 1.00 68.13  ? 296 ALA   A CA  1 
ATOM   2217 C C   . ALA   B 1 81  ? -51.160 17.427  22.931 1.00 68.46  ? 296 ALA   A C   1 
ATOM   2218 O O   . ALA   B 1 81  ? -50.043 17.012  23.272 1.00 67.35  ? 296 ALA   A O   1 
ATOM   2219 C CB  . ALA   B 1 81  ? -52.472 16.080  24.571 1.00 63.92  ? 296 ALA   A CB  1 
ATOM   2220 N N   . PHE   B 1 82  ? -51.426 17.872  21.696 1.00 66.89  ? 297 PHE   A N   1 
ATOM   2221 C CA  . PHE   B 1 82  ? -50.544 17.667  20.545 1.00 68.01  ? 297 PHE   A CA  1 
ATOM   2222 C C   . PHE   B 1 82  ? -49.883 18.969  20.114 1.00 69.87  ? 297 PHE   A C   1 
ATOM   2223 O O   . PHE   B 1 82  ? -50.566 19.901  19.667 1.00 71.39  ? 297 PHE   A O   1 
ATOM   2224 C CB  . PHE   B 1 82  ? -51.324 17.092  19.371 1.00 67.71  ? 297 PHE   A CB  1 
ATOM   2225 C CG  . PHE   B 1 82  ? -51.737 15.679  19.563 1.00 70.40  ? 297 PHE   A CG  1 
ATOM   2226 C CD1 . PHE   B 1 82  ? -52.854 15.368  20.313 1.00 70.63  ? 297 PHE   A CD1 1 
ATOM   2227 C CD2 . PHE   B 1 82  ? -51.011 14.655  18.993 1.00 69.30  ? 297 PHE   A CD2 1 
ATOM   2228 C CE1 . PHE   B 1 82  ? -53.236 14.063  20.478 1.00 75.39  ? 297 PHE   A CE1 1 
ATOM   2229 C CE2 . PHE   B 1 82  ? -51.396 13.353  19.145 1.00 75.15  ? 297 PHE   A CE2 1 
ATOM   2230 C CZ  . PHE   B 1 82  ? -52.506 13.055  19.897 1.00 79.98  ? 297 PHE   A CZ  1 
ATOM   2231 N N   . PHE   B 1 83  ? -48.553 18.996  20.158 1.00 65.38  ? 298 PHE   A N   1 
ATOM   2232 C CA  . PHE   B 1 83  ? -47.770 20.174  19.818 1.00 64.85  ? 298 PHE   A CA  1 
ATOM   2233 C C   . PHE   B 1 83  ? -46.764 19.853  18.730 1.00 63.48  ? 298 PHE   A C   1 
ATOM   2234 O O   . PHE   B 1 83  ? -46.254 18.729  18.654 1.00 58.02  ? 298 PHE   A O   1 
ATOM   2235 C CB  . PHE   B 1 83  ? -47.072 20.704  21.034 1.00 64.18  ? 298 PHE   A CB  1 
ATOM   2236 C CG  . PHE   B 1 83  ? -48.009 20.987  22.136 1.00 67.64  ? 298 PHE   A CG  1 
ATOM   2237 C CD1 . PHE   B 1 83  ? -48.393 19.978  22.996 1.00 72.73  ? 298 PHE   A CD1 1 
ATOM   2238 C CD2 . PHE   B 1 83  ? -48.556 22.245  22.287 1.00 69.38  ? 298 PHE   A CD2 1 
ATOM   2239 C CE1 . PHE   B 1 83  ? -49.293 20.227  24.011 1.00 72.36  ? 298 PHE   A CE1 1 
ATOM   2240 C CE2 . PHE   B 1 83  ? -49.453 22.503  23.289 1.00 73.72  ? 298 PHE   A CE2 1 
ATOM   2241 C CZ  . PHE   B 1 83  ? -49.827 21.493  24.157 1.00 72.49  ? 298 PHE   A CZ  1 
ATOM   2242 N N   . LEU   B 1 84  ? -46.559 20.828  17.842 1.00 70.00  ? 299 LEU   A N   1 
ATOM   2243 C CA  . LEU   B 1 84  ? -45.522 20.788  16.816 1.00 63.44  ? 299 LEU   A CA  1 
ATOM   2244 C C   . LEU   B 1 84  ? -44.393 21.727  17.215 1.00 60.56  ? 299 LEU   A C   1 
ATOM   2245 O O   . LEU   B 1 84  ? -44.631 22.904  17.503 1.00 64.33  ? 299 LEU   A O   1 
ATOM   2246 C CB  . LEU   B 1 84  ? -46.071 21.189  15.448 1.00 65.06  ? 299 LEU   A CB  1 
ATOM   2247 C CG  . LEU   B 1 84  ? -45.026 21.468  14.361 1.00 64.69  ? 299 LEU   A CG  1 
ATOM   2248 C CD1 . LEU   B 1 84  ? -44.261 20.216  14.008 1.00 59.56  ? 299 LEU   A CD1 1 
ATOM   2249 C CD2 . LEU   B 1 84  ? -45.676 22.040  13.119 1.00 67.37  ? 299 LEU   A CD2 1 
ATOM   2250 N N   . VAL   B 1 85  ? -43.176 21.206  17.263 1.00 56.07  ? 300 VAL   A N   1 
ATOM   2251 C CA  . VAL   B 1 85  ? -41.993 22.024  17.482 1.00 61.46  ? 300 VAL   A CA  1 
ATOM   2252 C C   . VAL   B 1 85  ? -41.176 21.974  16.203 1.00 65.76  ? 300 VAL   A C   1 
ATOM   2253 O O   . VAL   B 1 85  ? -40.851 20.884  15.714 1.00 64.46  ? 300 VAL   A O   1 
ATOM   2254 C CB  . VAL   B 1 85  ? -41.165 21.540  18.680 1.00 59.90  ? 300 VAL   A CB  1 
ATOM   2255 C CG1 . VAL   B 1 85  ? -39.866 22.320  18.778 1.00 62.01  ? 300 VAL   A CG1 1 
ATOM   2256 C CG2 . VAL   B 1 85  ? -41.955 21.681  19.959 1.00 62.47  ? 300 VAL   A CG2 1 
ATOM   2257 N N   . LYS   B 1 86  ? -40.871 23.142  15.643 1.00 63.31  ? 301 LYS   A N   1 
ATOM   2258 C CA  . LYS   B 1 86  ? -39.897 23.250  14.571 1.00 64.95  ? 301 LYS   A CA  1 
ATOM   2259 C C   . LYS   B 1 86  ? -38.573 23.663  15.200 1.00 67.21  ? 301 LYS   A C   1 
ATOM   2260 O O   . LYS   B 1 86  ? -38.507 24.696  15.875 1.00 67.04  ? 301 LYS   A O   1 
ATOM   2261 C CB  . LYS   B 1 86  ? -40.339 24.270  13.522 1.00 71.86  ? 301 LYS   A CB  1 
ATOM   2262 C CG  . LYS   B 1 86  ? -39.674 24.111  12.139 1.00 70.09  ? 301 LYS   A CG  1 
ATOM   2263 C CD  . LYS   B 1 86  ? -40.514 24.802  11.043 1.00 84.23  ? 301 LYS   A CD  1 
ATOM   2264 C CE  . LYS   B 1 86  ? -42.023 24.973  11.429 1.00 87.04  ? 301 LYS   A CE  1 
ATOM   2265 N NZ  . LYS   B 1 86  ? -43.005 25.398  10.354 1.00 83.16  ? 301 LYS   A NZ  1 
ATOM   2266 N N   . PHE   B 1 87  ? -37.528 22.867  14.981 1.00 66.31  ? 302 PHE   A N   1 
ATOM   2267 C CA  . PHE   B 1 87  ? -36.203 23.158  15.516 1.00 66.68  ? 302 PHE   A CA  1 
ATOM   2268 C C   . PHE   B 1 87  ? -35.273 23.773  14.469 1.00 68.71  ? 302 PHE   A C   1 
ATOM   2269 O O   . PHE   B 1 87  ? -35.386 23.517  13.262 1.00 65.43  ? 302 PHE   A O   1 
ATOM   2270 C CB  . PHE   B 1 87  ? -35.553 21.894  16.069 1.00 63.05  ? 302 PHE   A CB  1 
ATOM   2271 C CG  . PHE   B 1 87  ? -35.852 21.651  17.509 1.00 66.17  ? 302 PHE   A CG  1 
ATOM   2272 C CD1 . PHE   B 1 87  ? -35.819 22.686  18.417 1.00 68.90  ? 302 PHE   A CD1 1 
ATOM   2273 C CD2 . PHE   B 1 87  ? -36.166 20.391  17.963 1.00 65.72  ? 302 PHE   A CD2 1 
ATOM   2274 C CE1 . PHE   B 1 87  ? -36.094 22.467  19.756 1.00 66.16  ? 302 PHE   A CE1 1 
ATOM   2275 C CE2 . PHE   B 1 87  ? -36.442 20.183  19.298 1.00 66.65  ? 302 PHE   A CE2 1 
ATOM   2276 C CZ  . PHE   B 1 87  ? -36.406 21.222  20.186 1.00 63.93  ? 302 PHE   A CZ  1 
ATOM   2277 N N   . TRP   B 1 88  ? -34.325 24.575  14.959 1.00 65.95  ? 303 TRP   A N   1 
ATOM   2278 C CA  . TRP   B 1 88  ? -33.197 25.065  14.168 1.00 65.66  ? 303 TRP   A CA  1 
ATOM   2279 C C   . TRP   B 1 88  ? -31.905 24.711  14.907 1.00 64.71  ? 303 TRP   A C   1 
ATOM   2280 O O   . TRP   B 1 88  ? -31.424 25.488  15.730 1.00 66.16  ? 303 TRP   A O   1 
ATOM   2281 C CB  . TRP   B 1 88  ? -33.332 26.551  13.925 1.00 67.90  ? 303 TRP   A CB  1 
ATOM   2282 C CG  . TRP   B 1 88  ? -34.283 26.838  12.827 1.00 68.03  ? 303 TRP   A CG  1 
ATOM   2283 C CD1 . TRP   B 1 88  ? -34.000 26.872  11.509 1.00 65.31  ? 303 TRP   A CD1 1 
ATOM   2284 C CD2 . TRP   B 1 88  ? -35.689 27.101  12.948 1.00 71.83  ? 303 TRP   A CD2 1 
ATOM   2285 N NE1 . TRP   B 1 88  ? -35.136 27.140  10.788 1.00 66.48  ? 303 TRP   A NE1 1 
ATOM   2286 C CE2 . TRP   B 1 88  ? -36.186 27.297  11.649 1.00 69.23  ? 303 TRP   A CE2 1 
ATOM   2287 C CE3 . TRP   B 1 88  ? -36.571 27.202  14.029 1.00 72.97  ? 303 TRP   A CE3 1 
ATOM   2288 C CZ2 . TRP   B 1 88  ? -37.524 27.587  11.395 1.00 77.76  ? 303 TRP   A CZ2 1 
ATOM   2289 C CZ3 . TRP   B 1 88  ? -37.901 27.496  13.776 1.00 72.98  ? 303 TRP   A CZ3 1 
ATOM   2290 C CH2 . TRP   B 1 88  ? -38.364 27.681  12.469 1.00 79.23  ? 303 TRP   A CH2 1 
ATOM   2291 N N   . ALA   B 1 89  ? -31.328 23.551  14.596 1.00 64.06  ? 304 ALA   A N   1 
ATOM   2292 C CA  . ALA   B 1 89  ? -30.270 22.991  15.424 1.00 65.13  ? 304 ALA   A CA  1 
ATOM   2293 C C   . ALA   B 1 89  ? -28.904 23.579  15.099 1.00 69.43  ? 304 ALA   A C   1 
ATOM   2294 O O   . ALA   B 1 89  ? -28.587 23.884  13.945 1.00 71.48  ? 304 ALA   A O   1 
ATOM   2295 C CB  . ALA   B 1 89  ? -30.211 21.478  15.267 1.00 60.61  ? 304 ALA   A CB  1 
ATOM   2296 N N   . ASP   B 1 90  ? -28.085 23.713  16.139 1.00 66.74  ? 305 ASP   A N   1 
ATOM   2297 C CA  . ASP   B 1 90  ? -26.690 24.124  16.016 1.00 73.57  ? 305 ASP   A CA  1 
ATOM   2298 C C   . ASP   B 1 90  ? -25.821 22.883  15.809 1.00 75.70  ? 305 ASP   A C   1 
ATOM   2299 O O   . ASP   B 1 90  ? -25.738 22.031  16.697 1.00 75.61  ? 305 ASP   A O   1 
ATOM   2300 C CB  . ASP   B 1 90  ? -26.270 24.883  17.277 1.00 74.53  ? 305 ASP   A CB  1 
ATOM   2301 C CG  . ASP   B 1 90  ? -24.933 25.586  17.138 1.00 78.50  ? 305 ASP   A CG  1 
ATOM   2302 O OD1 . ASP   B 1 90  ? -24.198 25.289  16.177 1.00 85.76  ? 305 ASP   A OD1 1 
ATOM   2303 O OD2 . ASP   B 1 90  ? -24.610 26.428  18.003 1.00 76.00  ? 305 ASP   A OD2 1 
ATOM   2304 N N   . LEU   B 1 91  ? -25.183 22.772  14.643 1.00 77.64  ? 306 LEU   A N   1 
ATOM   2305 C CA  . LEU   B 1 91  ? -24.263 21.672  14.364 1.00 79.50  ? 306 LEU   A CA  1 
ATOM   2306 C C   . LEU   B 1 91  ? -22.820 22.145  14.306 1.00 87.92  ? 306 LEU   A C   1 
ATOM   2307 O O   . LEU   B 1 91  ? -21.949 21.419  13.811 1.00 90.38  ? 306 LEU   A O   1 
ATOM   2308 C CB  . LEU   B 1 91  ? -24.619 20.985  13.050 1.00 73.99  ? 306 LEU   A CB  1 
ATOM   2309 C CG  . LEU   B 1 91  ? -26.005 20.379  13.006 1.00 69.55  ? 306 LEU   A CG  1 
ATOM   2310 C CD1 . LEU   B 1 91  ? -26.188 19.748  11.658 1.00 69.22  ? 306 LEU   A CD1 1 
ATOM   2311 C CD2 . LEU   B 1 91  ? -26.142 19.372  14.103 1.00 66.46  ? 306 LEU   A CD2 1 
ATOM   2312 N N   . ASN   B 1 92  ? -22.557 23.352  14.781 1.00 96.30  ? 307 ASN   A N   1 
ATOM   2313 C CA  . ASN   B 1 92  ? -21.238 23.964  14.753 1.00 99.37  ? 307 ASN   A CA  1 
ATOM   2314 C C   . ASN   B 1 92  ? -20.631 23.749  16.138 1.00 101.97 ? 307 ASN   A C   1 
ATOM   2315 O O   . ASN   B 1 92  ? -20.780 24.577  17.044 1.00 102.17 ? 307 ASN   A O   1 
ATOM   2316 C CB  . ASN   B 1 92  ? -21.369 25.436  14.373 1.00 103.03 ? 307 ASN   A CB  1 
ATOM   2317 C CG  . ASN   B 1 92  ? -20.038 26.128  14.222 1.00 109.79 ? 307 ASN   A CG  1 
ATOM   2318 O OD1 . ASN   B 1 92  ? -19.067 25.545  13.742 1.00 110.22 ? 307 ASN   A OD1 1 
ATOM   2319 N ND2 . ASN   B 1 92  ? -19.983 27.388  14.640 1.00 114.25 ? 307 ASN   A ND2 1 
ATOM   2320 N N   . TRP   B 1 93  ? -19.974 22.597  16.312 1.00 91.87  ? 308 TRP   A N   1 
ATOM   2321 C CA  . TRP   B 1 93  ? -19.285 22.272  17.558 1.00 90.89  ? 308 TRP   A CA  1 
ATOM   2322 C C   . TRP   B 1 93  ? -17.937 21.608  17.300 1.00 96.61  ? 308 TRP   A C   1 
ATOM   2323 O O   . TRP   B 1 93  ? -17.798 20.790  16.388 1.00 92.36  ? 308 TRP   A O   1 
ATOM   2324 C CB  . TRP   B 1 93  ? -20.137 21.371  18.467 1.00 84.30  ? 308 TRP   A CB  1 
ATOM   2325 C CG  . TRP   B 1 93  ? -20.148 19.901  18.134 1.00 80.54  ? 308 TRP   A CG  1 
ATOM   2326 C CD1 . TRP   B 1 93  ? -19.352 18.922  18.672 1.00 76.33  ? 308 TRP   A CD1 1 
ATOM   2327 C CD2 . TRP   B 1 93  ? -21.028 19.240  17.210 1.00 81.10  ? 308 TRP   A CD2 1 
ATOM   2328 N NE1 . TRP   B 1 93  ? -19.679 17.698  18.134 1.00 74.73  ? 308 TRP   A NE1 1 
ATOM   2329 C CE2 . TRP   B 1 93  ? -20.702 17.865  17.232 1.00 79.27  ? 308 TRP   A CE2 1 
ATOM   2330 C CE3 . TRP   B 1 93  ? -22.048 19.680  16.354 1.00 79.94  ? 308 TRP   A CE3 1 
ATOM   2331 C CZ2 . TRP   B 1 93  ? -21.365 16.926  16.430 1.00 77.98  ? 308 TRP   A CZ2 1 
ATOM   2332 C CZ3 . TRP   B 1 93  ? -22.704 18.751  15.557 1.00 76.69  ? 308 TRP   A CZ3 1 
ATOM   2333 C CH2 . TRP   B 1 93  ? -22.361 17.389  15.604 1.00 77.85  ? 308 TRP   A CH2 1 
ATOM   2334 N N   . GLY   B 1 94  ? -16.954 21.963  18.130 1.00 106.38 ? 309 GLY   A N   1 
ATOM   2335 C CA  . GLY   B 1 94  ? -15.579 21.528  17.990 1.00 116.56 ? 309 GLY   A CA  1 
ATOM   2336 C C   . GLY   B 1 94  ? -14.646 22.703  18.254 1.00 129.57 ? 309 GLY   A C   1 
ATOM   2337 O O   . GLY   B 1 94  ? -15.102 23.839  18.378 1.00 130.91 ? 309 GLY   A O   1 
ATOM   2338 N N   . PRO   B 1 95  ? -13.355 22.458  18.475 1.00 139.51 ? 310 PRO   A N   1 
ATOM   2339 C CA  . PRO   B 1 95  ? -12.394 23.572  18.412 1.00 142.48 ? 310 PRO   A CA  1 
ATOM   2340 C C   . PRO   B 1 95  ? -12.240 24.154  17.013 1.00 142.35 ? 310 PRO   A C   1 
ATOM   2341 O O   . PRO   B 1 95  ? -12.715 25.266  16.764 1.00 141.39 ? 310 PRO   A O   1 
ATOM   2342 C CB  . PRO   B 1 95  ? -11.091 22.928  18.917 1.00 144.97 ? 310 PRO   A CB  1 
ATOM   2343 C CG  . PRO   B 1 95  ? -11.437 21.432  19.033 1.00 145.84 ? 310 PRO   A CG  1 
ATOM   2344 C CD  . PRO   B 1 95  ? -12.851 21.455  19.422 1.00 144.09 ? 310 PRO   A CD  1 
ATOM   2345 N N   . SER   B 1 96  ? -11.588 23.431  16.100 1.00 143.13 ? 311 SER   A N   1 
ATOM   2346 C CA  . SER   B 1 96  ? -11.457 23.882  14.695 1.00 137.26 ? 311 SER   A CA  1 
ATOM   2347 C C   . SER   B 1 96  ? -10.833 22.798  13.829 1.00 138.86 ? 311 SER   A C   1 
ATOM   2348 O O   . SER   B 1 96  ? -10.327 23.083  12.739 1.00 140.79 ? 311 SER   A O   1 
ATOM   2349 C CB  . SER   B 1 96  ? -10.620 25.161  14.602 1.00 138.39 ? 311 SER   A CB  1 
ATOM   2350 O OG  . SER   B 1 96  ? -10.188 25.379  13.259 1.00 139.68 ? 311 SER   A OG  1 
ATOM   2351 N N   . GLY   B 1 109 ? -15.394 11.655  19.171 1.00 102.82 ? 324 GLY   A N   1 
ATOM   2352 C CA  . GLY   B 1 109 ? -15.643 11.396  20.579 1.00 107.07 ? 324 GLY   A CA  1 
ATOM   2353 C C   . GLY   B 1 109 ? -16.637 12.334  21.249 1.00 108.57 ? 324 GLY   A C   1 
ATOM   2354 O O   . GLY   B 1 109 ? -17.076 13.324  20.652 1.00 105.69 ? 324 GLY   A O   1 
ATOM   2355 N N   . GLY   B 1 110 ? -16.994 12.019  22.489 1.00 108.18 ? 325 GLY   A N   1 
ATOM   2356 C CA  . GLY   B 1 110 ? -17.908 12.825  23.278 1.00 108.68 ? 325 GLY   A CA  1 
ATOM   2357 C C   . GLY   B 1 110 ? -19.028 11.994  23.884 1.00 107.26 ? 325 GLY   A C   1 
ATOM   2358 O O   . GLY   B 1 110 ? -19.246 10.835  23.539 1.00 109.95 ? 325 GLY   A O   1 
ATOM   2359 N N   . PHE   B 1 111 ? -19.736 12.623  24.826 1.00 92.10  ? 326 PHE   A N   1 
ATOM   2360 C CA  . PHE   B 1 111 ? -20.967 12.067  25.383 1.00 84.39  ? 326 PHE   A CA  1 
ATOM   2361 C C   . PHE   B 1 111 ? -22.160 12.816  24.801 1.00 77.77  ? 326 PHE   A C   1 
ATOM   2362 O O   . PHE   B 1 111 ? -22.245 14.041  24.925 1.00 79.73  ? 326 PHE   A O   1 
ATOM   2363 C CB  . PHE   B 1 111 ? -21.008 12.145  26.911 1.00 87.86  ? 326 PHE   A CB  1 
ATOM   2364 C CG  . PHE   B 1 111 ? -22.363 11.792  27.479 1.00 81.97  ? 326 PHE   A CG  1 
ATOM   2365 C CD1 . PHE   B 1 111 ? -22.724 10.469  27.663 1.00 76.60  ? 326 PHE   A CD1 1 
ATOM   2366 C CD2 . PHE   B 1 111 ? -23.296 12.781  27.762 1.00 80.64  ? 326 PHE   A CD2 1 
ATOM   2367 C CE1 . PHE   B 1 111 ? -23.969 10.141  28.150 1.00 76.96  ? 326 PHE   A CE1 1 
ATOM   2368 C CE2 . PHE   B 1 111 ? -24.539 12.456  28.232 1.00 77.16  ? 326 PHE   A CE2 1 
ATOM   2369 C CZ  . PHE   B 1 111 ? -24.875 11.133  28.433 1.00 77.69  ? 326 PHE   A CZ  1 
ATOM   2370 N N   . TYR   B 1 112 ? -23.093 12.075  24.206 1.00 72.93  ? 327 TYR   A N   1 
ATOM   2371 C CA  . TYR   B 1 112 ? -24.219 12.631  23.452 1.00 73.30  ? 327 TYR   A CA  1 
ATOM   2372 C C   . TYR   B 1 112 ? -25.471 12.281  24.240 1.00 74.31  ? 327 TYR   A C   1 
ATOM   2373 O O   . TYR   B 1 112 ? -25.972 11.153  24.158 1.00 71.33  ? 327 TYR   A O   1 
ATOM   2374 C CB  . TYR   B 1 112 ? -24.282 12.068  22.022 1.00 75.54  ? 327 TYR   A CB  1 
ATOM   2375 C CG  . TYR   B 1 112 ? -23.261 12.642  21.053 1.00 76.22  ? 327 TYR   A CG  1 
ATOM   2376 C CD1 . TYR   B 1 112 ? -21.914 12.364  21.196 1.00 74.24  ? 327 TYR   A CD1 1 
ATOM   2377 C CD2 . TYR   B 1 112 ? -23.653 13.445  19.986 1.00 77.47  ? 327 TYR   A CD2 1 
ATOM   2378 C CE1 . TYR   B 1 112 ? -20.991 12.881  20.331 1.00 80.83  ? 327 TYR   A CE1 1 
ATOM   2379 C CE2 . TYR   B 1 112 ? -22.727 13.966  19.103 1.00 69.47  ? 327 TYR   A CE2 1 
ATOM   2380 C CZ  . TYR   B 1 112 ? -21.391 13.679  19.285 1.00 74.28  ? 327 TYR   A CZ  1 
ATOM   2381 O OH  . TYR   B 1 112 ? -20.418 14.180  18.434 1.00 81.37  ? 327 TYR   A OH  1 
ATOM   2382 N N   . GLY   B 1 113 ? -25.967 13.253  25.008 1.00 74.29  ? 328 GLY   A N   1 
ATOM   2383 C CA  . GLY   B 1 113 ? -27.069 13.046  25.917 1.00 70.24  ? 328 GLY   A CA  1 
ATOM   2384 C C   . GLY   B 1 113 ? -28.333 13.764  25.467 1.00 67.89  ? 328 GLY   A C   1 
ATOM   2385 O O   . GLY   B 1 113 ? -28.361 14.510  24.485 1.00 65.85  ? 328 GLY   A O   1 
ATOM   2386 N N   . VAL   B 1 114 ? -29.401 13.489  26.211 1.00 66.57  ? 329 VAL   A N   1 
ATOM   2387 C CA  . VAL   B 1 114 ? -30.700 14.125  26.048 1.00 67.31  ? 329 VAL   A CA  1 
ATOM   2388 C C   . VAL   B 1 114 ? -31.319 14.290  27.434 1.00 69.21  ? 329 VAL   A C   1 
ATOM   2389 O O   . VAL   B 1 114 ? -31.437 13.315  28.184 1.00 70.15  ? 329 VAL   A O   1 
ATOM   2390 C CB  . VAL   B 1 114 ? -31.619 13.300  25.126 1.00 63.70  ? 329 VAL   A CB  1 
ATOM   2391 C CG1 . VAL   B 1 114 ? -33.031 13.794  25.233 1.00 70.03  ? 329 VAL   A CG1 1 
ATOM   2392 C CG2 . VAL   B 1 114 ? -31.183 13.435  23.695 1.00 68.64  ? 329 VAL   A CG2 1 
ATOM   2393 N N   . SER   B 1 115 ? -31.704 15.517  27.785 1.00 69.23  ? 330 SER   A N   1 
ATOM   2394 C CA  . SER   B 1 115 ? -32.274 15.807  29.098 1.00 67.58  ? 330 SER   A CA  1 
ATOM   2395 C C   . SER   B 1 115 ? -33.676 16.373  28.919 1.00 70.34  ? 330 SER   A C   1 
ATOM   2396 O O   . SER   B 1 115 ? -33.843 17.427  28.298 1.00 71.95  ? 330 SER   A O   1 
ATOM   2397 C CB  . SER   B 1 115 ? -31.390 16.783  29.884 1.00 66.66  ? 330 SER   A CB  1 
ATOM   2398 O OG  . SER   B 1 115 ? -30.482 16.109  30.754 1.00 64.27  ? 330 SER   A OG  1 
ATOM   2399 N N   . SER   B 1 116 ? -34.679 15.669  29.451 1.00 68.80  ? 331 SER   A N   1 
ATOM   2400 C CA  . SER   B 1 116 ? -36.044 16.168  29.534 1.00 69.06  ? 331 SER   A CA  1 
ATOM   2401 C C   . SER   B 1 116 ? -36.476 16.378  30.977 1.00 76.11  ? 331 SER   A C   1 
ATOM   2402 O O   . SER   B 1 116 ? -36.095 15.623  31.879 1.00 77.70  ? 331 SER   A O   1 
ATOM   2403 C CB  . SER   B 1 116 ? -37.027 15.227  28.893 1.00 64.96  ? 331 SER   A CB  1 
ATOM   2404 O OG  . SER   B 1 116 ? -37.086 15.469  27.525 1.00 65.20  ? 331 SER   A OG  1 
ATOM   2405 N N   . GLN   B 1 117 ? -37.305 17.395  31.184 1.00 80.40  ? 332 GLN   A N   1 
ATOM   2406 C CA  . GLN   B 1 117 ? -37.875 17.633  32.497 1.00 82.47  ? 332 GLN   A CA  1 
ATOM   2407 C C   . GLN   B 1 117 ? -39.337 18.010  32.340 1.00 79.82  ? 332 GLN   A C   1 
ATOM   2408 O O   . GLN   B 1 117 ? -39.693 18.770  31.435 1.00 79.71  ? 332 GLN   A O   1 
ATOM   2409 C CB  . GLN   B 1 117 ? -37.118 18.720  33.243 1.00 84.25  ? 332 GLN   A CB  1 
ATOM   2410 C CG  . GLN   B 1 117 ? -37.271 18.596  34.735 1.00 86.82  ? 332 GLN   A CG  1 
ATOM   2411 C CD  . GLN   B 1 117 ? -36.373 19.557  35.487 1.00 95.87  ? 332 GLN   A CD  1 
ATOM   2412 O OE1 . GLN   B 1 117 ? -35.236 19.815  35.067 1.00 101.62 ? 332 GLN   A OE1 1 
ATOM   2413 N NE2 . GLN   B 1 117 ? -36.862 20.072  36.620 1.00 89.82  ? 332 GLN   A NE2 1 
ATOM   2414 N N   . TYR   B 1 118 ? -40.180 17.463  33.211 1.00 71.08  ? 333 TYR   A N   1 
ATOM   2415 C CA  . TYR   B 1 118 ? -41.613 17.696  33.152 1.00 69.49  ? 333 TYR   A CA  1 
ATOM   2416 C C   . TYR   B 1 118 ? -42.117 18.091  34.531 1.00 71.52  ? 333 TYR   A C   1 
ATOM   2417 O O   . TYR   B 1 118 ? -41.393 18.019  35.528 1.00 72.89  ? 333 TYR   A O   1 
ATOM   2418 C CB  . TYR   B 1 118 ? -42.365 16.457  32.663 1.00 70.41  ? 333 TYR   A CB  1 
ATOM   2419 C CG  . TYR   B 1 118 ? -42.028 16.028  31.263 1.00 72.31  ? 333 TYR   A CG  1 
ATOM   2420 C CD1 . TYR   B 1 118 ? -42.550 16.696  30.169 1.00 71.66  ? 333 TYR   A CD1 1 
ATOM   2421 C CD2 . TYR   B 1 118 ? -41.203 14.939  31.034 1.00 72.64  ? 333 TYR   A CD2 1 
ATOM   2422 C CE1 . TYR   B 1 118 ? -42.251 16.302  28.884 1.00 71.22  ? 333 TYR   A CE1 1 
ATOM   2423 C CE2 . TYR   B 1 118 ? -40.899 14.537  29.755 1.00 73.67  ? 333 TYR   A CE2 1 
ATOM   2424 C CZ  . TYR   B 1 118 ? -41.425 15.221  28.681 1.00 72.79  ? 333 TYR   A CZ  1 
ATOM   2425 O OH  . TYR   B 1 118 ? -41.124 14.814  27.401 1.00 75.43  ? 333 TYR   A OH  1 
ATOM   2426 N N   . GLU   B 1 119 ? -43.388 18.482  34.585 1.00 70.53  ? 334 GLU   A N   1 
ATOM   2427 C CA  . GLU   B 1 119 ? -43.997 18.948  35.820 1.00 67.82  ? 334 GLU   A CA  1 
ATOM   2428 C C   . GLU   B 1 119 ? -45.466 18.578  35.864 1.00 68.76  ? 334 GLU   A C   1 
ATOM   2429 O O   . GLU   B 1 119 ? -46.145 18.505  34.836 1.00 66.26  ? 334 GLU   A O   1 
ATOM   2430 C CB  . GLU   B 1 119 ? -43.896 20.457  35.980 1.00 69.56  ? 334 GLU   A CB  1 
ATOM   2431 C CG  . GLU   B 1 119 ? -42.738 20.921  36.790 1.00 75.17  ? 334 GLU   A CG  1 
ATOM   2432 C CD  . GLU   B 1 119 ? -42.737 22.412  36.911 1.00 79.77  ? 334 GLU   A CD  1 
ATOM   2433 O OE1 . GLU   B 1 119 ? -43.745 23.015  36.493 1.00 77.35  ? 334 GLU   A OE1 1 
ATOM   2434 O OE2 . GLU   B 1 119 ? -41.737 22.979  37.406 1.00 84.99  ? 334 GLU   A OE2 1 
ATOM   2435 N N   . SER   B 1 120 ? -45.965 18.394  37.080 1.00 69.63  ? 335 SER   A N   1 
ATOM   2436 C CA  . SER   B 1 120 ? -47.371 18.090  37.248 1.00 68.08  ? 335 SER   A CA  1 
ATOM   2437 C C   . SER   B 1 120 ? -47.856 18.609  38.587 1.00 68.67  ? 335 SER   A C   1 
ATOM   2438 O O   . SER   B 1 120 ? -47.074 18.835  39.516 1.00 67.28  ? 335 SER   A O   1 
ATOM   2439 C CB  . SER   B 1 120 ? -47.637 16.596  37.162 1.00 66.69  ? 335 SER   A CB  1 
ATOM   2440 O OG  . SER   B 1 120 ? -49.019 16.390  36.978 1.00 71.57  ? 335 SER   A OG  1 
ATOM   2441 N N   . LEU   B 1 121 ? -49.173 18.790  38.671 1.00 67.15  ? 336 LEU   A N   1 
ATOM   2442 C CA  . LEU   B 1 121 ? -49.799 18.932  39.975 1.00 70.13  ? 336 LEU   A CA  1 
ATOM   2443 C C   . LEU   B 1 121 ? -50.160 17.573  40.572 1.00 73.14  ? 336 LEU   A C   1 
ATOM   2444 O O   . LEU   B 1 121 ? -49.911 17.343  41.758 1.00 71.38  ? 336 LEU   A O   1 
ATOM   2445 C CB  . LEU   B 1 121 ? -51.045 19.805  39.887 1.00 64.19  ? 336 LEU   A CB  1 
ATOM   2446 C CG  . LEU   B 1 121 ? -50.587 21.232  39.660 1.00 64.73  ? 336 LEU   A CG  1 
ATOM   2447 C CD1 . LEU   B 1 121 ? -51.723 22.071  39.088 1.00 66.22  ? 336 LEU   A CD1 1 
ATOM   2448 C CD2 . LEU   B 1 121 ? -49.945 21.858  40.876 1.00 67.65  ? 336 LEU   A CD2 1 
ATOM   2449 N N   . GLU   B 1 122 ? -50.723 16.659  39.781 1.00 74.41  ? 337 GLU   A N   1 
ATOM   2450 C CA  . GLU   B 1 122 ? -51.015 15.344  40.316 1.00 73.66  ? 337 GLU   A CA  1 
ATOM   2451 C C   . GLU   B 1 122 ? -49.786 14.448  40.235 1.00 73.45  ? 337 GLU   A C   1 
ATOM   2452 O O   . GLU   B 1 122 ? -48.824 14.745  39.524 1.00 73.19  ? 337 GLU   A O   1 
ATOM   2453 C CB  . GLU   B 1 122 ? -52.194 14.712  39.589 1.00 76.60  ? 337 GLU   A CB  1 
ATOM   2454 C CG  . GLU   B 1 122 ? -52.110 14.723  38.091 1.00 80.56  ? 337 GLU   A CG  1 
ATOM   2455 C CD  . GLU   B 1 122 ? -53.495 14.758  37.453 1.00 86.95  ? 337 GLU   A CD  1 
ATOM   2456 O OE1 . GLU   B 1 122 ? -54.128 15.847  37.430 1.00 84.92  ? 337 GLU   A OE1 1 
ATOM   2457 O OE2 . GLU   B 1 122 ? -53.953 13.681  36.999 1.00 89.76  ? 337 GLU   A OE2 1 
ATOM   2458 N N   . HIS   B 1 123 ? -49.825 13.341  40.993 1.00 71.19  ? 338 HIS   A N   1 
ATOM   2459 C CA  . HIS   B 1 123 ? -48.705 12.403  41.119 1.00 71.34  ? 338 HIS   A CA  1 
ATOM   2460 C C   . HIS   B 1 123 ? -48.868 11.230  40.152 1.00 67.20  ? 338 HIS   A C   1 
ATOM   2461 O O   . HIS   B 1 123 ? -49.797 10.426  40.291 1.00 66.06  ? 338 HIS   A O   1 
ATOM   2462 C CB  . HIS   B 1 123 ? -48.580 11.867  42.547 1.00 69.87  ? 338 HIS   A CB  1 
ATOM   2463 C CG  . HIS   B 1 123 ? -47.447 10.897  42.728 1.00 67.50  ? 338 HIS   A CG  1 
ATOM   2464 N ND1 . HIS   B 1 123 ? -47.435 9.643   42.152 1.00 64.13  ? 338 HIS   A ND1 1 
ATOM   2465 C CD2 . HIS   B 1 123 ? -46.290 11.001  43.426 1.00 65.22  ? 338 HIS   A CD2 1 
ATOM   2466 C CE1 . HIS   B 1 123 ? -46.320 9.020   42.487 1.00 67.62  ? 338 HIS   A CE1 1 
ATOM   2467 N NE2 . HIS   B 1 123 ? -45.608 9.820   43.260 1.00 65.64  ? 338 HIS   A NE2 1 
ATOM   2468 N N   . MET   B 1 124 ? -47.931 11.098  39.216 1.00 67.75  ? 339 MET   A N   1 
ATOM   2469 C CA  . MET   B 1 124 ? -48.053 10.127  38.142 1.00 65.09  ? 339 MET   A CA  1 
ATOM   2470 C C   . MET   B 1 124 ? -46.731 9.407   37.952 1.00 64.08  ? 339 MET   A C   1 
ATOM   2471 O O   . MET   B 1 124 ? -45.688 9.817   38.458 1.00 66.33  ? 339 MET   A O   1 
ATOM   2472 C CB  . MET   B 1 124 ? -48.452 10.814  36.845 1.00 66.40  ? 339 MET   A CB  1 
ATOM   2473 C CG  . MET   B 1 124 ? -49.924 10.961  36.669 1.00 67.63  ? 339 MET   A CG  1 
ATOM   2474 S SD  . MET   B 1 124 ? -50.184 12.159  35.371 1.00 62.91  ? 339 MET   A SD  1 
ATOM   2475 C CE  . MET   B 1 124 ? -49.021 13.408  35.866 1.00 69.75  ? 339 MET   A CE  1 
ATOM   2476 N N   . THR   B 1 125 ? -46.776 8.323   37.202 1.00 67.45  ? 340 THR   A N   1 
ATOM   2477 C CA  . THR   B 1 125 ? -45.578 7.785   36.575 1.00 72.01  ? 340 THR   A CA  1 
ATOM   2478 C C   . THR   B 1 125 ? -45.730 7.916   35.057 1.00 66.69  ? 340 THR   A C   1 
ATOM   2479 O O   . THR   B 1 125 ? -46.782 7.581   34.495 1.00 65.00  ? 340 THR   A O   1 
ATOM   2480 C CB  . THR   B 1 125 ? -45.339 6.346   37.042 1.00 73.55  ? 340 THR   A CB  1 
ATOM   2481 O OG1 . THR   B 1 125 ? -46.442 5.526   36.651 1.00 77.43  ? 340 THR   A OG1 1 
ATOM   2482 C CG2 . THR   B 1 125 ? -45.260 6.312   38.561 1.00 76.03  ? 340 THR   A CG2 1 
ATOM   2483 N N   . LEU   B 1 126 ? -44.714 8.472   34.402 1.00 67.84  ? 341 LEU   A N   1 
ATOM   2484 C CA  . LEU   B 1 126 ? -44.741 8.690   32.955 1.00 70.15  ? 341 LEU   A CA  1 
ATOM   2485 C C   . LEU   B 1 126 ? -43.967 7.597   32.212 1.00 66.28  ? 341 LEU   A C   1 
ATOM   2486 O O   . LEU   B 1 126 ? -42.811 7.316   32.554 1.00 63.74  ? 341 LEU   A O   1 
ATOM   2487 C CB  . LEU   B 1 126 ? -44.144 10.058  32.613 1.00 69.95  ? 341 LEU   A CB  1 
ATOM   2488 C CG  . LEU   B 1 126 ? -44.509 11.305  33.422 1.00 65.92  ? 341 LEU   A CG  1 
ATOM   2489 C CD1 . LEU   B 1 126 ? -43.717 12.490  32.927 1.00 65.96  ? 341 LEU   A CD1 1 
ATOM   2490 C CD2 . LEU   B 1 126 ? -45.975 11.595  33.291 1.00 65.03  ? 341 LEU   A CD2 1 
ATOM   2491 N N   . THR   B 1 127 ? -44.590 6.985   31.195 1.00 64.68  ? 342 THR   A N   1 
ATOM   2492 C CA  . THR   B 1 127 ? -43.823 6.343   30.120 1.00 70.91  ? 342 THR   A CA  1 
ATOM   2493 C C   . THR   B 1 127 ? -43.689 7.341   28.965 1.00 67.02  ? 342 THR   A C   1 
ATOM   2494 O O   . THR   B 1 127 ? -44.697 7.782   28.392 1.00 65.06  ? 342 THR   A O   1 
ATOM   2495 C CB  . THR   B 1 127 ? -44.428 5.032   29.593 1.00 68.29  ? 342 THR   A CB  1 
ATOM   2496 O OG1 . THR   B 1 127 ? -45.187 5.293   28.406 1.00 74.22  ? 342 THR   A OG1 1 
ATOM   2497 C CG2 . THR   B 1 127 ? -45.306 4.342   30.596 1.00 59.16  ? 342 THR   A CG2 1 
ATOM   2498 N N   . CYS   B 1 128 ? -42.448 7.709   28.640 1.00 68.12  ? 343 CYS   A N   1 
ATOM   2499 C CA  . CYS   B 1 128 ? -42.133 8.594   27.517 1.00 67.56  ? 343 CYS   A CA  1 
ATOM   2500 C C   . CYS   B 1 128 ? -41.520 7.815   26.354 1.00 64.40  ? 343 CYS   A C   1 
ATOM   2501 O O   . CYS   B 1 128 ? -40.426 7.254   26.475 1.00 63.53  ? 343 CYS   A O   1 
ATOM   2502 C CB  . CYS   B 1 128 ? -41.209 9.728   27.964 1.00 70.89  ? 343 CYS   A CB  1 
ATOM   2503 S SG  . CYS   B 1 128 ? -41.591 10.460  29.625 1.00 73.55  ? 343 CYS   A SG  1 
ATOM   2504 N N   . SER   B 1 129 ? -42.213 7.796   25.224 1.00 66.91  ? 344 SER   A N   1 
ATOM   2505 C CA  . SER   B 1 129 ? -41.718 7.098   24.050 1.00 67.73  ? 344 SER   A CA  1 
ATOM   2506 C C   . SER   B 1 129 ? -41.198 8.102   23.022 1.00 65.99  ? 344 SER   A C   1 
ATOM   2507 O O   . SER   B 1 129 ? -41.883 9.076   22.692 1.00 68.34  ? 344 SER   A O   1 
ATOM   2508 C CB  . SER   B 1 129 ? -42.816 6.225   23.443 1.00 69.97  ? 344 SER   A CB  1 
ATOM   2509 O OG  . SER   B 1 129 ? -42.623 6.049   22.045 1.00 76.15  ? 344 SER   A OG  1 
ATOM   2510 N N   . SER   B 1 130 ? -39.985 7.875   22.532 1.00 62.88  ? 345 SER   A N   1 
ATOM   2511 C CA  . SER   B 1 130 ? -39.444 8.599   21.388 1.00 59.47  ? 345 SER   A CA  1 
ATOM   2512 C C   . SER   B 1 130 ? -39.390 7.694   20.168 1.00 61.58  ? 345 SER   A C   1 
ATOM   2513 O O   . SER   B 1 130 ? -38.931 6.551   20.256 1.00 64.45  ? 345 SER   A O   1 
ATOM   2514 C CB  . SER   B 1 130 ? -38.058 9.142   21.692 1.00 59.24  ? 345 SER   A CB  1 
ATOM   2515 O OG  . SER   B 1 130 ? -38.159 10.230  22.587 1.00 62.92  ? 345 SER   A OG  1 
ATOM   2516 N N   . LYS   B 1 131 ? -39.859 8.207   19.037 1.00 61.22  ? 346 LYS   A N   1 
ATOM   2517 C CA  . LYS   B 1 131 ? -39.882 7.482   17.771 1.00 56.42  ? 346 LYS   A CA  1 
ATOM   2518 C C   . LYS   B 1 131 ? -39.204 8.346   16.720 1.00 58.68  ? 346 LYS   A C   1 
ATOM   2519 O O   . LYS   B 1 131 ? -39.806 9.292   16.200 1.00 58.40  ? 346 LYS   A O   1 
ATOM   2520 C CB  . LYS   B 1 131 ? -41.307 7.154   17.370 1.00 62.69  ? 346 LYS   A CB  1 
ATOM   2521 C CG  . LYS   B 1 131 ? -42.022 6.355   18.415 1.00 73.56  ? 346 LYS   A CG  1 
ATOM   2522 C CD  . LYS   B 1 131 ? -43.250 5.646   17.867 1.00 85.17  ? 346 LYS   A CD  1 
ATOM   2523 C CE  . LYS   B 1 131 ? -44.454 6.574   17.791 1.00 89.06  ? 346 LYS   A CE  1 
ATOM   2524 N NZ  . LYS   B 1 131 ? -45.713 5.778   17.832 1.00 99.80  ? 346 LYS   A NZ  1 
ATOM   2525 N N   . VAL   B 1 132 ? -37.957 8.023   16.404 1.00 61.72  ? 347 VAL   A N   1 
ATOM   2526 C CA  . VAL   B 1 132 ? -37.241 8.686   15.314 1.00 61.89  ? 347 VAL   A CA  1 
ATOM   2527 C C   . VAL   B 1 132 ? -37.668 8.086   13.979 1.00 62.33  ? 347 VAL   A C   1 
ATOM   2528 O O   . VAL   B 1 132 ? -37.499 6.884   13.743 1.00 67.21  ? 347 VAL   A O   1 
ATOM   2529 C CB  . VAL   B 1 132 ? -35.727 8.556   15.494 1.00 60.55  ? 347 VAL   A CB  1 
ATOM   2530 C CG1 . VAL   B 1 132 ? -35.023 9.177   14.303 1.00 64.43  ? 347 VAL   A CG1 1 
ATOM   2531 C CG2 . VAL   B 1 132 ? -35.290 9.161   16.828 1.00 55.20  ? 347 VAL   A CG2 1 
ATOM   2532 N N   . CYS   B 1 133 ? -38.195 8.917   13.093 1.00 61.05  ? 348 CYS   A N   1 
ATOM   2533 C CA  . CYS   B 1 133 ? -38.628 8.457   11.783 1.00 72.34  ? 348 CYS   A CA  1 
ATOM   2534 C C   . CYS   B 1 133 ? -37.687 8.976   10.699 1.00 74.34  ? 348 CYS   A C   1 
ATOM   2535 O O   . CYS   B 1 133 ? -37.214 10.113  10.753 1.00 68.46  ? 348 CYS   A O   1 
ATOM   2536 C CB  . CYS   B 1 133 ? -40.065 8.877   11.502 1.00 78.01  ? 348 CYS   A CB  1 
ATOM   2537 S SG  . CYS   B 1 133 ? -41.129 8.492   12.862 1.00 83.88  ? 348 CYS   A SG  1 
ATOM   2538 N N   . SER   B 1 134 ? -37.383 8.119   9.733  1.00 80.97  ? 349 SER   A N   1 
ATOM   2539 C CA  . SER   B 1 134 ? -36.478 8.464   8.644  1.00 77.93  ? 349 SER   A CA  1 
ATOM   2540 C C   . SER   B 1 134 ? -37.181 8.095   7.352  1.00 79.54  ? 349 SER   A C   1 
ATOM   2541 O O   . SER   B 1 134 ? -37.445 6.916   7.109  1.00 82.91  ? 349 SER   A O   1 
ATOM   2542 C CB  . SER   B 1 134 ? -35.155 7.728   8.780  1.00 74.95  ? 349 SER   A CB  1 
ATOM   2543 O OG  . SER   B 1 134 ? -34.237 8.229   7.856  1.00 73.11  ? 349 SER   A OG  1 
ATOM   2544 N N   . PHE   B 1 135 ? -37.514 9.098   6.550  1.00 81.70  ? 350 PHE   A N   1 
ATOM   2545 C CA  . PHE   B 1 135 ? -38.389 8.934   5.392  1.00 85.86  ? 350 PHE   A CA  1 
ATOM   2546 C C   . PHE   B 1 135 ? -39.690 8.239   5.807  1.00 94.98  ? 350 PHE   A C   1 
ATOM   2547 O O   . PHE   B 1 135 ? -40.074 7.189   5.298  1.00 98.48  ? 350 PHE   A O   1 
ATOM   2548 C CB  . PHE   B 1 135 ? -37.665 8.194   4.259  1.00 76.34  ? 350 PHE   A CB  1 
ATOM   2549 C CG  . PHE   B 1 135 ? -36.423 8.900   3.777  1.00 73.28  ? 350 PHE   A CG  1 
ATOM   2550 C CD1 . PHE   B 1 135 ? -35.207 8.712   4.416  1.00 69.09  ? 350 PHE   A CD1 1 
ATOM   2551 C CD2 . PHE   B 1 135 ? -36.474 9.767   2.679  1.00 74.69  ? 350 PHE   A CD2 1 
ATOM   2552 C CE1 . PHE   B 1 135 ? -34.056 9.373   3.970  1.00 71.25  ? 350 PHE   A CE1 1 
ATOM   2553 C CE2 . PHE   B 1 135 ? -35.325 10.428  2.217  1.00 65.35  ? 350 PHE   A CE2 1 
ATOM   2554 C CZ  . PHE   B 1 135 ? -34.116 10.239  2.864  1.00 65.33  ? 350 PHE   A CZ  1 
ATOM   2555 N N   . GLY   B 1 136 ? -40.365 8.849   6.773  1.00 137.63 ? 351 GLY   A N   1 
ATOM   2556 C CA  . GLY   B 1 136 ? -41.610 8.300   7.270  1.00 142.38 ? 351 GLY   A CA  1 
ATOM   2557 C C   . GLY   B 1 136 ? -41.435 7.050   8.109  1.00 139.70 ? 351 GLY   A C   1 
ATOM   2558 O O   . GLY   B 1 136 ? -42.036 6.929   9.183  1.00 140.53 ? 351 GLY   A O   1 
ATOM   2559 N N   . LYS   B 1 137 ? -40.611 6.118   7.633  1.00 99.09  ? 352 LYS   A N   1 
ATOM   2560 C CA  . LYS   B 1 137 ? -40.435 4.854   8.334  1.00 96.43  ? 352 LYS   A CA  1 
ATOM   2561 C C   . LYS   B 1 137 ? -39.631 5.054   9.610  1.00 87.43  ? 352 LYS   A C   1 
ATOM   2562 O O   . LYS   B 1 137 ? -38.674 5.834   9.651  1.00 82.21  ? 352 LYS   A O   1 
ATOM   2563 C CB  . LYS   B 1 137 ? -39.765 3.824   7.420  1.00 94.64  ? 352 LYS   A CB  1 
ATOM   2564 C CG  . LYS   B 1 137 ? -40.625 3.469   6.211  1.00 93.58  ? 352 LYS   A CG  1 
ATOM   2565 C CD  . LYS   B 1 137 ? -39.859 2.708   5.143  1.00 99.70  ? 352 LYS   A CD  1 
ATOM   2566 C CE  . LYS   B 1 137 ? -40.137 3.291   3.754  1.00 92.56  ? 352 LYS   A CE  1 
ATOM   2567 N NZ  . LYS   B 1 137 ? -39.728 4.741   3.699  1.00 81.51  ? 352 LYS   A NZ  1 
ATOM   2568 N N   . GLN   B 1 138 ? -40.034 4.338   10.656 1.00 82.69  ? 353 GLN   A N   1 
ATOM   2569 C CA  . GLN   B 1 138 ? -39.510 4.541   12.000 1.00 79.05  ? 353 GLN   A CA  1 
ATOM   2570 C C   . GLN   B 1 138 ? -38.256 3.697   12.160 1.00 71.65  ? 353 GLN   A C   1 
ATOM   2571 O O   . GLN   B 1 138 ? -38.312 2.473   12.033 1.00 70.53  ? 353 GLN   A O   1 
ATOM   2572 C CB  . GLN   B 1 138 ? -40.581 4.177   13.034 1.00 82.44  ? 353 GLN   A CB  1 
ATOM   2573 C CG  . GLN   B 1 138 ? -40.123 3.928   14.455 1.00 77.21  ? 353 GLN   A CG  1 
ATOM   2574 C CD  . GLN   B 1 138 ? -41.229 3.293   15.305 1.00 89.09  ? 353 GLN   A CD  1 
ATOM   2575 O OE1 . GLN   B 1 138 ? -42.397 3.253   14.912 1.00 95.07  ? 353 GLN   A OE1 1 
ATOM   2576 N NE2 . GLN   B 1 138 ? -40.853 2.769   16.460 1.00 89.65  ? 353 GLN   A NE2 1 
ATOM   2577 N N   . VAL   B 1 139 ? -37.125 4.350   12.421 1.00 68.91  ? 354 VAL   A N   1 
ATOM   2578 C CA  . VAL   B 1 139 ? -35.853 3.646   12.523 1.00 68.27  ? 354 VAL   A CA  1 
ATOM   2579 C C   . VAL   B 1 139 ? -35.386 3.484   13.958 1.00 68.68  ? 354 VAL   A C   1 
ATOM   2580 O O   . VAL   B 1 139 ? -34.496 2.652   14.211 1.00 67.86  ? 354 VAL   A O   1 
ATOM   2581 C CB  . VAL   B 1 139 ? -34.763 4.351   11.688 1.00 69.75  ? 354 VAL   A CB  1 
ATOM   2582 C CG1 . VAL   B 1 139 ? -35.240 4.506   10.274 1.00 71.39  ? 354 VAL   A CG1 1 
ATOM   2583 C CG2 . VAL   B 1 139 ? -34.454 5.709   12.258 1.00 72.57  ? 354 VAL   A CG2 1 
ATOM   2584 N N   . VAL   B 1 140 ? -35.945 4.249   14.900 1.00 65.36  ? 355 VAL   A N   1 
ATOM   2585 C CA  . VAL   B 1 140 ? -35.629 4.119   16.323 1.00 68.09  ? 355 VAL   A CA  1 
ATOM   2586 C C   . VAL   B 1 140 ? -36.904 4.323   17.142 1.00 66.60  ? 355 VAL   A C   1 
ATOM   2587 O O   . VAL   B 1 140 ? -37.685 5.241   16.878 1.00 65.73  ? 355 VAL   A O   1 
ATOM   2588 C CB  . VAL   B 1 140 ? -34.541 5.121   16.770 1.00 65.98  ? 355 VAL   A CB  1 
ATOM   2589 C CG1 . VAL   B 1 140 ? -34.596 5.333   18.272 1.00 61.77  ? 355 VAL   A CG1 1 
ATOM   2590 C CG2 . VAL   B 1 140 ? -33.170 4.640   16.371 1.00 71.15  ? 355 VAL   A CG2 1 
ATOM   2591 N N   . GLU   B 1 141 ? -37.124 3.452   18.125 1.00 65.02  ? 356 GLU   A N   1 
ATOM   2592 C CA  . GLU   B 1 141 ? -38.090 3.688   19.195 1.00 66.57  ? 356 GLU   A CA  1 
ATOM   2593 C C   . GLU   B 1 141 ? -37.362 3.555   20.523 1.00 63.19  ? 356 GLU   A C   1 
ATOM   2594 O O   . GLU   B 1 141 ? -36.735 2.526   20.787 1.00 66.06  ? 356 GLU   A O   1 
ATOM   2595 C CB  . GLU   B 1 141 ? -39.265 2.709   19.161 1.00 68.42  ? 356 GLU   A CB  1 
ATOM   2596 C CG  . GLU   B 1 141 ? -40.025 2.696   20.485 1.00 74.23  ? 356 GLU   A CG  1 
ATOM   2597 C CD  . GLU   B 1 141 ? -41.542 2.586   20.351 1.00 77.00  ? 356 GLU   A CD  1 
ATOM   2598 O OE1 . GLU   B 1 141 ? -42.028 1.786   19.528 1.00 79.74  ? 356 GLU   A OE1 1 
ATOM   2599 O OE2 . GLU   B 1 141 ? -42.254 3.349   21.043 1.00 77.54  ? 356 GLU   A OE2 1 
ATOM   2600 N N   . LYS   B 1 142 ? -37.445 4.584   21.349 1.00 61.17  ? 357 LYS   A N   1 
ATOM   2601 C CA  . LYS   B 1 142 ? -36.848 4.575   22.673 1.00 62.89  ? 357 LYS   A CA  1 
ATOM   2602 C C   . LYS   B 1 142 ? -37.998 4.700   23.668 1.00 61.80  ? 357 LYS   A C   1 
ATOM   2603 O O   . LYS   B 1 142 ? -38.965 5.410   23.399 1.00 63.55  ? 357 LYS   A O   1 
ATOM   2604 C CB  . LYS   B 1 142 ? -35.834 5.724   22.800 1.00 62.58  ? 357 LYS   A CB  1 
ATOM   2605 C CG  . LYS   B 1 142 ? -34.673 5.522   23.785 1.00 67.39  ? 357 LYS   A CG  1 
ATOM   2606 C CD  . LYS   B 1 142 ? -33.751 6.772   23.816 1.00 74.13  ? 357 LYS   A CD  1 
ATOM   2607 C CE  . LYS   B 1 142 ? -33.365 7.147   25.275 1.00 81.98  ? 357 LYS   A CE  1 
ATOM   2608 N NZ  . LYS   B 1 142 ? -33.238 8.628   25.564 1.00 75.10  ? 357 LYS   A NZ  1 
ATOM   2609 N N   . VAL   B 1 143 ? -37.948 3.970   24.786 1.00 66.17  ? 358 VAL   A N   1 
ATOM   2610 C CA  . VAL   B 1 143 ? -39.054 4.003   25.752 1.00 68.30  ? 358 VAL   A CA  1 
ATOM   2611 C C   . VAL   B 1 143 ? -38.516 4.088   27.172 1.00 64.69  ? 358 VAL   A C   1 
ATOM   2612 O O   . VAL   B 1 143 ? -37.843 3.164   27.636 1.00 68.59  ? 358 VAL   A O   1 
ATOM   2613 C CB  . VAL   B 1 143 ? -39.986 2.791   25.632 1.00 62.83  ? 358 VAL   A CB  1 
ATOM   2614 C CG1 . VAL   B 1 143 ? -41.074 2.886   26.690 1.00 56.80  ? 358 VAL   A CG1 1 
ATOM   2615 C CG2 . VAL   B 1 143 ? -40.575 2.745   24.234 1.00 69.55  ? 358 VAL   A CG2 1 
ATOM   2616 N N   . GLU   B 1 144 ? -38.848 5.172   27.874 1.00 64.52  ? 359 GLU   A N   1 
ATOM   2617 C CA  . GLU   B 1 144 ? -38.405 5.399   29.242 1.00 67.70  ? 359 GLU   A CA  1 
ATOM   2618 C C   . GLU   B 1 144 ? -39.593 5.525   30.189 1.00 67.07  ? 359 GLU   A C   1 
ATOM   2619 O O   . GLU   B 1 144 ? -40.736 5.758   29.782 1.00 68.53  ? 359 GLU   A O   1 
ATOM   2620 C CB  . GLU   B 1 144 ? -37.542 6.653   29.363 1.00 67.80  ? 359 GLU   A CB  1 
ATOM   2621 C CG  . GLU   B 1 144 ? -36.675 6.914   28.182 1.00 74.07  ? 359 GLU   A CG  1 
ATOM   2622 C CD  . GLU   B 1 144 ? -35.333 7.458   28.594 1.00 82.56  ? 359 GLU   A CD  1 
ATOM   2623 O OE1 . GLU   B 1 144 ? -34.842 7.030   29.675 1.00 78.63  ? 359 GLU   A OE1 1 
ATOM   2624 O OE2 . GLU   B 1 144 ? -34.773 8.296   27.834 1.00 83.13  ? 359 GLU   A OE2 1 
ATOM   2625 N N   . THR   B 1 145 ? -39.300 5.372   31.471 1.00 66.04  ? 360 THR   A N   1 
ATOM   2626 C CA  . THR   B 1 145 ? -40.315 5.428   32.516 1.00 73.61  ? 360 THR   A CA  1 
ATOM   2627 C C   . THR   B 1 145 ? -39.810 6.330   33.639 1.00 73.64  ? 360 THR   A C   1 
ATOM   2628 O O   . THR   B 1 145 ? -38.734 6.089   34.199 1.00 75.42  ? 360 THR   A O   1 
ATOM   2629 C CB  . THR   B 1 145 ? -40.637 4.017   33.013 1.00 66.67  ? 360 THR   A CB  1 
ATOM   2630 O OG1 . THR   B 1 145 ? -39.429 3.250   33.016 1.00 69.89  ? 360 THR   A OG1 1 
ATOM   2631 C CG2 . THR   B 1 145 ? -41.631 3.336   32.078 1.00 61.62  ? 360 THR   A CG2 1 
ATOM   2632 N N   . GLU   B 1 146 ? -40.557 7.393   33.936 1.00 71.65  ? 361 GLU   A N   1 
ATOM   2633 C CA  . GLU   B 1 146 ? -40.200 8.290   35.029 1.00 80.77  ? 361 GLU   A CA  1 
ATOM   2634 C C   . GLU   B 1 146 ? -41.366 8.458   35.995 1.00 80.74  ? 361 GLU   A C   1 
ATOM   2635 O O   . GLU   B 1 146 ? -42.486 8.797   35.589 1.00 70.03  ? 361 GLU   A O   1 
ATOM   2636 C CB  . GLU   B 1 146 ? -39.746 9.658   34.519 1.00 75.80  ? 361 GLU   A CB  1 
ATOM   2637 C CG  . GLU   B 1 146 ? -39.041 10.502  35.596 1.00 77.49  ? 361 GLU   A CG  1 
ATOM   2638 C CD  . GLU   B 1 146 ? -37.806 9.839   36.229 1.00 81.19  ? 361 GLU   A CD  1 
ATOM   2639 O OE1 . GLU   B 1 146 ? -37.374 10.313  37.308 1.00 82.17  ? 361 GLU   A OE1 1 
ATOM   2640 O OE2 . GLU   B 1 146 ? -37.227 8.899   35.634 1.00 88.79  ? 361 GLU   A OE2 1 
ATOM   2641 N N   . ARG   B 1 147 ? -41.094 8.221   37.269 1.00 98.06  ? 362 ARG   A N   1 
ATOM   2642 C CA  . ARG   B 1 147 ? -42.085 8.388   38.316 1.00 100.75 ? 362 ARG   A CA  1 
ATOM   2643 C C   . ARG   B 1 147 ? -41.920 9.751   38.973 1.00 102.10 ? 362 ARG   A C   1 
ATOM   2644 O O   . ARG   B 1 147 ? -40.851 10.363  38.934 1.00 102.22 ? 362 ARG   A O   1 
ATOM   2645 C CB  . ARG   B 1 147 ? -41.986 7.269   39.361 1.00 105.43 ? 362 ARG   A CB  1 
ATOM   2646 C CG  . ARG   B 1 147 ? -40.697 7.238   40.194 1.00 108.24 ? 362 ARG   A CG  1 
ATOM   2647 C CD  . ARG   B 1 147 ? -39.468 6.692   39.427 1.00 112.11 ? 362 ARG   A CD  1 
ATOM   2648 N NE  . ARG   B 1 147 ? -39.741 5.501   38.618 1.00 115.60 ? 362 ARG   A NE  1 
ATOM   2649 C CZ  . ARG   B 1 147 ? -40.014 4.293   39.104 1.00 118.68 ? 362 ARG   A CZ  1 
ATOM   2650 N NH1 . ARG   B 1 147 ? -40.079 4.071   40.408 1.00 116.52 ? 362 ARG   A NH1 1 
ATOM   2651 N NH2 . ARG   B 1 147 ? -40.229 3.283   38.260 1.00 124.07 ? 362 ARG   A NH2 1 
ATOM   2652 N N   . ALA   B 1 148 ? -43.011 10.224  39.570 1.00 83.30  ? 363 ALA   A N   1 
ATOM   2653 C CA  . ALA   B 1 148 ? -43.044 11.568  40.119 1.00 75.79  ? 363 ALA   A CA  1 
ATOM   2654 C C   . ALA   B 1 148 ? -42.055 11.720  41.263 1.00 73.82  ? 363 ALA   A C   1 
ATOM   2655 O O   . ALA   B 1 148 ? -41.867 10.809  42.072 1.00 74.21  ? 363 ALA   A O   1 
ATOM   2656 C CB  . ALA   B 1 148 ? -44.457 11.895  40.595 1.00 72.36  ? 363 ALA   A CB  1 
ATOM   2657 N N   . GLN   B 1 149 ? -41.403 12.876  41.310 1.00 71.86  ? 364 GLN   A N   1 
ATOM   2658 C CA  . GLN   B 1 149 ? -40.593 13.298  42.445 1.00 72.05  ? 364 GLN   A CA  1 
ATOM   2659 C C   . GLN   B 1 149 ? -41.165 14.612  42.965 1.00 74.44  ? 364 GLN   A C   1 
ATOM   2660 O O   . GLN   B 1 149 ? -41.332 15.562  42.194 1.00 73.09  ? 364 GLN   A O   1 
ATOM   2661 C CB  . GLN   B 1 149 ? -39.125 13.458  42.055 1.00 69.87  ? 364 GLN   A CB  1 
ATOM   2662 C CG  . GLN   B 1 149 ? -38.179 13.028  43.128 1.00 73.25  ? 364 GLN   A CG  1 
ATOM   2663 C CD  . GLN   B 1 149 ? -37.655 14.207  43.914 1.00 82.12  ? 364 GLN   A CD  1 
ATOM   2664 O OE1 . GLN   B 1 149 ? -37.200 15.193  43.326 1.00 83.20  ? 364 GLN   A OE1 1 
ATOM   2665 N NE2 . GLN   B 1 149 ? -37.755 14.137  45.253 1.00 79.58  ? 364 GLN   A NE2 1 
ATOM   2666 N N   . LEU   B 1 150 ? -41.467 14.665  44.266 1.00 78.19  ? 365 LEU   A N   1 
ATOM   2667 C CA  . LEU   B 1 150 ? -42.060 15.867  44.840 1.00 80.62  ? 365 LEU   A CA  1 
ATOM   2668 C C   . LEU   B 1 150 ? -41.004 16.953  44.988 1.00 80.57  ? 365 LEU   A C   1 
ATOM   2669 O O   . LEU   B 1 150 ? -39.916 16.705  45.515 1.00 75.56  ? 365 LEU   A O   1 
ATOM   2670 C CB  . LEU   B 1 150 ? -42.712 15.552  46.191 1.00 84.93  ? 365 LEU   A CB  1 
ATOM   2671 C CG  . LEU   B 1 150 ? -43.171 16.702  47.109 1.00 78.57  ? 365 LEU   A CG  1 
ATOM   2672 C CD1 . LEU   B 1 150 ? -44.434 17.434  46.634 1.00 74.54  ? 365 LEU   A CD1 1 
ATOM   2673 C CD2 . LEU   B 1 150 ? -43.375 16.135  48.492 1.00 79.31  ? 365 LEU   A CD2 1 
ATOM   2674 N N   . GLU   B 1 151 ? -41.313 18.147  44.484 1.00 100.31 ? 366 GLU   A N   1 
ATOM   2675 C CA  . GLU   B 1 151 ? -40.461 19.311  44.672 1.00 100.74 ? 366 GLU   A CA  1 
ATOM   2676 C C   . GLU   B 1 151 ? -41.348 20.502  44.977 1.00 107.29 ? 366 GLU   A C   1 
ATOM   2677 O O   . GLU   B 1 151 ? -42.573 20.381  44.979 1.00 109.81 ? 366 GLU   A O   1 
ATOM   2678 C CB  . GLU   B 1 151 ? -39.575 19.576  43.458 1.00 99.25  ? 366 GLU   A CB  1 
ATOM   2679 C CG  . GLU   B 1 151 ? -38.182 19.027  43.641 1.00 103.30 ? 366 GLU   A CG  1 
ATOM   2680 C CD  . GLU   B 1 151 ? -37.228 19.465  42.558 1.00 106.92 ? 366 GLU   A CD  1 
ATOM   2681 O OE1 . GLU   B 1 151 ? -37.513 20.475  41.881 1.00 107.98 ? 366 GLU   A OE1 1 
ATOM   2682 O OE2 . GLU   B 1 151 ? -36.185 18.799  42.388 1.00 109.14 ? 366 GLU   A OE2 1 
ATOM   2683 N N   . ASP   B 1 152 ? -40.716 21.661  45.220 1.00 105.62 ? 367 ASP   A N   1 
ATOM   2684 C CA  . ASP   B 1 152 ? -41.358 22.866  45.746 1.00 105.68 ? 367 ASP   A CA  1 
ATOM   2685 C C   . ASP   B 1 152 ? -42.852 22.897  45.449 1.00 102.86 ? 367 ASP   A C   1 
ATOM   2686 O O   . ASP   B 1 152 ? -43.306 23.607  44.546 1.00 107.41 ? 367 ASP   A O   1 
ATOM   2687 C CB  . ASP   B 1 152 ? -40.675 24.119  45.184 1.00 113.15 ? 367 ASP   A CB  1 
ATOM   2688 C CG  . ASP   B 1 152 ? -40.522 25.231  46.231 1.00 117.12 ? 367 ASP   A CG  1 
ATOM   2689 O OD1 . ASP   B 1 152 ? -41.171 25.155  47.306 1.00 114.64 ? 367 ASP   A OD1 1 
ATOM   2690 O OD2 . ASP   B 1 152 ? -39.749 26.186  45.966 1.00 117.74 ? 367 ASP   A OD2 1 
ATOM   2691 N N   . GLY   B 1 153 ? -43.609 22.069  46.172 1.00 90.15  ? 368 GLY   A N   1 
ATOM   2692 C CA  . GLY   B 1 153 ? -45.049 22.025  46.080 1.00 82.52  ? 368 GLY   A CA  1 
ATOM   2693 C C   . GLY   B 1 153 ? -45.617 21.458  44.806 1.00 84.60  ? 368 GLY   A C   1 
ATOM   2694 O O   . GLY   B 1 153 ? -46.844 21.486  44.647 1.00 74.90  ? 368 GLY   A O   1 
ATOM   2695 N N   . ARG   B 1 154 ? -44.772 20.953  43.893 1.00 91.91  ? 369 ARG   A N   1 
ATOM   2696 C CA  . ARG   B 1 154 ? -45.201 20.301  42.656 1.00 86.42  ? 369 ARG   A CA  1 
ATOM   2697 C C   . ARG   B 1 154 ? -44.441 18.982  42.448 1.00 84.00  ? 369 ARG   A C   1 
ATOM   2698 O O   . ARG   B 1 154 ? -43.455 18.678  43.132 1.00 82.70  ? 369 ARG   A O   1 
ATOM   2699 C CB  . ARG   B 1 154 ? -45.026 21.243  41.449 1.00 87.82  ? 369 ARG   A CB  1 
ATOM   2700 C CG  . ARG   B 1 154 ? -43.590 21.392  40.911 1.00 91.07  ? 369 ARG   A CG  1 
ATOM   2701 C CD  . ARG   B 1 154 ? -43.501 22.612  39.999 1.00 93.92  ? 369 ARG   A CD  1 
ATOM   2702 N NE  . ARG   B 1 154 ? -42.141 23.086  39.750 1.00 89.45  ? 369 ARG   A NE  1 
ATOM   2703 C CZ  . ARG   B 1 154 ? -41.639 24.204  40.268 1.00 98.79  ? 369 ARG   A CZ  1 
ATOM   2704 N NH1 . ARG   B 1 154 ? -42.310 24.919  41.169 1.00 105.38 ? 369 ARG   A NH1 1 
ATOM   2705 N NH2 . ARG   B 1 154 ? -40.433 24.614  39.883 1.00 99.98  ? 369 ARG   A NH2 1 
ATOM   2706 N N   . PHE   B 1 155 ? -44.925 18.186  41.490 1.00 74.08  ? 370 PHE   A N   1 
ATOM   2707 C CA  . PHE   B 1 155 ? -44.251 16.964  41.058 1.00 75.45  ? 370 PHE   A CA  1 
ATOM   2708 C C   . PHE   B 1 155 ? -43.443 17.223  39.785 1.00 75.96  ? 370 PHE   A C   1 
ATOM   2709 O O   . PHE   B 1 155 ? -43.974 17.733  38.790 1.00 71.88  ? 370 PHE   A O   1 
ATOM   2710 C CB  . PHE   B 1 155 ? -45.252 15.827  40.826 1.00 70.76  ? 370 PHE   A CB  1 
ATOM   2711 C CG  . PHE   B 1 155 ? -45.995 15.420  42.065 1.00 74.97  ? 370 PHE   A CG  1 
ATOM   2712 C CD1 . PHE   B 1 155 ? -45.342 14.772  43.102 1.00 73.81  ? 370 PHE   A CD1 1 
ATOM   2713 C CD2 . PHE   B 1 155 ? -47.346 15.693  42.205 1.00 75.22  ? 370 PHE   A CD2 1 
ATOM   2714 C CE1 . PHE   B 1 155 ? -46.023 14.411  44.247 1.00 69.19  ? 370 PHE   A CE1 1 
ATOM   2715 C CE2 . PHE   B 1 155 ? -48.024 15.322  43.349 1.00 68.42  ? 370 PHE   A CE2 1 
ATOM   2716 C CZ  . PHE   B 1 155 ? -47.359 14.682  44.359 1.00 65.25  ? 370 PHE   A CZ  1 
ATOM   2717 N N   . VAL   B 1 156 ? -42.159 16.865  39.827 1.00 74.27  ? 371 VAL   A N   1 
ATOM   2718 C CA  . VAL   B 1 156 ? -41.253 16.996  38.696 1.00 72.80  ? 371 VAL   A CA  1 
ATOM   2719 C C   . VAL   B 1 156 ? -40.857 15.608  38.197 1.00 74.18  ? 371 VAL   A C   1 
ATOM   2720 O O   . VAL   B 1 156 ? -40.778 14.636  38.958 1.00 72.12  ? 371 VAL   A O   1 
ATOM   2721 C CB  . VAL   B 1 156 ? -40.010 17.833  39.061 1.00 72.41  ? 371 VAL   A CB  1 
ATOM   2722 C CG1 . VAL   B 1 156 ? -40.431 19.045  39.819 1.00 84.10  ? 371 VAL   A CG1 1 
ATOM   2723 C CG2 . VAL   B 1 156 ? -39.045 17.024  39.898 1.00 76.38  ? 371 VAL   A CG2 1 
ATOM   2724 N N   . TYR   B 1 157 ? -40.620 15.520  36.899 1.00 69.69  ? 372 TYR   A N   1 
ATOM   2725 C CA  . TYR   B 1 157 ? -40.188 14.289  36.253 1.00 71.14  ? 372 TYR   A CA  1 
ATOM   2726 C C   . TYR   B 1 157 ? -38.864 14.592  35.565 1.00 75.18  ? 372 TYR   A C   1 
ATOM   2727 O O   . TYR   B 1 157 ? -38.826 15.355  34.588 1.00 77.47  ? 372 TYR   A O   1 
ATOM   2728 C CB  . TYR   B 1 157 ? -41.244 13.842  35.255 1.00 67.81  ? 372 TYR   A CB  1 
ATOM   2729 C CG  . TYR   B 1 157 ? -42.617 13.769  35.840 1.00 68.54  ? 372 TYR   A CG  1 
ATOM   2730 C CD1 . TYR   B 1 157 ? -42.978 12.756  36.729 1.00 72.43  ? 372 TYR   A CD1 1 
ATOM   2731 C CD2 . TYR   B 1 157 ? -43.521 14.785  35.610 1.00 68.81  ? 372 TYR   A CD2 1 
ATOM   2732 C CE1 . TYR   B 1 157 ? -44.247 12.705  37.284 1.00 67.72  ? 372 TYR   A CE1 1 
ATOM   2733 C CE2 . TYR   B 1 157 ? -44.791 14.752  36.183 1.00 70.79  ? 372 TYR   A CE2 1 
ATOM   2734 C CZ  . TYR   B 1 157 ? -45.138 13.707  37.023 1.00 66.99  ? 372 TYR   A CZ  1 
ATOM   2735 O OH  . TYR   B 1 157 ? -46.379 13.661  37.593 1.00 68.60  ? 372 TYR   A OH  1 
ATOM   2736 N N   . ARG   B 1 158 ? -37.779 14.031  36.079 1.00 72.57  ? 373 ARG   A N   1 
ATOM   2737 C CA  . ARG   B 1 158 ? -36.454 14.352  35.573 1.00 70.56  ? 373 ARG   A CA  1 
ATOM   2738 C C   . ARG   B 1 158 ? -35.899 13.162  34.804 1.00 73.81  ? 373 ARG   A C   1 
ATOM   2739 O O   . ARG   B 1 158 ? -35.539 12.140  35.396 1.00 74.57  ? 373 ARG   A O   1 
ATOM   2740 C CB  . ARG   B 1 158 ? -35.537 14.771  36.707 1.00 70.54  ? 373 ARG   A CB  1 
ATOM   2741 C CG  . ARG   B 1 158 ? -35.792 16.203  37.137 1.00 76.23  ? 373 ARG   A CG  1 
ATOM   2742 C CD  . ARG   B 1 158 ? -34.658 16.751  37.969 1.00 74.24  ? 373 ARG   A CD  1 
ATOM   2743 N NE  . ARG   B 1 158 ? -34.868 18.163  38.251 1.00 87.41  ? 373 ARG   A NE  1 
ATOM   2744 C CZ  . ARG   B 1 158 ? -35.428 18.627  39.364 1.00 92.80  ? 373 ARG   A CZ  1 
ATOM   2745 N NH1 . ARG   B 1 158 ? -35.862 17.811  40.311 1.00 89.39  ? 373 ARG   A NH1 1 
ATOM   2746 N NH2 . ARG   B 1 158 ? -35.554 19.943  39.530 1.00 90.80  ? 373 ARG   A NH2 1 
ATOM   2747 N N   . LEU   B 1 159 ? -35.838 13.298  33.483 1.00 73.86  ? 374 LEU   A N   1 
ATOM   2748 C CA  . LEU   B 1 159 ? -35.211 12.317  32.606 1.00 68.40  ? 374 LEU   A CA  1 
