data_8U40
# 
_entry.id   8U40 
# 
_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   8U40         pdb_00008u40 10.2210/pdb8u40/pdb 
WWPDB D_1000277308 ?            ?                   
# 
_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       2025-03-12 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8U40 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 6WTM unspecified 
PDB . 8FTC unspecified 
PDB . 7MBI unspecified 
PDB . 7R7H unspecified 
# 
_pdbx_contact_author.id                 5 
_pdbx_contact_author.email              mlemieux@ualberta.ca 
_pdbx_contact_author.name_first         'M. Joanne' 
_pdbx_contact_author.name_last          Lemieux 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4745-9153 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chen, P.'       1 0000-0002-0434-6346 
'Arutyunova, E.' 2 0000-0003-4119-3622 
'Lu, J.'         3 0000-0002-4090-5176 
'Young, H.S.'    4 0000-0002-5990-8422 
'Lemieux, M.J.'  5 0000-0003-4745-9153 
# 
_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                     'Crystal structure of main protease of SARS-CoV-2 complexed with 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 'Chen, P.'       1 0000-0002-0434-6346 
primary 'Arutyunova, E.' 2 0000-0003-4119-3622 
primary 'Lu, J.'         3 0000-0002-4090-5176 
primary 'Young, H.S.'    4 0000-0002-5990-8422 
primary 'Lemieux, M.J.'  5 0000-0003-4745-9153 
# 
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 '3C-like proteinase nsp5' 33825.547 2  3.4.22.69 ? ? ? 
2 non-polymer syn 
;N-[(2S)-3-cyclopropyl-1-({(1E,2R)-1-imino-3-[(3R)-2-oxo-2,3-dihydropyridin-3-yl]propan-2-yl}amino)-1-oxopropan-2-yl]-5,7-difluoro-1H-indole-2-carboxamide
;
455.457   2  ?         ? ? ? 
3 water       nat water 18.015    90 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
_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       
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;N-[(2S)-3-cyclopropyl-1-({(1E,2R)-1-imino-3-[(3R)-2-oxo-2,3-dihydropyridin-3-yl]propan-2-yl}amino)-1-oxopropan-2-yl]-5,7-difluoro-1H-indole-2-carboxamide
;
V8X 
3 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE n 
1 306 GLN 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                   306 
_entity_src_gen.gene_src_common_name               2019-nCoV,SARS-CoV-2 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_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      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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 
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 
HOH non-polymer         . WATER ? 'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'      181.189 
V8X non-polymer         . 
;N-[(2S)-3-cyclopropyl-1-({(1E,2R)-1-imino-3-[(3R)-2-oxo-2,3-dihydropyridin-3-yl]propan-2-yl}amino)-1-oxopropan-2-yl]-5,7-difluoro-1H-indole-2-carboxamide
;
? 'C23 H23 F2 N5 O3' 455.457 
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   SER 1   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
A 1 306 GLN 306 306 306 GLN GLN A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   GLY 2   2   2   GLY GLY B . n 
B 1 3   PHE 3   3   3   PHE PHE B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   MET 6   6   6   MET MET B . n 
B 1 7   ALA 7   7   7   ALA ALA B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  LYS 12  12  12  LYS LYS B . n 
B 1 13  VAL 13  13  13  VAL VAL B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  CYS 16  16  16  CYS CYS B . n 
B 1 17  MET 17  17  17  MET MET B . n 
B 1 18  VAL 18  18  18  VAL VAL B . n 
B 1 19  GLN 19  19  19  GLN GLN B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  THR 21  21  21  THR THR B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  THR 24  24  24  THR THR B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  THR 26  26  26  THR THR B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  ASN 28  28  28  ASN ASN B . n 
B 1 29  GLY 29  29  29  GLY GLY B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  TRP 31  31  31  TRP TRP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  ASP 33  33  33  ASP ASP B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  TYR 37  37  37  TYR TYR B . n 
B 1 38  CYS 38  38  38  CYS CYS B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  ARG 40  40  40  ARG ARG B . n 
B 1 41  HIS 41  41  41  HIS HIS B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  ILE 43  43  43  ILE ILE B . n 
B 1 44  CYS 44  44  44  CYS CYS B . n 
B 1 45  THR 45  45  45  THR THR B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  MET 49  49  49  MET MET B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  ASN 51  51  51  ASN ASN B . n 
B 1 52  PRO 52  52  52  PRO PRO B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  ARG 60  60  60  ARG ARG B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  GLN 74  74  74  GLN GLN B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  MET 82  82  82  MET MET B . n 
B 1 83  GLN 83  83  83  GLN GLN B . n 
B 1 84  ASN 84  84  84  ASN ASN B . n 
B 1 85  CYS 85  85  85  CYS CYS B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  THR 93  93  93  THR THR B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  ASN 95  95  95  ASN ASN B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  LYS 97  97  97  LYS LYS B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  PRO 99  99  99  PRO PRO B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 PHE 103 103 103 PHE PHE B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 ARG 105 105 105 ARG ARG B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 PRO 108 108 108 PRO PRO B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 THR 111 111 111 THR THR B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 SER 113 113 113 SER SER B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 CYS 117 117 117 CYS CYS B . n 
B 1 118 TYR 118 118 118 TYR TYR B . n 
B 1 119 ASN 119 119 119 ASN ASN B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 SER 121 121 121 SER SER B . n 
B 1 122 PRO 122 122 122 PRO PRO B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 GLY 124 124 124 GLY GLY B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 GLN 127 127 127 GLN GLN B . n 
B 1 128 CYS 128 128 128 CYS CYS B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 MET 130 130 130 MET MET B . n 
B 1 131 ARG 131 131 131 ARG ARG B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 ASN 133 133 133 ASN ASN B . n 
B 1 134 PHE 134 134 134 PHE PHE B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 ILE 136 136 136 ILE ILE B . n 
B 1 137 LYS 137 137 137 LYS LYS B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 SER 144 144 144 SER SER B . n 
B 1 145 CYS 145 145 145 CYS CYS B . n 
B 1 146 GLY 146 146 146 GLY GLY B . n 
B 1 147 SER 147 147 147 SER SER B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 PHE 150 150 150 PHE PHE B . n 
B 1 151 ASN 151 151 151 ASN ASN B . n 
B 1 152 ILE 152 152 152 ILE ILE B . n 
B 1 153 ASP 153 153 153 ASP ASP B . n 
B 1 154 TYR 154 154 154 TYR TYR B . n 
B 1 155 ASP 155 155 155 ASP ASP B . n 
B 1 156 CYS 156 156 156 CYS CYS B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 SER 158 158 158 SER SER B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 CYS 160 160 160 CYS CYS B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 MET 162 162 162 MET MET B . n 
B 1 163 HIS 163 163 163 HIS HIS B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 MET 165 165 165 MET MET B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 LEU 167 167 167 LEU LEU B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 THR 169 169 169 THR THR B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 VAL 171 171 171 VAL VAL B . n 
B 1 172 HIS 172 172 172 HIS HIS B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 GLU 178 178 178 GLU GLU B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 TYR 182 182 182 TYR TYR B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 PHE 185 185 185 PHE PHE B . n 
B 1 186 VAL 186 186 186 VAL VAL B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 ARG 188 188 188 ARG ARG B . n 
B 1 189 GLN 189 189 189 GLN GLN B . n 
B 1 190 THR 190 190 190 THR THR B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 ALA 193 193 193 ALA ALA B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 THR 196 196 196 THR THR B . n 
B 1 197 ASP 197 197 197 ASP ASP B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 ILE 200 200 200 ILE ILE B . n 
B 1 201 THR 201 201 201 THR THR B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 VAL 204 204 204 VAL VAL B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 TRP 207 207 207 TRP TRP B . n 
B 1 208 LEU 208 208 208 LEU LEU B . n 
B 1 209 TYR 209 209 209 TYR TYR B . n 
B 1 210 ALA 210 210 210 ALA ALA B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 VAL 212 212 212 VAL VAL B . n 
B 1 213 ILE 213 213 213 ILE ILE B . n 
B 1 214 ASN 214 214 214 ASN ASN B . n 
B 1 215 GLY 215 215 215 GLY GLY B . n 
B 1 216 ASP 216 216 216 ASP ASP B . n 
B 1 217 ARG 217 217 217 ARG ARG B . n 
B 1 218 TRP 218 218 218 TRP TRP B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 LEU 220 220 220 LEU LEU B . n 
B 1 221 ASN 221 221 221 ASN ASN B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 PHE 223 223 223 PHE PHE B . n 
B 1 224 THR 224 224 224 THR THR B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 ASN 228 228 228 ASN ASN B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 PHE 230 230 230 PHE PHE B . n 
B 1 231 ASN 231 231 231 ASN ASN B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 VAL 233 233 233 VAL VAL B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 MET 235 235 235 MET MET B . n 
B 1 236 LYS 236 236 236 LYS LYS B . n 
B 1 237 TYR 237 237 237 TYR TYR B . n 
B 1 238 ASN 238 238 238 ASN ASN B . n 
B 1 239 TYR 239 239 239 TYR TYR B . n 
B 1 240 GLU 240 240 240 GLU GLU B . n 
B 1 241 PRO 241 241 241 PRO PRO B . n 
B 1 242 LEU 242 242 242 LEU LEU B . n 
B 1 243 THR 243 243 243 THR THR B . n 
B 1 244 GLN 244 244 244 GLN GLN B . n 
B 1 245 ASP 245 245 245 ASP ASP B . n 
B 1 246 HIS 246 246 246 HIS HIS B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 ASP 248 248 248 ASP ASP B . n 
B 1 249 ILE 249 249 249 ILE ILE B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 PRO 252 252 252 PRO PRO B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 THR 257 257 257 THR THR B . n 
B 1 258 GLY 258 258 258 GLY GLY B . n 
B 1 259 ILE 259 259 259 ILE ILE B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 VAL 261 261 261 VAL VAL B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ASP 263 263 263 ASP ASP B . n 
B 1 264 MET 264 264 264 MET MET B . n 
B 1 265 CYS 265 265 265 CYS CYS B . n 
B 1 266 ALA 266 266 266 ALA ALA B . n 
B 1 267 SER 267 267 267 SER SER B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 LYS 269 269 269 LYS LYS B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 LEU 271 271 271 LEU LEU B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 GLN 273 273 273 GLN GLN B . n 
B 1 274 ASN 274 274 274 ASN ASN B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 MET 276 276 276 MET MET B . n 
B 1 277 ASN 277 277 277 ASN ASN B . n 
B 1 278 GLY 278 278 278 GLY GLY B . n 
B 1 279 ARG 279 279 279 ARG ARG B . n 
B 1 280 THR 280 280 280 THR THR B . n 
B 1 281 ILE 281 281 281 ILE ILE B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 GLY 283 283 283 GLY GLY B . n 
B 1 284 SER 284 284 284 SER SER B . n 
B 1 285 ALA 285 285 285 ALA ALA B . n 
B 1 286 LEU 286 286 286 LEU LEU B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 GLU 288 288 288 GLU GLU B . n 
B 1 289 ASP 289 289 289 ASP ASP B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 PHE 291 291 291 PHE PHE B . n 
B 1 292 THR 292 292 292 THR THR B . n 
B 1 293 PRO 293 293 293 PRO PRO B . n 
B 1 294 PHE 294 294 294 PHE PHE B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 VAL 296 296 296 VAL VAL B . n 
B 1 297 VAL 297 297 297 VAL VAL B . n 
B 1 298 ARG 298 298 298 ARG ARG B . n 
B 1 299 GLN 299 299 299 GLN GLN B . n 
B 1 300 CYS 300 300 300 CYS CYS B . n 
B 1 301 SER 301 301 301 SER SER B . n 
B 1 302 GLY 302 302 302 GLY GLY B . n 
B 1 303 VAL 303 303 303 VAL VAL B . n 
B 1 304 THR 304 304 304 THR THR B . n 
B 1 305 PHE 305 305 305 PHE PHE B . n 
B 1 306 GLN 306 306 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        V8X 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   V8X 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 V8X 1  401 401 V8X TGZ A . 
D 2 V8X 1  401 401 V8X TGZ B . 
E 3 HOH 1  501 73  HOH HOH A . 
E 3 HOH 2  502 89  HOH HOH A . 
E 3 HOH 3  503 84  HOH HOH A . 
E 3 HOH 4  504 39  HOH HOH A . 
E 3 HOH 5  505 75  HOH HOH A . 
E 3 HOH 6  506 45  HOH HOH A . 
E 3 HOH 7  507 3   HOH HOH A . 
E 3 HOH 8  508 13  HOH HOH A . 
E 3 HOH 9  509 64  HOH HOH A . 
E 3 HOH 10 510 70  HOH HOH A . 
E 3 HOH 11 511 18  HOH HOH A . 
E 3 HOH 12 512 38  HOH HOH A . 
E 3 HOH 13 513 12  HOH HOH A . 
E 3 HOH 14 514 87  HOH HOH A . 
E 3 HOH 15 515 15  HOH HOH A . 
E 3 HOH 16 516 5   HOH HOH A . 
E 3 HOH 17 517 25  HOH HOH A . 
E 3 HOH 18 518 24  HOH HOH A . 
E 3 HOH 19 519 9   HOH HOH A . 
E 3 HOH 20 520 6   HOH HOH A . 
E 3 HOH 21 521 27  HOH HOH A . 
E 3 HOH 22 522 49  HOH HOH A . 
E 3 HOH 23 523 42  HOH HOH A . 
E 3 HOH 24 524 11  HOH HOH A . 
E 3 HOH 25 525 61  HOH HOH A . 
E 3 HOH 26 526 65  HOH HOH A . 
E 3 HOH 27 527 69  HOH HOH A . 
E 3 HOH 28 528 86  HOH HOH A . 
E 3 HOH 29 529 81  HOH HOH A . 
E 3 HOH 30 530 76  HOH HOH A . 
E 3 HOH 31 531 20  HOH HOH A . 
E 3 HOH 32 532 22  HOH HOH A . 
E 3 HOH 33 533 4   HOH HOH A . 
E 3 HOH 34 534 35  HOH HOH A . 
E 3 HOH 35 535 33  HOH HOH A . 
E 3 HOH 36 536 23  HOH HOH A . 
E 3 HOH 37 537 28  HOH HOH A . 
E 3 HOH 38 538 80  HOH HOH A . 
E 3 HOH 39 539 88  HOH HOH A . 
E 3 HOH 40 540 54  HOH HOH A . 
E 3 HOH 41 541 78  HOH HOH A . 
E 3 HOH 42 542 37  HOH HOH A . 
E 3 HOH 43 543 79  HOH HOH A . 
E 3 HOH 44 544 59  HOH HOH A . 
E 3 HOH 45 545 74  HOH HOH A . 
E 3 HOH 46 546 10  HOH HOH A . 
E 3 HOH 47 547 29  HOH HOH A . 
E 3 HOH 48 548 85  HOH HOH A . 
F 3 HOH 1  501 83  HOH HOH B . 
F 3 HOH 2  502 56  HOH HOH B . 
F 3 HOH 3  503 32  HOH HOH B . 
F 3 HOH 4  504 53  HOH HOH B . 
F 3 HOH 5  505 31  HOH HOH B . 
F 3 HOH 6  506 8   HOH HOH B . 
F 3 HOH 7  507 21  HOH HOH B . 
F 3 HOH 8  508 57  HOH HOH B . 
F 3 HOH 9  509 91  HOH HOH B . 
F 3 HOH 10 510 1   HOH HOH B . 
F 3 HOH 11 511 17  HOH HOH B . 
F 3 HOH 12 512 41  HOH HOH B . 
F 3 HOH 13 513 2   HOH HOH B . 
F 3 HOH 14 514 7   HOH HOH B . 
F 3 HOH 15 515 52  HOH HOH B . 
F 3 HOH 16 516 55  HOH HOH B . 
F 3 HOH 17 517 16  HOH HOH B . 
F 3 HOH 18 518 14  HOH HOH B . 
F 3 HOH 19 519 19  HOH HOH B . 
F 3 HOH 20 520 82  HOH HOH B . 
F 3 HOH 21 521 67  HOH HOH B . 
F 3 HOH 22 522 62  HOH HOH B . 
F 3 HOH 23 523 34  HOH HOH B . 
F 3 HOH 24 524 40  HOH HOH B . 
F 3 HOH 25 525 30  HOH HOH B . 
F 3 HOH 26 526 26  HOH HOH B . 
F 3 HOH 27 527 43  HOH HOH B . 
F 3 HOH 28 528 60  HOH HOH B . 
F 3 HOH 29 529 77  HOH HOH B . 
F 3 HOH 30 530 36  HOH HOH B . 
F 3 HOH 31 531 46  HOH HOH B . 
F 3 HOH 32 532 71  HOH HOH B . 
F 3 HOH 33 533 51  HOH HOH B . 
F 3 HOH 34 534 50  HOH HOH B . 
F 3 HOH 35 535 48  HOH HOH B . 
F 3 HOH 36 536 90  HOH HOH B . 
F 3 HOH 37 537 58  HOH HOH B . 
F 3 HOH 38 538 72  HOH HOH B . 
F 3 HOH 39 539 63  HOH HOH B . 
F 3 HOH 40 540 92  HOH HOH B . 
F 3 HOH 41 541 47  HOH HOH B . 
F 3 HOH 42 542 68  HOH HOH B . 
# 
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 scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   101.64 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8U40 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     46.110 
_cell.length_a_esd                 ? 
_cell.length_b                     54.093 
_cell.length_b_esd                 ? 
_cell.length_c                     113.458 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8U40 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8U40 
_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             2.05 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.96 
_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              8.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M Potassium Thiocynate, 20% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     93 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-05-28 
_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   0.9795 
_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                        'SSRL BEAMLINE BL12-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-1 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8U40 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.2 
_reflns.d_resolution_low                               32.02 
_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                                     27705 
_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                           98.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.48 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.51 
_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                                0.066 
_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                                   0.9990000000000001 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.06 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_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 
_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 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_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 
2.20 2.33 ? ? ? ? ? ? 4408 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.6829999999999999   ? ? 1 1 0.9259999999999999 ? ? ? ? 0.619 ? ? ? ? ? ? 
? ? ? 
2.33 2.49 ? ? ? ? ? ? 4166 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.452                ? ? 2 1 0.9690000000000001 ? ? ? ? 0.409 ? ? ? ? ? ? 
? ? ? 
2.49 2.69 ? ? ? ? ? ? 3906 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.293                ? ? 3 1 0.988              ? ? ? ? 0.266 ? ? ? ? ? ? 
? ? ? 
2.69 2.95 ? ? ? ? ? ? 3618 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.175                ? ? 4 1 0.996              ? ? ? ? 0.159 ? ? ? ? ? ? 
? ? ? 
2.95 3.29 ? ? ? ? ? ? 3274 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.096                ? ? 5 1 0.998              ? ? ? ? 0.087 ? ? ? ? ? ? 
? ? ? 
3.29 3.8  ? ? ? ? ? ? 2837 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.06                 ? ? 6 1 0.9990000000000001 ? ? ? ? 
0.054000000000000006 ? ? ? ? ? ? ? ? ? 
3.80 4.64 ? ? ? ? ? ? 2483 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.039                ? ? 7 1 0.9990000000000001 ? ? ? ? 
0.036000000000000004 ? ? ? ? ? ? ? ? ? 
4.64 6.51 ? ? ? ? ? ? 1931 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.036000000000000004 ? ? 8 1 0.9990000000000001 ? ? ? ? 0.033 ? ? ? ? ? ? 
? ? ? 
6.51 9.55 ? ? ? ? ? ? 1082 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.031                ? ? 9 1 0.9990000000000001 ? ? ? ? 
0.027999999999999997 ? ? ? ? ? ? ? ? ? 
# 
_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                                 8U40 
_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                            2.20 
_refine.ls_d_res_low                             32.02 
_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                     27543 
_refine.ls_number_reflns_R_free                  1440 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.93 
_refine.ls_percent_reflns_R_free                 5.23 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2285 
_refine.ls_R_factor_R_free                       0.2740 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2258 
_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          SAD 
_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                 46.15 
_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                            0.28 
_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        4725 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         66 
_refine_hist.number_atoms_solvent             90 
_refine_hist.number_atoms_total               4881 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        32.02 
# 
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' ? 0.011 ? 4911 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.261 ? 6682 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.843 ? 665  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.061 ? 749  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008 ? 864  ? 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' 2.20 2.28  . . 123 2610 98.00  . . . . 0.3887 . . . . . . . . . . . 0.4275 
'X-RAY DIFFRACTION' 2.28 2.37  . . 153 2601 98.00  . . . . 0.3401 . . . . . . . . . . . 0.3911 
'X-RAY DIFFRACTION' 2.37 2.48  . . 137 2589 98.00  . . . . 0.2764 . . . . . . . . . . . 0.3860 
'X-RAY DIFFRACTION' 2.48 2.61  . . 139 2589 98.00  . . . . 0.2821 . . . . . . . . . . . 0.3337 
'X-RAY DIFFRACTION' 2.61 2.77  . . 137 2641 100.00 . . . . 0.2682 . . . . . . . . . . . 0.3548 
'X-RAY DIFFRACTION' 2.77 2.98  . . 143 2637 99.00  . . . . 0.2723 . . . . . . . . . . . 0.3829 
'X-RAY DIFFRACTION' 2.98 3.28  . . 157 2620 99.00  . . . . 0.2474 . . . . . . . . . . . 0.3000 
'X-RAY DIFFRACTION' 3.28 3.76  . . 145 2584 96.00  . . . . 0.2153 . . . . . . . . . . . 0.2965 
'X-RAY DIFFRACTION' 3.76 4.73  . . 155 2656 99.00  . . . . 0.1749 . . . . . . . . . . . 0.1968 
'X-RAY DIFFRACTION' 4.73 32.02 . . 151 2576 94.00  . . . . 0.1760 . . . . . . . . . . . 0.2091 
# 
_struct.entry_id                     8U40 
_struct.title                        'Crystal structure of main protease of SARS-CoV-2 complexed with 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        8U40 
_struct_keywords.text            'SARS-CoV-2, Main protease, inhibitor, inhibitory activity, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_struct_ref.pdbx_align_begin           3264 
# 
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 8U40 A 1 ? 306 ? P0DTD1 3264 ? 3569 ? 1 306 
2 1 8U40 B 1 ? 306 ? P0DTD1 3264 ? 3569 ? 1 306 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3140  ? 
1 MORE         -19   ? 
1 'SSA (A^2)'  24740 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_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 SER A 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 GLU A 47  ? ASN A 51  ? GLU A 47  ASN A 51  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 SER A 62  ? PHE A 66  ? SER A 62  PHE A 66  5 ? 5  
HELX_P HELX_P6  AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P8  AA8 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P9  AA9 LEU A 250 ? THR A 257 ? LEU A 250 THR A 257 1 ? 8  
HELX_P HELX_P10 AB1 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P11 AB2 THR A 292 ? GLY A 302 ? THR A 292 GLY A 302 1 ? 11 
HELX_P HELX_P12 AB3 SER B 10  ? GLY B 15  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P13 AB4 HIS B 41  ? CYS B 44  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P14 AB5 GLU B 47  ? ASN B 51  ? GLU B 47  ASN B 51  5 ? 5  
HELX_P HELX_P15 AB6 ASN B 53  ? ARG B 60  ? ASN B 53  ARG B 60  1 ? 8  
HELX_P HELX_P16 AB7 SER B 62  ? HIS B 64  ? SER B 62  HIS B 64  5 ? 3  
HELX_P HELX_P17 AB8 ILE B 200 ? ASN B 214 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P18 AB9 THR B 226 ? LYS B 236 ? THR B 226 LYS B 236 1 ? 11 
HELX_P HELX_P19 AC1 THR B 243 ? LEU B 250 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P20 AC2 LEU B 250 ? THR B 257 ? LEU B 250 THR B 257 1 ? 8  
HELX_P HELX_P21 AC3 ALA B 260 ? GLY B 275 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P22 AC4 THR B 292 ? GLY B 302 ? THR B 292 GLY B 302 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale none ? A CYS 145 SG ? ? ? 1_555 C V8X . C02 ? ? A CYS 145 A V8X 401 1_555 ? ? ? ? ? ? ? 1.782 ? ? 
covale2 covale none ? B CYS 145 SG ? ? ? 1_555 D V8X . C02 ? ? B CYS 145 B V8X 401 1_555 ? ? ? ? ? ? ? 1.786 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 V8X C . ? CYS A 145 ? V8X A 401 ? 1_555 CYS A 145 ? 1_555 C02 SG CYS 1 V8X None 'Covalent chemical modification' 
2 V8X D . ? CYS B 145 ? V8X B 401 ? 1_555 CYS B 145 ? 1_555 C02 SG CYS 1 V8X None 'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
AA5 ? 5 ? 
AA6 ? 3 ? 
# 
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 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? 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 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 LEU A 67  ? ALA A 70  ? LEU A 67  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
AA4 1 VAL B 73  ? LEU B 75  ? VAL B 73  LEU B 75  
AA4 2 PHE B 66  ? ALA B 70  ? PHE B 66  ALA B 70  
AA4 3 MET B 17  ? CYS B 22  ? MET B 17  CYS B 22  
AA4 4 THR B 25  ? LEU B 32  ? THR B 25  LEU B 32  
AA4 5 VAL B 35  ? PRO B 39  ? VAL B 35  PRO B 39  
AA4 6 VAL B 86  ? VAL B 91  ? VAL B 86  VAL B 91  
AA4 7 VAL B 77  ? GLN B 83  ? VAL B 77  GLN B 83  
AA5 1 TYR B 101 ? PHE B 103 ? TYR B 101 PHE B 103 
AA5 2 VAL B 157 ? GLU B 166 ? VAL B 157 GLU B 166 
AA5 3 VAL B 148 ? ILE B 152 ? VAL B 148 ILE B 152 
AA5 4 THR B 111 ? TYR B 118 ? THR B 111 TYR B 118 
AA5 5 SER B 121 ? ALA B 129 ? SER B 121 ALA B 129 
AA6 1 TYR B 101 ? PHE B 103 ? TYR B 101 PHE B 103 
AA6 2 VAL B 157 ? GLU B 166 ? VAL B 157 GLU B 166 
AA6 3 HIS B 172 ? THR B 175 ? HIS B 172 THR B 175 
# 
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 VAL A 73  ? O VAL A 73  N ALA A 70  ? N ALA A 70  
AA1 2 3 O LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 5 6 N CYS A 38  ? N CYS A 38  O LEU A 87  ? O LEU A 87  
AA1 6 7 O LYS A 90  ? O LYS A 90  N ILE A 78  ? N ILE A 78  
AA2 1 2 N LYS A 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 
AA3 1 2 N LYS A 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA3 2 3 N MET A 162 ? N MET A 162 O THR A 175 ? O THR A 175 
AA4 1 2 O VAL B 73  ? O VAL B 73  N ALA B 70  ? N ALA B 70  
AA4 2 3 O LEU B 67  ? O LEU B 67  N THR B 21  ? N THR B 21  
AA4 3 4 N VAL B 20  ? N VAL B 20  O LEU B 27  ? O LEU B 27  
AA4 4 5 N LEU B 30  ? N LEU B 30  O TYR B 37  ? O TYR B 37  
AA4 5 6 N CYS B 38  ? N CYS B 38  O LEU B 87  ? O LEU B 87  
AA4 6 7 O LYS B 90  ? O LYS B 90  N GLY B 79  ? N GLY B 79  
AA5 1 2 N LYS B 102 ? N LYS B 102 O PHE B 159 ? O PHE B 159 
AA5 2 3 O SER B 158 ? O SER B 158 N ASN B 151 ? N ASN B 151 
AA5 3 4 O PHE B 150 ? O PHE B 150 N SER B 113 ? N SER B 113 
AA5 4 5 N ALA B 116 ? N ALA B 116 O SER B 123 ? O SER B 123 
AA6 1 2 N LYS B 102 ? N LYS B 102 O PHE B 159 ? O PHE B 159 
AA6 2 3 N MET B 162 ? N MET B 162 O THR B 175 ? O THR B 175 
# 
_pdbx_entry_details.entry_id                   8U40 
_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   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A ASP 245 ? ? O A HOH 501 ? ? 2.09 
2 1 OD1 A ASP 245 ? ? O A HOH 501 ? ? 2.12 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 33  ? ? 52.60   -132.30 
2  1 ASN A 51  ? ? -156.84 87.63   
3  1 ASN A 84  ? ? 53.88   -129.88 
4  1 TYR A 154 ? ? 62.46   -98.48  
5  1 GLN A 189 ? ? -68.18  69.59   
6  1 ARG A 217 ? ? -140.35 -0.87   
7  1 LEU A 250 ? ? -64.13  2.90    
8  1 ASP B 33  ? ? 51.74   -134.84 
9  1 ASN B 51  ? ? -160.85 80.78   
10 1 ASN B 84  ? ? 51.66   -131.26 
11 1 TYR B 154 ? ? -154.94 -65.42  
12 1 GLN B 189 ? ? -67.71  66.09   
13 1 ASN B 238 ? ? 71.65   39.67   
14 1 GLU B 240 ? ? -36.61  122.81  
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -5.8464 
_pdbx_refine_tls.origin_y         12.7356 
_pdbx_refine_tls.origin_z         -27.8272 
_pdbx_refine_tls.T[1][1]          0.2032 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0004 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0142 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.4699 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0342 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.3711 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.9392 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.3452 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -1.0561 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.6363 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.3848 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.8469 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0850 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.4941 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.1890 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.1436 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0871 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.1965 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.1866 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.3385 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.1267 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_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   all 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     B 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     GLN 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      306 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    B 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    GLN 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     306 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
V8X C14  C Y N 372 
V8X C10  C N N 373 
V8X C12  C N N 374 
V8X C13  C Y N 375 
V8X C15  C Y N 376 
V8X C16  C Y N 377 
V8X C17  C Y N 378 
V8X F18  F N N 379 
V8X C02  C N N 380 
V8X C03  C N R 381 
V8X C05  C N N 382 
V8X C06  C N S 383 
V8X C07  C N N 384 
V8X C08  C N N 385 
V8X C09  C N N 386 
V8X C19  C Y N 387 
V8X C20  C Y N 388 
V8X C22  C Y N 389 
V8X C26  C N N 390 
V8X C27  C N N 391 
V8X C28  C N N 392 
V8X C29  C N N 393 
V8X C30  C N N 394 
V8X C32  C N N 395 
V8X F21  F N N 396 
V8X N01  N N N 397 
V8X N04  N N N 398 
V8X N11  N N N 399 
V8X N23  N Y N 400 
V8X N31  N N N 401 
V8X O24  O N N 402 
V8X O25  O N N 403 
V8X O33  O N N 404 
V8X H141 H N N 405 
V8X H102 H N N 406 
V8X H101 H N N 407 
V8X H161 H N N 408 
V8X H1   H N N 409 
V8X H031 H N N 410 
V8X H061 H N N 411 
V8X H072 H N N 412 
V8X H071 H N N 413 
V8X H081 H N N 414 
V8X H092 H N N 415 
V8X H091 H N N 416 
V8X H191 H N N 417 
V8X H262 H N N 418 
V8X H261 H N N 419 
V8X H281 H N N 420 
V8X H291 H N N 421 
V8X H301 H N N 422 
V8X H011 H N N 423 
V8X H041 H N N 424 
V8X H111 H N N 425 
V8X H3   H N N 426 
V8X H2   H N N 427 
VAL N    N N N 428 
VAL CA   C N S 429 
VAL C    C N N 430 
VAL O    O N N 431 
VAL CB   C N N 432 
VAL CG1  C N N 433 
VAL CG2  C N N 434 
VAL OXT  O N N 435 
VAL H    H N N 436 
VAL H2   H N N 437 
VAL HA   H N N 438 
VAL HB   H N N 439 
VAL HG11 H N N 440 
VAL HG12 H N N 441 
VAL HG13 H N N 442 
VAL HG21 H N N 443 
VAL HG22 H N N 444 
VAL HG23 H N N 445 
VAL HXT  H N N 446 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
V8X C09 C10  sing N N 358 
V8X C09 C08  sing N N 359 
V8X C10 C08  sing N N 360 
V8X C08 C07  sing N N 361 
V8X F18 C17  sing N N 362 
V8X C16 C17  doub Y N 363 
V8X C16 C15  sing Y N 364 
V8X C17 C19  sing Y N 365 
V8X C07 C06  sing N N 366 
V8X C15 C14  sing Y N 367 
V8X C15 C22  doub Y N 368 
V8X C14 C13  doub Y N 369 
V8X C19 C20  doub Y N 370 
V8X N11 C06  sing N N 371 
V8X N11 C12  sing N N 372 
V8X C22 C20  sing Y N 373 
V8X C22 N23  sing Y N 374 
V8X C20 F21  sing N N 375 
V8X C06 C05  sing N N 376 
V8X C13 N23  sing Y N 377 
V8X C13 C12  sing N N 378 
V8X C12 O24  doub N N 379 
V8X C05 N04  sing N N 380 
V8X C05 O25  doub N N 381 
V8X N04 C03  sing N N 382 
V8X C02 C03  sing N N 383 
V8X C02 N01  doub N N 384 
V8X C03 C26  sing N N 385 
V8X C26 C27  sing N N 386 
V8X O33 C32  doub N N 387 
V8X C27 C32  sing N N 388 
V8X C27 C28  doub N N 389 
V8X C32 N31  sing N N 390 
V8X C28 C29  sing N N 391 
V8X N31 C30  doub N N 392 
V8X C29 C30  sing N N 393 
V8X C14 H141 sing N N 394 
V8X C10 H102 sing N N 395 
V8X C10 H101 sing N N 396 
V8X C16 H161 sing N N 397 
V8X C02 H1   sing N N 398 
V8X C03 H031 sing N N 399 
V8X C06 H061 sing N N 400 
V8X C07 H072 sing N N 401 
V8X C07 H071 sing N N 402 
V8X C08 H081 sing N N 403 
V8X C09 H092 sing N N 404 
V8X C09 H091 sing N N 405 
V8X C19 H191 sing N N 406 
V8X C26 H262 sing N N 407 
V8X C26 H261 sing N N 408 
V8X C28 H281 sing N N 409 
V8X C29 H291 sing N N 410 
V8X C30 H301 sing N N 411 
V8X N01 H011 sing N N 412 
V8X N04 H041 sing N N 413 
V8X N11 H111 sing N N 414 
V8X N23 H3   sing N N 415 
V8X C29 H2   sing N N 416 
VAL N   CA   sing N N 417 
VAL N   H    sing N N 418 
VAL N   H2   sing N N 419 
VAL CA  C    sing N N 420 
VAL CA  CB   sing N N 421 
VAL CA  HA   sing N N 422 
VAL C   O    doub N N 423 
VAL C   OXT  sing N N 424 
VAL CB  CG1  sing N N 425 
VAL CB  CG2  sing N N 426 
VAL CB  HB   sing N N 427 
VAL CG1 HG11 sing N N 428 
VAL CG1 HG12 sing N N 429 
VAL CG1 HG13 sing N N 430 
VAL CG2 HG21 sing N N 431 
VAL CG2 HG22 sing N N 432 
VAL CG2 HG23 sing N N 433 
VAL OXT HXT  sing N N 434 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Canadian Institutes of Health Research (CIHR)'                     Canada ? 1 
'Natural Sciences and Engineering Research Council (NSERC, Canada)' Canada ? 2 
# 
_atom_sites.entry_id                    8U40 
_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]   0.021687 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004468 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018487 
_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]   0.008999 
_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 
F 
H 
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    . SER A 1 1   ? -21.759 16.709  -22.140 1.00 44.81  ? 1   SER A N    1 
ATOM   2    C CA   . SER A 1 1   ? -21.252 18.007  -22.570 1.00 49.28  ? 1   SER A CA   1 
ATOM   3    C C    . SER A 1 1   ? -19.705 18.043  -22.549 1.00 49.82  ? 1   SER A C    1 
ATOM   4    O O    . SER A 1 1   ? -19.075 17.183  -21.938 1.00 45.00  ? 1   SER A O    1 
ATOM   5    C CB   . SER A 1 1   ? -21.835 19.100  -21.668 1.00 50.86  ? 1   SER A CB   1 
ATOM   6    O OG   . SER A 1 1   ? -21.338 20.369  -22.041 1.00 56.40  ? 1   SER A OG   1 
ATOM   7    N N    . GLY A 1 2   ? -19.114 19.047  -23.183 1.00 49.21  ? 2   GLY A N    1 
ATOM   8    C CA   . GLY A 1 2   ? -17.674 19.206  -23.283 1.00 46.36  ? 2   GLY A CA   1 
ATOM   9    C C    . GLY A 1 2   ? -17.168 18.770  -24.647 1.00 46.79  ? 2   GLY A C    1 
ATOM   10   O O    . GLY A 1 2   ? -17.778 17.943  -25.335 1.00 47.02  ? 2   GLY A O    1 
ATOM   11   N N    . PHE A 1 3   ? -16.029 19.315  -25.057 1.00 47.39  ? 3   PHE A N    1 
ATOM   12   C CA   . PHE A 1 3   ? -15.611 19.080  -26.435 1.00 45.08  ? 3   PHE A CA   1 
ATOM   13   C C    . PHE A 1 3   ? -14.097 19.075  -26.512 1.00 45.38  ? 3   PHE A C    1 
ATOM   14   O O    . PHE A 1 3   ? -13.465 20.106  -26.275 1.00 44.67  ? 3   PHE A O    1 
ATOM   15   C CB   . PHE A 1 3   ? -16.200 20.137  -27.383 1.00 43.76  ? 3   PHE A CB   1 
ATOM   16   C CG   . PHE A 1 3   ? -16.199 19.696  -28.795 1.00 42.30  ? 3   PHE A CG   1 
ATOM   17   C CD1  . PHE A 1 3   ? -17.076 18.719  -29.224 1.00 44.36  ? 3   PHE A CD1  1 
ATOM   18   C CD2  . PHE A 1 3   ? -15.253 20.174  -29.678 1.00 43.36  ? 3   PHE A CD2  1 
ATOM   19   C CE1  . PHE A 1 3   ? -17.061 18.275  -30.539 1.00 42.11  ? 3   PHE A CE1  1 
ATOM   20   C CE2  . PHE A 1 3   ? -15.218 19.730  -30.984 1.00 45.82  ? 3   PHE A CE2  1 
ATOM   21   C CZ   . PHE A 1 3   ? -16.133 18.773  -31.413 1.00 46.51  ? 3   PHE A CZ   1 
ATOM   22   N N    . ARG A 1 4   ? -13.527 17.925  -26.893 1.00 46.25  ? 4   ARG A N    1 
ATOM   23   C CA   . ARG A 1 4   ? -12.085 17.707  -26.872 1.00 44.76  ? 4   ARG A CA   1 
ATOM   24   C C    . ARG A 1 4   ? -11.603 17.145  -28.190 1.00 43.91  ? 4   ARG A C    1 
ATOM   25   O O    . ARG A 1 4   ? -12.320 16.408  -28.869 1.00 43.71  ? 4   ARG A O    1 
ATOM   26   C CB   . ARG A 1 4   ? -11.675 16.711  -25.787 1.00 44.11  ? 4   ARG A CB   1 
ATOM   27   C CG   . ARG A 1 4   ? -12.340 16.954  -24.501 1.00 44.54  ? 4   ARG A CG   1 
ATOM   28   C CD   . ARG A 1 4   ? -11.500 17.955  -23.726 1.00 53.00  ? 4   ARG A CD   1 
ATOM   29   N NE   . ARG A 1 4   ? -10.086 17.869  -24.074 1.00 48.97  ? 4   ARG A NE   1 
ATOM   30   C CZ   . ARG A 1 4   ? -9.187  17.271  -23.300 1.00 54.93  ? 4   ARG A CZ   1 
ATOM   31   N NH1  . ARG A 1 4   ? -9.539  16.717  -22.142 1.00 48.07  ? 4   ARG A NH1  1 
ATOM   32   N NH2  . ARG A 1 4   ? -7.908  17.224  -23.692 1.00 52.59  ? 4   ARG A NH2  1 
ATOM   33   N N    . LYS A 1 5   ? -10.352 17.457  -28.513 1.00 44.86  ? 5   LYS A N    1 
ATOM   34   C CA   . LYS A 1 5   ? -9.647  16.677  -29.511 1.00 43.76  ? 5   LYS A CA   1 
ATOM   35   C C    . LYS A 1 5   ? -9.582  15.236  -29.013 1.00 42.56  ? 5   LYS A C    1 
ATOM   36   O O    . LYS A 1 5   ? -8.941  14.935  -27.998 1.00 45.79  ? 5   LYS A O    1 
ATOM   37   C CB   . LYS A 1 5   ? -8.255  17.265  -29.758 1.00 43.61  ? 5   LYS A CB   1 
ATOM   38   C CG   . LYS A 1 5   ? -8.053  17.708  -31.158 1.00 44.77  ? 5   LYS A CG   1 
ATOM   39   C CD   . LYS A 1 5   ? -7.060  18.844  -31.239 1.00 58.07  ? 5   LYS A CD   1 
ATOM   40   C CE   . LYS A 1 5   ? -7.245  19.621  -32.536 1.00 52.35  ? 5   LYS A CE   1 
ATOM   41   N NZ   . LYS A 1 5   ? -6.515  20.921  -32.482 1.00 60.00  ? 5   LYS A NZ   1 
ATOM   42   N N    . MET A 1 6   ? -10.258 14.341  -29.711 1.00 39.01  ? 6   MET A N    1 
ATOM   43   C CA   . MET A 1 6   ? -10.393 12.959  -29.294 1.00 40.73  ? 6   MET A CA   1 
ATOM   44   C C    . MET A 1 6   ? -9.869  12.040  -30.373 1.00 38.42  ? 6   MET A C    1 
ATOM   45   O O    . MET A 1 6   ? -10.369 12.064  -31.493 1.00 40.00  ? 6   MET A O    1 
ATOM   46   C CB   . MET A 1 6   ? -11.835 12.588  -29.033 1.00 40.59  ? 6   MET A CB   1 
ATOM   47   C CG   . MET A 1 6   ? -12.020 11.863  -27.766 1.00 43.48  ? 6   MET A CG   1 
ATOM   48   S SD   . MET A 1 6   ? -13.783 11.806  -27.460 1.00 53.66  ? 6   MET A SD   1 
ATOM   49   C CE   . MET A 1 6   ? -14.259 10.851  -28.885 1.00 50.02  ? 6   MET A CE   1 
ATOM   50   N N    . ALA A 1 7   ? -8.933  11.179  -30.009 1.00 35.54  ? 7   ALA A N    1 
ATOM   51   C CA   . ALA A 1 7   ? -8.465  10.143  -30.910 1.00 36.30  ? 7   ALA A CA   1 
ATOM   52   C C    . ALA A 1 7   ? -9.349  8.897   -30.831 1.00 40.01  ? 7   ALA A C    1 
ATOM   53   O O    . ALA A 1 7   ? -10.007 8.641   -29.825 1.00 40.82  ? 7   ALA A O    1 
ATOM   54   C CB   . ALA A 1 7   ? -7.030  9.776   -30.557 1.00 33.02  ? 7   ALA A CB   1 
ATOM   55   N N    . PHE A 1 8   ? -9.303  8.082   -31.882 1.00 39.87  ? 8   PHE A N    1 
ATOM   56   C CA   . PHE A 1 8   ? -9.934  6.768   -31.835 1.00 39.55  ? 8   PHE A CA   1 
ATOM   57   C C    . PHE A 1 8   ? -9.213  5.848   -30.853 1.00 39.35  ? 8   PHE A C    1 
ATOM   58   O O    . PHE A 1 8   ? -8.000  5.972   -30.642 1.00 36.94  ? 8   PHE A O    1 
ATOM   59   C CB   . PHE A 1 8   ? -9.911  6.122   -33.215 1.00 42.34  ? 8   PHE A CB   1 
ATOM   60   C CG   . PHE A 1 8   ? -10.889 6.728   -34.189 1.00 45.00  ? 8   PHE A CG   1 
ATOM   61   C CD1  . PHE A 1 8   ? -12.221 6.426   -34.126 1.00 54.89  ? 8   PHE A CD1  1 
ATOM   62   C CD2  . PHE A 1 8   ? -10.470 7.662   -35.096 1.00 42.53  ? 8   PHE A CD2  1 
ATOM   63   C CE1  . PHE A 1 8   ? -13.106 7.005   -35.000 1.00 57.64  ? 8   PHE A CE1  1 
ATOM   64   C CE2  . PHE A 1 8   ? -11.336 8.248   -35.962 1.00 49.89  ? 8   PHE A CE2  1 
ATOM   65   C CZ   . PHE A 1 8   ? -12.662 7.917   -35.920 1.00 56.11  ? 8   PHE A CZ   1 
ATOM   66   N N    . PRO A 1 9   ? -9.920  4.864   -30.296 1.00 39.99  ? 9   PRO A N    1 
ATOM   67   C CA   . PRO A 1 9   ? -9.236  3.827   -29.511 1.00 37.65  ? 9   PRO A CA   1 
ATOM   68   C C    . PRO A 1 9   ? -8.194  3.127   -30.378 1.00 39.92  ? 9   PRO A C    1 
ATOM   69   O O    . PRO A 1 9   ? -8.431  2.827   -31.547 1.00 41.20  ? 9   PRO A O    1 
ATOM   70   C CB   . PRO A 1 9   ? -10.368 2.877   -29.093 1.00 40.69  ? 9   PRO A CB   1 
ATOM   71   C CG   . PRO A 1 9   ? -11.649 3.564   -29.474 1.00 44.65  ? 9   PRO A CG   1 
ATOM   72   C CD   . PRO A 1 9   ? -11.324 4.527   -30.567 1.00 43.50  ? 9   PRO A CD   1 
ATOM   73   N N    . SER A 1 10  ? -7.023  2.900   -29.809 1.00 38.79  ? 10  SER A N    1 
ATOM   74   C CA   . SER A 1 10  ? -5.861  2.526   -30.591 1.00 37.14  ? 10  SER A CA   1 
ATOM   75   C C    . SER A 1 10  ? -5.553  1.039   -30.497 1.00 38.86  ? 10  SER A C    1 
ATOM   76   O O    . SER A 1 10  ? -4.519  0.603   -31.016 1.00 38.95  ? 10  SER A O    1 
ATOM   77   C CB   . SER A 1 10  ? -4.657  3.367   -30.147 1.00 35.33  ? 10  SER A CB   1 
ATOM   78   O OG   . SER A 1 10  ? -4.177  2.963   -28.858 1.00 40.05  ? 10  SER A OG   1 
ATOM   79   N N    . GLY A 1 11  ? -6.428  0.256   -29.847 1.00 38.39  ? 11  GLY A N    1 
ATOM   80   C CA   . GLY A 1 11  ? -6.139  -1.156  -29.599 1.00 36.71  ? 11  GLY A CA   1 
ATOM   81   C C    . GLY A 1 11  ? -5.860  -1.951  -30.863 1.00 37.96  ? 11  GLY A C    1 
ATOM   82   O O    . GLY A 1 11  ? -4.840  -2.639  -30.962 1.00 44.21  ? 11  GLY A O    1 
ATOM   83   N N    . LYS A 1 12  ? -6.778  -1.888  -31.837 1.00 41.35  ? 12  LYS A N    1 
ATOM   84   C CA   . LYS A 1 12  ? -6.649  -2.681  -33.064 1.00 42.17  ? 12  LYS A CA   1 
ATOM   85   C C    . LYS A 1 12  ? -5.369  -2.336  -33.839 1.00 40.42  ? 12  LYS A C    1 
ATOM   86   O O    . LYS A 1 12  ? -4.840  -3.167  -34.584 1.00 41.40  ? 12  LYS A O    1 
ATOM   87   C CB   . LYS A 1 12  ? -7.877  -2.445  -33.955 1.00 43.33  ? 12  LYS A CB   1 
ATOM   88   C CG   . LYS A 1 12  ? -9.124  -3.164  -33.526 1.00 43.07  ? 12  LYS A CG   1 
ATOM   89   C CD   . LYS A 1 12  ? -10.284 -2.179  -33.371 1.00 54.39  ? 12  LYS A CD   1 
ATOM   90   C CE   . LYS A 1 12  ? -10.352 -1.564  -31.942 1.00 58.13  ? 12  LYS A CE   1 
ATOM   91   N NZ   . LYS A 1 12  ? -11.528 -0.622  -31.733 1.00 58.15  ? 12  LYS A NZ   1 
ATOM   92   N N    . VAL A 1 13  ? -4.867  -1.118  -33.689 1.00 38.08  ? 13  VAL A N    1 
ATOM   93   C CA   . VAL A 1 13  ? -3.637  -0.732  -34.365 1.00 40.12  ? 13  VAL A CA   1 
ATOM   94   C C    . VAL A 1 13  ? -2.430  -1.184  -33.567 1.00 44.14  ? 13  VAL A C    1 
ATOM   95   O O    . VAL A 1 13  ? -1.399  -1.545  -34.143 1.00 47.62  ? 13  VAL A O    1 
ATOM   96   C CB   . VAL A 1 13  ? -3.631  0.779   -34.613 1.00 40.25  ? 13  VAL A CB   1 
ATOM   97   C CG1  . VAL A 1 13  ? -2.365  1.208   -35.424 1.00 39.95  ? 13  VAL A CG1  1 
ATOM   98   C CG2  . VAL A 1 13  ? -4.896  1.170   -35.319 1.00 35.33  ? 13  VAL A CG2  1 
ATOM   99   N N    . GLU A 1 14  ? -2.528  -1.218  -32.238 1.00 40.91  ? 14  GLU A N    1 
ATOM   100  C CA   . GLU A 1 14  ? -1.364  -1.625  -31.461 1.00 42.92  ? 14  GLU A CA   1 
ATOM   101  C C    . GLU A 1 14  ? -0.899  -3.017  -31.864 1.00 44.27  ? 14  GLU A C    1 
ATOM   102  O O    . GLU A 1 14  ? 0.312   -3.281  -31.943 1.00 43.22  ? 14  GLU A O    1 
ATOM   103  C CB   . GLU A 1 14  ? -1.677  -1.580  -29.956 1.00 40.99  ? 14  GLU A CB   1 
ATOM   104  C CG   . GLU A 1 14  ? -2.007  -0.140  -29.430 1.00 40.83  ? 14  GLU A CG   1 
ATOM   105  C CD   . GLU A 1 14  ? -2.491  -0.134  -27.974 1.00 40.58  ? 14  GLU A CD   1 
ATOM   106  O OE1  . GLU A 1 14  ? -1.803  -0.702  -27.102 1.00 47.58  ? 14  GLU A OE1  1 
ATOM   107  O OE2  . GLU A 1 14  ? -3.558  0.435   -27.707 1.00 40.71  ? 14  GLU A OE2  1 
ATOM   108  N N    . GLY A 1 15  ? -1.841  -3.936  -32.086 1.00 44.38  ? 15  GLY A N    1 
ATOM   109  C CA   . GLY A 1 15  ? -1.477  -5.315  -32.418 1.00 45.62  ? 15  GLY A CA   1 
ATOM   110  C C    . GLY A 1 15  ? -0.794  -5.482  -33.771 1.00 47.80  ? 15  GLY A C    1 
ATOM   111  O O    . GLY A 1 15  ? -0.344  -6.588  -34.084 1.00 45.45  ? 15  GLY A O    1 
ATOM   112  N N    . CYS A 1 16  ? -0.699  -4.404  -34.554 1.00 43.85  ? 16  CYS A N    1 
ATOM   113  C CA   . CYS A 1 16  ? -0.098  -4.409  -35.873 1.00 43.71  ? 16  CYS A CA   1 
ATOM   114  C C    . CYS A 1 16  ? 1.272   -3.739  -35.939 1.00 47.56  ? 16  CYS A C    1 
ATOM   115  O O    . CYS A 1 16  ? 1.829   -3.658  -37.040 1.00 47.07  ? 16  CYS A O    1 
ATOM   116  C CB   . CYS A 1 16  ? -1.016  -3.723  -36.896 1.00 44.01  ? 16  CYS A CB   1 
ATOM   117  S SG   . CYS A 1 16  ? -2.745  -4.314  -36.930 1.00 48.84  ? 16  CYS A SG   1 
ATOM   118  N N    . MET A 1 17  ? 1.838   -3.243  -34.830 1.00 43.77  ? 17  MET A N    1 
ATOM   119  C CA   . MET A 1 17  ? 3.097   -2.508  -34.918 1.00 44.70  ? 17  MET A CA   1 
ATOM   120  C C    . MET A 1 17  ? 4.282   -3.406  -34.624 1.00 46.69  ? 17  MET A C    1 
ATOM   121  O O    . MET A 1 17  ? 4.330   -4.094  -33.598 1.00 48.97  ? 17  MET A O    1 
ATOM   122  C CB   . MET A 1 17  ? 3.132   -1.258  -34.035 1.00 46.29  ? 17  MET A CB   1 
ATOM   123  C CG   . MET A 1 17  ? 1.862   -0.477  -34.143 1.00 41.11  ? 17  MET A CG   1 
ATOM   124  S SD   . MET A 1 17  ? 1.771   0.360   -35.739 1.00 44.60  ? 17  MET A SD   1 
ATOM   125  C CE   . MET A 1 17  ? 3.481   0.869   -36.066 1.00 40.47  ? 17  MET A CE   1 
ATOM   126  N N    . VAL A 1 18  ? 5.230   -3.405  -35.548 1.00 47.07  ? 18  VAL A N    1 
ATOM   127  C CA   . VAL A 1 18  ? 6.472   -4.132  -35.401 1.00 50.93  ? 18  VAL A CA   1 
ATOM   128  C C    . VAL A 1 18  ? 7.613   -3.152  -35.636 1.00 50.39  ? 18  VAL A C    1 
ATOM   129  O O    . VAL A 1 18  ? 7.410   -2.002  -36.041 1.00 47.86  ? 18  VAL A O    1 
ATOM   130  C CB   . VAL A 1 18  ? 6.560   -5.334  -36.367 1.00 53.31  ? 18  VAL A CB   1 
ATOM   131  C CG1  . VAL A 1 18  ? 5.313   -6.201  -36.254 1.00 53.81  ? 18  VAL A CG1  1 
ATOM   132  C CG2  . VAL A 1 18  ? 6.730   -4.853  -37.795 1.00 47.31  ? 18  VAL A CG2  1 
ATOM   133  N N    . GLN A 1 19  ? 8.824   -3.624  -35.360 1.00 54.18  ? 19  GLN A N    1 
ATOM   134  C CA   . GLN A 1 19  ? 10.044  -2.873  -35.607 1.00 54.55  ? 19  GLN A CA   1 
ATOM   135  C C    . GLN A 1 19  ? 10.789  -3.524  -36.763 1.00 56.30  ? 19  GLN A C    1 
ATOM   136  O O    . GLN A 1 19  ? 10.975  -4.746  -36.783 1.00 57.51  ? 19  GLN A O    1 
ATOM   137  C CB   . GLN A 1 19  ? 10.933  -2.813  -34.358 1.00 54.54  ? 19  GLN A CB   1 
ATOM   138  C CG   . GLN A 1 19  ? 11.668  -4.075  -34.051 1.00 65.29  ? 19  GLN A CG   1 
ATOM   139  C CD   . GLN A 1 19  ? 12.991  -3.814  -33.352 1.00 72.64  ? 19  GLN A CD   1 
ATOM   140  O OE1  . GLN A 1 19  ? 14.024  -4.426  -33.680 1.00 74.49  ? 19  GLN A OE1  1 
ATOM   141  N NE2  . GLN A 1 19  ? 12.974  -2.889  -32.392 1.00 69.15  ? 19  GLN A NE2  1 
ATOM   142  N N    . VAL A 1 20  ? 11.172  -2.720  -37.744 1.00 54.93  ? 20  VAL A N    1 
ATOM   143  C CA   . VAL A 1 20  ? 11.898  -3.201  -38.908 1.00 52.62  ? 20  VAL A CA   1 
ATOM   144  C C    . VAL A 1 20  ? 13.310  -2.657  -38.854 1.00 54.17  ? 20  VAL A C    1 
ATOM   145  O O    . VAL A 1 20  ? 13.512  -1.441  -38.737 1.00 48.20  ? 20  VAL A O    1 
ATOM   146  C CB   . VAL A 1 20  ? 11.221  -2.783  -40.218 1.00 50.46  ? 20  VAL A CB   1 
ATOM   147  C CG1  . VAL A 1 20  ? 12.044  -3.279  -41.387 1.00 48.31  ? 20  VAL A CG1  1 
ATOM   148  C CG2  . VAL A 1 20  ? 9.820   -3.343  -40.267 1.00 50.08  ? 20  VAL A CG2  1 
ATOM   149  N N    . THR A 1 21  ? 14.282  -3.554  -38.964 1.00 54.35  ? 21  THR A N    1 
ATOM   150  C CA   . THR A 1 21  ? 15.689  -3.197  -38.945 1.00 58.24  ? 21  THR A CA   1 
ATOM   151  C C    . THR A 1 21  ? 16.351  -3.611  -40.253 1.00 57.93  ? 21  THR A C    1 
ATOM   152  O O    . THR A 1 21  ? 16.276  -4.778  -40.654 1.00 58.41  ? 21  THR A O    1 
ATOM   153  C CB   . THR A 1 21  ? 16.400  -3.868  -37.773 1.00 61.10  ? 21  THR A CB   1 
ATOM   154  O OG1  . THR A 1 21  ? 15.615  -3.690  -36.586 1.00 62.47  ? 21  THR A OG1  1 
ATOM   155  C CG2  . THR A 1 21  ? 17.806  -3.271  -37.596 1.00 58.96  ? 21  THR A CG2  1 
ATOM   156  N N    . CYS A 1 22  ? 17.002  -2.655  -40.907 1.00 59.10  ? 22  CYS A N    1 
ATOM   157  C CA   . CYS A 1 22  ? 17.845  -2.912  -42.067 1.00 59.77  ? 22  CYS A CA   1 
ATOM   158  C C    . CYS A 1 22  ? 19.215  -2.305  -41.826 1.00 60.09  ? 22  CYS A C    1 
ATOM   159  O O    . CYS A 1 22  ? 19.334  -1.082  -41.700 1.00 61.33  ? 22  CYS A O    1 
ATOM   160  C CB   . CYS A 1 22  ? 17.235  -2.325  -43.342 1.00 58.41  ? 22  CYS A CB   1 
ATOM   161  S SG   . CYS A 1 22  ? 18.096  -2.920  -44.801 1.00 63.28  ? 22  CYS A SG   1 
ATOM   162  N N    . GLY A 1 23  ? 20.235  -3.144  -41.751 1.00 67.96  ? 23  GLY A N    1 
ATOM   163  C CA   . GLY A 1 23  ? 21.557  -2.623  -41.443 1.00 72.46  ? 23  GLY A CA   1 
ATOM   164  C C    . GLY A 1 23  ? 21.561  -1.947  -40.082 1.00 70.42  ? 23  GLY A C    1 
ATOM   165  O O    . GLY A 1 23  ? 21.261  -2.565  -39.046 1.00 64.73  ? 23  GLY A O    1 
ATOM   166  N N    . THR A 1 24  ? 21.936  -0.665  -40.071 1.00 69.31  ? 24  THR A N    1 
ATOM   167  C CA   . THR A 1 24  ? 21.908  0.124   -38.848 1.00 72.90  ? 24  THR A CA   1 
ATOM   168  C C    . THR A 1 24  ? 20.570  0.796   -38.566 1.00 68.90  ? 24  THR A C    1 
ATOM   169  O O    . THR A 1 24  ? 20.326  1.191   -37.422 1.00 71.60  ? 24  THR A O    1 
ATOM   170  C CB   . THR A 1 24  ? 22.941  1.236   -38.925 1.00 86.20  ? 24  THR A CB   1 
ATOM   171  O OG1  . THR A 1 24  ? 23.202  1.720   -37.606 1.00 92.68  ? 24  THR A OG1  1 
ATOM   172  C CG2  . THR A 1 24  ? 22.400  2.395   -39.781 1.00 83.47  ? 24  THR A CG2  1 
ATOM   173  N N    . THR A 1 25  ? 19.690  0.895   -39.552 1.00 61.55  ? 25  THR A N    1 
ATOM   174  C CA   . THR A 1 25  ? 18.436  1.615   -39.399 1.00 58.33  ? 25  THR A CA   1 
ATOM   175  C C    . THR A 1 25  ? 17.352  0.741   -38.791 1.00 57.19  ? 25  THR A C    1 
ATOM   176  O O    . THR A 1 25  ? 17.235  -0.442  -39.125 1.00 56.43  ? 25  THR A O    1 
ATOM   177  C CB   . THR A 1 25  ? 17.969  2.153   -40.746 1.00 57.99  ? 25  THR A CB   1 
ATOM   178  O OG1  . THR A 1 25  ? 18.957  3.055   -41.264 1.00 65.72  ? 25  THR A OG1  1 
ATOM   179  C CG2  . THR A 1 25  ? 16.643  2.863   -40.602 1.00 53.85  ? 25  THR A CG2  1 
ATOM   180  N N    . THR A 1 26  ? 16.550  1.337   -37.904 1.00 55.03  ? 26  THR A N    1 
ATOM   181  C CA   . THR A 1 26  ? 15.378  0.663   -37.362 1.00 51.17  ? 26  THR A CA   1 
ATOM   182  C C    . THR A 1 26  ? 14.242  1.666   -37.262 1.00 49.24  ? 26  THR A C    1 
ATOM   183  O O    . THR A 1 26  ? 14.402  2.759   -36.711 1.00 48.15  ? 26  THR A O    1 
ATOM   184  C CB   . THR A 1 26  ? 15.651  0.040   -35.984 1.00 53.97  ? 26  THR A CB   1 
ATOM   185  O OG1  . THR A 1 26  ? 16.561  -1.058  -36.116 1.00 61.71  ? 26  THR A OG1  1 
ATOM   186  C CG2  . THR A 1 26  ? 14.365  -0.499  -35.377 1.00 53.06  ? 26  THR A CG2  1 
ATOM   187  N N    . LEU A 1 27  ? 13.097  1.294   -37.813 1.00 49.31  ? 27  LEU A N    1 
ATOM   188  C CA   . LEU A 1 27  ? 11.915  2.119   -37.728 1.00 43.93  ? 27  LEU A CA   1 
ATOM   189  C C    . LEU A 1 27  ? 10.716  1.196   -37.567 1.00 45.60  ? 27  LEU A C    1 
ATOM   190  O O    . LEU A 1 27  ? 10.858  -0.028  -37.446 1.00 43.53  ? 27  LEU A O    1 
ATOM   191  C CB   . LEU A 1 27  ? 11.814  3.033   -38.946 1.00 46.90  ? 27  LEU A CB   1 
ATOM   192  C CG   . LEU A 1 27  ? 12.219  2.467   -40.307 1.00 46.75  ? 27  LEU A CG   1 
ATOM   193  C CD1  . LEU A 1 27  ? 11.311  1.323   -40.680 1.00 47.20  ? 27  LEU A CD1  1 
ATOM   194  C CD2  . LEU A 1 27  ? 12.201  3.550   -41.373 1.00 42.25  ? 27  LEU A CD2  1 
ATOM   195  N N    . ASN A 1 28  ? 9.526   1.783   -37.568 1.00 40.08  ? 28  ASN A N    1 
ATOM   196  C CA   . ASN A 1 28  ? 8.323   1.004   -37.318 1.00 43.33  ? 28  ASN A CA   1 
ATOM   197  C C    . ASN A 1 28  ? 7.730   0.514   -38.626 1.00 42.89  ? 28  ASN A C    1 
ATOM   198  O O    . ASN A 1 28  ? 7.908   1.138   -39.674 1.00 41.69  ? 28  ASN A O    1 
ATOM   199  C CB   . ASN A 1 28  ? 7.291   1.828   -36.537 1.00 40.89  ? 28  ASN A CB   1 
ATOM   200  C CG   . ASN A 1 28  ? 7.918   2.529   -35.333 1.00 44.69  ? 28  ASN A CG   1 
ATOM   201  O OD1  . ASN A 1 28  ? 8.266   1.890   -34.328 1.00 51.00  ? 28  ASN A OD1  1 
ATOM   202  N ND2  . ASN A 1 28  ? 8.109   3.831   -35.450 1.00 42.42  ? 28  ASN A ND2  1 
ATOM   203  N N    . GLY A 1 29  ? 7.041   -0.624  -38.552 1.00 42.34  ? 29  GLY A N    1 
ATOM   204  C CA   . GLY A 1 29  ? 6.285   -1.129  -39.676 1.00 41.51  ? 29  GLY A CA   1 
ATOM   205  C C    . GLY A 1 29  ? 4.919   -1.631  -39.243 1.00 44.60  ? 29  GLY A C    1 
ATOM   206  O O    . GLY A 1 29  ? 4.673   -1.902  -38.060 1.00 42.88  ? 29  GLY A O    1 
ATOM   207  N N    . LEU A 1 30  ? 4.040   -1.789  -40.236 1.00 42.22  ? 30  LEU A N    1 
ATOM   208  C CA   . LEU A 1 30  ? 2.657   -2.205  -40.023 1.00 43.38  ? 30  LEU A CA   1 
ATOM   209  C C    . LEU A 1 30  ? 2.449   -3.642  -40.527 1.00 42.61  ? 30  LEU A C    1 
ATOM   210  O O    . LEU A 1 30  ? 2.576   -3.912  -41.725 1.00 41.89  ? 30  LEU A O    1 
ATOM   211  C CB   . LEU A 1 30  ? 1.730   -1.233  -40.739 1.00 40.27  ? 30  LEU A CB   1 
ATOM   212  C CG   . LEU A 1 30  ? 0.217   -1.373  -40.550 1.00 40.55  ? 30  LEU A CG   1 
ATOM   213  C CD1  . LEU A 1 30  ? -0.236  -0.751  -39.253 1.00 40.76  ? 30  LEU A CD1  1 
ATOM   214  C CD2  . LEU A 1 30  ? -0.475  -0.704  -41.706 1.00 35.97  ? 30  LEU A CD2  1 
ATOM   215  N N    . TRP A 1 31  ? 2.115   -4.554  -39.616 1.00 44.46  ? 31  TRP A N    1 
ATOM   216  C CA   . TRP A 1 31  ? 2.001   -5.992  -39.902 1.00 46.20  ? 31  TRP A CA   1 
ATOM   217  C C    . TRP A 1 31  ? 0.530   -6.363  -40.112 1.00 48.54  ? 31  TRP A C    1 
ATOM   218  O O    . TRP A 1 31  ? -0.248  -6.473  -39.152 1.00 48.87  ? 31  TRP A O    1 
ATOM   219  C CB   . TRP A 1 31  ? 2.622   -6.796  -38.766 1.00 46.11  ? 31  TRP A CB   1 
ATOM   220  C CG   . TRP A 1 31  ? 2.699   -8.272  -38.987 1.00 54.07  ? 31  TRP A CG   1 
ATOM   221  C CD1  . TRP A 1 31  ? 2.664   -8.934  -40.180 1.00 54.03  ? 31  TRP A CD1  1 
ATOM   222  C CD2  . TRP A 1 31  ? 2.839   -9.280  -37.972 1.00 56.84  ? 31  TRP A CD2  1 
ATOM   223  N NE1  . TRP A 1 31  ? 2.775   -10.297 -39.970 1.00 55.84  ? 31  TRP A NE1  1 
ATOM   224  C CE2  . TRP A 1 31  ? 2.883   -10.531 -38.623 1.00 59.01  ? 31  TRP A CE2  1 
ATOM   225  C CE3  . TRP A 1 31  ? 2.933   -9.246  -36.581 1.00 53.34  ? 31  TRP A CE3  1 
ATOM   226  C CZ2  . TRP A 1 31  ? 2.997   -11.732 -37.923 1.00 61.48  ? 31  TRP A CZ2  1 
ATOM   227  C CZ3  . TRP A 1 31  ? 3.068   -10.442 -35.890 1.00 60.49  ? 31  TRP A CZ3  1 
ATOM   228  C CH2  . TRP A 1 31  ? 3.096   -11.667 -36.560 1.00 59.37  ? 31  TRP A CH2  1 
ATOM   229  N N    . LEU A 1 32  ? 0.154   -6.556  -41.374 1.00 48.84  ? 32  LEU A N    1 
ATOM   230  C CA   . LEU A 1 32  ? -1.185  -6.980  -41.770 1.00 50.27  ? 32  LEU A CA   1 
ATOM   231  C C    . LEU A 1 32  ? -1.084  -8.257  -42.605 1.00 55.37  ? 32  LEU A C    1 
ATOM   232  O O    . LEU A 1 32  ? -0.344  -8.306  -43.598 1.00 51.45  ? 32  LEU A O    1 
ATOM   233  C CB   . LEU A 1 32  ? -1.873  -5.871  -42.550 1.00 45.73  ? 32  LEU A CB   1 
ATOM   234  C CG   . LEU A 1 32  ? -2.009  -4.582  -41.725 1.00 46.76  ? 32  LEU A CG   1 
ATOM   235  C CD1  . LEU A 1 32  ? -2.216  -3.423  -42.615 1.00 39.04  ? 32  LEU A CD1  1 
ATOM   236  C CD2  . LEU A 1 32  ? -3.158  -4.676  -40.727 1.00 45.25  ? 32  LEU A CD2  1 
ATOM   237  N N    . ASP A 1 33  ? -1.812  -9.291  -42.196 1.00 53.11  ? 33  ASP A N    1 
ATOM   238  C CA   . ASP A 1 33  ? -1.726  -10.612 -42.845 1.00 54.56  ? 33  ASP A CA   1 
ATOM   239  C C    . ASP A 1 33  ? -0.247  -10.993 -42.870 1.00 55.96  ? 33  ASP A C    1 
ATOM   240  O O    . ASP A 1 33  ? 0.412   -10.907 -41.826 1.00 56.59  ? 33  ASP A O    1 
ATOM   241  C CB   . ASP A 1 33  ? -2.413  -10.578 -44.209 1.00 55.35  ? 33  ASP A CB   1 
ATOM   242  C CG   . ASP A 1 33  ? -3.870  -10.167 -44.116 1.00 54.85  ? 33  ASP A CG   1 
ATOM   243  O OD1  . ASP A 1 33  ? -4.598  -10.832 -43.346 1.00 61.11  ? 33  ASP A OD1  1 
ATOM   244  O OD2  . ASP A 1 33  ? -4.280  -9.183  -44.785 1.00 60.31  ? 33  ASP A OD2  1 
ATOM   245  N N    . ASP A 1 34  ? 0.293   -11.448 -44.002 1.00 57.01  ? 34  ASP A N    1 
ATOM   246  C CA   . ASP A 1 34  ? 1.679   -11.886 -44.098 1.00 60.04  ? 34  ASP A CA   1 
ATOM   247  C C    . ASP A 1 34  ? 2.567   -10.848 -44.788 1.00 56.34  ? 34  ASP A C    1 
ATOM   248  O O    . ASP A 1 34  ? 3.584   -11.202 -45.400 1.00 58.79  ? 34  ASP A O    1 
ATOM   249  C CB   . ASP A 1 34  ? 1.777   -13.274 -44.763 1.00 62.09  ? 34  ASP A CB   1 
ATOM   250  C CG   . ASP A 1 34  ? 1.375   -13.291 -46.250 1.00 64.25  ? 34  ASP A CG   1 
ATOM   251  O OD1  . ASP A 1 34  ? 0.567   -12.433 -46.688 1.00 58.98  ? 34  ASP A OD1  1 
ATOM   252  O OD2  . ASP A 1 34  ? 1.875   -14.200 -46.972 1.00 66.07  ? 34  ASP A OD2  1 
ATOM   253  N N    . VAL A 1 35  ? 2.232   -9.563  -44.634 1.00 55.40  ? 35  VAL A N    1 
ATOM   254  C CA   . VAL A 1 35  ? 2.977   -8.452  -45.220 1.00 51.13  ? 35  VAL A CA   1 
ATOM   255  C C    . VAL A 1 35  ? 3.239   -7.396  -44.147 1.00 52.08  ? 35  VAL A C    1 
ATOM   256  O O    . VAL A 1 35  ? 2.330   -7.021  -43.397 1.00 50.78  ? 35  VAL A O    1 
ATOM   257  C CB   . VAL A 1 35  ? 2.199   -7.820  -46.391 1.00 50.62  ? 35  VAL A CB   1 
ATOM   258  C CG1  . VAL A 1 35  ? 2.946   -6.611  -46.946 1.00 49.04  ? 35  VAL A CG1  1 
ATOM   259  C CG2  . VAL A 1 35  ? 1.922   -8.853  -47.490 1.00 55.34  ? 35  VAL A CG2  1 
ATOM   260  N N    . VAL A 1 36  ? 4.473   -6.902  -44.093 1.00 49.40  ? 36  VAL A N    1 
ATOM   261  C CA   . VAL A 1 36  ? 4.870   -5.807  -43.216 1.00 45.28  ? 36  VAL A CA   1 
ATOM   262  C C    . VAL A 1 36  ? 5.120   -4.583  -44.086 1.00 47.01  ? 36  VAL A C    1 
ATOM   263  O O    . VAL A 1 36  ? 5.859   -4.663  -45.076 1.00 47.14  ? 36  VAL A O    1 
ATOM   264  C CB   . VAL A 1 36  ? 6.123   -6.175  -42.399 1.00 46.17  ? 36  VAL A CB   1 
ATOM   265  C CG1  . VAL A 1 36  ? 6.682   -4.954  -41.634 1.00 43.41  ? 36  VAL A CG1  1 
ATOM   266  C CG2  . VAL A 1 36  ? 5.796   -7.281  -41.423 1.00 46.36  ? 36  VAL A CG2  1 
ATOM   267  N N    . TYR A 1 37  ? 4.533   -3.453  -43.714 1.00 40.60  ? 37  TYR A N    1 
ATOM   268  C CA   . TYR A 1 37  ? 4.653   -2.199  -44.465 1.00 39.95  ? 37  TYR A CA   1 
ATOM   269  C C    . TYR A 1 37  ? 5.512   -1.215  -43.691 1.00 41.44  ? 37  TYR A C    1 
ATOM   270  O O    . TYR A 1 37  ? 5.214   -0.934  -42.525 1.00 42.37  ? 37  TYR A O    1 
ATOM   271  C CB   . TYR A 1 37  ? 3.286   -1.557  -44.726 1.00 37.23  ? 37  TYR A CB   1 
ATOM   272  C CG   . TYR A 1 37  ? 2.344   -2.472  -45.446 1.00 45.09  ? 37  TYR A CG   1 
ATOM   273  C CD1  . TYR A 1 37  ? 1.826   -3.594  -44.816 1.00 45.36  ? 37  TYR A CD1  1 
ATOM   274  C CD2  . TYR A 1 37  ? 1.976   -2.227  -46.760 1.00 45.29  ? 37  TYR A CD2  1 
ATOM   275  C CE1  . TYR A 1 37  ? 0.976   -4.456  -45.469 1.00 47.43  ? 37  TYR A CE1  1 
ATOM   276  C CE2  . TYR A 1 37  ? 1.106   -3.089  -47.427 1.00 48.98  ? 37  TYR A CE2  1 
ATOM   277  C CZ   . TYR A 1 37  ? 0.617   -4.205  -46.776 1.00 49.83  ? 37  TYR A CZ   1 
ATOM   278  O OH   . TYR A 1 37  ? -0.226  -5.086  -47.418 1.00 53.18  ? 37  TYR A OH   1 
ATOM   279  N N    . CYS A 1 38  ? 6.520   -0.637  -44.344 1.00 39.60  ? 38  CYS A N    1 
ATOM   280  C CA   . CYS A 1 38  ? 7.380   0.322   -43.662 1.00 38.74  ? 38  CYS A CA   1 
ATOM   281  C C    . CYS A 1 38  ? 7.955   1.316   -44.657 1.00 42.40  ? 38  CYS A C    1 
ATOM   282  O O    . CYS A 1 38  ? 7.910   1.088   -45.871 1.00 40.34  ? 38  CYS A O    1 
ATOM   283  C CB   . CYS A 1 38  ? 8.500   -0.381  -42.898 1.00 40.92  ? 38  CYS A CB   1 
ATOM   284  S SG   . CYS A 1 38  ? 9.870   -0.931  -43.915 1.00 46.29  ? 38  CYS A SG   1 
ATOM   285  N N    . PRO A 1 39  ? 8.435   2.467   -44.179 1.00 40.83  ? 39  PRO A N    1 
ATOM   286  C CA   . PRO A 1 39  ? 8.999   3.462   -45.098 1.00 38.95  ? 39  PRO A CA   1 
ATOM   287  C C    . PRO A 1 39  ? 10.233  2.917   -45.805 1.00 40.97  ? 39  PRO A C    1 
ATOM   288  O O    . PRO A 1 39  ? 11.067  2.216   -45.212 1.00 40.32  ? 39  PRO A O    1 
ATOM   289  C CB   . PRO A 1 39  ? 9.342   4.640   -44.180 1.00 39.20  ? 39  PRO A CB   1 
ATOM   290  C CG   . PRO A 1 39  ? 8.445   4.419   -42.922 1.00 41.03  ? 39  PRO A CG   1 
ATOM   291  C CD   . PRO A 1 39  ? 8.420   2.926   -42.779 1.00 39.79  ? 39  PRO A CD   1 
ATOM   292  N N    . ARG A 1 40  ? 10.346  3.217   -47.096 1.00 37.42  ? 40  ARG A N    1 
ATOM   293  C CA   . ARG A 1 40  ? 11.457  2.609   -47.824 1.00 42.66  ? 40  ARG A CA   1 
ATOM   294  C C    . ARG A 1 40  ? 12.809  3.133   -47.359 1.00 40.97  ? 40  ARG A C    1 
ATOM   295  O O    . ARG A 1 40  ? 13.824  2.480   -47.607 1.00 44.05  ? 40  ARG A O    1 
ATOM   296  C CB   . ARG A 1 40  ? 11.298  2.818   -49.340 1.00 44.34  ? 40  ARG A CB   1 
ATOM   297  C CG   . ARG A 1 40  ? 11.300  4.260   -49.825 1.00 40.29  ? 40  ARG A CG   1 
ATOM   298  C CD   . ARG A 1 40  ? 11.560  4.308   -51.311 1.00 43.54  ? 40  ARG A CD   1 
ATOM   299  N NE   . ARG A 1 40  ? 11.454  5.652   -51.882 1.00 39.99  ? 40  ARG A NE   1 
ATOM   300  C CZ   . ARG A 1 40  ? 11.377  5.890   -53.187 1.00 42.47  ? 40  ARG A CZ   1 
ATOM   301  N NH1  . ARG A 1 40  ? 11.407  4.900   -54.075 1.00 41.03  ? 40  ARG A NH1  1 
ATOM   302  N NH2  . ARG A 1 40  ? 11.252  7.145   -53.615 1.00 36.15  ? 40  ARG A NH2  1 
ATOM   303  N N    . HIS A 1 41  ? 12.864  4.256   -46.646 1.00 41.69  ? 41  HIS A N    1 
ATOM   304  C CA   . HIS A 1 41  ? 14.197  4.771   -46.351 1.00 42.96  ? 41  HIS A CA   1 
ATOM   305  C C    . HIS A 1 41  ? 14.859  4.024   -45.214 1.00 43.83  ? 41  HIS A C    1 
ATOM   306  O O    . HIS A 1 41  ? 15.993  4.366   -44.851 1.00 44.84  ? 41  HIS A O    1 
ATOM   307  C CB   . HIS A 1 41  ? 14.169  6.283   -46.068 1.00 43.97  ? 41  HIS A CB   1 
ATOM   308  C CG   . HIS A 1 41  ? 13.488  6.668   -44.792 1.00 47.13  ? 41  HIS A CG   1 
ATOM   309  N ND1  . HIS A 1 41  ? 14.032  6.421   -43.548 1.00 50.54  ? 41  HIS A ND1  1 
ATOM   310  C CD2  . HIS A 1 41  ? 12.285  7.246   -44.568 1.00 46.86  ? 41  HIS A CD2  1 
ATOM   311  C CE1  . HIS A 1 41  ? 13.212  6.876   -42.615 1.00 48.09  ? 41  HIS A CE1  1 
ATOM   312  N NE2  . HIS A 1 41  ? 12.153  7.396   -43.207 1.00 46.42  ? 41  HIS A NE2  1 
ATOM   313  N N    . VAL A 1 42  ? 14.225  2.966   -44.708 1.00 40.61  ? 42  VAL A N    1 
ATOM   314  C CA   . VAL A 1 42  ? 14.946  2.071   -43.813 1.00 47.41  ? 42  VAL A CA   1 
ATOM   315  C C    . VAL A 1 42  ? 16.141  1.414   -44.510 1.00 50.86  ? 42  VAL A C    1 
ATOM   316  O O    . VAL A 1 42  ? 17.086  0.988   -43.836 1.00 46.65  ? 42  VAL A O    1 
ATOM   317  C CB   . VAL A 1 42  ? 14.014  1.010   -43.209 1.00 39.33  ? 42  VAL A CB   1 
ATOM   318  C CG1  . VAL A 1 42  ? 13.478  0.061   -44.289 1.00 44.21  ? 42  VAL A CG1  1 
ATOM   319  C CG2  . VAL A 1 42  ? 14.768  0.195   -42.149 1.00 47.72  ? 42  VAL A CG2  1 
ATOM   320  N N    . ILE A 1 43  ? 16.152  1.332   -45.846 1.00 47.89  ? 43  ILE A N    1 
ATOM   321  C CA   . ILE A 1 43  ? 17.333  0.737   -46.483 1.00 54.25  ? 43  ILE A CA   1 
ATOM   322  C C    . ILE A 1 43  ? 18.473  1.732   -46.668 1.00 50.66  ? 43  ILE A C    1 
ATOM   323  O O    . ILE A 1 43  ? 19.566  1.336   -47.076 1.00 50.70  ? 43  ILE A O    1 
ATOM   324  C CB   . ILE A 1 43  ? 17.017  0.096   -47.850 1.00 51.64  ? 43  ILE A CB   1 
ATOM   325  C CG1  . ILE A 1 43  ? 16.776  1.188   -48.897 1.00 50.49  ? 43  ILE A CG1  1 
ATOM   326  C CG2  . ILE A 1 43  ? 15.812  -0.888  -47.731 1.00 50.14  ? 43  ILE A CG2  1 
ATOM   327  C CD1  . ILE A 1 43  ? 16.023  0.722   -50.137 1.00 53.85  ? 43  ILE A CD1  1 
ATOM   328  N N    . CYS A 1 44  ? 18.284  3.003   -46.348 1.00 50.15  ? 44  CYS A N    1 
ATOM   329  C CA   . CYS A 1 44  ? 19.366  3.949   -46.539 1.00 56.43  ? 44  CYS A CA   1 
ATOM   330  C C    . CYS A 1 44  ? 20.225  4.044   -45.293 1.00 64.29  ? 44  CYS A C    1 
ATOM   331  O O    . CYS A 1 44  ? 19.750  3.885   -44.166 1.00 64.68  ? 44  CYS A O    1 
ATOM   332  C CB   . CYS A 1 44  ? 18.837  5.325   -46.885 1.00 56.07  ? 44  CYS A CB   1 
ATOM   333  S SG   . CYS A 1 44  ? 17.773  5.288   -48.297 1.00 50.53  ? 44  CYS A SG   1 
ATOM   334  N N    . THR A 1 45  ? 21.503  4.313   -45.515 1.00 70.78  ? 45  THR A N    1 
ATOM   335  C CA   . THR A 1 45  ? 22.447  4.544   -44.438 1.00 78.52  ? 45  THR A CA   1 
ATOM   336  C C    . THR A 1 45  ? 22.463  6.033   -44.111 1.00 82.98  ? 45  THR A C    1 
ATOM   337  O O    . THR A 1 45  ? 21.582  6.796   -44.516 1.00 80.53  ? 45  THR A O    1 
ATOM   338  C CB   . THR A 1 45  ? 23.837  4.045   -44.815 1.00 79.18  ? 45  THR A CB   1 
ATOM   339  O OG1  . THR A 1 45  ? 24.373  4.894   -45.831 1.00 83.65  ? 45  THR A OG1  1 
ATOM   340  C CG2  . THR A 1 45  ? 23.771  2.620   -45.327 1.00 75.22  ? 45  THR A CG2  1 
ATOM   341  N N    . SER A 1 46  ? 23.481  6.462   -43.369 1.00 90.96  ? 46  SER A N    1 
ATOM   342  C CA   . SER A 1 46  ? 23.579  7.866   -42.997 1.00 93.89  ? 46  SER A CA   1 
ATOM   343  C C    . SER A 1 46  ? 23.793  8.760   -44.220 1.00 94.12  ? 46  SER A C    1 
ATOM   344  O O    . SER A 1 46  ? 23.163  9.821   -44.336 1.00 87.81  ? 46  SER A O    1 
ATOM   345  C CB   . SER A 1 46  ? 24.693  8.045   -41.973 1.00 90.40  ? 46  SER A CB   1 
ATOM   346  O OG   . SER A 1 46  ? 24.507  9.267   -41.295 1.00 94.44  ? 46  SER A OG   1 
ATOM   347  N N    . GLU A 1 47  ? 24.695  8.363   -45.130 1.00 93.77  ? 47  GLU A N    1 
ATOM   348  C CA   . GLU A 1 47  ? 24.980  9.172   -46.315 1.00 91.69  ? 47  GLU A CA   1 
ATOM   349  C C    . GLU A 1 47  ? 23.921  9.005   -47.399 1.00 86.38  ? 47  GLU A C    1 
ATOM   350  O O    . GLU A 1 47  ? 23.521  9.995   -48.022 1.00 89.48  ? 47  GLU A O    1 
ATOM   351  C CB   . GLU A 1 47  ? 26.363  8.844   -46.880 1.00 98.36  ? 47  GLU A CB   1 
ATOM   352  C CG   . GLU A 1 47  ? 26.627  7.371   -47.160 1.00 102.52 ? 47  GLU A CG   1 
ATOM   353  C CD   . GLU A 1 47  ? 27.257  6.659   -45.969 1.00 108.72 ? 47  GLU A CD   1 
ATOM   354  O OE1  . GLU A 1 47  ? 27.255  7.245   -44.865 1.00 109.66 ? 47  GLU A OE1  1 
ATOM   355  O OE2  . GLU A 1 47  ? 27.766  5.525   -46.136 1.00 110.15 ? 47  GLU A OE2  1 
ATOM   356  N N    . ASP A 1 48  ? 23.451  7.777   -47.642 1.00 80.73  ? 48  ASP A N    1 
ATOM   357  C CA   . ASP A 1 48  ? 22.501  7.515   -48.726 1.00 74.64  ? 48  ASP A CA   1 
ATOM   358  C C    . ASP A 1 48  ? 21.380  8.556   -48.828 1.00 67.24  ? 48  ASP A C    1 
ATOM   359  O O    . ASP A 1 48  ? 20.913  8.845   -49.937 1.00 60.33  ? 48  ASP A O    1 
ATOM   360  C CB   . ASP A 1 48  ? 21.882  6.120   -48.574 1.00 74.34  ? 48  ASP A CB   1 
ATOM   361  C CG   . ASP A 1 48  ? 22.852  4.990   -48.948 1.00 78.79  ? 48  ASP A CG   1 
ATOM   362  O OD1  . ASP A 1 48  ? 23.692  5.196   -49.862 1.00 76.78  ? 48  ASP A OD1  1 
ATOM   363  O OD2  . ASP A 1 48  ? 22.752  3.887   -48.336 1.00 77.15  ? 48  ASP A OD2  1 
ATOM   364  N N    . MET A 1 49  ? 20.985  9.167   -47.693 1.00 72.59  ? 49  MET A N    1 
ATOM   365  C CA   . MET A 1 49  ? 19.787  10.014  -47.614 1.00 63.72  ? 49  MET A CA   1 
ATOM   366  C C    . MET A 1 49  ? 19.916  11.287  -48.441 1.00 57.51  ? 49  MET A C    1 
ATOM   367  O O    . MET A 1 49  ? 18.898  11.857  -48.855 1.00 53.08  ? 49  MET A O    1 
ATOM   368  C CB   . MET A 1 49  ? 19.480  10.383  -46.161 1.00 65.71  ? 49  MET A CB   1 
ATOM   369  C CG   . MET A 1 49  ? 18.945  9.248   -45.307 1.00 64.82  ? 49  MET A CG   1 
ATOM   370  S SD   . MET A 1 49  ? 17.404  8.494   -45.874 1.00 69.93  ? 49  MET A SD   1 
ATOM   371  C CE   . MET A 1 49  ? 16.612  9.838   -46.771 1.00 55.56  ? 49  MET A CE   1 
ATOM   372  N N    . LEU A 1 50  ? 21.135  11.736  -48.711 1.00 60.56  ? 50  LEU A N    1 
ATOM   373  C CA   . LEU A 1 50  ? 21.315  13.013  -49.395 1.00 63.56  ? 50  LEU A CA   1 
ATOM   374  C C    . LEU A 1 50  ? 20.577  13.039  -50.740 1.00 63.15  ? 50  LEU A C    1 
ATOM   375  O O    . LEU A 1 50  ? 19.864  14.001  -51.046 1.00 62.92  ? 50  LEU A O    1 
ATOM   376  C CB   . LEU A 1 50  ? 22.803  13.293  -49.544 1.00 61.69  ? 50  LEU A CB   1 
ATOM   377  C CG   . LEU A 1 50  ? 23.242  14.756  -49.667 1.00 75.13  ? 50  LEU A CG   1 
ATOM   378  C CD1  . LEU A 1 50  ? 24.765  14.853  -49.858 1.00 75.68  ? 50  LEU A CD1  1 
ATOM   379  C CD2  . LEU A 1 50  ? 22.496  15.467  -50.793 1.00 79.28  ? 50  LEU A CD2  1 
ATOM   380  N N    . ASN A 1 51  ? 20.746  11.996  -51.569 1.00 62.12  ? 51  ASN A N    1 
ATOM   381  C CA   . ASN A 1 51  ? 19.893  11.770  -52.746 1.00 61.26  ? 51  ASN A CA   1 
ATOM   382  C C    . ASN A 1 51  ? 19.964  10.287  -53.091 1.00 56.22  ? 51  ASN A C    1 
ATOM   383  O O    . ASN A 1 51  ? 20.805  9.862   -53.896 1.00 53.50  ? 51  ASN A O    1 
ATOM   384  C CB   . ASN A 1 51  ? 20.318  12.617  -53.949 1.00 63.43  ? 51  ASN A CB   1 
ATOM   385  C CG   . ASN A 1 51  ? 21.820  12.792  -54.034 1.00 74.35  ? 51  ASN A CG   1 
ATOM   386  O OD1  . ASN A 1 51  ? 22.577  11.896  -53.638 1.00 74.09  ? 51  ASN A OD1  1 
ATOM   387  N ND2  . ASN A 1 51  ? 22.268  13.953  -54.531 1.00 79.98  ? 51  ASN A ND2  1 
ATOM   388  N N    . PRO A 1 52  ? 19.118  9.463   -52.501 1.00 53.44  ? 52  PRO A N    1 
ATOM   389  C CA   . PRO A 1 52  ? 19.292  8.018   -52.668 1.00 53.30  ? 52  PRO A CA   1 
ATOM   390  C C    . PRO A 1 52  ? 18.762  7.551   -54.014 1.00 49.67  ? 52  PRO A C    1 
ATOM   391  O O    . PRO A 1 52  ? 17.766  8.051   -54.529 1.00 46.73  ? 52  PRO A O    1 
ATOM   392  C CB   . PRO A 1 52  ? 18.488  7.431   -51.499 1.00 52.85  ? 52  PRO A CB   1 
ATOM   393  C CG   . PRO A 1 52  ? 17.371  8.464   -51.240 1.00 50.72  ? 52  PRO A CG   1 
ATOM   394  C CD   . PRO A 1 52  ? 17.907  9.814   -51.733 1.00 54.92  ? 52  PRO A CD   1 
ATOM   395  N N    . ASN A 1 53  ? 19.451  6.596   -54.603 1.00 49.98  ? 53  ASN A N    1 
ATOM   396  C CA   . ASN A 1 53  ? 18.845  5.833   -55.685 1.00 52.73  ? 53  ASN A CA   1 
ATOM   397  C C    . ASN A 1 53  ? 18.234  4.581   -55.062 1.00 50.37  ? 53  ASN A C    1 
ATOM   398  O O    . ASN A 1 53  ? 18.936  3.601   -54.791 1.00 47.75  ? 53  ASN A O    1 
ATOM   399  C CB   . ASN A 1 53  ? 19.875  5.517   -56.764 1.00 51.58  ? 53  ASN A CB   1 
ATOM   400  C CG   . ASN A 1 53  ? 19.224  5.063   -58.038 1.00 54.46  ? 53  ASN A CG   1 
ATOM   401  O OD1  . ASN A 1 53  ? 18.332  4.198   -58.022 1.00 53.65  ? 53  ASN A OD1  1 
ATOM   402  N ND2  . ASN A 1 53  ? 19.596  5.698   -59.145 1.00 54.56  ? 53  ASN A ND2  1 
ATOM   403  N N    . TYR A 1 54  ? 16.924  4.602   -54.829 1.00 47.26  ? 54  TYR A N    1 
ATOM   404  C CA   . TYR A 1 54  ? 16.310  3.517   -54.061 1.00 48.94  ? 54  TYR A CA   1 
ATOM   405  C C    . TYR A 1 54  ? 16.305  2.197   -54.835 1.00 51.85  ? 54  TYR A C    1 
ATOM   406  O O    . TYR A 1 54  ? 16.609  1.133   -54.276 1.00 51.40  ? 54  TYR A O    1 
ATOM   407  C CB   . TYR A 1 54  ? 14.889  3.904   -53.641 1.00 48.54  ? 54  TYR A CB   1 
ATOM   408  C CG   . TYR A 1 54  ? 14.844  4.882   -52.469 1.00 47.93  ? 54  TYR A CG   1 
ATOM   409  C CD1  . TYR A 1 54  ? 15.132  4.455   -51.169 1.00 45.73  ? 54  TYR A CD1  1 
ATOM   410  C CD2  . TYR A 1 54  ? 14.527  6.238   -52.666 1.00 43.89  ? 54  TYR A CD2  1 
ATOM   411  C CE1  . TYR A 1 54  ? 15.099  5.339   -50.097 1.00 45.31  ? 54  TYR A CE1  1 
ATOM   412  C CE2  . TYR A 1 54  ? 14.483  7.128   -51.590 1.00 45.87  ? 54  TYR A CE2  1 
ATOM   413  C CZ   . TYR A 1 54  ? 14.768  6.664   -50.304 1.00 45.24  ? 54  TYR A CZ   1 
ATOM   414  O OH   . TYR A 1 54  ? 14.742  7.540   -49.237 1.00 44.35  ? 54  TYR A OH   1 
ATOM   415  N N    . GLU A 1 55  ? 15.931  2.234   -56.115 1.00 51.56  ? 55  GLU A N    1 
ATOM   416  C CA   . GLU A 1 55  ? 15.984  1.022   -56.926 1.00 53.10  ? 55  GLU A CA   1 
ATOM   417  C C    . GLU A 1 55  ? 17.357  0.380   -56.811 1.00 46.98  ? 55  GLU A C    1 
ATOM   418  O O    . GLU A 1 55  ? 17.484  -0.772  -56.376 1.00 49.50  ? 55  GLU A O    1 
ATOM   419  C CB   . GLU A 1 55  ? 15.634  1.324   -58.386 1.00 53.97  ? 55  GLU A CB   1 
ATOM   420  C CG   . GLU A 1 55  ? 14.295  2.037   -58.550 1.00 60.18  ? 55  GLU A CG   1 
ATOM   421  C CD   . GLU A 1 55  ? 14.294  3.471   -57.963 1.00 66.81  ? 55  GLU A CD   1 
ATOM   422  O OE1  . GLU A 1 55  ? 15.254  3.832   -57.235 1.00 67.26  ? 55  GLU A OE1  1 
ATOM   423  O OE2  . GLU A 1 55  ? 13.331  4.234   -58.220 1.00 67.04  ? 55  GLU A OE2  1 