ATOM   2749 C C   . LEU   B 1 159 ? -33.947 12.950  32.036 1.00 69.70  ? 374 LEU   A C   1 
ATOM   2750 O O   . LEU   B 1 159 ? -33.860 13.284  30.848 1.00 72.06  ? 374 LEU   A O   1 
ATOM   2751 C CB  . LEU   B 1 159 ? -36.180 11.865  31.493 1.00 66.70  ? 374 LEU   A CB  1 
ATOM   2752 C CG  . LEU   B 1 159 ? -37.625 11.478  31.845 1.00 68.20  ? 374 LEU   A CG  1 
ATOM   2753 C CD1 . LEU   B 1 159 ? -38.521 12.698  32.043 1.00 71.44  ? 374 LEU   A CD1 1 
ATOM   2754 C CD2 . LEU   B 1 159 ? -38.235 10.552  30.826 1.00 62.53  ? 374 LEU   A CD2 1 
ATOM   2755 N N   . LEU   B 1 160 ? -32.965 13.137  32.914 1.00 69.33  ? 375 LEU   A N   1 
ATOM   2756 C CA  . LEU   B 1 160 ? -31.762 13.880  32.579 1.00 70.12  ? 375 LEU   A CA  1 
ATOM   2757 C C   . LEU   B 1 160 ? -30.642 12.974  32.080 1.00 70.24  ? 375 LEU   A C   1 
ATOM   2758 O O   . LEU   B 1 160 ? -30.423 11.874  32.606 1.00 63.01  ? 375 LEU   A O   1 
ATOM   2759 C CB  . LEU   B 1 160 ? -31.267 14.685  33.778 1.00 68.10  ? 375 LEU   A CB  1 
ATOM   2760 C CG  . LEU   B 1 160 ? -32.311 15.415  34.613 1.00 69.92  ? 375 LEU   A CG  1 
ATOM   2761 C CD1 . LEU   B 1 160 ? -31.704 15.735  35.977 1.00 65.13  ? 375 LEU   A CD1 1 
ATOM   2762 C CD2 . LEU   B 1 160 ? -32.810 16.667  33.892 1.00 71.93  ? 375 LEU   A CD2 1 
ATOM   2763 N N   . ARG   B 1 161 ? -29.951 13.465  31.037 1.00 72.64  ? 376 ARG   A N   1 
ATOM   2764 C CA  . ARG   B 1 161 ? -28.715 12.891  30.497 1.00 72.05  ? 376 ARG   A CA  1 
ATOM   2765 C C   . ARG   B 1 161 ? -28.885 11.430  30.070 1.00 72.29  ? 376 ARG   A C   1 
ATOM   2766 O O   . ARG   B 1 161 ? -28.055 10.569  30.374 1.00 70.30  ? 376 ARG   A O   1 
ATOM   2767 C CB  . ARG   B 1 161 ? -27.573 13.053  31.499 1.00 75.14  ? 376 ARG   A CB  1 
ATOM   2768 C CG  . ARG   B 1 161 ? -27.284 14.509  31.903 1.00 76.16  ? 376 ARG   A CG  1 
ATOM   2769 C CD  . ARG   B 1 161 ? -25.954 14.574  32.631 1.00 83.60  ? 376 ARG   A CD  1 
ATOM   2770 N NE  . ARG   B 1 161 ? -25.011 13.650  32.012 1.00 86.82  ? 376 ARG   A NE  1 
ATOM   2771 C CZ  . ARG   B 1 161 ? -23.767 13.957  31.674 1.00 91.28  ? 376 ARG   A CZ  1 
ATOM   2772 N NH1 . ARG   B 1 161 ? -23.229 15.121  32.007 1.00 96.60  ? 376 ARG   A NH1 1 
ATOM   2773 N NH2 . ARG   B 1 161 ? -23.044 13.076  30.979 1.00 86.08  ? 376 ARG   A NH2 1 
ATOM   2774 N N   . SER   B 1 162 ? -29.963 11.149  29.346 1.00 67.05  ? 377 SER   A N   1 
ATOM   2775 C CA  . SER   B 1 162 ? -30.125 9.841   28.720 1.00 66.12  ? 377 SER   A CA  1 
ATOM   2776 C C   . SER   B 1 162 ? -29.136 9.736   27.568 1.00 70.75  ? 377 SER   A C   1 
ATOM   2777 O O   . SER   B 1 162 ? -28.990 10.696  26.798 1.00 67.83  ? 377 SER   A O   1 
ATOM   2778 C CB  . SER   B 1 162 ? -31.542 9.677   28.180 1.00 68.45  ? 377 SER   A CB  1 
ATOM   2779 O OG  . SER   B 1 162 ? -32.491 10.336  29.021 1.00 74.43  ? 377 SER   A OG  1 
ATOM   2780 N N   . PRO   B 1 163 ? -28.432 8.620   27.416 1.00 72.78  ? 378 PRO   A N   1 
ATOM   2781 C CA  . PRO   B 1 163 ? -27.579 8.464   26.231 1.00 69.20  ? 378 PRO   A CA  1 
ATOM   2782 C C   . PRO   B 1 163 ? -28.421 8.491   24.968 1.00 69.93  ? 378 PRO   A C   1 
ATOM   2783 O O   . PRO   B 1 163 ? -29.329 7.677   24.790 1.00 65.12  ? 378 PRO   A O   1 
ATOM   2784 C CB  . PRO   B 1 163 ? -26.914 7.104   26.445 1.00 69.55  ? 378 PRO   A CB  1 
ATOM   2785 C CG  . PRO   B 1 163 ? -26.972 6.896   27.941 1.00 74.36  ? 378 PRO   A CG  1 
ATOM   2786 C CD  . PRO   B 1 163 ? -28.300 7.486   28.342 1.00 71.01  ? 378 PRO   A CD  1 
ATOM   2787 N N   . MET   B 1 164 ? -28.142 9.486   24.121 1.00 73.57  ? 379 MET   A N   1 
ATOM   2788 C CA  . MET   B 1 164 ? -28.703 9.560   22.780 1.00 71.88  ? 379 MET   A CA  1 
ATOM   2789 C C   . MET   B 1 164 ? -28.225 8.371   21.952 1.00 75.24  ? 379 MET   A C   1 
ATOM   2790 O O   . MET   B 1 164 ? -27.075 7.937   22.073 1.00 75.00  ? 379 MET   A O   1 
ATOM   2791 C CB  . MET   B 1 164 ? -28.302 10.882  22.131 1.00 68.03  ? 379 MET   A CB  1 
ATOM   2792 C CG  . MET   B 1 164 ? -28.559 10.919  20.647 1.00 76.33  ? 379 MET   A CG  1 
ATOM   2793 S SD  . MET   B 1 164 ? -28.272 12.490  19.814 1.00 72.10  ? 379 MET   A SD  1 
ATOM   2794 C CE  . MET   B 1 164 ? -27.285 13.406  20.968 1.00 71.84  ? 379 MET   A CE  1 
ATOM   2795 N N   . CYS   B 1 165 ? -29.118 7.818   21.133 1.00 78.94  ? 380 CYS   A N   1 
ATOM   2796 C CA  . CYS   B 1 165 ? -28.846 6.511   20.549 1.00 82.56  ? 380 CYS   A CA  1 
ATOM   2797 C C   . CYS   B 1 165 ? -27.841 6.591   19.407 1.00 85.30  ? 380 CYS   A C   1 
ATOM   2798 O O   . CYS   B 1 165 ? -27.715 7.614   18.722 1.00 80.89  ? 380 CYS   A O   1 
ATOM   2799 C CB  . CYS   B 1 165 ? -30.126 5.861   20.037 1.00 84.72  ? 380 CYS   A CB  1 
ATOM   2800 S SG  . CYS   B 1 165 ? -30.895 6.717   18.663 1.00 87.48  ? 380 CYS   A SG  1 
ATOM   2801 N N   . GLU   B 1 166 ? -27.155 5.463   19.187 1.00 88.89  ? 381 GLU   A N   1 
ATOM   2802 C CA  . GLU   B 1 166 ? -26.068 5.403   18.219 1.00 89.23  ? 381 GLU   A CA  1 
ATOM   2803 C C   . GLU   B 1 166 ? -26.504 5.830   16.825 1.00 89.40  ? 381 GLU   A C   1 
ATOM   2804 O O   . GLU   B 1 166 ? -25.673 6.287   16.036 1.00 89.62  ? 381 GLU   A O   1 
ATOM   2805 C CB  . GLU   B 1 166 ? -25.502 3.990   18.148 1.00 97.50  ? 381 GLU   A CB  1 
ATOM   2806 C CG  . GLU   B 1 166 ? -24.768 3.465   19.381 1.00 104.66 ? 381 GLU   A CG  1 
ATOM   2807 C CD  . GLU   B 1 166 ? -25.641 3.220   20.610 1.00 106.00 ? 381 GLU   A CD  1 
ATOM   2808 O OE1 . GLU   B 1 166 ? -25.158 2.504   21.525 1.00 112.54 ? 381 GLU   A OE1 1 
ATOM   2809 O OE2 . GLU   B 1 166 ? -26.783 3.724   20.672 1.00 104.74 ? 381 GLU   A OE2 1 
ATOM   2810 N N   . TYR   B 1 167 ? -27.778 5.637   16.483 1.00 82.97  ? 382 TYR   A N   1 
ATOM   2811 C CA  . TYR   B 1 167 ? -28.267 6.104   15.198 1.00 76.33  ? 382 TYR   A CA  1 
ATOM   2812 C C   . TYR   B 1 167 ? -28.086 7.608   15.092 1.00 78.65  ? 382 TYR   A C   1 
ATOM   2813 O O   . TYR   B 1 167 ? -27.407 8.099   14.186 1.00 81.33  ? 382 TYR   A O   1 
ATOM   2814 C CB  . TYR   B 1 167 ? -29.733 5.696   15.004 1.00 77.37  ? 382 TYR   A CB  1 
ATOM   2815 C CG  . TYR   B 1 167 ? -30.331 6.067   13.652 1.00 81.21  ? 382 TYR   A CG  1 
ATOM   2816 C CD1 . TYR   B 1 167 ? -30.519 7.396   13.287 1.00 82.34  ? 382 TYR   A CD1 1 
ATOM   2817 C CD2 . TYR   B 1 167 ? -30.668 5.084   12.718 1.00 80.97  ? 382 TYR   A CD2 1 
ATOM   2818 C CE1 . TYR   B 1 167 ? -31.035 7.746   12.038 1.00 82.41  ? 382 TYR   A CE1 1 
ATOM   2819 C CE2 . TYR   B 1 167 ? -31.196 5.424   11.467 1.00 77.69  ? 382 TYR   A CE2 1 
ATOM   2820 C CZ  . TYR   B 1 167 ? -31.379 6.766   11.136 1.00 81.06  ? 382 TYR   A CZ  1 
ATOM   2821 O OH  . TYR   B 1 167 ? -31.904 7.162   9.916  1.00 76.12  ? 382 TYR   A OH  1 
ATOM   2822 N N   . LEU   B 1 168 ? -28.677 8.360   16.022 1.00 79.12  ? 383 LEU   A N   1 
ATOM   2823 C CA  . LEU   B 1 168 ? -28.578 9.812   15.958 1.00 74.55  ? 383 LEU   A CA  1 
ATOM   2824 C C   . LEU   B 1 168 ? -27.132 10.285  15.993 1.00 71.75  ? 383 LEU   A C   1 
ATOM   2825 O O   . LEU   B 1 168 ? -26.768 11.216  15.271 1.00 70.19  ? 383 LEU   A O   1 
ATOM   2826 C CB  . LEU   B 1 168 ? -29.371 10.448  17.093 1.00 77.50  ? 383 LEU   A CB  1 
ATOM   2827 C CG  . LEU   B 1 168 ? -30.870 10.630  16.850 1.00 76.57  ? 383 LEU   A CG  1 
ATOM   2828 C CD1 . LEU   B 1 168 ? -31.063 11.240  15.474 1.00 76.26  ? 383 LEU   A CD1 1 
ATOM   2829 C CD2 . LEU   B 1 168 ? -31.674 9.362   16.999 1.00 78.96  ? 383 LEU   A CD2 1 
ATOM   2830 N N   . VAL   B 1 169 ? -26.294 9.666   16.819 1.00 72.14  ? 384 VAL   A N   1 
ATOM   2831 C CA  . VAL   B 1 169 ? -24.894 10.075  16.884 1.00 72.63  ? 384 VAL   A CA  1 
ATOM   2832 C C   . VAL   B 1 169 ? -24.206 9.871   15.529 1.00 76.41  ? 384 VAL   A C   1 
ATOM   2833 O O   . VAL   B 1 169 ? -23.534 10.775  15.020 1.00 72.69  ? 384 VAL   A O   1 
ATOM   2834 C CB  . VAL   B 1 169 ? -24.180 9.324   18.020 1.00 74.04  ? 384 VAL   A CB  1 
ATOM   2835 C CG1 . VAL   B 1 169 ? -22.883 10.010  18.396 1.00 71.57  ? 384 VAL   A CG1 1 
ATOM   2836 C CG2 . VAL   B 1 169 ? -25.093 9.229   19.220 1.00 77.74  ? 384 VAL   A CG2 1 
ATOM   2837 N N   . ASN   B 1 170 ? -24.365 8.683   14.924 1.00 76.18  ? 385 ASN   A N   1 
ATOM   2838 C CA  . ASN   B 1 170 ? -23.801 8.410   13.600 1.00 73.60  ? 385 ASN   A CA  1 
ATOM   2839 C C   . ASN   B 1 170 ? -24.299 9.421   12.576 1.00 73.66  ? 385 ASN   A C   1 
ATOM   2840 O O   . ASN   B 1 170 ? -23.508 10.073  11.879 1.00 73.79  ? 385 ASN   A O   1 
ATOM   2841 C CB  . ASN   B 1 170 ? -24.188 7.001   13.152 1.00 78.57  ? 385 ASN   A CB  1 
ATOM   2842 C CG  . ASN   B 1 170 ? -23.520 5.908   13.978 1.00 92.53  ? 385 ASN   A CG  1 
ATOM   2843 O OD1 . ASN   B 1 170 ? -22.669 6.171   14.834 1.00 93.11  ? 385 ASN   A OD1 1 
ATOM   2844 N ND2 . ASN   B 1 170 ? -23.933 4.665   13.739 1.00 95.96  ? 385 ASN   A ND2 1 
ATOM   2845 N N   . PHE   B 1 171 ? -25.623 9.547   12.468 1.00 70.54  ? 386 PHE   A N   1 
ATOM   2846 C CA  . PHE   B 1 171 ? -26.245 10.531  11.589 1.00 68.62  ? 386 PHE   A CA  1 
ATOM   2847 C C   . PHE   B 1 171 ? -25.759 11.953  11.868 1.00 71.77  ? 386 PHE   A C   1 
ATOM   2848 O O   . PHE   B 1 171 ? -25.734 12.775  10.949 1.00 73.80  ? 386 PHE   A O   1 
ATOM   2849 C CB  . PHE   B 1 171 ? -27.763 10.426  11.744 1.00 67.00  ? 386 PHE   A CB  1 
ATOM   2850 C CG  . PHE   B 1 171 ? -28.547 11.457  10.993 1.00 66.70  ? 386 PHE   A CG  1 
ATOM   2851 C CD1 . PHE   B 1 171 ? -28.954 11.228  9.700  1.00 65.95  ? 386 PHE   A CD1 1 
ATOM   2852 C CD2 . PHE   B 1 171 ? -28.942 12.630  11.601 1.00 67.34  ? 386 PHE   A CD2 1 
ATOM   2853 C CE1 . PHE   B 1 171 ? -29.712 12.160  9.016  1.00 62.78  ? 386 PHE   A CE1 1 
ATOM   2854 C CE2 . PHE   B 1 171 ? -29.709 13.563  10.911 1.00 63.28  ? 386 PHE   A CE2 1 
ATOM   2855 C CZ  . PHE   B 1 171 ? -30.087 13.319  9.620  1.00 62.64  ? 386 PHE   A CZ  1 
ATOM   2856 N N   . LEU   B 1 172 ? -25.393 12.273  13.120 1.00 73.29  ? 387 LEU   A N   1 
ATOM   2857 C CA  . LEU   B 1 172 ? -24.865 13.600  13.435 1.00 67.09  ? 387 LEU   A CA  1 
ATOM   2858 C C   . LEU   B 1 172 ? -23.430 13.762  12.941 1.00 69.18  ? 387 LEU   A C   1 
ATOM   2859 O O   . LEU   B 1 172 ? -23.037 14.851  12.515 1.00 71.79  ? 387 LEU   A O   1 
ATOM   2860 C CB  . LEU   B 1 172 ? -24.926 13.858  14.942 1.00 63.83  ? 387 LEU   A CB  1 
ATOM   2861 C CG  . LEU   B 1 172 ? -26.184 14.459  15.584 1.00 69.18  ? 387 LEU   A CG  1 
ATOM   2862 C CD1 . LEU   B 1 172 ? -25.891 15.152  16.913 1.00 61.85  ? 387 LEU   A CD1 1 
ATOM   2863 C CD2 . LEU   B 1 172 ? -26.890 15.408  14.641 1.00 65.33  ? 387 LEU   A CD2 1 
ATOM   2864 N N   . HIS   B 1 173 ? -22.619 12.709  13.025 1.00 65.67  ? 388 HIS   A N   1 
ATOM   2865 C CA  . HIS   B 1 173 ? -21.266 12.817  12.497 1.00 73.97  ? 388 HIS   A CA  1 
ATOM   2866 C C   . HIS   B 1 173 ? -21.292 12.952  10.983 1.00 78.35  ? 388 HIS   A C   1 
ATOM   2867 O O   . HIS   B 1 173 ? -20.462 13.655  10.393 1.00 75.05  ? 388 HIS   A O   1 
ATOM   2868 C CB  . HIS   B 1 173 ? -20.423 11.610  12.906 1.00 72.79  ? 388 HIS   A CB  1 
ATOM   2869 C CG  . HIS   B 1 173 ? -19.391 11.923  13.945 1.00 79.25  ? 388 HIS   A CG  1 
ATOM   2870 N N   . LYS   B 1 174 ? -22.252 12.289  10.344 1.00 75.71  ? 389 LYS   A N   1 
ATOM   2871 C CA  . LYS   B 1 174 ? -22.386 12.378  8.902  1.00 72.25  ? 389 LYS   A CA  1 
ATOM   2872 C C   . LYS   B 1 174 ? -22.966 13.729  8.494  1.00 72.55  ? 389 LYS   A C   1 
ATOM   2873 O O   . LYS   B 1 174 ? -22.460 14.384  7.578  1.00 75.35  ? 389 LYS   A O   1 
ATOM   2874 C CB  . LYS   B 1 174 ? -23.247 11.214  8.411  1.00 72.18  ? 389 LYS   A CB  1 
ATOM   2875 C CG  . LYS   B 1 174 ? -22.627 9.823   8.682  1.00 71.22  ? 389 LYS   A CG  1 
ATOM   2876 C CD  . LYS   B 1 174 ? -23.630 8.676   8.476  1.00 70.93  ? 389 LYS   A CD  1 
ATOM   2877 C CE  . LYS   B 1 174 ? -22.975 7.297   8.614  1.00 75.92  ? 389 LYS   A CE  1 
ATOM   2878 N NZ  . LYS   B 1 174 ? -22.589 6.922   10.027 1.00 82.57  ? 389 LYS   A NZ  1 
ATOM   2879 N N   . LEU   B 1 175 ? -24.010 14.174  9.187  1.00 70.59  ? 390 LEU   A N   1 
ATOM   2880 C CA  . LEU   B 1 175 ? -24.637 15.457  8.881  1.00 68.24  ? 390 LEU   A CA  1 
ATOM   2881 C C   . LEU   B 1 175 ? -23.691 16.619  9.126  1.00 72.14  ? 390 LEU   A C   1 
ATOM   2882 O O   . LEU   B 1 175 ? -23.725 17.619  8.400  1.00 71.46  ? 390 LEU   A O   1 
ATOM   2883 C CB  . LEU   B 1 175 ? -25.892 15.636  9.733  1.00 69.15  ? 390 LEU   A CB  1 
ATOM   2884 C CG  . LEU   B 1 175 ? -26.904 16.705  9.336  1.00 65.48  ? 390 LEU   A CG  1 
ATOM   2885 C CD1 . LEU   B 1 175 ? -27.503 16.408  7.977  1.00 61.28  ? 390 LEU   A CD1 1 
ATOM   2886 C CD2 . LEU   B 1 175 ? -27.991 16.807  10.398 1.00 61.69  ? 390 LEU   A CD2 1 
ATOM   2887 N N   . ARG   B 1 176 ? -22.864 16.525  10.167 1.00 77.48  ? 391 ARG   A N   1 
ATOM   2888 C CA  . ARG   B 1 176 ? -22.033 17.661  10.552 1.00 79.68  ? 391 ARG   A CA  1 
ATOM   2889 C C   . ARG   B 1 176 ? -21.172 18.115  9.388  1.00 80.16  ? 391 ARG   A C   1 
ATOM   2890 O O   . ARG   B 1 176 ? -21.068 19.315  9.106  1.00 80.14  ? 391 ARG   A O   1 
ATOM   2891 C CB  . ARG   B 1 176 ? -21.160 17.283  11.754 1.00 81.36  ? 391 ARG   A CB  1 
ATOM   2892 C CG  . ARG   B 1 176 ? -20.636 18.457  12.590 1.00 84.79  ? 391 ARG   A CG  1 
ATOM   2893 C CD  . ARG   B 1 176 ? -19.294 18.114  13.235 1.00 86.48  ? 391 ARG   A CD  1 
ATOM   2894 N NE  . ARG   B 1 176 ? -19.267 16.732  13.704 1.00 91.14  ? 391 ARG   A NE  1 
ATOM   2895 C CZ  . ARG   B 1 176 ? -18.587 16.304  14.763 1.00 96.90  ? 391 ARG   A CZ  1 
ATOM   2896 N NH1 . ARG   B 1 176 ? -17.841 17.127  15.484 1.00 99.37  ? 391 ARG   A NH1 1 
ATOM   2897 N NH2 . ARG   B 1 176 ? -18.676 15.021  15.121 1.00 93.04  ? 391 ARG   A NH2 1 
ATOM   2898 N N   . GLN   B 1 177 ? -20.613 17.159  8.657  1.00 92.24  ? 392 GLN   A N   1 
ATOM   2899 C CA  . GLN   B 1 177 ? -19.537 17.393  7.714  1.00 91.95  ? 392 GLN   A CA  1 
ATOM   2900 C C   . GLN   B 1 177 ? -20.000 17.773  6.310  1.00 91.33  ? 392 GLN   A C   1 
ATOM   2901 O O   . GLN   B 1 177 ? -19.148 18.117  5.487  1.00 93.76  ? 392 GLN   A O   1 
ATOM   2902 C CB  . GLN   B 1 177 ? -18.648 16.151  7.666  1.00 94.20  ? 392 GLN   A CB  1 
ATOM   2903 C CG  . GLN   B 1 177 ? -19.291 14.948  7.003  1.00 95.01  ? 392 GLN   A CG  1 
ATOM   2904 C CD  . GLN   B 1 177 ? -18.665 13.631  7.444  1.00 96.26  ? 392 GLN   A CD  1 
ATOM   2905 O OE1 . GLN   B 1 177 ? -18.917 12.583  6.847  1.00 94.29  ? 392 GLN   A OE1 1 
ATOM   2906 N NE2 . GLN   B 1 177 ? -17.847 13.680  8.500  1.00 95.26  ? 392 GLN   A NE2 1 
ATOM   2907 N N   . LEU   B 1 178 ? -21.299 17.725  6.008  1.00 72.31  ? 393 LEU   A N   1 
ATOM   2908 C CA  . LEU   B 1 178 ? -21.791 18.288  4.757  1.00 69.90  ? 393 LEU   A CA  1 
ATOM   2909 C C   . LEU   B 1 178 ? -21.298 19.726  4.595  1.00 71.82  ? 393 LEU   A C   1 
ATOM   2910 O O   . LEU   B 1 178 ? -21.248 20.478  5.577  1.00 72.66  ? 393 LEU   A O   1 
ATOM   2911 C CB  . LEU   B 1 178 ? -23.314 18.277  4.712  1.00 65.26  ? 393 LEU   A CB  1 
ATOM   2912 C CG  . LEU   B 1 178 ? -24.013 16.961  4.941  1.00 61.22  ? 393 LEU   A CG  1 
ATOM   2913 C CD1 . LEU   B 1 178 ? -25.389 17.039  4.336  1.00 59.91  ? 393 LEU   A CD1 1 
ATOM   2914 C CD2 . LEU   B 1 178 ? -23.227 15.858  4.321  1.00 70.15  ? 393 LEU   A CD2 1 
ATOM   2915 N N   . PRO   B 1 179 ? -20.938 20.152  3.378  1.00 70.77  ? 394 PRO   A N   1 
ATOM   2916 C CA  . PRO   B 1 179 ? -20.266 21.450  3.226  1.00 70.22  ? 394 PRO   A CA  1 
ATOM   2917 C C   . PRO   B 1 179 ? -21.183 22.661  3.177  1.00 67.74  ? 394 PRO   A C   1 
ATOM   2918 O O   . PRO   B 1 179 ? -20.660 23.782  3.198  1.00 68.71  ? 394 PRO   A O   1 
ATOM   2919 C CB  . PRO   B 1 179 ? -19.498 21.298  1.897  1.00 67.83  ? 394 PRO   A CB  1 
ATOM   2920 C CG  . PRO   B 1 179 ? -19.818 19.934  1.367  1.00 70.95  ? 394 PRO   A CG  1 
ATOM   2921 C CD  . PRO   B 1 179 ? -21.001 19.420  2.105  1.00 70.42  ? 394 PRO   A CD  1 
ATOM   2922 N N   . GLU   B 1 180 ? -22.509 22.499  3.104  1.00 66.64  ? 395 GLU   A N   1 
ATOM   2923 C CA  . GLU   B 1 180 ? -23.407 23.640  2.975  1.00 68.92  ? 395 GLU   A CA  1 
ATOM   2924 C C   . GLU   B 1 180 ? -24.657 23.493  3.832  1.00 73.03  ? 395 GLU   A C   1 
ATOM   2925 O O   . GLU   B 1 180 ? -25.228 22.406  3.943  1.00 66.12  ? 395 GLU   A O   1 
ATOM   2926 C CB  . GLU   B 1 180 ? -23.829 23.860  1.524  1.00 70.14  ? 395 GLU   A CB  1 
ATOM   2927 C CG  . GLU   B 1 180 ? -22.661 24.046  0.572  1.00 72.43  ? 395 GLU   A CG  1 
ATOM   2928 C CD  . GLU   B 1 180 ? -22.118 25.457  0.558  1.00 69.78  ? 395 GLU   A CD  1 
ATOM   2929 O OE1 . GLU   B 1 180 ? -22.214 26.155  1.586  1.00 68.96  ? 395 GLU   A OE1 1 
ATOM   2930 O OE2 . GLU   B 1 180 ? -21.591 25.866  -0.505 1.00 78.39  ? 395 GLU   A OE2 1 
ATOM   2931 N N   . ARG   B 1 181 ? -25.090 24.618  4.411  1.00 95.51  ? 396 ARG   A N   1 
ATOM   2932 C CA  . ARG   B 1 181 ? -26.284 24.615  5.250  1.00 93.72  ? 396 ARG   A CA  1 
ATOM   2933 C C   . ARG   B 1 181 ? -27.492 24.091  4.486  1.00 90.32  ? 396 ARG   A C   1 
ATOM   2934 O O   . ARG   B 1 181 ? -28.266 23.281  5.017  1.00 89.26  ? 396 ARG   A O   1 
ATOM   2935 C CB  . ARG   B 1 181 ? -26.564 26.021  5.788  1.00 96.43  ? 396 ARG   A CB  1 
ATOM   2936 C CG  . ARG   B 1 181 ? -26.468 26.180  7.314  1.00 96.54  ? 396 ARG   A CG  1 
ATOM   2937 C CD  . ARG   B 1 181 ? -25.130 25.705  7.862  1.00 100.45 ? 396 ARG   A CD  1 
ATOM   2938 N NE  . ARG   B 1 181 ? -25.165 25.565  9.312  1.00 103.76 ? 396 ARG   A NE  1 
ATOM   2939 C CZ  . ARG   B 1 181 ? -24.144 25.160  10.058 1.00 105.09 ? 396 ARG   A CZ  1 
ATOM   2940 N NH1 . ARG   B 1 181 ? -22.958 24.906  9.525  1.00 105.36 ? 396 ARG   A NH1 1 
ATOM   2941 N NH2 . ARG   B 1 181 ? -24.318 25.012  11.373 1.00 103.95 ? 396 ARG   A NH2 1 
ATOM   2942 N N   . TYR   B 1 182 ? -27.669 24.527  3.233  1.00 72.08  ? 397 TYR   A N   1 
ATOM   2943 C CA  . TYR   B 1 182 ? -28.819 24.063  2.465  1.00 67.04  ? 397 TYR   A CA  1 
ATOM   2944 C C   . TYR   B 1 182 ? -28.766 22.560  2.215  1.00 65.78  ? 397 TYR   A C   1 
ATOM   2945 O O   . TYR   B 1 182 ? -29.815 21.941  1.995  1.00 63.88  ? 397 TYR   A O   1 
ATOM   2946 C CB  . TYR   B 1 182 ? -28.953 24.838  1.138  1.00 66.63  ? 397 TYR   A CB  1 
ATOM   2947 C CG  . TYR   B 1 182 ? -28.009 24.425  0.018  1.00 68.80  ? 397 TYR   A CG  1 
ATOM   2948 C CD1 . TYR   B 1 182 ? -28.356 23.418  -0.879 1.00 66.05  ? 397 TYR   A CD1 1 
ATOM   2949 C CD2 . TYR   B 1 182 ? -26.770 25.036  -0.131 1.00 64.50  ? 397 TYR   A CD2 1 
ATOM   2950 C CE1 . TYR   B 1 182 ? -27.498 23.027  -1.874 1.00 66.94  ? 397 TYR   A CE1 1 
ATOM   2951 C CE2 . TYR   B 1 182 ? -25.910 24.664  -1.127 1.00 67.27  ? 397 TYR   A CE2 1 
ATOM   2952 C CZ  . TYR   B 1 182 ? -26.268 23.656  -2.014 1.00 73.96  ? 397 TYR   A CZ  1 
ATOM   2953 O OH  . TYR   B 1 182 ? -25.394 23.279  -3.049 1.00 72.43  ? 397 TYR   A OH  1 
ATOM   2954 N N   . MET   B 1 183 ? -27.592 21.936  2.282  1.00 63.31  ? 398 MET   A N   1 
ATOM   2955 C CA  . MET   B 1 183 ? -27.635 20.496  2.079  1.00 63.70  ? 398 MET   A CA  1 
ATOM   2956 C C   . MET   B 1 183 ? -28.074 19.765  3.341  1.00 62.09  ? 398 MET   A C   1 
ATOM   2957 O O   . MET   B 1 183 ? -28.786 18.760  3.238  1.00 55.30  ? 398 MET   A O   1 
ATOM   2958 C CB  . MET   B 1 183 ? -26.299 19.942  1.574  1.00 63.59  ? 398 MET   A CB  1 
ATOM   2959 C CG  . MET   B 1 183 ? -25.874 20.460  0.185  1.00 62.31  ? 398 MET   A CG  1 
ATOM   2960 S SD  . MET   B 1 183 ? -24.121 20.181  -0.074 1.00 63.50  ? 398 MET   A SD  1 
ATOM   2961 C CE  . MET   B 1 183 ? -24.017 20.359  -1.866 1.00 72.16  ? 398 MET   A CE  1 
ATOM   2962 N N   . MET   B 1 184 ? -27.706 20.261  4.536  1.00 69.11  ? 399 MET   A N   1 
ATOM   2963 C CA  . MET   B 1 184 ? -28.255 19.671  5.758  1.00 60.71  ? 399 MET   A CA  1 
ATOM   2964 C C   . MET   B 1 184 ? -29.767 19.791  5.779  1.00 55.22  ? 399 MET   A C   1 
ATOM   2965 O O   . MET   B 1 184 ? -30.457 18.850  6.178  1.00 57.51  ? 399 MET   A O   1 
ATOM   2966 C CB  . MET   B 1 184 ? -27.630 20.285  7.012  1.00 54.79  ? 399 MET   A CB  1 
ATOM   2967 C CG  . MET   B 1 184 ? -26.135 20.344  6.941  1.00 59.77  ? 399 MET   A CG  1 
ATOM   2968 S SD  . MET   B 1 184 ? -25.334 21.544  8.014  1.00 61.03  ? 399 MET   A SD  1 
ATOM   2969 C CE  . MET   B 1 184 ? -23.759 20.759  8.419  1.00 64.28  ? 399 MET   A CE  1 
ATOM   2970 N N   . ASN   B 1 185 ? -30.313 20.897  5.285  1.00 55.38  ? 400 ASN   A N   1 
ATOM   2971 C CA  . ASN   B 1 185 ? -31.769 21.008  5.318  1.00 60.31  ? 400 ASN   A CA  1 
ATOM   2972 C C   . ASN   B 1 185 ? -32.443 20.039  4.345  1.00 59.46  ? 400 ASN   A C   1 
ATOM   2973 O O   . ASN   B 1 185 ? -33.553 19.564  4.615  1.00 60.04  ? 400 ASN   A O   1 
ATOM   2974 C CB  . ASN   B 1 185 ? -32.202 22.452  5.058  1.00 62.30  ? 400 ASN   A CB  1 
ATOM   2975 C CG  . ASN   B 1 185 ? -31.954 23.365  6.265  1.00 60.49  ? 400 ASN   A CG  1 
ATOM   2976 O OD1 . ASN   B 1 185 ? -31.503 22.918  7.313  1.00 59.21  ? 400 ASN   A OD1 1 
ATOM   2977 N ND2 . ASN   B 1 185 ? -32.257 24.640  6.116  1.00 64.48  ? 400 ASN   A ND2 1 
ATOM   2978 N N   . SER   B 1 186 ? -31.787 19.722  3.224  1.00 63.72  ? 401 SER   A N   1 
ATOM   2979 C CA  . SER   B 1 186 ? -32.327 18.734  2.294  1.00 62.09  ? 401 SER   A CA  1 
ATOM   2980 C C   . SER   B 1 186 ? -32.383 17.355  2.935  1.00 61.14  ? 401 SER   A C   1 
ATOM   2981 O O   . SER   B 1 186 ? -33.385 16.636  2.804  1.00 60.62  ? 401 SER   A O   1 
ATOM   2982 C CB  . SER   B 1 186 ? -31.481 18.696  1.021  1.00 58.77  ? 401 SER   A CB  1 
ATOM   2983 O OG  . SER   B 1 186 ? -32.047 19.496  -0.011 1.00 62.11  ? 401 SER   A OG  1 
ATOM   2984 N N   . VAL   B 1 187 ? -31.304 16.968  3.623  1.00 59.13  ? 402 VAL   A N   1 
ATOM   2985 C CA  . VAL   B 1 187 ? -31.273 15.692  4.322  1.00 58.41  ? 402 VAL   A CA  1 
ATOM   2986 C C   . VAL   B 1 187 ? -32.334 15.669  5.408  1.00 62.82  ? 402 VAL   A C   1 
ATOM   2987 O O   . VAL   B 1 187 ? -33.077 14.688  5.548  1.00 62.06  ? 402 VAL   A O   1 
ATOM   2988 C CB  . VAL   B 1 187 ? -29.874 15.448  4.913  1.00 58.06  ? 402 VAL   A CB  1 
ATOM   2989 C CG1 . VAL   B 1 187 ? -29.825 14.104  5.622  1.00 59.19  ? 402 VAL   A CG1 1 
ATOM   2990 C CG2 . VAL   B 1 187 ? -28.798 15.572  3.845  1.00 61.82  ? 402 VAL   A CG2 1 
ATOM   2991 N N   . LEU   B 1 188 ? -32.437 16.767  6.182  1.00 63.82  ? 403 LEU   A N   1 
ATOM   2992 C CA  . LEU   B 1 188 ? -33.262 16.787  7.389  1.00 59.98  ? 403 LEU   A CA  1 
ATOM   2993 C C   . LEU   B 1 188 ? -34.744 16.865  7.073  1.00 62.03  ? 403 LEU   A C   1 
ATOM   2994 O O   . LEU   B 1 188 ? -35.555 16.353  7.852  1.00 62.91  ? 403 LEU   A O   1 
ATOM   2995 C CB  . LEU   B 1 188 ? -32.855 17.943  8.291  1.00 57.88  ? 403 LEU   A CB  1 
ATOM   2996 C CG  . LEU   B 1 188 ? -31.535 17.704  9.031  1.00 57.34  ? 403 LEU   A CG  1 
ATOM   2997 C CD1 . LEU   B 1 188 ? -31.096 18.968  9.711  1.00 59.51  ? 403 LEU   A CD1 1 
ATOM   2998 C CD2 . LEU   B 1 188 ? -31.667 16.615  10.039 1.00 55.15  ? 403 LEU   A CD2 1 
ATOM   2999 N N   . GLU   B 1 189 ? -35.116 17.469  5.940  1.00 65.55  ? 404 GLU   A N   1 
ATOM   3000 C CA  . GLU   B 1 189 ? -36.486 17.431  5.432  1.00 64.90  ? 404 GLU   A CA  1 
ATOM   3001 C C   . GLU   B 1 189 ? -37.175 16.079  5.677  1.00 67.00  ? 404 GLU   A C   1 
ATOM   3002 O O   . GLU   B 1 189 ? -38.380 16.045  5.914  1.00 70.58  ? 404 GLU   A O   1 
ATOM   3003 C CB  . GLU   B 1 189 ? -36.498 17.771  3.930  1.00 68.53  ? 404 GLU   A CB  1 
ATOM   3004 C CG  . GLU   B 1 189 ? -36.982 19.187  3.559  1.00 74.55  ? 404 GLU   A CG  1 
ATOM   3005 C CD  . GLU   B 1 189 ? -36.400 19.712  2.222  1.00 78.39  ? 404 GLU   A CD  1 
ATOM   3006 O OE1 . GLU   B 1 189 ? -36.403 18.950  1.228  1.00 79.16  ? 404 GLU   A OE1 1 
ATOM   3007 O OE2 . GLU   B 1 189 ? -35.998 20.905  2.136  1.00 81.05  ? 404 GLU   A OE2 1 
ATOM   3008 N N   . ASN   B 1 190 ? -36.438 14.960  5.645  1.00 67.44  ? 405 ASN   A N   1 
ATOM   3009 C CA  . ASN   B 1 190 ? -37.033 13.628  5.777  1.00 68.99  ? 405 ASN   A CA  1 
ATOM   3010 C C   . ASN   B 1 190 ? -36.947 13.049  7.185  1.00 69.45  ? 405 ASN   A C   1 
ATOM   3011 O O   . ASN   B 1 190 ? -37.627 12.057  7.477  1.00 73.60  ? 405 ASN   A O   1 
ATOM   3012 C CB  . ASN   B 1 190 ? -36.355 12.636  4.828  1.00 67.68  ? 405 ASN   A CB  1 
ATOM   3013 C CG  . ASN   B 1 190 ? -36.009 13.252  3.499  1.00 68.65  ? 405 ASN   A CG  1 
ATOM   3014 O OD1 . ASN   B 1 190 ? -36.853 13.353  2.612  1.00 72.62  ? 405 ASN   A OD1 1 
ATOM   3015 N ND2 . ASN   B 1 190 ? -34.762 13.683  3.353  1.00 67.84  ? 405 ASN   A ND2 1 
ATOM   3016 N N   . PHE   B 1 191 ? -36.140 13.632  8.053  1.00 62.15  ? 406 PHE   A N   1 
ATOM   3017 C CA  . PHE   B 1 191 ? -35.894 13.088  9.376  1.00 62.38  ? 406 PHE   A CA  1 
ATOM   3018 C C   . PHE   B 1 191 ? -36.763 13.833  10.402 1.00 64.59  ? 406 PHE   A C   1 
ATOM   3019 O O   . PHE   B 1 191 ? -36.695 15.062  10.502 1.00 66.82  ? 406 PHE   A O   1 
ATOM   3020 C CB  . PHE   B 1 191 ? -34.394 13.190  9.671  1.00 60.30  ? 406 PHE   A CB  1 
ATOM   3021 C CG  . PHE   B 1 191 ? -34.051 13.236  11.135 1.00 66.28  ? 406 PHE   A CG  1 
ATOM   3022 C CD1 . PHE   B 1 191 ? -34.069 14.442  11.851 1.00 64.88  ? 406 PHE   A CD1 1 
ATOM   3023 C CD2 . PHE   B 1 191 ? -33.697 12.074  11.805 1.00 68.68  ? 406 PHE   A CD2 1 
ATOM   3024 C CE1 . PHE   B 1 191 ? -33.753 14.477  13.197 1.00 58.52  ? 406 PHE   A CE1 1 
ATOM   3025 C CE2 . PHE   B 1 191 ? -33.381 12.106  13.157 1.00 66.35  ? 406 PHE   A CE2 1 
ATOM   3026 C CZ  . PHE   B 1 191 ? -33.407 13.309  13.847 1.00 63.22  ? 406 PHE   A CZ  1 
ATOM   3027 N N   . THR   B 1 192 ? -37.588 13.097  11.156 1.00 64.96  ? 407 THR   A N   1 
ATOM   3028 C CA  . THR   B 1 192 ? -38.483 13.696  12.147 1.00 64.56  ? 407 THR   A CA  1 
ATOM   3029 C C   . THR   B 1 192 ? -38.561 12.822  13.400 1.00 60.64  ? 407 THR   A C   1 
ATOM   3030 O O   . THR   B 1 192 ? -38.275 11.630  13.356 1.00 60.87  ? 407 THR   A O   1 
ATOM   3031 C CB  . THR   B 1 192 ? -39.907 13.896  11.593 1.00 67.57  ? 407 THR   A CB  1 
ATOM   3032 O OG1 . THR   B 1 192 ? -40.491 12.628  11.275 1.00 65.03  ? 407 THR   A OG1 1 
ATOM   3033 C CG2 . THR   B 1 192 ? -39.907 14.781  10.362 1.00 72.28  ? 407 THR   A CG2 1 
ATOM   3034 N N   . ILE   B 1 193 ? -38.986 13.424  14.522 1.00 57.39  ? 408 ILE   A N   1 
ATOM   3035 C CA  . ILE   B 1 193 ? -39.160 12.707  15.781 1.00 58.14  ? 408 ILE   A CA  1 
ATOM   3036 C C   . ILE   B 1 193 ? -40.597 12.868  16.247 1.00 57.42  ? 408 ILE   A C   1 
ATOM   3037 O O   . ILE   B 1 193 ? -41.258 13.852  15.920 1.00 58.23  ? 408 ILE   A O   1 
ATOM   3038 C CB  . ILE   B 1 193 ? -38.173 13.170  16.875 1.00 52.82  ? 408 ILE   A CB  1 
ATOM   3039 C CG1 . ILE   B 1 193 ? -36.764 13.231  16.287 1.00 53.45  ? 408 ILE   A CG1 1 
ATOM   3040 C CG2 . ILE   B 1 193 ? -38.208 12.201  18.068 1.00 52.84  ? 408 ILE   A CG2 1 
ATOM   3041 C CD1 . ILE   B 1 193 ? -35.626 13.092  17.263 1.00 50.65  ? 408 ILE   A CD1 1 
ATOM   3042 N N   . LEU   B 1 194 ? -41.096 11.866  16.978 1.00 59.11  ? 409 LEU   A N   1 
ATOM   3043 C CA  . LEU   B 1 194 ? -42.458 11.879  17.517 1.00 57.62  ? 409 LEU   A CA  1 
ATOM   3044 C C   . LEU   B 1 194 ? -42.385 11.392  18.954 1.00 55.59  ? 409 LEU   A C   1 
ATOM   3045 O O   . LEU   B 1 194 ? -42.077 10.226  19.192 1.00 58.21  ? 409 LEU   A O   1 
ATOM   3046 C CB  . LEU   B 1 194 ? -43.400 11.004  16.695 1.00 57.58  ? 409 LEU   A CB  1 
ATOM   3047 C CG  . LEU   B 1 194 ? -44.844 10.967  17.163 1.00 60.02  ? 409 LEU   A CG  1 
ATOM   3048 C CD1 . LEU   B 1 194 ? -45.265 12.364  17.487 1.00 57.53  ? 409 LEU   A CD1 1 
ATOM   3049 C CD2 . LEU   B 1 194 ? -45.732 10.387  16.084 1.00 73.72  ? 409 LEU   A CD2 1 
ATOM   3050 N N   . GLN   B 1 195 ? -42.654 12.285  19.905 1.00 58.63  ? 410 GLN   A N   1 
ATOM   3051 C CA  . GLN   B 1 195 ? -42.582 11.985  21.332 1.00 55.71  ? 410 GLN   A CA  1 
ATOM   3052 C C   . GLN   B 1 195 ? -43.977 11.845  21.916 1.00 53.63  ? 410 GLN   A C   1 
ATOM   3053 O O   . GLN   B 1 195 ? -44.833 12.699  21.692 1.00 57.28  ? 410 GLN   A O   1 
ATOM   3054 C CB  . GLN   B 1 195 ? -41.829 13.088  22.042 1.00 52.64  ? 410 GLN   A CB  1 
ATOM   3055 C CG  . GLN   B 1 195 ? -40.393 12.811  22.132 1.00 55.57  ? 410 GLN   A CG  1 
ATOM   3056 C CD  . GLN   B 1 195 ? -39.747 13.697  23.140 1.00 63.75  ? 410 GLN   A CD  1 
ATOM   3057 O OE1 . GLN   B 1 195 ? -38.535 13.706  23.278 1.00 74.55  ? 410 GLN   A OE1 1 
ATOM   3058 N NE2 . GLN   B 1 195 ? -40.548 14.495  23.827 1.00 67.06  ? 410 GLN   A NE2 1 
ATOM   3059 N N   . VAL   B 1 196 ? -44.219 10.766  22.643 1.00 57.81  ? 411 VAL   A N   1 
ATOM   3060 C CA  . VAL   B 1 196 ? -45.519 10.551  23.278 1.00 64.95  ? 411 VAL   A CA  1 
ATOM   3061 C C   . VAL   B 1 196 ? -45.312 10.270  24.759 1.00 63.23  ? 411 VAL   A C   1 
ATOM   3062 O O   . VAL   B 1 196 ? -44.739 9.235   25.120 1.00 63.49  ? 411 VAL   A O   1 
ATOM   3063 C CB  . VAL   B 1 196 ? -46.311 9.411   22.624 1.00 65.35  ? 411 VAL   A CB  1 
ATOM   3064 C CG1 . VAL   B 1 196 ? -47.646 9.212   23.362 1.00 65.13  ? 411 VAL   A CG1 1 
ATOM   3065 C CG2 . VAL   B 1 196 ? -46.555 9.730   21.164 1.00 66.11  ? 411 VAL   A CG2 1 
ATOM   3066 N N   . VAL   B 1 197 ? -45.795 11.174  25.616 1.00 66.68  ? 412 VAL   A N   1 
ATOM   3067 C CA  . VAL   B 1 197 ? -45.825 10.954  27.063 1.00 67.68  ? 412 VAL   A CA  1 
ATOM   3068 C C   . VAL   B 1 197 ? -47.222 10.532  27.473 1.00 63.65  ? 412 VAL   A C   1 
ATOM   3069 O O   . VAL   B 1 197 ? -48.215 11.160  27.090 1.00 63.41  ? 412 VAL   A O   1 
ATOM   3070 C CB  . VAL   B 1 197 ? -45.411 12.202  27.856 1.00 67.40  ? 412 VAL   A CB  1 
ATOM   3071 C CG1 . VAL   B 1 197 ? -45.160 11.785  29.300 1.00 68.08  ? 412 VAL   A CG1 1 
ATOM   3072 C CG2 . VAL   B 1 197 ? -44.181 12.868  27.260 1.00 63.44  ? 412 VAL   A CG2 1 
ATOM   3073 N N   . THR   B 1 198 ? -47.304 9.480   28.269 1.00 69.56  ? 413 THR   A N   1 
ATOM   3074 C CA  . THR   B 1 198 ? -48.587 9.018   28.771 1.00 70.53  ? 413 THR   A CA  1 
ATOM   3075 C C   . THR   B 1 198 ? -48.470 8.672   30.244 1.00 68.68  ? 413 THR   A C   1 
ATOM   3076 O O   . THR   B 1 198 ? -47.382 8.406   30.767 1.00 66.97  ? 413 THR   A O   1 
ATOM   3077 C CB  . THR   B 1 198 ? -49.081 7.789   28.027 1.00 65.35  ? 413 THR   A CB  1 
ATOM   3078 O OG1 . THR   B 1 198 ? -48.201 6.713   28.327 1.00 62.84  ? 413 THR   A OG1 1 
ATOM   3079 C CG2 . THR   B 1 198 ? -49.064 8.036   26.553 1.00 67.94  ? 413 THR   A CG2 1 
ATOM   3080 N N   . ASN   B 1 199 ? -49.624 8.694   30.902 1.00 70.58  ? 414 ASN   A N   1 
ATOM   3081 C CA  . ASN   B 1 199 ? -49.814 8.116   32.226 1.00 73.11  ? 414 ASN   A CA  1 
ATOM   3082 C C   . ASN   B 1 199 ? -49.516 6.630   32.167 1.00 69.90  ? 414 ASN   A C   1 
ATOM   3083 O O   . ASN   B 1 199 ? -50.279 5.889   31.541 1.00 73.19  ? 414 ASN   A O   1 
ATOM   3084 C CB  . ASN   B 1 199 ? -51.261 8.342   32.672 1.00 76.97  ? 414 ASN   A CB  1 
ATOM   3085 C CG  . ASN   B 1 199 ? -51.440 8.333   34.163 1.00 73.26  ? 414 ASN   A CG  1 
ATOM   3086 O OD1 . ASN   B 1 199 ? -50.718 7.668   34.906 1.00 73.36  ? 414 ASN   A OD1 1 
ATOM   3087 N ND2 . ASN   B 1 199 ? -52.408 9.104   34.614 1.00 72.37  ? 414 ASN   A ND2 1 
ATOM   3088 N N   . ARG   B 1 200 ? -48.423 6.181   32.790 1.00 68.60  ? 415 ARG   A N   1 
ATOM   3089 C CA  . ARG   B 1 200 ? -48.142 4.743   32.820 1.00 74.52  ? 415 ARG   A CA  1 
ATOM   3090 C C   . ARG   B 1 200 ? -49.345 3.960   33.326 1.00 74.24  ? 415 ARG   A C   1 
ATOM   3091 O O   . ARG   B 1 200 ? -49.814 3.031   32.665 1.00 73.68  ? 415 ARG   A O   1 
ATOM   3092 C CB  . ARG   B 1 200 ? -46.913 4.436   33.687 1.00 71.42  ? 415 ARG   A CB  1 
ATOM   3093 C CG  . ARG   B 1 200 ? -46.360 2.999   33.542 1.00 65.10  ? 415 ARG   A CG  1 
ATOM   3094 C CD  . ARG   B 1 200 ? -46.899 2.047   34.621 1.00 78.38  ? 415 ARG   A CD  1 
ATOM   3095 N NE  . ARG   B 1 200 ? -46.355 2.305   35.954 1.00 79.67  ? 415 ARG   A NE  1 
ATOM   3096 C CZ  . ARG   B 1 200 ? -45.171 1.879   36.384 1.00 80.93  ? 415 ARG   A CZ  1 
ATOM   3097 N NH1 . ARG   B 1 200 ? -44.404 1.090   35.642 1.00 80.39  ? 415 ARG   A NH1 1 
ATOM   3098 N NH2 . ARG   B 1 200 ? -44.743 2.256   37.587 1.00 81.04  ? 415 ARG   A NH2 1 
ATOM   3099 N N   . ASP   B 1 201 ? -49.878 4.356   34.487 1.00 82.09  ? 416 ASP   A N   1 
ATOM   3100 C CA  . ASP   B 1 201 ? -50.869 3.570   35.219 1.00 82.83  ? 416 ASP   A CA  1 
ATOM   3101 C C   . ASP   B 1 201 ? -52.243 3.578   34.568 1.00 81.10  ? 416 ASP   A C   1 
ATOM   3102 O O   . ASP   B 1 201 ? -53.091 2.769   34.950 1.00 81.80  ? 416 ASP   A O   1 
ATOM   3103 C CB  . ASP   B 1 201 ? -50.993 4.074   36.666 1.00 82.41  ? 416 ASP   A CB  1 
ATOM   3104 C CG  . ASP   B 1 201 ? -49.687 3.966   37.435 1.00 84.54  ? 416 ASP   A CG  1 
ATOM   3105 O OD1 . ASP   B 1 201 ? -48.898 3.043   37.135 1.00 84.35  ? 416 ASP   A OD1 1 
ATOM   3106 O OD2 . ASP   B 1 201 ? -49.442 4.807   38.329 1.00 85.25  ? 416 ASP   A OD2 1 
ATOM   3107 N N   . THR   B 1 202 ? -52.502 4.467   33.619 1.00 79.86  ? 417 THR   A N   1 
ATOM   3108 C CA  . THR   B 1 202 ? -53.822 4.525   33.026 1.00 81.57  ? 417 THR   A CA  1 
ATOM   3109 C C   . THR   B 1 202 ? -53.819 4.461   31.504 1.00 83.22  ? 417 THR   A C   1 
ATOM   3110 O O   . THR   B 1 202 ? -54.898 4.432   30.905 1.00 82.86  ? 417 THR   A O   1 
ATOM   3111 C CB  . THR   B 1 202 ? -54.554 5.788   33.496 1.00 82.00  ? 417 THR   A CB  1 
ATOM   3112 O OG1 . THR   B 1 202 ? -54.208 6.886   32.645 1.00 85.05  ? 417 THR   A OG1 1 
ATOM   3113 C CG2 . THR   B 1 202 ? -54.174 6.131   34.928 1.00 82.05  ? 417 THR   A CG2 1 
ATOM   3114 N N   . GLN   B 1 203 ? -52.652 4.422   30.863 1.00 86.81  ? 418 GLN   A N   1 
ATOM   3115 C CA  . GLN   B 1 203 ? -52.506 4.315   29.409 1.00 89.98  ? 418 GLN   A CA  1 
ATOM   3116 C C   . GLN   B 1 203 ? -52.982 5.552   28.655 1.00 88.63  ? 418 GLN   A C   1 
ATOM   3117 O O   . GLN   B 1 203 ? -52.998 5.538   27.415 1.00 89.66  ? 418 GLN   A O   1 
ATOM   3118 C CB  . GLN   B 1 203 ? -53.239 3.090   28.839 1.00 88.88  ? 418 GLN   A CB  1 
ATOM   3119 C CG  . GLN   B 1 203 ? -52.709 1.702   29.199 1.00 93.50  ? 418 GLN   A CG  1 
ATOM   3120 C CD  . GLN   B 1 203 ? -51.193 1.540   29.190 1.00 97.07  ? 418 GLN   A CD  1 
ATOM   3121 O OE1 . GLN   B 1 203 ? -50.425 2.488   29.005 1.00 95.89  ? 418 GLN   A OE1 1 
ATOM   3122 N NE2 . GLN   B 1 203 ? -50.759 0.298   29.374 1.00 99.59  ? 418 GLN   A NE2 1 
ATOM   3123 N N   . GLU   B 1 204 ? -53.371 6.615   29.357 1.00 82.43  ? 419 GLU   A N   1 
ATOM   3124 C CA  . GLU   B 1 204 ? -53.919 7.800   28.721 1.00 84.12  ? 419 GLU   A CA  1 
ATOM   3125 C C   . GLU   B 1 204 ? -52.798 8.769   28.381 1.00 82.76  ? 419 GLU   A C   1 
ATOM   3126 O O   . GLU   B 1 204 ? -51.802 8.874   29.105 1.00 79.37  ? 419 GLU   A O   1 
ATOM   3127 C CB  . GLU   B 1 204 ? -54.967 8.476   29.617 1.00 86.18  ? 419 GLU   A CB  1 
ATOM   3128 C CG  . GLU   B 1 204 ? -54.434 9.346   30.752 1.00 85.60  ? 419 GLU   A CG  1 
ATOM   3129 C CD  . GLU   B 1 204 ? -55.470 9.593   31.858 1.00 88.06  ? 419 GLU   A CD  1 
ATOM   3130 O OE1 . GLU   B 1 204 ? -56.621 10.003  31.557 1.00 88.16  ? 419 GLU   A OE1 1 
ATOM   3131 O OE2 . GLU   B 1 204 ? -55.121 9.366   33.041 1.00 88.64  ? 419 GLU   A OE2 1 
ATOM   3132 N N   . LEU   B 1 205 ? -52.972 9.469   27.256 1.00 74.55  ? 420 LEU   A N   1 
ATOM   3133 C CA  . LEU   B 1 205 ? -51.925 10.307  26.689 1.00 70.65  ? 420 LEU   A CA  1 
ATOM   3134 C C   . LEU   B 1 205 ? -51.861 11.651  27.405 1.00 68.63  ? 420 LEU   A C   1 
ATOM   3135 O O   . LEU   B 1 205 ? -52.874 12.334  27.561 1.00 66.32  ? 420 LEU   A O   1 
ATOM   3136 C CB  . LEU   B 1 205 ? -52.183 10.506  25.196 1.00 72.18  ? 420 LEU   A CB  1 
ATOM   3137 C CG  . LEU   B 1 205 ? -51.166 11.214  24.304 1.00 65.96  ? 420 LEU   A CG  1 
ATOM   3138 C CD1 . LEU   B 1 205 ? -51.394 10.791  22.875 1.00 69.94  ? 420 LEU   A CD1 1 
ATOM   3139 C CD2 . LEU   B 1 205 ? -51.285 12.712  24.421 1.00 65.21  ? 420 LEU   A CD2 1 
ATOM   3140 N N   . LEU   B 1 206 ? -50.659 12.046  27.806 1.00 65.07  ? 421 LEU   A N   1 
ATOM   3141 C CA  . LEU   B 1 206 ? -50.458 13.331  28.452 1.00 64.33  ? 421 LEU   A CA  1 
ATOM   3142 C C   . LEU   B 1 206 ? -49.886 14.382  27.512 1.00 68.53  ? 421 LEU   A C   1 
ATOM   3143 O O   . LEU   B 1 206 ? -50.296 15.550  27.582 1.00 65.92  ? 421 LEU   A O   1 
ATOM   3144 C CB  . LEU   B 1 206 ? -49.542 13.166  29.670 1.00 63.99  ? 421 LEU   A CB  1 
ATOM   3145 C CG  . LEU   B 1 206 ? -49.999 12.120  30.691 1.00 64.54  ? 421 LEU   A CG  1 
ATOM   3146 C CD1 . LEU   B 1 206 ? -49.016 12.042  31.827 1.00 62.31  ? 421 LEU   A CD1 1 
ATOM   3147 C CD2 . LEU   B 1 206 ? -51.387 12.456  31.213 1.00 66.28  ? 421 LEU   A CD2 1 
ATOM   3148 N N   . LEU   B 1 207 ? -48.952 13.988  26.636 1.00 66.64  ? 422 LEU   A N   1 
ATOM   3149 C CA  . LEU   B 1 207 ? -48.299 14.875  25.678 1.00 64.52  ? 422 LEU   A CA  1 
ATOM   3150 C C   . LEU   B 1 207 ? -47.896 14.101  24.439 1.00 63.50  ? 422 LEU   A C   1 
ATOM   3151 O O   . LEU   B 1 207 ? -47.355 12.995  24.527 1.00 65.05  ? 422 LEU   A O   1 
ATOM   3152 C CB  . LEU   B 1 207 ? -47.017 15.524  26.218 1.00 63.80  ? 422 LEU   A CB  1 
ATOM   3153 C CG  . LEU   B 1 207 ? -46.960 16.660  27.216 1.00 61.96  ? 422 LEU   A CG  1 
ATOM   3154 C CD1 . LEU   B 1 207 ? -45.597 17.302  27.130 1.00 60.31  ? 422 LEU   A CD1 1 
ATOM   3155 C CD2 . LEU   B 1 207 ? -48.023 17.641  26.859 1.00 68.66  ? 422 LEU   A CD2 1 
ATOM   3156 N N   . CYS   B 1 208 ? -48.088 14.724  23.290 1.00 63.49  ? 423 CYS   A N   1 
ATOM   3157 C CA  . CYS   B 1 208 ? -47.570 14.189  22.038 1.00 60.49  ? 423 CYS   A CA  1 
ATOM   3158 C C   . CYS   B 1 208 ? -46.978 15.341  21.237 1.00 55.59  ? 423 CYS   A C   1 
ATOM   3159 O O   . CYS   B 1 208 ? -47.731 16.143  20.680 1.00 59.21  ? 423 CYS   A O   1 
ATOM   3160 C CB  . CYS   B 1 208 ? -48.666 13.487  21.261 1.00 62.68  ? 423 CYS   A CB  1 
ATOM   3161 S SG  . CYS   B 1 208 ? -48.074 12.879  19.705 1.00 65.70  ? 423 CYS   A SG  1 
ATOM   3162 N N   . THR   B 1 209 ? -45.645 15.406  21.169 1.00 55.99  ? 424 THR   A N   1 
ATOM   3163 C CA  . THR   B 1 209 ? -44.926 16.421  20.396 1.00 59.22  ? 424 THR   A CA  1 
ATOM   3164 C C   . THR   B 1 209 ? -44.327 15.848  19.117 1.00 57.06  ? 424 THR   A C   1 
ATOM   3165 O O   . THR   B 1 209 ? -43.644 14.812  19.146 1.00 53.09  ? 424 THR   A O   1 
ATOM   3166 C CB  . THR   B 1 209 ? -43.804 17.051  21.214 1.00 57.32  ? 424 THR   A CB  1 
ATOM   3167 O OG1 . THR   B 1 209 ? -44.286 17.330  22.527 1.00 66.55  ? 424 THR   A OG1 1 
ATOM   3168 C CG2 . THR   B 1 209 ? -43.329 18.329  20.565 1.00 57.90  ? 424 THR   A CG2 1 
ATOM   3169 N N   . ALA   B 1 210 ? -44.566 16.548  18.005 1.00 61.70  ? 425 ALA   A N   1 
ATOM   3170 C CA  . ALA   B 1 210 ? -43.934 16.283  16.715 1.00 55.04  ? 425 ALA   A CA  1 
ATOM   3171 C C   . ALA   B 1 210 ? -42.783 17.255  16.530 1.00 54.23  ? 425 ALA   A C   1 
ATOM   3172 O O   . ALA   B 1 210 ? -42.970 18.466  16.677 1.00 59.53  ? 425 ALA   A O   1 
ATOM   3173 C CB  . ALA   B 1 210 ? -44.940 16.441  15.576 1.00 50.00  ? 425 ALA   A CB  1 
ATOM   3174 N N   . TYR   B 1 211 ? -41.601 16.738  16.206 1.00 53.69  ? 426 TYR   A N   1 
ATOM   3175 C CA  . TYR   B 1 211 ? -40.430 17.575  15.959 1.00 56.35  ? 426 TYR   A CA  1 
ATOM   3176 C C   . TYR   B 1 211 ? -40.004 17.532  14.490 1.00 60.07  ? 426 TYR   A C   1 
ATOM   3177 O O   . TYR   B 1 211 ? -39.833 16.449  13.917 1.00 59.15  ? 426 TYR   A O   1 
ATOM   3178 C CB  . TYR   B 1 211 ? -39.245 17.169  16.839 1.00 54.84  ? 426 TYR   A CB  1 
ATOM   3179 C CG  . TYR   B 1 211 ? -39.524 17.201  18.327 1.00 60.03  ? 426 TYR   A CG  1 
ATOM   3180 C CD1 . TYR   B 1 211 ? -38.872 18.114  19.146 1.00 62.36  ? 426 TYR   A CD1 1 
ATOM   3181 C CD2 . TYR   B 1 211 ? -40.349 16.256  18.938 1.00 62.40  ? 426 TYR   A CD2 1 
ATOM   3182 C CE1 . TYR   B 1 211 ? -39.085 18.148  20.529 1.00 64.40  ? 426 TYR   A CE1 1 
ATOM   3183 C CE2 . TYR   B 1 211 ? -40.567 16.270  20.327 1.00 65.38  ? 426 TYR   A CE2 1 
ATOM   3184 C CZ  . TYR   B 1 211 ? -39.936 17.227  21.121 1.00 64.27  ? 426 TYR   A CZ  1 
ATOM   3185 O OH  . TYR   B 1 211 ? -40.142 17.237  22.492 1.00 59.77  ? 426 TYR   A OH  1 
ATOM   3186 N N   . VAL   B 1 212 ? -39.798 18.712  13.893 1.00 60.98  ? 427 VAL   A N   1 
ATOM   3187 C CA  . VAL   B 1 212 ? -39.197 18.845  12.568 1.00 61.66  ? 427 VAL   A CA  1 
ATOM   3188 C C   . VAL   B 1 212 ? -37.937 19.690  12.680 1.00 62.87  ? 427 VAL   A C   1 
ATOM   3189 O O   . VAL   B 1 212 ? -37.781 20.496  13.600 1.00 60.54  ? 427 VAL   A O   1 
ATOM   3190 C CB  . VAL   B 1 212 ? -40.139 19.471  11.534 1.00 56.61  ? 427 VAL   A CB  1 
ATOM   3191 C CG1 . VAL   B 1 212 ? -41.144 18.445  11.024 1.00 54.23  ? 427 VAL   A CG1 1 
ATOM   3192 C CG2 . VAL   B 1 212 ? -40.772 20.711  12.107 1.00 57.15  ? 427 VAL   A CG2 1 
ATOM   3193 N N   . PHE   B 1 213 ? -37.048 19.533  11.688 1.00 64.46  ? 428 PHE   A N   1 
ATOM   3194 C CA  . PHE   B 1 213 ? -35.702 20.074  11.815 1.00 64.88  ? 428 PHE   A CA  1 
ATOM   3195 C C   . PHE   B 1 213 ? -35.198 20.845  10.597 1.00 66.74  ? 428 PHE   A C   1 
ATOM   3196 O O   . PHE   B 1 213 ? -35.444 20.481  9.444  1.00 68.72  ? 428 PHE   A O   1 
ATOM   3197 C CB  . PHE   B 1 213 ? -34.736 18.954  12.127 1.00 62.05  ? 428 PHE   A CB  1 
ATOM   3198 C CG  . PHE   B 1 213 ? -35.071 18.234  13.384 1.00 60.66  ? 428 PHE   A CG  1 
ATOM   3199 C CD1 . PHE   B 1 213 ? -36.021 17.226  13.387 1.00 61.77  ? 428 PHE   A CD1 1 
ATOM   3200 C CD2 . PHE   B 1 213 ? -34.441 18.559  14.564 1.00 59.74  ? 428 PHE   A CD2 1 
ATOM   3201 C CE1 . PHE   B 1 213 ? -36.326 16.558  14.531 1.00 59.47  ? 428 PHE   A CE1 1 
ATOM   3202 C CE2 . PHE   B 1 213 ? -34.737 17.885  15.714 1.00 59.21  ? 428 PHE   A CE2 1 
ATOM   3203 C CZ  . PHE   B 1 213 ? -35.679 16.881  15.697 1.00 59.97  ? 428 PHE   A CZ  1 
ATOM   3204 N N   . GLU   B 1 214 ? -34.502 21.935  10.887 1.00 62.34  ? 429 GLU   A N   1 
ATOM   3205 C CA  . GLU   B 1 214 ? -33.509 22.527  10.013 1.00 60.66  ? 429 GLU   A CA  1 
ATOM   3206 C C   . GLU   B 1 214 ? -32.270 22.773  10.863 1.00 62.60  ? 429 GLU   A C   1 
ATOM   3207 O O   . GLU   B 1 214 ? -32.268 22.516  12.071 1.00 65.47  ? 429 GLU   A O   1 
ATOM   3208 C CB  . GLU   B 1 214 ? -34.012 23.826  9.376  1.00 60.76  ? 429 GLU   A CB  1 
ATOM   3209 C CG  . GLU   B 1 214 ? -35.359 23.711  8.715  1.00 61.99  ? 429 GLU   A CG  1 
ATOM   3210 C CD  . GLU   B 1 214 ? -35.637 24.876  7.795  1.00 66.87  ? 429 GLU   A CD  1 
ATOM   3211 O OE1 . GLU   B 1 214 ? -34.825 25.836  7.768  1.00 64.38  ? 429 GLU   A OE1 1 
ATOM   3212 O OE2 . GLU   B 1 214 ? -36.658 24.817  7.078  1.00 72.94  ? 429 GLU   A OE2 1 
ATOM   3213 N N   . VAL   B 1 215 ? -31.207 23.271  10.244 1.00 63.92  ? 430 VAL   A N   1 
ATOM   3214 C CA  . VAL   B 1 215 ? -30.022 23.683  10.978 1.00 65.33  ? 430 VAL   A CA  1 
ATOM   3215 C C   . VAL   B 1 215 ? -30.009 25.201  10.979 1.00 68.45  ? 430 VAL   A C   1 
ATOM   3216 O O   . VAL   B 1 215 ? -30.461 25.842  10.022 1.00 70.08  ? 430 VAL   A O   1 
ATOM   3217 C CB  . VAL   B 1 215 ? -28.721 23.132  10.362 1.00 65.64  ? 430 VAL   A CB  1 
ATOM   3218 C CG1 . VAL   B 1 215 ? -28.800 21.615  10.228 1.00 58.31  ? 430 VAL   A CG1 1 
ATOM   3219 C CG2 . VAL   B 1 215 ? -28.434 23.815  9.056  1.00 71.14  ? 430 VAL   A CG2 1 
ATOM   3220 N N   . SER   B 1 216 ? -29.526 25.781  12.072 1.00 68.57  ? 431 SER   A N   1 
ATOM   3221 C CA  . SER   B 1 216 ? -29.404 27.223  12.157 1.00 72.86  ? 431 SER   A CA  1 
ATOM   3222 C C   . SER   B 1 216 ? -27.988 27.626  11.802 1.00 81.22  ? 431 SER   A C   1 
ATOM   3223 O O   . SER   B 1 216 ? -27.057 26.814  11.821 1.00 82.73  ? 431 SER   A O   1 
ATOM   3224 C CB  . SER   B 1 216 ? -29.751 27.762  13.544 1.00 73.85  ? 431 SER   A CB  1 
ATOM   3225 O OG  . SER   B 1 216 ? -29.133 29.036  13.729 1.00 78.33  ? 431 SER   A OG  1 
ATOM   3226 N N   . THR   B 1 217 ? -27.843 28.907  11.482 1.00 86.66  ? 432 THR   A N   1 
ATOM   3227 C CA  . THR   B 1 217 ? -26.573 29.425  11.028 1.00 95.34  ? 432 THR   A CA  1 
ATOM   3228 C C   . THR   B 1 217 ? -25.574 29.412  12.182 1.00 102.51 ? 432 THR   A C   1 
ATOM   3229 O O   . THR   B 1 217 ? -25.925 29.239  13.355 1.00 93.87  ? 432 THR   A O   1 
ATOM   3230 C CB  . THR   B 1 217 ? -26.755 30.827  10.450 1.00 92.38  ? 432 THR   A CB  1 
ATOM   3231 O OG1 . THR   B 1 217 ? -26.392 31.801  11.434 1.00 98.39  ? 432 THR   A OG1 1 
ATOM   3232 C CG2 . THR   B 1 217 ? -28.223 31.038  10.063 1.00 83.64  ? 432 THR   A CG2 1 
ATOM   3233 N N   . SER   B 1 218 ? -24.303 29.584  11.823 1.00 126.66 ? 433 SER   A N   1 
ATOM   3234 C CA  . SER   B 1 218 ? -23.222 29.377  12.780 1.00 127.48 ? 433 SER   A CA  1 
ATOM   3235 C C   . SER   B 1 218 ? -23.334 30.333  13.964 1.00 126.86 ? 433 SER   A C   1 
ATOM   3236 O O   . SER   B 1 218 ? -23.270 29.911  15.126 1.00 125.20 ? 433 SER   A O   1 
ATOM   3237 C CB  . SER   B 1 218 ? -21.883 29.537  12.064 1.00 126.77 ? 433 SER   A CB  1 
ATOM   3238 O OG  . SER   B 1 218 ? -21.941 28.915  10.788 1.00 130.78 ? 433 SER   A OG  1 
ATOM   3239 N N   . GLU   B 1 219 ? -23.523 31.629  13.683 1.00 127.36 ? 434 GLU   A N   1 
ATOM   3240 C CA  . GLU   B 1 219 ? -23.543 32.646  14.734 1.00 124.21 ? 434 GLU   A CA  1 
ATOM   3241 C C   . GLU   B 1 219 ? -24.926 32.849  15.338 1.00 123.90 ? 434 GLU   A C   1 
ATOM   3242 O O   . GLU   B 1 219 ? -25.033 33.152  16.531 1.00 119.32 ? 434 GLU   A O   1 
ATOM   3243 C CB  . GLU   B 1 219 ? -23.037 33.983  14.190 1.00 125.58 ? 434 GLU   A CB  1 
ATOM   3244 C CG  . GLU   B 1 219 ? -23.905 34.599  13.094 1.00 124.64 ? 434 GLU   A CG  1 
ATOM   3245 C CD  . GLU   B 1 219 ? -23.937 36.116  13.147 1.00 131.72 ? 434 GLU   A CD  1 
ATOM   3246 O OE1 . GLU   B 1 219 ? -23.998 36.670  14.262 1.00 131.22 ? 434 GLU   A OE1 1 
ATOM   3247 O OE2 . GLU   B 1 219 ? -23.896 36.762  12.077 1.00 135.78 ? 434 GLU   A OE2 1 
ATOM   3248 N N   . ARG   B 1 220 ? -25.982 32.690  14.536 1.00 107.82 ? 435 ARG   A N   1 
ATOM   3249 C CA  . ARG   B 1 220 ? -27.353 33.022  14.908 1.00 93.74  ? 435 ARG   A CA  1 
ATOM   3250 C C   . ARG   B 1 220 ? -27.953 32.054  15.925 1.00 87.41  ? 435 ARG   A C   1 
ATOM   3251 O O   . ARG   B 1 220 ? -28.974 32.379  16.537 1.00 89.25  ? 435 ARG   A O   1 
ATOM   3252 C CB  . ARG   B 1 220 ? -28.204 33.078  13.637 1.00 87.87  ? 435 ARG   A CB  1 
ATOM   3253 C CG  . ARG   B 1 220 ? -29.642 33.429  13.831 1.00 83.02  ? 435 ARG   A CG  1 
ATOM   3254 C CD  . ARG   B 1 220 ? -30.348 33.685  12.512 1.00 83.80  ? 435 ARG   A CD  1 
ATOM   3255 N NE  . ARG   B 1 220 ? -31.768 33.923  12.754 1.00 86.76  ? 435 ARG   A NE  1 
ATOM   3256 C CZ  . ARG   B 1 220 ? -32.702 34.055  11.818 1.00 87.09  ? 435 ARG   A CZ  1 
ATOM   3257 N NH1 . ARG   B 1 220 ? -32.399 34.043  10.517 1.00 78.97  ? 435 ARG   A NH1 1 
ATOM   3258 N NH2 . ARG   B 1 220 ? -33.973 34.200  12.196 1.00 84.58  ? 435 ARG   A NH2 1 
ATOM   3259 N N   . GLY   B 1 221 ? -27.362 30.887  16.131 1.00 88.87  ? 436 GLY   A N   1 
ATOM   3260 C CA  . GLY   B 1 221 ? -27.683 30.094  17.300 1.00 79.76  ? 436 GLY   A CA  1 
ATOM   3261 C C   . GLY   B 1 221 ? -28.985 29.315  17.187 1.00 74.75  ? 436 GLY   A C   1 
ATOM   3262 O O   . GLY   B 1 221 ? -29.862 29.603  16.371 1.00 73.46  ? 436 GLY   A O   1 
ATOM   3263 N N   . ALA   B 1 222 ? -29.101 28.316  18.070 1.00 73.27  ? 437 ALA   A N   1 
ATOM   3264 C CA  . ALA   B 1 222 ? -30.245 27.412  18.121 1.00 67.19  ? 437 ALA   A CA  1 
ATOM   3265 C C   . ALA   B 1 222 ? -31.548 28.169  18.375 1.00 67.13  ? 437 ALA   A C   1 
ATOM   3266 O O   . ALA   B 1 222 ? -31.563 29.215  19.033 1.00 68.26  ? 437 ALA   A O   1 
ATOM   3267 C CB  . ALA   B 1 222 ? -30.019 26.364  19.207 1.00 61.05  ? 437 ALA   A CB  1 
ATOM   3268 N N   . GLN   B 1 223 ? -32.649 27.635  17.830 1.00 68.95  ? 438 GLN   A N   1 
ATOM   3269 C CA  . GLN   B 1 223 ? -33.952 28.299  17.873 1.00 74.04  ? 438 GLN   A CA  1 
ATOM   3270 C C   . GLN   B 1 223 ? -35.059 27.274  17.676 1.00 70.73  ? 438 GLN   A C   1 
ATOM   3271 O O   . GLN   B 1 223 ? -34.854 26.237  17.051 1.00 72.17  ? 438 GLN   A O   1 
ATOM   3272 C CB  . GLN   B 1 223 ? -34.074 29.423  16.816 1.00 78.57  ? 438 GLN   A CB  1 
ATOM   3273 C CG  . GLN   B 1 223 ? -35.477 30.087  16.800 1.00 83.44  ? 438 GLN   A CG  1 
ATOM   3274 C CD  . GLN   B 1 223 ? -35.518 31.540  16.374 1.00 84.30  ? 438 GLN   A CD  1 
ATOM   3275 O OE1 . GLN   B 1 223 ? -35.107 31.890  15.276 1.00 84.58  ? 438 GLN   A OE1 1 
ATOM   3276 N NE2 . GLN   B 1 223 ? -36.027 32.397  17.254 1.00 87.99  ? 438 GLN   A NE2 1 
ATOM   3277 N N   . HIS   B 1 224 ? -36.239 27.575  18.221 1.00 67.13  ? 439 HIS   A N   1 
ATOM   3278 C CA  . HIS   B 1 224 ? -37.419 26.742  18.032 1.00 69.11  ? 439 HIS   A CA  1 
ATOM   3279 C C   . HIS   B 1 224 ? -38.647 27.629  17.896 1.00 66.71  ? 439 HIS   A C   1 
ATOM   3280 O O   . HIS   B 1 224 ? -38.591 28.841  18.103 1.00 70.38  ? 439 HIS   A O   1 
ATOM   3281 C CB  . HIS   B 1 224 ? -37.595 25.736  19.178 1.00 68.55  ? 439 HIS   A CB  1 