ATOM   424  N N    . ASP A 1 56  ? 18.408  1.146   -57.106 1.00 49.78  ? 56  ASP A N    1 
ATOM   425  C CA   . ASP A 1 56  ? 19.769  0.627   -56.951 1.00 54.14  ? 56  ASP A CA   1 
ATOM   426  C C    . ASP A 1 56  ? 20.036  0.181   -55.518 1.00 54.15  ? 56  ASP A C    1 
ATOM   427  O O    . ASP A 1 56  ? 20.751  -0.806  -55.287 1.00 52.97  ? 56  ASP A O    1 
ATOM   428  C CB   . ASP A 1 56  ? 20.816  1.674   -57.353 1.00 58.35  ? 56  ASP A CB   1 
ATOM   429  C CG   . ASP A 1 56  ? 20.892  1.911   -58.856 1.00 56.92  ? 56  ASP A CG   1 
ATOM   430  O OD1  . ASP A 1 56  ? 20.053  1.375   -59.613 1.00 54.67  ? 56  ASP A OD1  1 
ATOM   431  O OD2  . ASP A 1 56  ? 21.793  2.679   -59.263 1.00 58.29  ? 56  ASP A OD2  1 
ATOM   432  N N    . LEU A 1 57  ? 19.546  0.951   -54.534 1.00 52.93  ? 57  LEU A N    1 
ATOM   433  C CA   . LEU A 1 57  ? 19.854  0.626   -53.143 1.00 53.15  ? 57  LEU A CA   1 
ATOM   434  C C    . LEU A 1 57  ? 19.175  -0.674  -52.726 1.00 50.88  ? 57  LEU A C    1 
ATOM   435  O O    . LEU A 1 57  ? 19.786  -1.520  -52.060 1.00 52.30  ? 57  LEU A O    1 
ATOM   436  C CB   . LEU A 1 57  ? 19.455  1.796   -52.237 1.00 53.74  ? 57  LEU A CB   1 
ATOM   437  C CG   . LEU A 1 57  ? 20.593  2.829   -52.085 1.00 58.65  ? 57  LEU A CG   1 
ATOM   438  C CD1  . LEU A 1 57  ? 20.188  4.013   -51.194 1.00 56.82  ? 57  LEU A CD1  1 
ATOM   439  C CD2  . LEU A 1 57  ? 21.864  2.149   -51.561 1.00 54.69  ? 57  LEU A CD2  1 
ATOM   440  N N    . LEU A 1 58  ? 17.926  -0.863  -53.148 1.00 52.23  ? 58  LEU A N    1 
ATOM   441  C CA   . LEU A 1 58  ? 17.184  -2.080  -52.831 1.00 54.32  ? 58  LEU A CA   1 
ATOM   442  C C    . LEU A 1 58  ? 17.730  -3.294  -53.587 1.00 53.15  ? 58  LEU A C    1 
ATOM   443  O O    . LEU A 1 58  ? 17.672  -4.423  -53.082 1.00 54.54  ? 58  LEU A O    1 
ATOM   444  C CB   . LEU A 1 58  ? 15.698  -1.856  -53.147 1.00 49.09  ? 58  LEU A CB   1 
ATOM   445  C CG   . LEU A 1 58  ? 14.763  -3.009  -52.812 1.00 51.87  ? 58  LEU A CG   1 
ATOM   446  C CD1  . LEU A 1 58  ? 14.927  -3.366  -51.359 1.00 52.95  ? 58  LEU A CD1  1 
ATOM   447  C CD2  . LEU A 1 58  ? 13.329  -2.610  -53.113 1.00 47.19  ? 58  LEU A CD2  1 
ATOM   448  N N    . ILE A 1 59  ? 18.278  -3.087  -54.788 1.00 55.72  ? 59  ILE A N    1 
ATOM   449  C CA   . ILE A 1 59  ? 18.879  -4.208  -55.509 1.00 51.51  ? 59  ILE A CA   1 
ATOM   450  C C    . ILE A 1 59  ? 20.020  -4.794  -54.704 1.00 53.65  ? 59  ILE A C    1 
ATOM   451  O O    . ILE A 1 59  ? 20.178  -6.018  -54.642 1.00 58.87  ? 59  ILE A O    1 
ATOM   452  C CB   . ILE A 1 59  ? 19.309  -3.772  -56.919 1.00 51.21  ? 59  ILE A CB   1 
ATOM   453  C CG1  . ILE A 1 59  ? 18.059  -3.765  -57.801 1.00 48.97  ? 59  ILE A CG1  1 
ATOM   454  C CG2  . ILE A 1 59  ? 20.430  -4.702  -57.484 1.00 51.53  ? 59  ILE A CG2  1 
ATOM   455  C CD1  . ILE A 1 59  ? 18.179  -2.920  -59.021 1.00 52.05  ? 59  ILE A CD1  1 
ATOM   456  N N    . ARG A 1 60  ? 20.774  -3.946  -53.991 1.00 53.83  ? 60  ARG A N    1 
ATOM   457  C CA   . ARG A 1 60  ? 21.859  -4.461  -53.158 1.00 53.25  ? 60  ARG A CA   1 
ATOM   458  C C    . ARG A 1 60  ? 21.364  -5.187  -51.899 1.00 60.57  ? 60  ARG A C    1 
ATOM   459  O O    . ARG A 1 60  ? 22.181  -5.815  -51.217 1.00 56.97  ? 60  ARG A O    1 
ATOM   460  C CB   . ARG A 1 60  ? 22.817  -3.328  -52.746 1.00 62.72  ? 60  ARG A CB   1 
ATOM   461  C CG   . ARG A 1 60  ? 23.894  -2.879  -53.781 1.00 72.05  ? 60  ARG A CG   1 
ATOM   462  C CD   . ARG A 1 60  ? 23.604  -1.453  -54.322 1.00 76.74  ? 60  ARG A CD   1 
ATOM   463  N NE   . ARG A 1 60  ? 24.643  -0.941  -55.218 1.00 84.44  ? 60  ARG A NE   1 
ATOM   464  C CZ   . ARG A 1 60  ? 24.439  -0.535  -56.468 1.00 80.38  ? 60  ARG A CZ   1 
ATOM   465  N NH1  . ARG A 1 60  ? 23.242  -0.608  -57.035 1.00 72.70  ? 60  ARG A NH1  1 
ATOM   466  N NH2  . ARG A 1 60  ? 25.465  -0.049  -57.172 1.00 79.87  ? 60  ARG A NH2  1 
ATOM   467  N N    . LYS A 1 61  ? 20.072  -5.108  -51.557 1.00 59.41  ? 61  LYS A N    1 
ATOM   468  C CA   . LYS A 1 61  ? 19.536  -5.814  -50.396 1.00 62.88  ? 61  LYS A CA   1 
ATOM   469  C C    . LYS A 1 61  ? 18.910  -7.141  -50.803 1.00 62.66  ? 61  LYS A C    1 
ATOM   470  O O    . LYS A 1 61  ? 18.320  -7.268  -51.883 1.00 62.53  ? 61  LYS A O    1 
ATOM   471  C CB   . LYS A 1 61  ? 18.468  -4.990  -49.648 1.00 59.31  ? 61  LYS A CB   1 
ATOM   472  C CG   . LYS A 1 61  ? 18.902  -3.634  -49.110 1.00 58.42  ? 61  LYS A CG   1 
ATOM   473  C CD   . LYS A 1 61  ? 19.820  -3.781  -47.926 1.00 60.14  ? 61  LYS A CD   1 
ATOM   474  C CE   . LYS A 1 61  ? 20.722  -2.585  -47.819 1.00 57.21  ? 61  LYS A CE   1 
ATOM   475  N NZ   . LYS A 1 61  ? 21.328  -2.626  -46.474 1.00 66.52  ? 61  LYS A NZ   1 
ATOM   476  N N    . SER A 1 62  ? 19.026  -8.118  -49.902 1.00 60.12  ? 62  SER A N    1 
ATOM   477  C CA   . SER A 1 62  ? 18.394  -9.427  -50.001 1.00 63.66  ? 62  SER A CA   1 
ATOM   478  C C    . SER A 1 62  ? 17.434  -9.592  -48.828 1.00 66.44  ? 62  SER A C    1 
ATOM   479  O O    . SER A 1 62  ? 17.316  -8.715  -47.965 1.00 65.55  ? 62  SER A O    1 
ATOM   480  C CB   . SER A 1 62  ? 19.422  -10.565 -50.044 1.00 65.02  ? 62  SER A CB   1 
ATOM   481  O OG   . SER A 1 62  ? 20.324  -10.418 -51.132 1.00 67.35  ? 62  SER A OG   1 
ATOM   482  N N    . ASN A 1 63  ? 16.738  -10.733 -48.816 1.00 66.28  ? 63  ASN A N    1 
ATOM   483  C CA   . ASN A 1 63  ? 15.698  -10.955 -47.819 1.00 64.93  ? 63  ASN A CA   1 
ATOM   484  C C    . ASN A 1 63  ? 16.271  -10.948 -46.405 1.00 65.57  ? 63  ASN A C    1 
ATOM   485  O O    . ASN A 1 63  ? 15.653  -10.399 -45.487 1.00 65.85  ? 63  ASN A O    1 
ATOM   486  C CB   . ASN A 1 63  ? 14.975  -12.272 -48.089 1.00 62.50  ? 63  ASN A CB   1 
ATOM   487  C CG   . ASN A 1 63  ? 13.877  -12.129 -49.126 1.00 63.97  ? 63  ASN A CG   1 
ATOM   488  O OD1  . ASN A 1 63  ? 13.283  -11.066 -49.290 1.00 58.32  ? 63  ASN A OD1  1 
ATOM   489  N ND2  . ASN A 1 63  ? 13.573  -13.226 -49.804 1.00 68.58  ? 63  ASN A ND2  1 
ATOM   490  N N    . HIS A 1 64  ? 17.448  -11.550 -46.202 1.00 67.51  ? 64  HIS A N    1 
ATOM   491  C CA   . HIS A 1 64  ? 17.969  -11.695 -44.843 1.00 68.08  ? 64  HIS A CA   1 
ATOM   492  C C    . HIS A 1 64  ? 18.611  -10.416 -44.301 1.00 67.84  ? 64  HIS A C    1 
ATOM   493  O O    . HIS A 1 64  ? 19.061  -10.405 -43.150 1.00 66.69  ? 64  HIS A O    1 
ATOM   494  C CB   . HIS A 1 64  ? 18.961  -12.859 -44.751 1.00 68.89  ? 64  HIS A CB   1 
ATOM   495  C CG   . HIS A 1 64  ? 20.109  -12.785 -45.703 1.00 72.47  ? 64  HIS A CG   1 
ATOM   496  N ND1  . HIS A 1 64  ? 20.966  -11.707 -45.752 1.00 73.88  ? 64  HIS A ND1  1 
ATOM   497  C CD2  . HIS A 1 64  ? 20.590  -13.686 -46.591 1.00 76.95  ? 64  HIS A CD2  1 
ATOM   498  C CE1  . HIS A 1 64  ? 21.910  -11.937 -46.647 1.00 71.68  ? 64  HIS A CE1  1 
ATOM   499  N NE2  . HIS A 1 64  ? 21.701  -13.129 -47.175 1.00 75.83  ? 64  HIS A NE2  1 
ATOM   500  N N    . ASN A 1 65  ? 18.720  -9.362  -45.112 1.00 66.85  ? 65  ASN A N    1 
ATOM   501  C CA   . ASN A 1 65  ? 19.141  -8.054  -44.626 1.00 65.19  ? 65  ASN A CA   1 
ATOM   502  C C    . ASN A 1 65  ? 18.032  -7.321  -43.885 1.00 64.02  ? 65  ASN A C    1 
ATOM   503  O O    . ASN A 1 65  ? 18.135  -6.110  -43.652 1.00 58.45  ? 65  ASN A O    1 
ATOM   504  C CB   . ASN A 1 65  ? 19.632  -7.187  -45.787 1.00 64.36  ? 65  ASN A CB   1 
ATOM   505  C CG   . ASN A 1 65  ? 20.609  -7.921  -46.706 1.00 67.81  ? 65  ASN A CG   1 
ATOM   506  O OD1  . ASN A 1 65  ? 20.536  -7.793  -47.928 1.00 66.01  ? 65  ASN A OD1  1 
ATOM   507  N ND2  . ASN A 1 65  ? 21.556  -8.650  -46.115 1.00 65.70  ? 65  ASN A ND2  1 
ATOM   508  N N    . PHE A 1 66  ? 16.942  -8.002  -43.567 1.00 63.74  ? 66  PHE A N    1 
ATOM   509  C CA   . PHE A 1 66  ? 15.798  -7.358  -42.939 1.00 63.78  ? 66  PHE A CA   1 
ATOM   510  C C    . PHE A 1 66  ? 15.469  -8.152  -41.691 1.00 60.85  ? 66  PHE A C    1 
ATOM   511  O O    . PHE A 1 66  ? 15.224  -9.358  -41.779 1.00 65.70  ? 66  PHE A O    1 
ATOM   512  C CB   . PHE A 1 66  ? 14.596  -7.305  -43.894 1.00 58.88  ? 66  PHE A CB   1 
ATOM   513  C CG   . PHE A 1 66  ? 14.760  -6.330  -45.022 1.00 59.43  ? 66  PHE A CG   1 
ATOM   514  C CD1  . PHE A 1 66  ? 14.678  -4.961  -44.796 1.00 58.25  ? 66  PHE A CD1  1 
ATOM   515  C CD2  . PHE A 1 66  ? 15.003  -6.776  -46.305 1.00 59.04  ? 66  PHE A CD2  1 
ATOM   516  C CE1  . PHE A 1 66  ? 14.845  -4.053  -45.834 1.00 61.17  ? 66  PHE A CE1  1 
ATOM   517  C CE2  . PHE A 1 66  ? 15.163  -5.882  -47.355 1.00 60.80  ? 66  PHE A CE2  1 
ATOM   518  C CZ   . PHE A 1 66  ? 15.081  -4.510  -47.124 1.00 58.76  ? 66  PHE A CZ   1 
ATOM   519  N N    . LEU A 1 67  ? 15.460  -7.493  -40.538 1.00 58.62  ? 67  LEU A N    1 
ATOM   520  C CA   . LEU A 1 67  ? 15.025  -8.137  -39.305 1.00 66.20  ? 67  LEU A CA   1 
ATOM   521  C C    . LEU A 1 67  ? 13.719  -7.489  -38.867 1.00 66.54  ? 67  LEU A C    1 
ATOM   522  O O    . LEU A 1 67  ? 13.690  -6.296  -38.540 1.00 61.55  ? 67  LEU A O    1 
ATOM   523  C CB   . LEU A 1 67  ? 16.069  -8.033  -38.194 1.00 72.79  ? 67  LEU A CB   1 
ATOM   524  C CG   . LEU A 1 67  ? 15.384  -8.563  -36.929 1.00 79.44  ? 67  LEU A CG   1 
ATOM   525  C CD1  . LEU A 1 67  ? 15.243  -10.060 -37.055 1.00 84.50  ? 67  LEU A CD1  1 
ATOM   526  C CD2  . LEU A 1 67  ? 16.060  -8.153  -35.583 1.00 85.20  ? 67  LEU A CD2  1 
ATOM   527  N N    . VAL A 1 68  ? 12.648  -8.277  -38.867 1.00 68.92  ? 68  VAL A N    1 
ATOM   528  C CA   . VAL A 1 68  ? 11.324  -7.827  -38.459 1.00 67.08  ? 68  VAL A CA   1 
ATOM   529  C C    . VAL A 1 68  ? 11.028  -8.460  -37.108 1.00 71.60  ? 68  VAL A C    1 
ATOM   530  O O    . VAL A 1 68  ? 11.164  -9.681  -36.942 1.00 73.94  ? 68  VAL A O    1 
ATOM   531  C CB   . VAL A 1 68  ? 10.247  -8.191  -39.500 1.00 63.23  ? 68  VAL A CB   1 
ATOM   532  C CG1  . VAL A 1 68  ? 8.854   -7.922  -38.958 1.00 57.59  ? 68  VAL A CG1  1 
ATOM   533  C CG2  . VAL A 1 68  ? 10.467  -7.417  -40.775 1.00 56.69  ? 68  VAL A CG2  1 
ATOM   534  N N    . GLN A 1 69  ? 10.611  -7.630  -36.151 1.00 68.98  ? 69  GLN A N    1 
ATOM   535  C CA   . GLN A 1 69  ? 10.357  -8.074  -34.789 1.00 74.60  ? 69  GLN A CA   1 
ATOM   536  C C    . GLN A 1 69  ? 8.987   -7.594  -34.328 1.00 70.73  ? 69  GLN A C    1 
ATOM   537  O O    . GLN A 1 69  ? 8.689   -6.396  -34.419 1.00 64.59  ? 69  GLN A O    1 
ATOM   538  C CB   . GLN A 1 69  ? 11.461  -7.536  -33.883 1.00 76.25  ? 69  GLN A CB   1 
ATOM   539  C CG   . GLN A 1 69  ? 12.484  -8.584  -33.555 1.00 85.10  ? 69  GLN A CG   1 
ATOM   540  C CD   . GLN A 1 69  ? 13.400  -8.183  -32.417 1.00 91.00  ? 69  GLN A CD   1 
ATOM   541  O OE1  . GLN A 1 69  ? 14.487  -7.598  -32.614 1.00 93.24  ? 69  GLN A OE1  1 
ATOM   542  N NE2  . GLN A 1 69  ? 12.963  -8.493  -31.207 1.00 92.24  ? 69  GLN A NE2  1 
ATOM   543  N N    . ALA A 1 70  ? 8.156   -8.525  -33.847 1.00 76.16  ? 70  ALA A N    1 
ATOM   544  C CA   . ALA A 1 70  ? 6.852   -8.233  -33.238 1.00 77.94  ? 70  ALA A CA   1 
ATOM   545  C C    . ALA A 1 70  ? 6.994   -8.600  -31.769 1.00 83.84  ? 70  ALA A C    1 
ATOM   546  O O    . ALA A 1 70  ? 6.833   -9.760  -31.390 1.00 87.25  ? 70  ALA A O    1 
ATOM   547  C CB   . ALA A 1 70  ? 5.725   -9.025  -33.907 1.00 72.49  ? 70  ALA A CB   1 
ATOM   548  N N    . GLY A 1 71  ? 7.314   -7.617  -30.945 1.00 83.68  ? 71  GLY A N    1 
ATOM   549  C CA   . GLY A 1 71  ? 7.784   -7.960  -29.616 1.00 82.27  ? 71  GLY A CA   1 
ATOM   550  C C    . GLY A 1 71  ? 9.068   -8.761  -29.720 1.00 88.06  ? 71  GLY A C    1 
ATOM   551  O O    . GLY A 1 71  ? 10.086  -8.291  -30.236 1.00 90.68  ? 71  GLY A O    1 
ATOM   552  N N    . ASN A 1 72  ? 9.047   -9.994  -29.228 1.00 92.56  ? 72  ASN A N    1 
ATOM   553  C CA   . ASN A 1 72  ? 10.201  -10.867 -29.367 1.00 98.94  ? 72  ASN A CA   1 
ATOM   554  C C    . ASN A 1 72  ? 10.064  -11.870 -30.503 1.00 101.05 ? 72  ASN A C    1 
ATOM   555  O O    . ASN A 1 72  ? 11.063  -12.490 -30.885 1.00 100.91 ? 72  ASN A O    1 
ATOM   556  C CB   . ASN A 1 72  ? 10.440  -11.628 -28.060 1.00 104.87 ? 72  ASN A CB   1 
ATOM   557  C CG   . ASN A 1 72  ? 10.304  -10.744 -26.848 1.00 109.33 ? 72  ASN A CG   1 
ATOM   558  O OD1  . ASN A 1 72  ? 10.603  -9.548  -26.900 1.00 108.74 ? 72  ASN A OD1  1 
ATOM   559  N ND2  . ASN A 1 72  ? 9.847   -11.324 -25.742 1.00 112.71 ? 72  ASN A ND2  1 
ATOM   560  N N    . VAL A 1 73  ? 8.865   -12.027 -31.069 1.00 99.83  ? 73  VAL A N    1 
ATOM   561  C CA   . VAL A 1 73  ? 8.691   -12.948 -32.182 1.00 97.94  ? 73  VAL A CA   1 
ATOM   562  C C    . VAL A 1 73  ? 9.511   -12.457 -33.364 1.00 94.73  ? 73  VAL A C    1 
ATOM   563  O O    . VAL A 1 73  ? 9.440   -11.281 -33.748 1.00 92.35  ? 73  VAL A O    1 
ATOM   564  C CB   . VAL A 1 73  ? 7.204   -13.083 -32.543 1.00 97.33  ? 73  VAL A CB   1 
ATOM   565  C CG1  . VAL A 1 73  ? 6.959   -14.383 -33.296 1.00 100.16 ? 73  VAL A CG1  1 
ATOM   566  C CG2  . VAL A 1 73  ? 6.329   -13.007 -31.287 1.00 99.83  ? 73  VAL A CG2  1 
ATOM   567  N N    . GLN A 1 74  ? 10.305  -13.351 -33.942 1.00 92.96  ? 74  GLN A N    1 
ATOM   568  C CA   . GLN A 1 74  ? 11.139  -13.019 -35.092 1.00 93.62  ? 74  GLN A CA   1 
ATOM   569  C C    . GLN A 1 74  ? 10.465  -13.571 -36.348 1.00 89.77  ? 74  GLN A C    1 
ATOM   570  O O    . GLN A 1 74  ? 10.466  -14.787 -36.583 1.00 84.82  ? 74  GLN A O    1 
ATOM   571  C CB   . GLN A 1 74  ? 12.550  -13.583 -34.927 1.00 98.05  ? 74  GLN A CB   1 
ATOM   572  C CG   . GLN A 1 74  ? 13.295  -13.042 -33.715 1.00 102.58 ? 74  GLN A CG   1 
ATOM   573  C CD   . GLN A 1 74  ? 14.158  -11.835 -34.045 1.00 101.32 ? 74  GLN A CD   1 
ATOM   574  O OE1  . GLN A 1 74  ? 13.986  -10.771 -33.460 1.00 98.26  ? 74  GLN A OE1  1 
ATOM   575  N NE2  . GLN A 1 74  ? 15.083  -11.991 -34.983 1.00 100.54 ? 74  GLN A NE2  1 
ATOM   576  N N    . LEU A 1 75  ? 9.897   -12.679 -37.153 1.00 81.10  ? 75  LEU A N    1 
ATOM   577  C CA   . LEU A 1 75  ? 9.301   -13.086 -38.414 1.00 78.88  ? 75  LEU A CA   1 
ATOM   578  C C    . LEU A 1 75  ? 10.381  -13.192 -39.484 1.00 80.56  ? 75  LEU A C    1 
ATOM   579  O O    . LEU A 1 75  ? 11.214  -12.288 -39.630 1.00 81.45  ? 75  LEU A O    1 
ATOM   580  C CB   . LEU A 1 75  ? 8.244   -12.069 -38.835 1.00 72.87  ? 75  LEU A CB   1 
ATOM   581  C CG   . LEU A 1 75  ? 7.058   -11.828 -37.910 1.00 67.92  ? 75  LEU A CG   1 
ATOM   582  C CD1  . LEU A 1 75  ? 7.445   -10.794 -36.887 1.00 74.94  ? 75  LEU A CD1  1 
ATOM   583  C CD2  . LEU A 1 75  ? 5.923   -11.271 -38.719 1.00 65.34  ? 75  LEU A CD2  1 
ATOM   584  N N    . ARG A 1 76  ? 10.389  -14.304 -40.214 1.00 76.05  ? 76  ARG A N    1 
ATOM   585  C CA   . ARG A 1 76  ? 11.314  -14.455 -41.326 1.00 75.04  ? 76  ARG A CA   1 
ATOM   586  C C    . ARG A 1 76  ? 10.756  -13.773 -42.572 1.00 72.47  ? 76  ARG A C    1 
ATOM   587  O O    . ARG A 1 76  ? 9.553   -13.841 -42.862 1.00 69.31  ? 76  ARG A O    1 
ATOM   588  C CB   . ARG A 1 76  ? 11.618  -15.924 -41.585 1.00 73.57  ? 76  ARG A CB   1 
ATOM   589  C CG   . ARG A 1 76  ? 12.984  -16.149 -42.234 1.00 80.36  ? 76  ARG A CG   1 
ATOM   590  C CD   . ARG A 1 76  ? 13.990  -16.679 -41.240 1.00 82.47  ? 76  ARG A CD   1 
ATOM   591  N NE   . ARG A 1 76  ? 13.859  -18.118 -41.064 1.00 88.86  ? 76  ARG A NE   1 
ATOM   592  C CZ   . ARG A 1 76  ? 14.610  -18.838 -40.244 1.00 89.51  ? 76  ARG A CZ   1 
ATOM   593  N NH1  . ARG A 1 76  ? 15.581  -18.283 -39.531 1.00 92.81  ? 76  ARG A NH1  1 
ATOM   594  N NH2  . ARG A 1 76  ? 14.366  -20.140 -40.115 1.00 83.63  ? 76  ARG A NH2  1 
ATOM   595  N N    . VAL A 1 77  ? 11.626  -13.056 -43.264 1.00 68.34  ? 77  VAL A N    1 
ATOM   596  C CA   . VAL A 1 77  ? 11.246  -12.349 -44.464 1.00 67.20  ? 77  VAL A CA   1 
ATOM   597  C C    . VAL A 1 77  ? 11.520  -13.267 -45.631 1.00 67.40  ? 77  VAL A C    1 
ATOM   598  O O    . VAL A 1 77  ? 12.608  -13.857 -45.745 1.00 68.29  ? 77  VAL A O    1 
ATOM   599  C CB   . VAL A 1 77  ? 12.008  -11.016 -44.587 1.00 66.60  ? 77  VAL A CB   1 
ATOM   600  C CG1  . VAL A 1 77  ? 11.668  -10.302 -45.892 1.00 60.97  ? 77  VAL A CG1  1 
ATOM   601  C CG2  . VAL A 1 77  ? 11.697  -10.106 -43.354 1.00 63.25  ? 77  VAL A CG2  1 
ATOM   602  N N    . ILE A 1 78  ? 10.502  -13.418 -46.480 1.00 64.13  ? 78  ILE A N    1 
ATOM   603  C CA   . ILE A 1 78  ? 10.569  -14.396 -47.577 1.00 65.70  ? 78  ILE A CA   1 
ATOM   604  C C    . ILE A 1 78  ? 10.297  -13.776 -48.961 1.00 65.62  ? 78  ILE A C    1 
ATOM   605  O O    . ILE A 1 78  ? 10.177  -14.480 -49.974 1.00 65.38  ? 78  ILE A O    1 
ATOM   606  C CB   . ILE A 1 78  ? 9.625   -15.581 -47.307 1.00 62.84  ? 78  ILE A CB   1 
ATOM   607  C CG1  . ILE A 1 78  ? 8.176   -15.119 -47.149 1.00 66.66  ? 78  ILE A CG1  1 
ATOM   608  C CG2  . ILE A 1 78  ? 10.105  -16.320 -46.028 1.00 60.48  ? 78  ILE A CG2  1 
ATOM   609  C CD1  . ILE A 1 78  ? 7.207   -16.309 -47.011 1.00 65.65  ? 78  ILE A CD1  1 
ATOM   610  N N    . GLY A 1 79  ? 10.263  -12.451 -49.025 1.00 63.01  ? 79  GLY A N    1 
ATOM   611  C CA   . GLY A 1 79  ? 10.059  -11.724 -50.268 1.00 59.49  ? 79  GLY A CA   1 
ATOM   612  C C    . GLY A 1 79  ? 9.950   -10.246 -49.985 1.00 61.42  ? 79  GLY A C    1 
ATOM   613  O O    . GLY A 1 79  ? 9.437   -9.873  -48.930 1.00 61.12  ? 79  GLY A O    1 
ATOM   614  N N    . HIS A 1 80  ? 10.457  -9.398  -50.878 1.00 60.57  ? 80  HIS A N    1 
ATOM   615  C CA   . HIS A 1 80  ? 10.474  -7.958  -50.668 1.00 55.82  ? 80  HIS A CA   1 
ATOM   616  C C    . HIS A 1 80  ? 10.181  -7.220  -51.968 1.00 56.64  ? 80  HIS A C    1 
ATOM   617  O O    . HIS A 1 80  ? 10.623  -7.629  -53.051 1.00 53.41  ? 80  HIS A O    1 
ATOM   618  C CB   . HIS A 1 80  ? 11.810  -7.480  -50.092 1.00 54.29  ? 80  HIS A CB   1 
ATOM   619  C CG   . HIS A 1 80  ? 12.988  -7.725  -50.985 1.00 56.93  ? 80  HIS A CG   1 
ATOM   620  N ND1  . HIS A 1 80  ? 13.772  -8.855  -50.888 1.00 58.79  ? 80  HIS A ND1  1 
ATOM   621  C CD2  . HIS A 1 80  ? 13.553  -6.960  -51.950 1.00 53.01  ? 80  HIS A CD2  1 
ATOM   622  C CE1  . HIS A 1 80  ? 14.756  -8.786  -51.770 1.00 57.79  ? 80  HIS A CE1  1 
ATOM   623  N NE2  . HIS A 1 80  ? 14.643  -7.648  -52.430 1.00 55.41  ? 80  HIS A NE2  1 
ATOM   624  N N    . SER A 1 81  ? 9.464   -6.107  -51.848 1.00 50.27  ? 81  SER A N    1 
ATOM   625  C CA   . SER A 1 81  ? 9.009   -5.357  -53.003 1.00 49.11  ? 81  SER A CA   1 
ATOM   626  C C    . SER A 1 81  ? 8.886   -3.900  -52.576 1.00 52.90  ? 81  SER A C    1 
ATOM   627  O O    . SER A 1 81  ? 8.759   -3.589  -51.388 1.00 50.83  ? 81  SER A O    1 
ATOM   628  C CB   . SER A 1 81  ? 7.686   -5.941  -53.521 1.00 50.75  ? 81  SER A CB   1 
ATOM   629  O OG   . SER A 1 81  ? 6.901   -5.013  -54.240 1.00 57.47  ? 81  SER A OG   1 
ATOM   630  N N    . MET A 1 82  ? 8.957   -3.004  -53.545 1.00 47.69  ? 82  MET A N    1 
ATOM   631  C CA   . MET A 1 82  ? 8.954   -1.582  -53.265 1.00 44.81  ? 82  MET A CA   1 
ATOM   632  C C    . MET A 1 82  ? 7.776   -0.999  -54.024 1.00 48.21  ? 82  MET A C    1 
ATOM   633  O O    . MET A 1 82  ? 7.785   -0.973  -55.259 1.00 53.83  ? 82  MET A O    1 
ATOM   634  C CB   . MET A 1 82  ? 10.240  -0.922  -53.722 1.00 45.49  ? 82  MET A CB   1 
ATOM   635  C CG   . MET A 1 82  ? 10.075  0.560   -53.954 1.00 46.65  ? 82  MET A CG   1 
ATOM   636  S SD   . MET A 1 82  ? 11.619  1.373   -53.495 1.00 49.96  ? 82  MET A SD   1 
ATOM   637  C CE   . MET A 1 82  ? 12.637  0.918   -54.893 1.00 50.97  ? 82  MET A CE   1 
ATOM   638  N N    . GLN A 1 83  ? 6.790   -0.494  -53.319 1.00 43.31  ? 83  GLN A N    1 
ATOM   639  C CA   . GLN A 1 83  ? 5.656   0.163   -53.939 1.00 45.41  ? 83  GLN A CA   1 
ATOM   640  C C    . GLN A 1 83  ? 5.726   1.648   -53.596 1.00 41.83  ? 83  GLN A C    1 
ATOM   641  O O    . GLN A 1 83  ? 5.503   2.035   -52.449 1.00 39.83  ? 83  GLN A O    1 
ATOM   642  C CB   . GLN A 1 83  ? 4.343   -0.473  -53.475 1.00 46.80  ? 83  GLN A CB   1 
ATOM   643  C CG   . GLN A 1 83  ? 3.083   0.330   -53.892 1.00 46.42  ? 83  GLN A CG   1 
ATOM   644  C CD   . GLN A 1 83  ? 1.757   -0.354  -53.492 1.00 49.68  ? 83  GLN A CD   1 
ATOM   645  O OE1  . GLN A 1 83  ? 1.733   -1.297  -52.672 1.00 52.35  ? 83  GLN A OE1  1 
ATOM   646  N NE2  . GLN A 1 83  ? 0.651   0.130   -54.069 1.00 52.21  ? 83  GLN A NE2  1 
ATOM   647  N N    . ASN A 1 84  ? 6.041   2.486   -54.583 1.00 43.74  ? 84  ASN A N    1 
ATOM   648  C CA   . ASN A 1 84  ? 6.178   3.923   -54.341 1.00 39.64  ? 84  ASN A CA   1 
ATOM   649  C C    . ASN A 1 84  ? 7.176   4.120   -53.196 1.00 43.35  ? 84  ASN A C    1 
ATOM   650  O O    . ASN A 1 84  ? 8.257   3.514   -53.213 1.00 37.76  ? 84  ASN A O    1 
ATOM   651  C CB   . ASN A 1 84  ? 4.801   4.477   -54.115 1.00 43.24  ? 84  ASN A CB   1 
ATOM   652  C CG   . ASN A 1 84  ? 3.898   4.259   -55.311 1.00 47.69  ? 84  ASN A CG   1 
ATOM   653  O OD1  . ASN A 1 84  ? 4.313   4.477   -56.445 1.00 43.95  ? 84  ASN A OD1  1 
ATOM   654  N ND2  . ASN A 1 84  ? 2.655   3.870   -55.064 1.00 47.21  ? 84  ASN A ND2  1 
ATOM   655  N N    . CYS A 1 85  ? 6.860   4.905   -52.164 1.00 40.78  ? 85  CYS A N    1 
ATOM   656  C CA   . CYS A 1 85  ? 7.836   5.143   -51.105 1.00 39.83  ? 85  CYS A CA   1 
ATOM   657  C C    . CYS A 1 85  ? 7.735   4.137   -49.964 1.00 39.40  ? 85  CYS A C    1 
ATOM   658  O O    . CYS A 1 85  ? 8.387   4.308   -48.923 1.00 40.86  ? 85  CYS A O    1 
ATOM   659  C CB   . CYS A 1 85  ? 7.720   6.570   -50.605 1.00 35.48  ? 85  CYS A CB   1 
ATOM   660  S SG   . CYS A 1 85  ? 8.122   7.734   -51.954 1.00 36.20  ? 85  CYS A SG   1 
ATOM   661  N N    . VAL A 1 86  ? 7.054   3.022   -50.186 1.00 38.44  ? 86  VAL A N    1 
ATOM   662  C CA   . VAL A 1 86  ? 6.801   2.043   -49.140 1.00 39.83  ? 86  VAL A CA   1 
ATOM   663  C C    . VAL A 1 86  ? 7.477   0.756   -49.521 1.00 41.51  ? 86  VAL A C    1 
ATOM   664  O O    . VAL A 1 86  ? 7.405   0.323   -50.674 1.00 42.50  ? 86  VAL A O    1 
ATOM   665  C CB   . VAL A 1 86  ? 5.286   1.819   -48.910 1.00 40.46  ? 86  VAL A CB   1 
ATOM   666  C CG1  . VAL A 1 86  ? 5.042   0.531   -48.205 1.00 43.82  ? 86  VAL A CG1  1 
ATOM   667  C CG2  . VAL A 1 86  ? 4.715   2.973   -48.072 1.00 41.69  ? 86  VAL A CG2  1 
ATOM   668  N N    . LEU A 1 87  ? 8.130   0.145   -48.548 1.00 42.58  ? 87  LEU A N    1 
ATOM   669  C CA   . LEU A 1 87  ? 8.699   -1.171  -48.717 1.00 44.32  ? 87  LEU A CA   1 
ATOM   670  C C    . LEU A 1 87  ? 7.752   -2.190  -48.094 1.00 49.01  ? 87  LEU A C    1 
ATOM   671  O O    . LEU A 1 87  ? 7.189   -1.943  -47.023 1.00 46.83  ? 87  LEU A O    1 
ATOM   672  C CB   . LEU A 1 87  ? 10.079  -1.228  -48.070 1.00 41.45  ? 87  LEU A CB   1 
ATOM   673  C CG   . LEU A 1 87  ? 10.716  -2.577  -47.850 1.00 52.32  ? 87  LEU A CG   1 
ATOM   674  C CD1  . LEU A 1 87  ? 11.181  -3.112  -49.202 1.00 54.15  ? 87  LEU A CD1  1 
ATOM   675  C CD2  . LEU A 1 87  ? 11.898  -2.434  -46.892 1.00 51.81  ? 87  LEU A CD2  1 
ATOM   676  N N    . LYS A 1 88  ? 7.562   -3.317  -48.787 1.00 48.99  ? 88  LYS A N    1 
ATOM   677  C CA   . LYS A 1 88  ? 6.703   -4.414  -48.362 1.00 47.34  ? 88  LYS A CA   1 
ATOM   678  C C    . LYS A 1 88  ? 7.556   -5.659  -48.219 1.00 52.14  ? 88  LYS A C    1 
ATOM   679  O O    . LYS A 1 88  ? 8.139   -6.132  -49.203 1.00 56.54  ? 88  LYS A O    1 
ATOM   680  C CB   . LYS A 1 88  ? 5.553   -4.652  -49.349 1.00 48.18  ? 88  LYS A CB   1 
ATOM   681  C CG   . LYS A 1 88  ? 4.448   -3.612  -49.201 1.00 51.86  ? 88  LYS A CG   1 
ATOM   682  C CD   . LYS A 1 88  ? 3.700   -3.294  -50.483 1.00 55.60  ? 88  LYS A CD   1 
ATOM   683  C CE   . LYS A 1 88  ? 3.868   -4.405  -51.509 1.00 55.33  ? 88  LYS A CE   1 
ATOM   684  N NZ   . LYS A 1 88  ? 2.682   -4.371  -52.420 1.00 63.97  ? 88  LYS A NZ   1 
ATOM   685  N N    . LEU A 1 89  ? 7.646   -6.166  -46.991 1.00 49.10  ? 89  LEU A N    1 
ATOM   686  C CA   . LEU A 1 89  ? 8.370   -7.381  -46.663 1.00 56.24  ? 89  LEU A CA   1 
ATOM   687  C C    . LEU A 1 89  ? 7.351   -8.490  -46.471 1.00 58.01  ? 89  LEU A C    1 
ATOM   688  O O    . LEU A 1 89  ? 6.510   -8.408  -45.566 1.00 55.30  ? 89  LEU A O    1 
ATOM   689  C CB   . LEU A 1 89  ? 9.204   -7.209  -45.389 1.00 54.07  ? 89  LEU A CB   1 
ATOM   690  C CG   . LEU A 1 89  ? 10.011  -5.914  -45.372 1.00 53.08  ? 89  LEU A CG   1 
ATOM   691  C CD1  . LEU A 1 89  ? 10.514  -5.626  -43.974 1.00 49.97  ? 89  LEU A CD1  1 
ATOM   692  C CD2  . LEU A 1 89  ? 11.174  -6.022  -46.356 1.00 57.37  ? 89  LEU A CD2  1 
ATOM   693  N N    . LYS A 1 90  ? 7.400   -9.507  -47.329 1.00 60.61  ? 90  LYS A N    1 
ATOM   694  C CA   . LYS A 1 90  ? 6.501   -10.631 -47.162 1.00 58.48  ? 90  LYS A CA   1 
ATOM   695  C C    . LYS A 1 90  ? 7.127   -11.585 -46.166 1.00 61.51  ? 90  LYS A C    1 
ATOM   696  O O    . LYS A 1 90  ? 8.297   -11.961 -46.295 1.00 63.56  ? 90  LYS A O    1 
ATOM   697  C CB   . LYS A 1 90  ? 6.188   -11.308 -48.492 1.00 62.79  ? 90  LYS A CB   1 
ATOM   698  C CG   . LYS A 1 90  ? 5.453   -12.628 -48.325 1.00 67.80  ? 90  LYS A CG   1 
ATOM   699  C CD   . LYS A 1 90  ? 4.228   -12.755 -49.234 1.00 67.08  ? 90  LYS A CD   1 
ATOM   700  C CE   . LYS A 1 90  ? 3.835   -14.248 -49.335 1.00 69.88  ? 90  LYS A CE   1 
ATOM   701  N NZ   . LYS A 1 90  ? 2.697   -14.459 -50.267 1.00 74.96  ? 90  LYS A NZ   1 
ATOM   702  N N    . VAL A 1 91  ? 6.371   -11.908 -45.124 1.00 62.28  ? 91  VAL A N    1 
ATOM   703  C CA   . VAL A 1 91  ? 6.875   -12.709 -44.022 1.00 65.32  ? 91  VAL A CA   1 
ATOM   704  C C    . VAL A 1 91  ? 6.149   -14.050 -43.996 1.00 68.13  ? 91  VAL A C    1 
ATOM   705  O O    . VAL A 1 91  ? 5.190   -14.287 -44.734 1.00 68.42  ? 91  VAL A O    1 
ATOM   706  C CB   . VAL A 1 91  ? 6.743   -11.972 -42.680 1.00 69.09  ? 91  VAL A CB   1 
ATOM   707  C CG1  . VAL A 1 91  ? 7.776   -10.847 -42.610 1.00 64.09  ? 91  VAL A CG1  1 
ATOM   708  C CG2  . VAL A 1 91  ? 5.311   -11.415 -42.534 1.00 61.26  ? 91  VAL A CG2  1 
ATOM   709  N N    . ASP A 1 92  ? 6.600   -14.926 -43.109 1.00 65.99  ? 92  ASP A N    1 
ATOM   710  C CA   . ASP A 1 92  ? 6.072   -16.276 -43.110 1.00 74.43  ? 92  ASP A CA   1 
ATOM   711  C C    . ASP A 1 92  ? 4.860   -16.457 -42.199 1.00 77.14  ? 92  ASP A C    1 
ATOM   712  O O    . ASP A 1 92  ? 4.127   -17.436 -42.371 1.00 79.10  ? 92  ASP A O    1 
ATOM   713  C CB   . ASP A 1 92  ? 7.182   -17.273 -42.731 1.00 73.97  ? 92  ASP A CB   1 
ATOM   714  C CG   . ASP A 1 92  ? 7.655   -17.112 -41.300 1.00 72.27  ? 92  ASP A CG   1 
ATOM   715  O OD1  . ASP A 1 92  ? 7.119   -16.233 -40.587 1.00 75.91  ? 92  ASP A OD1  1 
ATOM   716  O OD2  . ASP A 1 92  ? 8.555   -17.868 -40.889 1.00 68.97  ? 92  ASP A OD2  1 
ATOM   717  N N    . THR A 1 93  ? 4.623   -15.552 -41.249 1.00 73.93  ? 93  THR A N    1 
ATOM   718  C CA   . THR A 1 93  ? 3.521   -15.680 -40.299 1.00 66.49  ? 93  THR A CA   1 
ATOM   719  C C    . THR A 1 93  ? 2.507   -14.575 -40.541 1.00 67.25  ? 93  THR A C    1 
ATOM   720  O O    . THR A 1 93  ? 2.875   -13.398 -40.633 1.00 65.11  ? 93  THR A O    1 
ATOM   721  C CB   . THR A 1 93  ? 4.019   -15.624 -38.855 1.00 70.34  ? 93  THR A CB   1 
ATOM   722  O OG1  . THR A 1 93  ? 4.883   -16.740 -38.606 1.00 75.97  ? 93  THR A OG1  1 
ATOM   723  C CG2  . THR A 1 93  ? 2.849   -15.693 -37.884 1.00 70.64  ? 93  THR A CG2  1 
ATOM   724  N N    . ALA A 1 94  ? 1.237   -14.951 -40.667 1.00 65.24  ? 94  ALA A N    1 
ATOM   725  C CA   . ALA A 1 94  ? 0.187   -13.957 -40.803 1.00 60.57  ? 94  ALA A CA   1 
ATOM   726  C C    . ALA A 1 94  ? -0.125  -13.419 -39.417 1.00 61.55  ? 94  ALA A C    1 
ATOM   727  O O    . ALA A 1 94  ? -0.366  -14.194 -38.491 1.00 57.16  ? 94  ALA A O    1 
ATOM   728  C CB   . ALA A 1 94  ? -1.064  -14.549 -41.449 1.00 60.74  ? 94  ALA A CB   1 
ATOM   729  N N    . ASN A 1 95  ? -0.050  -12.091 -39.258 1.00 60.01  ? 95  ASN A N    1 
ATOM   730  C CA   . ASN A 1 95  ? -0.330  -11.480 -37.969 1.00 56.60  ? 95  ASN A CA   1 
ATOM   731  C C    . ASN A 1 95  ? -1.672  -11.984 -37.451 1.00 55.87  ? 95  ASN A C    1 
ATOM   732  O O    . ASN A 1 95  ? -2.716  -11.667 -38.036 1.00 58.09  ? 95  ASN A O    1 
ATOM   733  C CB   . ASN A 1 95  ? -0.329  -9.951  -38.093 1.00 53.99  ? 95  ASN A CB   1 
ATOM   734  C CG   . ASN A 1 95  ? -0.832  -9.247  -36.819 1.00 54.80  ? 95  ASN A CG   1 
ATOM   735  O OD1  . ASN A 1 95  ? -0.681  -9.749  -35.695 1.00 54.86  ? 95  ASN A OD1  1 
ATOM   736  N ND2  . ASN A 1 95  ? -1.435  -8.078  -37.001 1.00 54.84  ? 95  ASN A ND2  1 
ATOM   737  N N    . PRO A 1 96  ? -1.699  -12.739 -36.353 1.00 54.48  ? 96  PRO A N    1 
ATOM   738  C CA   . PRO A 1 96  ? -2.997  -13.170 -35.789 1.00 55.89  ? 96  PRO A CA   1 
ATOM   739  C C    . PRO A 1 96  ? -3.895  -12.022 -35.360 1.00 60.63  ? 96  PRO A C    1 
ATOM   740  O O    . PRO A 1 96  ? -5.122  -12.176 -35.339 1.00 62.14  ? 96  PRO A O    1 
ATOM   741  C CB   . PRO A 1 96  ? -2.597  -14.053 -34.602 1.00 60.19  ? 96  PRO A CB   1 
ATOM   742  C CG   . PRO A 1 96  ? -1.207  -13.674 -34.263 1.00 63.23  ? 96  PRO A CG   1 
ATOM   743  C CD   . PRO A 1 96  ? -0.558  -13.108 -35.497 1.00 55.68  ? 96  PRO A CD   1 
ATOM   744  N N    . LYS A 1 97  ? -3.342  -10.854 -35.055 1.00 60.19  ? 97  LYS A N    1 
ATOM   745  C CA   . LYS A 1 97  ? -4.157  -9.739  -34.601 1.00 57.35  ? 97  LYS A CA   1 
ATOM   746  C C    . LYS A 1 97  ? -4.718  -8.914  -35.741 1.00 55.87  ? 97  LYS A C    1 
ATOM   747  O O    . LYS A 1 97  ? -5.303  -7.864  -35.473 1.00 58.13  ? 97  LYS A O    1 
ATOM   748  C CB   . LYS A 1 97  ? -3.355  -8.825  -33.662 1.00 60.31  ? 97  LYS A CB   1 
ATOM   749  C CG   . LYS A 1 97  ? -2.911  -9.469  -32.373 1.00 59.27  ? 97  LYS A CG   1 
ATOM   750  C CD   . LYS A 1 97  ? -1.641  -10.271 -32.613 1.00 72.85  ? 97  LYS A CD   1 
ATOM   751  C CE   . LYS A 1 97  ? -1.075  -10.845 -31.321 1.00 84.45  ? 97  LYS A CE   1 
ATOM   752  N NZ   . LYS A 1 97  ? 0.416   -10.938 -31.326 1.00 94.94  ? 97  LYS A NZ   1 
ATOM   753  N N    . THR A 1 98  ? -4.520  -9.327  -36.999 1.00 54.99  ? 98  THR A N    1 
ATOM   754  C CA   . THR A 1 98  ? -4.901  -8.484  -38.129 1.00 53.38  ? 98  THR A CA   1 
ATOM   755  C C    . THR A 1 98  ? -6.377  -8.114  -37.992 1.00 51.09  ? 98  THR A C    1 
ATOM   756  O O    . THR A 1 98  ? -7.225  -9.010  -37.878 1.00 49.41  ? 98  THR A O    1 
ATOM   757  C CB   . THR A 1 98  ? -4.642  -9.187  -39.479 1.00 53.46  ? 98  THR A CB   1 
ATOM   758  O OG1  . THR A 1 98  ? -3.279  -9.600  -39.571 1.00 55.64  ? 98  THR A OG1  1 
ATOM   759  C CG2  . THR A 1 98  ? -4.921  -8.283  -40.660 1.00 47.82  ? 98  THR A CG2  1 
ATOM   760  N N    . PRO A 1 99  ? -6.709  -6.836  -37.896 1.00 51.48  ? 99  PRO A N    1 
ATOM   761  C CA   . PRO A 1 99  ? -8.113  -6.429  -37.853 1.00 47.62  ? 99  PRO A CA   1 
ATOM   762  C C    . PRO A 1 99  ? -8.646  -6.364  -39.272 1.00 50.52  ? 99  PRO A C    1 
ATOM   763  O O    . PRO A 1 99  ? -7.892  -6.414  -40.246 1.00 51.08  ? 99  PRO A O    1 
ATOM   764  C CB   . PRO A 1 99  ? -8.064  -5.030  -37.241 1.00 48.76  ? 99  PRO A CB   1 
ATOM   765  C CG   . PRO A 1 99  ? -6.744  -4.465  -37.830 1.00 44.49  ? 99  PRO A CG   1 
ATOM   766  C CD   . PRO A 1 99  ? -5.798  -5.682  -37.880 1.00 49.50  ? 99  PRO A CD   1 
ATOM   767  N N    . LYS A 1 100 ? -9.965  -6.231  -39.364 1.00 49.03  ? 100 LYS A N    1 
ATOM   768  C CA   . LYS A 1 100 ? -10.602 -5.807  -40.602 1.00 55.56  ? 100 LYS A CA   1 
ATOM   769  C C    . LYS A 1 100 ? -10.072 -4.430  -40.996 1.00 50.48  ? 100 LYS A C    1 
ATOM   770  O O    . LYS A 1 100 ? -10.174 -3.473  -40.216 1.00 51.75  ? 100 LYS A O    1 
ATOM   771  C CB   . LYS A 1 100 ? -12.130 -5.772  -40.416 1.00 58.45  ? 100 LYS A CB   1 
ATOM   772  C CG   . LYS A 1 100 ? -12.967 -6.094  -41.685 1.00 66.89  ? 100 LYS A CG   1 
ATOM   773  C CD   . LYS A 1 100 ? -12.762 -4.998  -42.747 1.00 72.76  ? 100 LYS A CD   1 
ATOM   774  C CE   . LYS A 1 100 ? -12.966 -5.470  -44.206 1.00 76.83  ? 100 LYS A CE   1 
ATOM   775  N NZ   . LYS A 1 100 ? -12.645 -4.341  -45.162 1.00 66.60  ? 100 LYS A NZ   1 
ATOM   776  N N    . TYR A 1 101 ? -9.494  -4.316  -42.194 1.00 50.36  ? 101 TYR A N    1 
ATOM   777  C CA   . TYR A 1 101 ? -8.835  -3.068  -42.559 1.00 51.85  ? 101 TYR A CA   1 
ATOM   778  C C    . TYR A 1 101 ? -9.094  -2.696  -44.011 1.00 51.83  ? 101 TYR A C    1 
ATOM   779  O O    . TYR A 1 101 ? -9.456  -3.529  -44.842 1.00 48.41  ? 101 TYR A O    1 
ATOM   780  C CB   . TYR A 1 101 ? -7.315  -3.142  -42.305 1.00 44.97  ? 101 TYR A CB   1 
ATOM   781  C CG   . TYR A 1 101 ? -6.535  -3.977  -43.305 1.00 46.93  ? 101 TYR A CG   1 
ATOM   782  C CD1  . TYR A 1 101 ? -6.443  -5.355  -43.149 1.00 47.51  ? 101 TYR A CD1  1 
ATOM   783  C CD2  . TYR A 1 101 ? -5.898  -3.399  -44.393 1.00 45.12  ? 101 TYR A CD2  1 
ATOM   784  C CE1  . TYR A 1 101 ? -5.739  -6.140  -44.043 1.00 51.26  ? 101 TYR A CE1  1 
ATOM   785  C CE2  . TYR A 1 101 ? -5.177  -4.189  -45.305 1.00 44.48  ? 101 TYR A CE2  1 
ATOM   786  C CZ   . TYR A 1 101 ? -5.106  -5.553  -45.120 1.00 49.80  ? 101 TYR A CZ   1 
ATOM   787  O OH   . TYR A 1 101 ? -4.409  -6.363  -46.002 1.00 57.73  ? 101 TYR A OH   1 
ATOM   788  N N    . LYS A 1 102 ? -8.884  -1.407  -44.286 1.00 47.92  ? 102 LYS A N    1 
ATOM   789  C CA   . LYS A 1 102 ? -8.809  -0.824  -45.619 1.00 46.58  ? 102 LYS A CA   1 
ATOM   790  C C    . LYS A 1 102 ? -7.566  0.050   -45.671 1.00 44.11  ? 102 LYS A C    1 
ATOM   791  O O    . LYS A 1 102 ? -7.062  0.472   -44.630 1.00 44.63  ? 102 LYS A O    1 
ATOM   792  C CB   . LYS A 1 102 ? -10.011 0.082   -45.975 1.00 49.11  ? 102 LYS A CB   1 
ATOM   793  C CG   . LYS A 1 102 ? -11.407 -0.544  -46.140 1.00 60.72  ? 102 LYS A CG   1 
ATOM   794  C CD   . LYS A 1 102 ? -12.422 0.136   -45.212 1.00 65.74  ? 102 LYS A CD   1 
ATOM   795  C CE   . LYS A 1 102 ? -13.900 -0.272  -45.465 1.00 72.87  ? 102 LYS A CE   1 
ATOM   796  N NZ   . LYS A 1 102 ? -14.710 -0.445  -44.210 1.00 79.88  ? 102 LYS A NZ   1 
ATOM   797  N N    . PHE A 1 103 ? -7.090  0.333   -46.888 1.00 43.07  ? 103 PHE A N    1 
ATOM   798  C CA   . PHE A 1 103 ? -6.175  1.430   -47.184 1.00 39.65  ? 103 PHE A CA   1 
ATOM   799  C C    . PHE A 1 103 ? -6.948  2.513   -47.894 1.00 44.02  ? 103 PHE A C    1 
ATOM   800  O O    . PHE A 1 103 ? -7.693  2.231   -48.837 1.00 51.09  ? 103 PHE A O    1 
ATOM   801  C CB   . PHE A 1 103 ? -5.015  1.019   -48.090 1.00 37.94  ? 103 PHE A CB   1 
ATOM   802  C CG   . PHE A 1 103 ? -4.021  0.109   -47.440 1.00 38.61  ? 103 PHE A CG   1 
ATOM   803  C CD1  . PHE A 1 103 ? -4.054  -0.114  -46.078 1.00 39.18  ? 103 PHE A CD1  1 
ATOM   804  C CD2  . PHE A 1 103 ? -3.081  -0.559  -48.206 1.00 34.01  ? 103 PHE A CD2  1 
ATOM   805  C CE1  . PHE A 1 103 ? -3.146  -0.971  -45.472 1.00 37.67  ? 103 PHE A CE1  1 
ATOM   806  C CE2  . PHE A 1 103 ? -2.186  -1.398  -47.621 1.00 38.04  ? 103 PHE A CE2  1 
ATOM   807  C CZ   . PHE A 1 103 ? -2.209  -1.612  -46.252 1.00 43.14  ? 103 PHE A CZ   1 
ATOM   808  N N    . VAL A 1 104 ? -6.755  3.745   -47.453 1.00 39.64  ? 104 VAL A N    1 
ATOM   809  C CA   . VAL A 1 104 ? -7.579  4.864   -47.859 1.00 38.03  ? 104 VAL A CA   1 
ATOM   810  C C    . VAL A 1 104 ? -6.668  6.068   -48.007 1.00 42.58  ? 104 VAL A C    1 
ATOM   811  O O    . VAL A 1 104 ? -5.785  6.296   -47.169 1.00 45.82  ? 104 VAL A O    1 
ATOM   812  C CB   . VAL A 1 104 ? -8.691  5.108   -46.820 1.00 43.51  ? 104 VAL A CB   1 
ATOM   813  C CG1  . VAL A 1 104 ? -9.113  6.557   -46.792 1.00 41.48  ? 104 VAL A CG1  1 
ATOM   814  C CG2  . VAL A 1 104 ? -9.879  4.198   -47.149 1.00 44.05  ? 104 VAL A CG2  1 
ATOM   815  N N    . ARG A 1 105 ? -6.857  6.823   -49.078 1.00 39.45  ? 105 ARG A N    1 
ATOM   816  C CA   . ARG A 1 105 ? -6.139  8.075   -49.283 1.00 41.71  ? 105 ARG A CA   1 
ATOM   817  C C    . ARG A 1 105 ? -7.084  9.214   -48.931 1.00 40.99  ? 105 ARG A C    1 
ATOM   818  O O    . ARG A 1 105 ? -8.063  9.450   -49.637 1.00 46.23  ? 105 ARG A O    1 
ATOM   819  C CB   . ARG A 1 105 ? -5.638  8.195   -50.719 1.00 43.50  ? 105 ARG A CB   1 
ATOM   820  C CG   . ARG A 1 105 ? -4.913  9.532   -51.002 1.00 42.70  ? 105 ARG A CG   1 
ATOM   821  C CD   . ARG A 1 105 ? -4.083  9.468   -52.301 1.00 45.07  ? 105 ARG A CD   1 
ATOM   822  N NE   . ARG A 1 105 ? -3.258  10.669  -52.436 1.00 44.37  ? 105 ARG A NE   1 
ATOM   823  C CZ   . ARG A 1 105 ? -1.976  10.739  -52.100 1.00 37.68  ? 105 ARG A CZ   1 
ATOM   824  N NH1  . ARG A 1 105 ? -1.331  9.686   -51.606 1.00 33.95  ? 105 ARG A NH1  1 
ATOM   825  N NH2  . ARG A 1 105 ? -1.322  11.888  -52.280 1.00 38.10  ? 105 ARG A NH2  1 
ATOM   826  N N    . ILE A 1 106 ? -6.802  9.925   -47.844 1.00 41.68  ? 106 ILE A N    1 
ATOM   827  C CA   . ILE A 1 106 ? -7.743  10.927  -47.370 1.00 39.18  ? 106 ILE A CA   1 
ATOM   828  C C    . ILE A 1 106 ? -7.498  12.235  -48.098 1.00 41.84  ? 106 ILE A C    1 
ATOM   829  O O    . ILE A 1 106 ? -6.407  12.504  -48.596 1.00 39.78  ? 106 ILE A O    1 
ATOM   830  C CB   . ILE A 1 106 ? -7.692  11.141  -45.841 1.00 39.88  ? 106 ILE A CB   1 
ATOM   831  C CG1  . ILE A 1 106 ? -6.256  11.404  -45.388 1.00 39.16  ? 106 ILE A CG1  1 
ATOM   832  C CG2  . ILE A 1 106 ? -8.294  9.918   -45.094 1.00 40.87  ? 106 ILE A CG2  1 
ATOM   833  C CD1  . ILE A 1 106 ? -5.957  12.886  -45.271 1.00 43.43  ? 106 ILE A CD1  1 
ATOM   834  N N    . GLN A 1 107 ? -8.556  13.045  -48.154 1.00 39.88  ? 107 GLN A N    1 
ATOM   835  C CA   . GLN A 1 107 ? -8.646  14.371  -48.707 1.00 43.36  ? 107 GLN A CA   1 
ATOM   836  C C    . GLN A 1 107 ? -8.119  15.391  -47.704 1.00 44.25  ? 107 GLN A C    1 
ATOM   837  O O    . GLN A 1 107 ? -8.283  15.214  -46.495 1.00 39.45  ? 107 GLN A O    1 
ATOM   838  C CB   . GLN A 1 107 ? -10.104 14.702  -49.031 1.00 46.33  ? 107 GLN A CB   1 
ATOM   839  C CG   . GLN A 1 107 ? -10.666 13.903  -50.171 1.00 51.14  ? 107 GLN A CG   1 
ATOM   840  C CD   . GLN A 1 107 ? -9.896  14.198  -51.447 1.00 52.14  ? 107 GLN A CD   1 
ATOM   841  O OE1  . GLN A 1 107 ? -9.874  15.343  -51.937 1.00 51.62  ? 107 GLN A OE1  1 
ATOM   842  N NE2  . GLN A 1 107 ? -9.207  13.183  -51.955 1.00 48.23  ? 107 GLN A NE2  1 
ATOM   843  N N    . PRO A 1 108 ? -7.514  16.472  -48.184 1.00 42.07  ? 108 PRO A N    1 
ATOM   844  C CA   . PRO A 1 108 ? -7.244  17.616  -47.312 1.00 42.09  ? 108 PRO A CA   1 
ATOM   845  C C    . PRO A 1 108 ? -8.489  18.018  -46.540 1.00 45.66  ? 108 PRO A C    1 
ATOM   846  O O    . PRO A 1 108 ? -9.613  17.889  -47.024 1.00 49.61  ? 108 PRO A O    1 
ATOM   847  C CB   . PRO A 1 108 ? -6.811  18.722  -48.283 1.00 42.22  ? 108 PRO A CB   1 
ATOM   848  C CG   . PRO A 1 108 ? -7.290  18.278  -49.624 1.00 41.69  ? 108 PRO A CG   1 
ATOM   849  C CD   . PRO A 1 108 ? -7.212  16.768  -49.591 1.00 43.96  ? 108 PRO A CD   1 
ATOM   850  N N    . GLY A 1 109 ? -8.279  18.482  -45.309 1.00 42.58  ? 109 GLY A N    1 
ATOM   851  C CA   . GLY A 1 109 ? -9.370  18.857  -44.455 1.00 41.46  ? 109 GLY A CA   1 
ATOM   852  C C    . GLY A 1 109 ? -9.902  17.733  -43.593 1.00 42.25  ? 109 GLY A C    1 
ATOM   853  O O    . GLY A 1 109 ? -10.558 18.012  -42.584 1.00 42.47  ? 109 GLY A O    1 
ATOM   854  N N    . GLN A 1 110 ? -9.639  16.473  -43.959 1.00 40.26  ? 110 GLN A N    1 
ATOM   855  C CA   . GLN A 1 110 ? -10.071 15.332  -43.160 1.00 43.51  ? 110 GLN A CA   1 
ATOM   856  C C    . GLN A 1 110 ? -9.114  15.089  -41.984 1.00 43.44  ? 110 GLN A C    1 
ATOM   857  O O    . GLN A 1 110 ? -7.964  15.539  -41.969 1.00 36.41  ? 110 GLN A O    1 
ATOM   858  C CB   . GLN A 1 110 ? -10.178 14.054  -44.018 1.00 42.35  ? 110 GLN A CB   1 
ATOM   859  C CG   . GLN A 1 110 ? -11.391 14.031  -45.029 1.00 48.46  ? 110 GLN A CG   1 
ATOM   860  C CD   . GLN A 1 110 ? -12.671 14.709  -44.483 1.00 54.85  ? 110 GLN A CD   1 
ATOM   861  O OE1  . GLN A 1 110 ? -13.476 14.093  -43.769 1.00 56.90  ? 110 GLN A OE1  1 
ATOM   862  N NE2  . GLN A 1 110 ? -12.838 15.997  -44.802 1.00 55.65  ? 110 GLN A NE2  1 
ATOM   863  N N    . THR A 1 111 ? -9.607  14.344  -40.994 1.00 42.26  ? 111 THR A N    1 
ATOM   864  C CA   . THR A 1 111 ? -8.879  14.109  -39.765 1.00 39.37  ? 111 THR A CA   1 
ATOM   865  C C    . THR A 1 111 ? -8.660  12.623  -39.569 1.00 34.66  ? 111 THR A C    1 
ATOM   866  O O    . THR A 1 111 ? -9.361  11.789  -40.152 1.00 34.20  ? 111 THR A O    1 
ATOM   867  C CB   . THR A 1 111 ? -9.632  14.672  -38.560 1.00 38.96  ? 111 THR A CB   1 
ATOM   868  O OG1  . THR A 1 111 ? -10.917 14.036  -38.481 1.00 33.09  ? 111 THR A OG1  1 
ATOM   869  C CG2  . THR A 1 111 ? -9.786  16.181  -38.676 1.00 36.58  ? 111 THR A CG2  1 
ATOM   870  N N    . PHE A 1 112 ? -7.698  12.300  -38.702 1.00 30.63  ? 112 PHE A N    1 
ATOM   871  C CA   . PHE A 1 112 ? -7.370  10.916  -38.378 1.00 35.48  ? 112 PHE A CA   1 
ATOM   872  C C    . PHE A 1 112 ? -6.580  10.914  -37.076 1.00 35.04  ? 112 PHE A C    1 
ATOM   873  O O    . PHE A 1 112 ? -6.123  11.961  -36.602 1.00 36.92  ? 112 PHE A O    1 
ATOM   874  C CB   . PHE A 1 112 ? -6.572  10.228  -39.520 1.00 35.33  ? 112 PHE A CB   1 
ATOM   875  C CG   . PHE A 1 112 ? -5.280  10.951  -39.935 1.00 32.50  ? 112 PHE A CG   1 
ATOM   876  C CD1  . PHE A 1 112 ? -5.295  11.958  -40.905 1.00 34.25  ? 112 PHE A CD1  1 
ATOM   877  C CD2  . PHE A 1 112 ? -4.056  10.562  -39.413 1.00 31.77  ? 112 PHE A CD2  1 
ATOM   878  C CE1  . PHE A 1 112 ? -4.113  12.593  -41.312 1.00 39.40  ? 112 PHE A CE1  1 
ATOM   879  C CE2  . PHE A 1 112 ? -2.847  11.180  -39.819 1.00 29.18  ? 112 PHE A CE2  1 
ATOM   880  C CZ   . PHE A 1 112 ? -2.871  12.198  -40.754 1.00 35.72  ? 112 PHE A CZ   1 
ATOM   881  N N    . SER A 1 113 ? -6.471  9.723   -36.485 1.00 26.55  ? 113 SER A N    1 
ATOM   882  C CA   . SER A 1 113 ? -5.718  9.453   -35.269 1.00 34.76  ? 113 SER A CA   1 
ATOM   883  C C    . SER A 1 113 ? -4.352  8.914   -35.643 1.00 33.36  ? 113 SER A C    1 
ATOM   884  O O    . SER A 1 113 ? -4.225  8.154   -36.600 1.00 34.53  ? 113 SER A O    1 
ATOM   885  C CB   . SER A 1 113 ? -6.415  8.424   -34.380 1.00 33.95  ? 113 SER A CB   1 
ATOM   886  O OG   . SER A 1 113 ? -7.606  8.977   -33.855 1.00 37.32  ? 113 SER A OG   1 
ATOM   887  N N    . VAL A 1 114 ? -3.341  9.321   -34.886 1.00 32.57  ? 114 VAL A N    1 
ATOM   888  C CA   . VAL A 1 114 ? -1.964  8.896   -35.053 1.00 31.05  ? 114 VAL A CA   1 
ATOM   889  C C    . VAL A 1 114 ? -1.547  8.145   -33.805 1.00 33.63  ? 114 VAL A C    1 
ATOM   890  O O    . VAL A 1 114 ? -1.698  8.656   -32.690 1.00 31.15  ? 114 VAL A O    1 
ATOM   891  C CB   . VAL A 1 114 ? -1.014  10.085  -35.290 1.00 33.77  ? 114 VAL A CB   1 
ATOM   892  C CG1  . VAL A 1 114 ? 0.423   9.570   -35.323 1.00 30.96  ? 114 VAL A CG1  1 
ATOM   893  C CG2  . VAL A 1 114 ? -1.361  10.819  -36.581 1.00 32.90  ? 114 VAL A CG2  1 
ATOM   894  N N    . LEU A 1 115 ? -1.006  6.945   -33.990 1.00 31.24  ? 115 LEU A N    1 
ATOM   895  C CA   . LEU A 1 115 ? -0.410  6.181   -32.914 1.00 34.04  ? 115 LEU A CA   1 
ATOM   896  C C    . LEU A 1 115 ? 1.092   6.326   -33.094 1.00 35.97  ? 115 LEU A C    1 
ATOM   897  O O    . LEU A 1 115 ? 1.689   5.670   -33.959 1.00 33.25  ? 115 LEU A O    1 
ATOM   898  C CB   . LEU A 1 115 ? -0.852  4.717   -32.953 1.00 35.60  ? 115 LEU A CB   1 
ATOM   899  C CG   . LEU A 1 115 ? -0.215  3.848   -31.869 1.00 36.67  ? 115 LEU A CG   1 
ATOM   900  C CD1  . LEU A 1 115 ? -0.805  4.172   -30.486 1.00 38.15  ? 115 LEU A CD1  1 
ATOM   901  C CD2  . LEU A 1 115 ? -0.314  2.352   -32.182 1.00 38.65  ? 115 LEU A CD2  1 
ATOM   902  N N    . ALA A 1 116 ? 1.689   7.236   -32.319 1.00 35.29  ? 116 ALA A N    1 
ATOM   903  C CA   . ALA A 1 116 ? 3.126   7.468   -32.374 1.00 38.71  ? 116 ALA A CA   1 
ATOM   904  C C    . ALA A 1 116 ? 3.845   6.289   -31.741 1.00 41.55  ? 116 ALA A C    1 
ATOM   905  O O    . ALA A 1 116 ? 3.542   5.906   -30.602 1.00 38.32  ? 116 ALA A O    1 
ATOM   906  C CB   . ALA A 1 116 ? 3.506   8.778   -31.657 1.00 35.20  ? 116 ALA A CB   1 
ATOM   907  N N    . CYS A 1 117 ? 4.833   5.741   -32.466 1.00 38.78  ? 117 CYS A N    1 
ATOM   908  C CA   . CYS A 1 117 ? 5.541   4.536   -32.069 1.00 42.32  ? 117 CYS A CA   1 
ATOM   909  C C    . CYS A 1 117 ? 7.041   4.729   -32.192 1.00 44.05  ? 117 CYS A C    1 
ATOM   910  O O    . CYS A 1 117 ? 7.510   5.504   -33.027 1.00 43.27  ? 117 CYS A O    1 
ATOM   911  C CB   . CYS A 1 117 ? 5.145   3.342   -32.940 1.00 44.38  ? 117 CYS A CB   1 
ATOM   912  S SG   . CYS A 1 117 ? 3.449   2.826   -32.738 1.00 47.22  ? 117 CYS A SG   1 
ATOM   913  N N    . TYR A 1 118 ? 7.783   3.994   -31.356 1.00 48.34  ? 118 TYR A N    1 
ATOM   914  C CA   . TYR A 1 118 ? 9.244   3.962   -31.347 1.00 51.16  ? 118 TYR A CA   1 
ATOM   915  C C    . TYR A 1 118 ? 9.678   2.521   -31.129 1.00 54.04  ? 118 TYR A C    1 
ATOM   916  O O    . TYR A 1 118 ? 9.218   1.864   -30.184 1.00 54.28  ? 118 TYR A O    1 
ATOM   917  C CB   . TYR A 1 118 ? 9.841   4.904   -30.267 1.00 49.97  ? 118 TYR A CB   1 
ATOM   918  C CG   . TYR A 1 118 ? 9.450   6.347   -30.555 1.00 52.85  ? 118 TYR A CG   1 
ATOM   919  C CD1  . TYR A 1 118 ? 10.213  7.143   -31.427 1.00 51.72  ? 118 TYR A CD1  1 
ATOM   920  C CD2  . TYR A 1 118 ? 8.257   6.878   -30.064 1.00 50.36  ? 118 TYR A CD2  1 
ATOM   921  C CE1  . TYR A 1 118 ? 9.833   8.449   -31.747 1.00 47.02  ? 118 TYR A CE1  1 
ATOM   922  C CE2  . TYR A 1 118 ? 7.858   8.178   -30.400 1.00 50.47  ? 118 TYR A CE2  1 
ATOM   923  C CZ   . TYR A 1 118 ? 8.659   8.957   -31.233 1.00 49.19  ? 118 TYR A CZ   1 
ATOM   924  O OH   . TYR A 1 118 ? 8.272   10.240  -31.566 1.00 47.29  ? 118 TYR A OH   1 
ATOM   925  N N    . ASN A 1 119 ? 10.507  2.016   -32.049 1.00 51.75  ? 119 ASN A N    1 
ATOM   926  C CA   . ASN A 1 119 ? 11.042  0.660   -31.976 1.00 54.08  ? 119 ASN A CA   1 
ATOM   927  C C    . ASN A 1 119 ? 9.937   -0.384  -32.008 1.00 56.09  ? 119 ASN A C    1 
ATOM   928  O O    . ASN A 1 119 ? 10.058  -1.437  -31.371 1.00 55.38  ? 119 ASN A O    1 
ATOM   929  C CB   . ASN A 1 119 ? 11.894  0.469   -30.721 1.00 56.09  ? 119 ASN A CB   1 
ATOM   930  C CG   . ASN A 1 119 ? 13.146  1.286   -30.761 1.00 63.46  ? 119 ASN A CG   1 
ATOM   931  O OD1  . ASN A 1 119 ? 13.982  1.107   -31.648 1.00 67.51  ? 119 ASN A OD1  1 
ATOM   932  N ND2  . ASN A 1 119 ? 13.286  2.206   -29.814 1.00 64.50  ? 119 ASN A ND2  1 
ATOM   933  N N    . GLY A 1 120 ? 8.863   -0.094  -32.740 1.00 51.27  ? 120 GLY A N    1 
ATOM   934  C CA   . GLY A 1 120 ? 7.725   -0.979  -32.794 1.00 50.47  ? 120 GLY A CA   1 
ATOM   935  C C    . GLY A 1 120 ? 6.846   -0.987  -31.562 1.00 53.82  ? 120 GLY A C    1 
ATOM   936  O O    . GLY A 1 120 ? 6.004   -1.888  -31.433 1.00 52.55  ? 120 GLY A O    1 
ATOM   937  N N    . SER A 1 121 ? 6.996   -0.013  -30.660 1.00 54.41  ? 121 SER A N    1 
ATOM   938  C CA   . SER A 1 121 ? 6.209   0.041   -29.424 1.00 57.13  ? 121 SER A CA   1 
ATOM   939  C C    . SER A 1 121 ? 5.368   1.308   -29.373 1.00 53.56  ? 121 SER A C    1 
ATOM   940  O O    . SER A 1 121 ? 5.922   2.421   -29.418 1.00 50.77  ? 121 SER A O    1 
ATOM   941  C CB   . SER A 1 121 ? 7.091   -0.046  -28.176 1.00 53.12  ? 121 SER A CB   1 
ATOM   942  O OG   . SER A 1 121 ? 7.690   -1.323  -28.097 1.00 64.68  ? 121 SER A OG   1 
ATOM   943  N N    . PRO A 1 122 ? 4.045   1.197   -29.278 1.00 52.35  ? 122 PRO A N    1 
ATOM   944  C CA   . PRO A 1 122 ? 3.216   2.407   -29.202 1.00 49.57  ? 122 PRO A CA   1 
ATOM   945  C C    . PRO A 1 122 ? 3.591   3.275   -28.007 1.00 53.20  ? 122 PRO A C    1 
ATOM   946  O O    . PRO A 1 122 ? 3.841   2.788   -26.903 1.00 58.00  ? 122 PRO A O    1 
ATOM   947  C CB   . PRO A 1 122 ? 1.782   1.872   -29.097 1.00 52.08  ? 122 PRO A CB   1 
ATOM   948  C CG   . PRO A 1 122 ? 1.876   0.384   -28.924 1.00 56.25  ? 122 PRO A CG   1 
ATOM   949  C CD   . PRO A 1 122 ? 3.314   -0.053  -29.007 1.00 52.97  ? 122 PRO A CD   1 
ATOM   950  N N    . SER A 1 123 ? 3.641   4.582   -28.250 1.00 52.33  ? 123 SER A N    1 
ATOM   951  C CA   . SER A 1 123 ? 3.977   5.563   -27.228 1.00 55.98  ? 123 SER A CA   1 
ATOM   952  C C    . SER A 1 123 ? 2.817   6.487   -26.868 1.00 52.69  ? 123 SER A C    1 
ATOM   953  O O    . SER A 1 123 ? 2.693   6.874   -25.701 1.00 53.56  ? 123 SER A O    1 
ATOM   954  C CB   . SER A 1 123 ? 5.179   6.398   -27.694 1.00 56.20  ? 123 SER A CB   1 
ATOM   955  O OG   . SER A 1 123 ? 5.288   7.626   -27.007 1.00 60.30  ? 123 SER A OG   1 
ATOM   956  N N    . GLY A 1 124 ? 1.961   6.832   -27.825 1.00 42.72  ? 124 GLY A N    1 
ATOM   957  C CA   . GLY A 1 124 ? 0.855   7.726   -27.540 1.00 39.88  ? 124 GLY A CA   1 
ATOM   958  C C    . GLY A 1 124 ? -0.016  7.883   -28.764 1.00 40.41  ? 124 GLY A C    1 
ATOM   959  O O    . GLY A 1 124 ? 0.374   7.533   -29.883 1.00 35.16  ? 124 GLY A O    1 
ATOM   960  N N    . VAL A 1 125 ? -1.223  8.387   -28.531 1.00 37.34  ? 125 VAL A N    1 
ATOM   961  C CA   . VAL A 1 125 ? -2.188  8.585   -29.602 1.00 34.51  ? 125 VAL A CA   1 
ATOM   962  C C    . VAL A 1 125 ? -2.736  10.005  -29.519 1.00 33.11  ? 125 VAL A C    1 
ATOM   963  O O    . VAL A 1 125 ? -2.913  10.543  -28.421 1.00 34.42  ? 125 VAL A O    1 
ATOM   964  C CB   . VAL A 1 125 ? -3.321  7.532   -29.525 1.00 34.85  ? 125 VAL A CB   1 
ATOM   965  C CG1  . VAL A 1 125 ? -4.113  7.718   -28.241 1.00 37.16  ? 125 VAL A CG1  1 
ATOM   966  C CG2  . VAL A 1 125 ? -4.235  7.639   -30.715 1.00 35.68  ? 125 VAL A CG2  1 
ATOM   967  N N    . TYR A 1 126 ? -2.987  10.616  -30.678 1.00 35.73  ? 126 TYR A N    1 
ATOM   968  C CA   . TYR A 1 126 ? -3.575  11.955  -30.751 1.00 35.76  ? 126 TYR A CA   1 
ATOM   969  C C    . TYR A 1 126 ? -4.256  12.114  -32.108 1.00 36.48  ? 126 TYR A C    1 
ATOM   970  O O    . TYR A 1 126 ? -4.045  11.321  -33.027 1.00 34.49  ? 126 TYR A O    1 
ATOM   971  C CB   . TYR A 1 126 ? -2.511  13.059  -30.542 1.00 36.57  ? 126 TYR A CB   1 
ATOM   972  C CG   . TYR A 1 126 ? -1.307  12.933  -31.476 1.00 39.32  ? 126 TYR A CG   1 
ATOM   973  C CD1  . TYR A 1 126 ? -1.295  13.548  -32.720 1.00 41.40  ? 126 TYR A CD1  1 
ATOM   974  C CD2  . TYR A 1 126 ? -0.195  12.179  -31.117 1.00 39.88  ? 126 TYR A CD2  1 
ATOM   975  C CE1  . TYR A 1 126 ? -0.197  13.426  -33.590 1.00 38.39  ? 126 TYR A CE1  1 
ATOM   976  C CE2  . TYR A 1 126 ? 0.912   12.061  -31.975 1.00 42.23  ? 126 TYR A CE2  1 
ATOM   977  C CZ   . TYR A 1 126 ? 0.888   12.678  -33.224 1.00 40.14  ? 126 TYR A CZ   1 
ATOM   978  O OH   . TYR A 1 126 ? 1.974   12.588  -34.087 1.00 41.84  ? 126 TYR A OH   1 
ATOM   979  N N    . GLN A 1 127 ? -5.040  13.180  -32.241 1.00 36.06  ? 127 GLN A N    1 
ATOM   980  C CA   . GLN A 1 127 ? -5.806  13.434  -33.453 1.00 38.24  ? 127 GLN A CA   1 
ATOM   981  C C    . GLN A 1 127 ? -5.163  14.567  -34.255 1.00 39.13  ? 127 GLN A C    1 
ATOM   982  O O    . GLN A 1 127 ? -4.661  15.536  -33.682 1.00 39.68  ? 127 GLN A O    1 
ATOM   983  C CB   . GLN A 1 127 ? -7.261  13.761  -33.108 1.00 32.68  ? 127 GLN A CB   1 
ATOM   984  C CG   . GLN A 1 127 ? -8.198  13.710  -34.293 1.00 42.23  ? 127 GLN A CG   1 
ATOM   985  C CD   . GLN A 1 127 ? -8.901  12.369  -34.480 1.00 42.65  ? 127 GLN A CD   1 
ATOM   986  O OE1  . GLN A 1 127 ? -8.383  11.309  -34.114 1.00 38.92  ? 127 GLN A OE1  1 
ATOM   987  N NE2  . GLN A 1 127 ? -10.096 12.414  -35.075 1.00 42.96  ? 127 GLN A NE2  1 
ATOM   988  N N    . CYS A 1 128 ? -5.153  14.431  -35.586 1.00 37.10  ? 128 CYS A N    1 
ATOM   989  C CA   A CYS A 1 128 ? -4.535  15.383  -36.512 0.53 37.81  ? 128 CYS A CA   1 
ATOM   990  C CA   B CYS A 1 128 ? -4.667  15.528  -36.407 0.47 37.70  ? 128 CYS A CA   1 
ATOM   991  C C    . CYS A 1 128 ? -5.459  15.611  -37.702 1.00 40.19  ? 128 CYS A C    1 
ATOM   992  O O    . CYS A 1 128 ? -6.265  14.737  -38.049 1.00 37.43  ? 128 CYS A O    1 
ATOM   993  C CB   A CYS A 1 128 ? -3.194  14.876  -37.078 0.53 36.49  ? 128 CYS A CB   1 
ATOM   994  C CB   B CYS A 1 128 ? -3.190  15.379  -36.726 0.47 37.96  ? 128 CYS A CB   1 
ATOM   995  S SG   A CYS A 1 128 ? -1.765  14.852  -35.987 0.53 42.34  ? 128 CYS A SG   1 
ATOM   996  S SG   B CYS A 1 128 ? -2.946  13.959  -37.714 0.47 36.81  ? 128 CYS A SG   1 
ATOM   997  N N    . ALA A 1 129 ? -5.254  16.724  -38.394 1.00 37.11  ? 129 ALA A N    1 
ATOM   998  C CA   . ALA A 1 129 ? -5.925  16.994  -39.653 1.00 39.61  ? 129 ALA A CA   1 
ATOM   999  C C    . ALA A 1 129 ? -4.911  17.024  -40.792 1.00 37.24  ? 129 ALA A C    1 
ATOM   1000 O O    . ALA A 1 129 ? -3.800  17.539  -40.644 1.00 35.09  ? 129 ALA A O    1 
ATOM   1001 C CB   . ALA A 1 129 ? -6.671  18.321  -39.592 1.00 39.71  ? 129 ALA A CB   1 
ATOM   1002 N N    . MET A 1 130 ? -5.281  16.476  -41.937 1.00 35.18  ? 130 MET A N    1 
ATOM   1003 C CA   . MET A 1 130 ? -4.458  16.696  -43.119 1.00 36.65  ? 130 MET A CA   1 
ATOM   1004 C C    . MET A 1 130 ? -4.679  18.154  -43.568 1.00 35.46  ? 130 MET A C    1 
ATOM   1005 O O    . MET A 1 130 ? -5.777  18.513  -44.009 1.00 39.01  ? 130 MET A O    1 
ATOM   1006 C CB   . MET A 1 130 ? -4.820  15.660  -44.181 1.00 40.84  ? 130 MET A CB   1 
ATOM   1007 C CG   . MET A 1 130 ? -4.105  15.817  -45.514 1.00 38.70  ? 130 MET A CG   1 
ATOM   1008 S SD   . MET A 1 130 ? -2.329  15.614  -45.223 1.00 45.29  ? 130 MET A SD   1 
ATOM   1009 C CE   . MET A 1 130 ? -2.279  13.903  -44.690 1.00 35.17  ? 130 MET A CE   1 
ATOM   1010 N N    . ARG A 1 131 ? -3.677  19.031  -43.360 1.00 35.56  ? 131 ARG A N    1 
ATOM   1011 C CA   . ARG A 1 131 ? -3.808  20.436  -43.745 1.00 39.10  ? 131 ARG A CA   1 
ATOM   1012 C C    . ARG A 1 131 ? -4.098  20.576  -45.246 1.00 41.68  ? 131 ARG A C    1 
ATOM   1013 O O    . ARG A 1 131 ? -3.801  19.680  -46.045 1.00 37.02  ? 131 ARG A O    1 
ATOM   1014 C CB   . ARG A 1 131 ? -2.541  21.240  -43.431 1.00 38.24  ? 131 ARG A CB   1 
ATOM   1015 C CG   . ARG A 1 131 ? -1.977  21.123  -42.029 1.00 41.50  ? 131 ARG A CG   1 
ATOM   1016 C CD   . ARG A 1 131 ? -2.850  21.765  -40.988 1.00 43.91  ? 131 ARG A CD   1 
ATOM   1017 N NE   . ARG A 1 131 ? -3.387  23.057  -41.391 1.00 46.00  ? 131 ARG A NE   1 
ATOM   1018 C CZ   . ARG A 1 131 ? -4.514  23.540  -40.894 1.00 46.20  ? 131 ARG A CZ   1 
ATOM   1019 N NH1  . ARG A 1 131 ? -5.192  22.877  -39.961 1.00 41.10  ? 131 ARG A NH1  1 
ATOM   1020 N NH2  . ARG A 1 131 ? -4.966  24.712  -41.328 1.00 39.50  ? 131 ARG A NH2  1 
ATOM   1021 N N    . PRO A 1 132 ? -4.645  21.717  -45.657 1.00 40.30  ? 132 PRO A N    1 
ATOM   1022 C CA   . PRO A 1 132 ? -4.796  21.969  -47.093 1.00 42.57  ? 132 PRO A CA   1 
ATOM   1023 C C    . PRO A 1 132 ? -3.495  21.843  -47.857 1.00 43.44  ? 132 PRO A C    1 
ATOM   1024 O O    . PRO A 1 132 ? -3.520  21.488  -49.041 1.00 43.53  ? 132 PRO A O    1 
ATOM   1025 C CB   . PRO A 1 132 ? -5.347  23.405  -47.140 1.00 45.47  ? 132 PRO A CB   1 
ATOM   1026 C CG   . PRO A 1 132 ? -6.086  23.560  -45.900 1.00 47.94  ? 132 PRO A CG   1 
ATOM   1027 C CD   . PRO A 1 132 ? -5.249  22.788  -44.851 1.00 45.54  ? 132 PRO A CD   1 
ATOM   1028 N N    . ASN A 1 133 ? -2.350  22.074  -47.217 1.00 42.82  ? 133 ASN A N    1 
ATOM   1029 C CA   . ASN A 1 133 ? -1.070  21.988  -47.903 1.00 40.35  ? 133 ASN A CA   1 
ATOM   1030 C C    . ASN A 1 133 ? -0.419  20.614  -47.745 1.00 38.14  ? 133 ASN A C    1 
ATOM   1031 O O    . ASN A 1 133 ? 0.790   20.461  -48.003 1.00 37.00  ? 133 ASN A O    1 
ATOM   1032 C CB   . ASN A 1 133 ? -0.146  23.108  -47.429 1.00 40.10  ? 133 ASN A CB   1 
ATOM   1033 C CG   . ASN A 1 133 ? 0.268   22.956  -45.950 1.00 43.37  ? 133 ASN A CG   1 
ATOM   1034 O OD1  . ASN A 1 133 ? -0.128  22.010  -45.272 1.00 34.30  ? 133 ASN A OD1  1 
ATOM   1035 N ND2  . ASN A 1 133 ? 1.042   23.909  -45.456 1.00 41.05  ? 133 ASN A ND2  1 
ATOM   1036 N N    . PHE A 1 134 ? -1.187  19.618  -47.312 1.00 34.96  ? 134 PHE A N    1 
ATOM   1037 C CA   . PHE A 1 134 ? -0.762  18.220  -47.262 1.00 36.58  ? 134 PHE A CA   1 
ATOM   1038 C C    . PHE A 1 134 ? 0.338   17.923  -46.236 1.00 37.22  ? 134 PHE A C    1 
ATOM   1039 O O    . PHE A 1 134 ? 1.039   16.911  -46.357 1.00 40.44  ? 134 PHE A O    1 
ATOM   1040 C CB   . PHE A 1 134 ? -0.359  17.756  -48.664 1.00 40.87  ? 134 PHE A CB   1 
ATOM   1041 C CG   . PHE A 1 134 ? -1.554  17.589  -49.589 1.00 40.53  ? 134 PHE A CG   1 
ATOM   1042 C CD1  . PHE A 1 134 ? -2.445  16.565  -49.396 1.00 39.89  ? 134 PHE A CD1  1 
ATOM   1043 C CD2  . PHE A 1 134 ? -1.837  18.541  -50.570 1.00 39.70  ? 134 PHE A CD2  1 
ATOM   1044 C CE1  . PHE A 1 134 ? -3.566  16.403  -50.247 1.00 44.80  ? 134 PHE A CE1  1 
ATOM   1045 C CE2  . PHE A 1 134 ? -2.955  18.406  -51.410 1.00 42.11  ? 134 PHE A CE2  1 
ATOM   1046 C CZ   . PHE A 1 134 ? -3.825  17.334  -51.241 1.00 41.81  ? 134 PHE A CZ   1 
ATOM   1047 N N    . THR A 1 135 ? 0.468   18.748  -45.193 1.00 39.60  ? 135 THR A N    1 
ATOM   1048 C CA   . THR A 1 135 ? 1.280   18.441  -44.020 1.00 40.30  ? 135 THR A CA   1 
ATOM   1049 C C    . THR A 1 135 ? 0.392   18.148  -42.810 1.00 38.67  ? 135 THR A C    1 
ATOM   1050 O O    . THR A 1 135 ? -0.824  18.375  -42.814 1.00 41.14  ? 135 THR A O    1 
ATOM   1051 C CB   . THR A 1 135 ? 2.226   19.600  -43.703 1.00 37.05  ? 135 THR A CB   1 
ATOM   1052 O OG1  . THR A 1 135 ? 1.478   20.723  -43.223 1.00 35.35  ? 135 THR A OG1  1 
ATOM   1053 C CG2  . THR A 1 135 ? 2.965   20.023  -44.941 1.00 40.97  ? 135 THR A CG2  1 
ATOM   1054 N N    . ILE A 1 136 ? 1.003   17.638  -41.745 1.00 38.46  ? 136 ILE A N    1 
ATOM   1055 C CA   . ILE A 1 136 ? 0.291   17.480  -40.483 1.00 38.25  ? 136 ILE A CA   1 
ATOM   1056 C C    . ILE A 1 136 ? 1.113   18.095  -39.351 1.00 42.56  ? 136 ILE A C    1 
ATOM   1057 O O    . ILE A 1 136 ? 2.339   18.233  -39.435 1.00 35.82  ? 136 ILE A O    1 
ATOM   1058 C CB   . ILE A 1 136 ? -0.088  16.016  -40.199 1.00 35.72  ? 136 ILE A CB   1 
ATOM   1059 C CG1  . ILE A 1 136 ? 1.154   15.154  -39.923 1.00 37.67  ? 136 ILE A CG1  1 
ATOM   1060 C CG2  . ILE A 1 136 ? -0.909  15.463  -41.351 1.00 36.16  ? 136 ILE A CG2  1 
ATOM   1061 C CD1  . ILE A 1 136 ? 0.812   13.755  -39.490 1.00 33.03  ? 136 ILE A CD1  1 
ATOM   1062 N N    . LYS A 1 137 ? 0.409   18.535  -38.312 1.00 41.67  ? 137 LYS A N    1 
ATOM   1063 C CA   . LYS A 1 137 ? 1.006   19.190  -37.154 1.00 42.13  ? 137 LYS A CA   1 
ATOM   1064 C C    . LYS A 1 137 ? 0.965   18.141  -36.046 1.00 43.67  ? 137 LYS A C    1 
ATOM   1065 O O    . LYS A 1 137 ? -0.019  18.020  -35.311 1.00 45.61  ? 137 LYS A O    1 
ATOM   1066 C CB   . LYS A 1 137 ? 0.251   20.467  -36.781 1.00 44.46  ? 137 LYS A CB   1 
ATOM   1067 C CG   . LYS A 1 137 ? 0.591   21.673  -37.632 1.00 48.77  ? 137 LYS A CG   1 
ATOM   1068 C CD   . LYS A 1 137 ? -0.032  22.948  -37.070 1.00 58.34  ? 137 LYS A CD   1 
ATOM   1069 C CE   . LYS A 1 137 ? -0.327  23.992  -38.166 1.00 69.32  ? 137 LYS A CE   1 
ATOM   1070 N NZ   . LYS A 1 137 ? -1.518  24.846  -37.809 1.00 66.28  ? 137 LYS A NZ   1 
ATOM   1071 N N    . GLY A 1 138 ? 2.021   17.334  -35.964 1.00 43.63  ? 138 GLY A N    1 
ATOM   1072 C CA   . GLY A 1 138 ? 2.016   16.282  -34.973 1.00 43.24  ? 138 GLY A CA   1 
ATOM   1073 C C    . GLY A 1 138 ? 3.152   16.367  -33.979 1.00 43.20  ? 138 GLY A C    1 
ATOM   1074 O O    . GLY A 1 138 ? 3.636   17.461  -33.653 1.00 46.92  ? 138 GLY A O    1 
ATOM   1075 N N    . SER A 1 139 ? 3.586   15.202  -33.493 1.00 45.55  ? 139 SER A N    1 
ATOM   1076 C CA   . SER A 1 139 ? 4.636   15.087  -32.474 1.00 44.14  ? 139 SER A CA   1 
ATOM   1077 C C    . SER A 1 139 ? 5.410   13.822  -32.825 1.00 41.26  ? 139 SER A C    1 
ATOM   1078 O O    . SER A 1 139 ? 4.957   12.709  -32.533 1.00 40.02  ? 139 SER A O    1 
ATOM   1079 C CB   . SER A 1 139 ? 4.039   15.006  -31.068 1.00 46.20  ? 139 SER A CB   1 
ATOM   1080 O OG   . SER A 1 139 ? 5.049   14.854  -30.067 1.00 44.20  ? 139 SER A OG   1 
ATOM   1081 N N    . PHE A 1 140 ? 6.511   13.989  -33.542 1.00 38.43  ? 140 PHE A N    1 
ATOM   1082 C CA   . PHE A 1 140 ? 7.311   12.860  -34.005 1.00 44.36  ? 140 PHE A CA   1 
ATOM   1083 C C    . PHE A 1 140 ? 8.771   13.170  -33.712 1.00 45.32  ? 140 PHE A C    1 
ATOM   1084 O O    . PHE A 1 140 ? 9.253   14.252  -34.060 1.00 41.21  ? 140 PHE A O    1 
ATOM   1085 C CB   . PHE A 1 140 ? 7.154   12.587  -35.519 1.00 42.80  ? 140 PHE A CB   1 
ATOM   1086 C CG   . PHE A 1 140 ? 5.748   12.240  -35.965 1.00 40.45  ? 140 PHE A CG   1 
ATOM   1087 C CD1  . PHE A 1 140 ? 5.243   10.968  -35.797 1.00 40.72  ? 140 PHE A CD1  1 
ATOM   1088 C CD2  . PHE A 1 140 ? 4.977   13.173  -36.649 1.00 39.83  ? 140 PHE A CD2  1 
ATOM   1089 C CE1  . PHE A 1 140 ? 3.955   10.642  -36.243 1.00 39.79  ? 140 PHE A CE1  1 
ATOM   1090 C CE2  . PHE A 1 140 ? 3.704   12.860  -37.099 1.00 38.61  ? 140 PHE A CE2  1 
ATOM   1091 C CZ   . PHE A 1 140 ? 3.192   11.596  -36.905 1.00 40.00  ? 140 PHE A CZ   1 
ATOM   1092 N N    . LEU A 1 141 ? 9.462   12.247  -33.059 1.00 46.48  ? 141 LEU A N    1 
ATOM   1093 C CA   . LEU A 1 141 ? 10.906  12.342  -32.904 1.00 52.22  ? 141 LEU A CA   1 
ATOM   1094 C C    . LEU A 1 141 ? 11.591  11.385  -33.876 1.00 51.51  ? 141 LEU A C    1 
ATOM   1095 O O    . LEU A 1 141 ? 10.943  10.621  -34.604 1.00 45.63  ? 141 LEU A O    1 
ATOM   1096 C CB   . LEU A 1 141 ? 11.316  12.038  -31.458 1.00 50.11  ? 141 LEU A CB   1 
ATOM   1097 C CG   . LEU A 1 141 ? 10.631  12.961  -30.434 1.00 56.89  ? 141 LEU A CG   1 
ATOM   1098 C CD1  . LEU A 1 141 ? 10.767  12.410  -28.996 1.00 56.87  ? 141 LEU A CD1  1 
ATOM   1099 C CD2  . LEU A 1 141 ? 11.125  14.435  -30.540 1.00 50.81  ? 141 LEU A CD2  1 
ATOM   1100 N N    . ASN A 1 142 ? 12.921  11.466  -33.908 1.00 52.74  ? 142 ASN A N    1 
ATOM   1101 C CA   . ASN A 1 142 ? 13.712  10.481  -34.632 1.00 53.61  ? 142 ASN A CA   1 
ATOM   1102 C C    . ASN A 1 142 ? 13.231  9.089   -34.247 1.00 53.98  ? 142 ASN A C    1 
ATOM   1103 O O    . ASN A 1 142 ? 12.963  8.822   -33.070 1.00 53.26  ? 142 ASN A O    1 
ATOM   1104 C CB   . ASN A 1 142 ? 15.189  10.648  -34.279 1.00 56.36  ? 142 ASN A CB   1 
ATOM   1105 C CG   . ASN A 1 142 ? 16.119  10.244  -35.417 1.00 72.16  ? 142 ASN A CG   1 
ATOM   1106 O OD1  . ASN A 1 142 ? 16.571  9.093   -35.500 1.00 74.03  ? 142 ASN A OD1  1 
ATOM   1107 N ND2  . ASN A 1 142 ? 16.427  11.204  -36.293 1.00 70.20  ? 142 ASN A ND2  1 
ATOM   1108 N N    . GLY A 1 143 ? 13.099  8.208   -35.238 1.00 51.60  ? 143 GLY A N    1 
ATOM   1109 C CA   . GLY A 1 143 ? 12.595  6.867   -34.994 1.00 50.34  ? 143 GLY A CA   1 
ATOM   1110 C C    . GLY A 1 143 ? 11.085  6.707   -34.997 1.00 48.09  ? 143 GLY A C    1 
ATOM   1111 O O    . GLY A 1 143 ? 10.593  5.576   -34.882 1.00 48.81  ? 143 GLY A O    1 
ATOM   1112 N N    . SER A 1 144 ? 10.326  7.779   -35.158 1.00 48.10  ? 144 SER A N    1 
ATOM   1113 C CA   . SER A 1 144 ? 8.877   7.631   -35.240 1.00 42.10  ? 144 SER A CA   1 
ATOM   1114 C C    . SER A 1 144 ? 8.385   7.157   -36.606 1.00 44.36  ? 144 SER A C    1 
ATOM   1115 O O    . SER A 1 144 ? 7.183   6.860   -36.748 1.00 37.85  ? 144 SER A O    1 
ATOM   1116 C CB   . SER A 1 144 ? 8.205   8.975   -34.905 1.00 44.16  ? 144 SER A CB   1 
ATOM   1117 O OG   . SER A 1 144 ? 8.589   10.007  -35.803 1.00 41.76  ? 144 SER A OG   1 
ATOM   1118 N N    . CYS A 1 145 ? 9.277   7.078   -37.598 1.00 44.30  ? 145 CYS A N    1 
ATOM   1119 C CA   . CYS A 1 145 ? 8.891   6.729   -38.961 1.00 42.69  ? 145 CYS A CA   1 
ATOM   1120 C C    . CYS A 1 145 ? 8.220   5.362   -39.040 1.00 38.13  ? 145 CYS A C    1 
ATOM   1121 O O    . CYS A 1 145 ? 8.651   4.391   -38.411 1.00 37.34  ? 145 CYS A O    1 
ATOM   1122 C CB   . CYS A 1 145 ? 10.127  6.757   -39.876 1.00 45.11  ? 145 CYS A CB   1 
ATOM   1123 S SG   . CYS A 1 145 ? 10.568  8.456   -40.288 1.00 51.77  ? 145 CYS A SG   1 
ATOM   1124 N N    . GLY A 1 146 ? 7.212   5.272   -39.895 1.00 37.04  ? 146 GLY A N    1 
ATOM   1125 C CA   . GLY A 1 146 ? 6.394   4.092   -39.938 1.00 39.67  ? 146 GLY A CA   1 
ATOM   1126 C C    . GLY A 1 146 ? 5.251   4.094   -38.954 1.00 38.99  ? 146 GLY A C    1 
ATOM   1127 O O    . GLY A 1 146 ? 4.439   3.164   -38.993 1.00 37.87  ? 146 GLY A O    1 
ATOM   1128 N N    . SER A 1 147 ? 5.146   5.119   -38.096 1.00 37.00  ? 147 SER A N    1 
ATOM   1129 C CA   . SER A 1 147 ? 3.929   5.308   -37.307 1.00 37.91  ? 147 SER A CA   1 
ATOM   1130 C C    . SER A 1 147 ? 2.787   5.635   -38.256 1.00 34.02  ? 147 SER A C    1 
ATOM   1131 O O    . SER A 1 147 ? 2.983   6.314   -39.270 1.00 34.45  ? 147 SER A O    1 
ATOM   1132 C CB   . SER A 1 147 ? 4.091   6.458   -36.300 1.00 34.09  ? 147 SER A CB   1 
ATOM   1133 O OG   . SER A 1 147 ? 5.121   6.206   -35.358 1.00 35.32  ? 147 SER A OG   1 
ATOM   1134 N N    . VAL A 1 148 ? 1.579   5.162   -37.933 1.00 33.30  ? 148 VAL A N    1 
ATOM   1135 C CA   . VAL A 1 148 ? 0.493   5.277   -38.901 1.00 29.94  ? 148 VAL A CA   1 
ATOM   1136 C C    . VAL A 1 148 ? -0.661  6.054   -38.304 1.00 29.29  ? 148 VAL A C    1 
ATOM   1137 O O    . VAL A 1 148 ? -0.857  6.083   -37.083 1.00 29.62  ? 148 VAL A O    1 
ATOM   1138 C CB   . VAL A 1 148 ? 0.040   3.887   -39.392 1.00 31.70  ? 148 VAL A CB   1 
ATOM   1139 C CG1  . VAL A 1 148 ? 1.243   3.099   -39.948 1.00 31.05  ? 148 VAL A CG1  1 
ATOM   1140 C CG2  . VAL A 1 148 ? -0.553  3.108   -38.279 1.00 32.37  ? 148 VAL A CG2  1 
ATOM   1141 N N    . GLY A 1 149 ? -1.405  6.716   -39.195 1.00 27.05  ? 149 GLY A N    1 
ATOM   1142 C CA   . GLY A 1 149 ? -2.648  7.391   -38.877 1.00 31.76  ? 149 GLY A CA   1 
ATOM   1143 C C    . GLY A 1 149 ? -3.826  6.605   -39.442 1.00 37.05  ? 149 GLY A C    1 
ATOM   1144 O O    . GLY A 1 149 ? -3.698  5.905   -40.448 1.00 31.53  ? 149 GLY A O    1 
ATOM   1145 N N    . PHE A 1 150 ? -4.979  6.703   -38.780 1.00 32.83  ? 150 PHE A N    1 
ATOM   1146 C CA   . PHE A 1 150 ? -6.072  5.794   -39.081 1.00 36.04  ? 150 PHE A CA   1 
ATOM   1147 C C    . PHE A 1 150 ? -7.395  6.362   -38.598 1.00 36.73  ? 150 PHE A C    1 
ATOM   1148 O O    . PHE A 1 150 ? -7.458  7.203   -37.695 1.00 35.93  ? 150 PHE A O    1 
ATOM   1149 C CB   . PHE A 1 150 ? -5.837  4.433   -38.437 1.00 34.35  ? 150 PHE A CB   1 
ATOM   1150 C CG   . PHE A 1 150 ? -5.774  4.494   -36.955 1.00 35.56  ? 150 PHE A CG   1 
ATOM   1151 C CD1  . PHE A 1 150 ? -4.579  4.843   -36.317 1.00 38.35  ? 150 PHE A CD1  1 
ATOM   1152 C CD2  . PHE A 1 150 ? -6.886  4.231   -36.188 1.00 35.09  ? 150 PHE A CD2  1 
ATOM   1153 C CE1  . PHE A 1 150 ? -4.515  4.919   -34.935 1.00 36.64  ? 150 PHE A CE1  1 
ATOM   1154 C CE2  . PHE A 1 150 ? -6.836  4.313   -34.800 1.00 37.04  ? 150 PHE A CE2  1 
ATOM   1155 C CZ   . PHE A 1 150 ? -5.655  4.647   -34.174 1.00 39.31  ? 150 PHE A CZ   1 
ATOM   1156 N N    . ASN A 1 151 ? -8.454  5.857   -39.204 1.00 40.39  ? 151 ASN A N    1 
ATOM   1157 C CA   . ASN A 1 151 ? -9.819  6.070   -38.756 1.00 43.02  ? 151 ASN A CA   1 
ATOM   1158 C C    . ASN A 1 151 ? -10.462 4.705   -38.501 1.00 47.30  ? 151 ASN A C    1 
ATOM   1159 O O    . ASN A 1 151 ? -10.110 3.705   -39.141 1.00 43.52  ? 151 ASN A O    1 
ATOM   1160 C CB   . ASN A 1 151 ? -10.606 6.871   -39.806 1.00 39.44  ? 151 ASN A CB   1 
ATOM   1161 C CG   . ASN A 1 151 ? -10.230 8.335   -39.823 1.00 40.87  ? 151 ASN A CG   1 
ATOM   1162 O OD1  . ASN A 1 151 ? -9.501  8.808   -40.703 1.00 41.61  ? 151 ASN A OD1  1 
ATOM   1163 N ND2  . ASN A 1 151 ? -10.767 9.078   -38.873 1.00 40.84  ? 151 ASN A ND2  1 
ATOM   1164 N N    . ILE A 1 152 ? -11.371 4.646   -37.531 1.00 50.59  ? 152 ILE A N    1 
ATOM   1165 C CA   . ILE A 1 152 ? -12.099 3.421   -37.217 1.00 55.42  ? 152 ILE A CA   1 
ATOM   1166 C C    . ILE A 1 152 ? -13.562 3.699   -37.519 1.00 70.93  ? 152 ILE A C    1 
ATOM   1167 O O    . ILE A 1 152 ? -14.138 4.652   -36.980 1.00 68.45  ? 152 ILE A O    1 
ATOM   1168 C CB   . ILE A 1 152 ? -11.930 3.010   -35.750 1.00 57.92  ? 152 ILE A CB   1 
ATOM   1169 C CG1  . ILE A 1 152 ? -10.467 2.757   -35.400 1.00 51.66  ? 152 ILE A CG1  1 
ATOM   1170 C CG2  . ILE A 1 152 ? -12.708 1.713   -35.473 1.00 64.13  ? 152 ILE A CG2  1 
ATOM   1171 C CD1  . ILE A 1 152 ? -10.279 1.816   -34.225 1.00 54.11  ? 152 ILE A CD1  1 
ATOM   1172 N N    . ASP A 1 153 ? -14.170 2.882   -38.372 1.00 101.59 ? 153 ASP A N    1 
ATOM   1173 C CA   . ASP A 1 153 ? -15.602 3.018   -38.626 1.00 103.30 ? 153 ASP A CA   1 
ATOM   1174 C C    . ASP A 1 153 ? -16.285 1.719   -38.211 1.00 108.46 ? 153 ASP A C    1 
ATOM   1175 O O    . ASP A 1 153 ? -16.239 0.707   -38.918 1.00 107.37 ? 153 ASP A O    1 
ATOM   1176 C CB   . ASP A 1 153 ? -15.911 3.433   -40.079 1.00 108.95 ? 153 ASP A CB   1 
ATOM   1177 C CG   . ASP A 1 153 ? -15.914 2.272   -41.073 1.00 114.34 ? 153 ASP A CG   1 
ATOM   1178 O OD1  . ASP A 1 153 ? -15.048 1.373   -40.990 1.00 110.03 ? 153 ASP A OD1  1 
ATOM   1179 O OD2  . ASP A 1 153 ? -16.803 2.262   -41.953 1.00 119.75 ? 153 ASP A OD2  1 
ATOM   1180 N N    . TYR A 1 154 ? -16.912 1.743   -37.042 1.00 114.77 ? 154 TYR A N    1 
ATOM   1181 C CA   . TYR A 1 154 ? -17.520 0.525   -36.536 1.00 119.01 ? 154 TYR A CA   1 
ATOM   1182 C C    . TYR A 1 154 ? -16.461 -0.553  -36.298 1.00 117.09 ? 154 TYR A C    1 
ATOM   1183 O O    . TYR A 1 154 ? -15.800 -0.523  -35.256 1.00 117.75 ? 154 TYR A O    1 
ATOM   1184 C CB   . TYR A 1 154 ? -18.612 0.151   -37.535 1.00 119.62 ? 154 TYR A CB   1 
ATOM   1185 C CG   . TYR A 1 154 ? -19.465 1.394   -37.821 1.00 130.46 ? 154 TYR A CG   1 
ATOM   1186 C CD1  . TYR A 1 154 ? -19.675 2.362   -36.827 1.00 130.29 ? 154 TYR A CD1  1 
ATOM   1187 C CD2  . TYR A 1 154 ? -19.949 1.666   -39.100 1.00 127.59 ? 154 TYR A CD2  1 
ATOM   1188 C CE1  . TYR A 1 154 ? -20.413 3.513   -37.075 1.00 128.52 ? 154 TYR A CE1  1 
ATOM   1189 C CE2  . TYR A 1 154 ? -20.680 2.831   -39.360 1.00 128.72 ? 154 TYR A CE2  1 
ATOM   1190 C CZ   . TYR A 1 154 ? -20.916 3.742   -38.341 1.00 133.26 ? 154 TYR A CZ   1 
ATOM   1191 O OH   . TYR A 1 154 ? -21.647 4.885   -38.589 1.00 136.59 ? 154 TYR A OH   1 
ATOM   1192 N N    . ASP A 1 155 ? -16.266 -1.501  -37.214 1.00 99.46  ? 155 ASP A N    1 
ATOM   1193 C CA   . ASP A 1 155 ? -15.334 -2.604  -36.964 1.00 93.92  ? 155 ASP A CA   1 
ATOM   1194 C C    . ASP A 1 155 ? -14.076 -2.569  -37.837 1.00 80.67  ? 155 ASP A C    1 
ATOM   1195 O O    . ASP A 1 155 ? -13.198 -3.436  -37.690 1.00 70.03  ? 155 ASP A O    1 
ATOM   1196 C CB   . ASP A 1 155 ? -16.026 -3.964  -37.149 1.00 91.78  ? 155 ASP A CB   1 
ATOM   1197 C CG   . ASP A 1 155 ? -16.546 -4.183  -38.564 1.00 88.73  ? 155 ASP A CG   1 
ATOM   1198 O OD1  . ASP A 1 155 ? -16.418 -3.268  -39.416 1.00 85.26  ? 155 ASP A OD1  1 
ATOM   1199 O OD2  . ASP A 1 155 ? -17.066 -5.299  -38.822 1.00 85.24  ? 155 ASP A OD2  1 
ATOM   1200 N N    . CYS A 1 156 ? -13.963 -1.600  -38.732 1.00 77.09  ? 156 CYS A N    1 
ATOM   1201 C CA   . CYS A 1 156 ? -12.957 -1.600  -39.782 1.00 68.42  ? 156 CYS A CA   1 
ATOM   1202 C C    . CYS A 1 156 ? -11.938 -0.481  -39.596 1.00 59.20  ? 156 CYS A C    1 
ATOM   1203 O O    . CYS A 1 156 ? -12.307 0.694   -39.551 1.00 57.91  ? 156 CYS A O    1 
ATOM   1204 C CB   . CYS A 1 156 ? -13.650 -1.451  -41.130 1.00 67.17  ? 156 CYS A CB   1 
ATOM   1205 S SG   . CYS A 1 156 ? -12.548 -1.572  -42.506 1.00 65.69  ? 156 CYS A SG   1 
ATOM   1206 N N    . VAL A 1 157 ? -10.659 -0.839  -39.520 1.00 51.36  ? 157 VAL A N    1 
ATOM   1207 C CA   . VAL A 1 157 ? -9.598  0.171   -39.450 1.00 48.32  ? 157 VAL A CA   1 
ATOM   1208 C C    . VAL A 1 157 ? -9.272  0.662   -40.865 1.00 46.44  ? 157 VAL A C    1 
ATOM   1209 O O    . VAL A 1 157 ? -8.904  -0.127  -41.739 1.00 46.83  ? 157 VAL A O    1 
ATOM   1210 C CB   . VAL A 1 157 ? -8.345  -0.398  -38.768 1.00 43.85  ? 157 VAL A CB   1 
ATOM   1211 C CG1  . VAL A 1 157 ? -7.184  0.594   -38.851 1.00 41.35  ? 157 VAL A CG1  1 
ATOM   1212 C CG2  . VAL A 1 157 ? -8.645  -0.821  -37.326 1.00 43.20  ? 157 VAL A CG2  1 
ATOM   1213 N N    . SER A 1 158 ? -9.429  1.958   -41.104 1.00 43.42  ? 158 SER A N    1 
ATOM   1214 C CA   . SER A 1 158 ? -8.998  2.584   -42.353 1.00 43.12  ? 158 SER A CA   1 
ATOM   1215 C C    . SER A 1 158 ? -7.661  3.275   -42.109 1.00 42.60  ? 158 SER A C    1 