ATOM   3282 C CG  . HIS   B 1 224 ? -37.665 26.375  20.525 1.00 70.60  ? 439 HIS   A CG  1 
ATOM   3283 N ND1 . HIS   B 1 224 ? -38.858 26.685  21.145 1.00 69.53  ? 439 HIS   A ND1 1 
ATOM   3284 C CD2 . HIS   B 1 224 ? -36.685 26.804  21.354 1.00 70.65  ? 439 HIS   A CD2 1 
ATOM   3285 C CE1 . HIS   B 1 224 ? -38.608 27.261  22.308 1.00 70.09  ? 439 HIS   A CE1 1 
ATOM   3286 N NE2 . HIS   B 1 224 ? -37.298 27.353  22.456 1.00 71.16  ? 439 HIS   A NE2 1 
ATOM   3287 N N   . HIS   B 1 225 ? -39.759 27.006  17.519 1.00 64.63  ? 440 HIS   A N   1 
ATOM   3288 C CA  . HIS   B 1 225 ? -41.043 27.693  17.384 1.00 71.74  ? 440 HIS   A CA  1 
ATOM   3289 C C   . HIS   B 1 225 ? -42.081 26.622  17.691 1.00 71.34  ? 440 HIS   A C   1 
ATOM   3290 O O   . HIS   B 1 225 ? -42.163 25.619  16.970 1.00 65.14  ? 440 HIS   A O   1 
ATOM   3291 C CB  . HIS   B 1 225 ? -41.212 28.293  15.982 1.00 74.38  ? 440 HIS   A CB  1 
ATOM   3292 C CG  . HIS   B 1 225 ? -42.202 29.419  15.884 1.00 78.09  ? 440 HIS   A CG  1 
ATOM   3293 N ND1 . HIS   B 1 225 ? -43.229 29.423  14.965 1.00 82.47  ? 440 HIS   A ND1 1 
ATOM   3294 C CD2 . HIS   B 1 225 ? -42.287 30.604  16.537 1.00 86.87  ? 440 HIS   A CD2 1 
ATOM   3295 C CE1 . HIS   B 1 225 ? -43.928 30.539  15.076 1.00 87.97  ? 440 HIS   A CE1 1 
ATOM   3296 N NE2 . HIS   B 1 225 ? -43.377 31.275  16.023 1.00 92.91  ? 440 HIS   A NE2 1 
ATOM   3297 N N   . ILE   B 1 226 ? -42.819 26.796  18.806 1.00 74.00  ? 441 ILE   A N   1 
ATOM   3298 C CA  . ILE   B 1 226 ? -43.744 25.779  19.301 1.00 69.26  ? 441 ILE   A CA  1 
ATOM   3299 C C   . ILE   B 1 226 ? -45.141 26.121  18.822 1.00 70.59  ? 441 ILE   A C   1 
ATOM   3300 O O   . ILE   B 1 226 ? -45.543 27.292  18.846 1.00 74.01  ? 441 ILE   A O   1 
ATOM   3301 C CB  . ILE   B 1 226 ? -43.685 25.667  20.834 1.00 63.78  ? 441 ILE   A CB  1 
ATOM   3302 C CG1 . ILE   B 1 226 ? -42.245 25.431  21.283 1.00 64.07  ? 441 ILE   A CG1 1 
ATOM   3303 C CG2 . ILE   B 1 226 ? -44.580 24.562  21.323 1.00 63.85  ? 441 ILE   A CG2 1 
ATOM   3304 C CD1 . ILE   B 1 226 ? -42.081 25.236  22.747 1.00 63.47  ? 441 ILE   A CD1 1 
ATOM   3305 N N   . TYR   B 1 227 ? -45.868 25.113  18.342 1.00 68.53  ? 442 TYR   A N   1 
ATOM   3306 C CA  . TYR   B 1 227 ? -47.213 25.320  17.825 1.00 73.82  ? 442 TYR   A CA  1 
ATOM   3307 C C   . TYR   B 1 227 ? -48.168 24.274  18.381 1.00 74.37  ? 442 TYR   A C   1 
ATOM   3308 O O   . TYR   B 1 227 ? -47.768 23.188  18.806 1.00 69.22  ? 442 TYR   A O   1 
ATOM   3309 C CB  . TYR   B 1 227 ? -47.322 25.218  16.293 1.00 78.19  ? 442 TYR   A CB  1 
ATOM   3310 C CG  . TYR   B 1 227 ? -46.339 25.954  15.412 1.00 76.89  ? 442 TYR   A CG  1 
ATOM   3311 C CD1 . TYR   B 1 227 ? -45.004 25.590  15.363 1.00 73.00  ? 442 TYR   A CD1 1 
ATOM   3312 C CD2 . TYR   B 1 227 ? -46.775 26.965  14.567 1.00 82.05  ? 442 TYR   A CD2 1 
ATOM   3313 C CE1 . TYR   B 1 227 ? -44.113 26.243  14.521 1.00 79.11  ? 442 TYR   A CE1 1 
ATOM   3314 C CE2 . TYR   B 1 227 ? -45.900 27.622  13.723 1.00 87.82  ? 442 TYR   A CE2 1 
ATOM   3315 C CZ  . TYR   B 1 227 ? -44.568 27.252  13.692 1.00 85.08  ? 442 TYR   A CZ  1 
ATOM   3316 O OH  . TYR   B 1 227 ? -43.695 27.921  12.849 1.00 88.12  ? 442 TYR   A OH  1 
ATOM   3317 N N   . ARG   B 1 228 ? -49.449 24.605  18.307 1.00 83.62  ? 443 ARG   A N   1 
ATOM   3318 C CA  . ARG   B 1 228 ? -50.521 23.661  18.560 1.00 84.86  ? 443 ARG   A CA  1 
ATOM   3319 C C   . ARG   B 1 228 ? -50.925 23.015  17.245 1.00 85.56  ? 443 ARG   A C   1 
ATOM   3320 O O   . ARG   B 1 228 ? -51.138 23.720  16.259 1.00 88.85  ? 443 ARG   A O   1 
ATOM   3321 C CB  . ARG   B 1 228 ? -51.723 24.385  19.167 1.00 91.54  ? 443 ARG   A CB  1 
ATOM   3322 C CG  . ARG   B 1 228 ? -51.455 25.039  20.524 1.00 92.42  ? 443 ARG   A CG  1 
ATOM   3323 C CD  . ARG   B 1 228 ? -52.498 24.636  21.587 1.00 93.98  ? 443 ARG   A CD  1 
ATOM   3324 N NE  . ARG   B 1 228 ? -53.870 24.914  21.173 1.00 100.02 ? 443 ARG   A NE  1 
ATOM   3325 C CZ  . ARG   B 1 228 ? -54.897 24.102  21.389 1.00 101.93 ? 443 ARG   A CZ  1 
ATOM   3326 N NH1 . ARG   B 1 228 ? -54.751 22.958  22.044 1.00 94.65  ? 443 ARG   A NH1 1 
ATOM   3327 N NH2 . ARG   B 1 228 ? -56.106 24.454  20.955 1.00 106.41 ? 443 ARG   A NH2 1 
ATOM   3328 N N   . LEU   B 1 229 ? -51.059 21.691  17.217 1.00 78.52  ? 444 LEU   A N   1 
ATOM   3329 C CA  . LEU   B 1 229 ? -51.719 21.090  16.069 1.00 80.73  ? 444 LEU   A CA  1 
ATOM   3330 C C   . LEU   B 1 229 ? -53.225 21.035  16.271 1.00 84.69  ? 444 LEU   A C   1 
ATOM   3331 O O   . LEU   B 1 229 ? -53.710 20.630  17.335 1.00 86.86  ? 444 LEU   A O   1 
ATOM   3332 C CB  . LEU   B 1 229 ? -51.185 19.710  15.718 1.00 80.07  ? 444 LEU   A CB  1 
ATOM   3333 C CG  . LEU   B 1 229 ? -49.674 19.520  15.669 1.00 76.86  ? 444 LEU   A CG  1 
ATOM   3334 C CD1 . LEU   B 1 229 ? -49.169 19.004  16.963 1.00 70.69  ? 444 LEU   A CD1 1 
ATOM   3335 C CD2 . LEU   B 1 229 ? -49.302 18.595  14.496 1.00 83.04  ? 444 LEU   A CD2 1 
ATOM   3336 N N   . VAL   B 1 230 ? -53.955 21.461  15.237 1.00 87.02  ? 445 VAL   A N   1 
ATOM   3337 C CA  . VAL   B 1 230 ? -55.410 21.525  15.247 1.00 88.07  ? 445 VAL   A CA  1 
ATOM   3338 C C   . VAL   B 1 230 ? -55.943 20.752  14.046 1.00 92.36  ? 445 VAL   A C   1 
ATOM   3339 O O   . VAL   B 1 230 ? -55.193 20.025  13.382 1.00 89.57  ? 445 VAL   A O   1 
ATOM   3340 C CB  . VAL   B 1 230 ? -55.892 22.991  15.269 1.00 89.89  ? 445 VAL   A CB  1 
ATOM   3341 C CG1 . VAL   B 1 230 ? -55.062 23.795  16.256 1.00 90.32  ? 445 VAL   A CG1 1 
ATOM   3342 C CG2 . VAL   B 1 230 ? -55.826 23.641  13.889 1.00 95.78  ? 445 VAL   A CG2 1 
ATOM   3343 N N   . ARG   B 1 231 ? -57.243 20.867  13.778 1.00 92.90  ? 446 ARG   A N   1 
ATOM   3344 C CA  . ARG   B 1 231 ? -57.831 20.118  12.677 1.00 95.24  ? 446 ARG   A CA  1 
ATOM   3345 C C   . ARG   B 1 231 ? -59.076 20.801  12.114 1.00 96.34  ? 446 ARG   A C   1 
ATOM   3346 O O   . ARG   B 1 231 ? -60.129 20.821  12.749 1.00 98.08  ? 446 ARG   A O   1 
ATOM   3347 C CB  . ARG   B 1 231 ? -58.163 18.702  13.140 1.00 95.97  ? 446 ARG   A CB  1 
ATOM   3348 C CG  . ARG   B 1 231 ? -57.873 17.636  12.123 1.00 100.86 ? 446 ARG   A CG  1 
ATOM   3349 C CD  . ARG   B 1 231 ? -57.535 16.317  12.793 1.00 102.94 ? 446 ARG   A CD  1 
ATOM   3350 N NE  . ARG   B 1 231 ? -58.282 15.224  12.185 1.00 112.41 ? 446 ARG   A NE  1 
ATOM   3351 C CZ  . ARG   B 1 231 ? -58.309 13.975  12.630 1.00 113.56 ? 446 ARG   A CZ  1 
ATOM   3352 N NH1 . ARG   B 1 231 ? -57.584 13.594  13.668 1.00 110.69 ? 446 ARG   A NH1 1 
ATOM   3353 N NH2 . ARG   B 1 231 ? -59.082 13.084  12.012 1.00 119.01 ? 446 ARG   A NH2 1 
HETATM 3354 C C13 . A1H3X C 2 .   ? -36.310 -10.398 17.254 1.00 58.08  ? 501 A1H3X B C13 1 
HETATM 3355 C C17 . A1H3X C 2 .   ? -36.662 -13.777 13.788 1.00 60.99  ? 501 A1H3X B C17 1 
HETATM 3356 C C20 . A1H3X C 2 .   ? -36.560 -14.355 10.963 1.00 61.99  ? 501 A1H3X B C20 1 
HETATM 3357 C C21 . A1H3X C 2 .   ? -35.888 -13.279 11.523 1.00 64.20  ? 501 A1H3X B C21 1 
HETATM 3358 C C22 . A1H3X C 2 .   ? -35.937 -12.996 12.900 1.00 63.66  ? 501 A1H3X B C22 1 
HETATM 3359 C C24 . A1H3X C 2 .   ? -34.048 -11.867 18.168 1.00 58.29  ? 501 A1H3X B C24 1 
HETATM 3360 C C01 . A1H3X C 2 .   ? -39.605 -6.073  20.775 1.00 66.20  ? 501 A1H3X B C01 1 
HETATM 3361 C C02 . A1H3X C 2 .   ? -39.382 -4.835  19.877 1.00 67.44  ? 501 A1H3X B C02 1 
HETATM 3362 C C04 . A1H3X C 2 .   ? -38.556 -6.258  18.065 1.00 65.29  ? 501 A1H3X B C04 1 
HETATM 3363 C C06 . A1H3X C 2 .   ? -37.567 -7.380  18.164 1.00 60.33  ? 501 A1H3X B C06 1 
HETATM 3364 C C07 . A1H3X C 2 .   ? -36.440 -7.402  18.912 1.00 60.74  ? 501 A1H3X B C07 1 
HETATM 3365 C C08 . A1H3X C 2 .   ? -35.496 -8.543  18.987 1.00 62.04  ? 501 A1H3X B C08 1 
HETATM 3366 C C09 . A1H3X C 2 .   ? -34.382 -8.608  19.833 1.00 63.61  ? 501 A1H3X B C09 1 
HETATM 3367 C C11 . A1H3X C 2 .   ? -34.363 -10.586 18.694 1.00 63.96  ? 501 A1H3X B C11 1 
HETATM 3368 C C12 . A1H3X C 2 .   ? -35.486 -9.832  18.253 1.00 60.31  ? 501 A1H3X B C12 1 
HETATM 3369 C C14 . A1H3X C 2 .   ? -36.018 -11.666 16.729 1.00 58.86  ? 501 A1H3X B C14 1 
HETATM 3370 C C16 . A1H3X C 2 .   ? -36.706 -13.521 15.305 1.00 59.19  ? 501 A1H3X B C16 1 
HETATM 3371 C C18 . A1H3X C 2 .   ? -37.336 -14.873 13.207 1.00 67.54  ? 501 A1H3X B C18 1 
HETATM 3372 C C19 . A1H3X C 2 .   ? -37.292 -15.162 11.821 1.00 66.95  ? 501 A1H3X B C19 1 
HETATM 3373 C C23 . A1H3X C 2 .   ? -34.893 -12.388 17.191 1.00 57.81  ? 501 A1H3X B C23 1 
HETATM 3374 N N10 . A1H3X C 2 .   ? -33.688 -9.834  19.670 1.00 67.24  ? 501 A1H3X B N10 1 
HETATM 3375 O O03 . A1H3X C 2 .   ? -38.382 -5.135  18.842 1.00 71.09  ? 501 A1H3X B O03 1 
HETATM 3376 O O05 . A1H3X C 2 .   ? -39.564 -6.288  17.353 1.00 67.12  ? 501 A1H3X B O05 1 
HETATM 3377 O O15 . A1H3X C 2 .   ? -36.860 -12.176 15.727 1.00 60.00  ? 501 A1H3X B O15 1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . TRP A 3   ? 1.2381 1.3120 1.5325 0.2426  -0.4102 0.1474  218 TRP B N   
2    C CA  . TRP A 3   ? 1.2822 1.2903 1.4937 0.2025  -0.3883 0.1653  218 TRP B CA  
3    C C   . TRP A 3   ? 1.2687 1.2752 1.4791 0.2003  -0.3402 0.1462  218 TRP B C   
4    O O   . TRP A 3   ? 1.2184 1.2359 1.4009 0.1694  -0.3051 0.1432  218 TRP B O   
5    C CB  . TRP A 3   ? 1.2565 1.2854 1.4310 0.1617  -0.3818 0.1759  218 TRP B CB  
6    C CG  . TRP A 3   ? 1.2823 1.2779 1.4160 0.1491  -0.4263 0.2035  218 TRP B CG  
7    C CD1 . TRP A 3   ? 1.3286 1.2710 1.3791 0.1138  -0.4296 0.2257  218 TRP B CD1 
8    C CD2 . TRP A 3   ? 1.2824 1.3018 1.4557 0.1712  -0.4751 0.2115  218 TRP B CD2 
9    N NE1 . TRP A 3   ? 1.3616 1.2896 1.3917 0.1093  -0.4775 0.2493  218 TRP B NE1 
10   C CE2 . TRP A 3   ? 1.3433 1.3146 1.4491 0.1450  -0.5080 0.2420  218 TRP B CE2 
11   C CE3 . TRP A 3   ? 1.2492 1.3329 1.5103 0.2111  -0.4944 0.1943  218 TRP B CE3 
12   C CZ2 . TRP A 3   ? 1.3752 1.3524 1.4963 0.1568  -0.5628 0.2588  218 TRP B CZ2 
13   C CZ3 . TRP A 3   ? 1.2777 1.3723 1.5608 0.2262  -0.5483 0.2080  218 TRP B CZ3 
14   C CH2 . TRP A 3   ? 1.3419 1.3790 1.5541 0.1988  -0.5836 0.2416  218 TRP B CH2 
15   N N   . GLN A 4   ? 1.2782 1.2679 1.5189 0.2349  -0.3428 0.1318  219 GLN B N   
16   C CA  . GLN A 4   ? 1.2096 1.2057 1.4573 0.2377  -0.3011 0.1105  219 GLN B CA  
17   C C   . GLN A 4   ? 1.2156 1.1307 1.3952 0.2134  -0.2892 0.1267  219 GLN B C   
18   O O   . GLN A 4   ? 1.2520 1.0985 1.3903 0.2073  -0.3195 0.1509  219 GLN B O   
19   C CB  . GLN A 4   ? 1.1141 1.1345 1.4253 0.2872  -0.3090 0.0818  219 GLN B CB  
20   C CG  . GLN A 4   ? 1.0502 1.1813 1.4371 0.3079  -0.3020 0.0563  219 GLN B CG  
21   C CD  . GLN A 4   ? 1.0260 1.1851 1.4788 0.3652  -0.3223 0.0253  219 GLN B CD  
22   O OE1 . GLN A 4   ? 1.0638 1.1535 1.5050 0.3899  -0.3364 0.0185  219 GLN B OE1 
23   N NE2 . GLN A 4   ? 0.9482 1.2109 1.4720 0.3871  -0.3264 0.0047  219 GLN B NE2 
24   N N   . ALA A 5   ? 1.2254 1.1525 1.3938 0.1971  -0.2462 0.1146  220 ALA B N   
25   C CA  . ALA A 5   ? 1.2503 1.1188 1.3596 0.1710  -0.2293 0.1269  220 ALA B CA  
26   C C   . ALA A 5   ? 1.2612 1.0748 1.3703 0.1906  -0.2394 0.1240  220 ALA B C   
27   O O   . ALA A 5   ? 1.2220 1.0536 1.3799 0.2261  -0.2422 0.1003  220 ALA B O   
28   C CB  . ALA A 5   ? 1.1621 1.0629 1.2643 0.1497  -0.1847 0.1137  220 ALA B CB  
29   N N   . ARG A 6   ? 1.3194 1.0684 1.3715 0.1655  -0.2456 0.1471  221 ARG B N   
30   C CA  . ARG A 6   ? 1.3271 1.0147 1.3691 0.1738  -0.2558 0.1483  221 ARG B CA  
31   C C   . ARG A 6   ? 1.2919 0.9698 1.3014 0.1461  -0.2188 0.1471  221 ARG B C   
32   O O   . ARG A 6   ? 1.3168 0.9552 1.3257 0.1531  -0.2204 0.1414  221 ARG B O   
33   C CB  . ARG A 6   ? 1.4156 1.0281 1.4194 0.1650  -0.3045 0.1818  221 ARG B CB  
34   C CG  . ARG A 6   ? 1.5546 1.1439 1.4867 0.1137  -0.2979 0.2143  221 ARG B CG  
35   C CD  . ARG A 6   ? 1.6173 1.2082 1.5220 0.0988  -0.3271 0.2399  221 ARG B CD  
36   N NE  . ARG A 6   ? 1.7083 1.2957 1.5436 0.0491  -0.3127 0.2639  221 ARG B NE  
37   C CZ  . ARG A 6   ? 1.6673 1.2768 1.4675 0.0263  -0.3191 0.2787  221 ARG B CZ  
38   N NH1 . ARG A 6   ? 1.6003 1.2350 1.4284 0.0458  -0.3411 0.2750  221 ARG B NH1 
39   N NH2 . ARG A 6   ? 1.6704 1.2825 1.4064 -0.0177 -0.3035 0.2957  221 ARG B NH2 
40   N N   . GLY A 7   ? 1.2525 0.9652 1.2373 0.1170  -0.1883 0.1497  222 GLY B N   
41   C CA  . GLY A 7   ? 1.1452 0.8632 1.1114 0.0971  -0.1524 0.1423  222 GLY B CA  
42   C C   . GLY A 7   ? 1.0174 0.7957 1.0055 0.0971  -0.1198 0.1215  222 GLY B C   
43   O O   . GLY A 7   ? 0.9807 0.7976 0.9967 0.1081  -0.1243 0.1144  222 GLY B O   
44   N N   . LEU A 8   ? 0.9170 0.7014 0.8925 0.0828  -0.0904 0.1132  223 LEU B N   
45   C CA  . LEU A 8   ? 0.8836 0.7122 0.8723 0.0786  -0.0643 0.0969  223 LEU B CA  
46   C C   . LEU A 8   ? 0.9021 0.7400 0.8577 0.0567  -0.0632 0.1040  223 LEU B C   
47   O O   . LEU A 8   ? 0.8538 0.6874 0.7779 0.0384  -0.0488 0.1041  223 LEU B O   
48   C CB  . LEU A 8   ? 0.8641 0.6923 0.8540 0.0752  -0.0390 0.0848  223 LEU B CB  
49   C CG  . LEU A 8   ? 0.7505 0.6160 0.7667 0.0797  -0.0186 0.0671  223 LEU B CG  
50   C CD1 . LEU A 8   ? 0.7314 0.5868 0.7395 0.0736  0.0002  0.0601  223 LEU B CD1 
51   C CD2 . LEU A 8   ? 0.7476 0.6358 0.7568 0.0667  -0.0157 0.0661  223 LEU B CD2 
52   N N   . GLY A 9   ? 0.9101 0.7658 0.8740 0.0594  -0.0794 0.1069  224 GLY B N   
53   C CA  . GLY A 9   ? 0.9433 0.8069 0.8744 0.0406  -0.0822 0.1099  224 GLY B CA  
54   C C   . GLY A 9   ? 0.9604 0.8390 0.9043 0.0452  -0.1074 0.1163  224 GLY B C   
55   O O   . GLY A 9   ? 0.9358 0.8198 0.9143 0.0642  -0.1245 0.1203  224 GLY B O   
56   N N   . THR A 10  ? 0.9630 0.8517 0.8807 0.0292  -0.1109 0.1140  225 THR B N   
57   C CA  . THR A 10  ? 0.9583 0.8599 0.8783 0.0274  -0.1377 0.1218  225 THR B CA  
58   C C   . THR A 10  ? 1.0737 0.9573 0.9346 0.0077  -0.1508 0.1346  225 THR B C   
59   O O   . THR A 10  ? 1.1066 0.9741 0.9287 -0.0049 -0.1377 0.1382  225 THR B O   
60   C CB  . THR A 10  ? 0.8857 0.8169 0.8261 0.0223  -0.1353 0.1069  225 THR B CB  
61   O OG1 . THR A 10  ? 0.8923 0.8139 0.7941 0.0065  -0.1233 0.0933  225 THR B OG1 
62   C CG2 . THR A 10  ? 0.8597 0.8129 0.8483 0.0333  -0.1179 0.0963  225 THR B CG2 
63   N N   . ALA A 11  ? 1.0867 0.9796 0.9402 0.0026  -0.1771 0.1421  226 ALA B N   
64   C CA  . ALA A 11  ? 1.1024 0.9843 0.8945 -0.0191 -0.1911 0.1538  226 ALA B CA  
65   C C   . ALA A 11  ? 1.0890 0.9810 0.8412 -0.0353 -0.1678 0.1313  226 ALA B C   
66   O O   . ALA A 11  ? 1.1272 1.0180 0.8227 -0.0547 -0.1663 0.1355  226 ALA B O   
67   C CB  . ALA A 11  ? 1.1039 0.9960 0.8992 -0.0205 -0.2265 0.1644  226 ALA B CB  
68   N N   . ARG A 12  ? 0.9460 0.8501 0.7267 -0.0278 -0.1518 0.1065  227 ARG B N   
69   C CA  . ARG A 12  ? 0.9651 0.8745 0.7158 -0.0359 -0.1362 0.0792  227 ARG B CA  
70   C C   . ARG A 12  ? 0.9854 0.8944 0.7323 -0.0324 -0.1053 0.0674  227 ARG B C   
71   O O   . ARG A 12  ? 1.0798 0.9998 0.7890 -0.0400 -0.0918 0.0490  227 ARG B O   
72   C CB  . ARG A 12  ? 0.9728 0.8856 0.7532 -0.0321 -0.1433 0.0607  227 ARG B CB  
73   C CG  . ARG A 12  ? 0.9830 0.9043 0.7727 -0.0386 -0.1751 0.0718  227 ARG B CG  
74   C CD  . ARG A 12  ? 0.9140 0.8349 0.7170 -0.0450 -0.1857 0.0531  227 ARG B CD  
75   N NE  . ARG A 12  ? 1.0398 0.9457 0.7943 -0.0516 -0.1846 0.0254  227 ARG B NE  
76   C CZ  . ARG A 12  ? 1.0931 0.9819 0.8504 -0.0531 -0.1889 0.0008  227 ARG B CZ  
77   N NH1 . ARG A 12  ? 1.0643 0.9493 0.8664 -0.0554 -0.1948 0.0058  227 ARG B NH1 
78   N NH2 . ARG A 12  ? 1.0927 0.9687 0.8055 -0.0528 -0.1889 -0.0304 227 ARG B NH2 
79   N N   . LEU A 13  ? 0.9448 0.8471 0.7305 -0.0205 -0.0941 0.0752  228 LEU B N   
80   C CA  . LEU A 13  ? 0.9629 0.8666 0.7508 -0.0170 -0.0670 0.0626  228 LEU B CA  
81   C C   . LEU A 13  ? 0.9934 0.8846 0.8051 -0.0106 -0.0626 0.0820  228 LEU B C   
82   O O   . LEU A 13  ? 1.0159 0.9025 0.8664 0.0023  -0.0723 0.0897  228 LEU B O   
83   C CB  . LEU A 13  ? 0.8952 0.7998 0.7102 -0.0068 -0.0581 0.0377  228 LEU B CB  
84   C CG  . LEU A 13  ? 0.9038 0.8125 0.7205 -0.0015 -0.0338 0.0213  228 LEU B CG  
85   C CD1 . LEU A 13  ? 0.8902 0.8188 0.6627 -0.0107 -0.0236 0.0080  228 LEU B CD1 
86   C CD2 . LEU A 13  ? 0.8062 0.7061 0.6496 0.0088  -0.0330 0.0007  228 LEU B CD2 
87   N N   . GLN A 14  ? 1.0516 0.9409 0.8401 -0.0204 -0.0491 0.0879  229 GLN B N   
88   C CA  . GLN A 14  ? 1.0764 0.9455 0.8803 -0.0172 -0.0486 0.1055  229 GLN B CA  
89   C C   . GLN A 14  ? 1.0126 0.8900 0.8231 -0.0178 -0.0222 0.0923  229 GLN B C   
90   O O   . GLN A 14  ? 0.9787 0.8808 0.7671 -0.0273 -0.0060 0.0771  229 GLN B O   
91   C CB  . GLN A 14  ? 1.1335 0.9831 0.8999 -0.0355 -0.0669 0.1350  229 GLN B CB  
92   C CG  . GLN A 14  ? 1.1884 1.0286 0.9464 -0.0349 -0.0979 0.1504  229 GLN B CG  
93   C CD  . GLN A 14  ? 1.2189 1.0816 0.9291 -0.0547 -0.0999 0.1465  229 GLN B CD  
94   O OE1 . GLN A 14  ? 1.1998 1.0883 0.8821 -0.0677 -0.0771 0.1304  229 GLN B OE1 
95   N NE2 . GLN A 14  ? 1.2399 1.0975 0.9414 -0.0555 -0.1282 0.1583  229 GLN B NE2 
96   N N   . LEU A 15  ? 0.9202 0.7817 0.7633 -0.0055 -0.0190 0.0949  230 LEU B N   
97   C CA  . LEU A 15  ? 0.8808 0.7463 0.7290 -0.0084 0.0013  0.0875  230 LEU B CA  
98   C C   . LEU A 15  ? 0.9287 0.7826 0.7447 -0.0311 -0.0018 0.1089  230 LEU B C   
99   O O   . LEU A 15  ? 0.9673 0.7881 0.7753 -0.0345 -0.0240 0.1319  230 LEU B O   
100  C CB  . LEU A 15  ? 0.8477 0.7004 0.7362 0.0101  0.0041  0.0824  230 LEU B CB  
101  C CG  . LEU A 15  ? 0.8243 0.6817 0.7210 0.0082  0.0230  0.0730  230 LEU B CG  
102  C CD1 . LEU A 15  ? 0.7415 0.6253 0.6445 0.0117  0.0378  0.0508  230 LEU B CD1 
103  C CD2 . LEU A 15  ? 0.8400 0.6796 0.7664 0.0232  0.0212  0.0721  230 LEU B CD2 
104  N N   . VAL A 16  ? 0.8728 0.7553 0.6709 -0.0478 0.0176  0.1019  231 VAL B N   
105  C CA  . VAL A 16  ? 0.9547 0.8341 0.7224 -0.0772 0.0168  0.1243  231 VAL B CA  
106  C C   . VAL A 16  ? 0.9558 0.8290 0.7452 -0.0777 0.0277  0.1218  231 VAL B C   
107  O O   . VAL A 16  ? 1.0357 0.8714 0.8187 -0.0901 0.0134  0.1438  231 VAL B O   
108  C CB  . VAL A 16  ? 0.9247 0.8559 0.6527 -0.1026 0.0310  0.1201  231 VAL B CB  
109  C CG1 . VAL A 16  ? 0.9333 0.8690 0.6274 -0.1418 0.0302  0.1483  231 VAL B CG1 
110  C CG2 . VAL A 16  ? 0.9366 0.8686 0.6378 -0.1037 0.0166  0.1235  231 VAL B CG2 
111  N N   . GLU A 17  ? 0.9223 0.8279 0.7364 -0.0647 0.0490  0.0949  232 GLU B N   
112  C CA  . GLU A 17  ? 0.9656 0.8649 0.8018 -0.0640 0.0569  0.0920  232 GLU B CA  
113  C C   . GLU A 17  ? 0.9308 0.8447 0.8026 -0.0373 0.0689  0.0641  232 GLU B C   
114  O O   . GLU A 17  ? 0.9072 0.8476 0.7821 -0.0264 0.0755  0.0443  232 GLU B O   
115  C CB  . GLU A 17  ? 0.9855 0.9195 0.8026 -0.0959 0.0692  0.0995  232 GLU B CB  
116  C CG  . GLU A 17  ? 1.0362 0.9368 0.8626 -0.1063 0.0622  0.1134  232 GLU B CG  
117  C CD  . GLU A 17  ? 1.0609 1.0058 0.8860 -0.1329 0.0780  0.1130  232 GLU B CD  
118  O OE1 . GLU A 17  ? 1.0955 1.0365 0.8916 -0.1705 0.0703  0.1399  232 GLU B OE1 
119  O OE2 . GLU A 17  ? 1.1074 1.0902 0.9617 -0.1178 0.0951  0.0875  232 GLU B OE2 
120  N N   . PHE A 18  ? 0.8573 0.7478 0.7526 -0.0273 0.0675  0.0631  233 PHE B N   
121  C CA  . PHE A 18  ? 0.8091 0.7111 0.7331 -0.0092 0.0766  0.0426  233 PHE B CA  
122  C C   . PHE A 18  ? 0.8271 0.7222 0.7614 -0.0157 0.0804  0.0443  233 PHE B C   
123  O O   . PHE A 18  ? 0.8600 0.7234 0.7861 -0.0251 0.0706  0.0596  233 PHE B O   
124  C CB  . PHE A 18  ? 0.7999 0.6824 0.7417 0.0114  0.0683  0.0385  233 PHE B CB  
125  C CG  . PHE A 18  ? 0.8172 0.7022 0.7827 0.0230  0.0734  0.0259  233 PHE B CG  
126  C CD1 . PHE A 18  ? 0.8017 0.7059 0.7755 0.0287  0.0779  0.0104  233 PHE B CD1 
127  C CD2 . PHE A 18  ? 0.8372 0.7041 0.8144 0.0285  0.0712  0.0285  233 PHE B CD2 
128  C CE1 . PHE A 18  ? 0.8122 0.7139 0.8034 0.0361  0.0779  0.0035  233 PHE B CE1 
129  C CE2 . PHE A 18  ? 0.7936 0.6660 0.7861 0.0349  0.0755  0.0190  233 PHE B CE2 
130  C CZ  . PHE A 18  ? 0.7791 0.6673 0.7775 0.0368  0.0778  0.0094  233 PHE B CZ  
131  N N   . SER A 19  ? 0.7812 0.7024 0.7332 -0.0100 0.0906  0.0279  234 SER B N   
132  C CA  . SER A 19  ? 0.7873 0.7005 0.7515 -0.0136 0.0916  0.0278  234 SER B CA  
133  C C   . SER A 19  ? 0.7763 0.7117 0.7633 0.0004  0.0968  0.0091  234 SER B C   
134  O O   . SER A 19  ? 0.7409 0.7042 0.7340 0.0090  0.1004  -0.0051 234 SER B O   
135  C CB  . SER A 19  ? 0.7699 0.6962 0.7217 -0.0413 0.0944  0.0394  234 SER B CB  
136  O OG  . SER A 19  ? 0.7900 0.7724 0.7423 -0.0489 0.1073  0.0294  234 SER B OG  
137  N N   . ALA A 20  ? 0.7313 0.6503 0.7290 0.0038  0.0938  0.0081  235 ALA B N   
138  C CA  . ALA A 20  ? 0.6953 0.6317 0.7114 0.0111  0.0944  -0.0044 235 ALA B CA  
139  C C   . ALA A 20  ? 0.6154 0.5612 0.6344 -0.0052 0.0963  -0.0015 235 ALA B C   
140  O O   . ALA A 20  ? 0.6918 0.6091 0.6985 -0.0166 0.0923  0.0094  235 ALA B O   
141  C CB  . ALA A 20  ? 0.7379 0.6515 0.7587 0.0234  0.0876  -0.0057 235 ALA B CB  
142  N N   . PHE A 21  ? 0.5773 0.5627 0.6136 -0.0062 0.0996  -0.0122 236 PHE B N   
143  C CA  . PHE A 21  ? 0.6231 0.6287 0.6633 -0.0278 0.1017  -0.0077 236 PHE B CA  
144  C C   . PHE A 21  ? 0.6146 0.6570 0.6827 -0.0193 0.0996  -0.0227 236 PHE B C   
145  O O   . PHE A 21  ? 0.6223 0.6719 0.7046 0.0038  0.0948  -0.0363 236 PHE B O   
146  C CB  . PHE A 21  ? 0.7388 0.7777 0.7680 -0.0515 0.1109  0.0007  236 PHE B CB  
147  C CG  . PHE A 21  ? 0.6059 0.7044 0.6466 -0.0420 0.1219  -0.0164 236 PHE B CG  
148  C CD1 . PHE A 21  ? 0.6417 0.7332 0.6681 -0.0304 0.1240  -0.0197 236 PHE B CD1 
149  C CD2 . PHE A 21  ? 0.6149 0.7793 0.6820 -0.0428 0.1287  -0.0325 236 PHE B CD2 
150  C CE1 . PHE A 21  ? 0.6787 0.8242 0.7130 -0.0191 0.1327  -0.0414 236 PHE B CE1 
151  C CE2 . PHE A 21  ? 0.6706 0.8950 0.7506 -0.0286 0.1383  -0.0558 236 PHE B CE2 
152  C CZ  . PHE A 21  ? 0.6358 0.8480 0.6973 -0.0163 0.1402  -0.0614 236 PHE B CZ  
153  N N   . VAL A 22  ? 0.6353 0.6986 0.7114 -0.0389 0.0991  -0.0195 237 VAL B N   
154  C CA  . VAL A 22  ? 0.7233 0.8332 0.8308 -0.0328 0.0955  -0.0337 237 VAL B CA  
155  C C   . VAL A 22  ? 0.7103 0.8768 0.8283 -0.0622 0.1035  -0.0302 237 VAL B C   
156  O O   . VAL A 22  ? 0.7060 0.8508 0.8027 -0.0926 0.1034  -0.0114 237 VAL B O   
157  C CB  . VAL A 22  ? 0.6252 0.7011 0.7345 -0.0269 0.0806  -0.0330 237 VAL B CB  
158  C CG1 . VAL A 22  ? 0.7522 0.7868 0.8377 -0.0498 0.0774  -0.0190 237 VAL B CG1 
159  C CG2 . VAL A 22  ? 0.5502 0.6723 0.6928 -0.0207 0.0718  -0.0456 237 VAL B CG2 
160  N N   . GLU A 23  ? 0.6596 0.9001 0.8116 -0.0538 0.1082  -0.0487 238 GLU B N   
161  C CA  . GLU A 23  ? 0.7279 1.0403 0.8963 -0.0839 0.1169  -0.0469 238 GLU B CA  
162  C C   . GLU A 23  ? 0.7318 1.0801 0.9380 -0.0772 0.1053  -0.0590 238 GLU B C   
163  O O   . GLU A 23  ? 0.7501 1.1152 0.9847 -0.0412 0.0969  -0.0808 238 GLU B O   
164  C CB  . GLU A 23  ? 0.6606 1.0563 0.8405 -0.0825 0.1363  -0.0626 238 GLU B CB  
165  C CG  . GLU A 23  ? 0.6431 1.0055 0.7825 -0.0895 0.1455  -0.0504 238 GLU B CG  
166  C CD  . GLU A 23  ? 0.6809 1.1139 0.8274 -0.0749 0.1617  -0.0744 238 GLU B CD  
167  O OE1 . GLU A 23  ? 0.6418 1.1293 0.8265 -0.0424 0.1620  -0.1077 238 GLU B OE1 
168  O OE2 . GLU A 23  ? 0.6673 1.0999 0.7795 -0.0950 0.1718  -0.0612 238 GLU B OE2 
169  N N   . PRO A 24  ? 0.7742 1.1302 0.9813 -0.1108 0.1001  -0.0450 239 PRO B N   
170  C CA  . PRO A 24  ? 0.8334 1.2237 1.0762 -0.1060 0.0860  -0.0553 239 PRO B CA  
171  C C   . PRO A 24  ? 0.8589 1.3623 1.1527 -0.0956 0.0945  -0.0791 239 PRO B C   
172  O O   . PRO A 24  ? 0.8693 1.4334 1.1659 -0.1047 0.1148  -0.0846 239 PRO B O   
173  C CB  . PRO A 24  ? 0.8653 1.2358 1.0911 -0.1519 0.0789  -0.0333 239 PRO B CB  
174  C CG  . PRO A 24  ? 0.8821 1.2267 1.0710 -0.1829 0.0898  -0.0124 239 PRO B CG  
175  C CD  . PRO A 24  ? 0.8184 1.1576 0.9952 -0.1577 0.1040  -0.0189 239 PRO B CD  
176  N N   . PRO A 25  ? 0.8524 1.3908 1.1875 -0.0749 0.0783  -0.0957 240 PRO B N   
177  C CA  . PRO A 25  ? 0.8172 1.4762 1.2096 -0.0631 0.0847  -0.1227 240 PRO B CA  
178  C C   . PRO A 25  ? 0.8331 1.5792 1.2330 -0.1129 0.1047  -0.1127 240 PRO B C   
179  O O   . PRO A 25  ? 0.8148 1.6602 1.2399 -0.1104 0.1251  -0.1321 240 PRO B O   
180  C CB  . PRO A 25  ? 0.8254 1.4899 1.2548 -0.0419 0.0566  -0.1329 240 PRO B CB  
181  C CG  . PRO A 25  ? 0.8950 1.4406 1.2849 -0.0243 0.0377  -0.1200 240 PRO B CG  
182  C CD  . PRO A 25  ? 0.8783 1.3517 1.2102 -0.0561 0.0521  -0.0935 240 PRO B CD  
183  N N   . ASP A 26  ? 0.8873 1.5976 1.2618 -0.1606 0.0986  -0.0827 241 ASP B N   
184  C CA  . ASP A 26  ? 0.9158 1.7005 1.2925 -0.2176 0.1123  -0.0662 241 ASP B CA  
185  C C   . ASP A 26  ? 0.9194 1.7051 1.2562 -0.2431 0.1350  -0.0512 241 ASP B C   
186  O O   . ASP A 26  ? 0.9178 1.7548 1.2447 -0.2988 0.1447  -0.0300 241 ASP B O   
187  C CB  . ASP A 26  ? 0.9423 1.6684 1.2973 -0.2612 0.0922  -0.0381 241 ASP B CB  
188  C CG  . ASP A 26  ? 1.0099 1.5926 1.3043 -0.2612 0.0803  -0.0177 241 ASP B CG  
189  O OD1 . ASP A 26  ? 1.0112 1.5518 1.2632 -0.2924 0.0868  0.0054  241 ASP B OD1 
190  O OD2 . ASP A 26  ? 1.0270 1.5430 1.3167 -0.2300 0.0630  -0.0253 241 ASP B OD2 
191  N N   . ALA A 27  ? 0.8681 1.6000 1.1804 -0.2072 0.1412  -0.0597 242 ALA B N   
192  C CA  . ALA A 27  ? 0.8563 1.5945 1.1314 -0.2285 0.1606  -0.0473 242 ALA B CA  
193  C C   . ALA A 27  ? 0.8546 1.7384 1.1616 -0.2346 0.1863  -0.0698 242 ALA B C   
194  O O   . ALA A 27  ? 0.8122 1.7359 1.0900 -0.2786 0.2031  -0.0510 242 ALA B O   
195  C CB  . ALA A 27  ? 0.7741 1.4214 1.0184 -0.1881 0.1583  -0.0524 242 ALA B CB  
196  N N   . VAL A 28  ? 0.8595 1.8279 1.2257 -0.1923 0.1881  -0.1104 243 VAL B N   
197  C CA  . VAL A 28  ? 0.7194 1.8414 1.1227 -0.1934 0.2134  -0.1399 243 VAL B CA  
198  C C   . VAL A 28  ? 0.8303 2.0430 1.2414 -0.2572 0.2223  -0.1184 243 VAL B C   
199  O O   . VAL A 28  ? 0.8003 2.0944 1.2077 -0.2642 0.2358  -0.1305 243 VAL B O   
200  C CB  . VAL A 28  ? 0.5802 1.7679 1.0512 -0.1268 0.2067  -0.1927 243 VAL B CB  
201  C CG1 . VAL A 28  ? 0.6712 1.7389 1.1287 -0.0685 0.1855  -0.2053 243 VAL B CG1 
202  C CG2 . VAL A 28  ? 0.5981 1.8360 1.1223 -0.1322 0.1906  -0.1956 243 VAL B CG2 
203  N N   . ASP A 29  ? 1.0165 2.1792 1.4205 -0.2983 0.2049  -0.0847 244 ASP B N   
204  C CA  . ASP A 29  ? 1.0566 2.2595 1.4465 -0.3633 0.2036  -0.0543 244 ASP B CA  
205  C C   . ASP A 29  ? 1.0889 2.2021 1.4054 -0.4196 0.2005  -0.0057 244 ASP B C   
206  O O   . ASP A 29  ? 1.1030 2.2423 1.3807 -0.4445 0.2121  0.0064  244 ASP B O   
207  C CB  . ASP A 29  ? 1.0411 2.2494 1.4702 -0.3768 0.1818  -0.0493 244 ASP B CB  
208  C CG  . ASP A 29  ? 1.0556 2.3664 1.5553 -0.3293 0.1809  -0.0929 244 ASP B CG  
209  O OD1 . ASP A 29  ? 1.0243 2.3492 1.5532 -0.2652 0.1846  -0.1315 244 ASP B OD1 
210  O OD2 . ASP A 29  ? 1.1248 2.4965 1.6493 -0.3551 0.1735  -0.0886 244 ASP B OD2 
211  N N   . SER A 30  ? 0.9400 1.9329 1.2303 -0.4342 0.1790  0.0210  245 SER B N   
212  C CA  . SER A 30  ? 0.9229 1.8096 1.1435 -0.4765 0.1687  0.0640  245 SER B CA  
213  C C   . SER A 30  ? 0.9346 1.7033 1.1263 -0.4203 0.1627  0.0545  245 SER B C   
214  O O   . SER A 30  ? 0.9296 1.6129 1.1269 -0.3828 0.1444  0.0448  245 SER B O   
215  C CB  . SER A 30  ? 0.9986 1.8106 1.1995 -0.5268 0.1390  0.0984  245 SER B CB  
216  O OG  . SER A 30  ? 1.0302 1.7882 1.1708 -0.5808 0.1277  0.1399  245 SER B OG  
217  N N   . TYR A 31  ? 0.9100 1.6827 1.0711 -0.4163 0.1785  0.0566  246 TYR B N   
218  C CA  . TYR A 31  ? 0.8383 1.5184 0.9785 -0.3628 0.1749  0.0445  246 TYR B CA  
219  C C   . TYR A 31  ? 0.8358 1.3680 0.9346 -0.3688 0.1474  0.0725  246 TYR B C   
220  O O   . TYR A 31  ? 0.9355 1.4262 1.0063 -0.4199 0.1310  0.1061  246 TYR B O   
221  C CB  . TYR A 31  ? 0.7791 1.4938 0.8904 -0.3639 0.1948  0.0436  246 TYR B CB  
222  C CG  . TYR A 31  ? 0.6942 1.3169 0.7824 -0.3151 0.1897  0.0342  246 TYR B CG  
223  C CD1 . TYR A 31  ? 0.7025 1.3280 0.8243 -0.2522 0.1924  -0.0048 246 TYR B CD1 
224  C CD2 . TYR A 31  ? 0.7277 1.2608 0.7616 -0.3336 0.1786  0.0657  246 TYR B CD2 
225  C CE1 . TYR A 31  ? 0.6839 1.2282 0.7850 -0.2132 0.1862  -0.0110 246 TYR B CE1 
226  C CE2 . TYR A 31  ? 0.7322 1.1917 0.7493 -0.2912 0.1737  0.0571  246 TYR B CE2 
227  C CZ  . TYR A 31  ? 0.7339 1.2011 0.7846 -0.2329 0.1787  0.0191  246 TYR B CZ  
228  O OH  . TYR A 31  ? 0.7250 1.1222 0.7596 -0.1959 0.1726  0.0126  246 TYR B OH  
229  N N   . GLN A 32  ? 0.8251 1.2801 0.9218 -0.3157 0.1406  0.0562  247 GLN B N   
230  C CA  . GLN A 32  ? 0.8578 1.1831 0.9177 -0.3088 0.1189  0.0735  247 GLN B CA  
231  C C   . GLN A 32  ? 0.7935 1.0823 0.8629 -0.2484 0.1215  0.0482  247 GLN B C   
232  O O   . GLN A 32  ? 0.7772 1.1160 0.8843 -0.2155 0.1287  0.0203  247 GLN B O   
233  C CB  . GLN A 32  ? 0.9246 1.1947 0.9848 -0.3273 0.0957  0.0837  247 GLN B CB  
234  C CG  . GLN A 32  ? 0.9309 1.2455 1.0361 -0.3045 0.0955  0.0584  247 GLN B CG  
235  C CD  . GLN A 32  ? 1.0493 1.2880 1.1445 -0.3141 0.0701  0.0649  247 GLN B CD  
236  O OE1 . GLN A 32  ? 1.1355 1.3234 1.2016 -0.3558 0.0529  0.0894  247 GLN B OE1 
237  N NE2 . GLN A 32  ? 1.0469 1.2723 1.1622 -0.2764 0.0645  0.0430  247 GLN B NE2 
238  N N   . ARG A 33  ? 0.8438 1.0498 0.8804 -0.2354 0.1135  0.0583  248 ARG B N   
239  C CA  . ARG A 33  ? 0.8416 1.0089 0.8849 -0.1850 0.1133  0.0386  248 ARG B CA  
240  C C   . ARG A 33  ? 0.8949 0.9618 0.9151 -0.1782 0.0941  0.0489  248 ARG B C   
241  O O   . ARG A 33  ? 0.9528 0.9687 0.9435 -0.2042 0.0812  0.0714  248 ARG B O   
242  C CB  . ARG A 33  ? 0.8482 1.0318 0.8804 -0.1682 0.1257  0.0330  248 ARG B CB  
243  C CG  . ARG A 33  ? 0.8770 1.0008 0.8678 -0.1848 0.1175  0.0582  248 ARG B CG  
244  C CD  . ARG A 33  ? 0.8564 0.9582 0.8409 -0.1497 0.1206  0.0472  248 ARG B CD  
245  N NE  . ARG A 33  ? 0.9292 1.1067 0.9183 -0.1474 0.1385  0.0330  248 ARG B NE  
246  C CZ  . ARG A 33  ? 0.9632 1.1379 0.9343 -0.1354 0.1423  0.0299  248 ARG B CZ  
247  N NH1 . ARG A 33  ? 0.9306 1.0335 0.8827 -0.1225 0.1294  0.0410  248 ARG B NH1 
248  N NH2 . ARG A 33  ? 0.9871 1.2386 0.9604 -0.1360 0.1591  0.0129  248 ARG B NH2 
249  N N   . HIS A 34  ? 0.8615 0.9024 0.8949 -0.1440 0.0900  0.0318  249 HIS B N   
250  C CA  . HIS A 34  ? 0.7942 0.7554 0.8091 -0.1305 0.0759  0.0335  249 HIS B CA  
251  C C   . HIS A 34  ? 0.7478 0.6877 0.7565 -0.0996 0.0807  0.0280  249 HIS B C   
252  O O   . HIS A 34  ? 0.7536 0.7249 0.7796 -0.0766 0.0892  0.0141  249 HIS B O   
253  C CB  . HIS A 34  ? 0.8179 0.7708 0.8459 -0.1190 0.0684  0.0198  249 HIS B CB  
254  C CG  . HIS A 34  ? 0.9169 0.8015 0.9256 -0.1038 0.0571  0.0157  249 HIS B CG  
255  N ND1 . HIS A 34  ? 0.8802 0.7563 0.8913 -0.0734 0.0604  0.0030  249 HIS B ND1 
256  C CD2 . HIS A 34  ? 0.9319 0.7568 0.9188 -0.1144 0.0415  0.0205  249 HIS B CD2 
257  C CE1 . HIS A 34  ? 0.9125 0.7386 0.9061 -0.0654 0.0515  -0.0019 249 HIS B CE1 
258  N NE2 . HIS A 34  ? 0.9576 0.7484 0.9373 -0.0864 0.0387  0.0061  249 HIS B NE2 
259  N N   . LEU A 35  ? 0.7263 0.6111 0.7119 -0.0994 0.0716  0.0388  250 LEU B N   
260  C CA  . LEU A 35  ? 0.7471 0.6134 0.7280 -0.0734 0.0738  0.0355  250 LEU B CA  
261  C C   . LEU A 35  ? 0.8413 0.6734 0.8250 -0.0487 0.0681  0.0227  250 LEU B C   
262  O O   . LEU A 35  ? 0.8725 0.6589 0.8451 -0.0493 0.0550  0.0224  250 LEU B O   
263  C CB  . LEU A 35  ? 0.7883 0.6205 0.7455 -0.0851 0.0644  0.0540  250 LEU B CB  
264  C CG  . LEU A 35  ? 0.8293 0.6952 0.7733 -0.1147 0.0695  0.0708  250 LEU B CG  
265  C CD1 . LEU A 35  ? 0.8551 0.6693 0.7721 -0.1229 0.0524  0.0910  250 LEU B CD1 
266  C CD2 . LEU A 35  ? 0.8138 0.7391 0.7702 -0.1006 0.0882  0.0577  250 LEU B CD2 
267  N N   . PHE A 36  ? 0.7843 0.6389 0.7811 -0.0278 0.0761  0.0112  251 PHE B N   
268  C CA  . PHE A 36  ? 0.8023 0.6375 0.7987 -0.0083 0.0737  0.0015  251 PHE B CA  
269  C C   . PHE A 36  ? 0.8267 0.6356 0.8156 0.0039  0.0696  0.0042  251 PHE B C   
270  O O   . PHE A 36  ? 0.7791 0.5590 0.7630 0.0131  0.0617  -0.0031 251 PHE B O   
271  C CB  . PHE A 36  ? 0.8001 0.6643 0.8087 0.0036  0.0793  -0.0050 251 PHE B CB  
272  C CG  . PHE A 36  ? 0.7560 0.6451 0.7761 -0.0028 0.0781  -0.0093 251 PHE B CG  
273  C CD1 . PHE A 36  ? 0.7990 0.6807 0.8159 -0.0088 0.0722  -0.0139 251 PHE B CD1 
274  C CD2 . PHE A 36  ? 0.6712 0.5931 0.7067 -0.0003 0.0806  -0.0117 251 PHE B CD2 
275  C CE1 . PHE A 36  ? 0.7677 0.6744 0.7978 -0.0140 0.0676  -0.0171 251 PHE B CE1 
276  C CE2 . PHE A 36  ? 0.6996 0.6480 0.7519 -0.0014 0.0760  -0.0183 251 PHE B CE2 
277  C CZ  . PHE A 36  ? 0.7571 0.6977 0.8072 -0.0092 0.0688  -0.0190 251 PHE B CZ  
278  N N   . VAL A 37  ? 0.7983 0.6196 0.7878 0.0064  0.0733  0.0117  252 VAL B N   
279  C CA  . VAL A 37  ? 0.7966 0.5973 0.7808 0.0158  0.0665  0.0172  252 VAL B CA  
280  C C   . VAL A 37  ? 0.7897 0.5978 0.7630 0.0017  0.0664  0.0317  252 VAL B C   
281  O O   . VAL A 37  ? 0.7990 0.6396 0.7734 -0.0094 0.0759  0.0316  252 VAL B O   
282  C CB  . VAL A 37  ? 0.7851 0.6021 0.7808 0.0351  0.0705  0.0096  252 VAL B CB  
283  C CG1 . VAL A 37  ? 0.7912 0.6111 0.7929 0.0452  0.0725  -0.0046 252 VAL B CG1 
284  C CG2 . VAL A 37  ? 0.7626 0.6097 0.7634 0.0328  0.0782  0.0104  252 VAL B CG2 
285  N N   . HIS A 38  ? 0.8007 0.5822 0.7635 0.0035  0.0543  0.0423  253 HIS B N   
286  C CA  . HIS A 38  ? 0.8341 0.6184 0.7773 -0.0166 0.0511  0.0600  253 HIS B CA  
287  C C   . HIS A 38  ? 0.8201 0.5716 0.7523 -0.0106 0.0329  0.0725  253 HIS B C   
288  O O   . HIS A 38  ? 0.9074 0.6120 0.8321 -0.0114 0.0129  0.0805  253 HIS B O   
289  C CB  . HIS A 38  ? 0.8292 0.6061 0.7581 -0.0463 0.0479  0.0720  253 HIS B CB  
290  C CG  . HIS A 38  ? 0.9488 0.7273 0.8506 -0.0749 0.0420  0.0951  253 HIS B CG  
291  N ND1 . HIS A 38  ? 0.9974 0.7225 0.8763 -0.0914 0.0173  0.1176  253 HIS B ND1 
292  C CD2 . HIS A 38  ? 0.9395 0.7679 0.8303 -0.0915 0.0558  0.0991  253 HIS B CD2 
293  C CE1 . HIS A 38  ? 0.9265 0.6691 0.7782 -0.1219 0.0165  0.1391  253 HIS B CE1 
294  N NE2 . HIS A 38  ? 0.9410 0.7514 0.7996 -0.1218 0.0421  0.1262  253 HIS B NE2 
295  N N   . ILE A 39  ? 0.8373 0.6090 0.7684 -0.0041 0.0354  0.0739  254 ILE B N   
296  C CA  . ILE A 39  ? 0.8887 0.6345 0.8081 -0.0011 0.0156  0.0884  254 ILE B CA  
297  C C   . ILE A 39  ? 0.9257 0.6772 0.8112 -0.0315 0.0126  0.1097  254 ILE B C   
298  O O   . ILE A 39  ? 0.9429 0.7380 0.8210 -0.0459 0.0317  0.1050  254 ILE B O   
299  C CB  . ILE A 39  ? 0.8676 0.6348 0.8053 0.0215  0.0173  0.0781  254 ILE B CB  
300  C CG1 . ILE A 39  ? 0.8318 0.6091 0.7999 0.0443  0.0247  0.0581  254 ILE B CG1 
301  C CG2 . ILE A 39  ? 0.8843 0.6268 0.8147 0.0273  -0.0067 0.0923  254 ILE B CG2 
302  C CD1 . ILE A 39  ? 0.7117 0.5163 0.6999 0.0606  0.0255  0.0504  254 ILE B CD1 
303  N N   . SER A 40  ? 0.9746 0.6847 0.8385 -0.0414 -0.0129 0.1323  255 SER B N   
304  C CA  . SER A 40  ? 1.0557 0.7717 0.8795 -0.0777 -0.0178 0.1576  255 SER B CA  
305  C C   . SER A 40  ? 1.1002 0.7749 0.9050 -0.0769 -0.0494 0.1796  255 SER B C   
306  O O   . SER A 40  ? 1.1893 0.8029 0.9921 -0.0735 -0.0792 0.1928  255 SER B O   
307  C CB  . SER A 40  ? 1.0605 0.7619 0.8666 -0.1112 -0.0206 0.1734  255 SER B CB  
308  O OG  . SER A 40  ? 1.1874 0.9109 0.9532 -0.1527 -0.0207 0.1984  255 SER B OG  
309  N N   . GLN A 41  ? 1.1240 0.8278 0.9144 -0.0789 -0.0470 0.1824  256 GLN B N   
310  C CA  . GLN A 41  ? 1.1867 0.8560 0.9596 -0.0775 -0.0794 0.2037  256 GLN B CA  
311  C C   . GLN A 41  ? 1.2641 0.9471 0.9825 -0.1202 -0.0839 0.2315  256 GLN B C   
312  O O   . GLN A 41  ? 1.2565 0.9755 0.9589 -0.1231 -0.0776 0.2285  256 GLN B O   
313  C CB  . GLN A 41  ? 1.0767 0.7688 0.8782 -0.0444 -0.0778 0.1844  256 GLN B CB  
314  C CG  . GLN A 41  ? 1.0619 0.7758 0.9112 -0.0132 -0.0572 0.1528  256 GLN B CG  
315  C CD  . GLN A 41  ? 1.0090 0.7289 0.8929 0.0190  -0.0685 0.1410  256 GLN B CD  
316  O OE1 . GLN A 41  ? 1.0145 0.7598 0.8952 0.0193  -0.0696 0.1404  256 GLN B OE1 
317  N NE2 . GLN A 41  ? 0.9764 0.6784 0.8942 0.0457  -0.0767 0.1294  256 GLN B NE2 
318  N N   . HIS A 42  ? 1.4964 1.1515 1.1833 -0.1567 -0.0962 0.2591  257 HIS B N   
319  C CA  . HIS A 42  ? 1.5437 1.2163 1.1723 -0.2064 -0.1016 0.2911  257 HIS B CA  
320  C C   . HIS A 42  ? 1.5431 1.1474 1.1380 -0.2191 -0.1507 0.3300  257 HIS B C   
321  O O   . HIS A 42  ? 1.6001 1.1585 1.1586 -0.2575 -0.1773 0.3668  257 HIS B O   
322  C CB  . HIS A 42  ? 1.5714 1.2626 1.1802 -0.2497 -0.0881 0.3046  257 HIS B CB  
323  C CG  . HIS A 42  ? 1.5466 1.3119 1.1853 -0.2408 -0.0432 0.2688  257 HIS B CG  
324  N ND1 . HIS A 42  ? 1.5734 1.3699 1.2087 -0.2728 -0.0269 0.2729  257 HIS B ND1 
325  C CD2 . HIS A 42  ? 1.4755 1.2876 1.1491 -0.2041 -0.0155 0.2294  257 HIS B CD2 
326  C CE1 . HIS A 42  ? 1.5131 1.3742 1.1823 -0.2521 0.0087  0.2357  257 HIS B CE1 
327  N NE2 . HIS A 42  ? 1.4664 1.3331 1.1574 -0.2107 0.0148  0.2096  257 HIS B NE2 
328  N N   . PRO A 49  ? 1.5793 0.9669 1.6208 0.2552  -0.4629 0.1878  264 PRO B N   
329  C CA  . PRO A 49  ? 1.5051 0.9596 1.6240 0.3106  -0.4493 0.1383  264 PRO B CA  
330  C C   . PRO A 49  ? 1.4508 1.0029 1.5931 0.3051  -0.3917 0.1178  264 PRO B C   
331  O O   . PRO A 49  ? 1.3803 0.9380 1.4879 0.2693  -0.3505 0.1227  264 PRO B O   
332  C CB  . PRO A 49  ? 1.4830 0.8965 1.6100 0.3279  -0.4480 0.1101  264 PRO B CB  
333  C CG  . PRO A 49  ? 1.6036 0.9447 1.6615 0.2765  -0.4453 0.1442  264 PRO B CG  
334  C CD  . PRO A 49  ? 1.5857 0.9172 1.5898 0.2293  -0.4513 0.1931  264 PRO B CD  
335  N N   . PRO A 50  ? 1.3896 1.0254 1.5898 0.3349  -0.3866 0.0944  265 PRO B N   
336  C CA  . PRO A 50  ? 1.2897 1.0238 1.5115 0.3225  -0.3316 0.0754  265 PRO B CA  
337  C C   . PRO A 50  ? 1.1749 0.9330 1.4151 0.3342  -0.2939 0.0419  265 PRO B C   
338  O O   . PRO A 50  ? 1.1621 0.9049 1.4345 0.3748  -0.3093 0.0132  265 PRO B O   
339  C CB  . PRO A 50  ? 1.2178 1.0315 1.5031 0.3545  -0.3459 0.0586  265 PRO B CB  
340  C CG  . PRO A 50  ? 1.2724 1.0372 1.5882 0.4028  -0.4020 0.0498  265 PRO B CG  
341  C CD  . PRO A 50  ? 1.3637 1.0100 1.6082 0.3739  -0.4344 0.0907  265 PRO B CD  
342  N N   . LEU A 51  ? 1.1328 0.9271 1.3512 0.2994  -0.2469 0.0439  266 LEU B N   
343  C CA  . LEU A 51  ? 1.0768 0.8951 1.3057 0.3040  -0.2110 0.0166  266 LEU B CA  
344  C C   . LEU A 51  ? 1.0497 0.9599 1.3443 0.3400  -0.1984 -0.0217 266 LEU B C   
345  O O   . LEU A 51  ? 1.0197 0.9891 1.3523 0.3528  -0.2090 -0.0245 266 LEU B O   
346  C CB  . LEU A 51  ? 1.0305 0.8660 1.2228 0.2597  -0.1693 0.0292  266 LEU B CB  
347  C CG  . LEU A 51  ? 1.0568 0.8256 1.1863 0.2209  -0.1717 0.0619  266 LEU B CG  
348  C CD1 . LEU A 51  ? 1.0075 0.8153 1.1153 0.1861  -0.1414 0.0722  266 LEU B CD1 
349  C CD2 . LEU A 51  ? 1.0063 0.7193 1.1110 0.2149  -0.1667 0.0592  266 LEU B CD2 
350  N N   . GLU A 52  ? 1.0671 0.9952 1.3746 0.3546  -0.1758 -0.0519 267 GLU B N   
351  C CA  . GLU A 52  ? 1.0314 1.0559 1.3980 0.3874  -0.1605 -0.0919 267 GLU B CA  
352  C C   . GLU A 52  ? 0.9977 1.1130 1.3711 0.3546  -0.1198 -0.0877 267 GLU B C   
353  O O   . GLU A 52  ? 1.0096 1.1075 1.3419 0.3153  -0.0941 -0.0696 267 GLU B O   
354  C CB  . GLU A 52  ? 1.0564 1.0680 1.4287 0.4140  -0.1523 -0.1281 267 GLU B CB  
355  C CG  . GLU A 52  ? 1.1250 1.0569 1.5055 0.4570  -0.1992 -0.1432 267 GLU B CG  
356  C CD  . GLU A 52  ? 1.2368 1.1238 1.6006 0.4693  -0.1936 -0.1700 267 GLU B CD  
357  O OE1 . GLU A 52  ? 1.1976 1.1553 1.5705 0.4667  -0.1538 -0.1963 267 GLU B OE1 
358  O OE2 . GLU A 52  ? 1.3187 1.1022 1.6534 0.4724  -0.2278 -0.1611 267 GLU B OE2 
359  N N   . SER A 53  ? 0.8191 1.0322 1.2461 0.3707  -0.1170 -0.1048 268 SER B N   
360  C CA  . SER A 53  ? 0.7774 1.0778 1.2131 0.3359  -0.0851 -0.0975 268 SER B CA  
361  C C   . SER A 53  ? 0.7501 1.1216 1.1992 0.3354  -0.0485 -0.1257 268 SER B C   
362  O O   . SER A 53  ? 0.7736 1.1626 1.2469 0.3740  -0.0486 -0.1623 268 SER B O   
363  C CB  . SER A 53  ? 0.7495 1.1298 1.2362 0.3453  -0.1005 -0.0983 268 SER B CB  
364  O OG  . SER A 53  ? 0.7987 1.2282 1.3437 0.3993  -0.1161 -0.1363 268 SER B OG  
365  N N   . VAL A 54  ? 0.7240 1.1346 1.1545 0.2903  -0.0200 -0.1087 269 VAL B N   
366  C CA  . VAL A 54  ? 0.6587 1.1423 1.0939 0.2776  0.0143  -0.1265 269 VAL B CA  
367  C C   . VAL A 54  ? 0.6837 1.2485 1.1300 0.2355  0.0284  -0.1071 269 VAL B C   
368  O O   . VAL A 54  ? 0.7002 1.2184 1.1130 0.1984  0.0241  -0.0736 269 VAL B O   
369  C CB  . VAL A 54  ? 0.6861 1.0977 1.0668 0.2574  0.0301  -0.1186 269 VAL B CB  
370  C CG1 . VAL A 54  ? 0.6609 1.1402 1.0314 0.2220  0.0625  -0.1173 269 VAL B CG1 
371  C CG2 . VAL A 54  ? 0.6347 0.9946 1.0129 0.2978  0.0205  -0.1469 269 VAL B CG2 
372  N N   . ASP A 55  ? 0.6803 1.3684 1.1739 0.2405  0.0434  -0.1291 270 ASP B N   
373  C CA  . ASP A 55  ? 0.6792 1.4520 1.1874 0.1962  0.0529  -0.1086 270 ASP B CA  
374  C C   . ASP A 55  ? 0.7275 1.4706 1.1829 0.1418  0.0710  -0.0804 270 ASP B C   
375  O O   . ASP A 55  ? 0.7341 1.4845 1.1684 0.1371  0.0926  -0.0915 270 ASP B O   
376  C CB  . ASP A 55  ? 0.6347 1.5580 1.2028 0.2091  0.0693  -0.1397 270 ASP B CB  
377  C CG  . ASP A 55  ? 0.6619 1.6797 1.2473 0.1571  0.0766  -0.1153 270 ASP B CG  
378  O OD1 . ASP A 55  ? 0.6571 1.6635 1.2003 0.1038  0.0908  -0.0877 270 ASP B OD1 
379  O OD2 . ASP A 55  ? 0.6355 1.7366 1.2766 0.1682  0.0646  -0.1226 270 ASP B OD2 
380  N N   . VAL A 56  ? 0.7716 1.4792 1.2051 0.1021  0.0586  -0.0452 271 VAL B N   
381  C CA  . VAL A 56  ? 0.7713 1.4245 1.1525 0.0567  0.0657  -0.0181 271 VAL B CA  
382  C C   . VAL A 56  ? 0.8041 1.5451 1.1860 0.0218  0.0895  -0.0167 271 VAL B C   
383  O O   . VAL A 56  ? 0.8289 1.5293 1.1682 -0.0042 0.0985  -0.0037 271 VAL B O   
384  C CB  . VAL A 56  ? 0.7056 1.3082 1.0681 0.0256  0.0432  0.0130  271 VAL B CB  
385  C CG1 . VAL A 56  ? 0.7035 1.4014 1.1042 -0.0013 0.0370  0.0224  271 VAL B CG1 
386  C CG2 . VAL A 56  ? 0.7381 1.2675 1.0478 -0.0103 0.0439  0.0355  271 VAL B CG2 
387  N N   . ARG A 57  ? 0.7211 1.5888 1.1515 0.0203  0.0994  -0.0303 272 ARG B N   
388  C CA  . ARG A 57  ? 0.7054 1.6721 1.1344 -0.0213 0.1227  -0.0256 272 ARG B CA  
389  C C   . ARG A 57  ? 0.7098 1.6741 1.1134 -0.0072 0.1459  -0.0471 272 ARG B C   
390  O O   . ARG A 57  ? 0.7274 1.6982 1.0931 -0.0508 0.1575  -0.0281 272 ARG B O   
391  C CB  . ARG A 57  ? 0.6360 1.7551 1.1285 -0.0198 0.1315  -0.0428 272 ARG B CB  
392  C CG  . ARG A 57  ? 0.6178 1.7653 1.1339 -0.0527 0.1103  -0.0154 272 ARG B CG  
393  C CD  . ARG A 57  ? 0.5645 1.8616 1.1562 -0.0312 0.1165  -0.0429 272 ARG B CD  
394  N NE  . ARG A 57  ? 0.6079 1.9153 1.2331 -0.0369 0.0891  -0.0280 272 ARG B NE  
395  C CZ  . ARG A 57  ? 0.5992 1.9590 1.2852 0.0122  0.0768  -0.0551 272 ARG B CZ  
396  N NH1 . ARG A 57  ? 0.5810 1.9730 1.3008 0.0762  0.0860  -0.1004 272 ARG B NH1 
397  N NH2 . ARG A 57  ? 0.5556 1.9336 1.2694 -0.0025 0.0509  -0.0373 272 ARG B NH2 
398  N N   . GLN A 58  ? 0.6931 1.6400 1.1136 0.0519  0.1487  -0.0854 273 GLN B N   
399  C CA  . GLN A 58  ? 0.6887 1.6252 1.0848 0.0699  0.1671  -0.1106 273 GLN B CA  
400  C C   . GLN A 58  ? 0.7628 1.5883 1.0952 0.0434  0.1644  -0.0841 273 GLN B C   
401  O O   . GLN A 58  ? 0.7552 1.5674 1.0629 0.0532  0.1776  -0.1015 273 GLN B O   
402  C CB  . GLN A 58  ? 0.6659 1.5732 1.0889 0.1393  0.1593  -0.1534 273 GLN B CB  
403  C CG  . GLN A 58  ? 0.6385 1.6464 1.1306 0.1788  0.1557  -0.1864 273 GLN B CG  
404  C CD  . GLN A 58  ? 0.6949 1.8278 1.2131 0.1968  0.1820  -0.2314 273 GLN B CD  
405  O OE1 . GLN A 58  ? 0.6890 1.8992 1.1907 0.1495  0.2024  -0.2191 273 GLN B OE1 
406  N NE2 . GLN A 58  ? 0.7026 1.8037 1.2356 0.2551  0.1708  -0.2736 273 GLN B NE2 
407  N N   . ILE A 59  ? 0.8414 1.5879 1.1479 0.0128  0.1459  -0.0457 274 ILE B N   
408  C CA  . ILE A 59  ? 0.8991 1.5465 1.1521 -0.0073 0.1411  -0.0245 274 ILE B CA  
409  C C   . ILE A 59  ? 0.9538 1.5875 1.1807 -0.0645 0.1302  0.0168  274 ILE B C   
410  O O   . ILE A 59  ? 0.9888 1.5338 1.1765 -0.0799 0.1186  0.0364  274 ILE B O   
411  C CB  . ILE A 59  ? 0.8699 1.4030 1.1110 0.0257  0.1242  -0.0267 274 ILE B CB  
412  C CG1 . ILE A 59  ? 0.8618 1.3758 1.1236 0.0302  0.1039  -0.0147 274 ILE B CG1 
413  C CG2 . ILE A 59  ? 0.8305 1.3548 1.0845 0.0749  0.1297  -0.0627 274 ILE B CG2 
414  C CD1 . ILE A 59  ? 0.7814 1.1966 1.0288 0.0571  0.0881  -0.0148 274 ILE B CD1 
415  N N   . TYR A 60  ? 0.9489 1.6711 1.1989 -0.0966 0.1312  0.0292  275 TYR B N   
416  C CA  . TYR A 60  ? 0.9820 1.6856 1.2089 -0.1538 0.1136  0.0701  275 TYR B CA  
417  C C   . TYR A 60  ? 1.0391 1.7067 1.2160 -0.1906 0.1134  0.0917  275 TYR B C   
418  O O   . TYR A 60  ? 1.0912 1.6616 1.2347 -0.2088 0.0902  0.1160  275 TYR B O   
419  C CB  . TYR A 60  ? 0.9330 1.7582 1.1948 -0.1869 0.1181  0.0783  275 TYR B CB  
420  C CG  . TYR A 60  ? 0.9188 1.7498 1.2192 -0.1728 0.1011  0.0771  275 TYR B CG  
421  C CD1 . TYR A 60  ? 0.8991 1.8281 1.2317 -0.2087 0.0977  0.0905  275 TYR B CD1 
422  C CD2 . TYR A 60  ? 0.9176 1.6543 1.2178 -0.1300 0.0859  0.0667  275 TYR B CD2 
423  C CE1 . TYR A 60  ? 0.8749 1.8077 1.2425 -0.1959 0.0790  0.0897  275 TYR B CE1 
424  C CE2 . TYR A 60  ? 0.9067 1.6448 1.2358 -0.1191 0.0679  0.0674  275 TYR B CE2 
425  C CZ  . TYR A 60  ? 0.8689 1.7016 1.2320 -0.1500 0.0635  0.0781  275 TYR B CZ  
426  O OH  . TYR A 60  ? 0.8758 1.7033 1.2661 -0.1369 0.0424  0.0782  275 TYR B OH  
427  N N   . ASP A 61  ? 1.0433 1.7906 1.2145 -0.2003 0.1374  0.0810  276 ASP B N   
428  C CA  . ASP A 61  ? 1.0956 1.8256 1.2177 -0.2416 0.1363  0.1046  276 ASP B CA  
429  C C   . ASP A 61  ? 1.1413 1.7656 1.2314 -0.2139 0.1308  0.0971  276 ASP B C   
430  O O   . ASP A 61  ? 1.1612 1.7585 1.2098 -0.2446 0.1246  0.1174  276 ASP B O   
431  C CB  . ASP A 61  ? 1.1289 1.9909 1.2532 -0.2610 0.1661  0.0922  276 ASP B CB  
432  C CG  . ASP A 61  ? 1.1346 2.0509 1.2910 -0.2002 0.1931  0.0384  276 ASP B CG  
433  O OD1 . ASP A 61  ? 1.0227 1.8588 1.1916 -0.1478 0.1859  0.0168  276 ASP B OD1 
434  O OD2 . ASP A 61  ? 1.0920 2.1319 1.2594 -0.2064 0.2198  0.0172  276 ASP B OD2 
435  N N   . LYS A 62  ? 1.1755 1.7423 1.2831 -0.1603 0.1306  0.0710  277 LYS B N   
436  C CA  . LYS A 62  ? 1.1182 1.5864 1.1992 -0.1378 0.1232  0.0664  277 LYS B CA  
437  C C   . LYS A 62  ? 1.1007 1.4685 1.1667 -0.1456 0.0947  0.0897  277 LYS B C   
438  O O   . LYS A 62  ? 1.0574 1.3496 1.1056 -0.1277 0.0876  0.0859  277 LYS B O   
439  C CB  . LYS A 62  ? 1.0116 1.4679 1.1145 -0.0812 0.1356  0.0283  277 LYS B CB  
440  C CG  . LYS A 62  ? 0.9703 1.4526 1.0584 -0.0681 0.1542  0.0040  277 LYS B CG  
441  C CD  . LYS A 62  ? 0.9028 1.4044 1.0194 -0.0158 0.1664  -0.0389 277 LYS B CD  
442  C CE  . LYS A 62  ? 0.9371 1.3356 1.0488 0.0171  0.1531  -0.0459 277 LYS B CE  
443  N NZ  . LYS A 62  ? 0.7766 1.1723 0.9008 0.0614  0.1591  -0.0851 277 LYS B NZ  
444  N N   . PHE A 63  ? 1.3955 1.7258 0.9323 -0.4476 -0.1952 0.2441  278 PHE B N   
445  C CA  . PHE A 63  ? 1.5014 1.8093 1.1453 -0.4092 -0.2336 0.2721  278 PHE B CA  
446  C C   . PHE A 63  ? 1.7124 2.0452 1.4236 -0.4195 -0.2592 0.3338  278 PHE B C   
447  O O   . PHE A 63  ? 1.6412 2.0099 1.3120 -0.4552 -0.2474 0.3542  278 PHE B O   
448  C CB  . PHE A 63  ? 1.4274 1.6956 1.1221 -0.3482 -0.2059 0.2156  278 PHE B CB  
449  C CG  . PHE A 63  ? 1.2911 1.5272 0.9458 -0.3329 -0.1957 0.1682  278 PHE B CG  
450  C CD1 . PHE A 63  ? 1.1204 1.3320 0.8114 -0.3196 -0.2327 0.1790  278 PHE B CD1 
451  C CD2 . PHE A 63  ? 1.2365 1.4674 0.8176 -0.3352 -0.1478 0.1139  278 PHE B CD2 
452  C CE1 . PHE A 63  ? 1.0721 1.2549 0.7227 -0.3082 -0.2234 0.1361  278 PHE B CE1 
453  C CE2 . PHE A 63  ? 1.2003 1.4004 0.7444 -0.3236 -0.1371 0.0715  278 PHE B CE2 
454  C CZ  . PHE A 63  ? 1.1068 1.2835 0.6828 -0.3106 -0.1761 0.0830  278 PHE B CZ  
455  N N   . PRO A 64  ? 2.2005 2.5156 2.0139 -0.3929 -0.2928 0.3653  279 PRO B N   
456  C CA  . PRO A 64  ? 2.1893 2.5251 2.0724 -0.4033 -0.3135 0.4238  279 PRO B CA  
457  C C   . PRO A 64  ? 2.1876 2.5344 2.0786 -0.3920 -0.2755 0.4027  279 PRO B C   
458  O O   . PRO A 64  ? 2.2023 2.5379 2.0657 -0.3672 -0.2346 0.3436  279 PRO B O   
459  C CB  . PRO A 64  ? 2.1494 2.4524 2.1463 -0.3677 -0.3423 0.4398  279 PRO B CB  
460  C CG  . PRO A 64  ? 2.0887 2.3675 2.0616 -0.3584 -0.3554 0.4163  279 PRO B CG  
461  C CD  . PRO A 64  ? 2.1295 2.4067 1.9983 -0.3598 -0.3156 0.3545  279 PRO B CD  
462  N N   . GLU A 65  ? 1.7251 2.0962 1.6595 -0.4112 -0.2900 0.4558  280 GLU B N   
463  C CA  . GLU A 65  ? 1.5732 1.9613 1.5142 -0.4079 -0.2577 0.4447  280 GLU B CA  
464  C C   . GLU A 65  ? 1.5017 1.8726 1.5598 -0.3767 -0.2671 0.4609  280 GLU B C   
465  O O   . GLU A 65  ? 1.4423 1.7850 1.5458 -0.3337 -0.2502 0.4157  280 GLU B O   
466  C CB  . GLU A 65  ? 1.4548 1.8889 1.3306 -0.4634 -0.2587 0.4859  280 GLU B CB  
467  C CG  . GLU A 65  ? 1.4333 1.8861 1.1990 -0.4851 -0.2161 0.4398  280 GLU B CG  
468  C CD  . GLU A 65  ? 1.3827 1.8215 1.1601 -0.4434 -0.1664 0.3754  280 GLU B CD  
469  O OE1 . GLU A 65  ? 1.3421 1.7744 1.2007 -0.4128 -0.1631 0.3778  280 GLU B OE1 
470  O OE2 . GLU A 65  ? 1.3535 1.7898 1.0612 -0.4433 -0.1290 0.3233  280 GLU B OE2 
471  N N   . LYS A 66  ? 1.4233 1.8106 1.5345 -0.3987 -0.2915 0.5233  281 LYS B N   