ATOM   1216 O O    . SER A 1 158 ? -7.606  4.357   -41.507 1.00 35.84  ? 158 SER A O    1 
ATOM   1217 C CB   . SER A 1 158 ? -10.016 3.601   -42.865 1.00 39.86  ? 158 SER A CB   1 
ATOM   1218 O OG   . SER A 1 158 ? -11.056 2.923   -43.532 1.00 48.31  ? 158 SER A OG   1 
ATOM   1219 N N    . PHE A 1 159 ? -6.599  2.670   -42.607 1.00 39.75  ? 159 PHE A N    1 
ATOM   1220 C CA   . PHE A 1 159 ? -5.287  3.287   -42.571 1.00 39.56  ? 159 PHE A CA   1 
ATOM   1221 C C    . PHE A 1 159 ? -5.162  4.314   -43.680 1.00 40.61  ? 159 PHE A C    1 
ATOM   1222 O O    . PHE A 1 159 ? -5.472  4.028   -44.841 1.00 39.92  ? 159 PHE A O    1 
ATOM   1223 C CB   . PHE A 1 159 ? -4.219  2.223   -42.722 1.00 35.99  ? 159 PHE A CB   1 
ATOM   1224 C CG   . PHE A 1 159 ? -4.178  1.230   -41.573 1.00 38.13  ? 159 PHE A CG   1 
ATOM   1225 C CD1  . PHE A 1 159 ? -3.615  1.578   -40.344 1.00 35.73  ? 159 PHE A CD1  1 
ATOM   1226 C CD2  . PHE A 1 159 ? -4.655  -0.056  -41.738 1.00 39.72  ? 159 PHE A CD2  1 
ATOM   1227 C CE1  . PHE A 1 159 ? -3.534  0.650   -39.298 1.00 35.61  ? 159 PHE A CE1  1 
ATOM   1228 C CE2  . PHE A 1 159 ? -4.570  -1.008  -40.696 1.00 40.74  ? 159 PHE A CE2  1 
ATOM   1229 C CZ   . PHE A 1 159 ? -4.012  -0.653  -39.478 1.00 39.61  ? 159 PHE A CZ   1 
ATOM   1230 N N    . CYS A 1 160 ? -4.725  5.518   -43.327 1.00 38.54  ? 160 CYS A N    1 
ATOM   1231 C CA   . CYS A 1 160 ? -4.573  6.553   -44.324 1.00 36.15  ? 160 CYS A CA   1 
ATOM   1232 C C    . CYS A 1 160 ? -3.207  7.231   -44.355 1.00 36.28  ? 160 CYS A C    1 
ATOM   1233 O O    . CYS A 1 160 ? -2.963  8.018   -45.278 1.00 39.42  ? 160 CYS A O    1 
ATOM   1234 C CB   . CYS A 1 160 ? -5.642  7.633   -44.137 1.00 40.93  ? 160 CYS A CB   1 
ATOM   1235 S SG   . CYS A 1 160 ? -5.633  8.424   -42.504 1.00 39.70  ? 160 CYS A SG   1 
ATOM   1236 N N    . TYR A 1 161 ? -2.321  6.993   -43.383 1.00 33.91  ? 161 TYR A N    1 
ATOM   1237 C CA   . TYR A 1 161 ? -1.108  7.797   -43.325 1.00 30.48  ? 161 TYR A CA   1 
ATOM   1238 C C    . TYR A 1 161 ? -0.009  6.982   -42.711 1.00 32.35  ? 161 TYR A C    1 
ATOM   1239 O O    . TYR A 1 161 ? -0.237  6.257   -41.747 1.00 32.94  ? 161 TYR A O    1 
ATOM   1240 C CB   . TYR A 1 161 ? -1.333  9.079   -42.513 1.00 30.73  ? 161 TYR A CB   1 
ATOM   1241 C CG   . TYR A 1 161 ? -0.096  9.943   -42.303 1.00 36.96  ? 161 TYR A CG   1 
ATOM   1242 C CD1  . TYR A 1 161 ? 0.316   10.860  -43.260 1.00 34.75  ? 161 TYR A CD1  1 
ATOM   1243 C CD2  . TYR A 1 161 ? 0.638   9.856   -41.124 1.00 31.18  ? 161 TYR A CD2  1 
ATOM   1244 C CE1  . TYR A 1 161 ? 1.454   11.665  -43.047 1.00 34.88  ? 161 TYR A CE1  1 
ATOM   1245 C CE2  . TYR A 1 161 ? 1.747   10.646  -40.908 1.00 34.24  ? 161 TYR A CE2  1 
ATOM   1246 C CZ   . TYR A 1 161 ? 2.161   11.544  -41.867 1.00 35.40  ? 161 TYR A CZ   1 
ATOM   1247 O OH   . TYR A 1 161 ? 3.287   12.317  -41.627 1.00 32.99  ? 161 TYR A OH   1 
ATOM   1248 N N    . MET A 1 162 ? 1.185   7.105   -43.272 1.00 35.66  ? 162 MET A N    1 
ATOM   1249 C CA   . MET A 1 162 ? 2.383   6.521   -42.695 1.00 34.39  ? 162 MET A CA   1 
ATOM   1250 C C    . MET A 1 162 ? 3.423   7.623   -42.643 1.00 33.86  ? 162 MET A C    1 
ATOM   1251 O O    . MET A 1 162 ? 3.614   8.345   -43.630 1.00 31.24  ? 162 MET A O    1 
ATOM   1252 C CB   . MET A 1 162 ? 2.920   5.354   -43.525 1.00 34.99  ? 162 MET A CB   1 
ATOM   1253 C CG   . MET A 1 162 ? 4.218   4.824   -42.998 1.00 34.62  ? 162 MET A CG   1 
ATOM   1254 S SD   . MET A 1 162 ? 4.728   3.266   -43.765 1.00 39.93  ? 162 MET A SD   1 
ATOM   1255 C CE   . MET A 1 162 ? 4.116   2.077   -42.541 1.00 35.84  ? 162 MET A CE   1 
ATOM   1256 N N    . HIS A 1 163 ? 4.064   7.778   -41.486 1.00 32.82  ? 163 HIS A N    1 
ATOM   1257 C CA   . HIS A 1 163 ? 4.972   8.892   -41.295 1.00 35.93  ? 163 HIS A CA   1 
ATOM   1258 C C    . HIS A 1 163 ? 6.328   8.617   -41.914 1.00 36.25  ? 163 HIS A C    1 
ATOM   1259 O O    . HIS A 1 163 ? 6.894   7.528   -41.721 1.00 34.92  ? 163 HIS A O    1 
ATOM   1260 C CB   . HIS A 1 163 ? 5.161   9.166   -39.806 1.00 35.43  ? 163 HIS A CB   1 
ATOM   1261 C CG   . HIS A 1 163 ? 6.007   10.361  -39.545 1.00 37.72  ? 163 HIS A CG   1 
ATOM   1262 N ND1  . HIS A 1 163 ? 5.656   11.616  -39.989 1.00 34.20  ? 163 HIS A ND1  1 
ATOM   1263 C CD2  . HIS A 1 163 ? 7.210   10.494  -38.939 1.00 37.05  ? 163 HIS A CD2  1 
ATOM   1264 C CE1  . HIS A 1 163 ? 6.603   12.476  -39.655 1.00 37.30  ? 163 HIS A CE1  1 
ATOM   1265 N NE2  . HIS A 1 163 ? 7.555   11.820  -39.012 1.00 39.02  ? 163 HIS A NE2  1 
ATOM   1266 N N    . HIS A 1 164 ? 6.886   9.648   -42.601 1.00 31.24  ? 164 HIS A N    1 
ATOM   1267 C CA   . HIS A 1 164 ? 8.191   9.580   -43.266 1.00 39.29  ? 164 HIS A CA   1 
ATOM   1268 C C    . HIS A 1 164 ? 9.183   10.663  -42.847 1.00 42.79  ? 164 HIS A C    1 
ATOM   1269 O O    . HIS A 1 164 ? 10.387  10.394  -42.860 1.00 40.04  ? 164 HIS A O    1 
ATOM   1270 C CB   . HIS A 1 164 ? 8.054   9.680   -44.789 1.00 35.16  ? 164 HIS A CB   1 
ATOM   1271 C CG   . HIS A 1 164 ? 7.549   8.430   -45.433 1.00 37.68  ? 164 HIS A CG   1 
ATOM   1272 N ND1  . HIS A 1 164 ? 8.344   7.627   -46.220 1.00 35.87  ? 164 HIS A ND1  1 
ATOM   1273 C CD2  . HIS A 1 164 ? 6.313   7.866   -45.438 1.00 33.52  ? 164 HIS A CD2  1 
ATOM   1274 C CE1  . HIS A 1 164 ? 7.634   6.596   -46.649 1.00 35.68  ? 164 HIS A CE1  1 
ATOM   1275 N NE2  . HIS A 1 164 ? 6.401   6.714   -46.181 1.00 37.89  ? 164 HIS A NE2  1 
ATOM   1276 N N    . MET A 1 165 ? 8.738   11.884  -42.539 1.00 39.61  ? 165 MET A N    1 
ATOM   1277 C CA   . MET A 1 165 ? 9.721   12.956  -42.405 1.00 42.40  ? 165 MET A CA   1 
ATOM   1278 C C    . MET A 1 165 ? 9.139   14.223  -41.776 1.00 39.47  ? 165 MET A C    1 
ATOM   1279 O O    . MET A 1 165 ? 7.926   14.461  -41.804 1.00 38.82  ? 165 MET A O    1 
ATOM   1280 C CB   . MET A 1 165 ? 10.302  13.296  -43.760 1.00 43.54  ? 165 MET A CB   1 
ATOM   1281 C CG   . MET A 1 165 ? 9.366   14.034  -44.668 1.00 43.83  ? 165 MET A CG   1 
ATOM   1282 S SD   . MET A 1 165 ? 10.113  13.972  -46.320 1.00 58.69  ? 165 MET A SD   1 
ATOM   1283 C CE   . MET A 1 165 ? 10.939  15.580  -46.318 1.00 52.85  ? 165 MET A CE   1 
ATOM   1284 N N    . GLU A 1 166 ? 10.039  15.066  -41.263 1.00 41.09  ? 166 GLU A N    1 
ATOM   1285 C CA   . GLU A 1 166 ? 9.673   16.378  -40.740 1.00 45.06  ? 166 GLU A CA   1 
ATOM   1286 C C    . GLU A 1 166 ? 10.250  17.495  -41.614 1.00 48.69  ? 166 GLU A C    1 
ATOM   1287 O O    . GLU A 1 166 ? 11.357  17.369  -42.156 1.00 44.72  ? 166 GLU A O    1 
ATOM   1288 C CB   . GLU A 1 166 ? 10.162  16.540  -39.294 1.00 48.08  ? 166 GLU A CB   1 
ATOM   1289 C CG   . GLU A 1 166 ? 9.986   17.941  -38.687 1.00 47.35  ? 166 GLU A CG   1 
ATOM   1290 C CD   . GLU A 1 166 ? 10.183  17.965  -37.162 1.00 52.13  ? 166 GLU A CD   1 
ATOM   1291 O OE1  . GLU A 1 166 ? 9.560   17.167  -36.416 1.00 51.38  ? 166 GLU A OE1  1 
ATOM   1292 O OE2  . GLU A 1 166 ? 11.037  18.772  -36.723 1.00 56.59  ? 166 GLU A OE2  1 
ATOM   1293 N N    . LEU A 1 167 ? 9.496   18.593  -41.744 1.00 46.14  ? 167 LEU A N    1 
ATOM   1294 C CA   . LEU A 1 167 ? 9.914   19.724  -42.570 1.00 48.88  ? 167 LEU A CA   1 
ATOM   1295 C C    . LEU A 1 167 ? 10.622  20.770  -41.721 1.00 50.75  ? 167 LEU A C    1 
ATOM   1296 O O    . LEU A 1 167 ? 10.599  20.708  -40.487 1.00 52.85  ? 167 LEU A O    1 
ATOM   1297 C CB   . LEU A 1 167 ? 8.701   20.331  -43.286 1.00 47.05  ? 167 LEU A CB   1 
ATOM   1298 C CG   . LEU A 1 167 ? 7.947   19.352  -44.212 1.00 45.01  ? 167 LEU A CG   1 
ATOM   1299 C CD1  . LEU A 1 167 ? 6.800   20.047  -44.951 1.00 45.74  ? 167 LEU A CD1  1 
ATOM   1300 C CD2  . LEU A 1 167 ? 8.936   18.706  -45.180 1.00 44.31  ? 167 LEU A CD2  1 
ATOM   1301 N N    . PRO A 1 168 ? 11.281  21.752  -42.362 1.00 48.95  ? 168 PRO A N    1 
ATOM   1302 C CA   . PRO A 1 168 ? 11.926  22.826  -41.589 1.00 50.01  ? 168 PRO A CA   1 
ATOM   1303 C C    . PRO A 1 168 ? 10.971  23.596  -40.705 1.00 53.29  ? 168 PRO A C    1 
ATOM   1304 O O    . PRO A 1 168 ? 11.350  24.053  -39.621 1.00 52.97  ? 168 PRO A O    1 
ATOM   1305 C CB   . PRO A 1 168 ? 12.513  23.734  -42.677 1.00 51.81  ? 168 PRO A CB   1 
ATOM   1306 C CG   . PRO A 1 168 ? 12.631  22.867  -43.878 1.00 54.37  ? 168 PRO A CG   1 
ATOM   1307 C CD   . PRO A 1 168 ? 11.474  21.932  -43.809 1.00 51.46  ? 168 PRO A CD   1 
ATOM   1308 N N    . THR A 1 169 ? 9.742   23.795  -41.158 1.00 51.28  ? 169 THR A N    1 
ATOM   1309 C CA   . THR A 1 169 ? 8.795   24.532  -40.343 1.00 52.88  ? 169 THR A CA   1 
ATOM   1310 C C    . THR A 1 169 ? 8.371   23.754  -39.102 1.00 53.70  ? 169 THR A C    1 
ATOM   1311 O O    . THR A 1 169 ? 7.646   24.306  -38.266 1.00 51.64  ? 169 THR A O    1 
ATOM   1312 C CB   . THR A 1 169 ? 7.572   24.905  -41.188 1.00 48.69  ? 169 THR A CB   1 
ATOM   1313 O OG1  . THR A 1 169 ? 7.074   23.719  -41.801 1.00 47.68  ? 169 THR A OG1  1 
ATOM   1314 C CG2  . THR A 1 169 ? 7.951   25.949  -42.293 1.00 50.76  ? 169 THR A CG2  1 
ATOM   1315 N N    . GLY A 1 170 ? 8.776   22.489  -38.966 1.00 48.34  ? 170 GLY A N    1 
ATOM   1316 C CA   . GLY A 1 170 ? 8.316   21.716  -37.839 1.00 45.94  ? 170 GLY A CA   1 
ATOM   1317 C C    . GLY A 1 170 ? 6.986   21.038  -38.045 1.00 51.14  ? 170 GLY A C    1 
ATOM   1318 O O    . GLY A 1 170 ? 6.366   20.604  -37.062 1.00 51.29  ? 170 GLY A O    1 
ATOM   1319 N N    . VAL A 1 171 ? 6.510   20.958  -39.281 1.00 46.84  ? 171 VAL A N    1 
ATOM   1320 C CA   . VAL A 1 171 ? 5.331   20.164  -39.580 1.00 44.17  ? 171 VAL A CA   1 
ATOM   1321 C C    . VAL A 1 171 ? 5.801   18.855  -40.216 1.00 45.40  ? 171 VAL A C    1 
ATOM   1322 O O    . VAL A 1 171 ? 7.000   18.671  -40.498 1.00 40.64  ? 171 VAL A O    1 
ATOM   1323 C CB   . VAL A 1 171 ? 4.365   20.950  -40.489 1.00 45.77  ? 171 VAL A CB   1 
ATOM   1324 C CG1  . VAL A 1 171 ? 3.880   22.263  -39.769 1.00 46.08  ? 171 VAL A CG1  1 
ATOM   1325 C CG2  . VAL A 1 171 ? 5.031   21.279  -41.781 1.00 42.30  ? 171 VAL A CG2  1 
ATOM   1326 N N    . HIS A 1 172 ? 4.862   17.946  -40.472 1.00 40.28  ? 172 HIS A N    1 
ATOM   1327 C CA   . HIS A 1 172 ? 5.203   16.575  -40.816 1.00 40.90  ? 172 HIS A CA   1 
ATOM   1328 C C    . HIS A 1 172 ? 4.578   16.169  -42.149 1.00 40.47  ? 172 HIS A C    1 
ATOM   1329 O O    . HIS A 1 172 ? 3.525   16.679  -42.531 1.00 36.11  ? 172 HIS A O    1 
ATOM   1330 C CB   . HIS A 1 172 ? 4.758   15.658  -39.662 1.00 39.88  ? 172 HIS A CB   1 
ATOM   1331 C CG   . HIS A 1 172 ? 5.341   16.067  -38.342 1.00 42.75  ? 172 HIS A CG   1 
ATOM   1332 N ND1  . HIS A 1 172 ? 4.590   16.626  -37.331 1.00 42.57  ? 172 HIS A ND1  1 
ATOM   1333 C CD2  . HIS A 1 172 ? 6.619   16.033  -37.888 1.00 42.18  ? 172 HIS A CD2  1 
ATOM   1334 C CE1  . HIS A 1 172 ? 5.377   16.897  -36.302 1.00 43.99  ? 172 HIS A CE1  1 
ATOM   1335 N NE2  . HIS A 1 172 ? 6.611   16.545  -36.614 1.00 45.19  ? 172 HIS A NE2  1 
ATOM   1336 N N    . ALA A 1 173 ? 5.250   15.240  -42.844 1.00 36.72  ? 173 ALA A N    1 
ATOM   1337 C CA   . ALA A 1 173 ? 4.841   14.760  -44.157 1.00 36.62  ? 173 ALA A CA   1 
ATOM   1338 C C    . ALA A 1 173 ? 4.996   13.247  -44.229 1.00 36.50  ? 173 ALA A C    1 
ATOM   1339 O O    . ALA A 1 173 ? 5.893   12.663  -43.610 1.00 34.31  ? 173 ALA A O    1 
ATOM   1340 C CB   . ALA A 1 173 ? 5.674   15.443  -45.272 1.00 39.39  ? 173 ALA A CB   1 
ATOM   1341 N N    . GLY A 1 174 ? 4.115   12.611  -44.990 1.00 32.96  ? 174 GLY A N    1 
ATOM   1342 C CA   . GLY A 1 174 ? 4.187   11.170  -45.168 1.00 32.97  ? 174 GLY A CA   1 
ATOM   1343 C C    . GLY A 1 174 ? 3.326   10.707  -46.324 1.00 35.15  ? 174 GLY A C    1 
ATOM   1344 O O    . GLY A 1 174 ? 2.861   11.504  -47.136 1.00 35.64  ? 174 GLY A O    1 
ATOM   1345 N N    . THR A 1 175 ? 3.104   9.399   -46.376 1.00 30.57  ? 175 THR A N    1 
ATOM   1346 C CA   . THR A 1 175 ? 2.464   8.758   -47.509 1.00 36.52  ? 175 THR A CA   1 
ATOM   1347 C C    . THR A 1 175 ? 1.187   8.064   -47.066 1.00 37.57  ? 175 THR A C    1 
ATOM   1348 O O    . THR A 1 175 ? 0.952   7.833   -45.867 1.00 31.78  ? 175 THR A O    1 
ATOM   1349 C CB   . THR A 1 175 ? 3.387   7.725   -48.167 1.00 35.15  ? 175 THR A CB   1 
ATOM   1350 O OG1  . THR A 1 175 ? 3.609   6.635   -47.257 1.00 30.84  ? 175 THR A OG1  1 
ATOM   1351 C CG2  . THR A 1 175 ? 4.724   8.345   -48.582 1.00 34.82  ? 175 THR A CG2  1 
ATOM   1352 N N    . ASP A 1 176 ? 0.374   7.693   -48.065 1.00 35.86  ? 176 ASP A N    1 
ATOM   1353 C CA   . ASP A 1 176 ? -0.709  6.740   -47.860 1.00 34.61  ? 176 ASP A CA   1 
ATOM   1354 C C    . ASP A 1 176 ? -0.118  5.353   -47.762 1.00 33.60  ? 176 ASP A C    1 
ATOM   1355 O O    . ASP A 1 176 ? 1.086   5.159   -47.944 1.00 32.46  ? 176 ASP A O    1 
ATOM   1356 C CB   . ASP A 1 176 ? -1.746  6.862   -48.983 1.00 39.75  ? 176 ASP A CB   1 
ATOM   1357 C CG   . ASP A 1 176 ? -1.189  6.483   -50.382 1.00 38.34  ? 176 ASP A CG   1 
ATOM   1358 O OD1  . ASP A 1 176 ? -0.326  5.563   -50.517 1.00 35.07  ? 176 ASP A OD1  1 
ATOM   1359 O OD2  . ASP A 1 176 ? -1.617  7.149   -51.346 1.00 40.68  ? 176 ASP A OD2  1 
ATOM   1360 N N    . LEU A 1 177 ? -0.939  4.359   -47.479 1.00 34.59  ? 177 LEU A N    1 
ATOM   1361 C CA   . LEU A 1 177 ? -0.309  3.060   -47.261 1.00 39.18  ? 177 LEU A CA   1 
ATOM   1362 C C    . LEU A 1 177 ? 0.092   2.410   -48.568 1.00 38.88  ? 177 LEU A C    1 
ATOM   1363 O O    . LEU A 1 177 ? 0.657   1.318   -48.546 1.00 34.72  ? 177 LEU A O    1 
ATOM   1364 C CB   . LEU A 1 177 ? -1.211  2.107   -46.446 1.00 37.18  ? 177 LEU A CB   1 
ATOM   1365 C CG   . LEU A 1 177 ? -0.977  2.143   -44.924 1.00 38.40  ? 177 LEU A CG   1 
ATOM   1366 C CD1  . LEU A 1 177 ? 0.339   1.557   -44.571 1.00 33.19  ? 177 LEU A CD1  1 
ATOM   1367 C CD2  . LEU A 1 177 ? -1.044  3.647   -44.433 1.00 38.13  ? 177 LEU A CD2  1 
ATOM   1368 N N    . GLU A 1 178 ? -0.183  3.055   -49.695 1.00 40.26  ? 178 GLU A N    1 
ATOM   1369 C CA   . GLU A 1 178 ? 0.348   2.585   -50.972 1.00 42.02  ? 178 GLU A CA   1 
ATOM   1370 C C    . GLU A 1 178 ? 1.677   3.235   -51.321 1.00 41.50  ? 178 GLU A C    1 
ATOM   1371 O O    . GLU A 1 178 ? 2.304   2.833   -52.302 1.00 45.04  ? 178 GLU A O    1 
ATOM   1372 C CB   . GLU A 1 178 ? -0.673  2.850   -52.070 1.00 44.80  ? 178 GLU A CB   1 
ATOM   1373 C CG   . GLU A 1 178 ? -1.621  1.703   -52.288 1.00 46.93  ? 178 GLU A CG   1 
ATOM   1374 C CD   . GLU A 1 178 ? -2.916  2.182   -52.931 1.00 56.56  ? 178 GLU A CD   1 
ATOM   1375 O OE1  . GLU A 1 178 ? -2.978  3.316   -53.475 1.00 61.87  ? 178 GLU A OE1  1 
ATOM   1376 O OE2  . GLU A 1 178 ? -3.895  1.408   -52.847 1.00 65.65  ? 178 GLU A OE2  1 
ATOM   1377 N N    . GLY A 1 179 ? 2.123   4.217   -50.532 1.00 42.90  ? 179 GLY A N    1 
ATOM   1378 C CA   . GLY A 1 179 ? 3.456   4.775   -50.642 1.00 39.56  ? 179 GLY A CA   1 
ATOM   1379 C C    . GLY A 1 179 ? 3.548   6.087   -51.365 1.00 36.67  ? 179 GLY A C    1 
ATOM   1380 O O    . GLY A 1 179 ? 4.660   6.565   -51.585 1.00 35.29  ? 179 GLY A O    1 
ATOM   1381 N N    . ASN A 1 180 ? 2.431   6.669   -51.770 1.00 33.69  ? 180 ASN A N    1 
ATOM   1382 C CA   . ASN A 1 180 ? 2.431   7.939   -52.472 1.00 37.76  ? 180 ASN A CA   1 
ATOM   1383 C C    . ASN A 1 180 ? 2.285   9.043   -51.434 1.00 39.51  ? 180 ASN A C    1 
ATOM   1384 O O    . ASN A 1 180 ? 1.326   9.054   -50.652 1.00 37.83  ? 180 ASN A O    1 
ATOM   1385 C CB   . ASN A 1 180 ? 1.300   8.003   -53.506 1.00 40.77  ? 180 ASN A CB   1 
ATOM   1386 C CG   . ASN A 1 180 ? 1.340   6.841   -54.472 1.00 43.29  ? 180 ASN A CG   1 
ATOM   1387 O OD1  . ASN A 1 180 ? 2.229   6.757   -55.310 1.00 45.07  ? 180 ASN A OD1  1 
ATOM   1388 N ND2  . ASN A 1 180 ? 0.404   5.907   -54.321 1.00 44.07  ? 180 ASN A ND2  1 
ATOM   1389 N N    . PHE A 1 181 ? 3.227   9.969   -51.424 1.00 35.45  ? 181 PHE A N    1 
ATOM   1390 C CA   . PHE A 1 181 ? 3.165   11.044  -50.452 1.00 36.68  ? 181 PHE A CA   1 
ATOM   1391 C C    . PHE A 1 181 ? 1.869   11.812  -50.619 1.00 39.59  ? 181 PHE A C    1 
ATOM   1392 O O    . PHE A 1 181 ? 1.303   11.888  -51.711 1.00 36.28  ? 181 PHE A O    1 
ATOM   1393 C CB   . PHE A 1 181 ? 4.351   11.998  -50.635 1.00 35.46  ? 181 PHE A CB   1 
ATOM   1394 C CG   . PHE A 1 181 ? 5.532   11.680  -49.746 1.00 37.79  ? 181 PHE A CG   1 
ATOM   1395 C CD1  . PHE A 1 181 ? 6.490   10.758  -50.151 1.00 36.21  ? 181 PHE A CD1  1 
ATOM   1396 C CD2  . PHE A 1 181 ? 5.703   12.333  -48.521 1.00 36.77  ? 181 PHE A CD2  1 
ATOM   1397 C CE1  . PHE A 1 181 ? 7.595   10.469  -49.349 1.00 39.53  ? 181 PHE A CE1  1 
ATOM   1398 C CE2  . PHE A 1 181 ? 6.816   12.060  -47.698 1.00 36.79  ? 181 PHE A CE2  1 
ATOM   1399 C CZ   . PHE A 1 181 ? 7.762   11.136  -48.106 1.00 38.80  ? 181 PHE A CZ   1 
ATOM   1400 N N    . TYR A 1 182 ? 1.391   12.367  -49.516 1.00 37.68  ? 182 TYR A N    1 
ATOM   1401 C CA   . TYR A 1 182 ? 0.544   13.534  -49.597 1.00 34.14  ? 182 TYR A CA   1 
ATOM   1402 C C    . TYR A 1 182 ? 1.435   14.742  -49.839 1.00 37.70  ? 182 TYR A C    1 
ATOM   1403 O O    . TYR A 1 182 ? 2.465   14.901  -49.173 1.00 39.11  ? 182 TYR A O    1 
ATOM   1404 C CB   . TYR A 1 182 ? -0.253  13.705  -48.299 1.00 35.36  ? 182 TYR A CB   1 
ATOM   1405 C CG   . TYR A 1 182 ? -1.193  12.536  -48.001 1.00 38.36  ? 182 TYR A CG   1 
ATOM   1406 C CD1  . TYR A 1 182 ? -2.483  12.518  -48.506 1.00 35.25  ? 182 TYR A CD1  1 
ATOM   1407 C CD2  . TYR A 1 182 ? -0.796  11.482  -47.199 1.00 34.32  ? 182 TYR A CD2  1 
ATOM   1408 C CE1  . TYR A 1 182 ? -3.360  11.472  -48.239 1.00 36.77  ? 182 TYR A CE1  1 
ATOM   1409 C CE2  . TYR A 1 182 ? -1.668  10.413  -46.925 1.00 34.72  ? 182 TYR A CE2  1 
ATOM   1410 C CZ   . TYR A 1 182 ? -2.956  10.426  -47.465 1.00 38.67  ? 182 TYR A CZ   1 
ATOM   1411 O OH   . TYR A 1 182 ? -3.862  9.404   -47.221 1.00 34.07  ? 182 TYR A OH   1 
ATOM   1412 N N    . GLY A 1 183 ? 1.063   15.577  -50.812 1.00 30.23  ? 183 GLY A N    1 
ATOM   1413 C CA   . GLY A 1 183 ? 1.788   16.797  -51.099 1.00 35.68  ? 183 GLY A CA   1 
ATOM   1414 C C    . GLY A 1 183 ? 2.954   16.545  -52.023 1.00 38.59  ? 183 GLY A C    1 
ATOM   1415 O O    . GLY A 1 183 ? 3.143   15.435  -52.546 1.00 37.97  ? 183 GLY A O    1 
ATOM   1416 N N    . PRO A 1 184 ? 3.775   17.559  -52.218 1.00 36.28  ? 184 PRO A N    1 
ATOM   1417 C CA   . PRO A 1 184 ? 4.831   17.476  -53.239 1.00 37.38  ? 184 PRO A CA   1 
ATOM   1418 C C    . PRO A 1 184 ? 6.129   16.872  -52.751 1.00 43.42  ? 184 PRO A C    1 
ATOM   1419 O O    . PRO A 1 184 ? 7.153   17.029  -53.417 1.00 46.36  ? 184 PRO A O    1 
ATOM   1420 C CB   . PRO A 1 184 ? 5.044   18.935  -53.619 1.00 36.43  ? 184 PRO A CB   1 
ATOM   1421 C CG   . PRO A 1 184 ? 4.834   19.653  -52.303 1.00 40.97  ? 184 PRO A CG   1 
ATOM   1422 C CD   . PRO A 1 184 ? 3.806   18.845  -51.515 1.00 39.48  ? 184 PRO A CD   1 
ATOM   1423 N N    . PHE A 1 185 ? 6.110   16.167  -51.623 1.00 38.18  ? 185 PHE A N    1 
ATOM   1424 C CA   . PHE A 1 185 ? 7.342   15.859  -50.915 1.00 40.12  ? 185 PHE A CA   1 
ATOM   1425 C C    . PHE A 1 185 ? 7.996   14.601  -51.472 1.00 37.11  ? 185 PHE A C    1 
ATOM   1426 O O    . PHE A 1 185 ? 7.328   13.737  -52.043 1.00 36.02  ? 185 PHE A O    1 
ATOM   1427 C CB   . PHE A 1 185 ? 7.036   15.718  -49.411 1.00 40.06  ? 185 PHE A CB   1 
ATOM   1428 C CG   . PHE A 1 185 ? 6.337   16.923  -48.859 1.00 37.27  ? 185 PHE A CG   1 
ATOM   1429 C CD1  . PHE A 1 185 ? 6.970   18.148  -48.870 1.00 38.82  ? 185 PHE A CD1  1 
ATOM   1430 C CD2  . PHE A 1 185 ? 5.015   16.855  -48.454 1.00 36.41  ? 185 PHE A CD2  1 
ATOM   1431 C CE1  . PHE A 1 185 ? 6.316   19.293  -48.431 1.00 43.71  ? 185 PHE A CE1  1 
ATOM   1432 C CE2  . PHE A 1 185 ? 4.352   17.998  -48.008 1.00 37.53  ? 185 PHE A CE2  1 
ATOM   1433 C CZ   . PHE A 1 185 ? 4.998   19.207  -47.992 1.00 40.14  ? 185 PHE A CZ   1 
ATOM   1434 N N    . VAL A 1 186 ? 9.319   14.512  -51.306 1.00 30.44  ? 186 VAL A N    1 
ATOM   1435 C CA   . VAL A 1 186 ? 10.073  13.308  -51.627 1.00 39.46  ? 186 VAL A CA   1 
ATOM   1436 C C    . VAL A 1 186 ? 10.883  12.882  -50.412 1.00 42.33  ? 186 VAL A C    1 
ATOM   1437 O O    . VAL A 1 186 ? 11.289  13.709  -49.581 1.00 38.50  ? 186 VAL A O    1 
ATOM   1438 C CB   . VAL A 1 186 ? 11.013  13.500  -52.839 1.00 41.54  ? 186 VAL A CB   1 
ATOM   1439 C CG1  . VAL A 1 186 ? 10.182  13.830  -54.089 1.00 41.33  ? 186 VAL A CG1  1 
ATOM   1440 C CG2  . VAL A 1 186 ? 12.017  14.609  -52.537 1.00 44.58  ? 186 VAL A CG2  1 
ATOM   1441 N N    . ASP A 1 187 ? 11.160  11.576  -50.344 1.00 38.12  ? 187 ASP A N    1 
ATOM   1442 C CA   . ASP A 1 187 ? 11.900  11.000  -49.236 1.00 39.76  ? 187 ASP A CA   1 
ATOM   1443 C C    . ASP A 1 187 ? 13.394  11.049  -49.549 1.00 44.00  ? 187 ASP A C    1 
ATOM   1444 O O    . ASP A 1 187 ? 14.039  10.045  -49.889 1.00 39.30  ? 187 ASP A O    1 
ATOM   1445 C CB   . ASP A 1 187 ? 11.402  9.590   -48.899 1.00 41.73  ? 187 ASP A CB   1 
ATOM   1446 C CG   . ASP A 1 187 ? 11.304  8.657   -50.115 1.00 43.71  ? 187 ASP A CG   1 
ATOM   1447 O OD1  . ASP A 1 187 ? 11.560  9.091   -51.260 1.00 43.94  ? 187 ASP A OD1  1 
ATOM   1448 O OD2  . ASP A 1 187 ? 11.030  7.455   -49.904 1.00 35.75  ? 187 ASP A OD2  1 
ATOM   1449 N N    . ARG A 1 188 ? 13.949  12.265  -49.405 1.00 44.91  ? 188 ARG A N    1 
ATOM   1450 C CA   . ARG A 1 188 ? 15.389  12.496  -49.345 1.00 46.18  ? 188 ARG A CA   1 
ATOM   1451 C C    . ARG A 1 188 ? 15.700  13.560  -48.289 1.00 49.72  ? 188 ARG A C    1 
ATOM   1452 O O    . ARG A 1 188 ? 14.878  14.442  -48.007 1.00 46.05  ? 188 ARG A O    1 
ATOM   1453 C CB   . ARG A 1 188 ? 15.983  12.908  -50.700 1.00 48.59  ? 188 ARG A CB   1 
ATOM   1454 C CG   . ARG A 1 188 ? 15.312  14.063  -51.430 1.00 53.78  ? 188 ARG A CG   1 
ATOM   1455 C CD   . ARG A 1 188 ? 15.801  14.158  -52.903 1.00 60.33  ? 188 ARG A CD   1 
ATOM   1456 N NE   . ARG A 1 188 ? 14.826  13.513  -53.785 1.00 66.07  ? 188 ARG A NE   1 
ATOM   1457 C CZ   . ARG A 1 188 ? 14.585  13.834  -55.052 1.00 67.18  ? 188 ARG A CZ   1 
ATOM   1458 N NH1  . ARG A 1 188 ? 15.274  14.784  -55.673 1.00 63.76  ? 188 ARG A NH1  1 
ATOM   1459 N NH2  . ARG A 1 188 ? 13.637  13.168  -55.716 1.00 63.94  ? 188 ARG A NH2  1 
ATOM   1460 N N    . GLN A 1 189 ? 16.913  13.469  -47.719 1.00 52.38  ? 189 GLN A N    1 
ATOM   1461 C CA   . GLN A 1 189 ? 17.388  14.344  -46.644 1.00 51.45  ? 189 GLN A CA   1 
ATOM   1462 C C    . GLN A 1 189 ? 17.585  15.753  -47.148 1.00 51.60  ? 189 GLN A C    1 
ATOM   1463 O O    . GLN A 1 189 ? 18.720  16.233  -47.258 1.00 53.39  ? 189 GLN A O    1 
ATOM   1464 C CB   . GLN A 1 189 ? 18.707  13.850  -46.043 1.00 53.94  ? 189 GLN A CB   1 
ATOM   1465 C CG   . GLN A 1 189 ? 18.958  14.340  -44.611 1.00 57.30  ? 189 GLN A CG   1 
ATOM   1466 C CD   . GLN A 1 189 ? 18.266  13.475  -43.515 1.00 63.62  ? 189 GLN A CD   1 
ATOM   1467 O OE1  . GLN A 1 189 ? 17.168  12.891  -43.710 1.00 56.20  ? 189 GLN A OE1  1 
ATOM   1468 N NE2  . GLN A 1 189 ? 18.907  13.420  -42.343 1.00 64.94  ? 189 GLN A NE2  1 
ATOM   1469 N N    . THR A 1 190 ? 16.482  16.420  -47.452 1.00 51.44  ? 190 THR A N    1 
ATOM   1470 C CA   . THR A 1 190 ? 16.519  17.755  -48.018 1.00 58.31  ? 190 THR A CA   1 
ATOM   1471 C C    . THR A 1 190 ? 15.477  18.630  -47.327 1.00 58.68  ? 190 THR A C    1 
ATOM   1472 O O    . THR A 1 190 ? 14.461  18.143  -46.812 1.00 53.54  ? 190 THR A O    1 
ATOM   1473 C CB   . THR A 1 190 ? 16.274  17.695  -49.534 1.00 57.20  ? 190 THR A CB   1 
ATOM   1474 O OG1  . THR A 1 190 ? 16.993  18.748  -50.175 1.00 64.03  ? 190 THR A OG1  1 
ATOM   1475 C CG2  . THR A 1 190 ? 14.808  17.864  -49.836 1.00 53.50  ? 190 THR A CG2  1 
ATOM   1476 N N    . ALA A 1 191 ? 15.730  19.940  -47.352 1.00 69.35  ? 191 ALA A N    1 
ATOM   1477 C CA   . ALA A 1 191 ? 14.761  20.931  -46.884 1.00 68.18  ? 191 ALA A CA   1 
ATOM   1478 C C    . ALA A 1 191 ? 13.740  21.181  -47.987 1.00 63.25  ? 191 ALA A C    1 
ATOM   1479 O O    . ALA A 1 191 ? 14.109  21.558  -49.105 1.00 60.54  ? 191 ALA A O    1 
ATOM   1480 C CB   . ALA A 1 191 ? 15.448  22.237  -46.485 1.00 74.88  ? 191 ALA A CB   1 
ATOM   1481 N N    . GLN A 1 192 ? 12.470  20.954  -47.672 1.00 54.85  ? 192 GLN A N    1 
ATOM   1482 C CA   . GLN A 1 192 ? 11.379  21.029  -48.632 1.00 56.27  ? 192 GLN A CA   1 
ATOM   1483 C C    . GLN A 1 192 ? 10.262  21.901  -48.080 1.00 56.52  ? 192 GLN A C    1 
ATOM   1484 O O    . GLN A 1 192 ? 9.942   21.840  -46.887 1.00 56.38  ? 192 GLN A O    1 
ATOM   1485 C CB   . GLN A 1 192 ? 10.843  19.633  -48.971 1.00 51.82  ? 192 GLN A CB   1 
ATOM   1486 C CG   . GLN A 1 192 ? 11.906  18.714  -49.562 1.00 48.73  ? 192 GLN A CG   1 
ATOM   1487 C CD   . GLN A 1 192 ? 11.445  17.282  -49.643 1.00 42.78  ? 192 GLN A CD   1 
ATOM   1488 O OE1  . GLN A 1 192 ? 10.377  16.989  -50.184 1.00 40.09  ? 192 GLN A OE1  1 
ATOM   1489 N NE2  . GLN A 1 192 ? 12.238  16.373  -49.074 1.00 41.85  ? 192 GLN A NE2  1 
ATOM   1490 N N    . ALA A 1 193 ? 9.683   22.714  -48.958 1.00 53.60  ? 193 ALA A N    1 
ATOM   1491 C CA   . ALA A 1 193 ? 8.708   23.729  -48.583 1.00 52.75  ? 193 ALA A CA   1 
ATOM   1492 C C    . ALA A 1 193 ? 7.315   23.199  -48.887 1.00 52.81  ? 193 ALA A C    1 
ATOM   1493 O O    . ALA A 1 193 ? 7.042   22.777  -50.017 1.00 51.02  ? 193 ALA A O    1 
ATOM   1494 C CB   . ALA A 1 193 ? 8.960   25.031  -49.338 1.00 52.27  ? 193 ALA A CB   1 
ATOM   1495 N N    . ALA A 1 194 ? 6.465   23.144  -47.866 1.00 52.32  ? 194 ALA A N    1 
ATOM   1496 C CA   . ALA A 1 194 ? 5.049   22.943  -48.112 1.00 48.97  ? 194 ALA A CA   1 
ATOM   1497 C C    . ALA A 1 194 ? 4.446   24.252  -48.611 1.00 51.25  ? 194 ALA A C    1 
ATOM   1498 O O    . ALA A 1 194 ? 5.060   25.321  -48.526 1.00 50.08  ? 194 ALA A O    1 
ATOM   1499 C CB   . ALA A 1 194 ? 4.354   22.447  -46.844 1.00 48.00  ? 194 ALA A CB   1 
ATOM   1500 N N    . GLY A 1 195 ? 3.238   24.188  -49.147 1.00 48.12  ? 195 GLY A N    1 
ATOM   1501 C CA   . GLY A 1 195 ? 2.631   25.425  -49.626 1.00 55.60  ? 195 GLY A CA   1 
ATOM   1502 C C    . GLY A 1 195 ? 2.373   26.435  -48.504 1.00 56.25  ? 195 GLY A C    1 
ATOM   1503 O O    . GLY A 1 195 ? 2.561   26.172  -47.314 1.00 51.89  ? 195 GLY A O    1 
ATOM   1504 N N    . THR A 1 196 ? 1.963   27.643  -48.905 1.00 53.25  ? 196 THR A N    1 
ATOM   1505 C CA   . THR A 1 196 ? 1.109   28.430  -48.032 1.00 52.50  ? 196 THR A CA   1 
ATOM   1506 C C    . THR A 1 196 ? -0.004  27.535  -47.484 1.00 53.01  ? 196 THR A C    1 
ATOM   1507 O O    . THR A 1 196 ? -0.551  26.682  -48.187 1.00 50.98  ? 196 THR A O    1 
ATOM   1508 C CB   . THR A 1 196 ? 0.498   29.617  -48.779 1.00 50.84  ? 196 THR A CB   1 
ATOM   1509 O OG1  . THR A 1 196 ? 1.536   30.411  -49.368 1.00 56.77  ? 196 THR A OG1  1 
ATOM   1510 C CG2  . THR A 1 196 ? -0.275  30.477  -47.798 1.00 49.42  ? 196 THR A CG2  1 
ATOM   1511 N N    . ASP A 1 197 ? -0.339  27.714  -46.228 1.00 52.43  ? 197 ASP A N    1 
ATOM   1512 C CA   . ASP A 1 197 ? -1.466  26.977  -45.681 1.00 53.37  ? 197 ASP A CA   1 
ATOM   1513 C C    . ASP A 1 197 ? -2.711  27.847  -45.711 1.00 59.50  ? 197 ASP A C    1 
ATOM   1514 O O    . ASP A 1 197 ? -2.656  29.073  -45.837 1.00 62.93  ? 197 ASP A O    1 
ATOM   1515 C CB   . ASP A 1 197 ? -1.205  26.506  -44.248 1.00 54.24  ? 197 ASP A CB   1 
ATOM   1516 C CG   . ASP A 1 197 ? -2.007  25.241  -43.891 1.00 56.68  ? 197 ASP A CG   1 
ATOM   1517 O OD1  . ASP A 1 197 ? -2.618  24.584  -44.796 1.00 50.87  ? 197 ASP A OD1  1 
ATOM   1518 O OD2  . ASP A 1 197 ? -2.076  24.939  -42.678 1.00 55.08  ? 197 ASP A OD2  1 
ATOM   1519 N N    . THR A 1 198 ? -3.843  27.195  -45.571 1.00 60.24  ? 198 THR A N    1 
ATOM   1520 C CA   . THR A 1 198 ? -5.096  27.897  -45.416 1.00 62.29  ? 198 THR A CA   1 
ATOM   1521 C C    . THR A 1 198 ? -5.858  27.240  -44.275 1.00 54.95  ? 198 THR A C    1 
ATOM   1522 O O    . THR A 1 198 ? -5.632  26.074  -43.934 1.00 50.13  ? 198 THR A O    1 
ATOM   1523 C CB   . THR A 1 198 ? -5.919  27.868  -46.727 1.00 63.11  ? 198 THR A CB   1 
ATOM   1524 O OG1  . THR A 1 198 ? -6.071  26.515  -47.182 1.00 62.99  ? 198 THR A OG1  1 
ATOM   1525 C CG2  . THR A 1 198 ? -5.207  28.659  -47.805 1.00 64.99  ? 198 THR A CG2  1 
ATOM   1526 N N    . THR A 1 199 ? -6.749  28.016  -43.677 1.00 55.16  ? 199 THR A N    1 
ATOM   1527 C CA   . THR A 1 199 ? -7.631  27.514  -42.641 1.00 52.55  ? 199 THR A CA   1 
ATOM   1528 C C    . THR A 1 199 ? -8.792  26.739  -43.268 1.00 55.83  ? 199 THR A C    1 
ATOM   1529 O O    . THR A 1 199 ? -9.384  27.176  -44.261 1.00 58.62  ? 199 THR A O    1 
ATOM   1530 C CB   . THR A 1 199 ? -8.118  28.683  -41.812 1.00 51.74  ? 199 THR A CB   1 
ATOM   1531 O OG1  . THR A 1 199 ? -6.973  29.385  -41.332 1.00 51.53  ? 199 THR A OG1  1 
ATOM   1532 C CG2  . THR A 1 199 ? -8.911  28.200  -40.635 1.00 53.42  ? 199 THR A CG2  1 
ATOM   1533 N N    . ILE A 1 200 ? -9.100  25.575  -42.705 1.00 51.88  ? 200 ILE A N    1 
ATOM   1534 C CA   . ILE A 1 200 ? -10.164 24.738  -43.241 1.00 50.17  ? 200 ILE A CA   1 
ATOM   1535 C C    . ILE A 1 200 ? -11.513 25.335  -42.853 1.00 52.47  ? 200 ILE A C    1 
ATOM   1536 O O    . ILE A 1 200 ? -12.081 24.993  -41.811 1.00 46.13  ? 200 ILE A O    1 
ATOM   1537 C CB   . ILE A 1 200 ? -10.019 23.291  -42.755 1.00 49.71  ? 200 ILE A CB   1 
ATOM   1538 C CG1  . ILE A 1 200 ? -8.564  22.815  -42.939 1.00 48.67  ? 200 ILE A CG1  1 
ATOM   1539 C CG2  . ILE A 1 200 ? -11.017 22.384  -43.493 1.00 47.66  ? 200 ILE A CG2  1 
ATOM   1540 C CD1  . ILE A 1 200 ? -8.204  21.579  -42.088 1.00 40.73  ? 200 ILE A CD1  1 
ATOM   1541 N N    . THR A 1 201 ? -12.043 26.218  -43.711 1.00 56.63  ? 201 THR A N    1 
ATOM   1542 C CA   . THR A 1 201 ? -13.222 27.006  -43.352 1.00 51.51  ? 201 THR A CA   1 
ATOM   1543 C C    . THR A 1 201 ? -14.373 26.141  -42.843 1.00 45.56  ? 201 THR A C    1 
ATOM   1544 O O    . THR A 1 201 ? -15.027 26.492  -41.848 1.00 45.37  ? 201 THR A O    1 
ATOM   1545 C CB   . THR A 1 201 ? -13.671 27.840  -44.544 1.00 53.73  ? 201 THR A CB   1 
ATOM   1546 O OG1  . THR A 1 201 ? -12.549 28.570  -45.058 1.00 60.05  ? 201 THR A OG1  1 
ATOM   1547 C CG2  . THR A 1 201 ? -14.746 28.818  -44.092 1.00 55.68  ? 201 THR A CG2  1 
ATOM   1548 N N    . VAL A 1 202 ? -14.645 25.023  -43.518 1.00 43.10  ? 202 VAL A N    1 
ATOM   1549 C CA   . VAL A 1 202 ? -15.773 24.174  -43.140 1.00 47.73  ? 202 VAL A CA   1 
ATOM   1550 C C    . VAL A 1 202 ? -15.576 23.628  -41.728 1.00 46.59  ? 202 VAL A C    1 
ATOM   1551 O O    . VAL A 1 202 ? -16.514 23.615  -40.920 1.00 45.57  ? 202 VAL A O    1 
ATOM   1552 C CB   . VAL A 1 202 ? -15.996 23.057  -44.189 1.00 44.01  ? 202 VAL A CB   1 
ATOM   1553 C CG1  . VAL A 1 202 ? -15.209 21.814  -43.907 1.00 44.25  ? 202 VAL A CG1  1 
ATOM   1554 C CG2  . VAL A 1 202 ? -17.457 22.683  -44.249 1.00 48.09  ? 202 VAL A CG2  1 
ATOM   1555 N N    . ASN A 1 203 ? -14.354 23.181  -41.401 1.00 44.28  ? 203 ASN A N    1 
ATOM   1556 C CA   . ASN A 1 203 ? -14.084 22.714  -40.039 1.00 46.30  ? 203 ASN A CA   1 
ATOM   1557 C C    . ASN A 1 203 ? -14.272 23.825  -39.019 1.00 41.11  ? 203 ASN A C    1 
ATOM   1558 O O    . ASN A 1 203 ? -14.836 23.593  -37.943 1.00 38.88  ? 203 ASN A O    1 
ATOM   1559 C CB   . ASN A 1 203 ? -12.676 22.148  -39.933 1.00 41.29  ? 203 ASN A CB   1 
ATOM   1560 C CG   . ASN A 1 203 ? -12.532 20.879  -40.678 1.00 43.43  ? 203 ASN A CG   1 
ATOM   1561 O OD1  . ASN A 1 203 ? -13.415 20.514  -41.461 1.00 42.87  ? 203 ASN A OD1  1 
ATOM   1562 N ND2  . ASN A 1 203 ? -11.418 20.179  -40.460 1.00 40.60  ? 203 ASN A ND2  1 
ATOM   1563 N N    . VAL A 1 204 ? -13.833 25.046  -39.335 1.00 40.22  ? 204 VAL A N    1 
ATOM   1564 C CA   . VAL A 1 204 ? -14.008 26.133  -38.374 1.00 42.04  ? 204 VAL A CA   1 
ATOM   1565 C C    . VAL A 1 204 ? -15.483 26.330  -38.057 1.00 45.91  ? 204 VAL A C    1 
ATOM   1566 O O    . VAL A 1 204 ? -15.857 26.630  -36.915 1.00 48.40  ? 204 VAL A O    1 
ATOM   1567 C CB   . VAL A 1 204 ? -13.374 27.438  -38.893 1.00 45.18  ? 204 VAL A CB   1 
ATOM   1568 C CG1  . VAL A 1 204 ? -13.740 28.613  -37.961 1.00 49.02  ? 204 VAL A CG1  1 
ATOM   1569 C CG2  . VAL A 1 204 ? -11.852 27.305  -39.015 1.00 45.63  ? 204 VAL A CG2  1 
ATOM   1570 N N    . LEU A 1 205 ? -16.343 26.204  -39.063 1.00 46.44  ? 205 LEU A N    1 
ATOM   1571 C CA   . LEU A 1 205 ? -17.768 26.377  -38.803 1.00 48.89  ? 205 LEU A CA   1 
ATOM   1572 C C    . LEU A 1 205 ? -18.335 25.202  -38.009 1.00 43.86  ? 205 LEU A C    1 
ATOM   1573 O O    . LEU A 1 205 ? -19.156 25.400  -37.110 1.00 44.70  ? 205 LEU A O    1 
ATOM   1574 C CB   . LEU A 1 205 ? -18.532 26.560  -40.119 1.00 50.65  ? 205 LEU A CB   1 
ATOM   1575 C CG   . LEU A 1 205 ? -18.169 27.807  -40.937 1.00 51.94  ? 205 LEU A CG   1 
ATOM   1576 C CD1  . LEU A 1 205 ? -18.726 27.723  -42.368 1.00 51.55  ? 205 LEU A CD1  1 
ATOM   1577 C CD2  . LEU A 1 205 ? -18.632 29.085  -40.245 1.00 48.82  ? 205 LEU A CD2  1 
ATOM   1578 N N    . ALA A 1 206 ? -17.922 23.972  -38.325 1.00 42.70  ? 206 ALA A N    1 
ATOM   1579 C CA   . ALA A 1 206 ? -18.371 22.834  -37.522 1.00 42.90  ? 206 ALA A CA   1 
ATOM   1580 C C    . ALA A 1 206 ? -17.983 23.000  -36.050 1.00 45.52  ? 206 ALA A C    1 
ATOM   1581 O O    . ALA A 1 206 ? -18.736 22.600  -35.142 1.00 49.13  ? 206 ALA A O    1 
ATOM   1582 C CB   . ALA A 1 206 ? -17.815 21.536  -38.113 1.00 38.96  ? 206 ALA A CB   1 
ATOM   1583 N N    . TRP A 1 207 ? -16.839 23.627  -35.785 1.00 44.32  ? 207 TRP A N    1 
ATOM   1584 C CA   . TRP A 1 207 ? -16.424 23.838  -34.401 1.00 44.15  ? 207 TRP A CA   1 
ATOM   1585 C C    . TRP A 1 207 ? -17.263 24.941  -33.744 1.00 46.04  ? 207 TRP A C    1 
ATOM   1586 O O    . TRP A 1 207 ? -17.683 24.804  -32.584 1.00 44.43  ? 207 TRP A O    1 
ATOM   1587 C CB   . TRP A 1 207 ? -14.915 24.141  -34.387 1.00 43.27  ? 207 TRP A CB   1 
ATOM   1588 C CG   . TRP A 1 207 ? -14.256 24.546  -33.050 1.00 48.56  ? 207 TRP A CG   1 
ATOM   1589 C CD1  . TRP A 1 207 ? -13.876 23.723  -32.012 1.00 46.11  ? 207 TRP A CD1  1 
ATOM   1590 C CD2  . TRP A 1 207 ? -13.900 25.878  -32.649 1.00 47.37  ? 207 TRP A CD2  1 
ATOM   1591 N NE1  . TRP A 1 207 ? -13.309 24.468  -31.012 1.00 46.52  ? 207 TRP A NE1  1 
ATOM   1592 C CE2  . TRP A 1 207 ? -13.317 25.790  -31.375 1.00 47.13  ? 207 TRP A CE2  1 
ATOM   1593 C CE3  . TRP A 1 207 ? -14.019 27.134  -33.251 1.00 46.24  ? 207 TRP A CE3  1 
ATOM   1594 C CZ2  . TRP A 1 207 ? -12.858 26.904  -30.697 1.00 50.88  ? 207 TRP A CZ2  1 
ATOM   1595 C CZ3  . TRP A 1 207 ? -13.575 28.234  -32.579 1.00 47.91  ? 207 TRP A CZ3  1 
ATOM   1596 C CH2  . TRP A 1 207 ? -12.988 28.120  -31.315 1.00 48.82  ? 207 TRP A CH2  1 
ATOM   1597 N N    . LEU A 1 208 ? -17.582 26.013  -34.484 1.00 47.24  ? 208 LEU A N    1 
ATOM   1598 C CA   . LEU A 1 208 ? -18.508 27.017  -33.947 1.00 45.73  ? 208 LEU A CA   1 
ATOM   1599 C C    . LEU A 1 208 ? -19.850 26.382  -33.610 1.00 41.19  ? 208 LEU A C    1 
ATOM   1600 O O    . LEU A 1 208 ? -20.483 26.742  -32.622 1.00 46.48  ? 208 LEU A O    1 
ATOM   1601 C CB   . LEU A 1 208 ? -18.697 28.172  -34.948 1.00 48.13  ? 208 LEU A CB   1 
ATOM   1602 C CG   . LEU A 1 208 ? -17.466 29.058  -35.128 1.00 49.07  ? 208 LEU A CG   1 
ATOM   1603 C CD1  . LEU A 1 208 ? -17.687 30.158  -36.134 1.00 53.61  ? 208 LEU A CD1  1 
ATOM   1604 C CD2  . LEU A 1 208 ? -17.034 29.661  -33.773 1.00 45.69  ? 208 LEU A CD2  1 
ATOM   1605 N N    . TYR A 1 209 ? -20.313 25.437  -34.431 1.00 47.72  ? 209 TYR A N    1 
ATOM   1606 C CA   . TYR A 1 209 ? -21.545 24.736  -34.076 1.00 46.66  ? 209 TYR A CA   1 
ATOM   1607 C C    . TYR A 1 209 ? -21.342 23.885  -32.824 1.00 46.70  ? 209 TYR A C    1 
ATOM   1608 O O    . TYR A 1 209 ? -22.150 23.942  -31.890 1.00 48.96  ? 209 TYR A O    1 
ATOM   1609 C CB   . TYR A 1 209 ? -22.024 23.878  -35.242 1.00 49.11  ? 209 TYR A CB   1 
ATOM   1610 C CG   . TYR A 1 209 ? -22.830 24.635  -36.283 1.00 53.81  ? 209 TYR A CG   1 
ATOM   1611 C CD1  . TYR A 1 209 ? -24.078 25.165  -35.976 1.00 56.39  ? 209 TYR A CD1  1 
ATOM   1612 C CD2  . TYR A 1 209 ? -22.358 24.780  -37.575 1.00 51.95  ? 209 TYR A CD2  1 
ATOM   1613 C CE1  . TYR A 1 209 ? -24.825 25.836  -36.923 1.00 58.49  ? 209 TYR A CE1  1 
ATOM   1614 C CE2  . TYR A 1 209 ? -23.085 25.452  -38.523 1.00 55.49  ? 209 TYR A CE2  1 
ATOM   1615 C CZ   . TYR A 1 209 ? -24.326 25.975  -38.197 1.00 59.06  ? 209 TYR A CZ   1 
ATOM   1616 O OH   . TYR A 1 209 ? -25.056 26.653  -39.144 1.00 56.42  ? 209 TYR A OH   1 
ATOM   1617 N N    . ALA A 1 210 ? -20.243 23.115  -32.771 1.00 45.15  ? 210 ALA A N    1 
ATOM   1618 C CA   . ALA A 1 210 ? -19.904 22.396  -31.542 1.00 47.48  ? 210 ALA A CA   1 
ATOM   1619 C C    . ALA A 1 210 ? -19.956 23.331  -30.345 1.00 46.43  ? 210 ALA A C    1 
ATOM   1620 O O    . ALA A 1 210 ? -20.520 22.988  -29.299 1.00 45.63  ? 210 ALA A O    1 
ATOM   1621 C CB   . ALA A 1 210 ? -18.514 21.749  -31.661 1.00 43.99  ? 210 ALA A CB   1 
ATOM   1622 N N    . ALA A 1 211 ? -19.415 24.543  -30.501 1.00 46.35  ? 211 ALA A N    1 
ATOM   1623 C CA   . ALA A 1 211 ? -19.476 25.540  -29.438 1.00 45.01  ? 211 ALA A CA   1 
ATOM   1624 C C    . ALA A 1 211 ? -20.912 25.854  -29.041 1.00 52.10  ? 211 ALA A C    1 
ATOM   1625 O O    . ALA A 1 211 ? -21.239 25.924  -27.851 1.00 51.96  ? 211 ALA A O    1 
ATOM   1626 C CB   . ALA A 1 211 ? -18.769 26.819  -29.890 1.00 48.81  ? 211 ALA A CB   1 
ATOM   1627 N N    . VAL A 1 212 ? -21.777 26.108  -30.027 1.00 50.56  ? 212 VAL A N    1 
ATOM   1628 C CA   . VAL A 1 212 ? -23.177 26.385  -29.713 1.00 51.22  ? 212 VAL A CA   1 
ATOM   1629 C C    . VAL A 1 212 ? -23.806 25.195  -29.002 1.00 47.82  ? 212 VAL A C    1 
ATOM   1630 O O    . VAL A 1 212 ? -24.517 25.347  -28.001 1.00 52.33  ? 212 VAL A O    1 
ATOM   1631 C CB   . VAL A 1 212 ? -23.956 26.742  -30.996 1.00 55.18  ? 212 VAL A CB   1 
ATOM   1632 C CG1  . VAL A 1 212 ? -25.440 26.939  -30.668 1.00 53.84  ? 212 VAL A CG1  1 
ATOM   1633 C CG2  . VAL A 1 212 ? -23.345 27.974  -31.673 1.00 53.13  ? 212 VAL A CG2  1 
ATOM   1634 N N    . ILE A 1 213 ? -23.540 23.987  -29.504 1.00 49.56  ? 213 ILE A N    1 
ATOM   1635 C CA   . ILE A 1 213 ? -24.049 22.782  -28.858 1.00 49.75  ? 213 ILE A CA   1 
ATOM   1636 C C    . ILE A 1 213 ? -23.679 22.775  -27.385 1.00 51.29  ? 213 ILE A C    1 
ATOM   1637 O O    . ILE A 1 213 ? -24.481 22.370  -26.534 1.00 56.58  ? 213 ILE A O    1 
ATOM   1638 C CB   . ILE A 1 213 ? -23.510 21.532  -29.567 1.00 50.12  ? 213 ILE A CB   1 
ATOM   1639 C CG1  . ILE A 1 213 ? -23.694 21.658  -31.063 1.00 52.06  ? 213 ILE A CG1  1 
ATOM   1640 C CG2  . ILE A 1 213 ? -24.231 20.278  -29.041 1.00 47.05  ? 213 ILE A CG2  1 
ATOM   1641 C CD1  . ILE A 1 213 ? -24.970 21.064  -31.475 1.00 55.37  ? 213 ILE A CD1  1 
ATOM   1642 N N    . ASN A 1 214 ? -22.485 23.276  -27.053 1.00 49.65  ? 214 ASN A N    1 
ATOM   1643 C CA   . ASN A 1 214 ? -21.948 23.177  -25.699 1.00 52.04  ? 214 ASN A CA   1 
ATOM   1644 C C    . ASN A 1 214 ? -22.097 24.477  -24.910 1.00 54.41  ? 214 ASN A C    1 
ATOM   1645 O O    . ASN A 1 214 ? -21.316 24.731  -23.979 1.00 53.71  ? 214 ASN A O    1 
ATOM   1646 C CB   . ASN A 1 214 ? -20.481 22.756  -25.753 1.00 50.21  ? 214 ASN A CB   1 
ATOM   1647 C CG   . ASN A 1 214 ? -20.310 21.245  -25.881 1.00 53.68  ? 214 ASN A CG   1 
ATOM   1648 O OD1  . ASN A 1 214 ? -19.982 20.566  -24.912 1.00 57.10  ? 214 ASN A OD1  1 
ATOM   1649 N ND2  . ASN A 1 214 ? -20.533 20.716  -27.085 1.00 51.23  ? 214 ASN A ND2  1 
ATOM   1650 N N    . GLY A 1 215 ? -23.100 25.308  -25.242 1.00 55.32  ? 215 GLY A N    1 
ATOM   1651 C CA   . GLY A 1 215 ? -23.424 26.466  -24.412 1.00 57.26  ? 215 GLY A CA   1 
ATOM   1652 C C    . GLY A 1 215 ? -22.714 27.776  -24.728 1.00 61.15  ? 215 GLY A C    1 
ATOM   1653 O O    . GLY A 1 215 ? -23.094 28.812  -24.164 1.00 64.90  ? 215 GLY A O    1 
ATOM   1654 N N    . ASP A 1 216 ? -21.664 27.767  -25.554 1.00 60.89  ? 216 ASP A N    1 
ATOM   1655 C CA   . ASP A 1 216 ? -20.951 28.994  -25.903 1.00 61.47  ? 216 ASP A CA   1 
ATOM   1656 C C    . ASP A 1 216 ? -21.692 29.683  -27.044 1.00 60.36  ? 216 ASP A C    1 
ATOM   1657 O O    . ASP A 1 216 ? -21.881 29.095  -28.113 1.00 62.34  ? 216 ASP A O    1 
ATOM   1658 C CB   . ASP A 1 216 ? -19.499 28.709  -26.293 1.00 59.43  ? 216 ASP A CB   1 
ATOM   1659 C CG   . ASP A 1 216 ? -18.642 28.228  -25.107 1.00 73.88  ? 216 ASP A CG   1 
ATOM   1660 O OD1  . ASP A 1 216 ? -17.502 28.739  -24.975 1.00 69.61  ? 216 ASP A OD1  1 
ATOM   1661 O OD2  . ASP A 1 216 ? -19.096 27.364  -24.308 1.00 70.97  ? 216 ASP A OD2  1 
ATOM   1662 N N    . ARG A 1 217 ? -22.125 30.915  -26.820 1.00 65.81  ? 217 ARG A N    1 
ATOM   1663 C CA   . ARG A 1 217 ? -22.890 31.613  -27.842 1.00 64.93  ? 217 ARG A CA   1 
ATOM   1664 C C    . ARG A 1 217 ? -22.554 33.095  -27.988 1.00 64.29  ? 217 ARG A C    1 
ATOM   1665 O O    . ARG A 1 217 ? -23.128 33.748  -28.866 1.00 66.60  ? 217 ARG A O    1 
ATOM   1666 C CB   . ARG A 1 217 ? -24.391 31.455  -27.555 1.00 62.01  ? 217 ARG A CB   1 
ATOM   1667 C CG   . ARG A 1 217 ? -24.847 30.006  -27.588 1.00 66.10  ? 217 ARG A CG   1 
ATOM   1668 C CD   . ARG A 1 217 ? -26.264 29.893  -27.064 1.00 71.99  ? 217 ARG A CD   1 
ATOM   1669 N NE   . ARG A 1 217 ? -27.141 30.773  -27.824 1.00 72.14  ? 217 ARG A NE   1 
ATOM   1670 C CZ   . ARG A 1 217 ? -27.790 30.436  -28.934 1.00 71.07  ? 217 ARG A CZ   1 
ATOM   1671 N NH1  . ARG A 1 217 ? -27.741 29.204  -29.423 1.00 63.67  ? 217 ARG A NH1  1 
ATOM   1672 N NH2  . ARG A 1 217 ? -28.542 31.349  -29.545 1.00 72.13  ? 217 ARG A NH2  1 
ATOM   1673 N N    . TRP A 1 218 ? -21.627 33.637  -27.185 1.00 66.86  ? 218 TRP A N    1 
ATOM   1674 C CA   . TRP A 1 218 ? -21.310 35.063  -27.203 1.00 64.18  ? 218 TRP A CA   1 
ATOM   1675 C C    . TRP A 1 218 ? -21.004 35.587  -28.602 1.00 63.70  ? 218 TRP A C    1 
ATOM   1676 O O    . TRP A 1 218 ? -21.087 36.796  -28.829 1.00 62.11  ? 218 TRP A O    1 
ATOM   1677 C CB   . TRP A 1 218 ? -20.118 35.347  -26.251 1.00 66.15  ? 218 TRP A CB   1 
ATOM   1678 C CG   . TRP A 1 218 ? -18.726 34.805  -26.694 1.00 66.27  ? 218 TRP A CG   1 
ATOM   1679 C CD1  . TRP A 1 218 ? -18.092 33.688  -26.219 1.00 66.38  ? 218 TRP A CD1  1 
ATOM   1680 C CD2  . TRP A 1 218 ? -17.824 35.388  -27.649 1.00 70.99  ? 218 TRP A CD2  1 
ATOM   1681 N NE1  . TRP A 1 218 ? -16.874 33.523  -26.832 1.00 65.78  ? 218 TRP A NE1  1 
ATOM   1682 C CE2  . TRP A 1 218 ? -16.680 34.551  -27.712 1.00 70.22  ? 218 TRP A CE2  1 
ATOM   1683 C CE3  . TRP A 1 218 ? -17.879 36.522  -28.474 1.00 70.26  ? 218 TRP A CE3  1 
ATOM   1684 C CZ2  . TRP A 1 218 ? -15.602 34.814  -28.557 1.00 70.56  ? 218 TRP A CZ2  1 
ATOM   1685 C CZ3  . TRP A 1 218 ? -16.808 36.784  -29.313 1.00 71.21  ? 218 TRP A CZ3  1 
ATOM   1686 C CH2  . TRP A 1 218 ? -15.685 35.931  -29.352 1.00 73.80  ? 218 TRP A CH2  1 
ATOM   1687 N N    . PHE A 1 219 ? -20.668 34.719  -29.551 1.00 63.16  ? 219 PHE A N    1 
ATOM   1688 C CA   . PHE A 1 219 ? -20.264 35.163  -30.876 1.00 65.08  ? 219 PHE A CA   1 
ATOM   1689 C C    . PHE A 1 219 ? -21.406 35.176  -31.878 1.00 61.65  ? 219 PHE A C    1 
ATOM   1690 O O    . PHE A 1 219 ? -21.165 35.483  -33.043 1.00 65.97  ? 219 PHE A O    1 
ATOM   1691 C CB   . PHE A 1 219 ? -19.143 34.266  -31.417 1.00 60.75  ? 219 PHE A CB   1 
ATOM   1692 C CG   . PHE A 1 219 ? -19.464 32.810  -31.333 1.00 60.06  ? 219 PHE A CG   1 
ATOM   1693 C CD1  . PHE A 1 219 ? -19.147 32.077  -30.199 1.00 60.91  ? 219 PHE A CD1  1 
ATOM   1694 C CD2  . PHE A 1 219 ? -20.095 32.170  -32.388 1.00 57.99  ? 219 PHE A CD2  1 
ATOM   1695 C CE1  . PHE A 1 219 ? -19.458 30.738  -30.127 1.00 54.51  ? 219 PHE A CE1  1 
ATOM   1696 C CE2  . PHE A 1 219 ? -20.402 30.835  -32.310 1.00 56.22  ? 219 PHE A CE2  1 
ATOM   1697 C CZ   . PHE A 1 219 ? -20.087 30.127  -31.177 1.00 53.26  ? 219 PHE A CZ   1 
ATOM   1698 N N    . LEU A 1 220 ? -22.619 34.806  -31.480 1.00 61.00  ? 220 LEU A N    1 
ATOM   1699 C CA   . LEU A 1 220 ? -23.731 34.701  -32.423 1.00 65.82  ? 220 LEU A CA   1 
ATOM   1700 C C    . LEU A 1 220 ? -24.303 36.091  -32.733 1.00 71.97  ? 220 LEU A C    1 
ATOM   1701 O O    . LEU A 1 220 ? -24.801 36.781  -31.834 1.00 69.60  ? 220 LEU A O    1 
ATOM   1702 C CB   . LEU A 1 220 ? -24.821 33.786  -31.878 1.00 65.41  ? 220 LEU A CB   1 
ATOM   1703 C CG   . LEU A 1 220 ? -24.494 32.307  -31.796 1.00 62.65  ? 220 LEU A CG   1 
ATOM   1704 C CD1  . LEU A 1 220 ? -25.709 31.497  -31.322 1.00 60.25  ? 220 LEU A CD1  1 
ATOM   1705 C CD2  . LEU A 1 220 ? -23.981 31.839  -33.144 1.00 64.11  ? 220 LEU A CD2  1 
ATOM   1706 N N    . ASN A 1 221 ? -24.224 36.502  -33.998 1.00 72.90  ? 221 ASN A N    1 
ATOM   1707 C CA   . ASN A 1 221 ? -24.708 37.806  -34.429 1.00 79.23  ? 221 ASN A CA   1 
ATOM   1708 C C    . ASN A 1 221 ? -26.197 37.748  -34.740 1.00 82.46  ? 221 ASN A C    1 
ATOM   1709 O O    . ASN A 1 221 ? -26.812 36.686  -34.789 1.00 84.59  ? 221 ASN A O    1 
ATOM   1710 C CB   . ASN A 1 221 ? -23.954 38.276  -35.674 1.00 77.41  ? 221 ASN A CB   1 
ATOM   1711 C CG   . ASN A 1 221 ? -24.180 37.365  -36.882 1.00 75.05  ? 221 ASN A CG   1 
ATOM   1712 O OD1  . ASN A 1 221 ? -24.975 36.410  -36.860 1.00 72.12  ? 221 ASN A OD1  1 
ATOM   1713 N ND2  . ASN A 1 221 ? -23.458 37.655  -37.947 1.00 76.58  ? 221 ASN A ND2  1 
ATOM   1714 N N    . ARG A 1 222 ? -26.765 38.917  -34.997 1.00 92.58  ? 222 ARG A N    1 
ATOM   1715 C CA   . ARG A 1 222 ? -28.034 39.032  -35.705 1.00 99.79  ? 222 ARG A CA   1 
ATOM   1716 C C    . ARG A 1 222 ? -27.807 39.160  -37.204 1.00 94.34  ? 222 ARG A C    1 
ATOM   1717 O O    . ARG A 1 222 ? -28.560 38.594  -38.009 1.00 94.53  ? 222 ARG A O    1 
ATOM   1718 C CB   . ARG A 1 222 ? -28.806 40.265  -35.219 1.00 110.64 ? 222 ARG A CB   1 
ATOM   1719 C CG   . ARG A 1 222 ? -28.068 41.569  -35.500 1.00 108.14 ? 222 ARG A CG   1 
ATOM   1720 C CD   . ARG A 1 222 ? -26.978 41.836  -34.477 1.00 112.98 ? 222 ARG A CD   1 
ATOM   1721 N NE   . ARG A 1 222 ? -27.423 41.583  -33.113 1.00 112.59 ? 222 ARG A NE   1 
ATOM   1722 C CZ   . ARG A 1 222 ? -27.900 42.523  -32.308 1.00 116.13 ? 222 ARG A CZ   1 
ATOM   1723 N NH1  . ARG A 1 222 ? -28.010 43.781  -32.704 1.00 115.51 ? 222 ARG A NH1  1 
ATOM   1724 N NH2  . ARG A 1 222 ? -28.283 42.191  -31.078 1.00 117.44 ? 222 ARG A NH2  1 
ATOM   1725 N N    . PHE A 1 223 ? -26.740 39.870  -37.566 1.00 88.19  ? 223 PHE A N    1 
ATOM   1726 C CA   . PHE A 1 223 ? -26.401 40.113  -38.957 1.00 88.00  ? 223 PHE A CA   1 
ATOM   1727 C C    . PHE A 1 223 ? -26.364 38.787  -39.719 1.00 80.42  ? 223 PHE A C    1 
ATOM   1728 O O    . PHE A 1 223 ? -26.156 37.716  -39.133 1.00 79.38  ? 223 PHE A O    1 
ATOM   1729 C CB   . PHE A 1 223 ? -25.050 40.828  -38.981 1.00 85.39  ? 223 PHE A CB   1 
ATOM   1730 C CG   . PHE A 1 223 ? -25.159 42.300  -39.252 1.00 95.23  ? 223 PHE A CG   1 
ATOM   1731 C CD1  . PHE A 1 223 ? -24.512 43.196  -38.393 1.00 101.19 ? 223 PHE A CD1  1 
ATOM   1732 C CD2  . PHE A 1 223 ? -25.936 42.804  -40.272 1.00 96.14  ? 223 PHE A CD2  1 
ATOM   1733 C CE1  . PHE A 1 223 ? -24.635 44.568  -38.557 1.00 103.98 ? 223 PHE A CE1  1 
ATOM   1734 C CE2  . PHE A 1 223 ? -26.064 44.201  -40.460 1.00 101.05 ? 223 PHE A CE2  1 
ATOM   1735 C CZ   . PHE A 1 223 ? -25.403 45.080  -39.589 1.00 108.08 ? 223 PHE A CZ   1 
ATOM   1736 N N    . THR A 1 224 ? -26.597 38.837  -41.033 1.00 76.76  ? 224 THR A N    1 
ATOM   1737 C CA   . THR A 1 224 ? -26.395 37.661  -41.883 1.00 73.04  ? 224 THR A CA   1 
ATOM   1738 C C    . THR A 1 224 ? -25.491 38.068  -43.027 1.00 75.48  ? 224 THR A C    1 
ATOM   1739 O O    . THR A 1 224 ? -25.056 39.221  -43.108 1.00 78.20  ? 224 THR A O    1 
ATOM   1740 C CB   . THR A 1 224 ? -27.679 37.046  -42.452 1.00 75.80  ? 224 THR A CB   1 
ATOM   1741 O OG1  . THR A 1 224 ? -27.382 35.751  -43.014 1.00 67.07  ? 224 THR A OG1  1 
ATOM   1742 C CG2  . THR A 1 224 ? -28.251 37.895  -43.469 1.00 77.29  ? 224 THR A CG2  1 
ATOM   1743 N N    . THR A 1 225 ? -25.194 37.130  -43.926 1.00 70.56  ? 225 THR A N    1 
ATOM   1744 C CA   . THR A 1 225 ? -24.315 37.445  -45.048 1.00 72.63  ? 225 THR A CA   1 
ATOM   1745 C C    . THR A 1 225 ? -24.662 36.537  -46.227 1.00 74.33  ? 225 THR A C    1 
ATOM   1746 O O    . THR A 1 225 ? -25.649 35.791  -46.203 1.00 71.95  ? 225 THR A O    1 
ATOM   1747 C CB   . THR A 1 225 ? -22.831 37.308  -44.663 1.00 77.87  ? 225 THR A CB   1 
ATOM   1748 O OG1  . THR A 1 225 ? -21.993 37.803  -45.728 1.00 79.26  ? 225 THR A OG1  1 
ATOM   1749 C CG2  . THR A 1 225 ? -22.472 35.848  -44.401 1.00 75.20  ? 225 THR A CG2  1 
ATOM   1750 N N    . THR A 1 226 ? -23.840 36.605  -47.264 1.00 72.55  ? 226 THR A N    1 
ATOM   1751 C CA   . THR A 1 226 ? -24.033 35.805  -48.457 1.00 75.04  ? 226 THR A CA   1 
ATOM   1752 C C    . THR A 1 226 ? -22.800 34.956  -48.690 1.00 73.35  ? 226 THR A C    1 
ATOM   1753 O O    . THR A 1 226 ? -21.685 35.366  -48.357 1.00 76.85  ? 226 THR A O    1 
ATOM   1754 C CB   . THR A 1 226 ? -24.287 36.692  -49.698 1.00 77.63  ? 226 THR A CB   1 
ATOM   1755 O OG1  . THR A 1 226 ? -23.032 37.078  -50.278 1.00 79.37  ? 226 THR A OG1  1 
ATOM   1756 C CG2  . THR A 1 226 ? -25.069 37.940  -49.328 1.00 71.06  ? 226 THR A CG2  1 
ATOM   1757 N N    . LEU A 1 227 ? -23.003 33.782  -49.292 1.00 68.66  ? 227 LEU A N    1 
ATOM   1758 C CA   . LEU A 1 227 ? -21.873 32.925  -49.607 1.00 71.32  ? 227 LEU A CA   1 
ATOM   1759 C C    . LEU A 1 227 ? -20.844 33.651  -50.460 1.00 75.25  ? 227 LEU A C    1 
ATOM   1760 O O    . LEU A 1 227 ? -19.650 33.334  -50.402 1.00 78.76  ? 227 LEU A O    1 
ATOM   1761 C CB   . LEU A 1 227 ? -22.350 31.656  -50.313 1.00 66.75  ? 227 LEU A CB   1 
ATOM   1762 C CG   . LEU A 1 227 ? -21.186 30.842  -50.875 1.00 71.53  ? 227 LEU A CG   1 
ATOM   1763 C CD1  . LEU A 1 227 ? -20.437 30.160  -49.717 1.00 71.32  ? 227 LEU A CD1  1 
ATOM   1764 C CD2  . LEU A 1 227 ? -21.645 29.805  -51.889 1.00 63.04  ? 227 LEU A CD2  1 
ATOM   1765 N N    . ASN A 1 228 ? -21.283 34.622  -51.260 1.00 73.83  ? 228 ASN A N    1 
ATOM   1766 C CA   . ASN A 1 228 ? -20.361 35.320  -52.141 1.00 73.16  ? 228 ASN A CA   1 
ATOM   1767 C C    . ASN A 1 228 ? -19.533 36.339  -51.363 1.00 77.75  ? 228 ASN A C    1 
ATOM   1768 O O    . ASN A 1 228 ? -18.308 36.382  -51.508 1.00 82.39  ? 228 ASN A O    1 
ATOM   1769 C CB   . ASN A 1 228 ? -21.134 35.972  -53.300 1.00 74.71  ? 228 ASN A CB   1 
ATOM   1770 C CG   . ASN A 1 228 ? -21.018 35.174  -54.611 1.00 63.20  ? 228 ASN A CG   1 
ATOM   1771 O OD1  . ASN A 1 228 ? -20.486 34.063  -54.642 1.00 60.35  ? 228 ASN A OD1  1 
ATOM   1772 N ND2  . ASN A 1 228 ? -21.562 35.730  -55.688 1.00 66.28  ? 228 ASN A ND2  1 
ATOM   1773 N N    . ASP A 1 229 ? -20.171 37.138  -50.498 1.00 78.03  ? 229 ASP A N    1 
ATOM   1774 C CA   . ASP A 1 229 ? -19.428 38.153  -49.751 1.00 84.73  ? 229 ASP A CA   1 
ATOM   1775 C C    . ASP A 1 229 ? -18.622 37.558  -48.605 1.00 85.57  ? 229 ASP A C    1 
ATOM   1776 O O    . ASP A 1 229 ? -17.571 38.106  -48.244 1.00 82.49  ? 229 ASP A O    1 
ATOM   1777 C CB   . ASP A 1 229 ? -20.353 39.222  -49.145 1.00 83.21  ? 229 ASP A CB   1 
ATOM   1778 C CG   . ASP A 1 229 ? -21.270 39.893  -50.166 1.00 83.30  ? 229 ASP A CG   1 
ATOM   1779 O OD1  . ASP A 1 229 ? -21.163 39.616  -51.374 1.00 80.47  ? 229 ASP A OD1  1 
ATOM   1780 O OD2  . ASP A 1 229 ? -22.096 40.734  -49.736 1.00 88.05  ? 229 ASP A OD2  1 
ATOM   1781 N N    . PHE A 1 230 ? -19.110 36.484  -47.981 1.00 90.27  ? 230 PHE A N    1 
ATOM   1782 C CA   . PHE A 1 230 ? -18.270 35.793  -47.011 1.00 89.77  ? 230 PHE A CA   1 
ATOM   1783 C C    . PHE A 1 230 ? -16.963 35.326  -47.633 1.00 87.13  ? 230 PHE A C    1 
ATOM   1784 O O    . PHE A 1 230 ? -15.894 35.450  -47.023 1.00 88.18  ? 230 PHE A O    1 
ATOM   1785 C CB   . PHE A 1 230 ? -18.973 34.591  -46.396 1.00 87.05  ? 230 PHE A CB   1 
ATOM   1786 C CG   . PHE A 1 230 ? -18.056 33.773  -45.527 1.00 91.34  ? 230 PHE A CG   1 
ATOM   1787 C CD1  . PHE A 1 230 ? -17.515 34.330  -44.375 1.00 89.82  ? 230 PHE A CD1  1 
ATOM   1788 C CD2  . PHE A 1 230 ? -17.658 32.499  -45.894 1.00 85.75  ? 230 PHE A CD2  1 
ATOM   1789 C CE1  . PHE A 1 230 ? -16.650 33.612  -43.574 1.00 80.49  ? 230 PHE A CE1  1 
ATOM   1790 C CE2  . PHE A 1 230 ? -16.790 31.784  -45.093 1.00 79.73  ? 230 PHE A CE2  1 
ATOM   1791 C CZ   . PHE A 1 230 ? -16.287 32.347  -43.937 1.00 78.95  ? 230 PHE A CZ   1 
ATOM   1792 N N    . ASN A 1 231 ? -17.022 34.770  -48.839 1.00 81.18  ? 231 ASN A N    1 
ATOM   1793 C CA   . ASN A 1 231 ? -15.786 34.290  -49.442 1.00 78.59  ? 231 ASN A CA   1 
ATOM   1794 C C    . ASN A 1 231 ? -14.807 35.425  -49.712 1.00 83.61  ? 231 ASN A C    1 
ATOM   1795 O O    . ASN A 1 231 ? -13.590 35.225  -49.632 1.00 85.16  ? 231 ASN A O    1 
ATOM   1796 C CB   . ASN A 1 231 ? -16.105 33.512  -50.710 1.00 73.05  ? 231 ASN A CB   1 
ATOM   1797 C CG   . ASN A 1 231 ? -16.287 32.040  -50.440 1.00 77.56  ? 231 ASN A CG   1 
ATOM   1798 O OD1  . ASN A 1 231 ? -17.164 31.387  -51.019 1.00 75.85  ? 231 ASN A OD1  1 
ATOM   1799 N ND2  . ASN A 1 231 ? -15.484 31.509  -49.527 1.00 77.89  ? 231 ASN A ND2  1 
ATOM   1800 N N    . LEU A 1 232 ? -15.311 36.623  -50.022 1.00 83.19  ? 232 LEU A N    1 
ATOM   1801 C CA   . LEU A 1 232 ? -14.437 37.789  -50.101 1.00 84.36  ? 232 LEU A CA   1 
ATOM   1802 C C    . LEU A 1 232 ? -13.774 38.057  -48.762 1.00 83.07  ? 232 LEU A C    1 
ATOM   1803 O O    . LEU A 1 232 ? -12.622 38.500  -48.715 1.00 85.05  ? 232 LEU A O    1 
ATOM   1804 C CB   . LEU A 1 232 ? -15.201 39.033  -50.579 1.00 87.84  ? 232 LEU A CB   1 
ATOM   1805 C CG   . LEU A 1 232 ? -15.436 39.217  -52.091 1.00 96.83  ? 232 LEU A CG   1 
ATOM   1806 C CD1  . LEU A 1 232 ? -14.189 38.882  -52.921 1.00 95.72  ? 232 LEU A CD1  1 
ATOM   1807 C CD2  . LEU A 1 232 ? -16.631 38.413  -52.592 1.00 95.52  ? 232 LEU A CD2  1 
ATOM   1808 N N    . VAL A 1 233 ? -14.476 37.771  -47.669 1.00 83.23  ? 233 VAL A N    1 
ATOM   1809 C CA   . VAL A 1 233 ? -13.878 37.886  -46.349 1.00 79.66  ? 233 VAL A CA   1 
ATOM   1810 C C    . VAL A 1 233 ? -12.986 36.687  -46.042 1.00 78.81  ? 233 VAL A C    1 
ATOM   1811 O O    . VAL A 1 233 ? -11.990 36.823  -45.328 1.00 77.31  ? 233 VAL A O    1 
ATOM   1812 C CB   . VAL A 1 233 ? -14.998 38.032  -45.313 1.00 84.09  ? 233 VAL A CB   1 
ATOM   1813 C CG1  . VAL A 1 233 ? -14.467 37.762  -43.918 1.00 82.71  ? 233 VAL A CG1  1 
ATOM   1814 C CG2  . VAL A 1 233 ? -15.635 39.415  -45.407 1.00 80.71  ? 233 VAL A CG2  1 
ATOM   1815 N N    . ALA A 1 234 ? -13.311 35.508  -46.578 1.00 81.43  ? 234 ALA A N    1 
ATOM   1816 C CA   . ALA A 1 234 ? -12.460 34.333  -46.399 1.00 78.44  ? 234 ALA A CA   1 
ATOM   1817 C C    . ALA A 1 234 ? -11.087 34.553  -47.020 1.00 80.15  ? 234 ALA A C    1 
ATOM   1818 O O    . ALA A 1 234 ? -10.054 34.408  -46.355 1.00 77.95  ? 234 ALA A O    1 
ATOM   1819 C CB   . ALA A 1 234 ? -13.121 33.098  -47.013 1.00 71.65  ? 234 ALA A CB   1 
ATOM   1820 N N    . MET A 1 235 ? -11.060 34.892  -48.311 1.00 80.86  ? 235 MET A N    1 
ATOM   1821 C CA   . MET A 1 235 ? -9.796  35.071  -49.017 1.00 82.64  ? 235 MET A CA   1 
ATOM   1822 C C    . MET A 1 235 ? -8.907  36.143  -48.382 1.00 78.93  ? 235 MET A C    1 
ATOM   1823 O O    . MET A 1 235 ? -7.677  36.012  -48.385 1.00 76.40  ? 235 MET A O    1 
ATOM   1824 C CB   . MET A 1 235 ? -10.063 35.370  -50.491 1.00 90.59  ? 235 MET A CB   1 
ATOM   1825 C CG   . MET A 1 235 ? -9.033  34.700  -51.360 1.00 97.46  ? 235 MET A CG   1 
ATOM   1826 S SD   . MET A 1 235 ? -8.548  33.129  -50.574 1.00 110.60 ? 235 MET A SD   1 
ATOM   1827 C CE   . MET A 1 235 ? -10.130 32.404  -50.089 1.00 85.09  ? 235 MET A CE   1 
ATOM   1828 N N    . LYS A 1 236 ? -9.490  37.214  -47.843 1.00 76.26  ? 236 LYS A N    1 
ATOM   1829 C CA   . LYS A 1 236 ? -8.625  38.223  -47.241 1.00 75.11  ? 236 LYS A CA   1 
ATOM   1830 C C    . LYS A 1 236 ? -7.895  37.684  -46.024 1.00 78.83  ? 236 LYS A C    1 
ATOM   1831 O O    . LYS A 1 236 ? -6.877  38.254  -45.613 1.00 81.95  ? 236 LYS A O    1 
ATOM   1832 C CB   . LYS A 1 236 ? -9.436  39.451  -46.816 1.00 81.68  ? 236 LYS A CB   1 
ATOM   1833 C CG   . LYS A 1 236 ? -8.582  40.619  -46.304 1.00 84.11  ? 236 LYS A CG   1 
ATOM   1834 C CD   . LYS A 1 236 ? -9.423  41.755  -45.690 1.00 85.76  ? 236 LYS A CD   1 
ATOM   1835 C CE   . LYS A 1 236 ? -9.643  42.898  -46.685 1.00 86.12  ? 236 LYS A CE   1 
ATOM   1836 N NZ   . LYS A 1 236 ? -8.889  44.139  -46.320 1.00 87.52  ? 236 LYS A NZ   1 
ATOM   1837 N N    . TYR A 1 237 ? -8.412  36.610  -45.434 1.00 78.07  ? 237 TYR A N    1 
ATOM   1838 C CA   . TYR A 1 237 ? -7.895  36.016  -44.208 1.00 76.14  ? 237 TYR A CA   1 
ATOM   1839 C C    . TYR A 1 237 ? -7.309  34.617  -44.369 1.00 73.67  ? 237 TYR A C    1 
ATOM   1840 O O    . TYR A 1 237 ? -6.985  33.991  -43.359 1.00 73.59  ? 237 TYR A O    1 
ATOM   1841 C CB   . TYR A 1 237 ? -9.016  35.983  -43.164 1.00 70.41  ? 237 TYR A CB   1 
ATOM   1842 C CG   . TYR A 1 237 ? -9.349  37.319  -42.553 1.00 71.61  ? 237 TYR A CG   1 
ATOM   1843 C CD1  . TYR A 1 237 ? -8.687  37.745  -41.406 1.00 70.44  ? 237 TYR A CD1  1 
ATOM   1844 C CD2  . TYR A 1 237 ? -10.269 38.179  -43.140 1.00 70.87  ? 237 TYR A CD2  1 
ATOM   1845 C CE1  . TYR A 1 237 ? -8.967  38.962  -40.822 1.00 75.32  ? 237 TYR A CE1  1 
ATOM   1846 C CE2  . TYR A 1 237 ? -10.550 39.422  -42.565 1.00 73.44  ? 237 TYR A CE2  1 
ATOM   1847 C CZ   . TYR A 1 237 ? -9.892  39.804  -41.402 1.00 75.39  ? 237 TYR A CZ   1 
ATOM   1848 O OH   . TYR A 1 237 ? -10.145 41.014  -40.783 1.00 78.14  ? 237 TYR A OH   1 
ATOM   1849 N N    . ASN A 1 238 ? -7.108  34.117  -45.588 1.00 78.34  ? 238 ASN A N    1 
ATOM   1850 C CA   . ASN A 1 238 ? -6.496  32.803  -45.757 1.00 76.16  ? 238 ASN A CA   1 
ATOM   1851 C C    . ASN A 1 238 ? -7.430  31.658  -45.428 1.00 72.33  ? 238 ASN A C    1 
ATOM   1852 O O    . ASN A 1 238 ? -6.972  30.606  -45.001 1.00 71.95  ? 238 ASN A O    1 
ATOM   1853 C CB   . ASN A 1 238 ? -5.229  32.653  -44.914 1.00 82.04  ? 238 ASN A CB   1 
ATOM   1854 C CG   . ASN A 1 238 ? -4.188  31.841  -45.603 1.00 82.18  ? 238 ASN A CG   1 
ATOM   1855 O OD1  . ASN A 1 238 ? -3.008  31.910  -45.277 1.00 87.96  ? 238 ASN A OD1  1 
ATOM   1856 N ND2  . ASN A 1 238 ? -4.636  30.965  -46.504 1.00 83.27  ? 238 ASN A ND2  1 
ATOM   1857 N N    . TYR A 1 239 ? -8.728  31.801  -45.600 1.00 69.87  ? 239 TYR A N    1 
ATOM   1858 C CA   . TYR A 1 239 ? -9.566  30.649  -45.356 1.00 67.25  ? 239 TYR A CA   1 
ATOM   1859 C C    . TYR A 1 239 ? -9.850  30.004  -46.710 1.00 70.67  ? 239 TYR A C    1 
ATOM   1860 O O    . TYR A 1 239 ? -10.118 30.715  -47.677 1.00 73.88  ? 239 TYR A O    1 
ATOM   1861 C CB   . TYR A 1 239 ? -10.860 31.103  -44.689 1.00 61.02  ? 239 TYR A CB   1 
ATOM   1862 C CG   . TYR A 1 239 ? -10.793 31.186  -43.187 1.00 60.87  ? 239 TYR A CG   1 
ATOM   1863 C CD1  . TYR A 1 239 ? -9.801  31.935  -42.548 1.00 62.20  ? 239 TYR A CD1  1 
ATOM   1864 C CD2  . TYR A 1 239 ? -11.714 30.509  -42.397 1.00 57.48  ? 239 TYR A CD2  1 
ATOM   1865 C CE1  . TYR A 1 239 ? -9.736  32.011  -41.137 1.00 59.00  ? 239 TYR A CE1  1 
ATOM   1866 C CE2  . TYR A 1 239 ? -11.664 30.577  -41.002 1.00 59.48  ? 239 TYR A CE2  1 
ATOM   1867 C CZ   . TYR A 1 239 ? -10.670 31.323  -40.377 1.00 56.03  ? 239 TYR A CZ   1 
ATOM   1868 O OH   . TYR A 1 239 ? -10.642 31.356  -39.008 1.00 55.34  ? 239 TYR A OH   1 
ATOM   1869 N N    . GLU A 1 240 ? -9.786  28.676  -46.795 1.00 73.56  ? 240 GLU A N    1 
ATOM   1870 C CA   . GLU A 1 240 ? -10.204 28.033  -48.030 1.00 73.56  ? 240 GLU A CA   1 
ATOM   1871 C C    . GLU A 1 240 ? -11.635 28.464  -48.349 1.00 76.09  ? 240 GLU A C    1 
ATOM   1872 O O    . GLU A 1 240 ? -12.467 28.584  -47.445 1.00 75.10  ? 240 GLU A O    1 
ATOM   1873 C CB   . GLU A 1 240 ? -10.022 26.518  -48.051 1.00 69.66  ? 240 GLU A CB   1 
ATOM   1874 C CG   . GLU A 1 240 ? -11.177 25.687  -47.645 1.00 74.03  ? 240 GLU A CG   1 
ATOM   1875 C CD   . GLU A 1 240 ? -10.681 24.286  -47.309 1.00 83.23  ? 240 GLU A CD   1 
ATOM   1876 O OE1  . GLU A 1 240 ? -9.437  24.143  -47.154 1.00 80.61  ? 240 GLU A OE1  1 
ATOM   1877 O OE2  . GLU A 1 240 ? -11.512 23.338  -47.178 1.00 83.67  ? 240 GLU A OE2  1 
ATOM   1878 N N    . PRO A 1 241 ? -11.948 28.710  -49.613 1.00 78.64  ? 241 PRO A N    1 
ATOM   1879 C CA   . PRO A 1 241 ? -13.294 29.153  -49.986 1.00 73.44  ? 241 PRO A CA   1 
ATOM   1880 C C    . PRO A 1 241 ? -14.368 28.154  -49.596 1.00 70.74  ? 241 PRO A C    1 
ATOM   1881 O O    . PRO A 1 241 ? -14.217 26.940  -49.746 1.00 72.04  ? 241 PRO A O    1 
ATOM   1882 C CB   . PRO A 1 241 ? -13.193 29.292  -51.504 1.00 73.19  ? 241 PRO A CB   1 
ATOM   1883 C CG   . PRO A 1 241 ? -11.738 29.595  -51.739 1.00 78.91  ? 241 PRO A CG   1 
ATOM   1884 C CD   . PRO A 1 241 ? -11.008 28.759  -50.739 1.00 75.44  ? 241 PRO A CD   1 
ATOM   1885 N N    . LEU A 1 242 ? -15.443 28.698  -49.027 1.00 72.43  ? 242 LEU A N    1 
ATOM   1886 C CA   . LEU A 1 242 ? -16.633 27.934  -48.671 1.00 70.93  ? 242 LEU A CA   1 
ATOM   1887 C C    . LEU A 1 242 ? -17.494 27.722  -49.917 1.00 71.17  ? 242 LEU A C    1 
ATOM   1888 O O    . LEU A 1 242 ? -17.958 28.689  -50.545 1.00 72.05  ? 242 LEU A O    1 
ATOM   1889 C CB   . LEU A 1 242 ? -17.444 28.677  -47.603 1.00 65.53  ? 242 LEU A CB   1 
ATOM   1890 C CG   . LEU A 1 242 ? -18.199 27.935  -46.482 1.00 60.83  ? 242 LEU A CG   1 
ATOM   1891 C CD1  . LEU A 1 242 ? -18.758 28.942  -45.530 1.00 68.20  ? 242 LEU A CD1  1 
ATOM   1892 C CD2  . LEU A 1 242 ? -19.322 27.017  -46.958 1.00 64.61  ? 242 LEU A CD2  1 
ATOM   1893 N N    . THR A 1 243 ? -17.689 26.460  -50.277 1.00 67.26  ? 243 THR A N    1 
ATOM   1894 C CA   . THR A 1 243 ? -18.541 26.051  -51.380 1.00 68.57  ? 243 THR A CA   1 
ATOM   1895 C C    . THR A 1 243 ? -19.912 25.606  -50.885 1.00 69.10  ? 243 THR A C    1 
ATOM   1896 O O    . THR A 1 243 ? -20.115 25.317  -49.703 1.00 67.66  ? 243 THR A O    1 
ATOM   1897 C CB   . THR A 1 243 ? -17.903 24.907  -52.163 1.00 66.51  ? 243 THR A CB   1 
ATOM   1898 O OG1  . THR A 1 243 ? -18.264 23.669  -51.545 1.00 69.16  ? 243 THR A OG1  1 
ATOM   1899 C CG2  . THR A 1 243 ? -16.396 25.043  -52.170 1.00 69.95  ? 243 THR A CG2  1 
ATOM   1900 N N    . GLN A 1 244 ? -20.862 25.558  -51.829 1.00 73.92  ? 244 GLN A N    1 
ATOM   1901 C CA   . GLN A 1 244 ? -22.215 25.082  -51.542 1.00 71.72  ? 244 GLN A CA   1 
ATOM   1902 C C    . GLN A 1 244 ? -22.208 23.619  -51.138 1.00 67.69  ? 244 GLN A C    1 
ATOM   1903 O O    . GLN A 1 244 ? -23.077 23.170  -50.376 1.00 68.15  ? 244 GLN A O    1 
ATOM   1904 C CB   . GLN A 1 244 ? -23.130 25.294  -52.758 1.00 74.05  ? 244 GLN A CB   1 
ATOM   1905 C CG   . GLN A 1 244 ? -24.405 24.430  -52.775 1.00 73.17  ? 244 GLN A CG   1 
ATOM   1906 C CD   . GLN A 1 244 ? -25.210 24.480  -51.466 1.00 73.00  ? 244 GLN A CD   1 
ATOM   1907 O OE1  . GLN A 1 244 ? -25.702 25.538  -51.050 1.00 67.38  ? 244 GLN A OE1  1 
ATOM   1908 N NE2  . GLN A 1 244 ? -25.370 23.314  -50.833 1.00 69.86  ? 244 GLN A NE2  1 
ATOM   1909 N N    . ASP A 1 245 ? -21.237 22.857  -51.626 1.00 68.33  ? 245 ASP A N    1 
ATOM   1910 C CA   . ASP A 1 245 ? -21.090 21.505  -51.117 1.00 67.43  ? 245 ASP A CA   1 
ATOM   1911 C C    . ASP A 1 245 ? -20.791 21.522  -49.622 1.00 67.40  ? 245 ASP A C    1 
ATOM   1912 O O    . ASP A 1 245 ? -21.253 20.649  -48.879 1.00 68.51  ? 245 ASP A O    1 
ATOM   1913 C CB   . ASP A 1 245 ? -19.979 20.796  -51.868 1.00 69.58  ? 245 ASP A CB   1 
ATOM   1914 C CG   . ASP A 1 245 ? -20.374 19.416  -52.285 1.00 77.95  ? 245 ASP A CG   1 
ATOM   1915 O OD1  . ASP A 1 245 ? -20.787 18.623  -51.411 1.00 80.64  ? 245 ASP A OD1  1 
ATOM   1916 O OD2  . ASP A 1 245 ? -20.266 19.124  -53.490 1.00 84.09  ? 245 ASP A OD2  1 
ATOM   1917 N N    . HIS A 1 246 ? -20.019 22.517  -49.166 1.00 67.25  ? 246 HIS A N    1 
ATOM   1918 C CA   . HIS A 1 246 ? -19.728 22.665  -47.740 1.00 66.78  ? 246 HIS A CA   1 
ATOM   1919 C C    . HIS A 1 246 ? -20.979 23.026  -46.942 1.00 64.48  ? 246 HIS A C    1 
ATOM   1920 O O    . HIS A 1 246 ? -21.206 22.470  -45.860 1.00 60.60  ? 246 HIS A O    1 
ATOM   1921 C CB   . HIS A 1 246 ? -18.645 23.730  -47.527 1.00 62.76  ? 246 HIS A CB   1 
ATOM   1922 C CG   . HIS A 1 246 ? -17.285 23.319  -48.011 1.00 62.72  ? 246 HIS A CG   1 
ATOM   1923 N ND1  . HIS A 1 246 ? -16.373 24.222  -48.524 1.00 63.43  ? 246 HIS A ND1  1 
ATOM   1924 C CD2  . HIS A 1 246 ? -16.697 22.100  -48.101 1.00 57.27  ? 246 HIS A CD2  1 
ATOM   1925 C CE1  . HIS A 1 246 ? -15.271 23.580  -48.876 1.00 59.67  ? 246 HIS A CE1  1 
ATOM   1926 N NE2  . HIS A 1 246 ? -15.442 22.291  -48.629 1.00 55.43  ? 246 HIS A NE2  1 
ATOM   1927 N N    . VAL A 1 247 ? -21.820 23.935  -47.467 1.00 65.49  ? 247 VAL A N    1 
ATOM   1928 C CA   . VAL A 1 247 ? -23.073 24.263  -46.779 1.00 61.52  ? 247 VAL A CA   1 
ATOM   1929 C C    . VAL A 1 247 ? -23.898 23.010  -46.519 1.00 62.82  ? 247 VAL A C    1 
ATOM   1930 O O    . VAL A 1 247 ? -24.416 22.804  -45.416 1.00 62.58  ? 247 VAL A O    1 
ATOM   1931 C CB   . VAL A 1 247 ? -23.863 25.316  -47.571 1.00 66.09  ? 247 VAL A CB   1 
ATOM   1932 C CG1  . VAL A 1 247 ? -25.102 25.732  -46.805 1.00 66.80  ? 247 VAL A CG1  1 
ATOM   1933 C CG2  . VAL A 1 247 ? -22.987 26.533  -47.826 1.00 66.09  ? 247 VAL A CG2  1 
ATOM   1934 N N    . ASP A 1 248 ? -24.003 22.131  -47.512 1.00 64.37  ? 248 ASP A N    1 
ATOM   1935 C CA   . ASP A 1 248 ? -24.845 20.947  -47.354 1.00 64.13  ? 248 ASP A CA   1 
ATOM   1936 C C    . ASP A 1 248 ? -24.249 19.927  -46.386 1.00 64.24  ? 248 ASP A C    1 
ATOM   1937 O O    . ASP A 1 248 ? -24.990 19.192  -45.712 1.00 60.38  ? 248 ASP A O    1 
ATOM   1938 C CB   . ASP A 1 248 ? -25.123 20.329  -48.720 1.00 70.76  ? 248 ASP A CB   1 
ATOM   1939 C CG   . ASP A 1 248 ? -26.555 20.637  -49.216 1.00 70.01  ? 248 ASP A CG   1 
ATOM   1940 O OD1  . ASP A 1 248 ? -27.310 21.387  -48.523 1.00 65.93  ? 248 ASP A OD1  1 
ATOM   1941 O OD2  . ASP A 1 248 ? -26.915 20.122  -50.293 1.00 66.20  ? 248 ASP A OD2  1 
ATOM   1942 N N    . ILE A 1 249 ? -22.922 19.836  -46.324 1.00 63.66  ? 249 ILE A N    1 
ATOM   1943 C CA   . ILE A 1 249 ? -22.290 18.993  -45.313 1.00 65.13  ? 249 ILE A CA   1 
ATOM   1944 C C    . ILE A 1 249 ? -22.572 19.555  -43.917 1.00 61.87  ? 249 ILE A C    1 
ATOM   1945 O O    . ILE A 1 249 ? -22.999 18.829  -43.009 1.00 58.45  ? 249 ILE A O    1 
ATOM   1946 C CB   . ILE A 1 249 ? -20.785 18.868  -45.612 1.00 63.72  ? 249 ILE A CB   1 
ATOM   1947 C CG1  . ILE A 1 249 ? -20.188 17.634  -44.964 1.00 66.01  ? 249 ILE A CG1  1 
ATOM   1948 C CG2  . ILE A 1 249 ? -20.032 20.103  -45.197 1.00 63.18  ? 249 ILE A CG2  1 
ATOM   1949 C CD1  . ILE A 1 249 ? -19.214 16.933  -45.910 1.00 69.94  ? 249 ILE A CD1  1 
ATOM   1950 N N    . LEU A 1 250 ? -22.371 20.865  -43.741 1.00 58.54  ? 250 LEU A N    1 
ATOM   1951 C CA   . LEU A 1 250 ? -22.657 21.563  -42.494 1.00 61.42  ? 250 LEU A CA   1 
ATOM   1952 C C    . LEU A 1 250 ? -24.143 21.538  -42.165 1.00 63.06  ? 250 LEU A C    1 
ATOM   1953 O O    . LEU A 1 250 ? -24.568 22.155  -41.180 1.00 62.18  ? 250 LEU A O    1 
ATOM   1954 C CB   . LEU A 1 250 ? -22.206 23.021  -42.550 1.00 58.48  ? 250 LEU A CB   1 
ATOM   1955 C CG   . LEU A 1 250 ? -20.721 23.340  -42.450 1.00 56.20  ? 250 LEU A CG   1 
ATOM   1956 C CD1  . LEU A 1 250 ? -20.521 24.802  -42.819 1.00 53.41  ? 250 LEU A CD1  1 
ATOM   1957 C CD2  . LEU A 1 250 ? -20.173 23.023  -41.067 1.00 50.20  ? 250 LEU A CD2  1 
ATOM   1958 N N    . GLY A 1 251 ? -24.946 20.862  -42.985 1.00 70.90  ? 251 GLY A N    1 
ATOM   1959 C CA   . GLY A 1 251 ? -26.379 21.015  -42.907 1.00 66.53  ? 251 GLY A CA   1 
ATOM   1960 C C    . GLY A 1 251 ? -27.057 20.499  -41.657 1.00 64.39  ? 251 GLY A C    1 
ATOM   1961 O O    . GLY A 1 251 ? -27.886 21.198  -41.061 1.00 65.67  ? 251 GLY A O    1 
ATOM   1962 N N    . PRO A 1 252 ? -26.740 19.270  -41.235 1.00 60.24  ? 252 PRO A N    1 
ATOM   1963 C CA   . PRO A 1 252 ? -27.370 18.743  -40.010 1.00 58.36  ? 252 PRO A CA   1 
ATOM   1964 C C    . PRO A 1 252 ? -26.965 19.505  -38.754 1.00 60.02  ? 252 PRO A C    1 
ATOM   1965 O O    . PRO A 1 252 ? -27.749 19.570  -37.800 1.00 59.83  ? 252 PRO A O    1 
ATOM   1966 C CB   . PRO A 1 252 ? -26.907 17.277  -39.970 1.00 59.50  ? 252 PRO A CB   1 
ATOM   1967 C CG   . PRO A 1 252 ? -26.515 16.958  -41.358 1.00 58.61  ? 252 PRO A CG   1 
ATOM   1968 C CD   . PRO A 1 252 ? -25.968 18.237  -41.944 1.00 61.47  ? 252 PRO A CD   1 
ATOM   1969 N N    . LEU A 1 253 ? -25.753 20.068  -38.716 1.00 59.90  ? 253 LEU A N    1 
ATOM   1970 C CA   . LEU A 1 253 ? -25.341 20.883  -37.575 1.00 57.30  ? 253 LEU A CA   1 
ATOM   1971 C C    . LEU A 1 253 ? -26.063 22.222  -37.585 1.00 57.98  ? 253 LEU A C    1 
ATOM   1972 O O    . LEU A 1 253 ? -26.565 22.684  -36.550 1.00 54.77  ? 253 LEU A O    1 
ATOM   1973 C CB   . LEU A 1 253 ? -23.827 21.109  -37.624 1.00 52.84  ? 253 LEU A CB   1 
ATOM   1974 C CG   . LEU A 1 253 ? -22.820 20.030  -37.188 1.00 50.58  ? 253 LEU A CG   1 
ATOM   1975 C CD1  . LEU A 1 253 ? -21.426 20.525  -37.440 1.00 44.51  ? 253 LEU A CD1  1 
ATOM   1976 C CD2  . LEU A 1 253 ? -22.988 19.669  -35.711 1.00 49.34  ? 253 LEU A CD2  1 
ATOM   1977 N N    . SER A 1 254 ? -26.083 22.880  -38.750 1.00 58.65  ? 254 SER A N    1 
ATOM   1978 C CA   . SER A 1 254 ? -26.914 24.063  -38.940 1.00 58.62  ? 254 SER A CA   1 
ATOM   1979 C C    . SER A 1 254 ? -28.353 23.779  -38.552 1.00 57.49  ? 254 SER A C    1 
ATOM   1980 O O    . SER A 1 254 ? -29.047 24.663  -38.035 1.00 58.11  ? 254 SER A O    1 
ATOM   1981 C CB   . SER A 1 254 ? -26.846 24.514  -40.410 1.00 59.79  ? 254 SER A CB   1 
ATOM   1982 O OG   . SER A 1 254 ? -27.769 25.553  -40.680 1.00 60.52  ? 254 SER A OG   1 
ATOM   1983 N N    . ALA A 1 255 ? -28.797 22.538  -38.756 1.00 56.32  ? 255 ALA A N    1 
ATOM   1984 C CA   . ALA A 1 255 ? -30.179 22.164  -38.496 1.00 56.66  ? 255 ALA A CA   1 
ATOM   1985 C C    . ALA A 1 255 ? -30.416 21.889  -37.030 1.00 58.68  ? 255 ALA A C    1 
ATOM   1986 O O    . ALA A 1 255 ? -31.351 22.438  -36.437 1.00 60.67  ? 255 ALA A O    1 
ATOM   1987 C CB   . ALA A 1 255 ? -30.542 20.933  -39.318 1.00 60.25  ? 255 ALA A CB   1 
ATOM   1988 N N    . GLN A 1 256 ? -29.556 21.054  -36.430 1.00 58.91  ? 256 GLN A N    1 
ATOM   1989 C CA   . GLN A 1 256 ? -29.650 20.752  -35.001 1.00 58.80  ? 256 GLN A CA   1 
ATOM   1990 C C    . GLN A 1 256 ? -29.662 22.014  -34.167 1.00 54.34  ? 256 GLN A C    1 
ATOM   1991 O O    . GLN A 1 256 ? -30.456 22.147  -33.228 1.00 58.79  ? 256 GLN A O    1 
ATOM   1992 C CB   . GLN A 1 256 ? -28.477 19.877  -34.580 1.00 64.50  ? 256 GLN A CB   1 
ATOM   1993 C CG   . GLN A 1 256 ? -28.792 18.966  -33.422 1.00 68.40  ? 256 GLN A CG   1 
ATOM   1994 C CD   . GLN A 1 256 ? -27.542 18.352  -32.806 1.00 77.17  ? 256 GLN A CD   1 
ATOM   1995 O OE1  . GLN A 1 256 ? -26.626 17.908  -33.526 1.00 77.46  ? 256 GLN A OE1  1 
ATOM   1996 N NE2  . GLN A 1 256 ? -27.549 18.221  -31.469 1.00 78.27  ? 256 GLN A NE2  1 
ATOM   1997 N N    . THR A 1 257 ? -28.770 22.952  -34.485 1.00 55.81  ? 257 THR A N    1 
ATOM   1998 C CA   . THR A 1 257 ? -28.649 24.180  -33.715 1.00 56.99  ? 257 THR A CA   1 
ATOM   1999 C C    . THR A 1 257 ? -29.645 25.246  -34.133 1.00 57.77  ? 257 THR A C    1 
ATOM   2000 O O    . THR A 1 257 ? -29.688 26.292  -33.491 1.00 54.06  ? 257 THR A O    1 
ATOM   2001 C CB   . THR A 1 257 ? -27.237 24.777  -33.838 1.00 57.31  ? 257 THR A CB   1 
ATOM   2002 O OG1  . THR A 1 257 ? -26.925 25.059  -35.215 1.00 54.52  ? 257 THR A OG1  1 
ATOM   2003 C CG2  . THR A 1 257 ? -26.176 23.830  -33.253 1.00 57.92  ? 257 THR A CG2  1 
ATOM   2004 N N    . GLY A 1 258 ? -30.423 25.041  -35.193 1.00 56.61  ? 258 GLY A N    1 
ATOM   2005 C CA   . GLY A 1 258 ? -31.325 26.115  -35.558 1.00 58.83  ? 258 GLY A CA   1 
ATOM   2006 C C    . GLY A 1 258 ? -30.654 27.373  -36.064 1.00 60.91  ? 258 GLY A C    1 
ATOM   2007 O O    . GLY A 1 258 ? -31.241 28.454  -35.964 1.00 59.05  ? 258 GLY A O    1 