472  C CA  . LYS A 66  ? 1.3355 1.7050 1.5595 -0.3729 -0.2943 0.5352  281 LYS B CA  
473  C C   . LYS A 66  ? 1.3165 1.6435 1.6131 -0.3381 -0.3101 0.5186  281 LYS B C   
474  O O   . LYS A 66  ? 1.3407 1.6580 1.6324 -0.3453 -0.3393 0.5383  281 LYS B O   
475  C CB  . LYS A 66  ? 1.2530 1.6440 1.5257 -0.4052 -0.3206 0.6114  281 LYS B CB  
476  N N   . LYS A 67  ? 1.2695 1.5743 1.6305 -0.3031 -0.2894 0.4805  282 LYS B N   
477  C CA  . LYS A 67  ? 1.2231 1.4878 1.6607 -0.2707 -0.2968 0.4570  282 LYS B CA  
478  C C   . LYS A 67  ? 1.2018 1.4452 1.6012 -0.2607 -0.3116 0.4358  282 LYS B C   
479  O O   . LYS A 67  ? 1.1579 1.4023 1.5552 -0.2800 -0.3438 0.4774  282 LYS B O   
480  C CB  . LYS A 67  ? 1.1396 1.3911 1.6895 -0.2766 -0.3199 0.5081  282 LYS B CB  
481  C CG  . LYS A 67  ? 1.0073 1.2531 1.6365 -0.2650 -0.2970 0.4963  282 LYS B CG  
482  C CD  . LYS A 67  ? 0.9418 1.2180 1.5803 -0.2940 -0.2965 0.5465  282 LYS B CD  
483  C CE  . LYS A 67  ? 0.8628 1.1314 1.5891 -0.2867 -0.2757 0.5400  282 LYS B CE  
484  N NZ  . LYS A 67  ? 0.8087 1.0952 1.4937 -0.2746 -0.2397 0.4876  282 LYS B NZ  
485  N N   . GLY A 68  ? 1.2347 1.4600 1.6092 -0.2310 -0.2894 0.3735  283 GLY B N   
486  C CA  . GLY A 68  ? 1.1688 1.3698 1.5126 -0.2186 -0.3005 0.3481  283 GLY B CA  
487  C C   . GLY A 68  ? 1.2471 1.4635 1.4770 -0.2347 -0.2929 0.3335  283 GLY B C   
488  O O   . GLY A 68  ? 1.2203 1.4192 1.4178 -0.2315 -0.3051 0.3192  283 GLY B O   
489  N N   . GLY A 69  ? 1.3562 1.6049 1.5249 -0.2550 -0.2714 0.3360  284 GLY B N   
490  C CA  . GLY A 69  ? 1.3763 1.6369 1.4383 -0.2690 -0.2514 0.3081  284 GLY B CA  
491  C C   . GLY A 69  ? 1.1386 1.3849 1.1834 -0.2336 -0.2125 0.2426  284 GLY B C   
492  O O   . GLY A 69  ? 1.0565 1.2893 1.1670 -0.2012 -0.2034 0.2215  284 GLY B O   
493  N N   . LEU A 70  ? 1.1854 1.4370 1.1412 -0.2431 -0.1876 0.2111  285 LEU B N   
494  C CA  . LEU A 70  ? 1.0807 1.3165 1.0214 -0.2089 -0.1507 0.1514  285 LEU B CA  
495  C C   . LEU A 70  ? 1.0457 1.2997 1.0248 -0.1894 -0.1203 0.1372  285 LEU B C   
496  O O   . LEU A 70  ? 0.9957 1.2363 1.0223 -0.1525 -0.1087 0.1074  285 LEU B O   
497  C CB  . LEU A 70  ? 0.9962 1.2342 0.8379 -0.2273 -0.1244 0.1220  285 LEU B CB  
498  C CG  . LEU A 70  ? 1.0394 1.2502 0.8765 -0.1886 -0.0942 0.0642  285 LEU B CG  
499  C CD1 . LEU A 70  ? 0.8975 1.0758 0.8040 -0.1527 -0.1200 0.0568  285 LEU B CD1 
500  C CD2 . LEU A 70  ? 1.1006 1.3026 0.8464 -0.2086 -0.0747 0.0361  285 LEU B CD2 
501  N N   . ARG A 71  ? 1.0785 1.3665 1.0362 -0.2159 -0.1069 0.1588  286 ARG B N   
502  C CA  . ARG A 71  ? 1.0880 1.3973 1.0801 -0.1987 -0.0764 0.1448  286 ARG B CA  
503  C C   . ARG A 71  ? 1.0367 1.3413 1.1244 -0.1787 -0.0957 0.1606  286 ARG B C   
504  O O   . ARG A 71  ? 1.0152 1.3172 1.1459 -0.1466 -0.0797 0.1315  286 ARG B O   
505  C CB  . ARG A 71  ? 1.0961 1.4430 1.0450 -0.2343 -0.0583 0.1651  286 ARG B CB  
506  C CG  . ARG A 71  ? 1.0711 1.4439 1.0522 -0.2180 -0.0235 0.1494  286 ARG B CG  
507  C CD  . ARG A 71  ? 1.0850 1.4941 1.0217 -0.2556 -0.0055 0.1688  286 ARG B CD  
508  N NE  . ARG A 71  ? 1.1657 1.5779 1.0528 -0.3000 -0.0348 0.2082  286 ARG B NE  
509  C CZ  . ARG A 71  ? 1.1617 1.5919 0.9624 -0.3400 -0.0189 0.2077  286 ARG B CZ  
510  N NH1 . ARG A 71  ? 1.1427 1.5883 0.9002 -0.3426 0.0304  0.1698  286 ARG B NH1 
511  N NH2 . ARG A 71  ? 1.1698 1.6047 0.9290 -0.3807 -0.0522 0.2468  286 ARG B NH2 
512  N N   . GLU A 72  ? 1.2182 1.5223 1.3429 -0.1992 -0.1294 0.2072  287 GLU B N   
513  C CA  . GLU A 72  ? 1.1645 1.4645 1.3823 -0.1864 -0.1414 0.2215  287 GLU B CA  
514  C C   . GLU A 72  ? 1.1097 1.3779 1.3772 -0.1530 -0.1480 0.1900  287 GLU B C   
515  O O   . GLU A 72  ? 1.0622 1.3308 1.3978 -0.1389 -0.1443 0.1827  287 GLU B O   
516  C CB  . GLU A 72  ? 1.2255 1.5256 1.4807 -0.2142 -0.1751 0.2790  287 GLU B CB  
517  C CG  . GLU A 72  ? 1.3373 1.6720 1.5464 -0.2527 -0.1733 0.3178  287 GLU B CG  
518  C CD  . GLU A 72  ? 1.3486 1.6902 1.6263 -0.2720 -0.1958 0.3728  287 GLU B CD  
519  O OE1 . GLU A 72  ? 1.3435 1.6597 1.7060 -0.2563 -0.2118 0.3798  287 GLU B OE1 
520  O OE2 . GLU A 72  ? 1.2765 1.6480 1.5254 -0.3043 -0.1955 0.4085  287 GLU B OE2 
521  N N   . LEU A 73  ? 1.0548 1.2967 1.2877 -0.1438 -0.1574 0.1709  288 LEU B N   
522  C CA  . LEU A 73  ? 0.9515 1.1640 1.2208 -0.1131 -0.1607 0.1366  288 LEU B CA  
523  C C   . LEU A 73  ? 0.9326 1.1554 1.1878 -0.0865 -0.1271 0.0925  288 LEU B C   
524  O O   . LEU A 73  ? 0.9410 1.1621 1.2504 -0.0662 -0.1228 0.0734  288 LEU B O   
525  C CB  . LEU A 73  ? 0.8969 1.0793 1.1320 -0.1140 -0.1819 0.1327  288 LEU B CB  
526  C CG  . LEU A 73  ? 0.8757 1.0373 1.1697 -0.1237 -0.2187 0.1664  288 LEU B CG  
527  C CD1 . LEU A 73  ? 0.8077 0.9466 1.0636 -0.1283 -0.2405 0.1672  288 LEU B CD1 
528  C CD2 . LEU A 73  ? 0.8586 1.0028 1.2357 -0.1018 -0.2185 0.1472  288 LEU B CD2 
529  N N   . TYR A 74  ? 0.8994 1.1348 1.0849 -0.0886 -0.1019 0.0769  289 TYR B N   
530  C CA  . TYR A 74  ? 0.8476 1.0963 1.0268 -0.0634 -0.0668 0.0408  289 TYR B CA  
531  C C   . TYR A 74  ? 0.9240 1.2076 1.1553 -0.0583 -0.0516 0.0466  289 TYR B C   
532  O O   . TYR A 74  ? 0.9627 1.2594 1.2156 -0.0336 -0.0305 0.0216  289 TYR B O   
533  C CB  . TYR A 74  ? 0.8618 1.1183 0.9626 -0.0727 -0.0374 0.0262  289 TYR B CB  
534  C CG  . TYR A 74  ? 0.8540 1.1063 0.9461 -0.0421 -0.0047 -0.0152 289 TYR B CG  
535  C CD1 . TYR A 74  ? 0.8616 1.1450 0.9849 -0.0248 0.0263  -0.0258 289 TYR B CD1 
536  C CD2 . TYR A 74  ? 0.8308 1.0497 0.8876 -0.0309 -0.0042 -0.0411 289 TYR B CD2 
537  C CE1 . TYR A 74  ? 0.8643 1.1458 0.9899 0.0044  0.0561  -0.0579 289 TYR B CE1 
538  C CE2 . TYR A 74  ? 0.8314 1.0447 0.8862 -0.0024 0.0269  -0.0760 289 TYR B CE2 
539  C CZ  . TYR A 74  ? 0.8510 1.0959 0.9434 0.0159  0.0567  -0.0827 289 TYR B CZ  
540  O OH  . TYR A 74  ? 0.8921 1.1327 0.9926 0.0457  0.0872  -0.1122 289 TYR B OH  
541  N N   . ASP A 75  ? 0.9552 1.2567 1.2086 -0.0822 -0.0617 0.0810  290 ASP B N   
542  C CA  . ASP A 75  ? 0.9389 1.2740 1.2429 -0.0796 -0.0476 0.0854  290 ASP B CA  
543  C C   . ASP A 75  ? 0.9074 1.2328 1.2870 -0.0697 -0.0646 0.0824  290 ASP B C   
544  O O   . ASP A 75  ? 0.8626 1.2159 1.2834 -0.0621 -0.0506 0.0739  290 ASP B O   
545  C CB  . ASP A 75  ? 1.0237 1.3833 1.3218 -0.1103 -0.0474 0.1216  290 ASP B CB  
546  C CG  . ASP A 75  ? 1.0527 1.4255 1.2721 -0.1284 -0.0287 0.1243  290 ASP B CG  
547  O OD1 . ASP A 75  ? 1.1040 1.4649 1.2843 -0.1541 -0.0480 0.1486  290 ASP B OD1 
548  O OD2 . ASP A 75  ? 1.0872 1.4841 1.2858 -0.1190 0.0064  0.1023  290 ASP B OD2 
549  N N   . ARG A 76  ? 1.0352 1.3243 1.4355 -0.0726 -0.0930 0.0886  291 ARG B N   
550  C CA  . ARG A 76  ? 0.9840 1.2598 1.4520 -0.0639 -0.1038 0.0757  291 ARG B CA  
551  C C   . ARG A 76  ? 0.9336 1.2040 1.3961 -0.0368 -0.0953 0.0369  291 ARG B C   
552  O O   . ARG A 76  ? 0.8649 1.1413 1.3772 -0.0311 -0.0951 0.0214  291 ARG B O   
553  C CB  . ARG A 76  ? 0.9980 1.2359 1.4975 -0.0757 -0.1336 0.0944  291 ARG B CB  
554  C CG  . ARG A 76  ? 1.0705 1.3087 1.5480 -0.1001 -0.1471 0.1372  291 ARG B CG  
555  C CD  . ARG A 76  ? 1.1538 1.3714 1.6992 -0.1169 -0.1709 0.1704  291 ARG B CD  
556  N NE  . ARG A 76  ? 1.2410 1.4626 1.7586 -0.1403 -0.1877 0.2162  291 ARG B NE  
557  C CZ  . ARG A 76  ? 1.2774 1.4798 1.8402 -0.1549 -0.2141 0.2545  291 ARG B CZ  
558  N NH1 . ARG A 76  ? 1.3377 1.5107 1.9800 -0.1479 -0.2238 0.2496  291 ARG B NH1 
559  N NH2 . ARG A 76  ? 1.2641 1.4793 1.7947 -0.1793 -0.2301 0.3002  291 ARG B NH2 
560  N N   . GLY A 77  ? 0.8576 1.1187 1.2608 -0.0228 -0.0866 0.0212  292 GLY B N   
561  C CA  . GLY A 77  ? 0.7701 1.0228 1.1683 0.0031  -0.0792 -0.0118 292 GLY B CA  
562  C C   . GLY A 77  ? 0.7572 0.9701 1.1771 0.0063  -0.1046 -0.0227 292 GLY B C   
563  O O   . GLY A 77  ? 0.7596 0.9501 1.1974 -0.0103 -0.1266 -0.0038 292 GLY B O   
564  N N   . PRO A 78  ? 0.7583 0.9624 1.1807 0.0273  -0.1016 -0.0517 293 PRO B N   
565  C CA  . PRO A 78  ? 0.6892 0.9175 1.0986 0.0497  -0.0772 -0.0705 293 PRO B CA  
566  C C   . PRO A 78  ? 0.6593 0.8750 1.0031 0.0587  -0.0608 -0.0773 293 PRO B C   
567  O O   . PRO A 78  ? 0.7086 0.8872 1.0169 0.0562  -0.0741 -0.0826 293 PRO B O   
568  C CB  . PRO A 78  ? 0.7034 0.9162 1.1390 0.0629  -0.0883 -0.0942 293 PRO B CB  
569  C CG  . PRO A 78  ? 0.6460 0.8107 1.0727 0.0545  -0.1134 -0.0962 293 PRO B CG  
570  C CD  . PRO A 78  ? 0.6941 0.8595 1.1345 0.0300  -0.1238 -0.0663 293 PRO B CD  
571  N N   . PRO A 79  ? 0.7263 1.0277 0.8132 -0.0690 -0.0685 0.0396  294 PRO B N   
572  C CA  . PRO A 79  ? 0.7275 1.0485 0.8264 -0.0331 -0.0584 0.0365  294 PRO B CA  
573  C C   . PRO A 79  ? 0.7363 0.9854 0.8047 0.0055  -0.0627 0.0345  294 PRO B C   
574  O O   . PRO A 79  ? 0.7409 0.9616 0.8013 0.0215  -0.0495 0.0340  294 PRO B O   
575  C CB  . PRO A 79  ? 0.6733 1.1048 0.8151 -0.0165 -0.0670 0.0278  294 PRO B CB  
576  C CG  . PRO A 79  ? 0.6817 1.1609 0.8381 -0.0592 -0.0759 0.0301  294 PRO B CG  
577  C CD  . PRO A 79  ? 0.7388 1.1277 0.8551 -0.0784 -0.0840 0.0353  294 PRO B CD  
578  N N   . HIS A 80  ? 0.7252 0.9411 0.7716 0.0158  -0.0813 0.0343  295 HIS B N   
579  C CA  . HIS A 80  ? 0.7230 0.8694 0.7343 0.0470  -0.0879 0.0345  295 HIS B CA  
580  C C   . HIS A 80  ? 0.7625 0.8248 0.7404 0.0319  -0.0722 0.0381  295 HIS B C   
581  O O   . HIS A 80  ? 0.7814 0.7863 0.7289 0.0519  -0.0740 0.0385  295 HIS B O   
582  C CB  . HIS A 80  ? 0.7721 0.9071 0.7631 0.0542  -0.1135 0.0364  295 HIS B CB  
583  C CG  . HIS A 80  ? 0.8587 0.9470 0.8198 0.0170  -0.1134 0.0395  295 HIS B CG  
584  N ND1 . HIS A 80  ? 0.8667 0.9950 0.8409 -0.0150 -0.1197 0.0380  295 HIS B ND1 
585  C CD2 . HIS A 80  ? 0.8608 0.8689 0.7791 0.0059  -0.1070 0.0410  295 HIS B CD2 
586  C CE1 . HIS A 80  ? 0.8637 0.9339 0.8033 -0.0418 -0.1169 0.0370  295 HIS B CE1 
587  N NE2 . HIS A 80  ? 0.8742 0.8754 0.7815 -0.0291 -0.1084 0.0384  295 HIS B NE2 
588  N N   . ALA A 81  ? 0.7551 0.8085 0.7378 -0.0025 -0.0581 0.0404  296 ALA B N   
589  C CA  . ALA A 81  ? 0.7697 0.7536 0.7287 -0.0133 -0.0443 0.0416  296 ALA B CA  
590  C C   . ALA A 81  ? 0.7698 0.7516 0.7381 -0.0042 -0.0287 0.0436  296 ALA B C   
591  O O   . ALA A 81  ? 0.7461 0.6790 0.7003 -0.0119 -0.0182 0.0446  296 ALA B O   
592  C CB  . ALA A 81  ? 0.8116 0.7774 0.7691 -0.0500 -0.0402 0.0414  296 ALA B CB  
593  N N   . PHE A 82  ? 0.7878 0.8258 0.7794 0.0123  -0.0270 0.0424  297 PHE B N   
594  C CA  . PHE A 82  ? 0.7293 0.7763 0.7288 0.0155  -0.0120 0.0437  297 PHE B CA  
595  C C   . PHE A 82  ? 0.7289 0.7571 0.7147 0.0513  -0.0118 0.0365  297 PHE B C   
596  O O   . PHE A 82  ? 0.7207 0.7697 0.7096 0.0798  -0.0232 0.0294  297 PHE B O   
597  C CB  . PHE A 82  ? 0.6873 0.8145 0.7192 0.0019  -0.0067 0.0453  297 PHE B CB  
598  C CG  . PHE A 82  ? 0.7178 0.8473 0.7555 -0.0401 -0.0051 0.0548  297 PHE B CG  
599  C CD1 . PHE A 82  ? 0.7568 0.8956 0.7981 -0.0570 -0.0169 0.0539  297 PHE B CD1 
600  C CD2 . PHE A 82  ? 0.7488 0.8638 0.7838 -0.0636 0.0058  0.0651  297 PHE B CD2 
601  C CE1 . PHE A 82  ? 0.7955 0.9254 0.8372 -0.0973 -0.0166 0.0609  297 PHE B CE1 
602  C CE2 . PHE A 82  ? 0.7645 0.8678 0.7994 -0.1018 0.0043  0.0746  297 PHE B CE2 
603  C CZ  . PHE A 82  ? 0.8117 0.9201 0.8497 -0.1188 -0.0063 0.0714  297 PHE B CZ  
604  N N   . PHE A 83  ? 0.7011 0.6873 0.6708 0.0502  -0.0008 0.0379  298 PHE B N   
605  C CA  . PHE A 83  ? 0.7452 0.6995 0.6945 0.0771  0.0000  0.0307  298 PHE B CA  
606  C C   . PHE A 83  ? 0.7504 0.7126 0.7019 0.0725  0.0146  0.0306  298 PHE B C   
607  O O   . PHE A 83  ? 0.7312 0.6900 0.6874 0.0472  0.0221  0.0398  298 PHE B O   
608  C CB  . PHE A 83  ? 0.7921 0.6702 0.7058 0.0762  -0.0046 0.0318  298 PHE B CB  
609  C CG  . PHE A 83  ? 0.8084 0.6712 0.7090 0.0797  -0.0201 0.0329  298 PHE B CG  
610  C CD1 . PHE A 83  ? 0.7983 0.6601 0.7015 0.0542  -0.0216 0.0373  298 PHE B CD1 
611  C CD2 . PHE A 83  ? 0.7876 0.6360 0.6717 0.1089  -0.0351 0.0292  298 PHE B CD2 
612  C CE1 . PHE A 83  ? 0.7975 0.6502 0.6860 0.0545  -0.0366 0.0384  298 PHE B CE1 
613  C CE2 . PHE A 83  ? 0.8800 0.7156 0.7493 0.1113  -0.0526 0.0330  298 PHE B CE2 
614  C CZ  . PHE A 83  ? 0.8906 0.7309 0.7612 0.0822  -0.0528 0.0378  298 PHE B CZ  
615  N N   . LEU A 84  ? 0.7559 0.7243 0.7009 0.0984  0.0166  0.0196  299 LEU B N   
616  C CA  . LEU A 84  ? 0.7513 0.7166 0.6880 0.0956  0.0287  0.0173  299 LEU B CA  
617  C C   . LEU A 84  ? 0.7885 0.6838 0.6908 0.1073  0.0256  0.0117  299 LEU B C   
618  O O   . LEU A 84  ? 0.7824 0.6486 0.6680 0.1317  0.0154  0.0032  299 LEU B O   
619  C CB  . LEU A 84  ? 0.7316 0.7629 0.6848 0.1117  0.0363  0.0053  299 LEU B CB  
620  C CG  . LEU A 84  ? 0.7602 0.7898 0.6974 0.1179  0.0473  -0.0041 299 LEU B CG  
621  C CD1 . LEU A 84  ? 0.7305 0.7621 0.6642 0.0846  0.0564  0.0109  299 LEU B CD1 
622  C CD2 . LEU A 84  ? 0.7751 0.8761 0.7305 0.1399  0.0543  -0.0221 299 LEU B CD2 
623  N N   . VAL A 85  ? 0.7799 0.6466 0.6705 0.0881  0.0323  0.0175  300 VAL B N   
624  C CA  . VAL A 85  ? 0.8552 0.6639 0.7141 0.0909  0.0315  0.0120  300 VAL B CA  
625  C C   . VAL A 85  ? 0.8480 0.6709 0.7020 0.0886  0.0404  0.0073  300 VAL B C   
626  O O   . VAL A 85  ? 0.8175 0.6621 0.6837 0.0687  0.0461  0.0173  300 VAL B O   
627  C CB  . VAL A 85  ? 0.8425 0.6114 0.6931 0.0690  0.0307  0.0202  300 VAL B CB  
628  C CG1 . VAL A 85  ? 0.8042 0.5309 0.6276 0.0628  0.0333  0.0151  300 VAL B CG1 
629  C CG2 . VAL A 85  ? 0.8076 0.5529 0.6492 0.0719  0.0215  0.0216  300 VAL B CG2 
630  N N   . LYS A 86  ? 0.8971 0.7043 0.7302 0.1094  0.0399  -0.0081 301 LYS B N   
631  C CA  . LYS A 86  ? 0.8792 0.6940 0.6996 0.1068  0.0478  -0.0162 301 LYS B CA  
632  C C   . LYS A 86  ? 0.8966 0.6506 0.6862 0.0948  0.0449  -0.0176 301 LYS B C   
633  O O   . LYS A 86  ? 0.9266 0.6257 0.6906 0.1033  0.0371  -0.0235 301 LYS B O   
634  C CB  . LYS A 86  ? 0.9141 0.7487 0.7290 0.1368  0.0500  -0.0371 301 LYS B CB  
635  C CG  . LYS A 86  ? 0.9416 0.7621 0.7297 0.1371  0.0559  -0.0514 301 LYS B CG  
636  C CD  . LYS A 86  ? 1.0161 0.8916 0.8123 0.1592  0.0649  -0.0712 301 LYS B CD  
637  C CE  . LYS A 86  ? 1.0166 0.8952 0.7878 0.1493  0.0740  -0.0827 301 LYS B CE  
638  N NZ  . LYS A 86  ? 1.0009 0.8553 0.7615 0.1142  0.0718  -0.0631 301 LYS B NZ  
639  N N   . PHE A 87  ? 0.8780 0.6427 0.6688 0.0729  0.0495  -0.0111 302 PHE B N   
640  C CA  . PHE A 87  ? 0.9287 0.6513 0.6971 0.0565  0.0472  -0.0124 302 PHE B CA  
641  C C   . PHE A 87  ? 0.9475 0.6668 0.6907 0.0559  0.0500  -0.0258 302 PHE B C   
642  O O   . PHE A 87  ? 0.8562 0.6199 0.6064 0.0574  0.0556  -0.0272 302 PHE B O   
643  C CB  . PHE A 87  ? 0.8678 0.6076 0.6597 0.0336  0.0474  0.0033  302 PHE B CB  
644  C CG  . PHE A 87  ? 0.8886 0.6073 0.6895 0.0277  0.0449  0.0092  302 PHE B CG  
645  C CD1 . PHE A 87  ? 0.9593 0.6294 0.7327 0.0272  0.0419  0.0023  302 PHE B CD1 
646  C CD2 . PHE A 87  ? 0.8658 0.6092 0.6979 0.0204  0.0450  0.0213  302 PHE B CD2 
647  C CE1 . PHE A 87  ? 0.9141 0.5689 0.6911 0.0181  0.0410  0.0070  302 PHE B CE1 
648  C CE2 . PHE A 87  ? 0.8762 0.6022 0.7143 0.0145  0.0442  0.0228  302 PHE B CE2 
649  C CZ  . PHE A 87  ? 0.8976 0.5833 0.7082 0.0126  0.0432  0.0155  302 PHE B CZ  
650  N N   . TRP A 88  ? 0.9603 0.6262 0.6700 0.0497  0.0460  -0.0359 303 TRP B N   
651  C CA  . TRP A 88  ? 0.9640 0.6218 0.6480 0.0376  0.0470  -0.0468 303 TRP B CA  
652  C C   . TRP A 88  ? 0.9277 0.5830 0.6163 0.0076  0.0443  -0.0370 303 TRP B C   
653  O O   . TRP A 88  ? 0.9859 0.5980 0.6570 -0.0049 0.0412  -0.0389 303 TRP B O   
654  C CB  . TRP A 88  ? 1.0602 0.6571 0.7002 0.0511  0.0433  -0.0681 303 TRP B CB  
655  C CG  . TRP A 88  ? 1.1031 0.7188 0.7449 0.0836  0.0468  -0.0826 303 TRP B CG  
656  C CD1 . TRP A 88  ? 1.0149 0.6656 0.6507 0.0907  0.0545  -0.0978 303 TRP B CD1 
657  C CD2 . TRP A 88  ? 1.0990 0.7118 0.7533 0.1140  0.0434  -0.0846 303 TRP B CD2 
658  N NE1 . TRP A 88  ? 0.9919 0.6650 0.6382 0.1244  0.0581  -0.1115 303 TRP B NE1 
659  C CE2 . TRP A 88  ? 1.0500 0.7010 0.7095 0.1406  0.0501  -0.1035 303 TRP B CE2 
660  C CE3 . TRP A 88  ? 1.0392 0.6246 0.6997 0.1207  0.0348  -0.0732 303 TRP B CE3 
661  C CZ2 . TRP A 88  ? 1.0679 0.7354 0.7447 0.1762  0.0476  -0.1122 303 TRP B CZ2 
662  C CZ3 . TRP A 88  ? 1.0677 0.6638 0.7413 0.1547  0.0300  -0.0792 303 TRP B CZ3 
663  C CH2 . TRP A 88  ? 1.1577 0.7970 0.8422 0.1834  0.0361  -0.0990 303 TRP B CH2 
664  N N   . ALA A 89  ? 0.8458 0.5494 0.5572 -0.0045 0.0448  -0.0267 304 ALA B N   
665  C CA  . ALA A 89  ? 0.9462 0.6605 0.6739 -0.0267 0.0408  -0.0179 304 ALA B CA  
666  C C   . ALA A 89  ? 0.9695 0.6637 0.6670 -0.0471 0.0376  -0.0303 304 ALA B C   
667  O O   . ALA A 89  ? 1.0043 0.6996 0.6771 -0.0480 0.0370  -0.0404 304 ALA B O   
668  C CB  . ALA A 89  ? 0.9218 0.6891 0.6838 -0.0290 0.0377  -0.0008 304 ALA B CB  
669  N N   . ASP A 90  ? 1.0069 0.6850 0.7043 -0.0666 0.0364  -0.0313 305 ASP B N   
670  C CA  . ASP A 90  ? 1.0474 0.7219 0.7246 -0.0936 0.0326  -0.0408 305 ASP B CA  
671  C C   . ASP A 90  ? 1.0214 0.7604 0.7367 -0.1019 0.0267  -0.0308 305 ASP B C   
672  O O   . ASP A 90  ? 0.9623 0.7305 0.7164 -0.1034 0.0262  -0.0220 305 ASP B O   
673  C CB  . ASP A 90  ? 1.0706 0.7081 0.7305 -0.1161 0.0345  -0.0461 305 ASP B CB  
674  C CG  . ASP A 90  ? 1.1609 0.7932 0.7954 -0.1503 0.0308  -0.0574 305 ASP B CG  
675  O OD1 . ASP A 90  ? 1.1512 0.8303 0.8004 -0.1584 0.0254  -0.0579 305 ASP B OD1 
676  O OD2 . ASP A 90  ? 1.2234 0.8025 0.8196 -0.1718 0.0319  -0.0649 305 ASP B OD2 
677  N N   . LEU A 91  ? 1.0609 0.8214 0.7640 -0.1054 0.0209  -0.0327 306 LEU B N   
678  C CA  . LEU A 91  ? 1.0823 0.9008 0.8160 -0.1118 0.0103  -0.0208 306 LEU B CA  
679  C C   . LEU A 91  ? 1.1661 1.0016 0.8863 -0.1394 0.0018  -0.0306 306 LEU B C   
680  O O   . LEU A 91  ? 1.1402 1.0176 0.8680 -0.1439 -0.0100 -0.0235 306 LEU B O   
681  C CB  . LEU A 91  ? 1.0290 0.8717 0.7613 -0.0981 0.0067  -0.0092 306 LEU B CB  
682  C CG  . LEU A 91  ? 1.0173 0.8578 0.7589 -0.0759 0.0136  0.0012  306 LEU B CG  
683  C CD1 . LEU A 91  ? 1.0552 0.9335 0.7944 -0.0773 0.0061  0.0153  306 LEU B CD1 
684  C CD2 . LEU A 91  ? 0.9840 0.8278 0.7668 -0.0666 0.0137  0.0137  306 LEU B CD2 
685  N N   . ASN A 92  ? 1.2078 1.0129 0.9065 -0.1612 0.0059  -0.0455 307 ASN B N   
686  C CA  . ASN A 92  ? 1.2642 1.0889 0.9502 -0.1933 -0.0021 -0.0560 307 ASN B CA  
687  C C   . ASN A 92  ? 1.2109 1.0604 0.9278 -0.2128 0.0001  -0.0578 307 ASN B C   
688  O O   . ASN A 92  ? 1.2259 1.0332 0.9141 -0.2346 0.0080  -0.0686 307 ASN B O   
689  C CB  . ASN A 92  ? 1.4195 1.1831 1.0416 -0.2092 0.0005  -0.0754 307 ASN B CB  
690  C CG  . ASN A 92  ? 1.4644 1.2497 1.0669 -0.2443 -0.0098 -0.0869 307 ASN B CG  
691  O OD1 . ASN A 92  ? 1.3896 1.2347 1.0125 -0.2462 -0.0215 -0.0800 307 ASN B OD1 
692  N ND2 . ASN A 92  ? 1.4963 1.2302 1.0556 -0.2746 -0.0074 -0.1036 307 ASN B ND2 
693  N N   . TRP A 93  ? 1.1997 1.1172 0.9732 -0.2050 -0.0074 -0.0476 308 TRP B N   
694  C CA  . TRP A 93  ? 1.1920 1.1498 1.0051 -0.2186 -0.0035 -0.0525 308 TRP B CA  
695  C C   . TRP A 93  ? 1.1929 1.2273 1.0388 -0.2355 -0.0179 -0.0561 308 TRP B C   
696  O O   . TRP A 93  ? 1.2296 1.2665 1.0447 -0.2622 -0.0254 -0.0644 308 TRP B O   
697  C CB  . TRP A 93  ? 1.1392 1.1119 0.9993 -0.1883 0.0016  -0.0423 308 TRP B CB  
698  C CG  . TRP A 93  ? 1.1131 1.1212 1.0124 -0.1567 -0.0126 -0.0253 308 TRP B CG  
699  C CD1 . TRP A 93  ? 1.0735 1.1449 1.0287 -0.1452 -0.0251 -0.0212 308 TRP B CD1 
700  C CD2 . TRP A 93  ? 1.1446 1.1241 1.0281 -0.1335 -0.0165 -0.0096 308 TRP B CD2 
701  N NE1 . TRP A 93  ? 1.1029 1.1758 1.0722 -0.1174 -0.0390 -0.0014 308 TRP B NE1 
702  C CE2 . TRP A 93  ? 1.1309 1.1510 1.0561 -0.1132 -0.0326 0.0063  308 TRP B CE2 
703  C CE3 . TRP A 93  ? 1.1566 1.0837 0.9957 -0.1282 -0.0084 -0.0085 308 TRP B CE3 
704  C CZ2 . TRP A 93  ? 1.1058 1.1116 1.0234 -0.0945 -0.0400 0.0259  308 TRP B CZ2 
705  C CZ3 . TRP A 93  ? 1.1523 1.0784 0.9911 -0.1077 -0.0136 0.0079  308 TRP B CZ3 
706  C CH2 . TRP A 93  ? 1.1110 1.0743 0.9857 -0.0947 -0.0287 0.0260  308 TRP B CH2 
707  N N   . SER A 108 ? 1.2728 1.6259 1.4659 -0.0438 -0.1567 0.0265  323 SER B N   
708  C CA  . SER A 108 ? 1.2656 1.6860 1.4863 -0.0671 -0.1476 -0.0011 323 SER B CA  
709  C C   . SER A 108 ? 1.2254 1.6900 1.5142 -0.0442 -0.1388 -0.0211 323 SER B C   
710  O O   . SER A 108 ? 1.1961 1.7252 1.5139 -0.0642 -0.1275 -0.0463 323 SER B O   
711  C CB  . SER A 108 ? 1.3616 1.7454 1.5257 -0.1100 -0.1188 -0.0156 323 SER B CB  
712  O OG  . SER A 108 ? 1.3698 1.7151 1.4719 -0.1286 -0.1252 -0.0030 323 SER B OG  
713  N N   . GLY A 109 ? 1.1073 1.5369 1.4185 -0.0051 -0.1430 -0.0114 324 GLY B N   
714  C CA  . GLY A 109 ? 0.9512 1.4224 1.3309 0.0268  -0.1413 -0.0303 324 GLY B CA  
715  C C   . GLY A 109 ? 0.9583 1.4352 1.3455 0.0116  -0.1042 -0.0590 324 GLY B C   
716  O O   . GLY A 109 ? 0.8805 1.4355 1.3224 0.0143  -0.0972 -0.0862 324 GLY B O   
717  N N   . GLY A 110 ? 0.8943 1.2937 1.2275 -0.0045 -0.0811 -0.0537 325 GLY B N   
718  C CA  . GLY A 110 ? 0.7419 1.1350 1.0706 -0.0210 -0.0481 -0.0762 325 GLY B CA  
719  C C   . GLY A 110 ? 0.6916 1.0145 1.0087 0.0021  -0.0391 -0.0696 325 GLY B C   
720  O O   . GLY A 110 ? 0.7763 1.0547 1.0890 0.0287  -0.0577 -0.0474 325 GLY B O   
721  N N   . PHE A 111 ? 0.4671 1.2857 0.7388 0.1541  -0.0185 -0.0415 326 PHE B N   
722  C CA  . PHE A 111 ? 0.4447 1.1929 0.6977 0.1732  -0.0074 -0.0391 326 PHE B CA  
723  C C   . PHE A 111 ? 0.4240 1.0787 0.6491 0.1447  -0.0044 -0.0301 326 PHE B C   
724  O O   . PHE A 111 ? 0.4395 1.0910 0.6648 0.1024  0.0001  -0.0294 326 PHE B O   
725  C CB  . PHE A 111 ? 0.4149 1.2093 0.6832 0.1699  0.0083  -0.0489 326 PHE B CB  
726  C CG  . PHE A 111 ? 0.4128 1.1300 0.6572 0.1754  0.0194  -0.0473 326 PHE B CG  
727  C CD1 . PHE A 111 ? 0.4325 1.1059 0.6646 0.2209  0.0190  -0.0501 326 PHE B CD1 
728  C CD2 . PHE A 111 ? 0.4100 1.0917 0.6412 0.1343  0.0278  -0.0422 326 PHE B CD2 
729  C CE1 . PHE A 111 ? 0.4398 1.0423 0.6489 0.2220  0.0276  -0.0502 326 PHE B CE1 
730  C CE2 . PHE A 111 ? 0.4164 1.0315 0.6254 0.1387  0.0354  -0.0408 326 PHE B CE2 
731  C CZ  . PHE A 111 ? 0.4377 1.0162 0.6366 0.1810  0.0357  -0.0461 326 PHE B CZ  
732  N N   . TYR A 112 ? 0.4535 1.0324 0.6550 0.1684  -0.0068 -0.0232 327 TYR B N   
733  C CA  . TYR A 112 ? 0.4961 0.9920 0.6742 0.1478  -0.0039 -0.0161 327 TYR B CA  
734  C C   . TYR A 112 ? 0.4798 0.9311 0.6479 0.1552  0.0071  -0.0170 327 TYR B C   
735  O O   . TYR A 112 ? 0.5031 0.9479 0.6680 0.1896  0.0089  -0.0201 327 TYR B O   
736  C CB  . TYR A 112 ? 0.4912 0.9386 0.6489 0.1633  -0.0127 -0.0079 327 TYR B CB  
737  C CG  . TYR A 112 ? 0.4997 0.9809 0.6603 0.1487  -0.0236 -0.0082 327 TYR B CG  
738  C CD1 . TYR A 112 ? 0.4603 1.0141 0.6365 0.1649  -0.0339 -0.0110 327 TYR B CD1 
739  C CD2 . TYR A 112 ? 0.4883 0.9324 0.6367 0.1193  -0.0245 -0.0081 327 TYR B CD2 
740  C CE1 . TYR A 112 ? 0.4889 1.0770 0.6660 0.1485  -0.0452 -0.0132 327 TYR B CE1 
741  C CE2 . TYR A 112 ? 0.4559 0.9292 0.6038 0.1046  -0.0344 -0.0121 327 TYR B CE2 
742  C CZ  . TYR A 112 ? 0.4900 1.0351 0.6511 0.1175  -0.0450 -0.0144 327 TYR B CZ  
743  O OH  . TYR A 112 ? 0.5938 1.1724 0.7534 0.1004  -0.0563 -0.0202 327 TYR B OH  
744  N N   . GLY A 113 ? 0.4212 0.8381 0.5820 0.1246  0.0128  -0.0146 328 GLY B N   
745  C CA  . GLY A 113 ? 0.4449 0.8306 0.5962 0.1282  0.0219  -0.0165 328 GLY B CA  
746  C C   . GLY A 113 ? 0.4946 0.8172 0.6311 0.1056  0.0227  -0.0101 328 GLY B C   
747  O O   . GLY A 113 ? 0.5455 0.8535 0.6818 0.0820  0.0180  -0.0054 328 GLY B O   
748  N N   . VAL A 114 ? 0.5262 0.8122 0.6504 0.1148  0.0280  -0.0118 329 VAL B N   
749  C CA  . VAL A 114 ? 0.5826 0.8173 0.6948 0.0972  0.0284  -0.0072 329 VAL B CA  
750  C C   . VAL A 114 ? 0.6362 0.8823 0.7425 0.0907  0.0352  -0.0111 329 VAL B C   
751  O O   . VAL A 114 ? 0.6167 0.8851 0.7218 0.1108  0.0413  -0.0210 329 VAL B O   
752  C CB  . VAL A 114 ? 0.6194 0.7966 0.7190 0.1122  0.0267  -0.0058 329 VAL B CB  
753  C CG1 . VAL A 114 ? 0.6344 0.7713 0.7289 0.0929  0.0250  -0.0014 329 VAL B CG1 
754  C CG2 . VAL A 114 ? 0.6379 0.8119 0.7378 0.1246  0.0216  -0.0021 329 VAL B CG2 
755  N N   . SER A 115 ? 0.6210 0.8517 0.7217 0.0642  0.0336  -0.0039 330 SER B N   
756  C CA  . SER A 115 ? 0.6554 0.8938 0.7444 0.0540  0.0384  -0.0046 330 SER B CA  
757  C C   . SER A 115 ? 0.6849 0.8716 0.7619 0.0438  0.0323  0.0019  330 SER B C   
758  O O   . SER A 115 ? 0.6999 0.8616 0.7806 0.0303  0.0245  0.0110  330 SER B O   
759  C CB  . SER A 115 ? 0.6064 0.8908 0.6979 0.0272  0.0413  0.0018  330 SER B CB  
760  O OG  . SER A 115 ? 0.5668 0.9157 0.6711 0.0360  0.0492  -0.0071 330 SER B OG  
761  N N   . SER A 116 ? 0.7385 0.9116 0.8017 0.0509  0.0349  -0.0047 331 SER B N   
762  C CA  . SER A 116 ? 0.7556 0.8916 0.8087 0.0403  0.0277  0.0006  331 SER B CA  
763  C C   . SER A 116 ? 0.7999 0.9543 0.8344 0.0291  0.0301  0.0002  331 SER B C   
764  O O   . SER A 116 ? 0.8270 1.0134 0.8544 0.0377  0.0399  -0.0115 331 SER B O   
765  C CB  . SER A 116 ? 0.7806 0.8779 0.8319 0.0554  0.0264  -0.0075 331 SER B CB  
766  O OG  . SER A 116 ? 0.8414 0.9224 0.9050 0.0645  0.0252  -0.0058 331 SER B OG  
767  N N   . GLN A 117 ? 0.7563 0.8923 0.7816 0.0118  0.0205  0.0123  332 GLN B N   
768  C CA  . GLN A 117 ? 0.7068 0.8576 0.7088 -0.0004 0.0205  0.0144  332 GLN B CA  
769  C C   . GLN A 117 ? 0.7020 0.8194 0.6963 -0.0057 0.0067  0.0209  332 GLN B C   
770  O O   . GLN A 117 ? 0.7067 0.7989 0.7121 -0.0103 -0.0044 0.0333  332 GLN B O   
771  C CB  . GLN A 117 ? 0.7553 0.9366 0.7492 -0.0234 0.0225  0.0294  332 GLN B CB  
772  C CG  . GLN A 117 ? 0.7575 0.9656 0.7227 -0.0378 0.0261  0.0320  332 GLN B CG  
773  C CD  . GLN A 117 ? 0.8044 1.0642 0.7655 -0.0553 0.0379  0.0371  332 GLN B CD  
774  O OE1 . GLN A 117 ? 0.8472 1.1229 0.8293 -0.0567 0.0419  0.0379  332 GLN B OE1 
775  N NE2 . GLN A 117 ? 0.8165 1.1082 0.7500 -0.0708 0.0439  0.0399  332 GLN B NE2 
776  N N   . TYR A 118 ? 0.6855 0.8054 0.6614 -0.0040 0.0069  0.0105  333 TYR B N   
777  C CA  . TYR A 118 ? 0.7480 0.8467 0.7167 -0.0092 -0.0073 0.0142  333 TYR B CA  
778  C C   . TYR A 118 ? 0.7852 0.9056 0.7217 -0.0225 -0.0098 0.0167  333 TYR B C   
779  O O   . TYR A 118 ? 0.7840 0.9344 0.7037 -0.0234 0.0032  0.0066  333 TYR B O   
780  C CB  . TYR A 118 ? 0.7238 0.8000 0.7012 0.0036  -0.0070 -0.0040 333 TYR B CB  
781  C CG  . TYR A 118 ? 0.7813 0.8385 0.7839 0.0162  -0.0021 -0.0070 333 TYR B CG  
782  C CD1 . TYR A 118 ? 0.7816 0.8441 0.7869 0.0300  0.0109  -0.0171 333 TYR B CD1 
783  C CD2 . TYR A 118 ? 0.7412 0.7790 0.7641 0.0158  -0.0107 0.0000  333 TYR B CD2 
784  C CE1 . TYR A 118 ? 0.7296 0.7755 0.7527 0.0409  0.0138  -0.0171 333 TYR B CE1 
785  C CE2 . TYR A 118 ? 0.7386 0.7629 0.7797 0.0253  -0.0051 -0.0025 333 TYR B CE2 
786  C CZ  . TYR A 118 ? 0.7217 0.7484 0.7606 0.0368  0.0065  -0.0097 333 TYR B CZ  
787  O OH  . TYR A 118 ? 0.7627 0.7763 0.8145 0.0459  0.0106  -0.0100 333 TYR B OH  
788  N N   . GLU A 119 ? 0.7965 0.9054 0.7242 -0.0316 -0.0269 0.0294  334 GLU B N   
789  C CA  . GLU A 119 ? 0.8298 0.9570 0.7231 -0.0445 -0.0331 0.0331  334 GLU B CA  
790  C C   . GLU A 119 ? 0.8723 0.9892 0.7639 -0.0419 -0.0467 0.0230  334 GLU B C   
791  O O   . GLU A 119 ? 0.8455 0.9416 0.7641 -0.0341 -0.0555 0.0222  334 GLU B O   
792  C CB  . GLU A 119 ? 0.9253 1.0516 0.8028 -0.0613 -0.0452 0.0639  334 GLU B CB  
793  C CG  . GLU A 119 ? 0.9973 1.1400 0.8701 -0.0729 -0.0322 0.0746  334 GLU B CG  
794  C CD  . GLU A 119 ? 1.1265 1.2723 0.9663 -0.0965 -0.0416 0.1035  334 GLU B CD  
795  O OE1 . GLU A 119 ? 1.1643 1.3108 0.9782 -0.1011 -0.0551 0.1100  334 GLU B OE1 
796  O OE2 . GLU A 119 ? 1.1310 1.2770 0.9695 -0.1118 -0.0371 0.1204  334 GLU B OE2 
797  N N   . SER A 120 ? 0.9039 1.0409 0.7626 -0.0505 -0.0486 0.0147  335 SER B N   
798  C CA  . SER A 120 ? 0.8895 1.0228 0.7441 -0.0521 -0.0633 0.0040  335 SER B CA  
799  C C   . SER A 120 ? 0.9889 1.1469 0.8023 -0.0671 -0.0750 0.0126  335 SER B C   
800  O O   . SER A 120 ? 1.0180 1.1978 0.8015 -0.0767 -0.0660 0.0201  335 SER B O   
801  C CB  . SER A 120 ? 0.8804 1.0046 0.7376 -0.0446 -0.0516 -0.0296 335 SER B CB  
802  O OG  . SER A 120 ? 0.9527 1.0788 0.8001 -0.0528 -0.0660 -0.0414 335 SER B OG  
803  N N   . LEU A 121 ? 0.9942 1.1539 0.8057 -0.0707 -0.0954 0.0118  336 LEU B N   
804  C CA  . LEU A 121 ? 0.9714 1.1579 0.7388 -0.0847 -0.1064 0.0137  336 LEU B CA  
805  C C   . LEU A 121 ? 0.9622 1.1605 0.7073 -0.0878 -0.0943 -0.0237 336 LEU B C   
806  O O   . LEU A 121 ? 1.0552 1.2795 0.7580 -0.0974 -0.0879 -0.0301 336 LEU B O   
807  C CB  . LEU A 121 ? 0.9690 1.1593 0.7414 -0.0867 -0.1369 0.0302  336 LEU B CB  
808  C CG  . LEU A 121 ? 0.9901 1.1715 0.7592 -0.0862 -0.1536 0.0710  336 LEU B CG  
809  C CD1 . LEU A 121 ? 0.9606 1.1581 0.7122 -0.0895 -0.1854 0.0874  336 LEU B CD1 
810  C CD2 . LEU A 121 ? 0.9515 1.1352 0.6874 -0.0979 -0.1385 0.0885  336 LEU B CD2 
811  N N   . GLU A 122 ? 0.9832 1.1605 0.7538 -0.0806 -0.0900 -0.0492 337 GLU B N   
812  C CA  . GLU A 122 ? 1.0003 1.1745 0.7505 -0.0820 -0.0790 -0.0871 337 GLU B CA  
813  C C   . GLU A 122 ? 1.0092 1.1656 0.7678 -0.0661 -0.0526 -0.1039 337 GLU B C   
814  O O   . GLU A 122 ? 1.0035 1.1497 0.7898 -0.0553 -0.0442 -0.0879 337 GLU B O   
815  C CB  . GLU A 122 ? 0.9842 1.1415 0.7524 -0.0878 -0.0918 -0.1049 337 GLU B CB  
816  C CG  . GLU A 122 ? 1.0431 1.1841 0.8601 -0.0816 -0.0987 -0.0872 337 GLU B CG  
817  C CD  . GLU A 122 ? 1.0682 1.1998 0.9048 -0.0913 -0.1084 -0.1053 337 GLU B CD  
818  O OE1 . GLU A 122 ? 1.0456 1.1724 0.8567 -0.1028 -0.1076 -0.1344 337 GLU B OE1 
819  O OE2 . GLU A 122 ? 0.9899 1.1197 0.8667 -0.0885 -0.1155 -0.0920 337 GLU B OE2 
820  N N   . HIS A 123 ? 1.0113 1.1643 0.7445 -0.0634 -0.0410 -0.1381 338 HIS B N   
821  C CA  . HIS A 123 ? 0.9954 1.1382 0.7294 -0.0441 -0.0173 -0.1585 338 HIS B CA  
822  C C   . HIS A 123 ? 0.9903 1.0803 0.7451 -0.0336 -0.0144 -0.1793 338 HIS B C   
823  O O   . HIS A 123 ? 1.0259 1.0931 0.7649 -0.0416 -0.0203 -0.2050 338 HIS B O   
824  C CB  . HIS A 123 ? 0.9932 1.1653 0.6828 -0.0445 -0.0060 -0.1853 338 HIS B CB  
825  C CG  . HIS A 123 ? 1.0076 1.1657 0.6969 -0.0201 0.0158  -0.2167 338 HIS B CG  
826  N ND1 . HIS A 123 ? 1.0502 1.2372 0.7495 -0.0039 0.0342  -0.2114 338 HIS B ND1 
827  C CD2 . HIS A 123 ? 1.0325 1.1507 0.7119 -0.0079 0.0209  -0.2543 338 HIS B CD2 
828  C CE1 . HIS A 123 ? 1.0460 1.2151 0.7447 0.0213  0.0492  -0.2442 338 HIS B CE1 
829  N NE2 . HIS A 123 ? 1.0962 1.2179 0.7810 0.0200  0.0414  -0.2704 338 HIS B NE2 
830  N N   . MET A 124 ? 0.9380 1.0070 0.7255 -0.0184 -0.0064 -0.1676 339 MET B N   
831  C CA  . MET A 124 ? 0.9694 0.9852 0.7725 -0.0101 -0.0039 -0.1821 339 MET B CA  
832  C C   . MET A 124 ? 0.9260 0.9269 0.7400 0.0172  0.0135  -0.1869 339 MET B C   
833  O O   . MET A 124 ? 0.9154 0.9538 0.7306 0.0283  0.0238  -0.1792 339 MET B O   
834  C CB  . MET A 124 ? 0.9841 0.9848 0.8189 -0.0229 -0.0174 -0.1612 339 MET B CB  
835  C CG  . MET A 124 ? 1.0035 1.0405 0.8389 -0.0424 -0.0362 -0.1432 339 MET B CG  
836  S SD  . MET A 124 ? 0.9255 0.9623 0.8055 -0.0491 -0.0502 -0.1161 339 MET B SD  
837  C CE  . MET A 124 ? 0.8569 0.8990 0.7572 -0.0311 -0.0392 -0.0905 339 MET B CE  
838  N N   . THR A 125 ? 0.9477 0.8941 0.7664 0.0269  0.0162  -0.2011 340 THR B N   
839  C CA  . THR A 125 ? 0.9770 0.9008 0.8093 0.0544  0.0280  -0.2012 340 THR B CA  
840  C C   . THR A 125 ? 0.9889 0.8880 0.8507 0.0478  0.0219  -0.1766 340 THR B C   
841  O O   . THR A 125 ? 1.0172 0.8756 0.8790 0.0330  0.0149  -0.1801 340 THR B O   
842  C CB  . THR A 125 ? 1.0617 0.9339 0.8720 0.0734  0.0347  -0.2341 340 THR B CB  
843  O OG1 . THR A 125 ? 1.1337 1.0178 0.9111 0.0674  0.0353  -0.2628 340 THR B OG1 
844  C CG2 . THR A 125 ? 1.0715 0.9499 0.8900 0.1098  0.0478  -0.2379 340 THR B CG2 
845  N N   . LEU A 126 ? 0.9559 0.8832 0.8417 0.0558  0.0250  -0.1529 341 LEU B N   
846  C CA  . LEU A 126 ? 0.8975 0.8093 0.8102 0.0507  0.0206  -0.1307 341 LEU B CA  
847  C C   . LEU A 126 ? 0.9166 0.7843 0.8322 0.0709  0.0273  -0.1333 341 LEU B C   
848  O O   . LEU A 126 ? 0.9228 0.7899 0.8310 0.0963  0.0357  -0.1440 341 LEU B O   
849  C CB  . LEU A 126 ? 0.8292 0.7858 0.7626 0.0493  0.0199  -0.1063 341 LEU B CB  
850  C CG  . LEU A 126 ? 0.7439 0.7392 0.6715 0.0312  0.0115  -0.0975 341 LEU B CG  
851  C CD1 . LEU A 126 ? 0.6751 0.6977 0.6226 0.0281  0.0090  -0.0719 341 LEU B CD1 
852  C CD2 . LEU A 126 ? 0.7791 0.7614 0.7045 0.0118  -0.0016 -0.1003 341 LEU B CD2 
853  N N   . THR A 127 ? 0.9220 0.7554 0.8479 0.0601  0.0233  -0.1229 342 THR B N   
854  C CA  . THR A 127 ? 0.8938 0.6924 0.8243 0.0762  0.0279  -0.1145 342 THR B CA  
855  C C   . THR A 127 ? 0.8380 0.6614 0.7950 0.0688  0.0261  -0.0900 342 THR B C   
856  O O   . THR A 127 ? 0.8214 0.6592 0.7917 0.0468  0.0204  -0.0822 342 THR B O   
857  C CB  . THR A 127 ? 0.9319 0.6615 0.8446 0.0694  0.0267  -0.1232 342 THR B CB  
858  O OG1 . THR A 127 ? 1.0106 0.7159 0.8977 0.0684  0.0260  -0.1499 342 THR B OG1 
859  C CG2 . THR A 127 ? 0.9300 0.6206 0.8373 0.0945  0.0309  -0.1160 342 THR B CG2 
860  N N   . CYS A 128 ? 0.8218 0.6535 0.7870 0.0889  0.0305  -0.0799 343 CYS B N   
861  C CA  . CYS A 128 ? 0.7808 0.6452 0.7690 0.0848  0.0294  -0.0607 343 CYS B CA  
862  C C   . CYS A 128 ? 0.8463 0.6827 0.8345 0.0955  0.0318  -0.0502 343 CYS B C   
863  O O   . CYS A 128 ? 0.8492 0.6795 0.8305 0.1201  0.0344  -0.0517 343 CYS B O   
864  C CB  . CYS A 128 ? 0.8110 0.7253 0.8073 0.0948  0.0315  -0.0589 343 CYS B CB  
865  S SG  . CYS A 128 ? 0.8670 0.8173 0.8626 0.0749  0.0267  -0.0604 343 CYS B SG  
866  N N   . SER A 129 ? 0.7958 0.6190 0.7910 0.0780  0.0306  -0.0397 344 SER B N   
867  C CA  . SER A 129 ? 0.8440 0.6398 0.8334 0.0833  0.0331  -0.0276 344 SER B CA  
868  C C   . SER A 129 ? 0.7776 0.6113 0.7865 0.0817  0.0334  -0.0146 344 SER B C   
869  O O   . SER A 129 ? 0.8152 0.6754 0.8420 0.0655  0.0319  -0.0131 344 SER B O   
870  C CB  . SER A 129 ? 0.8804 0.6326 0.8585 0.0615  0.0341  -0.0259 344 SER B CB  
871  O OG  . SER A 129 ? 0.9194 0.6923 0.9132 0.0446  0.0362  -0.0141 344 SER B OG  
872  N N   . SER A 130 ? 0.7927 0.6275 0.7972 0.0998  0.0342  -0.0063 345 SER B N   
873  C CA  . SER A 130 ? 0.8369 0.7019 0.8542 0.0980  0.0342  0.0041  345 SER B CA  
874  C C   . SER A 130 ? 0.8156 0.6518 0.8165 0.0989  0.0363  0.0166  345 SER B C   
875  O O   . SER A 130 ? 0.8373 0.6629 0.8246 0.1195  0.0339  0.0230  345 SER B O   
876  C CB  . SER A 130 ? 0.8122 0.7163 0.8388 0.1150  0.0319  0.0031  345 SER B CB  
877  O OG  . SER A 130 ? 0.8087 0.7449 0.8514 0.1042  0.0306  -0.0024 345 SER B OG  
878  N N   . LYS A 131 ? 0.8350 0.6633 0.8370 0.0768  0.0403  0.0209  346 LYS B N   
879  C CA  . LYS A 131 ? 0.8781 0.6875 0.8628 0.0718  0.0441  0.0349  346 LYS B CA  
880  C C   . LYS A 131 ? 0.8104 0.6630 0.8070 0.0724  0.0451  0.0385  346 LYS B C   
881  O O   . LYS A 131 ? 0.7515 0.6352 0.7697 0.0593  0.0476  0.0315  346 LYS B O   
882  C CB  . LYS A 131 ? 0.9240 0.7108 0.9036 0.0439  0.0502  0.0367  346 LYS B CB  
883  C CG  . LYS A 131 ? 1.0436 0.7925 1.0154 0.0359  0.0485  0.0279  346 LYS B CG  
884  C CD  . LYS A 131 ? 1.1623 0.8809 1.1215 0.0056  0.0545  0.0336  346 LYS B CD  
885  C CE  . LYS A 131 ? 1.2416 0.9042 1.1815 -0.0013 0.0514  0.0259  346 LYS B CE  
886  N NZ  . LYS A 131 ? 1.2365 0.9243 1.1981 -0.0195 0.0494  0.0086  346 LYS B NZ  
887  N N   . VAL A 132 ? 0.8273 0.6812 0.8091 0.0889  0.0419  0.0480  347 VAL B N   
888  C CA  . VAL A 132 ? 0.8520 0.7414 0.8370 0.0877  0.0425  0.0509  347 VAL B CA  
889  C C   . VAL A 132 ? 0.8888 0.7611 0.8506 0.0739  0.0492  0.0638  347 VAL B C   
890  O O   . VAL A 132 ? 0.8931 0.7249 0.8253 0.0790  0.0476  0.0788  347 VAL B O   
891  C CB  . VAL A 132 ? 0.8594 0.7690 0.8408 0.1108  0.0339  0.0537  347 VAL B CB  
892  C CG1 . VAL A 132 ? 0.8486 0.7921 0.8277 0.1065  0.0337  0.0556  347 VAL B CG1 
893  C CG2 . VAL A 132 ? 0.7801 0.7149 0.7846 0.1193  0.0297  0.0413  347 VAL B CG2 
894  N N   . CYS A 133 ? 0.8862 0.7886 0.8593 0.0571  0.0567  0.0582  348 CYS B N   
895  C CA  . CYS A 133 ? 0.9505 0.8474 0.9030 0.0393  0.0663  0.0686  348 CYS B CA  
896  C C   . CYS A 133 ? 0.9493 0.8839 0.8957 0.0412  0.0681  0.0674  348 CYS B C   
897  O O   . CYS A 133 ? 0.8660 0.8371 0.8366 0.0447  0.0669  0.0509  348 CYS B O   
898  C CB  . CYS A 133 ? 0.9938 0.9004 0.9649 0.0150  0.0766  0.0601  348 CYS B CB  
899  S SG  . CYS A 133 ? 0.9691 0.8452 0.9538 0.0091  0.0730  0.0541  348 CYS B SG  
900  N N   . SER A 134 ? 1.0590 0.9809 0.9694 0.0379  0.0703  0.0851  349 SER B N   
901  C CA  . SER A 134 ? 1.0764 1.0346 0.9734 0.0348  0.0739  0.0841  349 SER B CA  
902  C C   . SER A 134 ? 1.1281 1.0915 1.0088 0.0084  0.0902  0.0903  349 SER B C   
903  O O   . SER A 134 ? 1.1790 1.1043 1.0265 -0.0028 0.0930  0.1128  349 SER B O   
904  C CB  . SER A 134 ? 1.1116 1.0616 0.9760 0.0526  0.0620  0.1008  349 SER B CB  
905  O OG  . SER A 134 ? 1.1957 1.1619 1.0278 0.0407  0.0685  0.1104  349 SER B OG  
906  N N   . PHE A 135 ? 1.0302 1.0405 0.9327 -0.0016 0.1009  0.0702  350 PHE B N   
907  C CA  . PHE A 135 ? 1.0530 1.0842 0.9508 -0.0277 0.1192  0.0701  350 PHE B CA  
908  C C   . PHE A 135 ? 1.1383 1.1460 1.0503 -0.0455 0.1245  0.0744  350 PHE B C   
909  O O   . PHE A 135 ? 1.2180 1.2247 1.1134 -0.0722 0.1377  0.0856  350 PHE B O   
910  C CB  . PHE A 135 ? 1.0879 1.1138 0.9345 -0.0404 0.1255  0.0926  350 PHE B CB  
911  C CG  . PHE A 135 ? 1.0435 1.1095 0.8749 -0.0315 0.1251  0.0836  350 PHE B CG  
912  C CD1 . PHE A 135 ? 1.0532 1.1087 0.8673 -0.0095 0.1077  0.0903  350 PHE B CD1 
913  C CD2 . PHE A 135 ? 0.9887 1.1072 0.8227 -0.0456 0.1422  0.0666  350 PHE B CD2 
914  C CE1 . PHE A 135 ? 1.0095 1.1040 0.8076 -0.0044 0.1060  0.0802  350 PHE B CE1 
915  C CE2 . PHE A 135 ? 0.9627 1.1170 0.7792 -0.0385 0.1418  0.0548  350 PHE B CE2 
916  C CZ  . PHE A 135 ? 0.9604 1.1010 0.7577 -0.0193 0.1230  0.0618  350 PHE B CZ  
917  N N   . GLY A 136 ? 1.1182 1.1080 1.0584 -0.0341 0.1143  0.0660  351 GLY B N   
918  C CA  . GLY A 136 ? 1.2172 1.1855 1.1692 -0.0516 0.1172  0.0677  351 GLY B CA  
919  C C   . GLY A 136 ? 1.2933 1.1946 1.2096 -0.0580 0.1125  0.0907  351 GLY B C   
920  O O   . GLY A 136 ? 1.4182 1.2948 1.3421 -0.0732 0.1129  0.0899  351 GLY B O   
921  N N   . LYS A 137 ? 1.2148 1.0840 1.0913 -0.0463 0.1066  0.1104  352 LYS B N   
922  C CA  . LYS A 137 ? 1.2057 1.0022 1.0475 -0.0437 0.0985  0.1315  352 LYS B CA  
923  C C   . LYS A 137 ? 1.1782 0.9553 1.0356 -0.0117 0.0832  0.1222  352 LYS B C   
924  O O   . LYS A 137 ? 1.1147 0.9245 0.9862 0.0123  0.0758  0.1136  352 LYS B O   
925  C CB  . LYS A 137 ? 1.1861 0.9577 0.9775 -0.0415 0.0968  0.1586  352 LYS B CB  
926  C CG  . LYS A 137 ? 1.2071 0.9730 0.9872 -0.0032 0.0799  0.1639  352 LYS B CG  
927  C CD  . LYS A 137 ? 1.3013 1.0802 1.0420 -0.0016 0.0789  0.1831  352 LYS B CD  
928  C CE  . LYS A 137 ? 1.3510 1.0865 1.0590 0.0304  0.0595  0.2044  352 LYS B CE  
929  N NZ  . LYS A 137 ? 1.3979 1.0502 1.0587 0.0232  0.0561  0.2347  352 LYS B NZ  
930  N N   . GLN A 138 ? 1.2321 0.9604 1.0880 -0.0143 0.0793  0.1213  353 GLN B N   
931  C CA  . GLN A 138 ? 1.1887 0.8987 1.0553 0.0153  0.0667  0.1117  353 GLN B CA  
932  C C   . GLN A 138 ? 1.1996 0.8824 1.0369 0.0457  0.0555  0.1277  353 GLN B C   
933  O O   . GLN A 138 ? 1.3105 0.9335 1.1086 0.0448  0.0527  0.1483  353 GLN B O   
934  C CB  . GLN A 138 ? 1.2125 0.8721 1.0766 0.0047  0.0656  0.1060  353 GLN B CB  
935  C CG  . GLN A 138 ? 1.2003 0.8665 1.0879 0.0273  0.0575  0.0866  353 GLN B CG  
936  C CD  . GLN A 138 ? 1.2436 0.8446 1.1054 0.0497  0.0486  0.0895  353 GLN B CD  
937  O OE1 . GLN A 138 ? 1.2816 0.8435 1.1393 0.0410  0.0480  0.0795  353 GLN B OE1 
938  N NE2 . GLN A 138 ? 1.2088 0.7993 1.0531 0.0803  0.0408  0.1014  353 GLN B NE2 
939  N N   . VAL A 139 ? 1.0413 0.7679 0.8969 0.0714  0.0482  0.1194  354 VAL B N   
940  C CA  . VAL A 139 ? 1.0125 0.7348 0.8467 0.1007  0.0365  0.1330  354 VAL B CA  
941  C C   . VAL A 139 ? 1.0113 0.7142 0.8523 0.1333  0.0255  0.1262  354 VAL B C   
942  O O   . VAL A 139 ? 1.0214 0.6821 0.8352 0.1572  0.0155  0.1406  354 VAL B O   
943  C CB  . VAL A 139 ? 0.9810 0.7723 0.8305 0.1046  0.0355  0.1268  354 VAL B CB  
944  C CG1 . VAL A 139 ? 0.8773 0.6790 0.7139 0.1368  0.0206  0.1362  354 VAL B CG1 
945  C CG2 . VAL A 139 ? 1.0780 0.8871 0.9135 0.0774  0.0466  0.1335  354 VAL B CG2 
946  N N   . VAL A 140 ? 1.0100 0.7450 0.8861 0.1359  0.0270  0.1042  355 VAL B N   
947  C CA  . VAL A 140 ? 0.9742 0.7090 0.8622 0.1649  0.0196  0.0927  355 VAL B CA  
948  C C   . VAL A 140 ? 0.9595 0.6976 0.8706 0.1505  0.0259  0.0729  355 VAL B C   
949  O O   . VAL A 140 ? 0.8878 0.6581 0.8196 0.1264  0.0325  0.0652  355 VAL B O   
950  C CB  . VAL A 140 ? 0.9181 0.7163 0.8250 0.1867  0.0121  0.0885  355 VAL B CB  
951  C CG1 . VAL A 140 ? 0.9349 0.7617 0.8688 0.2019  0.0109  0.0694  355 VAL B CG1 
952  C CG2 . VAL A 140 ? 0.9620 0.7449 0.8429 0.2154  0.0003  0.1063  355 VAL B CG2 
953  N N   . GLU A 141 ? 0.9917 0.6935 0.8966 0.1662  0.0232  0.0643  356 GLU B N   
954  C CA  . GLU A 141 ? 0.9648 0.6670 0.8850 0.1539  0.0276  0.0454  356 GLU B CA  
955  C C   . GLU A 141 ? 0.9085 0.6239 0.8367 0.1840  0.0237  0.0302  356 GLU B C   
956  O O   . GLU A 141 ? 0.9334 0.6238 0.8465 0.2150  0.0177  0.0331  356 GLU B O   
957  C CB  . GLU A 141 ? 1.0285 0.6645 0.9266 0.1323  0.0309  0.0466  356 GLU B CB  
958  C CG  . GLU A 141 ? 0.9978 0.6425 0.9119 0.1110  0.0348  0.0282  356 GLU B CG  
959  C CD  . GLU A 141 ? 1.1341 0.7145 1.0258 0.0883  0.0366  0.0270  356 GLU B CD  
960  O OE1 . GLU A 141 ? 1.1892 0.7099 1.0502 0.0883  0.0354  0.0420  356 GLU B OE1 
961  O OE2 . GLU A 141 ? 1.1771 0.7651 1.0799 0.0686  0.0382  0.0118  356 GLU B OE2 
962  N N   . LYS A 142 ? 0.9092 0.6671 0.8608 0.1760  0.0270  0.0144  357 LYS B N   
963  C CA  . LYS A 142 ? 0.9193 0.6925 0.8766 0.1978  0.0267  -0.0030 357 LYS B CA  
964  C C   . LYS A 142 ? 0.8795 0.6412 0.8371 0.1774  0.0308  -0.0184 357 LYS B C   
965  O O   . LYS A 142 ? 0.8413 0.6218 0.8111 0.1491  0.0327  -0.0166 357 LYS B O   
966  C CB  . LYS A 142 ? 0.8398 0.6883 0.8226 0.2079  0.0263  -0.0061 357 LYS B CB  
967  C CG  . LYS A 142 ? 0.9673 0.8459 0.9585 0.2221  0.0294  -0.0253 357 LYS B CG  
968  C CD  . LYS A 142 ? 1.0383 0.9485 1.0356 0.2594  0.0264  -0.0289 357 LYS B CD  
969  C CE  . LYS A 142 ? 1.0533 1.0024 1.0596 0.2735  0.0323  -0.0504 357 LYS B CE  
970  N NZ  . LYS A 142 ? 1.1081 1.1136 1.1308 0.3069  0.0304  -0.0551 357 LYS B NZ  
971  N N   . VAL A 143 ? 0.9405 0.6693 0.8831 0.1930  0.0310  -0.0343 358 VAL B N   
972  C CA  . VAL A 143 ? 0.9417 0.6612 0.8802 0.1751  0.0335  -0.0517 358 VAL B CA  
973  C C   . VAL A 143 ? 0.9419 0.6939 0.8831 0.1983  0.0363  -0.0720 358 VAL B C   
974  O O   . VAL A 143 ? 0.9512 0.6850 0.8826 0.2318  0.0357  -0.0805 358 VAL B O   
975  C CB  . VAL A 143 ? 0.9305 0.5706 0.8417 0.1637  0.0321  -0.0562 358 VAL B CB  
976  C CG1 . VAL A 143 ? 0.9446 0.5881 0.8554 0.1375  0.0331  -0.0728 358 VAL B CG1 
977  C CG2 . VAL A 143 ? 0.9664 0.5760 0.8716 0.1437  0.0313  -0.0345 358 VAL B CG2 
978  N N   . GLU A 144 ? 1.0009 0.8024 0.9545 0.1815  0.0391  -0.0793 359 GLU B N   
979  C CA  . GLU A 144 ? 0.9980 0.8399 0.9522 0.1963  0.0440  -0.0983 359 GLU B CA  
980  C C   . GLU A 144 ? 0.9789 0.8149 0.9207 0.1734  0.0445  -0.1128 359 GLU B C   
981  O O   . GLU A 144 ? 1.0023 0.8245 0.9450 0.1443  0.0402  -0.1049 359 GLU B O   
982  C CB  . GLU A 144 ? 0.9625 0.8820 0.9409 0.1958  0.0466  -0.0899 359 GLU B CB  
983  C CG  . GLU A 144 ? 1.0251 0.9638 1.0157 0.2223  0.0455  -0.0815 359 GLU B CG  
984  C CD  . GLU A 144 ? 1.0580 1.0752 1.0722 0.2185  0.0482  -0.0761 359 GLU B CD  
985  O OE1 . GLU A 144 ? 1.0173 1.0500 1.0443 0.1977  0.0447  -0.0591 359 GLU B OE1 
986  O OE2 . GLU A 144 ? 1.0828 1.1465 1.1025 0.2356  0.0543  -0.0905 359 GLU B OE2 
987  N N   . THR A 145 ? 0.8947 0.7466 0.8251 0.1878  0.0497  -0.1355 360 THR B N   
988  C CA  . THR A 145 ? 0.9124 0.7736 0.8288 0.1669  0.0501  -0.1503 360 THR B CA  
989  C C   . THR A 145 ? 0.9066 0.8436 0.8292 0.1683  0.0571  -0.1546 360 THR B C   
990  O O   . THR A 145 ? 0.9200 0.8956 0.8535 0.1925  0.0639  -0.1577 360 THR B O   
991  C CB  . THR A 145 ? 0.9052 0.7088 0.7932 0.1770  0.0506  -0.1774 360 THR B CB  
992  O OG1 . THR A 145 ? 0.9740 0.7827 0.8581 0.2171  0.0574  -0.1949 360 THR B OG1 
993  C CG2 . THR A 145 ? 0.9336 0.6589 0.8123 0.1666  0.0437  -0.1700 360 THR B CG2 
994  N N   . GLU A 146 ? 0.8807 0.8432 0.7968 0.1407  0.0546  -0.1527 361 GLU B N   
995  C CA  . GLU A 146 ? 0.9024 0.9332 0.8175 0.1361  0.0614  -0.1541 361 GLU B CA  
996  C C   . GLU A 146 ? 0.9645 0.9999 0.8529 0.1167  0.0593  -0.1676 361 GLU B C   
997  O O   . GLU A 146 ? 0.9382 0.9545 0.8232 0.0920  0.0481  -0.1576 361 GLU B O   
998  C CB  . GLU A 146 ? 0.8315 0.9022 0.7688 0.1187  0.0584  -0.1252 361 GLU B CB  
999  C CG  . GLU A 146 ? 0.8201 0.9569 0.7527 0.1061  0.0648  -0.1216 361 GLU B CG  
1000 C CD  . GLU A 146 ? 0.8258 1.0131 0.7643 0.1295  0.0791  -0.1363 361 GLU B CD  
1001 O OE1 . GLU A 146 ? 0.8514 1.0266 0.8049 0.1577  0.0812  -0.1425 361 GLU B OE1 
1002 O OE2 . GLU A 146 ? 0.8076 1.0512 0.7358 0.1194  0.0878  -0.1403 361 GLU B OE2 
1003 N N   . ARG A 147 ? 0.9377 1.0031 0.8076 0.1294  0.0698  -0.1919 362 ARG B N   
1004 C CA  . ARG A 147 ? 0.9385 1.0209 0.7783 0.1115  0.0693  -0.2064 362 ARG B CA  
1005 C C   . ARG A 147 ? 0.9090 1.0497 0.7488 0.0852  0.0678  -0.1818 362 ARG B C   
1006 O O   . ARG A 147 ? 0.9074 1.0916 0.7647 0.0874  0.0748  -0.1665 362 ARG B O   
1007 C CB  . ARG A 147 ? 1.0126 1.1113 0.8318 0.1367  0.0833  -0.2431 362 ARG B CB  
1008 C CG  . ARG A 147 ? 1.0396 1.1077 0.8228 0.1299  0.0804  -0.2730 362 ARG B CG  
1009 C CD  . ARG A 147 ? 1.1257 1.2598 0.8832 0.1137  0.0869  -0.2801 362 ARG B CD  
1010 N NE  . ARG A 147 ? 1.2725 1.3912 0.9923 0.1175  0.0898  -0.3198 362 ARG B NE  
1011 C CZ  . ARG A 147 ? 1.2233 1.3906 0.9104 0.1005  0.0935  -0.3310 362 ARG B CZ  
1012 N NH1 . ARG A 147 ? 1.1587 1.3922 0.8448 0.0791  0.0958  -0.3036 362 ARG B NH1 
1013 N NH2 . ARG A 147 ? 1.2489 1.3951 0.9001 0.1034  0.0946  -0.3704 362 ARG B NH2 
1014 N N   . ALA A 148 ? 0.8620 1.0017 0.6809 0.0593  0.0570  -0.1770 363 ALA B N   
1015 C CA  . ALA A 148 ? 0.9066 1.0934 0.7169 0.0344  0.0533  -0.1524 363 ALA B CA  
1016 C C   . ALA A 148 ? 0.9662 1.2165 0.7582 0.0366  0.0706  -0.1628 363 ALA B C   
1017 O O   . ALA A 148 ? 0.9788 1.2398 0.7530 0.0534  0.0825  -0.1960 363 ALA B O   
1018 C CB  . ALA A 148 ? 0.8913 1.0663 0.6783 0.0107  0.0366  -0.1485 363 ALA B CB  
1019 N N   . GLN A 149 ? 0.9091 1.2022 0.7051 0.0186  0.0725  -0.1351 364 GLN B N   
1020 C CA  . GLN A 149 ? 0.9020 1.2631 0.6753 0.0089  0.0878  -0.1388 364 GLN B CA  
1021 C C   . GLN A 149 ? 0.9395 1.3143 0.6866 -0.0267 0.0761  -0.1077 364 GLN B C   
1022 O O   . GLN A 149 ? 0.9231 1.2791 0.6859 -0.0413 0.0637  -0.0744 364 GLN B O   
1023 C CB  . GLN A 149 ? 0.8804 1.2895 0.6809 0.0183  0.1041  -0.1353 364 GLN B CB  
1024 C CG  . GLN A 149 ? 0.8629 1.2551 0.6931 0.0571  0.1112  -0.1595 364 GLN B CG  
1025 C CD  . GLN A 149 ? 0.9312 1.3665 0.7965 0.0636  0.1201  -0.1479 364 GLN B CD  
1026 O OE1 . GLN A 149 ? 0.8151 1.2230 0.7071 0.0602  0.1100  -0.1253 364 GLN B OE1 
1027 N NE2 . GLN A 149 ? 0.7802 1.2895 0.6459 0.0726  0.1395  -0.1657 364 GLN B NE2 
1028 N N   . LEU A 150 ? 1.0588 1.4635 0.7634 -0.0389 0.0793  -0.1193 365 LEU B N   
1029 C CA  . LEU A 150 ? 1.0593 1.4746 0.7296 -0.0711 0.0658  -0.0904 365 LEU B CA  
1030 C C   . LEU A 150 ? 1.0676 1.5254 0.7356 -0.0940 0.0741  -0.0590 365 LEU B C   
1031 O O   . LEU A 150 ? 0.9987 1.5153 0.6633 -0.0938 0.0969  -0.0719 365 LEU B O   
1032 C CB  . LEU A 150 ? 1.0189 1.4611 0.6404 -0.0774 0.0690  -0.1147 365 LEU B CB  
1033 C CG  . LEU A 150 ? 1.0932 1.5367 0.6727 -0.1063 0.0490  -0.0899 365 LEU B CG  
1034 C CD1 . LEU A 150 ? 1.1178 1.5070 0.7205 -0.1110 0.0215  -0.0579 365 LEU B CD1 
1035 C CD2 . LEU A 150 ? 1.0173 1.4694 0.5558 -0.1053 0.0470  -0.1247 365 LEU B CD2 
1036 N N   . GLU A 151 ? 1.1945 1.6225 0.8661 -0.1136 0.0558  -0.0191 366 GLU B N   
1037 C CA  . GLU A 151 ? 1.1861 1.6430 0.8473 -0.1425 0.0604  0.0143  366 GLU B CA  
1038 C C   . GLU A 151 ? 1.2811 1.7220 0.8993 -0.1701 0.0398  0.0483  366 GLU B C   
1039 O O   . GLU A 151 ? 1.3296 1.7753 0.9140 -0.1704 0.0325  0.0371  366 GLU B O   
1040 C CB  . GLU A 151 ? 1.1601 1.5917 0.8663 -0.1391 0.0585  0.0306  366 GLU B CB  
1041 C CG  . GLU A 151 ? 1.1694 1.6107 0.9158 -0.1067 0.0737  -0.0029 366 GLU B CG  
1042 C CD  . GLU A 151 ? 1.1942 1.6780 0.9669 -0.1115 0.0899  0.0011  366 GLU B CD  
1043 O OE1 . GLU A 151 ? 1.1847 1.6465 0.9722 -0.1286 0.0809  0.0295  366 GLU B OE1 
1044 O OE2 . GLU A 151 ? 1.1707 1.7118 0.9496 -0.0976 0.1112  -0.0262 366 GLU B OE2 
1045 N N   . ASP A 152 ? 1.3649 1.7841 0.9814 -0.1928 0.0288  0.0892  367 ASP B N   
1046 C CA  . ASP A 152 ? 1.4365 1.8476 1.0033 -0.2219 0.0118  0.1261  367 ASP B CA  
1047 C C   . ASP A 152 ? 1.4928 1.8602 1.0511 -0.2088 -0.0171 0.1293  367 ASP B C   
1048 O O   . ASP A 152 ? 1.5397 1.8537 1.1142 -0.2045 -0.0408 0.1537  367 ASP B O   
1049 C CB  . ASP A 152 ? 1.4273 1.8108 0.9957 -0.2471 0.0048  0.1685  367 ASP B CB  
1050 C CG  . ASP A 152 ? 1.5555 1.9274 1.0663 -0.2791 -0.0120 0.2110  367 ASP B CG  
1051 O OD1 . ASP A 152 ? 1.4846 1.9059 0.9472 -0.2963 -0.0028 0.2090  367 ASP B OD1 
1052 O OD2 . ASP A 152 ? 1.6294 1.9411 1.1404 -0.2865 -0.0348 0.2467  367 ASP B OD2 
1053 N N   . GLY A 153 ? 1.4357 1.8307 0.9678 -0.2026 -0.0152 0.1022  368 GLY B N   
1054 C CA  . GLY A 153 ? 1.4434 1.8115 0.9668 -0.1926 -0.0414 0.0991  368 GLY B CA  
1055 C C   . GLY A 153 ? 1.4502 1.7796 1.0255 -0.1638 -0.0493 0.0758  368 GLY B C   
1056 O O   . GLY A 153 ? 1.4271 1.7435 0.9993 -0.1568 -0.0688 0.0671  368 GLY B O   
1057 N N   . ARG A 154 ? 1.3551 1.6698 0.9764 -0.1490 -0.0349 0.0657  369 ARG B N   
1058 C CA  . ARG A 154 ? 1.2500 1.5260 0.9193 -0.1251 -0.0411 0.0500  369 ARG B CA  
1059 C C   . ARG A 154 ? 1.2084 1.4955 0.9033 -0.1075 -0.0154 0.0166  369 ARG B C   
1060 O O   . ARG A 154 ? 1.1992 1.5246 0.8840 -0.1120 0.0059  0.0100  369 ARG B O   
1061 C CB  . ARG A 154 ? 1.2959 1.5313 0.9961 -0.1236 -0.0561 0.0813  369 ARG B CB  
1062 C CG  . ARG A 154 ? 1.3072 1.5483 1.0108 -0.1366 -0.0429 0.1018  369 ARG B CG  
1063 C CD  . ARG A 154 ? 1.3599 1.5568 1.0733 -0.1427 -0.0631 0.1384  369 ARG B CD  
1064 N NE  . ARG A 154 ? 1.3871 1.5822 1.1124 -0.1547 -0.0502 0.1514  369 ARG B NE  
1065 C CZ  . ARG A 154 ? 1.3822 1.5338 1.1236 -0.1577 -0.0625 0.1750  369 ARG B CZ  
1066 N NH1 . ARG A 154 ? 1.3548 1.4614 1.1035 -0.1462 -0.0880 0.1897  369 ARG B NH1 
1067 N NH2 . ARG A 154 ? 1.3455 1.5008 1.0969 -0.1719 -0.0492 0.1819  369 ARG B NH2 
1068 N N   . PHE A 155 ? 1.1012 1.3561 0.8298 -0.0873 -0.0182 -0.0032 370 PHE B N   
1069 C CA  . PHE A 155 ? 1.0303 1.2835 0.7831 -0.0666 0.0016  -0.0322 370 PHE B CA  
1070 C C   . PHE A 155 ? 0.9507 1.1852 0.7442 -0.0584 0.0046  -0.0174 370 PHE B C   
1071 O O   . PHE A 155 ? 0.9610 1.1680 0.7714 -0.0629 -0.0112 0.0063  370 PHE B O   
1072 C CB  . PHE A 155 ? 0.9949 1.2188 0.7538 -0.0530 -0.0029 -0.0619 370 PHE B CB  
1073 C CG  . PHE A 155 ? 1.0263 1.2674 0.7445 -0.0617 -0.0061 -0.0817 370 PHE B CG  
1074 C CD1 . PHE A 155 ? 1.0467 1.3187 0.7389 -0.0562 0.0133  -0.1096 370 PHE B CD1 
1075 C CD2 . PHE A 155 ? 1.0231 1.2558 0.7284 -0.0748 -0.0290 -0.0736 370 PHE B CD2 
1076 C CE1 . PHE A 155 ? 1.0172 1.3067 0.6673 -0.0652 0.0108  -0.1310 370 PHE B CE1 
1077 C CE2 . PHE A 155 ? 1.0195 1.2719 0.6839 -0.0850 -0.0335 -0.0930 370 PHE B CE2 
1078 C CZ  . PHE A 155 ? 0.9785 1.2574 0.6132 -0.0811 -0.0132 -0.1222 370 PHE B CZ  
1079 N N   . VAL A 156 ? 0.8769 1.1288 0.6857 -0.0445 0.0241  -0.0331 371 VAL B N   
1080 C CA  . VAL A 156 ? 0.8388 1.0840 0.6818 -0.0389 0.0282  -0.0205 371 VAL B CA  
1081 C C   . VAL A 156 ? 0.8198 1.0552 0.6866 -0.0110 0.0398  -0.0466 371 VAL B C   
1082 O O   . VAL A 156 ? 0.8277 1.0819 0.6826 0.0030  0.0526  -0.0735 371 VAL B O   
1083 C CB  . VAL A 156 ? 0.9091 1.1995 0.7448 -0.0567 0.0390  -0.0041 371 VAL B CB  
1084 C CG1 . VAL A 156 ? 0.8592 1.1579 0.7305 -0.0460 0.0486  -0.0048 371 VAL B CG1 
1085 C CG2 . VAL A 156 ? 0.9707 1.2484 0.7883 -0.0840 0.0230  0.0309  371 VAL B CG2 
1086 N N   . TYR A 157 ? 0.7725 0.9765 0.6705 -0.0018 0.0347  -0.0388 372 TYR B N   
1087 C CA  . TYR A 157 ? 0.7538 0.9400 0.6719 0.0240  0.0423  -0.0574 372 TYR B CA  
1088 C C   . TYR A 157 ? 0.7027 0.9024 0.6478 0.0286  0.0466  -0.0455 372 TYR B C   
1089 O O   . TYR A 157 ? 0.7442 0.9296 0.7023 0.0161  0.0373  -0.0246 372 TYR B O   
1090 C CB  . TYR A 157 ? 0.7139 0.8474 0.6393 0.0291  0.0313  -0.0616 372 TYR B CB  
1091 C CG  . TYR A 157 ? 0.7185 0.8396 0.6207 0.0177  0.0219  -0.0694 372 TYR B CG  
1092 C CD1 . TYR A 157 ? 0.7568 0.8836 0.6514 -0.0025 0.0076  -0.0498 372 TYR B CD1 
1093 C CD2 . TYR A 157 ? 0.6990 0.7989 0.5869 0.0274  0.0252  -0.0965 372 TYR B CD2 
1094 C CE1 . TYR A 157 ? 0.7922 0.9138 0.6670 -0.0126 -0.0036 -0.0568 372 TYR B CE1 
1095 C CE2 . TYR A 157 ? 0.7250 0.8154 0.5923 0.0140  0.0151  -0.1055 372 TYR B CE2 
1096 C CZ  . TYR A 157 ? 0.8047 0.9107 0.6663 -0.0059 0.0006  -0.0856 372 TYR B CZ  
1097 O OH  . TYR A 157 ? 0.8810 0.9848 0.7224 -0.0189 -0.0116 -0.0947 372 TYR B OH  
1098 N N   . ARG A 158 ? 0.6876 0.9161 0.6415 0.0479  0.0598  -0.0606 373 ARG B N   
1099 C CA  . ARG A 158 ? 0.6802 0.9426 0.6569 0.0486  0.0649  -0.0513 373 ARG B CA  
1100 C C   . ARG A 158 ? 0.7056 0.9574 0.7010 0.0805  0.0684  -0.0652 373 ARG B C   
1101 O O   . ARG A 158 ? 0.6997 0.9681 0.6913 0.1046  0.0778  -0.0869 373 ARG B O   
1102 C CB  . ARG A 158 ? 0.6659 0.9974 0.6355 0.0371  0.0777  -0.0529 373 ARG B CB  
1103 C CG  . ARG A 158 ? 0.7104 1.0548 0.6683 -0.0002 0.0729  -0.0271 373 ARG B CG  
1104 C CD  . ARG A 158 ? 0.7647 1.1838 0.7215 -0.0153 0.0877  -0.0264 373 ARG B CD  
1105 N NE  . ARG A 158 ? 0.8263 1.2587 0.7529 -0.0502 0.0868  -0.0077 373 ARG B NE  
1106 C CZ  . ARG A 158 ? 0.8736 1.3167 0.7680 -0.0541 0.0904  -0.0152 373 ARG B CZ  
1107 N NH1 . ARG A 158 ? 0.8909 1.3315 0.7797 -0.0262 0.0961  -0.0442 373 ARG B NH1 
1108 N NH2 . ARG A 158 ? 0.9311 1.3833 0.7947 -0.0877 0.0873  0.0071  373 ARG B NH2 
1109 N N   . LEU A 159 ? 0.7002 0.9248 0.7139 0.0818  0.0605  -0.0526 374 LEU B N   
1110 C CA  . LEU A 159 ? 0.7034 0.9172 0.7324 0.1093  0.0612  -0.0593 374 LEU B CA  
1111 C C   . LEU A 159 ? 0.6519 0.9046 0.7031 0.1036  0.0607  -0.0475 374 LEU B C   
1112 O O   . LEU A 159 ? 0.7337 0.9624 0.7958 0.1027  0.0533  -0.0371 374 LEU B O   
1113 C CB  . LEU A 159 ? 0.7475 0.8941 0.7734 0.1139  0.0526  -0.0562 374 LEU B CB  
1114 C CG  . LEU A 159 ? 0.7670 0.8756 0.7715 0.1119  0.0512  -0.0678 374 LEU B CG  
1115 C CD1 . LEU A 159 ? 0.7130 0.8099 0.7123 0.0837  0.0427  -0.0554 374 LEU B CD1 
1116 C CD2 . LEU A 159 ? 0.8141 0.8668 0.8136 0.1298  0.0490  -0.0755 374 LEU B CD2 
1117 N N   . LEU A 160 ? 0.6371 0.9545 0.6942 0.0973  0.0691  -0.0503 375 LEU B N   
1118 C CA  . LEU A 160 ? 0.6316 0.9912 0.7083 0.0823  0.0681  -0.0393 375 LEU B CA  
1119 C C   . LEU A 160 ? 0.5700 0.9566 0.6676 0.1117  0.0683  -0.0478 375 LEU B C   
1120 O O   . LEU A 160 ? 0.5459 0.9495 0.6450 0.1435  0.0741  -0.0646 375 LEU B O   
1121 C CB  . LEU A 160 ? 0.5928 1.0170 0.6675 0.0571  0.0776  -0.0371 375 LEU B CB  
1122 C CG  . LEU A 160 ? 0.6144 1.0152 0.6625 0.0304  0.0766  -0.0273 375 LEU B CG  
1123 C CD1 . LEU A 160 ? 0.6384 1.1039 0.6745 0.0198  0.0910  -0.0348 375 LEU B CD1 
1124 C CD2 . LEU A 160 ? 0.5876 0.9564 0.6342 -0.0013 0.0652  -0.0037 375 LEU B CD2 
1125 N N   . ARG A 161 ? 0.5807 0.9695 0.6928 0.1025  0.0606  -0.0367 376 ARG B N   
1126 C CA  . ARG A 161 ? 0.5547 0.9897 0.6883 0.1222  0.0589  -0.0415 376 ARG B CA  
1127 C C   . ARG A 161 ? 0.5537 0.9559 0.6849 0.1644  0.0550  -0.0492 376 ARG B C   
1128 O O   . ARG A 161 ? 0.5277 0.9745 0.6740 0.1928  0.0549  -0.0577 376 ARG B O   
1129 C CB  . ARG A 161 ? 0.4416 0.9677 0.5915 0.1203  0.0693  -0.0513 376 ARG B CB  
1130 C CG  . ARG A 161 ? 0.4315 0.9951 0.5855 0.0745  0.0716  -0.0400 376 ARG B CG  
1131 C CD  . ARG A 161 ? 0.4364 1.0984 0.6088 0.0692  0.0830  -0.0494 376 ARG B CD  
1132 N NE  . ARG A 161 ? 0.4321 1.1516 0.6325 0.1017  0.0808  -0.0614 376 ARG B NE  
1133 C CZ  . ARG A 161 ? 0.4221 1.1819 0.6438 0.0897  0.0731  -0.0568 376 ARG B CZ  
1134 N NH1 . ARG A 161 ? 0.4517 1.1906 0.6687 0.0466  0.0670  -0.0421 376 ARG B NH1 
1135 N NH2 . ARG A 161 ? 0.4201 1.2424 0.6680 0.1227  0.0701  -0.0683 376 ARG B NH2 
1136 N N   . SER A 162 ? 0.5952 0.9208 0.7071 0.1688  0.0512  -0.0459 377 SER B N   
1137 C CA  . SER A 162 ? 0.5961 0.8794 0.7009 0.2031  0.0462  -0.0487 377 SER B CA  
1138 C C   . SER A 162 ? 0.5868 0.8899 0.7044 0.2106  0.0373  -0.0394 377 SER B C   
1139 O O   . SER A 162 ? 0.6167 0.9230 0.7391 0.1836  0.0331  -0.0288 377 SER B O   
1140 C CB  . SER A 162 ? 0.6521 0.8530 0.7353 0.1968  0.0432  -0.0434 377 SER B CB  
1141 O OG  . SER A 162 ? 0.6502 0.8341 0.7220 0.1771  0.0479  -0.0477 377 SER B OG  
1142 N N   . PRO A 163 ? 0.5502 0.8684 0.6727 0.2474  0.0331  -0.0438 378 PRO B N   
1143 C CA  . PRO A 163 ? 0.5708 0.9083 0.7017 0.2549  0.0222  -0.0336 378 PRO B CA  
1144 C C   . PRO A 163 ? 0.6118 0.8766 0.7213 0.2474  0.0157  -0.0192 378 PRO B C   
1145 O O   . PRO A 163 ? 0.6680 0.8669 0.7567 0.2595  0.0163  -0.0176 378 PRO B O   
1146 C CB  . PRO A 163 ? 0.5680 0.9328 0.7062 0.3024  0.0179  -0.0416 378 PRO B CB  
1147 C CG  . PRO A 163 ? 0.5397 0.9152 0.6788 0.3157  0.0300  -0.0607 378 PRO B CG  
1148 C CD  . PRO A 163 ? 0.5558 0.8674 0.6735 0.2866  0.0362  -0.0584 378 PRO B CD  
1149 N N   . MET A 164 ? 0.6297 0.9080 0.7436 0.2241  0.0105  -0.0102 379 MET B N   
1150 C CA  . MET A 164 ? 0.6055 0.8291 0.7005 0.2163  0.0059  0.0019  379 MET B CA  
1151 C C   . MET A 164 ? 0.6393 0.8324 0.7169 0.2501  -0.0015 0.0099  379 MET B C   
1152 O O   . MET A 164 ? 0.6525 0.8862 0.7386 0.2782  -0.0088 0.0088  379 MET B O   
1153 C CB  . MET A 164 ? 0.5722 0.8271 0.6753 0.1921  0.0009  0.0054  379 MET B CB  
1154 C CG  . MET A 164 ? 0.6772 0.8839 0.7677 0.1683  0.0030  0.0105  379 MET B CG  
1155 S SD  . MET A 164 ? 0.6485 0.8872 0.7519 0.1338  0.0003  0.0063  379 MET B SD  
1156 C CE  . MET A 164 ? 0.5503 0.8371 0.6546 0.1446  -0.0109 0.0076  379 MET B CE  
1157 N N   . CYS A 165 ? 0.7070 0.8290 0.7598 0.2475  -0.0003 0.0188  380 CYS B N   
1158 C CA  . CYS A 165 ? 0.7931 0.8743 0.8221 0.2746  -0.0082 0.0313  380 CYS B CA  
1159 C C   . CYS A 165 ? 0.7175 0.8292 0.7426 0.2754  -0.0184 0.0429  380 CYS B C   
1160 O O   . CYS A 165 ? 0.6744 0.8055 0.7041 0.2469  -0.0166 0.0431  380 CYS B O   
1161 C CB  . CYS A 165 ? 0.7978 0.7982 0.7994 0.2634  -0.0037 0.0397  380 CYS B CB  
1162 S SG  . CYS A 165 ? 0.8811 0.8735 0.8883 0.2190  0.0062  0.0374  380 CYS B SG  
1163 N N   . GLU A 166 ? 0.8736 0.7648 0.7036 0.2394  -0.0109 -0.0096 381 GLU B N   
1164 C CA  . GLU A 166 ? 0.9105 0.8149 0.7271 0.2459  -0.0167 -0.0028 381 GLU B CA  
1165 C C   . GLU A 166 ? 0.9626 0.8096 0.7618 0.2196  -0.0064 0.0171  381 GLU B C   
1166 O O   . GLU A 166 ? 0.9307 0.8009 0.7284 0.2110  -0.0058 0.0234  381 GLU B O   
1167 C CB  . GLU A 166 ? 0.9960 0.8881 0.7856 0.2934  -0.0372 -0.0130 381 GLU B CB  
1168 C CG  . GLU A 166 ? 1.1214 1.0668 0.9075 0.3096  -0.0478 -0.0152 381 GLU B CG  
1169 C CD  . GLU A 166 ? 1.2753 1.1551 1.0150 0.3401  -0.0636 -0.0070 381 GLU B CD  
1170 O OE1 . GLU A 166 ? 1.3561 1.1412 1.0627 0.3426  -0.0652 0.0033  381 GLU B OE1 
1171 O OE2 . GLU A 166 ? 1.3115 1.2340 1.0450 0.3589  -0.0752 -0.0098 381 GLU B OE2 
1172 N N   . TYR A 167 ? 0.9781 0.7588 0.7660 0.2040  0.0027  0.0248  382 TYR B N   
1173 C CA  . TYR A 167 ? 0.9299 0.6705 0.7062 0.1756  0.0150  0.0400  382 TYR B CA  
1174 C C   . TYR A 167 ? 0.9156 0.7041 0.7248 0.1468  0.0265  0.0412  382 TYR B C   
1175 O O   . TYR A 167 ? 0.9626 0.7525 0.7663 0.1336  0.0307  0.0482  382 TYR B O   
1176 C CB  . TYR A 167 ? 0.9909 0.6650 0.7527 0.1611  0.0233  0.0447  382 TYR B CB  
1177 C CG  . TYR A 167 ? 1.0728 0.7193 0.8252 0.1306  0.0374  0.0569  382 TYR B CG  
1178 C CD1 . TYR A 167 ? 1.0975 0.7081 0.8122 0.1315  0.0347  0.0689  382 TYR B CD1 
1179 C CD2 . TYR A 167 ? 1.0963 0.7596 0.8774 0.1026  0.0523  0.0551  382 TYR B CD2 
1180 C CE1 . TYR A 167 ? 1.0565 0.6528 0.7633 0.1029  0.0486  0.0773  382 TYR B CE1 
1181 C CE2 . TYR A 167 ? 1.0251 0.6742 0.8004 0.0780  0.0647  0.0616  382 TYR B CE2 
1182 C CZ  . TYR A 167 ? 1.0252 0.6435 0.7640 0.0772  0.0638  0.0719  382 TYR B CZ  
1183 O OH  . TYR A 167 ? 1.1058 0.7192 0.8394 0.0521  0.0771  0.0757  382 TYR B OH  
1184 N N   . LEU A 168 ? 0.8882 0.7113 0.7283 0.1365  0.0306  0.0342  383 LEU B N   
1185 C CA  . LEU A 168 ? 0.8652 0.7246 0.7311 0.1105  0.0376  0.0362  383 LEU B CA  
1186 C C   . LEU A 168 ? 0.8133 0.7260 0.6837 0.1116  0.0304  0.0346  383 LEU B C   
1187 O O   . LEU A 168 ? 0.7862 0.7043 0.6599 0.0926  0.0338  0.0392  383 LEU B O   
1188 C CB  . LEU A 168 ? 0.8907 0.7734 0.7828 0.0999  0.0406  0.0313  383 LEU B CB  
1189 C CG  . LEU A 168 ? 0.9382 0.7827 0.8362 0.0815  0.0515  0.0349  383 LEU B CG  
1190 C CD1 . LEU A 168 ? 0.8666 0.7391 0.7905 0.0695  0.0527  0.0317  383 LEU B CD1 
1191 C CD2 . LEU A 168 ? 0.9545 0.7839 0.8486 0.0661  0.0573  0.0412  383 LEU B CD2 
1192 N N   . VAL A 169 ? 0.8432 0.7994 0.7142 0.1333  0.0198  0.0257  384 VAL B N   
1193 C CA  . VAL A 169 ? 0.8431 0.8598 0.7189 0.1314  0.0132  0.0223  384 VAL B CA  
1194 C C   . VAL A 169 ? 0.8466 0.8396 0.7005 0.1337  0.0116  0.0290  384 VAL B C   
1195 O O   . VAL A 169 ? 0.8353 0.8526 0.6941 0.1139  0.0129  0.0309  384 VAL B O   
1196 C CB  . VAL A 169 ? 0.7461 0.8228 0.6262 0.1591  0.0015  0.0077  384 VAL B CB  
1197 C CG1 . VAL A 169 ? 0.6865 0.8342 0.5724 0.1529  -0.0044 0.0030  384 VAL B CG1 
1198 C CG2 . VAL A 169 ? 0.6911 0.7993 0.5923 0.1543  0.0040  -0.0003 384 VAL B CG2 
1199 N N   . ASN A 170 ? 0.9903 0.9327 0.8162 0.1566  0.0078  0.0328  385 ASN B N   
1200 C CA  . ASN A 170 ? 1.0279 0.9485 0.8274 0.1603  0.0051  0.0403  385 ASN B CA  
1201 C C   . ASN A 170 ? 1.0493 0.9381 0.8488 0.1295  0.0188  0.0487  385 ASN B C   
1202 O O   . ASN A 170 ? 1.0828 0.9874 0.8778 0.1190  0.0191  0.0498  385 ASN B O   
1203 C CB  . ASN A 170 ? 1.0923 0.9569 0.8547 0.1899  -0.0040 0.0451  385 ASN B CB  
1204 C CG  . ASN A 170 ? 1.1850 1.0865 0.9404 0.2293  -0.0230 0.0343  385 ASN B CG  
1205 O OD1 . ASN A 170 ? 1.1811 1.1593 0.9566 0.2316  -0.0281 0.0241  385 ASN B OD1 
1206 N ND2 . ASN A 170 ? 1.2125 1.0603 0.9379 0.2604  -0.0348 0.0350  385 ASN B ND2 
1207 N N   . PHE A 171 ? 0.9082 0.7575 0.7138 0.1158  0.0297  0.0518  386 PHE B N   
1208 C CA  . PHE A 171 ? 0.8885 0.7191 0.7003 0.0893  0.0422  0.0547  386 PHE B CA  
1209 C C   . PHE A 171 ? 0.8770 0.7482 0.7107 0.0716  0.0418  0.0498  386 PHE B C   
1210 O O   . PHE A 171 ? 0.9052 0.7673 0.7366 0.0570  0.0470  0.0493  386 PHE B O   
1211 C CB  . PHE A 171 ? 0.9264 0.7286 0.7507 0.0788  0.0518  0.0545  386 PHE B CB  
1212 C CG  . PHE A 171 ? 0.9019 0.6942 0.7375 0.0561  0.0633  0.0531  386 PHE B CG  
1213 C CD1 . PHE A 171 ? 0.9672 0.7310 0.7824 0.0482  0.0718  0.0561  386 PHE B CD1 
1214 C CD2 . PHE A 171 ? 0.8928 0.7047 0.7574 0.0436  0.0645  0.0479  386 PHE B CD2 
1215 C CE1 . PHE A 171 ? 0.9458 0.7097 0.7736 0.0310  0.0819  0.0501  386 PHE B CE1 
1216 C CE2 . PHE A 171 ? 0.9148 0.7172 0.7897 0.0291  0.0720  0.0434  386 PHE B CE2 
1217 C CZ  . PHE A 171 ? 0.9269 0.7094 0.7856 0.0243  0.0812  0.0425  386 PHE B CZ  
1218 N N   . LEU A 172 ? 0.9006 0.8162 0.7530 0.0711  0.0351  0.0453  387 LEU B N   
1219 C CA  . LEU A 172 ? 0.8796 0.8243 0.7480 0.0480  0.0336  0.0427  387 LEU B CA  
1220 C C   . LEU A 172 ? 0.8733 0.8500 0.7313 0.0458  0.0268  0.0398  387 LEU B C   
1221 O O   . LEU A 172 ? 0.8968 0.8727 0.7566 0.0252  0.0271  0.0379  387 LEU B O   
1222 C CB  . LEU A 172 ? 0.9012 0.8825 0.7895 0.0410  0.0298  0.0408  387 LEU B CB  
1223 C CG  . LEU A 172 ? 0.8481 0.8066 0.7510 0.0346  0.0352  0.0429  387 LEU B CG  
1224 C CD1 . LEU A 172 ? 0.7539 0.7564 0.6716 0.0217  0.0301  0.0424  387 LEU B CD1 
1225 C CD2 . LEU A 172 ? 0.8025 0.7187 0.7089 0.0201  0.0412  0.0450  387 LEU B CD2 
1226 N N   . HIS A 173 ? 0.8309 0.8366 0.6775 0.0679  0.0190  0.0377  388 HIS B N   
1227 C CA  . HIS A 173 ? 0.9204 0.9616 0.7566 0.0674  0.0119  0.0338  388 HIS B CA  
1228 C C   . HIS A 173 ? 0.9813 0.9825 0.7961 0.0660  0.0164  0.0376  388 HIS B C   
1229 O O   . HIS A 173 ? 0.9593 0.9789 0.7693 0.0531  0.0141  0.0334  388 HIS B O   
1230 C CB  . HIS A 173 ? 0.9123 0.9954 0.7401 0.0978  0.0004  0.0290  388 HIS B CB  
1231 C CG  . HIS A 173 ? 0.9491 1.0966 0.7983 0.0986  -0.0049 0.0201  388 HIS B CG  
1232 N ND1 . HIS A 173 ? 0.9077 1.0512 0.7748 0.0896  0.0003  0.0206  388 HIS B ND1 
1233 C CD2 . HIS A 173 ? 0.9847 1.2101 0.8400 0.1067  -0.0150 0.0090  388 HIS B CD2 
1234 C CE1 . HIS A 173 ? 0.8797 1.0949 0.7615 0.0912  -0.0055 0.0108  388 HIS B CE1 
1235 N NE2 . HIS A 173 ? 0.9488 1.2176 0.8250 0.1011  -0.0145 0.0027  388 HIS B NE2 
1236 N N   . LYS A 174 ? 0.9516 0.9015 0.7507 0.0780  0.0223  0.0447  389 LYS B N   
1237 C CA  . LYS A 174 ? 0.9840 0.9000 0.7622 0.0718  0.0289  0.0482  389 LYS B CA  
1238 C C   . LYS A 174 ? 1.0319 0.9371 0.8269 0.0461  0.0381  0.0423  389 LYS B C   
1239 O O   . LYS A 174 ? 1.0722 0.9854 0.8616 0.0348  0.0382  0.0363  389 LYS B O   
1240 C CB  . LYS A 174 ? 0.9496 0.8143 0.7044 0.0842  0.0335  0.0580  389 LYS B CB  
1241 C CG  . LYS A 174 ? 0.8570 0.7171 0.5873 0.1140  0.0207  0.0637  389 LYS B CG  
1242 C CD  . LYS A 174 ? 0.9446 0.7403 0.6456 0.1177  0.0254  0.0751  389 LYS B CD  
1243 C CE  . LYS A 174 ? 0.9188 0.6901 0.6061 0.1451  0.0140  0.0781  389 LYS B CE  
1244 N NZ  . LYS A 174 ? 0.9899 0.7010 0.6657 0.1336  0.0239  0.0851  389 LYS B NZ  
1245 N N   . LEU A 175 ? 0.9822 0.8705 0.7975 0.0386  0.0438  0.0419  390 LEU B N   
1246 C CA  . LEU A 175 ? 0.9869 0.8607 0.8175 0.0203  0.0494  0.0350  390 LEU B CA  
1247 C C   . LEU A 175 ? 1.0040 0.9007 0.8444 0.0043  0.0409  0.0285  390 LEU B C   
1248 O O   . LEU A 175 ? 0.9992 0.8786 0.8446 -0.0081 0.0417  0.0206  390 LEU B O   
1249 C CB  . LEU A 175 ? 0.9239 0.7783 0.7728 0.0190  0.0548  0.0366  390 LEU B CB  
1250 C CG  . LEU A 175 ? 0.9656 0.8051 0.8336 0.0065  0.0571  0.0294  390 LEU B CG  
1251 C CD1 . LEU A 175 ? 0.9690 0.7875 0.8332 0.0069  0.0687  0.0233  390 LEU B CD1 
1252 C CD2 . LEU A 175 ? 0.9285 0.7682 0.8154 0.0059  0.0552  0.0332  390 LEU B CD2 
1253 N N   . ARG A 176 ? 1.2290 1.1646 1.0701 0.0039  0.0319  0.0300  391 ARG B N   
1254 C CA  . ARG A 176 ? 1.2275 1.1859 1.0727 -0.0179 0.0236  0.0246  391 ARG B CA  
1255 C C   . ARG A 176 ? 1.2289 1.1990 1.0575 -0.0214 0.0208  0.0173  391 ARG B C   
1256 O O   . ARG A 176 ? 1.2378 1.2040 1.0656 -0.0422 0.0159  0.0096  391 ARG B O   
1257 C CB  . ARG A 176 ? 1.2047 1.2120 1.0589 -0.0218 0.0164  0.0274  391 ARG B CB  
1258 C CG  . ARG A 176 ? 1.2034 1.2660 1.0488 -0.0182 0.0091  0.0228  391 ARG B CG  
1259 C CD  . ARG A 176 ? 1.2087 1.3326 1.0663 -0.0237 0.0029  0.0218  391 ARG B CD  
1260 N NE  . ARG A 176 ? 1.2315 1.3575 1.0965 -0.0597 0.0002  0.0232  391 ARG B NE  
1261 C CZ  . ARG A 176 ? 1.2268 1.4105 1.0987 -0.0793 -0.0049 0.0221  391 ARG B CZ  
1262 N NH1 . ARG A 176 ? 1.2213 1.4757 1.0988 -0.0627 -0.0078 0.0157  391 ARG B NH1 
1263 N NH2 . ARG A 176 ? 1.2368 1.4079 1.1076 -0.1164 -0.0083 0.0269  391 ARG B NH2 
1264 N N   . GLN A 177 ? 1.0709 1.0501 0.8830 -0.0018 0.0224  0.0196  392 GLN B N   
1265 C CA  . GLN A 177 ? 1.1103 1.1093 0.9048 -0.0036 0.0185  0.0133  392 GLN B CA  
1266 C C   . GLN A 177 ? 1.1278 1.0922 0.9109 -0.0080 0.0263  0.0068  392 GLN B C   
1267 O O   . GLN A 177 ? 1.1197 1.0993 0.8889 -0.0137 0.0232  -0.0015 392 GLN B O   
1268 C CB  . GLN A 177 ? 1.1323 1.1594 0.9103 0.0216  0.0132  0.0194  392 GLN B CB  
1269 C CG  . GLN A 177 ? 1.1750 1.1636 0.9293 0.0409  0.0193  0.0284  392 GLN B CG  
1270 C CD  . GLN A 177 ? 1.2172 1.2258 0.9477 0.0675  0.0089  0.0347  392 GLN B CD  
1271 O OE1 . GLN A 177 ? 1.2723 1.3172 1.0113 0.0823  -0.0010 0.0335  392 GLN B OE1 
1272 N NE2 . GLN A 177 ? 1.2683 1.2561 0.9670 0.0746  0.0100  0.0404  392 GLN B NE2 
1273 N N   . LEU A 178 ? 1.0842 1.0094 0.8738 -0.0061 0.0362  0.0079  393 LEU B N   
1274 C CA  . LEU A 178 ? 0.9865 0.8886 0.7699 -0.0101 0.0446  -0.0023 393 LEU B CA  
1275 C C   . LEU A 178 ? 0.9986 0.9032 0.7853 -0.0262 0.0375  -0.0185 393 LEU B C   
1276 O O   . LEU A 178 ? 1.0110 0.9172 0.8098 -0.0389 0.0281  -0.0193 393 LEU B O   
1277 C CB  . LEU A 178 ? 0.9719 0.8437 0.7703 -0.0085 0.0540  -0.0028 393 LEU B CB  
1278 C CG  . LEU A 178 ? 1.0105 0.8704 0.8055 0.0028  0.0617  0.0113  393 LEU B CG  
1279 C CD1 . LEU A 178 ? 0.9735 0.8118 0.7834 0.0004  0.0721  0.0061  393 LEU B CD1 
1280 C CD2 . LEU A 178 ? 0.9477 0.8091 0.7111 0.0109  0.0649  0.0201  393 LEU B CD2 
1281 N N   . PRO A 179 ? 1.0202 0.9239 0.7937 -0.0281 0.0409  -0.0320 394 PRO B N   
1282 C CA  . PRO A 179 ? 0.9241 0.8269 0.6962 -0.0427 0.0320  -0.0501 394 PRO B CA  
1283 C C   . PRO A 179 ? 0.9124 0.7776 0.6981 -0.0468 0.0298  -0.0661 394 PRO B C   
1284 O O   . PRO A 179 ? 0.9987 0.8513 0.7806 -0.0591 0.0192  -0.0812 394 PRO B O   
1285 C CB  . PRO A 179 ? 0.9999 0.9237 0.7489 -0.0396 0.0364  -0.0589 394 PRO B CB  
1286 C CG  . PRO A 179 ? 1.0356 0.9673 0.7705 -0.0247 0.0465  -0.0411 394 PRO B CG  
1287 C CD  . PRO A 179 ? 1.0139 0.9220 0.7667 -0.0188 0.0517  -0.0301 394 PRO B CD  
1288 N N   . GLU A 180 ? 0.8932 0.7386 0.6931 -0.0364 0.0375  -0.0645 395 GLU B N   
1289 C CA  . GLU A 180 ? 0.8796 0.6928 0.6921 -0.0335 0.0337  -0.0823 395 GLU B CA  
1290 C C   . GLU A 180 ? 0.9259 0.7223 0.7583 -0.0266 0.0356  -0.0717 395 GLU B C   
1291 O O   . GLU A 180 ? 0.9587 0.7693 0.7947 -0.0205 0.0467  -0.0572 395 GLU B O   
1292 C CB  . GLU A 180 ? 0.9809 0.8031 0.7892 -0.0234 0.0437  -0.1038 395 GLU B CB  
1293 C CG  . GLU A 180 ? 0.9851 0.8230 0.7736 -0.0294 0.0409  -0.1196 395 GLU B CG  
1294 C CD  . GLU A 180 ? 1.0279 0.8332 0.8168 -0.0346 0.0242  -0.1414 395 GLU B CD  
1295 O OE1 . GLU A 180 ? 1.0480 0.8157 0.8503 -0.0318 0.0145  -0.1425 395 GLU B OE1 
1296 O OE2 . GLU A 180 ? 1.0821 0.8955 0.8550 -0.0418 0.0193  -0.1571 395 GLU B OE2 
1297 N N   . ARG A 181 ? 0.9906 0.7523 0.8326 -0.0276 0.0231  -0.0791 396 ARG B N   
1298 C CA  . ARG A 181 ? 0.9147 0.6614 0.7748 -0.0205 0.0229  -0.0704 396 ARG B CA  
1299 C C   . ARG A 181 ? 0.8909 0.6511 0.7635 -0.0038 0.0374  -0.0807 396 ARG B C   
1300 O O   . ARG A 181 ? 0.8752 0.6430 0.7598 0.0001  0.0451  -0.0687 396 ARG B O   
1301 C CB  . ARG A 181 ? 0.9421 0.6426 0.8034 -0.0241 0.0030  -0.0762 396 ARG B CB  
1302 C CG  . ARG A 181 ? 0.9900 0.6779 0.8566 -0.0340 -0.0048 -0.0542 396 ARG B CG  
1303 C CD  . ARG A 181 ? 1.0951 0.7294 0.9517 -0.0443 -0.0277 -0.0549 396 ARG B CD  
1304 N NE  . ARG A 181 ? 1.1382 0.7350 1.0000 -0.0227 -0.0370 -0.0753 396 ARG B NE  
1305 C CZ  . ARG A 181 ? 1.1455 0.7409 1.0256 -0.0028 -0.0354 -0.0772 396 ARG B CZ  
1306 N NH1 . ARG A 181 ? 1.0756 0.7014 0.9703 -0.0033 -0.0234 -0.0597 396 ARG B NH1 
1307 N NH2 . ARG A 181 ? 1.0887 0.6548 0.9729 0.0199  -0.0467 -0.1000 396 ARG B NH2 
1308 N N   . TYR A 182 ? 0.9168 0.6853 0.7864 0.0043  0.0417  -0.1045 397 TYR B N   
1309 C CA  . TYR A 182 ? 0.8632 0.6546 0.7456 0.0165  0.0560  -0.1171 397 TYR B CA  
1310 C C   . TYR A 182 ? 0.8806 0.7005 0.7545 0.0091  0.0745  -0.0992 397 TYR B C   
1311 O O   . TYR A 182 ? 0.8761 0.7081 0.7614 0.0115  0.0854  -0.0966 397 TYR B O   
1312 C CB  . TYR A 182 ? 0.9143 0.7175 0.7950 0.0266  0.0566  -0.1501 397 TYR B CB  
1313 C CG  . TYR A 182 ? 0.9121 0.7456 0.7716 0.0180  0.0681  -0.1538 397 TYR B CG  
1314 C CD1 . TYR A 182 ? 0.9235 0.7953 0.7769 0.0137  0.0886  -0.1503 397 TYR B CD1 
1315 C CD2 . TYR A 182 ? 0.9329 0.7562 0.7749 0.0117  0.0578  -0.1607 397 TYR B CD2 
1316 C CE1 . TYR A 182 ? 0.9279 0.8253 0.7565 0.0046  0.0980  -0.1508 397 TYR B CE1 
1317 C CE2 . TYR A 182 ? 0.9203 0.7749 0.7413 0.0045  0.0675  -0.1639 397 TYR B CE2 
1318 C CZ  . TYR A 182 ? 0.9498 0.8407 0.7633 0.0018  0.0874  -0.1578 397 TYR B CZ  
1319 O OH  . TYR A 182 ? 0.9465 0.8664 0.7339 -0.0065 0.0963  -0.1579 397 TYR B OH  
1320 N N   . MET A 183 ? 0.9872 0.8154 0.8391 -0.0002 0.0763  -0.0864 398 MET B N   
1321 C CA  . MET A 183 ? 0.9730 0.8138 0.8102 -0.0051 0.0881  -0.0650 398 MET B CA  
1322 C C   . MET A 183 ? 0.9561 0.7829 0.8046 -0.0042 0.0850  -0.0448 398 MET B C   
1323 O O   . MET A 183 ? 0.9369 0.7648 0.7843 -0.0046 0.0953  -0.0346 398 MET B O   
1324 C CB  . MET A 183 ? 0.9580 0.8090 0.7687 -0.0101 0.0855  -0.0568 398 MET B CB  
1325 C CG  . MET A 183 ? 0.9474 0.8182 0.7420 -0.0125 0.0914  -0.0750 398 MET B CG  
1326 S SD  . MET A 183 ? 1.0725 0.9571 0.8386 -0.0174 0.0831  -0.0686 398 MET B SD  
1327 C CE  . MET A 183 ? 0.9584 0.8697 0.6945 -0.0217 0.0984  -0.0740 398 MET B CE  
1328 N N   . MET A 184 ? 0.9378 0.7515 0.7950 -0.0054 0.0706  -0.0399 399 MET B N   
1329 C CA  . MET A 184 ? 0.8543 0.6613 0.7229 -0.0050 0.0673  -0.0235 399 MET B CA  
1330 C C   . MET A 184 ? 0.8397 0.6404 0.7277 0.0003  0.0733  -0.0278 399 MET B C   
1331 O O   . MET A 184 ? 0.8953 0.6982 0.7851 0.0012  0.0808  -0.0167 399 MET B O   
1332 C CB  . MET A 184 ? 0.8569 0.6553 0.7303 -0.0123 0.0512  -0.0200 399 MET B CB  
1333 C CG  . MET A 184 ? 0.8460 0.6647 0.7077 -0.0177 0.0469  -0.0064 399 MET B CG  
1334 S SD  . MET A 184 ? 0.8411 0.6568 0.7004 -0.0362 0.0295  -0.0087 399 MET B SD  
1335 C CE  . MET A 184 ? 0.9067 0.7605 0.7470 -0.0406 0.0280  -0.0070 399 MET B CE  
1336 N N   . ASN A 185 ? 0.8149 0.6079 0.7165 0.0052  0.0688  -0.0459 400 ASN B N   
1337 C CA  . ASN A 185 ? 0.8136 0.6089 0.7356 0.0124  0.0731  -0.0528 400 ASN B CA  
1338 C C   . ASN A 185 ? 0.8242 0.6441 0.7440 0.0106  0.0920  -0.0585 400 ASN B C   
1339 O O   . ASN A 185 ? 0.8358 0.6640 0.7703 0.0115  0.0983  -0.0593 400 ASN B O   
1340 C CB  . ASN A 185 ? 0.8682 0.6494 0.8036 0.0234  0.0602  -0.0731 400 ASN B CB  
1341 C CG  . ASN A 185 ? 0.9088 0.6573 0.8449 0.0211  0.0405  -0.0626 400 ASN B CG  
1342 O OD1 . ASN A 185 ? 0.9091 0.6570 0.8459 0.0133  0.0395  -0.0426 400 ASN B OD1 
1343 N ND2 . ASN A 185 ? 0.9389 0.6586 0.8717 0.0266  0.0240  -0.0765 400 ASN B ND2 
1344 N N   . SER A 186 ? 0.8075 0.6406 0.7070 0.0050  0.1010  -0.0619 401 SER B N   
1345 C CA  . SER A 186 ? 0.8222 0.6776 0.7122 -0.0036 0.1194  -0.0643 401 SER B CA  
1346 C C   . SER A 186 ? 0.8769 0.7190 0.7529 -0.0123 0.1256  -0.0402 401 SER B C   
1347 O O   . SER A 186 ? 0.8810 0.7300 0.7617 -0.0198 0.1362  -0.0400 401 SER B O   
1348 C CB  . SER A 186 ? 0.8402 0.7116 0.7062 -0.0093 0.1261  -0.0714 401 SER B CB  
1349 O OG  . SER A 186 ? 0.9681 0.8456 0.8434 0.0004  0.1173  -0.0947 401 SER B OG  
1350 N N   . VAL A 187 ? 0.8710 0.6952 0.7282 -0.0111 0.1183  -0.0219 402 VAL B N   
1351 C CA  . VAL A 187 ? 0.8590 0.6643 0.7039 -0.0122 0.1185  -0.0014 402 VAL B CA  
1352 C C   . VAL A 187 ? 0.8464 0.6478 0.7173 -0.0099 0.1172  -0.0018 402 VAL B C   
1353 O O   . VAL A 187 ? 0.8175 0.6154 0.6871 -0.0175 0.1267  0.0005  402 VAL B O   
1354 C CB  . VAL A 187 ? 0.8727 0.6701 0.7043 -0.0040 0.1060  0.0117  402 VAL B CB  
1355 C CG1 . VAL A 187 ? 0.7607 0.5387 0.5779 0.0006  0.1043  0.0289  402 VAL B CG1 
1356 C CG2 . VAL A 187 ? 0.8593 0.6658 0.6667 -0.0058 0.1058  0.0097  402 VAL B CG2 
1357 N N   . LEU A 188 ? 0.8604 0.6626 0.7529 -0.0021 0.1048  -0.0049 403 LEU B N   
1358 C CA  . LEU A 188 ? 0.8408 0.6409 0.7564 0.0010  0.1003  -0.0037 403 LEU B CA  
1359 C C   . LEU A 188 ? 0.8483 0.6605 0.7813 -0.0016 0.1095  -0.0166 403 LEU B C   
1360 O O   . LEU A 188 ? 0.8354 0.6481 0.7849 0.0000  0.1073  -0.0151 403 LEU B O   
1361 C CB  . LEU A 188 ? 0.8343 0.6315 0.7637 0.0055  0.0849  -0.0060 403 LEU B CB  
1362 C CG  . LEU A 188 ? 0.8535 0.6492 0.7714 0.0040  0.0746  0.0058  403 LEU B CG  
1363 C CD1 . LEU A 188 ? 0.8635 0.6519 0.7924 0.0014  0.0603  0.0034  403 LEU B CD1 
1364 C CD2 . LEU A 188 ? 0.8146 0.6141 0.7289 0.0062  0.0750  0.0195  403 LEU B CD2 
1365 N N   . GLU A 189 ? 0.8656 0.6947 0.7961 -0.0057 0.1194  -0.0311 404 GLU B N   
1366 C CA  . GLU A 189 ? 0.8951 0.7492 0.8442 -0.0090 0.1288  -0.0469 404 GLU B CA  
1367 C C   . GLU A 189 ? 0.9072 0.7592 0.8445 -0.0253 0.1418  -0.0371 404 GLU B C   
1368 O O   . GLU A 189 ? 0.9527 0.8260 0.9073 -0.0310 0.1485  -0.0473 404 GLU B O   
1369 C CB  . GLU A 189 ? 0.8841 0.7680 0.8342 -0.0093 0.1365  -0.0689 404 GLU B CB  
1370 C CG  . GLU A 189 ? 0.9206 0.8402 0.9010 -0.0016 0.1381  -0.0939 404 GLU B CG  
1371 C CD  . GLU A 189 ? 1.1926 1.1427 1.1787 0.0079  0.1393  -0.1214 404 GLU B CD  
1372 O OE1 . GLU A 189 ? 1.2381 1.1995 1.2018 -0.0040 0.1503  -0.1223 404 GLU B OE1 
1373 O OE2 . GLU A 189 ? 1.2283 1.1908 1.2394 0.0287  0.1280  -0.1432 404 GLU B OE2 
1374 N N   . ASN A 190 ? 0.8578 0.6830 0.7639 -0.0325 0.1439  -0.0185 405 ASN B N   
1375 C CA  . ASN A 190 ? 0.9340 0.7405 0.8191 -0.0482 0.1528  -0.0068 405 ASN B CA  
1376 C C   . ASN A 190 ? 0.9054 0.6815 0.7876 -0.0389 0.1424  0.0079  405 ASN B C   
1377 O O   . ASN A 190 ? 0.9717 0.7177 0.8287 -0.0469 0.1449  0.0196  405 ASN B O   
1378 C CB  . ASN A 190 ? 0.9930 0.7855 0.8373 -0.0621 0.1609  0.0027  405 ASN B CB  
1379 C CG  . ASN A 190 ? 0.9621 0.7940 0.8094 -0.0717 0.1719  -0.0145 405 ASN B CG  
1380 O OD1 . ASN A 190 ? 0.8782 0.7436 0.7413 -0.0845 0.1833  -0.0300 405 ASN B OD1 
1381 N ND2 . ASN A 190 ? 0.9653 0.8004 0.7995 -0.0649 0.1684  -0.0151 405 ASN B ND2 
1382 N N   . PHE A 191 ? 0.8377 0.6202 0.7424 -0.0228 0.1299  0.0069  406 PHE B N   
1383 C CA  . PHE A 191 ? 0.8694 0.6363 0.7736 -0.0126 0.1195  0.0178  406 PHE B CA  
1384 C C   . PHE A 191 ? 0.8387 0.6218 0.7741 -0.0101 0.1158  0.0106  406 PHE B C   
1385 O O   . PHE A 191 ? 0.8969 0.6966 0.8531 -0.0045 0.1093  0.0034  406 PHE B O   
1386 C CB  . PHE A 191 ? 0.8307 0.5989 0.7294 -0.0008 0.1080  0.0240  406 PHE B CB  
1387 C CG  . PHE A 191 ? 0.9177 0.6846 0.8187 0.0096  0.0977  0.0318  406 PHE B CG  
1388 C CD1 . PHE A 191 ? 0.8920 0.6770 0.8173 0.0122  0.0895  0.0296  406 PHE B CD1 
1389 C CD2 . PHE A 191 ? 0.9297 0.6780 0.8059 0.0178  0.0948  0.0406  406 PHE B CD2 
1390 C CE1 . PHE A 191 ? 0.8395 0.6338 0.7669 0.0195  0.0813  0.0349  406 PHE B CE1 
1391 C CE2 . PHE A 191 ? 0.9331 0.6897 0.8133 0.0307  0.0850  0.0432  406 PHE B CE2 
1392 C CZ  . PHE A 191 ? 0.9039 0.6885 0.8110 0.0299  0.0796  0.0398  406 PHE B CZ  
1393 N N   . THR A 192 ? 0.8341 0.6093 0.7702 -0.0146 0.1190  0.0119  407 THR B N   
1394 C CA  . THR A 192 ? 0.9119 0.7048 0.8753 -0.0119 0.1145  0.0059  407 THR B CA  
1395 C C   . THR A 192 ? 0.9044 0.6843 0.8621 -0.0079 0.1100  0.0122  407 THR B C   
1396 O O   . THR A 192 ? 0.8955 0.6481 0.8276 -0.0066 0.1107  0.0189  407 THR B O   
1397 C CB  . THR A 192 ? 0.8871 0.7007 0.8671 -0.0231 0.1242  -0.0081 407 THR B CB  
1398 O OG1 . THR A 192 ? 0.9543 0.7523 0.9187 -0.0381 0.1336  -0.0069 407 THR B OG1 
1399 C CG2 . THR A 192 ? 0.9242 0.7557 0.9068 -0.0266 0.1309  -0.0188 407 THR B CG2 
1400 N N   . ILE A 193 ? 0.8670 0.6662 0.8470 -0.0041 0.1037  0.0088  408 ILE B N   
1401 C CA  . ILE A 193 ? 0.8599 0.6574 0.8390 0.0010  0.0988  0.0109  408 ILE B CA  
1402 C C   . ILE A 193 ? 0.8135 0.6286 0.8132 -0.0056 0.1008  0.0016  408 ILE B C   
1403 O O   . ILE A 193 ? 0.7846 0.6230 0.8054 -0.0051 0.0972  -0.0026 408 ILE B O   
1404 C CB  . ILE A 193 ? 0.8066 0.6207 0.7897 0.0118  0.0866  0.0177  408 ILE B CB  
1405 C CG1 . ILE A 193 ? 0.8224 0.6241 0.7834 0.0202  0.0841  0.0244  408 ILE B CG1 
1406 C CG2 . ILE A 193 ? 0.8454 0.6745 0.8362 0.0156  0.0819  0.0152  408 ILE B CG2 
1407 C CD1 . ILE A 193 ? 0.7721 0.6007 0.7375 0.0259  0.0736  0.0294  408 ILE B CD1 
1408 N N   . LEU A 194 ? 0.8137 0.6154 0.8052 -0.0107 0.1048  -0.0026 409 LEU B N   
1409 C CA  . LEU A 194 ? 0.8532 0.6750 0.8630 -0.0170 0.1056  -0.0125 409 LEU B CA  
1410 C C   . LEU A 194 ? 0.8554 0.6833 0.8657 -0.0067 0.0968  -0.0122 409 LEU B C   
1411 O O   . LEU A 194 ? 0.8635 0.6676 0.8536 0.0012  0.0946  -0.0105 409 LEU B O   
1412 C CB  . LEU A 194 ? 0.8450 0.6506 0.8448 -0.0362 0.1175  -0.0209 409 LEU B CB  
1413 C CG  . LEU A 194 ? 0.8494 0.6863 0.8719 -0.0475 0.1206  -0.0345 409 LEU B CG  
1414 C CD1 . LEU A 194 ? 0.7701 0.6495 0.8219 -0.0405 0.1164  -0.0388 409 LEU B CD1 
1415 C CD2 . LEU A 194 ? 0.9716 0.7969 0.9820 -0.0730 0.1337  -0.0426 409 LEU B CD2 
1416 N N   . GLN A 195 ? 0.9116 0.7735 0.9433 -0.0048 0.0904  -0.0147 410 GLN B N   
1417 C CA  . GLN A 195 ? 0.8949 0.7750 0.9286 0.0029  0.0825  -0.0153 410 GLN B CA  
1418 C C   . GLN A 195 ? 0.8924 0.7922 0.9403 -0.0041 0.0832  -0.0266 410 GLN B C   
1419 O O   . GLN A 195 ? 0.8778 0.8023 0.9441 -0.0079 0.0806  -0.0276 410 GLN B O   
1420 C CB  . GLN A 195 ? 0.8843 0.7898 0.9246 0.0080  0.0722  -0.0043 410 GLN B CB  
1421 C CG  . GLN A 195 ? 0.9152 0.8512 0.9583 0.0112  0.0650  -0.0049 410 GLN B CG  
1422 C CD  . GLN A 195 ? 1.0240 0.9768 1.0605 0.0135  0.0576  0.0064  410 GLN B CD  
1423 O OE1 . GLN A 195 ? 1.0624 1.0102 1.0869 0.0216  0.0586  0.0060  410 GLN B OE1 
1424 N NE2 . GLN A 195 ? 1.0379 1.0098 1.0798 0.0054  0.0488  0.0169  410 GLN B NE2 
1425 N N   . VAL A 196 ? 0.7809 0.6686 0.8189 -0.0042 0.0851  -0.0367 411 VAL B N   
1426 C CA  . VAL A 196 ? 0.8041 0.7073 0.8525 -0.0136 0.0869  -0.0504 411 VAL B CA  
1427 C C   . VAL A 196 ? 0.7667 0.6915 0.8149 -0.0036 0.0793  -0.0566 411 VAL B C   
1428 O O   . VAL A 196 ? 0.7650 0.6675 0.7955 0.0066  0.0777  -0.0622 411 VAL B O   
1429 C CB  . VAL A 196 ? 0.8194 0.6845 0.8529 -0.0287 0.0966  -0.0604 411 VAL B CB  
1430 C CG1 . VAL A 196 ? 0.7435 0.6303 0.7893 -0.0417 0.0982  -0.0763 411 VAL B CG1 
1431 C CG2 . VAL A 196 ? 0.8501 0.7030 0.8821 -0.0406 0.1055  -0.0549 411 VAL B CG2 
1432 N N   . VAL A 197 ? 0.7477 0.7172 0.8137 -0.0051 0.0733  -0.0567 412 VAL B N   
1433 C CA  . VAL A 197 ? 0.7367 0.7383 0.8039 0.0006  0.0671  -0.0645 412 VAL B CA  
1434 C C   . VAL A 197 ? 0.7316 0.7444 0.8074 -0.0096 0.0694  -0.0814 412 VAL B C   
1435 O O   . VAL A 197 ? 0.7233 0.7527 0.8146 -0.0195 0.0702  -0.0814 412 VAL B O   
1436 C CB  . VAL A 197 ? 0.7026 0.7473 0.7772 0.0022  0.0576  -0.0504 412 VAL B CB  
1437 C CG1 . VAL A 197 ? 0.7120 0.7938 0.7819 0.0084  0.0528  -0.0581 412 VAL B CG1 
1438 C CG2 . VAL A 197 ? 0.6748 0.7056 0.7435 0.0047  0.0556  -0.0325 412 VAL B CG2 
1439 N N   . THR A 198 ? 0.7593 0.7645 0.8250 -0.0058 0.0694  -0.0983 413 THR B N   
1440 C CA  . THR A 198 ? 0.7685 0.7809 0.8390 -0.0173 0.0713  -0.1174 413 THR B CA  
1441 C C   . THR A 198 ? 0.7960 0.8384 0.8639 -0.0071 0.0649  -0.1322 413 THR B C   
1442 O O   . THR A 198 ? 0.7979 0.8392 0.8546 0.0100  0.0610  -0.1334 413 THR B O   
1443 C CB  . THR A 198 ? 0.8425 0.7960 0.8955 -0.0287 0.0789  -0.1283 413 THR B CB  
1444 O OG1 . THR A 198 ? 0.8950 0.8008 0.9242 -0.0139 0.0775  -0.1240 413 THR B OG1 
1445 C CG2 . THR A 198 ? 0.8375 0.7835 0.8987 -0.0477 0.0875  -0.1214 413 THR B CG2 
1446 N N   . ASN A 199 ? 0.8288 0.9042 0.9079 -0.0170 0.0636  -0.1457 414 ASN B N   
1447 C CA  . ASN A 199 ? 0.8497 0.9518 0.9250 -0.0100 0.0587  -0.1662 414 ASN B CA  
1448 C C   . ASN A 199 ? 0.9427 0.9863 0.9955 -0.0022 0.0598  -0.1862 414 ASN B C   
1449 O O   . ASN A 199 ? 1.0225 1.0209 1.0668 -0.0179 0.0644  -0.1960 414 ASN B O   
1450 C CB  . ASN A 199 ? 0.8862 1.0299 0.9767 -0.0251 0.0575  -0.1776 414 ASN B CB  
1451 C CG  . ASN A 199 ? 0.9541 1.1450 1.0438 -0.0183 0.0514  -0.1962 414 ASN B CG  
1452 O OD1 . ASN A 199 ? 0.9346 1.1231 1.0117 -0.0017 0.0489  -0.2075 414 ASN B OD1 
1453 N ND2 . ASN A 199 ? 0.9394 1.1785 1.0425 -0.0296 0.0483  -0.2015 414 ASN B ND2 
1454 N N   . ARG A 200 ? 0.9014 0.9453 0.9422 0.0213  0.0542  -0.1931 415 ARG B N   
1455 C CA  . ARG A 200 ? 0.9772 0.9589 0.9926 0.0356  0.0507  -0.2134 415 ARG B CA  
1456 C C   . ARG A 200 ? 1.0495 1.0172 1.0586 0.0259  0.0491  -0.2415 415 ARG B C   
1457 O O   . ARG A 200 ? 1.1349 1.0271 1.1196 0.0216  0.0480  -0.2531 415 ARG B O   
1458 C CB  . ARG A 200 ? 0.9670 0.9704 0.9751 0.0679  0.0427  -0.2220 415 ARG B CB  
1459 C CG  . ARG A 200 ? 1.0396 0.9740 1.0185 0.0907  0.0345  -0.2453 415 ARG B CG  
1460 C CD  . ARG A 200 ? 1.0175 0.9931 0.9943 0.1268  0.0249  -0.2641 415 ARG B CD  
1461 N NE  . ARG A 200 ? 1.0604 1.0929 1.0465 0.1309  0.0217  -0.2920 415 ARG B NE  
1462 C CZ  . ARG A 200 ? 1.0627 1.1557 1.0522 0.1587  0.0148  -0.3141 415 ARG B CZ  
1463 N NH1 . ARG A 200 ? 1.0870 1.1911 1.0715 0.1871  0.0092  -0.3140 415 ARG B NH1 
1464 N NH2 . ARG A 200 ? 1.0687 1.2203 1.0674 0.1577  0.0135  -0.3383 415 ARG B NH2 
1465 N N   . ASP A 201 ? 1.0764 1.1129 1.1036 0.0206  0.0478  -0.2525 416 ASP B N   
1466 C CA  . ASP A 201 ? 1.1088 1.1373 1.1304 0.0111  0.0457  -0.2821 416 ASP B CA  
1467 C C   . ASP A 201 ? 1.1123 1.1143 1.1375 -0.0230 0.0532  -0.2790 416 ASP B C   
1468 O O   . ASP A 201 ? 1.1820 1.1189 1.1859 -0.0361 0.0535  -0.2953 416 ASP B O   
1469 C CB  . ASP A 201 ? 1.1000 1.2169 1.1386 0.0150  0.0419  -0.2958 416 ASP B CB  
1470 C CG  . ASP A 201 ? 1.1022 1.2694 1.1413 0.0429  0.0365  -0.2975 416 ASP B CG  
1471 O OD1 . ASP A 201 ? 1.0426 1.1724 1.0648 0.0683  0.0318  -0.3085 416 ASP B OD1 
1472 O OD2 . ASP A 201 ? 1.0901 1.3379 1.1450 0.0384  0.0361  -0.2882 416 ASP B OD2 
1473 N N   . THR A 202 ? 1.0308 1.0837 1.0810 -0.0383 0.0582  -0.2596 417 THR B N   
1474 C CA  . THR A 202 ? 1.0517 1.1077 1.1124 -0.0688 0.0646  -0.2622 417 THR B CA  
1475 C C   . THR A 202 ? 1.0609 1.0656 1.1149 -0.0847 0.0732  -0.2456 417 THR B C   
1476 O O   . THR A 202 ? 1.0424 1.0500 1.1031 -0.1128 0.0798  -0.2509 417 THR B O   
1477 C CB  . THR A 202 ? 1.0180 1.1586 1.1088 -0.0737 0.0627  -0.2532 417 THR B CB  
1478 O OG1 . THR A 202 ? 0.9910 1.1433 1.0926 -0.0660 0.0634  -0.2236 417 THR B OG1 
1479 C CG2 . THR A 202 ? 0.9800 1.1798 1.0752 -0.0598 0.0543  -0.2644 417 THR B CG2 
1480 N N   . GLN A 203 ? 1.0529 1.0190 1.0945 -0.0688 0.0735  -0.2272 418 GLN B N   
1481 C CA  . GLN A 203 ? 1.1053 1.0244 1.1373 -0.0821 0.0815  -0.2105 418 GLN B CA  
1482 C C   . GLN A 203 ? 0.9767 0.9463 1.0370 -0.0931 0.0874  -0.1948 418 GLN B C   
1483 O O   . GLN A 203 ? 1.0200 0.9631 1.0756 -0.1066 0.0953  -0.1843 418 GLN B O   
1484 C CB  . GLN A 203 ? 1.1345 0.9857 1.1393 -0.1100 0.0865  -0.2237 418 GLN B CB  
1485 C CG  . GLN A 203 ? 1.1499 0.9198 1.1152 -0.0964 0.0784  -0.2347 418 GLN B CG  
1486 C CD  . GLN A 203 ? 1.1807 0.9242 1.1339 -0.0643 0.0732  -0.2175 418 GLN B CD  
1487 O OE1 . GLN A 203 ? 1.2058 0.9465 1.1512 -0.0331 0.0628  -0.2275 418 GLN B OE1 
1488 N NE2 . GLN A 203 ? 1.1459 0.8770 1.0986 -0.0712 0.0803  -0.1940 418 GLN B NE2 
1489 N N   . GLU A 204 ? 0.9221 0.9625 1.0092 -0.0866 0.0823  -0.1935 419 GLU B N   
1490 C CA  . GLU A 204 ? 0.8887 0.9703 1.0000 -0.0922 0.0844  -0.1814 419 GLU B CA  
1491 C C   . GLU A 204 ? 0.8831 0.9607 0.9959 -0.0728 0.0813  -0.1565 419 GLU B C   
1492 O O   . GLU A 204 ? 0.9005 0.9736 1.0041 -0.0547 0.0753  -0.1481 419 GLU B O   
1493 C CB  . GLU A 204 ? 0.9244 1.0774 1.0598 -0.0927 0.0772  -0.1893 419 GLU B CB  
1494 C CG  . GLU A 204 ? 0.9403 1.1273 1.0766 -0.0729 0.0658  -0.1830 419 GLU B CG  
1495 C CD  . GLU A 204 ? 0.9515 1.2005 1.1027 -0.0778 0.0587  -0.1962 419 GLU B CD  
1496 O OE1 . GLU A 204 ? 0.9158 1.1982 1.0860 -0.0869 0.0581  -0.1995 419 GLU B OE1 
1497 O OE2 . GLU A 204 ? 0.9191 1.1875 1.0630 -0.0719 0.0535  -0.2056 419 GLU B OE2 
1498 N N   . LEU A 205 ? 0.8379 0.9219 0.9626 -0.0777 0.0853  -0.1469 420 LEU B N   
1499 C CA  . LEU A 205 ? 0.7639 0.8376 0.8883 -0.0625 0.0827  -0.1254 420 LEU B CA  
1500 C C   . LEU A 205 ? 0.6846 0.8036 0.8244 -0.0476 0.0696  -0.1135 420 LEU B C   
1501 O O   . LEU A 205 ? 0.6263 0.7886 0.7843 -0.0495 0.0640  -0.1198 420 LEU B O   
1502 C CB  . LEU A 205 ? 0.7691 0.8295 0.8972 -0.0734 0.0922  -0.1234 420 LEU B CB  
1503 C CG  . LEU A 205 ? 0.7319 0.7776 0.8587 -0.0598 0.0906  -0.1046 420 LEU B CG  
1504 C CD1 . LEU A 205 ? 0.7620 0.7574 0.8677 -0.0698 0.1020  -0.1017 420 LEU B CD1 
1505 C CD2 . LEU A 205 ? 0.7223 0.8078 0.8730 -0.0549 0.0864  -0.1046 420 LEU B CD2 
1506 N N   . LEU A 206 ? 0.6370 0.7458 0.7667 -0.0339 0.0633  -0.0961 421 LEU B N   
1507 C CA  . LEU A 206 ? 0.6640 0.8038 0.7991 -0.0244 0.0494  -0.0806 421 LEU B CA  
1508 C C   . LEU A 206 ? 0.7014 0.8216 0.8352 -0.0167 0.0450  -0.0619 421 LEU B C   
1509 O O   . LEU A 206 ? 0.7514 0.8882 0.8917 -0.0105 0.0325  -0.0526 421 LEU B O   
1510 C CB  . LEU A 206 ? 0.7265 0.8827 0.8489 -0.0203 0.0436  -0.0759 421 LEU B CB  
1511 C CG  . LEU A 206 ? 0.6568 0.8291 0.7764 -0.0239 0.0471  -0.0971 421 LEU B CG  
1512 C CD1 . LEU A 206 ? 0.6401 0.8184 0.7448 -0.0156 0.0455  -0.0960 421 LEU B CD1 
1513 C CD2 . LEU A 206 ? 0.6385 0.8586 0.7701 -0.0292 0.0400  -0.1054 421 LEU B CD2 
1514 N N   . LEU A 207 ? 0.7088 0.7910 0.8319 -0.0158 0.0530  -0.0568 422 LEU B N   
1515 C CA  . LEU A 207 ? 0.6990 0.7615 0.8198 -0.0094 0.0491  -0.0418 422 LEU B CA  
1516 C C   . LEU A 207 ? 0.7207 0.7464 0.8338 -0.0121 0.0619  -0.0442 422 LEU B C   
1517 O O   . LEU A 207 ? 0.7507 0.7547 0.8487 -0.0128 0.0680  -0.0451 422 LEU B O   
1518 C CB  . LEU A 207 ? 0.7087 0.7717 0.8158 -0.0055 0.0386  -0.0231 422 LEU B CB  
1519 C CG  . LEU A 207 ? 0.6919 0.7498 0.7967 -0.0013 0.0241  -0.0062 422 LEU B CG  
1520 C CD1 . LEU A 207 ? 0.6735 0.7548 0.7909 0.0031  0.0128  -0.0099 422 LEU B CD1 
1521 C CD2 . LEU A 207 ? 0.7570 0.8225 0.8439 -0.0068 0.0160  0.0105  422 LEU B CD2 
1522 N N   . CYS A 208 ? 0.7553 0.7756 0.8769 -0.0117 0.0647  -0.0460 423 CYS B N   
1523 C CA  . CYS A 208 ? 0.7205 0.7103 0.8329 -0.0163 0.0766  -0.0470 423 CYS B CA  
1524 C C   . CYS A 208 ? 0.6969 0.6785 0.8107 -0.0066 0.0704  -0.0374 423 CYS B C   
1525 O O   . CYS A 208 ? 0.6782 0.6793 0.8074 0.0006  0.0629  -0.0417 423 CYS B O   
1526 C CB  . CYS A 208 ? 0.6998 0.6987 0.8203 -0.0309 0.0890  -0.0642 423 CYS B CB  
1527 S SG  . CYS A 208 ? 0.7766 0.7400 0.8794 -0.0431 0.1045  -0.0641 423 CYS B SG  
1528 N N   . THR A 209 ? 0.7024 0.6555 0.7993 -0.0043 0.0719  -0.0264 424 THR B N   
1529 C CA  . THR A 209 ? 0.7366 0.6784 0.8317 0.0037  0.0643  -0.0175 424 THR B CA  
1530 C C   . THR A 209 ? 0.7257 0.6429 0.8085 0.0009  0.0751  -0.0174 424 THR B C   
1531 O O   . THR A 209 ? 0.7241 0.6222 0.7895 0.0001  0.0777  -0.0093 424 THR B O   
1532 C CB  . THR A 209 ? 0.7104 0.6490 0.7951 0.0068  0.0511  -0.0012 424 THR B CB  
1533 O OG1 . THR A 209 ? 0.7425 0.7059 0.8328 0.0055  0.0440  -0.0007 424 THR B OG1 
1534 C CG2 . THR A 209 ? 0.6948 0.6204 0.7783 0.0131  0.0384  0.0062  424 THR B CG2 
1535 N N   . ALA A 210 ? 0.6752 0.5979 0.7667 0.0011  0.0800  -0.0275 425 ALA B N   
1536 C CA  . ALA A 210 ? 0.7430 0.6476 0.8224 -0.0016 0.0888  -0.0275 425 ALA B CA  
1537 C C   . ALA A 210 ? 0.7344 0.6233 0.8071 0.0086  0.0773  -0.0176 425 ALA B C   
1538 O O   . ALA A 210 ? 0.7341 0.6279 0.8169 0.0185  0.0639  -0.0186 425 ALA B O   
1539 C CB  . ALA A 210 ? 0.7509 0.6787 0.8433 -0.0062 0.0985  -0.0450 425 ALA B CB  
1540 N N   . TYR A 211 ? 0.7412 0.6086 0.7945 0.0062  0.0806  -0.0082 426 TYR B N   
1541 C CA  . TYR A 211 ? 0.7353 0.5888 0.7797 0.0112  0.0707  0.0004  426 TYR B CA  
1542 C C   . TYR A 211 ? 0.8093 0.6537 0.8456 0.0107  0.0788  -0.0057 426 TYR B C   
1543 O O   . TYR A 211 ? 0.8116 0.6481 0.8333 0.0044  0.0904  -0.0043 426 TYR B O   
1544 C CB  . TYR A 211 ? 0.7344 0.5824 0.7639 0.0090  0.0668  0.0140  426 TYR B CB  
1545 C CG  . TYR A 211 ? 0.8028 0.6666 0.8374 0.0079  0.0579  0.0204  426 TYR B CG  
1546 C CD1 . TYR A 211 ? 0.7698 0.6351 0.8041 0.0058  0.0431  0.0293  426 TYR B CD1 
1547 C CD2 . TYR A 211 ? 0.7868 0.6618 0.8224 0.0074  0.0635  0.0176  426 TYR B CD2 
1548 C CE1 . TYR A 211 ? 0.7940 0.6777 0.8290 0.0013  0.0356  0.0365  426 TYR B CE1 
1549 C CE2 . TYR A 211 ? 0.8254 0.7215 0.8650 0.0061  0.0561  0.0214  426 TYR B CE2 
1550 C CZ  . TYR A 211 ? 0.8122 0.7158 0.8515 0.0021  0.0429  0.0315  426 TYR B CZ  
1551 O OH  . TYR A 211 ? 0.7728 0.7011 0.8126 -0.0026 0.0359  0.0366  426 TYR B OH  
1552 N N   . VAL A 212 ? 0.7902 0.6330 0.8327 0.0181  0.0712  -0.0129 427 VAL B N   
1553 C CA  . VAL A 212 ? 0.7790 0.6161 0.8124 0.0185  0.0770  -0.0197 427 VAL B CA  
1554 C C   . VAL A 212 ? 0.7672 0.5831 0.7885 0.0209  0.0637  -0.0110 427 VAL B C   
1555 O O   . VAL A 212 ? 0.8161 0.6224 0.8384 0.0220  0.0490  -0.0027 427 VAL B O   
1556 C CB  . VAL A 212 ? 0.7444 0.6017 0.7940 0.0259  0.0799  -0.0410 427 VAL B CB  
1557 C CG1 . VAL A 212 ? 0.7818 0.6671 0.8419 0.0168  0.0948  -0.0500 427 VAL B CG1 
1558 C CG2 . VAL A 212 ? 0.8006 0.6531 0.8634 0.0417  0.0607  -0.0466 427 VAL B CG2 
1559 N N   . PHE A 213 ? 0.8004 0.6095 0.8071 0.0183  0.0687  -0.0120 428 PHE B N   
1560 C CA  . PHE A 213 ? 0.8000 0.5932 0.7919 0.0152  0.0583  -0.0026 428 PHE B CA  
1561 C C   . PHE A 213 ? 0.8400 0.6238 0.8252 0.0185  0.0557  -0.0145 428 PHE B C   
1562 O O   . PHE A 213 ? 0.9117 0.7071 0.8966 0.0207  0.0674  -0.0270 428 PHE B O   
1563 C CB  . PHE A 213 ? 0.8093 0.6069 0.7857 0.0089  0.0644  0.0100  428 PHE B CB  
1564 C CG  . PHE A 213 ? 0.8473 0.6539 0.8278 0.0076  0.0634  0.0197  428 PHE B CG  
1565 C CD1 . PHE A 213 ? 0.8283 0.6401 0.8157 0.0089  0.0731  0.0166  428 PHE B CD1 
1566 C CD2 . PHE A 213 ? 0.7740 0.5874 0.7506 0.0029  0.0531  0.0303  428 PHE B CD2 
1567 C CE1 . PHE A 213 ? 0.8089 0.6289 0.7996 0.0090  0.0715  0.0224  428 PHE B CE1 
1568 C CE2 . PHE A 213 ? 0.7686 0.5974 0.7496 0.0027  0.0527  0.0360  428 PHE B CE2 
1569 C CZ  . PHE A 213 ? 0.7508 0.5812 0.7389 0.0075  0.0614  0.0314  428 PHE B CZ  
1570 N N   . GLU A 214 ? 0.8480 0.6112 0.8251 0.0161  0.0400  -0.0108 429 GLU B N   
1571 C CA  . GLU A 214 ? 0.8450 0.5943 0.8101 0.0159  0.0349  -0.0199 429 GLU B CA  
1572 C C   . GLU A 214 ? 0.8768 0.6154 0.8254 0.0010  0.0245  -0.0052 429 GLU B C   
1573 O O   . GLU A 214 ? 0.8458 0.5928 0.7939 -0.0076 0.0220  0.0104  429 GLU B O   
1574 C CB  . GLU A 214 ? 0.8345 0.5624 0.8063 0.0291  0.0216  -0.0373 429 GLU B CB  
1575 C CG  . GLU A 214 ? 0.8685 0.6194 0.8542 0.0432  0.0328  -0.0597 429 GLU B CG  
1576 C CD  . GLU A 214 ? 0.9705 0.7025 0.9626 0.0623  0.0165  -0.0812 429 GLU B CD  
1577 O OE1 . GLU A 214 ? 0.9739 0.6782 0.9516 0.0639  0.0050  -0.0894 429 GLU B OE1 
1578 O OE2 . GLU A 214 ? 0.9499 0.6934 0.9606 0.0771  0.0133  -0.0909 429 GLU B OE2 
1579 N N   . VAL A 215 ? 0.9446 0.6696 0.8794 -0.0036 0.0183  -0.0121 430 VAL B N   
1580 C CA  . VAL A 215 ? 0.9635 0.6828 0.8822 -0.0222 0.0078  -0.0001 430 VAL B CA  
1581 C C   . VAL A 215 ? 0.9875 0.6624 0.8957 -0.0282 -0.0126 -0.0044 430 VAL B C   
1582 O O   . VAL A 215 ? 1.0346 0.6843 0.9456 -0.0130 -0.0183 -0.0218 430 VAL B O   
1583 C CB  . VAL A 215 ? 0.9477 0.6885 0.8536 -0.0283 0.0149  -0.0016 430 VAL B CB  
1584 C CG1 . VAL A 215 ? 0.9377 0.7129 0.8465 -0.0247 0.0279  0.0091  430 VAL B CG1 
1585 C CG2 . VAL A 215 ? 0.9445 0.6797 0.8474 -0.0179 0.0202  -0.0210 430 VAL B CG2 
1586 N N   . SER A 216 ? 1.0140 0.6799 0.9078 -0.0510 -0.0244 0.0110  431 SER B N   
1587 C CA  . SER A 216 ? 1.1387 0.7528 1.0140 -0.0645 -0.0469 0.0144  431 SER B CA  
1588 C C   . SER A 216 ? 1.2777 0.8801 1.1310 -0.0860 -0.0541 0.0109  431 SER B C   
1589 O O   . SER A 216 ? 1.3017 0.9440 1.1506 -0.1052 -0.0475 0.0198  431 SER B O   
1590 C CB  . SER A 216 ? 1.1046 0.7208 0.9752 -0.0820 -0.0543 0.0366  431 SER B CB  
1591 O OG  . SER A 216 ? 1.1984 0.7550 1.0471 -0.0936 -0.0779 0.0435  431 SER B OG  
1592 N N   . THR A 217 ? 1.4320 0.9826 1.2720 -0.0811 -0.0685 -0.0047 432 THR B N   
1593 C CA  . THR A 217 ? 1.4849 1.0117 1.2998 -0.1045 -0.0796 -0.0097 432 THR B CA  
1594 C C   . THR A 217 ? 1.5332 1.0570 1.3268 -0.1449 -0.0899 0.0130  432 THR B C   
1595 O O   . THR A 217 ? 1.6104 1.0736 1.3806 -0.1606 -0.1111 0.0215  432 THR B O   
1596 C CB  . THR A 217 ? 1.5397 0.9944 1.3394 -0.0919 -0.0998 -0.0292 432 THR B CB  
1597 O OG1 . THR A 217 ? 1.6351 1.0368 1.4264 -0.0877 -0.1187 -0.0190 432 THR B OG1 
1598 C CG2 . THR A 217 ? 1.4819 0.9513 1.3013 -0.0554 -0.0891 -0.0570 432 THR B CG2 
1599 N N   . SER A 218 ? 1.7405 1.3292 1.5390 -0.1627 -0.0767 0.0222  433 SER B N   
1600 C CA  . SER A 218 ? 1.7815 1.3943 1.5699 -0.1963 -0.0806 0.0441  433 SER B CA  
1601 C C   . SER A 218 ? 1.8413 1.4166 1.5944 -0.2401 -0.0994 0.0499  433 SER B C   
1602 O O   . SER A 218 ? 1.8669 1.4901 1.6119 -0.2726 -0.0967 0.0554  433 SER B O   
1603 C CB  . SER A 218 ? 1.7645 1.4649 1.5709 -0.1963 -0.0621 0.0477  433 SER B CB  
1604 O OG  . SER A 218 ? 1.7720 1.5039 1.5629 -0.2295 -0.0654 0.0480  433 SER B OG  
1605 N N   . GLU A 219 ? 1.7015 1.1894 1.4320 -0.2405 -0.1200 0.0467  434 GLU B N   
1606 C CA  . GLU A 219 ? 1.6200 1.0539 1.3131 -0.2816 -0.1418 0.0656  434 GLU B CA  
1607 C C   . GLU A 219 ? 1.5663 0.9840 1.2616 -0.2727 -0.1468 0.0841  434 GLU B C   
1608 O O   . GLU A 219 ? 1.5932 1.0110 1.2665 -0.3099 -0.1547 0.1071  434 GLU B O   
1609 C CB  . GLU A 219 ? 1.7074 1.0411 1.3664 -0.2872 -0.1668 0.0541  434 GLU B CB  
1610 C CG  . GLU A 219 ? 1.6878 1.0267 1.3459 -0.2860 -0.1635 0.0291  434 GLU B CG  
1611 C CD  . GLU A 219 ? 1.7728 1.0101 1.3870 -0.3071 -0.1919 0.0215  434 GLU B CD  
1612 O OE1 . GLU A 219 ? 1.7616 0.9135 1.3502 -0.3057 -0.2150 0.0312  434 GLU B OE1 
1613 O OE2 . GLU A 219 ? 1.8140 1.0532 1.4162 -0.3251 -0.1930 0.0057  434 GLU B OE2 
1614 N N   . ARG A 220 ? 1.4640 0.8734 1.1852 -0.2256 -0.1418 0.0733  435 ARG B N   
1615 C CA  . ARG A 220 ? 1.4223 0.8408 1.1568 -0.2101 -0.1404 0.0867  435 ARG B CA  
1616 C C   . ARG A 220 ? 1.3937 0.9088 1.1599 -0.2066 -0.1143 0.0908  435 ARG B C   
1617 O O   . ARG A 220 ? 1.3545 0.9159 1.1457 -0.1855 -0.0957 0.0752  435 ARG B O   
1618 C CB  . ARG A 220 ? 1.3505 0.7319 1.1024 -0.1615 -0.1448 0.0695  435 ARG B CB  
1619 C CG  . ARG A 220 ? 1.3562 0.6692 1.0923 -0.1473 -0.1612 0.0480  435 ARG B CG  
1620 C CD  . ARG A 220 ? 1.3449 0.6470 1.1062 -0.0957 -0.1610 0.0248  435 ARG B CD  
1621 N NE  . ARG A 220 ? 1.3302 0.6143 1.0953 -0.0785 -0.1716 0.0356  435 ARG B NE  
1622 C CZ  . ARG A 220 ? 1.3289 0.5699 1.0975 -0.0405 -0.1879 0.0193  435 ARG B CZ  
1623 N NH1 . ARG A 220 ? 1.3332 0.5449 1.1027 -0.0145 -0.1952 -0.0103 435 ARG B NH1 
1624 N NH2 . ARG A 220 ? 1.3192 0.5513 1.0909 -0.0266 -0.1979 0.0309  435 ARG B NH2 