ATOM   2008 N N    . ILE A 1 259 ? -29.422 27.285  -36.567 1.00 61.18  ? 259 ILE A N    1 
ATOM   2009 C CA   . ILE A 1 259 ? -28.674 28.471  -36.983 1.00 61.46  ? 259 ILE A CA   1 
ATOM   2010 C C    . ILE A 1 259 ? -28.226 28.276  -38.422 1.00 58.68  ? 259 ILE A C    1 
ATOM   2011 O O    . ILE A 1 259 ? -27.438 27.368  -38.709 1.00 57.22  ? 259 ILE A O    1 
ATOM   2012 C CB   . ILE A 1 259 ? -27.467 28.748  -36.079 1.00 58.63  ? 259 ILE A CB   1 
ATOM   2013 C CG1  . ILE A 1 259 ? -27.940 29.204  -34.711 1.00 56.37  ? 259 ILE A CG1  1 
ATOM   2014 C CG2  . ILE A 1 259 ? -26.579 29.827  -36.696 1.00 58.23  ? 259 ILE A CG2  1 
ATOM   2015 C CD1  . ILE A 1 259 ? -26.838 29.196  -33.692 1.00 61.87  ? 259 ILE A CD1  1 
ATOM   2016 N N    . ALA A 1 260 ? -28.715 29.125  -39.325 1.00 60.13  ? 260 ALA A N    1 
ATOM   2017 C CA   . ALA A 1 260 ? -28.411 28.938  -40.743 1.00 63.10  ? 260 ALA A CA   1 
ATOM   2018 C C    . ALA A 1 260 ? -26.922 29.132  -41.026 1.00 59.71  ? 260 ALA A C    1 
ATOM   2019 O O    . ALA A 1 260 ? -26.280 30.057  -40.508 1.00 62.50  ? 260 ALA A O    1 
ATOM   2020 C CB   . ALA A 1 260 ? -29.226 29.903  -41.599 1.00 62.87  ? 260 ALA A CB   1 
ATOM   2021 N N    . VAL A 1 261 ? -26.382 28.259  -41.866 1.00 59.38  ? 261 VAL A N    1 
ATOM   2022 C CA   . VAL A 1 261 ? -24.985 28.318  -42.281 1.00 58.53  ? 261 VAL A CA   1 
ATOM   2023 C C    . VAL A 1 261 ? -24.575 29.754  -42.587 1.00 65.00  ? 261 VAL A C    1 
ATOM   2024 O O    . VAL A 1 261 ? -23.550 30.243  -42.086 1.00 61.14  ? 261 VAL A O    1 
ATOM   2025 C CB   . VAL A 1 261 ? -24.767 27.426  -43.504 1.00 56.95  ? 261 VAL A CB   1 
ATOM   2026 C CG1  . VAL A 1 261 ? -23.272 27.248  -43.769 1.00 63.82  ? 261 VAL A CG1  1 
ATOM   2027 C CG2  . VAL A 1 261 ? -25.448 26.074  -43.307 1.00 58.74  ? 261 VAL A CG2  1 
ATOM   2028 N N    . LEU A 1 262 ? -25.408 30.448  -43.374 1.00 61.88  ? 262 LEU A N    1 
ATOM   2029 C CA   . LEU A 1 262 ? -25.134 31.832  -43.744 1.00 63.77  ? 262 LEU A CA   1 
ATOM   2030 C C    . LEU A 1 262 ? -25.029 32.715  -42.513 1.00 62.45  ? 262 LEU A C    1 
ATOM   2031 O O    . LEU A 1 262 ? -24.154 33.586  -42.431 1.00 62.48  ? 262 LEU A O    1 
ATOM   2032 C CB   . LEU A 1 262 ? -26.237 32.356  -44.673 1.00 68.38  ? 262 LEU A CB   1 
ATOM   2033 C CG   . LEU A 1 262 ? -26.422 31.688  -46.035 1.00 69.00  ? 262 LEU A CG   1 
ATOM   2034 C CD1  . LEU A 1 262 ? -25.154 31.817  -46.844 1.00 73.13  ? 262 LEU A CD1  1 
ATOM   2035 C CD2  . LEU A 1 262 ? -26.795 30.208  -45.868 1.00 65.19  ? 262 LEU A CD2  1 
ATOM   2036 N N    . ASP A 1 263 ? -25.931 32.528  -41.556 1.00 62.41  ? 263 ASP A N    1 
ATOM   2037 C CA   . ASP A 1 263 ? -25.883 33.337  -40.348 1.00 65.65  ? 263 ASP A CA   1 
ATOM   2038 C C    . ASP A 1 263 ? -24.580 33.083  -39.593 1.00 64.02  ? 263 ASP A C    1 
ATOM   2039 O O    . ASP A 1 263 ? -23.877 34.028  -39.201 1.00 60.29  ? 263 ASP A O    1 
ATOM   2040 C CB   . ASP A 1 263 ? -27.102 33.032  -39.481 1.00 67.64  ? 263 ASP A CB   1 
ATOM   2041 C CG   . ASP A 1 263 ? -28.376 33.617  -40.054 1.00 71.93  ? 263 ASP A CG   1 
ATOM   2042 O OD1  . ASP A 1 263 ? -28.325 34.163  -41.185 1.00 72.23  ? 263 ASP A OD1  1 
ATOM   2043 O OD2  . ASP A 1 263 ? -29.421 33.533  -39.368 1.00 72.52  ? 263 ASP A OD2  1 
ATOM   2044 N N    . MET A 1 264 ? -24.223 31.805  -39.413 1.00 63.25  ? 264 MET A N    1 
ATOM   2045 C CA   . MET A 1 264 ? -22.939 31.475  -38.791 1.00 60.25  ? 264 MET A CA   1 
ATOM   2046 C C    . MET A 1 264 ? -21.770 32.112  -39.514 1.00 60.26  ? 264 MET A C    1 
ATOM   2047 O O    . MET A 1 264 ? -20.877 32.670  -38.869 1.00 60.15  ? 264 MET A O    1 
ATOM   2048 C CB   . MET A 1 264 ? -22.771 29.957  -38.702 1.00 58.32  ? 264 MET A CB   1 
ATOM   2049 C CG   . MET A 1 264 ? -21.651 29.562  -37.761 1.00 59.08  ? 264 MET A CG   1 
ATOM   2050 S SD   . MET A 1 264 ? -22.132 29.862  -36.070 1.00 58.99  ? 264 MET A SD   1 
ATOM   2051 C CE   . MET A 1 264 ? -22.751 28.246  -35.572 1.00 55.71  ? 264 MET A CE   1 
ATOM   2052 N N    . CYS A 1 265 ? -21.794 32.110  -40.847 1.00 60.07  ? 265 CYS A N    1 
ATOM   2053 C CA   . CYS A 1 265 ? -20.715 32.744  -41.596 1.00 62.69  ? 265 CYS A CA   1 
ATOM   2054 C C    . CYS A 1 265 ? -20.535 34.203  -41.201 1.00 63.25  ? 265 CYS A C    1 
ATOM   2055 O O    . CYS A 1 265 ? -19.401 34.705  -41.160 1.00 62.07  ? 265 CYS A O    1 
ATOM   2056 C CB   . CYS A 1 265 ? -20.993 32.658  -43.087 1.00 62.75  ? 265 CYS A CB   1 
ATOM   2057 S SG   . CYS A 1 265 ? -20.704 31.061  -43.748 1.00 61.66  ? 265 CYS A SG   1 
ATOM   2058 N N    . ALA A 1 266 ? -21.643 34.911  -40.947 1.00 64.65  ? 266 ALA A N    1 
ATOM   2059 C CA   . ALA A 1 266 ? -21.547 36.318  -40.586 1.00 63.23  ? 266 ALA A CA   1 
ATOM   2060 C C    . ALA A 1 266 ? -20.905 36.488  -39.213 1.00 65.93  ? 266 ALA A C    1 
ATOM   2061 O O    . ALA A 1 266 ? -20.067 37.382  -39.026 1.00 62.64  ? 266 ALA A O    1 
ATOM   2062 C CB   . ALA A 1 266 ? -22.930 36.970  -40.647 1.00 68.61  ? 266 ALA A CB   1 
ATOM   2063 N N    . SER A 1 267 ? -21.269 35.623  -38.247 1.00 64.74  ? 267 SER A N    1 
ATOM   2064 C CA   . SER A 1 267 ? -20.595 35.610  -36.947 1.00 66.81  ? 267 SER A CA   1 
ATOM   2065 C C    . SER A 1 267 ? -19.110 35.305  -37.107 1.00 61.24  ? 267 SER A C    1 
ATOM   2066 O O    . SER A 1 267 ? -18.257 35.935  -36.465 1.00 61.41  ? 267 SER A O    1 
ATOM   2067 C CB   . SER A 1 267 ? -21.252 34.597  -36.008 1.00 66.40  ? 267 SER A CB   1 
ATOM   2068 O OG   . SER A 1 267 ? -22.637 34.840  -35.889 1.00 64.50  ? 267 SER A OG   1 
ATOM   2069 N N    . LEU A 1 268 ? -18.785 34.339  -37.951 1.00 58.92  ? 268 LEU A N    1 
ATOM   2070 C CA   . LEU A 1 268 ? -17.385 34.096  -38.255 1.00 62.23  ? 268 LEU A CA   1 
ATOM   2071 C C    . LEU A 1 268 ? -16.721 35.360  -38.799 1.00 67.54  ? 268 LEU A C    1 
ATOM   2072 O O    . LEU A 1 268 ? -15.626 35.732  -38.360 1.00 68.87  ? 268 LEU A O    1 
ATOM   2073 C CB   . LEU A 1 268 ? -17.281 32.959  -39.261 1.00 57.76  ? 268 LEU A CB   1 
ATOM   2074 C CG   . LEU A 1 268 ? -15.891 32.456  -39.601 1.00 57.35  ? 268 LEU A CG   1 
ATOM   2075 C CD1  . LEU A 1 268 ? -15.055 32.384  -38.345 1.00 56.52  ? 268 LEU A CD1  1 
ATOM   2076 C CD2  . LEU A 1 268 ? -15.982 31.133  -40.262 1.00 54.40  ? 268 LEU A CD2  1 
ATOM   2077 N N    . LYS A 1 269 ? -17.409 36.080  -39.695 1.00 68.07  ? 269 LYS A N    1 
ATOM   2078 C CA   . LYS A 1 269 ? -16.852 37.305  -40.274 1.00 66.93  ? 269 LYS A CA   1 
ATOM   2079 C C    . LYS A 1 269 ? -16.389 38.264  -39.192 1.00 66.64  ? 269 LYS A C    1 
ATOM   2080 O O    . LYS A 1 269 ? -15.269 38.787  -39.233 1.00 69.07  ? 269 LYS A O    1 
ATOM   2081 C CB   . LYS A 1 269 ? -17.879 37.993  -41.178 1.00 69.79  ? 269 LYS A CB   1 
ATOM   2082 C CG   . LYS A 1 269 ? -17.271 38.795  -42.311 1.00 78.69  ? 269 LYS A CG   1 
ATOM   2083 C CD   . LYS A 1 269 ? -18.227 39.880  -42.816 1.00 81.25  ? 269 LYS A CD   1 
ATOM   2084 C CE   . LYS A 1 269 ? -19.181 39.341  -43.889 1.00 87.12  ? 269 LYS A CE   1 
ATOM   2085 N NZ   . LYS A 1 269 ? -20.012 40.454  -44.462 1.00 86.89  ? 269 LYS A NZ   1 
ATOM   2086 N N    . GLU A 1 270 ? -17.271 38.557  -38.243 1.00 65.86  ? 270 GLU A N    1 
ATOM   2087 C CA   . GLU A 1 270 ? -16.919 39.495  -37.197 1.00 69.28  ? 270 GLU A CA   1 
ATOM   2088 C C    . GLU A 1 270 ? -15.761 38.973  -36.359 1.00 72.70  ? 270 GLU A C    1 
ATOM   2089 O O    . GLU A 1 270 ? -14.881 39.744  -35.949 1.00 73.65  ? 270 GLU A O    1 
ATOM   2090 C CB   . GLU A 1 270 ? -18.141 39.758  -36.327 1.00 72.92  ? 270 GLU A CB   1 
ATOM   2091 C CG   . GLU A 1 270 ? -17.943 40.860  -35.321 1.00 76.04  ? 270 GLU A CG   1 
ATOM   2092 C CD   . GLU A 1 270 ? -19.143 40.997  -34.423 1.00 85.02  ? 270 GLU A CD   1 
ATOM   2093 O OE1  . GLU A 1 270 ? -20.186 40.417  -34.797 1.00 94.27  ? 270 GLU A OE1  1 
ATOM   2094 O OE2  . GLU A 1 270 ? -19.049 41.669  -33.364 1.00 84.47  ? 270 GLU A OE2  1 
ATOM   2095 N N    . LEU A 1 271 ? -15.762 37.670  -36.063 1.00 68.80  ? 271 LEU A N    1 
ATOM   2096 C CA   . LEU A 1 271 ? -14.641 37.078  -35.340 1.00 68.19  ? 271 LEU A CA   1 
ATOM   2097 C C    . LEU A 1 271 ? -13.334 37.308  -36.088 1.00 67.91  ? 271 LEU A C    1 
ATOM   2098 O O    . LEU A 1 271 ? -12.310 37.648  -35.483 1.00 69.31  ? 271 LEU A O    1 
ATOM   2099 C CB   . LEU A 1 271 ? -14.889 35.578  -35.133 1.00 64.24  ? 271 LEU A CB   1 
ATOM   2100 C CG   . LEU A 1 271 ? -15.869 35.188  -34.004 1.00 62.45  ? 271 LEU A CG   1 
ATOM   2101 C CD1  . LEU A 1 271 ? -16.113 33.663  -33.979 1.00 60.03  ? 271 LEU A CD1  1 
ATOM   2102 C CD2  . LEU A 1 271 ? -15.400 35.671  -32.650 1.00 63.83  ? 271 LEU A CD2  1 
ATOM   2103 N N    . LEU A 1 272 ? -13.371 37.189  -37.417 1.00 65.91  ? 272 LEU A N    1 
ATOM   2104 C CA   . LEU A 1 272 ? -12.168 37.374  -38.224 1.00 70.33  ? 272 LEU A CA   1 
ATOM   2105 C C    . LEU A 1 272 ? -11.759 38.846  -38.303 1.00 73.19  ? 272 LEU A C    1 
ATOM   2106 O O    . LEU A 1 272 ? -10.562 39.159  -38.327 1.00 74.81  ? 272 LEU A O    1 
ATOM   2107 C CB   . LEU A 1 272 ? -12.385 36.796  -39.627 1.00 70.99  ? 272 LEU A CB   1 
ATOM   2108 C CG   . LEU A 1 272 ? -12.534 35.269  -39.779 1.00 69.11  ? 272 LEU A CG   1 
ATOM   2109 C CD1  . LEU A 1 272 ? -13.899 34.890  -40.336 1.00 66.66  ? 272 LEU A CD1  1 
ATOM   2110 C CD2  . LEU A 1 272 ? -11.465 34.679  -40.666 1.00 63.39  ? 272 LEU A CD2  1 
ATOM   2111 N N    . GLN A 1 273 ? -12.734 39.765  -38.375 1.00 72.90  ? 273 GLN A N    1 
ATOM   2112 C CA   . GLN A 1 273 ? -12.426 41.192  -38.475 1.00 75.08  ? 273 GLN A CA   1 
ATOM   2113 C C    . GLN A 1 273 ? -12.138 41.811  -37.126 1.00 76.80  ? 273 GLN A C    1 
ATOM   2114 O O    . GLN A 1 273 ? -11.463 42.841  -37.057 1.00 80.79  ? 273 GLN A O    1 
ATOM   2115 C CB   . GLN A 1 273 ? -13.579 41.954  -39.135 1.00 73.89  ? 273 GLN A CB   1 
ATOM   2116 C CG   . GLN A 1 273 ? -14.074 41.310  -40.426 1.00 77.33  ? 273 GLN A CG   1 
ATOM   2117 C CD   . GLN A 1 273 ? -15.072 42.170  -41.201 1.00 76.74  ? 273 GLN A CD   1 
ATOM   2118 O OE1  . GLN A 1 273 ? -15.763 41.670  -42.094 1.00 74.28  ? 273 GLN A OE1  1 
ATOM   2119 N NE2  . GLN A 1 273 ? -15.173 43.452  -40.844 1.00 71.71  ? 273 GLN A NE2  1 
ATOM   2120 N N    . ASN A 1 274 ? -12.601 41.185  -36.056 1.00 74.62  ? 274 ASN A N    1 
ATOM   2121 C CA   . ASN A 1 274 ? -12.659 41.796  -34.744 1.00 75.02  ? 274 ASN A CA   1 
ATOM   2122 C C    . ASN A 1 274 ? -11.917 40.988  -33.689 1.00 77.09  ? 274 ASN A C    1 
ATOM   2123 O O    . ASN A 1 274 ? -11.895 41.393  -32.521 1.00 75.95  ? 274 ASN A O    1 
ATOM   2124 C CB   . ASN A 1 274 ? -14.129 41.982  -34.338 1.00 80.72  ? 274 ASN A CB   1 
ATOM   2125 C CG   . ASN A 1 274 ? -14.860 43.001  -35.213 1.00 82.75  ? 274 ASN A CG   1 
ATOM   2126 O OD1  . ASN A 1 274 ? -15.906 42.702  -35.793 1.00 83.44  ? 274 ASN A OD1  1 
ATOM   2127 N ND2  . ASN A 1 274 ? -14.366 44.239  -35.219 1.00 82.71  ? 274 ASN A ND2  1 
ATOM   2128 N N    . GLY A 1 275 ? -11.287 39.873  -34.065 1.00 74.92  ? 275 GLY A N    1 
ATOM   2129 C CA   . GLY A 1 275 ? -10.637 39.142  -33.008 1.00 76.18  ? 275 GLY A CA   1 
ATOM   2130 C C    . GLY A 1 275 ? -11.640 38.616  -31.988 1.00 72.37  ? 275 GLY A C    1 
ATOM   2131 O O    . GLY A 1 275 ? -12.850 38.617  -32.178 1.00 69.75  ? 275 GLY A O    1 
ATOM   2132 N N    . MET A 1 276 ? -11.088 38.136  -30.887 1.00 74.23  ? 276 MET A N    1 
ATOM   2133 C CA   . MET A 1 276 ? -11.880 37.481  -29.865 1.00 74.65  ? 276 MET A CA   1 
ATOM   2134 C C    . MET A 1 276 ? -11.998 38.287  -28.582 1.00 77.47  ? 276 MET A C    1 
ATOM   2135 O O    . MET A 1 276 ? -12.726 37.880  -27.668 1.00 78.16  ? 276 MET A O    1 
ATOM   2136 C CB   . MET A 1 276 ? -11.293 36.100  -29.591 1.00 71.32  ? 276 MET A CB   1 
ATOM   2137 C CG   . MET A 1 276 ? -12.115 35.011  -30.218 1.00 71.25  ? 276 MET A CG   1 
ATOM   2138 S SD   . MET A 1 276 ? -11.563 33.402  -29.677 1.00 65.56  ? 276 MET A SD   1 
ATOM   2139 C CE   . MET A 1 276 ? -11.496 32.502  -31.232 1.00 50.64  ? 276 MET A CE   1 
ATOM   2140 N N    . ASN A 1 277 ? -11.345 39.436  -28.499 1.00 78.36  ? 277 ASN A N    1 
ATOM   2141 C CA   . ASN A 1 277 ? -11.513 40.321  -27.359 1.00 83.71  ? 277 ASN A CA   1 
ATOM   2142 C C    . ASN A 1 277 ? -10.962 39.726  -26.076 1.00 83.24  ? 277 ASN A C    1 
ATOM   2143 O O    . ASN A 1 277 ? -11.438 40.067  -24.992 1.00 86.79  ? 277 ASN A O    1 
ATOM   2144 C CB   . ASN A 1 277 ? -12.985 40.679  -27.153 1.00 87.52  ? 277 ASN A CB   1 
ATOM   2145 C CG   . ASN A 1 277 ? -13.395 41.887  -27.926 1.00 94.37  ? 277 ASN A CG   1 
ATOM   2146 O OD1  . ASN A 1 277 ? -12.634 42.393  -28.748 1.00 98.37  ? 277 ASN A OD1  1 
ATOM   2147 N ND2  . ASN A 1 277 ? -14.594 42.389  -27.647 1.00 98.88  ? 277 ASN A ND2  1 
ATOM   2148 N N    . GLY A 1 278 ? -9.979  38.832  -26.169 1.00 80.63  ? 278 GLY A N    1 
ATOM   2149 C CA   . GLY A 1 278 ? -9.513  38.161  -24.969 1.00 79.84  ? 278 GLY A CA   1 
ATOM   2150 C C    . GLY A 1 278 ? -10.518 37.203  -24.378 1.00 73.90  ? 278 GLY A C    1 
ATOM   2151 O O    . GLY A 1 278 ? -10.452 36.890  -23.188 1.00 73.17  ? 278 GLY A O    1 
ATOM   2152 N N    . ARG A 1 279 ? -11.464 36.751  -25.182 1.00 72.07  ? 279 ARG A N    1 
ATOM   2153 C CA   . ARG A 1 279 ? -12.478 35.794  -24.787 1.00 71.58  ? 279 ARG A CA   1 
ATOM   2154 C C    . ARG A 1 279 ? -12.071 34.434  -25.342 1.00 66.23  ? 279 ARG A C    1 
ATOM   2155 O O    . ARG A 1 279 ? -11.036 34.302  -25.997 1.00 66.98  ? 279 ARG A O    1 
ATOM   2156 C CB   . ARG A 1 279 ? -13.846 36.253  -25.294 1.00 76.08  ? 279 ARG A CB   1 
ATOM   2157 C CG   . ARG A 1 279 ? -14.124 37.735  -25.008 1.00 85.10  ? 279 ARG A CG   1 
ATOM   2158 C CD   . ARG A 1 279 ? -15.527 38.122  -25.415 1.00 86.53  ? 279 ARG A CD   1 
ATOM   2159 N NE   . ARG A 1 279 ? -16.512 37.397  -24.622 1.00 92.15  ? 279 ARG A NE   1 
ATOM   2160 C CZ   . ARG A 1 279 ? -17.824 37.535  -24.757 1.00 89.08  ? 279 ARG A CZ   1 
ATOM   2161 N NH1  . ARG A 1 279 ? -18.340 38.394  -25.622 1.00 88.49  ? 279 ARG A NH1  1 
ATOM   2162 N NH2  . ARG A 1 279 ? -18.635 36.796  -24.003 1.00 84.19  ? 279 ARG A NH2  1 
ATOM   2163 N N    . THR A 1 280 ? -12.912 33.423  -25.135 1.00 63.99  ? 280 THR A N    1 
ATOM   2164 C CA   . THR A 1 280 ? -12.563 32.085  -25.581 1.00 59.51  ? 280 THR A CA   1 
ATOM   2165 C C    . THR A 1 280 ? -13.795 31.368  -26.078 1.00 57.10  ? 280 THR A C    1 
ATOM   2166 O O    . THR A 1 280 ? -14.922 31.631  -25.637 1.00 59.71  ? 280 THR A O    1 
ATOM   2167 C CB   . THR A 1 280 ? -11.884 31.262  -24.474 1.00 58.30  ? 280 THR A CB   1 
ATOM   2168 O OG1  . THR A 1 280 ? -12.771 31.137  -23.363 1.00 60.59  ? 280 THR A OG1  1 
ATOM   2169 C CG2  . THR A 1 280 ? -10.620 31.977  -23.991 1.00 54.84  ? 280 THR A CG2  1 
ATOM   2170 N N    . ILE A 1 281 ? -13.536 30.423  -26.980 1.00 54.36  ? 281 ILE A N    1 
ATOM   2171 C CA   . ILE A 1 281 ? -14.560 29.560  -27.543 1.00 53.81  ? 281 ILE A CA   1 
ATOM   2172 C C    . ILE A 1 281 ? -14.125 28.131  -27.291 1.00 52.19  ? 281 ILE A C    1 
ATOM   2173 O O    . ILE A 1 281 ? -13.077 27.724  -27.791 1.00 48.58  ? 281 ILE A O    1 
ATOM   2174 C CB   . ILE A 1 281 ? -14.752 29.802  -29.056 1.00 51.31  ? 281 ILE A CB   1 
ATOM   2175 C CG1  . ILE A 1 281 ? -14.848 31.305  -29.292 1.00 52.95  ? 281 ILE A CG1  1 
ATOM   2176 C CG2  . ILE A 1 281 ? -15.947 29.114  -29.578 1.00 47.90  ? 281 ILE A CG2  1 
ATOM   2177 C CD1  . ILE A 1 281 ? -15.490 31.704  -30.607 1.00 56.87  ? 281 ILE A CD1  1 
ATOM   2178 N N    . LEU A 1 282 ? -14.920 27.354  -26.542 1.00 50.94  ? 282 LEU A N    1 
ATOM   2179 C CA   . LEU A 1 282 ? -14.537 25.966  -26.229 1.00 47.18  ? 282 LEU A CA   1 
ATOM   2180 C C    . LEU A 1 282 ? -13.108 25.885  -25.681 1.00 49.66  ? 282 LEU A C    1 
ATOM   2181 O O    . LEU A 1 282 ? -12.323 25.002  -26.047 1.00 50.29  ? 282 LEU A O    1 
ATOM   2182 C CB   . LEU A 1 282 ? -14.687 25.077  -27.461 1.00 44.47  ? 282 LEU A CB   1 
ATOM   2183 C CG   . LEU A 1 282 ? -16.157 24.792  -27.777 1.00 49.89  ? 282 LEU A CG   1 
ATOM   2184 C CD1  . LEU A 1 282 ? -16.302 23.792  -28.905 1.00 42.87  ? 282 LEU A CD1  1 
ATOM   2185 C CD2  . LEU A 1 282 ? -16.871 24.288  -26.516 1.00 49.21  ? 282 LEU A CD2  1 
ATOM   2186 N N    . GLY A 1 283 ? -12.750 26.852  -24.838 1.00 46.33  ? 283 GLY A N    1 
ATOM   2187 C CA   . GLY A 1 283 ? -11.471 26.846  -24.162 1.00 48.88  ? 283 GLY A CA   1 
ATOM   2188 C C    . GLY A 1 283 ? -10.281 27.255  -25.005 1.00 57.25  ? 283 GLY A C    1 
ATOM   2189 O O    . GLY A 1 283 ? -9.138  27.025  -24.590 1.00 61.18  ? 283 GLY A O    1 
ATOM   2190 N N    . SER A 1 284 ? -10.494 27.867  -26.167 1.00 50.64  ? 284 SER A N    1 
ATOM   2191 C CA   . SER A 1 284 ? -9.394  28.335  -26.994 1.00 50.95  ? 284 SER A CA   1 
ATOM   2192 C C    . SER A 1 284 ? -9.530  29.823  -27.282 1.00 54.07  ? 284 SER A C    1 
ATOM   2193 O O    . SER A 1 284 ? -10.638 30.346  -27.391 1.00 56.89  ? 284 SER A O    1 
ATOM   2194 C CB   . SER A 1 284 ? -9.350  27.574  -28.317 1.00 52.88  ? 284 SER A CB   1 
ATOM   2195 O OG   . SER A 1 284 ? -8.444  28.182  -29.210 1.00 53.64  ? 284 SER A OG   1 
ATOM   2196 N N    . ALA A 1 285 ? -8.394  30.500  -27.434 1.00 52.43  ? 285 ALA A N    1 
ATOM   2197 C CA   . ALA A 1 285 ? -8.384  31.874  -27.909 1.00 52.50  ? 285 ALA A CA   1 
ATOM   2198 C C    . ALA A 1 285 ? -8.151  31.981  -29.413 1.00 53.50  ? 285 ALA A C    1 
ATOM   2199 O O    . ALA A 1 285 ? -7.840  33.067  -29.898 1.00 57.15  ? 285 ALA A O    1 
ATOM   2200 C CB   . ALA A 1 285 ? -7.334  32.693  -27.166 1.00 53.54  ? 285 ALA A CB   1 
ATOM   2201 N N    . LEU A 1 286 ? -8.297  30.886  -30.158 1.00 50.05  ? 286 LEU A N    1 
ATOM   2202 C CA   . LEU A 1 286 ? -8.167  30.897  -31.605 1.00 51.79  ? 286 LEU A CA   1 
ATOM   2203 C C    . LEU A 1 286 ? -9.327  30.119  -32.200 1.00 53.34  ? 286 LEU A C    1 
ATOM   2204 O O    . LEU A 1 286 ? -10.012 29.357  -31.508 1.00 54.15  ? 286 LEU A O    1 
ATOM   2205 C CB   . LEU A 1 286 ? -6.850  30.272  -32.075 1.00 53.13  ? 286 LEU A CB   1 
ATOM   2206 C CG   . LEU A 1 286 ? -5.585  30.774  -31.405 1.00 55.65  ? 286 LEU A CG   1 
ATOM   2207 C CD1  . LEU A 1 286 ? -4.510  29.726  -31.515 1.00 52.98  ? 286 LEU A CD1  1 
ATOM   2208 C CD2  . LEU A 1 286 ? -5.143  32.092  -32.042 1.00 54.72  ? 286 LEU A CD2  1 
ATOM   2209 N N    . LEU A 1 287 ? -9.509  30.284  -33.506 1.00 48.77  ? 287 LEU A N    1 
ATOM   2210 C CA   . LEU A 1 287 ? -10.512 29.524  -34.235 1.00 49.43  ? 287 LEU A CA   1 
ATOM   2211 C C    . LEU A 1 287 ? -9.945  28.163  -34.619 1.00 47.78  ? 287 LEU A C    1 
ATOM   2212 O O    . LEU A 1 287 ? -8.925  28.078  -35.306 1.00 49.24  ? 287 LEU A O    1 
ATOM   2213 C CB   . LEU A 1 287 ? -10.955 30.314  -35.456 1.00 46.77  ? 287 LEU A CB   1 
ATOM   2214 C CG   . LEU A 1 287 ? -11.458 31.686  -35.018 1.00 48.15  ? 287 LEU A CG   1 
ATOM   2215 C CD1  . LEU A 1 287 ? -11.570 32.661  -36.175 1.00 52.88  ? 287 LEU A CD1  1 
ATOM   2216 C CD2  . LEU A 1 287 ? -12.782 31.548  -34.276 1.00 50.75  ? 287 LEU A CD2  1 
ATOM   2217 N N    . GLU A 1 288 ? -10.588 27.101  -34.154 1.00 45.93  ? 288 GLU A N    1 
ATOM   2218 C CA   . GLU A 1 288 ? -10.110 25.742  -34.366 1.00 46.42  ? 288 GLU A CA   1 
ATOM   2219 C C    . GLU A 1 288 ? -10.631 25.172  -35.678 1.00 43.43  ? 288 GLU A C    1 
ATOM   2220 O O    . GLU A 1 288 ? -11.840 25.121  -35.893 1.00 44.53  ? 288 GLU A O    1 
ATOM   2221 C CB   . GLU A 1 288 ? -10.555 24.841  -33.216 1.00 49.28  ? 288 GLU A CB   1 
ATOM   2222 C CG   . GLU A 1 288 ? -9.884  25.182  -31.919 1.00 51.01  ? 288 GLU A CG   1 
ATOM   2223 C CD   . GLU A 1 288 ? -8.421  24.782  -31.950 1.00 57.33  ? 288 GLU A CD   1 
ATOM   2224 O OE1  . GLU A 1 288 ? -8.106  23.720  -32.567 1.00 58.12  ? 288 GLU A OE1  1 
ATOM   2225 O OE2  . GLU A 1 288 ? -7.601  25.552  -31.385 1.00 61.66  ? 288 GLU A OE2  1 
ATOM   2226 N N    . ASP A 1 289 ? -9.724  24.661  -36.515 1.00 42.48  ? 289 ASP A N    1 
ATOM   2227 C CA   . ASP A 1 289 ? -10.089 24.103  -37.810 1.00 43.83  ? 289 ASP A CA   1 
ATOM   2228 C C    . ASP A 1 289 ? -9.661  22.642  -37.945 1.00 41.89  ? 289 ASP A C    1 
ATOM   2229 O O    . ASP A 1 289 ? -9.481  22.150  -39.056 1.00 42.32  ? 289 ASP A O    1 
ATOM   2230 C CB   . ASP A 1 289 ? -9.499  24.950  -38.952 1.00 41.75  ? 289 ASP A CB   1 
ATOM   2231 C CG   . ASP A 1 289 ? -8.016  24.632  -39.238 1.00 44.44  ? 289 ASP A CG   1 
ATOM   2232 O OD1  . ASP A 1 289 ? -7.321  24.068  -38.371 1.00 46.65  ? 289 ASP A OD1  1 
ATOM   2233 O OD2  . ASP A 1 289 ? -7.528  24.952  -40.337 1.00 49.55  ? 289 ASP A OD2  1 
ATOM   2234 N N    . GLU A 1 290 ? -9.512  21.912  -36.839 1.00 38.35  ? 290 GLU A N    1 
ATOM   2235 C CA   . GLU A 1 290 ? -9.118  20.507  -36.935 1.00 42.28  ? 290 GLU A CA   1 
ATOM   2236 C C    . GLU A 1 290 ? -10.223 19.561  -36.472 1.00 40.28  ? 290 GLU A C    1 
ATOM   2237 O O    . GLU A 1 290 ? -9.952  18.437  -36.061 1.00 36.25  ? 290 GLU A O    1 
ATOM   2238 C CB   . GLU A 1 290 ? -7.800  20.248  -36.198 1.00 41.22  ? 290 GLU A CB   1 
ATOM   2239 C CG   . GLU A 1 290 ? -6.601  21.043  -36.771 1.00 43.35  ? 290 GLU A CG   1 
ATOM   2240 C CD   . GLU A 1 290 ? -5.305  20.221  -36.957 1.00 45.02  ? 290 GLU A CD   1 
ATOM   2241 O OE1  . GLU A 1 290 ? -5.055  19.274  -36.175 1.00 45.51  ? 290 GLU A OE1  1 
ATOM   2242 O OE2  . GLU A 1 290 ? -4.498  20.565  -37.858 1.00 41.10  ? 290 GLU A OE2  1 
ATOM   2243 N N    . PHE A 1 291 ? -11.475 20.001  -36.563 1.00 40.22  ? 291 PHE A N    1 
ATOM   2244 C CA   . PHE A 1 291 ? -12.648 19.163  -36.337 1.00 43.09  ? 291 PHE A CA   1 
ATOM   2245 C C    . PHE A 1 291 ? -13.511 19.161  -37.595 1.00 40.08  ? 291 PHE A C    1 
ATOM   2246 O O    . PHE A 1 291 ? -14.015 20.220  -37.990 1.00 37.51  ? 291 PHE A O    1 
ATOM   2247 C CB   . PHE A 1 291 ? -13.460 19.704  -35.147 1.00 39.08  ? 291 PHE A CB   1 
ATOM   2248 C CG   . PHE A 1 291 ? -12.779 19.566  -33.832 1.00 40.61  ? 291 PHE A CG   1 
ATOM   2249 C CD1  . PHE A 1 291 ? -12.695 18.329  -33.207 1.00 44.03  ? 291 PHE A CD1  1 
ATOM   2250 C CD2  . PHE A 1 291 ? -12.184 20.651  -33.241 1.00 41.08  ? 291 PHE A CD2  1 
ATOM   2251 C CE1  . PHE A 1 291 ? -12.057 18.197  -32.000 1.00 42.86  ? 291 PHE A CE1  1 
ATOM   2252 C CE2  . PHE A 1 291 ? -11.557 20.529  -32.014 1.00 48.74  ? 291 PHE A CE2  1 
ATOM   2253 C CZ   . PHE A 1 291 ? -11.493 19.302  -31.396 1.00 46.39  ? 291 PHE A CZ   1 
ATOM   2254 N N    . THR A 1 292 ? -13.727 17.982  -38.196 1.00 40.49  ? 292 THR A N    1 
ATOM   2255 C CA   . THR A 1 292 ? -14.662 17.903  -39.320 1.00 43.84  ? 292 THR A CA   1 
ATOM   2256 C C    . THR A 1 292 ? -16.105 17.986  -38.821 1.00 44.50  ? 292 THR A C    1 
ATOM   2257 O O    . THR A 1 292 ? -16.370 17.773  -37.638 1.00 41.43  ? 292 THR A O    1 
ATOM   2258 C CB   . THR A 1 292 ? -14.542 16.611  -40.105 1.00 40.43  ? 292 THR A CB   1 
ATOM   2259 O OG1  . THR A 1 292 ? -14.781 15.517  -39.221 1.00 45.28  ? 292 THR A OG1  1 
ATOM   2260 C CG2  . THR A 1 292 ? -13.160 16.474  -40.760 1.00 43.00  ? 292 THR A CG2  1 
ATOM   2261 N N    . PRO A 1 293 ? -17.062 18.303  -39.716 1.00 44.32  ? 293 PRO A N    1 
ATOM   2262 C CA   . PRO A 1 293 ? -18.476 18.181  -39.330 1.00 45.37  ? 293 PRO A CA   1 
ATOM   2263 C C    . PRO A 1 293 ? -18.789 16.821  -38.754 1.00 43.77  ? 293 PRO A C    1 
ATOM   2264 O O    . PRO A 1 293 ? -19.510 16.723  -37.753 1.00 40.71  ? 293 PRO A O    1 
ATOM   2265 C CB   . PRO A 1 293 ? -19.223 18.438  -40.650 1.00 45.58  ? 293 PRO A CB   1 
ATOM   2266 C CG   . PRO A 1 293 ? -18.328 19.345  -41.408 1.00 46.35  ? 293 PRO A CG   1 
ATOM   2267 C CD   . PRO A 1 293 ? -16.920 18.825  -41.088 1.00 45.03  ? 293 PRO A CD   1 
ATOM   2268 N N    . PHE A 1 294 ? -18.217 15.767  -39.329 1.00 40.90  ? 294 PHE A N    1 
ATOM   2269 C CA   . PHE A 1 294 ? -18.490 14.428  -38.831 1.00 44.53  ? 294 PHE A CA   1 
ATOM   2270 C C    . PHE A 1 294 ? -17.897 14.224  -37.437 1.00 48.65  ? 294 PHE A C    1 
ATOM   2271 O O    . PHE A 1 294 ? -18.526 13.586  -36.587 1.00 49.97  ? 294 PHE A O    1 
ATOM   2272 C CB   . PHE A 1 294 ? -17.959 13.397  -39.824 1.00 50.84  ? 294 PHE A CB   1 
ATOM   2273 C CG   . PHE A 1 294 ? -18.173 11.949  -39.401 1.00 61.29  ? 294 PHE A CG   1 
ATOM   2274 C CD1  . PHE A 1 294 ? -17.298 11.288  -38.534 1.00 63.18  ? 294 PHE A CD1  1 
ATOM   2275 C CD2  . PHE A 1 294 ? -19.242 11.238  -39.916 1.00 68.71  ? 294 PHE A CD2  1 
ATOM   2276 C CE1  . PHE A 1 294 ? -17.516 9.947   -38.179 1.00 63.70  ? 294 PHE A CE1  1 
ATOM   2277 C CE2  . PHE A 1 294 ? -19.453 9.913   -39.569 1.00 69.07  ? 294 PHE A CE2  1 
ATOM   2278 C CZ   . PHE A 1 294 ? -18.593 9.268   -38.702 1.00 64.66  ? 294 PHE A CZ   1 
ATOM   2279 N N    . ASP A 1 295 ? -16.696 14.763  -37.168 1.00 46.00  ? 295 ASP A N    1 
ATOM   2280 C CA   . ASP A 1 295 ? -16.146 14.643  -35.816 1.00 46.24  ? 295 ASP A CA   1 
ATOM   2281 C C    . ASP A 1 295 ? -17.036 15.337  -34.796 1.00 45.70  ? 295 ASP A C    1 
ATOM   2282 O O    . ASP A 1 295 ? -17.223 14.821  -33.691 1.00 45.98  ? 295 ASP A O    1 
ATOM   2283 C CB   . ASP A 1 295 ? -14.745 15.233  -35.707 1.00 44.04  ? 295 ASP A CB   1 
ATOM   2284 C CG   . ASP A 1 295 ? -13.816 14.729  -36.779 1.00 47.64  ? 295 ASP A CG   1 
ATOM   2285 O OD1  . ASP A 1 295 ? -14.008 13.578  -37.240 1.00 50.52  ? 295 ASP A OD1  1 
ATOM   2286 O OD2  . ASP A 1 295 ? -12.887 15.487  -37.146 1.00 43.29  ? 295 ASP A OD2  1 
ATOM   2287 N N    . VAL A 1 296 ? -17.538 16.536  -35.112 1.00 46.47  ? 296 VAL A N    1 
ATOM   2288 C CA   . VAL A 1 296 ? -18.451 17.212  -34.186 1.00 45.77  ? 296 VAL A CA   1 
ATOM   2289 C C    . VAL A 1 296 ? -19.626 16.301  -33.856 1.00 49.04  ? 296 VAL A C    1 
ATOM   2290 O O    . VAL A 1 296 ? -19.977 16.118  -32.685 1.00 51.27  ? 296 VAL A O    1 
ATOM   2291 C CB   . VAL A 1 296 ? -18.931 18.568  -34.748 1.00 43.77  ? 296 VAL A CB   1 
ATOM   2292 C CG1  . VAL A 1 296 ? -20.032 19.155  -33.866 1.00 43.76  ? 296 VAL A CG1  1 
ATOM   2293 C CG2  . VAL A 1 296 ? -17.793 19.571  -34.822 1.00 42.80  ? 296 VAL A CG2  1 
ATOM   2294 N N    . VAL A 1 297 ? -20.230 15.687  -34.884 1.00 49.10  ? 297 VAL A N    1 
ATOM   2295 C CA   . VAL A 1 297 ? -21.439 14.889  -34.674 1.00 50.83  ? 297 VAL A CA   1 
ATOM   2296 C C    . VAL A 1 297 ? -21.123 13.628  -33.875 1.00 54.96  ? 297 VAL A C    1 
ATOM   2297 O O    . VAL A 1 297 ? -21.811 13.307  -32.894 1.00 58.33  ? 297 VAL A O    1 
ATOM   2298 C CB   . VAL A 1 297 ? -22.104 14.544  -36.022 1.00 51.33  ? 297 VAL A CB   1 
ATOM   2299 C CG1  . VAL A 1 297 ? -23.001 13.344  -35.843 1.00 49.56  ? 297 VAL A CG1  1 
ATOM   2300 C CG2  . VAL A 1 297 ? -22.920 15.730  -36.555 1.00 49.74  ? 297 VAL A CG2  1 
ATOM   2301 N N    . ARG A 1 298 ? -20.068 12.906  -34.267 1.00 52.10  ? 298 ARG A N    1 
ATOM   2302 C CA   . ARG A 1 298 ? -19.702 11.682  -33.551 1.00 55.43  ? 298 ARG A CA   1 
ATOM   2303 C C    . ARG A 1 298 ? -19.424 11.972  -32.074 1.00 55.66  ? 298 ARG A C    1 
ATOM   2304 O O    . ARG A 1 298 ? -19.827 11.215  -31.181 1.00 56.74  ? 298 ARG A O    1 
ATOM   2305 C CB   . ARG A 1 298 ? -18.481 11.022  -34.191 1.00 61.18  ? 298 ARG A CB   1 
ATOM   2306 C CG   . ARG A 1 298 ? -17.480 10.542  -33.133 1.00 65.79  ? 298 ARG A CG   1 
ATOM   2307 C CD   . ARG A 1 298 ? -16.587 9.443   -33.688 1.00 73.72  ? 298 ARG A CD   1 
ATOM   2308 N NE   . ARG A 1 298 ? -15.487 10.000  -34.475 1.00 72.85  ? 298 ARG A NE   1 
ATOM   2309 C CZ   . ARG A 1 298 ? -14.284 10.352  -34.024 1.00 69.70  ? 298 ARG A CZ   1 
ATOM   2310 N NH1  . ARG A 1 298 ? -13.914 10.162  -32.750 1.00 68.99  ? 298 ARG A NH1  1 
ATOM   2311 N NH2  . ARG A 1 298 ? -13.436 10.943  -34.872 1.00 56.71  ? 298 ARG A NH2  1 
ATOM   2312 N N    . GLN A 1 299 ? -18.706 13.056  -31.797 1.00 54.35  ? 299 GLN A N    1 
ATOM   2313 C CA   . GLN A 1 299 ? -18.448 13.401  -30.405 1.00 54.61  ? 299 GLN A CA   1 
ATOM   2314 C C    . GLN A 1 299 ? -19.724 13.875  -29.723 1.00 56.10  ? 299 GLN A C    1 
ATOM   2315 O O    . GLN A 1 299 ? -20.058 13.430  -28.620 1.00 59.49  ? 299 GLN A O    1 
ATOM   2316 C CB   . GLN A 1 299 ? -17.363 14.474  -30.307 1.00 48.86  ? 299 GLN A CB   1 
ATOM   2317 C CG   . GLN A 1 299 ? -16.970 14.717  -28.880 1.00 49.86  ? 299 GLN A CG   1 
ATOM   2318 C CD   . GLN A 1 299 ? -15.689 15.489  -28.719 1.00 46.78  ? 299 GLN A CD   1 
ATOM   2319 O OE1  . GLN A 1 299 ? -15.436 16.021  -27.639 1.00 46.22  ? 299 GLN A OE1  1 
ATOM   2320 N NE2  . GLN A 1 299 ? -14.896 15.605  -29.792 1.00 41.92  ? 299 GLN A NE2  1 
ATOM   2321 N N    . CYS A 1 300 ? -20.466 14.767  -30.371 1.00 57.42  ? 300 CYS A N    1 
ATOM   2322 C CA   . CYS A 1 300 ? -21.653 15.338  -29.747 1.00 58.75  ? 300 CYS A CA   1 
ATOM   2323 C C    . CYS A 1 300 ? -22.853 14.389  -29.729 1.00 61.29  ? 300 CYS A C    1 
ATOM   2324 O O    . CYS A 1 300 ? -23.861 14.714  -29.092 1.00 62.89  ? 300 CYS A O    1 
ATOM   2325 C CB   . CYS A 1 300 ? -22.003 16.654  -30.436 1.00 53.39  ? 300 CYS A CB   1 
ATOM   2326 S SG   . CYS A 1 300 ? -20.817 17.950  -29.968 1.00 56.63  ? 300 CYS A SG   1 
ATOM   2327 N N    . SER A 1 301 ? -22.753 13.208  -30.358 1.00 71.66  ? 301 SER A N    1 
ATOM   2328 C CA   . SER A 1 301 ? -23.796 12.185  -30.288 1.00 71.06  ? 301 SER A CA   1 
ATOM   2329 C C    . SER A 1 301 ? -23.320 10.817  -29.794 1.00 74.30  ? 301 SER A C    1 
ATOM   2330 O O    . SER A 1 301 ? -24.114 9.867   -29.811 1.00 72.95  ? 301 SER A O    1 
ATOM   2331 C CB   . SER A 1 301 ? -24.457 12.034  -31.659 1.00 73.19  ? 301 SER A CB   1 
ATOM   2332 O OG   . SER A 1 301 ? -24.888 13.313  -32.103 1.00 78.79  ? 301 SER A OG   1 
ATOM   2333 N N    . GLY A 1 302 ? -22.052 10.678  -29.387 1.00 68.88  ? 302 GLY A N    1 
ATOM   2334 C CA   . GLY A 1 302 ? -21.605 9.524   -28.621 1.00 64.33  ? 302 GLY A CA   1 
ATOM   2335 C C    . GLY A 1 302 ? -21.336 8.260   -29.406 1.00 68.51  ? 302 GLY A C    1 
ATOM   2336 O O    . GLY A 1 302 ? -21.528 7.159   -28.877 1.00 66.71  ? 302 GLY A O    1 
ATOM   2337 N N    . VAL A 1 303 ? -20.884 8.381   -30.655 1.00 66.55  ? 303 VAL A N    1 
ATOM   2338 C CA   . VAL A 1 303 ? -20.678 7.199   -31.484 1.00 78.33  ? 303 VAL A CA   1 
ATOM   2339 C C    . VAL A 1 303 ? -19.617 6.295   -30.852 1.00 79.96  ? 303 VAL A C    1 
ATOM   2340 O O    . VAL A 1 303 ? -18.586 6.768   -30.351 1.00 77.23  ? 303 VAL A O    1 
ATOM   2341 C CB   . VAL A 1 303 ? -20.295 7.634   -32.912 1.00 76.23  ? 303 VAL A CB   1 
ATOM   2342 C CG1  . VAL A 1 303 ? -19.709 6.478   -33.732 1.00 79.64  ? 303 VAL A CG1  1 
ATOM   2343 C CG2  . VAL A 1 303 ? -21.500 8.259   -33.612 1.00 75.70  ? 303 VAL A CG2  1 
ATOM   2344 N N    . THR A 1 304 ? -19.865 4.981   -30.874 1.00 81.71  ? 304 THR A N    1 
ATOM   2345 C CA   . THR A 1 304 ? -18.899 3.976   -30.423 1.00 83.36  ? 304 THR A CA   1 
ATOM   2346 C C    . THR A 1 304 ? -18.484 3.093   -31.605 1.00 91.95  ? 304 THR A C    1 
ATOM   2347 O O    . THR A 1 304 ? -18.926 3.284   -32.743 1.00 96.37  ? 304 THR A O    1 
ATOM   2348 C CB   . THR A 1 304 ? -19.440 3.141   -29.243 1.00 78.18  ? 304 THR A CB   1 
ATOM   2349 O OG1  . THR A 1 304 ? -20.411 2.181   -29.687 1.00 82.12  ? 304 THR A OG1  1 
ATOM   2350 C CG2  . THR A 1 304 ? -20.027 4.030   -28.143 1.00 70.69  ? 304 THR A CG2  1 
ATOM   2351 N N    . PHE A 1 305 ? -17.619 2.116   -31.329 1.00 89.48  ? 305 PHE A N    1 
ATOM   2352 C CA   . PHE A 1 305 ? -17.038 1.304   -32.389 1.00 101.72 ? 305 PHE A CA   1 
ATOM   2353 C C    . PHE A 1 305 ? -16.863 -0.135  -31.927 1.00 108.28 ? 305 PHE A C    1 
ATOM   2354 O O    . PHE A 1 305 ? -16.422 -0.391  -30.803 1.00 99.55  ? 305 PHE A O    1 
ATOM   2355 C CB   . PHE A 1 305 ? -15.684 1.892   -32.838 1.00 95.88  ? 305 PHE A CB   1 
ATOM   2356 C CG   . PHE A 1 305 ? -15.754 3.351   -33.200 1.00 88.35  ? 305 PHE A CG   1 
ATOM   2357 C CD1  . PHE A 1 305 ? -16.378 3.763   -34.368 1.00 92.26  ? 305 PHE A CD1  1 
ATOM   2358 C CD2  . PHE A 1 305 ? -15.252 4.313   -32.339 1.00 81.71  ? 305 PHE A CD2  1 
ATOM   2359 C CE1  . PHE A 1 305 ? -16.464 5.107   -34.693 1.00 92.27  ? 305 PHE A CE1  1 
ATOM   2360 C CE2  . PHE A 1 305 ? -15.339 5.663   -32.651 1.00 83.53  ? 305 PHE A CE2  1 
ATOM   2361 C CZ   . PHE A 1 305 ? -15.947 6.061   -33.832 1.00 86.60  ? 305 PHE A CZ   1 
ATOM   2362 N N    . GLN A 1 306 ? -17.223 -1.066  -32.810 1.00 118.85 ? 306 GLN A N    1 
ATOM   2363 C CA   . GLN A 1 306 ? -17.092 -2.497  -32.555 1.00 121.45 ? 306 GLN A CA   1 
ATOM   2364 C C    . GLN A 1 306 ? -16.003 -3.111  -33.431 1.00 117.36 ? 306 GLN A C    1 
ATOM   2365 O O    . GLN A 1 306 ? -16.201 -4.162  -34.038 1.00 114.54 ? 306 GLN A O    1 
ATOM   2366 C CB   . GLN A 1 306 ? -18.428 -3.212  -32.791 1.00 125.83 ? 306 GLN A CB   1 
ATOM   2367 C CG   . GLN A 1 306 ? -19.392 -3.117  -31.619 1.00 129.57 ? 306 GLN A CG   1 
ATOM   2368 C CD   . GLN A 1 306 ? -20.456 -4.196  -31.656 1.00 137.57 ? 306 GLN A CD   1 
ATOM   2369 O OE1  . GLN A 1 306 ? -20.833 -4.680  -32.726 1.00 137.17 ? 306 GLN A OE1  1 
ATOM   2370 N NE2  . GLN A 1 306 ? -20.939 -4.589  -30.482 1.00 139.02 ? 306 GLN A NE2  1 
ATOM   2371 N N    . SER B 1 1   ? 10.115  16.711  -33.412 1.00 46.52  ? 1   SER B N    1 
ATOM   2372 C CA   . SER B 1 1   ? 9.613   18.012  -32.994 1.00 52.17  ? 1   SER B CA   1 
ATOM   2373 C C    . SER B 1 1   ? 8.085   18.029  -33.011 1.00 47.36  ? 1   SER B C    1 
ATOM   2374 O O    . SER B 1 1   ? 7.452   17.130  -33.573 1.00 44.92  ? 1   SER B O    1 
ATOM   2375 C CB   . SER B 1 1   ? 10.182  19.119  -33.888 1.00 57.40  ? 1   SER B CB   1 
ATOM   2376 O OG   . SER B 1 1   ? 9.730   20.394  -33.467 1.00 61.50  ? 1   SER B OG   1 
ATOM   2377 N N    . GLY B 1 2   ? 7.498   19.047  -32.397 1.00 47.89  ? 2   GLY B N    1 
ATOM   2378 C CA   . GLY B 1 2   ? 6.056   19.156  -32.287 1.00 47.99  ? 2   GLY B CA   1 
ATOM   2379 C C    . GLY B 1 2   ? 5.575   18.721  -30.915 1.00 50.28  ? 2   GLY B C    1 
ATOM   2380 O O    . GLY B 1 2   ? 6.205   17.904  -30.234 1.00 51.32  ? 2   GLY B O    1 
ATOM   2381 N N    . PHE B 1 3   ? 4.427   19.254  -30.499 1.00 50.64  ? 3   PHE B N    1 
ATOM   2382 C CA   . PHE B 1 3   ? 3.989   19.043  -29.120 1.00 48.53  ? 3   PHE B CA   1 
ATOM   2383 C C    . PHE B 1 3   ? 2.474   19.053  -29.076 1.00 48.77  ? 3   PHE B C    1 
ATOM   2384 O O    . PHE B 1 3   ? 1.852   20.094  -29.304 1.00 49.62  ? 3   PHE B O    1 
ATOM   2385 C CB   . PHE B 1 3   ? 4.562   20.104  -28.183 1.00 49.42  ? 3   PHE B CB   1 
ATOM   2386 C CG   . PHE B 1 3   ? 4.576   19.669  -26.768 1.00 46.61  ? 3   PHE B CG   1 
ATOM   2387 C CD1  . PHE B 1 3   ? 5.503   18.749  -26.331 1.00 47.80  ? 3   PHE B CD1  1 
ATOM   2388 C CD2  . PHE B 1 3   ? 3.591   20.084  -25.895 1.00 48.27  ? 3   PHE B CD2  1 
ATOM   2389 C CE1  . PHE B 1 3   ? 5.511   18.317  -25.017 1.00 48.68  ? 3   PHE B CE1  1 
ATOM   2390 C CE2  . PHE B 1 3   ? 3.578   19.651  -24.587 1.00 50.74  ? 3   PHE B CE2  1 
ATOM   2391 C CZ   . PHE B 1 3   ? 4.550   18.761  -24.147 1.00 51.60  ? 3   PHE B CZ   1 
ATOM   2392 N N    . ARG B 1 4   ? 1.893   17.900  -28.739 1.00 48.44  ? 4   ARG B N    1 
ATOM   2393 C CA   . ARG B 1 4   ? 0.456   17.688  -28.761 1.00 45.46  ? 4   ARG B CA   1 
ATOM   2394 C C    . ARG B 1 4   ? -0.009  17.137  -27.431 1.00 44.69  ? 4   ARG B C    1 
ATOM   2395 O O    . ARG B 1 4   ? 0.743   16.463  -26.726 1.00 47.07  ? 4   ARG B O    1 
ATOM   2396 C CB   . ARG B 1 4   ? 0.051   16.690  -29.860 1.00 44.37  ? 4   ARG B CB   1 
ATOM   2397 C CG   . ARG B 1 4   ? 0.757   16.931  -31.134 1.00 44.06  ? 4   ARG B CG   1 
ATOM   2398 C CD   . ARG B 1 4   ? -0.048  17.952  -31.915 1.00 54.26  ? 4   ARG B CD   1 
ATOM   2399 N NE   . ARG B 1 4   ? -1.460  17.880  -31.560 1.00 48.78  ? 4   ARG B NE   1 
ATOM   2400 C CZ   . ARG B 1 4   ? -2.375  17.271  -32.300 1.00 51.62  ? 4   ARG B CZ   1 
ATOM   2401 N NH1  . ARG B 1 4   ? -2.053  16.699  -33.457 1.00 50.15  ? 4   ARG B NH1  1 
ATOM   2402 N NH2  . ARG B 1 4   ? -3.640  17.224  -31.871 1.00 51.08  ? 4   ARG B NH2  1 
ATOM   2403 N N    . LYS B 1 5   ? -1.262  17.419  -27.103 1.00 46.57  ? 5   LYS B N    1 
ATOM   2404 C CA   . LYS B 1 5   ? -1.941  16.643  -26.085 1.00 44.69  ? 5   LYS B CA   1 
ATOM   2405 C C    . LYS B 1 5   ? -2.027  15.202  -26.567 1.00 42.80  ? 5   LYS B C    1 
ATOM   2406 O O    . LYS B 1 5   ? -2.667  14.908  -27.581 1.00 46.68  ? 5   LYS B O    1 
ATOM   2407 C CB   . LYS B 1 5   ? -3.334  17.219  -25.823 1.00 44.22  ? 5   LYS B CB   1 
ATOM   2408 C CG   . LYS B 1 5   ? -3.506  17.715  -24.434 1.00 46.60  ? 5   LYS B CG   1 
ATOM   2409 C CD   . LYS B 1 5   ? -4.472  18.887  -24.372 1.00 58.77  ? 5   LYS B CD   1 
ATOM   2410 C CE   . LYS B 1 5   ? -4.391  19.554  -22.998 1.00 54.64  ? 5   LYS B CE   1 
ATOM   2411 N NZ   . LYS B 1 5   ? -5.071  20.884  -23.004 1.00 63.74  ? 5   LYS B NZ   1 
ATOM   2412 N N    . MET B 1 6   ? -1.369  14.307  -25.852 1.00 40.74  ? 6   MET B N    1 
ATOM   2413 C CA   . MET B 1 6   ? -1.230  12.924  -26.263 1.00 41.19  ? 6   MET B CA   1 
ATOM   2414 C C    . MET B 1 6   ? -1.744  12.006  -25.174 1.00 37.83  ? 6   MET B C    1 
ATOM   2415 O O    . MET B 1 6   ? -1.232  12.029  -24.054 1.00 40.61  ? 6   MET B O    1 
ATOM   2416 C CB   . MET B 1 6   ? 0.220   12.583  -26.549 1.00 41.81  ? 6   MET B CB   1 
ATOM   2417 C CG   . MET B 1 6   ? 0.392   11.907  -27.848 1.00 44.13  ? 6   MET B CG   1 
ATOM   2418 S SD   . MET B 1 6   ? 2.157   11.816  -28.112 1.00 54.62  ? 6   MET B SD   1 
ATOM   2419 C CE   . MET B 1 6   ? 2.596   10.807  -26.730 1.00 48.93  ? 6   MET B CE   1 
ATOM   2420 N N    . ALA B 1 7   ? -2.706  11.168  -25.524 1.00 36.05  ? 7   ALA B N    1 
ATOM   2421 C CA   . ALA B 1 7   ? -3.178  10.123  -24.637 1.00 37.06  ? 7   ALA B CA   1 
ATOM   2422 C C    . ALA B 1 7   ? -2.270  8.893   -24.711 1.00 40.99  ? 7   ALA B C    1 
ATOM   2423 O O    . ALA B 1 7   ? -1.610  8.641   -25.717 1.00 43.09  ? 7   ALA B O    1 
ATOM   2424 C CB   . ALA B 1 7   ? -4.605  9.744   -25.021 1.00 37.21  ? 7   ALA B CB   1 
ATOM   2425 N N    . PHE B 1 8   ? -2.294  8.086   -23.657 1.00 40.27  ? 8   PHE B N    1 
ATOM   2426 C CA   . PHE B 1 8   ? -1.686  6.768   -23.714 1.00 40.84  ? 8   PHE B CA   1 
ATOM   2427 C C    . PHE B 1 8   ? -2.431  5.855   -24.691 1.00 41.91  ? 8   PHE B C    1 
ATOM   2428 O O    . PHE B 1 8   ? -3.642  6.005   -24.907 1.00 34.77  ? 8   PHE B O    1 
ATOM   2429 C CB   . PHE B 1 8   ? -1.692  6.122   -22.343 1.00 43.40  ? 8   PHE B CB   1 
ATOM   2430 C CG   . PHE B 1 8   ? -0.701  6.711   -21.375 1.00 47.44  ? 8   PHE B CG   1 
ATOM   2431 C CD1  . PHE B 1 8   ? 0.617   6.337   -21.408 1.00 55.81  ? 8   PHE B CD1  1 
ATOM   2432 C CD2  . PHE B 1 8   ? -1.095  7.660   -20.462 1.00 47.37  ? 8   PHE B CD2  1 
ATOM   2433 C CE1  . PHE B 1 8   ? 1.520   6.884   -20.529 1.00 62.28  ? 8   PHE B CE1  1 
ATOM   2434 C CE2  . PHE B 1 8   ? -0.207  8.211   -19.591 1.00 52.44  ? 8   PHE B CE2  1 
ATOM   2435 C CZ   . PHE B 1 8   ? 1.105   7.824   -19.618 1.00 59.71  ? 8   PHE B CZ   1 
ATOM   2436 N N    . PRO B 1 9   ? -1.736  4.880   -25.275 1.00 42.41  ? 9   PRO B N    1 
ATOM   2437 C CA   . PRO B 1 9   ? -2.429  3.860   -26.083 1.00 39.73  ? 9   PRO B CA   1 
ATOM   2438 C C    . PRO B 1 9   ? -3.459  3.111   -25.235 1.00 37.02  ? 9   PRO B C    1 
ATOM   2439 O O    . PRO B 1 9   ? -3.181  2.688   -24.117 1.00 40.90  ? 9   PRO B O    1 
ATOM   2440 C CB   . PRO B 1 9   ? -1.288  2.943   -26.553 1.00 43.21  ? 9   PRO B CB   1 
ATOM   2441 C CG   . PRO B 1 9   ? -0.138  3.231   -25.625 1.00 48.41  ? 9   PRO B CG   1 
ATOM   2442 C CD   . PRO B 1 9   ? -0.285  4.649   -25.179 1.00 45.72  ? 9   PRO B CD   1 
ATOM   2443 N N    . SER B 1 10  ? -4.662  2.966   -25.769 1.00 37.85  ? 10  SER B N    1 
ATOM   2444 C CA   . SER B 1 10  ? -5.805  2.553   -24.972 1.00 37.64  ? 10  SER B CA   1 
ATOM   2445 C C    . SER B 1 10  ? -6.091  1.064   -25.050 1.00 41.73  ? 10  SER B C    1 
ATOM   2446 O O    . SER B 1 10  ? -7.101  0.612   -24.484 1.00 40.63  ? 10  SER B O    1 
ATOM   2447 C CB   . SER B 1 10  ? -7.033  3.346   -25.394 1.00 36.94  ? 10  SER B CB   1 
ATOM   2448 O OG   . SER B 1 10  ? -7.404  3.095   -26.743 1.00 40.59  ? 10  SER B OG   1 
ATOM   2449 N N    . GLY B 1 11  ? -5.220  0.285   -25.709 1.00 41.22  ? 11  GLY B N    1 
ATOM   2450 C CA   . GLY B 1 11  ? -5.484  -1.128  -25.922 1.00 37.35  ? 11  GLY B CA   1 
ATOM   2451 C C    . GLY B 1 11  ? -5.735  -1.934  -24.676 1.00 38.66  ? 11  GLY B C    1 
ATOM   2452 O O    . GLY B 1 11  ? -6.787  -2.565  -24.554 1.00 46.49  ? 11  GLY B O    1 
ATOM   2453 N N    . LYS B 1 12  ? -4.792  -1.909  -23.731 1.00 41.14  ? 12  LYS B N    1 
ATOM   2454 C CA   . LYS B 1 12  ? -4.930  -2.668  -22.492 1.00 40.85  ? 12  LYS B CA   1 
ATOM   2455 C C    . LYS B 1 12  ? -6.222  -2.325  -21.736 1.00 38.81  ? 12  LYS B C    1 
ATOM   2456 O O    . LYS B 1 12  ? -6.761  -3.161  -21.002 1.00 42.65  ? 12  LYS B O    1 
ATOM   2457 C CB   . LYS B 1 12  ? -3.705  -2.409  -21.604 1.00 44.60  ? 12  LYS B CB   1 
ATOM   2458 C CG   . LYS B 1 12  ? -2.485  -3.162  -22.004 1.00 45.15  ? 12  LYS B CG   1 
ATOM   2459 C CD   . LYS B 1 12  ? -1.297  -2.213  -22.217 1.00 57.23  ? 12  LYS B CD   1 
ATOM   2460 C CE   . LYS B 1 12  ? -1.263  -1.664  -23.685 1.00 61.75  ? 12  LYS B CE   1 
ATOM   2461 N NZ   . LYS B 1 12  ? -0.206  -0.605  -23.953 1.00 61.69  ? 12  LYS B NZ   1 
ATOM   2462 N N    . VAL B 1 13  ? -6.698  -1.098  -21.846 1.00 37.48  ? 13  VAL B N    1 
ATOM   2463 C CA   . VAL B 1 13  ? -7.933  -0.732  -21.167 1.00 43.48  ? 13  VAL B CA   1 
ATOM   2464 C C    . VAL B 1 13  ? -9.151  -1.223  -21.955 1.00 45.19  ? 13  VAL B C    1 
ATOM   2465 O O    . VAL B 1 13  ? -10.177 -1.582  -21.360 1.00 43.92  ? 13  VAL B O    1 
ATOM   2466 C CB   . VAL B 1 13  ? -7.989  0.788   -20.933 1.00 41.94  ? 13  VAL B CB   1 
ATOM   2467 C CG1  . VAL B 1 13  ? -9.317  1.181   -20.208 1.00 39.15  ? 13  VAL B CG1  1 
ATOM   2468 C CG2  . VAL B 1 13  ? -6.755  1.249   -20.138 1.00 36.82  ? 13  VAL B CG2  1 
ATOM   2469 N N    . GLU B 1 14  ? -9.075  -1.234  -23.290 1.00 41.61  ? 14  GLU B N    1 
ATOM   2470 C CA   . GLU B 1 14  ? -10.237 -1.618  -24.082 1.00 43.05  ? 14  GLU B CA   1 
ATOM   2471 C C    . GLU B 1 14  ? -10.724 -3.018  -23.710 1.00 42.67  ? 14  GLU B C    1 
ATOM   2472 O O    . GLU B 1 14  ? -11.925 -3.238  -23.520 1.00 43.37  ? 14  GLU B O    1 
ATOM   2473 C CB   . GLU B 1 14  ? -9.900  -1.557  -25.576 1.00 41.66  ? 14  GLU B CB   1 
ATOM   2474 C CG   . GLU B 1 14  ? -9.667  -0.151  -26.102 1.00 40.73  ? 14  GLU B CG   1 
ATOM   2475 C CD   . GLU B 1 14  ? -9.189  -0.141  -27.559 1.00 42.39  ? 14  GLU B CD   1 
ATOM   2476 O OE1  . GLU B 1 14  ? -9.918  -0.656  -28.423 1.00 49.79  ? 14  GLU B OE1  1 
ATOM   2477 O OE2  . GLU B 1 14  ? -8.101  0.381   -27.852 1.00 38.76  ? 14  GLU B OE2  1 
ATOM   2478 N N    . GLY B 1 15  ? -9.809  -3.965  -23.554 1.00 40.11  ? 15  GLY B N    1 
ATOM   2479 C CA   . GLY B 1 15  ? -10.215 -5.312  -23.193 1.00 46.71  ? 15  GLY B CA   1 
ATOM   2480 C C    . GLY B 1 15  ? -10.834 -5.441  -21.819 1.00 49.05  ? 15  GLY B C    1 
ATOM   2481 O O    . GLY B 1 15  ? -11.128 -6.557  -21.381 1.00 45.88  ? 15  GLY B O    1 
ATOM   2482 N N    . CYS B 1 16  ? -11.016 -4.328  -21.112 1.00 46.24  ? 16  CYS B N    1 
ATOM   2483 C CA   . CYS B 1 16  ? -11.542 -4.355  -19.754 1.00 43.28  ? 16  CYS B CA   1 
ATOM   2484 C C    . CYS B 1 16  ? -12.912 -3.697  -19.629 1.00 43.88  ? 16  CYS B C    1 
ATOM   2485 O O    . CYS B 1 16  ? -13.491 -3.720  -18.530 1.00 44.61  ? 16  CYS B O    1 
ATOM   2486 C CB   . CYS B 1 16  ? -10.561 -3.679  -18.783 1.00 46.77  ? 16  CYS B CB   1 
ATOM   2487 S SG   . CYS B 1 16  ? -8.887  -4.399  -18.645 1.00 51.11  ? 16  CYS B SG   1 
ATOM   2488 N N    . MET B 1 17  ? -13.451 -3.126  -20.706 1.00 38.29  ? 17  MET B N    1 
ATOM   2489 C CA   . MET B 1 17  ? -14.721 -2.414  -20.634 1.00 43.29  ? 17  MET B CA   1 
ATOM   2490 C C    . MET B 1 17  ? -15.899 -3.342  -20.923 1.00 48.14  ? 17  MET B C    1 
ATOM   2491 O O    . MET B 1 17  ? -16.002 -3.932  -22.006 1.00 50.80  ? 17  MET B O    1 
ATOM   2492 C CB   . MET B 1 17  ? -14.726 -1.224  -21.595 1.00 41.67  ? 17  MET B CB   1 
ATOM   2493 C CG   . MET B 1 17  ? -13.439 -0.446  -21.485 1.00 42.30  ? 17  MET B CG   1 
ATOM   2494 S SD   . MET B 1 17  ? -13.378 0.336   -19.844 1.00 43.44  ? 17  MET B SD   1 
ATOM   2495 C CE   . MET B 1 17  ? -15.104 0.817   -19.497 1.00 37.83  ? 17  MET B CE   1 
ATOM   2496 N N    . VAL B 1 18  ? -16.798 -3.440  -19.953 1.00 46.83  ? 18  VAL B N    1 
ATOM   2497 C CA   . VAL B 1 18  ? -18.047 -4.161  -20.100 1.00 50.06  ? 18  VAL B CA   1 
ATOM   2498 C C    . VAL B 1 18  ? -19.199 -3.177  -19.901 1.00 51.40  ? 18  VAL B C    1 
ATOM   2499 O O    . VAL B 1 18  ? -19.002 -1.996  -19.595 1.00 46.62  ? 18  VAL B O    1 
ATOM   2500 C CB   . VAL B 1 18  ? -18.147 -5.347  -19.123 1.00 50.36  ? 18  VAL B CB   1 
ATOM   2501 C CG1  . VAL B 1 18  ? -16.914 -6.218  -19.224 1.00 52.84  ? 18  VAL B CG1  1 
ATOM   2502 C CG2  . VAL B 1 18  ? -18.348 -4.864  -17.694 1.00 47.55  ? 18  VAL B CG2  1 
ATOM   2503 N N    . GLN B 1 19  ? -20.413 -3.668  -20.132 1.00 54.67  ? 19  GLN B N    1 
ATOM   2504 C CA   . GLN B 1 19  ? -21.622 -2.880  -19.920 1.00 52.20  ? 19  GLN B CA   1 
ATOM   2505 C C    . GLN B 1 19  ? -22.388 -3.493  -18.763 1.00 54.53  ? 19  GLN B C    1 
ATOM   2506 O O    . GLN B 1 19  ? -22.554 -4.717  -18.700 1.00 57.46  ? 19  GLN B O    1 
ATOM   2507 C CB   . GLN B 1 19  ? -22.494 -2.810  -21.176 1.00 55.52  ? 19  GLN B CB   1 
ATOM   2508 C CG   . GLN B 1 19  ? -23.297 -4.061  -21.455 1.00 66.61  ? 19  GLN B CG   1 
ATOM   2509 C CD   . GLN B 1 19  ? -24.615 -3.758  -22.159 1.00 71.82  ? 19  GLN B CD   1 
ATOM   2510 O OE1  . GLN B 1 19  ? -24.653 -2.947  -23.096 1.00 70.19  ? 19  GLN B OE1  1 
ATOM   2511 N NE2  . GLN B 1 19  ? -25.706 -4.412  -21.713 1.00 68.62  ? 19  GLN B NE2  1 
ATOM   2512 N N    . VAL B 1 20  ? -22.795 -2.664  -17.813 1.00 53.92  ? 20  VAL B N    1 
ATOM   2513 C CA   . VAL B 1 20  ? -23.533 -3.143  -16.658 1.00 50.87  ? 20  VAL B CA   1 
ATOM   2514 C C    . VAL B 1 20  ? -24.941 -2.588  -16.735 1.00 52.69  ? 20  VAL B C    1 
ATOM   2515 O O    . VAL B 1 20  ? -25.135 -1.383  -16.958 1.00 48.92  ? 20  VAL B O    1 
ATOM   2516 C CB   . VAL B 1 20  ? -22.851 -2.756  -15.340 1.00 50.34  ? 20  VAL B CB   1 
ATOM   2517 C CG1  . VAL B 1 20  ? -23.678 -3.235  -14.159 1.00 47.67  ? 20  VAL B CG1  1 
ATOM   2518 C CG2  . VAL B 1 20  ? -21.466 -3.347  -15.303 1.00 51.37  ? 20  VAL B CG2  1 
ATOM   2519 N N    . THR B 1 21  ? -25.922 -3.478  -16.582 1.00 55.24  ? 21  THR B N    1 
ATOM   2520 C CA   . THR B 1 21  ? -27.328 -3.114  -16.615 1.00 55.68  ? 21  THR B CA   1 
ATOM   2521 C C    . THR B 1 21  ? -28.007 -3.565  -15.333 1.00 54.71  ? 21  THR B C    1 
ATOM   2522 O O    . THR B 1 21  ? -27.903 -4.732  -14.941 1.00 55.89  ? 21  THR B O    1 
ATOM   2523 C CB   . THR B 1 21  ? -28.021 -3.737  -17.816 1.00 57.53  ? 21  THR B CB   1 
ATOM   2524 O OG1  . THR B 1 21  ? -27.179 -3.584  -18.965 1.00 57.32  ? 21  THR B OG1  1 
ATOM   2525 C CG2  . THR B 1 21  ? -29.360 -3.028  -18.052 1.00 57.32  ? 21  THR B CG2  1 
ATOM   2526 N N    . CYS B 1 22  ? -28.681 -2.629  -14.679 1.00 55.22  ? 22  CYS B N    1 
ATOM   2527 C CA   . CYS B 1 22  ? -29.518 -2.905  -13.521 1.00 58.36  ? 22  CYS B CA   1 
ATOM   2528 C C    . CYS B 1 22  ? -30.876 -2.265  -13.762 1.00 60.97  ? 22  CYS B C    1 
ATOM   2529 O O    . CYS B 1 22  ? -30.958 -1.044  -13.934 1.00 61.53  ? 22  CYS B O    1 
ATOM   2530 C CB   . CYS B 1 22  ? -28.881 -2.356  -12.246 1.00 55.40  ? 22  CYS B CB   1 
ATOM   2531 S SG   . CYS B 1 22  ? -29.719 -2.875  -10.797 1.00 62.24  ? 22  CYS B SG   1 
ATOM   2532 N N    . GLY B 1 23  ? -31.922 -3.087  -13.847 1.00 68.12  ? 23  GLY B N    1 
ATOM   2533 C CA   . GLY B 1 23  ? -33.247 -2.555  -14.148 1.00 64.69  ? 23  GLY B CA   1 
ATOM   2534 C C    . GLY B 1 23  ? -33.228 -1.853  -15.495 1.00 61.57  ? 23  GLY B C    1 
ATOM   2535 O O    . GLY B 1 23  ? -32.836 -2.434  -16.519 1.00 58.21  ? 23  GLY B O    1 
ATOM   2536 N N    . THR B 1 24  ? -33.592 -0.565  -15.494 1.00 62.13  ? 24  THR B N    1 
ATOM   2537 C CA   . THR B 1 24  ? -33.564 0.234   -16.713 1.00 68.27  ? 24  THR B CA   1 
ATOM   2538 C C    . THR B 1 24  ? -32.202 0.864   -17.000 1.00 66.04  ? 24  THR B C    1 
ATOM   2539 O O    . THR B 1 24  ? -31.945 1.250   -18.148 1.00 66.97  ? 24  THR B O    1 
ATOM   2540 C CB   . THR B 1 24  ? -34.604 1.360   -16.639 1.00 81.74  ? 24  THR B CB   1 
ATOM   2541 O OG1  . THR B 1 24  ? -34.837 1.869   -17.956 1.00 89.99  ? 24  THR B OG1  1 
ATOM   2542 C CG2  . THR B 1 24  ? -34.120 2.513   -15.741 1.00 78.03  ? 24  THR B CG2  1 
ATOM   2543 N N    . THR B 1 25  ? -31.312 0.942   -16.015 1.00 62.11  ? 25  THR B N    1 
ATOM   2544 C CA   . THR B 1 25  ? -30.066 1.683   -16.174 1.00 58.07  ? 25  THR B CA   1 
ATOM   2545 C C    . THR B 1 25  ? -28.966 0.813   -16.768 1.00 54.77  ? 25  THR B C    1 
ATOM   2546 O O    . THR B 1 25  ? -28.816 -0.358  -16.400 1.00 54.89  ? 25  THR B O    1 
ATOM   2547 C CB   . THR B 1 25  ? -29.602 2.247   -14.839 1.00 58.49  ? 25  THR B CB   1 
ATOM   2548 O OG1  . THR B 1 25  ? -30.580 3.180   -14.346 1.00 65.77  ? 25  THR B OG1  1 
ATOM   2549 C CG2  . THR B 1 25  ? -28.276 2.952   -15.023 1.00 53.21  ? 25  THR B CG2  1 
ATOM   2550 N N    . THR B 1 26  ? -28.213 1.387   -17.712 1.00 53.28  ? 26  THR B N    1 
ATOM   2551 C CA   . THR B 1 26  ? -27.025 0.750   -18.258 1.00 51.06  ? 26  THR B CA   1 
ATOM   2552 C C    . THR B 1 26  ? -25.876 1.741   -18.329 1.00 48.30  ? 26  THR B C    1 
ATOM   2553 O O    . THR B 1 26  ? -25.997 2.802   -18.945 1.00 47.26  ? 26  THR B O    1 
ATOM   2554 C CB   . THR B 1 26  ? -27.282 0.157   -19.653 1.00 52.78  ? 26  THR B CB   1 
ATOM   2555 O OG1  . THR B 1 26  ? -28.176 -0.962  -19.546 1.00 61.06  ? 26  THR B OG1  1 
ATOM   2556 C CG2  . THR B 1 26  ? -25.977 -0.310  -20.296 1.00 50.53  ? 26  THR B CG2  1 
ATOM   2557 N N    . LEU B 1 27  ? -24.741 1.365   -17.748 1.00 48.81  ? 27  LEU B N    1 
ATOM   2558 C CA   . LEU B 1 27  ? -23.525 2.156   -17.870 1.00 44.70  ? 27  LEU B CA   1 
ATOM   2559 C C    . LEU B 1 27  ? -22.329 1.216   -18.014 1.00 45.25  ? 27  LEU B C    1 
ATOM   2560 O O    . LEU B 1 27  ? -22.472 -0.017  -18.054 1.00 45.44  ? 27  LEU B O    1 
ATOM   2561 C CB   . LEU B 1 27  ? -23.388 3.102   -16.678 1.00 43.24  ? 27  LEU B CB   1 
ATOM   2562 C CG   . LEU B 1 27  ? -23.841 2.526   -15.338 1.00 44.12  ? 27  LEU B CG   1 
ATOM   2563 C CD1  . LEU B 1 27  ? -22.935 1.418   -14.917 1.00 43.59  ? 27  LEU B CD1  1 
ATOM   2564 C CD2  . LEU B 1 27  ? -23.879 3.601   -14.270 1.00 42.49  ? 27  LEU B CD2  1 
ATOM   2565 N N    . ASN B 1 28  ? -21.133 1.797   -18.042 1.00 39.58  ? 28  ASN B N    1 
ATOM   2566 C CA   . ASN B 1 28  ? -19.930 1.003   -18.265 1.00 41.09  ? 28  ASN B CA   1 
ATOM   2567 C C    . ASN B 1 28  ? -19.348 0.506   -16.954 1.00 41.56  ? 28  ASN B C    1 
ATOM   2568 O O    . ASN B 1 28  ? -19.577 1.085   -15.888 1.00 40.71  ? 28  ASN B O    1 
ATOM   2569 C CB   . ASN B 1 28  ? -18.894 1.814   -19.029 1.00 41.44  ? 28  ASN B CB   1 
ATOM   2570 C CG   . ASN B 1 28  ? -19.516 2.596   -20.176 1.00 44.18  ? 28  ASN B CG   1 
ATOM   2571 O OD1  . ASN B 1 28  ? -19.796 2.039   -21.240 1.00 50.18  ? 28  ASN B OD1  1 
ATOM   2572 N ND2  . ASN B 1 28  ? -19.752 3.889   -19.959 1.00 41.53  ? 28  ASN B ND2  1 
ATOM   2573 N N    . GLY B 1 29  ? -18.643 -0.623  -17.036 1.00 39.87  ? 29  GLY B N    1 
ATOM   2574 C CA   . GLY B 1 29  ? -17.937 -1.164  -15.894 1.00 39.82  ? 29  GLY B CA   1 
ATOM   2575 C C    . GLY B 1 29  ? -16.556 -1.629  -16.314 1.00 44.09  ? 29  GLY B C    1 
ATOM   2576 O O    . GLY B 1 29  ? -16.261 -1.759  -17.507 1.00 40.37  ? 29  GLY B O    1 
ATOM   2577 N N    . LEU B 1 30  ? -15.710 -1.880  -15.318 1.00 42.43  ? 30  LEU B N    1 
ATOM   2578 C CA   . LEU B 1 30  ? -14.312 -2.226  -15.549 1.00 44.82  ? 30  LEU B CA   1 
ATOM   2579 C C    . LEU B 1 30  ? -14.055 -3.634  -15.019 1.00 43.33  ? 30  LEU B C    1 
ATOM   2580 O O    . LEU B 1 30  ? -14.177 -3.885  -13.820 1.00 44.66  ? 30  LEU B O    1 
ATOM   2581 C CB   . LEU B 1 30  ? -13.387 -1.207  -14.876 1.00 46.60  ? 30  LEU B CB   1 
ATOM   2582 C CG   . LEU B 1 30  ? -11.863 -1.340  -15.054 1.00 42.25  ? 30  LEU B CG   1 
ATOM   2583 C CD1  . LEU B 1 30  ? -11.401 -0.620  -16.257 1.00 40.73  ? 30  LEU B CD1  1 
ATOM   2584 C CD2  . LEU B 1 30  ? -11.113 -0.845  -13.827 1.00 42.49  ? 30  LEU B CD2  1 
ATOM   2585 N N    . TRP B 1 31  ? -13.670 -4.545  -15.914 1.00 45.98  ? 31  TRP B N    1 
ATOM   2586 C CA   . TRP B 1 31  ? -13.596 -5.976  -15.610 1.00 46.32  ? 31  TRP B CA   1 
ATOM   2587 C C    . TRP B 1 31  ? -12.137 -6.375  -15.409 1.00 46.65  ? 31  TRP B C    1 
ATOM   2588 O O    . TRP B 1 31  ? -11.361 -6.458  -16.372 1.00 46.09  ? 31  TRP B O    1 
ATOM   2589 C CB   . TRP B 1 31  ? -14.263 -6.780  -16.729 1.00 48.72  ? 31  TRP B CB   1 
ATOM   2590 C CG   . TRP B 1 31  ? -14.323 -8.300  -16.532 1.00 54.59  ? 31  TRP B CG   1 
ATOM   2591 C CD1  . TRP B 1 31  ? -14.254 -8.997  -15.357 1.00 55.55  ? 31  TRP B CD1  1 
ATOM   2592 C CD2  . TRP B 1 31  ? -14.450 -9.280  -17.570 1.00 57.45  ? 31  TRP B CD2  1 
ATOM   2593 N NE1  . TRP B 1 31  ? -14.340 -10.359 -15.599 1.00 57.41  ? 31  TRP B NE1  1 
ATOM   2594 C CE2  . TRP B 1 31  ? -14.458 -10.552 -16.954 1.00 62.12  ? 31  TRP B CE2  1 
ATOM   2595 C CE3  . TRP B 1 31  ? -14.563 -9.204  -18.962 1.00 54.81  ? 31  TRP B CE3  1 
ATOM   2596 C CZ2  . TRP B 1 31  ? -14.556 -11.734 -17.691 1.00 62.72  ? 31  TRP B CZ2  1 
ATOM   2597 C CZ3  . TRP B 1 31  ? -14.673 -10.374 -19.680 1.00 59.85  ? 31  TRP B CZ3  1 
ATOM   2598 C CH2  . TRP B 1 31  ? -14.664 -11.623 -19.045 1.00 58.40  ? 31  TRP B CH2  1 
ATOM   2599 N N    . LEU B 1 32  ? -11.779 -6.655  -14.162 1.00 48.27  ? 32  LEU B N    1 
ATOM   2600 C CA   . LEU B 1 32  ? -10.436 -7.063  -13.778 1.00 50.38  ? 32  LEU B CA   1 
ATOM   2601 C C    . LEU B 1 32  ? -10.530 -8.312  -12.918 1.00 54.53  ? 32  LEU B C    1 
ATOM   2602 O O    . LEU B 1 32  ? -11.231 -8.320  -11.891 1.00 52.94  ? 32  LEU B O    1 
ATOM   2603 C CB   . LEU B 1 32  ? -9.714  -5.933  -13.028 1.00 49.19  ? 32  LEU B CB   1 
ATOM   2604 C CG   . LEU B 1 32  ? -9.608  -4.618  -13.835 1.00 49.09  ? 32  LEU B CG   1 
ATOM   2605 C CD1  . LEU B 1 32  ? -9.352  -3.432  -12.923 1.00 46.90  ? 32  LEU B CD1  1 
ATOM   2606 C CD2  . LEU B 1 32  ? -8.525  -4.708  -14.894 1.00 47.44  ? 32  LEU B CD2  1 
ATOM   2607 N N    . ASP B 1 33  ? -9.815  -9.362  -13.330 1.00 53.48  ? 33  ASP B N    1 
ATOM   2608 C CA   . ASP B 1 33  ? -9.910  -10.674 -12.684 1.00 58.35  ? 33  ASP B CA   1 
ATOM   2609 C C    . ASP B 1 33  ? -11.397 -11.031 -12.628 1.00 56.17  ? 33  ASP B C    1 
ATOM   2610 O O    . ASP B 1 33  ? -12.095 -10.860 -13.638 1.00 55.53  ? 33  ASP B O    1 
ATOM   2611 C CB   . ASP B 1 33  ? -9.189  -10.641 -11.334 1.00 61.56  ? 33  ASP B CB   1 
ATOM   2612 C CG   . ASP B 1 33  ? -7.737  -10.202 -11.456 1.00 64.49  ? 33  ASP B CG   1 
ATOM   2613 O OD1  . ASP B 1 33  ? -6.988  -10.834 -12.232 1.00 71.06  ? 33  ASP B OD1  1 
ATOM   2614 O OD2  . ASP B 1 33  ? -7.346  -9.222  -10.783 1.00 66.47  ? 33  ASP B OD2  1 
ATOM   2615 N N    . ASP B 1 34  ? -11.910 -11.525 -11.503 1.00 57.96  ? 34  ASP B N    1 
ATOM   2616 C CA   . ASP B 1 34  ? -13.311 -11.908 -11.382 1.00 62.93  ? 34  ASP B CA   1 
ATOM   2617 C C    . ASP B 1 34  ? -14.172 -10.816 -10.755 1.00 59.80  ? 34  ASP B C    1 
ATOM   2618 O O    . ASP B 1 34  ? -15.199 -11.128 -10.148 1.00 59.25  ? 34  ASP B O    1 
ATOM   2619 C CB   . ASP B 1 34  ? -13.466 -13.226 -10.604 1.00 63.00  ? 34  ASP B CB   1 
ATOM   2620 C CG   . ASP B 1 34  ? -12.867 -13.194 -9.187  1.00 65.76  ? 34  ASP B CG   1 
ATOM   2621 O OD1  . ASP B 1 34  ? -12.021 -12.310 -8.912  1.00 63.54  ? 34  ASP B OD1  1 
ATOM   2622 O OD2  . ASP B 1 34  ? -13.234 -14.088 -8.362  1.00 65.35  ? 34  ASP B OD2  1 
ATOM   2623 N N    . VAL B 1 35  ? -13.813 -9.536  -10.931 1.00 58.83  ? 35  VAL B N    1 
ATOM   2624 C CA   . VAL B 1 35  ? -14.560 -8.431  -10.332 1.00 53.81  ? 35  VAL B CA   1 
ATOM   2625 C C    . VAL B 1 35  ? -14.853 -7.399  -11.401 1.00 51.24  ? 35  VAL B C    1 
ATOM   2626 O O    . VAL B 1 35  ? -13.979 -7.058  -12.204 1.00 53.22  ? 35  VAL B O    1 
ATOM   2627 C CB   . VAL B 1 35  ? -13.813 -7.768  -9.154  1.00 54.24  ? 35  VAL B CB   1 
ATOM   2628 C CG1  . VAL B 1 35  ? -14.636 -6.603  -8.611  1.00 53.01  ? 35  VAL B CG1  1 
ATOM   2629 C CG2  . VAL B 1 35  ? -13.497 -8.778  -8.020  1.00 56.99  ? 35  VAL B CG2  1 
ATOM   2630 N N    . VAL B 1 36  ? -16.083 -6.893  -11.417 1.00 50.39  ? 36  VAL B N    1 
ATOM   2631 C CA   . VAL B 1 36  ? -16.465 -5.798  -12.299 1.00 48.09  ? 36  VAL B CA   1 
ATOM   2632 C C    . VAL B 1 36  ? -16.711 -4.563  -11.438 1.00 47.33  ? 36  VAL B C    1 
ATOM   2633 O O    . VAL B 1 36  ? -17.418 -4.635  -10.422 1.00 48.32  ? 36  VAL B O    1 
ATOM   2634 C CB   . VAL B 1 36  ? -17.697 -6.148  -13.153 1.00 47.77  ? 36  VAL B CB   1 
ATOM   2635 C CG1  . VAL B 1 36  ? -18.188 -4.910  -13.968 1.00 45.52  ? 36  VAL B CG1  1 
ATOM   2636 C CG2  . VAL B 1 36  ? -17.341 -7.251  -14.105 1.00 49.99  ? 36  VAL B CG2  1 
ATOM   2637 N N    . TYR B 1 37  ? -16.131 -3.437  -11.845 1.00 45.68  ? 37  TYR B N    1 
ATOM   2638 C CA   . TYR B 1 37  ? -16.207 -2.186  -11.100 1.00 44.97  ? 37  TYR B CA   1 
ATOM   2639 C C    . TYR B 1 37  ? -17.084 -1.216  -11.862 1.00 43.20  ? 37  TYR B C    1 
ATOM   2640 O O    . TYR B 1 37  ? -16.838 -0.983  -13.044 1.00 41.95  ? 37  TYR B O    1 
ATOM   2641 C CB   . TYR B 1 37  ? -14.815 -1.576  -10.895 1.00 44.74  ? 37  TYR B CB   1 
ATOM   2642 C CG   . TYR B 1 37  ? -13.884 -2.494  -10.146 1.00 46.65  ? 37  TYR B CG   1 
ATOM   2643 C CD1  . TYR B 1 37  ? -13.290 -3.587  -10.774 1.00 47.40  ? 37  TYR B CD1  1 
ATOM   2644 C CD2  . TYR B 1 37  ? -13.646 -2.310  -8.793  1.00 47.88  ? 37  TYR B CD2  1 
ATOM   2645 C CE1  . TYR B 1 37  ? -12.459 -4.443  -10.081 1.00 49.35  ? 37  TYR B CE1  1 
ATOM   2646 C CE2  . TYR B 1 37  ? -12.811 -3.163  -8.095  1.00 49.82  ? 37  TYR B CE2  1 
ATOM   2647 C CZ   . TYR B 1 37  ? -12.219 -4.228  -8.745  1.00 50.57  ? 37  TYR B CZ   1 
ATOM   2648 O OH   . TYR B 1 37  ? -11.393 -5.087  -8.046  1.00 52.69  ? 37  TYR B OH   1 
ATOM   2649 N N    . CYS B 1 38  ? -18.090 -0.643  -11.198 1.00 43.18  ? 38  CYS B N    1 
ATOM   2650 C CA   . CYS B 1 38  ? -18.944 0.318   -11.883 1.00 41.68  ? 38  CYS B CA   1 
ATOM   2651 C C    . CYS B 1 38  ? -19.529 1.319   -10.893 1.00 41.64  ? 38  CYS B C    1 
ATOM   2652 O O    . CYS B 1 38  ? -19.551 1.073   -9.682  1.00 42.91  ? 38  CYS B O    1 
ATOM   2653 C CB   . CYS B 1 38  ? -20.068 -0.379  -12.664 1.00 41.93  ? 38  CYS B CB   1 
ATOM   2654 S SG   . CYS B 1 38  ? -21.453 -0.886  -11.630 1.00 45.19  ? 38  CYS B SG   1 
ATOM   2655 N N    . PRO B 1 39  ? -20.014 2.455   -11.381 1.00 40.31  ? 39  PRO B N    1 
ATOM   2656 C CA   . PRO B 1 39  ? -20.598 3.456   -10.482 1.00 40.32  ? 39  PRO B CA   1 
ATOM   2657 C C    . PRO B 1 39  ? -21.841 2.909   -9.792  1.00 42.01  ? 39  PRO B C    1 
ATOM   2658 O O    . PRO B 1 39  ? -22.674 2.226   -10.405 1.00 42.24  ? 39  PRO B O    1 
ATOM   2659 C CB   . PRO B 1 39  ? -20.941 4.621   -11.418 1.00 38.76  ? 39  PRO B CB   1 
ATOM   2660 C CG   . PRO B 1 39  ? -20.139 4.331   -12.730 1.00 38.06  ? 39  PRO B CG   1 
ATOM   2661 C CD   . PRO B 1 39  ? -20.067 2.849   -12.800 1.00 38.86  ? 39  PRO B CD   1 
ATOM   2662 N N    . ARG B 1 40  ? -21.951 3.187   -8.496  1.00 42.36  ? 40  ARG B N    1 
ATOM   2663 C CA   . ARG B 1 40  ? -23.047 2.612   -7.742  1.00 43.65  ? 40  ARG B CA   1 
ATOM   2664 C C    . ARG B 1 40  ? -24.405 3.127   -8.210  1.00 43.14  ? 40  ARG B C    1 
ATOM   2665 O O    . ARG B 1 40  ? -25.421 2.465   -7.975  1.00 44.18  ? 40  ARG B O    1 
ATOM   2666 C CB   . ARG B 1 40  ? -22.855 2.859   -6.230  1.00 44.75  ? 40  ARG B CB   1 
ATOM   2667 C CG   . ARG B 1 40  ? -23.073 4.298   -5.734  1.00 44.10  ? 40  ARG B CG   1 
ATOM   2668 C CD   . ARG B 1 40  ? -23.095 4.337   -4.220  1.00 45.47  ? 40  ARG B CD   1 
ATOM   2669 N NE   . ARG B 1 40  ? -23.068 5.685   -3.662  1.00 45.03  ? 40  ARG B NE   1 
ATOM   2670 C CZ   . ARG B 1 40  ? -22.965 5.929   -2.359  1.00 46.12  ? 40  ARG B CZ   1 
ATOM   2671 N NH1  . ARG B 1 40  ? -22.935 4.948   -1.466  1.00 47.69  ? 40  ARG B NH1  1 
ATOM   2672 N NH2  . ARG B 1 40  ? -22.873 7.186   -1.941  1.00 45.73  ? 40  ARG B NH2  1 
ATOM   2673 N N    . HIS B 1 41  ? -24.462 4.263   -8.885  1.00 43.48  ? 41  HIS B N    1 
ATOM   2674 C CA   . HIS B 1 41  ? -25.779 4.790   -9.200  1.00 46.20  ? 41  HIS B CA   1 
ATOM   2675 C C    . HIS B 1 41  ? -26.457 4.036   -10.332 1.00 45.85  ? 41  HIS B C    1 
ATOM   2676 O O    . HIS B 1 41  ? -27.581 4.398   -10.695 1.00 45.74  ? 41  HIS B O    1 
ATOM   2677 C CB   . HIS B 1 41  ? -25.714 6.295   -9.501  1.00 43.00  ? 41  HIS B CB   1 
ATOM   2678 C CG   . HIS B 1 41  ? -25.094 6.648   -10.810 1.00 45.07  ? 41  HIS B CG   1 
ATOM   2679 N ND1  . HIS B 1 41  ? -25.728 6.444   -12.018 1.00 49.62  ? 41  HIS B ND1  1 
ATOM   2680 C CD2  . HIS B 1 41  ? -23.895 7.207   -11.104 1.00 45.83  ? 41  HIS B CD2  1 
ATOM   2681 C CE1  . HIS B 1 41  ? -24.953 6.876   -12.998 1.00 46.50  ? 41  HIS B CE1  1 
ATOM   2682 N NE2  . HIS B 1 41  ? -23.839 7.350   -12.471 1.00 47.74  ? 41  HIS B NE2  1 
ATOM   2683 N N    . VAL B 1 42  ? -25.846 2.962   -10.837 1.00 41.69  ? 42  VAL B N    1 
ATOM   2684 C CA   . VAL B 1 42  ? -26.572 2.065   -11.727 1.00 50.04  ? 42  VAL B CA   1 
ATOM   2685 C C    . VAL B 1 42  ? -27.747 1.394   -11.006 1.00 50.92  ? 42  VAL B C    1 
ATOM   2686 O O    . VAL B 1 42  ? -28.692 0.943   -11.657 1.00 51.52  ? 42  VAL B O    1 
ATOM   2687 C CB   . VAL B 1 42  ? -25.617 1.019   -12.328 1.00 42.20  ? 42  VAL B CB   1 
ATOM   2688 C CG1  . VAL B 1 42  ? -25.151 0.042   -11.258 1.00 43.73  ? 42  VAL B CG1  1 
ATOM   2689 C CG2  . VAL B 1 42  ? -26.308 0.266   -13.456 1.00 48.73  ? 42  VAL B CG2  1 
ATOM   2690 N N    . ILE B 1 43  ? -27.714 1.356   -9.673  1.00 46.78  ? 43  ILE B N    1 
ATOM   2691 C CA   . ILE B 1 43  ? -28.801 0.854   -8.836  1.00 50.50  ? 43  ILE B CA   1 
ATOM   2692 C C    . ILE B 1 43  ? -30.049 1.740   -8.868  1.00 51.95  ? 43  ILE B C    1 
ATOM   2693 O O    . ILE B 1 43  ? -31.123 1.310   -8.436  1.00 51.25  ? 43  ILE B O    1 
ATOM   2694 C CB   . ILE B 1 43  ? -28.268 0.684   -7.397  1.00 48.66  ? 43  ILE B CB   1 
ATOM   2695 C CG1  . ILE B 1 43  ? -27.753 -0.732  -7.172  1.00 52.24  ? 43  ILE B CG1  1 
ATOM   2696 C CG2  . ILE B 1 43  ? -29.249 1.097   -6.366  1.00 52.26  ? 43  ILE B CG2  1 
ATOM   2697 C CD1  . ILE B 1 43  ? -26.917 -1.216  -8.246  1.00 53.97  ? 43  ILE B CD1  1 
ATOM   2698 N N    . CYS B 1 44  ? -29.940 2.975   -9.322  1.00 50.22  ? 44  CYS B N    1 
ATOM   2699 C CA   . CYS B 1 44  ? -30.995 3.950   -9.120  1.00 57.99  ? 44  CYS B CA   1 
ATOM   2700 C C    . CYS B 1 44  ? -31.847 4.089   -10.373 1.00 66.34  ? 44  CYS B C    1 
ATOM   2701 O O    . CYS B 1 44  ? -31.356 3.978   -11.501 1.00 62.69  ? 44  CYS B O    1 
ATOM   2702 C CB   . CYS B 1 44  ? -30.417 5.311   -8.735  1.00 56.98  ? 44  CYS B CB   1 
ATOM   2703 S SG   . CYS B 1 44  ? -29.411 5.284   -7.231  1.00 48.79  ? 44  CYS B SG   1 
ATOM   2704 N N    . THR B 1 45  ? -33.129 4.368   -10.152 1.00 73.25  ? 45  THR B N    1 
ATOM   2705 C CA   . THR B 1 45  ? -34.084 4.636   -11.215 1.00 80.83  ? 45  THR B CA   1 
ATOM   2706 C C    . THR B 1 45  ? -34.061 6.124   -11.552 1.00 85.47  ? 45  THR B C    1 
ATOM   2707 O O    . THR B 1 45  ? -33.202 6.877   -11.088 1.00 85.01  ? 45  THR B O    1 
ATOM   2708 C CB   . THR B 1 45  ? -35.480 4.192   -10.807 1.00 78.90  ? 45  THR B CB   1 
ATOM   2709 O OG1  . THR B 1 45  ? -36.001 5.133   -9.865  1.00 85.23  ? 45  THR B OG1  1 
ATOM   2710 C CG2  . THR B 1 45  ? -35.429 2.819   -10.174 1.00 75.50  ? 45  THR B CG2  1 
ATOM   2711 N N    . SER B 1 46  ? -35.033 6.569   -12.349 1.00 93.62  ? 46  SER B N    1 
ATOM   2712 C CA   . SER B 1 46  ? -35.097 7.982   -12.706 1.00 96.19  ? 46  SER B CA   1 
ATOM   2713 C C    . SER B 1 46  ? -35.337 8.861   -11.476 1.00 97.02  ? 46  SER B C    1 
ATOM   2714 O O    . SER B 1 46  ? -34.751 9.945   -11.355 1.00 92.35  ? 46  SER B O    1 
ATOM   2715 C CB   . SER B 1 46  ? -36.174 8.196   -13.766 1.00 91.97  ? 46  SER B CB   1 
ATOM   2716 O OG   . SER B 1 46  ? -36.255 9.561   -14.122 1.00 96.85  ? 46  SER B OG   1 
ATOM   2717 N N    . GLU B 1 47  ? -36.201 8.418   -10.556 1.00 94.21  ? 47  GLU B N    1 
ATOM   2718 C CA   . GLU B 1 47  ? -36.521 9.212   -9.374  1.00 92.72  ? 47  GLU B CA   1 
ATOM   2719 C C    . GLU B 1 47  ? -35.569 8.976   -8.211  1.00 85.65  ? 47  GLU B C    1 
ATOM   2720 O O    . GLU B 1 47  ? -35.317 9.911   -7.445  1.00 84.41  ? 47  GLU B O    1 
ATOM   2721 C CB   . GLU B 1 47  ? -37.954 8.947   -8.895  1.00 100.35 ? 47  GLU B CB   1 
ATOM   2722 C CG   . GLU B 1 47  ? -38.213 7.548   -8.365  1.00 101.24 ? 47  GLU B CG   1 
ATOM   2723 C CD   . GLU B 1 47  ? -38.833 6.637   -9.414  1.00 108.17 ? 47  GLU B CD   1 
ATOM   2724 O OE1  . GLU B 1 47  ? -38.941 7.069   -10.585 1.00 107.41 ? 47  GLU B OE1  1 
ATOM   2725 O OE2  . GLU B 1 47  ? -39.214 5.494   -9.070  1.00 107.76 ? 47  GLU B OE2  1 
ATOM   2726 N N    . ASP B 1 48  ? -35.048 7.754   -8.041  1.00 83.09  ? 48  ASP B N    1 
ATOM   2727 C CA   . ASP B 1 48  ? -34.144 7.481   -6.920  1.00 76.96  ? 48  ASP B CA   1 
ATOM   2728 C C    . ASP B 1 48  ? -33.039 8.532   -6.787  1.00 68.55  ? 48  ASP B C    1 
ATOM   2729 O O    . ASP B 1 48  ? -32.582 8.815   -5.666  1.00 61.08  ? 48  ASP B O    1 
ATOM   2730 C CB   . ASP B 1 48  ? -33.517 6.087   -7.073  1.00 76.79  ? 48  ASP B CB   1 
ATOM   2731 C CG   . ASP B 1 48  ? -34.468 4.950   -6.679  1.00 78.23  ? 48  ASP B CG   1 
ATOM   2732 O OD1  . ASP B 1 48  ? -34.369 3.857   -7.303  1.00 76.13  ? 48  ASP B OD1  1 
ATOM   2733 O OD2  . ASP B 1 48  ? -35.279 5.133   -5.732  1.00 77.12  ? 48  ASP B OD2  1 
ATOM   2734 N N    . MET B 1 49  ? -32.664 9.179   -7.902  1.00 73.54  ? 49  MET B N    1 
ATOM   2735 C CA   . MET B 1 49  ? -31.457 10.004  -7.979  1.00 64.81  ? 49  MET B CA   1 
ATOM   2736 C C    . MET B 1 49  ? -31.565 11.273  -7.137  1.00 61.37  ? 49  MET B C    1 
ATOM   2737 O O    . MET B 1 49  ? -30.536 11.827  -6.747  1.00 55.43  ? 49  MET B O    1 
ATOM   2738 C CB   . MET B 1 49  ? -31.160 10.385  -9.438  1.00 68.23  ? 49  MET B CB   1 
ATOM   2739 C CG   . MET B 1 49  ? -30.561 9.282   -10.337 1.00 69.24  ? 49  MET B CG   1 
ATOM   2740 S SD   . MET B 1 49  ? -29.047 8.497   -9.716  1.00 73.17  ? 49  MET B SD   1 
ATOM   2741 C CE   . MET B 1 49  ? -28.273 9.817   -8.783  1.00 56.14  ? 49  MET B CE   1 
ATOM   2742 N N    . LEU B 1 50  ? -32.778 11.741  -6.838  1.00 65.56  ? 50  LEU B N    1 
ATOM   2743 C CA   . LEU B 1 50  ? -32.925 13.015  -6.142  1.00 65.78  ? 50  LEU B CA   1 
ATOM   2744 C C    . LEU B 1 50  ? -32.149 13.015  -4.822  1.00 65.45  ? 50  LEU B C    1 
ATOM   2745 O O    . LEU B 1 50  ? -31.421 13.965  -4.521  1.00 66.72  ? 50  LEU B O    1 
ATOM   2746 C CB   . LEU B 1 50  ? -34.412 13.320  -5.940  1.00 70.52  ? 50  LEU B CB   1 
ATOM   2747 C CG   . LEU B 1 50  ? -34.786 14.790  -5.746  1.00 80.05  ? 50  LEU B CG   1 
ATOM   2748 C CD1  . LEU B 1 50  ? -34.321 15.238  -4.394  1.00 79.27  ? 50  LEU B CD1  1 
ATOM   2749 C CD2  . LEU B 1 50  ? -34.174 15.639  -6.836  1.00 79.27  ? 50  LEU B CD2  1 
ATOM   2750 N N    . ASN B 1 51  ? -32.280 11.962  -4.027  1.00 65.28  ? 51  ASN B N    1 
ATOM   2751 C CA   . ASN B 1 51  ? -31.468 11.791  -2.823  1.00 64.54  ? 51  ASN B CA   1 
ATOM   2752 C C    . ASN B 1 51  ? -31.517 10.318  -2.429  1.00 57.56  ? 51  ASN B C    1 
ATOM   2753 O O    . ASN B 1 51  ? -32.279 9.923   -1.536  1.00 56.04  ? 51  ASN B O    1 
ATOM   2754 C CB   . ASN B 1 51  ? -31.905 12.691  -1.666  1.00 70.72  ? 51  ASN B CB   1 
ATOM   2755 C CG   . ASN B 1 51  ? -33.401 12.832  -1.567  1.00 81.45  ? 51  ASN B CG   1 
ATOM   2756 O OD1  . ASN B 1 51  ? -34.145 11.949  -1.996  1.00 79.39  ? 51  ASN B OD1  1 
ATOM   2757 N ND2  . ASN B 1 51  ? -33.858 13.925  -0.940  1.00 85.17  ? 51  ASN B ND2  1 
ATOM   2758 N N    . PRO B 1 52  ? -30.721 9.470   -3.068  1.00 56.32  ? 52  PRO B N    1 
ATOM   2759 C CA   . PRO B 1 52  ? -30.889 8.034   -2.851  1.00 52.18  ? 52  PRO B CA   1 
ATOM   2760 C C    . PRO B 1 52  ? -30.331 7.610   -1.509  1.00 50.42  ? 52  PRO B C    1 
ATOM   2761 O O    . PRO B 1 52  ? -29.353 8.162   -1.007  1.00 51.11  ? 52  PRO B O    1 
ATOM   2762 C CB   . PRO B 1 52  ? -30.124 7.411   -4.024  1.00 55.23  ? 52  PRO B CB   1 
ATOM   2763 C CG   . PRO B 1 52  ? -29.037 8.417   -4.356  1.00 52.66  ? 52  PRO B CG   1 
ATOM   2764 C CD   . PRO B 1 52  ? -29.632 9.780   -4.019  1.00 57.20  ? 52  PRO B CD   1 
ATOM   2765 N N    . ASN B 1 53  ? -31.002 6.662   -0.892  1.00 49.25  ? 53  ASN B N    1 
ATOM   2766 C CA   . ASN B 1 53  ? -30.384 5.917   0.195   1.00 53.05  ? 53  ASN B CA   1 
ATOM   2767 C C    . ASN B 1 53  ? -29.791 4.659   -0.438  1.00 55.66  ? 53  ASN B C    1 
ATOM   2768 O O    . ASN B 1 53  ? -30.495 3.667   -0.653  1.00 55.38  ? 53  ASN B O    1 
ATOM   2769 C CB   . ASN B 1 53  ? -31.398 5.607   1.286   1.00 52.17  ? 53  ASN B CB   1 
ATOM   2770 C CG   . ASN B 1 53  ? -30.754 5.052   2.532   1.00 53.49  ? 53  ASN B CG   1 
ATOM   2771 O OD1  . ASN B 1 53  ? -29.873 4.186   2.461   1.00 56.65  ? 53  ASN B OD1  1 
ATOM   2772 N ND2  . ASN B 1 53  ? -31.182 5.549   3.691   1.00 54.43  ? 53  ASN B ND2  1 
ATOM   2773 N N    . TYR B 1 54  ? -28.486 4.693   -0.736  1.00 49.76  ? 54  TYR B N    1 
ATOM   2774 C CA   . TYR B 1 54  ? -27.875 3.605   -1.495  1.00 49.72  ? 54  TYR B CA   1 
ATOM   2775 C C    . TYR B 1 54  ? -27.885 2.286   -0.720  1.00 54.82  ? 54  TYR B C    1 
ATOM   2776 O O    . TYR B 1 54  ? -28.191 1.232   -1.285  1.00 57.34  ? 54  TYR B O    1 
ATOM   2777 C CB   . TYR B 1 54  ? -26.454 3.998   -1.895  1.00 48.58  ? 54  TYR B CB   1 
ATOM   2778 C CG   . TYR B 1 54  ? -26.412 4.950   -3.080  1.00 46.73  ? 54  TYR B CG   1 
ATOM   2779 C CD1  . TYR B 1 54  ? -26.702 4.500   -4.358  1.00 46.02  ? 54  TYR B CD1  1 
ATOM   2780 C CD2  . TYR B 1 54  ? -26.119 6.306   -2.917  1.00 45.85  ? 54  TYR B CD2  1 
ATOM   2781 C CE1  . TYR B 1 54  ? -26.679 5.352   -5.443  1.00 44.45  ? 54  TYR B CE1  1 
ATOM   2782 C CE2  . TYR B 1 54  ? -26.082 7.174   -4.028  1.00 44.30  ? 54  TYR B CE2  1 
ATOM   2783 C CZ   . TYR B 1 54  ? -26.367 6.683   -5.275  1.00 43.61  ? 54  TYR B CZ   1 
ATOM   2784 O OH   . TYR B 1 54  ? -26.347 7.511   -6.377  1.00 42.20  ? 54  TYR B OH   1 
ATOM   2785 N N    . GLU B 1 55  ? -27.552 2.311   0.569   1.00 55.02  ? 55  GLU B N    1 
ATOM   2786 C CA   . GLU B 1 55  ? -27.580 1.090   1.362   1.00 58.48  ? 55  GLU B CA   1 
ATOM   2787 C C    . GLU B 1 55  ? -28.941 0.419   1.255   1.00 56.62  ? 55  GLU B C    1 
ATOM   2788 O O    . GLU B 1 55  ? -29.046 -0.733  0.823   1.00 56.65  ? 55  GLU B O    1 
ATOM   2789 C CB   . GLU B 1 55  ? -27.249 1.379   2.832   1.00 57.48  ? 55  GLU B CB   1 
ATOM   2790 C CG   . GLU B 1 55  ? -25.939 2.108   3.029   1.00 68.39  ? 55  GLU B CG   1 
ATOM   2791 C CD   . GLU B 1 55  ? -25.929 3.515   2.411   1.00 74.20  ? 55  GLU B CD   1 
ATOM   2792 O OE1  . GLU B 1 55  ? -26.905 3.888   1.708   1.00 70.28  ? 55  GLU B OE1  1 
ATOM   2793 O OE2  . GLU B 1 55  ? -24.914 4.224   2.580   1.00 77.38  ? 55  GLU B OE2  1 
ATOM   2794 N N    . ASP B 1 56  ? -30.001 1.156   1.602   1.00 56.33  ? 56  ASP B N    1 
ATOM   2795 C CA   . ASP B 1 56  ? -31.363 0.641   1.449   1.00 59.75  ? 56  ASP B CA   1 
ATOM   2796 C C    . ASP B 1 56  ? -31.630 0.189   0.018   1.00 59.35  ? 56  ASP B C    1 
ATOM   2797 O O    . ASP B 1 56  ? -32.315 -0.815  -0.208  1.00 60.53  ? 56  ASP B O    1 
ATOM   2798 C CB   . ASP B 1 56  ? -32.397 1.697   1.854   1.00 57.94  ? 56  ASP B CB   1 