1625 N N   . GLY A 221 ? 1.2546 0.7981 1.0166 -0.2268 -0.1141 0.1112  436 GLY B N   
1626 C CA  . GLY A 221 ? 1.1491 0.7780 0.9410 -0.2169 -0.0920 0.1119  436 GLY B CA  
1627 C C   . GLY A 221 ? 1.0900 0.7191 0.9106 -0.1741 -0.0835 0.1033  436 GLY B C   
1628 O O   . GLY A 221 ? 1.1462 0.7247 0.9692 -0.1492 -0.0906 0.0912  436 GLY B O   
1629 N N   . ALA A 222 ? 1.0208 0.7073 0.8624 -0.1656 -0.0693 0.1072  437 ALA B N   
1630 C CA  . ALA A 222 ? 0.9347 0.6236 0.8025 -0.1294 -0.0604 0.0979  437 ALA B CA  
1631 C C   . ALA A 222 ? 0.9864 0.6190 0.8451 -0.1216 -0.0785 0.1033  437 ALA B C   
1632 O O   . ALA A 222 ? 1.0882 0.6754 0.9169 -0.1444 -0.0988 0.1174  437 ALA B O   
1633 C CB  . ALA A 222 ? 0.8819 0.6360 0.7696 -0.1239 -0.0442 0.1004  437 ALA B CB  
1634 N N   . GLN A 223 ? 0.9263 0.5610 0.8089 -0.0895 -0.0722 0.0917  438 GLN B N   
1635 C CA  . GLN A 223 ? 0.9559 0.5463 0.8361 -0.0723 -0.0891 0.0914  438 GLN B CA  
1636 C C   . GLN A 223 ? 0.8906 0.5178 0.8049 -0.0426 -0.0732 0.0768  438 GLN B C   
1637 O O   . GLN A 223 ? 0.8503 0.5193 0.7831 -0.0370 -0.0518 0.0674  438 GLN B O   
1638 C CB  . GLN A 223 ? 1.0740 0.5975 0.9376 -0.0624 -0.1077 0.0806  438 GLN B CB  
1639 C CG  . GLN A 223 ? 1.2002 0.6544 1.0271 -0.0766 -0.1379 0.0971  438 GLN B CG  
1640 C CD  . GLN A 223 ? 1.2973 0.6789 1.1075 -0.0598 -0.1585 0.0817  438 GLN B CD  
1641 O OE1 . GLN A 223 ? 1.3041 0.6940 1.1262 -0.0485 -0.1482 0.0606  438 GLN B OE1 
1642 N NE2 . GLN A 223 ? 1.2383 0.5459 1.0176 -0.0576 -0.1894 0.0916  438 GLN B NE2 
1643 N N   . HIS A 224 ? 0.8427 0.4537 0.7627 -0.0249 -0.0847 0.0754  439 HIS B N   
1644 C CA  . HIS A 224 ? 0.8488 0.5022 0.8005 -0.0033 -0.0692 0.0622  439 HIS B CA  
1645 C C   . HIS A 224 ? 0.8583 0.4895 0.8157 0.0211  -0.0863 0.0548  439 HIS B C   
1646 O O   . HIS A 224 ? 0.8708 0.4540 0.8043 0.0196  -0.1117 0.0662  439 HIS B O   
1647 C CB  . HIS A 224 ? 0.8292 0.5319 0.7885 -0.0172 -0.0556 0.0737  439 HIS B CB  
1648 C CG  . HIS A 224 ? 0.9013 0.5966 0.8439 -0.0310 -0.0719 0.0932  439 HIS B CG  
1649 N ND1 . HIS A 224 ? 0.8959 0.6024 0.8495 -0.0178 -0.0771 0.0926  439 HIS B ND1 
1650 C CD2 . HIS A 224 ? 0.8558 0.5326 0.7681 -0.0590 -0.0856 0.1144  439 HIS B CD2 
1651 C CE1 . HIS A 224 ? 0.8567 0.5508 0.7863 -0.0356 -0.0935 0.1136  439 HIS B CE1 
1652 N NE2 . HIS A 224 ? 0.8997 0.5748 0.8029 -0.0624 -0.0986 0.1276  439 HIS B NE2 
1653 N N   . HIS A 225 ? 0.8805 0.5478 0.8680 0.0429  -0.0731 0.0351  440 HIS B N   
1654 C CA  . HIS A 225 ? 0.9100 0.5780 0.9110 0.0688  -0.0859 0.0235  440 HIS B CA  
1655 C C   . HIS A 225 ? 0.8610 0.5876 0.8883 0.0693  -0.0674 0.0186  440 HIS B C   
1656 O O   . HIS A 225 ? 0.8174 0.5785 0.8595 0.0627  -0.0430 0.0103  440 HIS B O   
1657 C CB  . HIS A 225 ? 0.9470 0.6057 0.9601 0.0969  -0.0898 -0.0043 440 HIS B CB  
1658 C CG  . HIS A 225 ? 1.0016 0.6372 1.0153 0.1271  -0.1164 -0.0145 440 HIS B CG  
1659 N ND1 . HIS A 225 ? 0.9860 0.6450 1.0104 0.1368  -0.1237 -0.0114 440 HIS B ND1 
1660 C CD2 . HIS A 225 ? 1.1427 0.7350 1.1473 0.1535  -0.1390 -0.0303 440 HIS B CD2 
1661 C CE1 . HIS A 225 ? 1.0645 0.6963 1.0860 0.1687  -0.1506 -0.0233 440 HIS B CE1 
1662 N NE2 . HIS A 225 ? 1.1422 0.7315 1.1517 0.1808  -0.1608 -0.0358 440 HIS B NE2 
1663 N N   . ILE A 226 ? 0.8121 0.5459 0.8415 0.0757  -0.0803 0.0245  441 ILE B N   
1664 C CA  . ILE A 226 ? 0.8256 0.6127 0.8779 0.0750  -0.0658 0.0189  441 ILE B CA  
1665 C C   . ILE A 226 ? 0.8557 0.6655 0.9320 0.1031  -0.0721 -0.0044 441 ILE B C   
1666 O O   . ILE A 226 ? 0.8607 0.6417 0.9289 0.1241  -0.0979 -0.0058 441 ILE B O   
1667 C CB  . ILE A 226 ? 0.8509 0.6429 0.8888 0.0588  -0.0741 0.0414  441 ILE B CB  
1668 C CG1 . ILE A 226 ? 0.8137 0.6014 0.8323 0.0308  -0.0652 0.0598  441 ILE B CG1 
1669 C CG2 . ILE A 226 ? 0.7949 0.6398 0.8565 0.0612  -0.0623 0.0317  441 ILE B CG2 
1670 C CD1 . ILE A 226 ? 0.7457 0.5226 0.7376 0.0122  -0.0817 0.0849  441 ILE B CD1 
1671 N N   . TYR A 227 ? 0.8098 0.6709 0.9135 0.1034  -0.0497 -0.0236 442 TYR B N   
1672 C CA  . TYR A 227 ? 0.8405 0.7409 0.9711 0.1260  -0.0516 -0.0497 442 TYR B CA  
1673 C C   . TYR A 227 ? 0.7785 0.7305 0.9275 0.1153  -0.0382 -0.0540 442 TYR B C   
1674 O O   . TYR A 227 ? 0.7235 0.6825 0.8684 0.0915  -0.0199 -0.0446 442 TYR B O   
1675 C CB  . TYR A 227 ? 0.8627 0.7849 1.0095 0.1329  -0.0355 -0.0754 442 TYR B CB  
1676 C CG  . TYR A 227 ? 0.8487 0.7272 0.9812 0.1473  -0.0482 -0.0792 442 TYR B CG  
1677 C CD1 . TYR A 227 ? 0.8171 0.6614 0.9292 0.1289  -0.0396 -0.0655 442 TYR B CD1 
1678 C CD2 . TYR A 227 ? 0.9423 0.8148 1.0812 0.1811  -0.0702 -0.0988 442 TYR B CD2 
1679 C CE1 . TYR A 227 ? 0.9231 0.7270 1.0208 0.1398  -0.0516 -0.0704 442 TYR B CE1 
1680 C CE2 . TYR A 227 ? 0.9793 0.8065 1.1030 0.1953  -0.0835 -0.1051 442 TYR B CE2 
1681 C CZ  . TYR A 227 ? 1.0012 0.7938 1.1040 0.1725  -0.0734 -0.0905 442 TYR B CZ  
1682 O OH  . TYR A 227 ? 1.1061 0.8536 1.1927 0.1843  -0.0867 -0.0982 442 TYR B OH  
1683 N N   . ARG A 228 ? 0.8204 0.8089 0.9894 0.1347  -0.0485 -0.0708 443 ARG B N   
1684 C CA  . ARG A 228 ? 0.7926 0.8397 0.9840 0.1249  -0.0343 -0.0831 443 ARG B CA  
1685 C C   . ARG A 228 ? 0.7681 0.8598 0.9818 0.1186  -0.0105 -0.1096 443 ARG B C   
1686 O O   . ARG A 228 ? 0.8104 0.9227 1.0387 0.1397  -0.0155 -0.1314 443 ARG B O   
1687 C CB  . ARG A 228 ? 0.8583 0.9323 1.0611 0.1482  -0.0572 -0.0907 443 ARG B CB  
1688 C CG  . ARG A 228 ? 0.9064 0.9456 1.0841 0.1472  -0.0789 -0.0627 443 ARG B CG  
1689 C CD  . ARG A 228 ? 0.9499 0.9838 1.1255 0.1810  -0.1125 -0.0655 443 ARG B CD  
1690 N NE  . ARG A 228 ? 0.9641 1.0665 1.1746 0.2016  -0.1122 -0.0975 443 ARG B NE  
1691 C CZ  . ARG A 228 ? 1.0204 1.1310 1.2414 0.2401  -0.1342 -0.1172 443 ARG B CZ  
1692 N NH1 . ARG A 228 ? 1.0223 1.0660 1.2187 0.2634  -0.1600 -0.1079 443 ARG B NH1 
1693 N NH2 . ARG A 228 ? 0.9761 1.1644 1.2321 0.2560  -0.1315 -0.1488 443 ARG B NH2 
1694 N N   . LEU A 229 ? 0.7476 0.8541 0.9616 0.0895  0.0142  -0.1087 444 LEU B N   
1695 C CA  . LEU A 229 ? 0.7259 0.8756 0.9558 0.0754  0.0371  -0.1312 444 LEU B CA  
1696 C C   . LEU A 229 ? 0.7648 0.9831 1.0228 0.0780  0.0370  -0.1546 444 LEU B C   
1697 O O   . LEU A 229 ? 0.7369 0.9674 0.9970 0.0691  0.0347  -0.1496 444 LEU B O   
1698 C CB  . LEU A 229 ? 0.7251 0.8538 0.9378 0.0427  0.0600  -0.1198 444 LEU B CB  
1699 C CG  . LEU A 229 ? 0.7266 0.8029 0.9150 0.0391  0.0643  -0.1032 444 LEU B CG  
1700 C CD1 . LEU A 229 ? 0.6521 0.7080 0.8219 0.0114  0.0845  -0.0943 444 LEU B CD1 
1701 C CD2 . LEU A 229 ? 0.7831 0.8702 0.9782 0.0520  0.0649  -0.1187 444 LEU B CD2 
1702 N N   . VAL A 230 ? 0.7960 1.0660 1.0763 0.0897  0.0398  -0.1826 445 VAL B N   
1703 C CA  . VAL A 230 ? 0.7782 1.1258 1.0892 0.0977  0.0366  -0.2098 445 VAL B CA  
1704 C C   . VAL A 230 ? 0.7833 1.1945 1.1108 0.0757  0.0618  -0.2370 445 VAL B C   
1705 O O   . VAL A 230 ? 0.7942 1.1833 1.1060 0.0539  0.0808  -0.2320 445 VAL B O   
1706 C CB  . VAL A 230 ? 0.7547 1.1153 1.0794 0.1450  0.0058  -0.2216 445 VAL B CB  
1707 C CG1 . VAL A 230 ? 0.7289 1.0319 1.0330 0.1593  -0.0196 -0.1929 445 VAL B CG1 
1708 C CG2 . VAL A 230 ? 0.7203 1.0645 1.0430 0.1674  0.0014  -0.2323 445 VAL B CG2 
1709 N N   . ARG A 231 ? 0.7519 1.2473 1.1100 0.0803  0.0611  -0.2661 446 ARG B N   
1710 C CA  . ARG A 231 ? 0.7653 1.3363 1.1397 0.0502  0.0864  -0.2931 446 ARG B CA  
1711 C C   . ARG A 231 ? 0.6881 1.3603 1.1007 0.0651  0.0783  -0.3273 446 ARG B C   
1712 O O   . ARG A 231 ? 0.7538 1.5054 1.1905 0.0708  0.0849  -0.3601 446 ARG B O   
1713 C CB  . ARG A 231 ? 0.8046 1.3493 1.1567 -0.0033 0.1112  -0.2774 446 ARG B CB  
1714 C CG  . ARG A 231 ? 0.8430 1.4359 1.1943 -0.0455 0.1401  -0.2949 446 ARG B CG  
1715 C CD  . ARG A 231 ? 0.8414 1.3654 1.1541 -0.0911 0.1592  -0.2695 446 ARG B CD  
1716 N NE  . ARG A 231 ? 0.8858 1.4246 1.1972 -0.1252 0.1669  -0.2726 446 ARG B NE  
1717 C CZ  . ARG A 231 ? 0.9317 1.4142 1.2097 -0.1655 0.1809  -0.2560 446 ARG B CZ  
1718 N NH1 . ARG A 231 ? 0.9543 1.3640 1.1970 -0.1765 0.1889  -0.2337 446 ARG B NH1 
1719 N NH2 . ARG A 231 ? 0.9340 1.4301 1.2121 -0.1933 0.1848  -0.2625 446 ARG B NH2 
1720 N N   . GLY B 7   ? 1.3049 0.8790 1.3031 0.3096  0.2345  -0.0095 222 GLY A N   
1721 C CA  . GLY B 7   ? 1.2896 0.8994 1.2727 0.2627  0.2148  -0.0217 222 GLY A CA  
1722 C C   . GLY B 7   ? 1.3162 0.9916 1.3137 0.2631  0.1733  0.0009  222 GLY A C   
1723 O O   . GLY B 7   ? 1.3450 1.0572 1.3678 0.2929  0.1565  0.0206  222 GLY A O   
1724 N N   . LEU B 8   ? 1.1012 0.7928 1.0849 0.2293  0.1572  -0.0033 223 LEU A N   
1725 C CA  . LEU B 8   ? 1.0440 0.7884 1.0409 0.2256  0.1216  0.0115  223 LEU A CA  
1726 C C   . LEU B 8   ? 1.0294 0.8358 1.0506 0.2082  0.1104  0.0040  223 LEU A C   
1727 O O   . LEU B 8   ? 0.9984 0.8264 1.0154 0.1780  0.1038  -0.0033 223 LEU A O   
1728 C CB  . LEU B 8   ? 1.0069 0.7366 0.9820 0.2039  0.1138  0.0120  223 LEU A CB  
1729 C CG  . LEU B 8   ? 0.9555 0.7229 0.9388 0.1975  0.0833  0.0209  223 LEU A CG  
1730 C CD1 . LEU B 8   ? 0.9299 0.7265 0.9316 0.2209  0.0605  0.0348  223 LEU A CD1 
1731 C CD2 . LEU B 8   ? 0.9622 0.7019 0.9206 0.1914  0.0854  0.0240  223 LEU A CD2 
1732 N N   . GLY B 9   ? 0.9581 0.7986 1.0071 0.2283  0.1086  0.0096  224 GLY A N   
1733 C CA  . GLY B 9   ? 0.9249 0.8262 0.9974 0.2111  0.1013  0.0067  224 GLY A CA  
1734 C C   . GLY B 9   ? 0.8606 0.8051 0.9694 0.2361  0.0999  0.0157  224 GLY A C   
1735 O O   . GLY B 9   ? 0.9170 0.8487 1.0350 0.2703  0.1018  0.0257  224 GLY A O   
1736 N N   . THR B 10  ? 0.8107 0.8132 0.9421 0.2188  0.0964  0.0155  225 THR A N   
1737 C CA  . THR B 10  ? 0.7956 0.8533 0.9668 0.2370  0.1003  0.0214  225 THR A CA  
1738 C C   . THR B 10  ? 0.8034 0.8824 0.9734 0.2293  0.1329  0.0023  225 THR A C   
1739 O O   . THR B 10  ? 0.8226 0.8676 0.9570 0.2118  0.1523  -0.0180 225 THR A O   
1740 C CB  . THR B 10  ? 0.7494 0.8657 0.9532 0.2204  0.0695  0.0391  225 THR A CB  
1741 O OG1 . THR B 10  ? 0.7147 0.8434 0.9086 0.1823  0.0644  0.0397  225 THR A OG1 
1742 C CG2 . THR B 10  ? 0.7465 0.8449 0.9489 0.2286  0.0396  0.0507  225 THR A CG2 
1743 N N   . ALA B 11  ? 0.7758 0.9185 0.9848 0.2403  0.1397  0.0068  226 ALA A N   
1744 C CA  . ALA B 11  ? 0.7450 0.9249 0.9520 0.2262  0.1689  -0.0106 226 ALA A CA  
1745 C C   . ALA B 11  ? 0.7282 0.9361 0.9161 0.1793  0.1562  -0.0052 226 ALA A C   
1746 O O   . ALA B 11  ? 0.7363 0.9538 0.8960 0.1589  0.1783  -0.0234 226 ALA A O   
1747 C CB  . ALA B 11  ? 0.6716 0.9258 0.9303 0.2472  0.1791  -0.0038 226 ALA A CB  
1748 N N   . ARG B 12  ? 0.6792 0.8983 0.8802 0.1624  0.1213  0.0195  227 ARG A N   
1749 C CA  . ARG B 12  ? 0.6222 0.8714 0.8167 0.1237  0.1078  0.0347  227 ARG A CA  
1750 C C   . ARG B 12  ? 0.6874 0.8909 0.8447 0.1058  0.0952  0.0344  227 ARG A C   
1751 O O   . ARG B 12  ? 0.7001 0.9280 0.8417 0.0772  0.0929  0.0433  227 ARG A O   
1752 C CB  . ARG B 12  ? 0.6953 0.9798 0.9318 0.1142  0.0801  0.0615  227 ARG A CB  
1753 C CG  . ARG B 12  ? 0.7147 1.0661 0.9967 0.1241  0.0900  0.0657  227 ARG A CG  
1754 C CD  . ARG B 12  ? 0.7299 1.1181 1.0517 0.1012  0.0630  0.0907  227 ARG A CD  
1755 N NE  . ARG B 12  ? 0.7035 1.0920 1.0132 0.0632  0.0546  0.1100  227 ARG A NE  
1756 C CZ  . ARG B 12  ? 0.7114 1.1092 1.0490 0.0377  0.0323  0.1325  227 ARG A CZ  
1757 N NH1 . ARG B 12  ? 0.7111 1.1244 1.0883 0.0404  0.0144  0.1336  227 ARG A NH1 
1758 N NH2 . ARG B 12  ? 0.7188 1.1109 1.0448 0.0078  0.0278  0.1551  227 ARG A NH2 
1759 N N   . LEU B 13  ? 0.7761 0.9214 0.9206 0.1221  0.0869  0.0280  228 LEU A N   
1760 C CA  . LEU B 13  ? 0.7446 0.8545 0.8602 0.1068  0.0767  0.0275  228 LEU A CA  
1761 C C   . LEU B 13  ? 0.8191 0.8684 0.9115 0.1257  0.0889  0.0085  228 LEU A C   
1762 O O   . LEU B 13  ? 0.8150 0.8423 0.9187 0.1546  0.0917  0.0080  228 LEU A O   
1763 C CB  . LEU B 13  ? 0.6668 0.7738 0.8005 0.0999  0.0450  0.0508  228 LEU A CB  
1764 C CG  . LEU B 13  ? 0.7448 0.8292 0.8600 0.0866  0.0333  0.0555  228 LEU A CG  
1765 C CD1 . LEU B 13  ? 0.7243 0.8481 0.8272 0.0599  0.0363  0.0645  228 LEU A CD1 
1766 C CD2 . LEU B 13  ? 0.7970 0.8646 0.9340 0.0902  0.0071  0.0719  228 LEU A CD2 
1767 N N   . GLN B 14  ? 0.8232 0.8500 0.8839 0.1080  0.0966  -0.0046 229 GLN A N   
1768 C CA  . GLN B 14  ? 0.8377 0.8040 0.8751 0.1178  0.1107  -0.0212 229 GLN A CA  
1769 C C   . GLN B 14  ? 0.8775 0.8353 0.8974 0.0953  0.0997  -0.0202 229 GLN A C   
1770 O O   . GLN B 14  ? 0.8608 0.8578 0.8730 0.0680  0.0956  -0.0204 229 GLN A O   
1771 C CB  . GLN B 14  ? 0.8368 0.7802 0.8534 0.1175  0.1465  -0.0512 229 GLN A CB  
1772 C CG  . GLN B 14  ? 0.8854 0.8372 0.9242 0.1468  0.1625  -0.0534 229 GLN A CG  
1773 C CD  . GLN B 14  ? 0.9254 0.9320 0.9638 0.1306  0.1789  -0.0673 229 GLN A CD  
1774 O OE1 . GLN B 14  ? 0.9309 0.9575 0.9413 0.0966  0.1839  -0.0816 229 GLN A OE1 
1775 N NE2 . GLN B 14  ? 0.8750 0.9190 0.9458 0.1527  0.1850  -0.0601 229 GLN A NE2 
1776 N N   . LEU B 15  ? 0.8820 0.7954 0.8960 0.1077  0.0957  -0.0173 230 LEU A N   
1777 C CA  . LEU B 15  ? 0.9346 0.8416 0.9362 0.0897  0.0896  -0.0178 230 LEU A CA  
1778 C C   . LEU B 15  ? 0.9536 0.8354 0.9273 0.0691  0.1155  -0.0436 230 LEU A C   
1779 O O   . LEU B 15  ? 0.9525 0.7825 0.9133 0.0811  0.1387  -0.0570 230 LEU A O   
1780 C CB  . LEU B 15  ? 0.9681 0.8431 0.9722 0.1091  0.0783  -0.0059 230 LEU A CB  
1781 C CG  . LEU B 15  ? 0.9275 0.7798 0.9152 0.0981  0.0843  -0.0106 230 LEU A CG  
1782 C CD1 . LEU B 15  ? 0.8937 0.7915 0.8920 0.0763  0.0710  -0.0062 230 LEU A CD1 
1783 C CD2 . LEU B 15  ? 0.9407 0.7633 0.9259 0.1223  0.0772  0.0006  230 LEU A CD2 
1784 N N   . VAL B 16  ? 0.9748 0.8943 0.9409 0.0374  0.1113  -0.0498 231 VAL A N   
1785 C CA  . VAL B 16  ? 1.0329 0.9423 0.9725 0.0066  0.1332  -0.0792 231 VAL A CA  
1786 C C   . VAL B 16  ? 1.0732 0.9661 1.0082 -0.0079 0.1336  -0.0805 231 VAL A C   
1787 O O   . VAL B 16  ? 1.1621 1.0050 1.0776 -0.0210 0.1579  -0.1017 231 VAL A O   
1788 C CB  . VAL B 16  ? 1.0694 1.0497 1.0011 -0.0241 0.1274  -0.0865 231 VAL A CB  
1789 C CG1 . VAL B 16  ? 1.1890 1.1729 1.0919 -0.0645 0.1447  -0.1204 231 VAL A CG1 
1790 C CG2 . VAL B 16  ? 0.9305 0.9260 0.8629 -0.0126 0.1354  -0.0891 231 VAL A CG2 
1791 N N   . GLU B 17  ? 1.0287 0.9604 0.9843 -0.0044 0.1092  -0.0572 232 GLU A N   
1792 C CA  . GLU B 17  ? 1.0042 0.9385 0.9628 -0.0166 0.1088  -0.0558 232 GLU A CA  
1793 C C   . GLU B 17  ? 0.9529 0.8991 0.9367 0.0111  0.0875  -0.0288 232 GLU A C   
1794 O O   . GLU B 17  ? 0.9275 0.9174 0.9328 0.0185  0.0658  -0.0110 232 GLU A O   
1795 C CB  . GLU B 17  ? 1.0620 1.0624 1.0205 -0.0559 0.1039  -0.0656 232 GLU A CB  
1796 C CG  . GLU B 17  ? 1.0601 1.0672 1.0229 -0.0754 0.1101  -0.0704 232 GLU A CG  
1797 C CD  . GLU B 17  ? 1.1832 1.1617 1.1189 -0.1146 0.1367  -0.1048 232 GLU A CD  
1798 O OE1 . GLU B 17  ? 1.2700 1.2108 1.1823 -0.1190 0.1527  -0.1260 232 GLU A OE1 
1799 O OE2 . GLU B 17  ? 1.2003 1.1925 1.1398 -0.1417 0.1439  -0.1122 232 GLU A OE2 
1800 N N   . PHE B 18  ? 1.0008 0.9063 0.9801 0.0252  0.0953  -0.0261 233 PHE A N   
1801 C CA  . PHE B 18  ? 0.9515 0.8723 0.9504 0.0447  0.0804  -0.0093 233 PHE A CA  
1802 C C   . PHE B 18  ? 0.9375 0.8638 0.9345 0.0300  0.0937  -0.0139 233 PHE A C   
1803 O O   . PHE B 18  ? 0.9477 0.8350 0.9217 0.0148  0.1164  -0.0254 233 PHE A O   
1804 C CB  . PHE B 18  ? 0.8925 0.7713 0.8865 0.0782  0.0752  -0.0007 233 PHE A CB  
1805 C CG  . PHE B 18  ? 0.9227 0.8133 0.9315 0.0954  0.0635  0.0083  233 PHE A CG  
1806 C CD1 . PHE B 18  ? 0.9082 0.8331 0.9469 0.1031  0.0432  0.0184  233 PHE A CD1 
1807 C CD2 . PHE B 18  ? 0.9853 0.8528 0.9779 0.1027  0.0759  0.0066  233 PHE A CD2 
1808 C CE1 . PHE B 18  ? 0.9040 0.8334 0.9584 0.1208  0.0363  0.0220  233 PHE A CE1 
1809 C CE2 . PHE B 18  ? 0.9096 0.7910 0.9142 0.1189  0.0689  0.0093  233 PHE A CE2 
1810 C CZ  . PHE B 18  ? 0.8949 0.8045 0.9314 0.1290  0.0498  0.0145  233 PHE A CZ  
1811 N N   . SER B 19  ? 0.9823 0.9562 1.0067 0.0355  0.0817  -0.0036 234 SER A N   
1812 C CA  . SER B 19  ? 0.9463 0.9411 0.9771 0.0232  0.0947  -0.0064 234 SER A CA  
1813 C C   . SER B 19  ? 0.8987 0.9346 0.9635 0.0475  0.0816  0.0068  234 SER A C   
1814 O O   . SER B 19  ? 0.8643 0.9396 0.9578 0.0573  0.0615  0.0189  234 SER A O   
1815 C CB  . SER B 19  ? 0.9323 0.9732 0.9673 -0.0196 0.1017  -0.0181 234 SER A CB  
1816 O OG  . SER B 19  ? 0.9129 1.0312 0.9788 -0.0241 0.0799  -0.0080 234 SER A OG  
1817 N N   . ALA B 20  ? 0.8770 0.9012 0.9376 0.0580  0.0956  0.0051  235 ALA A N   
1818 C CA  . ALA B 20  ? 0.8093 0.8762 0.9036 0.0787  0.0921  0.0113  235 ALA A CA  
1819 C C   . ALA B 20  ? 0.7380 0.8518 0.8441 0.0545  0.1112  0.0074  235 ALA A C   
1820 O O   . ALA B 20  ? 0.7596 0.8416 0.8352 0.0331  0.1327  -0.0001 235 ALA A O   
1821 C CB  . ALA B 20  ? 0.7836 0.8063 0.8625 0.1117  0.0940  0.0084  235 ALA A CB  
1822 N N   . PHE B 21  ? 0.6417 0.8330 0.7952 0.0576  0.1039  0.0152  236 PHE A N   
1823 C CA  . PHE B 21  ? 0.6762 0.9351 0.8506 0.0252  0.1168  0.0124  236 PHE A CA  
1824 C C   . PHE B 21  ? 0.7170 1.0566 0.9485 0.0491  0.1133  0.0235  236 PHE A C   
1825 O O   . PHE B 21  ? 0.7537 1.0960 1.0109 0.0876  0.0973  0.0350  236 PHE A O   
1826 C CB  . PHE B 21  ? 0.8249 1.1188 0.9989 -0.0156 0.1063  0.0089  236 PHE A CB  
1827 C CG  . PHE B 21  ? 0.8510 1.1993 1.0563 -0.0023 0.0766  0.0258  236 PHE A CG  
1828 C CD1 . PHE B 21  ? 0.7934 1.0931 0.9808 0.0159  0.0607  0.0322  236 PHE A CD1 
1829 C CD2 . PHE B 21  ? 0.8447 1.2981 1.0993 -0.0077 0.0646  0.0393  236 PHE A CD2 
1830 C CE1 . PHE B 21  ? 0.7443 1.0908 0.9581 0.0269  0.0358  0.0532  236 PHE A CE1 
1831 C CE2 . PHE B 21  ? 0.8148 1.3177 1.0960 0.0070  0.0371  0.0623  236 PHE A CE2 
1832 C CZ  . PHE B 21  ? 0.7916 1.2370 1.0501 0.0234  0.0237  0.0700  236 PHE A CZ  
1833 N N   . VAL B 22  ? 0.7046 1.1091 0.9590 0.0261  0.1304  0.0204  237 VAL A N   
1834 C CA  . VAL B 22  ? 0.7336 1.2390 1.0531 0.0438  0.1277  0.0323  237 VAL A CA  
1835 C C   . VAL B 22  ? 0.7606 1.3609 1.1072 -0.0041 0.1227  0.0336  237 VAL A C   
1836 O O   . VAL B 22  ? 0.7673 1.3566 1.0865 -0.0525 0.1402  0.0179  237 VAL A O   
1837 C CB  . VAL B 22  ? 0.7442 1.2580 1.0753 0.0665  0.1561  0.0261  237 VAL A CB  
1838 C CG1 . VAL B 22  ? 0.6725 1.1643 0.9655 0.0253  0.1871  0.0130  237 VAL A CG1 
1839 C CG2 . VAL B 22  ? 0.6385 1.2649 1.0458 0.0886  0.1554  0.0386  237 VAL A CG2 
1840 N N   . GLU B 23  ? 0.8307 1.5219 1.2292 0.0077  0.0981  0.0531  238 GLU A N   
1841 C CA  . GLU B 23  ? 0.8159 1.6236 1.2492 -0.0342 0.0879  0.0567  238 GLU A CA  
1842 C C   . GLU B 23  ? 0.8084 1.7254 1.3128 -0.0154 0.0966  0.0688  238 GLU A C   
1843 O O   . GLU B 23  ? 0.8233 1.7434 1.3640 0.0433  0.0964  0.0844  238 GLU A O   
1844 C CB  . GLU B 23  ? 0.8009 1.6553 1.2451 -0.0333 0.0516  0.0763  238 GLU A CB  
1845 C CG  . GLU B 23  ? 0.8568 1.6329 1.2363 -0.0628 0.0443  0.0615  238 GLU A CG  
1846 C CD  . GLU B 23  ? 0.8208 1.6391 1.2078 -0.0531 0.0105  0.0857  238 GLU A CD  
1847 O OE1 . GLU B 23  ? 0.8541 1.6999 1.2120 -0.0988 -0.0003 0.0744  238 GLU A OE1 
1848 O OE2 . GLU B 23  ? 0.7552 1.5771 1.1753 -0.0009 -0.0036 0.1158  238 GLU A OE2 
1849 N N   . PRO B 24  ? 0.8311 1.8396 1.3595 -0.0642 0.1059  0.0604  239 PRO A N   
1850 C CA  . PRO B 24  ? 0.8165 1.9340 1.4154 -0.0478 0.1201  0.0699  239 PRO A CA  
1851 C C   . PRO B 24  ? 0.7993 2.0124 1.4700 0.0049  0.0930  0.1033  239 PRO A C   
1852 O O   . PRO B 24  ? 0.7566 1.9881 1.4264 0.0071  0.0590  0.1216  239 PRO A O   
1853 C CB  . PRO B 24  ? 0.8134 2.0180 1.4229 -0.1234 0.1275  0.0549  239 PRO A CB  
1854 C CG  . PRO B 24  ? 0.7722 1.9439 1.3320 -0.1701 0.1040  0.0435  239 PRO A CG  
1855 C CD  . PRO B 24  ? 0.8235 1.8388 1.3173 -0.1394 0.1069  0.0384  239 PRO A CD  
1856 N N   . PRO B 25  ? 0.8054 2.0792 1.5397 0.0521  0.1090  0.1144  240 PRO A N   
1857 C CA  . PRO B 25  ? 0.7857 2.1604 1.6025 0.1081  0.0887  0.1498  240 PRO A CA  
1858 C C   . PRO B 25  ? 0.7432 2.2600 1.6010 0.0737  0.0552  0.1713  240 PRO A C   
1859 O O   . PRO B 25  ? 0.7004 2.2319 1.5763 0.1089  0.0235  0.2027  240 PRO A O   
1860 C CB  . PRO B 25  ? 0.7252 2.1525 1.5980 0.1432  0.1242  0.1447  240 PRO A CB  
1861 C CG  . PRO B 25  ? 0.7769 2.0713 1.5774 0.1351  0.1582  0.1115  240 PRO A CG  
1862 C CD  . PRO B 25  ? 0.8470 2.0857 1.5740 0.0606  0.1517  0.0939  240 PRO A CD  
1863 N N   . GLN B 32  ? 1.1017 2.1280 1.4872 -0.4117 0.1239  -0.0655 247 GLN A N   
1864 C CA  . GLN B 32  ? 1.1850 2.0754 1.5076 -0.3838 0.1226  -0.0706 247 GLN A CA  
1865 C C   . GLN B 32  ? 1.1544 1.9880 1.4824 -0.3026 0.1208  -0.0411 247 GLN A C   
1866 O O   . GLN B 32  ? 1.0904 2.0041 1.4674 -0.2578 0.0995  -0.0130 247 GLN A O   
1867 C CB  . GLN B 32  ? 1.2454 2.0038 1.5081 -0.4263 0.1570  -0.1025 247 GLN A CB  
1868 C CG  . GLN B 32  ? 1.3122 2.0611 1.5375 -0.4882 0.1525  -0.1390 247 GLN A CG  
1869 C CD  . GLN B 32  ? 1.3739 1.9591 1.5337 -0.4979 0.1810  -0.1632 247 GLN A CD  
1870 O OE1 . GLN B 32  ? 1.3571 1.8998 1.4916 -0.5607 0.2037  -0.1980 247 GLN A OE1 
1871 N NE2 . GLN B 32  ? 1.3673 1.8594 1.5020 -0.4356 0.1809  -0.1449 247 GLN A NE2 
1872 N N   . ARG B 33  ? 1.2003 1.8962 1.4786 -0.2842 0.1431  -0.0477 248 ARG A N   
1873 C CA  . ARG B 33  ? 1.1235 1.7592 1.3985 -0.2145 0.1412  -0.0267 248 ARG A CA  
1874 C C   . ARG B 33  ? 1.1500 1.6589 1.3742 -0.2109 0.1722  -0.0356 248 ARG A C   
1875 O O   . ARG B 33  ? 1.2152 1.6577 1.3992 -0.2534 0.1903  -0.0552 248 ARG A O   
1876 C CB  . ARG B 33  ? 1.0959 1.7088 1.3578 -0.1809 0.1115  -0.0159 248 ARG A CB  
1877 C CG  . ARG B 33  ? 1.1061 1.6158 1.3060 -0.1997 0.1164  -0.0359 248 ARG A CG  
1878 C CD  . ARG B 33  ? 1.1217 1.5801 1.3068 -0.1512 0.0974  -0.0209 248 ARG A CD  
1879 N NE  . ARG B 33  ? 1.0953 1.6388 1.3116 -0.1378 0.0651  -0.0004 248 ARG A NE  
1880 C CZ  . ARG B 33  ? 1.1356 1.6525 1.3353 -0.1178 0.0470  0.0099  248 ARG A CZ  
1881 N NH1 . ARG B 33  ? 1.1846 1.5994 1.3417 -0.1073 0.0567  -0.0009 248 ARG A NH1 
1882 N NH2 . ARG B 33  ? 1.1003 1.7002 1.3291 -0.1077 0.0188  0.0349  248 ARG A NH2 
1883 N N   . HIS B 34  ? 0.8809 1.3560 1.1065 -0.1586 0.1783  -0.0206 249 HIS A N   
1884 C CA  . HIS B 34  ? 0.8867 1.2561 1.0644 -0.1478 0.2044  -0.0223 249 HIS A CA  
1885 C C   . HIS B 34  ? 0.8467 1.1299 0.9895 -0.1046 0.1895  -0.0178 249 HIS A C   
1886 O O   . HIS B 34  ? 0.8551 1.1602 1.0203 -0.0615 0.1689  -0.0072 249 HIS A O   
1887 C CB  . HIS B 34  ? 0.8520 1.2518 1.0488 -0.1257 0.2256  -0.0127 249 HIS A CB  
1888 C CG  . HIS B 34  ? 0.8373 1.1387 0.9796 -0.1137 0.2502  -0.0099 249 HIS A CG  
1889 N ND1 . HIS B 34  ? 0.8666 1.1277 0.9795 -0.1551 0.2814  -0.0111 249 HIS A ND1 
1890 C CD2 . HIS B 34  ? 0.8337 1.0716 0.9443 -0.0668 0.2471  -0.0040 249 HIS A CD2 
1891 C CE1 . HIS B 34  ? 0.9126 1.0924 0.9771 -0.1304 0.2957  -0.0013 249 HIS A CE1 
1892 N NE2 . HIS B 34  ? 0.8736 1.0421 0.9350 -0.0780 0.2741  0.0011  249 HIS A NE2 
1893 N N   . LEU B 35  ? 0.8507 1.0360 0.9423 -0.1156 0.2016  -0.0247 250 LEU A N   
1894 C CA  . LEU B 35  ? 0.8423 0.9497 0.9014 -0.0792 0.1894  -0.0208 250 LEU A CA  
1895 C C   . LEU B 35  ? 0.8754 0.9280 0.9061 -0.0478 0.2040  -0.0105 250 LEU A C   
1896 O O   . LEU B 35  ? 0.9419 0.9528 0.9444 -0.0667 0.2307  -0.0081 250 LEU A O   
1897 C CB  . LEU B 35  ? 0.8779 0.9175 0.9016 -0.1060 0.1958  -0.0338 250 LEU A CB  
1898 C CG  . LEU B 35  ? 0.8675 0.9336 0.8972 -0.1289 0.1791  -0.0482 250 LEU A CG  
1899 C CD1 . LEU B 35  ? 0.8909 0.9337 0.9145 -0.0897 0.1566  -0.0404 250 LEU A CD1 
1900 C CD2 . LEU B 35  ? 0.8406 1.0207 0.9143 -0.1527 0.1644  -0.0495 250 LEU A CD2 
1901 N N   . PHE B 36  ? 0.8494 0.9006 0.8847 -0.0027 0.1873  -0.0043 251 PHE A N   
1902 C CA  . PHE B 36  ? 0.8443 0.8423 0.8425 0.0252  0.1972  0.0018  251 PHE A CA  
1903 C C   . PHE B 36  ? 0.8921 0.8068 0.8467 0.0303  0.1951  0.0057  251 PHE A C   
1904 O O   . PHE B 36  ? 0.8591 0.7224 0.7756 0.0254  0.2153  0.0146  251 PHE A O   
1905 C CB  . PHE B 36  ? 0.8493 0.8699 0.8650 0.0676  0.1808  0.0007  251 PHE A CB  
1906 C CG  . PHE B 36  ? 0.7549 0.8561 0.8203 0.0729  0.1840  -0.0016 251 PHE A CG  
1907 C CD1 . PHE B 36  ? 0.7613 0.8991 0.8302 0.0622  0.2116  -0.0020 251 PHE A CD1 
1908 C CD2 . PHE B 36  ? 0.6617 0.8057 0.7733 0.0897  0.1609  0.0002  251 PHE A CD2 
1909 C CE1 . PHE B 36  ? 0.7541 0.9756 0.8765 0.0711  0.2162  -0.0036 251 PHE A CE1 
1910 C CE2 . PHE B 36  ? 0.7223 0.9436 0.8864 0.1009  0.1638  0.0022  251 PHE A CE2 
1911 C CZ  . PHE B 36  ? 0.7866 1.0500 0.9585 0.0930  0.1918  -0.0012 251 PHE A CZ  
1912 N N   . VAL B 37  ? 1.0102 0.9141 0.9725 0.0416  0.1718  0.0024  252 VAL A N   
1913 C CA  . VAL B 37  ? 1.0239 0.8622 0.9564 0.0469  0.1698  0.0047  252 VAL A CA  
1914 C C   . VAL B 37  ? 0.9933 0.8425 0.9418 0.0253  0.1617  -0.0061 252 VAL A C   
1915 O O   . VAL B 37  ? 0.9863 0.8969 0.9674 0.0153  0.1479  -0.0108 252 VAL A O   
1916 C CB  . VAL B 37  ? 1.0053 0.8226 0.9263 0.0862  0.1501  0.0108  252 VAL A CB  
1917 C CG1 . VAL B 37  ? 0.9689 0.7719 0.8600 0.1035  0.1606  0.0190  252 VAL A CG1 
1918 C CG2 . VAL B 37  ? 0.9328 0.7961 0.8907 0.0995  0.1250  0.0058  252 VAL A CG2 
1919 N N   . HIS B 38  ? 0.9051 0.6961 0.8294 0.0200  0.1715  -0.0093 253 HIS A N   
1920 C CA  . HIS B 38  ? 0.9724 0.7703 0.9033 -0.0062 0.1715  -0.0259 253 HIS A CA  
1921 C C   . HIS B 38  ? 1.0144 0.7429 0.9215 0.0073  0.1802  -0.0279 253 HIS A C   
1922 O O   . HIS B 38  ? 1.0796 0.7440 0.9629 0.0005  0.2055  -0.0275 253 HIS A O   
1923 C CB  . HIS B 38  ? 0.9343 0.7495 0.8680 -0.0537 0.1910  -0.0405 253 HIS A CB  
1924 C CG  . HIS B 38  ? 1.0187 0.8522 0.9547 -0.0866 0.1902  -0.0634 253 HIS A CG  
1925 N ND1 . HIS B 38  ? 1.0395 0.9367 0.9954 -0.0836 0.1645  -0.0650 253 HIS A ND1 
1926 C CD2 . HIS B 38  ? 1.1175 0.9148 1.0356 -0.1257 0.2130  -0.0871 253 HIS A CD2 
1927 C CE1 . HIS B 38  ? 1.0251 0.9320 0.9714 -0.1189 0.1705  -0.0888 253 HIS A CE1 
1928 N NE2 . HIS B 38  ? 1.0961 0.9411 1.0198 -0.1457 0.2002  -0.1062 253 HIS A NE2 
1929 N N   . ILE B 39  ? 1.0113 0.7538 0.9282 0.0273  0.1611  -0.0278 254 ILE A N   
1930 C CA  . ILE B 39  ? 1.0412 0.7374 0.9457 0.0395  0.1694  -0.0331 254 ILE A CA  
1931 C C   . ILE B 39  ? 1.0701 0.7921 0.9791 0.0092  0.1729  -0.0572 254 ILE A C   
1932 O O   . ILE B 39  ? 1.0059 0.7922 0.9335 0.0039  0.1515  -0.0570 254 ILE A O   
1933 C CB  . ILE B 39  ? 1.0505 0.7546 0.9645 0.0787  0.1476  -0.0179 254 ILE A CB  
1934 C CG1 . ILE B 39  ? 1.0198 0.7045 0.9225 0.1060  0.1425  0.0022  254 ILE A CG1 
1935 C CG2 . ILE B 39  ? 1.0335 0.7055 0.9437 0.0924  0.1575  -0.0237 254 ILE A CG2 
1936 C CD1 . ILE B 39  ? 0.9536 0.6647 0.8701 0.1345  0.1154  0.0122  254 ILE A CD1 
1937 N N   . SER B 40  ? 1.1232 0.7937 1.0129 -0.0111 0.2009  -0.0777 255 SER A N   
1938 C CA  . SER B 40  ? 1.1857 0.8752 1.0706 -0.0419 0.2084  -0.1078 255 SER A CA  
1939 C C   . SER B 40  ? 1.2138 0.8452 1.0872 -0.0205 0.2275  -0.1190 255 SER A C   
1940 O O   . SER B 40  ? 1.2445 0.7986 1.1074 0.0004  0.2484  -0.1119 255 SER A O   
1941 C CB  . SER B 40  ? 1.1822 0.8667 1.0553 -0.0935 0.2277  -0.1331 255 SER A CB  
1942 O OG  . SER B 40  ? 1.2795 1.0144 1.1482 -0.1285 0.2250  -0.1620 255 SER A OG  
1943 N N   . GLN B 41  ? 1.2736 0.9453 1.1505 -0.0226 0.2215  -0.1331 256 GLN A N   
1944 C CA  . GLN B 41  ? 1.4143 1.0414 1.2866 0.0026  0.2415  -0.1443 256 GLN A CA  
1945 C C   . GLN B 41  ? 1.5537 1.2079 1.4125 -0.0267 0.2547  -0.1820 256 GLN A C   
1946 O O   . GLN B 41  ? 1.5353 1.1917 1.3978 -0.0050 0.2634  -0.1893 256 GLN A O   
1947 C CB  . GLN B 41  ? 1.2935 0.9448 1.1891 0.0490  0.2202  -0.1138 256 GLN A CB  
1948 C CG  . GLN B 41  ? 1.1597 0.7823 1.0617 0.0807  0.2091  -0.0807 256 GLN A CG  
1949 C CD  . GLN B 41  ? 1.1040 0.7425 1.0266 0.1244  0.1934  -0.0579 256 GLN A CD  
1950 O OE1 . GLN B 41  ? 1.1159 0.7245 1.0387 0.1549  0.1902  -0.0351 256 GLN A OE1 
1951 N NE2 . GLN B 41  ? 1.1398 0.8320 1.0794 0.1249  0.1832  -0.0629 256 GLN A NE2 
1952 N N   . HIS B 42  ? 1.8592 1.5402 1.7017 -0.0769 0.2573  -0.2075 257 HIS A N   
1953 C CA  . HIS B 42  ? 1.9033 1.6373 1.7280 -0.1115 0.2612  -0.2413 257 HIS A CA  
1954 C C   . HIS B 42  ? 1.9437 1.6149 1.7458 -0.1129 0.3011  -0.2843 257 HIS A C   
1955 O O   . HIS B 42  ? 2.0243 1.6043 1.8140 -0.1189 0.3326  -0.3059 257 HIS A O   
1956 C CB  . HIS B 42  ? 1.9036 1.6876 1.7175 -0.1670 0.2520  -0.2574 257 HIS A CB  
1957 C CG  . HIS B 42  ? 1.8445 1.7344 1.6781 -0.1710 0.2117  -0.2260 257 HIS A CG  
1958 N ND1 . HIS B 42  ? 1.8191 1.7478 1.6697 -0.1869 0.1932  -0.2083 257 HIS A ND1 
1959 C CD2 . HIS B 42  ? 1.7829 1.7475 1.6236 -0.1612 0.1889  -0.2079 257 HIS A CD2 
1960 C CE1 . HIS B 42  ? 1.7391 1.7570 1.6089 -0.1815 0.1603  -0.1798 257 HIS A CE1 
1961 N NE2 . HIS B 42  ? 1.7055 1.7434 1.5682 -0.1674 0.1567  -0.1773 257 HIS A NE2 
1962 N N   . PRO B 50  ? 1.5142 0.8526 1.5249 0.4589  0.2886  0.1112  265 PRO A N   
1963 C CA  . PRO B 50  ? 1.3960 0.8332 1.4303 0.4734  0.2524  0.1235  265 PRO A CA  
1964 C C   . PRO B 50  ? 1.4042 0.8697 1.4126 0.4627  0.2214  0.1492  265 PRO A C   
1965 O O   . PRO B 50  ? 1.4556 0.8909 1.4438 0.4744  0.2189  0.1823  265 PRO A O   
1966 C CB  . PRO B 50  ? 1.4013 0.8714 1.4743 0.5220  0.2464  0.1497  265 PRO A CB  
1967 C CG  . PRO B 50  ? 1.4859 0.8642 1.5443 0.5363  0.2731  0.1669  265 PRO A CG  
1968 C CD  . PRO B 50  ? 1.5087 0.8082 1.5226 0.4927  0.2942  0.1487  265 PRO A CD  
1969 N N   . LEU B 51  ? 1.2941 0.8149 1.3024 0.4431  0.1997  0.1359  266 LEU A N   
1970 C CA  . LEU B 51  ? 1.3069 0.8453 1.2865 0.4314  0.1744  0.1538  266 LEU A CA  
1971 C C   . LEU B 51  ? 1.3611 0.9373 1.3429 0.4636  0.1492  0.1947  266 LEU A C   
1972 O O   . LEU B 51  ? 1.3326 0.9683 1.3511 0.4904  0.1335  0.2047  266 LEU A O   
1973 C CB  . LEU B 51  ? 1.2055 0.8022 1.1925 0.4128  0.1524  0.1351  266 LEU A CB  
1974 C CG  . LEU B 51  ? 1.2008 0.7746 1.1798 0.3786  0.1703  0.0990  266 LEU A CG  
1975 C CD1 . LEU B 51  ? 1.1214 0.7642 1.1095 0.3605  0.1392  0.0907  266 LEU A CD1 
1976 C CD2 . LEU B 51  ? 1.1558 0.6544 1.0955 0.3514  0.1931  0.0923  266 LEU A CD2 
1977 N N   . GLU B 52  ? 1.3328 0.8750 1.2749 0.4608  0.1483  0.2191  267 GLU A N   
1978 C CA  . GLU B 52  ? 1.2999 0.8855 1.2307 0.4854  0.1208  0.2575  267 GLU A CA  
1979 C C   . GLU B 52  ? 1.2253 0.8992 1.1668 0.4833  0.0826  0.2506  267 GLU A C   
1980 O O   . GLU B 52  ? 1.2272 0.9107 1.1681 0.4583  0.0788  0.2221  267 GLU A O   
1981 C CB  . GLU B 52  ? 1.3992 0.9353 1.2770 0.4755  0.1292  0.2798  267 GLU A CB  
1982 C CG  . GLU B 52  ? 1.4753 0.9671 1.3408 0.4988  0.1438  0.3189  267 GLU A CG  
1983 C CD  . GLU B 52  ? 1.5731 1.0212 1.3838 0.4845  0.1538  0.3418  267 GLU A CD  
1984 O OE1 . GLU B 52  ? 1.5424 1.0408 1.3231 0.4886  0.1279  0.3599  267 GLU A OE1 
1985 O OE2 . GLU B 52  ? 1.6863 1.0519 1.4824 0.4675  0.1885  0.3404  267 GLU A OE2 
1986 N N   . SER B 53  ? 1.2121 0.9521 1.1643 0.5088  0.0537  0.2771  268 SER A N   
1987 C CA  . SER B 53  ? 1.1671 0.9938 1.1304 0.5049  0.0157  0.2695  268 SER A CA  
1988 C C   . SER B 53  ? 1.2417 1.0894 1.1544 0.5046  -0.0082 0.2889  268 SER A C   
1989 O O   . SER B 53  ? 1.3208 1.1352 1.1978 0.5160  0.0005  0.3188  268 SER A O   
1990 C CB  . SER B 53  ? 1.1833 1.0895 1.1994 0.5286  -0.0040 0.2789  268 SER A CB  
1991 O OG  . SER B 53  ? 1.2575 1.2038 1.2622 0.5528  -0.0256 0.3157  268 SER A OG  
1992 N N   . VAL B 54  ? 1.2567 1.1604 1.1646 0.4913  -0.0379 0.2707  269 VAL A N   
1993 C CA  . VAL B 54  ? 1.2862 1.2187 1.1409 0.4888  -0.0636 0.2784  269 VAL A CA  
1994 C C   . VAL B 54  ? 1.2615 1.2917 1.1399 0.4780  -0.1060 0.2599  269 VAL A C   
1995 O O   . VAL B 54  ? 1.2107 1.2598 1.1320 0.4547  -0.1096 0.2276  269 VAL A O   
1996 C CB  . VAL B 54  ? 1.2472 1.1240 1.0639 0.4517  -0.0462 0.2496  269 VAL A CB  
1997 C CG1 . VAL B 54  ? 1.2612 1.1888 1.0456 0.4271  -0.0755 0.2276  269 VAL A CG1 
1998 C CG2 . VAL B 54  ? 1.2591 1.0590 1.0338 0.4622  -0.0138 0.2783  269 VAL A CG2 
1999 N N   . ASP B 55  ? 1.2725 1.3679 1.1237 0.4895  -0.1378 0.2794  270 ASP A N   
2000 C CA  . ASP B 55  ? 1.2403 1.4322 1.1199 0.4729  -0.1780 0.2582  270 ASP A CA  
2001 C C   . ASP B 55  ? 1.2624 1.4467 1.1162 0.4236  -0.1870 0.2083  270 ASP A C   
2002 O O   . ASP B 55  ? 1.3224 1.4706 1.1177 0.4129  -0.1790 0.2019  270 ASP A O   
2003 C CB  . ASP B 55  ? 1.3080 1.5862 1.1741 0.4967  -0.2118 0.2920  270 ASP A CB  
2004 C CG  . ASP B 55  ? 1.3030 1.6911 1.2024 0.4764  -0.2559 0.2681  270 ASP A CG  
2005 O OD1 . ASP B 55  ? 1.2997 1.7589 1.2431 0.4881  -0.2721 0.2879  270 ASP A OD1 
2006 O OD2 . ASP B 55  ? 1.3647 1.7513 1.2534 0.4298  -0.2658 0.2196  270 ASP A OD2 
2007 N N   . VAL B 56  ? 1.2916 1.5085 1.1925 0.3948  -0.2006 0.1741  271 VAL A N   
2008 C CA  . VAL B 56  ? 1.2738 1.4721 1.1628 0.3509  -0.2053 0.1270  271 VAL A CA  
2009 C C   . VAL B 56  ? 1.4112 1.6602 1.2556 0.3344  -0.2368 0.1090  271 VAL A C   
2010 O O   . VAL B 56  ? 1.4599 1.6772 1.2755 0.3055  -0.2339 0.0716  271 VAL A O   
2011 C CB  . VAL B 56  ? 1.1724 1.3855 1.1271 0.3261  -0.2081 0.1035  271 VAL A CB  
2012 C CG1 . VAL B 56  ? 1.1819 1.4933 1.1790 0.3241  -0.2419 0.1072  271 VAL A CG1 
2013 C CG2 . VAL B 56  ? 1.1749 1.3480 1.1236 0.2856  -0.2054 0.0609  271 VAL A CG2 
2014 N N   . ARG B 57  ? 1.5185 1.8487 1.3552 0.3528  -0.2664 0.1337  272 ARG A N   
2015 C CA  . ARG B 57  ? 1.5414 1.9210 1.3208 0.3366  -0.2949 0.1165  272 ARG A CA  
2016 C C   . ARG B 57  ? 1.5883 1.9050 1.2935 0.3395  -0.2711 0.1159  272 ARG A C   
2017 O O   . ARG B 57  ? 1.6599 1.9789 1.3187 0.3124  -0.2784 0.0773  272 ARG A O   
2018 C CB  . ARG B 57  ? 1.5302 2.0121 1.3033 0.3625  -0.3295 0.1545  272 ARG A CB  
2019 C CG  . ARG B 57  ? 1.4925 2.0543 1.3423 0.3767  -0.3502 0.1751  272 ARG A CG  
2020 C CD  . ARG B 57  ? 1.4908 2.1202 1.3344 0.4250  -0.3659 0.2363  272 ARG A CD  
2021 N NE  . ARG B 57  ? 1.5658 2.1122 1.3686 0.4586  -0.3306 0.2780  272 ARG A NE  
2022 C CZ  . ARG B 57  ? 1.5480 2.0785 1.2728 0.4614  -0.3292 0.2926  272 ARG A CZ  
2023 N NH1 . ARG B 57  ? 1.5896 2.1821 1.2597 0.4342  -0.3607 0.2663  272 ARG A NH1 
2024 N NH2 . ARG B 57  ? 1.5138 1.9640 1.2145 0.4883  -0.2931 0.3318  272 ARG A NH2 
2025 N N   . GLN B 58  ? 1.5006 1.7598 1.1950 0.3707  -0.2398 0.1564  273 GLN A N   
2026 C CA  . GLN B 58  ? 1.4724 1.6820 1.0984 0.3766  -0.2156 0.1682  273 GLN A CA  
2027 C C   . GLN B 58  ? 1.4751 1.6205 1.0893 0.3463  -0.1903 0.1231  273 GLN A C   
2028 O O   . GLN B 58  ? 1.5134 1.6244 1.0742 0.3475  -0.1679 0.1288  273 GLN A O   
2029 C CB  . GLN B 58  ? 1.4368 1.5958 1.0652 0.4140  -0.1870 0.2237  273 GLN A CB  
2030 C CG  . GLN B 58  ? 1.4271 1.6448 1.0811 0.4520  -0.2085 0.2713  273 GLN A CG  
2031 C CD  . GLN B 58  ? 1.4216 1.6216 1.0280 0.4889  -0.1965 0.3322  273 GLN A CD  
2032 O OE1 . GLN B 58  ? 1.4334 1.6248 0.9697 0.4804  -0.1910 0.3371  273 GLN A OE1 
2033 N NE2 . GLN B 58  ? 1.4141 1.6041 1.0692 0.5154  -0.1858 0.3697  273 GLN A NE2 
2034 N N   . ILE B 59  ? 1.4626 1.5938 1.1264 0.3209  -0.1919 0.0828  274 ILE A N   
2035 C CA  . ILE B 59  ? 1.4688 1.5433 1.1275 0.2975  -0.1688 0.0443  274 ILE A CA  
2036 C C   . ILE B 59  ? 1.5100 1.5984 1.1981 0.2658  -0.1878 -0.0062 274 ILE A C   
2037 O O   . ILE B 59  ? 1.5033 1.5436 1.2192 0.2506  -0.1708 -0.0313 274 ILE A O   
2038 C CB  . ILE B 59  ? 1.4203 1.4290 1.1141 0.3036  -0.1349 0.0588  274 ILE A CB  
2039 C CG1 . ILE B 59  ? 1.3676 1.3851 1.1290 0.3050  -0.1421 0.0655  274 ILE A CG1 
2040 C CG2 . ILE B 59  ? 1.3855 1.3631 1.0460 0.3281  -0.1100 0.1026  274 ILE A CG2 
2041 C CD1 . ILE B 59  ? 1.2013 1.1616 0.9941 0.3009  -0.1122 0.0659  274 ILE A CD1 
2042 N N   . TYR B 60  ? 1.5664 1.7209 1.2495 0.2543  -0.2233 -0.0204 275 TYR A N   
2043 C CA  . TYR B 60  ? 1.6026 1.7643 1.3115 0.2187  -0.2407 -0.0709 275 TYR A CA  
2044 C C   . TYR B 60  ? 1.6344 1.7653 1.2951 0.2006  -0.2310 -0.1187 275 TYR A C   
2045 O O   . TYR B 60  ? 1.6446 1.7484 1.3298 0.1737  -0.2327 -0.1627 275 TYR A O   
2046 C CB  . TYR B 60  ? 1.6001 1.8490 1.3211 0.2059  -0.2823 -0.0747 275 TYR A CB  
2047 C CG  . TYR B 60  ? 1.5298 1.8152 1.3233 0.2115  -0.2940 -0.0469 275 TYR A CG  
2048 C CD1 . TYR B 60  ? 1.4992 1.7332 1.3472 0.2134  -0.2704 -0.0378 275 TYR A CD1 
2049 C CD2 . TYR B 60  ? 1.4999 1.8812 1.3076 0.2145  -0.3287 -0.0304 275 TYR A CD2 
2050 C CE1 . TYR B 60  ? 1.4593 1.7322 1.3705 0.2181  -0.2776 -0.0152 275 TYR A CE1 
2051 C CE2 . TYR B 60  ? 1.4531 1.8764 1.3311 0.2215  -0.3365 -0.0062 275 TYR A CE2 
2052 C CZ  . TYR B 60  ? 1.4282 1.7949 1.3564 0.2232  -0.3091 0.0001  275 TYR A CZ  
2053 O OH  . TYR B 60  ? 1.3604 1.7733 1.3561 0.2301  -0.3132 0.0218  275 TYR A OH  
2054 N N   . ASP B 61  ? 1.6424 1.7759 1.2356 0.2158  -0.2185 -0.1099 276 ASP A N   
2055 C CA  . ASP B 61  ? 1.6571 1.7695 1.1979 0.2035  -0.2045 -0.1546 276 ASP A CA  
2056 C C   . ASP B 61  ? 1.6585 1.6960 1.2214 0.2066  -0.1663 -0.1675 276 ASP A C   
2057 O O   . ASP B 61  ? 1.6451 1.6582 1.1869 0.1957  -0.1529 -0.2136 276 ASP A O   
2058 C CB  . ASP B 61  ? 1.6653 1.8160 1.1249 0.2196  -0.2019 -0.1325 276 ASP A CB  
2059 C CG  . ASP B 61  ? 1.6391 1.7741 1.0984 0.2510  -0.1822 -0.0673 276 ASP A CG  
2060 O OD1 . ASP B 61  ? 1.5754 1.6979 1.0927 0.2620  -0.1843 -0.0362 276 ASP A OD1 
2061 O OD2 . ASP B 61  ? 1.7191 1.8517 1.1194 0.2631  -0.1622 -0.0483 276 ASP A OD2 
2062 N N   . LYS B 62  ? 1.6100 1.6150 1.2152 0.2219  -0.1482 -0.1295 277 LYS A N   
2063 C CA  . LYS B 62  ? 1.5150 1.4657 1.1360 0.2279  -0.1126 -0.1305 277 LYS A CA  
2064 C C   . LYS B 62  ? 1.4713 1.3836 1.1602 0.2160  -0.1100 -0.1488 277 LYS A C   
2065 O O   . LYS B 62  ? 1.4129 1.2909 1.1289 0.2225  -0.0854 -0.1385 277 LYS A O   
2066 C CB  . LYS B 62  ? 1.4011 1.3407 1.0206 0.2475  -0.0929 -0.0790 277 LYS A CB  
2067 C CG  . LYS B 62  ? 1.4745 1.4492 1.0365 0.2629  -0.0989 -0.0441 277 LYS A CG  
2068 C CD  . LYS B 62  ? 1.4460 1.3911 1.0088 0.2800  -0.0731 0.0046  277 LYS A CD  
2069 C CE  . LYS B 62  ? 1.3851 1.2934 0.9379 0.2751  -0.0355 -0.0025 277 LYS A CE  
2070 N NZ  . LYS B 62  ? 1.2483 1.1341 0.7774 0.2858  -0.0094 0.0430  277 LYS A NZ  
2071 N N   . PHE B 63  ? 1.4862 1.5738 1.3715 -0.0419 0.3537  -0.1795 278 PHE A N   
2072 C CA  . PHE B 63  ? 1.5681 1.6151 1.5120 -0.0300 0.3506  -0.1792 278 PHE A CA  
2073 C C   . PHE B 63  ? 1.7694 1.7657 1.6989 -0.0371 0.3399  -0.2210 278 PHE A C   
2074 O O   . PHE B 63  ? 1.7382 1.7316 1.6137 -0.0540 0.3278  -0.2460 278 PHE A O   
2075 C CB  . PHE B 63  ? 1.4455 1.5033 1.4344 -0.0376 0.3265  -0.1335 278 PHE A CB  
2076 C CG  . PHE B 63  ? 1.2018 1.3039 1.2157 -0.0259 0.3347  -0.0951 278 PHE A CG  
2077 C CD1 . PHE B 63  ? 1.0322 1.1313 1.0963 0.0027  0.3530  -0.0866 278 PHE A CD1 
2078 C CD2 . PHE B 63  ? 1.1407 1.2876 1.1286 -0.0426 0.3240  -0.0695 278 PHE A CD2 
2079 C CE1 . PHE B 63  ? 0.9262 1.0643 1.0168 0.0145  0.3577  -0.0539 278 PHE A CE1 
2080 C CE2 . PHE B 63  ? 1.0674 1.2542 1.0830 -0.0318 0.3295  -0.0354 278 PHE A CE2 
2081 C CZ  . PHE B 63  ? 0.9141 1.0959 0.9823 -0.0031 0.3454  -0.0282 278 PHE A CZ  
2082 N N   . PRO B 64  ? 2.2492 2.2045 2.2276 -0.0232 0.3433  -0.2302 279 PRO A N   
2083 C CA  . PRO B 64  ? 2.2747 2.1797 2.2483 -0.0299 0.3312  -0.2695 279 PRO A CA  
2084 C C   . PRO B 64  ? 2.2837 2.1798 2.2528 -0.0590 0.2937  -0.2592 279 PRO A C   
2085 O O   . PRO B 64  ? 2.3060 2.2319 2.2825 -0.0723 0.2779  -0.2192 279 PRO A O   
2086 C CB  . PRO B 64  ? 2.2072 2.0783 2.2465 -0.0083 0.3425  -0.2681 279 PRO A CB  
2087 C CG  . PRO B 64  ? 2.1414 2.0433 2.2238 0.0020  0.3457  -0.2187 279 PRO A CG  
2088 C CD  . PRO B 64  ? 2.1457 2.0986 2.1895 -0.0008 0.3547  -0.2035 279 PRO A CD  
2089 N N   . GLU B 65  ? 1.9803 1.8346 1.9381 -0.0687 0.2779  -0.2971 280 GLU A N   
2090 C CA  . GLU B 65  ? 1.9564 1.7959 1.9162 -0.0963 0.2405  -0.2912 280 GLU A CA  
2091 C C   . GLU B 65  ? 1.9114 1.6987 1.9296 -0.0947 0.2281  -0.3019 280 GLU A C   
2092 O O   . GLU B 65  ? 1.9431 1.6967 1.9699 -0.0786 0.2422  -0.3383 280 GLU A O   
2093 C CB  . GLU B 65  ? 1.9070 1.7493 1.7941 -0.1136 0.2250  -0.3263 280 GLU A CB  
2094 C CG  . GLU B 65  ? 1.9144 1.8103 1.7424 -0.1120 0.2417  -0.3176 280 GLU A CG  
2095 C CD  . GLU B 65  ? 1.9426 1.8774 1.7626 -0.1346 0.2214  -0.2740 280 GLU A CD  
2096 O OE1 . GLU B 65  ? 1.9041 1.8275 1.7682 -0.1488 0.1975  -0.2460 280 GLU A OE1 
2097 O OE2 . GLU B 65  ? 1.9143 1.8932 1.6854 -0.1374 0.2299  -0.2661 280 GLU A OE2 
2098 N N   . LYS B 66  ? 1.8343 1.6171 1.8957 -0.1107 0.2022  -0.2675 281 LYS A N   
2099 C CA  . LYS B 66  ? 1.7751 1.5170 1.9067 -0.1083 0.1911  -0.2617 281 LYS A CA  
2100 C C   . LYS B 66  ? 1.7443 1.4828 1.9248 -0.0772 0.2214  -0.2486 281 LYS A C   
2101 O O   . LYS B 66  ? 1.6889 1.4333 1.9268 -0.0695 0.2197  -0.2064 281 LYS A O   
2102 C CB  . LYS B 66  ? 1.8331 1.5249 1.9578 -0.1178 0.1735  -0.3131 281 LYS A CB  
2103 N N   . LYS B 67  ? 1.7589 1.4902 1.9155 -0.0575 0.2493  -0.2838 282 LYS A N   
2104 C CA  . LYS B 67  ? 1.7230 1.4506 1.9183 -0.0266 0.2802  -0.2785 282 LYS A CA  
2105 C C   . LYS B 67  ? 1.6577 1.4273 1.8779 -0.0145 0.2893  -0.2262 282 LYS A C   
2106 O O   . LYS B 67  ? 1.6169 1.4130 1.8219 0.0035  0.3140  -0.2233 282 LYS A O   
2107 C CB  . LYS B 67  ? 1.7099 1.4361 1.8580 -0.0110 0.3081  -0.3224 282 LYS A CB  
2108 C CG  . LYS B 67  ? 1.5614 1.2765 1.7439 0.0210  0.3411  -0.3292 282 LYS A CG  
2109 C CD  . LYS B 67  ? 1.4257 1.1164 1.5707 0.0321  0.3592  -0.3859 282 LYS A CD  
2110 C CE  . LYS B 67  ? 1.4172 1.0757 1.6135 0.0577  0.3804  -0.3978 282 LYS A CE  
2111 N NZ  . LYS B 67  ? 1.3654 1.0089 1.6358 0.0583  0.3674  -0.3609 282 LYS A NZ  
2112 N N   . GLY B 68  ? 1.6082 1.3841 1.8687 -0.0228 0.2682  -0.1849 283 GLY A N   
2113 C CA  . GLY B 68  ? 1.4741 1.2913 1.7537 -0.0122 0.2698  -0.1356 283 GLY A CA  
2114 C C   . GLY B 68  ? 1.4818 1.3426 1.7066 -0.0215 0.2709  -0.1291 283 GLY A C   
2115 O O   . GLY B 68  ? 1.3886 1.2815 1.6215 -0.0034 0.2842  -0.1051 283 GLY A O   
2116 N N   . GLY B 69  ? 1.5604 1.4232 1.7316 -0.0482 0.2562  -0.1502 284 GLY A N   
2117 C CA  . GLY B 69  ? 1.5738 1.4785 1.6909 -0.0569 0.2594  -0.1461 284 GLY A CA  
2118 C C   . GLY B 69  ? 1.3479 1.2929 1.4769 -0.0632 0.2439  -0.0961 284 GLY A C   
2119 O O   . GLY B 69  ? 1.2527 1.1947 1.4277 -0.0607 0.2294  -0.0640 284 GLY A O   
2120 N N   . LEU B 70  ? 1.3167 1.3020 1.4037 -0.0700 0.2474  -0.0888 285 LEU A N   
2121 C CA  . LEU B 70  ? 1.2033 1.2288 1.2976 -0.0767 0.2314  -0.0438 285 LEU A CA  
2122 C C   . LEU B 70  ? 1.2929 1.3160 1.3779 -0.1059 0.1984  -0.0298 285 LEU A C   
2123 O O   . LEU B 70  ? 1.2358 1.2724 1.3541 -0.1062 0.1813  0.0092  285 LEU A O   
2124 C CB  . LEU B 70  ? 1.1690 1.2378 1.2243 -0.0784 0.2427  -0.0393 285 LEU A CB  
2125 C CG  . LEU B 70  ? 1.0277 1.1357 1.1122 -0.0704 0.2346  0.0071  285 LEU A CG  
2126 C CD1 . LEU B 70  ? 0.8726 0.9650 1.0195 -0.0429 0.2372  0.0245  285 LEU A CD1 
2127 C CD2 . LEU B 70  ? 1.0054 1.1524 1.0737 -0.0624 0.2522  0.0127  285 LEU A CD2 
2128 N N   . ARG B 71  ? 1.2798 1.2875 1.3193 -0.1292 0.1880  -0.0612 286 ARG A N   
2129 C CA  . ARG B 71  ? 1.3481 1.3494 1.3826 -0.1574 0.1550  -0.0504 286 ARG A CA  
2130 C C   . ARG B 71  ? 1.3700 1.3359 1.4653 -0.1534 0.1433  -0.0396 286 ARG A C   
2131 O O   . ARG B 71  ? 1.3559 1.3296 1.4768 -0.1650 0.1202  -0.0051 286 ARG A O   
2132 C CB  . ARG B 71  ? 1.3980 1.3871 1.3714 -0.1796 0.1453  -0.0913 286 ARG A CB  
2133 C CG  . ARG B 71  ? 1.4196 1.4174 1.3699 -0.2118 0.1110  -0.0787 286 ARG A CG  
2134 C CD  . ARG B 71  ? 1.4788 1.4394 1.4767 -0.2230 0.0858  -0.0724 286 ARG A CD  
2135 N NE  . ARG B 71  ? 1.5249 1.4860 1.5006 -0.2545 0.0519  -0.0690 286 ARG A NE  
2136 C CZ  . ARG B 71  ? 1.5431 1.4822 1.4764 -0.2718 0.0362  -0.1100 286 ARG A CZ  
2137 N NH1 . ARG B 71  ? 1.4882 1.4050 1.3906 -0.2601 0.0518  -0.1591 286 ARG A NH1 
2138 N NH2 . ARG B 71  ? 1.5149 1.4538 1.4367 -0.2998 0.0029  -0.1026 286 ARG A NH2 
2139 N N   . GLU B 72  ? 1.4532 1.3826 1.5755 -0.1355 0.1599  -0.0658 287 GLU A N   
2140 C CA  . GLU B 72  ? 1.4442 1.3411 1.6296 -0.1303 0.1506  -0.0539 287 GLU A CA  
2141 C C   . GLU B 72  ? 1.3693 1.2896 1.6067 -0.1092 0.1539  -0.0033 287 GLU A C   
2142 O O   . GLU B 72  ? 1.3468 1.2669 1.6227 -0.1152 0.1342  0.0296  287 GLU A O   
2143 C CB  . GLU B 72  ? 1.4940 1.3479 1.6962 -0.1146 0.1689  -0.0940 287 GLU A CB  
2144 C CG  . GLU B 72  ? 1.5687 1.3769 1.7966 -0.1309 0.1471  -0.1137 287 GLU A CG  
2145 C CD  . GLU B 72  ? 1.6280 1.4313 1.8021 -0.1621 0.1217  -0.1403 287 GLU A CD  
2146 O OE1 . GLU B 72  ? 1.6069 1.3926 1.8041 -0.1837 0.0915  -0.1320 287 GLU A OE1 
2147 O OE2 . GLU B 72  ? 1.6769 1.4962 1.7861 -0.1640 0.1317  -0.1678 287 GLU A OE2 
2148 N N   . LEU B 73  ? 1.3150 1.2567 1.5558 -0.0822 0.1780  0.0038  288 LEU A N   
2149 C CA  . LEU B 73  ? 1.1885 1.1513 1.4772 -0.0565 0.1803  0.0473  288 LEU A CA  
2150 C C   . LEU B 73  ? 1.1452 1.1451 1.4279 -0.0694 0.1562  0.0883  288 LEU A C   
2151 O O   . LEU B 73  ? 1.1207 1.1272 1.4455 -0.0604 0.1439  0.1253  288 LEU A O   
2152 C CB  . LEU B 73  ? 1.1024 1.0806 1.3930 -0.0261 0.2075  0.0425  288 LEU A CB  
2153 C CG  . LEU B 73  ? 1.1094 1.0529 1.4284 -0.0027 0.2320  0.0160  288 LEU A CG  
2154 C CD1 . LEU B 73  ? 1.0300 0.9884 1.3377 0.0200  0.2582  0.0029  288 LEU A CD1 
2155 C CD2 . LEU B 73  ? 1.0264 0.9593 1.4094 0.0197  0.2297  0.0456  288 LEU A CD2 
2156 N N   . TYR B 74  ? 1.1414 1.1677 1.3722 -0.0895 0.1496  0.0835  289 TYR A N   
2157 C CA  . TYR B 74  ? 1.1080 1.1727 1.3314 -0.1003 0.1280  0.1219  289 TYR A CA  
2158 C C   . TYR B 74  ? 1.2058 1.2616 1.4457 -0.1214 0.1004  0.1428  289 TYR A C   
2159 O O   . TYR B 74  ? 1.1716 1.2546 1.4282 -0.1198 0.0837  0.1836  289 TYR A O   
2160 C CB  . TYR B 74  ? 1.0942 1.1864 1.2587 -0.1206 0.1267  0.1103  289 TYR A CB  
2161 C CG  . TYR B 74  ? 1.0298 1.1669 1.1915 -0.1232 0.1106  0.1500  289 TYR A CG  
2162 C CD1 . TYR B 74  ? 1.1060 1.2549 1.2588 -0.1481 0.0823  0.1732  289 TYR A CD1 
2163 C CD2 . TYR B 74  ? 0.9525 1.1195 1.1234 -0.1006 0.1218  0.1641  289 TYR A CD2 
2164 C CE1 . TYR B 74  ? 1.0338 1.2232 1.1848 -0.1499 0.0665  0.2090  289 TYR A CE1 
2165 C CE2 . TYR B 74  ? 0.9131 1.1199 1.0850 -0.1022 0.1040  0.1993  289 TYR A CE2 
2166 C CZ  . TYR B 74  ? 0.9273 1.1450 1.0879 -0.1268 0.0768  0.2212  289 TYR A CZ  
2167 O OH  . TYR B 74  ? 0.8763 1.1325 1.0384 -0.1281 0.0582  0.2555  289 TYR A OH  
2168 N N   . ASP B 75  ? 1.3692 1.3873 1.6076 -0.1403 0.0940  0.1160  290 ASP A N   
2169 C CA  . ASP B 75  ? 1.3553 1.3627 1.6181 -0.1607 0.0669  0.1366  290 ASP A CA  
2170 C C   . ASP B 75  ? 1.3168 1.3171 1.6498 -0.1361 0.0689  0.1704  290 ASP A C   
2171 O O   . ASP B 75  ? 1.2546 1.2726 1.6144 -0.1393 0.0503  0.2118  290 ASP A O   
2172 C CB  . ASP B 75  ? 1.4215 1.3891 1.6656 -0.1874 0.0562  0.0954  290 ASP A CB  
2173 C CG  . ASP B 75  ? 1.4514 1.4304 1.6231 -0.2123 0.0494  0.0669  290 ASP A CG  
2174 O OD1 . ASP B 75  ? 1.4366 1.4565 1.5790 -0.2161 0.0468  0.0884  290 ASP A OD1 
2175 O OD2 . ASP B 75  ? 1.5137 1.4619 1.6586 -0.2263 0.0458  0.0232  290 ASP A OD2 
2176 N N   . ARG B 76  ? 1.2032 1.1798 1.5671 -0.1101 0.0919  0.1549  291 ARG A N   
2177 C CA  . ARG B 76  ? 1.1065 1.0818 1.5359 -0.0808 0.0977  0.1890  291 ARG A CA  
2178 C C   . ARG B 76  ? 1.0542 1.0738 1.4932 -0.0548 0.0979  0.2317  291 ARG A C   
2179 O O   . ARG B 76  ? 1.0417 1.0688 1.5312 -0.0282 0.0996  0.2665  291 ARG A O   
2180 C CB  . ARG B 76  ? 1.1186 1.0641 1.5736 -0.0552 0.1246  0.1627  291 ARG A CB  
2181 C CG  . ARG B 76  ? 1.1473 1.0448 1.6054 -0.0745 0.1237  0.1213  291 ARG A CG  
2182 C CD  . ARG B 76  ? 1.0996 0.9691 1.6195 -0.0491 0.1393  0.1232  291 ARG A CD  
2183 N NE  . ARG B 76  ? 1.1406 0.9967 1.6474 -0.0271 0.1683  0.0883  291 ARG A NE  
2184 C CZ  . ARG B 76  ? 1.2190 1.0469 1.6902 -0.0395 0.1759  0.0367  291 ARG A CZ  
2185 N NH1 . ARG B 76  ? 1.2834 1.0913 1.7261 -0.0728 0.1556  0.0102  291 ARG A NH1 
2186 N NH2 . ARG B 76  ? 1.1961 1.0162 1.6597 -0.0160 0.2040  0.0106  291 ARG A NH2 
2187 N N   . GLY B 77  ? 1.0307 1.0806 1.4244 -0.0597 0.0958  0.2299  292 GLY A N   
2188 C CA  . GLY B 77  ? 0.9568 1.0482 1.3575 -0.0365 0.0911  0.2670  292 GLY A CA  
2189 C C   . GLY B 77  ? 0.9093 1.0037 1.3432 0.0090  0.1124  0.2718  292 GLY A C   
2190 O O   . GLY B 77  ? 0.9397 1.0050 1.3875 0.0213  0.1337  0.2449  292 GLY A O   
2191 N N   . PRO B 78  ? 0.7974 0.9269 1.2439 0.0360  0.1057  0.3049  293 PRO A N   
2192 C CA  . PRO B 78  ? 0.7853 0.9515 1.2145 0.0251  0.0810  0.3353  293 PRO A CA  
2193 C C   . PRO B 78  ? 0.7320 0.9171 1.1165 0.0117  0.0802  0.3174  293 PRO A C   
2194 O O   . PRO B 78  ? 0.7573 0.9451 1.1425 0.0337  0.0965  0.3017  293 PRO A O   
2195 C CB  . PRO B 78  ? 0.8188 1.0100 1.2881 0.0701  0.0776  0.3742  293 PRO A CB  
2196 C CG  . PRO B 78  ? 0.7502 0.9267 1.2419 0.1068  0.1030  0.3553  293 PRO A CG  
2197 C CD  . PRO B 78  ? 0.7569 0.8913 1.2413 0.0844  0.1213  0.3154  293 PRO A CD  
2198 N N   . PRO B 79  ? 0.7022 1.0836 0.9008 0.0919  0.0162  0.1667  294 PRO A N   
2199 C CA  . PRO B 79  ? 0.7166 1.0793 0.9091 0.1198  0.0144  0.1789  294 PRO A CA  
2200 C C   . PRO B 79  ? 0.7209 0.9898 0.8996 0.1558  0.0364  0.1764  294 PRO A C   
2201 O O   . PRO B 79  ? 0.8046 1.0259 0.9660 0.1634  0.0344  0.1745  294 PRO A O   
2202 C CB  . PRO B 79  ? 0.6798 1.1576 0.9080 0.1472  0.0142  0.2160  294 PRO A CB  
2203 C CG  . PRO B 79  ? 0.6833 1.2533 0.9337 0.1155  0.0057  0.2162  294 PRO A CG  
2204 C CD  . PRO B 79  ? 0.6815 1.1829 0.9172 0.0918  0.0147  0.1894  294 PRO A CD  
2205 N N   . HIS B 80  ? 0.7506 0.9932 0.9344 0.1751  0.0591  0.1751  295 HIS A N   
2206 C CA  . HIS B 80  ? 0.7804 0.9362 0.9482 0.2042  0.0851  0.1689  295 HIS A CA  
2207 C C   . HIS B 80  ? 0.7829 0.8519 0.9166 0.1768  0.0799  0.1350  295 HIS A C   
2208 O O   . HIS B 80  ? 0.7653 0.7641 0.8816 0.1907  0.0993  0.1240  295 HIS A O   
2209 C CB  . HIS B 80  ? 0.8245 0.9877 1.0054 0.2305  0.1128  0.1761  295 HIS A CB  
2210 C CG  . HIS B 80  ? 0.8209 0.9915 0.9980 0.1999  0.1076  0.1567  295 HIS A CG  
2211 N ND1 . HIS B 80  ? 0.8059 0.9014 0.9523 0.1815  0.1109  0.1273  295 HIS A ND1 
2212 C CD2 . HIS B 80  ? 0.7749 1.0231 0.9741 0.1830  0.0997  0.1643  295 HIS A CD2 
2213 C CE1 . HIS B 80  ? 0.8192 0.9404 0.9672 0.1590  0.1067  0.1201  295 HIS A CE1 
2214 N NE2 . HIS B 80  ? 0.8948 1.1040 1.0745 0.1577  0.1009  0.1411  295 HIS A NE2 
2215 N N   . ALA B 81  ? 0.7623 0.8367 0.8850 0.1383  0.0571  0.1189  296 ALA A N   
2216 C CA  . ALA B 81  ? 0.8298 0.8361 0.9226 0.1167  0.0519  0.0926  296 ALA A CA  
2217 C C   . ALA B 81  ? 0.8500 0.8243 0.9269 0.1090  0.0392  0.0868  296 ALA A C   
2218 O O   . ALA B 81  ? 0.8594 0.7860 0.9137 0.0939  0.0347  0.0680  296 ALA A O   
2219 C CB  . ALA B 81  ? 0.7746 0.7936 0.8603 0.0849  0.0413  0.0817  296 ALA A CB  
2220 N N   . PHE B 82  ? 0.8161 0.8210 0.9043 0.1215  0.0345  0.1048  297 PHE A N   
2221 C CA  . PHE B 82  ? 0.8406 0.8291 0.9143 0.1117  0.0207  0.1017  297 PHE A CA  
2222 C C   . PHE B 82  ? 0.8790 0.8270 0.9489 0.1376  0.0355  0.1095  297 PHE A C   
2223 O O   . PHE B 82  ? 0.8849 0.8572 0.9704 0.1672  0.0479  0.1340  297 PHE A O   
2224 C CB  . PHE B 82  ? 0.8100 0.8693 0.8935 0.1007  0.0034  0.1154  297 PHE A CB  
2225 C CG  . PHE B 82  ? 0.8376 0.9217 0.9155 0.0637  -0.0099 0.1018  297 PHE A CG  
2226 C CD1 . PHE B 82  ? 0.8191 0.9491 0.9154 0.0576  -0.0062 0.1064  297 PHE A CD1 
2227 C CD2 . PHE B 82  ? 0.8413 0.8982 0.8934 0.0348  -0.0221 0.0845  297 PHE A CD2 
2228 C CE1 . PHE B 82  ? 0.8768 1.0225 0.9651 0.0193  -0.0144 0.0935  297 PHE A CE1 
2229 C CE2 . PHE B 82  ? 0.9161 0.9821 0.9573 -0.0007 -0.0281 0.0714  297 PHE A CE2 
2230 C CZ  . PHE B 82  ? 0.9571 1.0657 1.0160 -0.0105 -0.0241 0.0755  297 PHE A CZ  
2231 N N   . PHE B 83  ? 0.8481 0.7389 0.8973 0.1266  0.0352  0.0915  298 PHE A N   
2232 C CA  . PHE B 83  ? 0.8595 0.7032 0.9013 0.1420  0.0515  0.0940  298 PHE A CA  
2233 C C   . PHE B 83  ? 0.8500 0.6834 0.8787 0.1297  0.0381  0.0910  298 PHE A C   
2234 O O   . PHE B 83  ? 0.7829 0.6207 0.8010 0.1070  0.0205  0.0770  298 PHE A O   
2235 C CB  . PHE B 83  ? 0.8735 0.6624 0.9026 0.1370  0.0685  0.0725  298 PHE A CB  
2236 C CG  . PHE B 83  ? 0.9127 0.7077 0.9497 0.1484  0.0837  0.0728  298 PHE A CG  
2237 C CD1 . PHE B 83  ? 0.9678 0.7893 1.0062 0.1332  0.0722  0.0632  298 PHE A CD1 
2238 C CD2 . PHE B 83  ? 0.9408 0.7131 0.9824 0.1769  0.1132  0.0850  298 PHE A CD2 
2239 C CE1 . PHE B 83  ? 0.9575 0.7889 1.0031 0.1442  0.0874  0.0644  298 PHE A CE1 
2240 C CE2 . PHE B 83  ? 0.9915 0.7701 1.0394 0.1905  0.1303  0.0859  298 PHE A CE2 
2241 C CZ  . PHE B 83  ? 0.9638 0.7757 1.0147 0.1733  0.1162  0.0750  298 PHE A CZ  
2242 N N   . LEU B 84  ? 0.9371 0.7570 0.9656 0.1480  0.0495  0.1075  299 LEU A N   
2243 C CA  . LEU B 84  ? 0.8637 0.6678 0.8790 0.1398  0.0428  0.1063  299 LEU A CA  
2244 C C   . LEU B 84  ? 0.8521 0.5924 0.8566 0.1370  0.0631  0.0938  299 LEU A C   
2245 O O   . LEU B 84  ? 0.9108 0.6169 0.9165 0.1544  0.0895  0.1016  299 LEU A O   
2246 C CB  . LEU B 84  ? 0.8706 0.7108 0.8906 0.1599  0.0416  0.1360  299 LEU A CB  
2247 C CG  . LEU B 84  ? 0.8785 0.6960 0.8836 0.1577  0.0423  0.1395  299 LEU A CG  
2248 C CD1 . LEU B 84  ? 0.8155 0.6410 0.8063 0.1295  0.0201  0.1190  299 LEU A CD1 
2249 C CD2 . LEU B 84  ? 0.8984 0.7543 0.9070 0.1837  0.0451  0.1742  299 LEU A CD2 
2250 N N   . VAL B 85  ? 0.8043 0.5292 0.7969 0.1143  0.0537  0.0740  300 VAL A N   
2251 C CA  . VAL B 85  ? 0.8911 0.5701 0.8742 0.1039  0.0701  0.0610  300 VAL A CA  
2252 C C   . VAL B 85  ? 0.9469 0.6277 0.9238 0.1012  0.0649  0.0691  300 VAL A C   
2253 O O   . VAL B 85  ? 0.9225 0.6313 0.8955 0.0928  0.0442  0.0659  300 VAL A O   
2254 C CB  . VAL B 85  ? 0.8749 0.5494 0.8516 0.0803  0.0646  0.0332  300 VAL A CB  
2255 C CG1 . VAL B 85  ? 0.9148 0.5587 0.8826 0.0622  0.0786  0.0184  300 VAL A CG1 
2256 C CG2 . VAL B 85  ? 0.9079 0.5788 0.8869 0.0827  0.0725  0.0249  300 VAL A CG2 
2257 N N   . LYS B 86  ? 0.9288 0.5749 0.9018 0.1091  0.0870  0.0802  301 LYS A N   
2258 C CA  . LYS B 86  ? 0.9537 0.5949 0.9191 0.1030  0.0872  0.0855  301 LYS A CA  
2259 C C   . LYS B 86  ? 0.9941 0.6054 0.9541 0.0760  0.0987  0.0614  301 LYS A C   
2260 O O   . LYS B 86  ? 1.0079 0.5755 0.9639 0.0693  0.1238  0.0526  301 LYS A O   
2261 C CB  . LYS B 86  ? 1.0478 0.6718 1.0107 0.1276  0.1067  0.1161  301 LYS A CB  
2262 C CG  . LYS B 86  ? 1.0235 0.6618 0.9778 0.1276  0.1005  0.1293  301 LYS A CG  
2263 C CD  . LYS B 86  ? 1.2005 0.8474 1.1526 0.1602  0.1118  0.1678  301 LYS A CD  
2264 C CE  . LYS B 86  ? 1.2240 0.8949 1.1884 0.1876  0.1134  0.1862  301 LYS A CE  
2265 N NZ  . LYS B 86  ? 1.1612 0.8714 1.1272 0.2241  0.1171  0.2288  301 LYS A NZ  
2266 N N   . PHE B 87  ? 0.9747 0.6117 0.9331 0.0598  0.0827  0.0503  302 PHE A N   
2267 C CA  . PHE B 87  ? 0.9818 0.6131 0.9387 0.0325  0.0900  0.0294  302 PHE A CA  
2268 C C   . PHE B 87  ? 1.0130 0.6314 0.9662 0.0250  0.1034  0.0373  302 PHE A C   
2269 O O   . PHE B 87  ? 0.9691 0.5974 0.9194 0.0409  0.0982  0.0571  302 PHE A O   
2270 C CB  . PHE B 87  ? 0.9196 0.5964 0.8795 0.0231  0.0670  0.0155  302 PHE A CB  
2271 C CG  . PHE B 87  ? 0.9560 0.6410 0.9171 0.0157  0.0626  -0.0010 302 PHE A CG  
2272 C CD1 . PHE B 87  ? 1.0007 0.6592 0.9581 -0.0011 0.0811  -0.0170 302 PHE A CD1 
2273 C CD2 . PHE B 87  ? 0.9403 0.6549 0.9019 0.0241  0.0431  -0.0012 302 PHE A CD2 
2274 C CE1 . PHE B 87  ? 0.9631 0.6327 0.9179 -0.0086 0.0775  -0.0330 302 PHE A CE1 
2275 C CE2 . PHE B 87  ? 0.9492 0.6730 0.9101 0.0185  0.0404  -0.0138 302 PHE A CE2 
2276 C CZ  . PHE B 87  ? 0.9221 0.6273 0.8798 0.0026  0.0562  -0.0296 302 PHE A CZ  
2277 N N   . TRP B 88  ? 0.9847 0.5848 0.9362 -0.0033 0.1214  0.0200  303 TRP A N   
2278 C CA  . TRP B 88  ? 0.9825 0.5796 0.9327 -0.0200 0.1341  0.0222  303 TRP A CA  
2279 C C   . TRP B 88  ? 0.9525 0.5959 0.9103 -0.0521 0.1257  -0.0022 303 TRP A C   
2280 O O   . TRP B 88  ? 0.9761 0.6067 0.9310 -0.0844 0.1416  -0.0241 303 TRP A O   
2281 C CB  . TRP B 88  ? 1.0375 0.5656 0.9767 -0.0267 0.1712  0.0278  303 TRP A CB  
2282 C CG  . TRP B 88  ? 1.0495 0.5519 0.9832 0.0102  0.1790  0.0620  303 TRP A CG  
2283 C CD1 . TRP B 88  ? 1.0144 0.5228 0.9443 0.0221  0.1812  0.0853  303 TRP A CD1 
2284 C CD2 . TRP B 88  ? 1.1062 0.5851 1.0377 0.0420  0.1849  0.0792  303 TRP A CD2 
2285 N NE1 . TRP B 88  ? 1.0359 0.5301 0.9601 0.0590  0.1865  0.1168  303 TRP A NE1 
2286 C CE2 . TRP B 88  ? 1.0749 0.5534 1.0021 0.0726  0.1893  0.1147  303 TRP A CE2 
2287 C CE3 . TRP B 88  ? 1.1252 0.5894 1.0581 0.0486  0.1880  0.0696  303 TRP A CE3 
2288 C CZ2 . TRP B 88  ? 1.1850 0.6576 1.1121 0.1105  0.1953  0.1428  303 TRP A CZ2 
2289 C CZ3 . TRP B 88  ? 1.1289 0.5813 1.0626 0.0866  0.1960  0.0965  303 TRP A CZ3 
2290 C CH2 . TRP B 88  ? 1.2058 0.6667 1.1380 0.1176  0.1989  0.1337  303 TRP A CH2 
2291 N N   . ALA B 89  ? 0.9229 0.6226 0.8885 -0.0434 0.1030  0.0019  304 ALA A N   
2292 C CA  . ALA B 89  ? 0.9130 0.6731 0.8884 -0.0624 0.0912  -0.0149 304 ALA A CA  
2293 C C   . ALA B 89  ? 0.9562 0.7428 0.9389 -0.0923 0.1041  -0.0212 304 ALA A C   
2294 O O   . ALA B 89  ? 0.9874 0.7596 0.9690 -0.0888 0.1150  -0.0070 304 ALA A O   
2295 C CB  . ALA B 89  ? 0.8402 0.6441 0.8187 -0.0356 0.0676  -0.0048 304 ALA A CB  
2296 N N   . ASP B 90  ? 0.9039 0.7380 0.8940 -0.1237 0.1024  -0.0425 305 ASP A N   
2297 C CA  . ASP B 90  ? 0.9696 0.8544 0.9712 -0.1580 0.1108  -0.0512 305 ASP A CA  
2298 C C   . ASP B 90  ? 0.9626 0.9332 0.9806 -0.1369 0.0905  -0.0380 305 ASP A C   
2299 O O   . ASP B 90  ? 0.9422 0.9652 0.9654 -0.1256 0.0722  -0.0401 305 ASP A O   
2300 C CB  . ASP B 90  ? 0.9760 0.8807 0.9752 -0.2062 0.1188  -0.0825 305 ASP A CB  
2301 C CG  . ASP B 90  ? 1.0078 0.9581 1.0167 -0.2543 0.1331  -0.0960 305 ASP A CG  
2302 O OD1 . ASP B 90  ? 1.0833 1.0689 1.1063 -0.2451 0.1325  -0.0785 305 ASP A OD1 
2303 O OD2 . ASP B 90  ? 0.9777 0.9313 0.9787 -0.3043 0.1462  -0.1259 305 ASP A OD2 
2304 N N   . LEU B 91  ? 0.9809 0.9640 1.0052 -0.1284 0.0966  -0.0222 306 LEU A N   
2305 C CA  . LEU B 91  ? 0.9737 1.0346 1.0123 -0.1061 0.0845  -0.0083 306 LEU A CA  
2306 C C   . LEU B 91  ? 1.0480 1.1854 1.1073 -0.1395 0.0937  -0.0133 306 LEU A C   
2307 O O   . LEU B 91  ? 1.0534 1.2543 1.1263 -0.1199 0.0906  0.0023  306 LEU A O   
2308 C CB  . LEU B 91  ? 0.9194 0.9449 0.9471 -0.0667 0.0847  0.0136  306 LEU A CB  
2309 C CG  . LEU B 91  ? 0.8896 0.8547 0.8981 -0.0364 0.0744  0.0188  306 LEU A CG  
2310 C CD1 . LEU B 91  ? 0.8978 0.8398 0.8924 -0.0072 0.0759  0.0360  306 LEU A CD1 
2311 C CD2 . LEU B 91  ? 0.8387 0.8370 0.8494 -0.0209 0.0579  0.0156  306 LEU A CD2 
2312 N N   . ASN B 92  ? 1.1559 1.2870 1.2160 -0.1908 0.1078  -0.0351 307 ASN A N   
2313 C CA  . ASN B 92  ? 1.1647 1.3676 1.2434 -0.2354 0.1193  -0.0444 307 ASN A CA  
2314 C C   . ASN B 92  ? 1.1598 1.4626 1.2520 -0.2604 0.1036  -0.0620 307 ASN A C   
2315 O O   . ASN B 92  ? 1.1698 1.4602 1.2521 -0.3060 0.1098  -0.0905 307 ASN A O   
2316 C CB  . ASN B 92  ? 1.2422 1.3656 1.3071 -0.2806 0.1496  -0.0590 307 ASN A CB  
2317 C CG  . ASN B 92  ? 1.3002 1.4891 1.3822 -0.3338 0.1659  -0.0698 307 ASN A CG  
2318 O OD1 . ASN B 92  ? 1.2684 1.5458 1.3738 -0.3232 0.1594  -0.0542 307 ASN A OD1 
2319 N ND2 . ASN B 92  ? 1.3759 1.5202 1.4449 -0.3932 0.1904  -0.0973 307 ASN A ND2 
2320 N N   . TRP B 93  ? 0.9924 1.3943 1.1040 -0.2271 0.0850  -0.0436 308 TRP A N   
2321 C CA  . TRP B 93  ? 0.9355 1.4555 1.0626 -0.2425 0.0685  -0.0517 308 TRP A CA  
2322 C C   . TRP B 93  ? 0.9530 1.6058 1.1118 -0.2276 0.0633  -0.0300 308 TRP A C   
2323 O O   . TRP B 93  ? 0.8995 1.5465 1.0634 -0.1776 0.0654  -0.0021 308 TRP A O   
2324 C CB  . TRP B 93  ? 0.8604 1.3682 0.9744 -0.2037 0.0492  -0.0462 308 TRP A CB  
2325 C CG  . TRP B 93  ? 0.8047 1.3325 0.9231 -0.1351 0.0386  -0.0122 308 TRP A CG  
2326 C CD1 . TRP B 93  ? 0.7083 1.3479 0.8438 -0.1051 0.0268  0.0085  308 TRP A CD1 
2327 C CD2 . TRP B 93  ? 0.8504 1.2798 0.9514 -0.0884 0.0422  0.0046  308 TRP A CD2 
2328 N NE1 . TRP B 93  ? 0.7034 1.3056 0.8306 -0.0418 0.0272  0.0364  308 TRP A NE1 
2329 C CE2 . TRP B 93  ? 0.8105 1.2857 0.9158 -0.0348 0.0356  0.0317  308 TRP A CE2 
2330 C CE3 . TRP B 93  ? 0.8816 1.1932 0.9626 -0.0871 0.0519  0.0004  308 TRP A CE3 
2331 C CZ2 . TRP B 93  ? 0.8262 1.2243 0.9125 0.0126  0.0397  0.0485  308 TRP A CZ2 
2332 C CZ3 . TRP B 93  ? 0.8652 1.1176 0.9310 -0.0403 0.0513  0.0187  308 TRP A CZ3 
2333 C CH2 . TRP B 93  ? 0.8664 1.1581 0.9333 0.0054  0.0458  0.0395  308 TRP A CH2 
2334 N N   . GLY B 94  ? 1.0288 1.8057 1.2075 -0.2718 0.0576  -0.0436 309 GLY A N   
2335 C CA  . GLY B 94  ? 1.0961 2.0223 1.3103 -0.2665 0.0541  -0.0242 309 GLY A CA  
2336 C C   . GLY B 94  ? 1.2289 2.2355 1.4588 -0.3495 0.0632  -0.0528 309 GLY A C   
2337 O O   . GLY B 94  ? 1.2814 2.2029 1.4897 -0.4069 0.0774  -0.0868 309 GLY A O   
2338 N N   . PRO B 95  ? 1.2865 2.4620 1.5522 -0.3602 0.0562  -0.0414 310 PRO A N   
2339 C CA  . PRO B 95  ? 1.2937 2.5433 1.5767 -0.4430 0.0697  -0.0671 310 PRO A CA  
2340 C C   . PRO B 95  ? 1.3186 2.4873 1.6028 -0.4544 0.0975  -0.0631 310 PRO A C   
2341 O O   . PRO B 95  ? 1.3533 2.4062 1.6127 -0.5059 0.1188  -0.0916 310 PRO A O   
2342 C CB  . PRO B 95  ? 1.2384 2.7056 1.5641 -0.4352 0.0526  -0.0455 310 PRO A CB  
2343 C CG  . PRO B 95  ? 1.2462 2.7222 1.5730 -0.3351 0.0364  -0.0025 310 PRO A CG  
2344 C CD  . PRO B 95  ? 1.2899 2.6103 1.5746 -0.3234 0.0325  -0.0191 310 PRO A CD  
2345 N N   . SER B 96  ? 1.3012 2.5260 1.6111 -0.4051 0.1008  -0.0268 311 SER A N   
2346 C CA  . SER B 96  ? 1.2524 2.4017 1.5609 -0.4081 0.1274  -0.0185 311 SER A CA  
2347 C C   . SER B 96  ? 1.2431 2.4577 1.5753 -0.3377 0.1281  0.0242  311 SER A C   
2348 O O   . SER B 96  ? 1.2663 2.4753 1.6078 -0.3429 0.1489  0.0347  311 SER A O   
2349 C CB  . SER B 96  ? 1.2469 2.4427 1.5686 -0.4998 0.1481  -0.0455 311 SER A CB  
2350 O OG  . SER B 96  ? 1.2693 2.4382 1.5995 -0.4943 0.1724  -0.0275 311 SER A OG  
2351 N N   . GLY B 109 ? 0.8843 1.9468 1.0757 0.2597  0.0492  0.2329  324 GLY A N   
2352 C CA  . GLY B 109 ? 0.9222 2.0368 1.1092 0.2650  0.0331  0.2403  324 GLY A CA  
2353 C C   . GLY B 109 ? 0.9649 2.0231 1.1370 0.2018  0.0129  0.1985  324 GLY A C   
2354 O O   . GLY B 109 ? 0.9536 1.9401 1.1221 0.1497  0.0114  0.1635  324 GLY A O   
2355 N N   . GLY B 110 ? 0.9534 2.0422 1.1147 0.2098  0.0004  0.2047  325 GLY A N   
2356 C CA  . GLY B 110 ? 0.9798 2.0247 1.1249 0.1559  -0.0163 0.1678  325 GLY A CA  
2357 C C   . GLY B 110 ? 1.0036 1.9560 1.1159 0.1908  -0.0151 0.1775  325 GLY A C   
2358 O O   . GLY B 110 ? 1.0629 1.9550 1.1597 0.2507  0.0013  0.2074  325 GLY A O   
2359 N N   . PHE B 111 ? 0.8200 1.7602 0.9193 0.1492  -0.0300 0.1500  326 PHE A N   
2360 C CA  . PHE B 111 ? 0.7655 1.6074 0.8336 0.1683  -0.0293 0.1510  326 PHE A CA  
2361 C C   . PHE B 111 ? 0.7331 1.4363 0.7855 0.1297  -0.0274 0.1137  326 PHE A C   
2362 O O   . PHE B 111 ? 0.7547 1.4627 0.8120 0.0723  -0.0348 0.0786  326 PHE A O   
2363 C CB  . PHE B 111 ? 0.7836 1.7101 0.8447 0.1565  -0.0451 0.1507  326 PHE A CB  
2364 C CG  . PHE B 111 ? 0.7547 1.5753 0.7845 0.1644  -0.0438 0.1450  326 PHE A CG  
2365 C CD1 . PHE B 111 ? 0.7070 1.4848 0.7187 0.2252  -0.0314 0.1820  326 PHE A CD1 
2366 C CD2 . PHE B 111 ? 0.7636 1.5194 0.7810 0.1119  -0.0506 0.1034  326 PHE A CD2 
2367 C CE1 . PHE B 111 ? 0.7523 1.4353 0.7367 0.2284  -0.0286 0.1767  326 PHE A CE1 
2368 C CE2 . PHE B 111 ? 0.7580 1.4235 0.7502 0.1202  -0.0481 0.0998  326 PHE A CE2 
2369 C CZ  . PHE B 111 ? 0.7808 1.4136 0.7576 0.1761  -0.0384 0.1359  326 PHE A CZ  
2370 N N   . TYR B 112 ? 0.7191 1.3011 0.7507 0.1609  -0.0155 0.1219  327 TYR A N   
2371 C CA  . TYR B 112 ? 0.7694 1.2275 0.7881 0.1347  -0.0123 0.0947  327 TYR A CA  
2372 C C   . TYR B 112 ? 0.8118 1.2044 0.8072 0.1390  -0.0149 0.0907  327 TYR A C   
2373 O O   . TYR B 112 ? 0.7988 1.1352 0.7761 0.1779  -0.0050 0.1112  327 TYR A O   
2374 C CB  . TYR B 112 ? 0.8249 1.2076 0.8379 0.1615  0.0031  0.1052  327 TYR A CB  
2375 C CG  . TYR B 112 ? 0.8117 1.2383 0.8462 0.1488  0.0075  0.1029  327 TYR A CG  
2376 C CD1 . TYR B 112 ? 0.7414 1.2819 0.7975 0.1676  0.0093  0.1247  327 TYR A CD1 
2377 C CD2 . TYR B 112 ? 0.8503 1.2093 0.8838 0.1205  0.0112  0.0825  327 TYR A CD2 
2378 C CE1 . TYR B 112 ? 0.8028 1.3882 0.8802 0.1544  0.0146  0.1232  327 TYR A CE1 
2379 C CE2 . TYR B 112 ? 0.7303 1.1273 0.7818 0.1084  0.0174  0.0820  327 TYR A CE2 
2380 C CZ  . TYR B 112 ? 0.7461 1.2561 0.8201 0.1237  0.0192  0.1012  327 TYR A CZ  
2381 O OH  . TYR B 112 ? 0.8131 1.3710 0.9077 0.1106  0.0266  0.1020  327 TYR A OH  
2382 N N   . GLY B 113 ? 0.8107 1.2079 0.8042 0.0973  -0.0249 0.0634  328 GLY A N   
2383 C CA  . GLY B 113 ? 0.7802 1.1345 0.7542 0.0978  -0.0276 0.0587  328 GLY A CA  
2384 C C   . GLY B 113 ? 0.7871 1.0393 0.7530 0.0719  -0.0245 0.0331  328 GLY A C   
2385 O O   . GLY B 113 ? 0.7713 0.9856 0.7451 0.0525  -0.0205 0.0189  328 GLY A O   
2386 N N   . VAL B 114 ? 0.7893 1.0011 0.7391 0.0758  -0.0250 0.0313  329 VAL A N   
2387 C CA  . VAL B 114 ? 0.8279 0.9587 0.7709 0.0560  -0.0218 0.0110  329 VAL A CA  
2388 C C   . VAL B 114 ? 0.8515 0.9964 0.7818 0.0456  -0.0250 0.0018  329 VAL A C   
2389 O O   . VAL B 114 ? 0.8608 1.0247 0.7800 0.0704  -0.0261 0.0213  329 VAL A O   
2390 C CB  . VAL B 114 ? 0.8120 0.8610 0.7475 0.0793  -0.0150 0.0235  329 VAL A CB  
2391 C CG1 . VAL B 114 ? 0.9139 0.9027 0.8441 0.0645  -0.0132 0.0090  329 VAL A CG1 
2392 C CG2 . VAL B 114 ? 0.8791 0.9059 0.8231 0.0810  -0.0109 0.0249  329 VAL A CG2 
2393 N N   . SER B 115 ? 0.8568 0.9883 0.7854 0.0105  -0.0229 -0.0270 330 SER A N   
2394 C CA  . SER B 115 ? 0.8370 0.9805 0.7501 -0.0029 -0.0232 -0.0404 330 SER A CA  
2395 C C   . SER B 115 ? 0.9016 0.9607 0.8102 -0.0096 -0.0128 -0.0538 330 SER A C   
2396 O O   . SER B 115 ? 0.9339 0.9523 0.8476 -0.0295 -0.0039 -0.0714 330 SER A O   
2397 C CB  . SER B 115 ? 0.8038 1.0164 0.7127 -0.0414 -0.0259 -0.0660 330 SER A CB  
2398 O OG  . SER B 115 ? 0.7408 1.0544 0.6466 -0.0317 -0.0378 -0.0510 330 SER A OG  
2399 N N   . SER B 116 ? 0.8931 0.9284 0.7925 0.0088  -0.0118 -0.0425 331 SER A N   
2400 C CA  . SER B 116 ? 0.9173 0.8929 0.8138 0.0042  -0.0019 -0.0529 331 SER A CA  
2401 C C   . SER B 116 ? 1.0056 1.0018 0.8843 -0.0051 0.0016  -0.0647 331 SER A C   
2402 O O   . SER B 116 ? 1.0125 1.0599 0.8798 0.0040  -0.0055 -0.0533 331 SER A O   
2403 C CB  . SER B 116 ? 0.8786 0.8098 0.7800 0.0280  -0.0012 -0.0322 331 SER A CB  
2404 O OG  . SER B 116 ? 0.8890 0.7850 0.8034 0.0294  -0.0001 -0.0301 331 SER A OG  
2405 N N   . GLN B 117 ? 1.0754 1.0301 0.9495 -0.0198 0.0152  -0.0852 332 GLN A N   
2406 C CA  . GLN B 117 ? 1.1049 1.0691 0.9595 -0.0275 0.0225  -0.0982 332 GLN A CA  
2407 C C   . GLN B 117 ? 1.0900 0.9936 0.9493 -0.0182 0.0378  -0.0989 332 GLN A C   
2408 O O   . GLN B 117 ? 1.1002 0.9570 0.9713 -0.0188 0.0481  -0.1032 332 GLN A O   
2409 C CB  . GLN B 117 ? 1.1247 1.1161 0.9604 -0.0630 0.0287  -0.1314 332 GLN A CB  
2410 C CG  . GLN B 117 ? 1.1522 1.1850 0.9617 -0.0708 0.0293  -0.1413 332 GLN A CG  
2411 C CD  . GLN B 117 ? 1.2609 1.3346 1.0469 -0.1129 0.0331  -0.1772 332 GLN A CD  
2412 O OE1 . GLN B 117 ? 1.3190 1.4303 1.1117 -0.1328 0.0252  -0.1844 332 GLN A OE1 
2413 N NE2 . GLN B 117 ? 1.1950 1.2662 0.9516 -0.1298 0.0462  -0.2013 332 GLN A NE2 
2414 N N   . TYR B 118 ? 0.9800 0.8901 0.8307 -0.0073 0.0404  -0.0912 333 TYR A N   
2415 C CA  . TYR B 118 ? 0.9711 0.8398 0.8294 0.0041  0.0546  -0.0878 333 TYR A CA  
2416 C C   . TYR B 118 ? 1.0015 0.8786 0.8372 -0.0030 0.0682  -0.1037 333 TYR A C   
2417 O O   . TYR B 118 ? 1.0128 0.9317 0.8252 -0.0166 0.0636  -0.1152 333 TYR A O   
2418 C CB  . TYR B 118 ? 0.9784 0.8444 0.8524 0.0247  0.0464  -0.0587 333 TYR A CB  
2419 C CG  . TYR B 118 ? 1.0011 0.8534 0.8928 0.0311  0.0359  -0.0450 333 TYR A CG  
2420 C CD1 . TYR B 118 ? 0.9975 0.8183 0.9069 0.0338  0.0412  -0.0449 333 TYR A CD1 
2421 C CD2 . TYR B 118 ? 1.0001 0.8715 0.8884 0.0375  0.0232  -0.0301 333 TYR A CD2 
2422 C CE1 . TYR B 118 ? 0.9909 0.8028 0.9125 0.0383  0.0316  -0.0334 333 TYR A CE1 
2423 C CE2 . TYR B 118 ? 1.0147 0.8699 0.9147 0.0431  0.0165  -0.0199 333 TYR A CE2 
2424 C CZ  . TYR B 118 ? 1.0076 0.8345 0.9234 0.0413  0.0196  -0.0231 333 TYR A CZ  
2425 O OH  . TYR B 118 ? 1.0428 0.8570 0.9662 0.0454  0.0129  -0.0140 333 TYR A OH  
2426 N N   . GLU B 119 ? 0.9978 0.8421 0.8400 0.0079  0.0854  -0.1027 334 GLU A N   
2427 C CA  . GLU B 119 ? 0.9709 0.8150 0.7911 0.0040  0.1037  -0.1185 334 GLU A CA  
2428 C C   . GLU B 119 ? 0.9802 0.8156 0.8169 0.0257  0.1134  -0.0992 334 GLU A C   
2429 O O   . GLU B 119 ? 0.9445 0.7632 0.8098 0.0403  0.1132  -0.0818 334 GLU A O   
2430 C CB  . GLU B 119 ? 1.0128 0.8147 0.8155 -0.0114 0.1287  -0.1506 334 GLU A CB  
2431 C CG  . GLU B 119 ? 1.0872 0.9122 0.8566 -0.0443 0.1280  -0.1818 334 GLU A CG  
2432 C CD  . GLU B 119 ? 1.1723 0.9393 0.9194 -0.0638 0.1596  -0.2165 334 GLU A CD  
2433 O OE1 . GLU B 119 ? 1.1572 0.8671 0.9148 -0.0428 0.1839  -0.2108 334 GLU A OE1 
2434 O OE2 . GLU B 119 ? 1.2438 1.0231 0.9623 -0.1001 0.1622  -0.2484 334 GLU A OE2 
2435 N N   . SER B 120 ? 0.9911 0.8453 0.8091 0.0261  0.1229  -0.1030 335 SER A N   
2436 C CA  . SER B 120 ? 0.9663 0.8204 0.8000 0.0439  0.1348  -0.0859 335 SER A CA  
2437 C C   . SER B 120 ? 0.9820 0.8389 0.7881 0.0421  0.1573  -0.1033 335 SER A C   
2438 O O   . SER B 120 ? 0.9715 0.8425 0.7425 0.0245  0.1577  -0.1252 335 SER A O   
2439 C CB  . SER B 120 ? 0.9348 0.8182 0.7809 0.0496  0.1178  -0.0569 335 SER A CB  
2440 O OG  . SER B 120 ? 0.9878 0.8735 0.8579 0.0618  0.1283  -0.0405 335 SER A OG  
2441 N N   . LEU B 121 ? 0.9596 0.8100 0.7818 0.0600  0.1766  -0.0931 336 LEU A N   
2442 C CA  . LEU B 121 ? 1.0014 0.8634 0.8000 0.0621  0.1972  -0.1020 336 LEU A CA  
2443 C C   . LEU B 121 ? 1.0240 0.9308 0.8241 0.0634  0.1850  -0.0779 336 LEU A C   
2444 O O   . LEU B 121 ? 1.0054 0.9347 0.7719 0.0556  0.1881  -0.0859 336 LEU A O   
2445 C CB  . LEU B 121 ? 0.9290 0.7670 0.7429 0.0844  0.2288  -0.1008 336 LEU A CB  
2446 C CG  . LEU B 121 ? 0.9614 0.7415 0.7568 0.0818  0.2511  -0.1292 336 LEU A CG  
2447 C CD1 . LEU B 121 ? 0.9814 0.7325 0.8022 0.1139  0.2809  -0.1167 336 LEU A CD1 
2448 C CD2 . LEU B 121 ? 1.0216 0.7853 0.7635 0.0589  0.2673  -0.1680 336 LEU A CD2 
2449 N N   . GLU B 122 ? 1.0246 0.9439 0.8589 0.0706  0.1728  -0.0489 337 GLU A N   
2450 C CA  . GLU B 122 ? 1.0061 0.9552 0.8374 0.0682  0.1660  -0.0264 337 GLU A CA  
2451 C C   . GLU B 122 ? 1.0070 0.9618 0.8220 0.0596  0.1431  -0.0190 337 GLU A C   
2452 O O   . GLU B 122 ? 1.0077 0.9493 0.8240 0.0552  0.1292  -0.0281 337 GLU A O   
2453 C CB  . GLU B 122 ? 1.0266 0.9869 0.8970 0.0729  0.1672  -0.0017 337 GLU A CB  
2454 C CG  . GLU B 122 ? 1.0708 1.0184 0.9718 0.0724  0.1525  0.0046  337 GLU A CG  
2455 C CD  . GLU B 122 ? 1.1305 1.1021 1.0710 0.0789  0.1607  0.0204  337 GLU A CD  
2456 O OE1 . GLU B 122 ? 1.0994 1.0740 1.0533 0.0963  0.1783  0.0157  337 GLU A OE1 
2457 O OE2 . GLU B 122 ? 1.1549 1.1443 1.1115 0.0663  0.1518  0.0381  337 GLU A OE2 
2458 N N   . HIS B 123 ? 0.9770 0.9523 0.7757 0.0599  0.1424  0.0004  338 HIS A N   
2459 C CA  . HIS B 123 ? 0.9824 0.9671 0.7610 0.0601  0.1267  0.0145  338 HIS A CA  
2460 C C   . HIS B 123 ? 0.9308 0.8931 0.7294 0.0611  0.1201  0.0398  338 HIS A C   
2461 O O   . HIS B 123 ? 0.9158 0.8736 0.7207 0.0590  0.1311  0.0582  338 HIS A O   
2462 C CB  . HIS B 123 ? 0.9649 0.9821 0.7076 0.0641  0.1338  0.0250  338 HIS A CB  
2463 C CG  . HIS B 123 ? 0.9364 0.9702 0.6580 0.0723  0.1210  0.0464  338 HIS A CG  
2464 N ND1 . HIS B 123 ? 0.8995 0.9080 0.6290 0.0803  0.1203  0.0765  338 HIS A ND1 
2465 C CD2 . HIS B 123 ? 0.9031 0.9797 0.5951 0.0751  0.1109  0.0433  338 HIS A CD2 
2466 C CE1 . HIS B 123 ? 0.9444 0.9744 0.6506 0.0939  0.1126  0.0943  338 HIS A CE1 
2467 N NE2 . HIS B 123 ? 0.9096 0.9894 0.5950 0.0913  0.1046  0.0761  338 HIS A NE2 
2468 N N   . MET B 124 ? 0.9408 0.8883 0.7452 0.0616  0.1045  0.0396  339 MET A N   
2469 C CA  . MET B 124 ? 0.9118 0.8295 0.7318 0.0597  0.1004  0.0567  339 MET A CA  
2470 C C   . MET B 124 ? 0.9070 0.8189 0.7090 0.0697  0.0906  0.0692  339 MET A C   
2471 O O   . MET B 124 ? 0.9310 0.8723 0.7167 0.0765  0.0823  0.0630  339 MET A O   
2472 C CB  . MET B 124 ? 0.9227 0.8254 0.7749 0.0525  0.0941  0.0438  339 MET A CB  
2473 C CG  . MET B 124 ? 0.9277 0.8372 0.8047 0.0457  0.1048  0.0457  339 MET A CG  
2474 S SD  . MET B 124 ? 0.8578 0.7650 0.7675 0.0470  0.0980  0.0316  339 MET A SD  
2475 C CE  . MET B 124 ? 0.9529 0.8545 0.8429 0.0546  0.0965  0.0084  339 MET A CE  
2476 N N   . THR B 125 ? 0.9607 0.8372 0.7647 0.0697  0.0934  0.0865  340 THR A N   
2477 C CA  . THR B 125 ? 1.0266 0.8879 0.8217 0.0814  0.0858  0.0958  340 THR A CA  
2478 C C   . THR B 125 ? 0.9618 0.7920 0.7802 0.0698  0.0786  0.0848  340 THR A C   
2479 O O   . THR B 125 ? 0.9436 0.7512 0.7747 0.0538  0.0851  0.0843  340 THR A O   
2480 C CB  . THR B 125 ? 1.0631 0.9006 0.8307 0.0963  0.1013  0.1273  340 THR A CB  
2481 O OG1 . THR B 125 ? 1.1267 0.9179 0.8972 0.0798  0.1174  0.1341  340 THR A OG1 
2482 C CG2 . THR B 125 ? 1.0888 0.9669 0.8329 0.1088  0.1077  0.1400  340 THR A CG2 
2483 N N   . LEU B 126 ? 0.9718 0.8096 0.7961 0.0752  0.0650  0.0749  341 LEU A N   
2484 C CA  . LEU B 126 ? 1.0027 0.8165 0.8461 0.0663  0.0574  0.0649  341 LEU A CA  
2485 C C   . LEU B 126 ? 0.9700 0.7490 0.7994 0.0754  0.0605  0.0789  341 LEU A C   
2486 O O   . LEU B 126 ? 0.9384 0.7304 0.7531 0.0952  0.0595  0.0903  341 LEU A O   
2487 C CB  . LEU B 126 ? 0.9874 0.8248 0.8455 0.0650  0.0446  0.0447  341 LEU A CB  
2488 C CG  . LEU B 126 ? 0.9258 0.7901 0.7887 0.0597  0.0460  0.0273  341 LEU A CG  
2489 C CD1 . LEU B 126 ? 0.9214 0.7925 0.7922 0.0556  0.0382  0.0083  341 LEU A CD1 
2490 C CD2 . LEU B 126 ? 0.9112 0.7681 0.7918 0.0524  0.0543  0.0249  341 LEU A CD2 
2491 N N   . THR B 127 ? 0.9620 0.7010 0.7944 0.0612  0.0658  0.0780  342 THR A N   
2492 C CA  . THR B 127 ? 1.0565 0.7593 0.8786 0.0664  0.0674  0.0811  342 THR A CA  
2493 C C   . THR B 127 ? 0.9950 0.7115 0.8399 0.0579  0.0510  0.0629  342 THR A C   
2494 O O   . THR B 127 ? 0.9625 0.6846 0.8251 0.0389  0.0464  0.0521  342 THR A O   
2495 C CB  . THR B 127 ? 1.0495 0.6929 0.8522 0.0521  0.0861  0.0872  342 THR A CB  
2496 O OG1 . THR B 127 ? 1.1211 0.7598 0.9391 0.0252  0.0787  0.0695  342 THR A OG1 
2497 C CG2 . THR B 127 ? 0.9422 0.5732 0.7325 0.0441  0.1033  0.0989  342 THR A CG2 
2498 N N   . CYS B 128 ? 1.0048 0.7334 0.8500 0.0731  0.0432  0.0622  343 CYS A N   
2499 C CA  . CYS B 128 ? 0.9893 0.7259 0.8520 0.0674  0.0308  0.0483  343 CYS A CA  
2500 C C   . CYS B 128 ? 0.9653 0.6665 0.8150 0.0715  0.0351  0.0516  343 CYS A C   
2501 O O   . CYS B 128 ? 0.9608 0.6570 0.7961 0.0920  0.0410  0.0634  343 CYS A O   
2502 C CB  . CYS B 128 ? 1.0140 0.7924 0.8871 0.0748  0.0208  0.0412  343 CYS A CB  
2503 S SG  . CYS B 128 ? 1.0347 0.8515 0.9083 0.0725  0.0215  0.0359  343 CYS A SG  
2504 N N   . SER B 129 ? 1.0021 0.6843 0.8559 0.0534  0.0330  0.0421  344 SER A N   
2505 C CA  . SER B 129 ? 1.0303 0.6761 0.8671 0.0532  0.0387  0.0408  344 SER A CA  
2506 C C   . SER B 129 ? 0.9955 0.6632 0.8487 0.0539  0.0251  0.0320  344 SER A C   
2507 O O   . SER B 129 ? 1.0098 0.7030 0.8838 0.0424  0.0143  0.0246  344 SER A O   
2508 C CB  . SER B 129 ? 1.0756 0.6855 0.8975 0.0268  0.0479  0.0341  344 SER A CB  
2509 O OG  . SER B 129 ? 1.1639 0.7541 0.9753 0.0170  0.0470  0.0241  344 SER A OG  
2510 N N   . SER B 130 ? 0.9623 0.6211 0.8059 0.0701  0.0285  0.0359  345 SER A N   
2511 C CA  . SER B 130 ? 0.9121 0.5824 0.7651 0.0693  0.0201  0.0291  345 SER A CA  
2512 C C   . SER B 130 ? 0.9610 0.5893 0.7893 0.0642  0.0296  0.0253  345 SER A C   
2513 O O   . SER B 130 ? 1.0193 0.6081 0.8215 0.0758  0.0470  0.0317  345 SER A O   
2514 C CB  . SER B 130 ? 0.8954 0.5974 0.7582 0.0880  0.0171  0.0346  345 SER A CB  
2515 O OG  . SER B 130 ? 0.9224 0.6627 0.8056 0.0832  0.0080  0.0304  345 SER A OG  
2516 N N   . LYS B 131 ? 0.9525 0.5879 0.7857 0.0483  0.0208  0.0156  346 LYS A N   
2517 C CA  . LYS B 131 ? 0.9116 0.5138 0.7182 0.0374  0.0282  0.0072  346 LYS A CA  
2518 C C   . LYS B 131 ? 0.9296 0.5543 0.7455 0.0435  0.0197  0.0061  346 LYS A C   
2519 O O   . LYS B 131 ? 0.9097 0.5663 0.7430 0.0332  0.0064  0.0044  346 LYS A O   
2520 C CB  . LYS B 131 ? 0.9942 0.5943 0.7934 0.0057  0.0253  -0.0035 346 LYS A CB  
2521 C CG  . LYS B 131 ? 1.1415 0.7205 0.9330 -0.0040 0.0356  -0.0020 346 LYS A CG  
2522 C CD  . LYS B 131 ? 1.2982 0.8659 1.0721 -0.0423 0.0393  -0.0159 346 LYS A CD  
2523 C CE  . LYS B 131 ? 1.3141 0.9494 1.1204 -0.0587 0.0194  -0.0160 346 LYS A CE  
2524 N NZ  . LYS B 131 ? 1.4533 1.0898 1.2488 -0.0966 0.0248  -0.0257 346 LYS A NZ  
2525 N N   . VAL B 132 ? 0.9768 0.5870 0.7811 0.0627  0.0297  0.0102  347 VAL A N   
2526 C CA  . VAL B 132 ? 0.9720 0.5988 0.7805 0.0674  0.0257  0.0095  347 VAL A CA  
2527 C C   . VAL B 132 ? 0.9971 0.5962 0.7748 0.0509  0.0308  -0.0023 347 VAL A C   
2528 O O   . VAL B 132 ? 1.0869 0.6369 0.8300 0.0509  0.0492  -0.0085 347 VAL A O   
2529 C CB  . VAL B 132 ? 0.9526 0.5853 0.7627 0.0941  0.0354  0.0194  347 VAL A CB  
2530 C CG1 . VAL B 132 ? 0.9957 0.6440 0.8083 0.0962  0.0340  0.0186  347 VAL A CG1 
2531 C CG2 . VAL B 132 ? 0.8622 0.5349 0.7001 0.1044  0.0286  0.0285  347 VAL A CG2 
2532 N N   . CYS B 133 ? 0.9681 0.5971 0.7543 0.0376  0.0174  -0.0050 348 CYS A N   
2533 C CA  . CYS B 133 ? 1.1250 0.7429 0.8808 0.0186  0.0191  -0.0170 348 CYS A CA  
2534 C C   . CYS B 133 ? 1.1482 0.7766 0.8997 0.0305  0.0205  -0.0134 348 CYS A C   
2535 O O   . CYS B 133 ? 1.0533 0.7141 0.8338 0.0436  0.0128  -0.0011 348 CYS A O   
2536 C CB  . CYS B 133 ? 1.1809 0.8374 0.9457 -0.0059 0.0029  -0.0196 348 CYS A CB  
2537 S SG  . CYS B 133 ? 1.2508 0.9070 1.0295 -0.0179 0.0013  -0.0203 348 CYS A SG  
2538 N N   . SER B 134 ? 1.2562 0.8519 0.9682 0.0247  0.0338  -0.0255 349 SER A N   
2539 C CA  . SER B 134 ? 1.2187 0.8215 0.9209 0.0358  0.0385  -0.0229 349 SER A CA  
2540 C C   . SER B 134 ? 1.2519 0.8539 0.9163 0.0095  0.0372  -0.0387 349 SER A C   
2541 O O   . SER B 134 ? 1.3238 0.8797 0.9469 -0.0079 0.0520  -0.0582 349 SER A O   
2542 C CB  . SER B 134 ? 1.1982 0.7635 0.8858 0.0613  0.0615  -0.0210 349 SER A CB  
2543 O OG  . SER B 134 ? 1.1692 0.7525 0.8562 0.0738  0.0653  -0.0155 349 SER A OG  
2544 N N   . PHE B 135 ? 1.2585 0.9111 0.9344 0.0052  0.0213  -0.0301 350 PHE A N   
2545 C CA  . PHE B 135 ? 1.3131 0.9905 0.9586 -0.0221 0.0134  -0.0414 350 PHE A CA  
2546 C C   . PHE B 135 ? 1.4309 1.1109 1.0670 -0.0541 0.0071  -0.0564 350 PHE A C   
2547 O O   . PHE B 135 ? 1.4990 1.1521 1.0906 -0.0842 0.0165  -0.0811 350 PHE A O   
2548 C CB  . PHE B 135 ? 1.2204 0.8637 0.8163 -0.0260 0.0313  -0.0576 350 PHE A CB  
2549 C CG  . PHE B 135 ? 1.1756 0.8263 0.7824 0.0034  0.0379  -0.0416 350 PHE A CG  
2550 C CD1 . PHE B 135 ? 1.1290 0.7472 0.7490 0.0310  0.0545  -0.0351 350 PHE A CD1 
2551 C CD2 . PHE B 135 ? 1.1785 0.8763 0.7831 0.0034  0.0281  -0.0303 350 PHE A CD2 
2552 C CE1 . PHE B 135 ? 1.1465 0.7811 0.7795 0.0538  0.0610  -0.0205 350 PHE A CE1 
2553 C CE2 . PHE B 135 ? 1.0551 0.7587 0.6693 0.0273  0.0368  -0.0151 350 PHE A CE2 
2554 C CZ  . PHE B 135 ? 1.0597 0.7331 0.6894 0.0502  0.0530  -0.0115 350 PHE A CZ  
2555 N N   . GLY B 136 ? 1.9469 1.6581 1.6243 -0.0497 -0.0063 -0.0424 351 GLY A N   
2556 C CA  . GLY B 136 ? 2.0033 1.7269 1.6797 -0.0788 -0.0124 -0.0529 351 GLY A CA  
2557 C C   . GLY B 136 ? 2.0003 1.6521 1.6555 -0.0880 0.0076  -0.0695 351 GLY A C   
2558 O O   . GLY B 136 ? 2.0038 1.6560 1.6797 -0.0922 0.0056  -0.0662 351 GLY A O   
2559 N N   . LYS B 137 ? 1.5219 1.1091 1.1339 -0.0884 0.0302  -0.0853 352 LYS A N   
2560 C CA  . LYS B 137 ? 1.5240 1.0321 1.1079 -0.0937 0.0561  -0.0983 352 LYS A CA  
2561 C C   . LYS B 137 ? 1.4053 0.8949 1.0217 -0.0536 0.0620  -0.0768 352 LYS A C   
2562 O O   . LYS B 137 ? 1.3234 0.8349 0.9654 -0.0208 0.0572  -0.0597 352 LYS A O   
2563 C CB  . LYS B 137 ? 1.5444 0.9826 1.0689 -0.1004 0.0845  -0.1197 352 LYS A CB  
2564 C CG  . LYS B 137 ? 1.5394 0.9941 1.0221 -0.1496 0.0807  -0.1475 352 LYS A CG  
2565 C CD  . LYS B 137 ? 1.6576 1.0503 1.0802 -0.1532 0.1081  -0.1691 352 LYS A CD  
2566 C CE  . LYS B 137 ? 1.5499 1.0095 0.9576 -0.1736 0.0890  -0.1774 352 LYS A CE  
2567 N NZ  . LYS B 137 ? 1.3660 0.9022 0.8286 -0.1357 0.0627  -0.1434 352 LYS A NZ  
2568 N N   . GLN B 138 ? 1.3581 0.8118 0.9719 -0.0593 0.0732  -0.0778 353 GLN A N   
2569 C CA  . GLN B 138 ? 1.3023 0.7539 0.9473 -0.0263 0.0750  -0.0568 353 GLN A CA  
2570 C C   . GLN B 138 ? 1.2383 0.6268 0.8575 0.0056  0.1044  -0.0509 353 GLN A C   
2571 O O   . GLN B 138 ? 1.2640 0.5780 0.8378 -0.0037 0.1331  -0.0629 353 GLN A O   
2572 C CB  . GLN B 138 ? 1.3437 0.7920 0.9967 -0.0460 0.0740  -0.0575 353 GLN A CB  
2573 C CG  . GLN B 138 ? 1.2798 0.7073 0.9465 -0.0174 0.0845  -0.0395 353 GLN A CG  
2574 C CD  . GLN B 138 ? 1.4382 0.8472 1.0996 -0.0424 0.0910  -0.0433 353 GLN A CD  
2575 O OE1 . GLN B 138 ? 1.5081 0.9374 1.1666 -0.0822 0.0824  -0.0583 353 GLN A OE1 
2576 N NE2 . GLN B 138 ? 1.4570 0.8330 1.1162 -0.0195 0.1072  -0.0281 353 GLN A NE2 
2577 N N   . VAL B 139 ? 1.1841 0.6031 0.8310 0.0429  0.1000  -0.0318 354 VAL A N   
2578 C CA  . VAL B 139 ? 1.1955 0.5744 0.8242 0.0798  0.1269  -0.0207 354 VAL A CA  
2579 C C   . VAL B 139 ? 1.1912 0.5776 0.8407 0.1105  0.1320  0.0023  354 VAL A C   
2580 O O   . VAL B 139 ? 1.1998 0.5487 0.8299 0.1442  0.1594  0.0160  354 VAL A O   
2581 C CB  . VAL B 139 ? 1.1976 0.6137 0.8388 0.1000  0.1223  -0.0146 354 VAL A CB  
2582 C CG1 . VAL B 139 ? 1.2274 0.6405 0.8445 0.0712  0.1173  -0.0351 354 VAL A CG1 
2583 C CG2 . VAL B 139 ? 1.1893 0.6836 0.8843 0.1091  0.0954  0.0004  354 VAL A CG2 
2584 N N   . VAL B 140 ? 1.1204 0.5564 0.8067 0.1025  0.1086  0.0085  355 VAL A N   
2585 C CA  . VAL B 140 ? 1.1444 0.5952 0.8474 0.1266  0.1112  0.0286  355 VAL A CA  
2586 C C   . VAL B 140 ? 1.1182 0.5786 0.8337 0.1005  0.0978  0.0236  355 VAL A C   
2587 O O   . VAL B 140 ? 1.0869 0.5858 0.8246 0.0757  0.0750  0.0131  355 VAL A O   
2588 C CB  . VAL B 140 ? 1.0799 0.6051 0.8219 0.1512  0.0957  0.0442  355 VAL A CB  
2589 C CG1 . VAL B 140 ? 1.0073 0.5689 0.7709 0.1609  0.0877  0.0581  355 VAL A CG1 
2590 C CG2 . VAL B 140 ? 1.1501 0.6720 0.8814 0.1867  0.1152  0.0579  355 VAL A CG2 
2591 N N   . GLU B 141 ? 1.1149 0.5404 0.8153 0.1090  0.1147  0.0339  356 GLU A N   
2592 C CA  . GLU B 141 ? 1.1219 0.5682 0.8392 0.0938  0.1037  0.0358  356 GLU A CA  
2593 C C   . GLU B 141 ? 1.0689 0.5368 0.7951 0.1286  0.1092  0.0606  356 GLU A C   
2594 O O   . GLU B 141 ? 1.1285 0.5536 0.8280 0.1566  0.1358  0.0775  356 GLU A O   
2595 C CB  . GLU B 141 ? 1.1753 0.5617 0.8625 0.0626  0.1202  0.0241  356 GLU A CB  
2596 C CG  . GLU B 141 ? 1.2396 0.6410 0.9399 0.0575  0.1176  0.0335  356 GLU A CG  
2597 C CD  . GLU B 141 ? 1.2762 0.6740 0.9755 0.0120  0.1132  0.0163  356 GLU A CD  
2598 O OE1 . GLU B 141 ? 1.3384 0.6856 1.0057 -0.0175 0.1286  -0.0006 356 GLU A OE1 
2599 O OE2 . GLU B 141 ? 1.2544 0.7061 0.9854 0.0039  0.0946  0.0185  356 GLU A OE2 
2600 N N   . LYS B 142 ? 1.0100 0.5439 0.7703 0.1278  0.0864  0.0637  357 LYS A N   
2601 C CA  . LYS B 142 ? 1.0168 0.5875 0.7854 0.1546  0.0872  0.0846  357 LYS A CA  
2602 C C   . LYS B 142 ? 0.9991 0.5755 0.7735 0.1358  0.0817  0.0822  357 LYS A C   
2603 O O   . LYS B 142 ? 1.0118 0.6004 0.8024 0.1067  0.0669  0.0647  357 LYS A O   
2604 C CB  . LYS B 142 ? 0.9768 0.6245 0.7763 0.1652  0.0674  0.0861  357 LYS A CB  
2605 C CG  . LYS B 142 ? 1.0199 0.7181 0.8225 0.1997  0.0713  0.1105  357 LYS A CG  
2606 C CD  . LYS B 142 ? 1.0675 0.8476 0.9014 0.1963  0.0506  0.1046  357 LYS A CD  
2607 C CE  . LYS B 142 ? 1.1389 0.9922 0.9836 0.2032  0.0408  0.1146  357 LYS A CE  
2608 N NZ  . LYS B 142 ? 1.0235 0.9361 0.8940 0.1747  0.0196  0.0936  357 LYS A NZ  
2609 N N   . VAL B 143 ? 1.0623 0.6299 0.8221 0.1544  0.0960  0.1022  358 VAL A N   
2610 C CA  . VAL B 143 ? 1.0872 0.6582 0.8497 0.1370  0.0941  0.1012  358 VAL A CA  
2611 C C   . VAL B 143 ? 1.0243 0.6442 0.7896 0.1627  0.0928  0.1223  358 VAL A C   
2612 O O   . VAL B 143 ? 1.0861 0.6905 0.8294 0.1949  0.1122  0.1484  358 VAL A O   
2613 C CB  . VAL B 143 ? 1.0539 0.5474 0.7858 0.1210  0.1193  0.1017  358 VAL A CB  
2614 C CG1 . VAL B 143 ? 0.9704 0.4787 0.7090 0.1041  0.1173  0.1029  358 VAL A CG1 
2615 C CG2 . VAL B 143 ? 1.1523 0.6108 0.8793 0.0887  0.1181  0.0772  358 VAL A CG2 
2616 N N   . GLU B 144 ? 0.9949 0.6729 0.7837 0.1495  0.0725  0.1119  359 GLU A N   
2617 C CA  . GLU B 144 ? 1.0159 0.7511 0.8054 0.1663  0.0681  0.1261  359 GLU A CA  
2618 C C   . GLU B 144 ? 1.0079 0.7438 0.7968 0.1490  0.0689  0.1222  359 GLU A C   
2619 O O   . GLU B 144 ? 1.0320 0.7420 0.8298 0.1220  0.0674  0.1055  359 GLU A O   
2620 C CB  . GLU B 144 ? 0.9846 0.7943 0.7973 0.1641  0.0463  0.1142  359 GLU A CB  
2621 C CG  . GLU B 144 ? 1.0601 0.8713 0.8831 0.1674  0.0415  0.1082  359 GLU A CG  
2622 C CD  . GLU B 144 ? 1.1375 1.0280 0.9716 0.1806  0.0307  0.1139  359 GLU A CD  
2623 O OE1 . GLU B 144 ? 1.0760 1.0116 0.9000 0.2021  0.0337  0.1350  359 GLU A OE1 
2624 O OE2 . GLU B 144 ? 1.1315 1.0436 0.9837 0.1685  0.0202  0.0986  359 GLU A OE2 
2625 N N   . THR B 145 ? 0.9854 0.7601 0.7637 0.1663  0.0714  0.1396  360 THR A N   
2626 C CA  . THR B 145 ? 1.0808 0.8613 0.8546 0.1546  0.0749  0.1395  360 THR A CA  
2627 C C   . THR B 145 ? 1.0531 0.9136 0.8312 0.1582  0.0602  0.1357  360 THR A C   
2628 O O   . THR B 145 ? 1.0633 0.9714 0.8308 0.1831  0.0588  0.1549  360 THR A O   
2629 C CB  . THR B 145 ? 1.0194 0.7504 0.7634 0.1705  0.1017  0.1682  360 THR A CB  
2630 O OG1 . THR B 145 ? 1.0661 0.7973 0.7922 0.2085  0.1129  0.1964  360 THR A OG1 
2631 C CG2 . THR B 145 ? 0.9838 0.6349 0.7226 0.1467  0.1170  0.1594  360 THR A CG2 
2632 N N   . GLU B 146 ? 1.0171 0.8960 0.8094 0.1333  0.0506  0.1106  361 GLU A N   
2633 C CA  . GLU B 146 ? 1.1112 1.0567 0.9008 0.1292  0.0405  0.1002  361 GLU A CA  
2634 C C   . GLU B 146 ? 1.1137 1.0578 0.8964 0.1180  0.0484  0.0953  361 GLU A C   
2635 O O   . GLU B 146 ? 0.9845 0.8945 0.7818 0.1009  0.0523  0.0812  361 GLU A O   
2636 C CB  . GLU B 146 ? 1.0336 1.0038 0.8425 0.1096  0.0257  0.0698  361 GLU A CB  
2637 C CG  . GLU B 146 ? 1.0342 1.0765 0.8334 0.1011  0.0168  0.0563  361 GLU A CG  
2638 C CD  . GLU B 146 ? 1.0640 1.1729 0.8480 0.1237  0.0119  0.0811  361 GLU A CD  
2639 O OE1 . GLU B 146 ? 1.0580 1.2361 0.8279 0.1160  0.0053  0.0738  361 GLU A OE1 
2640 O OE2 . GLU B 146 ? 1.1637 1.2610 0.9488 0.1493  0.0154  0.1074  361 GLU A OE2 
2641 N N   . ARG B 147 ? 1.3255 1.3143 1.0861 0.1295  0.0511  0.1089  362 ARG A N   
2642 C CA  . ARG B 147 ? 1.3609 1.3566 1.1107 0.1210  0.0598  0.1052  362 ARG A CA  
2643 C C   . ARG B 147 ? 1.3621 1.4069 1.1102 0.1026  0.0505  0.0738  362 ARG A C   
2644 O O   . ARG B 147 ? 1.3495 1.4376 1.0970 0.0978  0.0374  0.0610  362 ARG A O   
2645 C CB  . ARG B 147 ? 1.4248 1.4356 1.1455 0.1446  0.0724  0.1407  362 ARG A CB  
2646 C CG  . ARG B 147 ? 1.4408 1.5306 1.1413 0.1642  0.0630  0.1556  362 ARG A CG  
2647 C CD  . ARG B 147 ? 1.4855 1.5834 1.1909 0.1878  0.0580  0.1755  362 ARG A CD  
2648 N NE  . ARG B 147 ? 1.5568 1.5743 1.2610 0.2054  0.0766  0.2003  362 ARG A NE  
2649 C CZ  . ARG B 147 ? 1.6153 1.5991 1.2950 0.2293  0.0995  0.2365  362 ARG A CZ  
2650 N NH1 . ARG B 147 ? 1.5810 1.6094 1.2370 0.2428  0.1053  0.2569  362 ARG A NH1 
2651 N NH2 . ARG B 147 ? 1.7131 1.6128 1.3883 0.2386  0.1198  0.2521  362 ARG A NH2 
2652 N N   . ALA B 148 ? 1.1277 1.1636 0.8736 0.0903  0.0602  0.0602  363 ALA A N   
2653 C CA  . ALA B 148 ? 1.0259 1.0875 0.7663 0.0708  0.0589  0.0259  363 ALA A CA  
2654 C C   . ALA B 148 ? 0.9869 1.1211 0.6966 0.0696  0.0516  0.0232  363 ALA A C   
2655 O O   . ALA B 148 ? 0.9877 1.1555 0.6763 0.0876  0.0534  0.0515  363 ALA A O   
2656 C CB  . ALA B 148 ? 0.9898 1.0279 0.7316 0.0646  0.0757  0.0174  363 ALA A CB  
2657 N N   . GLN B 149 ? 0.9547 1.1153 0.6603 0.0469  0.0445  -0.0104 364 GLN A N   
2658 C CA  . GLN B 149 ? 0.9421 1.1795 0.6159 0.0332  0.0381  -0.0249 364 GLN A CA  
2659 C C   . GLN B 149 ? 0.9836 1.2032 0.6418 0.0039  0.0516  -0.0688 364 GLN A C   
2660 O O   . GLN B 149 ? 0.9777 1.1476 0.6519 -0.0123 0.0578  -0.0955 364 GLN A O   
2661 C CB  . GLN B 149 ? 0.8944 1.1875 0.5727 0.0260  0.0196  -0.0279 364 GLN A CB  
2662 C CG  . GLN B 149 ? 0.9120 1.3082 0.5629 0.0316  0.0081  -0.0127 364 GLN A CG  
2663 C CD  . GLN B 149 ? 1.0132 1.4692 0.6378 -0.0100 0.0040  -0.0566 364 GLN A CD  
2664 O OE1 . GLN B 149 ? 1.0276 1.4716 0.6620 -0.0411 0.0019  -0.0911 364 GLN A OE1 
2665 N NE2 . GLN B 149 ? 0.9734 1.4896 0.5609 -0.0140 0.0057  -0.0578 364 GLN A NE2 
2666 N N   . LEU B 150 ? 1.0301 1.2864 0.6542 -0.0010 0.0594  -0.0750 365 LEU A N   
2667 C CA  . LEU B 150 ? 1.0763 1.3083 0.6788 -0.0266 0.0782  -0.1175 365 LEU A CA  
2668 C C   . LEU B 150 ? 1.0716 1.3363 0.6534 -0.0650 0.0732  -0.1597 365 LEU A C   
2669 O O   . LEU B 150 ? 0.9855 1.3367 0.5488 -0.0752 0.0551  -0.1573 365 LEU A O   
2670 C CB  . LEU B 150 ? 1.1322 1.3938 0.7008 -0.0206 0.0900  -0.1118 365 LEU A CB  
2671 C CG  . LEU B 150 ? 1.0671 1.3195 0.5988 -0.0471 0.1118  -0.1568 365 LEU A CG  
2672 C CD1 . LEU B 150 ? 1.0398 1.2026 0.5898 -0.0426 0.1392  -0.1724 365 LEU A CD1 
2673 C CD2 . LEU B 150 ? 1.0692 1.3819 0.5623 -0.0403 0.1148  -0.1438 365 LEU A CD2 
2674 N N   . GLU B 151 ? 1.3427 1.5402 0.9283 -0.0863 0.0907  -0.1963 366 GLU A N   
2675 C CA  . GLU B 151 ? 1.3528 1.5627 0.9123 -0.1308 0.0948  -0.2435 366 GLU A CA  
2676 C C   . GLU B 151 ? 1.4695 1.6014 1.0058 -0.1473 0.1303  -0.2833 366 GLU A C   
2677 O O   . GLU B 151 ? 1.5149 1.5955 1.0619 -0.1198 0.1481  -0.2694 366 GLU A O   
2678 C CB  . GLU B 151 ? 1.3275 1.5267 0.9169 -0.1412 0.0825  -0.2452 366 GLU A CB  
2679 C CG  . GLU B 151 ? 1.3444 1.6492 0.9315 -0.1512 0.0535  -0.2340 366 GLU A CG  
2680 C CD  . GLU B 151 ? 1.3831 1.6848 0.9947 -0.1694 0.0447  -0.2431 366 GLU A CD  
2681 O OE1 . GLU B 151 ? 1.4222 1.6412 1.0392 -0.1874 0.0644  -0.2704 366 GLU A OE1 
2682 O OE2 . GLU B 151 ? 1.3796 1.7627 1.0045 -0.1632 0.0205  -0.2203 366 GLU A OE2 
2683 N N   . ASP B 152 ? 1.4622 1.5850 0.9660 -0.1931 0.1434  -0.3328 367 ASP A N   
2684 C CA  . ASP B 152 ? 1.4996 1.5504 0.9652 -0.2152 0.1831  -0.3782 367 ASP A CA  
2685 C C   . ASP B 152 ? 1.4842 1.4531 0.9711 -0.1731 0.2090  -0.3587 367 ASP A C   
2686 O O   . ASP B 152 ? 1.5634 1.4470 1.0706 -0.1634 0.2307  -0.3626 367 ASP A O   
2687 C CB  . ASP B 152 ? 1.6166 1.6130 1.0698 -0.2580 0.2007  -0.4217 367 ASP A CB  
2688 C CG  . ASP B 152 ? 1.6953 1.6724 1.0821 -0.3092 0.2318  -0.4834 367 ASP A CG  
2689 O OD1 . ASP B 152 ? 1.6720 1.6596 1.0242 -0.3044 0.2455  -0.4926 367 ASP A OD1 
2690 O OD2 . ASP B 152 ? 1.7154 1.6654 1.0927 -0.3526 0.2418  -0.5164 367 ASP A OD2 
2691 N N   . GLY B 153 ? 1.3124 1.3154 0.7974 -0.1459 0.2060  -0.3329 368 GLY A N   
2692 C CA  . GLY B 153 ? 1.2278 1.1758 0.7317 -0.1091 0.2298  -0.3140 368 GLY A CA  
2693 C C   . GLY B 153 ? 1.2434 1.1632 0.8077 -0.0727 0.2194  -0.2716 368 GLY A C   
2694 O O   . GLY B 153 ? 1.1262 1.0090 0.7106 -0.0439 0.2394  -0.2556 368 GLY A O   
2695 N N   . ARG B 154 ? 1.3191 1.2608 0.9121 -0.0741 0.1898  -0.2535 369 ARG A N   
2696 C CA  . ARG B 154 ? 1.2384 1.1611 0.8840 -0.0444 0.1768  -0.2148 369 ARG A CA  
2697 C C   . ARG B 154 ? 1.1822 1.1665 0.8428 -0.0379 0.1414  -0.1826 369 ARG A C   
2698 O O   . ARG B 154 ? 1.1538 1.1993 0.7890 -0.0539 0.1255  -0.1881 369 ARG A O   
2699 C CB  . ARG B 154 ? 1.2704 1.1304 0.9359 -0.0483 0.1866  -0.2266 369 ARG A CB  
2700 C CG  . ARG B 154 ? 1.3056 1.1848 0.9699 -0.0748 0.1663  -0.2388 369 ARG A CG  
2701 C CD  . ARG B 154 ? 1.3645 1.1697 1.0344 -0.0842 0.1879  -0.2589 369 ARG A CD  
2702 N NE  . ARG B 154 ? 1.3078 1.1259 0.9650 -0.1212 0.1790  -0.2833 369 ARG A NE  
2703 C CZ  . ARG B 154 ? 1.4482 1.2398 1.0658 -0.1608 0.2019  -0.3286 369 ARG A CZ  
2704 N NH1 . ARG B 154 ? 1.5574 1.3082 1.1382 -0.1679 0.2351  -0.3564 369 ARG A NH1 
2705 N NH2 . ARG B 154 ? 1.4601 1.2659 1.0726 -0.1967 0.1938  -0.3482 369 ARG A NH2 
2706 N N   . PHE B 155 ? 1.0482 1.0177 0.7488 -0.0131 0.1312  -0.1479 370 PHE A N   
2707 C CA  . PHE B 155 ? 1.0485 1.0542 0.7642 -0.0031 0.1046  -0.1167 370 PHE A CA  
2708 C C   . PHE B 155 ? 1.0532 1.0410 0.7918 -0.0084 0.0919  -0.1188 370 PHE A C   
2709 O O   . PHE B 155 ? 1.0101 0.9476 0.7734 -0.0030 0.1001  -0.1200 370 PHE A O   
2710 C CB  . PHE B 155 ? 0.9844 0.9814 0.7226 0.0213  0.1044  -0.0803 370 PHE A CB  
2711 C CG  . PHE B 155 ? 1.0374 1.0568 0.7541 0.0272  0.1168  -0.0728 370 PHE A CG  
2712 C CD1 . PHE B 155 ? 1.0153 1.0882 0.7009 0.0270  0.1086  -0.0633 370 PHE A CD1 
2713 C CD2 . PHE B 155 ? 1.0453 1.0394 0.7732 0.0351  0.1377  -0.0725 370 PHE A CD2 
2714 C CE1 . PHE B 155 ? 0.9573 1.0512 0.6205 0.0328  0.1215  -0.0549 370 PHE A CE1 
2715 C CE2 . PHE B 155 ? 0.9583 0.9750 0.6664 0.0400  0.1509  -0.0651 370 PHE A CE2 
2716 C CZ  . PHE B 155 ? 0.9138 0.9770 0.5883 0.0380  0.1428  -0.0568 370 PHE A CZ  
2717 N N   . VAL B 156 ? 1.0186 1.0546 0.7490 -0.0169 0.0726  -0.1164 371 VAL A N   
2718 C CA  . VAL B 156 ? 0.9949 1.0256 0.7454 -0.0218 0.0598  -0.1159 371 VAL A CA  
2719 C C   . VAL B 156 ? 0.9996 1.0530 0.7660 0.0022  0.0422  -0.0778 371 VAL A C   
2720 O O   . VAL B 156 ? 0.9652 1.0572 0.7178 0.0167  0.0374  -0.0553 371 VAL A O   
2721 C CB  . VAL B 156 ? 0.9833 1.0547 0.7131 -0.0543 0.0554  -0.1469 371 VAL A CB  
2722 C CG1 . VAL B 156 ? 1.1495 1.1947 0.8511 -0.0799 0.0782  -0.1862 371 VAL A CG1 
2723 C CG2 . VAL B 156 ? 1.0090 1.1715 0.7216 -0.0532 0.0366  -0.1328 371 VAL A CG2 
2724 N N   . TYR B 157 ? 0.9440 0.9677 0.7361 0.0079  0.0361  -0.0697 372 TYR A N   
2725 C CA  . TYR B 157 ? 0.9559 0.9868 0.7601 0.0295  0.0244  -0.0378 372 TYR A CA  
2726 C C   . TYR B 157 ? 0.9958 1.0525 0.8081 0.0215  0.0127  -0.0436 372 TYR A C   
2727 O O   . TYR B 157 ? 1.0313 1.0528 0.8596 0.0105  0.0148  -0.0580 372 TYR A O   
2728 C CB  . TYR B 157 ? 0.9263 0.8981 0.7521 0.0415  0.0299  -0.0238 372 TYR A CB  
2729 C CG  . TYR B 157 ? 0.9427 0.8950 0.7665 0.0440  0.0429  -0.0218 372 TYR A CG  
2730 C CD1 . TYR B 157 ? 0.9918 0.9598 0.8005 0.0551  0.0468  -0.0014 372 TYR A CD1 
2731 C CD2 . TYR B 157 ? 0.9523 0.8747 0.7875 0.0367  0.0546  -0.0391 372 TYR A CD2 
2732 C CE1 . TYR B 157 ? 0.9365 0.8919 0.7448 0.0553  0.0603  0.0005  372 TYR A CE1 
2733 C CE2 . TYR B 157 ? 0.9797 0.8940 0.8158 0.0410  0.0683  -0.0358 372 TYR A CE2 
2734 C CZ  . TYR B 157 ? 0.9297 0.8628 0.7529 0.0482  0.0702  -0.0172 372 TYR A CZ  
2735 O OH  . TYR B 157 ? 0.9503 0.8806 0.7757 0.0508  0.0847  -0.0133 372 TYR A OH  
2736 N N   . ARG B 158 ? 0.9440 1.0676 0.7457 0.0283  0.0019  -0.0304 373 ARG A N   
2737 C CA  . ARG B 158 ? 0.9013 1.0682 0.7117 0.0188  -0.0090 -0.0359 373 ARG A CA  
2738 C C   . ARG B 158 ? 0.9372 1.1072 0.7599 0.0509  -0.0143 -0.0008 373 ARG A C   
2739 O O   . ARG B 158 ? 0.9371 1.1475 0.7486 0.0768  -0.0162 0.0283  373 ARG A O   
2740 C CB  . ARG B 158 ? 0.8775 1.1349 0.6680 -0.0011 -0.0168 -0.0498 373 ARG A CB  
2741 C CG  . ARG B 158 ? 0.9591 1.2017 0.7357 -0.0429 -0.0076 -0.0950 373 ARG A CG  
2742 C CD  . ARG B 158 ? 0.9087 1.2453 0.6667 -0.0753 -0.0165 -0.1168 373 ARG A CD  
2743 N NE  . ARG B 158 ? 1.0924 1.3964 0.8325 -0.1204 -0.0017 -0.1649 373 ARG A NE  
2744 C CZ  . ARG B 158 ? 1.1715 1.4749 0.8795 -0.1383 0.0093  -0.1888 373 ARG A CZ  
2745 N NH1 . ARG B 158 ? 1.1218 1.4605 0.8140 -0.1154 0.0052  -0.1680 373 ARG A NH1 
2746 N NH2 . ARG B 158 ? 1.1669 1.4281 0.8551 -0.1798 0.0285  -0.2345 373 ARG A NH2 
2747 N N   . LEU B 159 ? 0.9465 1.0707 0.7892 0.0511  -0.0137 -0.0026 374 LEU A N   
2748 C CA  . LEU B 159 ? 0.8754 0.9962 0.7273 0.0780  -0.0155 0.0245  374 LEU A CA  
2749 C C   . LEU B 159 ? 0.8717 1.0392 0.7375 0.0652  -0.0237 0.0146  374 LEU A C   
2750 O O   . LEU B 159 ? 0.9092 1.0382 0.7904 0.0598  -0.0223 0.0079  374 LEU A O   
2751 C CB  . LEU B 159 ? 0.8799 0.9143 0.7401 0.0866  -0.0074 0.0304  374 LEU A CB  
2752 C CG  . LEU B 159 ? 0.9179 0.9027 0.7707 0.0879  0.0016  0.0333  374 LEU A CG  
2753 C CD1 . LEU B 159 ? 0.9628 0.9300 0.8216 0.0635  0.0040  0.0061  374 LEU A CD1 
2754 C CD2 . LEU B 159 ? 0.8659 0.7887 0.7212 0.0993  0.0088  0.0473  374 LEU A CD2 
2755 N N   . LEU B 160 ? 0.8384 1.0976 0.6983 0.0581  -0.0322 0.0137  375 LEU A N   
2756 C CA  . LEU B 160 ? 0.8236 1.1440 0.6966 0.0358  -0.0400 -0.0006 375 LEU A CA  
2757 C C   . LEU B 160 ? 0.8032 1.1770 0.6886 0.0685  -0.0439 0.0322  375 LEU A C   
2758 O O   . LEU B 160 ? 0.7031 1.1114 0.5796 0.1060  -0.0430 0.0662  375 LEU A O   
2759 C CB  . LEU B 160 ? 0.7748 1.1785 0.6342 0.0011  -0.0471 -0.0247 375 LEU A CB  
2760 C CG  . LEU B 160 ? 0.8183 1.1815 0.6566 -0.0247 -0.0396 -0.0537 375 LEU A CG  
2761 C CD1 . LEU B 160 ? 0.7312 1.1958 0.5478 -0.0488 -0.0479 -0.0677 375 LEU A CD1 
2762 C CD2 . LEU B 160 ? 0.8686 1.1521 0.7124 -0.0574 -0.0275 -0.0884 375 LEU A CD2 
2763 N N   . ARG B 161 ? 0.8264 1.2023 0.7313 0.0562  -0.0447 0.0235  376 ARG A N   
2764 C CA  . ARG B 161 ? 0.7925 1.2319 0.7130 0.0808  -0.0470 0.0489  376 ARG A CA  
2765 C C   . ARG B 161 ? 0.8121 1.2080 0.7268 0.1356  -0.0362 0.0883  376 ARG A C   
2766 O O   . ARG B 161 ? 0.7647 1.2269 0.6796 0.1727  -0.0345 0.1219  376 ARG A O   
2767 C CB  . ARG B 161 ? 0.7845 1.3631 0.7074 0.0718  -0.0593 0.0532  376 ARG A CB  
2768 C CG  . ARG B 161 ? 0.7827 1.4047 0.7062 0.0087  -0.0665 0.0088  376 ARG A CG  
2769 C CD  . ARG B 161 ? 0.8225 1.6006 0.7531 -0.0025 -0.0801 0.0150  376 ARG A CD  
2770 N NE  . ARG B 161 ? 0.8375 1.6716 0.7894 0.0436  -0.0801 0.0564  376 ARG A NE  
2771 C CZ  . ARG B 161 ? 0.8524 1.7880 0.8280 0.0301  -0.0861 0.0581  376 ARG A CZ  
2772 N NH1 . ARG B 161 ? 0.8954 1.9002 0.8748 -0.0329 -0.0943 0.0204  376 ARG A NH1 
2773 N NH2 . ARG B 161 ? 0.7698 1.7365 0.7644 0.0794  -0.0809 0.0976  376 ARG A NH2 
2774 N N   . SER B 162 ? 0.7850 1.0696 0.6929 0.1405  -0.0262 0.0845  377 SER A N   
2775 C CA  . SER B 162 ? 0.7959 1.0220 0.6942 0.1825  -0.0114 0.1137  377 SER A CA  
2776 C C   . SER B 162 ? 0.8455 1.0844 0.7584 0.1955  -0.0072 0.1217  377 SER A C   
2777 O O   . SER B 162 ? 0.8052 1.0384 0.7335 0.1656  -0.0129 0.0978  377 SER A O   