ATOM   2799 C CG   . ASP B 1 56  ? -32.457 1.940   3.339   1.00 57.90  ? 56  ASP B CG   1 
ATOM   2800 O OD1  . ASP B 1 56  ? -31.684 1.324   4.118   1.00 58.91  ? 56  ASP B OD1  1 
ATOM   2801 O OD2  . ASP B 1 56  ? -33.307 2.776   3.728   1.00 62.76  ? 56  ASP B OD2  1 
ATOM   2802 N N    . LEU B 1 57  ? -31.140 0.948   -0.964  1.00 54.11  ? 57  LEU B N    1 
ATOM   2803 C CA   . LEU B 1 57  ? -31.487 0.657   -2.346  1.00 56.43  ? 57  LEU B CA   1 
ATOM   2804 C C    . LEU B 1 57  ? -30.796 -0.617  -2.833  1.00 60.70  ? 57  LEU B C    1 
ATOM   2805 O O    . LEU B 1 57  ? -31.378 -1.395  -3.597  1.00 61.17  ? 57  LEU B O    1 
ATOM   2806 C CB   . LEU B 1 57  ? -31.142 1.854   -3.241  1.00 59.40  ? 57  LEU B CB   1 
ATOM   2807 C CG   . LEU B 1 57  ? -32.254 2.897   -3.521  1.00 62.79  ? 57  LEU B CG   1 
ATOM   2808 C CD1  . LEU B 1 57  ? -31.761 3.996   -4.468  1.00 58.08  ? 57  LEU B CD1  1 
ATOM   2809 C CD2  . LEU B 1 57  ? -33.524 2.259   -4.082  1.00 59.90  ? 57  LEU B CD2  1 
ATOM   2810 N N    . LEU B 1 58  ? -29.537 -0.819  -2.436  1.00 61.17  ? 58  LEU B N    1 
ATOM   2811 C CA   . LEU B 1 58  ? -28.812 -2.047  -2.757  1.00 60.74  ? 58  LEU B CA   1 
ATOM   2812 C C    . LEU B 1 58  ? -29.331 -3.238  -1.947  1.00 58.11  ? 58  LEU B C    1 
ATOM   2813 O O    . LEU B 1 58  ? -29.203 -4.391  -2.373  1.00 58.11  ? 58  LEU B O    1 
ATOM   2814 C CB   . LEU B 1 58  ? -27.318 -1.841  -2.505  1.00 54.02  ? 58  LEU B CB   1 
ATOM   2815 C CG   . LEU B 1 58  ? -26.367 -2.986  -2.817  1.00 56.47  ? 58  LEU B CG   1 
ATOM   2816 C CD1  . LEU B 1 58  ? -26.501 -3.309  -4.291  1.00 57.23  ? 58  LEU B CD1  1 
ATOM   2817 C CD2  . LEU B 1 58  ? -24.913 -2.592  -2.494  1.00 54.21  ? 58  LEU B CD2  1 
ATOM   2818 N N    . ILE B 1 59  ? -29.885 -2.996  -0.766  1.00 58.16  ? 59  ILE B N    1 
ATOM   2819 C CA   . ILE B 1 59  ? -30.446 -4.117  -0.023  1.00 60.61  ? 59  ILE B CA   1 
ATOM   2820 C C    . ILE B 1 59  ? -31.595 -4.749  -0.789  1.00 63.99  ? 59  ILE B C    1 
ATOM   2821 O O    . ILE B 1 59  ? -31.798 -5.961  -0.704  1.00 66.24  ? 59  ILE B O    1 
ATOM   2822 C CB   . ILE B 1 59  ? -30.843 -3.686  1.391   1.00 61.63  ? 59  ILE B CB   1 
ATOM   2823 C CG1  . ILE B 1 59  ? -29.601 -3.778  2.279   1.00 62.09  ? 59  ILE B CG1  1 
ATOM   2824 C CG2  . ILE B 1 59  ? -31.984 -4.578  1.951   1.00 64.00  ? 59  ILE B CG2  1 
ATOM   2825 C CD1  . ILE B 1 59  ? -29.671 -2.968  3.557   1.00 62.42  ? 59  ILE B CD1  1 
ATOM   2826 N N    . ARG B 1 60  ? -32.330 -3.958  -1.581  1.00 62.38  ? 60  ARG B N    1 
ATOM   2827 C CA   . ARG B 1 60  ? -33.435 -4.441  -2.399  1.00 60.67  ? 60  ARG B CA   1 
ATOM   2828 C C    . ARG B 1 60  ? -32.975 -5.162  -3.669  1.00 67.35  ? 60  ARG B C    1 
ATOM   2829 O O    . ARG B 1 60  ? -33.805 -5.768  -4.354  1.00 67.73  ? 60  ARG B O    1 
ATOM   2830 C CB   . ARG B 1 60  ? -34.373 -3.271  -2.771  1.00 67.21  ? 60  ARG B CB   1 
ATOM   2831 C CG   . ARG B 1 60  ? -35.440 -2.858  -1.695  1.00 78.97  ? 60  ARG B CG   1 
ATOM   2832 C CD   . ARG B 1 60  ? -35.436 -1.328  -1.427  1.00 81.94  ? 60  ARG B CD   1 
ATOM   2833 N NE   . ARG B 1 60  ? -36.381 -0.885  -0.398  1.00 89.16  ? 60  ARG B NE   1 
ATOM   2834 C CZ   . ARG B 1 60  ? -36.099 -0.738  0.893   1.00 87.04  ? 60  ARG B CZ   1 
ATOM   2835 N NH1  . ARG B 1 60  ? -34.892 -0.995  1.373   1.00 79.95  ? 60  ARG B NH1  1 
ATOM   2836 N NH2  . ARG B 1 60  ? -37.056 -0.318  1.727   1.00 83.05  ? 60  ARG B NH2  1 
ATOM   2837 N N    . LYS B 1 61  ? -31.690 -5.105  -4.012  1.00 65.77  ? 61  LYS B N    1 
ATOM   2838 C CA   . LYS B 1 61  ? -31.142 -5.789  -5.176  1.00 62.47  ? 61  LYS B CA   1 
ATOM   2839 C C    . LYS B 1 61  ? -30.528 -7.128  -4.774  1.00 66.73  ? 61  LYS B C    1 
ATOM   2840 O O    . LYS B 1 61  ? -30.137 -7.339  -3.615  1.00 65.47  ? 61  LYS B O    1 
ATOM   2841 C CB   . LYS B 1 61  ? -30.100 -4.918  -5.886  1.00 60.03  ? 61  LYS B CB   1 
ATOM   2842 C CG   . LYS B 1 61  ? -30.622 -4.151  -7.124  1.00 57.89  ? 61  LYS B CG   1 
ATOM   2843 C CD   . LYS B 1 61  ? -31.890 -3.349  -6.834  1.00 60.85  ? 61  LYS B CD   1 
ATOM   2844 C CE   . LYS B 1 61  ? -32.263 -2.449  -7.988  1.00 56.63  ? 61  LYS B CE   1 
ATOM   2845 N NZ   . LYS B 1 61  ? -32.514 -3.220  -9.238  1.00 66.10  ? 61  LYS B NZ   1 
ATOM   2846 N N    . SER B 1 62  ? -30.536 -8.060  -5.734  1.00 64.11  ? 62  SER B N    1 
ATOM   2847 C CA   . SER B 1 62  ? -29.940 -9.382  -5.601  1.00 65.48  ? 62  SER B CA   1 
ATOM   2848 C C    . SER B 1 62  ? -29.039 -9.605  -6.805  1.00 65.79  ? 62  SER B C    1 
ATOM   2849 O O    . SER B 1 62  ? -29.029 -8.802  -7.748  1.00 66.12  ? 62  SER B O    1 
ATOM   2850 C CB   . SER B 1 62  ? -31.000 -10.492 -5.494  1.00 65.52  ? 62  SER B CB   1 
ATOM   2851 O OG   . SER B 1 62  ? -31.775 -10.386 -4.303  1.00 66.91  ? 62  SER B OG   1 
ATOM   2852 N N    . ASN B 1 63  ? -28.274 -10.707 -6.769  1.00 64.82  ? 63  ASN B N    1 
ATOM   2853 C CA   . ASN B 1 63  ? -27.266 -10.919 -7.812  1.00 66.33  ? 63  ASN B CA   1 
ATOM   2854 C C    . ASN B 1 63  ? -27.886 -10.896 -9.203  1.00 65.24  ? 63  ASN B C    1 
ATOM   2855 O O    . ASN B 1 63  ? -27.341 -10.271 -10.121 1.00 66.75  ? 63  ASN B O    1 
ATOM   2856 C CB   . ASN B 1 63  ? -26.516 -12.229 -7.585  1.00 68.00  ? 63  ASN B CB   1 
ATOM   2857 C CG   . ASN B 1 63  ? -25.506 -12.126 -6.462  1.00 68.08  ? 63  ASN B CG   1 
ATOM   2858 O OD1  . ASN B 1 63  ? -24.823 -11.110 -6.322  1.00 64.91  ? 63  ASN B OD1  1 
ATOM   2859 N ND2  . ASN B 1 63  ? -25.375 -13.190 -5.681  1.00 67.18  ? 63  ASN B ND2  1 
ATOM   2860 N N    . HIS B 1 64  ? -29.044 -11.549 -9.379  1.00 68.53  ? 64  HIS B N    1 
ATOM   2861 C CA   . HIS B 1 64  ? -29.581 -11.684 -10.731 1.00 72.77  ? 64  HIS B CA   1 
ATOM   2862 C C    . HIS B 1 64  ? -30.178 -10.382 -11.270 1.00 69.60  ? 64  HIS B C    1 
ATOM   2863 O O    . HIS B 1 64  ? -30.478 -10.308 -12.463 1.00 70.16  ? 64  HIS B O    1 
ATOM   2864 C CB   . HIS B 1 64  ? -30.582 -12.843 -10.806 1.00 73.16  ? 64  HIS B CB   1 
ATOM   2865 C CG   . HIS B 1 64  ? -31.749 -12.708 -9.894  1.00 71.98  ? 64  HIS B CG   1 
ATOM   2866 N ND1  . HIS B 1 64  ? -32.728 -11.759 -10.081 1.00 75.85  ? 64  HIS B ND1  1 
ATOM   2867 C CD2  . HIS B 1 64  ? -32.119 -13.425 -8.810  1.00 76.86  ? 64  HIS B CD2  1 
ATOM   2868 C CE1  . HIS B 1 64  ? -33.643 -11.883 -9.138  1.00 67.04  ? 64  HIS B CE1  1 
ATOM   2869 N NE2  . HIS B 1 64  ? -33.297 -12.888 -8.354  1.00 78.99  ? 64  HIS B NE2  1 
ATOM   2870 N N    . ASN B 1 65  ? -30.350 -9.351  -10.433 1.00 68.55  ? 65  ASN B N    1 
ATOM   2871 C CA   . ASN B 1 65  ? -30.769 -8.041  -10.952 1.00 65.29  ? 65  ASN B CA   1 
ATOM   2872 C C    . ASN B 1 65  ? -29.672 -7.320  -11.692 1.00 63.36  ? 65  ASN B C    1 
ATOM   2873 O O    . ASN B 1 65  ? -29.802 -6.117  -11.972 1.00 59.40  ? 65  ASN B O    1 
ATOM   2874 C CB   . ASN B 1 65  ? -31.260 -7.145  -9.825  1.00 66.13  ? 65  ASN B CB   1 
ATOM   2875 C CG   . ASN B 1 65  ? -32.284 -7.820  -8.962  1.00 70.27  ? 65  ASN B CG   1 
ATOM   2876 O OD1  . ASN B 1 65  ? -32.159 -7.844  -7.732  1.00 67.23  ? 65  ASN B OD1  1 
ATOM   2877 N ND2  . ASN B 1 65  ? -33.303 -8.400  -9.599  1.00 72.65  ? 65  ASN B ND2  1 
ATOM   2878 N N    . PHE B 1 66  ? -28.552 -7.966  -11.991 1.00 63.10  ? 66  PHE B N    1 
ATOM   2879 C CA   . PHE B 1 66  ? -27.431 -7.317  -12.661 1.00 63.91  ? 66  PHE B CA   1 
ATOM   2880 C C    . PHE B 1 66  ? -27.112 -8.120  -13.909 1.00 59.17  ? 66  PHE B C    1 
ATOM   2881 O O    . PHE B 1 66  ? -26.867 -9.326  -13.820 1.00 65.20  ? 66  PHE B O    1 
ATOM   2882 C CB   . PHE B 1 66  ? -26.200 -7.235  -11.744 1.00 62.68  ? 66  PHE B CB   1 
ATOM   2883 C CG   . PHE B 1 66  ? -26.368 -6.311  -10.573 1.00 58.03  ? 66  PHE B CG   1 
ATOM   2884 C CD1  . PHE B 1 66  ? -26.399 -4.936  -10.759 1.00 60.23  ? 66  PHE B CD1  1 
ATOM   2885 C CD2  . PHE B 1 66  ? -26.491 -6.808  -9.302  1.00 57.91  ? 66  PHE B CD2  1 
ATOM   2886 C CE1  . PHE B 1 66  ? -26.565 -4.078  -9.682  1.00 59.05  ? 66  PHE B CE1  1 
ATOM   2887 C CE2  . PHE B 1 66  ? -26.664 -5.959  -8.213  1.00 60.85  ? 66  PHE B CE2  1 
ATOM   2888 C CZ   . PHE B 1 66  ? -26.699 -4.584  -8.409  1.00 57.38  ? 66  PHE B CZ   1 
ATOM   2889 N N    . LEU B 1 67  ? -27.138 -7.471  -15.064 1.00 57.12  ? 67  LEU B N    1 
ATOM   2890 C CA   . LEU B 1 67  ? -26.689 -8.099  -16.300 1.00 63.42  ? 67  LEU B CA   1 
ATOM   2891 C C    . LEU B 1 67  ? -25.383 -7.437  -16.725 1.00 64.03  ? 67  LEU B C    1 
ATOM   2892 O O    . LEU B 1 67  ? -25.370 -6.262  -17.114 1.00 60.34  ? 67  LEU B O    1 
ATOM   2893 C CB   . LEU B 1 67  ? -27.724 -8.003  -17.423 1.00 68.52  ? 67  LEU B CB   1 
ATOM   2894 C CG   . LEU B 1 67  ? -26.989 -8.575  -18.648 1.00 78.79  ? 67  LEU B CG   1 
ATOM   2895 C CD1  . LEU B 1 67  ? -26.835 -10.089 -18.456 1.00 83.46  ? 67  LEU B CD1  1 
ATOM   2896 C CD2  . LEU B 1 67  ? -27.554 -8.209  -20.043 1.00 82.36  ? 67  LEU B CD2  1 
ATOM   2897 N N    . VAL B 1 68  ? -24.296 -8.199  -16.671 1.00 63.68  ? 68  VAL B N    1 
ATOM   2898 C CA   . VAL B 1 68  ? -22.981 -7.747  -17.103 1.00 64.59  ? 68  VAL B CA   1 
ATOM   2899 C C    . VAL B 1 68  ? -22.679 -8.409  -18.445 1.00 70.99  ? 68  VAL B C    1 
ATOM   2900 O O    . VAL B 1 68  ? -22.775 -9.644  -18.579 1.00 74.00  ? 68  VAL B O    1 
ATOM   2901 C CB   . VAL B 1 68  ? -21.903 -8.086  -16.062 1.00 64.06  ? 68  VAL B CB   1 
ATOM   2902 C CG1  . VAL B 1 68  ? -20.505 -7.977  -16.664 1.00 61.07  ? 68  VAL B CG1  1 
ATOM   2903 C CG2  . VAL B 1 68  ? -22.076 -7.253  -14.816 1.00 58.34  ? 68  VAL B CG2  1 
ATOM   2904 N N    . GLN B 1 69  ? -22.278 -7.601  -19.428 1.00 65.53  ? 69  GLN B N    1 
ATOM   2905 C CA   . GLN B 1 69  ? -22.035 -8.081  -20.781 1.00 72.36  ? 69  GLN B CA   1 
ATOM   2906 C C    . GLN B 1 69  ? -20.664 -7.614  -21.250 1.00 71.21  ? 69  GLN B C    1 
ATOM   2907 O O    . GLN B 1 69  ? -20.389 -6.406  -21.253 1.00 62.01  ? 69  GLN B O    1 
ATOM   2908 C CB   . GLN B 1 69  ? -23.079 -7.510  -21.745 1.00 75.60  ? 69  GLN B CB   1 
ATOM   2909 C CG   . GLN B 1 69  ? -24.347 -8.323  -21.820 1.00 84.98  ? 69  GLN B CG   1 
ATOM   2910 C CD   . GLN B 1 69  ? -25.114 -8.083  -23.124 1.00 91.03  ? 69  GLN B CD   1 
ATOM   2911 O OE1  . GLN B 1 69  ? -26.148 -7.387  -23.159 1.00 93.52  ? 69  GLN B OE1  1 
ATOM   2912 N NE2  . GLN B 1 69  ? -24.582 -8.641  -24.212 1.00 89.22  ? 69  GLN B NE2  1 
ATOM   2913 N N    . ALA B 1 70  ? -19.828 -8.555  -21.698 1.00 75.24  ? 70  ALA B N    1 
ATOM   2914 C CA   . ALA B 1 70  ? -18.527 -8.265  -22.320 1.00 76.20  ? 70  ALA B CA   1 
ATOM   2915 C C    . ALA B 1 70  ? -18.661 -8.604  -23.799 1.00 79.64  ? 70  ALA B C    1 
ATOM   2916 O O    . ALA B 1 70  ? -18.446 -9.746  -24.205 1.00 83.95  ? 70  ALA B O    1 
ATOM   2917 C CB   . ALA B 1 70  ? -17.398 -9.070  -21.667 1.00 71.59  ? 70  ALA B CB   1 
ATOM   2918 N N    . GLY B 1 71  ? -19.011 -7.604  -24.606 1.00 78.66  ? 71  GLY B N    1 
ATOM   2919 C CA   . GLY B 1 71  ? -19.486 -7.904  -25.942 1.00 80.67  ? 71  GLY B CA   1 
ATOM   2920 C C    . GLY B 1 71  ? -20.764 -8.724  -25.881 1.00 85.94  ? 71  GLY B C    1 
ATOM   2921 O O    . GLY B 1 71  ? -21.809 -8.225  -25.456 1.00 87.67  ? 71  GLY B O    1 
ATOM   2922 N N    . ASN B 1 72  ? -20.709 -9.983  -26.299 1.00 88.88  ? 72  ASN B N    1 
ATOM   2923 C CA   . ASN B 1 72  ? -21.863 -10.861 -26.177 1.00 93.21  ? 72  ASN B CA   1 
ATOM   2924 C C    . ASN B 1 72  ? -21.743 -11.845 -25.025 1.00 95.53  ? 72  ASN B C    1 
ATOM   2925 O O    . ASN B 1 72  ? -22.754 -12.437 -24.626 1.00 96.72  ? 72  ASN B O    1 
ATOM   2926 C CB   . ASN B 1 72  ? -22.075 -11.634 -27.480 1.00 97.51  ? 72  ASN B CB   1 
ATOM   2927 C CG   . ASN B 1 72  ? -21.947 -10.752 -28.701 1.00 103.79 ? 72  ASN B CG   1 
ATOM   2928 O OD1  . ASN B 1 72  ? -22.293 -9.567  -28.668 1.00 102.92 ? 72  ASN B OD1  1 
ATOM   2929 N ND2  . ASN B 1 72  ? -21.432 -11.321 -29.787 1.00 108.10 ? 72  ASN B ND2  1 
ATOM   2930 N N    . VAL B 1 73  ? -20.546 -12.014 -24.464 1.00 93.56  ? 73  VAL B N    1 
ATOM   2931 C CA   . VAL B 1 73  ? -20.384 -12.915 -23.332 1.00 93.70  ? 73  VAL B CA   1 
ATOM   2932 C C    . VAL B 1 73  ? -21.218 -12.409 -22.166 1.00 91.47  ? 73  VAL B C    1 
ATOM   2933 O O    . VAL B 1 73  ? -21.134 -11.234 -21.785 1.00 88.69  ? 73  VAL B O    1 
ATOM   2934 C CB   . VAL B 1 73  ? -18.902 -13.029 -22.948 1.00 92.47  ? 73  VAL B CB   1 
ATOM   2935 C CG1  . VAL B 1 73  ? -18.685 -14.236 -22.049 1.00 98.46  ? 73  VAL B CG1  1 
ATOM   2936 C CG2  . VAL B 1 73  ? -18.027 -13.101 -24.189 1.00 91.50  ? 73  VAL B CG2  1 
ATOM   2937 N N    . GLN B 1 74  ? -22.048 -13.282 -21.610 1.00 92.04  ? 74  GLN B N    1 
ATOM   2938 C CA   . GLN B 1 74  ? -22.857 -12.946 -20.439 1.00 94.15  ? 74  GLN B CA   1 
ATOM   2939 C C    . GLN B 1 74  ? -22.152 -13.503 -19.205 1.00 92.52  ? 74  GLN B C    1 
ATOM   2940 O O    . GLN B 1 74  ? -22.170 -14.712 -18.948 1.00 86.46  ? 74  GLN B O    1 
ATOM   2941 C CB   . GLN B 1 74  ? -24.276 -13.487 -20.568 1.00 99.10  ? 74  GLN B CB   1 
ATOM   2942 C CG   . GLN B 1 74  ? -24.970 -13.084 -21.846 1.00 102.72 ? 74  GLN B CG   1 
ATOM   2943 C CD   . GLN B 1 74  ? -25.722 -11.775 -21.693 1.00 100.97 ? 74  GLN B CD   1 
ATOM   2944 O OE1  . GLN B 1 74  ? -26.408 -11.552 -20.693 1.00 99.72  ? 74  GLN B OE1  1 
ATOM   2945 N NE2  . GLN B 1 74  ? -25.595 -10.903 -22.683 1.00 96.28  ? 74  GLN B NE2  1 
ATOM   2946 N N    . LEU B 1 75  ? -21.512 -12.620 -18.450 1.00 86.29  ? 75  LEU B N    1 
ATOM   2947 C CA   . LEU B 1 75  ? -20.936 -13.028 -17.187 1.00 83.00  ? 75  LEU B CA   1 
ATOM   2948 C C    . LEU B 1 75  ? -22.035 -13.140 -16.143 1.00 83.77  ? 75  LEU B C    1 
ATOM   2949 O O    . LEU B 1 75  ? -22.915 -12.271 -16.057 1.00 83.18  ? 75  LEU B O    1 
ATOM   2950 C CB   . LEU B 1 75  ? -19.900 -11.999 -16.742 1.00 77.41  ? 75  LEU B CB   1 
ATOM   2951 C CG   . LEU B 1 75  ? -18.701 -11.770 -17.651 1.00 69.93  ? 75  LEU B CG   1 
ATOM   2952 C CD1  . LEU B 1 75  ? -18.913 -10.521 -18.464 1.00 69.43  ? 75  LEU B CD1  1 
ATOM   2953 C CD2  . LEU B 1 75  ? -17.483 -11.611 -16.810 1.00 70.03  ? 75  LEU B CD2  1 
ATOM   2954 N N    . ARG B 1 76  ? -22.008 -14.214 -15.359 1.00 80.26  ? 76  ARG B N    1 
ATOM   2955 C CA   . ARG B 1 76  ? -22.955 -14.320 -14.264 1.00 79.53  ? 76  ARG B CA   1 
ATOM   2956 C C    . ARG B 1 76  ? -22.360 -13.729 -12.996 1.00 76.74  ? 76  ARG B C    1 
ATOM   2957 O O    . ARG B 1 76  ? -21.162 -13.838 -12.738 1.00 76.75  ? 76  ARG B O    1 
ATOM   2958 C CB   . ARG B 1 76  ? -23.499 -15.733 -14.038 1.00 83.00  ? 76  ARG B CB   1 
ATOM   2959 C CG   . ARG B 1 76  ? -25.033 -15.579 -13.871 1.00 86.25  ? 76  ARG B CG   1 
ATOM   2960 C CD   . ARG B 1 76  ? -25.958 -16.600 -14.498 1.00 89.19  ? 76  ARG B CD   1 
ATOM   2961 N NE   . ARG B 1 76  ? -25.567 -17.994 -14.360 1.00 97.92  ? 76  ARG B NE   1 
ATOM   2962 C CZ   . ARG B 1 76  ? -26.054 -18.958 -15.130 1.00 97.31  ? 76  ARG B CZ   1 
ATOM   2963 N NH1  . ARG B 1 76  ? -26.862 -18.686 -16.143 1.00 95.77  ? 76  ARG B NH1  1 
ATOM   2964 N NH2  . ARG B 1 76  ? -25.726 -20.222 -14.877 1.00 87.08  ? 76  ARG B NH2  1 
ATOM   2965 N N    . VAL B 1 77  ? -23.211 -13.096 -12.217 1.00 72.87  ? 77  VAL B N    1 
ATOM   2966 C CA   . VAL B 1 77  ? -22.821 -12.380 -11.014 1.00 69.20  ? 77  VAL B CA   1 
ATOM   2967 C C    . VAL B 1 77  ? -23.062 -13.268 -9.807  1.00 69.27  ? 77  VAL B C    1 
ATOM   2968 O O    . VAL B 1 77  ? -24.159 -13.803 -9.654  1.00 73.70  ? 77  VAL B O    1 
ATOM   2969 C CB   . VAL B 1 77  ? -23.617 -11.070 -10.908 1.00 68.90  ? 77  VAL B CB   1 
ATOM   2970 C CG1  . VAL B 1 77  ? -23.180 -10.276 -9.697  1.00 66.45  ? 77  VAL B CG1  1 
ATOM   2971 C CG2  . VAL B 1 77  ? -23.387 -10.233 -12.175 1.00 61.12  ? 77  VAL B CG2  1 
ATOM   2972 N N    . ILE B 1 78  ? -22.044 -13.473 -8.970  1.00 67.04  ? 78  ILE B N    1 
ATOM   2973 C CA   . ILE B 1 78  ? -22.155 -14.416 -7.864  1.00 71.52  ? 78  ILE B CA   1 
ATOM   2974 C C    . ILE B 1 78  ? -21.952 -13.740 -6.518  1.00 68.32  ? 78  ILE B C    1 
ATOM   2975 O O    . ILE B 1 78  ? -21.817 -14.418 -5.508  1.00 69.92  ? 78  ILE B O    1 
ATOM   2976 C CB   . ILE B 1 78  ? -21.164 -15.584 -8.045  1.00 71.25  ? 78  ILE B CB   1 
ATOM   2977 C CG1  . ILE B 1 78  ? -19.725 -15.059 -8.142  1.00 75.31  ? 78  ILE B CG1  1 
ATOM   2978 C CG2  . ILE B 1 78  ? -21.403 -16.274 -9.327  1.00 73.69  ? 78  ILE B CG2  1 
ATOM   2979 C CD1  . ILE B 1 78  ? -18.681 -16.126 -8.518  1.00 78.63  ? 78  ILE B CD1  1 
ATOM   2980 N N    . GLY B 1 79  ? -21.902 -12.407 -6.495  1.00 70.24  ? 79  GLY B N    1 
ATOM   2981 C CA   . GLY B 1 79  ? -21.663 -11.642 -5.286  1.00 63.90  ? 79  GLY B CA   1 
ATOM   2982 C C    . GLY B 1 79  ? -21.542 -10.169 -5.617  1.00 61.09  ? 79  GLY B C    1 
ATOM   2983 O O    . GLY B 1 79  ? -21.017 -9.804  -6.669  1.00 60.76  ? 79  GLY B O    1 
ATOM   2984 N N    . HIS B 1 80  ? -22.099 -9.313  -4.766  1.00 62.21  ? 80  HIS B N    1 
ATOM   2985 C CA   . HIS B 1 80  ? -22.149 -7.877  -5.011  1.00 63.83  ? 80  HIS B CA   1 
ATOM   2986 C C    . HIS B 1 80  ? -21.801 -7.147  -3.722  1.00 63.27  ? 80  HIS B C    1 
ATOM   2987 O O    . HIS B 1 80  ? -22.189 -7.578  -2.629  1.00 60.28  ? 80  HIS B O    1 
ATOM   2988 C CB   . HIS B 1 80  ? -23.542 -7.426  -5.528  1.00 58.09  ? 80  HIS B CB   1 
ATOM   2989 C CG   . HIS B 1 80  ? -24.665 -7.691  -4.564  1.00 58.94  ? 80  HIS B CG   1 
ATOM   2990 N ND1  . HIS B 1 80  ? -25.252 -8.930  -4.423  1.00 63.98  ? 80  HIS B ND1  1 
ATOM   2991 C CD2  . HIS B 1 80  ? -25.330 -6.867  -3.717  1.00 58.76  ? 80  HIS B CD2  1 
ATOM   2992 C CE1  . HIS B 1 80  ? -26.206 -8.869  -3.507  1.00 62.64  ? 80  HIS B CE1  1 
ATOM   2993 N NE2  . HIS B 1 80  ? -26.274 -7.628  -3.063  1.00 60.83  ? 80  HIS B NE2  1 
ATOM   2994 N N    . SER B 1 81  ? -21.050 -6.052  -3.854  1.00 57.26  ? 81  SER B N    1 
ATOM   2995 C CA   . SER B 1 81  ? -20.617 -5.320  -2.676  1.00 59.24  ? 81  SER B CA   1 
ATOM   2996 C C    . SER B 1 81  ? -20.497 -3.852  -3.053  1.00 55.25  ? 81  SER B C    1 
ATOM   2997 O O    . SER B 1 81  ? -20.309 -3.513  -4.222  1.00 53.02  ? 81  SER B O    1 
ATOM   2998 C CB   . SER B 1 81  ? -19.297 -5.891  -2.142  1.00 62.54  ? 81  SER B CB   1 
ATOM   2999 O OG   . SER B 1 81  ? -18.709 -5.067  -1.164  1.00 65.55  ? 81  SER B OG   1 
ATOM   3000 N N    . MET B 1 82  ? -20.619 -2.983  -2.058  1.00 54.67  ? 82  MET B N    1 
ATOM   3001 C CA   . MET B 1 82  ? -20.573 -1.544  -2.278  1.00 52.78  ? 82  MET B CA   1 
ATOM   3002 C C    . MET B 1 82  ? -19.355 -1.001  -1.549  1.00 53.17  ? 82  MET B C    1 
ATOM   3003 O O    . MET B 1 82  ? -19.287 -1.088  -0.317  1.00 54.54  ? 82  MET B O    1 
ATOM   3004 C CB   . MET B 1 82  ? -21.822 -0.870  -1.737  1.00 53.64  ? 82  MET B CB   1 
ATOM   3005 C CG   . MET B 1 82  ? -21.640 0.607   -1.616  1.00 55.58  ? 82  MET B CG   1 
ATOM   3006 S SD   . MET B 1 82  ? -23.139 1.484   -2.058  1.00 50.98  ? 82  MET B SD   1 
ATOM   3007 C CE   . MET B 1 82  ? -24.103 1.090   -0.622  1.00 51.97  ? 82  MET B CE   1 
ATOM   3008 N N    . GLN B 1 83  ? -18.409 -0.442  -2.288  1.00 51.77  ? 83  GLN B N    1 
ATOM   3009 C CA   . GLN B 1 83  ? -17.241 0.198   -1.690  1.00 56.00  ? 83  GLN B CA   1 
ATOM   3010 C C    . GLN B 1 83  ? -17.342 1.685   -1.992  1.00 50.26  ? 83  GLN B C    1 
ATOM   3011 O O    . GLN B 1 83  ? -17.177 2.088   -3.135  1.00 48.68  ? 83  GLN B O    1 
ATOM   3012 C CB   . GLN B 1 83  ? -15.931 -0.375  -2.241  1.00 60.45  ? 83  GLN B CB   1 
ATOM   3013 C CG   . GLN B 1 83  ? -14.673 0.240   -1.597  1.00 59.58  ? 83  GLN B CG   1 
ATOM   3014 C CD   . GLN B 1 83  ? -13.346 -0.401  -2.052  1.00 61.68  ? 83  GLN B CD   1 
ATOM   3015 O OE1  . GLN B 1 83  ? -13.289 -1.146  -3.043  1.00 58.46  ? 83  GLN B OE1  1 
ATOM   3016 N NE2  . GLN B 1 83  ? -12.284 -0.156  -1.275  1.00 61.88  ? 83  GLN B NE2  1 
ATOM   3017 N N    . ASN B 1 84  ? -17.628 2.502   -0.974  1.00 50.62  ? 84  ASN B N    1 
ATOM   3018 C CA   . ASN B 1 84  ? -17.790 3.942   -1.208  1.00 49.15  ? 84  ASN B CA   1 
ATOM   3019 C C    . ASN B 1 84  ? -18.794 4.105   -2.352  1.00 47.59  ? 84  ASN B C    1 
ATOM   3020 O O    . ASN B 1 84  ? -19.863 3.478   -2.314  1.00 47.99  ? 84  ASN B O    1 
ATOM   3021 C CB   . ASN B 1 84  ? -16.411 4.545   -1.435  1.00 48.81  ? 84  ASN B CB   1 
ATOM   3022 C CG   . ASN B 1 84  ? -15.468 4.279   -0.261  1.00 50.67  ? 84  ASN B CG   1 
ATOM   3023 O OD1  . ASN B 1 84  ? -15.835 4.468   0.888   1.00 51.75  ? 84  ASN B OD1  1 
ATOM   3024 N ND2  . ASN B 1 84  ? -14.254 3.815   -0.559  1.00 51.16  ? 84  ASN B ND2  1 
ATOM   3025 N N    . CYS B 1 85  ? -18.513 4.910   -3.370  1.00 45.98  ? 85  CYS B N    1 
ATOM   3026 C CA   . CYS B 1 85  ? -19.475 5.146   -4.438  1.00 44.62  ? 85  CYS B CA   1 
ATOM   3027 C C    . CYS B 1 85  ? -19.351 4.144   -5.579  1.00 44.22  ? 85  CYS B C    1 
ATOM   3028 O O    . CYS B 1 85  ? -19.924 4.358   -6.652  1.00 43.01  ? 85  CYS B O    1 
ATOM   3029 C CB   . CYS B 1 85  ? -19.363 6.586   -4.957  1.00 43.20  ? 85  CYS B CB   1 
ATOM   3030 S SG   . CYS B 1 85  ? -19.724 7.768   -3.604  1.00 43.83  ? 85  CYS B SG   1 
ATOM   3031 N N    . VAL B 1 86  ? -18.683 3.024   -5.351  1.00 45.36  ? 86  VAL B N    1 
ATOM   3032 C CA   . VAL B 1 86  ? -18.414 2.064   -6.409  1.00 45.13  ? 86  VAL B CA   1 
ATOM   3033 C C    . VAL B 1 86  ? -19.091 0.750   -6.063  1.00 46.60  ? 86  VAL B C    1 
ATOM   3034 O O    . VAL B 1 86  ? -19.045 0.288   -4.920  1.00 48.19  ? 86  VAL B O    1 
ATOM   3035 C CB   . VAL B 1 86  ? -16.894 1.869   -6.635  1.00 49.16  ? 86  VAL B CB   1 
ATOM   3036 C CG1  . VAL B 1 86  ? -16.603 0.519   -7.234  1.00 51.67  ? 86  VAL B CG1  1 
ATOM   3037 C CG2  . VAL B 1 86  ? -16.370 2.960   -7.599  1.00 43.53  ? 86  VAL B CG2  1 
ATOM   3038 N N    . LEU B 1 87  ? -19.731 0.155   -7.059  1.00 46.18  ? 87  LEU B N    1 
ATOM   3039 C CA   . LEU B 1 87  ? -20.309 -1.172  -6.896  1.00 49.57  ? 87  LEU B CA   1 
ATOM   3040 C C    . LEU B 1 87  ? -19.351 -2.199  -7.490  1.00 48.22  ? 87  LEU B C    1 
ATOM   3041 O O    . LEU B 1 87  ? -18.861 -2.015  -8.605  1.00 46.96  ? 87  LEU B O    1 
ATOM   3042 C CB   . LEU B 1 87  ? -21.680 -1.242  -7.566  1.00 47.26  ? 87  LEU B CB   1 
ATOM   3043 C CG   . LEU B 1 87  ? -22.382 -2.591  -7.697  1.00 52.28  ? 87  LEU B CG   1 
ATOM   3044 C CD1  . LEU B 1 87  ? -22.765 -3.174  -6.333  1.00 50.83  ? 87  LEU B CD1  1 
ATOM   3045 C CD2  . LEU B 1 87  ? -23.606 -2.443  -8.602  1.00 53.14  ? 87  LEU B CD2  1 
ATOM   3046 N N    . LYS B 1 88  ? -19.091 -3.266  -6.734  1.00 51.56  ? 88  LYS B N    1 
ATOM   3047 C CA   . LYS B 1 88  ? -18.262 -4.399  -7.143  1.00 54.00  ? 88  LYS B CA   1 
ATOM   3048 C C    . LYS B 1 88  ? -19.153 -5.630  -7.321  1.00 53.54  ? 88  LYS B C    1 
ATOM   3049 O O    . LYS B 1 88  ? -19.734 -6.133  -6.351  1.00 54.56  ? 88  LYS B O    1 
ATOM   3050 C CB   . LYS B 1 88  ? -17.143 -4.668  -6.124  1.00 53.27  ? 88  LYS B CB   1 
ATOM   3051 C CG   . LYS B 1 88  ? -15.917 -3.713  -6.311  1.00 58.93  ? 88  LYS B CG   1 
ATOM   3052 C CD   . LYS B 1 88  ? -15.260 -3.300  -4.993  1.00 55.38  ? 88  LYS B CD   1 
ATOM   3053 C CE   . LYS B 1 88  ? -15.446 -4.347  -3.957  1.00 56.66  ? 88  LYS B CE   1 
ATOM   3054 N NZ   . LYS B 1 88  ? -14.250 -4.493  -3.062  1.00 68.80  ? 88  LYS B NZ   1 
ATOM   3055 N N    . LEU B 1 89  ? -19.263 -6.097  -8.564  1.00 55.15  ? 89  LEU B N    1 
ATOM   3056 C CA   . LEU B 1 89  ? -20.001 -7.306  -8.920  1.00 57.11  ? 89  LEU B CA   1 
ATOM   3057 C C    . LEU B 1 89  ? -18.987 -8.420  -9.130  1.00 58.07  ? 89  LEU B C    1 
ATOM   3058 O O    . LEU B 1 89  ? -18.224 -8.389  -10.107 1.00 56.80  ? 89  LEU B O    1 
ATOM   3059 C CB   . LEU B 1 89  ? -20.816 -7.103  -10.196 1.00 54.69  ? 89  LEU B CB   1 
ATOM   3060 C CG   . LEU B 1 89  ? -21.694 -5.866  -10.209 1.00 53.59  ? 89  LEU B CG   1 
ATOM   3061 C CD1  . LEU B 1 89  ? -22.162 -5.578  -11.604 1.00 48.95  ? 89  LEU B CD1  1 
ATOM   3062 C CD2  . LEU B 1 89  ? -22.862 -6.074  -9.246  1.00 53.84  ? 89  LEU B CD2  1 
ATOM   3063 N N    . LYS B 1 90  ? -18.991 -9.409  -8.242  1.00 57.03  ? 90  LYS B N    1 
ATOM   3064 C CA   . LYS B 1 90  ? -18.110 -10.549 -8.421  1.00 61.58  ? 90  LYS B CA   1 
ATOM   3065 C C    . LYS B 1 90  ? -18.736 -11.483 -9.449  1.00 64.93  ? 90  LYS B C    1 
ATOM   3066 O O    . LYS B 1 90  ? -19.894 -11.889 -9.306  1.00 66.97  ? 90  LYS B O    1 
ATOM   3067 C CB   . LYS B 1 90  ? -17.843 -11.269 -7.100  1.00 61.95  ? 90  LYS B CB   1 
ATOM   3068 C CG   . LYS B 1 90  ? -16.928 -12.472 -7.294  1.00 68.63  ? 90  LYS B CG   1 
ATOM   3069 C CD   . LYS B 1 90  ? -15.922 -12.648 -6.174  1.00 67.02  ? 90  LYS B CD   1 
ATOM   3070 C CE   . LYS B 1 90  ? -15.367 -14.074 -6.201  1.00 70.92  ? 90  LYS B CE   1 
ATOM   3071 N NZ   . LYS B 1 90  ? -14.373 -14.354 -5.123  1.00 80.33  ? 90  LYS B NZ   1 
ATOM   3072 N N    . VAL B 1 91  ? -18.001 -11.766 -10.519 1.00 65.81  ? 91  VAL B N    1 
ATOM   3073 C CA   . VAL B 1 91  ? -18.496 -12.658 -11.559 1.00 69.67  ? 91  VAL B CA   1 
ATOM   3074 C C    . VAL B 1 91  ? -17.756 -13.990 -11.528 1.00 75.28  ? 91  VAL B C    1 
ATOM   3075 O O    . VAL B 1 91  ? -16.888 -14.226 -10.676 1.00 73.33  ? 91  VAL B O    1 
ATOM   3076 C CB   . VAL B 1 91  ? -18.403 -12.005 -12.939 1.00 71.63  ? 91  VAL B CB   1 
ATOM   3077 C CG1  . VAL B 1 91  ? -19.404 -10.867 -13.029 1.00 68.20  ? 91  VAL B CG1  1 
ATOM   3078 C CG2  . VAL B 1 91  ? -16.971 -11.502 -13.170 1.00 69.38  ? 91  VAL B CG2  1 
ATOM   3079 N N    . ASP B 1 92  ? -18.137 -14.892 -12.431 1.00 78.65  ? 92  ASP B N    1 
ATOM   3080 C CA   . ASP B 1 92  ? -17.616 -16.253 -12.404 1.00 82.42  ? 92  ASP B CA   1 
ATOM   3081 C C    . ASP B 1 92  ? -16.416 -16.453 -13.320 1.00 81.45  ? 92  ASP B C    1 
ATOM   3082 O O    . ASP B 1 92  ? -15.631 -17.376 -13.087 1.00 83.10  ? 92  ASP B O    1 
ATOM   3083 C CB   . ASP B 1 92  ? -18.723 -17.262 -12.760 1.00 79.88  ? 92  ASP B CB   1 
ATOM   3084 C CG   . ASP B 1 92  ? -19.285 -17.068 -14.170 1.00 80.33  ? 92  ASP B CG   1 
ATOM   3085 O OD1  . ASP B 1 92  ? -18.839 -16.154 -14.905 1.00 81.12  ? 92  ASP B OD1  1 
ATOM   3086 O OD2  . ASP B 1 92  ? -20.189 -17.841 -14.538 1.00 78.21  ? 92  ASP B OD2  1 
ATOM   3087 N N    . THR B 1 93  ? -16.241 -15.602 -14.330 1.00 78.80  ? 93  THR B N    1 
ATOM   3088 C CA   . THR B 1 93  ? -15.148 -15.714 -15.287 1.00 76.32  ? 93  THR B CA   1 
ATOM   3089 C C    . THR B 1 93  ? -14.155 -14.581 -15.059 1.00 75.86  ? 93  THR B C    1 
ATOM   3090 O O    . THR B 1 93  ? -14.528 -13.405 -15.128 1.00 69.85  ? 93  THR B O    1 
ATOM   3091 C CB   . THR B 1 93  ? -15.680 -15.665 -16.719 1.00 77.67  ? 93  THR B CB   1 
ATOM   3092 O OG1  . THR B 1 93  ? -16.534 -16.792 -16.941 1.00 88.35  ? 93  THR B OG1  1 
ATOM   3093 C CG2  . THR B 1 93  ? -14.531 -15.696 -17.719 1.00 71.91  ? 93  THR B CG2  1 
ATOM   3094 N N    . ALA B 1 94  ? -12.889 -14.935 -14.814 1.00 72.40  ? 94  ALA B N    1 
ATOM   3095 C CA   . ALA B 1 94  ? -11.832 -13.934 -14.751 1.00 60.09  ? 94  ALA B CA   1 
ATOM   3096 C C    . ALA B 1 94  ? -11.542 -13.421 -16.151 1.00 65.48  ? 94  ALA B C    1 
ATOM   3097 O O    . ALA B 1 94  ? -11.251 -14.209 -17.056 1.00 64.35  ? 94  ALA B O    1 
ATOM   3098 C CB   . ALA B 1 94  ? -10.571 -14.522 -14.125 1.00 63.42  ? 94  ALA B CB   1 
ATOM   3099 N N    . ASN B 1 95  ? -11.659 -12.104 -16.339 1.00 62.27  ? 95  ASN B N    1 
ATOM   3100 C CA   . ASN B 1 95  ? -11.326 -11.498 -17.611 1.00 58.65  ? 95  ASN B CA   1 
ATOM   3101 C C    . ASN B 1 95  ? -9.980  -12.054 -18.072 1.00 62.83  ? 95  ASN B C    1 
ATOM   3102 O O    . ASN B 1 95  ? -9.004  -11.977 -17.320 1.00 64.83  ? 95  ASN B O    1 
ATOM   3103 C CB   . ASN B 1 95  ? -11.271 -9.978  -17.485 1.00 54.68  ? 95  ASN B CB   1 
ATOM   3104 C CG   . ASN B 1 95  ? -10.821 -9.293  -18.775 1.00 59.52  ? 95  ASN B CG   1 
ATOM   3105 O OD1  . ASN B 1 95  ? -10.953 -9.845  -19.866 1.00 63.25  ? 95  ASN B OD1  1 
ATOM   3106 N ND2  . ASN B 1 95  ? -10.292 -8.073  -18.652 1.00 58.15  ? 95  ASN B ND2  1 
ATOM   3107 N N    . PRO B 1 96  ? -9.902  -12.687 -19.243 1.00 65.97  ? 96  PRO B N    1 
ATOM   3108 C CA   . PRO B 1 96  ? -8.590  -13.168 -19.705 1.00 66.18  ? 96  PRO B CA   1 
ATOM   3109 C C    . PRO B 1 96  ? -7.672  -12.046 -20.190 1.00 63.74  ? 96  PRO B C    1 
ATOM   3110 O O    . PRO B 1 96  ? -6.446  -12.202 -20.148 1.00 64.30  ? 96  PRO B O    1 
ATOM   3111 C CB   . PRO B 1 96  ? -8.956  -14.123 -20.845 1.00 66.13  ? 96  PRO B CB   1 
ATOM   3112 C CG   . PRO B 1 96  ? -10.229 -13.565 -21.385 1.00 69.30  ? 96  PRO B CG   1 
ATOM   3113 C CD   . PRO B 1 96  ? -10.964 -12.919 -20.235 1.00 63.91  ? 96  PRO B CD   1 
ATOM   3114 N N    . LYS B 1 97  ? -8.217  -10.905 -20.594 1.00 64.48  ? 97  LYS B N    1 
ATOM   3115 C CA   . LYS B 1 97  ? -7.420  -9.753  -21.001 1.00 63.80  ? 97  LYS B CA   1 
ATOM   3116 C C    . LYS B 1 97  ? -6.932  -8.904  -19.825 1.00 62.70  ? 97  LYS B C    1 
ATOM   3117 O O    . LYS B 1 97  ? -6.439  -7.797  -20.071 1.00 65.64  ? 97  LYS B O    1 
ATOM   3118 C CB   . LYS B 1 97  ? -8.225  -8.866  -21.961 1.00 63.21  ? 97  LYS B CB   1 
ATOM   3119 C CG   . LYS B 1 97  ? -8.735  -9.572  -23.205 1.00 69.49  ? 97  LYS B CG   1 
ATOM   3120 C CD   . LYS B 1 97  ? -10.071 -10.279 -22.923 1.00 75.50  ? 97  LYS B CD   1 
ATOM   3121 C CE   . LYS B 1 97  ? -10.686 -10.847 -24.205 1.00 88.31  ? 97  LYS B CE   1 
ATOM   3122 N NZ   . LYS B 1 97  ? -12.178 -10.828 -24.217 1.00 96.45  ? 97  LYS B NZ   1 
ATOM   3123 N N    . THR B 1 98  ? -7.083  -9.358  -18.577 1.00 59.14  ? 98  THR B N    1 
ATOM   3124 C CA   . THR B 1 98  ? -6.718  -8.531  -17.428 1.00 58.98  ? 98  THR B CA   1 
ATOM   3125 C C    . THR B 1 98  ? -5.242  -8.157  -17.546 1.00 57.60  ? 98  THR B C    1 
ATOM   3126 O O    . THR B 1 98  ? -4.384  -9.051  -17.537 1.00 56.04  ? 98  THR B O    1 
ATOM   3127 C CB   . THR B 1 98  ? -6.977  -9.254  -16.088 1.00 56.22  ? 98  THR B CB   1 
ATOM   3128 O OG1  . THR B 1 98  ? -8.369  -9.528  -15.938 1.00 59.19  ? 98  THR B OG1  1 
ATOM   3129 C CG2  . THR B 1 98  ? -6.559  -8.410  -14.889 1.00 52.81  ? 98  THR B CG2  1 
ATOM   3130 N N    . PRO B 1 99  ? -4.903  -6.882  -17.682 1.00 55.05  ? 99  PRO B N    1 
ATOM   3131 C CA   . PRO B 1 99  ? -3.495  -6.494  -17.729 1.00 48.61  ? 99  PRO B CA   1 
ATOM   3132 C C    . PRO B 1 99  ? -2.987  -6.382  -16.308 1.00 56.31  ? 99  PRO B C    1 
ATOM   3133 O O    . PRO B 1 99  ? -3.763  -6.468  -15.339 1.00 55.37  ? 99  PRO B O    1 
ATOM   3134 C CB   . PRO B 1 99  ? -3.514  -5.122  -18.407 1.00 52.20  ? 99  PRO B CB   1 
ATOM   3135 C CG   . PRO B 1 99  ? -4.851  -4.546  -17.932 1.00 51.97  ? 99  PRO B CG   1 
ATOM   3136 C CD   . PRO B 1 99  ? -5.799  -5.715  -17.699 1.00 49.99  ? 99  PRO B CD   1 
ATOM   3137 N N    . LYS B 1 100 ? -1.657  -6.235  -16.216 1.00 57.41  ? 100 LYS B N    1 
ATOM   3138 C CA   . LYS B 1 100 ? -1.000  -5.775  -14.998 1.00 59.92  ? 100 LYS B CA   1 
ATOM   3139 C C    . LYS B 1 100 ? -1.546  -4.391  -14.633 1.00 56.60  ? 100 LYS B C    1 
ATOM   3140 O O    . LYS B 1 100 ? -1.547  -3.457  -15.449 1.00 55.26  ? 100 LYS B O    1 
ATOM   3141 C CB   . LYS B 1 100 ? 0.518   -5.808  -15.198 1.00 64.55  ? 100 LYS B CB   1 
ATOM   3142 C CG   . LYS B 1 100 ? 1.425   -5.372  -13.987 1.00 73.56  ? 100 LYS B CG   1 
ATOM   3143 C CD   . LYS B 1 100 ? 1.728   -6.343  -12.874 1.00 81.76  ? 100 LYS B CD   1 
ATOM   3144 C CE   . LYS B 1 100 ? 1.858   -5.502  -11.518 1.00 85.79  ? 100 LYS B CE   1 
ATOM   3145 N NZ   . LYS B 1 100 ? 0.624   -5.021  -10.691 1.00 73.30  ? 100 LYS B NZ   1 
ATOM   3146 N N    . TYR B 1 101 ? -2.088  -4.277  -13.427 1.00 55.69  ? 101 TYR B N    1 
ATOM   3147 C CA   . TYR B 1 101 ? -2.802  -3.055  -13.088 1.00 57.81  ? 101 TYR B CA   1 
ATOM   3148 C C    . TYR B 1 101 ? -2.551  -2.681  -11.637 1.00 58.51  ? 101 TYR B C    1 
ATOM   3149 O O    . TYR B 1 101 ? -2.156  -3.505  -10.816 1.00 53.77  ? 101 TYR B O    1 
ATOM   3150 C CB   . TYR B 1 101 ? -4.320  -3.176  -13.354 1.00 48.80  ? 101 TYR B CB   1 
ATOM   3151 C CG   . TYR B 1 101 ? -5.092  -3.997  -12.339 1.00 50.23  ? 101 TYR B CG   1 
ATOM   3152 C CD1  . TYR B 1 101 ? -5.143  -5.387  -12.431 1.00 51.70  ? 101 TYR B CD1  1 
ATOM   3153 C CD2  . TYR B 1 101 ? -5.761  -3.390  -11.299 1.00 50.25  ? 101 TYR B CD2  1 
ATOM   3154 C CE1  . TYR B 1 101 ? -5.852  -6.150  -11.499 1.00 53.83  ? 101 TYR B CE1  1 
ATOM   3155 C CE2  . TYR B 1 101 ? -6.468  -4.131  -10.371 1.00 51.63  ? 101 TYR B CE2  1 
ATOM   3156 C CZ   . TYR B 1 101 ? -6.521  -5.507  -10.470 1.00 53.10  ? 101 TYR B CZ   1 
ATOM   3157 O OH   . TYR B 1 101 ? -7.223  -6.244  -9.540  1.00 61.74  ? 101 TYR B OH   1 
ATOM   3158 N N    . LYS B 1 102 ? -2.801  -1.399  -11.355 1.00 53.17  ? 102 LYS B N    1 
ATOM   3159 C CA   . LYS B 1 102 ? -2.840  -0.862  -10.013 1.00 53.69  ? 102 LYS B CA   1 
ATOM   3160 C C    . LYS B 1 102 ? -4.056  0.033   -9.942  1.00 49.71  ? 102 LYS B C    1 
ATOM   3161 O O    . LYS B 1 102 ? -4.601  0.406   -10.964 1.00 47.80  ? 102 LYS B O    1 
ATOM   3162 C CB   . LYS B 1 102 ? -1.614  -0.005  -9.656  1.00 60.63  ? 102 LYS B CB   1 
ATOM   3163 C CG   . LYS B 1 102 ? -0.263  -0.746  -9.587  1.00 69.17  ? 102 LYS B CG   1 
ATOM   3164 C CD   . LYS B 1 102 ? 0.893   0.062   -10.276 1.00 74.16  ? 102 LYS B CD   1 
ATOM   3165 C CE   . LYS B 1 102 ? 2.269   -0.655  -10.151 1.00 81.56  ? 102 LYS B CE   1 
ATOM   3166 N NZ   . LYS B 1 102 ? 3.139   -0.486  -11.404 1.00 89.22  ? 102 LYS B NZ   1 
ATOM   3167 N N    . PHE B 1 103 ? -4.466  0.362   -8.722  1.00 50.50  ? 103 PHE B N    1 
ATOM   3168 C CA   . PHE B 1 103 ? -5.429  1.416   -8.407  1.00 49.21  ? 103 PHE B CA   1 
ATOM   3169 C C    . PHE B 1 103 ? -4.692  2.552   -7.707  1.00 49.75  ? 103 PHE B C    1 
ATOM   3170 O O    . PHE B 1 103 ? -3.961  2.313   -6.737  1.00 53.38  ? 103 PHE B O    1 
ATOM   3171 C CB   . PHE B 1 103 ? -6.531  0.937   -7.463  1.00 49.87  ? 103 PHE B CB   1 
ATOM   3172 C CG   . PHE B 1 103 ? -7.571  0.087   -8.112  1.00 49.15  ? 103 PHE B CG   1 
ATOM   3173 C CD1  . PHE B 1 103 ? -7.587  -0.077  -9.480  1.00 47.76  ? 103 PHE B CD1  1 
ATOM   3174 C CD2  . PHE B 1 103 ? -8.508  -0.590  -7.340  1.00 50.05  ? 103 PHE B CD2  1 
ATOM   3175 C CE1  . PHE B 1 103 ? -8.533  -0.859  -10.082 1.00 47.26  ? 103 PHE B CE1  1 
ATOM   3176 C CE2  . PHE B 1 103 ? -9.448  -1.365  -7.923  1.00 49.60  ? 103 PHE B CE2  1 
ATOM   3177 C CZ   . PHE B 1 103 ? -9.469  -1.508  -9.293  1.00 48.23  ? 103 PHE B CZ   1 
ATOM   3178 N N    . VAL B 1 104 ? -4.900  3.780   -8.162  1.00 48.19  ? 104 VAL B N    1 
ATOM   3179 C CA   . VAL B 1 104 ? -4.096  4.914   -7.728  1.00 48.72  ? 104 VAL B CA   1 
ATOM   3180 C C    . VAL B 1 104 ? -4.986  6.141   -7.588  1.00 47.38  ? 104 VAL B C    1 
ATOM   3181 O O    . VAL B 1 104 ? -5.773  6.441   -8.492  1.00 47.00  ? 104 VAL B O    1 
ATOM   3182 C CB   . VAL B 1 104 ? -2.955  5.151   -8.741  1.00 52.03  ? 104 VAL B CB   1 
ATOM   3183 C CG1  . VAL B 1 104 ? -2.525  6.595   -8.771  1.00 48.79  ? 104 VAL B CG1  1 
ATOM   3184 C CG2  . VAL B 1 104 ? -1.759  4.268   -8.348  1.00 50.53  ? 104 VAL B CG2  1 
ATOM   3185 N N    . ARG B 1 105 ? -4.834  6.872   -6.485  1.00 48.43  ? 105 ARG B N    1 
ATOM   3186 C CA   . ARG B 1 105 ? -5.519  8.148   -6.284  1.00 50.12  ? 105 ARG B CA   1 
ATOM   3187 C C    . ARG B 1 105 ? -4.576  9.281   -6.688  1.00 47.43  ? 105 ARG B C    1 
ATOM   3188 O O    . ARG B 1 105 ? -3.594  9.550   -6.002  1.00 51.19  ? 105 ARG B O    1 
ATOM   3189 C CB   . ARG B 1 105 ? -5.947  8.298   -4.824  1.00 51.26  ? 105 ARG B CB   1 
ATOM   3190 C CG   . ARG B 1 105 ? -6.898  9.479   -4.598  1.00 47.82  ? 105 ARG B CG   1 
ATOM   3191 C CD   . ARG B 1 105 ? -7.519  9.442   -3.175  1.00 53.74  ? 105 ARG B CD   1 
ATOM   3192 N NE   . ARG B 1 105 ? -8.369  10.614  -2.970  1.00 52.13  ? 105 ARG B NE   1 
ATOM   3193 C CZ   . ARG B 1 105 ? -9.604  10.743  -3.438  1.00 46.75  ? 105 ARG B CZ   1 
ATOM   3194 N NH1  . ARG B 1 105 ? -10.185 9.785   -4.137  1.00 45.88  ? 105 ARG B NH1  1 
ATOM   3195 N NH2  . ARG B 1 105 ? -10.274 11.861  -3.195  1.00 46.28  ? 105 ARG B NH2  1 
ATOM   3196 N N    . ILE B 1 106 ? -4.855  9.948   -7.780  1.00 47.81  ? 106 ILE B N    1 
ATOM   3197 C CA   . ILE B 1 106 ? -3.890  10.951  -8.222  1.00 50.26  ? 106 ILE B CA   1 
ATOM   3198 C C    . ILE B 1 106 ? -4.063  12.257  -7.460  1.00 52.54  ? 106 ILE B C    1 
ATOM   3199 O O    . ILE B 1 106 ? -5.164  12.643  -7.044  1.00 50.22  ? 106 ILE B O    1 
ATOM   3200 C CB   . ILE B 1 106 ? -3.965  11.194  -9.732  1.00 44.05  ? 106 ILE B CB   1 
ATOM   3201 C CG1  . ILE B 1 106 ? -5.395  11.448  -10.181 1.00 46.37  ? 106 ILE B CG1  1 
ATOM   3202 C CG2  . ILE B 1 106 ? -3.244  10.101  -10.475 1.00 46.01  ? 106 ILE B CG2  1 
ATOM   3203 C CD1  . ILE B 1 106 ? -5.750  12.938  -10.342 1.00 49.68  ? 106 ILE B CD1  1 
ATOM   3204 N N    . GLN B 1 107 ? -2.935  12.950  -7.315  1.00 52.53  ? 107 GLN B N    1 
ATOM   3205 C CA   . GLN B 1 107 ? -2.892  14.299  -6.789  1.00 51.04  ? 107 GLN B CA   1 
ATOM   3206 C C    . GLN B 1 107 ? -3.469  15.290  -7.799  1.00 48.55  ? 107 GLN B C    1 
ATOM   3207 O O    . GLN B 1 107 ? -3.390  15.065  -9.018  1.00 45.05  ? 107 GLN B O    1 
ATOM   3208 C CB   . GLN B 1 107 ? -1.452  14.672  -6.487  1.00 51.68  ? 107 GLN B CB   1 
ATOM   3209 C CG   . GLN B 1 107 ? -0.901  13.989  -5.283  1.00 59.49  ? 107 GLN B CG   1 
ATOM   3210 C CD   . GLN B 1 107 ? -1.709  14.344  -4.057  1.00 65.31  ? 107 GLN B CD   1 
ATOM   3211 O OE1  . GLN B 1 107 ? -1.633  15.477  -3.559  1.00 64.17  ? 107 GLN B OE1  1 
ATOM   3212 N NE2  . GLN B 1 107 ? -2.508  13.387  -3.569  1.00 60.29  ? 107 GLN B NE2  1 
ATOM   3213 N N    . PRO B 1 108 ? -4.061  16.391  -7.319  1.00 46.37  ? 108 PRO B N    1 
ATOM   3214 C CA   . PRO B 1 108 ? -4.382  17.509  -8.216  1.00 48.06  ? 108 PRO B CA   1 
ATOM   3215 C C    . PRO B 1 108 ? -3.149  17.981  -8.980  1.00 47.27  ? 108 PRO B C    1 
ATOM   3216 O O    . PRO B 1 108 ? -2.028  17.953  -8.474  1.00 53.05  ? 108 PRO B O    1 
ATOM   3217 C CB   . PRO B 1 108 ? -4.896  18.596  -7.262  1.00 46.01  ? 108 PRO B CB   1 
ATOM   3218 C CG   . PRO B 1 108 ? -4.258  18.270  -5.943  1.00 50.00  ? 108 PRO B CG   1 
ATOM   3219 C CD   . PRO B 1 108 ? -4.260  16.754  -5.905  1.00 54.05  ? 108 PRO B CD   1 
ATOM   3220 N N    . GLY B 1 109 ? -3.364  18.426  -10.218 1.00 46.68  ? 109 GLY B N    1 
ATOM   3221 C CA   . GLY B 1 109 ? -2.264  18.807  -11.060 1.00 48.02  ? 109 GLY B CA   1 
ATOM   3222 C C    . GLY B 1 109 ? -1.757  17.710  -11.968 1.00 52.28  ? 109 GLY B C    1 
ATOM   3223 O O    . GLY B 1 109 ? -1.154  18.016  -13.009 1.00 48.13  ? 109 GLY B O    1 
ATOM   3224 N N    . GLN B 1 110 ? -1.986  16.442  -11.609 1.00 52.77  ? 110 GLN B N    1 
ATOM   3225 C CA   . GLN B 1 110 ? -1.539  15.298  -12.393 1.00 48.50  ? 110 GLN B CA   1 
ATOM   3226 C C    . GLN B 1 110 ? -2.483  15.065  -13.574 1.00 43.76  ? 110 GLN B C    1 
ATOM   3227 O O    . GLN B 1 110 ? -3.635  15.528  -13.603 1.00 42.67  ? 110 GLN B O    1 
ATOM   3228 C CB   . GLN B 1 110 ? -1.449  14.037  -11.513 1.00 49.43  ? 110 GLN B CB   1 
ATOM   3229 C CG   . GLN B 1 110 ? -0.239  13.934  -10.530 1.00 57.69  ? 110 GLN B CG   1 
ATOM   3230 C CD   . GLN B 1 110 ? 1.036   14.686  -10.959 1.00 68.53  ? 110 GLN B CD   1 
ATOM   3231 O OE1  . GLN B 1 110 ? 1.880   14.159  -11.701 1.00 63.83  ? 110 GLN B OE1  1 
ATOM   3232 N NE2  . GLN B 1 110 ? 1.202   15.907  -10.438 1.00 68.90  ? 110 GLN B NE2  1 
ATOM   3233 N N    . THR B 1 111 ? -1.978  14.350  -14.578 1.00 42.71  ? 111 THR B N    1 
ATOM   3234 C CA   . THR B 1 111 ? -2.732  14.095  -15.798 1.00 43.49  ? 111 THR B CA   1 
ATOM   3235 C C    . THR B 1 111 ? -2.954  12.602  -15.994 1.00 38.42  ? 111 THR B C    1 
ATOM   3236 O O    . THR B 1 111 ? -2.265  11.766  -15.411 1.00 39.66  ? 111 THR B O    1 
ATOM   3237 C CB   . THR B 1 111 ? -1.996  14.647  -17.023 1.00 44.00  ? 111 THR B CB   1 
ATOM   3238 O OG1  . THR B 1 111 ? -0.719  13.991  -17.102 1.00 39.89  ? 111 THR B OG1  1 
ATOM   3239 C CG2  . THR B 1 111 ? -1.840  16.168  -16.935 1.00 40.51  ? 111 THR B CG2  1 
ATOM   3240 N N    . PHE B 1 112 ? -3.880  12.288  -16.891 1.00 36.87  ? 112 PHE B N    1 
ATOM   3241 C CA   . PHE B 1 112 ? -4.217  10.905  -17.184 1.00 38.19  ? 112 PHE B CA   1 
ATOM   3242 C C    . PHE B 1 112 ? -5.021  10.851  -18.467 1.00 35.12  ? 112 PHE B C    1 
ATOM   3243 O O    . PHE B 1 112 ? -5.497  11.883  -18.964 1.00 36.91  ? 112 PHE B O    1 
ATOM   3244 C CB   . PHE B 1 112 ? -4.994  10.247  -16.024 1.00 40.28  ? 112 PHE B CB   1 
ATOM   3245 C CG   . PHE B 1 112 ? -6.312  10.947  -15.645 1.00 37.07  ? 112 PHE B CG   1 
ATOM   3246 C CD1  . PHE B 1 112 ? -6.344  11.908  -14.628 1.00 37.16  ? 112 PHE B CD1  1 
ATOM   3247 C CD2  . PHE B 1 112 ? -7.511  10.570  -16.241 1.00 35.22  ? 112 PHE B CD2  1 
ATOM   3248 C CE1  . PHE B 1 112 ? -7.558  12.512  -14.244 1.00 41.12  ? 112 PHE B CE1  1 
ATOM   3249 C CE2  . PHE B 1 112 ? -8.741  11.155  -15.858 1.00 34.75  ? 112 PHE B CE2  1 
ATOM   3250 C CZ   . PHE B 1 112 ? -8.773  12.132  -14.878 1.00 35.42  ? 112 PHE B CZ   1 
ATOM   3251 N N    . SER B 1 113 ? -5.105  9.651   -19.038 1.00 34.55  ? 113 SER B N    1 
ATOM   3252 C CA   . SER B 1 113 ? -5.897  9.416   -20.241 1.00 34.38  ? 113 SER B CA   1 
ATOM   3253 C C    . SER B 1 113 ? -7.272  8.883   -19.867 1.00 32.79  ? 113 SER B C    1 
ATOM   3254 O O    . SER B 1 113 ? -7.432  8.145   -18.891 1.00 35.08  ? 113 SER B O    1 
ATOM   3255 C CB   . SER B 1 113 ? -5.237  8.418   -21.200 1.00 35.99  ? 113 SER B CB   1 
ATOM   3256 O OG   . SER B 1 113 ? -4.000  8.899   -21.659 1.00 40.56  ? 113 SER B OG   1 
ATOM   3257 N N    . VAL B 1 114 ? -8.258  9.281   -20.653 1.00 31.59  ? 114 VAL B N    1 
ATOM   3258 C CA   . VAL B 1 114 ? -9.645  8.879   -20.497 1.00 31.61  ? 114 VAL B CA   1 
ATOM   3259 C C    . VAL B 1 114 ? -10.057 8.123   -21.749 1.00 32.47  ? 114 VAL B C    1 
ATOM   3260 O O    . VAL B 1 114 ? -9.939  8.643   -22.861 1.00 29.55  ? 114 VAL B O    1 
ATOM   3261 C CB   . VAL B 1 114 ? -10.580 10.093  -20.288 1.00 35.12  ? 114 VAL B CB   1 
ATOM   3262 C CG1  . VAL B 1 114 ? -12.029 9.618   -20.267 1.00 33.46  ? 114 VAL B CG1  1 
ATOM   3263 C CG2  . VAL B 1 114 ? -10.253 10.836  -18.985 1.00 32.51  ? 114 VAL B CG2  1 
ATOM   3264 N N    . LEU B 1 115 ? -10.578 6.916   -21.563 1.00 32.61  ? 115 LEU B N    1 
ATOM   3265 C CA   . LEU B 1 115 ? -11.194 6.148   -22.645 1.00 32.60  ? 115 LEU B CA   1 
ATOM   3266 C C    . LEU B 1 115 ? -12.698 6.296   -22.468 1.00 31.07  ? 115 LEU B C    1 
ATOM   3267 O O    . LEU B 1 115 ? -13.299 5.652   -21.601 1.00 31.72  ? 115 LEU B O    1 
ATOM   3268 C CB   . LEU B 1 115 ? -10.752 4.682   -22.593 1.00 34.94  ? 115 LEU B CB   1 
ATOM   3269 C CG   . LEU B 1 115 ? -11.426 3.793   -23.646 1.00 37.11  ? 115 LEU B CG   1 
ATOM   3270 C CD1  . LEU B 1 115 ? -10.873 4.127   -25.018 1.00 35.10  ? 115 LEU B CD1  1 
ATOM   3271 C CD2  . LEU B 1 115 ? -11.234 2.311   -23.299 1.00 36.22  ? 115 LEU B CD2  1 
ATOM   3272 N N    . ALA B 1 116 ? -13.281 7.192   -23.240 1.00 30.59  ? 116 ALA B N    1 
ATOM   3273 C CA   . ALA B 1 116 ? -14.710 7.443   -23.171 1.00 38.43  ? 116 ALA B CA   1 
ATOM   3274 C C    . ALA B 1 116 ? -15.451 6.282   -23.818 1.00 40.67  ? 116 ALA B C    1 
ATOM   3275 O O    . ALA B 1 116 ? -15.149 5.902   -24.955 1.00 37.76  ? 116 ALA B O    1 
ATOM   3276 C CB   . ALA B 1 116 ? -15.068 8.766   -23.865 1.00 32.12  ? 116 ALA B CB   1 
ATOM   3277 N N    . CYS B 1 117 ? -16.440 5.745   -23.097 1.00 37.31  ? 117 CYS B N    1 
ATOM   3278 C CA   . CYS B 1 117 ? -17.142 4.530   -23.467 1.00 42.90  ? 117 CYS B CA   1 
ATOM   3279 C C    . CYS B 1 117 ? -18.646 4.722   -23.352 1.00 44.80  ? 117 CYS B C    1 
ATOM   3280 O O    . CYS B 1 117 ? -19.120 5.457   -22.482 1.00 41.97  ? 117 CYS B O    1 
ATOM   3281 C CB   . CYS B 1 117 ? -16.727 3.377   -22.567 1.00 40.84  ? 117 CYS B CB   1 
ATOM   3282 S SG   . CYS B 1 117 ? -15.077 2.828   -22.906 1.00 44.39  ? 117 CYS B SG   1 
ATOM   3283 N N    . TYR B 1 118 ? -19.383 4.032   -24.232 1.00 47.09  ? 118 TYR B N    1 
ATOM   3284 C CA   . TYR B 1 118 ? -20.851 3.986   -24.221 1.00 49.30  ? 118 TYR B CA   1 
ATOM   3285 C C    . TYR B 1 118 ? -21.300 2.540   -24.440 1.00 52.36  ? 118 TYR B C    1 
ATOM   3286 O O    . TYR B 1 118 ? -20.863 1.876   -25.395 1.00 53.05  ? 118 TYR B O    1 
ATOM   3287 C CB   . TYR B 1 118 ? -21.453 4.936   -25.280 1.00 48.34  ? 118 TYR B CB   1 
ATOM   3288 C CG   . TYR B 1 118 ? -21.065 6.381   -24.994 1.00 51.97  ? 118 TYR B CG   1 
ATOM   3289 C CD1  . TYR B 1 118 ? -21.825 7.170   -24.116 1.00 49.63  ? 118 TYR B CD1  1 
ATOM   3290 C CD2  . TYR B 1 118 ? -19.885 6.929   -25.515 1.00 49.19  ? 118 TYR B CD2  1 
ATOM   3291 C CE1  . TYR B 1 118 ? -21.461 8.475   -23.809 1.00 46.21  ? 118 TYR B CE1  1 
ATOM   3292 C CE2  . TYR B 1 118 ? -19.501 8.240   -25.198 1.00 48.58  ? 118 TYR B CE2  1 
ATOM   3293 C CZ   . TYR B 1 118 ? -20.298 9.002   -24.347 1.00 47.44  ? 118 TYR B CZ   1 
ATOM   3294 O OH   . TYR B 1 118 ? -19.932 10.288  -24.028 1.00 44.18  ? 118 TYR B OH   1 
ATOM   3295 N N    . ASN B 1 119 ? -22.101 2.032   -23.502 1.00 48.81  ? 119 ASN B N    1 
ATOM   3296 C CA   . ASN B 1 119 ? -22.637 0.672   -23.558 1.00 53.00  ? 119 ASN B CA   1 
ATOM   3297 C C    . ASN B 1 119 ? -21.523 -0.364  -23.536 1.00 55.29  ? 119 ASN B C    1 
ATOM   3298 O O    . ASN B 1 119 ? -21.630 -1.422  -24.169 1.00 53.12  ? 119 ASN B O    1 
ATOM   3299 C CB   . ASN B 1 119 ? -23.523 0.485   -24.793 1.00 52.25  ? 119 ASN B CB   1 
ATOM   3300 C CG   . ASN B 1 119 ? -24.778 1.302   -24.707 1.00 55.85  ? 119 ASN B CG   1 
ATOM   3301 O OD1  . ASN B 1 119 ? -24.963 2.242   -25.475 1.00 64.65  ? 119 ASN B OD1  1 
ATOM   3302 N ND2  . ASN B 1 119 ? -25.627 0.989   -23.732 1.00 57.40  ? 119 ASN B ND2  1 
ATOM   3303 N N    . GLY B 1 120 ? -20.457 -0.057  -22.792 1.00 52.24  ? 120 GLY B N    1 
ATOM   3304 C CA   . GLY B 1 120 ? -19.295 -0.917  -22.724 1.00 48.69  ? 120 GLY B CA   1 
ATOM   3305 C C    . GLY B 1 120 ? -18.447 -0.966  -23.975 1.00 49.85  ? 120 GLY B C    1 
ATOM   3306 O O    . GLY B 1 120 ? -17.611 -1.873  -24.104 1.00 50.32  ? 120 GLY B O    1 
ATOM   3307 N N    . SER B 1 121 ? -18.620 -0.014  -24.895 1.00 49.51  ? 121 SER B N    1 
ATOM   3308 C CA   . SER B 1 121 ? -17.851 0.035   -26.139 1.00 55.83  ? 121 SER B CA   1 
ATOM   3309 C C    . SER B 1 121 ? -16.996 1.295   -26.216 1.00 53.40  ? 121 SER B C    1 
ATOM   3310 O O    . SER B 1 121 ? -17.545 2.412   -26.209 1.00 50.05  ? 121 SER B O    1 
ATOM   3311 C CB   . SER B 1 121 ? -18.772 -0.048  -27.362 1.00 57.01  ? 121 SER B CB   1 
ATOM   3312 O OG   . SER B 1 121 ? -19.221 -1.386  -27.547 1.00 67.19  ? 121 SER B OG   1 
ATOM   3313 N N    . PRO B 1 122 ? -15.666 1.172   -26.316 1.00 50.08  ? 122 PRO B N    1 
ATOM   3314 C CA   . PRO B 1 122 ? -14.814 2.370   -26.407 1.00 47.17  ? 122 PRO B CA   1 
ATOM   3315 C C    . PRO B 1 122 ? -15.210 3.260   -27.574 1.00 51.07  ? 122 PRO B C    1 
ATOM   3316 O O    . PRO B 1 122 ? -15.458 2.791   -28.683 1.00 57.62  ? 122 PRO B O    1 
ATOM   3317 C CB   . PRO B 1 122 ? -13.401 1.804   -26.607 1.00 51.89  ? 122 PRO B CB   1 
ATOM   3318 C CG   . PRO B 1 122 ? -13.525 0.268   -26.523 1.00 56.58  ? 122 PRO B CG   1 
ATOM   3319 C CD   . PRO B 1 122 ? -14.903 -0.069  -26.070 1.00 51.87  ? 122 PRO B CD   1 
ATOM   3320 N N    . SER B 1 123 ? -15.249 4.562   -27.318 1.00 48.94  ? 123 SER B N    1 
ATOM   3321 C CA   . SER B 1 123 ? -15.591 5.547   -28.335 1.00 52.90  ? 123 SER B CA   1 
ATOM   3322 C C    . SER B 1 123 ? -14.440 6.491   -28.690 1.00 50.86  ? 123 SER B C    1 
ATOM   3323 O O    . SER B 1 123 ? -14.330 6.904   -29.852 1.00 50.46  ? 123 SER B O    1 
ATOM   3324 C CB   . SER B 1 123 ? -16.804 6.364   -27.867 1.00 52.80  ? 123 SER B CB   1 
ATOM   3325 O OG   . SER B 1 123 ? -16.831 7.660   -28.420 1.00 56.95  ? 123 SER B OG   1 
ATOM   3326 N N    . GLY B 1 124 ? -13.584 6.841   -27.732 1.00 41.92  ? 124 GLY B N    1 
ATOM   3327 C CA   . GLY B 1 124 ? -12.495 7.762   -28.004 1.00 37.39  ? 124 GLY B CA   1 
ATOM   3328 C C    . GLY B 1 124 ? -11.613 7.912   -26.782 1.00 39.85  ? 124 GLY B C    1 
ATOM   3329 O O    . GLY B 1 124 ? -11.986 7.544   -25.660 1.00 33.12  ? 124 GLY B O    1 
ATOM   3330 N N    . VAL B 1 125 ? -10.416 8.428   -27.023 1.00 37.10  ? 125 VAL B N    1 
ATOM   3331 C CA   . VAL B 1 125 ? -9.430  8.590   -25.962 1.00 34.21  ? 125 VAL B CA   1 
ATOM   3332 C C    . VAL B 1 125 ? -8.883  10.011  -26.024 1.00 34.62  ? 125 VAL B C    1 
ATOM   3333 O O    . VAL B 1 125 ? -8.712  10.563  -27.112 1.00 32.76  ? 125 VAL B O    1 
ATOM   3334 C CB   . VAL B 1 125 ? -8.303  7.551   -26.099 1.00 34.02  ? 125 VAL B CB   1 
ATOM   3335 C CG1  . VAL B 1 125 ? -7.469  7.871   -27.328 1.00 36.20  ? 125 VAL B CG1  1 
ATOM   3336 C CG2  . VAL B 1 125 ? -7.441  7.525   -24.880 1.00 34.58  ? 125 VAL B CG2  1 
ATOM   3337 N N    . TYR B 1 126 ? -8.616  10.607  -24.861 1.00 36.54  ? 126 TYR B N    1 
ATOM   3338 C CA   . TYR B 1 126 ? -8.033  11.950  -24.804 1.00 35.91  ? 126 TYR B CA   1 
ATOM   3339 C C    . TYR B 1 126 ? -7.354  12.110  -23.446 1.00 35.21  ? 126 TYR B C    1 
ATOM   3340 O O    . TYR B 1 126 ? -7.572  11.317  -22.518 1.00 33.19  ? 126 TYR B O    1 
ATOM   3341 C CB   . TYR B 1 126 ? -9.101  13.052  -25.052 1.00 36.61  ? 126 TYR B CB   1 
ATOM   3342 C CG   . TYR B 1 126 ? -10.302 12.950  -24.108 1.00 39.37  ? 126 TYR B CG   1 
ATOM   3343 C CD1  . TYR B 1 126 ? -10.281 13.552  -22.851 1.00 42.55  ? 126 TYR B CD1  1 
ATOM   3344 C CD2  . TYR B 1 126 ? -11.431 12.224  -24.457 1.00 40.84  ? 126 TYR B CD2  1 
ATOM   3345 C CE1  . TYR B 1 126 ? -11.370 13.442  -21.963 1.00 40.50  ? 126 TYR B CE1  1 
ATOM   3346 C CE2  . TYR B 1 126 ? -12.529 12.118  -23.587 1.00 42.77  ? 126 TYR B CE2  1 
ATOM   3347 C CZ   . TYR B 1 126 ? -12.486 12.722  -22.337 1.00 41.64  ? 126 TYR B CZ   1 
ATOM   3348 O OH   . TYR B 1 126 ? -13.568 12.618  -21.474 1.00 41.61  ? 126 TYR B OH   1 
ATOM   3349 N N    . GLN B 1 127 ? -6.543  13.167  -23.324 1.00 34.14  ? 127 GLN B N    1 
ATOM   3350 C CA   . GLN B 1 127 ? -5.785  13.431  -22.102 1.00 40.99  ? 127 GLN B CA   1 
ATOM   3351 C C    . GLN B 1 127 ? -6.441  14.551  -21.286 1.00 39.67  ? 127 GLN B C    1 
ATOM   3352 O O    . GLN B 1 127 ? -6.993  15.499  -21.842 1.00 39.34  ? 127 GLN B O    1 
ATOM   3353 C CB   . GLN B 1 127 ? -4.336  13.791  -22.435 1.00 33.93  ? 127 GLN B CB   1 
ATOM   3354 C CG   . GLN B 1 127 ? -3.402  13.756  -21.258 1.00 42.81  ? 127 GLN B CG   1 
ATOM   3355 C CD   . GLN B 1 127 ? -2.703  12.405  -21.085 1.00 44.98  ? 127 GLN B CD   1 
ATOM   3356 O OE1  . GLN B 1 127 ? -3.238  11.366  -21.456 1.00 41.38  ? 127 GLN B OE1  1 
ATOM   3357 N NE2  . GLN B 1 127 ? -1.493  12.426  -20.520 1.00 45.28  ? 127 GLN B NE2  1 
ATOM   3358 N N    . CYS B 1 128 ? -6.386  14.439  -19.959 1.00 38.34  ? 128 CYS B N    1 
ATOM   3359 C CA   A CYS B 1 128 ? -7.051  15.362  -19.037 0.53 38.38  ? 128 CYS B CA   1 
ATOM   3360 C CA   B CYS B 1 128 ? -6.923  15.515  -19.147 0.47 38.40  ? 128 CYS B CA   1 
ATOM   3361 C C    . CYS B 1 128 ? -6.141  15.622  -17.851 1.00 40.35  ? 128 CYS B C    1 
ATOM   3362 O O    . CYS B 1 128 ? -5.312  14.771  -17.500 1.00 39.33  ? 128 CYS B O    1 
ATOM   3363 C CB   A CYS B 1 128 ? -8.360  14.792  -18.473 0.53 37.87  ? 128 CYS B CB   1 
ATOM   3364 C CB   B CYS B 1 128 ? -8.407  15.316  -18.863 0.47 38.76  ? 128 CYS B CB   1 
ATOM   3365 S SG   A CYS B 1 128 ? -9.780  14.828  -19.527 0.53 40.36  ? 128 CYS B SG   1 
ATOM   3366 S SG   B CYS B 1 128 ? -8.695  13.946  -17.791 0.47 39.02  ? 128 CYS B SG   1 
ATOM   3367 N N    . ALA B 1 129 ? -6.368  16.737  -17.169 1.00 37.07  ? 129 ALA B N    1 
ATOM   3368 C CA   . ALA B 1 129 ? -5.694  16.996  -15.912 1.00 40.09  ? 129 ALA B CA   1 
ATOM   3369 C C    . ALA B 1 129 ? -6.713  17.044  -14.781 1.00 36.86  ? 129 ALA B C    1 
ATOM   3370 O O    . ALA B 1 129 ? -7.835  17.522  -14.950 1.00 37.23  ? 129 ALA B O    1 
ATOM   3371 C CB   . ALA B 1 129 ? -4.893  18.287  -15.960 1.00 42.07  ? 129 ALA B CB   1 
ATOM   3372 N N    . MET B 1 130 ? -6.336  16.518  -13.633 1.00 38.51  ? 130 MET B N    1 
ATOM   3373 C CA   . MET B 1 130 ? -7.145  16.732  -12.446 1.00 40.86  ? 130 MET B CA   1 
ATOM   3374 C C    . MET B 1 130 ? -6.915  18.172  -11.981 1.00 39.48  ? 130 MET B C    1 
ATOM   3375 O O    . MET B 1 130 ? -5.846  18.484  -11.444 1.00 42.56  ? 130 MET B O    1 
ATOM   3376 C CB   . MET B 1 130 ? -6.780  15.709  -11.370 1.00 41.03  ? 130 MET B CB   1 
ATOM   3377 C CG   . MET B 1 130 ? -7.505  15.855  -10.020 1.00 40.60  ? 130 MET B CG   1 
ATOM   3378 S SD   . MET B 1 130 ? -9.265  15.706  -10.365 1.00 50.45  ? 130 MET B SD   1 
ATOM   3379 C CE   . MET B 1 130 ? -9.352  13.990  -10.889 1.00 43.87  ? 130 MET B CE   1 
ATOM   3380 N N    . ARG B 1 131 ? -7.904  19.056  -12.224 1.00 41.74  ? 131 ARG B N    1 
ATOM   3381 C CA   . ARG B 1 131 ? -7.799  20.461  -11.812 1.00 41.83  ? 131 ARG B CA   1 
ATOM   3382 C C    . ARG B 1 131 ? -7.545  20.575  -10.318 1.00 45.85  ? 131 ARG B C    1 
ATOM   3383 O O    . ARG B 1 131 ? -7.842  19.658  -9.548  1.00 44.63  ? 131 ARG B O    1 
ATOM   3384 C CB   . ARG B 1 131 ? -9.076  21.238  -12.124 1.00 38.86  ? 131 ARG B CB   1 
ATOM   3385 C CG   . ARG B 1 131 ? -9.613  21.125  -13.536 1.00 39.62  ? 131 ARG B CG   1 
ATOM   3386 C CD   . ARG B 1 131 ? -8.786  21.817  -14.602 1.00 46.10  ? 131 ARG B CD   1 
ATOM   3387 N NE   . ARG B 1 131 ? -8.164  23.052  -14.145 1.00 48.14  ? 131 ARG B NE   1 
ATOM   3388 C CZ   . ARG B 1 131 ? -7.050  23.539  -14.666 1.00 47.29  ? 131 ARG B CZ   1 
ATOM   3389 N NH1  . ARG B 1 131 ? -6.454  22.947  -15.692 1.00 45.19  ? 131 ARG B NH1  1 
ATOM   3390 N NH2  . ARG B 1 131 ? -6.517  24.635  -14.144 1.00 43.36  ? 131 ARG B NH2  1 
ATOM   3391 N N    . PRO B 1 132 ? -7.008  21.712  -9.876  1.00 46.67  ? 132 PRO B N    1 
ATOM   3392 C CA   . PRO B 1 132 ? -6.836  21.915  -8.442  1.00 46.68  ? 132 PRO B CA   1 
ATOM   3393 C C    . PRO B 1 132 ? -8.132  21.829  -7.667  1.00 43.91  ? 132 PRO B C    1 
ATOM   3394 O O    . PRO B 1 132 ? -8.098  21.558  -6.467  1.00 46.53  ? 132 PRO B O    1 
ATOM   3395 C CB   . PRO B 1 132 ? -6.206  23.318  -8.349  1.00 50.93  ? 132 PRO B CB   1 
ATOM   3396 C CG   . PRO B 1 132 ? -5.546  23.516  -9.617  1.00 49.75  ? 132 PRO B CG   1 
ATOM   3397 C CD   . PRO B 1 132 ? -6.474  22.844  -10.645 1.00 49.88  ? 132 PRO B CD   1 
ATOM   3398 N N    . ASN B 1 133 ? -9.267  22.062  -8.301  1.00 43.28  ? 133 ASN B N    1 
ATOM   3399 C CA   . ASN B 1 133 ? -10.556 21.984  -7.637  1.00 44.95  ? 133 ASN B CA   1 
ATOM   3400 C C    . ASN B 1 133 ? -11.212 20.612  -7.844  1.00 45.44  ? 133 ASN B C    1 
ATOM   3401 O O    . ASN B 1 133 ? -12.433 20.478  -7.670  1.00 44.13  ? 133 ASN B O    1 
ATOM   3402 C CB   . ASN B 1 133 ? -11.466 23.112  -8.149  1.00 44.98  ? 133 ASN B CB   1 
ATOM   3403 C CG   . ASN B 1 133 ? -11.867 22.915  -9.601  1.00 46.14  ? 133 ASN B CG   1 
ATOM   3404 O OD1  . ASN B 1 133 ? -11.453 21.952  -10.240 1.00 40.73  ? 133 ASN B OD1  1 
ATOM   3405 N ND2  . ASN B 1 133 ? -12.669 23.839  -10.138 1.00 48.37  ? 133 ASN B ND2  1 
ATOM   3406 N N    . PHE B 1 134 ? -10.438 19.620  -8.303  1.00 42.32  ? 134 PHE B N    1 
ATOM   3407 C CA   . PHE B 1 134 ? -10.830 18.212  -8.307  1.00 40.41  ? 134 PHE B CA   1 
ATOM   3408 C C    . PHE B 1 134 ? -11.935 17.897  -9.303  1.00 38.85  ? 134 PHE B C    1 
ATOM   3409 O O    . PHE B 1 134 ? -12.689 16.959  -9.094  1.00 41.88  ? 134 PHE B O    1 
ATOM   3410 C CB   . PHE B 1 134 ? -11.228 17.749  -6.908  1.00 41.48  ? 134 PHE B CB   1 
ATOM   3411 C CG   . PHE B 1 134 ? -10.055 17.591  -5.977  1.00 43.12  ? 134 PHE B CG   1 
ATOM   3412 C CD1  . PHE B 1 134 ? -9.131  16.599  -6.182  1.00 43.42  ? 134 PHE B CD1  1 
ATOM   3413 C CD2  . PHE B 1 134 ? -9.839  18.495  -4.952  1.00 44.48  ? 134 PHE B CD2  1 
ATOM   3414 C CE1  . PHE B 1 134 ? -8.032  16.451  -5.318  1.00 48.00  ? 134 PHE B CE1  1 
ATOM   3415 C CE2  . PHE B 1 134 ? -8.757  18.372  -4.092  1.00 47.31  ? 134 PHE B CE2  1 
ATOM   3416 C CZ   . PHE B 1 134 ? -7.838  17.344  -4.272  1.00 49.21  ? 134 PHE B CZ   1 
ATOM   3417 N N    . THR B 1 135 ? -12.048 18.679  -10.374 1.00 38.63  ? 135 THR B N    1 
ATOM   3418 C CA   . THR B 1 135 ? -12.866 18.377  -11.535 1.00 37.64  ? 135 THR B CA   1 
ATOM   3419 C C    . THR B 1 135 ? -11.984 18.141  -12.758 1.00 35.84  ? 135 THR B C    1 
ATOM   3420 O O    . THR B 1 135 ? -10.785 18.412  -12.768 1.00 39.50  ? 135 THR B O    1 
ATOM   3421 C CB   . THR B 1 135 ? -13.849 19.525  -11.823 1.00 41.92  ? 135 THR B CB   1 
ATOM   3422 O OG1  . THR B 1 135 ? -13.112 20.674  -12.253 1.00 37.27  ? 135 THR B OG1  1 
ATOM   3423 C CG2  . THR B 1 135 ? -14.595 19.890  -10.587 1.00 43.18  ? 135 THR B CG2  1 
ATOM   3424 N N    . ILE B 1 136 ? -12.590 17.671  -13.822 1.00 35.44  ? 136 ILE B N    1 
ATOM   3425 C CA   . ILE B 1 136 ? -11.877 17.539  -15.090 1.00 41.37  ? 136 ILE B CA   1 
ATOM   3426 C C    . ILE B 1 136 ? -12.709 18.141  -16.215 1.00 42.30  ? 136 ILE B C    1 
ATOM   3427 O O    . ILE B 1 136 ? -13.931 18.259  -16.111 1.00 36.61  ? 136 ILE B O    1 
ATOM   3428 C CB   . ILE B 1 136 ? -11.499 16.077  -15.401 1.00 37.34  ? 136 ILE B CB   1 
ATOM   3429 C CG1  . ILE B 1 136 ? -12.739 15.244  -15.751 1.00 39.57  ? 136 ILE B CG1  1 
ATOM   3430 C CG2  . ILE B 1 136 ? -10.713 15.491  -14.234 1.00 34.85  ? 136 ILE B CG2  1 
ATOM   3431 C CD1  . ILE B 1 136 ? -12.417 13.794  -16.083 1.00 34.76  ? 136 ILE B CD1  1 
ATOM   3432 N N    . LYS B 1 137 ? -12.020 18.582  -17.273 1.00 41.10  ? 137 LYS B N    1 
ATOM   3433 C CA   . LYS B 1 137 ? -12.643 19.196  -18.445 1.00 42.14  ? 137 LYS B CA   1 
ATOM   3434 C C    . LYS B 1 137 ? -12.613 18.146  -19.550 1.00 44.48  ? 137 LYS B C    1 
ATOM   3435 O O    . LYS B 1 137 ? -11.641 18.026  -20.307 1.00 47.08  ? 137 LYS B O    1 
ATOM   3436 C CB   . LYS B 1 137 ? -11.911 20.474  -18.847 1.00 46.86  ? 137 LYS B CB   1 
ATOM   3437 C CG   . LYS B 1 137 ? -12.194 21.690  -17.953 1.00 52.08  ? 137 LYS B CG   1 
ATOM   3438 C CD   . LYS B 1 137 ? -11.571 22.962  -18.523 1.00 55.48  ? 137 LYS B CD   1 
ATOM   3439 C CE   . LYS B 1 137 ? -11.281 23.991  -17.411 1.00 68.35  ? 137 LYS B CE   1 
ATOM   3440 N NZ   . LYS B 1 137 ? -10.033 24.787  -17.737 1.00 68.38  ? 137 LYS B NZ   1 
ATOM   3441 N N    . GLY B 1 138 ? -13.686 17.366  -19.646 1.00 45.70  ? 138 GLY B N    1 
ATOM   3442 C CA   . GLY B 1 138 ? -13.686 16.300  -20.615 1.00 41.91  ? 138 GLY B CA   1 
ATOM   3443 C C    . GLY B 1 138 ? -14.799 16.374  -21.631 1.00 43.17  ? 138 GLY B C    1 
ATOM   3444 O O    . GLY B 1 138 ? -15.275 17.460  -21.987 1.00 46.75  ? 138 GLY B O    1 
ATOM   3445 N N    . SER B 1 139 ? -15.219 15.208  -22.117 1.00 45.46  ? 139 SER B N    1 
ATOM   3446 C CA   . SER B 1 139 ? -16.265 15.091  -23.134 1.00 42.24  ? 139 SER B CA   1 
ATOM   3447 C C    . SER B 1 139 ? -17.023 13.819  -22.783 1.00 39.88  ? 139 SER B C    1 
ATOM   3448 O O    . SER B 1 139 ? -16.579 12.711  -23.103 1.00 37.92  ? 139 SER B O    1 
ATOM   3449 C CB   . SER B 1 139 ? -15.675 15.031  -24.542 1.00 44.09  ? 139 SER B CB   1 
ATOM   3450 O OG   . SER B 1 139 ? -16.684 14.819  -25.533 1.00 42.76  ? 139 SER B OG   1 
ATOM   3451 N N    . PHE B 1 140 ? -18.113 13.983  -22.053 1.00 37.20  ? 140 PHE B N    1 
ATOM   3452 C CA   . PHE B 1 140 ? -18.918 12.871  -21.557 1.00 43.16  ? 140 PHE B CA   1 
ATOM   3453 C C    . PHE B 1 140 ? -20.385 13.184  -21.856 1.00 44.96  ? 140 PHE B C    1 
ATOM   3454 O O    . PHE B 1 140 ? -20.870 14.264  -21.503 1.00 40.26  ? 140 PHE B O    1 
ATOM   3455 C CB   . PHE B 1 140 ? -18.752 12.654  -20.037 1.00 43.01  ? 140 PHE B CB   1 
ATOM   3456 C CG   . PHE B 1 140 ? -17.348 12.291  -19.585 1.00 42.19  ? 140 PHE B CG   1 
ATOM   3457 C CD1  . PHE B 1 140 ? -16.857 11.004  -19.746 1.00 41.51  ? 140 PHE B CD1  1 
ATOM   3458 C CD2  . PHE B 1 140 ? -16.560 13.218  -18.908 1.00 39.85  ? 140 PHE B CD2  1 
ATOM   3459 C CE1  . PHE B 1 140 ? -15.568 10.659  -19.290 1.00 42.78  ? 140 PHE B CE1  1 
ATOM   3460 C CE2  . PHE B 1 140 ? -15.289 12.885  -18.451 1.00 39.68  ? 140 PHE B CE2  1 
ATOM   3461 C CZ   . PHE B 1 140 ? -14.791 11.606  -18.634 1.00 40.12  ? 140 PHE B CZ   1 
ATOM   3462 N N    . LEU B 1 141 ? -21.081 12.266  -22.511 1.00 46.26  ? 141 LEU B N    1 
ATOM   3463 C CA   . LEU B 1 141 ? -22.521 12.377  -22.692 1.00 50.12  ? 141 LEU B CA   1 
ATOM   3464 C C    . LEU B 1 141 ? -23.217 11.444  -21.710 1.00 50.81  ? 141 LEU B C    1 
ATOM   3465 O O    . LEU B 1 141 ? -22.573 10.715  -20.946 1.00 44.14  ? 141 LEU B O    1 
ATOM   3466 C CB   . LEU B 1 141 ? -22.920 12.049  -24.134 1.00 46.60  ? 141 LEU B CB   1 
ATOM   3467 C CG   . LEU B 1 141 ? -22.220 12.970  -25.142 1.00 51.24  ? 141 LEU B CG   1 
ATOM   3468 C CD1  . LEU B 1 141 ? -22.374 12.471  -26.597 1.00 53.48  ? 141 LEU B CD1  1 
ATOM   3469 C CD2  . LEU B 1 141 ? -22.669 14.444  -24.962 1.00 46.73  ? 141 LEU B CD2  1 
ATOM   3470 N N    . ASN B 1 142 ? -24.551 11.498  -21.712 1.00 53.13  ? 142 ASN B N    1 
ATOM   3471 C CA   . ASN B 1 142 ? -25.346 10.526  -20.974 1.00 51.36  ? 142 ASN B CA   1 
ATOM   3472 C C    . ASN B 1 142 ? -24.874 9.122   -21.340 1.00 51.48  ? 142 ASN B C    1 
ATOM   3473 O O    . ASN B 1 142 ? -24.602 8.833   -22.516 1.00 47.71  ? 142 ASN B O    1 
ATOM   3474 C CB   . ASN B 1 142 ? -26.830 10.689  -21.320 1.00 54.57  ? 142 ASN B CB   1 
ATOM   3475 C CG   . ASN B 1 142 ? -27.750 10.277  -20.178 1.00 65.17  ? 142 ASN B CG   1 
ATOM   3476 O OD1  . ASN B 1 142 ? -28.155 9.111   -20.073 1.00 67.54  ? 142 ASN B OD1  1 
ATOM   3477 N ND2  . ASN B 1 142 ? -28.106 11.240  -19.327 1.00 66.76  ? 142 ASN B ND2  1 
ATOM   3478 N N    . GLY B 1 143 ? -24.724 8.266   -20.323 1.00 47.53  ? 143 GLY B N    1 
ATOM   3479 C CA   . GLY B 1 143 ? -24.232 6.918   -20.537 1.00 47.08  ? 143 GLY B CA   1 
ATOM   3480 C C    . GLY B 1 143 ? -22.718 6.745   -20.540 1.00 47.68  ? 143 GLY B C    1 
ATOM   3481 O O    . GLY B 1 143 ? -22.240 5.604   -20.638 1.00 46.47  ? 143 GLY B O    1 
ATOM   3482 N N    . SER B 1 144 ? -21.941 7.822   -20.404 1.00 47.26  ? 144 SER B N    1 
ATOM   3483 C CA   . SER B 1 144 ? -20.485 7.675   -20.320 1.00 41.87  ? 144 SER B CA   1 
ATOM   3484 C C    . SER B 1 144 ? -19.992 7.209   -18.951 1.00 42.02  ? 144 SER B C    1 
ATOM   3485 O O    . SER B 1 144 ? -18.802 6.882   -18.818 1.00 38.50  ? 144 SER B O    1 
ATOM   3486 C CB   . SER B 1 144 ? -19.805 9.013   -20.659 1.00 40.86  ? 144 SER B CB   1 
ATOM   3487 O OG   . SER B 1 144 ? -20.145 10.027  -19.722 1.00 38.90  ? 144 SER B OG   1 
ATOM   3488 N N    . CYS B 1 145 ? -20.879 7.130   -17.953 1.00 41.16  ? 145 CYS B N    1 
ATOM   3489 C CA   . CYS B 1 145 ? -20.496 6.766   -16.594 1.00 41.90  ? 145 CYS B CA   1 
ATOM   3490 C C    . CYS B 1 145 ? -19.825 5.396   -16.528 1.00 41.34  ? 145 CYS B C    1 
ATOM   3491 O O    . CYS B 1 145 ? -20.234 4.450   -17.207 1.00 37.03  ? 145 CYS B O    1 
ATOM   3492 C CB   . CYS B 1 145 ? -21.737 6.773   -15.687 1.00 43.38  ? 145 CYS B CB   1 
ATOM   3493 S SG   . CYS B 1 145 ? -22.220 8.461   -15.266 1.00 51.09  ? 145 CYS B SG   1 
ATOM   3494 N N    . GLY B 1 146 ? -18.835 5.272   -15.633 1.00 36.92  ? 146 GLY B N    1 
ATOM   3495 C CA   . GLY B 1 146 ? -18.000 4.101   -15.609 1.00 38.50  ? 146 GLY B CA   1 
ATOM   3496 C C    . GLY B 1 146 ? -16.842 4.123   -16.579 1.00 34.94  ? 146 GLY B C    1 
ATOM   3497 O O    . GLY B 1 146 ? -15.986 3.238   -16.491 1.00 36.33  ? 146 GLY B O    1 
ATOM   3498 N N    . SER B 1 147 ? -16.778 5.102   -17.498 1.00 34.91  ? 147 SER B N    1 
ATOM   3499 C CA   . SER B 1 147 ? -15.549 5.322   -18.262 1.00 37.22  ? 147 SER B CA   1 
ATOM   3500 C C    . SER B 1 147 ? -14.400 5.646   -17.301 1.00 35.82  ? 147 SER B C    1 
ATOM   3501 O O    . SER B 1 147 ? -14.603 6.272   -16.258 1.00 34.13  ? 147 SER B O    1 
ATOM   3502 C CB   . SER B 1 147 ? -15.712 6.468   -19.248 1.00 34.16  ? 147 SER B CB   1 
ATOM   3503 O OG   . SER B 1 147 ? -16.711 6.198   -20.214 1.00 31.24  ? 147 SER B OG   1 
ATOM   3504 N N    . VAL B 1 148 ? -13.189 5.193   -17.635 1.00 33.92  ? 148 VAL B N    1 
ATOM   3505 C CA   . VAL B 1 148 ? -12.100 5.278   -16.674 1.00 34.90  ? 148 VAL B CA   1 
ATOM   3506 C C    . VAL B 1 148 ? -10.946 6.090   -17.240 1.00 34.38  ? 148 VAL B C    1 
ATOM   3507 O O    . VAL B 1 148 ? -10.767 6.201   -18.451 1.00 33.43  ? 148 VAL B O    1 
ATOM   3508 C CB   . VAL B 1 148 ? -11.642 3.876   -16.233 1.00 36.24  ? 148 VAL B CB   1 
ATOM   3509 C CG1  . VAL B 1 148 ? -12.817 3.111   -15.628 1.00 36.93  ? 148 VAL B CG1  1 
ATOM   3510 C CG2  . VAL B 1 148 ? -11.055 3.139   -17.403 1.00 35.95  ? 148 VAL B CG2  1 
ATOM   3511 N N    . GLY B 1 149 ? -10.191 6.702   -16.327 1.00 35.13  ? 149 GLY B N    1 
ATOM   3512 C CA   . GLY B 1 149 ? -8.955  7.393   -16.642 1.00 35.11  ? 149 GLY B CA   1 
ATOM   3513 C C    . GLY B 1 149 ? -7.772  6.588   -16.121 1.00 36.52  ? 149 GLY B C    1 
ATOM   3514 O O    . GLY B 1 149 ? -7.886  5.866   -15.134 1.00 37.69  ? 149 GLY B O    1 
ATOM   3515 N N    . PHE B 1 150 ? -6.627  6.711   -16.796 1.00 36.52  ? 150 PHE B N    1 
ATOM   3516 C CA   . PHE B 1 150 ? -5.521  5.810   -16.484 1.00 39.70  ? 150 PHE B CA   1 
ATOM   3517 C C    . PHE B 1 150 ? -4.196  6.371   -16.985 1.00 38.12  ? 150 PHE B C    1 
ATOM   3518 O O    . PHE B 1 150 ? -4.140  7.193   -17.904 1.00 36.98  ? 150 PHE B O    1 
ATOM   3519 C CB   . PHE B 1 150 ? -5.750  4.433   -17.103 1.00 37.94  ? 150 PHE B CB   1 
ATOM   3520 C CG   . PHE B 1 150 ? -5.833  4.480   -18.593 1.00 36.53  ? 150 PHE B CG   1 
ATOM   3521 C CD1  . PHE B 1 150 ? -7.024  4.822   -19.216 1.00 37.31  ? 150 PHE B CD1  1 
ATOM   3522 C CD2  . PHE B 1 150 ? -4.737  4.191   -19.372 1.00 36.70  ? 150 PHE B CD2  1 
ATOM   3523 C CE1  . PHE B 1 150 ? -7.109  4.895   -20.615 1.00 36.84  ? 150 PHE B CE1  1 
ATOM   3524 C CE2  . PHE B 1 150 ? -4.802  4.249   -20.751 1.00 35.45  ? 150 PHE B CE2  1 
ATOM   3525 C CZ   . PHE B 1 150 ? -5.982  4.600   -21.376 1.00 38.05  ? 150 PHE B CZ   1 
ATOM   3526 N N    . ASN B 1 151 ? -3.136  5.857   -16.388 1.00 40.45  ? 151 ASN B N    1 
ATOM   3527 C CA   . ASN B 1 151 ? -1.756  6.006   -16.829 1.00 49.22  ? 151 ASN B CA   1 
ATOM   3528 C C    . ASN B 1 151 ? -1.157  4.617   -17.061 1.00 52.80  ? 151 ASN B C    1 
ATOM   3529 O O    . ASN B 1 151 ? -1.481  3.649   -16.348 1.00 50.55  ? 151 ASN B O    1 
ATOM   3530 C CB   . ASN B 1 151 ? -0.931  6.813   -15.789 1.00 47.51  ? 151 ASN B CB   1 
ATOM   3531 C CG   . ASN B 1 151 ? -1.346  8.280   -15.747 1.00 46.13  ? 151 ASN B CG   1 
ATOM   3532 O OD1  . ASN B 1 151 ? -2.055  8.718   -14.839 1.00 46.10  ? 151 ASN B OD1  1 
ATOM   3533 N ND2  . ASN B 1 151 ? -0.951  9.023   -16.756 1.00 46.39  ? 151 ASN B ND2  1 
ATOM   3534 N N    . ILE B 1 152 ? -0.257  4.541   -18.043 1.00 55.54  ? 152 ILE B N    1 
ATOM   3535 C CA   . ILE B 1 152 ? 0.515   3.337   -18.361 1.00 62.61  ? 152 ILE B CA   1 
ATOM   3536 C C    . ILE B 1 152 ? 1.967   3.607   -17.977 1.00 76.82  ? 152 ILE B C    1 
ATOM   3537 O O    . ILE B 1 152 ? 2.566   4.570   -18.475 1.00 73.03  ? 152 ILE B O    1 
ATOM   3538 C CB   . ILE B 1 152 ? 0.389   2.946   -19.840 1.00 61.85  ? 152 ILE B CB   1 
ATOM   3539 C CG1  . ILE B 1 152 ? -1.093  2.760   -20.220 1.00 56.23  ? 152 ILE B CG1  1 
ATOM   3540 C CG2  . ILE B 1 152 ? 1.164   1.661   -20.094 1.00 71.98  ? 152 ILE B CG2  1 
ATOM   3541 C CD1  . ILE B 1 152 ? -1.309  1.975   -21.496 1.00 56.30  ? 152 ILE B CD1  1 
ATOM   3542 N N    . ASP B 1 153 ? 2.524   2.792   -17.056 1.00 99.90  ? 153 ASP B N    1 
ATOM   3543 C CA   . ASP B 1 153 ? 3.917   2.988   -16.650 1.00 103.46 ? 153 ASP B CA   1 
ATOM   3544 C C    . ASP B 1 153 ? 4.870   2.379   -17.661 1.00 112.96 ? 153 ASP B C    1 
ATOM   3545 O O    . ASP B 1 153 ? 5.709   3.083   -18.226 1.00 124.89 ? 153 ASP B O    1 
ATOM   3546 C CB   . ASP B 1 153 ? 4.186   2.250   -15.328 1.00 107.37 ? 153 ASP B CB   1 
ATOM   3547 C CG   . ASP B 1 153 ? 3.420   2.802   -14.151 1.00 117.60 ? 153 ASP B CG   1 
ATOM   3548 O OD1  . ASP B 1 153 ? 2.168   2.927   -14.231 1.00 105.44 ? 153 ASP B OD1  1 
ATOM   3549 O OD2  . ASP B 1 153 ? 4.082   3.029   -13.110 1.00 114.79 ? 153 ASP B OD2  1 
ATOM   3550 N N    . TYR B 1 154 ? 4.713   1.093   -17.952 1.00 123.83 ? 154 TYR B N    1 
ATOM   3551 C CA   . TYR B 1 154 ? 5.400   0.461   -19.071 1.00 124.28 ? 154 TYR B CA   1 
ATOM   3552 C C    . TYR B 1 154 ? 4.561   -0.734  -19.481 1.00 123.41 ? 154 TYR B C    1 
ATOM   3553 O O    . TYR B 1 154 ? 4.022   -0.794  -20.592 1.00 121.75 ? 154 TYR B O    1 
ATOM   3554 C CB   . TYR B 1 154 ? 6.868   0.139   -18.765 1.00 128.45 ? 154 TYR B CB   1 
ATOM   3555 C CG   . TYR B 1 154 ? 7.670   1.423   -18.879 1.00 133.73 ? 154 TYR B CG   1 
ATOM   3556 C CD1  . TYR B 1 154 ? 7.941   1.974   -20.132 1.00 129.81 ? 154 TYR B CD1  1 
ATOM   3557 C CD2  . TYR B 1 154 ? 8.131   2.104   -17.749 1.00 131.34 ? 154 TYR B CD2  1 
ATOM   3558 C CE1  . TYR B 1 154 ? 8.642   3.166   -20.264 1.00 130.53 ? 154 TYR B CE1  1 
ATOM   3559 C CE2  . TYR B 1 154 ? 8.835   3.304   -17.871 1.00 128.99 ? 154 TYR B CE2  1 
ATOM   3560 C CZ   . TYR B 1 154 ? 9.093   3.826   -19.133 1.00 131.66 ? 154 TYR B CZ   1 
ATOM   3561 O OH   . TYR B 1 154 ? 9.791   5.011   -19.271 1.00 131.70 ? 154 TYR B OH   1 
ATOM   3562 N N    . ASP B 1 155 ? 4.480   -1.698  -18.571 1.00 103.18 ? 155 ASP B N    1 
ATOM   3563 C CA   . ASP B 1 155 ? 3.574   -2.832  -18.671 1.00 99.39  ? 155 ASP B CA   1 
ATOM   3564 C C    . ASP B 1 155 ? 2.296   -2.643  -17.847 1.00 88.70  ? 155 ASP B C    1 
ATOM   3565 O O    . ASP B 1 155 ? 1.314   -3.362  -18.079 1.00 80.04  ? 155 ASP B O    1 
ATOM   3566 C CB   . ASP B 1 155 ? 4.296   -4.133  -18.269 1.00 91.25  ? 155 ASP B CB   1 
ATOM   3567 C CG   . ASP B 1 155 ? 4.846   -4.102  -16.852 1.00 90.55  ? 155 ASP B CG   1 
ATOM   3568 O OD1  . ASP B 1 155 ? 4.587   -3.128  -16.115 1.00 93.47  ? 155 ASP B OD1  1 
ATOM   3569 O OD2  . ASP B 1 155 ? 5.554   -5.068  -16.478 1.00 89.62  ? 155 ASP B OD2  1 
ATOM   3570 N N    . CYS B 1 156 ? 2.261   -1.663  -16.940 1.00 85.02  ? 156 CYS B N    1 
ATOM   3571 C CA   . CYS B 1 156 ? 1.311   -1.618  -15.833 1.00 75.52  ? 156 CYS B CA   1 
ATOM   3572 C C    . CYS B 1 156 ? 0.326   -0.466  -16.003 1.00 66.09  ? 156 CYS B C    1 
ATOM   3573 O O    . CYS B 1 156 ? 0.723   0.705   -16.004 1.00 66.90  ? 156 CYS B O    1 
ATOM   3574 C CB   . CYS B 1 156 ? 2.063   -1.452  -14.522 1.00 72.42  ? 156 CYS B CB   1 
ATOM   3575 S SG   . CYS B 1 156 ? 0.997   -1.571  -13.104 1.00 70.63  ? 156 CYS B SG   1 
ATOM   3576 N N    . VAL B 1 157 ? -0.958  -0.799  -16.113 1.00 58.62  ? 157 VAL B N    1 
ATOM   3577 C CA   . VAL B 1 157 ? -2.025  0.202   -16.150 1.00 53.56  ? 157 VAL B CA   1 
ATOM   3578 C C    . VAL B 1 157 ? -2.334  0.685   -14.730 1.00 51.96  ? 157 VAL B C    1 
ATOM   3579 O O    . VAL B 1 157 ? -2.639  -0.119  -13.844 1.00 50.00  ? 157 VAL B O    1 
ATOM   3580 C CB   . VAL B 1 157 ? -3.283  -0.365  -16.824 1.00 47.82  ? 157 VAL B CB   1 
ATOM   3581 C CG1  . VAL B 1 157 ? -4.444  0.628   -16.734 1.00 45.63  ? 157 VAL B CG1  1 
ATOM   3582 C CG2  . VAL B 1 157 ? -2.999  -0.764  -18.262 1.00 50.37  ? 157 VAL B CG2  1 
ATOM   3583 N N    . SER B 1 158 ? -2.206  1.993   -14.492 1.00 50.63  ? 158 SER B N    1 
ATOM   3584 C CA   . SER B 1 158 ? -2.610  2.596   -13.221 1.00 46.78  ? 158 SER B CA   1 
ATOM   3585 C C    . SER B 1 158 ? -3.954  3.267   -13.462 1.00 46.57  ? 158 SER B C    1 
ATOM   3586 O O    . SER B 1 158 ? -4.043  4.258   -14.200 1.00 42.03  ? 158 SER B O    1 
ATOM   3587 C CB   . SER B 1 158 ? -1.594  3.604   -12.701 1.00 46.11  ? 158 SER B CB   1 
ATOM   3588 O OG   . SER B 1 158 ? -0.567  2.942   -12.003 1.00 52.16  ? 158 SER B OG   1 
ATOM   3589 N N    . PHE B 1 159 ? -5.001  2.679   -12.901 1.00 43.82  ? 159 PHE B N    1 
ATOM   3590 C CA   . PHE B 1 159 ? -6.325  3.273   -12.969 1.00 44.84  ? 159 PHE B CA   1 
ATOM   3591 C C    . PHE B 1 159 ? -6.452  4.290   -11.844 1.00 42.67  ? 159 PHE B C    1 
ATOM   3592 O O    . PHE B 1 159 ? -6.143  3.992   -10.688 1.00 44.28  ? 159 PHE B O    1 
ATOM   3593 C CB   . PHE B 1 159 ? -7.409  2.195   -12.847 1.00 45.68  ? 159 PHE B CB   1 
ATOM   3594 C CG   . PHE B 1 159 ? -7.470  1.229   -14.020 1.00 42.00  ? 159 PHE B CG   1 
ATOM   3595 C CD1  . PHE B 1 159 ? -8.027  1.609   -15.225 1.00 40.25  ? 159 PHE B CD1  1 
ATOM   3596 C CD2  . PHE B 1 159 ? -7.001  -0.073  -13.888 1.00 43.49  ? 159 PHE B CD2  1 
ATOM   3597 C CE1  . PHE B 1 159 ? -8.097  0.723   -16.290 1.00 39.93  ? 159 PHE B CE1  1 
ATOM   3598 C CE2  . PHE B 1 159 ? -7.080  -0.971  -14.948 1.00 43.20  ? 159 PHE B CE2  1 
ATOM   3599 C CZ   . PHE B 1 159 ? -7.623  -0.584  -16.137 1.00 41.43  ? 159 PHE B CZ   1 
ATOM   3600 N N    . CYS B 1 160 ? -6.900  5.491   -12.188 1.00 41.32  ? 160 CYS B N    1 
ATOM   3601 C CA   . CYS B 1 160 ? -7.011  6.556   -11.198 1.00 41.70  ? 160 CYS B CA   1 
ATOM   3602 C C    . CYS B 1 160 ? -8.379  7.245   -11.161 1.00 40.54  ? 160 CYS B C    1 
ATOM   3603 O O    . CYS B 1 160 ? -8.637  8.000   -10.219 1.00 43.11  ? 160 CYS B O    1 
ATOM   3604 C CB   . CYS B 1 160 ? -5.925  7.627   -11.445 1.00 41.73  ? 160 CYS B CB   1 
ATOM   3605 S SG   . CYS B 1 160 ? -6.024  8.365   -13.087 1.00 40.88  ? 160 CYS B SG   1 
ATOM   3606 N N    . TYR B 1 161 ? -9.258  7.024   -12.137 1.00 39.19  ? 161 TYR B N    1 
ATOM   3607 C CA   . TYR B 1 161 ? -10.485 7.796   -12.212 1.00 38.16  ? 161 TYR B CA   1 
ATOM   3608 C C    . TYR B 1 161 ? -11.587 6.962   -12.841 1.00 38.11  ? 161 TYR B C    1 
ATOM   3609 O O    . TYR B 1 161 ? -11.374 6.317   -13.870 1.00 36.96  ? 161 TYR B O    1 
ATOM   3610 C CB   . TYR B 1 161 ? -10.277 9.058   -13.058 1.00 37.00  ? 161 TYR B CB   1 
ATOM   3611 C CG   . TYR B 1 161 ? -11.516 9.909   -13.273 1.00 35.99  ? 161 TYR B CG   1 
ATOM   3612 C CD1  . TYR B 1 161 ? -12.005 10.751  -12.266 1.00 36.45  ? 161 TYR B CD1  1 
ATOM   3613 C CD2  . TYR B 1 161 ? -12.172 9.907   -14.497 1.00 34.70  ? 161 TYR B CD2  1 
ATOM   3614 C CE1  . TYR B 1 161 ? -13.130 11.545  -12.489 1.00 35.65  ? 161 TYR B CE1  1 
ATOM   3615 C CE2  . TYR B 1 161 ? -13.274 10.672  -14.717 1.00 33.96  ? 161 TYR B CE2  1 
ATOM   3616 C CZ   . TYR B 1 161 ? -13.760 11.490  -13.710 1.00 35.16  ? 161 TYR B CZ   1 
ATOM   3617 O OH   . TYR B 1 161 ? -14.887 12.259  -13.969 1.00 35.37  ? 161 TYR B OH   1 
ATOM   3618 N N    . MET B 1 162 ? -12.790 7.070   -12.278 1.00 38.74  ? 162 MET B N    1 
ATOM   3619 C CA   . MET B 1 162 ? -14.010 6.533   -12.880 1.00 36.88  ? 162 MET B CA   1 
ATOM   3620 C C    . MET B 1 162 ? -15.038 7.655   -12.938 1.00 36.05  ? 162 MET B C    1 
ATOM   3621 O O    . MET B 1 162 ? -15.289 8.326   -11.935 1.00 36.55  ? 162 MET B O    1 
ATOM   3622 C CB   . MET B 1 162 ? -14.575 5.350   -12.050 1.00 38.12  ? 162 MET B CB   1 
ATOM   3623 C CG   . MET B 1 162 ? -15.946 4.810   -12.543 1.00 37.77  ? 162 MET B CG   1 
ATOM   3624 S SD   . MET B 1 162 ? -16.338 3.192   -11.798 1.00 41.96  ? 162 MET B SD   1 
ATOM   3625 C CE   . MET B 1 162 ? -15.659 2.133   -13.107 1.00 39.24  ? 162 MET B CE   1 
ATOM   3626 N N    . HIS B 1 163 ? -15.646 7.836   -14.093 1.00 34.92  ? 163 HIS B N    1 
ATOM   3627 C CA   . HIS B 1 163 ? -16.564 8.939   -14.274 1.00 34.73  ? 163 HIS B CA   1 
ATOM   3628 C C    . HIS B 1 163 ? -17.922 8.660   -13.640 1.00 40.18  ? 163 HIS B C    1 
ATOM   3629 O O    . HIS B 1 163 ? -18.472 7.563   -13.796 1.00 38.06  ? 163 HIS B O    1 
ATOM   3630 C CB   . HIS B 1 163 ? -16.753 9.202   -15.753 1.00 35.97  ? 163 HIS B CB   1 
ATOM   3631 C CG   . HIS B 1 163 ? -17.601 10.391  -16.013 1.00 41.26  ? 163 HIS B CG   1 
ATOM   3632 N ND1  . HIS B 1 163 ? -17.290 11.632  -15.503 1.00 36.31  ? 163 HIS B ND1  1 
ATOM   3633 C CD2  . HIS B 1 163 ? -18.759 10.537  -16.702 1.00 39.69  ? 163 HIS B CD2  1 
ATOM   3634 C CE1  . HIS B 1 163 ? -18.221 12.496  -15.871 1.00 40.30  ? 163 HIS B CE1  1 
ATOM   3635 N NE2  . HIS B 1 163 ? -19.123 11.857  -16.600 1.00 39.38  ? 163 HIS B NE2  1 
ATOM   3636 N N    . HIS B 1 164 ? -18.487 9.693   -12.943 1.00 34.84  ? 164 HIS B N    1 
ATOM   3637 C CA   . HIS B 1 164 ? -19.791 9.623   -12.268 1.00 38.61  ? 164 HIS B CA   1 
ATOM   3638 C C    . HIS B 1 164 ? -20.790 10.706  -12.666 1.00 46.33  ? 164 HIS B C    1 
ATOM   3639 O O    . HIS B 1 164 ? -21.990 10.426  -12.664 1.00 45.41  ? 164 HIS B O    1 
ATOM   3640 C CB   . HIS B 1 164 ? -19.664 9.707   -10.783 1.00 37.42  ? 164 HIS B CB   1 
ATOM   3641 C CG   . HIS B 1 164 ? -19.160 8.460   -10.143 1.00 37.56  ? 164 HIS B CG   1 
ATOM   3642 N ND1  . HIS B 1 164 ? -19.943 7.681   -9.321  1.00 38.61  ? 164 HIS B ND1  1 
ATOM   3643 C CD2  . HIS B 1 164 ? -17.937 7.875   -10.176 1.00 37.87  ? 164 HIS B CD2  1 
ATOM   3644 C CE1  . HIS B 1 164 ? -19.223 6.672   -8.863  1.00 39.55  ? 164 HIS B CE1  1 
ATOM   3645 N NE2  . HIS B 1 164 ? -18.007 6.757   -9.385  1.00 39.12  ? 164 HIS B NE2  1 
ATOM   3646 N N    . MET B 1 165 ? -20.353 11.944  -12.924 1.00 43.96  ? 165 MET B N    1 
ATOM   3647 C CA   . MET B 1 165 ? -21.339 13.011  -13.105 1.00 44.09  ? 165 MET B CA   1 
ATOM   3648 C C    . MET B 1 165 ? -20.765 14.240  -13.811 1.00 43.28  ? 165 MET B C    1 
ATOM   3649 O O    . MET B 1 165 ? -19.552 14.479  -13.806 1.00 43.64  ? 165 MET B O    1 
ATOM   3650 C CB   . MET B 1 165 ? -21.914 13.444  -11.765 1.00 44.59  ? 165 MET B CB   1 
ATOM   3651 C CG   . MET B 1 165 ? -20.941 14.055  -10.857 1.00 43.61  ? 165 MET B CG   1 
ATOM   3652 S SD   . MET B 1 165 ? -21.637 14.076  -9.186  1.00 62.74  ? 165 MET B SD   1 
ATOM   3653 C CE   . MET B 1 165 ? -22.776 15.463  -9.412  1.00 59.20  ? 165 MET B CE   1 
ATOM   3654 N N    . GLU B 1 166 ? -21.667 15.059  -14.362 1.00 41.30  ? 166 GLU B N    1 
ATOM   3655 C CA   . GLU B 1 166 ? -21.302 16.373  -14.877 1.00 43.73  ? 166 GLU B CA   1 
ATOM   3656 C C    . GLU B 1 166 ? -21.867 17.479  -13.982 1.00 49.77  ? 166 GLU B C    1 
ATOM   3657 O O    . GLU B 1 166 ? -22.941 17.336  -13.393 1.00 46.66  ? 166 GLU B O    1 
ATOM   3658 C CB   . GLU B 1 166 ? -21.791 16.550  -16.317 1.00 47.33  ? 166 GLU B CB   1 
ATOM   3659 C CG   . GLU B 1 166 ? -21.588 17.933  -16.894 1.00 46.53  ? 166 GLU B CG   1 
ATOM   3660 C CD   . GLU B 1 166 ? -21.807 17.955  -18.393 1.00 51.33  ? 166 GLU B CD   1 
ATOM   3661 O OE1  . GLU B 1 166 ? -22.620 18.807  -18.808 1.00 65.85  ? 166 GLU B OE1  1 
ATOM   3662 O OE2  . GLU B 1 166 ? -21.223 17.147  -19.159 1.00 53.90  ? 166 GLU B OE2  1 
ATOM   3663 N N    . LEU B 1 167 ? -21.124 18.576  -13.860 1.00 48.82  ? 167 LEU B N    1 
ATOM   3664 C CA   . LEU B 1 167 ? -21.512 19.700  -13.021 1.00 50.59  ? 167 LEU B CA   1 
ATOM   3665 C C    . LEU B 1 167 ? -22.204 20.777  -13.854 1.00 50.43  ? 167 LEU B C    1 
ATOM   3666 O O    . LEU B 1 167 ? -22.161 20.752  -15.088 1.00 51.08  ? 167 LEU B O    1 
ATOM   3667 C CB   . LEU B 1 167 ? -20.285 20.282  -12.297 1.00 46.86  ? 167 LEU B CB   1 
ATOM   3668 C CG   . LEU B 1 167 ? -19.576 19.370  -11.277 1.00 44.42  ? 167 LEU B CG   1 
ATOM   3669 C CD1  . LEU B 1 167 ? -18.449 20.093  -10.551 1.00 43.65  ? 167 LEU B CD1  1 
ATOM   3670 C CD2  . LEU B 1 167 ? -20.580 18.792  -10.301 1.00 45.73  ? 167 LEU B CD2  1 
ATOM   3671 N N    . PRO B 1 168 ? -22.869 21.750  -13.197 1.00 48.33  ? 168 PRO B N    1 
ATOM   3672 C CA   . PRO B 1 168 ? -23.527 22.831  -13.958 1.00 50.45  ? 168 PRO B CA   1 
ATOM   3673 C C    . PRO B 1 168 ? -22.579 23.607  -14.849 1.00 51.80  ? 168 PRO B C    1 
ATOM   3674 O O    . PRO B 1 168 ? -22.933 23.953  -15.981 1.00 49.66  ? 168 PRO B O    1 
ATOM   3675 C CB   . PRO B 1 168 ? -24.116 23.742  -12.874 1.00 50.15  ? 168 PRO B CB   1 
ATOM   3676 C CG   . PRO B 1 168 ? -23.849 23.102  -11.564 1.00 56.86  ? 168 PRO B CG   1 
ATOM   3677 C CD   . PRO B 1 168 ? -23.077 21.847  -11.742 1.00 56.17  ? 168 PRO B CD   1 
ATOM   3678 N N    . THR B 1 169 ? -21.375 23.900  -14.364 1.00 50.95  ? 169 THR B N    1 
ATOM   3679 C CA   . THR B 1 169 ? -20.398 24.604  -15.184 1.00 51.00  ? 169 THR B CA   1 
ATOM   3680 C C    . THR B 1 169 ? -19.998 23.818  -16.427 1.00 51.41  ? 169 THR B C    1 
ATOM   3681 O O    . THR B 1 169 ? -19.305 24.370  -17.291 1.00 51.97  ? 169 THR B O    1 
ATOM   3682 C CB   . THR B 1 169 ? -19.165 24.932  -14.342 1.00 49.70  ? 169 THR B CB   1 
ATOM   3683 O OG1  . THR B 1 169 ? -18.669 23.719  -13.762 1.00 51.52  ? 169 THR B OG1  1 
ATOM   3684 C CG2  . THR B 1 169 ? -19.506 25.947  -13.196 1.00 49.89  ? 169 THR B CG2  1 
ATOM   3685 N N    . GLY B 1 170 ? -20.412 22.557  -16.557 1.00 48.69  ? 170 GLY B N    1 
ATOM   3686 C CA   . GLY B 1 170 ? -19.976 21.775  -17.694 1.00 47.36  ? 170 GLY B CA   1 
ATOM   3687 C C    . GLY B 1 170 ? -18.654 21.058  -17.510 1.00 49.97  ? 170 GLY B C    1 
ATOM   3688 O O    . GLY B 1 170 ? -18.070 20.592  -18.502 1.00 50.00  ? 170 GLY B O    1 
ATOM   3689 N N    . VAL B 1 171 ? -18.155 20.969  -16.285 1.00 47.18  ? 171 VAL B N    1 
ATOM   3690 C CA   . VAL B 1 171 ? -16.976 20.170  -15.999 1.00 45.78  ? 171 VAL B CA   1 
ATOM   3691 C C    . VAL B 1 171 ? -17.424 18.856  -15.356 1.00 47.28  ? 171 VAL B C    1 
ATOM   3692 O O    . VAL B 1 171 ? -18.622 18.640  -15.103 1.00 43.10  ? 171 VAL B O    1 
ATOM   3693 C CB   . VAL B 1 171 ? -16.002 20.956  -15.102 1.00 45.18  ? 171 VAL B CB   1 
ATOM   3694 C CG1  . VAL B 1 171 ? -15.519 22.256  -15.813 1.00 47.33  ? 171 VAL B CG1  1 
ATOM   3695 C CG2  . VAL B 1 171 ? -16.635 21.276  -13.787 1.00 41.02  ? 171 VAL B CG2  1 
ATOM   3696 N N    . HIS B 1 172 ? -16.464 17.979  -15.046 1.00 42.37  ? 172 HIS B N    1 
ATOM   3697 C CA   . HIS B 1 172 ? -16.786 16.594  -14.744 1.00 39.30  ? 172 HIS B CA   1 
ATOM   3698 C C    . HIS B 1 172 ? -16.175 16.173  -13.418 1.00 39.83  ? 172 HIS B C    1 
ATOM   3699 O O    . HIS B 1 172 ? -15.132 16.697  -13.007 1.00 35.82  ? 172 HIS B O    1 
ATOM   3700 C CB   . HIS B 1 172 ? -16.323 15.718  -15.902 1.00 38.52  ? 172 HIS B CB   1 
ATOM   3701 C CG   . HIS B 1 172 ? -16.936 16.097  -17.214 1.00 42.00  ? 172 HIS B CG   1 
ATOM   3702 N ND1  . HIS B 1 172 ? -16.209 16.645  -18.249 1.00 42.97  ? 172 HIS B ND1  1 
ATOM   3703 C CD2  . HIS B 1 172 ? -18.213 15.998  -17.662 1.00 41.36  ? 172 HIS B CD2  1 
ATOM   3704 C CE1  . HIS B 1 172 ? -17.008 16.862  -19.282 1.00 41.92  ? 172 HIS B CE1  1 
ATOM   3705 N NE2  . HIS B 1 172 ? -18.227 16.473  -18.954 1.00 41.78  ? 172 HIS B NE2  1 
ATOM   3706 N N    . ALA B 1 173 ? -16.869 15.255  -12.723 1.00 34.85  ? 173 ALA B N    1 
ATOM   3707 C CA   . ALA B 1 173 ? -16.439 14.777  -11.415 1.00 37.24  ? 173 ALA B CA   1 
ATOM   3708 C C    . ALA B 1 173 ? -16.580 13.260  -11.339 1.00 36.53  ? 173 ALA B C    1 
ATOM   3709 O O    . ALA B 1 173 ? -17.444 12.669  -11.994 1.00 34.95  ? 173 ALA B O    1 
ATOM   3710 C CB   . ALA B 1 173 ? -17.261 15.434  -10.277 1.00 41.18  ? 173 ALA B CB   1 
ATOM   3711 N N    . GLY B 1 174 ? -15.742 12.638  -10.519 1.00 38.71  ? 174 GLY B N    1 
ATOM   3712 C CA   . GLY B 1 174 ? -15.793 11.202  -10.370 1.00 36.82  ? 174 GLY B CA   1 
ATOM   3713 C C    . GLY B 1 174 ? -14.937 10.724  -9.229  1.00 38.18  ? 174 GLY B C    1 
ATOM   3714 O O    . GLY B 1 174 ? -14.512 11.500  -8.366  1.00 39.59  ? 174 GLY B O    1 
ATOM   3715 N N    . THR B 1 175 ? -14.711 9.421   -9.216  1.00 38.69  ? 175 THR B N    1 
ATOM   3716 C CA   . THR B 1 175 ? -14.069 8.773   -8.089  1.00 40.21  ? 175 THR B CA   1 
ATOM   3717 C C    . THR B 1 175 ? -12.794 8.076   -8.536  1.00 40.55  ? 175 THR B C    1 
ATOM   3718 O O    . THR B 1 175 ? -12.560 7.854   -9.736  1.00 39.58  ? 175 THR B O    1 
ATOM   3719 C CB   . THR B 1 175 ? -14.988 7.725   -7.427  1.00 41.03  ? 175 THR B CB   1 
ATOM   3720 O OG1  . THR B 1 175 ? -15.226 6.660   -8.354  1.00 40.61  ? 175 THR B OG1  1 
ATOM   3721 C CG2  . THR B 1 175 ? -16.327 8.360   -6.973  1.00 40.81  ? 175 THR B CG2  1 
ATOM   3722 N N    . ASP B 1 176 ? -11.981 7.744   -7.545  1.00 42.05  ? 176 ASP B N    1 
ATOM   3723 C CA   . ASP B 1 176 ? -10.926 6.761   -7.728  1.00 42.86  ? 176 ASP B CA   1 
ATOM   3724 C C    . ASP B 1 176 ? -11.543 5.356   -7.788  1.00 43.28  ? 176 ASP B C    1 
ATOM   3725 O O    . ASP B 1 176 ? -12.730 5.164   -7.527  1.00 43.15  ? 176 ASP B O    1 
ATOM   3726 C CB   . ASP B 1 176 ? -9.898  6.889   -6.597  1.00 44.57  ? 176 ASP B CB   1 
ATOM   3727 C CG   . ASP B 1 176 ? -10.445 6.479   -5.236  1.00 45.97  ? 176 ASP B CG   1 
ATOM   3728 O OD1  . ASP B 1 176 ? -11.415 5.710   -5.182  1.00 45.95  ? 176 ASP B OD1  1 
ATOM   3729 O OD2  . ASP B 1 176 ? -9.905  6.924   -4.197  1.00 47.24  ? 176 ASP B OD2  1 
ATOM   3730 N N    . LEU B 1 177 ? -10.729 4.356   -8.107  1.00 44.51  ? 177 LEU B N    1 
ATOM   3731 C CA   . LEU B 1 177 ? -11.319 3.033   -8.317  1.00 44.40  ? 177 LEU B CA   1 
ATOM   3732 C C    . LEU B 1 177 ? -11.720 2.381   -7.013  1.00 46.10  ? 177 LEU B C    1 
ATOM   3733 O O    . LEU B 1 177 ? -12.307 1.300   -7.032  1.00 46.71  ? 177 LEU B O    1 
ATOM   3734 C CB   . LEU B 1 177 ? -10.382 2.109   -9.115  1.00 44.72  ? 177 LEU B CB   1 
ATOM   3735 C CG   . LEU B 1 177 ? -10.631 2.104   -10.625 1.00 43.19  ? 177 LEU B CG   1 
ATOM   3736 C CD1  . LEU B 1 177 ? -11.951 1.446   -11.011 1.00 42.65  ? 177 LEU B CD1  1 
ATOM   3737 C CD2  . LEU B 1 177 ? -10.624 3.556   -11.158 1.00 41.51  ? 177 LEU B CD2  1 
ATOM   3738 N N    . GLU B 1 178 ? -11.395 2.986   -5.887  1.00 47.01  ? 178 GLU B N    1 
ATOM   3739 C CA   . GLU B 1 178 ? -11.938 2.573   -4.606  1.00 48.50  ? 178 GLU B CA   1 
ATOM   3740 C C    . GLU B 1 178 ? -13.276 3.237   -4.277  1.00 47.74  ? 178 GLU B C    1 
ATOM   3741 O O    . GLU B 1 178 ? -13.863 2.930   -3.247  1.00 48.89  ? 178 GLU B O    1 
ATOM   3742 C CB   . GLU B 1 178 ? -10.923 2.872   -3.524  1.00 50.05  ? 178 GLU B CB   1 
ATOM   3743 C CG   . GLU B 1 178 ? -10.021 1.719   -3.204  1.00 53.29  ? 178 GLU B CG   1 
ATOM   3744 C CD   . GLU B 1 178 ? -8.699  2.172   -2.611  1.00 68.54  ? 178 GLU B CD   1 
ATOM   3745 O OE1  . GLU B 1 178 ? -7.715  1.409   -2.701  1.00 72.86  ? 178 GLU B OE1  1 
ATOM   3746 O OE2  . GLU B 1 178 ? -8.632  3.293   -2.064  1.00 70.22  ? 178 GLU B OE2  1 
ATOM   3747 N N    . GLY B 1 179 ? -13.758 4.159   -5.103  1.00 45.96  ? 179 GLY B N    1 
ATOM   3748 C CA   . GLY B 1 179 ? -15.067 4.768   -4.938  1.00 46.52  ? 179 GLY B CA   1 
ATOM   3749 C C    . GLY B 1 179 ? -15.116 6.091   -4.191  1.00 45.18  ? 179 GLY B C    1 
ATOM   3750 O O    . GLY B 1 179 ? -16.210 6.606   -3.951  1.00 44.79  ? 179 GLY B O    1 
ATOM   3751 N N    . ASN B 1 180 ? -13.985 6.642   -3.785  1.00 45.72  ? 180 ASN B N    1 
ATOM   3752 C CA   . ASN B 1 180 ? -13.965 7.903   -3.063  1.00 45.86  ? 180 ASN B CA   1 
ATOM   3753 C C    . ASN B 1 180 ? -13.869 9.007   -4.097  1.00 44.27  ? 180 ASN B C    1 
ATOM   3754 O O    . ASN B 1 180 ? -12.974 8.985   -4.954  1.00 43.76  ? 180 ASN B O    1 
ATOM   3755 C CB   . ASN B 1 180 ? -12.803 7.949   -2.087  1.00 47.48  ? 180 ASN B CB   1 
ATOM   3756 C CG   . ASN B 1 180 ? -12.880 6.863   -1.086  1.00 49.18  ? 180 ASN B CG   1 
ATOM   3757 O OD1  . ASN B 1 180 ? -13.755 6.862   -0.242  1.00 49.74  ? 180 ASN B OD1  1 
ATOM   3758 N ND2  . ASN B 1 180 ? -12.003 5.881   -1.207  1.00 50.09  ? 180 ASN B ND2  1 
ATOM   3759 N N    . PHE B 1 181 ? -14.813 9.934   -4.068  1.00 43.56  ? 181 PHE B N    1 
ATOM   3760 C CA   . PHE B 1 181 ? -14.790 10.994  -5.065  1.00 42.18  ? 181 PHE B CA   1 
ATOM   3761 C C    . PHE B 1 181 ? -13.495 11.801  -4.956  1.00 42.60  ? 181 PHE B C    1 
ATOM   3762 O O    . PHE B 1 181 ? -12.913 11.960  -3.884  1.00 43.97  ? 181 PHE B O    1 
ATOM   3763 C CB   . PHE B 1 181 ? -15.999 11.928  -4.887  1.00 41.69  ? 181 PHE B CB   1 
ATOM   3764 C CG   . PHE B 1 181 ? -17.152 11.646  -5.834  1.00 40.53  ? 181 PHE B CG   1 
ATOM   3765 C CD1  . PHE B 1 181 ? -18.168 10.769  -5.465  1.00 40.94  ? 181 PHE B CD1  1 
ATOM   3766 C CD2  . PHE B 1 181 ? -17.252 12.300  -7.050  1.00 39.21  ? 181 PHE B CD2  1 
ATOM   3767 C CE1  . PHE B 1 181 ? -19.240 10.538  -6.303  1.00 40.09  ? 181 PHE B CE1  1 
ATOM   3768 C CE2  . PHE B 1 181 ? -18.327 12.068  -7.915  1.00 38.31  ? 181 PHE B CE2  1 
ATOM   3769 C CZ   . PHE B 1 181 ? -19.322 11.187  -7.550  1.00 40.09  ? 181 PHE B CZ   1 
ATOM   3770 N N    . TYR B 1 182 ? -13.051 12.324  -6.085  1.00 41.52  ? 182 TYR B N    1 
ATOM   3771 C CA   . TYR B 1 182 ? -12.169 13.473  -6.039  1.00 41.81  ? 182 TYR B CA   1 
ATOM   3772 C C    . TYR B 1 182 ? -13.055 14.687  -5.808  1.00 42.22  ? 182 TYR B C    1 
ATOM   3773 O O    . TYR B 1 182 ? -14.033 14.905  -6.555  1.00 41.02  ? 182 TYR B O    1 
ATOM   3774 C CB   . TYR B 1 182 ? -11.393 13.613  -7.352  1.00 40.87  ? 182 TYR B CB   1 
ATOM   3775 C CG   . TYR B 1 182 ? -10.430 12.461  -7.611  1.00 41.30  ? 182 TYR B CG   1 
ATOM   3776 C CD1  . TYR B 1 182 ? -9.183  12.461  -7.050  1.00 42.65  ? 182 TYR B CD1  1 
ATOM   3777 C CD2  . TYR B 1 182 ? -10.782 11.390  -8.442  1.00 40.47  ? 182 TYR B CD2  1 
ATOM   3778 C CE1  . TYR B 1 182 ? -8.301  11.441  -7.264  1.00 45.01  ? 182 TYR B CE1  1 
ATOM   3779 C CE2  . TYR B 1 182 ? -9.887  10.347  -8.678  1.00 41.01  ? 182 TYR B CE2  1 
ATOM   3780 C CZ   . TYR B 1 182 ? -8.641  10.386  -8.076  1.00 45.21  ? 182 TYR B CZ   1 
ATOM   3781 O OH   . TYR B 1 182 ? -7.706  9.377   -8.268  1.00 43.84  ? 182 TYR B OH   1 
ATOM   3782 N N    . GLY B 1 183 ? -12.710 15.481  -4.810  1.00 42.65  ? 183 GLY B N    1 
ATOM   3783 C CA   . GLY B 1 183 ? -13.440 16.686  -4.533  1.00 42.60  ? 183 GLY B CA   1 
ATOM   3784 C C    . GLY B 1 183 ? -14.537 16.513  -3.504  1.00 46.23  ? 183 GLY B C    1 
ATOM   3785 O O    . GLY B 1 183 ? -14.624 15.499  -2.796  1.00 44.47  ? 183 GLY B O    1 
ATOM   3786 N N    . PRO B 1 184 ? -15.380 17.534  -3.356  1.00 43.35  ? 184 PRO B N    1 
ATOM   3787 C CA   . PRO B 1 184 ? -16.418 17.491  -2.319  1.00 45.42  ? 184 PRO B CA   1 
ATOM   3788 C C    . PRO B 1 184 ? -17.741 16.916  -2.805  1.00 44.16  ? 184 PRO B C    1 
ATOM   3789 O O    . PRO B 1 184 ? -18.732 17.031  -2.084  1.00 50.28  ? 184 PRO B O    1 
ATOM   3790 C CB   . PRO B 1 184 ? -16.583 18.974  -1.992  1.00 46.33  ? 184 PRO B CB   1 
ATOM   3791 C CG   . PRO B 1 184 ? -16.531 19.573  -3.391  1.00 44.15  ? 184 PRO B CG   1 
ATOM   3792 C CD   . PRO B 1 184 ? -15.513 18.738  -4.181  1.00 44.41  ? 184 PRO B CD   1 
ATOM   3793 N N    . PHE B 1 185 ? -17.755 16.249  -3.957  1.00 41.57  ? 185 PHE B N    1 
ATOM   3794 C CA   . PHE B 1 185 ? -18.970 15.877  -4.653  1.00 40.67  ? 185 PHE B CA   1 
ATOM   3795 C C    . PHE B 1 185 ? -19.620 14.609  -4.075  1.00 41.20  ? 185 PHE B C    1 
ATOM   3796 O O    . PHE B 1 185 ? -18.975 13.766  -3.434  1.00 42.03  ? 185 PHE B O    1 
ATOM   3797 C CB   . PHE B 1 185 ? -18.645 15.705  -6.138  1.00 42.93  ? 185 PHE B CB   1 
ATOM   3798 C CG   . PHE B 1 185 ? -17.916 16.879  -6.702  1.00 45.18  ? 185 PHE B CG   1 
ATOM   3799 C CD1  . PHE B 1 185 ? -18.515 18.125  -6.712  1.00 47.36  ? 185 PHE B CD1  1 
ATOM   3800 C CD2  . PHE B 1 185 ? -16.599 16.764  -7.124  1.00 43.51  ? 185 PHE B CD2  1 
ATOM   3801 C CE1  . PHE B 1 185 ? -17.837 19.229  -7.194  1.00 50.94  ? 185 PHE B CE1  1 
ATOM   3802 C CE2  . PHE B 1 185 ? -15.906 17.866  -7.615  1.00 44.80  ? 185 PHE B CE2  1 
ATOM   3803 C CZ   . PHE B 1 185 ? -16.522 19.100  -7.650  1.00 48.13  ? 185 PHE B CZ   1 
ATOM   3804 N N    . VAL B 1 186 ? -20.938 14.497  -4.297  1.00 40.88  ? 186 VAL B N    1 
ATOM   3805 C CA   . VAL B 1 186 ? -21.687 13.303  -3.931  1.00 41.38  ? 186 VAL B CA   1 
ATOM   3806 C C    . VAL B 1 186 ? -22.489 12.862  -5.140  1.00 42.90  ? 186 VAL B C    1 
ATOM   3807 O O    . VAL B 1 186 ? -22.838 13.672  -6.010  1.00 40.97  ? 186 VAL B O    1 
ATOM   3808 C CB   . VAL B 1 186 ? -22.615 13.500  -2.717  1.00 42.46  ? 186 VAL B CB   1 
ATOM   3809 C CG1  . VAL B 1 186 ? -21.793 13.800  -1.436  1.00 43.64  ? 186 VAL B CG1  1 
ATOM   3810 C CG2  . VAL B 1 186 ? -23.660 14.576  -3.032  1.00 47.08  ? 186 VAL B CG2  1 
ATOM   3811 N N    . ASP B 1 187 ? -22.773 11.552  -5.198  1.00 40.72  ? 187 ASP B N    1 
ATOM   3812 C CA   . ASP B 1 187 ? -23.506 10.981  -6.328  1.00 42.28  ? 187 ASP B CA   1 
ATOM   3813 C C    . ASP B 1 187 ? -25.007 11.036  -6.012  1.00 46.34  ? 187 ASP B C    1 
ATOM   3814 O O    . ASP B 1 187 ? -25.615 10.083  -5.511  1.00 43.24  ? 187 ASP B O    1 
ATOM   3815 C CB   . ASP B 1 187 ? -23.008 9.571   -6.668  1.00 40.20  ? 187 ASP B CB   1 
ATOM   3816 C CG   . ASP B 1 187 ? -22.919 8.634   -5.463  1.00 41.66  ? 187 ASP B CG   1 
ATOM   3817 O OD1  . ASP B 1 187 ? -23.183 9.025   -4.297  1.00 44.04  ? 187 ASP B OD1  1 
ATOM   3818 O OD2  . ASP B 1 187 ? -22.592 7.457   -5.689  1.00 42.03  ? 187 ASP B OD2  1 
ATOM   3819 N N    . ARG B 1 188 ? -25.585 12.222  -6.261  1.00 48.42  ? 188 ARG B N    1 
ATOM   3820 C CA   . ARG B 1 188 ? -27.028 12.458  -6.269  1.00 48.56  ? 188 ARG B CA   1 
ATOM   3821 C C    . ARG B 1 188 ? -27.343 13.534  -7.305  1.00 54.54  ? 188 ARG B C    1 
ATOM   3822 O O    . ARG B 1 188 ? -26.501 14.388  -7.604  1.00 53.04  ? 188 ARG B O    1 
ATOM   3823 C CB   . ARG B 1 188 ? -27.561 12.841  -4.881  1.00 51.48  ? 188 ARG B CB   1 
ATOM   3824 C CG   . ARG B 1 188 ? -26.930 14.027  -4.170  1.00 53.74  ? 188 ARG B CG   1 
ATOM   3825 C CD   . ARG B 1 188 ? -27.375 14.098  -2.687  1.00 55.54  ? 188 ARG B CD   1 
ATOM   3826 N NE   . ARG B 1 188 ? -26.410 13.443  -1.799  1.00 55.93  ? 188 ARG B NE   1 
ATOM   3827 C CZ   . ARG B 1 188 ? -26.210 13.744  -0.520  1.00 62.11  ? 188 ARG B CZ   1 
ATOM   3828 N NH1  . ARG B 1 188 ? -26.931 14.672  0.096   1.00 63.73  ? 188 ARG B NH1  1 
ATOM   3829 N NH2  . ARG B 1 188 ? -25.272 13.084  0.165   1.00 62.32  ? 188 ARG B NH2  1 
ATOM   3830 N N    . GLN B 1 189 ? -28.549 13.443  -7.896  1.00 58.44  ? 189 GLN B N    1 
ATOM   3831 C CA   . GLN B 1 189 ? -29.015 14.332  -8.967  1.00 56.19  ? 189 GLN B CA   1 
ATOM   3832 C C    . GLN B 1 189 ? -29.224 15.748  -8.457  1.00 59.39  ? 189 GLN B C    1 
ATOM   3833 O O    . GLN B 1 189 ? -30.361 16.230  -8.403  1.00 63.47  ? 189 GLN B O    1 
ATOM   3834 C CB   . GLN B 1 189 ? -30.322 13.832  -9.586  1.00 55.88  ? 189 GLN B CB   1 
ATOM   3835 C CG   . GLN B 1 189 ? -30.572 14.329  -11.006 1.00 59.11  ? 189 GLN B CG   1 
ATOM   3836 C CD   . GLN B 1 189 ? -29.868 13.468  -12.082 1.00 69.73  ? 189 GLN B CD   1 
ATOM   3837 O OE1  . GLN B 1 189 ? -28.808 12.854  -11.834 1.00 60.75  ? 189 GLN B OE1  1 
ATOM   3838 N NE2  . GLN B 1 189 ? -30.436 13.463  -13.301 1.00 68.78  ? 189 GLN B NE2  1 
ATOM   3839 N N    . THR B 1 190 ? -28.140 16.406  -8.065  1.00 59.16  ? 190 THR B N    1 
ATOM   3840 C CA   . THR B 1 190 ? -28.170 17.752  -7.526  1.00 64.88  ? 190 THR B CA   1 
ATOM   3841 C C    . THR B 1 190 ? -27.150 18.626  -8.255  1.00 66.80  ? 190 THR B C    1 
ATOM   3842 O O    . THR B 1 190 ? -26.204 18.132  -8.880  1.00 61.49  ? 190 THR B O    1 
ATOM   3843 C CB   . THR B 1 190 ? -27.886 17.731  -6.026  1.00 63.23  ? 190 THR B CB   1 
ATOM   3844 O OG1  . THR B 1 190 ? -28.524 18.846  -5.390  1.00 71.41  ? 190 THR B OG1  1 
ATOM   3845 C CG2  . THR B 1 190 ? -26.408 17.823  -5.785  1.00 60.76  ? 190 THR B CG2  1 
ATOM   3846 N N    . ALA B 1 191 ? -27.351 19.941  -8.161  1.00 79.72  ? 191 ALA B N    1 
ATOM   3847 C CA   . ALA B 1 191 ? -26.394 20.917  -8.674  1.00 78.21  ? 191 ALA B CA   1 
ATOM   3848 C C    . ALA B 1 191 ? -25.353 21.163  -7.596  1.00 71.53  ? 191 ALA B C    1 
ATOM   3849 O O    . ALA B 1 191 ? -25.700 21.491  -6.455  1.00 71.61  ? 191 ALA B O    1 
ATOM   3850 C CB   . ALA B 1 191 ? -27.072 22.227  -9.071  1.00 83.26  ? 191 ALA B CB   1 
ATOM   3851 N N    . GLN B 1 192 ? -24.088 20.965  -7.946  1.00 61.62  ? 192 GLN B N    1 
ATOM   3852 C CA   . GLN B 1 192 ? -23.000 21.033  -6.983  1.00 61.71  ? 192 GLN B CA   1 
ATOM   3853 C C    . GLN B 1 192 ? -21.889 21.917  -7.526  1.00 57.19  ? 192 GLN B C    1 
ATOM   3854 O O    . GLN B 1 192 ? -21.591 21.905  -8.727  1.00 57.45  ? 192 GLN B O    1 
ATOM   3855 C CB   . GLN B 1 192 ? -22.470 19.642  -6.641  1.00 57.43  ? 192 GLN B CB   1 
ATOM   3856 C CG   . GLN B 1 192 ? -23.528 18.736  -6.040  1.00 55.63  ? 192 GLN B CG   1 
ATOM   3857 C CD   . GLN B 1 192 ? -23.072 17.291  -5.930  1.00 48.18  ? 192 GLN B CD   1 
ATOM   3858 O OE1  . GLN B 1 192 ? -22.082 16.994  -5.267  1.00 42.11  ? 192 GLN B OE1  1 
ATOM   3859 N NE2  . GLN B 1 192 ? -23.769 16.395  -6.626  1.00 42.26  ? 192 GLN B NE2  1 
ATOM   3860 N N    . ALA B 1 193 ? -21.308 22.699  -6.630  1.00 56.58  ? 193 ALA B N    1 
ATOM   3861 C CA   . ALA B 1 193 ? -20.346 23.732  -6.975  1.00 55.55  ? 193 ALA B CA   1 
ATOM   3862 C C    . ALA B 1 193 ? -18.943 23.214  -6.698  1.00 53.63  ? 193 ALA B C    1 
ATOM   3863 O O    . ALA B 1 193 ? -18.619 22.871  -5.553  1.00 48.17  ? 193 ALA B O    1 
ATOM   3864 C CB   . ALA B 1 193 ? -20.606 25.000  -6.160  1.00 53.94  ? 193 ALA B CB   1 
ATOM   3865 N N    . ALA B 1 194 ? -18.125 23.138  -7.746  1.00 51.43  ? 194 ALA B N    1 
ATOM   3866 C CA   . ALA B 1 194 ? -16.695 22.972  -7.552  1.00 51.08  ? 194 ALA B CA   1 
ATOM   3867 C C    . ALA B 1 194 ? -16.111 24.278  -7.017  1.00 53.23  ? 194 ALA B C    1 
ATOM   3868 O O    . ALA B 1 194 ? -16.708 25.348  -7.134  1.00 56.34  ? 194 ALA B O    1 
ATOM   3869 C CB   . ALA B 1 194 ? -16.029 22.568  -8.874  1.00 47.98  ? 194 ALA B CB   1 
ATOM   3870 N N    . GLY B 1 195 ? -14.938 24.196  -6.415  1.00 52.70  ? 195 GLY B N    1 
ATOM   3871 C CA   . GLY B 1 195 ? -14.339 25.428  -5.936  1.00 57.71  ? 195 GLY B CA   1 
ATOM   3872 C C    . GLY B 1 195 ? -13.988 26.425  -7.037  1.00 57.83  ? 195 GLY B C    1 
ATOM   3873 O O    . GLY B 1 195 ? -14.187 26.162  -8.233  1.00 52.29  ? 195 GLY B O    1 
ATOM   3874 N N    . THR B 1 196 ? -13.498 27.598  -6.636  1.00 61.34  ? 196 THR B N    1 
ATOM   3875 C CA   . THR B 1 196 ? -12.698 28.404  -7.544  1.00 59.21  ? 196 THR B CA   1 
ATOM   3876 C C    . THR B 1 196 ? -11.614 27.516  -8.153  1.00 56.30  ? 196 THR B C    1 
ATOM   3877 O O    . THR B 1 196 ? -10.996 26.702  -7.463  1.00 57.51  ? 196 THR B O    1 
ATOM   3878 C CB   . THR B 1 196 ? -12.032 29.570  -6.790  1.00 58.98  ? 196 THR B CB   1 
ATOM   3879 O OG1  . THR B 1 196 ? -13.010 30.312  -6.050  1.00 56.44  ? 196 THR B OG1  1 
ATOM   3880 C CG2  . THR B 1 196 ? -11.331 30.488  -7.777  1.00 56.25  ? 196 THR B CG2  1 
ATOM   3881 N N    . ASP B 1 197 ? -11.343 27.691  -9.427  1.00 56.64  ? 197 ASP B N    1 
ATOM   3882 C CA   . ASP B 1 197 ? -10.188 26.988  -9.958  1.00 60.01  ? 197 ASP B CA   1 
ATOM   3883 C C    . ASP B 1 197 ? -8.930  27.839  -9.818  1.00 65.56  ? 197 ASP B C    1 
ATOM   3884 O O    . ASP B 1 197 ? -8.966  29.031  -9.504  1.00 72.13  ? 197 ASP B O    1 
ATOM   3885 C CB   . ASP B 1 197 ? -10.380 26.583  -11.414 1.00 56.46  ? 197 ASP B CB   1 
ATOM   3886 C CG   . ASP B 1 197 ? -9.632  25.276  -11.755 1.00 58.96  ? 197 ASP B CG   1 
ATOM   3887 O OD1  . ASP B 1 197 ? -9.008  24.642  -10.841 1.00 53.71  ? 197 ASP B OD1  1 
ATOM   3888 O OD2  . ASP B 1 197 ? -9.648  24.908  -12.945 1.00 56.10  ? 197 ASP B OD2  1 
ATOM   3889 N N    . THR B 1 198 ? -7.801  27.197  -10.053 1.00 65.80  ? 198 THR B N    1 
ATOM   3890 C CA   . THR B 1 198 ? -6.541  27.896  -10.164 1.00 67.55  ? 198 THR B CA   1 
ATOM   3891 C C    . THR B 1 198 ? -5.785  27.250  -11.310 1.00 60.90  ? 198 THR B C    1 
ATOM   3892 O O    . THR B 1 198 ? -6.102  26.139  -11.748 1.00 55.06  ? 198 THR B O    1 
ATOM   3893 C CB   . THR B 1 198 ? -5.709  27.823  -8.864  1.00 71.17  ? 198 THR B CB   1 
ATOM   3894 O OG1  . THR B 1 198 ? -5.602  26.463  -8.433  1.00 72.81  ? 198 THR B OG1  1 
ATOM   3895 C CG2  . THR B 1 198 ? -6.365  28.619  -7.753  1.00 73.30  ? 198 THR B CG2  1 
ATOM   3896 N N    . THR B 1 199 ? -4.815  27.985  -11.826 1.00 62.26  ? 199 THR B N    1 
ATOM   3897 C CA   . THR B 1 199 ? -3.958  27.489  -12.884 1.00 59.29  ? 199 THR B CA   1 
ATOM   3898 C C    . THR B 1 199 ? -2.789  26.722  -12.274 1.00 60.47  ? 199 THR B C    1 
ATOM   3899 O O    . THR B 1 199 ? -2.195  27.161  -11.282 1.00 59.93  ? 199 THR B O    1 
ATOM   3900 C CB   . THR B 1 199 ? -3.489  28.660  -13.737 1.00 56.91  ? 199 THR B CB   1 
ATOM   3901 O OG1  . THR B 1 199 ? -4.650  29.334  -14.222 1.00 55.25  ? 199 THR B OG1  1 
ATOM   3902 C CG2  . THR B 1 199 ? -2.685  28.177  -14.903 1.00 55.49  ? 199 THR B CG2  1 
ATOM   3903 N N    . ILE B 1 200 ? -2.498  25.550  -12.838 1.00 55.69  ? 200 ILE B N    1 
ATOM   3904 C CA   . ILE B 1 200 ? -1.416  24.733  -12.312 1.00 55.87  ? 200 ILE B CA   1 
ATOM   3905 C C    . ILE B 1 200 ? -0.088  25.340  -12.740 1.00 55.68  ? 200 ILE B C    1 
ATOM   3906 O O    . ILE B 1 200 ? 0.455   25.004  -13.794 1.00 51.50  ? 200 ILE B O    1 
ATOM   3907 C CB   . ILE B 1 200 ? -1.549  23.269  -12.758 1.00 53.75  ? 200 ILE B CB   1 
ATOM   3908 C CG1  . ILE B 1 200 ? -3.000  22.788  -12.562 1.00 50.16  ? 200 ILE B CG1  1 
ATOM   3909 C CG2  . ILE B 1 200 ? -0.552  22.394  -11.976 1.00 49.62  ? 200 ILE B CG2  1 
ATOM   3910 C CD1  . ILE B 1 200 ? -3.435  21.744  -13.563 1.00 43.52  ? 200 ILE B CD1  1 
ATOM   3911 N N    . THR B 1 201 ? 0.462   26.196  -11.885 1.00 57.71  ? 201 THR B N    1 
ATOM   3912 C CA   . THR B 1 201 ? 1.641   26.974  -12.239 1.00 55.25  ? 201 THR B CA   1 
ATOM   3913 C C    . THR B 1 201 ? 2.788   26.094  -12.729 1.00 55.38  ? 201 THR B C    1 
ATOM   3914 O O    . THR B 1 201 ? 3.417   26.394  -13.753 1.00 56.85  ? 201 THR B O    1 
ATOM   3915 C CB   . THR B 1 201 ? 2.076   27.802  -11.029 1.00 61.54  ? 201 THR B CB   1 
ATOM   3916 O OG1  . THR B 1 201 ? 0.945   28.527  -10.524 1.00 66.50  ? 201 THR B OG1  1 
ATOM   3917 C CG2  . THR B 1 201 ? 3.188   28.761  -11.421 1.00 61.72  ? 201 THR B CG2  1 
ATOM   3918 N N    . VAL B 1 202 ? 3.074   24.997  -12.017 1.00 54.37  ? 202 VAL B N    1 
ATOM   3919 C CA   . VAL B 1 202 ? 4.194   24.140  -12.404 1.00 53.97  ? 202 VAL B CA   1 
ATOM   3920 C C    . VAL B 1 202 ? 3.996   23.597  -13.820 1.00 53.63  ? 202 VAL B C    1 
ATOM   3921 O O    . VAL B 1 202 ? 4.954   23.502  -14.595 1.00 55.12  ? 202 VAL B O    1 
ATOM   3922 C CB   . VAL B 1 202 ? 4.411   23.011  -11.367 1.00 54.11  ? 202 VAL B CB   1 
ATOM   3923 C CG1  . VAL B 1 202 ? 3.603   21.789  -11.685 1.00 51.99  ? 202 VAL B CG1  1 
ATOM   3924 C CG2  . VAL B 1 202 ? 5.855   22.619  -11.317 1.00 56.02  ? 202 VAL B CG2  1 
ATOM   3925 N N    . ASN B 1 203 ? 2.758   23.255  -14.191 1.00 49.05  ? 203 ASN B N    1 
ATOM   3926 C CA   . ASN B 1 203 ? 2.517   22.746  -15.540 1.00 52.49  ? 203 ASN B CA   1 
ATOM   3927 C C    . ASN B 1 203 ? 2.717   23.829  -16.595 1.00 51.18  ? 203 ASN B C    1 
ATOM   3928 O O    . ASN B 1 203 ? 3.259   23.555  -17.671 1.00 47.11  ? 203 ASN B O    1 
ATOM   3929 C CB   . ASN B 1 203 ? 1.111   22.161  -15.664 1.00 45.64  ? 203 ASN B CB   1 
ATOM   3930 C CG   . ASN B 1 203 ? 0.933   20.890  -14.859 1.00 47.47  ? 203 ASN B CG   1 
ATOM   3931 O OD1  . ASN B 1 203 ? 1.789   20.523  -14.053 1.00 46.60  ? 203 ASN B OD1  1 
ATOM   3932 N ND2  . ASN B 1 203 ? -0.202  20.231  -15.054 1.00 43.24  ? 203 ASN B ND2  1 
ATOM   3933 N N    . VAL B 1 204 ? 2.274   25.057  -16.310 1.00 50.65  ? 204 VAL B N    1 
ATOM   3934 C CA   . VAL B 1 204 ? 2.482   26.163  -17.241 1.00 52.09  ? 204 VAL B CA   1 
ATOM   3935 C C    . VAL B 1 204 ? 3.964   26.353  -17.518 1.00 49.85  ? 204 VAL B C    1 
ATOM   3936 O O    . VAL B 1 204 ? 4.385   26.518  -18.668 1.00 53.62  ? 204 VAL B O    1 
ATOM   3937 C CB   . VAL B 1 204 ? 1.840   27.451  -16.687 1.00 53.75  ? 204 VAL B CB   1 
ATOM   3938 C CG1  . VAL B 1 204 ? 2.151   28.641  -17.608 1.00 58.62  ? 204 VAL B CG1  1 
ATOM   3939 C CG2  . VAL B 1 204 ? 0.306   27.272  -16.576 1.00 47.80  ? 204 VAL B CG2  1 
ATOM   3940 N N    . LEU B 1 205 ? 4.778   26.290  -16.484 1.00 51.56  ? 205 LEU B N    1 
ATOM   3941 C CA   . LEU B 1 205 ? 6.211   26.403  -16.692 1.00 53.77  ? 205 LEU B CA   1 
ATOM   3942 C C    . LEU B 1 205 ? 6.735   25.242  -17.537 1.00 54.75  ? 205 LEU B C    1 
ATOM   3943 O O    . LEU B 1 205 ? 7.525   25.444  -18.466 1.00 54.50  ? 205 LEU B O    1 
ATOM   3944 C CB   . LEU B 1 205 ? 6.908   26.464  -15.340 1.00 55.88  ? 205 LEU B CB   1 
ATOM   3945 C CG   . LEU B 1 205 ? 6.661   27.764  -14.564 1.00 62.72  ? 205 LEU B CG   1 
ATOM   3946 C CD1  . LEU B 1 205 ? 7.297   27.700  -13.162 1.00 59.84  ? 205 LEU B CD1  1 
ATOM   3947 C CD2  . LEU B 1 205 ? 7.119   29.009  -15.324 1.00 62.70  ? 205 LEU B CD2  1 
ATOM   3948 N N    . ALA B 1 206 ? 6.292   24.014  -17.248 1.00 53.08  ? 206 ALA B N    1 
ATOM   3949 C CA   . ALA B 1 206 ? 6.754   22.877  -18.041 1.00 50.33  ? 206 ALA B CA   1 
ATOM   3950 C C    . ALA B 1 206 ? 6.366   23.035  -19.510 1.00 52.24  ? 206 ALA B C    1 
ATOM   3951 O O    . ALA B 1 206 ? 7.098   22.593  -20.412 1.00 51.38  ? 206 ALA B O    1 
ATOM   3952 C CB   . ALA B 1 206 ? 6.195   21.570  -17.465 1.00 49.36  ? 206 ALA B CB   1 
ATOM   3953 N N    . TRP B 1 207 ? 5.213   23.643  -19.773 1.00 49.72  ? 207 TRP B N    1 
ATOM   3954 C CA   . TRP B 1 207 ? 4.791   23.852  -21.154 1.00 47.15  ? 207 TRP B CA   1 
ATOM   3955 C C    . TRP B 1 207 ? 5.641   24.937  -21.827 1.00 52.41  ? 207 TRP B C    1 
ATOM   3956 O O    . TRP B 1 207 ? 6.033   24.782  -22.991 1.00 50.37  ? 207 TRP B O    1 
ATOM   3957 C CB   . TRP B 1 207 ? 3.300   24.183  -21.161 1.00 49.26  ? 207 TRP B CB   1 
ATOM   3958 C CG   . TRP B 1 207 ? 2.647   24.541  -22.483 1.00 52.68  ? 207 TRP B CG   1 
ATOM   3959 C CD1  . TRP B 1 207 ? 2.247   23.692  -23.491 1.00 51.77  ? 207 TRP B CD1  1 
ATOM   3960 C CD2  . TRP B 1 207 ? 2.288   25.859  -22.904 1.00 52.30  ? 207 TRP B CD2  1 
ATOM   3961 N NE1  . TRP B 1 207 ? 1.667   24.414  -24.505 1.00 50.32  ? 207 TRP B NE1  1 
ATOM   3962 C CE2  . TRP B 1 207 ? 1.683   25.744  -24.166 1.00 52.98  ? 207 TRP B CE2  1 
ATOM   3963 C CE3  . TRP B 1 207 ? 2.421   27.131  -22.325 1.00 51.93  ? 207 TRP B CE3  1 
ATOM   3964 C CZ2  . TRP B 1 207 ? 1.210   26.847  -24.857 1.00 54.21  ? 207 TRP B CZ2  1 
ATOM   3965 C CZ3  . TRP B 1 207 ? 1.964   28.221  -23.018 1.00 52.99  ? 207 TRP B CZ3  1 
ATOM   3966 C CH2  . TRP B 1 207 ? 1.354   28.072  -24.267 1.00 48.92  ? 207 TRP B CH2  1 
ATOM   3967 N N    . LEU B 1 208 ? 5.970   26.022  -21.101 1.00 48.81  ? 208 LEU B N    1 
ATOM   3968 C CA   . LEU B 1 208 ? 6.893   27.022  -21.637 1.00 52.36  ? 208 LEU B CA   1 
ATOM   3969 C C    . LEU B 1 208 ? 8.230   26.391  -21.975 1.00 53.61  ? 208 LEU B C    1 
ATOM   3970 O O    . LEU B 1 208 ? 8.889   26.796  -22.934 1.00 58.94  ? 208 LEU B O    1 
ATOM   3971 C CB   . LEU B 1 208 ? 7.113   28.179  -20.640 1.00 52.61  ? 208 LEU B CB   1 
ATOM   3972 C CG   . LEU B 1 208 ? 5.902   29.083  -20.394 1.00 52.41  ? 208 LEU B CG   1 
ATOM   3973 C CD1  . LEU B 1 208 ? 6.223   30.221  -19.453 1.00 57.40  ? 208 LEU B CD1  1 
ATOM   3974 C CD2  . LEU B 1 208 ? 5.322   29.612  -21.701 1.00 51.85  ? 208 LEU B CD2  1 
ATOM   3975 N N    . TYR B 1 209 ? 8.690   25.442  -21.156 1.00 56.35  ? 209 TYR B N    1 
ATOM   3976 C CA   . TYR B 1 209 ? 9.920   24.745  -21.508 1.00 54.26  ? 209 TYR B CA   1 
ATOM   3977 C C    . TYR B 1 209 ? 9.690   23.880  -22.741 1.00 53.19  ? 209 TYR B C    1 
ATOM   3978 O O    . TYR B 1 209 ? 10.510  23.878  -23.659 1.00 57.17  ? 209 TYR B O    1 
ATOM   3979 C CB   . TYR B 1 209 ? 10.427  23.901  -20.340 1.00 54.28  ? 209 TYR B CB   1 
ATOM   3980 C CG   . TYR B 1 209 ? 11.215  24.671  -19.299 1.00 58.74  ? 209 TYR B CG   1 
ATOM   3981 C CD1  . TYR B 1 209 ? 12.536  25.026  -19.523 1.00 63.43  ? 209 TYR B CD1  1 
ATOM   3982 C CD2  . TYR B 1 209 ? 10.639  25.031  -18.094 1.00 58.29  ? 209 TYR B CD2  1 
ATOM   3983 C CE1  . TYR B 1 209 ? 13.263  25.728  -18.574 1.00 65.71  ? 209 TYR B CE1  1 
ATOM   3984 C CE2  . TYR B 1 209 ? 11.347  25.733  -17.148 1.00 61.43  ? 209 TYR B CE2  1 
ATOM   3985 C CZ   . TYR B 1 209 ? 12.665  26.079  -17.390 1.00 66.74  ? 209 TYR B CZ   1 
ATOM   3986 O OH   . TYR B 1 209 ? 13.386  26.780  -16.449 1.00 65.73  ? 209 TYR B OH   1 
ATOM   3987 N N    . ALA B 1 210 ? 8.576   23.148  -22.792 1.00 48.76  ? 210 ALA B N    1 
ATOM   3988 C CA   . ALA B 1 210 ? 8.268   22.419  -24.015 1.00 57.12  ? 210 ALA B CA   1 
ATOM   3989 C C    . ALA B 1 210 ? 8.342   23.347  -25.221 1.00 56.20  ? 210 ALA B C    1 
ATOM   3990 O O    . ALA B 1 210 ? 8.876   22.975  -26.271 1.00 53.21  ? 210 ALA B O    1 
ATOM   3991 C CB   . ALA B 1 210 ? 6.883   21.765  -23.922 1.00 50.52  ? 210 ALA B CB   1 
ATOM   3992 N N    . ALA B 1 211 ? 7.818   24.568  -25.073 1.00 55.94  ? 211 ALA B N    1 
ATOM   3993 C CA   . ALA B 1 211 ? 7.902   25.584  -26.118 1.00 54.90  ? 211 ALA B CA   1 
ATOM   3994 C C    . ALA B 1 211 ? 9.343   25.844  -26.530 1.00 58.22  ? 211 ALA B C    1 
ATOM   3995 O O    . ALA B 1 211 ? 9.667   25.902  -27.719 1.00 58.80  ? 211 ALA B O    1 
ATOM   3996 C CB   . ALA B 1 211 ? 7.255   26.879  -25.627 1.00 55.53  ? 211 ALA B CB   1 
ATOM   3997 N N    . VAL B 1 212 ? 10.219  26.041  -25.554 1.00 55.87  ? 212 VAL B N    1 
ATOM   3998 C CA   . VAL B 1 212 ? 11.614  26.310  -25.863 1.00 58.54  ? 212 VAL B CA   1 
ATOM   3999 C C    . VAL B 1 212 ? 12.246  25.117  -26.568 1.00 55.16  ? 212 VAL B C    1 
ATOM   4000 O O    . VAL B 1 212 ? 13.000  25.279  -27.534 1.00 61.43  ? 212 VAL B O    1 
ATOM   4001 C CB   . VAL B 1 212 ? 12.357  26.699  -24.575 1.00 57.13  ? 212 VAL B CB   1 
ATOM   4002 C CG1  . VAL B 1 212 ? 13.836  26.940  -24.844 1.00 58.21  ? 212 VAL B CG1  1 
ATOM   4003 C CG2  . VAL B 1 212 ? 11.686  27.922  -23.974 1.00 59.31  ? 212 VAL B CG2  1 
ATOM   4004 N N    . ILE B 1 213 ? 11.957  23.905  -26.097 1.00 55.20  ? 213 ILE B N    1 
ATOM   4005 C CA   . ILE B 1 213 ? 12.451  22.708  -26.778 1.00 60.19  ? 213 ILE B CA   1 
ATOM   4006 C C    . ILE B 1 213 ? 12.091  22.747  -28.254 1.00 58.00  ? 213 ILE B C    1 
ATOM   4007 O O    . ILE B 1 213 ? 12.913  22.407  -29.116 1.00 62.06  ? 213 ILE B O    1 
ATOM   4008 C CB   . ILE B 1 213 ? 11.899  21.432  -26.110 1.00 60.15  ? 213 ILE B CB   1 
ATOM   4009 C CG1  . ILE B 1 213 ? 11.803  21.615  -24.611 1.00 57.57  ? 213 ILE B CG1  1 
ATOM   4010 C CG2  . ILE B 1 213 ? 12.777  20.231  -26.424 1.00 59.69  ? 213 ILE B CG2  1 
ATOM   4011 C CD1  . ILE B 1 213 ? 13.135  21.568  -23.991 1.00 57.30  ? 213 ILE B CD1  1 
ATOM   4012 N N    . ASN B 1 214 ? 10.871  23.194  -28.571 1.00 56.18  ? 214 ASN B N    1 
ATOM   4013 C CA   . ASN B 1 214 ? 10.333  23.149  -29.924 1.00 58.03  ? 214 ASN B CA   1 
ATOM   4014 C C    . ASN B 1 214 ? 10.494  24.474  -30.676 1.00 58.02  ? 214 ASN B C    1 
ATOM   4015 O O    . ASN B 1 214 ? 9.694   24.773  -31.570 1.00 56.65  ? 214 ASN B O    1 
ATOM   4016 C CB   . ASN B 1 214 ? 8.864   22.758  -29.874 1.00 55.32  ? 214 ASN B CB   1 
ATOM   4017 C CG   . ASN B 1 214 ? 8.669   21.269  -29.703 1.00 59.80  ? 214 ASN B CG   1 
ATOM   4018 O OD1  . ASN B 1 214 ? 8.287   20.576  -30.642 1.00 60.47  ? 214 ASN B OD1  1 
ATOM   4019 N ND2  . ASN B 1 214 ? 8.928   20.766  -28.495 1.00 58.01  ? 214 ASN B ND2  1 
ATOM   4020 N N    . GLY B 1 215 ? 11.494  25.294  -30.306 1.00 58.99  ? 215 GLY B N    1 
ATOM   4021 C CA   . GLY B 1 215 ? 11.867  26.465  -31.085 1.00 64.22  ? 215 GLY B CA   1 
ATOM   4022 C C    . GLY B 1 215 ? 11.158  27.780  -30.771 1.00 67.12  ? 215 GLY B C    1 
ATOM   4023 O O    . GLY B 1 215 ? 11.621  28.830  -31.239 1.00 69.46  ? 215 GLY B O    1 
ATOM   4024 N N    . ASP B 1 216 ? 10.041  27.770  -30.038 1.00 64.09  ? 216 ASP B N    1 
ATOM   4025 C CA   . ASP B 1 216 ? 9.344   29.007  -29.691 1.00 64.28  ? 216 ASP B CA   1 
ATOM   4026 C C    . ASP B 1 216 ? 10.091  29.678  -28.553 1.00 65.55  ? 216 ASP B C    1 
ATOM   4027 O O    . ASP B 1 216 ? 10.294  29.075  -27.498 1.00 71.08  ? 216 ASP B O    1 
ATOM   4028 C CB   . ASP B 1 216 ? 7.899   28.743  -29.285 1.00 61.28  ? 216 ASP B CB   1 
ATOM   4029 C CG   . ASP B 1 216 ? 7.054   28.210  -30.424 1.00 72.06  ? 216 ASP B CG   1 
ATOM   4030 O OD1  . ASP B 1 216 ? 7.616   27.582  -31.356 1.00 72.68  ? 216 ASP B OD1  1 
ATOM   4031 O OD2  . ASP B 1 216 ? 5.817   28.421  -30.382 1.00 68.28  ? 216 ASP B OD2  1 
ATOM   4032 N N    . ARG B 1 217 ? 10.507  30.911  -28.753 1.00 68.62  ? 217 ARG B N    1 
ATOM   4033 C CA   . ARG B 1 217 ? 11.293  31.582  -27.729 1.00 70.03  ? 217 ARG B CA   1 
ATOM   4034 C C    . ARG B 1 217 ? 10.964  33.071  -27.603 1.00 69.49  ? 217 ARG B C    1 
ATOM   4035 O O    . ARG B 1 217 ? 11.680  33.795  -26.893 1.00 69.60  ? 217 ARG B O    1 
ATOM   4036 C CB   . ARG B 1 217 ? 12.779  31.385  -28.041 1.00 64.70  ? 217 ARG B CB   1 
ATOM   4037 C CG   . ARG B 1 217 ? 13.243  29.966  -27.919 1.00 70.63  ? 217 ARG B CG   1 
ATOM   4038 C CD   . ARG B 1 217 ? 14.647  29.776  -28.478 1.00 71.40  ? 217 ARG B CD   1 
ATOM   4039 N NE   . ARG B 1 217 ? 15.506  30.725  -27.795 1.00 69.14  ? 217 ARG B NE   1 
ATOM   4040 C CZ   . ARG B 1 217 ? 16.164  30.437  -26.680 1.00 72.08  ? 217 ARG B CZ   1 
ATOM   4041 N NH1  . ARG B 1 217 ? 16.108  29.228  -26.151 1.00 69.03  ? 217 ARG B NH1  1 
ATOM   4042 N NH2  . ARG B 1 217 ? 16.957  31.359  -26.129 1.00 71.73  ? 217 ARG B NH2  1 
ATOM   4043 N N    . TRP B 1 218 ? 9.903   33.546  -28.263 1.00 72.42  ? 218 TRP B N    1 
ATOM   4044 C CA   . TRP B 1 218 ? 9.612   34.973  -28.292 1.00 71.87  ? 218 TRP B CA   1 
ATOM   4045 C C    . TRP B 1 218 ? 9.332   35.540  -26.913 1.00 70.29  ? 218 TRP B C    1 
ATOM   4046 O O    . TRP B 1 218 ? 9.487   36.750  -26.710 1.00 69.31  ? 218 TRP B O    1 
ATOM   4047 C CB   . TRP B 1 218 ? 8.428   35.244  -29.241 1.00 73.10  ? 218 TRP B CB   1 
ATOM   4048 C CG   . TRP B 1 218 ? 7.023   34.726  -28.817 1.00 67.99  ? 218 TRP B CG   1 
ATOM   4049 C CD1  . TRP B 1 218 ? 6.376   33.619  -29.298 1.00 69.62  ? 218 TRP B CD1  1 
ATOM   4050 C CD2  . TRP B 1 218 ? 6.112   35.342  -27.893 1.00 71.66  ? 218 TRP B CD2  1 
ATOM   4051 N NE1  . TRP B 1 218 ? 5.136   33.493  -28.720 1.00 70.07  ? 218 TRP B NE1  1 
ATOM   4052 C CE2  . TRP B 1 218 ? 4.949   34.533  -27.849 1.00 69.13  ? 218 TRP B CE2  1 
ATOM   4053 C CE3  . TRP B 1 218 ? 6.174   36.488  -27.081 1.00 74.69  ? 218 TRP B CE3  1 
ATOM   4054 C CZ2  . TRP B 1 218 ? 3.859   34.834  -27.039 1.00 69.12  ? 218 TRP B CZ2  1 
ATOM   4055 C CZ3  . TRP B 1 218 ? 5.086   36.785  -26.269 1.00 71.45  ? 218 TRP B CZ3  1 
ATOM   4056 C CH2  . TRP B 1 218 ? 3.947   35.959  -26.252 1.00 72.92  ? 218 TRP B CH2  1 
ATOM   4057 N N    . PHE B 1 219 ? 9.001   34.694  -25.945 1.00 69.81  ? 219 PHE B N    1 
ATOM   4058 C CA   . PHE B 1 219 ? 8.646   35.154  -24.609 1.00 68.18  ? 219 PHE B CA   1 
ATOM   4059 C C    . PHE B 1 219 ? 9.823   35.190  -23.653 1.00 66.97  ? 219 PHE B C    1 
ATOM   4060 O O    . PHE B 1 219 ? 9.652   35.646  -22.520 1.00 74.02  ? 219 PHE B O    1 
ATOM   4061 C CB   . PHE B 1 219 ? 7.550   34.260  -24.022 1.00 69.20  ? 219 PHE B CB   1 
ATOM   4062 C CG   . PHE B 1 219 ? 7.851   32.807  -24.153 1.00 67.11  ? 219 PHE B CG   1 
ATOM   4063 C CD1  . PHE B 1 219 ? 7.446   32.105  -25.269 1.00 66.86  ? 219 PHE B CD1  1 
ATOM   4064 C CD2  . PHE B 1 219 ? 8.587   32.152  -23.184 1.00 67.56  ? 219 PHE B CD2  1 
ATOM   4065 C CE1  . PHE B 1 219 ? 7.739   30.775  -25.401 1.00 64.57  ? 219 PHE B CE1  1 
ATOM   4066 C CE2  . PHE B 1 219 ? 8.876   30.813  -23.318 1.00 64.61  ? 219 PHE B CE2  1 
ATOM   4067 C CZ   . PHE B 1 219 ? 8.462   30.136  -24.422 1.00 62.27  ? 219 PHE B CZ   1 
ATOM   4068 N N    . LEU B 1 220 ? 11.009  34.755  -24.065 1.00 67.72  ? 220 LEU B N    1 
ATOM   4069 C CA   . LEU B 1 220 ? 12.143  34.685  -23.144 1.00 68.23  ? 220 LEU B CA   1 
ATOM   4070 C C    . LEU B 1 220 ? 12.701  36.080  -22.881 1.00 78.85  ? 220 LEU B C    1 
ATOM   4071 O O    . LEU B 1 220 ? 13.096  36.786  -23.816 1.00 78.27  ? 220 LEU B O    1 
ATOM   4072 C CB   . LEU B 1 220 ? 13.238  33.783  -23.705 1.00 71.12  ? 220 LEU B CB   1 
ATOM   4073 C CG   . LEU B 1 220 ? 12.905  32.306  -23.894 1.00 70.82  ? 220 LEU B CG   1 
ATOM   4074 C CD1  . LEU B 1 220 ? 14.155  31.540  -24.343 1.00 65.95  ? 220 LEU B CD1  1 
ATOM   4075 C CD2  . LEU B 1 220 ? 12.313  31.738  -22.602 1.00 72.58  ? 220 LEU B CD2  1 
ATOM   4076 N N    . ASN B 1 221 ? 12.767  36.465  -21.612 1.00 77.94  ? 221 ASN B N    1 
ATOM   4077 C CA   . ASN B 1 221 ? 13.279  37.761  -21.215 1.00 83.95  ? 221 ASN B CA   1 
ATOM   4078 C C    . ASN B 1 221 ? 14.707  37.638  -20.714 1.00 89.69  ? 221 ASN B C    1 
ATOM   4079 O O    . ASN B 1 221 ? 15.211  36.547  -20.449 1.00 94.46  ? 221 ASN B O    1 
ATOM   4080 C CB   . ASN B 1 221 ? 12.401  38.342  -20.108 1.00 89.48  ? 221 ASN B CB   1 
ATOM   4081 C CG   . ASN B 1 221 ? 12.510  37.553  -18.794 1.00 83.39  ? 221 ASN B CG   1 
ATOM   4082 O OD1  . ASN B 1 221 ? 13.279  36.592  -18.669 1.00 79.19  ? 221 ASN B OD1  1 
ATOM   4083 N ND2  . ASN B 1 221 ? 11.727  37.963  -17.813 1.00 81.92  ? 221 ASN B ND2  1 
ATOM   4084 N N    . ARG B 1 222 ? 15.354  38.783  -20.567 1.00 98.22  ? 222 ARG B N    1 
ATOM   4085 C CA   . ARG B 1 222 ? 16.574  38.854  -19.778 1.00 105.92 ? 222 ARG B CA   1 
ATOM   4086 C C    . ARG B 1 222 ? 16.279  39.153  -18.317 1.00 102.93 ? 222 ARG B C    1 
ATOM   4087 O O    . ARG B 1 222 ? 17.130  38.897  -17.451 1.00 105.18 ? 222 ARG B O    1 
ATOM   4088 C CB   . ARG B 1 222 ? 17.512  39.930  -20.332 1.00 116.75 ? 222 ARG B CB   1 
ATOM   4089 C CG   . ARG B 1 222 ? 17.252  41.326  -19.762 1.00 114.97 ? 222 ARG B CG   1 
ATOM   4090 C CD   . ARG B 1 222 ? 15.893  41.858  -20.229 1.00 117.03 ? 222 ARG B CD   1 
ATOM   4091 N NE   . ARG B 1 222 ? 15.725  41.817  -21.681 1.00 117.05 ? 222 ARG B NE   1 
ATOM   4092 C CZ   . ARG B 1 222 ? 16.011  42.822  -22.500 1.00 119.37 ? 222 ARG B CZ   1 
ATOM   4093 N NH1  . ARG B 1 222 ? 16.520  43.960  -22.049 1.00 120.13 ? 222 ARG B NH1  1 
ATOM   4094 N NH2  . ARG B 1 222 ? 15.782  42.683  -23.803 1.00 115.53 ? 222 ARG B NH2  1 
ATOM   4095 N N    . PHE B 1 223 ? 15.087  39.673  -18.030 1.00 93.09  ? 223 PHE B N    1 
ATOM   4096 C CA   . PHE B 1 223 ? 14.734  39.984  -16.659 1.00 95.77  ? 223 PHE B CA   1 
ATOM   4097 C C    . PHE B 1 223 ? 14.631  38.683  -15.871 1.00 88.35  ? 223 PHE B C    1 
ATOM   4098 O O    . PHE B 1 223 ? 14.301  37.631  -16.416 1.00 88.91  ? 223 PHE B O    1 
ATOM   4099 C CB   . PHE B 1 223 ? 13.411  40.750  -16.586 1.00 92.33  ? 223 PHE B CB   1 
ATOM   4100 C CG   . PHE B 1 223 ? 13.595  42.215  -16.281 1.00 101.71 ? 223 PHE B CG   1 
ATOM   4101 C CD1  . PHE B 1 223 ? 14.240  42.639  -15.119 1.00 101.93 ? 223 PHE B CD1  1 
ATOM   4102 C CD2  . PHE B 1 223 ? 13.105  43.173  -17.153 1.00 103.16 ? 223 PHE B CD2  1 
ATOM   4103 C CE1  . PHE B 1 223 ? 14.421  44.009  -14.848 1.00 104.18 ? 223 PHE B CE1  1 
ATOM   4104 C CE2  . PHE B 1 223 ? 13.271  44.525  -16.893 1.00 105.88 ? 223 PHE B CE2  1 
ATOM   4105 C CZ   . PHE B 1 223 ? 13.931  44.951  -15.738 1.00 111.52 ? 223 PHE B CZ   1 
ATOM   4106 N N    . THR B 1 224 ? 14.944  38.754  -14.585 1.00 89.08  ? 224 THR B N    1 
ATOM   4107 C CA   . THR B 1 224 ? 14.760  37.646  -13.658 1.00 86.48  ? 224 THR B CA   1 
ATOM   4108 C C    . THR B 1 224 ? 13.891  38.107  -12.495 1.00 87.70  ? 224 THR B C    1 
ATOM   4109 O O    . THR B 1 224 ? 13.688  39.301  -12.277 1.00 90.97  ? 224 THR B O    1 
ATOM   4110 C CB   . THR B 1 224 ? 16.099  37.109  -13.131 1.00 87.24  ? 224 THR B CB   1 
ATOM   4111 O OG1  . THR B 1 224 ? 15.906  35.792  -12.598 1.00 85.54  ? 224 THR B OG1  1 
ATOM   4112 C CG2  . THR B 1 224 ? 16.660  38.023  -12.036 1.00 91.15  ? 224 THR B CG2  1 
ATOM   4113 N N    . THR B 1 225 ? 13.382  37.156  -11.720 1.00 85.00  ? 225 THR B N    1 
ATOM   4114 C CA   . THR B 1 225 ? 12.606  37.511  -10.537 1.00 83.83  ? 225 THR B CA   1 
ATOM   4115 C C    . THR B 1 225 ? 13.043  36.639  -9.360  1.00 86.19  ? 225 THR B C    1 
ATOM   4116 O O    . THR B 1 225 ? 14.105  36.002  -9.368  1.00 86.06  ? 225 THR B O    1 
ATOM   4117 C CB   . THR B 1 225 ? 11.100  37.406  -10.844 1.00 83.03  ? 225 THR B CB   1 
ATOM   4118 O OG1  . THR B 1 225 ? 10.349  37.556  -9.631  1.00 86.94  ? 225 THR B OG1  1 
ATOM   4119 C CG2  . THR B 1 225 ? 10.745  36.054  -11.504 1.00 80.21  ? 225 THR B CG2  1 
ATOM   4120 N N    . THR B 1 226 ? 12.217  36.626  -8.317  1.00 85.52  ? 226 THR B N    1 
ATOM   4121 C CA   . THR B 1 226 ? 12.447  35.806  -7.144  1.00 86.98  ? 226 THR B CA   1 
ATOM   4122 C C    . THR B 1 226 ? 11.206  34.971  -6.874  1.00 82.04  ? 226 THR B C    1 
ATOM   4123 O O    . THR B 1 226 ? 10.091  35.355  -7.241  1.00 85.73  ? 226 THR B O    1 
ATOM   4124 C CB   . THR B 1 226 ? 12.727  36.677  -5.916  1.00 90.81  ? 226 THR B CB   1 
ATOM   4125 O OG1  . THR B 1 226 ? 11.487  37.256  -5.477  1.00 90.16  ? 226 THR B OG1  1 
ATOM   4126 C CG2  . THR B 1 226 ? 13.710  37.800  -6.266  1.00 91.81  ? 226 THR B CG2  1 
ATOM   4127 N N    . LEU B 1 227 ? 11.402  33.827  -6.219  1.00 81.79  ? 227 LEU B N    1 
ATOM   4128 C CA   . LEU B 1 227 ? 10.266  32.963  -5.914  1.00 81.13  ? 227 LEU B CA   1 
ATOM   4129 C C    . LEU B 1 227 ? 9.206   33.693  -5.090  1.00 83.16  ? 227 LEU B C    1 
ATOM   4130 O O    . LEU B 1 227 ? 8.002   33.468  -5.274  1.00 85.66  ? 227 LEU B O    1 
ATOM   4131 C CB   . LEU B 1 227 ? 10.734  31.695  -5.200  1.00 79.34  ? 227 LEU B CB   1 
ATOM   4132 C CG   . LEU B 1 227 ? 9.599   30.833  -4.645  1.00 79.71  ? 227 LEU B CG   1 
ATOM   4133 C CD1  . LEU B 1 227 ? 8.815   30.172  -5.793  1.00 76.17  ? 227 LEU B CD1  1 
ATOM   4134 C CD2  . LEU B 1 227 ? 10.133  29.792  -3.676  1.00 78.28  ? 227 LEU B CD2  1 
ATOM   4135 N N    . ASN B 1 228 ? 9.634   34.580  -4.179  1.00 83.91  ? 228 ASN B N    1 
ATOM   4136 C CA   . ASN B 1 228 ? 8.677   35.331  -3.370  1.00 83.68  ? 228 ASN B CA   1 
ATOM   4137 C C    . ASN B 1 228 ? 7.857   36.295  -4.221  1.00 87.38  ? 228 ASN B C    1 
ATOM   4138 O O    . ASN B 1 228 ? 6.623   36.298  -4.159  1.00 87.93  ? 228 ASN B O    1 
ATOM   4139 C CB   . ASN B 1 228 ? 9.423   36.092  -2.270  1.00 87.11  ? 228 ASN B CB   1 
ATOM   4140 C CG   . ASN B 1 228 ? 9.535   35.303  -0.983  1.00 87.06  ? 228 ASN B CG   1 
ATOM   4141 O OD1  . ASN B 1 228 ? 9.011   34.199  -0.863  1.00 84.84  ? 228 ASN B OD1  1 
ATOM   4142 N ND2  . ASN B 1 228 ? 10.228  35.874  -0.010  1.00 90.53  ? 228 ASN B ND2  1 
ATOM   4143 N N    . ASP B 1 229 ? 8.532   37.126  -5.020  1.00 90.11  ? 229 ASP B N    1 
ATOM   4144 C CA   . ASP B 1 229 ? 7.842   38.140  -5.817  1.00 91.37  ? 229 ASP B CA   1 
ATOM   4145 C C    . ASP B 1 229 ? 6.979   37.519  -6.902  1.00 90.29  ? 229 ASP B C    1 
ATOM   4146 O O    . ASP B 1 229 ? 5.878   38.010  -7.189  1.00 89.62  ? 229 ASP B O    1 
ATOM   4147 C CB   . ASP B 1 229 ? 8.844   39.124  -6.400  1.00 95.20  ? 229 ASP B CB   1 
ATOM   4148 C CG   . ASP B 1 229 ? 9.478   39.967  -5.328  1.00 99.58  ? 229 ASP B CG   1 
ATOM   4149 O OD1  . ASP B 1 229 ? 10.562  39.605  -4.823  1.00 102.48 ? 229 ASP B OD1  1 
ATOM   4150 O OD2  . ASP B 1 229 ? 8.840   40.966  -4.948  1.00 98.94  ? 229 ASP B OD2  1 
ATOM   4151 N N    . PHE B 1 230 ? 7.472   36.470  -7.553  1.00 89.11  ? 230 PHE B N    1 
ATOM   4152 C CA   . PHE B 1 230 ? 6.637   35.833  -8.558  1.00 90.35  ? 230 PHE B CA   1 
ATOM   4153 C C    . PHE B 1 230 ? 5.321   35.371  -7.955  1.00 86.90  ? 230 PHE B C    1 
ATOM   4154 O O    . PHE B 1 230 ? 4.276   35.404  -8.620  1.00 88.33  ? 230 PHE B O    1 
ATOM   4155 C CB   . PHE B 1 230 ? 7.347   34.642  -9.184  1.00 86.91  ? 230 PHE B CB   1 
ATOM   4156 C CG   . PHE B 1 230 ? 6.426   33.785  -9.997  1.00 91.82  ? 230 PHE B CG   1 
ATOM   4157 C CD1  . PHE B 1 230 ? 5.875   34.266  -11.174 1.00 89.44  ? 230 PHE B CD1  1 
ATOM   4158 C CD2  . PHE B 1 230 ? 6.064   32.519  -9.563  1.00 88.52  ? 230 PHE B CD2  1 
ATOM   4159 C CE1  . PHE B 1 230 ? 5.010   33.494  -11.918 1.00 80.68  ? 230 PHE B CE1  1 
ATOM   4160 C CE2  . PHE B 1 230 ? 5.202   31.746  -10.308 1.00 82.40  ? 230 PHE B CE2  1 
ATOM   4161 C CZ   . PHE B 1 230 ? 4.675   32.236  -11.485 1.00 79.66  ? 230 PHE B CZ   1 
ATOM   4162 N N    . ASN B 1 231 ? 5.350   34.910  -6.708  1.00 85.08  ? 231 ASN B N    1 
ATOM   4163 C CA   . ASN B 1 231 ? 4.116   34.399  -6.131  1.00 86.85  ? 231 ASN B CA   1 
ATOM   4164 C C    . ASN B 1 231 ? 3.122   35.524  -5.851  1.00 87.29  ? 231 ASN B C    1 
ATOM   4165 O O    . ASN B 1 231 ? 1.910   35.333  -6.013  1.00 86.88  ? 231 ASN B O    1 
ATOM   4166 C CB   . ASN B 1 231 ? 4.433   33.614  -4.856  1.00 82.95  ? 231 ASN B CB   1 
ATOM   4167 C CG   . ASN B 1 231 ? 4.628   32.128  -5.125  1.00 81.49  ? 231 ASN B CG   1 
ATOM   4168 O OD1  . ASN B 1 231 ? 5.539   31.494  -4.576  1.00 78.10  ? 231 ASN B OD1  1 
ATOM   4169 N ND2  . ASN B 1 231 ? 3.804   31.578  -6.017  1.00 79.92  ? 231 ASN B ND2  1 
ATOM   4170 N N    . LEU B 1 232 ? 3.609   36.712  -5.473  1.00 87.02  ? 232 LEU B N    1 
ATOM   4171 C CA   . LEU B 1 232 ? 2.717   37.864  -5.372  1.00 89.11  ? 232 LEU B CA   1 
ATOM   4172 C C    . LEU B 1 232 ? 2.108   38.182  -6.725  1.00 87.88  ? 232 LEU B C    1 
ATOM   4173 O O    . LEU B 1 232 ? 1.003   38.730  -6.800  1.00 89.51  ? 232 LEU B O    1 
ATOM   4174 C CB   . LEU B 1 232 ? 3.429   39.082  -4.775  1.00 92.17  ? 232 LEU B CB   1 
ATOM   4175 C CG   . LEU B 1 232 ? 3.734   39.100  -3.258  1.00 100.15 ? 232 LEU B CG   1 
ATOM   4176 C CD1  . LEU B 1 232 ? 2.576   38.512  -2.429  1.00 96.67  ? 232 LEU B CD1  1 
ATOM   4177 C CD2  . LEU B 1 232 ? 5.059   38.436  -2.880  1.00 96.89  ? 232 LEU B CD2  1 
ATOM   4178 N N    . VAL B 1 233 ? 2.790   37.800  -7.799  1.00 87.59  ? 233 VAL B N    1 
ATOM   4179 C CA   . VAL B 1 233 ? 2.229   37.959  -9.130  1.00 85.30  ? 233 VAL B CA   1 
ATOM   4180 C C    . VAL B 1 233 ? 1.376   36.755  -9.511  1.00 83.47  ? 233 VAL B C    1 
ATOM   4181 O O    . VAL B 1 233 ? 0.408   36.897  -10.265 1.00 81.16  ? 233 VAL B O    1 
ATOM   4182 C CB   . VAL B 1 233 ? 3.360   38.174  -10.148 1.00 85.77  ? 233 VAL B CB   1 
ATOM   4183 C CG1  . VAL B 1 233 ? 2.889   37.820  -11.530 1.00 85.64  ? 233 VAL B CG1  1 
ATOM   4184 C CG2  . VAL B 1 233 ? 3.887   39.611  -10.084 1.00 87.60  ? 233 VAL B CG2  1 
ATOM   4185 N N    . ALA B 1 234 ? 1.712   35.562  -9.017  1.00 86.25  ? 234 ALA B N    1 
ATOM   4186 C CA   . ALA B 1 234 ? 0.844   34.414  -9.264  1.00 81.29  ? 234 ALA B CA   1 
ATOM   4187 C C    . ALA B 1 234 ? -0.513  34.613  -8.605  1.00 80.77  ? 234 ALA B C    1 
ATOM   4188 O O    . ALA B 1 234 ? -1.558  34.401  -9.229  1.00 80.01  ? 234 ALA B O    1 
ATOM   4189 C CB   . ALA B 1 234 ? 1.497   33.134  -8.748  1.00 78.19  ? 234 ALA B CB   1 
ATOM   4190 N N    . MET B 1 235 ? -0.515  35.042  -7.339  1.00 80.81  ? 235 MET B N    1 
ATOM   4191 C CA   . MET B 1 235 ? -1.774  35.213  -6.615  1.00 84.76  ? 235 MET B CA   1 
ATOM   4192 C C    . MET B 1 235 ? -2.690  36.261  -7.244  1.00 83.88  ? 235 MET B C    1 
ATOM   4193 O O    . MET B 1 235 ? -3.904  36.040  -7.356  1.00 77.17  ? 235 MET B O    1 
ATOM   4194 C CB   . MET B 1 235 ? -1.499  35.532  -5.145  1.00 90.63  ? 235 MET B CB   1 
ATOM   4195 C CG   . MET B 1 235 ? -2.505  34.840  -4.224  1.00 96.57  ? 235 MET B CG   1 
ATOM   4196 S SD   . MET B 1 235 ? -2.992  33.171  -4.816  1.00 112.90 ? 235 MET B SD   1 
ATOM   4197 C CE   . MET B 1 235 ? -1.449  32.496  -5.463  1.00 83.05  ? 235 MET B CE   1 
ATOM   4198 N N    . LYS B 1 236 ? -2.141  37.405  -7.669  1.00 82.17  ? 236 LYS B N    1 
ATOM   4199 C CA   . LYS B 1 236 ? -2.994  38.393  -8.322  1.00 81.77  ? 236 LYS B CA   1 
ATOM   4200 C C    . LYS B 1 236 ? -3.679  37.818  -9.549  1.00 82.10  ? 236 LYS B C    1 
ATOM   4201 O O    . LYS B 1 236 ? -4.662  38.396  -10.022 1.00 90.40  ? 236 LYS B O    1 
ATOM   4202 C CB   . LYS B 1 236 ? -2.219  39.664  -8.682  1.00 92.10  ? 236 LYS B CB   1 
ATOM   4203 C CG   . LYS B 1 236 ? -2.961  40.594  -9.669  1.00 94.51  ? 236 LYS B CG   1 
ATOM   4204 C CD   . LYS B 1 236 ? -2.047  41.354  -10.634 1.00 92.93  ? 236 LYS B CD   1 
ATOM   4205 C CE   . LYS B 1 236 ? -2.250  42.885  -10.568 1.00 89.20  ? 236 LYS B CE   1 
ATOM   4206 N NZ   . LYS B 1 236 ? -2.693  43.395  -9.227  1.00 87.53  ? 236 LYS B NZ   1 
ATOM   4207 N N    . TYR B 1 237 ? -3.209  36.678  -10.059 1.00 82.10  ? 237 TYR B N    1 
ATOM   4208 C CA   . TYR B 1 237 ? -3.711  36.110  -11.306 1.00 80.83  ? 237 TYR B CA   1 
ATOM   4209 C C    . TYR B 1 237 ? -4.298  34.719  -11.134 1.00 79.16  ? 237 TYR B C    1 
ATOM   4210 O O    . TYR B 1 237 ? -4.626  34.070  -12.131 1.00 72.40  ? 237 TYR B O    1 
ATOM   4211 C CB   . TYR B 1 237 ? -2.630  36.073  -12.395 1.00 77.55  ? 237 TYR B CB   1 
ATOM   4212 C CG   . TYR B 1 237 ? -2.295  37.406  -13.019 1.00 77.98  ? 237 TYR B CG   1 
ATOM   4213 C CD1  . TYR B 1 237 ? -2.790  37.713  -14.287 1.00 77.12  ? 237 TYR B CD1  1 
ATOM   4214 C CD2  . TYR B 1 237 ? -1.500  38.343  -12.380 1.00 75.03  ? 237 TYR B CD2  1 
ATOM   4215 C CE1  . TYR B 1 237 ? -2.507  38.912  -14.902 1.00 80.63  ? 237 TYR B CE1  1 
ATOM   4216 C CE2  . TYR B 1 237 ? -1.209  39.567  -12.989 1.00 79.08  ? 237 TYR B CE2  1 
ATOM   4217 C CZ   . TYR B 1 237 ? -1.717  39.841  -14.256 1.00 83.84  ? 237 TYR B CZ   1 
ATOM   4218 O OH   . TYR B 1 237 ? -1.459  41.037  -14.898 1.00 86.10  ? 237 TYR B OH   1 
ATOM   4219 N N    . ASN B 1 238 ? -4.453  34.240  -9.905  1.00 84.16  ? 238 ASN B N    1 
ATOM   4220 C CA   . ASN B 1 238 ? -5.111  32.958  -9.692  1.00 81.03  ? 238 ASN B CA   1 
ATOM   4221 C C    . ASN B 1 238 ? -4.247  31.776  -10.140 1.00 76.92  ? 238 ASN B C    1 
ATOM   4222 O O    . ASN B 1 238 ? -4.742  30.816  -10.724 1.00 77.67  ? 238 ASN B O    1 
ATOM   4223 C CB   . ASN B 1 238 ? -6.454  32.969  -10.425 1.00 84.99  ? 238 ASN B CB   1 
ATOM   4224 C CG   . ASN B 1 238 ? -7.406  31.930  -9.919  1.00 91.96  ? 238 ASN B CG   1 
ATOM   4225 O OD1  . ASN B 1 238 ? -8.584  31.918  -10.288 1.00 93.25  ? 238 ASN B OD1  1 
ATOM   4226 N ND2  . ASN B 1 238 ? -6.919  31.066  -9.041  1.00 91.99  ? 238 ASN B ND2  1 
ATOM   4227 N N    . TYR B 1 239 ? -2.949  31.845  -9.881  1.00 75.20  ? 239 TYR B N    1 
ATOM   4228 C CA   . TYR B 1 239 ? -2.034  30.759  -10.193 1.00 69.58  ? 239 TYR B CA   1 
ATOM   4229 C C    . TYR B 1 239 ? -1.657  30.085  -8.881  1.00 77.22  ? 239 TYR B C    1 
ATOM   4230 O O    . TYR B 1 239 ? -1.186  30.751  -7.957  1.00 77.64  ? 239 TYR B O    1 
ATOM   4231 C CB   . TYR B 1 239 ? -0.782  31.273  -10.909 1.00 64.82  ? 239 TYR B CB   1 
ATOM   4232 C CG   . TYR B 1 239 ? -0.883  31.309  -12.412 1.00 66.71  ? 239 TYR B CG   1 
ATOM   4233 C CD1  . TYR B 1 239 ? -2.004  31.844  -13.045 1.00 66.40  ? 239 TYR B CD1  1 
ATOM   4234 C CD2  . TYR B 1 239 ? 0.140   30.811  -13.209 1.00 61.56  ? 239 TYR B CD2  1 
ATOM   4235 C CE1  . TYR B 1 239 ? -2.107  31.869  -14.437 1.00 63.43  ? 239 TYR B CE1  1 
ATOM   4236 C CE2  . TYR B 1 239 ? 0.050   30.837  -14.603 1.00 62.14  ? 239 TYR B CE2  1 
ATOM   4237 C CZ   . TYR B 1 239 ? -1.077  31.367  -15.213 1.00 61.37  ? 239 TYR B CZ   1 
ATOM   4238 O OH   . TYR B 1 239 ? -1.169  31.376  -16.590 1.00 59.70  ? 239 TYR B OH   1 
ATOM   4239 N N    . GLU B 1 240 ? -1.905  28.786  -8.788  1.00 81.05  ? 240 GLU B N    1 
ATOM   4240 C CA   . GLU B 1 240 ? -1.408  27.939  -7.706  1.00 80.71  ? 240 GLU B CA   1 
ATOM   4241 C C    . GLU B 1 240 ? -0.010  28.411  -7.333  1.00 79.74  ? 240 GLU B C    1 
ATOM   4242 O O    . GLU B 1 240 ? 0.865   28.479  -8.206  1.00 79.20  ? 240 GLU B O    1 
ATOM   4243 C CB   . GLU B 1 240 ? -1.431  26.497  -8.191  1.00 82.72  ? 240 GLU B CB   1 
ATOM   4244 C CG   . GLU B 1 240 ? -0.995  25.423  -7.274  1.00 85.47  ? 240 GLU B CG   1 
ATOM   4245 C CD   . GLU B 1 240 ? -1.232  24.096  -7.960  1.00 89.53  ? 240 GLU B CD   1 
ATOM   4246 O OE1  . GLU B 1 240 ? -2.422  23.748  -8.151  1.00 80.59  ? 240 GLU B OE1  1 
ATOM   4247 O OE2  . GLU B 1 240 ? -0.243  23.435  -8.360  1.00 91.08  ? 240 GLU B OE2  1 
ATOM   4248 N N    . PRO B 1 241 ? 0.240   28.778  -6.077  1.00 82.00  ? 241 PRO B N    1 
ATOM   4249 C CA   . PRO B 1 241 ? 1.590   29.218  -5.698  1.00 76.50  ? 241 PRO B CA   1 
ATOM   4250 C C    . PRO B 1 241 ? 2.649   28.186  -6.049  1.00 78.30  ? 241 PRO B C    1 
ATOM   4251 O O    . PRO B 1 241 ? 2.423   26.979  -5.964  1.00 81.10  ? 241 PRO B O    1 
ATOM   4252 C CB   . PRO B 1 241 ? 1.498   29.433  -4.182  1.00 73.48  ? 241 PRO B CB   1 
ATOM   4253 C CG   . PRO B 1 241 ? 0.056   29.361  -3.833  1.00 80.53  ? 241 PRO B CG   1 
ATOM   4254 C CD   . PRO B 1 241 ? -0.766  29.083  -5.047  1.00 78.23  ? 241 PRO B CD   1 
ATOM   4255 N N    . LEU B 1 242 ? 3.818   28.687  -6.446  1.00 79.44  ? 242 LEU B N    1 
ATOM   4256 C CA   . LEU B 1 242 ? 4.970   27.871  -6.817  1.00 77.03  ? 242 LEU B CA   1 
ATOM   4257 C C    . LEU B 1 242 ? 5.840   27.624  -5.588  1.00 78.57  ? 242 LEU B C    1 
ATOM   4258 O O    . LEU B 1 242 ? 6.310   28.579  -4.950  1.00 77.93  ? 242 LEU B O    1 
ATOM   4259 C CB   . LEU B 1 242 ? 5.791   28.566  -7.910  1.00 74.09  ? 242 LEU B CB   1 
ATOM   4260 C CG   . LEU B 1 242 ? 6.618   27.789  -8.946  1.00 70.85  ? 242 LEU B CG   1 
ATOM   4261 C CD1  . LEU B 1 242 ? 7.159   28.743  -9.973  1.00 72.96  ? 242 LEU B CD1  1 
ATOM   4262 C CD2  . LEU B 1 242 ? 7.765   27.024  -8.338  1.00 74.20  ? 242 LEU B CD2  1 
ATOM   4263 N N    . THR B 1 243 ? 6.079   26.354  -5.274  1.00 78.60  ? 243 THR B N    1 
ATOM   4264 C CA   . THR B 1 243 ? 6.915   25.972  -4.144  1.00 78.74  ? 243 THR B CA   1 
ATOM   4265 C C    . THR B 1 243 ? 8.317   25.603  -4.615  1.00 75.50  ? 243 THR B C    1 
ATOM   4266 O O    . THR B 1 243 ? 8.560   25.379  -5.801  1.00 73.48  ? 243 THR B O    1 
ATOM   4267 C CB   . THR B 1 243 ? 6.298   24.795  -3.378  1.00 80.57  ? 243 THR B CB   1 
ATOM   4268 O OG1  . THR B 1 243 ? 6.733   23.565  -3.976  1.00 81.16  ? 243 THR B OG1  1 
ATOM   4269 C CG2  . THR B 1 243 ? 4.777   24.863  -3.417  1.00 81.29  ? 243 THR B CG2  1 
ATOM   4270 N N    . GLN B 1 244 ? 9.237   25.514  -3.645  1.00 80.11  ? 244 GLN B N    1 
ATOM   4271 C CA   . GLN B 1 244 ? 10.604  25.065  -3.916  1.00 79.35  ? 244 GLN B CA   1 
ATOM   4272 C C    . GLN B 1 244 ? 10.621  23.623  -4.401  1.00 79.07  ? 244 GLN B C    1 
ATOM   4273 O O    . GLN B 1 244 ? 11.493  23.234  -5.191  1.00 78.80  ? 244 GLN B O    1 
ATOM   4274 C CB   . GLN B 1 244 ? 11.479  25.233  -2.660  1.00 79.74  ? 244 GLN B CB   1 
ATOM   4275 C CG   . GLN B 1 244 ? 12.779  24.414  -2.661  1.00 82.86  ? 244 GLN B CG   1 
ATOM   4276 C CD   . GLN B 1 244 ? 13.567  24.480  -3.980  1.00 86.60  ? 244 GLN B CD   1 
ATOM   4277 O OE1  . GLN B 1 244 ? 14.071  25.534  -4.378  1.00 84.01  ? 244 GLN B OE1  1 
ATOM   4278 N NE2  . GLN B 1 244 ? 13.623  23.353  -4.686  1.00 82.81  ? 244 GLN B NE2  1 
ATOM   4279 N N    . ASP B 1 245 ? 9.659   22.815  -3.960  1.00 78.50  ? 245 ASP B N    1 
ATOM   4280 C CA   . ASP B 1 245 ? 9.580   21.464  -4.490  1.00 79.53  ? 245 ASP B CA   1 
ATOM   4281 C C    . ASP B 1 245 ? 9.224   21.488  -5.968  1.00 78.21  ? 245 ASP B C    1 
ATOM   4282 O O    . ASP B 1 245 ? 9.684   20.634  -6.735  1.00 77.77  ? 245 ASP B O    1 
ATOM   4283 C CB   . ASP B 1 245 ? 8.549   20.660  -3.703  1.00 86.24  ? 245 ASP B CB   1 
ATOM   4284 C CG   . ASP B 1 245 ? 8.973   19.230  -3.503  1.00 92.63  ? 245 ASP B CG   1 
ATOM   4285 O OD1  . ASP B 1 245 ? 9.359   18.576  -4.501  1.00 93.45  ? 245 ASP B OD1  1 
ATOM   4286 O OD2  . ASP B 1 245 ? 8.950   18.776  -2.341  1.00 96.75  ? 245 ASP B OD2  1 
ATOM   4287 N N    . HIS B 1 246 ? 8.384   22.449  -6.375  1.00 76.81  ? 246 HIS B N    1 
ATOM   4288 C CA   . HIS B 1 246 ? 8.087   22.659  -7.790  1.00 74.15  ? 246 HIS B CA   1 
ATOM   4289 C C    . HIS B 1 246 ? 9.339   23.055  -8.576  1.00 73.14  ? 246 HIS B C    1 
ATOM   4290 O O    . HIS B 1 246 ? 9.601   22.509  -9.653  1.00 67.90  ? 246 HIS B O    1 
ATOM   4291 C CB   . HIS B 1 246 ? 7.009   23.732  -7.942  1.00 71.71  ? 246 HIS B CB   1 
ATOM   4292 C CG   . HIS B 1 246 ? 5.644   23.306  -7.493  1.00 72.15  ? 246 HIS B CG   1 
ATOM   4293 N ND1  . HIS B 1 246 ? 4.751   24.179  -6.907  1.00 74.43  ? 246 HIS B ND1  1 
ATOM   4294 C CD2  . HIS B 1 246 ? 5.011   22.109  -7.554  1.00 69.43  ? 246 HIS B CD2  1 
ATOM   4295 C CE1  . HIS B 1 246 ? 3.625   23.542  -6.636  1.00 70.07  ? 246 HIS B CE1  1 
ATOM   4296 N NE2  . HIS B 1 246 ? 3.755   22.286  -7.022  1.00 67.53  ? 246 HIS B NE2  1 
ATOM   4297 N N    . VAL B 1 247 ? 10.133  24.004  -8.050  1.00 73.41  ? 247 VAL B N    1 
ATOM   4298 C CA   . VAL B 1 247 ? 11.370  24.381  -8.734  1.00 69.41  ? 247 VAL B CA   1 
ATOM   4299 C C    . VAL B 1 247 ? 12.222  23.156  -9.017  1.00 70.91  ? 247 VAL B C    1 
ATOM   4300 O O    . VAL B 1 247 ? 12.719  22.969  -10.133 1.00 71.45  ? 247 VAL B O    1 
ATOM   4301 C CB   . VAL B 1 247 ? 12.144  25.426  -7.914  1.00 77.94  ? 247 VAL B CB   1 
ATOM   4302 C CG1  . VAL B 1 247 ? 13.411  25.832  -8.636  1.00 74.48  ? 247 VAL B CG1  1 
ATOM   4303 C CG2  . VAL B 1 247 ? 11.267  26.643  -7.683  1.00 79.19  ? 247 VAL B CG2  1 
ATOM   4304 N N    . ASP B 1 248 ? 12.357  22.276  -8.029  1.00 73.19  ? 248 ASP B N    1 
ATOM   4305 C CA   . ASP B 1 248 ? 13.236  21.119  -8.170  1.00 74.11  ? 248 ASP B CA   1 
ATOM   4306 C C    . ASP B 1 248 ? 12.681  20.081  -9.140  1.00 72.46  ? 248 ASP B C    1 
ATOM   4307 O O    . ASP B 1 248 ? 13.449  19.382  -9.812  1.00 71.11  ? 248 ASP B O    1 
ATOM   4308 C CB   . ASP B 1 248 ? 13.502  20.501  -6.800  1.00 79.56  ? 248 ASP B CB   1 
ATOM   4309 C CG   . ASP B 1 248 ? 14.934  20.740  -6.324  1.00 78.36  ? 248 ASP B CG   1 
ATOM   4310 O OD1  . ASP B 1 248 ? 15.748  21.281  -7.111  1.00 78.38  ? 248 ASP B OD1  1 
ATOM   4311 O OD2  . ASP B 1 248 ? 15.247  20.402  -5.163  1.00 80.07  ? 248 ASP B OD2  1 
ATOM   4312 N N    . ILE B 1 249 ? 11.360  19.946  -9.222  1.00 70.62  ? 249 ILE B N    1 
ATOM   4313 C CA   . ILE B 1 249 ? 10.793  19.014  -10.188 1.00 75.52  ? 249 ILE B CA   1 
ATOM   4314 C C    . ILE B 1 249 ? 10.996  19.540  -11.610 1.00 73.01  ? 249 ILE B C    1 
ATOM   4315 O O    . ILE B 1 249 ? 11.355  18.783  -12.525 1.00 66.64  ? 249 ILE B O    1 
ATOM   4316 C CB   . ILE B 1 249 ? 9.308   18.788  -9.853  1.00 73.74  ? 249 ILE B CB   1 
ATOM   4317 C CG1  . ILE B 1 249 ? 8.699   17.677  -10.688 1.00 74.45  ? 249 ILE B CG1  1 
ATOM   4318 C CG2  . ILE B 1 249 ? 8.504   20.017  -10.188 1.00 72.45  ? 249 ILE B CG2  1 
ATOM   4319 C CD1  . ILE B 1 249 ? 7.680   16.873  -9.869  1.00 79.30  ? 249 ILE B CD1  1 
ATOM   4320 N N    . LEU B 1 250 ? 10.799  20.848  -11.808 1.00 70.15  ? 250 LEU B N    1 
ATOM   4321 C CA   . LEU B 1 250 ? 11.074  21.523  -13.073 1.00 71.58  ? 250 LEU B CA   1 
ATOM   4322 C C    . LEU B 1 250 ? 12.564  21.480  -13.386 1.00 70.99  ? 250 LEU B C    1 
ATOM   4323 O O    . LEU B 1 250 ? 12.995  21.950  -14.441 1.00 71.47  ? 250 LEU B O    1 
ATOM   4324 C CB   . LEU B 1 250 ? 10.617  22.980  -13.037 1.00 66.75  ? 250 LEU B CB   1 
ATOM   4325 C CG   . LEU B 1 250 ? 9.132   23.281  -13.141 1.00 61.90  ? 250 LEU B CG   1 
ATOM   4326 C CD1  . LEU B 1 250 ? 8.887   24.703  -12.651 1.00 60.55  ? 250 LEU B CD1  1 
ATOM   4327 C CD2  . LEU B 1 250 ? 8.571   23.056  -14.535 1.00 57.40  ? 250 LEU B CD2  1 
ATOM   4328 N N    . GLY B 1 251 ? 13.360  20.922  -12.484 1.00 69.24  ? 251 GLY B N    1 
ATOM   4329 C CA   . GLY B 1 251 ? 14.794  21.028  -12.592 1.00 71.96  ? 251 GLY B CA   1 
ATOM   4330 C C    . GLY B 1 251 ? 15.452  20.519  -13.860 1.00 68.58  ? 251 GLY B C    1 
ATOM   4331 O O    . GLY B 1 251 ? 16.311  21.201  -14.430 1.00 69.72  ? 251 GLY B O    1 
ATOM   4332 N N    . PRO B 1 252 ? 15.121  19.307  -14.311 1.00 70.00  ? 252 PRO B N    1 
ATOM   4333 C CA   . PRO B 1 252 ? 15.779  18.802  -15.532 1.00 70.29  ? 252 PRO B CA   1 
ATOM   4334 C C    . PRO B 1 252 ? 15.330  19.525  -16.802 1.00 68.60  ? 252 PRO B C    1 
ATOM   4335 O O    . PRO B 1 252 ? 16.097  19.576  -17.772 1.00 68.97  ? 252 PRO B O    1 
ATOM   4336 C CB   . PRO B 1 252 ? 15.427  17.304  -15.559 1.00 70.13  ? 252 PRO B CB   1 
ATOM   4337 C CG   . PRO B 1 252 ? 14.625  17.023  -14.367 1.00 70.12  ? 252 PRO B CG   1 
ATOM   4338 C CD   . PRO B 1 252 ? 14.366  18.274  -13.588 1.00 70.80  ? 252 PRO B CD   1 
ATOM   4339 N N    . LEU B 1 253 ? 14.102  20.059  -16.839 1.00 70.39  ? 253 LEU B N    1 
ATOM   4340 C CA   . LEU B 1 253 ? 13.683  20.882  -17.973 1.00 65.96  ? 253 LEU B CA   1 
ATOM   4341 C C    . LEU B 1 253 ? 14.431  22.209  -17.976 1.00 69.00  ? 253 LEU B C    1 
ATOM   4342 O O    . LEU B 1 253 ? 14.984  22.624  -19.002 1.00 62.65  ? 253 LEU B O    1 
ATOM   4343 C CB   . LEU B 1 253 ? 12.175  21.143  -17.912 1.00 57.94  ? 253 LEU B CB   1 
ATOM   4344 C CG   . LEU B 1 253 ? 11.142  20.109  -18.366 1.00 55.18  ? 253 LEU B CG   1 
ATOM   4345 C CD1  . LEU B 1 253 ? 9.747   20.653  -18.201 1.00 53.39  ? 253 LEU B CD1  1 
ATOM   4346 C CD2  . LEU B 1 253 ? 11.380  19.685  -19.805 1.00 57.29  ? 253 LEU B CD2  1 
ATOM   4347 N N    . SER B 1 254 ? 14.431  22.900  -16.830 1.00 69.59  ? 254 SER B N    1 
ATOM   4348 C CA   . SER B 1 254 ? 15.272  24.076  -16.638 1.00 66.87  ? 254 SER B CA   1 
ATOM   4349 C C    . SER B 1 254 ? 16.719  23.779  -16.985 1.00 71.46  ? 254 SER B C    1 
ATOM   4350 O O    . SER B 1 254 ? 17.452  24.670  -17.432 1.00 74.72  ? 254 SER B O    1 
ATOM   4351 C CB   . SER B 1 254 ? 15.146  24.570  -15.187 1.00 68.70  ? 254 SER B CB   1 
ATOM   4352 O OG   . SER B 1 254 ? 16.170  25.470  -14.836 1.00 71.85  ? 254 SER B OG   1 
ATOM   4353 N N    . ALA B 1 255 ? 17.152  22.536  -16.788 1.00 69.34  ? 255 ALA B N    1 
ATOM   4354 C CA   . ALA B 1 255 ? 18.539  22.192  -17.061 1.00 71.63  ? 255 ALA B CA   1 
ATOM   4355 C C    . ALA B 1 255 ? 18.767  21.910  -18.535 1.00 70.16  ? 255 ALA B C    1 
ATOM   4356 O O    . ALA B 1 255 ? 19.741  22.392  -19.122 1.00 72.65  ? 255 ALA B O    1 
ATOM   4357 C CB   . ALA B 1 255 ? 18.957  20.987  -16.229 1.00 73.29  ? 255 ALA B CB   1 
ATOM   4358 N N    . GLN B 1 256 ? 17.894  21.104  -19.141 1.00 68.95  ? 256 GLN B N    1 
ATOM   4359 C CA   . GLN B 1 256 ? 18.017  20.799  -20.569 1.00 70.90  ? 256 GLN B CA   1 
ATOM   4360 C C    . GLN B 1 256 ? 18.083  22.079  -21.394 1.00 69.09  ? 256 GLN B C    1 
ATOM   4361 O O    . GLN B 1 256 ? 18.940  22.232  -22.270 1.00 71.29  ? 256 GLN B O    1 
ATOM   4362 C CB   . GLN B 1 256 ? 16.831  19.976  -21.054 1.00 72.20  ? 256 GLN B CB   1 
ATOM   4363 C CG   . GLN B 1 256 ? 17.175  18.975  -22.136 1.00 77.20  ? 256 GLN B CG   1 
ATOM   4364 C CD   . GLN B 1 256 ? 15.939  18.406  -22.785 1.00 82.12  ? 256 GLN B CD   1 
ATOM   4365 O OE1  . GLN B 1 256 ? 14.948  18.136  -22.093 1.00 78.80  ? 256 GLN B OE1  1 
ATOM   4366 N NE2  . GLN B 1 256 ? 16.098  17.942  -24.028 1.00 84.65  ? 256 GLN B NE2  1 
ATOM   4367 N N    . THR B 1 257 ? 17.182  23.026  -21.102 1.00 66.79  ? 257 THR B N    1 
ATOM   4368 C CA   . THR B 1 257 ? 17.056  24.273  -21.848 1.00 70.00  ? 257 THR B CA   1 
ATOM   4369 C C    . THR B 1 257 ? 18.033  25.362  -21.422 1.00 67.98  ? 257 THR B C    1 
ATOM   4370 O O    . THR B 1 257 ? 17.992  26.446  -22.003 1.00 68.25  ? 257 THR B O    1 
ATOM   4371 C CB   . THR B 1 257 ? 15.643  24.843  -21.702 1.00 68.53  ? 257 THR B CB   1 
ATOM   4372 O OG1  . THR B 1 257 ? 15.354  25.069  -20.314 1.00 63.73  ? 257 THR B OG1  1 
ATOM   4373 C CG2  . THR B 1 257 ? 14.597  23.901  -22.308 1.00 62.68  ? 257 THR B CG2  1 
ATOM   4374 N N    . GLY B 1 258 ? 18.890  25.128  -20.436 1.00 70.61  ? 258 GLY B N    1 
ATOM   4375 C CA   . GLY B 1 258 ? 19.789  26.177  -19.993 1.00 73.91  ? 258 GLY B CA   1 
ATOM   4376 C C    . GLY B 1 258 ? 19.120  27.434  -19.483 1.00 74.25  ? 258 GLY B C    1 
ATOM   4377 O O    . GLY B 1 258 ? 19.758  28.489  -19.442 1.00 76.72  ? 258 GLY B O    1 
ATOM   4378 N N    . ILE B 1 259 ? 17.866  27.353  -19.044 1.00 72.24  ? 259 ILE B N    1 
ATOM   4379 C CA   . ILE B 1 259 ? 17.112  28.524  -18.598 1.00 75.04  ? 259 ILE B CA   1 
ATOM   4380 C C    . ILE B 1 259 ? 16.683  28.336  -17.143 1.00 72.78  ? 259 ILE B C    1 
ATOM   4381 O O    . ILE B 1 259 ? 15.884  27.442  -16.842 1.00 70.65  ? 259 ILE B O    1 
ATOM   4382 C CB   . ILE B 1 259 ? 15.883  28.761  -19.480 1.00 69.05  ? 259 ILE B CB   1 