2778 C CB  . SER B 162 ? 0.8662 0.9811 0.7537 0.1733  -0.0035 0.1016  377 SER A CB  
2779 O OG  . SER B 162 ? 0.9460 1.0529 0.8292 0.1468  -0.0097 0.0818  377 SER A OG  
2780 N N   . PRO B 163 ? 0.8680 1.1222 0.7752 0.2414  0.0058  0.1562  378 PRO A N   
2781 C CA  . PRO B 163 ? 0.8182 1.0741 0.7369 0.2567  0.0139  0.1636  378 PRO A CA  
2782 C C   . PRO B 163 ? 0.8672 1.0120 0.7776 0.2425  0.0217  0.1444  378 PRO A C   
2783 O O   . PRO B 163 ? 0.8432 0.9006 0.7304 0.2537  0.0348  0.1485  378 PRO A O   
2784 C CB  . PRO B 163 ? 0.8212 1.0944 0.7271 0.3163  0.0335  0.2077  378 PRO A CB  
2785 C CG  . PRO B 163 ? 0.8637 1.1997 0.7621 0.3268  0.0271  0.2247  378 PRO A CG  
2786 C CD  . PRO B 163 ? 0.8444 1.1199 0.7336 0.2847  0.0169  0.1929  378 PRO A CD  
2787 N N   . MET B 164 ? 0.9044 1.0579 0.8331 0.2134  0.0136  0.1225  379 MET A N   
2788 C CA  . MET B 164 ? 0.9130 0.9825 0.8355 0.2034  0.0202  0.1086  379 MET A CA  
2789 C C   . MET B 164 ? 0.9726 1.0068 0.8793 0.2430  0.0412  0.1302  379 MET A C   
2790 O O   . MET B 164 ? 0.9469 1.0423 0.8607 0.2745  0.0490  0.1537  379 MET A O   
2791 C CB  . MET B 164 ? 0.8476 0.9452 0.7921 0.1692  0.0103  0.0872  379 MET A CB  
2792 C CG  . MET B 164 ? 0.9761 1.0091 0.9149 0.1662  0.0179  0.0801  379 MET A CG  
2793 S SD  . MET B 164 ? 0.9110 0.9580 0.8705 0.1273  0.0113  0.0586  379 MET A SD  
2794 C CE  . MET B 164 ? 0.8655 1.0158 0.8485 0.1034  0.0013  0.0518  379 MET A CE  
2795 N N   . CYS B 165 ? 1.0595 0.9974 0.9426 0.2418  0.0525  0.1226  380 CYS A N   
2796 C CA  . CYS B 165 ? 1.1322 1.0164 0.9884 0.2785  0.0789  0.1406  380 CYS A CA  
2797 C C   . CYS B 165 ? 1.1593 1.0602 1.0216 0.2911  0.0877  0.1434  380 CYS A C   
2798 O O   . CYS B 165 ? 1.0900 1.0128 0.9707 0.2631  0.0742  0.1258  380 CYS A O   
2799 C CB  . CYS B 165 ? 1.2055 0.9834 1.0299 0.2651  0.0898  0.1268  380 CYS A CB  
2800 S SG  . CYS B 165 ? 1.2523 0.9929 1.0786 0.2232  0.0773  0.0951  380 CYS A SG  
2801 N N   . GLU B 166 ? 1.2172 1.0999 1.0604 0.3360  0.1148  0.1676  381 GLU A N   
2802 C CA  . GLU B 166 ? 1.2115 1.1186 1.0600 0.3573  0.1280  0.1759  381 GLU A CA  
2803 C C   . GLU B 166 ? 1.2357 1.0870 1.0739 0.3274  0.1267  0.1488  381 GLU A C   
2804 O O   . GLU B 166 ? 1.2206 1.1111 1.0734 0.3291  0.1277  0.1489  381 GLU A O   
2805 C CB  . GLU B 166 ? 1.3386 1.2075 1.1584 0.4140  0.1653  0.2055  381 GLU A CB  
2806 C CG  . GLU B 166 ? 1.4020 1.3425 1.2321 0.4594  0.1726  0.2443  381 GLU A CG  
2807 C CD  . GLU B 166 ? 1.4283 1.3506 1.2485 0.4527  0.1652  0.2483  381 GLU A CD  
2808 O OE1 . GLU B 166 ? 1.5010 1.4583 1.3167 0.4980  0.1796  0.2847  381 GLU A OE1 
2809 O OE2 . GLU B 166 ? 1.4283 1.3065 1.2450 0.4063  0.1469  0.2186  381 GLU A OE2 
2810 N N   . TYR B 167 ? 1.1916 0.9572 1.0036 0.3012  0.1259  0.1276  382 TYR A N   
2811 C CA  . TYR B 167 ? 1.1238 0.8505 0.9259 0.2715  0.1212  0.1036  382 TYR A CA  
2812 C C   . TYR B 167 ? 1.1180 0.9123 0.9581 0.2421  0.0949  0.0940  382 TYR A C   
2813 O O   . TYR B 167 ? 1.1411 0.9594 0.9898 0.2404  0.0967  0.0925  382 TYR A O   
2814 C CB  . TYR B 167 ? 1.1743 0.8191 0.9464 0.2445  0.1209  0.0839  382 TYR A CB  
2815 C CG  . TYR B 167 ? 1.2389 0.8507 0.9959 0.2149  0.1160  0.0613  382 TYR A CG  
2816 C CD1 . TYR B 167 ? 1.2289 0.8856 1.0139 0.1890  0.0920  0.0525  382 TYR A CD1 
2817 C CD2 . TYR B 167 ? 1.2767 0.8123 0.9877 0.2135  0.1383  0.0495  382 TYR A CD2 
2818 C CE1 . TYR B 167 ? 1.2416 0.8775 1.0122 0.1670  0.0879  0.0375  382 TYR A CE1 
2819 C CE2 . TYR B 167 ? 1.2463 0.7647 0.9410 0.1854  0.1322  0.0293  382 TYR A CE2 
2820 C CZ  . TYR B 167 ? 1.2600 0.8337 0.9863 0.1646  0.1056  0.0260  382 TYR A CZ  
2821 O OH  . TYR B 167 ? 1.2046 0.7718 0.9159 0.1410  0.0987  0.0118  382 TYR A OH  
2822 N N   . LEU B 168 ? 1.1082 0.9291 0.9688 0.2188  0.0741  0.0873  383 LEU A N   
2823 C CA  . LEU B 168 ? 1.0246 0.8930 0.9151 0.1888  0.0554  0.0762  383 LEU A CA  
2824 C C   . LEU B 168 ? 0.9533 0.9027 0.8702 0.1970  0.0565  0.0869  383 LEU A C   
2825 O O   . LEU B 168 ? 0.9223 0.8914 0.8532 0.1777  0.0532  0.0795  383 LEU A O   
2826 C CB  . LEU B 168 ? 1.0537 0.9338 0.9572 0.1668  0.0389  0.0676  383 LEU A CB  
2827 C CG  . LEU B 168 ? 1.0657 0.8867 0.9568 0.1452  0.0323  0.0530  383 LEU A CG  
2828 C CD1 . LEU B 168 ? 1.0696 0.8701 0.9579 0.1311  0.0318  0.0447  383 LEU A CD1 
2829 C CD2 . LEU B 168 ? 1.1244 0.8888 0.9869 0.1561  0.0418  0.0554  383 LEU A CD2 
2830 N N   . VAL B 169 ? 0.9380 0.9406 0.8623 0.2253  0.0622  0.1064  384 VAL A N   
2831 C CA  . VAL B 169 ? 0.9028 1.0011 0.8556 0.2320  0.0624  0.1183  384 VAL A CA  
2832 C C   . VAL B 169 ? 0.9557 1.0439 0.9034 0.2471  0.0791  0.1235  384 VAL A C   
2833 O O   . VAL B 169 ? 0.8852 1.0216 0.8551 0.2271  0.0755  0.1187  384 VAL A O   
2834 C CB  . VAL B 169 ? 0.8954 1.0622 0.8554 0.2667  0.0661  0.1441  384 VAL A CB  
2835 C CG1 . VAL B 169 ? 0.8098 1.1030 0.8064 0.2595  0.0580  0.1521  384 VAL A CG1 
2836 C CG2 . VAL B 169 ? 0.9507 1.1006 0.9025 0.2577  0.0548  0.1398  384 VAL A CG2 
2837 N N   . ASN B 170 ? 0.9860 1.0073 0.9012 0.2804  0.1005  0.1322  385 ASN A N   
2838 C CA  . ASN B 170 ? 0.9645 0.9654 0.8667 0.2955  0.1196  0.1346  385 ASN A CA  
2839 C C   . ASN B 170 ? 0.9745 0.9480 0.8763 0.2560  0.1090  0.1124  385 ASN A C   
2840 O O   . ASN B 170 ? 0.9560 0.9729 0.8747 0.2488  0.1114  0.1140  385 ASN A O   
2841 C CB  . ASN B 170 ? 1.0736 0.9820 0.9297 0.3279  0.1465  0.1388  385 ASN A CB  
2842 C CG  . ASN B 170 ? 1.2452 1.1734 1.0971 0.3791  0.1672  0.1686  385 ASN A CG  
2843 O OD1 . ASN B 170 ? 1.2077 1.2359 1.0940 0.3940  0.1594  0.1891  385 ASN A OD1 
2844 N ND2 . ASN B 170 ? 1.3355 1.1681 1.1423 0.4054  0.1957  0.1716  385 ASN A ND2 
2845 N N   . PHE B 171 ? 0.9643 0.8694 0.8466 0.2318  0.0988  0.0945  386 PHE A N   
2846 C CA  . PHE B 171 ? 0.9478 0.8303 0.8291 0.1984  0.0882  0.0785  386 PHE A CA  
2847 C C   . PHE B 171 ? 0.9543 0.8996 0.8731 0.1717  0.0754  0.0768  386 PHE A C   
2848 O O   . PHE B 171 ? 0.9809 0.9217 0.9017 0.1538  0.0758  0.0722  386 PHE A O   
2849 C CB  . PHE B 171 ? 0.9544 0.7751 0.8162 0.1800  0.0775  0.0643  386 PHE A CB  
2850 C CG  . PHE B 171 ? 0.9554 0.7608 0.8180 0.1509  0.0659  0.0534  386 PHE A CG  
2851 C CD1 . PHE B 171 ? 0.9681 0.7357 0.8019 0.1477  0.0717  0.0475  386 PHE A CD1 
2852 C CD2 . PHE B 171 ? 0.9479 0.7746 0.8361 0.1281  0.0514  0.0497  386 PHE A CD2 
2853 C CE1 . PHE B 171 ? 0.9298 0.6916 0.7638 0.1262  0.0613  0.0432  386 PHE A CE1 
2854 C CE2 . PHE B 171 ? 0.9028 0.7114 0.7900 0.1088  0.0451  0.0452  386 PHE A CE2 
2855 C CZ  . PHE B 171 ? 0.9125 0.6934 0.7740 0.1098  0.0491  0.0443  386 PHE A CZ  
2856 N N   . LEU B 172 ? 0.9461 0.9475 0.8909 0.1660  0.0661  0.0796  387 LEU A N   
2857 C CA  . LEU B 172 ? 0.8385 0.8965 0.8140 0.1340  0.0581  0.0734  387 LEU A CA  
2858 C C   . LEU B 172 ? 0.8350 0.9633 0.8302 0.1394  0.0687  0.0844  387 LEU A C   
2859 O O   . LEU B 172 ? 0.8558 1.0053 0.8665 0.1099  0.0699  0.0780  387 LEU A O   
2860 C CB  . LEU B 172 ? 0.7778 0.8782 0.7694 0.1214  0.0454  0.0690  387 LEU A CB  
2861 C CG  . LEU B 172 ? 0.8631 0.9167 0.8487 0.0972  0.0341  0.0527  387 LEU A CG  
2862 C CD1 . LEU B 172 ? 0.7450 0.8561 0.7490 0.0726  0.0250  0.0432  387 LEU A CD1 
2863 C CD2 . LEU B 172 ? 0.8349 0.8329 0.8144 0.0754  0.0363  0.0426  387 LEU A CD2 
2864 N N   . HIS B 173 ? 0.7777 0.9445 0.7731 0.1775  0.0792  0.1028  388 HIS A N   
2865 C CA  . HIS B 173 ? 0.8511 1.0923 0.8673 0.1864  0.0911  0.1159  388 HIS A CA  
2866 C C   . HIS B 173 ? 0.9290 1.1204 0.9275 0.1864  0.1046  0.1133  388 HIS A C   
2867 O O   . HIS B 173 ? 0.8651 1.1038 0.8825 0.1711  0.1110  0.1158  388 HIS A O   
2868 C CB  . HIS B 173 ? 0.8176 1.1113 0.8368 0.2364  0.1034  0.1414  388 HIS A CB  
2869 C CG  . HIS B 173 ? 0.8440 1.2652 0.9020 0.2320  0.0949  0.1531  388 HIS A CG  
2870 N N   . LYS B 174 ? 0.9389 1.0383 0.8993 0.2000  0.1094  0.1077  389 LYS A N   
2871 C CA  . LYS B 174 ? 0.9182 0.9716 0.8552 0.1987  0.1207  0.1038  389 LYS A CA  
2872 C C   . LYS B 174 ? 0.9261 0.9614 0.8692 0.1578  0.1097  0.0922  389 LYS A C   
2873 O O   . LYS B 174 ? 0.9554 1.0049 0.9027 0.1469  0.1184  0.0954  389 LYS A O   
2874 C CB  . LYS B 174 ? 0.9614 0.9289 0.8522 0.2203  0.1295  0.0983  389 LYS A CB  
2875 C CG  . LYS B 174 ? 0.9543 0.9209 0.8309 0.2663  0.1506  0.1123  389 LYS A CG  
2876 C CD  . LYS B 174 ? 0.9997 0.8684 0.8271 0.2781  0.1608  0.1018  389 LYS A CD  
2877 C CE  . LYS B 174 ? 1.0764 0.9261 0.8822 0.3273  0.1914  0.1173  389 LYS A CE  
2878 N NZ  . LYS B 174 ? 1.1369 1.0332 0.9672 0.3521  0.1896  0.1377  389 LYS A NZ  
2879 N N   . LEU B 175 ? 0.9116 0.9155 0.8551 0.1374  0.0936  0.0813  390 LEU A N   
2880 C CA  . LEU B 175 ? 0.8886 0.8682 0.8360 0.1052  0.0876  0.0739  390 LEU A CA  
2881 C C   . LEU B 175 ? 0.9092 0.9436 0.8884 0.0776  0.0920  0.0744  390 LEU A C   
2882 O O   . LEU B 175 ? 0.9065 0.9233 0.8854 0.0574  0.0995  0.0750  390 LEU A O   
2883 C CB  . LEU B 175 ? 0.9141 0.8556 0.8579 0.0940  0.0727  0.0639  390 LEU A CB  
2884 C CG  . LEU B 175 ? 0.8838 0.7820 0.8220 0.0736  0.0694  0.0602  390 LEU A CG  
2885 C CD1 . LEU B 175 ? 0.8530 0.7135 0.7618 0.0844  0.0725  0.0654  390 LEU A CD1 
2886 C CD2 . LEU B 175 ? 0.8429 0.7179 0.7833 0.0666  0.0570  0.0516  390 LEU A CD2 
2887 N N   . ARG B 176 ? 0.9455 1.0480 0.9505 0.0740  0.0887  0.0743  391 ARG A N   
2888 C CA  . ARG B 176 ? 0.9448 1.1039 0.9787 0.0369  0.0921  0.0689  391 ARG A CA  
2889 C C   . ARG B 176 ? 0.9423 1.1218 0.9818 0.0300  0.1090  0.0776  391 ARG A C   
2890 O O   . ARG B 176 ? 0.9435 1.1118 0.9895 -0.0056 0.1178  0.0719  391 ARG A O   
2891 C CB  . ARG B 176 ? 0.9268 1.1783 0.9862 0.0376  0.0848  0.0702  391 ARG A CB  
2892 C CG  . ARG B 176 ? 0.9438 1.2503 1.0277 -0.0128 0.0827  0.0546  391 ARG A CG  
2893 C CD  . ARG B 176 ? 0.9125 1.3465 1.0267 -0.0123 0.0801  0.0629  391 ARG A CD  
2894 N NE  . ARG B 176 ? 0.9636 1.4252 1.0742 0.0390  0.0731  0.0810  391 ARG A NE  
2895 C CZ  . ARG B 176 ? 0.9966 1.5583 1.1267 0.0474  0.0643  0.0894  391 ARG A CZ  
2896 N NH1 . ARG B 176 ? 0.9879 1.6440 1.1437 0.0030  0.0583  0.0778  391 ARG A NH1 
2897 N NH2 . ARG B 176 ? 0.9489 1.5163 1.0698 0.1002  0.0630  0.1101  391 ARG A NH2 
2898 N N   . GLN B 177 ? 1.0909 1.2900 1.1236 0.0650  0.1175  0.0918  392 GLN A N   
2899 C CA  . GLN B 177 ? 1.0690 1.3123 1.1123 0.0639  0.1348  0.1026  392 GLN A CA  
2900 C C   . GLN B 177 ? 1.0925 1.2692 1.1085 0.0634  0.1462  0.1060  392 GLN A C   
2901 O O   . GLN B 177 ? 1.1100 1.3190 1.1334 0.0581  0.1624  0.1151  392 GLN A O   
2902 C CB  . GLN B 177 ? 1.0764 1.3778 1.1248 0.1073  0.1425  0.1184  392 GLN A CB  
2903 C CG  . GLN B 177 ? 1.1241 1.3537 1.1322 0.1502  0.1484  0.1223  392 GLN A CG  
2904 C CD  . GLN B 177 ? 1.1265 1.3950 1.1360 0.1970  0.1568  0.1368  392 GLN A CD  
2905 O OE1 . GLN B 177 ? 1.1314 1.3449 1.1063 0.2327  0.1703  0.1403  392 GLN A OE1 
2906 N NE2 . GLN B 177 ? 1.0695 1.4336 1.1162 0.1969  0.1511  0.1459  392 GLN A NE2 
2907 N N   . LEU B 178 ? 0.8891 0.9837 0.8745 0.0686  0.1384  0.1008  393 LEU A N   
2908 C CA  . LEU B 178 ? 0.8838 0.9273 0.8448 0.0641  0.1472  0.1063  393 LEU A CA  
2909 C C   . LEU B 178 ? 0.8977 0.9532 0.8778 0.0272  0.1602  0.1095  393 LEU A C   
2910 O O   . LEU B 178 ? 0.8976 0.9637 0.8995 -0.0026 0.1573  0.0995  393 LEU A O   
2911 C CB  . LEU B 178 ? 0.8576 0.8301 0.7919 0.0676  0.1341  0.1011  393 LEU A CB  
2912 C CG  . LEU B 178 ? 0.8220 0.7699 0.7339 0.0936  0.1225  0.0943  393 LEU A CG  
2913 C CD1 . LEU B 178 ? 0.8343 0.7258 0.7160 0.0939  0.1142  0.0930  393 LEU A CD1 
2914 C CD2 . LEU B 178 ? 0.9341 0.9001 0.8313 0.1212  0.1350  0.0984  393 LEU A CD2 
2915 N N   . PRO B 179 ? 0.8902 0.9396 0.8591 0.0260  0.1774  0.1221  394 PRO A N   
2916 C CA  . PRO B 179 ? 0.8725 0.9357 0.8599 -0.0110 0.1959  0.1263  394 PRO A CA  
2917 C C   . PRO B 179 ? 0.8691 0.8603 0.8443 -0.0322 0.2024  0.1279  394 PRO A C   
2918 O O   . PRO B 179 ? 0.8779 0.8670 0.8658 -0.0673 0.2221  0.1289  394 PRO A O   
2919 C CB  . PRO B 179 ? 0.8380 0.9240 0.8154 0.0017  0.2145  0.1425  394 PRO A CB  
2920 C CG  . PRO B 179 ? 0.8894 0.9675 0.8390 0.0451  0.2062  0.1439  394 PRO A CG  
2921 C CD  . PRO B 179 ? 0.9014 0.9358 0.8382 0.0560  0.1840  0.1320  394 PRO A CD  
2922 N N   . GLU B 180 ? 0.8827 0.8158 0.8336 -0.0126 0.1898  0.1296  395 GLU A N   
2923 C CA  . GLU B 180 ? 0.9377 0.8050 0.8762 -0.0231 0.1997  0.1378  395 GLU A CA  
2924 C C   . GLU B 180 ? 1.0032 0.8346 0.9372 -0.0142 0.1814  0.1285  395 GLU A C   
2925 O O   . GLU B 180 ? 0.9160 0.7557 0.8405 0.0097  0.1602  0.1234  395 GLU A O   
2926 C CB  . GLU B 180 ? 0.9728 0.8111 0.8810 -0.0030 0.2102  0.1622  395 GLU A CB  
2927 C CG  . GLU B 180 ? 0.9911 0.8610 0.9000 -0.0101 0.2311  0.1741  395 GLU A CG  
2928 C CD  . GLU B 180 ? 0.9615 0.8085 0.8814 -0.0449 0.2611  0.1819  395 GLU A CD  
2929 O OE1 . GLU B 180 ? 0.9536 0.7772 0.8894 -0.0727 0.2660  0.1681  395 GLU A OE1 
2930 O OE2 . GLU B 180 ? 1.0735 0.9221 0.9827 -0.0462 0.2827  0.2010  395 GLU A OE2 
2931 N N   . ARG B 181 ? 1.3016 1.0877 1.2397 -0.0344 0.1939  0.1265  396 ARG A N   
2932 C CA  . ARG B 181 ? 1.2915 1.0432 1.2265 -0.0258 0.1809  0.1192  396 ARG A CA  
2933 C C   . ARG B 181 ? 1.2618 0.9964 1.1735 0.0100  0.1670  0.1357  396 ARG A C   
2934 O O   . ARG B 181 ? 1.2467 0.9877 1.1569 0.0237  0.1449  0.1265  396 ARG A O   
2935 C CB  . ARG B 181 ? 1.3447 1.0383 1.2808 -0.0495 0.2053  0.1176  396 ARG A CB  
2936 C CG  . ARG B 181 ? 1.3396 1.0367 1.2919 -0.0769 0.2012  0.0890  396 ARG A CG  
2937 C CD  . ARG B 181 ? 1.3570 1.1281 1.3317 -0.1037 0.1937  0.0696  396 ARG A CD  
2938 N NE  . ARG B 181 ? 1.3882 1.1795 1.3749 -0.1223 0.1815  0.0442  396 ARG A NE  
2939 C CZ  . ARG B 181 ? 1.3732 1.2395 1.3804 -0.1444 0.1719  0.0274  396 ARG A CZ  
2940 N NH1 . ARG B 181 ? 1.3506 1.2802 1.3723 -0.1521 0.1750  0.0329  396 ARG A NH1 
2941 N NH2 . ARG B 181 ? 1.3504 1.2357 1.3636 -0.1574 0.1595  0.0067  396 ARG A NH2 
2942 N N   . TYR B 182 ? 1.0426 0.7613 0.9348 0.0234  0.1799  0.1606  397 TYR A N   
2943 C CA  . TYR B 182 ? 0.9870 0.7046 0.8557 0.0535  0.1654  0.1764  397 TYR A CA  
2944 C C   . TYR B 182 ? 0.9612 0.7189 0.8194 0.0647  0.1418  0.1626  397 TYR A C   
2945 O O   . TYR B 182 ? 0.9412 0.7029 0.7829 0.0803  0.1242  0.1637  397 TYR A O   
2946 C CB  . TYR B 182 ? 0.9941 0.6966 0.8410 0.0668  0.1846  0.2088  397 TYR A CB  
2947 C CG  . TYR B 182 ? 1.0158 0.7497 0.8488 0.0676  0.1901  0.2146  397 TYR A CG  
2948 C CD1 . TYR B 182 ? 0.9792 0.7445 0.7858 0.0864  0.1729  0.2163  397 TYR A CD1 
2949 C CD2 . TYR B 182 ? 0.9578 0.6909 0.8021 0.0466  0.2144  0.2164  397 TYR A CD2 
2950 C CE1 . TYR B 182 ? 0.9875 0.7781 0.7779 0.0882  0.1808  0.2197  397 TYR A CE1 
2951 C CE2 . TYR B 182 ? 0.9861 0.7510 0.8190 0.0490  0.2214  0.2226  397 TYR A CE2 
2952 C CZ  . TYR B 182 ? 1.0712 0.8629 0.8760 0.0721  0.2052  0.2247  397 TYR A CZ  
2953 O OH  . TYR B 182 ? 1.0475 0.8682 0.8363 0.0761  0.2156  0.2300  397 TYR A OH  
2954 N N   . MET B 183 ? 0.9171 0.7048 0.7836 0.0568  0.1433  0.1495  398 MET A N   
2955 C CA  . MET B 183 ? 0.9199 0.7297 0.7707 0.0713  0.1271  0.1372  398 MET A CA  
2956 C C   . MET B 183 ? 0.8955 0.7048 0.7587 0.0708  0.1096  0.1179  398 MET A C   
2957 O O   . MET B 183 ? 0.8174 0.6227 0.6609 0.0822  0.0957  0.1103  398 MET A O   
2958 C CB  . MET B 183 ? 0.9080 0.7500 0.7582 0.0733  0.1381  0.1345  398 MET A CB  
2959 C CG  . MET B 183 ? 0.8968 0.7425 0.7283 0.0762  0.1556  0.1536  398 MET A CG  
2960 S SD  . MET B 183 ? 0.8915 0.7829 0.7382 0.0728  0.1743  0.1522  398 MET A SD  
2961 C CE  . MET B 183 ? 1.0145 0.9042 0.8230 0.0844  0.1901  0.1722  398 MET A CE  
2962 N N   . MET B 184 ? 0.9737 0.7862 0.8659 0.0550  0.1114  0.1092  399 MET A N   
2963 C CA  . MET B 184 ? 0.8647 0.6757 0.7661 0.0556  0.0954  0.0941  399 MET A CA  
2964 C C   . MET B 184 ? 0.8092 0.5903 0.6986 0.0628  0.0847  0.0979  399 MET A C   
2965 O O   . MET B 184 ? 0.8410 0.6212 0.7227 0.0702  0.0697  0.0887  399 MET A O   
2966 C CB  . MET B 184 ? 0.7754 0.6006 0.7058 0.0342  0.0994  0.0833  399 MET A CB  
2967 C CG  . MET B 184 ? 0.8179 0.6885 0.7647 0.0229  0.1106  0.0823  399 MET A CG  
2968 S SD  . MET B 184 ? 0.8173 0.7085 0.7931 -0.0173 0.1220  0.0701  399 MET A SD  
2969 C CE  . MET B 184 ? 0.8199 0.8027 0.8196 -0.0192 0.1195  0.0659  399 MET A CE  
2970 N N   . ASN B 185 ? 0.8196 0.5786 0.7059 0.0626  0.0944  0.1143  400 ASN A N   
2971 C CA  . ASN B 185 ? 0.8893 0.6340 0.7681 0.0739  0.0847  0.1221  400 ASN A CA  
2972 C C   . ASN B 185 ? 0.8813 0.6447 0.7331 0.0865  0.0701  0.1253  400 ASN A C   
2973 O O   . ASN B 185 ? 0.8885 0.6571 0.7358 0.0903  0.0552  0.1219  400 ASN A O   
2974 C CB  . ASN B 185 ? 0.9233 0.6392 0.8046 0.0775  0.1031  0.1439  400 ASN A CB  
2975 C CG  . ASN B 185 ? 0.9038 0.5888 0.8057 0.0608  0.1178  0.1338  400 ASN A CG  
2976 O OD1 . ASN B 185 ? 0.8792 0.5755 0.7948 0.0459  0.1100  0.1110  400 ASN A OD1 
2977 N ND2 . ASN B 185 ? 0.9683 0.6131 0.8687 0.0635  0.1413  0.1511  400 ASN A ND2 
2978 N N   . SER B 186 ? 0.9377 0.7138 0.7697 0.0896  0.0754  0.1298  401 SER A N   
2979 C CA  . SER B 186 ? 0.9223 0.7149 0.7217 0.0951  0.0639  0.1264  401 SER A CA  
2980 C C   . SER B 186 ? 0.9138 0.7024 0.7066 0.0905  0.0530  0.1010  401 SER A C   
2981 O O   . SER B 186 ? 0.9122 0.7050 0.6862 0.0873  0.0399  0.0929  401 SER A O   
2982 C CB  . SER B 186 ? 0.8844 0.6875 0.6611 0.0988  0.0760  0.1340  401 SER A CB  
2983 O OG  . SER B 186 ? 0.9278 0.7428 0.6892 0.1070  0.0792  0.1594  401 SER A OG  
2984 N N   . VAL B 187 ? 0.8854 0.6689 0.6925 0.0899  0.0603  0.0899  402 VAL A N   
2985 C CA  . VAL B 187 ? 0.8815 0.6554 0.6822 0.0913  0.0553  0.0712  402 VAL A CA  
2986 C C   . VAL B 187 ? 0.9354 0.7015 0.7501 0.0855  0.0418  0.0658  402 VAL A C   
2987 O O   . VAL B 187 ? 0.9355 0.6904 0.7320 0.0823  0.0341  0.0540  402 VAL A O   
2988 C CB  . VAL B 187 ? 0.8676 0.6518 0.6865 0.0974  0.0666  0.0681  402 VAL A CB  
2989 C CG1 . VAL B 187 ? 0.8897 0.6603 0.6990 0.1062  0.0661  0.0549  402 VAL A CG1 
2990 C CG2 . VAL B 187 ? 0.9135 0.7123 0.7231 0.1036  0.0822  0.0757  402 VAL A CG2 
2991 N N   . LEU B 188 ? 0.9372 0.7059 0.7818 0.0817  0.0416  0.0733  403 LEU A N   
2992 C CA  . LEU B 188 ? 0.8854 0.6476 0.7458 0.0777  0.0322  0.0674  403 LEU A CA  
2993 C C   . LEU B 188 ? 0.9133 0.6784 0.7650 0.0777  0.0215  0.0733  403 LEU A C   
2994 O O   . LEU B 188 ? 0.9239 0.6872 0.7790 0.0739  0.0123  0.0651  403 LEU A O   
2995 C CB  . LEU B 188 ? 0.8498 0.6102 0.7389 0.0715  0.0396  0.0700  403 LEU A CB  
2996 C CG  . LEU B 188 ? 0.8331 0.6092 0.7364 0.0666  0.0448  0.0606  403 LEU A CG  
2997 C CD1 . LEU B 188 ? 0.8530 0.6296 0.7785 0.0511  0.0544  0.0596  403 LEU A CD1 
2998 C CD2 . LEU B 188 ? 0.8041 0.5842 0.7073 0.0710  0.0358  0.0496  403 LEU A CD2 
2999 N N   . GLU B 189 ? 0.9577 0.7347 0.7984 0.0824  0.0231  0.0895  404 GLU A N   
3000 C CA  . GLU B 189 ? 0.9452 0.7453 0.7755 0.0837  0.0114  0.0983  404 GLU A CA  
3001 C C   . GLU B 189 ? 0.9755 0.7807 0.7896 0.0707  -0.0017 0.0783  404 GLU A C   
3002 O O   . GLU B 189 ? 1.0118 0.8390 0.8311 0.0669  -0.0124 0.0812  404 GLU A O   
3003 C CB  . GLU B 189 ? 0.9911 0.8137 0.7990 0.0898  0.0137  0.1152  404 GLU A CB  
3004 C CG  . GLU B 189 ? 1.0597 0.8932 0.8798 0.1067  0.0216  0.1471  404 GLU A CG  
3005 C CD  . GLU B 189 ? 1.1119 0.9540 0.9125 0.1153  0.0325  0.1666  404 GLU A CD  
3006 O OE1 . GLU B 189 ? 1.1232 0.9911 0.8933 0.1096  0.0245  0.1607  404 GLU A OE1 
3007 O OE2 . GLU B 189 ? 1.1486 0.9700 0.9609 0.1265  0.0513  0.1880  404 GLU A OE2 
3008 N N   . ASN B 190 ? 0.9948 0.7786 0.7890 0.0641  0.0023  0.0591  405 ASN A N   
3009 C CA  . ASN B 190 ? 1.0256 0.7994 0.7962 0.0491  -0.0031 0.0390  405 ASN A CA  
3010 C C   . ASN B 190 ? 1.0353 0.7830 0.8204 0.0487  -0.0012 0.0285  405 ASN A C   
3011 O O   . ASN B 190 ? 1.0975 0.8326 0.8666 0.0349  -0.0037 0.0145  405 ASN A O   
3012 C CB  . ASN B 190 ? 1.0292 0.7828 0.7594 0.0443  0.0070  0.0244  405 ASN A CB  
3013 C CG  . ASN B 190 ? 1.0388 0.8153 0.7544 0.0492  0.0094  0.0361  405 ASN A CG  
3014 O OD1 . ASN B 190 ? 1.0845 0.8937 0.7811 0.0392  -0.0001 0.0394  405 ASN A OD1 
3015 N ND2 . ASN B 190 ? 1.0287 0.7957 0.7533 0.0642  0.0224  0.0441  405 ASN A ND2 
3016 N N   . PHE B 191 ? 0.9358 0.6774 0.7482 0.0608  0.0042  0.0346  406 PHE A N   
3017 C CA  . PHE B 191 ? 0.9405 0.6656 0.7642 0.0633  0.0065  0.0272  406 PHE A CA  
3018 C C   . PHE B 191 ? 0.9551 0.6927 0.8063 0.0605  -0.0018 0.0320  406 PHE A C   
3019 O O   . PHE B 191 ? 0.9725 0.7216 0.8448 0.0647  -0.0007 0.0423  406 PHE A O   
3020 C CB  . PHE B 191 ? 0.9108 0.6358 0.7447 0.0762  0.0172  0.0299  406 PHE A CB  
3021 C CG  . PHE B 191 ? 0.9770 0.7077 0.8337 0.0803  0.0168  0.0293  406 PHE A CG  
3022 C CD1 . PHE B 191 ? 0.9442 0.6922 0.8288 0.0752  0.0134  0.0330  406 PHE A CD1 
3023 C CD2 . PHE B 191 ? 1.0155 0.7325 0.8616 0.0896  0.0227  0.0255  406 PHE A CD2 
3024 C CE1 . PHE B 191 ? 0.8546 0.6138 0.7553 0.0753  0.0125  0.0296  406 PHE A CE1 
3025 C CE2 . PHE B 191 ? 0.9747 0.7069 0.8394 0.0947  0.0213  0.0276  406 PHE A CE2 
3026 C CZ  . PHE B 191 ? 0.9176 0.6751 0.8094 0.0855  0.0145  0.0281  406 PHE A CZ  
3027 N N   . THR B 192 ? 0.9631 0.6936 0.8116 0.0531  -0.0063 0.0245  407 THR A N   
3028 C CA  . THR B 192 ? 0.9459 0.6890 0.8179 0.0515  -0.0121 0.0284  407 THR A CA  
3029 C C   . THR B 192 ? 0.9017 0.6291 0.7731 0.0494  -0.0104 0.0202  407 THR A C   
3030 O O   . THR B 192 ? 0.9202 0.6238 0.7690 0.0474  -0.0046 0.0128  407 THR A O   
3031 C CB  . THR B 192 ? 0.9750 0.7448 0.8474 0.0434  -0.0213 0.0341  407 THR A CB  
3032 O OG1 . THR B 192 ? 0.9525 0.7182 0.8000 0.0256  -0.0245 0.0217  407 THR A OG1 
3033 C CG2 . THR B 192 ? 1.0279 0.8191 0.8992 0.0502  -0.0222 0.0481  407 THR A CG2 
3034 N N   . ILE B 193 ? 0.8502 0.5869 0.7433 0.0510  -0.0123 0.0225  408 ILE A N   
3035 C CA  . ILE B 193 ? 0.8630 0.5904 0.7557 0.0499  -0.0106 0.0177  408 ILE A CA  
3036 C C   . ILE B 193 ? 0.8457 0.5871 0.7491 0.0417  -0.0156 0.0190  408 ILE A C   
3037 O O   . ILE B 193 ? 0.8438 0.6060 0.7626 0.0438  -0.0187 0.0262  408 ILE A O   
3038 C CB  . ILE B 193 ? 0.7891 0.5228 0.6949 0.0587  -0.0070 0.0176  408 ILE A CB  
3039 C CG1 . ILE B 193 ? 0.7971 0.5341 0.6995 0.0662  -0.0025 0.0191  408 ILE A CG1 
3040 C CG2 . ILE B 193 ? 0.7941 0.5210 0.6927 0.0617  -0.0042 0.0165  408 ILE A CG2 
3041 C CD1 . ILE B 193 ? 0.7538 0.5088 0.6619 0.0742  0.0008  0.0196  408 ILE A CD1 
3042 N N   . LEU B 194 ? 0.8738 0.6041 0.7681 0.0343  -0.0136 0.0147  409 LEU A N   
3043 C CA  . LEU B 194 ? 0.8450 0.5938 0.7504 0.0246  -0.0168 0.0160  409 LEU A CA  
3044 C C   . LEU B 194 ? 0.8239 0.5598 0.7286 0.0274  -0.0107 0.0147  409 LEU A C   
3045 O O   . LEU B 194 ? 0.8736 0.5812 0.7571 0.0245  -0.0035 0.0122  409 LEU A O   
3046 C CB  . LEU B 194 ? 0.8477 0.6024 0.7376 0.0030  -0.0198 0.0113  409 LEU A CB  
3047 C CG  . LEU B 194 ? 0.8628 0.6505 0.7671 -0.0105 -0.0233 0.0137  409 LEU A CG  
3048 C CD1 . LEU B 194 ? 0.8094 0.6318 0.7448 0.0078  -0.0264 0.0262  409 LEU A CD1 
3049 C CD2 . LEU B 194 ? 1.0316 0.8455 0.9238 -0.0369 -0.0294 0.0083  409 LEU A CD2 
3050 N N   . GLN B 195 ? 0.8501 0.6032 0.7743 0.0345  -0.0106 0.0172  410 GLN A N   
3051 C CA  . GLN B 195 ? 0.8148 0.5643 0.7377 0.0379  -0.0054 0.0164  410 GLN A CA  
3052 C C   . GLN B 195 ? 0.7805 0.5449 0.7121 0.0291  -0.0040 0.0185  410 GLN A C   
3053 O O   . GLN B 195 ? 0.8122 0.6016 0.7627 0.0300  -0.0059 0.0218  410 GLN A O   
3054 C CB  . GLN B 195 ? 0.7691 0.5285 0.7024 0.0474  -0.0039 0.0134  410 GLN A CB  
3055 C CG  . GLN B 195 ? 0.8106 0.5670 0.7338 0.0540  -0.0036 0.0124  410 GLN A CG  
3056 C CD  . GLN B 195 ? 0.9056 0.6812 0.8353 0.0547  -0.0020 0.0058  410 GLN A CD  
3057 O OE1 . GLN B 195 ? 1.0386 0.8290 0.9651 0.0577  -0.0030 0.0047  410 GLN A OE1 
3058 N NE2 . GLN B 195 ? 0.9436 0.7227 0.8815 0.0505  0.0018  0.0004  410 GLN A NE2 
3059 N N   . VAL B 196 ? 0.8427 0.5933 0.7606 0.0227  0.0020  0.0194  411 VAL A N   
3060 C CA  . VAL B 196 ? 0.9245 0.6922 0.8509 0.0118  0.0053  0.0218  411 VAL A CA  
3061 C C   . VAL B 196 ? 0.9075 0.6684 0.8265 0.0194  0.0135  0.0247  411 VAL A C   
3062 O O   . VAL B 196 ? 0.9277 0.6603 0.8244 0.0214  0.0207  0.0286  411 VAL A O   
3063 C CB  . VAL B 196 ? 0.9366 0.6961 0.8505 -0.0129 0.0075  0.0198  411 VAL A CB  
3064 C CG1 . VAL B 196 ? 0.9207 0.7071 0.8468 -0.0269 0.0120  0.0231  411 VAL A CG1 
3065 C CG2 . VAL B 196 ? 0.9380 0.7171 0.8568 -0.0221 -0.0024 0.0166  411 VAL A CG2 
3066 N N   . VAL B 197 ? 0.9376 0.7234 0.8725 0.0258  0.0150  0.0243  412 VAL A N   
3067 C CA  . VAL B 197 ? 0.9522 0.7406 0.8789 0.0304  0.0229  0.0266  412 VAL A CA  
3068 C C   . VAL B 197 ? 0.8937 0.6967 0.8280 0.0183  0.0297  0.0316  412 VAL A C   
3069 O O   . VAL B 197 ? 0.8737 0.7052 0.8305 0.0149  0.0284  0.0320  412 VAL A O   
3070 C CB  . VAL B 197 ? 0.9416 0.7455 0.8740 0.0415  0.0241  0.0188  412 VAL A CB  
3071 C CG1 . VAL B 197 ? 0.9537 0.7639 0.8691 0.0455  0.0302  0.0209  412 VAL A CG1 
3072 C CG2 . VAL B 197 ? 0.8938 0.6917 0.8251 0.0467  0.0178  0.0117  412 VAL A CG2 
3073 N N   . THR B 198 ? 0.9798 0.7673 0.8960 0.0136  0.0390  0.0382  413 THR A N   
3074 C CA  . THR B 198 ? 0.9851 0.7873 0.9075 -0.0012 0.0481  0.0433  413 THR A CA  
3075 C C   . THR B 198 ? 0.9682 0.7668 0.8745 0.0074  0.0594  0.0507  413 THR A C   
3076 O O   . THR B 198 ? 0.9593 0.7409 0.8445 0.0223  0.0605  0.0549  413 THR A O   
3077 C CB  . THR B 198 ? 0.9306 0.7103 0.8421 -0.0271 0.0531  0.0446  413 THR A CB  
3078 O OG1 . THR B 198 ? 0.9271 0.6549 0.8057 -0.0223 0.0640  0.0506  413 THR A OG1 
3079 C CG2 . THR B 198 ? 0.9583 0.7443 0.8786 -0.0365 0.0411  0.0366  413 THR A CG2 
3080 N N   . ASN B 199 ? 0.9802 0.8038 0.8976 -0.0010 0.0681  0.0543  414 ASN A N   
3081 C CA  . ASN B 199 ? 1.0191 0.8397 0.9192 0.0013  0.0822  0.0643  414 ASN A CA  
3082 C C   . ASN B 199 ? 1.0035 0.7768 0.8755 -0.0081 0.0936  0.0757  414 ASN A C   
3083 O O   . ASN B 199 ? 1.0493 0.8084 0.9230 -0.0343 0.1003  0.0754  414 ASN A O   
3084 C CB  . ASN B 199 ? 1.0480 0.9069 0.9695 -0.0102 0.0909  0.0664  414 ASN A CB  
3085 C CG  . ASN B 199 ? 1.0018 0.8717 0.9101 -0.0006 0.1041  0.0733  414 ASN A CG  
3086 O OD1 . ASN B 199 ? 1.0209 0.8670 0.8996 0.0076  0.1102  0.0824  414 ASN A OD1 
3087 N ND2 . ASN B 199 ? 0.9701 0.8803 0.8995 0.0018  0.1100  0.0708  414 ASN A ND2 
3088 N N   . ARG B 200 ? 1.0039 0.7538 0.8486 0.0123  0.0982  0.0863  415 ARG A N   
3089 C CA  . ARG B 200 ? 1.1076 0.8027 0.9212 0.0106  0.1166  0.1023  415 ARG A CA  
3090 C C   . ARG B 200 ? 1.1099 0.7928 0.9180 -0.0129 0.1366  0.1103  415 ARG A C   
3091 O O   . ARG B 200 ? 1.1203 0.7609 0.9182 -0.0391 0.1500  0.1091  415 ARG A O   
3092 C CB  . ARG B 200 ? 1.0791 0.7687 0.8660 0.0438  0.1212  0.1204  415 ARG A CB  
3093 C CG  . ARG B 200 ? 1.0326 0.6562 0.7847 0.0539  0.1438  0.1414  415 ARG A CG  
3094 C CD  . ARG B 200 ? 1.2176 0.8159 0.9445 0.0545  0.1704  0.1644  415 ARG A CD  
3095 N NE  . ARG B 200 ? 1.2228 0.8656 0.9386 0.0846  0.1689  0.1828  415 ARG A NE  
3096 C CZ  . ARG B 200 ? 1.2465 0.8899 0.9386 0.1213  0.1739  0.2070  415 ARG A CZ  
3097 N NH1 . ARG B 200 ? 1.2626 0.8539 0.9378 0.1372  0.1860  0.2188  415 ARG A NH1 
3098 N NH2 . ARG B 200 ? 1.2307 0.9336 0.9147 0.1436  0.1679  0.2202  415 ARG A NH2 
3099 N N   . ASP B 201 ? 1.1949 0.9157 1.0086 -0.0076 0.1404  0.1161  416 ASP A N   
3100 C CA  . ASP B 201 ? 1.2103 0.9220 1.0149 -0.0254 0.1629  0.1286  416 ASP A CA  
3101 C C   . ASP B 201 ? 1.1719 0.9054 1.0043 -0.0638 0.1641  0.1167  416 ASP A C   
3102 O O   . ASP B 201 ? 1.1872 0.9084 1.0123 -0.0883 0.1847  0.1251  416 ASP A O   
3103 C CB  . ASP B 201 ? 1.1923 0.9455 0.9934 -0.0065 0.1664  0.1378  416 ASP A CB  
3104 C CG  . ASP B 201 ? 1.2311 0.9791 1.0021 0.0282  0.1655  0.1525  416 ASP A CG  
3105 O OD1 . ASP B 201 ? 1.2530 0.9526 0.9992 0.0393  0.1745  0.1675  416 ASP A OD1 
3106 O OD2 . ASP B 201 ? 1.2243 1.0198 0.9949 0.0445  0.1573  0.1490  416 ASP A OD2 
3107 N N   . THR B 202 ? 1.1329 0.9044 0.9971 -0.0700 0.1438  0.0995  417 THR A N   
3108 C CA  . THR B 202 ? 1.1309 0.9439 1.0245 -0.1033 0.1430  0.0919  417 THR A CA  
3109 C C   . THR B 202 ? 1.1499 0.9599 1.0523 -0.1244 0.1297  0.0776  417 THR A C   
3110 O O   . THR B 202 ? 1.1225 0.9776 1.0483 -0.1559 0.1272  0.0717  417 THR A O   
3111 C CB  . THR B 202 ? 1.0997 0.9867 1.0293 -0.0885 0.1352  0.0905  417 THR A CB  
3112 O OG1 . THR B 202 ? 1.1234 1.0337 1.0741 -0.0720 0.1149  0.0798  417 THR A OG1 
3113 C CG2 . THR B 202 ? 1.1057 0.9923 1.0196 -0.0600 0.1438  0.0988  417 THR A CG2 
3114 N N   . GLN B 203 ? 1.2160 0.9824 1.1001 -0.1090 0.1214  0.0727  418 GLN A N   
3115 C CA  . GLN B 203 ? 1.2588 1.0162 1.1438 -0.1270 0.1102  0.0589  418 GLN A CA  
3116 C C   . GLN B 203 ? 1.2046 1.0339 1.1291 -0.1226 0.0877  0.0518  418 GLN A C   
3117 O O   . GLN B 203 ? 1.2143 1.0507 1.1417 -0.1387 0.0769  0.0417  418 GLN A O   
3118 C CB  . GLN B 203 ? 1.2597 0.9896 1.1276 -0.1763 0.1260  0.0514  418 GLN A CB  
3119 C CG  . GLN B 203 ? 1.3661 1.0007 1.1857 -0.1842 0.1551  0.0573  418 GLN A CG  
3120 C CD  . GLN B 203 ? 1.4414 1.0143 1.2324 -0.1444 0.1576  0.0646  418 GLN A CD  
3121 O OE1 . GLN B 203 ? 1.4118 1.0131 1.2184 -0.1121 0.1362  0.0640  418 GLN A OE1 
3122 N NE2 . GLN B 203 ? 1.5167 1.0033 1.2641 -0.1470 0.1872  0.0730  418 GLN A NE2 
3123 N N   . GLU B 204 ? 1.1000 0.9801 1.0517 -0.0998 0.0833  0.0578  419 GLU A N   
3124 C CA  . GLU B 204 ? 1.0880 1.0323 1.0760 -0.0896 0.0689  0.0567  419 GLU A CA  
3125 C C   . GLU B 204 ? 1.0780 1.0026 1.0640 -0.0575 0.0573  0.0526  419 GLU A C   
3126 O O   . GLU B 204 ? 1.0543 0.9406 1.0208 -0.0376 0.0605  0.0518  419 GLU A O   
3127 C CB  . GLU B 204 ? 1.0851 1.0880 1.1015 -0.0791 0.0767  0.0659  419 GLU A CB  
3128 C CG  . GLU B 204 ? 1.0841 1.0731 1.0953 -0.0434 0.0830  0.0673  419 GLU A CG  
3129 C CD  . GLU B 204 ? 1.0961 1.1272 1.1228 -0.0387 0.0985  0.0756  419 GLU A CD  
3130 O OE1 . GLU B 204 ? 1.0643 1.1603 1.1250 -0.0413 0.1001  0.0827  419 GLU A OE1 
3131 O OE2 . GLU B 204 ? 1.1197 1.1244 1.1237 -0.0309 0.1099  0.0768  419 GLU A OE2 
3132 N N   . LEU B 205 ? 0.9566 0.9136 0.9625 -0.0544 0.0443  0.0512  420 LEU A N   
3133 C CA  . LEU B 205 ? 0.9155 0.8505 0.9182 -0.0308 0.0349  0.0472  420 LEU A CA  
3134 C C   . LEU B 205 ? 0.8813 0.8279 0.8983 0.0006  0.0401  0.0497  420 LEU A C   
3135 O O   . LEU B 205 ? 0.8281 0.8210 0.8707 0.0101  0.0458  0.0579  420 LEU A O   
3136 C CB  . LEU B 205 ? 0.9209 0.8858 0.9358 -0.0396 0.0218  0.0473  420 LEU A CB  
3137 C CG  . LEU B 205 ? 0.8510 0.7942 0.8611 -0.0217 0.0124  0.0444  420 LEU A CG  
3138 C CD1 . LEU B 205 ? 0.8952 0.8593 0.9030 -0.0426 0.0009  0.0424  420 LEU A CD1 
3139 C CD2 . LEU B 205 ? 0.8267 0.7917 0.8592 0.0097  0.0151  0.0525  420 LEU A CD2 
3140 N N   . LEU B 206 ? 0.8557 0.7617 0.8548 0.0158  0.0404  0.0421  421 LEU A N   
3141 C CA  . LEU B 206 ? 0.8451 0.7500 0.8491 0.0386  0.0485  0.0381  421 LEU A CA  
3142 C C   . LEU B 206 ? 0.8998 0.7938 0.9103 0.0520  0.0444  0.0355  421 LEU A C   
3143 O O   . LEU B 206 ? 0.8598 0.7612 0.8836 0.0703  0.0555  0.0378  421 LEU A O   
3144 C CB  . LEU B 206 ? 0.8586 0.7362 0.8365 0.0413  0.0534  0.0294  421 LEU A CB  
3145 C CG  . LEU B 206 ? 0.8678 0.7505 0.8339 0.0316  0.0606  0.0355  421 LEU A CG  
3146 C CD1 . LEU B 206 ? 0.8539 0.7207 0.7928 0.0383  0.0636  0.0302  421 LEU A CD1 
3147 C CD2 . LEU B 206 ? 0.8710 0.7903 0.8571 0.0334  0.0727  0.0415  421 LEU A CD2 
3148 N N   . LEU B 207 ? 0.8868 0.7592 0.8862 0.0449  0.0324  0.0322  422 LEU A N   
3149 C CA  . LEU B 207 ? 0.8630 0.7228 0.8658 0.0549  0.0289  0.0308  422 LEU A CA  
3150 C C   . LEU B 207 ? 0.8534 0.7094 0.8500 0.0429  0.0152  0.0326  422 LEU A C   
3151 O O   . LEU B 207 ? 0.8857 0.7222 0.8636 0.0305  0.0111  0.0283  422 LEU A O   
3152 C CB  . LEU B 207 ? 0.8701 0.6970 0.8570 0.0600  0.0331  0.0174  422 LEU A CB  
3153 C CG  . LEU B 207 ? 0.8520 0.6670 0.8353 0.0687  0.0494  0.0072  422 LEU A CG  
3154 C CD1 . LEU B 207 ? 0.8443 0.6332 0.8139 0.0645  0.0498  -0.0068 422 LEU A CD1 
3155 C CD2 . LEU B 207 ? 0.9276 0.7507 0.9304 0.0858  0.0630  0.0172  422 LEU A CD2 
3156 N N   . CYS B 208 ? 0.8445 0.7149 0.8529 0.0496  0.0112  0.0399  423 CYS A N   
3157 C CA  . CYS B 208 ? 0.8117 0.6766 0.8101 0.0396  -0.0003 0.0393  423 CYS A CA  
3158 C C   . CYS B 208 ? 0.7511 0.6071 0.7541 0.0559  0.0011  0.0436  423 CYS A C   
3159 O O   . CYS B 208 ? 0.7819 0.6659 0.8018 0.0694  0.0040  0.0577  423 CYS A O   
3160 C CB  . CYS B 208 ? 0.8235 0.7299 0.8282 0.0225  -0.0083 0.0455  423 CYS A CB  
3161 S SG  . CYS B 208 ? 0.8709 0.7693 0.8563 0.0078  -0.0198 0.0409  423 CYS A SG  
3162 N N   . THR B 209 ? 0.7727 0.5939 0.7609 0.0558  0.0008  0.0344  424 THR A N   
3163 C CA  . THR B 209 ? 0.8179 0.6248 0.8073 0.0661  0.0044  0.0372  424 THR A CA  
3164 C C   . THR B 209 ? 0.7948 0.6004 0.7727 0.0593  -0.0059 0.0383  424 THR A C   
3165 O O   . THR B 209 ? 0.7548 0.5461 0.7164 0.0488  -0.0109 0.0296  424 THR A O   
3166 C CB  . THR B 209 ? 0.8062 0.5832 0.7886 0.0666  0.0134  0.0244  424 THR A CB  
3167 O OG1 . THR B 209 ? 0.9225 0.6989 0.9073 0.0682  0.0227  0.0184  424 THR A OG1 
3168 C CG2 . THR B 209 ? 0.8189 0.5767 0.8043 0.0749  0.0241  0.0277  424 THR A CG2 
3169 N N   . ALA B 210 ? 0.8471 0.6662 0.8311 0.0684  -0.0060 0.0509  425 ALA A N   
3170 C CA  . ALA B 210 ? 0.7675 0.5853 0.7387 0.0645  -0.0129 0.0527  425 ALA A CA  
3171 C C   . ALA B 210 ? 0.7673 0.5559 0.7372 0.0731  -0.0031 0.0525  425 ALA A C   
3172 O O   . ALA B 210 ? 0.8340 0.6132 0.8145 0.0863  0.0100  0.0609  425 ALA A O   
3173 C CB  . ALA B 210 ? 0.6872 0.5488 0.6638 0.0682  -0.0195 0.0692  425 ALA A CB  
3174 N N   . TYR B 211 ? 0.7705 0.5431 0.7265 0.0656  -0.0060 0.0434  426 TYR A N   
3175 C CA  . TYR B 211 ? 0.8107 0.5639 0.7664 0.0681  0.0031  0.0423  426 TYR A CA  
3176 C C   . TYR B 211 ? 0.8598 0.6173 0.8054 0.0702  0.0006  0.0507  426 TYR A C   
3177 O O   . TYR B 211 ? 0.8511 0.6149 0.7816 0.0642  -0.0081 0.0464  426 TYR A O   
3178 C CB  . TYR B 211 ? 0.7959 0.5405 0.7474 0.0598  0.0037  0.0275  426 TYR A CB  
3179 C CG  . TYR B 211 ? 0.8597 0.6046 0.8165 0.0565  0.0061  0.0183  426 TYR A CG  
3180 C CD1 . TYR B 211 ? 0.8905 0.6279 0.8509 0.0497  0.0161  0.0080  426 TYR A CD1 
3181 C CD2 . TYR B 211 ? 0.8879 0.6410 0.8421 0.0560  -0.0004 0.0178  426 TYR A CD2 
3182 C CE1 . TYR B 211 ? 0.9152 0.6565 0.8755 0.0448  0.0187  -0.0025 426 TYR A CE1 
3183 C CE2 . TYR B 211 ? 0.9240 0.6797 0.8805 0.0538  0.0028  0.0105  426 TYR A CE2 
3184 C CZ  . TYR B 211 ? 0.9106 0.6620 0.8694 0.0492  0.0116  0.0002  426 TYR A CZ  
3185 O OH  . TYR B 211 ? 0.8524 0.6100 0.8087 0.0453  0.0148  -0.0087 426 TYR A OH  
3186 N N   . VAL B 212 ? 0.8728 0.6211 0.8229 0.0786  0.0118  0.0625  427 VAL A N   
3187 C CA  . VAL B 212 ? 0.8843 0.6347 0.8238 0.0810  0.0129  0.0716  427 VAL A CA  
3188 C C   . VAL B 212 ? 0.9069 0.6325 0.8492 0.0761  0.0278  0.0676  427 VAL A C   
3189 O O   . VAL B 212 ? 0.8812 0.5863 0.8326 0.0716  0.0402  0.0611  427 VAL A O   
3190 C CB  . VAL B 212 ? 0.8141 0.5832 0.7535 0.0962  0.0145  0.0955  427 VAL A CB  
3191 C CG1 . VAL B 212 ? 0.7728 0.5833 0.7043 0.0922  -0.0037 0.0969  427 VAL A CG1 
3192 C CG2 . VAL B 212 ? 0.8212 0.5744 0.7757 0.1114  0.0312  0.1084  427 VAL A CG2 
3193 N N   . PHE B 213 ? 0.9292 0.6582 0.8617 0.0743  0.0285  0.0706  428 PHE A N   
3194 C CA  . PHE B 213 ? 0.9370 0.6547 0.8733 0.0636  0.0407  0.0639  428 PHE A CA  
3195 C C   . PHE B 213 ? 0.9654 0.6746 0.8956 0.0667  0.0536  0.0792  428 PHE A C   
3196 O O   . PHE B 213 ? 0.9904 0.7131 0.9075 0.0766  0.0480  0.0916  428 PHE A O   
3197 C CB  . PHE B 213 ? 0.8956 0.6327 0.8291 0.0572  0.0316  0.0501  428 PHE A CB  
3198 C CG  . PHE B 213 ? 0.8746 0.6181 0.8121 0.0551  0.0225  0.0381  428 PHE A CG  
3199 C CD1 . PHE B 213 ? 0.8912 0.6364 0.8194 0.0613  0.0113  0.0382  428 PHE A CD1 
3200 C CD2 . PHE B 213 ? 0.8569 0.6076 0.8053 0.0440  0.0262  0.0262  428 PHE A CD2 
3201 C CE1 . PHE B 213 ? 0.8605 0.6082 0.7907 0.0597  0.0058  0.0298  428 PHE A CE1 
3202 C CE2 . PHE B 213 ? 0.8466 0.6069 0.7961 0.0442  0.0184  0.0181  428 PHE A CE2 
3203 C CZ  . PHE B 213 ? 0.8608 0.6164 0.8015 0.0538  0.0091  0.0213  428 PHE A CZ  
3204 N N   . GLU B 214 ? 0.9151 0.6013 0.8523 0.0551  0.0729  0.0771  429 GLU A N   
3205 C CA  . GLU B 214 ? 0.8971 0.5770 0.8306 0.0484  0.0879  0.0847  429 GLU A CA  
3206 C C   . GLU B 214 ? 0.9159 0.6022 0.8607 0.0215  0.0955  0.0644  429 GLU A C   
3207 O O   . GLU B 214 ? 0.9463 0.6423 0.8990 0.0112  0.0885  0.0466  429 GLU A O   
3208 C CB  . GLU B 214 ? 0.9130 0.5545 0.8409 0.0585  0.1109  0.1071  429 GLU A CB  
3209 C CG  . GLU B 214 ? 0.9281 0.5785 0.8486 0.0867  0.1030  0.1303  429 GLU A CG  
3210 C CD  . GLU B 214 ? 1.0020 0.6251 0.9138 0.1041  0.1269  0.1611  429 GLU A CD  
3211 O OE1 . GLU B 214 ? 0.9845 0.5669 0.8947 0.0913  0.1536  0.1619  429 GLU A OE1 
3212 O OE2 . GLU B 214 ? 1.0733 0.7193 0.9788 0.1296  0.1202  0.1857  429 GLU A OE2 
3213 N N   . VAL B 215 ? 0.9316 0.6203 0.8770 0.0082  0.1098  0.0673  430 VAL A N   
3214 C CA  . VAL B 215 ? 0.9400 0.6448 0.8975 -0.0235 0.1193  0.0486  430 VAL A CA  
3215 C C   . VAL B 215 ? 0.9993 0.6494 0.9522 -0.0433 0.1503  0.0492  430 VAL A C   
3216 O O   . VAL B 215 ? 1.0370 0.6473 0.9785 -0.0283 0.1666  0.0715  430 VAL A O   
3217 C CB  . VAL B 215 ? 0.9252 0.6796 0.8890 -0.0288 0.1164  0.0500  430 VAL A CB  
3218 C CG1 . VAL B 215 ? 0.8213 0.6121 0.7822 -0.0036 0.0934  0.0520  430 VAL A CG1 
3219 C CG2 . VAL B 215 ? 1.0050 0.7379 0.9601 -0.0276 0.1353  0.0685  430 VAL A CG2 
3220 N N   . SER B 216 ? 1.0004 0.6463 0.9586 -0.0770 0.1609  0.0251  431 SER A N   
3221 C CA  . SER B 216 ? 1.0788 0.6621 1.0273 -0.1033 0.1966  0.0198  431 SER A CA  
3222 C C   . SER B 216 ? 1.1742 0.7826 1.1290 -0.1400 0.2107  0.0122  431 SER A C   
3223 O O   . SER B 216 ? 1.1625 0.8476 1.1332 -0.1475 0.1912  0.0063  431 SER A O   
3224 C CB  . SER B 216 ? 1.1029 0.6570 1.0461 -0.1261 0.2064  -0.0069 431 SER A CB  
3225 O OG  . SER B 216 ? 1.1795 0.6848 1.1118 -0.1686 0.2430  -0.0230 431 SER A OG  
3226 N N   . THR B 217 ? 1.2697 0.8114 1.2114 -0.1618 0.2484  0.0141  432 THR A N   
3227 C CA  . THR B 217 ? 1.3730 0.9305 1.3190 -0.2002 0.2676  0.0092  432 THR A CA  
3228 C C   . THR B 217 ? 1.4397 1.0564 1.3987 -0.2524 0.2621  -0.0279 432 THR A C   
3229 O O   . THR B 217 ? 1.3275 0.9537 1.2856 -0.2611 0.2504  -0.0504 432 THR A O   
3230 C CB  . THR B 217 ? 1.3760 0.8342 1.2999 -0.2113 0.3149  0.0214  432 THR A CB  
3231 O OG1 . THR B 217 ? 1.4699 0.8850 1.3834 -0.2650 0.3439  -0.0121 432 THR A OG1 
3232 C CG2 . THR B 217 ? 1.2937 0.6836 1.2008 -0.1590 0.3218  0.0502  432 THR A CG2 
3233 N N   . SER B 218 ? 1.7250 1.3912 1.6964 -0.2877 0.2703  -0.0330 433 SER A N   
3234 C CA  . SER B 218 ? 1.6987 1.4563 1.6885 -0.3341 0.2583  -0.0630 433 SER A CA  
3235 C C   . SER B 218 ? 1.7109 1.4255 1.6838 -0.3857 0.2791  -0.0999 433 SER A C   
3236 O O   . SER B 218 ? 1.6691 1.4405 1.6474 -0.3998 0.2579  -0.1233 433 SER A O   
3237 C CB  . SER B 218 ? 1.6640 1.4818 1.6708 -0.3644 0.2689  -0.0588 433 SER A CB  
3238 O OG  . SER B 218 ? 1.7112 1.5356 1.7224 -0.3161 0.2612  -0.0239 433 SER A OG  
3239 N N   . GLU B 219 ? 1.7607 1.3697 1.7087 -0.4132 0.3238  -0.1049 434 GLU A N   
3240 C CA  . GLU B 219 ? 1.7472 1.3005 1.6715 -0.4696 0.3531  -0.1444 434 GLU A CA  
3241 C C   . GLU B 219 ? 1.7810 1.2454 1.6814 -0.4375 0.3600  -0.1463 434 GLU A C   
3242 O O   . GLU B 219 ? 1.7307 1.1868 1.6163 -0.4720 0.3651  -0.1822 434 GLU A O   
3243 C CB  . GLU B 219 ? 1.7995 1.2687 1.7032 -0.5187 0.4066  -0.1511 434 GLU A CB  
3244 C CG  . GLU B 219 ? 1.8335 1.1862 1.7160 -0.4673 0.4361  -0.1123 434 GLU A CG  
3245 C CD  . GLU B 219 ? 1.9655 1.2274 1.8119 -0.4816 0.4782  -0.1250 434 GLU A CD  
3246 O OE1 . GLU B 219 ? 1.9717 1.2167 1.7975 -0.5108 0.4873  -0.1621 434 GLU A OE1 
3247 O OE2 . GLU B 219 ? 2.0385 1.2460 1.8745 -0.4640 0.5048  -0.0977 434 GLU A OE2 
3248 N N   . ARG B 220 ? 1.5985 1.0038 1.4943 -0.3729 0.3606  -0.1081 435 ARG A N   
3249 C CA  . ARG B 220 ? 1.4568 0.7735 1.3315 -0.3370 0.3744  -0.1018 435 ARG A CA  
3250 C C   . ARG B 220 ? 1.3537 0.7289 1.2387 -0.3155 0.3350  -0.1133 435 ARG A C   
3251 O O   . ARG B 220 ? 1.4037 0.7162 1.2712 -0.2982 0.3479  -0.1180 435 ARG A O   
3252 C CB  . ARG B 220 ? 1.4012 0.6647 1.2728 -0.2750 0.3832  -0.0529 435 ARG A CB  
3253 C CG  . ARG B 220 ? 1.3720 0.5560 1.2264 -0.2296 0.3988  -0.0367 435 ARG A CG  
3254 C CD  . ARG B 220 ? 1.3940 0.5453 1.2447 -0.1718 0.4090  0.0131  435 ARG A CD  
3255 N NE  . ARG B 220 ? 1.4437 0.5659 1.2869 -0.1203 0.4116  0.0299  435 ARG A NE  
3256 C CZ  . ARG B 220 ? 1.4510 0.5646 1.2934 -0.0631 0.4140  0.0732  435 ARG A CZ  
3257 N NH1 . ARG B 220 ? 1.3448 0.4673 1.1884 -0.0468 0.4159  0.1054  435 ARG A NH1 
3258 N NH2 . ARG B 220 ? 1.4229 0.5272 1.2634 -0.0224 0.4147  0.0851  435 ARG A NH2 
3259 N N   . GLY B 221 ? 1.3252 0.8151 1.2364 -0.3135 0.2912  -0.1157 436 GLY A N   
3260 C CA  . GLY B 221 ? 1.1892 0.7353 1.1060 -0.3078 0.2604  -0.1328 436 GLY A CA  
3261 C C   . GLY B 221 ? 1.1289 0.6620 1.0492 -0.2452 0.2393  -0.1069 436 GLY A C   
3262 O O   . GLY B 221 ? 1.1364 0.6050 1.0499 -0.2074 0.2530  -0.0794 436 GLY A O   
3263 N N   . ALA B 222 ? 1.0839 0.6857 1.0142 -0.2362 0.2061  -0.1156 437 ALA A N   
3264 C CA  . ALA B 222 ? 1.0045 0.6090 0.9396 -0.1853 0.1830  -0.0957 437 ALA A CA  
3265 C C   . ALA B 222 ? 1.0392 0.5551 0.9562 -0.1673 0.2074  -0.0933 437 ALA A C   
3266 O O   . ALA B 222 ? 1.0793 0.5383 0.9760 -0.1976 0.2386  -0.1173 437 ALA A O   
3267 C CB  . ALA B 222 ? 0.8966 0.5825 0.8406 -0.1875 0.1513  -0.1089 437 ALA A CB  
3268 N N   . GLN B 223 ? 1.0636 0.5694 0.9866 -0.1181 0.1955  -0.0643 438 GLN A N   
3269 C CA  . GLN B 223 ? 1.1558 0.5904 1.0671 -0.0903 0.2184  -0.0521 438 GLN A CA  
3270 C C   . GLN B 223 ? 1.0980 0.5670 1.0224 -0.0457 0.1903  -0.0285 438 GLN A C   
3271 O O   . GLN B 223 ? 1.0938 0.6174 1.0311 -0.0327 0.1613  -0.0152 438 GLN A O   
3272 C CB  . GLN B 223 ? 1.2418 0.6017 1.1418 -0.0800 0.2552  -0.0304 438 GLN A CB  
3273 C CG  . GLN B 223 ? 1.3289 0.6225 1.2188 -0.0401 0.2812  -0.0092 438 GLN A CG  
3274 C CD  . GLN B 223 ? 1.3801 0.5749 1.2478 -0.0399 0.3341  0.0006  438 GLN A CD  
3275 O OE1 . GLN B 223 ? 1.3871 0.5723 1.2541 -0.0346 0.3440  0.0225  438 GLN A OE1 
3276 N NE2 . GLN B 223 ? 1.4450 0.6021 1.2963 -0.0423 0.3594  -0.0150 438 GLN A NE2 
3277 N N   . HIS B 224 ? 1.0653 0.5009 0.9844 -0.0243 0.2020  -0.0246 439 HIS A N   
3278 C CA  . HIS B 224 ? 1.0753 0.5433 1.0072 0.0143  0.1800  -0.0019 439 HIS A CA  
3279 C C   . HIS B 224 ? 1.0640 0.4797 0.9910 0.0471  0.2088  0.0192  439 HIS A C   
3280 O O   . HIS B 224 ? 1.1399 0.4840 1.0501 0.0412  0.2483  0.0136  439 HIS A O   
3281 C CB  . HIS B 224 ? 1.0505 0.5665 0.9877 0.0070  0.1543  -0.0201 439 HIS A CB  
3282 C CG  . HIS B 224 ? 1.0914 0.5770 1.0142 -0.0131 0.1739  -0.0478 439 HIS A CG  
3283 N ND1 . HIS B 224 ? 1.0880 0.5467 1.0070 0.0078  0.1883  -0.0446 439 HIS A ND1 
3284 C CD2 . HIS B 224 ? 1.0982 0.5790 1.0071 -0.0543 0.1833  -0.0806 439 HIS A CD2 
3285 C CE1 . HIS B 224 ? 1.1106 0.5418 1.0108 -0.0189 0.2069  -0.0757 439 HIS A CE1 
3286 N NE2 . HIS B 224 ? 1.1218 0.5673 1.0147 -0.0592 0.2035  -0.0990 439 HIS A NE2 
3287 N N   . HIS B 225 ? 1.0204 0.4738 0.9613 0.0820  0.1912  0.0447  440 HIS A N   
3288 C CA  . HIS B 225 ? 1.1187 0.5461 1.0611 0.1210  0.2145  0.0713  440 HIS A CA  
3289 C C   . HIS B 225 ? 1.0855 0.5794 1.0457 0.1376  0.1846  0.0788  440 HIS A C   
3290 O O   . HIS B 225 ? 0.9838 0.5363 0.9548 0.1402  0.1530  0.0897  440 HIS A O   
3291 C CB  . HIS B 225 ? 1.1569 0.5705 1.0987 0.1494  0.2290  0.1089  440 HIS A CB  
3292 C CG  . HIS B 225 ? 1.2213 0.5874 1.1582 0.1895  0.2683  0.1376  440 HIS A CG  
3293 N ND1 . HIS B 225 ? 1.2567 0.6704 1.2063 0.2325  0.2632  0.1800  440 HIS A ND1 
3294 C CD2 . HIS B 225 ? 1.3564 0.6673 1.2771 0.1850  0.3054  0.1255  440 HIS A CD2 
3295 C CE1 . HIS B 225 ? 1.3363 0.7261 1.2801 0.2564  0.2963  0.1949  440 HIS A CE1 
3296 N NE2 . HIS B 225 ? 1.4279 0.7496 1.3527 0.2288  0.3238  0.1623  440 HIS A NE2 
3297 N N   . ILE B 226 ? 1.1229 0.6056 1.0831 0.1439  0.1964  0.0691  441 ILE A N   
3298 C CA  . ILE B 226 ? 1.0374 0.5807 1.0134 0.1523  0.1711  0.0716  441 ILE A CA  
3299 C C   . ILE B 226 ? 1.0419 0.6073 1.0329 0.1954  0.1818  0.1080  441 ILE A C   
3300 O O   . ILE B 226 ? 1.1040 0.6193 1.0888 0.2215  0.2195  0.1226  441 ILE A O   
3301 C CB  . ILE B 226 ? 0.9752 0.5055 0.9426 0.1325  0.1755  0.0401  441 ILE A CB  
3302 C CG1 . ILE B 226 ? 0.9865 0.5081 0.9396 0.0914  0.1659  0.0077  441 ILE A CG1 
3303 C CG2 . ILE B 226 ? 0.9507 0.5418 0.9334 0.1385  0.1508  0.0439  441 ILE A CG2 
3304 C CD1 . ILE B 226 ? 0.9822 0.5055 0.9240 0.0696  0.1659  -0.0222 441 ILE A CD1 
3305 N N   . TYR B 227 ? 0.9843 0.6259 0.9936 0.2030  0.1513  0.1240  442 TYR A N   
3306 C CA  . TYR B 227 ? 1.0292 0.7185 1.0571 0.2414  0.1558  0.1608  442 TYR A CA  
3307 C C   . TYR B 227 ? 1.0070 0.7660 1.0529 0.2362  0.1324  0.1581  442 TYR A C   
3308 O O   . TYR B 227 ? 0.9375 0.7126 0.9801 0.2037  0.1073  0.1333  442 TYR A O   
3309 C CB  . TYR B 227 ? 1.0677 0.8023 1.1008 0.2559  0.1419  0.1914  442 TYR A CB  
3310 C CG  . TYR B 227 ? 1.0739 0.7577 1.0900 0.2572  0.1567  0.1985  442 TYR A CG  
3311 C CD1 . TYR B 227 ? 1.0398 0.6927 1.0412 0.2208  0.1457  0.1700  442 TYR A CD1 
3312 C CD2 . TYR B 227 ? 1.1420 0.8174 1.1580 0.2973  0.1820  0.2383  442 TYR A CD2 
3313 C CE1 . TYR B 227 ? 1.1353 0.7478 1.1228 0.2198  0.1599  0.1776  442 TYR A CE1 
3314 C CE2 . TYR B 227 ? 1.2365 0.8647 1.2356 0.2981  0.1976  0.2476  442 TYR A CE2 
3315 C CZ  . TYR B 227 ? 1.2166 0.8140 1.2020 0.2569  0.1859  0.2158  442 TYR A CZ  
3316 O OH  . TYR B 227 ? 1.2749 0.8284 1.2447 0.2557  0.2033  0.2256  442 TYR A OH  
3317 N N   . ARG B 228 ? 1.1027 0.9066 1.1680 0.2704  0.1427  0.1878  443 ARG A N   
3318 C CA  . ARG B 228 ? 1.0832 0.9709 1.1702 0.2665  0.1210  0.1931  443 ARG A CA  
3319 C C   . ARG B 228 ? 1.0609 1.0313 1.1588 0.2643  0.0929  0.2144  443 ARG A C   
3320 O O   . ARG B 228 ? 1.0953 1.0841 1.1966 0.2941  0.1017  0.2463  443 ARG A O   
3321 C CB  . ARG B 228 ? 1.1556 1.0618 1.2605 0.3055  0.1484  0.2158  443 ARG A CB  
3322 C CG  . ARG B 228 ? 1.1991 1.0240 1.2885 0.3069  0.1799  0.1920  443 ARG A CG  
3323 C CD  . ARG B 228 ? 1.1987 1.0675 1.3046 0.3112  0.1822  0.1900  443 ARG A CD  
3324 N NE  . ARG B 228 ? 1.2387 1.1864 1.3753 0.3529  0.1907  0.2316  443 ARG A NE  
3325 C CZ  . ARG B 228 ? 1.2229 1.2639 1.3861 0.3480  0.1726  0.2406  443 ARG A CZ  
3326 N NH1 . ARG B 228 ? 1.1268 1.1823 1.2870 0.3047  0.1482  0.2114  443 ARG A NH1 
3327 N NH2 . ARG B 228 ? 1.2418 1.3660 1.4354 0.3883  0.1815  0.2818  443 ARG A NH2 
3328 N N   . LEU B 229 ? 0.9546 0.9742 1.0546 0.2289  0.0618  0.1978  444 LEU A N   
3329 C CA  . LEU B 229 ? 0.9492 1.0595 1.0588 0.2235  0.0379  0.2162  444 LEU A CA  
3330 C C   . LEU B 229 ? 0.9580 1.1619 1.0979 0.2394  0.0373  0.2398  444 LEU A C   
3331 O O   . LEU B 229 ? 0.9802 1.1898 1.1302 0.2288  0.0399  0.2270  444 LEU A O   
3332 C CB  . LEU B 229 ? 0.9442 1.0615 1.0365 0.1761  0.0091  0.1880  444 LEU A CB  
3333 C CG  . LEU B 229 ? 0.9401 0.9751 1.0050 0.1577  0.0080  0.1624  444 LEU A CG  
3334 C CD1 . LEU B 229 ? 0.8815 0.8654 0.9390 0.1382  0.0109  0.1336  444 LEU A CD1 
3335 C CD2 . LEU B 229 ? 1.0159 1.0764 1.0629 0.1313  -0.0147 0.1548  444 LEU A CD2 
3336 N N   . VAL B 230 ? 0.9558 1.2401 1.1106 0.2662  0.0346  0.2769  445 VAL A N   
3337 C CA  . VAL B 230 ? 0.9208 1.3165 1.1089 0.2872  0.0342  0.3075  445 VAL A CA  
3338 C C   . VAL B 230 ? 0.9353 1.4462 1.1279 0.2627  0.0019  0.3173  445 VAL A C   
3339 O O   . VAL B 230 ? 0.9156 1.4058 1.0819 0.2247  -0.0186 0.2932  445 VAL A O   
3340 C CB  . VAL B 230 ? 0.9399 1.3318 1.1435 0.3546  0.0698  0.3509  445 VAL A CB  
3341 C CG1 . VAL B 230 ? 0.9974 1.2525 1.1820 0.3685  0.1037  0.3324  445 VAL A CG1 
3342 C CG2 . VAL B 230 ? 1.0042 1.4315 1.2037 0.3862  0.0703  0.3889  445 VAL A CG2 
3343 N N   . ARG B 231 ? 0.8892 1.5267 1.1137 0.2820  -0.0021 0.3511  446 ARG A N   
3344 C CA  . ARG B 231 ? 0.8760 1.6388 1.1038 0.2518  -0.0339 0.3576  446 ARG A CA  
3345 C C   . ARG B 231 ? 0.8304 1.7365 1.0937 0.2979  -0.0314 0.4128  446 ARG A C   
3346 O O   . ARG B 231 ? 0.8153 1.7981 1.1131 0.3102  -0.0253 0.4286  446 ARG A O   
3347 C CB  . ARG B 231 ? 0.8759 1.6684 1.1021 0.1853  -0.0554 0.3183  446 ARG A CB  
3348 C CG  . ARG B 231 ? 0.9370 1.7608 1.1346 0.1282  -0.0846 0.2922  446 ARG A CG  
3349 C CD  . ARG B 231 ? 0.9910 1.7528 1.1675 0.0659  -0.0919 0.2425  446 ARG A CD  
3350 N NE  . ARG B 231 ? 1.0789 1.9413 1.2508 0.0074  -0.1150 0.2270  446 ARG A NE  
3351 C CZ  . ARG B 231 ? 1.1089 1.9425 1.2633 -0.0525 -0.1196 0.1880  446 ARG A CZ  
3352 N NH1 . ARG B 231 ? 1.1186 1.8292 1.2581 -0.0590 -0.1051 0.1629  446 ARG A NH1 
3353 N NH2 . ARG B 231 ? 1.1470 2.0786 1.2963 -0.1085 -0.1374 0.1745  446 ARG A NH2 
# 