ATOM   4383 C CG1  . ILE B 1 259 ? 16.299  29.207  -20.870 1.00 68.87  ? 259 ILE B CG1  1 
ATOM   4384 C CG2  . ILE B 1 259 ? 14.983  29.804  -18.842 1.00 70.43  ? 259 ILE B CG2  1 
ATOM   4385 C CD1  . ILE B 1 259 ? 15.124  29.200  -21.835 1.00 65.65  ? 259 ILE B CD1  1 
ATOM   4386 N N    . ALA B 1 260 ? 17.158  29.209  -16.254 1.00 75.67  ? 260 ALA B N    1 
ATOM   4387 C CA   . ALA B 1 260 ? 16.838  29.061  -14.834 1.00 76.53  ? 260 ALA B CA   1 
ATOM   4388 C C    . ALA B 1 260 ? 15.335  29.182  -14.585 1.00 75.28  ? 260 ALA B C    1 
ATOM   4389 O O    . ALA B 1 260 ? 14.656  30.055  -15.138 1.00 72.85  ? 260 ALA B O    1 
ATOM   4390 C CB   . ALA B 1 260 ? 17.581  30.103  -14.002 1.00 80.21  ? 260 ALA B CB   1 
ATOM   4391 N N    . VAL B 1 261 ? 14.816  28.284  -13.749 1.00 73.35  ? 261 VAL B N    1 
ATOM   4392 C CA   . VAL B 1 261 ? 13.423  28.304  -13.317 1.00 70.81  ? 261 VAL B CA   1 
ATOM   4393 C C    . VAL B 1 261 ? 13.021  29.733  -12.979 1.00 73.65  ? 261 VAL B C    1 
ATOM   4394 O O    . VAL B 1 261 ? 11.959  30.212  -13.400 1.00 72.30  ? 261 VAL B O    1 
ATOM   4395 C CB   . VAL B 1 261 ? 13.202  27.394  -12.098 1.00 71.00  ? 261 VAL B CB   1 
ATOM   4396 C CG1  . VAL B 1 261 ? 11.702  27.242  -11.820 1.00 71.97  ? 261 VAL B CG1  1 
ATOM   4397 C CG2  . VAL B 1 261 ? 13.876  26.054  -12.287 1.00 70.91  ? 261 VAL B CG2  1 
ATOM   4398 N N    . LEU B 1 262 ? 13.885  30.413  -12.220 1.00 75.16  ? 262 LEU B N    1 
ATOM   4399 C CA   . LEU B 1 262 ? 13.648  31.799  -11.824 1.00 78.62  ? 262 LEU B CA   1 
ATOM   4400 C C    . LEU B 1 262 ? 13.461  32.705  -13.040 1.00 76.65  ? 262 LEU B C    1 
ATOM   4401 O O    . LEU B 1 262 ? 12.514  33.501  -13.103 1.00 75.13  ? 262 LEU B O    1 
ATOM   4402 C CB   . LEU B 1 262 ? 14.828  32.284  -10.978 1.00 81.86  ? 262 LEU B CB   1 
ATOM   4403 C CG   . LEU B 1 262 ? 14.889  31.816  -9.525  1.00 86.61  ? 262 LEU B CG   1 
ATOM   4404 C CD1  . LEU B 1 262 ? 13.727  32.382  -8.740  1.00 87.23  ? 262 LEU B CD1  1 
ATOM   4405 C CD2  . LEU B 1 262 ? 14.895  30.285  -9.475  1.00 80.48  ? 262 LEU B CD2  1 
ATOM   4406 N N    . ASP B 1 263 ? 14.359  32.598  -14.018 1.00 76.49  ? 263 ASP B N    1 
ATOM   4407 C CA   . ASP B 1 263 ? 14.252  33.437  -15.206 1.00 77.81  ? 263 ASP B CA   1 
ATOM   4408 C C    . ASP B 1 263 ? 12.946  33.169  -15.942 1.00 74.27  ? 263 ASP B C    1 
ATOM   4409 O O    . ASP B 1 263 ? 12.234  34.100  -16.335 1.00 71.85  ? 263 ASP B O    1 
ATOM   4410 C CB   . ASP B 1 263 ? 15.451  33.198  -16.116 1.00 77.03  ? 263 ASP B CB   1 
ATOM   4411 C CG   . ASP B 1 263 ? 16.718  33.755  -15.532 1.00 80.99  ? 263 ASP B CG   1 
ATOM   4412 O OD1  . ASP B 1 263 ? 16.625  34.440  -14.488 1.00 82.93  ? 263 ASP B OD1  1 
ATOM   4413 O OD2  . ASP B 1 263 ? 17.795  33.508  -16.113 1.00 82.53  ? 263 ASP B OD2  1 
ATOM   4414 N N    . MET B 1 264 ? 12.602  31.893  -16.121 1.00 73.09  ? 264 MET B N    1 
ATOM   4415 C CA   . MET B 1 264 ? 11.348  31.577  -16.792 1.00 67.85  ? 264 MET B CA   1 
ATOM   4416 C C    . MET B 1 264 ? 10.153  32.146  -16.046 1.00 68.00  ? 264 MET B C    1 
ATOM   4417 O O    . MET B 1 264 ? 9.188   32.603  -16.668 1.00 67.33  ? 264 MET B O    1 
ATOM   4418 C CB   . MET B 1 264 ? 11.200  30.070  -16.990 1.00 65.97  ? 264 MET B CB   1 
ATOM   4419 C CG   . MET B 1 264 ? 10.017  29.779  -17.877 1.00 65.26  ? 264 MET B CG   1 
ATOM   4420 S SD   . MET B 1 264 ? 10.490  29.933  -19.588 1.00 69.71  ? 264 MET B SD   1 
ATOM   4421 C CE   . MET B 1 264 ? 11.111  28.301  -20.055 1.00 62.89  ? 264 MET B CE   1 
ATOM   4422 N N    . CYS B 1 265 ? 10.191  32.127  -14.716 1.00 67.82  ? 265 CYS B N    1 
ATOM   4423 C CA   . CYS B 1 265 ? 9.119   32.761  -13.961 1.00 73.50  ? 265 CYS B CA   1 
ATOM   4424 C C    . CYS B 1 265 ? 8.928   34.216  -14.380 1.00 74.67  ? 265 CYS B C    1 
ATOM   4425 O O    . CYS B 1 265 ? 7.788   34.687  -14.496 1.00 71.97  ? 265 CYS B O    1 
ATOM   4426 C CB   . CYS B 1 265 ? 9.415   32.659  -12.463 1.00 77.99  ? 265 CYS B CB   1 
ATOM   4427 S SG   . CYS B 1 265 ? 9.049   31.015  -11.843 1.00 73.79  ? 265 CYS B SG   1 
ATOM   4428 N N    . ALA B 1 266 ? 10.036  34.944  -14.608 1.00 75.78  ? 266 ALA B N    1 
ATOM   4429 C CA   . ALA B 1 266 ? 9.954   36.349  -15.011 1.00 72.30  ? 266 ALA B CA   1 
ATOM   4430 C C    . ALA B 1 266 ? 9.275   36.510  -16.379 1.00 74.29  ? 266 ALA B C    1 
ATOM   4431 O O    . ALA B 1 266 ? 8.371   37.343  -16.532 1.00 71.63  ? 266 ALA B O    1 
ATOM   4432 C CB   . ALA B 1 266 ? 11.349  36.975  -14.997 1.00 75.91  ? 266 ALA B CB   1 
ATOM   4433 N N    . SER B 1 267 ? 9.677   35.699  -17.381 1.00 70.14  ? 267 SER B N    1 
ATOM   4434 C CA   . SER B 1 267 ? 8.991   35.707  -18.677 1.00 73.02  ? 267 SER B CA   1 
ATOM   4435 C C    . SER B 1 267 ? 7.507   35.392  -18.513 1.00 70.81  ? 267 SER B C    1 
ATOM   4436 O O    . SER B 1 267 ? 6.664   35.920  -19.250 1.00 70.31  ? 267 SER B O    1 
ATOM   4437 C CB   . SER B 1 267 ? 9.658   34.722  -19.652 1.00 71.09  ? 267 SER B CB   1 
ATOM   4438 O OG   . SER B 1 267 ? 11.063  34.932  -19.687 1.00 72.97  ? 267 SER B OG   1 
ATOM   4439 N N    . LEU B 1 268 ? 7.174   34.475  -17.602 1.00 71.60  ? 268 LEU B N    1 
ATOM   4440 C CA   . LEU B 1 268 ? 5.768   34.201  -17.329 1.00 70.65  ? 268 LEU B CA   1 
ATOM   4441 C C    . LEU B 1 268 ? 5.084   35.424  -16.707 1.00 72.38  ? 268 LEU B C    1 
ATOM   4442 O O    . LEU B 1 268 ? 3.960   35.770  -17.085 1.00 73.95  ? 268 LEU B O    1 
ATOM   4443 C CB   . LEU B 1 268 ? 5.638   32.998  -16.401 1.00 66.10  ? 268 LEU B CB   1 
ATOM   4444 C CG   . LEU B 1 268 ? 4.212   32.581  -16.047 1.00 61.68  ? 268 LEU B CG   1 
ATOM   4445 C CD1  . LEU B 1 268 ? 3.294   32.466  -17.274 1.00 60.85  ? 268 LEU B CD1  1 
ATOM   4446 C CD2  . LEU B 1 268 ? 4.253   31.297  -15.388 1.00 60.27  ? 268 LEU B CD2  1 
ATOM   4447 N N    . LYS B 1 269 ? 5.765   36.124  -15.791 1.00 73.21  ? 269 LYS B N    1 
ATOM   4448 C CA   . LYS B 1 269 ? 5.195   37.350  -15.226 1.00 75.67  ? 269 LYS B CA   1 
ATOM   4449 C C    . LYS B 1 269 ? 4.713   38.285  -16.327 1.00 76.99  ? 269 LYS B C    1 
ATOM   4450 O O    . LYS B 1 269 ? 3.579   38.781  -16.301 1.00 77.85  ? 269 LYS B O    1 
ATOM   4451 C CB   . LYS B 1 269 ? 6.199   38.054  -14.320 1.00 69.40  ? 269 LYS B CB   1 
ATOM   4452 C CG   . LYS B 1 269 ? 5.578   39.136  -13.478 1.00 77.60  ? 269 LYS B CG   1 
ATOM   4453 C CD   . LYS B 1 269 ? 6.613   40.152  -13.005 1.00 78.80  ? 269 LYS B CD   1 
ATOM   4454 C CE   . LYS B 1 269 ? 7.436   39.626  -11.836 1.00 80.04  ? 269 LYS B CE   1 
ATOM   4455 N NZ   . LYS B 1 269 ? 8.195   40.740  -11.196 1.00 80.12  ? 269 LYS B NZ   1 
ATOM   4456 N N    . GLU B 1 270 ? 5.578   38.553  -17.301 1.00 74.09  ? 270 GLU B N    1 
ATOM   4457 C CA   . GLU B 1 270 ? 5.228   39.502  -18.343 1.00 73.71  ? 270 GLU B CA   1 
ATOM   4458 C C    . GLU B 1 270 ? 4.112   38.961  -19.226 1.00 77.59  ? 270 GLU B C    1 
ATOM   4459 O O    . GLU B 1 270 ? 3.221   39.710  -19.638 1.00 78.30  ? 270 GLU B O    1 
ATOM   4460 C CB   . GLU B 1 270 ? 6.475   39.813  -19.156 1.00 76.16  ? 270 GLU B CB   1 
ATOM   4461 C CG   . GLU B 1 270 ? 6.251   40.498  -20.472 1.00 81.76  ? 270 GLU B CG   1 
ATOM   4462 C CD   . GLU B 1 270 ? 7.549   41.064  -20.975 1.00 85.84  ? 270 GLU B CD   1 
ATOM   4463 O OE1  . GLU B 1 270 ? 8.435   41.273  -20.115 1.00 89.15  ? 270 GLU B OE1  1 
ATOM   4464 O OE2  . GLU B 1 270 ? 7.688   41.294  -22.198 1.00 86.75  ? 270 GLU B OE2  1 
ATOM   4465 N N    . LEU B 1 271 ? 4.138   37.663  -19.526 1.00 74.91  ? 271 LEU B N    1 
ATOM   4466 C CA   . LEU B 1 271 ? 3.034   37.073  -20.264 1.00 72.37  ? 271 LEU B CA   1 
ATOM   4467 C C    . LEU B 1 271 ? 1.721   37.298  -19.527 1.00 74.90  ? 271 LEU B C    1 
ATOM   4468 O O    . LEU B 1 271 ? 0.683   37.551  -20.151 1.00 75.33  ? 271 LEU B O    1 
ATOM   4469 C CB   . LEU B 1 271 ? 3.287   35.583  -20.479 1.00 70.50  ? 271 LEU B CB   1 
ATOM   4470 C CG   . LEU B 1 271 ? 4.245   35.143  -21.590 1.00 70.44  ? 271 LEU B CG   1 
ATOM   4471 C CD1  . LEU B 1 271 ? 4.338   33.623  -21.603 1.00 65.52  ? 271 LEU B CD1  1 
ATOM   4472 C CD2  . LEU B 1 271 ? 3.775   35.657  -22.925 1.00 70.33  ? 271 LEU B CD2  1 
ATOM   4473 N N    . LEU B 1 272 ? 1.755   37.235  -18.192 1.00 70.40  ? 272 LEU B N    1 
ATOM   4474 C CA   . LEU B 1 272 ? 0.544   37.417  -17.399 1.00 78.04  ? 272 LEU B CA   1 
ATOM   4475 C C    . LEU B 1 272 ? 0.153   38.891  -17.299 1.00 79.07  ? 272 LEU B C    1 
ATOM   4476 O O    . LEU B 1 272 ? -1.036  39.226  -17.376 1.00 78.14  ? 272 LEU B O    1 
ATOM   4477 C CB   . LEU B 1 272 ? 0.743   36.830  -15.993 1.00 84.72  ? 272 LEU B CB   1 
ATOM   4478 C CG   . LEU B 1 272 ? 0.915   35.313  -15.794 1.00 78.97  ? 272 LEU B CG   1 
ATOM   4479 C CD1  . LEU B 1 272 ? 2.196   35.014  -15.025 1.00 76.62  ? 272 LEU B CD1  1 
ATOM   4480 C CD2  . LEU B 1 272 ? -0.261  34.718  -15.059 1.00 74.47  ? 272 LEU B CD2  1 
ATOM   4481 N N    . GLN B 1 273 ? 1.136   39.779  -17.124 1.00 79.46  ? 273 GLN B N    1 
ATOM   4482 C CA   . GLN B 1 273 ? 0.856   41.208  -17.028 1.00 80.35  ? 273 GLN B CA   1 
ATOM   4483 C C    . GLN B 1 273 ? 0.550   41.814  -18.386 1.00 81.62  ? 273 GLN B C    1 
ATOM   4484 O O    . GLN B 1 273 ? -0.150  42.826  -18.462 1.00 83.36  ? 273 GLN B O    1 
ATOM   4485 C CB   . GLN B 1 273 ? 2.038   41.933  -16.396 1.00 77.75  ? 273 GLN B CB   1 
ATOM   4486 C CG   . GLN B 1 273 ? 2.339   41.482  -14.984 1.00 79.97  ? 273 GLN B CG   1 
ATOM   4487 C CD   . GLN B 1 273 ? 3.347   42.380  -14.287 1.00 87.05  ? 273 GLN B CD   1 
ATOM   4488 O OE1  . GLN B 1 273 ? 4.261   41.897  -13.618 1.00 85.86  ? 273 GLN B OE1  1 
ATOM   4489 N NE2  . GLN B 1 273 ? 3.202   43.692  -14.463 1.00 89.41  ? 273 GLN B NE2  1 
ATOM   4490 N N    . ASN B 1 274 ? 1.045   41.207  -19.461 1.00 80.33  ? 274 ASN B N    1 
ATOM   4491 C CA   . ASN B 1 274 ? 1.040   41.832  -20.769 1.00 77.51  ? 274 ASN B CA   1 
ATOM   4492 C C    . ASN B 1 274 ? 0.267   41.045  -21.814 1.00 79.38  ? 274 ASN B C    1 
ATOM   4493 O O    . ASN B 1 274 ? 0.239   41.464  -22.975 1.00 77.89  ? 274 ASN B O    1 
ATOM   4494 C CB   . ASN B 1 274 ? 2.485   42.021  -21.250 1.00 79.16  ? 274 ASN B CB   1 
ATOM   4495 C CG   . ASN B 1 274 ? 3.244   43.022  -20.412 1.00 82.58  ? 274 ASN B CG   1 
ATOM   4496 O OD1  . ASN B 1 274 ? 4.333   42.737  -19.909 1.00 86.49  ? 274 ASN B OD1  1 
ATOM   4497 N ND2  . ASN B 1 274 ? 2.680   44.212  -20.268 1.00 83.99  ? 274 ASN B ND2  1 
ATOM   4498 N N    . GLY B 1 275 ? -0.352  39.921  -21.454 1.00 78.21  ? 275 GLY B N    1 
ATOM   4499 C CA   . GLY B 1 275 ? -0.995  39.196  -22.546 1.00 74.49  ? 275 GLY B CA   1 
ATOM   4500 C C    . GLY B 1 275 ? 0.048   38.714  -23.546 1.00 73.89  ? 275 GLY B C    1 
ATOM   4501 O O    . GLY B 1 275 ? 1.246   38.769  -23.319 1.00 73.52  ? 275 GLY B O    1 
ATOM   4502 N N    . MET B 1 276 ? -0.455  38.247  -24.686 1.00 69.36  ? 276 MET B N    1 
ATOM   4503 C CA   . MET B 1 276 ? 0.353   37.595  -25.710 1.00 75.72  ? 276 MET B CA   1 
ATOM   4504 C C    . MET B 1 276 ? 0.428   38.405  -26.996 1.00 81.28  ? 276 MET B C    1 
ATOM   4505 O O    . MET B 1 276 ? 0.978   37.920  -27.994 1.00 80.00  ? 276 MET B O    1 
ATOM   4506 C CB   . MET B 1 276 ? -0.162  36.201  -26.055 1.00 70.60  ? 276 MET B CB   1 
ATOM   4507 C CG   . MET B 1 276 ? 0.313   35.107  -25.158 1.00 66.90  ? 276 MET B CG   1 
ATOM   4508 S SD   . MET B 1 276 ? -0.180  33.522  -25.858 1.00 69.64  ? 276 MET B SD   1 
ATOM   4509 C CE   . MET B 1 276 ? -0.074  32.521  -24.349 1.00 58.77  ? 276 MET B CE   1 
ATOM   4510 N N    . ASN B 1 277 ? -0.118  39.617  -27.008 1.00 83.50  ? 277 ASN B N    1 
ATOM   4511 C CA   . ASN B 1 277 ? 0.043   40.503  -28.148 1.00 84.00  ? 277 ASN B CA   1 
ATOM   4512 C C    . ASN B 1 277 ? -0.548  39.911  -29.422 1.00 83.70  ? 277 ASN B C    1 
ATOM   4513 O O    . ASN B 1 277 ? -0.109  40.256  -30.519 1.00 85.56  ? 277 ASN B O    1 
ATOM   4514 C CB   . ASN B 1 277 ? 1.521   40.809  -28.379 1.00 86.44  ? 277 ASN B CB   1 
ATOM   4515 C CG   . ASN B 1 277 ? 1.950   42.076  -27.731 1.00 95.54  ? 277 ASN B CG   1 
ATOM   4516 O OD1  . ASN B 1 277 ? 1.136   42.782  -27.137 1.00 97.58  ? 277 ASN B OD1  1 
ATOM   4517 N ND2  . ASN B 1 277 ? 3.235   42.400  -27.852 1.00 101.78 ? 277 ASN B ND2  1 
ATOM   4518 N N    . GLY B 1 278 ? -1.529  39.009  -29.305 1.00 81.18  ? 278 GLY B N    1 
ATOM   4519 C CA   . GLY B 1 278 ? -2.060  38.346  -30.487 1.00 77.26  ? 278 GLY B CA   1 
ATOM   4520 C C    . GLY B 1 278 ? -1.173  37.276  -31.086 1.00 75.42  ? 278 GLY B C    1 
ATOM   4521 O O    . GLY B 1 278 ? -1.425  36.828  -32.210 1.00 74.89  ? 278 GLY B O    1 
ATOM   4522 N N    . ARG B 1 279 ? -0.141  36.862  -30.366 1.00 74.94  ? 279 ARG B N    1 
ATOM   4523 C CA   . ARG B 1 279 ? 0.814   35.855  -30.792 1.00 74.77  ? 279 ARG B CA   1 
ATOM   4524 C C    . ARG B 1 279 ? 0.428   34.502  -30.189 1.00 72.50  ? 279 ARG B C    1 
ATOM   4525 O O    . ARG B 1 279 ? -0.567  34.381  -29.469 1.00 72.88  ? 279 ARG B O    1 
ATOM   4526 C CB   . ARG B 1 279 ? 2.210   36.293  -30.360 1.00 80.41  ? 279 ARG B CB   1 
ATOM   4527 C CG   . ARG B 1 279 ? 2.525   37.719  -30.789 1.00 83.83  ? 279 ARG B CG   1 
ATOM   4528 C CD   . ARG B 1 279 ? 3.874   38.135  -30.283 1.00 86.42  ? 279 ARG B CD   1 
ATOM   4529 N NE   . ARG B 1 279 ? 4.918   37.371  -30.958 1.00 92.36  ? 279 ARG B NE   1 
ATOM   4530 C CZ   . ARG B 1 279 ? 6.214   37.539  -30.736 1.00 90.58  ? 279 ARG B CZ   1 
ATOM   4531 N NH1  . ARG B 1 279 ? 6.649   38.426  -29.855 1.00 87.76  ? 279 ARG B NH1  1 
ATOM   4532 N NH2  . ARG B 1 279 ? 7.091   36.772  -31.384 1.00 85.38  ? 279 ARG B NH2  1 
ATOM   4533 N N    . THR B 1 280 ? 1.232   33.473  -30.459 1.00 68.76  ? 280 THR B N    1 
ATOM   4534 C CA   . THR B 1 280 ? 0.896   32.131  -29.997 1.00 63.21  ? 280 THR B CA   1 
ATOM   4535 C C    . THR B 1 280 ? 2.131   31.414  -29.461 1.00 61.45  ? 280 THR B C    1 
ATOM   4536 O O    . THR B 1 280 ? 3.264   31.735  -29.817 1.00 64.33  ? 280 THR B O    1 
ATOM   4537 C CB   . THR B 1 280 ? 0.253   31.279  -31.102 1.00 60.77  ? 280 THR B CB   1 
ATOM   4538 O OG1  . THR B 1 280 ? 1.186   31.099  -32.171 1.00 60.62  ? 280 THR B OG1  1 
ATOM   4539 C CG2  . THR B 1 280 ? -1.007  31.946  -31.604 1.00 58.46  ? 280 THR B CG2  1 
ATOM   4540 N N    . ILE B 1 281 ? 1.887   30.447  -28.576 1.00 58.04  ? 281 ILE B N    1 
ATOM   4541 C CA   . ILE B 1 281 ? 2.907   29.571  -28.008 1.00 54.24  ? 281 ILE B CA   1 
ATOM   4542 C C    . ILE B 1 281 ? 2.469   28.134  -28.259 1.00 54.36  ? 281 ILE B C    1 
ATOM   4543 O O    . ILE B 1 281 ? 1.382   27.725  -27.841 1.00 52.92  ? 281 ILE B O    1 
ATOM   4544 C CB   . ILE B 1 281 ? 3.081   29.839  -26.509 1.00 57.21  ? 281 ILE B CB   1 
ATOM   4545 C CG1  . ILE B 1 281 ? 3.149   31.339  -26.248 1.00 56.20  ? 281 ILE B CG1  1 
ATOM   4546 C CG2  . ILE B 1 281 ? 4.301   29.252  -25.990 1.00 53.74  ? 281 ILE B CG2  1 
ATOM   4547 C CD1  . ILE B 1 281 ? 3.783   31.727  -24.984 1.00 60.20  ? 281 ILE B CD1  1 
ATOM   4548 N N    . LEU B 1 282 ? 3.291   27.377  -28.973 1.00 51.80  ? 282 LEU B N    1 
ATOM   4549 C CA   . LEU B 1 282 ? 2.916   26.013  -29.330 1.00 48.27  ? 282 LEU B CA   1 
ATOM   4550 C C    . LEU B 1 282 ? 1.498   25.945  -29.891 1.00 52.26  ? 282 LEU B C    1 
ATOM   4551 O O    . LEU B 1 282 ? 0.723   25.045  -29.556 1.00 50.85  ? 282 LEU B O    1 
ATOM   4552 C CB   . LEU B 1 282 ? 3.065   25.074  -28.134 1.00 47.70  ? 282 LEU B CB   1 
ATOM   4553 C CG   . LEU B 1 282 ? 4.523   24.826  -27.734 1.00 54.51  ? 282 LEU B CG   1 
ATOM   4554 C CD1  . LEU B 1 282 ? 4.630   23.786  -26.624 1.00 51.44  ? 282 LEU B CD1  1 
ATOM   4555 C CD2  . LEU B 1 282 ? 5.321   24.362  -28.966 1.00 54.25  ? 282 LEU B CD2  1 
ATOM   4556 N N    . GLY B 1 283 ? 1.141   26.923  -30.725 1.00 49.52  ? 283 GLY B N    1 
ATOM   4557 C CA   . GLY B 1 283 ? -0.136  26.883  -31.409 1.00 47.50  ? 283 GLY B CA   1 
ATOM   4558 C C    . GLY B 1 283 ? -1.345  27.254  -30.573 1.00 56.00  ? 283 GLY B C    1 
ATOM   4559 O O    . GLY B 1 283 ? -2.468  26.881  -30.928 1.00 60.13  ? 283 GLY B O    1 
ATOM   4560 N N    . SER B 1 284 ? -1.167  27.990  -29.479 1.00 51.99  ? 284 SER B N    1 
ATOM   4561 C CA   . SER B 1 284 ? -2.297  28.423  -28.672 1.00 53.78  ? 284 SER B CA   1 
ATOM   4562 C C    . SER B 1 284 ? -2.130  29.887  -28.296 1.00 53.62  ? 284 SER B C    1 
ATOM   4563 O O    . SER B 1 284 ? -1.009  30.369  -28.139 1.00 56.68  ? 284 SER B O    1 
ATOM   4564 C CB   . SER B 1 284 ? -2.427  27.563  -27.406 1.00 55.35  ? 284 SER B CB   1 
ATOM   4565 O OG   . SER B 1 284 ? -3.051  28.266  -26.349 1.00 55.82  ? 284 SER B OG   1 
ATOM   4566 N N    . ALA B 1 285 ? -3.250  30.593  -28.145 1.00 53.55  ? 285 ALA B N    1 
ATOM   4567 C CA   . ALA B 1 285 ? -3.218  31.956  -27.627 1.00 55.64  ? 285 ALA B CA   1 
ATOM   4568 C C    . ALA B 1 285 ? -3.416  32.013  -26.119 1.00 57.07  ? 285 ALA B C    1 
ATOM   4569 O O    . ALA B 1 285 ? -3.609  33.107  -25.574 1.00 59.08  ? 285 ALA B O    1 
ATOM   4570 C CB   . ALA B 1 285 ? -4.265  32.831  -28.312 1.00 56.90  ? 285 ALA B CB   1 
ATOM   4571 N N    . LEU B 1 286 ? -3.355  30.869  -25.431 1.00 53.94  ? 286 LEU B N    1 
ATOM   4572 C CA   . LEU B 1 286 ? -3.494  30.819  -23.984 1.00 58.01  ? 286 LEU B CA   1 
ATOM   4573 C C    . LEU B 1 286 ? -2.293  30.101  -23.385 1.00 56.31  ? 286 LEU B C    1 
ATOM   4574 O O    . LEU B 1 286 ? -1.593  29.349  -24.073 1.00 55.73  ? 286 LEU B O    1 
ATOM   4575 C CB   . LEU B 1 286 ? -4.780  30.101  -23.585 1.00 58.26  ? 286 LEU B CB   1 
ATOM   4576 C CG   . LEU B 1 286 ? -6.028  30.747  -24.169 1.00 55.24  ? 286 LEU B CG   1 
ATOM   4577 C CD1  . LEU B 1 286 ? -7.150  29.753  -24.218 1.00 53.53  ? 286 LEU B CD1  1 
ATOM   4578 C CD2  . LEU B 1 286 ? -6.401  31.974  -23.340 1.00 51.98  ? 286 LEU B CD2  1 
ATOM   4579 N N    . LEU B 1 287 ? -2.065  30.334  -22.093 1.00 53.91  ? 287 LEU B N    1 
ATOM   4580 C CA   . LEU B 1 287 ? -1.082  29.564  -21.337 1.00 52.03  ? 287 LEU B CA   1 
ATOM   4581 C C    . LEU B 1 287 ? -1.667  28.192  -20.959 1.00 53.05  ? 287 LEU B C    1 
ATOM   4582 O O    . LEU B 1 287 ? -2.724  28.111  -20.330 1.00 52.94  ? 287 LEU B O    1 
ATOM   4583 C CB   . LEU B 1 287 ? -0.679  30.364  -20.118 1.00 51.14  ? 287 LEU B CB   1 
ATOM   4584 C CG   . LEU B 1 287 ? -0.123  31.734  -20.482 1.00 53.07  ? 287 LEU B CG   1 
ATOM   4585 C CD1  . LEU B 1 287 ? 0.128   32.581  -19.238 1.00 55.01  ? 287 LEU B CD1  1 
ATOM   4586 C CD2  . LEU B 1 287 ? 1.160   31.578  -21.263 1.00 54.76  ? 287 LEU B CD2  1 
ATOM   4587 N N    . GLU B 1 288 ? -0.999  27.114  -21.370 1.00 49.76  ? 288 GLU B N    1 
ATOM   4588 C CA   . GLU B 1 288 ? -1.495  25.753  -21.175 1.00 50.09  ? 288 GLU B CA   1 
ATOM   4589 C C    . GLU B 1 288 ? -0.973  25.163  -19.872 1.00 45.85  ? 288 GLU B C    1 
ATOM   4590 O O    . GLU B 1 288 ? 0.239   25.128  -19.651 1.00 47.10  ? 288 GLU B O    1 
ATOM   4591 C CB   . GLU B 1 288 ? -1.046  24.871  -22.331 1.00 52.02  ? 288 GLU B CB   1 
ATOM   4592 C CG   . GLU B 1 288 ? -1.725  25.208  -23.611 1.00 56.09  ? 288 GLU B CG   1 
ATOM   4593 C CD   . GLU B 1 288 ? -3.177  24.798  -23.590 1.00 61.73  ? 288 GLU B CD   1 
ATOM   4594 O OE1  . GLU B 1 288 ? -3.504  23.796  -22.890 1.00 61.27  ? 288 GLU B OE1  1 
ATOM   4595 O OE2  . GLU B 1 288 ? -3.974  25.494  -24.263 1.00 62.44  ? 288 GLU B OE2  1 
ATOM   4596 N N    . ASP B 1 289 ? -1.882  24.677  -19.018 1.00 46.05  ? 289 ASP B N    1 
ATOM   4597 C CA   . ASP B 1 289 ? -1.493  24.105  -17.728 1.00 47.26  ? 289 ASP B CA   1 
ATOM   4598 C C    . ASP B 1 289 ? -1.915  22.638  -17.594 1.00 45.30  ? 289 ASP B C    1 
ATOM   4599 O O    . ASP B 1 289 ? -2.031  22.134  -16.478 1.00 44.98  ? 289 ASP B O    1 
ATOM   4600 C CB   . ASP B 1 289 ? -2.054  24.940  -16.562 1.00 43.27  ? 289 ASP B CB   1 
ATOM   4601 C CG   . ASP B 1 289 ? -3.551  24.665  -16.274 1.00 42.89  ? 289 ASP B CG   1 
ATOM   4602 O OD1  . ASP B 1 289 ? -4.273  24.169  -17.147 1.00 42.45  ? 289 ASP B OD1  1 
ATOM   4603 O OD2  . ASP B 1 289 ? -4.017  24.979  -15.162 1.00 51.04  ? 289 ASP B OD2  1 
ATOM   4604 N N    . GLU B 1 290 ? -2.148  21.928  -18.696 1.00 39.32  ? 290 GLU B N    1 
ATOM   4605 C CA   . GLU B 1 290 ? -2.505  20.515  -18.615 1.00 43.30  ? 290 GLU B CA   1 
ATOM   4606 C C    . GLU B 1 290 ? -1.379  19.585  -19.085 1.00 42.27  ? 290 GLU B C    1 
ATOM   4607 O O    . GLU B 1 290 ? -1.647  18.483  -19.545 1.00 40.82  ? 290 GLU B O    1 
ATOM   4608 C CB   . GLU B 1 290 ? -3.816  20.250  -19.365 1.00 41.08  ? 290 GLU B CB   1 
ATOM   4609 C CG   . GLU B 1 290 ? -4.999  21.042  -18.779 1.00 44.25  ? 290 GLU B CG   1 
ATOM   4610 C CD   . GLU B 1 290 ? -6.309  20.246  -18.581 1.00 46.67  ? 290 GLU B CD   1 
ATOM   4611 O OE1  . GLU B 1 290 ? -6.675  19.386  -19.421 1.00 46.11  ? 290 GLU B OE1  1 
ATOM   4612 O OE2  . GLU B 1 290 ? -7.014  20.533  -17.591 1.00 44.32  ? 290 GLU B OE2  1 
ATOM   4613 N N    . PHE B 1 291 ? -0.116  20.009  -18.960 1.00 41.31  ? 291 PHE B N    1 
ATOM   4614 C CA   . PHE B 1 291 ? 1.049   19.151  -19.173 1.00 44.93  ? 291 PHE B CA   1 
ATOM   4615 C C    . PHE B 1 291 ? 1.913   19.160  -17.924 1.00 44.52  ? 291 PHE B C    1 
ATOM   4616 O O    . PHE B 1 291 ? 2.403   20.224  -17.521 1.00 43.81  ? 291 PHE B O    1 
ATOM   4617 C CB   . PHE B 1 291 ? 1.882   19.635  -20.372 1.00 44.67  ? 291 PHE B CB   1 
ATOM   4618 C CG   . PHE B 1 291 ? 1.184   19.530  -21.689 1.00 42.83  ? 291 PHE B CG   1 
ATOM   4619 C CD1  . PHE B 1 291 ? 1.085   18.314  -22.345 1.00 47.42  ? 291 PHE B CD1  1 
ATOM   4620 C CD2  . PHE B 1 291 ? 0.598   20.635  -22.254 1.00 42.89  ? 291 PHE B CD2  1 
ATOM   4621 C CE1  . PHE B 1 291 ? 0.432   18.211  -23.552 1.00 45.51  ? 291 PHE B CE1  1 
ATOM   4622 C CE2  . PHE B 1 291 ? -0.036  20.547  -23.472 1.00 51.50  ? 291 PHE B CE2  1 
ATOM   4623 C CZ   . PHE B 1 291 ? -0.127  19.329  -24.120 1.00 49.00  ? 291 PHE B CZ   1 
ATOM   4624 N N    . THR B 1 292 ? 2.134   17.981  -17.324 1.00 44.17  ? 292 THR B N    1 
ATOM   4625 C CA   . THR B 1 292 ? 3.062   17.911  -16.201 1.00 48.89  ? 292 THR B CA   1 
ATOM   4626 C C    . THR B 1 292 ? 4.500   18.007  -16.711 1.00 46.51  ? 292 THR B C    1 
ATOM   4627 O O    . THR B 1 292 ? 4.753   17.814  -17.899 1.00 45.93  ? 292 THR B O    1 
ATOM   4628 C CB   . THR B 1 292 ? 2.920   16.613  -15.411 1.00 49.18  ? 292 THR B CB   1 
ATOM   4629 O OG1  . THR B 1 292 ? 3.211   15.513  -16.273 1.00 52.50  ? 292 THR B OG1  1 
ATOM   4630 C CG2  . THR B 1 292 ? 1.498   16.453  -14.841 1.00 46.63  ? 292 THR B CG2  1 
ATOM   4631 N N    . PRO B 1 293 ? 5.458   18.309  -15.837 1.00 48.61  ? 293 PRO B N    1 
ATOM   4632 C CA   . PRO B 1 293 ? 6.861   18.168  -16.246 1.00 50.08  ? 293 PRO B CA   1 
ATOM   4633 C C    . PRO B 1 293 ? 7.158   16.804  -16.849 1.00 54.96  ? 293 PRO B C    1 
ATOM   4634 O O    . PRO B 1 293 ? 7.883   16.714  -17.848 1.00 49.74  ? 293 PRO B O    1 
ATOM   4635 C CB   . PRO B 1 293 ? 7.627   18.399  -14.939 1.00 52.69  ? 293 PRO B CB   1 
ATOM   4636 C CG   . PRO B 1 293 ? 6.755   19.301  -14.167 1.00 52.58  ? 293 PRO B CG   1 
ATOM   4637 C CD   . PRO B 1 293 ? 5.337   18.826  -14.469 1.00 50.07  ? 293 PRO B CD   1 
ATOM   4638 N N    . PHE B 1 294 ? 6.574   15.738  -16.295 1.00 52.72  ? 294 PHE B N    1 
ATOM   4639 C CA   . PHE B 1 294 ? 6.847   14.395  -16.796 1.00 52.63  ? 294 PHE B CA   1 
ATOM   4640 C C    . PHE B 1 294 ? 6.244   14.196  -18.178 1.00 53.26  ? 294 PHE B C    1 
ATOM   4641 O O    . PHE B 1 294 ? 6.859   13.565  -19.044 1.00 54.79  ? 294 PHE B O    1 
ATOM   4642 C CB   . PHE B 1 294 ? 6.312   13.354  -15.799 1.00 61.40  ? 294 PHE B CB   1 
ATOM   4643 C CG   . PHE B 1 294 ? 6.531   11.909  -16.221 1.00 67.27  ? 294 PHE B CG   1 
ATOM   4644 C CD1  . PHE B 1 294 ? 5.585   11.248  -17.014 1.00 69.72  ? 294 PHE B CD1  1 
ATOM   4645 C CD2  . PHE B 1 294 ? 7.623   11.189  -15.769 1.00 74.09  ? 294 PHE B CD2  1 
ATOM   4646 C CE1  . PHE B 1 294 ? 5.768   9.924   -17.397 1.00 70.36  ? 294 PHE B CE1  1 
ATOM   4647 C CE2  . PHE B 1 294 ? 7.801   9.857   -16.141 1.00 72.48  ? 294 PHE B CE2  1 
ATOM   4648 C CZ   . PHE B 1 294 ? 6.875   9.230   -16.950 1.00 69.57  ? 294 PHE B CZ   1 
ATOM   4649 N N    . ASP B 1 295 ? 5.046   14.729  -18.417 1.00 51.27  ? 295 ASP B N    1 
ATOM   4650 C CA   . ASP B 1 295 ? 4.480   14.651  -19.758 1.00 51.12  ? 295 ASP B CA   1 
ATOM   4651 C C    . ASP B 1 295 ? 5.390   15.314  -20.783 1.00 53.08  ? 295 ASP B C    1 
ATOM   4652 O O    . ASP B 1 295 ? 5.545   14.803  -21.894 1.00 50.94  ? 295 ASP B O    1 
ATOM   4653 C CB   . ASP B 1 295 ? 3.115   15.302  -19.813 1.00 49.58  ? 295 ASP B CB   1 
ATOM   4654 C CG   . ASP B 1 295 ? 2.172   14.749  -18.781 1.00 53.30  ? 295 ASP B CG   1 
ATOM   4655 O OD1  . ASP B 1 295 ? 2.499   13.718  -18.149 1.00 57.21  ? 295 ASP B OD1  1 
ATOM   4656 O OD2  . ASP B 1 295 ? 1.099   15.357  -18.607 1.00 50.45  ? 295 ASP B OD2  1 
ATOM   4657 N N    . VAL B 1 296 ? 5.941   16.490  -20.462 1.00 53.83  ? 296 VAL B N    1 
ATOM   4658 C CA   . VAL B 1 296 ? 6.853   17.155  -21.395 1.00 52.52  ? 296 VAL B CA   1 
ATOM   4659 C C    . VAL B 1 296 ? 8.029   16.242  -21.722 1.00 54.40  ? 296 VAL B C    1 
ATOM   4660 O O    . VAL B 1 296 ? 8.347   16.011  -22.894 1.00 54.01  ? 296 VAL B O    1 
ATOM   4661 C CB   . VAL B 1 296 ? 7.325   18.517  -20.840 1.00 50.11  ? 296 VAL B CB   1 
ATOM   4662 C CG1  . VAL B 1 296 ? 8.457   19.075  -21.694 1.00 49.48  ? 296 VAL B CG1  1 
ATOM   4663 C CG2  . VAL B 1 296 ? 6.180   19.531  -20.810 1.00 49.07  ? 296 VAL B CG2  1 
ATOM   4664 N N    . VAL B 1 297 ? 8.669   15.682  -20.686 1.00 55.47  ? 297 VAL B N    1 
ATOM   4665 C CA   . VAL B 1 297 ? 9.845   14.838  -20.893 1.00 54.95  ? 297 VAL B CA   1 
ATOM   4666 C C    . VAL B 1 297 ? 9.477   13.580  -21.686 1.00 61.21  ? 297 VAL B C    1 
ATOM   4667 O O    . VAL B 1 297 ? 10.192  13.199  -22.625 1.00 64.52  ? 297 VAL B O    1 
ATOM   4668 C CB   . VAL B 1 297 ? 10.499  14.483  -19.549 1.00 56.77  ? 297 VAL B CB   1 
ATOM   4669 C CG1  . VAL B 1 297 ? 11.493  13.354  -19.741 1.00 56.38  ? 297 VAL B CG1  1 
ATOM   4670 C CG2  . VAL B 1 297 ? 11.222  15.701  -18.951 1.00 56.40  ? 297 VAL B CG2  1 
ATOM   4671 N N    . ARG B 1 298 ? 8.370   12.906  -21.317 1.00 58.85  ? 298 ARG B N    1 
ATOM   4672 C CA   . ARG B 1 298 ? 7.965   11.694  -22.034 1.00 60.40  ? 298 ARG B CA   1 
ATOM   4673 C C    . ARG B 1 298 ? 7.791   11.963  -23.506 1.00 59.10  ? 298 ARG B C    1 
ATOM   4674 O O    . ARG B 1 298 ? 8.274   11.203  -24.349 1.00 61.43  ? 298 ARG B O    1 
ATOM   4675 C CB   . ARG B 1 298 ? 6.660   11.105  -21.460 1.00 63.90  ? 298 ARG B CB   1 
ATOM   4676 C CG   . ARG B 1 298 ? 5.707   10.477  -22.486 1.00 71.12  ? 298 ARG B CG   1 
ATOM   4677 C CD   . ARG B 1 298 ? 4.674   9.494   -21.854 1.00 78.86  ? 298 ARG B CD   1 
ATOM   4678 N NE   . ARG B 1 298 ? 3.742   10.125  -20.927 1.00 76.05  ? 298 ARG B NE   1 
ATOM   4679 C CZ   . ARG B 1 298 ? 2.549   10.527  -21.332 1.00 69.87  ? 298 ARG B CZ   1 
ATOM   4680 N NH1  . ARG B 1 298 ? 2.191   10.375  -22.604 1.00 70.77  ? 298 ARG B NH1  1 
ATOM   4681 N NH2  . ARG B 1 298 ? 1.728   11.152  -20.470 1.00 59.90  ? 298 ARG B NH2  1 
ATOM   4682 N N    . GLN B 1 299 ? 7.085   13.036  -23.826 1.00 57.82  ? 299 GLN B N    1 
ATOM   4683 C CA   . GLN B 1 299 ? 6.859   13.390  -25.211 1.00 59.53  ? 299 GLN B CA   1 
ATOM   4684 C C    . GLN B 1 299 ? 8.138   13.868  -25.882 1.00 60.29  ? 299 GLN B C    1 
ATOM   4685 O O    . GLN B 1 299 ? 8.425   13.476  -27.016 1.00 62.61  ? 299 GLN B O    1 
ATOM   4686 C CB   . GLN B 1 299 ? 5.788   14.475  -25.295 1.00 53.79  ? 299 GLN B CB   1 
ATOM   4687 C CG   . GLN B 1 299 ? 5.341   14.701  -26.718 1.00 52.45  ? 299 GLN B CG   1 
ATOM   4688 C CD   . GLN B 1 299 ? 4.061   15.483  -26.855 1.00 48.98  ? 299 GLN B CD   1 
ATOM   4689 O OE1  . GLN B 1 299 ? 3.815   16.065  -27.908 1.00 49.58  ? 299 GLN B OE1  1 
ATOM   4690 N NE2  . GLN B 1 299 ? 3.250   15.535  -25.794 1.00 46.64  ? 299 GLN B NE2  1 
ATOM   4691 N N    . CYS B 1 300 ? 8.919   14.707  -25.210 1.00 61.69  ? 300 CYS B N    1 
ATOM   4692 C CA   . CYS B 1 300 ? 10.109  15.282  -25.834 1.00 64.94  ? 300 CYS B CA   1 
ATOM   4693 C C    . CYS B 1 300 ? 11.312  14.350  -25.813 1.00 67.58  ? 300 CYS B C    1 
ATOM   4694 O O    . CYS B 1 300 ? 12.365  14.723  -26.342 1.00 70.01  ? 300 CYS B O    1 
ATOM   4695 C CB   . CYS B 1 300 ? 10.453  16.629  -25.187 1.00 58.49  ? 300 CYS B CB   1 
ATOM   4696 S SG   . CYS B 1 300 ? 9.210   17.896  -25.607 1.00 61.43  ? 300 CYS B SG   1 
ATOM   4697 N N    . SER B 1 301 ? 11.174  13.147  -25.235 1.00 76.84  ? 301 SER B N    1 
ATOM   4698 C CA   . SER B 1 301 ? 12.203  12.114  -25.296 1.00 72.82  ? 301 SER B CA   1 
ATOM   4699 C C    . SER B 1 301 ? 11.707  10.762  -25.815 1.00 75.47  ? 301 SER B C    1 
ATOM   4700 O O    . SER B 1 301 ? 12.502  9.817   -25.873 1.00 72.45  ? 301 SER B O    1 
ATOM   4701 C CB   . SER B 1 301 ? 12.829  11.933  -23.912 1.00 78.22  ? 301 SER B CB   1 
ATOM   4702 O OG   . SER B 1 301 ? 13.287  13.190  -23.441 1.00 82.97  ? 301 SER B OG   1 
ATOM   4703 N N    . GLY B 1 302 ? 10.428  10.640  -26.172 1.00 71.55  ? 302 GLY B N    1 
ATOM   4704 C CA   . GLY B 1 302 ? 9.922   9.492   -26.913 1.00 68.49  ? 302 GLY B CA   1 
ATOM   4705 C C    . GLY B 1 302 ? 9.712   8.215   -26.128 1.00 71.16  ? 302 GLY B C    1 
ATOM   4706 O O    . GLY B 1 302 ? 10.013  7.125   -26.631 1.00 70.85  ? 302 GLY B O    1 
ATOM   4707 N N    . VAL B 1 303 ? 9.198   8.310   -24.904 1.00 73.26  ? 303 VAL B N    1 
ATOM   4708 C CA   . VAL B 1 303 ? 9.033   7.121   -24.074 1.00 84.04  ? 303 VAL B CA   1 
ATOM   4709 C C    . VAL B 1 303 ? 7.980   6.208   -24.701 1.00 84.05  ? 303 VAL B C    1 
ATOM   4710 O O    . VAL B 1 303 ? 6.971   6.679   -25.249 1.00 79.19  ? 303 VAL B O    1 
ATOM   4711 C CB   . VAL B 1 303 ? 8.662   7.538   -22.637 1.00 84.40  ? 303 VAL B CB   1 
ATOM   4712 C CG1  . VAL B 1 303 ? 8.162   6.357   -21.821 1.00 92.04  ? 303 VAL B CG1  1 
ATOM   4713 C CG2  . VAL B 1 303 ? 9.854   8.202   -21.949 1.00 82.26  ? 303 VAL B CG2  1 
ATOM   4714 N N    . THR B 1 304 ? 8.206   4.889   -24.618 1.00 85.50  ? 304 THR B N    1 
ATOM   4715 C CA   . THR B 1 304 ? 7.317   3.876   -25.187 1.00 83.81  ? 304 THR B CA   1 
ATOM   4716 C C    . THR B 1 304 ? 6.761   2.972   -24.087 1.00 93.85  ? 304 THR B C    1 
ATOM   4717 O O    . THR B 1 304 ? 7.225   2.978   -22.943 1.00 97.72  ? 304 THR B O    1 
ATOM   4718 C CB   . THR B 1 304 ? 8.025   3.009   -26.251 1.00 76.94  ? 304 THR B CB   1 
ATOM   4719 O OG1  . THR B 1 304 ? 9.346   2.657   -25.812 1.00 80.87  ? 304 THR B OG1  1 
ATOM   4720 C CG2  . THR B 1 304 ? 8.118   3.756   -27.574 1.00 66.82  ? 304 THR B CG2  1 
ATOM   4721 N N    . PHE B 1 305 ? 5.766   2.168   -24.459 1.00 90.72  ? 305 PHE B N    1 
ATOM   4722 C CA   . PHE B 1 305 ? 5.121   1.253   -23.521 1.00 99.24  ? 305 PHE B CA   1 
ATOM   4723 C C    . PHE B 1 305 ? 4.794   -0.085  -24.185 1.00 96.73  ? 305 PHE B C    1 
ATOM   4724 O O    . PHE B 1 305 ? 5.064   -1.148  -23.623 1.00 104.61 ? 305 PHE B O    1 
ATOM   4725 C CB   . PHE B 1 305 ? 3.841   1.896   -22.941 1.00 96.65  ? 305 PHE B CB   1 
ATOM   4726 C CG   . PHE B 1 305 ? 4.003   3.355   -22.562 1.00 90.74  ? 305 PHE B CG   1 
ATOM   4727 C CD1  . PHE B 1 305 ? 4.645   3.719   -21.387 1.00 96.01  ? 305 PHE B CD1  1 
ATOM   4728 C CD2  . PHE B 1 305 ? 3.533   4.363   -23.397 1.00 84.67  ? 305 PHE B CD2  1 
ATOM   4729 C CE1  . PHE B 1 305 ? 4.806   5.059   -21.041 1.00 93.59  ? 305 PHE B CE1  1 
ATOM   4730 C CE2  . PHE B 1 305 ? 3.695   5.712   -23.059 1.00 82.92  ? 305 PHE B CE2  1 
ATOM   4731 C CZ   . PHE B 1 305 ? 4.335   6.055   -21.878 1.00 89.11  ? 305 PHE B CZ   1 
HETATM 4732 C C14  . V8X C 2 .   ? 15.549  15.723  -43.212 1.00 49.79  ? 401 V8X A C14  1 
HETATM 4733 C C10  . V8X C 2 .   ? 12.473  11.232  -45.337 1.00 48.13  ? 401 V8X A C10  1 
HETATM 4734 C C12  . V8X C 2 .   ? 13.599  14.257  -42.262 1.00 48.14  ? 401 V8X A C12  1 
HETATM 4735 C C13  . V8X C 2 .   ? 14.311  15.575  -42.565 1.00 49.11  ? 401 V8X A C13  1 
HETATM 4736 C C15  . V8X C 2 .   ? 15.755  17.140  -43.318 1.00 52.63  ? 401 V8X A C15  1 
HETATM 4737 C C16  . V8X C 2 .   ? 16.787  17.969  -43.837 1.00 52.96  ? 401 V8X A C16  1 
HETATM 4738 C C17  . V8X C 2 .   ? 16.627  19.360  -43.760 1.00 56.39  ? 401 V8X A C17  1 
HETATM 4739 F F18  . V8X C 2 .   ? 17.592  20.167  -44.266 1.00 58.88  ? 401 V8X A F18  1 
HETATM 4740 C C02  . V8X C 2 .   ? 11.826  9.237   -39.297 1.00 52.67  ? 401 V8X A C02  1 
HETATM 4741 C C03  . V8X C 2 .   ? 11.860  10.798  -39.224 1.00 49.59  ? 401 V8X A C03  1 
HETATM 4742 C C05  . V8X C 2 .   ? 13.660  11.425  -41.152 1.00 52.34  ? 401 V8X A C05  1 
HETATM 4743 C C06  . V8X C 2 .   ? 13.641  11.802  -42.642 1.00 48.31  ? 401 V8X A C06  1 
HETATM 4744 C C07  . V8X C 2 .   ? 14.411  10.787  -43.526 1.00 49.86  ? 401 V8X A C07  1 
HETATM 4745 C C08  . V8X C 2 .   ? 13.561  10.305  -44.756 1.00 50.03  ? 401 V8X A C08  1 
HETATM 4746 C C09  . V8X C 2 .   ? 13.831  11.101  -46.030 1.00 49.16  ? 401 V8X A C09  1 
HETATM 4747 C C19  . V8X C 2 .   ? 15.490  19.953  -43.189 1.00 52.81  ? 401 V8X A C19  1 
HETATM 4748 C C20  . V8X C 2 .   ? 14.485  19.141  -42.672 1.00 53.31  ? 401 V8X A C20  1 
HETATM 4749 C C22  . V8X C 2 .   ? 14.641  17.726  -42.744 1.00 52.06  ? 401 V8X A C22  1 
HETATM 4750 C C26  . V8X C 2 .   ? 12.781  11.572  -38.324 1.00 56.50  ? 401 V8X A C26  1 
HETATM 4751 C C27  . V8X C 2 .   ? 12.191  12.851  -37.634 1.00 51.14  ? 401 V8X A C27  1 
HETATM 4752 C C28  . V8X C 2 .   ? 13.220  13.539  -36.979 1.00 54.96  ? 401 V8X A C28  1 
HETATM 4753 C C29  . V8X C 2 .   ? 12.950  14.692  -36.263 1.00 52.26  ? 401 V8X A C29  1 
HETATM 4754 C C30  . V8X C 2 .   ? 11.649  15.146  -36.197 1.00 49.73  ? 401 V8X A C30  1 
HETATM 4755 C C32  . V8X C 2 .   ? 10.859  13.393  -37.524 1.00 50.92  ? 401 V8X A C32  1 
HETATM 4756 F F21  . V8X C 2 .   ? 13.332  19.649  -42.103 1.00 54.51  ? 401 V8X A F21  1 
HETATM 4757 N N01  . V8X C 2 .   ? 12.079  8.572   -38.254 1.00 48.67  ? 401 V8X A N01  1 
HETATM 4758 N N04  . V8X C 2 .   ? 12.280  11.232  -40.582 1.00 49.12  ? 401 V8X A N04  1 
HETATM 4759 N N11  . V8X C 2 .   ? 14.243  13.092  -42.838 1.00 50.79  ? 401 V8X A N11  1 
HETATM 4760 N N23  . V8X C 2 .   ? 13.792  16.754  -42.307 1.00 46.76  ? 401 V8X A N23  1 
HETATM 4761 N N31  . V8X C 2 .   ? 10.666  14.509  -36.812 1.00 50.29  ? 401 V8X A N31  1 
HETATM 4762 O O24  . V8X C 2 .   ? 12.539  14.194  -41.700 1.00 47.04  ? 401 V8X A O24  1 
HETATM 4763 O O25  . V8X C 2 .   ? 14.717  11.330  -40.566 1.00 54.46  ? 401 V8X A O25  1 
HETATM 4764 O O33  . V8X C 2 .   ? 9.851   12.967  -38.003 1.00 51.13  ? 401 V8X A O33  1 
HETATM 4765 H H141 . V8X C 2 .   ? 16.211  14.933  -43.559 1.00 59.82  ? 401 V8X A H141 1 
HETATM 4766 H H102 . V8X C 2 .   ? 11.642  10.732  -45.831 1.00 57.83  ? 401 V8X A H102 1 
HETATM 4767 H H101 . V8X C 2 .   ? 12.308  12.162  -44.796 1.00 57.83  ? 401 V8X A H101 1 
HETATM 4768 H H161 . V8X C 2 .   ? 17.680  17.535  -44.282 1.00 63.62  ? 401 V8X A H161 1 
HETATM 4769 H H031 . V8X C 2 .   ? 10.873  11.013  -38.817 1.00 59.59  ? 401 V8X A H031 1 
HETATM 4770 H H061 . V8X C 2 .   ? 12.593  11.804  -42.940 1.00 58.04  ? 401 V8X A H061 1 
HETATM 4771 H H072 . V8X C 2 .   ? 15.324  11.258  -43.891 1.00 59.90  ? 401 V8X A H072 1 
HETATM 4772 H H071 . V8X C 2 .   ? 14.678  9.922   -42.920 1.00 59.90  ? 401 V8X A H071 1 
HETATM 4773 H H081 . V8X C 2 .   ? 13.299  9.252   -44.851 1.00 60.12  ? 401 V8X A H081 1 
HETATM 4774 H H092 . V8X C 2 .   ? 14.498  11.954  -45.916 1.00 59.06  ? 401 V8X A H092 1 
HETATM 4775 H H091 . V8X C 2 .   ? 13.832  10.523  -46.953 1.00 59.06  ? 401 V8X A H091 1 
HETATM 4776 H H191 . V8X C 2 .   ? 15.396  21.037  -43.151 1.00 63.45  ? 401 V8X A H191 1 
HETATM 4777 H H262 . V8X C 2 .   ? 13.641  11.882  -38.918 1.00 67.87  ? 401 V8X A H262 1 
HETATM 4778 H H261 . V8X C 2 .   ? 13.120  10.897  -37.538 1.00 67.87  ? 401 V8X A H261 1 
HETATM 4779 H H281 . V8X C 2 .   ? 14.240  13.164  -37.033 1.00 66.03  ? 401 V8X A H281 1 
HETATM 4780 H H301 . V8X C 2 .   ? 11.426  16.045  -35.627 1.00 59.75  ? 401 V8X A H301 1 
HETATM 4781 H H011 . V8X C 2 .   ? 12.066  7.570   -38.278 1.00 58.48  ? 401 V8X A H011 1 
HETATM 4782 H H041 . V8X C 2 .   ? 11.526  11.427  -41.219 1.00 59.02  ? 401 V8X A H041 1 
HETATM 4783 H H111 . V8X C 2 .   ? 15.095  13.186  -43.365 1.00 61.03  ? 401 V8X A H111 1 
HETATM 4784 H H2   . V8X C 2 .   ? 13.751  15.231  -35.760 1.00 62.78  ? 401 V8X A H2   1 
HETATM 4785 C C14  . V8X D 2 .   ? -27.149 15.783  -12.299 1.00 56.51  ? 401 V8X B C14  1 
HETATM 4786 C C10  . V8X D 2 .   ? -24.089 11.200  -10.165 1.00 50.36  ? 401 V8X B C10  1 
HETATM 4787 C C12  . V8X D 2 .   ? -25.237 14.277  -13.304 1.00 51.13  ? 401 V8X B C12  1 
HETATM 4788 C C13  . V8X D 2 .   ? -25.946 15.609  -13.004 1.00 55.60  ? 401 V8X B C13  1 
HETATM 4789 C C15  . V8X D 2 .   ? -27.342 17.203  -12.215 1.00 61.66  ? 401 V8X B C15  1 
HETATM 4790 C C16  . V8X D 2 .   ? -28.349 18.050  -11.672 1.00 62.42  ? 401 V8X B C16  1 
HETATM 4791 C C17  . V8X D 2 .   ? -28.195 19.438  -11.773 1.00 63.99  ? 401 V8X B C17  1 
HETATM 4792 F F18  . V8X D 2 .   ? -29.143 20.254  -11.251 1.00 66.96  ? 401 V8X B F18  1 
HETATM 4793 C C02  . V8X D 2 .   ? -23.469 9.226   -16.288 1.00 51.58  ? 401 V8X B C02  1 
HETATM 4794 C C03  . V8X D 2 .   ? -23.494 10.792  -16.376 1.00 49.56  ? 401 V8X B C03  1 
HETATM 4795 C C05  . V8X D 2 .   ? -25.215 11.435  -14.392 1.00 53.92  ? 401 V8X B C05  1 
HETATM 4796 C C06  . V8X D 2 .   ? -25.234 11.817  -12.918 1.00 48.82  ? 401 V8X B C06  1 
HETATM 4797 C C07  . V8X D 2 .   ? -25.970 10.774  -12.056 1.00 48.77  ? 401 V8X B C07  1 
HETATM 4798 C C08  . V8X D 2 .   ? -25.174 10.298  -10.784 1.00 49.95  ? 401 V8X B C08  1 
HETATM 4799 C C09  . V8X D 2 .   ? -25.469 11.099  -9.514  1.00 49.84  ? 401 V8X B C09  1 
HETATM 4800 C C19  . V8X D 2 .   ? -27.076 20.019  -12.387 1.00 62.61  ? 401 V8X B C19  1 
HETATM 4801 C C20  . V8X D 2 .   ? -26.087 19.194  -12.923 1.00 60.99  ? 401 V8X B C20  1 
HETATM 4802 C C22  . V8X D 2 .   ? -26.244 17.776  -12.833 1.00 59.98  ? 401 V8X B C22  1 
HETATM 4803 C C26  . V8X D 2 .   ? -24.439 11.643  -17.185 1.00 55.96  ? 401 V8X B C26  1 
HETATM 4804 C C27  . V8X D 2 .   ? -23.828 12.895  -17.901 1.00 51.80  ? 401 V8X B C27  1 
HETATM 4805 C C28  . V8X D 2 .   ? -24.829 13.560  -18.612 1.00 56.29  ? 401 V8X B C28  1 
HETATM 4806 C C29  . V8X D 2 .   ? -24.530 14.682  -19.367 1.00 54.91  ? 401 V8X B C29  1 
HETATM 4807 C C30  . V8X D 2 .   ? -23.226 15.137  -19.414 1.00 53.20  ? 401 V8X B C30  1 
HETATM 4808 C C32  . V8X D 2 .   ? -22.489 13.437  -17.994 1.00 51.92  ? 401 V8X B C32  1 
HETATM 4809 F F21  . V8X D 2 .   ? -24.971 19.716  -13.535 1.00 58.26  ? 401 V8X B F21  1 
HETATM 4810 N N01  . V8X D 2 .   ? -23.634 8.591   -17.376 1.00 48.31  ? 401 V8X B N01  1 
HETATM 4811 N N04  . V8X D 2 .   ? -23.842 11.238  -14.999 1.00 49.88  ? 401 V8X B N04  1 
HETATM 4812 N N11  . V8X D 2 .   ? -25.869 13.093  -12.752 1.00 52.09  ? 401 V8X B N11  1 
HETATM 4813 N N23  . V8X D 2 .   ? -25.433 16.787  -13.289 1.00 52.80  ? 401 V8X B N23  1 
HETATM 4814 N N31  . V8X D 2 .   ? -22.263 14.520  -18.750 1.00 51.50  ? 401 V8X B N31  1 
HETATM 4815 O O24  . V8X D 2 .   ? -24.182 14.228  -13.867 1.00 47.76  ? 401 V8X B O24  1 
HETATM 4816 O O25  . V8X D 2 .   ? -26.276 11.341  -14.953 1.00 56.40  ? 401 V8X B O25  1 
HETATM 4817 O O33  . V8X D 2 .   ? -21.502 13.033  -17.464 1.00 48.68  ? 401 V8X B O33  1 
HETATM 4818 H H141 . V8X D 2 .   ? -27.797 15.006  -11.899 1.00 67.89  ? 401 V8X B H141 1 
HETATM 4819 H H102 . V8X D 2 .   ? -23.286 10.681  -9.646  1.00 60.51  ? 401 V8X B H102 1 
HETATM 4820 H H101 . V8X D 2 .   ? -23.888 12.126  -10.698 1.00 60.51  ? 401 V8X B H101 1 
HETATM 4821 H H161 . V8X D 2 .   ? -29.224 17.625  -11.185 1.00 74.98  ? 401 V8X B H161 1 
HETATM 4822 H H031 . V8X D 2 .   ? -22.539 10.944  -16.878 1.00 59.55  ? 401 V8X B H031 1 
HETATM 4823 H H061 . V8X D 2 .   ? -24.198 11.862  -12.584 1.00 58.66  ? 401 V8X B H061 1 
HETATM 4824 H H072 . V8X D 2 .   ? -26.914 11.207  -11.726 1.00 58.60  ? 401 V8X B H072 1 
HETATM 4825 H H071 . V8X D 2 .   ? -26.178 9.903   -12.676 1.00 58.60  ? 401 V8X B H071 1 
HETATM 4826 H H081 . V8X D 2 .   ? -24.936 9.241   -10.673 1.00 60.02  ? 401 V8X B H081 1 
HETATM 4827 H H092 . V8X D 2 .   ? -26.113 11.967  -9.646  1.00 59.88  ? 401 V8X B H092 1 
HETATM 4828 H H091 . V8X D 2 .   ? -25.511 10.520  -8.593  1.00 59.88  ? 401 V8X B H091 1 
HETATM 4829 H H191 . V8X D 2 .   ? -26.980 21.101  -12.445 1.00 75.21  ? 401 V8X B H191 1 
HETATM 4830 H H262 . V8X D 2 .   ? -25.224 11.994  -16.516 1.00 67.23  ? 401 V8X B H262 1 
HETATM 4831 H H261 . V8X D 2 .   ? -24.885 11.008  -17.951 1.00 67.23  ? 401 V8X B H261 1 
HETATM 4832 H H281 . V8X D 2 .   ? -25.853 13.194  -18.573 1.00 67.62  ? 401 V8X B H281 1 
HETATM 4833 H H301 . V8X D 2 .   ? -22.988 16.018  -20.007 1.00 63.92  ? 401 V8X B H301 1 
HETATM 4834 H H011 . V8X D 2 .   ? -23.632 7.590   -17.376 1.00 58.04  ? 401 V8X B H011 1 
HETATM 4835 H H041 . V8X D 2 .   ? -23.064 11.433  -14.393 1.00 59.93  ? 401 V8X B H041 1 
HETATM 4836 H H111 . V8X D 2 .   ? -26.743 13.166  -12.259 1.00 62.59  ? 401 V8X B H111 1 
HETATM 4837 H H2   . V8X D 2 .   ? -25.313 15.199  -19.917 1.00 65.97  ? 401 V8X B H2   1 
HETATM 4838 O O    . HOH E 3 .   ? -21.801 18.745  -49.550 1.00 77.34  ? 501 HOH A O    1 
HETATM 4839 O O    . HOH E 3 .   ? -22.201 22.544  -21.662 1.00 56.77  ? 502 HOH A O    1 
HETATM 4840 O O    . HOH E 3 .   ? -12.828 2.215   -41.330 1.00 67.67  ? 503 HOH A O    1 
HETATM 4841 O O    . HOH E 3 .   ? 10.553  22.270  -51.156 1.00 53.36  ? 504 HOH A O    1 
HETATM 4842 O O    . HOH E 3 .   ? 10.026  10.196  -52.781 1.00 41.81  ? 505 HOH A O    1 
HETATM 4843 O O    . HOH E 3 .   ? -2.995  18.896  -34.935 1.00 45.41  ? 506 HOH A O    1 
HETATM 4844 O O    . HOH E 3 .   ? -12.328 22.788  -36.442 1.00 38.81  ? 507 HOH A O    1 
HETATM 4845 O O    . HOH E 3 .   ? -13.951 12.876  -39.720 1.00 47.14  ? 508 HOH A O    1 
HETATM 4846 O O    . HOH E 3 .   ? -22.027 32.325  -24.639 1.00 62.67  ? 509 HOH A O    1 
HETATM 4847 O O    . HOH E 3 .   ? -19.690 16.115  -25.469 1.00 48.87  ? 510 HOH A O    1 
HETATM 4848 O O    . HOH E 3 .   ? -8.816  7.126   -42.646 1.00 40.06  ? 511 HOH A O    1 
HETATM 4849 O O    . HOH E 3 .   ? 3.934   20.596  -35.977 1.00 44.87  ? 512 HOH A O    1 
HETATM 4850 O O    . HOH E 3 .   ? -13.516 19.036  -43.692 1.00 41.87  ? 513 HOH A O    1 
HETATM 4851 O O    . HOH E 3 .   ? -3.625  4.470   -47.581 1.00 40.50  ? 514 HOH A O    1 
HETATM 4852 O O    . HOH E 3 .   ? 7.313   11.524  -53.585 1.00 35.90  ? 515 HOH A O    1 
HETATM 4853 O O    . HOH E 3 .   ? 2.684   14.765  -46.265 1.00 33.74  ? 516 HOH A O    1 
HETATM 4854 O O    . HOH E 3 .   ? 2.306   23.259  -42.712 1.00 44.03  ? 517 HOH A O    1 
HETATM 4855 O O    . HOH E 3 .   ? 2.138   21.850  -50.003 1.00 47.93  ? 518 HOH A O    1 
HETATM 4856 O O    . HOH E 3 .   ? 1.583   3.503   -35.605 1.00 38.75  ? 519 HOH A O    1 
HETATM 4857 O O    . HOH E 3 .   ? -2.426  18.754  -38.542 1.00 36.80  ? 520 HOH A O    1 
HETATM 4858 O O    . HOH E 3 .   ? -28.135 27.833  -43.995 1.00 66.54  ? 521 HOH A O    1 
HETATM 4859 O O    . HOH E 3 .   ? -24.326 16.319  -23.196 1.00 44.10  ? 522 HOH A O    1 
HETATM 4860 O O    . HOH E 3 .   ? 22.013  5.798   -53.768 1.00 54.11  ? 523 HOH A O    1 
HETATM 4861 O O    . HOH E 3 .   ? -11.852 12.406  -41.365 1.00 42.30  ? 524 HOH A O    1 
HETATM 4862 O O    . HOH E 3 .   ? 6.626   1.219   -57.073 1.00 50.52  ? 525 HOH A O    1 
HETATM 4863 O O    . HOH E 3 .   ? -12.536 20.720  -46.629 1.00 59.98  ? 526 HOH A O    1 
HETATM 4864 O O    . HOH E 3 .   ? -7.455  -10.282 -43.080 1.00 65.49  ? 527 HOH A O    1 
HETATM 4865 O O    . HOH E 3 .   ? 5.189   10.126  -53.618 1.00 38.60  ? 528 HOH A O    1 
HETATM 4866 O O    . HOH E 3 .   ? 9.225   3.455   -56.009 1.00 47.09  ? 529 HOH A O    1 
HETATM 4867 O O    . HOH E 3 .   ? -10.863 15.833  -34.979 1.00 53.41  ? 530 HOH A O    1 
HETATM 4868 O O    . HOH E 3 .   ? -0.961  15.218  -52.952 1.00 47.15  ? 531 HOH A O    1 
HETATM 4869 O O    . HOH E 3 .   ? 8.420   21.075  -52.050 1.00 48.23  ? 532 HOH A O    1 
HETATM 4870 O O    . HOH E 3 .   ? -5.797  28.533  -27.813 1.00 44.64  ? 533 HOH A O    1 
HETATM 4871 O O    . HOH E 3 .   ? 16.059  15.983  -58.354 1.00 63.19  ? 534 HOH A O    1 
HETATM 4872 O O    . HOH E 3 .   ? -4.920  38.784  -43.345 1.00 68.80  ? 535 HOH A O    1 
HETATM 4873 O O    . HOH E 3 .   ? -8.867  5.995   -51.207 1.00 47.52  ? 536 HOH A O    1 
HETATM 4874 O O    . HOH E 3 .   ? 9.159   18.986  -52.228 1.00 44.97  ? 537 HOH A O    1 
HETATM 4875 O O    . HOH E 3 .   ? -5.714  14.156  -29.335 1.00 46.47  ? 538 HOH A O    1 
HETATM 4876 O O    . HOH E 3 .   ? -9.451  -7.131  -43.613 1.00 55.49  ? 539 HOH A O    1 
HETATM 4877 O O    . HOH E 3 .   ? -13.940 8.894   -39.280 1.00 52.65  ? 540 HOH A O    1 
HETATM 4878 O O    . HOH E 3 .   ? 6.274   10.584  -27.955 1.00 57.70  ? 541 HOH A O    1 
HETATM 4879 O O    . HOH E 3 .   ? 16.152  -12.326 -51.627 1.00 59.09  ? 542 HOH A O    1 
HETATM 4880 O O    . HOH E 3 .   ? 15.295  -5.062  -56.005 1.00 53.15  ? 543 HOH A O    1 
HETATM 4881 O O    . HOH E 3 .   ? 14.294  -12.017 -53.347 1.00 61.06  ? 544 HOH A O    1 
HETATM 4882 O O    . HOH E 3 .   ? 23.302  4.025   -55.568 1.00 52.86  ? 545 HOH A O    1 
HETATM 4883 O O    . HOH E 3 .   ? -33.024 32.844  -36.762 1.00 80.41  ? 546 HOH A O    1 
HETATM 4884 O O    . HOH E 3 .   ? 12.036  -1.895  -57.717 1.00 60.02  ? 547 HOH A O    1 
HETATM 4885 O O    . HOH E 3 .   ? 16.313  18.589  -59.570 1.00 63.31  ? 548 HOH A O    1 
HETATM 4886 O O    . HOH F 3 .   ? 10.646  22.443  -33.846 1.00 56.66  ? 501 HOH B O    1 
HETATM 4887 O O    . HOH F 3 .   ? -21.785 10.070  -2.775  1.00 43.45  ? 502 HOH B O    1 
HETATM 4888 O O    . HOH F 3 .   ? -22.024 22.369  -4.416  1.00 59.16  ? 503 HOH B O    1 
HETATM 4889 O O    . HOH F 3 .   ? -8.587  18.901  -20.710 1.00 45.98  ? 504 HOH B O    1 
HETATM 4890 O O    . HOH F 3 .   ? -2.730  7.243   -12.897 1.00 47.35  ? 505 HOH B O    1 
HETATM 4891 O O    . HOH F 3 .   ? 0.720   22.699  -19.092 1.00 44.55  ? 506 HOH B O    1 
HETATM 4892 O O    . HOH F 3 .   ? 2.408   12.823  -15.723 1.00 54.26  ? 507 HOH B O    1 
HETATM 4893 O O    . HOH F 3 .   ? -0.722  15.802  -20.413 1.00 51.86  ? 508 HOH B O    1 
HETATM 4894 O O    . HOH F 3 .   ? 10.431  32.323  -30.983 1.00 64.38  ? 509 HOH B O    1 
HETATM 4895 O O    . HOH F 3 .   ? -13.228 3.540   -19.987 1.00 36.30  ? 510 HOH B O    1 
HETATM 4896 O O    . HOH F 3 .   ? 1.946   19.023  -11.856 1.00 48.53  ? 511 HOH B O    1 
HETATM 4897 O O    . HOH F 3 .   ? -18.949 11.574  -1.906  1.00 44.07  ? 512 HOH B O    1 
HETATM 4898 O O    . HOH F 3 .   ? -14.306 14.786  -9.284  1.00 37.67  ? 513 HOH B O    1 
HETATM 4899 O O    . HOH F 3 .   ? -9.143  18.818  -16.959 1.00 37.64  ? 514 HOH B O    1 
HETATM 4900 O O    . HOH F 3 .   ? 12.674  16.370  -32.447 1.00 47.40  ? 515 HOH B O    1 
HETATM 4901 O O    . HOH F 3 .   ? -15.494 20.634  -19.490 1.00 43.79  ? 516 HOH B O    1 
HETATM 4902 O O    . HOH F 3 .   ? -13.732 21.838  -5.544  1.00 47.74  ? 517 HOH B O    1 
HETATM 4903 O O    . HOH F 3 .   ? 0.221   12.338  -14.123 1.00 48.00  ? 518 HOH B O    1 
HETATM 4904 O O    . HOH F 3 .   ? -13.909 23.378  -12.827 1.00 46.82  ? 519 HOH B O    1 
HETATM 4905 O O    . HOH F 3 .   ? -18.317 1.504   1.647   1.00 57.40  ? 520 HOH B O    1 
HETATM 4906 O O    . HOH F 3 .   ? -4.212  -10.203 -12.823 1.00 70.24  ? 521 HOH B O    1 
HETATM 4907 O O    . HOH F 3 .   ? 0.863   20.833  -9.063  1.00 61.26  ? 522 HOH B O    1 
HETATM 4908 O O    . HOH F 3 .   ? -27.823 15.780  2.654   1.00 63.77  ? 523 HOH B O    1 
HETATM 4909 O O    . HOH F 3 .   ? -19.907 21.315  -3.427  1.00 53.33  ? 524 HOH B O    1 
HETATM 4910 O O    . HOH F 3 .   ? -20.855 19.009  -3.502  1.00 48.20  ? 525 HOH B O    1 
HETATM 4911 O O    . HOH F 3 .   ? -16.775 10.008  -1.857  1.00 45.21  ? 526 HOH B O    1 
HETATM 4912 O O    . HOH F 3 .   ? -20.928 3.622   0.493   1.00 51.87  ? 527 HOH B O    1 
HETATM 4913 O O    . HOH F 3 .   ? -33.698 5.706   -1.901  1.00 55.70  ? 528 HOH B O    1 
HETATM 4914 O O    . HOH F 3 .   ? -5.852  14.142  -26.128 1.00 43.51  ? 529 HOH B O    1 
HETATM 4915 O O    . HOH F 3 .   ? 10.519  18.370  -29.530 1.00 72.28  ? 530 HOH B O    1 
HETATM 4916 O O    . HOH F 3 .   ? -27.688 -12.142 -3.827  1.00 68.06  ? 531 HOH B O    1 
HETATM 4917 O O    . HOH F 3 .   ? -24.719 10.518  -1.989  1.00 59.67  ? 532 HOH B O    1 
HETATM 4918 O O    . HOH F 3 .   ? -26.056 14.344  -21.891 1.00 62.57  ? 533 HOH B O    1 
HETATM 4919 O O    . HOH F 3 .   ? -17.944 10.634  -27.707 1.00 54.99  ? 534 HOH B O    1 
HETATM 4920 O O    . HOH F 3 .   ? -2.631  6.013   -4.246  1.00 56.02  ? 535 HOH B O    1 
HETATM 4921 O O    . HOH F 3 .   ? -2.319  -7.304  -12.104 1.00 59.42  ? 536 HOH B O    1 
HETATM 4922 O O    . HOH F 3 .   ? 2.428   8.771   -16.193 1.00 60.48  ? 537 HOH B O    1 
HETATM 4923 O O    . HOH F 3 .   ? 12.297  19.346  -30.597 1.00 75.02  ? 538 HOH B O    1 
HETATM 4924 O O    . HOH F 3 .   ? -33.128 4.955   -17.573 1.00 86.10  ? 539 HOH B O    1 
HETATM 4925 O O    . HOH F 3 .   ? -35.004 3.855   -0.228  1.00 54.41  ? 540 HOH B O    1 
HETATM 4926 O O    . HOH F 3 .   ? -23.397 -1.683  2.425   1.00 64.09  ? 541 HOH B O    1 
HETATM 4927 O O    . HOH F 3 .   ? -19.285 21.936  -0.583  1.00 58.04  ? 542 HOH B O    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   . SER A 1   ? 0.4735 0.7518 0.4773 0.0689  0.0012  -0.0596 1   SER A N   
2    C CA  . SER A 1   ? 0.5462 0.7994 0.5268 0.0741  -0.0050 -0.0647 1   SER A CA  
3    C C   . SER A 1   ? 0.5575 0.7946 0.5409 0.0631  -0.0097 -0.0560 1   SER A C   
4    O O   . SER A 1   ? 0.4880 0.7352 0.4868 0.0541  -0.0094 -0.0454 1   SER A O   
5    C CB  . SER A 1   ? 0.5782 0.8257 0.5285 0.0827  -0.0077 -0.0708 1   SER A CB  
6    O OG  . SER A 1   ? 0.6669 0.8850 0.5911 0.0869  -0.0118 -0.0759 1   SER A OG  
7    N N   . GLY A 2   ? 0.5633 0.7762 0.5302 0.0643  -0.0133 -0.0605 2   GLY A N   
8    C CA  . GLY A 2   ? 0.5310 0.7306 0.4998 0.0533  -0.0173 -0.0546 2   GLY A CA  
9    C C   . GLY A 2   ? 0.5321 0.7265 0.5192 0.0514  -0.0151 -0.0533 2   GLY A C   
10   O O   . GLY A 2   ? 0.5247 0.7314 0.5306 0.0552  -0.0103 -0.0537 2   GLY A O   
11   N N   . PHE A 3   ? 0.5475 0.7241 0.5290 0.0443  -0.0181 -0.0523 3   PHE A N   
12   C CA  . PHE A 3   ? 0.5167 0.6850 0.5112 0.0441  -0.0156 -0.0524 3   PHE A CA  
13   C C   . PHE A 3   ? 0.5196 0.6829 0.5217 0.0313  -0.0184 -0.0458 3   PHE A C   
14   O O   . PHE A 3   ? 0.5233 0.6695 0.5046 0.0255  -0.0215 -0.0495 3   PHE A O   
15   C CB  . PHE A 3   ? 0.5155 0.6604 0.4867 0.0552  -0.0138 -0.0634 3   PHE A CB  
16   C CG  . PHE A 3   ? 0.4927 0.6358 0.4789 0.0589  -0.0102 -0.0643 3   PHE A CG  
17   C CD1 . PHE A 3   ? 0.5048 0.6693 0.5113 0.0646  -0.0066 -0.0652 3   PHE A CD1 
18   C CD2 . PHE A 3   ? 0.5149 0.6364 0.4964 0.0546  -0.0100 -0.0643 3   PHE A CD2 
19   C CE1 . PHE A 3   ? 0.4718 0.6359 0.4923 0.0673  -0.0034 -0.0669 3   PHE A CE1 
20   C CE2 . PHE A 3   ? 0.5417 0.6620 0.5371 0.0582  -0.0066 -0.0649 3   PHE A CE2 
21   C CZ  . PHE A 3   ? 0.5368 0.6787 0.5517 0.0648  -0.0036 -0.0663 3   PHE A CZ  
22   N N   . ARG A 4   ? 0.5161 0.6941 0.5470 0.0270  -0.0165 -0.0369 4   ARG A N   
23   C CA  . ARG A 4   ? 0.4920 0.6739 0.5347 0.0161  -0.0192 -0.0290 4   ARG A CA  
24   C C   . ARG A 4   ? 0.4762 0.6545 0.5379 0.0159  -0.0152 -0.0265 4   ARG A C   
25   O O   . ARG A 4   ? 0.4681 0.6498 0.5428 0.0226  -0.0102 -0.0271 4   ARG A O   
26   C CB  . ARG A 4   ? 0.4698 0.6771 0.5290 0.0123  -0.0206 -0.0173 4   ARG A CB  
27   C CG  . ARG A 4   ? 0.4777 0.6924 0.5223 0.0143  -0.0230 -0.0184 4   ARG A CG  
28   C CD  . ARG A 4   ? 0.5919 0.8037 0.6180 0.0056  -0.0299 -0.0208 4   ARG A CD  
29   N NE  . ARG A 4   ? 0.5351 0.7525 0.5732 -0.0040 -0.0325 -0.0158 4   ARG A NE  
30   C CZ  . ARG A 4   ? 0.5982 0.8400 0.6489 -0.0088 -0.0361 -0.0058 4   ARG A CZ  
31   N NH1 . ARG A 4   ? 0.5053 0.7648 0.5565 -0.0049 -0.0372 0.0008  4   ARG A NH1 
32   N NH2 . ARG A 4   ? 0.5618 0.8121 0.6242 -0.0167 -0.0382 -0.0021 4   ARG A NH2 
33   N N   . LYS A 5   ? 0.4888 0.6627 0.5530 0.0071  -0.0173 -0.0241 5   LYS A N   
34   C CA  . LYS A 5   ? 0.4661 0.6435 0.5532 0.0057  -0.0139 -0.0182 5   LYS A CA  
35   C C   . LYS A 5   ? 0.4350 0.6357 0.5465 0.0075  -0.0116 -0.0064 5   LYS A C   
36   O O   . LYS A 5   ? 0.4685 0.6865 0.5847 0.0036  -0.0150 0.0018  5   LYS A O   
37   C CB  . LYS A 5   ? 0.4659 0.6395 0.5517 -0.0053 -0.0165 -0.0173 5   LYS A CB  
38   C CG  . LYS A 5   ? 0.4888 0.6409 0.5713 -0.0048 -0.0125 -0.0227 5   LYS A CG  
39   C CD  . LYS A 5   ? 0.6671 0.8057 0.7336 -0.0168 -0.0143 -0.0275 5   LYS A CD  
40   C CE  . LYS A 5   ? 0.6105 0.7174 0.6610 -0.0137 -0.0092 -0.0356 5   LYS A CE  
41   N NZ  . LYS A 5   ? 0.7225 0.8084 0.7487 -0.0260 -0.0089 -0.0425 5   LYS A NZ  
42   N N   . MET A 6   ? 0.3854 0.5860 0.5108 0.0138  -0.0052 -0.0058 6   MET A N   
43   C CA  . MET A 6   ? 0.3958 0.6116 0.5401 0.0159  -0.0001 0.0042  6   MET A CA  
44   C C   . MET A 6   ? 0.3605 0.5742 0.5252 0.0166  0.0061  0.0092  6   MET A C   
45   O O   . MET A 6   ? 0.3836 0.5862 0.5500 0.0191  0.0098  0.0016  6   MET A O   
46   C CB  . MET A 6   ? 0.3941 0.6121 0.5358 0.0210  0.0043  -0.0009 6   MET A CB  
47   C CG  . MET A 6   ? 0.4250 0.6573 0.5697 0.0209  0.0059  0.0079  6   MET A CG  
48   S SD  . MET A 6   ? 0.5555 0.7908 0.6924 0.0251  0.0104  -0.0018 6   MET A SD  
49   C CE  . MET A 6   ? 0.5047 0.7359 0.6601 0.0257  0.0201  -0.0060 6   MET A CE  
50   N N   . ALA A 7   ? 0.3152 0.5405 0.4946 0.0157  0.0077  0.0221  7   ALA A N   
51   C CA  . ALA A 7   ? 0.3194 0.5423 0.5176 0.0178  0.0151  0.0284  7   ALA A CA  
52   C C   . ALA A 7   ? 0.3639 0.5856 0.5707 0.0214  0.0252  0.0314  7   ALA A C   
53   O O   . ALA A 7   ? 0.3739 0.6017 0.5753 0.0222  0.0264  0.0334  7   ALA A O   
54   C CB  . ALA A 7   ? 0.2698 0.5066 0.4784 0.0173  0.0132  0.0414  7   ALA A CB  
55   N N   . PHE A 8   ? 0.3606 0.5737 0.5805 0.0226  0.0334  0.0319  8   PHE A N   
56   C CA  . PHE A 8   ? 0.3550 0.5644 0.5833 0.0238  0.0452  0.0356  8   PHE A CA  
57   C C   . PHE A 8   ? 0.3488 0.5645 0.5817 0.0275  0.0493  0.0526  8   PHE A C   
58   O O   . PHE A 8   ? 0.3143 0.5386 0.5505 0.0302  0.0445  0.0622  8   PHE A O   
59   C CB  . PHE A 8   ? 0.3905 0.5878 0.6304 0.0237  0.0534  0.0320  8   PHE A CB  
60   C CG  . PHE A 8   ? 0.4274 0.6198 0.6627 0.0220  0.0521  0.0152  8   PHE A CG  
61   C CD1 . PHE A 8   ? 0.5525 0.7473 0.7857 0.0199  0.0573  0.0057  8   PHE A CD1 
62   C CD2 . PHE A 8   ? 0.3989 0.5864 0.6305 0.0230  0.0457  0.0089  8   PHE A CD2 
63   C CE1 . PHE A 8   ? 0.5886 0.7841 0.8173 0.0203  0.0553  -0.0097 8   PHE A CE1 
64   C CE2 . PHE A 8   ? 0.4958 0.6793 0.7206 0.0241  0.0445  -0.0053 8   PHE A CE2 
65   C CZ  . PHE A 8   ? 0.5730 0.7623 0.7967 0.0237  0.0488  -0.0147 8   PHE A CZ  
66   N N   . PRO A 9   ? 0.3583 0.5701 0.5911 0.0280  0.0595  0.0567  9   PRO A N   
67   C CA  . PRO A 9   ? 0.3276 0.5402 0.5629 0.0341  0.0664  0.0742  9   PRO A CA  
68   C C   . PRO A 9   ? 0.3548 0.5600 0.6019 0.0388  0.0722  0.0825  9   PRO A C   
69   O O   . PRO A 9   ? 0.3731 0.5650 0.6274 0.0360  0.0784  0.0751  9   PRO A O   
70   C CB  . PRO A 9   ? 0.3706 0.5727 0.6025 0.0316  0.0798  0.0737  9   PRO A CB  
71   C CG  . PRO A 9   ? 0.4214 0.6253 0.6499 0.0239  0.0770  0.0552  9   PRO A CG  
72   C CD  . PRO A 9   ? 0.4054 0.6104 0.6370 0.0231  0.0674  0.0452  9   PRO A CD  
73   N N   . SER A 10  ? 0.3362 0.5525 0.5851 0.0468  0.0697  0.0975  10  SER A N   
74   C CA  . SER A 10  ? 0.3117 0.5278 0.5717 0.0524  0.0717  0.1050  10  SER A CA  
75   C C   . SER A 10  ? 0.3372 0.5397 0.5995 0.0622  0.0872  0.1199  10  SER A C   
76   O O   . SER A 10  ? 0.3353 0.5388 0.6058 0.0699  0.0901  0.1287  10  SER A O   
77   C CB  . SER A 10  ? 0.2795 0.5218 0.5410 0.0549  0.0580  0.1102  10  SER A CB  
78   O OG  . SER A 10  ? 0.3357 0.5940 0.5920 0.0635  0.0571  0.1249  10  SER A OG  
79   N N   . GLY A 11  ? 0.3387 0.5273 0.5926 0.0622  0.0983  0.1228  11  GLY A N   
80   C CA  . GLY A 11  ? 0.3243 0.4954 0.5751 0.0724  0.1148  0.1384  11  GLY A CA  
81   C C   . GLY A 11  ? 0.3448 0.4940 0.6037 0.0738  0.1269  0.1380  11  GLY A C   
82   O O   . GLY A 11  ? 0.4241 0.5705 0.6851 0.0866  0.1328  0.1524  11  GLY A O   
83   N N   . LYS A 12  ? 0.3913 0.5260 0.6540 0.0614  0.1310  0.1212  12  LYS A N   
84   C CA  . LYS A 12  ? 0.4071 0.5192 0.6760 0.0609  0.1436  0.1187  12  LYS A CA  
85   C C   . LYS A 12  ? 0.3778 0.5006 0.6574 0.0686  0.1361  0.1232  12  LYS A C   
86   O O   . LYS A 12  ? 0.3945 0.5006 0.6779 0.0746  0.1473  0.1286  12  LYS A O   
87   C CB  . LYS A 12  ? 0.4238 0.5273 0.6954 0.0456  0.1456  0.0974  12  LYS A CB  
88   C CG  . LYS A 12  ? 0.4283 0.5163 0.6917 0.0365  0.1592  0.0918  12  LYS A CG  
89   C CD  . LYS A 12  ? 0.5661 0.6719 0.8288 0.0253  0.1487  0.0746  12  LYS A CD  
90   C CE  . LYS A 12  ? 0.6102 0.7340 0.8644 0.0288  0.1389  0.0817  12  LYS A CE  
91   N NZ  . LYS A 12  ? 0.6061 0.7460 0.8575 0.0195  0.1299  0.0654  12  LYS A NZ  
92   N N   . VAL A 13  ? 0.3378 0.4874 0.6216 0.0678  0.1183  0.1204  13  VAL A N   
93   C CA  . VAL A 13  ? 0.3559 0.5186 0.6499 0.0733  0.1115  0.1241  13  VAL A CA  
94   C C   . VAL A 13  ? 0.4013 0.5800 0.6959 0.0884  0.1115  0.1439  13  VAL A C   
95   O O   . VAL A 13  ? 0.4416 0.6236 0.7443 0.0975  0.1145  0.1519  13  VAL A O   
96   C CB  . VAL A 13  ? 0.3506 0.5321 0.6468 0.0640  0.0944  0.1113  13  VAL A CB  
97   C CG1 . VAL A 13  ? 0.3389 0.5329 0.6459 0.0670  0.0888  0.1135  13  VAL A CG1 
98   C CG2 . VAL A 13  ? 0.2940 0.4613 0.5872 0.0526  0.0950  0.0929  13  VAL A CG2 
99   N N   . GLU A 14  ? 0.3595 0.5498 0.6451 0.0929  0.1088  0.1525  14  GLU A N   
100  C CA  . GLU A 14  ? 0.3784 0.5886 0.6637 0.1093  0.1079  0.1715  14  GLU A CA  
101  C C   . GLU A 14  ? 0.4032 0.5911 0.6876 0.1240  0.1258  0.1852  14  GLU A C   
102  O O   . GLU A 14  ? 0.3824 0.5869 0.6728 0.1382  0.1253  0.1977  14  GLU A O   
103  C CB  . GLU A 14  ? 0.3541 0.5764 0.6269 0.1128  0.1043  0.1789  14  GLU A CB  
104  C CG  . GLU A 14  ? 0.3445 0.5908 0.6159 0.0998  0.0860  0.1663  14  GLU A CG  
105  C CD  . GLU A 14  ? 0.3432 0.5977 0.6008 0.1023  0.0838  0.1720  14  GLU A CD  
106  O OE1 . GLU A 14  ? 0.4290 0.6971 0.6816 0.1172  0.0857  0.1888  14  GLU A OE1 
107  O OE2 . GLU A 14  ? 0.3491 0.5975 0.6001 0.0905  0.0803  0.1599  14  GLU A OE2 
108  N N   . GLY A 15  ? 0.4198 0.5705 0.6958 0.1210  0.1426  0.1831  15  GLY A N   
109  C CA  . GLY A 15  ? 0.4468 0.5690 0.7174 0.1346  0.1623  0.1960  15  GLY A CA  
110  C C   . GLY A 15  ? 0.4727 0.5886 0.7551 0.1369  0.1657  0.1934  15  GLY A C   
111  O O   . GLY A 15  ? 0.4520 0.5452 0.7296 0.1502  0.1818  0.2048  15  GLY A O   
112  N N   . CYS A 16  ? 0.4121 0.5460 0.7078 0.1252  0.1516  0.1791  16  CYS A N   
113  C CA  . CYS A 16  ? 0.4079 0.5379 0.7149 0.1257  0.1534  0.1748  16  CYS A CA  
114  C C   . CYS A 16  ? 0.4418 0.6073 0.7581 0.1324  0.1394  0.1805  16  CYS A C   
115  O O   . CYS A 16  ? 0.4364 0.5968 0.7554 0.1294  0.1380  0.1749  16  CYS A O   
116  C CB  . CYS A 16  ? 0.4136 0.5332 0.7252 0.1067  0.1493  0.1528  16  CYS A CB  
117  S SG  . CYS A 16  ? 0.4900 0.5751 0.7904 0.0927  0.1622  0.1397  16  CYS A SG  
118  N N   . MET A 17  ? 0.3832 0.5818 0.6980 0.1375  0.1275  0.1886  17  MET A N   
119  C CA  . MET A 17  ? 0.3831 0.6140 0.7010 0.1370  0.1124  0.1884  17  MET A CA  
120  C C   . MET A 17  ? 0.4077 0.6471 0.7191 0.1555  0.1174  0.2055  17  MET A C   
121  O O   . MET A 17  ? 0.4390 0.6807 0.7410 0.1697  0.1230  0.2200  17  MET A O   
122  C CB  . MET A 17  ? 0.3910 0.6567 0.7111 0.1279  0.0948  0.1830  17  MET A CB  
123  C CG  . MET A 17  ? 0.3278 0.5836 0.6506 0.1124  0.0916  0.1682  17  MET A CG  
124  S SD  . MET A 17  ? 0.3745 0.6170 0.7030 0.0968  0.0875  0.1491  17  MET A SD  
125  C CE  . MET A 17  ? 0.3114 0.5826 0.6438 0.0979  0.0774  0.1515  17  MET A CE  
126  N N   . VAL A 18  ? 0.4100 0.6534 0.7249 0.1561  0.1159  0.2036  18  VAL A N   
127  C CA  . VAL A 18  ? 0.4564 0.7128 0.7659 0.1729  0.1192  0.2176  18  VAL A CA  
128  C C   . VAL A 18  ? 0.4337 0.7288 0.7521 0.1662  0.1037  0.2110  18  VAL A C   
129  O O   . VAL A 18  ? 0.3958 0.6998 0.7230 0.1489  0.0931  0.1961  18  VAL A O   
130  C CB  . VAL A 18  ? 0.5008 0.7205 0.8044 0.1820  0.1370  0.2229  18  VAL A CB  
131  C CG1 . VAL A 18  ? 0.5238 0.7014 0.8194 0.1839  0.1540  0.2254  18  VAL A CG1 
132  C CG2 . VAL A 18  ? 0.4242 0.6364 0.7371 0.1696  0.1342  0.2090  18  VAL A CG2 
133  N N   . GLN A 19  ? 0.4753 0.7930 0.7904 0.1805  0.1037  0.2223  19  GLN A N   
134  C CA  . GLN A 19  ? 0.4642 0.8199 0.7884 0.1759  0.0918  0.2172  19  GLN A CA  
135  C C   . GLN A 19  ? 0.4900 0.8336 0.8156 0.1831  0.1005  0.2197  19  GLN A C   
136  O O   . GLN A 19  ? 0.5148 0.8402 0.8302 0.2007  0.1138  0.2329  19  GLN A O   
137  C CB  . GLN A 19  ? 0.4508 0.8500 0.7713 0.1860  0.0835  0.2264  19  GLN A CB  
138  C CG  . GLN A 19  ? 0.5903 0.9907 0.8996 0.2100  0.0939  0.2442  19  GLN A CG  
139  C CD  . GLN A 19  ? 0.6656 1.1182 0.9762 0.2173  0.0837  0.2487  19  GLN A CD  
140  O OE1 . GLN A 19  ? 0.6856 1.1500 0.9946 0.2310  0.0884  0.2564  19  GLN A OE1 
141  N NE2 . GLN A 19  ? 0.6097 1.0949 0.9229 0.2077  0.0700  0.2430  19  GLN A NE2 
142  N N   . VAL A 20  ? 0.4665 0.8174 0.8032 0.1697  0.0944  0.2070  20  VAL A N   
143  C CA  . VAL A 20  ? 0.4395 0.7813 0.7786 0.1748  0.1015  0.2078  20  VAL A CA  
144  C C   . VAL A 20  ? 0.4407 0.8286 0.7888 0.1750  0.0920  0.2070  20  VAL A C   
145  O O   . VAL A 20  ? 0.3532 0.7674 0.7108 0.1590  0.0798  0.1955  20  VAL A O   
146  C CB  . VAL A 20  ? 0.4208 0.7320 0.7646 0.1600  0.1042  0.1938  20  VAL A CB  
147  C CG1 . VAL A 20  ? 0.3952 0.6995 0.7408 0.1658  0.1112  0.1951  20  VAL A CG1 
148  C CG2 . VAL A 20  ? 0.4328 0.7014 0.7686 0.1589  0.1140  0.1932  20  VAL A CG2 
149  N N   . THR A 21  ? 0.4411 0.8382 0.7856 0.1926  0.0985  0.2188  21  THR A N   
150  C CA  . THR A 21  ? 0.4723 0.9150 0.8255 0.1950  0.0911  0.2190  21  THR A CA  
151  C C   . THR A 21  ? 0.4705 0.9028 0.8276 0.1991  0.0988  0.2186  21  THR A C   
152  O O   . THR A 21  ? 0.4899 0.8927 0.8366 0.2144  0.1121  0.2287  21  THR A O   
153  C CB  . THR A 21  ? 0.5015 0.9737 0.8462 0.2147  0.0910  0.2343  21  THR A CB  
154  O OG1 . THR A 21  ? 0.5210 0.9940 0.8587 0.2133  0.0866  0.2364  21  THR A OG1 
155  C CG2 . THR A 21  ? 0.4522 0.9800 0.8079 0.2134  0.0806  0.2316  21  THR A CG2 
156  N N   . CYS A 22  ? 0.4729 0.9286 0.8440 0.1851  0.0914  0.2068  22  CYS A N   
157  C CA  . CYS A 22  ? 0.4794 0.9357 0.8561 0.1887  0.0969  0.2061  22  CYS A CA  
158  C C   . CYS A 22  ? 0.4608 0.9723 0.8500 0.1866  0.0880  0.2038  22  CYS A C   
159  O O   . CYS A 22  ? 0.4649 1.0004 0.8650 0.1672  0.0780  0.1911  22  CYS A O   
160  C CB  . CYS A 22  ? 0.4707 0.8965 0.8522 0.1720  0.0990  0.1923  22  CYS A CB  
161  S SG  . CYS A 22  ? 0.5344 0.9512 0.9187 0.1799  0.1088  0.1939  22  CYS A SG  
162  N N   . GLY A 23  ? 0.5545 1.0863 0.9414 0.2058  0.0925  0.2158  23  GLY A N   
163  C CA  . GLY A 23  ? 0.5886 1.1772 0.9874 0.2045  0.0842  0.2139  23  GLY A CA  
164  C C   . GLY A 23  ? 0.5506 1.1747 0.9503 0.1978  0.0722  0.2119  23  GLY A C   
165  O O   . GLY A 23  ? 0.4828 1.1067 0.8698 0.2119  0.0728  0.2232  23  GLY A O   
166  N N   . THR A 24  ? 0.5217 1.1766 0.9353 0.1757  0.0622  0.1974  24  THR A N   
167  C CA  . THR A 24  ? 0.5562 1.2432 0.9703 0.1652  0.0505  0.1927  24  THR A CA  
168  C C   . THR A 24  ? 0.5172 1.1734 0.9271 0.1492  0.0471  0.1843  24  THR A C   
169  O O   . THR A 24  ? 0.5469 1.2212 0.9524 0.1450  0.0390  0.1837  24  THR A O   
170  C CB  . THR A 24  ? 0.7038 1.4379 1.1334 0.1465  0.0423  0.1801  24  THR A CB  
171  O OG1 . THR A 24  ? 0.7734 1.5473 1.2008 0.1420  0.0319  0.1790  24  THR A OG1 
172  C CG2 . THR A 24  ? 0.6739 1.3855 1.1120 0.1197  0.0417  0.1629  24  THR A CG2 
173  N N   . THR A 25  ? 0.4393 1.0503 0.8489 0.1414  0.0531  0.1783  25  THR A N   
174  C CA  . THR A 25  ? 0.4091 0.9923 0.8149 0.1256  0.0501  0.1691  25  THR A CA  
175  C C   . THR A 25  ? 0.4101 0.9613 0.8017 0.1394  0.0546  0.1797  25  THR A C   
176  O O   . THR A 25  ? 0.4112 0.9376 0.7952 0.1575  0.0649  0.1912  25  THR A O   
177  C CB  . THR A 25  ? 0.4138 0.9650 0.8245 0.1114  0.0548  0.1575  25  THR A CB  
178  O OG1 . THR A 25  ? 0.4975 1.0783 0.9212 0.0966  0.0516  0.1472  25  THR A OG1 
179  C CG2 . THR A 25  ? 0.3727 0.8953 0.7780 0.0970  0.0523  0.1488  25  THR A CG2 
180  N N   . THR A 26  ? 0.3844 0.9349 0.7717 0.1298  0.0477  0.1754  26  THR A N   
181  C CA  . THR A 26  ? 0.3503 0.8685 0.7253 0.1391  0.0523  0.1833  26  THR A CA  
182  C C   . THR A 26  ? 0.3318 0.8326 0.7065 0.1199  0.0471  0.1708  26  THR A C   
183  O O   . THR A 26  ? 0.3080 0.8349 0.6865 0.1045  0.0367  0.1614  26  THR A O   
184  C CB  . THR A 26  ? 0.3808 0.9230 0.7467 0.1553  0.0500  0.1968  26  THR A CB  
185  O OG1 . THR A 26  ? 0.4770 1.0283 0.8395 0.1768  0.0574  0.2104  26  THR A OG1 
186  C CG2 . THR A 26  ? 0.3844 0.8935 0.7381 0.1617  0.0549  0.2034  26  THR A CG2 
187  N N   . LEU A 27  ? 0.3494 0.8056 0.7187 0.1204  0.0548  0.1702  27  LEU A N   
188  C CA  . LEU A 27  ? 0.2881 0.7253 0.6555 0.1051  0.0511  0.1595  27  LEU A CA  
189  C C   . LEU A 27  ? 0.3252 0.7247 0.6829 0.1151  0.0599  0.1667  27  LEU A C   
190  O O   . LEU A 27  ? 0.3044 0.6933 0.6563 0.1328  0.0690  0.1800  27  LEU A O   
191  C CB  . LEU A 27  ? 0.3280 0.7521 0.7018 0.0885  0.0511  0.1451  27  LEU A CB  
192  C CG  . LEU A 27  ? 0.3315 0.7368 0.7082 0.0940  0.0604  0.1458  27  LEU A CG  
193  C CD1 . LEU A 27  ? 0.3538 0.7176 0.7219 0.1059  0.0714  0.1526  27  LEU A CD1 
194  C CD2 . LEU A 27  ? 0.2749 0.6733 0.6570 0.0766  0.0593  0.1316  27  LEU A CD2 
195  N N   . ASN A 28  ? 0.2629 0.6417 0.6183 0.1034  0.0583  0.1577  28  ASN A N   
196  C CA  . ASN A 28  ? 0.3174 0.6639 0.6650 0.1103  0.0665  0.1627  28  ASN A CA  
197  C C   . ASN A 28  ? 0.3253 0.6320 0.6722 0.1097  0.0773  0.1582  28  ASN A C   
198  O O   . ASN A 28  ? 0.3104 0.6120 0.6618 0.0998  0.0758  0.1477  28  ASN A O   
199  C CB  . ASN A 28  ? 0.2872 0.6345 0.6321 0.0992  0.0593  0.1555  28  ASN A CB  
200  C CG  . ASN A 28  ? 0.3214 0.7100 0.6665 0.0959  0.0470  0.1567  28  ASN A CG  
201  O OD1 . ASN A 28  ? 0.3973 0.8028 0.7377 0.1088  0.0469  0.1689  28  ASN A OD1 
202  N ND2 . ASN A 28  ? 0.2859 0.6905 0.6352 0.0788  0.0375  0.1439  28  ASN A ND2 
203  N N   . GLY A 29  ? 0.3300 0.6083 0.6703 0.1202  0.0891  0.1662  29  GLY A N   
204  C CA  . GLY A 29  ? 0.3332 0.5724 0.6715 0.1179  0.1000  0.1605  29  GLY A CA  
205  C C   . GLY A 29  ? 0.3827 0.5961 0.7158 0.1179  0.1078  0.1605  29  GLY A C   
206  O O   . GLY A 29  ? 0.3592 0.5813 0.6889 0.1243  0.1081  0.1694  29  GLY A O   
207  N N   . LEU A 30  ? 0.3632 0.5455 0.6954 0.1108  0.1150  0.1501  30  LEU A N   
208  C CA  . LEU A 30  ? 0.3872 0.5449 0.7162 0.1075  0.1235  0.1461  30  LEU A CA  
209  C C   . LEU A 30  ? 0.3902 0.5144 0.7143 0.1160  0.1424  0.1523  30  LEU A C   
210  O O   . LEU A 30  ? 0.3873 0.4935 0.7108 0.1136  0.1476  0.1463  30  LEU A O   
211  C CB  . LEU A 30  ? 0.3498 0.5001 0.6802 0.0917  0.1173  0.1272  30  LEU A CB  
212  C CG  . LEU A 30  ? 0.3599 0.4926 0.6882 0.0849  0.1230  0.1184  30  LEU A CG  
213  C CD1 . LEU A 30  ? 0.3558 0.5087 0.6843 0.0825  0.1151  0.1199  30  LEU A CD1 
214  C CD2 . LEU A 30  ? 0.3063 0.4272 0.6332 0.0731  0.1197  0.1002  30  LEU A CD2 
215  N N   . TRP A 31  ? 0.4189 0.5328 0.7378 0.1258  0.1536  0.1640  31  TRP A N   
216  C CA  . TRP A 31  ? 0.4551 0.5343 0.7658 0.1354  0.1744  0.1722  31  TRP A CA  
217  C C   . TRP A 31  ? 0.4949 0.5443 0.8052 0.1252  0.1872  0.1609  31  TRP A C   
218  O O   . TRP A 31  ? 0.4997 0.5480 0.8090 0.1250  0.1920  0.1630  31  TRP A O   
219  C CB  . TRP A 31  ? 0.4555 0.5394 0.7570 0.1539  0.1811  0.1929  31  TRP A CB  
220  C CG  . TRP A 31  ? 0.5733 0.6200 0.8612 0.1656  0.2032  0.2034  31  TRP A CG  
221  C CD1 . TRP A 31  ? 0.5840 0.6005 0.8683 0.1625  0.2154  0.1976  31  TRP A CD1 
222  C CD2 . TRP A 31  ? 0.6177 0.6518 0.8902 0.1823  0.2166  0.2213  31  TRP A CD2 
223  N NE1 . TRP A 31  ? 0.6232 0.6081 0.8903 0.1750  0.2362  0.2101  31  TRP A NE1 
224  C CE2 . TRP A 31  ? 0.6632 0.6571 0.9219 0.1877  0.2376  0.2250  31  TRP A CE2 
225  C CE3 . TRP A 31  ? 0.5692 0.6215 0.8358 0.1930  0.2132  0.2342  31  TRP A CE3 
226  C CZ2 . TRP A 31  ? 0.7096 0.6790 0.9473 0.2031  0.2560  0.2405  31  TRP A CZ2 
227  C CZ3 . TRP A 31  ? 0.6744 0.7034 0.9206 0.2097  0.2307  0.2508  31  TRP A CZ3 
228  C CH2 . TRP A 31  ? 0.6791 0.6662 0.9104 0.2144  0.2523  0.2536  31  TRP A CH2 
229  N N   . LEU A 32  ? 0.5059 0.5331 0.8167 0.1161  0.1931  0.1479  32  LEU A N   
230  C CA  . LEU A 32  ? 0.5332 0.5335 0.8433 0.1045  0.2064  0.1340  32  LEU A CA  
231  C C   . LEU A 32  ? 0.6134 0.5757 0.9148 0.1079  0.2265  0.1355  32  LEU A C   
232  O O   . LEU A 32  ? 0.5648 0.5247 0.8652 0.1093  0.2237  0.1347  32  LEU A O   
233  C CB  . LEU A 32  ? 0.4696 0.4820 0.7860 0.0880  0.1925  0.1132  32  LEU A CB  
234  C CG  . LEU A 32  ? 0.4700 0.5156 0.7909 0.0838  0.1736  0.1110  32  LEU A CG  
235  C CD1 . LEU A 32  ? 0.3682 0.4244 0.6906 0.0729  0.1586  0.0947  32  LEU A CD1 
236  C CD2 . LEU A 32  ? 0.4537 0.4967 0.7687 0.0767  0.1766  0.1076  32  LEU A CD2 
237  N N   . ASP A 33  ? 0.5979 0.5291 0.8909 0.1081  0.2474  0.1373  33  ASP A N   
238  C CA  . ASP A 33  ? 0.6347 0.5238 0.9145 0.1108  0.2693  0.1396  33  ASP A CA  
239  C C   . ASP A 33  ? 0.6530 0.5487 0.9247 0.1279  0.2670  0.1582  33  ASP A C   
240  O O   . ASP A 33  ? 0.6555 0.5700 0.9246 0.1419  0.2614  0.1747  33  ASP A O   
241  C CB  . ASP A 33  ? 0.6479 0.5238 0.9313 0.0938  0.2722  0.1177  33  ASP A CB  
242  C CG  . ASP A 33  ? 0.6395 0.5191 0.9253 0.0732  0.2699  0.0977  33  ASP A CG  
243  O OD1 . ASP A 33  ? 0.7294 0.5895 1.0030 0.0670  0.2822  0.0986  33  ASP A OD1 
244  O OD2 . ASP A 33  ? 0.6975 0.6000 0.9939 0.0627  0.2550  0.0816  33  ASP A OD2 
245  N N   . ASP A 34  ? 0.6719 0.5553 0.9389 0.1276  0.2717  0.1556  34  ASP A N   
246  C CA  . ASP A 34  ? 0.7104 0.6011 0.9697 0.1438  0.2716  0.1713  34  ASP A CA  
247  C C   . ASP A 34  ? 0.6480 0.5726 0.9201 0.1431  0.2507  0.1681  34  ASP A C   
248  O O   . ASP A 34  ? 0.6799 0.6062 0.9478 0.1514  0.2521  0.1742  34  ASP A O   
249  C CB  . ASP A 34  ? 0.7551 0.6074 0.9965 0.1467  0.2945  0.1727  34  ASP A CB  
250  C CG  . ASP A 34  ? 0.7860 0.6241 1.0309 0.1316  0.2971  0.1544  34  ASP A CG  
251  O OD1 . ASP A 34  ? 0.7119 0.5589 0.9700 0.1162  0.2867  0.1377  34  ASP A OD1 
252  O OD2 . ASP A 34  ? 0.8197 0.6381 1.0525 0.1362  0.3098  0.1567  34  ASP A OD2 
253  N N   . VAL A 35  ? 0.6223 0.5744 0.9084 0.1337  0.2319  0.1588  35  VAL A N   
254  C CA  . VAL A 35  ? 0.5547 0.5373 0.8508 0.1305  0.2126  0.1537  35  VAL A CA  
255  C C   . VAL A 35  ? 0.5516 0.5713 0.8557 0.1319  0.1952  0.1578  35  VAL A C   
256  O O   . VAL A 35  ? 0.5333 0.5561 0.8402 0.1261  0.1925  0.1536  35  VAL A O   
257  C CB  . VAL A 35  ? 0.5487 0.5244 0.8501 0.1138  0.2075  0.1331  35  VAL A CB  
258  C CG1 . VAL A 35  ? 0.5169 0.5208 0.8255 0.1105  0.1890  0.1282  35  VAL A CG1 
259  C CG2 . VAL A 35  ? 0.6227 0.5640 0.9160 0.1107  0.2244  0.1273  35  VAL A CG2 
260  N N   . VAL A 36  ? 0.5068 0.5557 0.8144 0.1386  0.1837  0.1647  36  VAL A N   
261  C CA  . VAL A 36  ? 0.4394 0.5266 0.7545 0.1375  0.1663  0.1662  36  VAL A CA  
262  C C   . VAL A 36  ? 0.4534 0.5565 0.7763 0.1253  0.1524  0.1525  36  VAL A C   
263  O O   . VAL A 36  ? 0.4555 0.5568 0.7788 0.1265  0.1535  0.1513  36  VAL A O   
264  C CB  . VAL A 36  ? 0.4434 0.5549 0.7558 0.1541  0.1649  0.1837  36  VAL A CB  
265  C CG1 . VAL A 36  ? 0.3910 0.5464 0.7119 0.1504  0.1460  0.1827  36  VAL A CG1 
266  C CG2 . VAL A 36  ? 0.4551 0.5500 0.7564 0.1670  0.1787  0.1978  36  VAL A CG2 
267  N N   . TYR A 37  ? 0.3659 0.4835 0.6933 0.1140  0.1403  0.1426  37  TYR A N   
268  C CA  . TYR A 37  ? 0.3524 0.4815 0.6841 0.1022  0.1285  0.1294  37  TYR A CA  
269  C C   . TYR A 37  ? 0.3567 0.5235 0.6942 0.1012  0.1150  0.1325  37  TYR A C   
270  O O   . TYR A 37  ? 0.3633 0.5451 0.7013 0.1010  0.1097  0.1357  37  TYR A O   
271  C CB  . TYR A 37  ? 0.3230 0.4386 0.6528 0.0894  0.1256  0.1139  37  TYR A CB  
272  C CG  . TYR A 37  ? 0.4352 0.5177 0.7603 0.0879  0.1385  0.1081  37  TYR A CG  
273  C CD1 . TYR A 37  ? 0.4448 0.5112 0.7675 0.0937  0.1513  0.1155  37  TYR A CD1 
274  C CD2 . TYR A 37  ? 0.4436 0.5110 0.7660 0.0805  0.1390  0.0949  37  TYR A CD2 
275  C CE1 . TYR A 37  ? 0.4825 0.5185 0.8012 0.0904  0.1650  0.1088  37  TYR A CE1 
276  C CE2 . TYR A 37  ? 0.5009 0.5408 0.8192 0.0777  0.1510  0.0880  37  TYR A CE2 
277  C CZ  . TYR A 37  ? 0.5173 0.5415 0.8344 0.0818  0.1643  0.0944  37  TYR A CZ  
278  O OH  . TYR A 37  ? 0.5702 0.5669 0.8836 0.0773  0.1782  0.0863  37  TYR A OH  
279  N N   . CYS A 38  ? 0.3267 0.5093 0.6687 0.0990  0.1098  0.1302  38  CYS A N   
280  C CA  . CYS A 38  ? 0.3010 0.5212 0.6497 0.0956  0.0981  0.1312  38  CYS A CA  
281  C C   . CYS A 38  ? 0.3432 0.5713 0.6966 0.0858  0.0935  0.1215  38  CYS A C   
282  O O   . CYS A 38  ? 0.3249 0.5316 0.6762 0.0854  0.0996  0.1171  38  CYS A O   
283  C CB  . CYS A 38  ? 0.3198 0.5645 0.6705 0.1093  0.0989  0.1461  38  CYS A CB  
284  S SG  . CYS A 38  ? 0.3847 0.6352 0.7388 0.1181  0.1044  0.1514  38  CYS A SG  
285  N N   . PRO A 39  ? 0.3117 0.5689 0.6707 0.0766  0.0836  0.1174  39  PRO A N   
286  C CA  . PRO A 39  ? 0.2840 0.5483 0.6476 0.0662  0.0813  0.1086  39  PRO A CA  
287  C C   . PRO A 39  ? 0.3045 0.5788 0.6734 0.0735  0.0859  0.1142  39  PRO A C   
288  O O   . PRO A 39  ? 0.2882 0.5833 0.6605 0.0842  0.0862  0.1247  39  PRO A O   
289  C CB  . PRO A 39  ? 0.2747 0.5712 0.6434 0.0548  0.0711  0.1049  39  PRO A CB  
290  C CG  . PRO A 39  ? 0.2998 0.5955 0.6635 0.0576  0.0674  0.1084  39  PRO A CG  
291  C CD  . PRO A 39  ? 0.2893 0.5726 0.6498 0.0741  0.0751  0.1201  39  PRO A CD  
292  N N   . ARG A 40  ? 0.2645 0.5239 0.6333 0.0690  0.0900  0.1075  40  ARG A N   
293  C CA  . ARG A 40  ? 0.3269 0.5936 0.7002 0.0770  0.0954  0.1130  40  ARG A CA  
294  C C   . ARG A 40  ? 0.2870 0.5980 0.6717 0.0740  0.0899  0.1151  40  ARG A C   
295  O O   . ARG A 40  ? 0.3197 0.6451 0.7090 0.0836  0.0933  0.1219  40  ARG A O   
296  C CB  . ARG A 40  ? 0.3577 0.5991 0.7278 0.0729  0.1013  0.1055  40  ARG A CB  
297  C CG  . ARG A 40  ? 0.3039 0.5502 0.6766 0.0576  0.0980  0.0948  40  ARG A CG  
298  C CD  . ARG A 40  ? 0.3514 0.5803 0.7224 0.0572  0.1049  0.0909  40  ARG A CD  
299  N NE  . ARG A 40  ? 0.3073 0.5337 0.6785 0.0434  0.1045  0.0814  40  ARG A NE  
300  C CZ  . ARG A 40  ? 0.3472 0.5522 0.7142 0.0420  0.1108  0.0763  40  ARG A CZ  
301  N NH1 . ARG A 40  ? 0.3368 0.5228 0.6994 0.0523  0.1169  0.0789  40  ARG A NH1 
302  N NH2 . ARG A 40  ? 0.2689 0.4698 0.6351 0.0299  0.1120  0.0686  40  ARG A NH2 
303  N N   . HIS A 41  ? 0.2869 0.6213 0.6759 0.0607  0.0818  0.1091  41  HIS A N   
304  C CA  . HIS A 41  ? 0.2849 0.6621 0.6853 0.0552  0.0775  0.1086  41  HIS A CA  
305  C C   . HIS A 41  ? 0.2850 0.6917 0.6886 0.0675  0.0737  0.1193  41  HIS A C   
306  O O   . HIS A 41  ? 0.2815 0.7276 0.6947 0.0641  0.0695  0.1190  41  HIS A O   
307  C CB  . HIS A 41  ? 0.2915 0.6841 0.6950 0.0338  0.0716  0.0975  41  HIS A CB  
308  C CG  . HIS A 41  ? 0.3306 0.7299 0.7302 0.0291  0.0638  0.0968  41  HIS A CG  
309  N ND1 . HIS A 41  ? 0.3617 0.7939 0.7648 0.0335  0.0570  0.1025  41  HIS A ND1 
310  C CD2 . HIS A 41  ? 0.3373 0.7142 0.7290 0.0217  0.0618  0.0915  41  HIS A CD2 
311  C CE1 . HIS A 41  ? 0.3333 0.7633 0.7306 0.0277  0.0510  0.1003  41  HIS A CE1 
312  N NE2 . HIS A 41  ? 0.3252 0.7225 0.7160 0.0202  0.0538  0.0935  41  HIS A NE2 
313  N N   . VAL A 42  ? 0.2531 0.6414 0.6484 0.0823  0.0763  0.1289  42  VAL A N   
314  C CA  . VAL A 42  ? 0.3309 0.7434 0.7269 0.0981  0.0755  0.1417  42  VAL A CA  
315  C C   . VAL A 42  ? 0.3684 0.7941 0.7699 0.1092  0.0811  0.1477  42  VAL A C   
316  O O   . VAL A 42  ? 0.3030 0.7616 0.7079 0.1198  0.0788  0.1563  42  VAL A O   
317  C CB  . VAL A 42  ? 0.2413 0.6271 0.6259 0.1119  0.0802  0.1518  42  VAL A CB  
318  C CG1 . VAL A 42  ? 0.3201 0.6625 0.6974 0.1200  0.0922  0.1543  42  VAL A CG1 
319  C CG2 . VAL A 42  ? 0.3390 0.7521 0.7221 0.1287  0.0794  0.1660  42  VAL A CG2 
320  N N   . ILE A 43  ? 0.3384 0.7411 0.7402 0.1075  0.0882  0.1435  43  ILE A N   
321  C CA  . ILE A 43  ? 0.4121 0.8299 0.8193 0.1181  0.0933  0.1492  43  ILE A CA  
322  C C   . ILE A 43  ? 0.3481 0.8071 0.7697 0.1057  0.0882  0.1412  43  ILE A C   
323  O O   . ILE A 43  ? 0.3394 0.8192 0.7677 0.1137  0.0913  0.1454  43  ILE A O   
324  C CB  . ILE A 43  ? 0.3943 0.7723 0.7953 0.1233  0.1040  0.1492  43  ILE A CB  
325  C CG1 . ILE A 43  ? 0.3822 0.7496 0.7866 0.1055  0.1036  0.1353  43  ILE A CG1 
326  C CG2 . ILE A 43  ? 0.3948 0.7291 0.7814 0.1324  0.1107  0.1550  43  ILE A CG2 
327  C CD1 . ILE A 43  ? 0.4434 0.7646 0.8381 0.1076  0.1125  0.1329  43  ILE A CD1 
328  N N   . CYS A 44  ? 0.3356 0.8080 0.7619 0.0859  0.0812  0.1300  44  CYS A N   
329  C CA  . CYS A 44  ? 0.3984 0.9078 0.8380 0.0716  0.0783  0.1217  44  CYS A CA  
330  C C   . CYS A 44  ? 0.4797 1.0370 0.9262 0.0727  0.0700  0.1252  44  CYS A C   
331  O O   . CYS A 44  ? 0.4854 1.0466 0.9256 0.0770  0.0641  0.1298  44  CYS A O   
332  C CB  . CYS A 44  ? 0.3971 0.8962 0.8371 0.0478  0.0769  0.1075  44  CYS A CB  
333  S SG  . CYS A 44  ? 0.3485 0.7934 0.7779 0.0470  0.0857  0.1037  44  CYS A SG  
334  N N   . THR A 45  ? 0.5452 1.1399 1.0041 0.0687  0.0697  0.1229  45  THR A N   
335  C CA  . THR A 45  ? 0.6240 1.2694 1.0900 0.0672  0.0615  0.1243  45  THR A CA  
336  C C   . THR A 45  ? 0.6737 1.3347 1.1445 0.0392  0.0557  0.1099  45  THR A C   
337  O O   . THR A 45  ? 0.6546 1.2844 1.1208 0.0241  0.0575  0.1008  45  THR A O   
338  C CB  . THR A 45  ? 0.6173 1.2976 1.0937 0.0773  0.0644  0.1294  45  THR A CB  
339  O OG1 . THR A 45  ? 0.6686 1.3538 1.1559 0.0592  0.0687  0.1178  45  THR A OG1 
340  C CG2 . THR A 45  ? 0.5774 1.2342 1.0466 0.1035  0.0724  0.1431  45  THR A CG2 
341  N N   . SER A 46  ? 0.7560 1.4656 1.2345 0.0321  0.0491  0.1077  46  SER A N   
342  C CA  . SER A 46  ? 0.7875 1.5120 1.2680 0.0043  0.0441  0.0941  46  SER A CA  
343  C C   . SER A 46  ? 0.7930 1.5031 1.2799 -0.0159 0.0520  0.0827  46  SER A C   
344  O O   . SER A 46  ? 0.7223 1.4104 1.2035 -0.0368 0.0527  0.0724  46  SER A O   
345  C CB  . SER A 46  ? 0.7225 1.5043 1.2081 0.0016  0.0357  0.0942  46  SER A CB  
346  O OG  . SER A 46  ? 0.7723 1.5626 1.2534 -0.0231 0.0295  0.0825  46  SER A OG  
347  N N   . GLU A 47  ? 0.7812 1.5031 1.2785 -0.0098 0.0588  0.0847  47  GLU A N   
348  C CA  . GLU A 47  ? 0.7571 1.4666 1.2602 -0.0282 0.0676  0.0748  47  GLU A CA  
349  C C   . GLU A 47  ? 0.7104 1.3662 1.2056 -0.0245 0.0763  0.0742  47  GLU A C   
350  O O   . GLU A 47  ? 0.7589 1.3905 1.2505 -0.0441 0.0817  0.0645  47  GLU A O   
351  C CB  . GLU A 47  ? 0.8251 1.5698 1.3424 -0.0238 0.0718  0.0768  47  GLU A CB  
352  C CG  . GLU A 47  ? 0.8765 1.6234 1.3955 0.0066  0.0743  0.0903  47  GLU A CG  
353  C CD  . GLU A 47  ? 0.9404 1.7301 1.4603 0.0232  0.0655  0.1002  47  GLU A CD  
354  O OE1 . GLU A 47  ? 0.9455 1.7583 1.4629 0.0125  0.0566  0.0966  47  GLU A OE1 
355  O OE2 . GLU A 47  ? 0.9546 1.7548 1.4759 0.0471  0.0680  0.1119  47  GLU A OE2 
356  N N   . ASP A 48  ? 0.6474 1.2828 1.1372 0.0001  0.0782  0.0846  48  ASP A N   
357  C CA  . ASP A 48  ? 0.5896 1.1766 1.0697 0.0051  0.0861  0.0844  48  ASP A CA  
358  C C   . ASP A 48  ? 0.5102 1.0648 0.9798 -0.0132 0.0867  0.0750  48  ASP A C   
359  O O   . ASP A 48  ? 0.4352 0.9585 0.8985 -0.0183 0.0946  0.0708  48  ASP A O   
360  C CB  . ASP A 48  ? 0.5962 1.1614 1.0668 0.0317  0.0859  0.0974  48  ASP A CB  
361  C CG  . ASP A 48  ? 0.6451 1.2269 1.1215 0.0520  0.0899  0.1076  48  ASP A CG  
362  O OD1 . ASP A 48  ? 0.6128 1.2064 1.0982 0.0472  0.0957  0.1036  48  ASP A OD1 
363  O OD2 . ASP A 48  ? 0.6265 1.2077 1.0971 0.0730  0.0881  0.1199  48  ASP A OD2 
364  N N   . MET A 49  ? 0.5762 1.1393 1.0427 -0.0234 0.0785  0.0720  49  MET A N   
365  C CA  . MET A 49  ? 0.4786 1.0097 0.9328 -0.0370 0.0781  0.0653  49  MET A CA  
366  C C   . MET A 49  ? 0.4045 0.9234 0.8574 -0.0614 0.0857  0.0541  49  MET A C   
367  O O   . MET A 49  ? 0.3643 0.8478 0.8045 -0.0693 0.0893  0.0501  49  MET A O   
368  C CB  . MET A 49  ? 0.4996 1.0466 0.9504 -0.0427 0.0674  0.0648  49  MET A CB  
369  C CG  . MET A 49  ? 0.4901 1.0363 0.9365 -0.0201 0.0613  0.0760  49  MET A CG  
370  S SD  . MET A 49  ? 0.5771 1.0699 1.0099 -0.0046 0.0659  0.0814  49  MET A SD  
371  C CE  . MET A 49  ? 0.4087 0.8688 0.8335 -0.0266 0.0714  0.0693  49  MET A CE  
372  N N   . LEU A 50  ? 0.4304 0.9760 0.8945 -0.0732 0.0890  0.0503  50  LEU A N   
373  C CA  . LEU A 50  ? 0.4743 1.0057 0.9350 -0.0982 0.0970  0.0413  50  LEU A CA  
374  C C   . LEU A 50  ? 0.4865 0.9756 0.9375 -0.0965 0.1084  0.0395  50  LEU A C   
375  O O   . LEU A 50  ? 0.4985 0.9560 0.9363 -0.1119 0.1132  0.0347  50  LEU A O   
376  C CB  . LEU A 50  ? 0.4339 1.0022 0.9080 -0.1080 0.0991  0.0395  50  LEU A CB  
377  C CG  . LEU A 50  ? 0.6074 1.1737 1.0733 -0.1381 0.1026  0.0307  50  LEU A CG  
378  C CD1 . LEU A 50  ? 0.5961 1.2035 1.0759 -0.1455 0.1047  0.0289  50  LEU A CD1 
379  C CD2 . LEU A 50  ? 0.6818 1.1982 1.1322 -0.1484 0.1139  0.0285  50  LEU A CD2 
380  N N   . ASN A 51  ? 0.4733 0.9606 0.9265 -0.0774 0.1123  0.0447  51  ASN A N   
381  C CA  . ASN A 51  ? 0.4811 0.9282 0.9182 -0.0693 0.1187  0.0477  51  ASN A CA  
382  C C   . ASN A 51  ? 0.4167 0.8620 0.8575 -0.0413 0.1176  0.0583  51  ASN A C   
383  O O   . ASN A 51  ? 0.3765 0.8321 0.8241 -0.0356 0.1234  0.0600  51  ASN A O   
384  C CB  . ASN A 51  ? 0.5143 0.9504 0.9453 -0.0861 0.1303  0.0421  51  ASN A CB  
385  C CG  . ASN A 51  ? 0.6337 1.1064 1.0850 -0.0962 0.1356  0.0361  51  ASN A CG  
386  O OD1 . ASN A 51  ? 0.6146 1.1181 1.0823 -0.0810 0.1308  0.0416  51  ASN A OD1 
387  N ND2 . ASN A 51  ? 0.7094 1.1688 1.1608 -0.1178 0.1452  0.0309  51  ASN A ND2 
388  N N   . PRO A 52  ? 0.3880 0.8187 0.8237 -0.0242 0.1112  0.0655  52  PRO A N   
389  C CA  . PRO A 52  ? 0.3861 0.8151 0.8241 0.0005  0.1112  0.0757  52  PRO A CA  
390  C C   . PRO A 52  ? 0.3570 0.7451 0.7851 0.0106  0.1191  0.0783  52  PRO A C   
391  O O   . PRO A 52  ? 0.3356 0.6875 0.7523 0.0058  0.1218  0.0748  52  PRO A O   
392  C CB  . PRO A 52  ? 0.3835 0.8074 0.8170 0.0114  0.1030  0.0814  52  PRO A CB  
393  C CG  . PRO A 52  ? 0.3675 0.7685 0.7910 -0.0034 0.1008  0.0746  52  PRO A CG  
394  C CD  . PRO A 52  ? 0.4168 0.8272 0.8426 -0.0272 0.1054  0.0647  52  PRO A CD  
395  N N   . ASN A 53  ? 0.3578 0.7510 0.7902 0.0251  0.1232  0.0843  53  ASN A N   
396  C CA  . ASN A 53  ? 0.4099 0.7619 0.8317 0.0385  0.1295  0.0880  53  ASN A CA  
397  C C   . ASN A 53  ? 0.3869 0.7239 0.8029 0.0566  0.1264  0.0965  53  ASN A C   
398  O O   . ASN A 53  ? 0.3466 0.7003 0.7674 0.0704  0.1269  0.1046  53  ASN A O   
399  C CB  . ASN A 53  ? 0.3905 0.7515 0.8179 0.0430  0.1371  0.0894  53  ASN A CB  
400  C CG  . ASN A 53  ? 0.4460 0.7622 0.8612 0.0514  0.1444  0.0901  53  ASN A CG  
401  O OD1 . ASN A 53  ? 0.4493 0.7347 0.8543 0.0633  0.1440  0.0938  53  ASN A OD1 
402  N ND2 . ASN A 53  ? 0.4491 0.7599 0.8640 0.0433  0.1515  0.0855  53  ASN A ND2 
403  N N   . TYR A 54  ? 0.3619 0.6669 0.7667 0.0564  0.1243  0.0948  54  TYR A N   
404  C CA  . TYR A 54  ? 0.3892 0.6820 0.7882 0.0699  0.1219  0.1020  54  TYR A CA  
405  C C   . TYR A 54  ? 0.4366 0.7045 0.8289 0.0856  0.1296  0.1085  54  TYR A C   
406  O O   . TYR A 54  ? 0.4289 0.7029 0.8212 0.0991  0.1306  0.1180  54  TYR A O   
407  C CB  . TYR A 54  ? 0.3961 0.6626 0.7855 0.0641  0.1183  0.0971  54  TYR A CB  
408  C CG  . TYR A 54  ? 0.3780 0.6704 0.7726 0.0521  0.1099  0.0938  54  TYR A CG  
409  C CD1 . TYR A 54  ? 0.3400 0.6583 0.7393 0.0575  0.1040  0.1002  54  TYR A CD1 
410  C CD2 . TYR A 54  ? 0.3281 0.6178 0.7219 0.0352  0.1089  0.0845  54  TYR A CD2 
411  C CE1 . TYR A 54  ? 0.3253 0.6676 0.7287 0.0458  0.0961  0.0965  54  TYR A CE1 
412  C CE2 . TYR A 54  ? 0.3446 0.6563 0.7419 0.0227  0.1019  0.0811  54  TYR A CE2 
413  C CZ  . TYR A 54  ? 0.3259 0.6648 0.7283 0.0278  0.0950  0.0867  54  TYR A CZ  
414  O OH  . TYR A 54  ? 0.3063 0.6675 0.7115 0.0149  0.0878  0.0826  54  TYR A OH  
415  N N   . GLU A 55  ? 0.4454 0.6831 0.8304 0.0842  0.1358  0.1037  55  GLU A N   
416  C CA  . GLU A 55  ? 0.4751 0.6895 0.8531 0.0969  0.1437  0.1086  55  GLU A CA  
417  C C   . GLU A 55  ? 0.3845 0.6289 0.7718 0.1077  0.1461  0.1176  55  GLU A C   
418  O O   . GLU A 55  ? 0.4185 0.6598 0.8025 0.1214  0.1490  0.1269  55  GLU A O   
419  C CB  . GLU A 55  ? 0.4980 0.6840 0.8685 0.0924  0.1494  0.1012  55  GLU A CB  
420  C CG  . GLU A 55  ? 0.5889 0.7478 0.9498 0.0829  0.1469  0.0916  55  GLU A CG  
421  C CD  . GLU A 55  ? 0.6641 0.8428 1.0317 0.0696  0.1409  0.0863  55  GLU A CD  
422  O OE1 . GLU A 55  ? 0.6534 0.8691 1.0331 0.0664  0.1374  0.0897  55  GLU A OE1 
423  O OE2 . GLU A 55  ? 0.6763 0.8344 1.0364 0.0622  0.1400  0.0782  55  GLU A OE2 
424  N N   . ASP A 56  ? 0.4055 0.6814 0.8045 0.1013  0.1454  0.1149  56  ASP A N   
425  C CA  . ASP A 56  ? 0.4455 0.7564 0.8552 0.1110  0.1470  0.1222  56  ASP A CA  
426  C C   . ASP A 56  ? 0.4352 0.7726 0.8495 0.1189  0.1412  0.1300  56  ASP A C   
427  O O   . ASP A 56  ? 0.4157 0.7655 0.8313 0.1348  0.1442  0.1400  56  ASP A O   
428  C CB  . ASP A 56  ? 0.4825 0.8286 0.9059 0.0989  0.1467  0.1158  56  ASP A CB  
429  C CG  . ASP A 56  ? 0.4728 0.7977 0.8923 0.0954  0.1546  0.1111  56  ASP A CG  
430  O OD1 . ASP A 56  ? 0.4631 0.7453 0.8690 0.1010  0.1592  0.1112  56  ASP A OD1 
431  O OD2 . ASP A 56  ? 0.4776 0.8298 0.9075 0.0856  0.1565  0.1064  56  ASP A OD2 
432  N N   . LEU A 57  ? 0.4153 0.7640 0.8318 0.1082  0.1330  0.1258  57  LEU A N   
433  C CA  . LEU A 57  ? 0.4071 0.7843 0.8280 0.1150  0.1269  0.1330  57  LEU A CA  
434  C C   . LEU A 57  ? 0.3924 0.7406 0.8004 0.1316  0.1307  0.1435  57  LEU A C   
435  O O   . LEU A 57  ? 0.4044 0.7699 0.8129 0.1468  0.1317  0.1547  57  LEU A O   
436  C CB  . LEU A 57  ? 0.4076 0.8018 0.8327 0.0984  0.1176  0.1252  57  LEU A CB  
437  C CG  . LEU A 57  ? 0.4487 0.8899 0.8897 0.0845  0.1137  0.1183  57  LEU A CG  
438  C CD1 . LEU A 57  ? 0.4201 0.8753 0.8636 0.0660  0.1056  0.1098  57  LEU A CD1 
439  C CD2 . LEU A 57  ? 0.3817 0.8636 0.8327 0.0977  0.1126  0.1270  57  LEU A CD2 
440  N N   . LEU A 58  ? 0.4284 0.7322 0.8241 0.1289  0.1342  0.1402  58  LEU A N   
441  C CA  . LEU A 58  ? 0.4695 0.7420 0.8524 0.1413  0.1401  0.1484  58  LEU A CA  
442  C C   . LEU A 58  ? 0.4615 0.7193 0.8387 0.1565  0.1510  0.1567  58  LEU A C   
443  O O   . LEU A 58  ? 0.4856 0.7324 0.8544 0.1708  0.1571  0.1676  58  LEU A O   
444  C CB  . LEU A 58  ? 0.4200 0.6525 0.7928 0.1312  0.1408  0.1399  58  LEU A CB  
445  C CG  . LEU A 58  ? 0.4705 0.6695 0.8306 0.1395  0.1478  0.1457  58  LEU A CG  
446  C CD1 . LEU A 58  ? 0.4770 0.6964 0.8384 0.1480  0.1446  0.1558  58  LEU A CD1 
447  C CD2 . LEU A 58  ? 0.4243 0.5917 0.7771 0.1273  0.1470  0.1347  58  LEU A CD2 
448  N N   . ILE A 59  ? 0.4935 0.7501 0.8737 0.1541  0.1546  0.1522  59  ILE A N   
449  C CA  . ILE A 59  ? 0.4459 0.6907 0.8207 0.1687  0.1650  0.1600  59  ILE A CA  
450  C C   . ILE A 59  ? 0.4595 0.7394 0.8397 0.1847  0.1650  0.1725  59  ILE A C   
451  O O   . ILE A 59  ? 0.5340 0.7989 0.9041 0.2011  0.1740  0.1835  59  ILE A O   
452  C CB  . ILE A 59  ? 0.4422 0.6833 0.8203 0.1628  0.1681  0.1525  59  ILE A CB  
453  C CG1 . ILE A 59  ? 0.4333 0.6282 0.7990 0.1538  0.1720  0.1438  59  ILE A CG1 
454  C CG2 . ILE A 59  ? 0.4436 0.6926 0.8219 0.1787  0.1765  0.1615  59  ILE A CG2 
455  C CD1 . ILE A 59  ? 0.4727 0.6639 0.8409 0.1435  0.1722  0.1340  59  ILE A CD1 
456  N N   . ARG A 60  ? 0.4414 0.7680 0.8361 0.1799  0.1553  0.1710  60  ARG A N   
457  C CA  . ARG A 60  ? 0.4196 0.7843 0.8194 0.1953  0.1542  0.1824  60  ARG A CA  
458  C C   . ARG A 60  ? 0.5179 0.8761 0.9074 0.2066  0.1542  0.1931  60  ARG A C   
459  O O   . ARG A 60  ? 0.4639 0.8477 0.8529 0.2231  0.1551  0.2049  60  ARG A O   
460  C CB  . ARG A 60  ? 0.5149 0.9345 0.9336 0.1848  0.1440  0.1762  60  ARG A CB  
461  C CG  . ARG A 60  ? 0.6210 1.0642 1.0524 0.1803  0.1461  0.1705  60  ARG A CG  
462  C CD  . ARG A 60  ? 0.6768 1.1222 1.1168 0.1557  0.1418  0.1546  60  ARG A CD  
463  N NE  . ARG A 60  ? 0.7617 1.2322 1.2143 0.1494  0.1446  0.1488  60  ARG A NE  
464  C CZ  . ARG A 60  ? 0.7186 1.1662 1.1693 0.1404  0.1502  0.1411  60  ARG A CZ  
465  N NH1 . ARG A 60  ? 0.6424 1.0412 1.0787 0.1374  0.1532  0.1383  60  ARG A NH1 
466  N NH2 . ARG A 60  ? 0.6987 1.1739 1.1619 0.1343  0.1532  0.1362  60  ARG A NH2 
467  N N   . LYS A 61  ? 0.5165 0.8431 0.8975 0.1987  0.1535  0.1896  61  LYS A N   
468  C CA  . LYS A 61  ? 0.5671 0.8846 0.9376 0.2089  0.1551  0.1996  61  LYS A CA  
469  C C   . LYS A 61  ? 0.5863 0.8554 0.9389 0.2203  0.1698  0.2071  61  LYS A C   
470  O O   . LYS A 61  ? 0.5982 0.8319 0.9458 0.2131  0.1761  0.1998  61  LYS A O   
471  C CB  . LYS A 61  ? 0.5229 0.8362 0.8946 0.1938  0.1464  0.1918  61  LYS A CB  
472  C CG  . LYS A 61  ? 0.4920 0.8490 0.8789 0.1798  0.1325  0.1834  61  LYS A CG  
473  C CD  . LYS A 61  ? 0.4974 0.8988 0.8887 0.1907  0.1270  0.1929  61  LYS A CD  
474  C CE  . LYS A 61  ? 0.4385 0.8881 0.8471 0.1775  0.1165  0.1839  61  LYS A CE  
475  N NZ  . LYS A 61  ? 0.5417 1.0329 0.9527 0.1853  0.1094  0.1915  61  LYS A NZ  
476  N N   . SER A 62  ? 0.5582 0.8259 0.9001 0.2376  0.1759  0.2212  62  SER A N   
477  C CA  . SER A 62  ? 0.6247 0.8468 0.9474 0.2485  0.1916  0.2295  62  SER A CA  
478  C C   . SER A 62  ? 0.6665 0.8765 0.9814 0.2480  0.1917  0.2332  62  SER A C   
479  O O   . SER A 62  ? 0.6429 0.8808 0.9670 0.2405  0.1789  0.2300  62  SER A O   
480  C CB  . SER A 62  ? 0.6439 0.8701 0.9566 0.2719  0.2026  0.2444  62  SER A CB  
481  O OG  . SER A 62  ? 0.6666 0.9053 0.9871 0.2727  0.2028  0.2411  62  SER A OG  
482  N N   . ASN A 63  ? 0.6847 0.8518 0.9819 0.2554  0.2071  0.2395  63  ASN A N   
483  C CA  . ASN A 63  ? 0.6762 0.8257 0.9652 0.2537  0.2098  0.2421  63  ASN A CA  
484  C C   . ASN A 63  ? 0.6728 0.8577 0.9610 0.2673  0.2039  0.2545  63  ASN A C   
485  O O   . ASN A 63  ? 0.6721 0.8663 0.9636 0.2602  0.1959  0.2525  63  ASN A O   
486  C CB  . ASN A 63  ? 0.6693 0.7669 0.9383 0.2596  0.2302  0.2467  63  ASN A CB  
487  C CG  . ASN A 63  ? 0.6997 0.7612 0.9695 0.2405  0.2341  0.2312  63  ASN A CG  
488  O OD1 . ASN A 63  ? 0.6214 0.6909 0.9037 0.2231  0.2219  0.2182  63  ASN A OD1 
489  N ND2 . ASN A 63  ? 0.7766 0.7977 1.0313 0.2440  0.2518  0.2321  63  ASN A ND2 
490  N N   . HIS A 64  ? 0.6920 0.8983 0.9749 0.2874  0.2077  0.2675  64  HIS A N   
491  C CA  . HIS A 64  ? 0.6899 0.9284 0.9684 0.3027  0.2038  0.2804  64  HIS A CA  
492  C C   . HIS A 64  ? 0.6612 0.9569 0.9594 0.2944  0.1834  0.2744  64  HIS A C   
493  O O   . HIS A 64  ? 0.6366 0.9649 0.9324 0.3051  0.1780  0.2833  64  HIS A O   
494  C CB  . HIS A 64  ? 0.7046 0.9456 0.9674 0.3292  0.2164  0.2970  64  HIS A CB  
495  C CG  . HIS A 64  ? 0.7397 1.0025 1.0113 0.3338  0.2146  0.2959  64  HIS A CG  
496  N ND1 . HIS A 64  ? 0.7332 1.0478 1.0260 0.3265  0.1980  0.2889  64  HIS A ND1 
497  C CD2 . HIS A 64  ? 0.8072 1.0484 1.0684 0.3460  0.2284  0.3013  64  HIS A CD2 
498  C CE1 . HIS A 64  ? 0.7009 1.0255 0.9971 0.3337  0.2014  0.2900  64  HIS A CE1 
499  N NE2 . HIS A 64  ? 0.7746 1.0551 1.0517 0.3460  0.2193  0.2977  64  HIS A NE2 
500  N N   . ASN A 65  ? 0.6383 0.9475 0.9543 0.2759  0.1729  0.2595  65  ASN A N   
501  C CA  . ASN A 65  ? 0.5952 0.9527 0.9292 0.2630  0.1549  0.2508  65  ASN A CA  
502  C C   . ASN A 65  ? 0.5816 0.9330 0.9176 0.2477  0.1469  0.2433  65  ASN A C   
503  O O   . ASN A 65  ? 0.4963 0.8783 0.8463 0.2320  0.1329  0.2325  65  ASN A O   
504  C CB  . ASN A 65  ? 0.5749 0.9453 0.9252 0.2483  0.1490  0.2373  65  ASN A CB  
505  C CG  . ASN A 65  ? 0.6193 0.9898 0.9676 0.2621  0.1581  0.2434  65  ASN A CG  
506  O OD1 . ASN A 65  ? 0.6019 0.9524 0.9539 0.2539  0.1619  0.2352  65  ASN A OD1 
507  N ND2 . ASN A 65  ? 0.5862 0.9815 0.9284 0.2835  0.1614  0.2576  65  ASN A ND2 
508  N N   . PHE A 66  ? 0.5962 0.9073 0.9183 0.2507  0.1563  0.2478  66  PHE A N   
509  C CA  . PHE A 66  ? 0.5992 0.9014 0.9228 0.2364  0.1499  0.2405  66  PHE A CA  
510  C C   . PHE A 66  ? 0.5689 0.8653 0.8778 0.2514  0.1561  0.2546  66  PHE A C   
511  O O   . PHE A 66  ? 0.6471 0.9091 0.9400 0.2651  0.1724  0.2648  66  PHE A O   
512  C CB  . PHE A 66  ? 0.5529 0.8088 0.8753 0.2217  0.1560  0.2291  66  PHE A CB  
513  C CG  . PHE A 66  ? 0.5536 0.8154 0.8892 0.2052  0.1486  0.2140  66  PHE A CG  
514  C CD1 . PHE A 66  ? 0.5256 0.8138 0.8737 0.1884  0.1339  0.2023  66  PHE A CD1 
515  C CD2 . PHE A 66  ? 0.5565 0.7965 0.8903 0.2064  0.1573  0.2116  66  PHE A CD2 
516  C CE1 . PHE A 66  ? 0.5582 0.8498 0.9160 0.1738  0.1290  0.1889  66  PHE A CE1 
517  C CE2 . PHE A 66  ? 0.5738 0.8184 0.9180 0.1922  0.1514  0.1984  66  PHE A CE2 
518  C CZ  . PHE A 66  ? 0.5356 0.8055 0.8915 0.1760  0.1376  0.1872  66  PHE A CZ  
519  N N   . LEU A 67  ? 0.5286 0.8573 0.8414 0.2487  0.1442  0.2550  67  LEU A N   
520  C CA  . LEU A 67  ? 0.6315 0.9542 0.9298 0.2615  0.1494  0.2674  67  LEU A CA  
521  C C   . LEU A 67  ? 0.6399 0.9475 0.9409 0.2451  0.1443  0.2585  67  LEU A C   
522  O O   . LEU A 67  ? 0.5628 0.8997 0.8762 0.2302  0.1287  0.2481  67  LEU A O   
523  C CB  . LEU A 67  ? 0.6983 1.0717 0.9956 0.2747  0.1408  0.2769  67  LEU A CB  
524  C CG  . LEU A 67  ? 0.7914 1.1540 1.0730 0.2851  0.1459  0.2879  67  LEU A CG  
525  C CD1 . LEU A 67  ? 0.8763 1.1977 1.1368 0.3052  0.1673  0.3024  67  LEU A CD1 
526  C CD2 . LEU A 67  ? 0.8471 1.2618 1.1281 0.2926  0.1336  0.2937  67  LEU A CD2 
527  N N   . VAL A 68  ? 0.6893 0.9512 0.9783 0.2473  0.1584  0.2619  68  VAL A N   
528  C CA  . VAL A 68  ? 0.6713 0.9157 0.9619 0.2337  0.1563  0.2545  68  VAL A CA  
529  C C   . VAL A 68  ? 0.7338 0.9768 1.0098 0.2479  0.1622  0.2685  68  VAL A C   
530  O O   . VAL A 68  ? 0.7768 0.9967 1.0359 0.2656  0.1786  0.2821  68  VAL A O   
531  C CB  . VAL A 68  ? 0.6396 0.8342 0.9286 0.2232  0.1685  0.2457  68  VAL A CB  
532  C CG1 . VAL A 68  ? 0.5744 0.7506 0.8631 0.2125  0.1690  0.2400  68  VAL A CG1 
533  C CG2 . VAL A 68  ? 0.5511 0.7493 0.8534 0.2084  0.1610  0.2308  68  VAL A CG2 
534  N N   . GLN A 69  ? 0.6913 0.9574 0.9722 0.2401  0.1497  0.2651  69  GLN A N   
535  C CA  . GLN A 69  ? 0.7655 1.0358 1.0331 0.2529  0.1530  0.2778  69  GLN A CA  
536  C C   . GLN A 69  ? 0.7210 0.9754 0.9911 0.2394  0.1511  0.2706  69  GLN A C   
537  O O   . GLN A 69  ? 0.6322 0.9054 0.9164 0.2212  0.1360  0.2566  69  GLN A O   
538  C CB  . GLN A 69  ? 0.7671 1.0929 1.0370 0.2597  0.1380  0.2824  69  GLN A CB  
539  C CG  . GLN A 69  ? 0.8812 1.2157 1.1364 0.2847  0.1473  0.2992  69  GLN A CG  
540  C CD  . GLN A 69  ? 0.9382 1.3269 1.1923 0.2935  0.1343  0.3048  69  GLN A CD  
541  O OE1 . GLN A 69  ? 0.9489 1.3796 1.2141 0.2911  0.1225  0.3002  69  GLN A OE1 
542  N NE2 . GLN A 69  ? 0.9586 1.3475 1.1987 0.3032  0.1370  0.3144  69  GLN A NE2 
543  N N   . ALA A 70  ? 0.8064 1.0254 1.0618 0.2480  0.1673  0.2797  70  ALA A N   
544  C CA  . ALA A 70  ? 0.8338 1.0380 1.0895 0.2387  0.1680  0.2756  70  ALA A CA  
545  C C   . ALA A 70  ? 0.9086 1.1278 1.1492 0.2548  0.1690  0.2908  70  ALA A C   
546  O O   . ALA A 70  ? 0.9680 1.1576 1.1894 0.2704  0.1874  0.3041  70  ALA A O   
547  C CB  . ALA A 70  ? 0.7850 0.9339 1.0355 0.2340  0.1880  0.2723  70  ALA A CB  
548  N N   . GLY A 71  ? 0.8893 1.1535 1.1366 0.2507  0.1500  0.2882  71  GLY A N   
549  C CA  . GLY A 71  ? 0.8689 1.1560 1.1011 0.2681  0.1491  0.3028  71  GLY A CA  
550  C C   . GLY A 71  ? 0.9420 1.2400 1.1639 0.2879  0.1552  0.3147  71  GLY A C   
551  O O   . GLY A 71  ? 0.9612 1.2903 1.1941 0.2852  0.1444  0.3096  71  GLY A O   
552  N N   . ASN A 72  ? 1.0150 1.2873 1.2146 0.3084  0.1737  0.3306  72  ASN A N   
553  C CA  . ASN A 72  ? 1.0980 1.3761 1.2853 0.3293  0.1823  0.3425  72  ASN A CA  
554  C C   . ASN A 72  ? 1.1434 1.3722 1.3238 0.3326  0.2026  0.3438  72  ASN A C   
555  O O   . ASN A 72  ? 1.1423 1.3762 1.3157 0.3475  0.2087  0.3511  72  ASN A O   
556  C CB  . ASN A 72  ? 1.1792 1.4630 1.3424 0.3527  0.1907  0.3596  72  ASN A CB  
557  C CG  . ASN A 72  ? 1.2212 1.5451 1.3877 0.3485  0.1735  0.3581  72  ASN A CG  
558  O OD1 . ASN A 72  ? 1.1937 1.5582 1.3796 0.3327  0.1524  0.3459  72  ASN A OD1 
559  N ND2 . ASN A 72  ? 1.2750 1.5864 1.4211 0.3621  0.1833  0.3696  72  ASN A ND2 
560  N N   . VAL A 73  ? 1.1426 1.3256 1.3249 0.3187  0.2132  0.3360  73  VAL A N   
561  C CA  . VAL A 73  ? 1.1366 1.2725 1.3122 0.3190  0.2326  0.3348  73  VAL A CA  
562  C C   . VAL A 73  ? 1.0836 1.2390 1.2765 0.3116  0.2221  0.3257  73  VAL A C   
563  O O   . VAL A 73  ? 1.0378 1.2185 1.2526 0.2936  0.2038  0.3121  73  VAL A O   
564  C CB  . VAL A 73  ? 1.1445 1.2326 1.3209 0.3023  0.2444  0.3251  73  VAL A CB  
565  C CG1 . VAL A 73  ? 1.2044 1.2377 1.3635 0.3068  0.2706  0.3269  73  VAL A CG1 
566  C CG2 . VAL A 73  ? 1.1803 1.2644 1.3484 0.3031  0.2459  0.3299  73  VAL A CG2 
567  N N   . GLN A 74  ? 1.0690 1.2122 1.2508 0.3258  0.2343  0.3331  74  GLN A N   
568  C CA  . GLN A 74  ? 1.0675 1.2264 1.2634 0.3210  0.2268  0.3259  74  GLN A CA  
569  C C   . GLN A 74  ? 1.0361 1.1440 1.2305 0.3105  0.2423  0.3174  74  GLN A C   
570  O O   . GLN A 74  ? 0.9927 1.0629 1.1671 0.3225  0.2636  0.3251  74  GLN A O   
571  C CB  . GLN A 74  ? 1.1183 1.3031 1.3041 0.3442  0.2287  0.3393  74  GLN A CB  
572  C CG  . GLN A 74  ? 1.1568 1.3967 1.3441 0.3543  0.2131  0.3464  74  GLN A CG  
573  C CD  . GLN A 74  ? 1.1151 1.4082 1.3263 0.3429  0.1902  0.3360  74  GLN A CD  
574  O OE1 . GLN A 74  ? 1.0613 1.3865 1.2854 0.3300  0.1729  0.3282  74  GLN A OE1 
575  N NE2 . GLN A 74  ? 1.1007 1.4023 1.3171 0.3469  0.1909  0.3351  74  GLN A NE2 
576  N N   . LEU A 75  ? 0.9200 1.0271 1.1342 0.2880  0.2320  0.3006  75  LEU A N   
577  C CA  . LEU A 75  ? 0.9059 0.9707 1.1204 0.2764  0.2443  0.2903  75  LEU A CA  
578  C C   . LEU A 75  ? 0.9226 0.9972 1.1412 0.2807  0.2428  0.2894  75  LEU A C   
579  O O   . LEU A 75  ? 0.9144 1.0316 1.1487 0.2783  0.2247  0.2860  75  LEU A O   
580  C CB  . LEU A 75  ? 0.8247 0.8866 1.0575 0.2519  0.2339  0.2724  75  LEU A CB  
581  C CG  . LEU A 75  ? 0.7653 0.8178 0.9974 0.2447  0.2343  0.2705  75  LEU A CG  
582  C CD1 . LEU A 75  ? 0.8345 0.9364 1.0764 0.2458  0.2135  0.2731  75  LEU A CD1 
583  C CD2 . LEU A 75  ? 0.7348 0.7679 0.9798 0.2223  0.2328  0.2519  75  LEU A CD2 
584  N N   . ARG A 76  ? 0.8835 0.9190 1.0873 0.2869  0.2625  0.2921  76  ARG A N   
585  C CA  . ARG A 76  ? 0.8680 0.9082 1.0751 0.2903  0.2627  0.2905  76  ARG A CA  
586  C C   . ARG A 76  ? 0.8335 0.8631 1.0568 0.2676  0.2564  0.2718  76  ARG A C   
587  O O   . ARG A 76  ? 0.8046 0.8016 1.0274 0.2528  0.2636  0.2614  76  ARG A O   
588  C CB  . ARG A 76  ? 0.8696 0.8737 1.0522 0.3073  0.2864  0.3013  76  ARG A CB  
589  C CG  . ARG A 76  ? 0.9488 0.9730 1.1314 0.3212  0.2849  0.3075  76  ARG A CG  
590  C CD  . ARG A 76  ? 0.9722 1.0206 1.1407 0.3476  0.2875  0.3262  76  ARG A CD  
591  N NE  . ARG A 76  ? 1.0774 1.0825 1.2164 0.3643  0.3132  0.3374  76  ARG A NE  
592  C CZ  . ARG A 76  ? 1.0888 1.1035 1.2086 0.3900  0.3213  0.3546  76  ARG A CZ  
593  N NH1 . ARG A 76  ? 1.1098 1.1788 1.2376 0.4023  0.3052  0.3626  76  ARG A NH1 
594  N NH2 . ARG A 76  ? 1.0392 1.0083 1.1300 0.4036  0.3466  0.3632  76  ARG A NH2 
595  N N   . VAL A 77  ? 0.7662 0.8262 1.0042 0.2647  0.2427  0.2669  77  VAL A N   
596  C CA  . VAL A 77  ? 0.7491 0.8029 1.0011 0.2452  0.2360  0.2497  77  VAL A CA  
597  C C   . VAL A 77  ? 0.7651 0.7886 1.0073 0.2492  0.2511  0.2494  77  VAL A C   
598  O O   . VAL A 77  ? 0.7759 0.8082 1.0108 0.2662  0.2562  0.2605  77  VAL A O   
599  C CB  . VAL A 77  ? 0.7190 0.8205 0.9910 0.2383  0.2140  0.2433  77  VAL A CB  
600  C CG1 . VAL A 77  ? 0.6468 0.7398 0.9302 0.2197  0.2084  0.2261  77  VAL A CG1 
601  C CG2 . VAL A 77  ? 0.6638 0.7954 0.9439 0.2334  0.1993  0.2429  77  VAL A CG2 
602  N N   . ILE A 78  ? 0.7360 0.7239 0.9770 0.2337  0.2589  0.2363  78  ILE A N   
603  C CA  . ILE A 78  ? 0.7713 0.7247 1.0002 0.2355  0.2756  0.2345  78  ILE A CA  
604  C C   . ILE A 78  ? 0.7680 0.7171 1.0084 0.2180  0.2692  0.2174  78  ILE A C   
605  O O   . ILE A 78  ? 0.7774 0.6976 1.0091 0.2157  0.2818  0.2125  78  ILE A O   
606  C CB  . ILE A 78  ? 0.7571 0.6643 0.9662 0.2361  0.2980  0.2361  78  ILE A CB  
607  C CG1 . ILE A 78  ? 0.8081 0.7009 1.0237 0.2161  0.2964  0.2221  78  ILE A CG1 
608  C CG2 . ILE A 78  ? 0.7317 0.6415 0.9248 0.2577  0.3067  0.2552  78  ILE A CG2 
609  C CD1 . ILE A 78  ? 0.8176 0.6632 1.0137 0.2137  0.3204  0.2204  78  ILE A CD1 
610  N N   . GLY A 79  ? 0.7190 0.6977 0.9774 0.2064  0.2497  0.2082  79  GLY A N   
611  C CA  . GLY A 79  ? 0.6713 0.6496 0.9394 0.1911  0.2421  0.1925  79  GLY A CA  
612  C C   . GLY A 79  ? 0.6795 0.6900 0.9640 0.1799  0.2218  0.1843  79  GLY A C   
613  O O   . GLY A 79  ? 0.6717 0.6918 0.9590 0.1778  0.2162  0.1857  79  GLY A O   
614  N N   . HIS A 80  ? 0.6601 0.6872 0.9540 0.1732  0.2114  0.1760  80  HIS A N   
615  C CA  . HIS A 80  ? 0.5854 0.6426 0.8928 0.1627  0.1936  0.1680  80  HIS A CA  
616  C C   . HIS A 80  ? 0.5971 0.6470 0.9080 0.1489  0.1889  0.1527  80  HIS A C   
617  O O   . HIS A 80  ? 0.5612 0.5996 0.8687 0.1511  0.1952  0.1514  80  HIS A O   
618  C CB  . HIS A 80  ? 0.5491 0.6484 0.8651 0.1721  0.1839  0.1771  80  HIS A CB  
619  C CG  . HIS A 80  ? 0.5791 0.6874 0.8967 0.1799  0.1868  0.1804  80  HIS A CG  
620  N ND1 . HIS A 80  ? 0.6063 0.7118 0.9158 0.1977  0.1976  0.1941  80  HIS A ND1 
621  C CD2 . HIS A 80  ? 0.5223 0.6438 0.8481 0.1731  0.1806  0.1724  80  HIS A CD2 
622  C CE1 . HIS A 80  ? 0.5881 0.7056 0.9020 0.2014  0.1975  0.1939  80  HIS A CE1 
623  N NE2 . HIS A 80  ? 0.5514 0.6786 0.8755 0.1863  0.1874  0.1809  80  HIS A NE2 
624  N N   . SER A 81  ? 0.5121 0.5693 0.8286 0.1356  0.1778  0.1414  81  SER A N   
625  C CA  . SER A 81  ? 0.5003 0.5486 0.8172 0.1230  0.1736  0.1267  81  SER A CA  
626  C C   . SER A 81  ? 0.5377 0.6099 0.8625 0.1136  0.1589  0.1198  81  SER A C   
627  O O   . SER A 81  ? 0.5048 0.5933 0.8333 0.1141  0.1530  0.1238  81  SER A O   
628  C CB  . SER A 81  ? 0.5353 0.5494 0.8435 0.1156  0.1821  0.1171  81  SER A CB  
629  O OG  . SER A 81  ? 0.6218 0.6320 0.9298 0.1027  0.1749  0.1017  81  SER A OG  
630  N N   . MET A 82  ? 0.4707 0.5444 0.7968 0.1055  0.1539  0.1098  82  MET A N   
631  C CA  . MET A 82  ? 0.4255 0.5197 0.7575 0.0967  0.1422  0.1033  82  MET A CA  
632  C C   . MET A 82  ? 0.4779 0.5512 0.8028 0.0862  0.1406  0.0890  82  MET A C   
633  O O   . MET A 82  ? 0.5552 0.6147 0.8754 0.0842  0.1440  0.0829  82  MET A O   
634  C CB  . MET A 82  ? 0.4236 0.5415 0.7635 0.0971  0.1390  0.1052  82  MET A CB  
635  C CG  . MET A 82  ? 0.4341 0.5613 0.7770 0.0853  0.1312  0.0952  82  MET A CG  
636  S SD  . MET A 82  ? 0.4566 0.6280 0.8138 0.0841  0.1256  0.1004  82  MET A SD  
637  C CE  . MET A 82  ? 0.4702 0.6379 0.8286 0.0899  0.1337  0.1024  82  MET A CE  
638  N N   . GLN A 83  ? 0.4165 0.4893 0.7399 0.0802  0.1352  0.0834  83  GLN A N   
639  C CA  . GLN A 83  ? 0.4505 0.5083 0.7666 0.0716  0.1326  0.0695  83  GLN A CA  
640  C C   . GLN A 83  ? 0.3983 0.4733 0.7177 0.0654  0.1232  0.0652  83  GLN A C   
641  O O   . GLN A 83  ? 0.3671 0.4560 0.6902 0.0636  0.1176  0.0672  83  GLN A O   
642  C CB  . GLN A 83  ? 0.4748 0.5173 0.7859 0.0698  0.1354  0.0651  83  GLN A CB  
643  C CG  . GLN A 83  ? 0.4751 0.5096 0.7789 0.0616  0.1306  0.0500  83  GLN A CG  
644  C CD  . GLN A 83  ? 0.5216 0.5441 0.8221 0.0590  0.1343  0.0441  83  GLN A CD  
645  O OE1 . GLN A 83  ? 0.5550 0.5747 0.8593 0.0625  0.1405  0.0521  83  GLN A OE1 
646  N NE2 . GLN A 83  ? 0.5582 0.5744 0.8512 0.0533  0.1313  0.0300  83  GLN A NE2 
647  N N   . ASN A 84  ? 0.4235 0.4970 0.7415 0.0619  0.1225  0.0594  84  ASN A N   
648  C CA  . ASN A 84  ? 0.3659 0.4530 0.6874 0.0553  0.1166  0.0555  84  ASN A CA  
649  C C   . ASN A 84  ? 0.3987 0.5160 0.7322 0.0551  0.1125  0.0650  84  ASN A C   
650  O O   . ASN A 84  ? 0.3214 0.4518 0.6614 0.0604  0.1151  0.0737  84  ASN A O   
651  C CB  . ASN A 84  ? 0.4179 0.4940 0.7312 0.0513  0.1129  0.0456  84  ASN A CB  
652  C CG  . ASN A 84  ? 0.4864 0.5387 0.7869 0.0518  0.1161  0.0355  84  ASN A CG  
653  O OD1 . ASN A 84  ? 0.4427 0.4873 0.7397 0.0523  0.1196  0.0331  84  ASN A OD1 
654  N ND2 . ASN A 84  ? 0.4857 0.5289 0.7792 0.0512  0.1148  0.0290  84  ASN A ND2 
655  N N   . CYS A 85  ? 0.3606 0.4919 0.6970 0.0494  0.1060  0.0637  85  CYS A N   
656  C CA  . CYS A 85  ? 0.3341 0.4980 0.6811 0.0475  0.1012  0.0714  85  CYS A CA  
657  C C   . CYS A 85  ? 0.3257 0.4977 0.6737 0.0551  0.0996  0.0802  85  CYS A C   
658  O O   . CYS A 85  ? 0.3322 0.5329 0.6873 0.0545  0.0944  0.0862  85  CYS A O   
659  C CB  . CYS A 85  ? 0.2739 0.4508 0.6235 0.0356  0.0958  0.0658  85  CYS A CB  
660  S SG  . CYS A 85  ? 0.2859 0.4538 0.6356 0.0269  0.1014  0.0580  85  CYS A SG  
661  N N   . VAL A 86  ? 0.3235 0.4722 0.6648 0.0623  0.1051  0.0816  86  VAL A N   
662  C CA  . VAL A 86  ? 0.3406 0.4911 0.6817 0.0695  0.1064  0.0900  86  VAL A CA  
663  C C   . VAL A 86  ? 0.3639 0.5078 0.7052 0.0806  0.1150  0.0994  86  VAL A C   
664  O O   . VAL A 86  ? 0.3851 0.5080 0.7219 0.0817  0.1217  0.0960  86  VAL A O   
665  C CB  . VAL A 86  ? 0.3585 0.4870 0.6919 0.0671  0.1077  0.0834  86  VAL A CB  
666  C CG1 . VAL A 86  ? 0.4037 0.5250 0.7362 0.0754  0.1142  0.0925  86  VAL A CG1 
667  C CG2 . VAL A 86  ? 0.3696 0.5109 0.7034 0.0591  0.0986  0.0777  86  VAL A CG2 
668  N N   . LEU A 87  ? 0.3701 0.5321 0.7155 0.0893  0.1153  0.1115  87  LEU A N   
669  C CA  . LEU A 87  ? 0.3954 0.5496 0.7390 0.1022  0.1249  0.1224  87  LEU A CA  
670  C C   . LEU A 87  ? 0.4643 0.5967 0.8012 0.1074  0.1326  0.1271  87  LEU A C   
671  O O   . LEU A 87  ? 0.4340 0.5741 0.7712 0.1056  0.1281  0.1281  87  LEU A O   
672  C CB  . LEU A 87  ? 0.3448 0.5342 0.6959 0.1106  0.1215  0.1334  87  LEU A CB  
673  C CG  . LEU A 87  ? 0.4843 0.6714 0.8322 0.1273  0.1307  0.1476  87  LEU A CG  
674  C CD1 . LEU A 87  ? 0.5140 0.6839 0.8596 0.1308  0.1392  0.1468  87  LEU A CD1 
675  C CD2 . LEU A 87  ? 0.4615 0.6905 0.8164 0.1350  0.1242  0.1572  87  LEU A CD2 
676  N N   . LYS A 88  ? 0.4755 0.5800 0.8060 0.1130  0.1450  0.1294  88  LYS A N   
677  C CA  . LYS A 88  ? 0.4653 0.5444 0.7888 0.1172  0.1564  0.1335  88  LYS A CA  
678  C C   . LYS A 88  ? 0.5292 0.6036 0.8481 0.1328  0.1678  0.1487  88  LYS A C   
679  O O   . LYS A 88  ? 0.5891 0.6538 0.9054 0.1365  0.1742  0.1494  88  LYS A O   
680  C CB  . LYS A 88  ? 0.4885 0.5357 0.8065 0.1077  0.1632  0.1203  88  LYS A CB  
681  C CG  . LYS A 88  ? 0.5337 0.5836 0.8532 0.0950  0.1537  0.1066  88  LYS A CG  
682  C CD  . LYS A 88  ? 0.5881 0.6207 0.9035 0.0851  0.1539  0.0908  88  LYS A CD  
683  C CE  . LYS A 88  ? 0.5943 0.6033 0.9045 0.0883  0.1669  0.0914  88  LYS A CE  
684  N NZ  . LYS A 88  ? 0.7116 0.7021 1.0168 0.0780  0.1693  0.0751  88  LYS A NZ  
685  N N   . LEU A 89  ? 0.4890 0.5708 0.8056 0.1428  0.1706  0.1611  89  LEU A N   
686  C CA  . LEU A 89  ? 0.5840 0.6602 0.8925 0.1599  0.1825  0.1771  89  LEU A CA  
687  C C   . LEU A 89  ? 0.6231 0.6609 0.9203 0.1616  0.1995  0.1793  89  LEU A C   
688  O O   . LEU A 89  ? 0.5899 0.6248 0.8866 0.1587  0.1995  0.1793  89  LEU A O   
689  C CB  . LEU A 89  ? 0.5439 0.6555 0.8549 0.1714  0.1750  0.1901  89  LEU A CB  
690  C CG  . LEU A 89  ? 0.5134 0.6663 0.8372 0.1650  0.1574  0.1847  89  LEU A CG  
691  C CD1 . LEU A 89  ? 0.4613 0.6498 0.7876 0.1721  0.1487  0.1940  89  LEU A CD1 
692  C CD2 . LEU A 89  ? 0.5636 0.7257 0.8904 0.1700  0.1585  0.1858  89  LEU A CD2 
693  N N   . LYS A 90  ? 0.6689 0.6772 0.9568 0.1651  0.2146  0.1800  90  LYS A N   
694  C CA  . LYS A 90  ? 0.6588 0.6291 0.9343 0.1657  0.2334  0.1814  90  LYS A CA  
695  C C   . LYS A 90  ? 0.7017 0.6707 0.9649 0.1850  0.2438  0.2006  90  LYS A C   
696  O O   . LYS A 90  ? 0.7251 0.7057 0.9841 0.1991  0.2451  0.2113  90  LYS A O   
697  C CB  . LYS A 90  ? 0.7262 0.6644 0.9950 0.1592  0.2461  0.1721  90  LYS A CB  
698  C CG  . LYS A 90  ? 0.8083 0.7064 1.0613 0.1606  0.2688  0.1740  90  LYS A CG  
699  C CD  . LYS A 90  ? 0.8082 0.6794 1.0609 0.1422  0.2762  0.1551  90  LYS A CD  
700  C CE  . LYS A 90  ? 0.8637 0.6939 1.0974 0.1443  0.3019  0.1567  90  LYS A CE  
701  N NZ  . LYS A 90  ? 0.9363 0.7428 1.1689 0.1256  0.3101  0.1367  90  LYS A NZ  
702  N N   . VAL A 91  ? 0.7171 0.6750 0.9743 0.1865  0.2505  0.2052  91  VAL A N   
703  C CA  . VAL A 91  ? 0.7600 0.7183 1.0035 0.2054  0.2594  0.2236  91  VAL A CA  
704  C C   . VAL A 91  ? 0.8181 0.7286 1.0418 0.2074  0.2848  0.2256  91  VAL A C   
705  O O   . VAL A 91  ? 0.8320 0.7129 1.0548 0.1924  0.2941  0.2116  91  VAL A O   
706  C CB  . VAL A 91  ? 0.7957 0.7837 1.0456 0.2076  0.2464  0.2292  91  VAL A CB  
707  C CG1 . VAL A 91  ? 0.7111 0.7483 0.9759 0.2088  0.2241  0.2294  91  VAL A CG1 
708  C CG2 . VAL A 91  ? 0.6979 0.6741 0.9556 0.1897  0.2442  0.2155  91  VAL A CG2 
709  N N   . ASP A 92  ? 0.7990 0.7030 1.0054 0.2259  0.2963  0.2423  92  ASP A N   
710  C CA  . ASP A 92  ? 0.9292 0.7861 1.1127 0.2292  0.3224  0.2444  92  ASP A CA  
711  C C   . ASP A 92  ? 0.9726 0.8087 1.1498 0.2222  0.3314  0.2418  92  ASP A C   
712  O O   . ASP A 92  ? 1.0170 0.8107 1.1777 0.2172  0.3530  0.2365  92  ASP A O   
713  C CB  . ASP A 92  ? 0.9311 0.7851 1.0943 0.2541  0.3339  0.2630  92  ASP A CB  
714  C CG  . ASP A 92  ? 0.9017 0.7833 1.0608 0.2711  0.3271  0.2793  92  ASP A CG  
715  O OD1 . ASP A 92  ? 0.9368 0.8389 1.1087 0.2630  0.3136  0.2763  92  ASP A OD1 
716  O OD2 . ASP A 92  ? 0.8650 0.7484 1.0071 0.2930  0.3355  0.2948  92  ASP A OD2 
717  N N   . THR A 93  ? 0.9185 0.7830 1.1076 0.2210  0.3161  0.2444  93  THR A N   
718  C CA  . THR A 93  ? 0.8321 0.6793 1.0152 0.2157  0.3239  0.2434  93  THR A CA  
719  C C   . THR A 93  ? 0.8310 0.6885 1.0358 0.1944  0.3106  0.2265  93  THR A C   
720  O O   . THR A 93  ? 0.7844 0.6806 1.0087 0.1912  0.2881  0.2236  93  THR A O   
721  C CB  . THR A 93  ? 0.8755 0.7458 1.0513 0.2339  0.3187  0.2616  93  THR A CB  
722  O OG1 . THR A 93  ? 0.9586 0.8164 1.1114 0.2552  0.3334  0.2768  93  THR A OG1 
723  C CG2 . THR A 93  ? 0.8873 0.7396 1.0570 0.2277  0.3261  0.2602  93  THR A CG2 
724  N N   . ALA A 94  ? 0.8184 0.6419 1.0187 0.1792  0.3248  0.2137  94  ALA A N   
725  C CA  . ALA A 94  ? 0.7499 0.5824 0.9692 0.1603  0.3140  0.1975  94  ALA A CA  
726  C C   . ALA A 94  ? 0.7554 0.6057 0.9777 0.1653  0.3059  0.2065  94  ALA A C   
727  O O   . ALA A 94  ? 0.7130 0.5423 0.9166 0.1726  0.3200  0.2166  94  ALA A O   
728  C CB  . ALA A 94  ? 0.7670 0.5604 0.9805 0.1407  0.3315  0.1785  94  ALA A CB  
729  N N   . ASN A 95  ? 0.7150 0.6064 0.9588 0.1621  0.2827  0.2025  95  ASN A N   
730  C CA  . ASN A 95  ? 0.6625 0.5771 0.9108 0.1666  0.2732  0.2094  95  ASN A CA  
731  C C   . ASN A 95  ? 0.6689 0.5517 0.9021 0.1512  0.2865  0.2019  95  ASN A C   
732  O O   . ASN A 95  ? 0.6972 0.5744 0.9356 0.1280  0.2851  0.1807  95  ASN A O   
733  C CB  . ASN A 95  ? 0.6067 0.5686 0.8760 0.1549  0.2464  0.1970  95  ASN A CB  
734  C CG  . ASN A 95  ? 0.6095 0.5960 0.8765 0.1495  0.2332  0.1975  95  ASN A CG  
735  O OD1 . ASN A 95  ? 0.6157 0.5993 0.8696 0.1622  0.2390  0.2134  95  ASN A OD1 
736  N ND2 . ASN A 95  ? 0.5986 0.6084 0.8768 0.1316  0.2160  0.1803  95  ASN A ND2 
737  N N   . PRO A 96  ? 0.6640 0.5282 0.8778 0.1629  0.2994  0.2181  96  PRO A N   
738  C CA  . PRO A 96  ? 0.6961 0.5324 0.8952 0.1461  0.3121  0.2104  96  PRO A CA  
739  C C   . PRO A 96  ? 0.7410 0.6110 0.9517 0.1267  0.2926  0.1950  96  PRO A C   
740  O O   . PRO A 96  ? 0.7674 0.6207 0.9730 0.1062  0.3004  0.1803  96  PRO A O   
741  C CB  . PRO A 96  ? 0.7650 0.5811 0.9407 0.1677  0.3269  0.2348  96  PRO A CB  
742  C CG  . PRO A 96  ? 0.7885 0.6429 0.9712 0.1931  0.3122  0.2522  96  PRO A CG  
743  C CD  . PRO A 96  ? 0.6784 0.5550 0.8822 0.1905  0.2997  0.2425  96  PRO A CD  
744  N N   . LYS A 97  ? 0.7146 0.6320 0.9404 0.1316  0.2678  0.1965  97  LYS A N   
745  C CA  . LYS A 97  ? 0.6660 0.6131 0.8999 0.1153  0.2499  0.1829  97  LYS A CA  
746  C C   . LYS A 97  ? 0.6380 0.5970 0.8878 0.0965  0.2389  0.1596  97  LYS A C   
747  O O   . LYS A 97  ? 0.6555 0.6410 0.9121 0.0853  0.2225  0.1481  97  LYS A O   
748  C CB  . LYS A 97  ? 0.6871 0.6777 0.9266 0.1278  0.2292  0.1943  97  LYS A CB  
749  C CG  . LYS A 97  ? 0.6806 0.6678 0.9036 0.1468  0.2366  0.2165  97  LYS A CG  
750  C CD  . LYS A 97  ? 0.8567 0.8356 1.0758 0.1713  0.2462  0.2355  97  LYS A CD  
751  C CE  . LYS A 97  ? 1.0086 0.9897 1.2104 0.1947  0.2519  0.2594  97  LYS A CE  
752  N NZ  . LYS A 97  ? 1.1315 1.1379 1.3380 0.2206  0.2468  0.2769  97  LYS A NZ  
753  N N   . THR A 98  ? 0.6314 0.5719 0.8860 0.0944  0.2472  0.1528  98  THR A N   
754  C CA  . THR A 98  ? 0.6014 0.5563 0.8705 0.0801  0.2354  0.1323  98  THR A CA  
755  C C   . THR A 98  ? 0.5718 0.5296 0.8398 0.0594  0.2334  0.1133  98  THR A C   
756  O O   . THR A 98  ? 0.5633 0.4933 0.8207 0.0496  0.2513  0.1085  98  THR A O   
757  C CB  . THR A 98  ? 0.6105 0.5394 0.8814 0.0797  0.2485  0.1270  98  THR A CB  
758  O OG1 . THR A 98  ? 0.6388 0.5654 0.9100 0.1007  0.2519  0.1455  98  THR A OG1 
759  C CG2 . THR A 98  ? 0.5288 0.4746 0.8135 0.0680  0.2356  0.1076  98  THR A CG2 
760  N N   . PRO A 99  ? 0.5630 0.5533 0.8397 0.0528  0.2131  0.1031  99  PRO A N   
761  C CA  . PRO A 99  ? 0.5122 0.5090 0.7882 0.0351  0.2105  0.0842  99  PRO A CA  
762  C C   . PRO A 99  ? 0.5481 0.5404 0.8312 0.0236  0.2122  0.0645  99  PRO A C   
763  O O   . PRO A 99  ? 0.5549 0.5420 0.8438 0.0293  0.2121  0.0654  99  PRO A O   
764  C CB  . PRO A 99  ? 0.5133 0.5456 0.7939 0.0367  0.1879  0.0831  99  PRO A CB  
765  C CG  . PRO A 99  ? 0.4519 0.4970 0.7416 0.0481  0.1767  0.0903  99  PRO A CG  
766  C CD  . PRO A 99  ? 0.5240 0.5463 0.8105 0.0612  0.1924  0.1075  99  PRO A CD  
767  N N   . LYS A 100 ? 0.5279 0.5251 0.8101 0.0077  0.2135  0.0464  100 LYS A N   
768  C CA  . LYS A 100 ? 0.6053 0.6113 0.8947 -0.0025 0.2090  0.0253  100 LYS A CA  
769  C C   . LYS A 100 ? 0.5296 0.5618 0.8264 0.0052  0.1873  0.0238  100 LYS A C   
770  O O   . LYS A 100 ? 0.5389 0.5925 0.8347 0.0077  0.1731  0.0257  100 LYS A O   
771  C CB  . LYS A 100 ? 0.6390 0.6552 0.9265 -0.0192 0.2118  0.0069  100 LYS A CB  
772  C CG  . LYS A 100 ? 0.7464 0.7598 1.0354 -0.0328 0.2172  -0.0154 100 LYS A CG  
773  C CD  . LYS A 100 ? 0.8118 0.8456 1.1072 -0.0274 0.1993  -0.0248 100 LYS A CD  
774  C CE  . LYS A 100 ? 0.8672 0.8902 1.1617 -0.0338 0.2041  -0.0397 100 LYS A CE  
775  N NZ  . LYS A 100 ? 0.7306 0.7713 1.0284 -0.0258 0.1866  -0.0454 100 LYS A NZ  
776  N N   . TYR A 101 ? 0.5276 0.5559 0.8301 0.0086  0.1856  0.0202  101 TYR A N   
777  C CA  . TYR A 101 ? 0.5382 0.5863 0.8456 0.0161  0.1676  0.0209  101 TYR A CA  
778  C C   . TYR A 101 ? 0.5373 0.5861 0.8460 0.0125  0.1635  0.0049  101 TYR A C   
779  O O   . TYR A 101 ? 0.4998 0.5324 0.8071 0.0063  0.1747  -0.0039 101 TYR A O   
780  C CB  . TYR A 101 ? 0.4508 0.4964 0.7614 0.0299  0.1659  0.0410  101 TYR A CB  
781  C CG  . TYR A 101 ? 0.4811 0.5068 0.7953 0.0352  0.1775  0.0453  101 TYR A CG  
782  C CD1 . TYR A 101 ? 0.4990 0.4979 0.8084 0.0370  0.1966  0.0532  101 TYR A CD1 
783  C CD2 . TYR A 101 ? 0.4566 0.4855 0.7723 0.0379  0.1683  0.0414  101 TYR A CD2 
784  C CE1 . TYR A 101 ? 0.5529 0.5312 0.8635 0.0429  0.2084  0.0573  101 TYR A CE1 
785  C CE2 . TYR A 101 ? 0.4552 0.4644 0.7706 0.0426  0.1777  0.0455  101 TYR A CE2 
786  C CZ  . TYR A 101 ? 0.5311 0.5159 0.8453 0.0457  0.1980  0.0532  101 TYR A CZ  
787  O OH  . TYR A 101 ? 0.6395 0.6026 0.9514 0.0510  0.2084  0.0574  101 TYR A OH  
788  N N   . LYS A 102 ? 0.4827 0.5482 0.7897 0.0163  0.1464  0.0015  102 LYS A N   
789  C CA  . LYS A 102 ? 0.4671 0.5324 0.7701 0.0169  0.1388  -0.0090 102 LYS A CA  
790  C C   . LYS A 102 ? 0.4341 0.5045 0.7373 0.0255  0.1279  0.0018  102 LYS A C   
791  O O   . LYS A 102 ? 0.4363 0.5172 0.7421 0.0292  0.1227  0.0129  102 LYS A O   
792  C CB  . LYS A 102 ? 0.4961 0.5774 0.7922 0.0124  0.1291  -0.0270 102 LYS A CB  
793  C CG  . LYS A 102 ? 0.6429 0.7273 0.9371 0.0020  0.1364  -0.0429 102 LYS A CG  
794  C CD  . LYS A 102 ? 0.7005 0.8058 0.9913 -0.0006 0.1293  -0.0491 102 LYS A CD  
795  C CE  . LYS A 102 ? 0.7886 0.9043 1.0758 -0.0111 0.1332  -0.0673 102 LYS A CE  
796  N NZ  . LYS A 102 ? 0.8738 1.0003 1.1611 -0.0174 0.1363  -0.0677 102 LYS A NZ  
797  N N   . PHE A 103 ? 0.4243 0.4883 0.7241 0.0275  0.1248  -0.0021 103 PHE A N   
798  C CA  . PHE A 103 ? 0.3797 0.4501 0.6767 0.0324  0.1138  0.0023  103 PHE A CA  
799  C C   . PHE A 103 ? 0.4362 0.5125 0.7238 0.0313  0.1053  -0.0125 103 PHE A C   
800  O O   . PHE A 103 ? 0.5289 0.6004 0.8118 0.0288  0.1081  -0.0246 103 PHE A O   
801  C CB  . PHE A 103 ? 0.3615 0.4200 0.6600 0.0363  0.1176  0.0093  103 PHE A CB  
802  C CG  . PHE A 103 ? 0.3688 0.4234 0.6747 0.0414  0.1248  0.0260  103 PHE A CG  
803  C CD1 . PHE A 103 ? 0.3717 0.4350 0.6822 0.0431  0.1259  0.0354  103 PHE A CD1 
804  C CD2 . PHE A 103 ? 0.3140 0.3568 0.6212 0.0456  0.1312  0.0326  103 PHE A CD2 
805  C CE1 . PHE A 103 ? 0.3516 0.4124 0.6672 0.0504  0.1331  0.0518  103 PHE A CE1 
806  C CE2 . PHE A 103 ? 0.3642 0.4044 0.6765 0.0526  0.1382  0.0484  103 PHE A CE2 
807  C CZ  . PHE A 103 ? 0.4246 0.4739 0.7408 0.0558  0.1393  0.0583  103 PHE A CZ  
808  N N   . VAL A 104 ? 0.3782 0.4651 0.6628 0.0336  0.0957  -0.0114 104 VAL A N   
809  C CA  . VAL A 104 ? 0.3594 0.4519 0.6335 0.0351  0.0885  -0.0242 104 VAL A CA  
810  C C   . VAL A 104 ? 0.4179 0.5102 0.6897 0.0387  0.0824  -0.0201 104 VAL A C   
811  O O   . VAL A 104 ? 0.4541 0.5528 0.7340 0.0380  0.0806  -0.0091 104 VAL A O   
812  C CB  . VAL A 104 ? 0.4248 0.5306 0.6977 0.0333  0.0857  -0.0298 104 VAL A CB  
813  C CG1 . VAL A 104 ? 0.4002 0.5128 0.6631 0.0380  0.0769  -0.0375 104 VAL A CG1 
814  C CG2 . VAL A 104 ? 0.4316 0.5387 0.7034 0.0287  0.0916  -0.0408 104 VAL A CG2 
815  N N   . ARG A 105 ? 0.3841 0.4700 0.6448 0.0424  0.0800  -0.0289 105 ARG A N   
816  C CA  . ARG A 105 ? 0.4154 0.4976 0.6718 0.0454  0.0765  -0.0274 105 ARG A CA  
817  C C   . ARG A 105 ? 0.4129 0.4955 0.6493 0.0482  0.0687  -0.0362 105 ARG A C   
818  O O   . ARG A 105 ? 0.4830 0.5646 0.7088 0.0541  0.0683  -0.0479 105 ARG A O   
819  C CB  . ARG A 105 ? 0.4448 0.5137 0.6944 0.0483  0.0792  -0.0296 105 ARG A CB  
820  C CG  . ARG A 105 ? 0.4411 0.5010 0.6804 0.0498  0.0767  -0.0285 105 ARG A CG  
821  C CD  . ARG A 105 ? 0.4741 0.5231 0.7154 0.0520  0.0827  -0.0272 105 ARG A CD  
822  N NE  . ARG A 105 ? 0.4731 0.5116 0.7014 0.0496  0.0807  -0.0244 105 ARG A NE  
823  C CZ  . ARG A 105 ? 0.3834 0.4266 0.6218 0.0425  0.0818  -0.0144 105 ARG A CZ  
824  N NH1 . ARG A 105 ? 0.3234 0.3820 0.5845 0.0400  0.0843  -0.0049 105 ARG A NH1 
825  N NH2 . ARG A 105 ? 0.3970 0.4294 0.6213 0.0381  0.0812  -0.0141 105 ARG A NH2 
826  N N   . ILE A 106 ? 0.4228 0.5079 0.6529 0.0448  0.0627  -0.0310 106 ILE A N   
827  C CA  . ILE A 106 ? 0.3979 0.4824 0.6082 0.0481  0.0563  -0.0388 106 ILE A CA  
828  C C   . ILE A 106 ? 0.4451 0.5114 0.6331 0.0526  0.0543  -0.0428 106 ILE A C   
829  O O   . ILE A 106 ? 0.4222 0.4782 0.6109 0.0494  0.0568  -0.0375 106 ILE A O   
830  C CB  . ILE A 106 ? 0.4039 0.4975 0.6139 0.0427  0.0511  -0.0329 106 ILE A CB  
831  C CG1 . ILE A 106 ? 0.3933 0.4861 0.6087 0.0355  0.0498  -0.0217 106 ILE A CG1 
832  C CG2 . ILE A 106 ? 0.4058 0.5150 0.6320 0.0403  0.0539  -0.0308 106 ILE A CG2 
833  C CD1 . ILE A 106 ? 0.4592 0.5388 0.6522 0.0336  0.0451  -0.0246 106 ILE A CD1 
834  N N   . GLN A 107 ? 0.4287 0.4910 0.5955 0.0608  0.0508  -0.0523 107 GLN A N   
835  C CA  . GLN A 107 ? 0.4891 0.5309 0.6275 0.0683  0.0497  -0.0573 107 GLN A CA  
836  C C   . GLN A 107 ? 0.5089 0.5397 0.6327 0.0619  0.0461  -0.0528 107 GLN A C   
837  O O   . GLN A 107 ? 0.4417 0.4854 0.5719 0.0565  0.0421  -0.0501 107 GLN A O   
838  C CB  . GLN A 107 ? 0.5308 0.5771 0.6526 0.0819  0.0475  -0.0689 107 GLN A CB  
839  C CG  . GLN A 107 ? 0.5851 0.6420 0.7162 0.0884  0.0509  -0.0761 107 GLN A CG  
840  C CD  . GLN A 107 ? 0.6066 0.6442 0.7304 0.0919  0.0555  -0.0748 107 GLN A CD  
841  O OE1 . GLN A 107 ? 0.6160 0.6326 0.7125 0.1008  0.0556  -0.0768 107 GLN A OE1 
842  N NE2 . GLN A 107 ? 0.5482 0.5899 0.6944 0.0851  0.0603  -0.0707 107 GLN A NE2 
843  N N   . PRO A 108 ? 0.4967 0.5027 0.5991 0.0619  0.0482  -0.0528 108 PRO A N   
844  C CA  . PRO A 108 ? 0.5089 0.5001 0.5901 0.0564  0.0458  -0.0522 108 PRO A CA  
845  C C   . PRO A 108 ? 0.5582 0.5531 0.6237 0.0650  0.0411  -0.0583 108 PRO A C   
846  O O   . PRO A 108 ? 0.6085 0.6088 0.6678 0.0788  0.0406  -0.0653 108 PRO A O   
847  C CB  . PRO A 108 ? 0.5307 0.4890 0.5844 0.0596  0.0514  -0.0545 108 PRO A CB  
848  C CG  . PRO A 108 ? 0.5238 0.4815 0.5788 0.0726  0.0549  -0.0584 108 PRO A CG  
849  C CD  . PRO A 108 ? 0.5302 0.5179 0.6223 0.0681  0.0538  -0.0550 108 PRO A CD  
850  N N   . GLY A 109 ? 0.5210 0.5160 0.5807 0.0566  0.0374  -0.0559 109 GLY A N   
851  C CA  . GLY A 109 ? 0.5101 0.5095 0.5556 0.0637  0.0331  -0.0609 109 GLY A CA  
852  C C   . GLY A 109 ? 0.5009 0.5324 0.5722 0.0612  0.0292  -0.0588 109 GLY A C   
853  O O   . GLY A 109 ? 0.5044 0.5421 0.5671 0.0627  0.0253  -0.0609 109 GLY A O   
854  N N   . GLN A 110 ? 0.4597 0.5095 0.5606 0.0575  0.0312  -0.0547 110 GLN A N   
855  C CA  . GLN A 110 ? 0.4844 0.5603 0.6085 0.0540  0.0299  -0.0519 110 GLN A CA  
856  C C   . GLN A 110 ? 0.4766 0.5610 0.6128 0.0415  0.0274  -0.0417 110 GLN A C   
857  O O   . GLN A 110 ? 0.3910 0.4668 0.5255 0.0337  0.0272  -0.0366 110 GLN A O   
858  C CB  . GLN A 110 ? 0.4579 0.5457 0.6055 0.0549  0.0348  -0.0518 110 GLN A CB  
859  C CG  . GLN A 110 ? 0.5368 0.6277 0.6768 0.0671  0.0364  -0.0637 110 GLN A CG  
860  C CD  . GLN A 110 ? 0.6219 0.7193 0.7430 0.0763  0.0323  -0.0723 110 GLN A CD  
861  O OE1 . GLN A 110 ? 0.6375 0.7556 0.7688 0.0747  0.0316  -0.0747 110 GLN A OE1 
862  N NE2 . GLN A 110 ? 0.6481 0.7263 0.7400 0.0863  0.0305  -0.0766 110 GLN A NE2 
863  N N   . THR A 111 ? 0.4513 0.5548 0.5997 0.0397  0.0259  -0.0390 111 THR A N   
864  C CA  . THR A 111 ? 0.4080 0.5227 0.5653 0.0307  0.0230  -0.0296 111 THR A CA  
865  C C   . THR A 111 ? 0.3338 0.4654 0.5178 0.0283  0.0271  -0.0212 111 THR A C   
866  O O   . THR A 111 ? 0.3236 0.4586 0.5174 0.0323  0.0322  -0.0246 111 THR A O   
867  C CB  . THR A 111 ? 0.4064 0.5254 0.5485 0.0316  0.0181  -0.0327 111 THR A CB  
868  O OG1 . THR A 111 ? 0.3266 0.4573 0.4734 0.0380  0.0200  -0.0377 111 THR A OG1 
869  C CG2 . THR A 111 ? 0.3935 0.4912 0.5052 0.0344  0.0153  -0.0404 111 THR A CG2 
870  N N   . PHE A 112 ? 0.2758 0.4181 0.4701 0.0220  0.0255  -0.0104 112 PHE A N   
871  C CA  . PHE A 112 ? 0.3254 0.4810 0.5416 0.0215  0.0302  -0.0001 112 PHE A CA  
872  C C   . PHE A 112 ? 0.3140 0.4844 0.5329 0.0171  0.0257  0.0101  112 PHE A C   
873  O O   . PHE A 112 ? 0.3419 0.5127 0.5483 0.0122  0.0191  0.0084  112 PHE A O   
874  C CB  . PHE A 112 ? 0.3198 0.4711 0.5514 0.0223  0.0365  0.0041  112 PHE A CB  
875  C CG  . PHE A 112 ? 0.2854 0.4338 0.5158 0.0181  0.0339  0.0071  112 PHE A CG  
876  C CD1 . PHE A 112 ? 0.3178 0.4493 0.5341 0.0179  0.0332  -0.0018 112 PHE A CD1 
877  C CD2 . PHE A 112 ? 0.2666 0.4304 0.5102 0.0148  0.0332  0.0187  112 PHE A CD2 
878  C CE1 . PHE A 112 ? 0.3848 0.5126 0.5997 0.0120  0.0327  0.0004  112 PHE A CE1 
879  C CE2 . PHE A 112 ? 0.2327 0.3984 0.4775 0.0092  0.0316  0.0205  112 PHE A CE2 
880  C CZ  . PHE A 112 ? 0.3265 0.4734 0.5571 0.0066  0.0317  0.0112  112 PHE A CZ  
881  N N   . SER A 113 ? 0.1979 0.3798 0.4311 0.0190  0.0299  0.0201  113 SER A N   
882  C CA  . SER A 113 ? 0.2946 0.4939 0.5323 0.0178  0.0268  0.0318  113 SER A CA  
883  C C   . SER A 113 ? 0.2687 0.4766 0.5220 0.0188  0.0292  0.0424  113 SER A C   
884  O O   . SER A 113 ? 0.2827 0.4824 0.5470 0.0224  0.0368  0.0442  113 SER A O   
885  C CB  . SER A 113 ? 0.2811 0.4861 0.5226 0.0217  0.0316  0.0379  113 SER A CB  
886  O OG  . SER A 113 ? 0.3294 0.5319 0.5567 0.0206  0.0286  0.0287  113 SER A OG  
887  N N   . VAL A 114 ? 0.2525 0.4788 0.5063 0.0155  0.0227  0.0487  114 VAL A N   
888  C CA  . VAL A 114 ? 0.2228 0.4655 0.4915 0.0169  0.0236  0.0591  114 VAL A CA  
889  C C   . VAL A 114 ? 0.2462 0.5113 0.5204 0.0228  0.0227  0.0726  114 VAL A C   
890  O O   . VAL A 114 ? 0.2140 0.4911 0.4784 0.0196  0.0156  0.0720  114 VAL A O   
891  C CB  . VAL A 114 ? 0.2559 0.5063 0.5207 0.0069  0.0169  0.0538  114 VAL A CB  
892  C CG1 . VAL A 114 ? 0.2062 0.4817 0.4885 0.0089  0.0175  0.0651  114 VAL A CG1 
893  C CG2 . VAL A 114 ? 0.2561 0.4811 0.5128 0.0029  0.0192  0.0419  114 VAL A CG2 
894  N N   . LEU A 115 ? 0.2096 0.4797 0.4977 0.0324  0.0303  0.0849  115 LEU A N   
895  C CA  . LEU A 115 ? 0.2362 0.5283 0.5289 0.0412  0.0305  0.0999  115 LEU A CA  
896  C C   . LEU A 115 ? 0.2477 0.5667 0.5522 0.0422  0.0268  0.1064  115 LEU A C   
897  O O   . LEU A 115 ? 0.2101 0.5266 0.5267 0.0486  0.0339  0.1119  115 LEU A O   
898  C CB  . LEU A 115 ? 0.2598 0.5364 0.5563 0.0529  0.0435  0.1099  115 LEU A CB  
899  C CG  . LEU A 115 ? 0.2664 0.5623 0.5647 0.0656  0.0456  0.1275  115 LEU A CG  
900  C CD1 . LEU A 115 ? 0.2864 0.5916 0.5716 0.0639  0.0395  0.1279  115 LEU A CD1 
901  C CD2 . LEU A 115 ? 0.2968 0.5731 0.5987 0.0783  0.0613  0.1389  115 LEU A CD2 
902  N N   . ALA A 116 ? 0.2315 0.5770 0.5323 0.0346  0.0158  0.1041  116 ALA A N   
903  C CA  . ALA A 116 ? 0.2600 0.6383 0.5724 0.0331  0.0113  0.1084  116 ALA A CA  
904  C C   . ALA A 116 ? 0.2845 0.6877 0.6065 0.0502  0.0146  0.1265  116 ALA A C   
905  O O   . ALA A 116 ? 0.2427 0.6552 0.5579 0.0575  0.0130  0.1340  116 ALA A O   
906  C CB  . ALA A 116 ? 0.2111 0.6113 0.5150 0.0180  -0.0007 0.0991  116 ALA A CB  
907  N N   . CYS A 117 ? 0.2467 0.6516 0.5751 0.0564  0.0190  0.1309  117 CYS A N   
908  C CA  . CYS A 117 ? 0.2884 0.7028 0.6167 0.0741  0.0240  0.1461  117 CYS A CA  
909  C C   . CYS A 117 ? 0.2985 0.7434 0.6318 0.0737  0.0190  0.1468  117 CYS A C   
910  O O   . CYS A 117 ? 0.2856 0.7333 0.6251 0.0612  0.0164  0.1364  117 CYS A O   
911  C CB  . CYS A 117 ? 0.3254 0.7056 0.6553 0.0859  0.0383  0.1526  117 CYS A CB  
912  S SG  . CYS A 117 ? 0.3742 0.7208 0.6993 0.0882  0.0474  0.1531  117 CYS A SG  
913  N N   . TYR A 118 ? 0.3462 0.8142 0.6763 0.0881  0.0185  0.1596  118 TYR A N   
914  C CA  . TYR A 118 ? 0.3693 0.8705 0.7038 0.0915  0.0147  0.1623  118 TYR A CA  
915  C C   . TYR A 118 ? 0.4077 0.9076 0.7381 0.1154  0.0237  0.1801  118 TYR A C   
916  O O   . TYR A 118 ? 0.4148 0.9121 0.7355 0.1280  0.0265  0.1912  118 TYR A O   
917  C CB  . TYR A 118 ? 0.3413 0.8843 0.6731 0.0813  0.0014  0.1567  118 TYR A CB  
918  C CG  . TYR A 118 ? 0.3781 0.9184 0.7118 0.0569  -0.0056 0.1390  118 TYR A CG  
919  C CD1 . TYR A 118 ? 0.3581 0.9069 0.7002 0.0422  -0.0073 0.1280  118 TYR A CD1 
920  C CD2 . TYR A 118 ? 0.3540 0.8792 0.6802 0.0491  -0.0085 0.1337  118 TYR A CD2 
921  C CE1 . TYR A 118 ? 0.3012 0.8430 0.6425 0.0201  -0.0115 0.1127  118 TYR A CE1 
922  C CE2 . TYR A 118 ? 0.3578 0.8766 0.6833 0.0279  -0.0134 0.1182  118 TYR A CE2 
923  C CZ  . TYR A 118 ? 0.3368 0.8631 0.6690 0.0135  -0.0145 0.1081  118 TYR A CZ  
924  O OH  . TYR A 118 ? 0.3168 0.8344 0.6457 -0.0075 -0.0176 0.0937  118 TYR A OH  
925  N N   . ASN A 119 ? 0.3772 0.8755 0.7135 0.1220  0.0296  0.1831  119 ASN A N   
926  C CA  . ASN A 119 ? 0.4093 0.9052 0.7403 0.1451  0.0393  0.1999  119 ASN A CA  
927  C C   . ASN A 119 ? 0.4519 0.9050 0.7743 0.1568  0.0527  0.2095  119 ASN A C   
928  O O   . ASN A 119 ? 0.4473 0.8979 0.7591 0.1763  0.0605  0.2252  119 ASN A O   
929  C CB  . ASN A 119 ? 0.4231 0.9604 0.7475 0.1566  0.0332  0.2094  119 ASN A CB  
930  C CG  . ASN A 119 ? 0.4989 1.0801 0.8322 0.1470  0.0227  0.2011  119 ASN A CG  
931  O OD1 . ASN A 119 ? 0.5459 1.1322 0.8870 0.1490  0.0259  0.2005  119 ASN A OD1 
932  N ND2 . ASN A 119 ? 0.5019 1.1150 0.8339 0.1355  0.0106  0.1938  119 ASN A ND2 
933  N N   . GLY A 120 ? 0.4009 0.8203 0.7267 0.1450  0.0563  0.1998  120 GLY A N   
934  C CA  . GLY A 120 ? 0.4064 0.7858 0.7256 0.1523  0.0694  0.2060  120 GLY A CA  
935  C C   . GLY A 120 ? 0.4510 0.8313 0.7624 0.1545  0.0681  0.2107  120 GLY A C   
936  O O   . GLY A 120 ? 0.4474 0.7970 0.7523 0.1635  0.0812  0.2187  120 GLY A O   
937  N N   . SER A 121 ? 0.4476 0.8609 0.7589 0.1460  0.0538  0.2055  121 SER A N   
938  C CA  . SER A 121 ? 0.4834 0.9010 0.7863 0.1481  0.0515  0.2098  121 SER A CA  
939  C C   . SER A 121 ? 0.4363 0.8554 0.7432 0.1274  0.0415  0.1936  121 SER A C   
940  O O   . SER A 121 ? 0.3914 0.8352 0.7025 0.1134  0.0290  0.1822  121 SER A O   
941  C CB  . SER A 121 ? 0.4226 0.8787 0.7169 0.1591  0.0442  0.2197  121 SER A CB  
942  O OG  . SER A 121 ? 0.5735 1.0241 0.8601 0.1812  0.0557  0.2366  121 SER A OG  
943  N N   . PRO A 122 ? 0.4302 0.8236 0.7353 0.1247  0.0474  0.1917  122 PRO A N   
944  C CA  . PRO A 122 ? 0.3939 0.7890 0.7006 0.1064  0.0382  0.1764  122 PRO A CA  
945  C C   . PRO A 122 ? 0.4297 0.8614 0.7303 0.1011  0.0236  0.1744  122 PRO A C   
946  O O   . PRO A 122 ? 0.4875 0.9364 0.7799 0.1132  0.0227  0.1863  122 PRO A O   
947  C CB  . PRO A 122 ? 0.4415 0.7987 0.7386 0.1062  0.0485  0.1751  122 PRO A CB  
948  C CG  . PRO A 122 ? 0.5003 0.8425 0.7944 0.1257  0.0637  0.1928  122 PRO A CG  
949  C CD  . PRO A 122 ? 0.4491 0.8153 0.7484 0.1398  0.0631  0.2049  122 PRO A CD  
950  N N   . SER A 123 ? 0.4143 0.8566 0.7173 0.0826  0.0128  0.1589  123 SER A N   
951  C CA  . SER A 123 ? 0.4520 0.9265 0.7483 0.0733  -0.0010 0.1534  123 SER A CA  
952  C C   . SER A 123 ? 0.4207 0.8774 0.7040 0.0590  -0.0059 0.1399  123 SER A C   
953  O O   . SER A 123 ? 0.4295 0.9038 0.7019 0.0571  -0.0136 0.1396  123 SER A O   
954  C CB  . SER A 123 ? 0.4457 0.9425 0.7472 0.0611  -0.0089 0.1440  123 SER A CB  
955  O OG  . SER A 123 ? 0.4923 1.0114 0.7875 0.0450  -0.0209 0.1327  123 SER A OG  
956  N N   . GLY A 124 ? 0.3074 0.7275 0.5881 0.0498  -0.0015 0.1281  124 GLY A N   
957  C CA  . GLY A 124 ? 0.2835 0.6836 0.5483 0.0380  -0.0056 0.1144  124 GLY A CA  
958  C C   . GLY A 124 ? 0.3030 0.6654 0.5671 0.0326  0.0010  0.1037  124 GLY A C   
959  O O   . GLY A 124 ? 0.2355 0.5891 0.5112 0.0345  0.0069  0.1046  124 GLY A O   
960  N N   . VAL A 125 ? 0.2757 0.6175 0.5254 0.0272  0.0002  0.0937  125 VAL A N   
961  C CA  . VAL A 125 ? 0.2516 0.5613 0.4984 0.0234  0.0056  0.0826  125 VAL A CA  
962  C C   . VAL A 125 ? 0.2426 0.5430 0.4723 0.0120  -0.0020 0.0671  125 VAL A C   
963  O O   . VAL A 125 ? 0.2598 0.5707 0.4773 0.0088  -0.0087 0.0653  125 VAL A O   
964  C CB  . VAL A 125 ? 0.2622 0.5534 0.5084 0.0313  0.0157  0.0863  125 VAL A CB  
965  C CG1 . VAL A 125 ? 0.2947 0.5903 0.5269 0.0312  0.0124  0.0859  125 VAL A CG1 
966  C CG2 . VAL A 125 ? 0.2818 0.5463 0.5275 0.0281  0.0213  0.0745  125 VAL A CG2 
967  N N   . TYR A 126 ? 0.2837 0.5632 0.5108 0.0069  -0.0004 0.0561  126 TYR A N   
968  C CA  . TYR A 126 ? 0.2958 0.5596 0.5033 -0.0014 -0.0053 0.0416  126 TYR A CA  
969  C C   . TYR A 126 ? 0.3146 0.5515 0.5201 0.0002  0.0003  0.0326  126 TYR A C   
970  O O   . TYR A 126 ? 0.2859 0.5186 0.5061 0.0046  0.0069  0.0367  126 TYR A O   
971  C CB  . TYR A 126 ? 0.3046 0.5796 0.5054 -0.0132 -0.0127 0.0371  126 TYR A CB  
972  C CG  . TYR A 126 ? 0.3318 0.6144 0.5479 -0.0165 -0.0105 0.0403  126 TYR A CG  
973  C CD1 . TYR A 126 ? 0.3672 0.6268 0.5790 -0.0211 -0.0071 0.0315  126 TYR A CD1 
974  C CD2 . TYR A 126 ? 0.3224 0.6361 0.5565 -0.0135 -0.0114 0.0524  126 TYR A CD2 
975  C CE1 . TYR A 126 ? 0.3220 0.5888 0.5478 -0.0243 -0.0043 0.0344  126 TYR A CE1 
976  C CE2 . TYR A 126 ? 0.3440 0.6676 0.5928 -0.0159 -0.0091 0.0552  126 TYR A CE2 
977  C CZ  . TYR A 126 ? 0.3270 0.6263 0.5720 -0.0220 -0.0053 0.0459  126 TYR A CZ  
978  O OH  . TYR A 126 ? 0.3407 0.6495 0.5997 -0.0249 -0.0024 0.0483  126 TYR A OH  
979  N N   . GLN A 127 ? 0.3220 0.5407 0.5075 -0.0028 -0.0021 0.0202  127 GLN A N   
980  C CA  . GLN A 127 ? 0.3593 0.5545 0.5392 0.0009  0.0025  0.0110  127 GLN A CA  
981  C C   . GLN A 127 ? 0.3796 0.5594 0.5480 -0.0059 0.0012  0.0037  127 GLN A C   
982  O O   . GLN A 127 ? 0.3911 0.5711 0.5456 -0.0146 -0.0037 0.0003  127 GLN A O   
983  C CB  . GLN A 127 ? 0.2974 0.4829 0.4614 0.0059  0.0022  0.0025  127 GLN A CB  
984  C CG  . GLN A 127 ? 0.4243 0.5939 0.5862 0.0127  0.0073  -0.0059 127 GLN A CG  
985  C CD  . GLN A 127 ? 0.4214 0.5986 0.6004 0.0180  0.0139  -0.0027 127 GLN A CD  
986  O OE1 . GLN A 127 ? 0.3647 0.5535 0.5606 0.0173  0.0172  0.0081  127 GLN A OE1 
987  N NE2 . GLN A 127 ? 0.4294 0.6001 0.6028 0.0236  0.0167  -0.0126 127 GLN A NE2 
988  N N   . CYS A 128 ? 0.3569 0.5227 0.5301 -0.0027 0.0066  0.0010  128 CYS A N   
989  C CA  A CYS A 128 ? 0.3752 0.5235 0.5379 -0.0082 0.0077  -0.0049 128 CYS A CA  
990  C CA  B CYS A 128 ? 0.3757 0.5222 0.5346 -0.0082 0.0071  -0.0061 128 CYS A CA  
991  C C   . CYS A 128 ? 0.4168 0.5413 0.5690 0.0005  0.0123  -0.0133 128 CYS A C   
992  O O   . CYS A 128 ? 0.3773 0.5052 0.5398 0.0091  0.0155  -0.0130 128 CYS A O   
993  C CB  A CYS A 128 ? 0.3476 0.5080 0.5306 -0.0130 0.0103  0.0028  128 CYS A CB  
994  C CB  B CYS A 128 ? 0.3699 0.5285 0.5439 -0.0165 0.0079  0.0002  128 CYS A CB  
995  S SG  A CYS A 128 ? 0.4073 0.5997 0.6018 -0.0240 0.0048  0.0112  128 CYS A SG  
996  S SG  B CYS A 128 ? 0.3439 0.5096 0.5449 -0.0082 0.0147  0.0085  128 CYS A SG  
997  N N   . ALA A 129 ? 0.3921 0.4933 0.5245 -0.0022 0.0137  -0.0204 129 ALA A N   
998  C CA  . ALA A 129 ? 0.4348 0.5140 0.5560 0.0072  0.0184  -0.0275 129 ALA A CA  
999  C C   . ALA A 129 ? 0.4055 0.4761 0.5333 0.0031  0.0233  -0.0255 129 ALA A C   
1000 O O   . ALA A 129 ? 0.3789 0.4491 0.5053 -0.0087 0.0232  -0.0235 129 ALA A O   
1001 C CB  . ALA A 129 ? 0.4561 0.5098 0.5428 0.0113  0.0177  -0.0373 129 ALA A CB  
1002 N N   . MET A 130 ? 0.3788 0.4441 0.5136 0.0121  0.0279  -0.0268 130 MET A N   
1003 C CA  . MET A 130 ? 0.4018 0.4537 0.5368 0.0098  0.0332  -0.0265 130 MET A CA  
1004 C C   . MET A 130 ? 0.4092 0.4285 0.5095 0.0110  0.0353  -0.0350 130 MET A C   
1005 O O   . MET A 130 ? 0.4653 0.4698 0.5471 0.0237  0.0361  -0.0419 130 MET A O   
1006 C CB  . MET A 130 ? 0.4482 0.5040 0.5996 0.0193  0.0376  -0.0260 130 MET A CB  
1007 C CG  . MET A 130 ? 0.4261 0.4675 0.5769 0.0193  0.0437  -0.0261 130 MET A CG  
1008 S SD  . MET A 130 ? 0.4977 0.5546 0.6684 0.0045  0.0447  -0.0160 130 MET A SD  
1009 C CE  . MET A 130 ? 0.3481 0.4357 0.5525 0.0081  0.0441  -0.0062 130 MET A CE  
1010 N N   . ARG A 131 ? 0.4177 0.4263 0.5069 -0.0023 0.0366  -0.0349 131 ARG A N   
1011 C CA  . ARG A 131 ? 0.4871 0.4589 0.5396 -0.0025 0.0408  -0.0425 131 ARG A CA  
1012 C C   . ARG A 131 ? 0.5312 0.4800 0.5725 0.0094  0.0476  -0.0454 131 ARG A C   
1013 O O   . ARG A 131 ? 0.4604 0.4218 0.5243 0.0123  0.0497  -0.0415 131 ARG A O   
1014 C CB  . ARG A 131 ? 0.4812 0.4455 0.5261 -0.0222 0.0434  -0.0426 131 ARG A CB  
1015 C CG  . ARG A 131 ? 0.5093 0.5006 0.5668 -0.0363 0.0368  -0.0398 131 ARG A CG  
1016 C CD  . ARG A 131 ? 0.5506 0.5327 0.5853 -0.0339 0.0325  -0.0451 131 ARG A CD  
1017 N NE  . ARG A 131 ? 0.6054 0.5435 0.5990 -0.0296 0.0383  -0.0537 131 ARG A NE  
1018 C CZ  . ARG A 131 ? 0.6205 0.5444 0.5907 -0.0185 0.0363  -0.0587 131 ARG A CZ  
1019 N NH1 . ARG A 131 ? 0.5422 0.4928 0.5267 -0.0128 0.0286  -0.0565 131 ARG A NH1 
1020 N NH2 . ARG A 131 ? 0.5631 0.4445 0.4934 -0.0121 0.0429  -0.0656 131 ARG A NH2 
1021 N N   . PRO A 132 ? 0.5379 0.4514 0.5421 0.0171  0.0519  -0.0522 132 PRO A N   
1022 C CA  . PRO A 132 ? 0.5793 0.4690 0.5690 0.0286  0.0590  -0.0544 132 PRO A CA  
1023 C C   . PRO A 132 ? 0.5873 0.4741 0.5891 0.0164  0.0653  -0.0502 132 PRO A C   
1024 O O   . PRO A 132 ? 0.5888 0.4709 0.5943 0.0255  0.0696  -0.0496 132 PRO A O   
1025 C CB  . PRO A 132 ? 0.6456 0.4938 0.5882 0.0362  0.0637  -0.0610 132 PRO A CB  
1026 C CG  . PRO A 132 ? 0.6756 0.5333 0.6127 0.0379  0.0570  -0.0635 132 PRO A CG  
1027 C CD  . PRO A 132 ? 0.6219 0.5146 0.5938 0.0188  0.0508  -0.0579 132 PRO A CD  
1028 N N   . ASN A 133 ? 0.5745 0.4680 0.5844 -0.0039 0.0657  -0.0475 133 ASN A N   
1029 C CA  . ASN A 133 ? 0.5387 0.4334 0.5610 -0.0165 0.0720  -0.0439 133 ASN A CA  
1030 C C   . ASN A 133 ? 0.4816 0.4193 0.5482 -0.0207 0.0676  -0.0358 133 ASN A C   
1031 O O   . ASN A 133 ? 0.4581 0.4073 0.5406 -0.0333 0.0713  -0.0319 133 ASN A O   
1032 C CB  . ASN A 133 ? 0.5476 0.4250 0.5509 -0.0373 0.0768  -0.0470 133 ASN A CB  
1033 C CG  . ASN A 133 ? 0.5735 0.4815 0.5928 -0.0523 0.0687  -0.0459 133 ASN A CG  
1034 O OD1 . ASN A 133 ? 0.4398 0.3799 0.4834 -0.0460 0.0599  -0.0416 133 ASN A OD1 
1035 N ND2 . ASN A 133 ? 0.5532 0.4500 0.5566 -0.0723 0.0723  -0.0503 133 ASN A ND2 
1036 N N   . PHE A 134 ? 0.4271 0.3885 0.5128 -0.0101 0.0608  -0.0333 134 PHE A N   
1037 C CA  . PHE A 134 ? 0.4236 0.4194 0.5470 -0.0096 0.0584  -0.0253 134 PHE A CA  
1038 C C   . PHE A 134 ? 0.4144 0.4405 0.5594 -0.0245 0.0547  -0.0188 134 PHE A C   
1039 O O   . PHE A 134 ? 0.4371 0.4887 0.6108 -0.0249 0.0552  -0.0110 134 PHE A O   
1040 C CB  . PHE A 134 ? 0.4768 0.4668 0.6092 -0.0044 0.0655  -0.0234 134 PHE A CB  
1041 C CG  . PHE A 134 ? 0.4819 0.4557 0.6024 0.0133  0.0671  -0.0288 134 PHE A CG  
1042 C CD1 . PHE A 134 ? 0.4626 0.4543 0.5987 0.0231  0.0632  -0.0288 134 PHE A CD1 
1043 C CD2 . PHE A 134 ? 0.4923 0.4331 0.5828 0.0199  0.0728  -0.0348 134 PHE A CD2 
1044 C CE1 . PHE A 134 ? 0.5312 0.5136 0.6573 0.0382  0.0644  -0.0355 134 PHE A CE1 
1045 C CE2 . PHE A 134 ? 0.5301 0.4609 0.6089 0.0376  0.0736  -0.0402 134 PHE A CE2 
1046 C CZ  . PHE A 134 ? 0.5123 0.4664 0.6100 0.0462  0.0688  -0.0412 134 PHE A CZ  
1047 N N   . THR A 135 ? 0.4492 0.4749 0.5804 -0.0355 0.0509  -0.0218 135 THR A N   
1048 C CA  . THR A 135 ? 0.4404 0.5001 0.5905 -0.0474 0.0452  -0.0166 135 THR A CA  
1049 C C   . THR A 135 ? 0.4159 0.4876 0.5658 -0.0419 0.0373  -0.0161 135 THR A C   
1050 O O   . THR A 135 ? 0.4593 0.5120 0.5918 -0.0313 0.0364  -0.0211 135 THR A O   
1051 C CB  . THR A 135 ? 0.4061 0.4601 0.5414 -0.0674 0.0472  -0.0217 135 THR A CB  
1052 O OG1 . THR A 135 ? 0.4058 0.4303 0.5072 -0.0696 0.0466  -0.0304 135 THR A OG1 
1053 C CG2 . THR A 135 ? 0.4636 0.4995 0.5938 -0.0732 0.0567  -0.0235 135 THR A CG2 
1054 N N   . ILE A 136 ? 0.3955 0.5013 0.5645 -0.0483 0.0317  -0.0098 136 ILE A N   
1055 C CA  . ILE A 136 ? 0.3898 0.5071 0.5562 -0.0454 0.0246  -0.0091 136 ILE A CA  
1056 C C   . ILE A 136 ? 0.4391 0.5754 0.6026 -0.0614 0.0195  -0.0101 136 ILE A C   
1057 O O   . ILE A 136 ? 0.3444 0.4982 0.5183 -0.0738 0.0206  -0.0085 136 ILE A O   
1058 C CB  . ILE A 136 ? 0.3419 0.4821 0.5333 -0.0329 0.0229  0.0003  136 ILE A CB  
1059 C CG1 . ILE A 136 ? 0.3457 0.5208 0.5649 -0.0361 0.0223  0.0112  136 ILE A CG1 
1060 C CG2 . ILE A 136 ? 0.3532 0.4749 0.5461 -0.0197 0.0284  -0.0012 136 ILE A CG2 
1061 C CD1 . ILE A 136 ? 0.2743 0.4676 0.5132 -0.0238 0.0220  0.0213  136 ILE A CD1 
1062 N N   . LYS A 137 ? 0.4344 0.5673 0.5818 -0.0619 0.0143  -0.0141 137 LYS A N   
1063 C CA  . LYS A 137 ? 0.4372 0.5860 0.5774 -0.0770 0.0090  -0.0170 137 LYS A CA  
1064 C C   . LYS A 137 ? 0.4373 0.6234 0.5985 -0.0705 0.0019  -0.0074 137 LYS A C   
1065 O O   . LYS A 137 ? 0.4659 0.6485 0.6187 -0.0627 -0.0016 -0.0077 137 LYS A O   
1066 C CB  . LYS A 137 ? 0.4901 0.6053 0.5939 -0.0814 0.0092  -0.0284 137 LYS A CB  
1067 C CG  . LYS A 137 ? 0.5652 0.6441 0.6438 -0.0920 0.0171  -0.0378 137 LYS A CG  
1068 C CD  . LYS A 137 ? 0.7104 0.7561 0.7503 -0.0970 0.0180  -0.0485 137 LYS A CD  
1069 C CE  . LYS A 137 ? 0.8774 0.8718 0.8847 -0.0956 0.0283  -0.0563 137 LYS A CE  
1070 N NZ  . LYS A 137 ? 0.8629 0.8218 0.8335 -0.0860 0.0293  -0.0635 137 LYS A NZ  
1071 N N   . GLY A 138 ? 0.4161 0.6376 0.6041 -0.0720 0.0008  0.0018  138 GLY A N   
1072 C CA  . GLY A 138 ? 0.3943 0.6486 0.6001 -0.0632 -0.0044 0.0126  138 GLY A CA  
1073 C C   . GLY A 138 ? 0.3769 0.6723 0.5920 -0.0738 -0.0108 0.0155  138 GLY A C   
1074 O O   . GLY A 138 ? 0.4284 0.7248 0.6294 -0.0911 -0.0131 0.0059  138 GLY A O   
1075 N N   . SER A 139 ? 0.3877 0.7176 0.6255 -0.0633 -0.0129 0.0286  139 SER A N   
1076 C CA  . SER A 139 ? 0.3505 0.7274 0.5993 -0.0688 -0.0198 0.0335  139 SER A CA  
1077 C C   . SER A 139 ? 0.2955 0.7005 0.5717 -0.0553 -0.0168 0.0479  139 SER A C   
1078 O O   . SER A 139 ? 0.2763 0.6838 0.5605 -0.0379 -0.0152 0.0595  139 SER A O   
1079 C CB  . SER A 139 ? 0.3761 0.7640 0.6152 -0.0649 -0.0268 0.0354  139 SER A CB  
1080 O OG  . SER A 139 ? 0.3310 0.7679 0.5803 -0.0684 -0.0339 0.0404  139 SER A OG  
1081 N N   . PHE A 140 ? 0.2499 0.6715 0.5387 -0.0630 -0.0144 0.0470  140 PHE A N   
1082 C CA  . PHE A 140 ? 0.3083 0.7552 0.6221 -0.0497 -0.0105 0.0602  140 PHE A CA  
1083 C C   . PHE A 140 ? 0.2995 0.7959 0.6265 -0.0606 -0.0148 0.0598  140 PHE A C   
1084 O O   . PHE A 140 ? 0.2499 0.7453 0.5706 -0.0813 -0.0148 0.0474  140 PHE A O   
1085 C CB  . PHE A 140 ? 0.2975 0.7126 0.6162 -0.0450 -0.0007 0.0599  140 PHE A CB  
1086 C CG  . PHE A 140 ? 0.2865 0.6565 0.5940 -0.0346 0.0042  0.0589  140 PHE A CG  
1087 C CD1 . PHE A 140 ? 0.2878 0.6557 0.6038 -0.0162 0.0076  0.0705  140 PHE A CD1 
1088 C CD2 . PHE A 140 ? 0.2984 0.6284 0.5866 -0.0430 0.0065  0.0462  140 PHE A CD2 
1089 C CE1 . PHE A 140 ? 0.2916 0.6218 0.5985 -0.0090 0.0126  0.0678  140 PHE A CE1 
1090 C CE2 . PHE A 140 ? 0.2976 0.5926 0.5768 -0.0331 0.0105  0.0443  140 PHE A CE2 
1091 C CZ  . PHE A 140 ? 0.3111 0.6079 0.6008 -0.0173 0.0134  0.0544  140 PHE A CZ  
1092 N N   . LEU A 141 ? 0.3036 0.8255 0.6369 -0.0455 -0.0173 0.0700  141 LEU A N   
1093 C CA  . LEU A 141 ? 0.3626 0.9192 0.7021 -0.0502 -0.0200 0.0687  141 LEU A CA  
1094 C C   . LEU A 141 ? 0.3494 0.9050 0.7028 -0.0356 -0.0125 0.0772  141 LEU A C   
1095 O O   . LEU A 141 ? 0.2834 0.8102 0.6400 -0.0220 -0.0052 0.0839  141 LEU A O   
1096 C CB  . LEU A 141 ? 0.3260 0.9171 0.6609 -0.0435 -0.0284 0.0739  141 LEU A CB  
1097 C CG  . LEU A 141 ? 0.4167 1.0089 0.7361 -0.0576 -0.0360 0.0650  141 LEU A CG  
1098 C CD1 . LEU A 141 ? 0.4086 1.0295 0.7226 -0.0452 -0.0431 0.0733  141 LEU A CD1 
1099 C CD2 . LEU A 141 ? 0.3404 0.9384 0.6520 -0.0868 -0.0386 0.0471  141 LEU A CD2 
1100 N N   . ASN A 142 ? 0.3520 0.9393 0.7126 -0.0395 -0.0140 0.0759  142 ASN A N   
1101 C CA  . ASN A 142 ? 0.3569 0.9504 0.7296 -0.0237 -0.0079 0.0849  142 ASN A CA  
1102 C C   . ASN A 142 ? 0.3652 0.9496 0.7363 0.0025  -0.0054 0.1006  142 ASN A C   
1103 O O   . ASN A 142 ? 0.3542 0.9514 0.7178 0.0096  -0.0109 0.1061  142 ASN A O   
1104 C CB  . ASN A 142 ? 0.3746 1.0135 0.7535 -0.0284 -0.0122 0.0832  142 ASN A CB  
1105 C CG  . ASN A 142 ? 0.5689 1.2122 0.9607 -0.0237 -0.0051 0.0853  142 ASN A CG  
1106 O OD1 . ASN A 142 ? 0.5878 1.2400 0.9849 -0.0024 -0.0022 0.0976  142 ASN A OD1 
1107 N ND2 . ASN A 142 ? 0.5453 1.1817 0.9405 -0.0439 -0.0016 0.0735  142 ASN A ND2 
1108 N N   . GLY A 143 ? 0.3414 0.9014 0.7176 0.0162  0.0037  0.1074  143 GLY A N   
1109 C CA  . GLY A 143 ? 0.3321 0.8761 0.7043 0.0393  0.0087  0.1218  143 GLY A CA  
1110 C C   . GLY A 143 ? 0.3192 0.8245 0.6836 0.0414  0.0121  0.1222  143 GLY A C   
1111 O O   . GLY A 143 ? 0.3357 0.8227 0.6962 0.0589  0.0184  0.1335  143 GLY A O   
1112 N N   . SER A 144 ? 0.3249 0.8162 0.6863 0.0243  0.0093  0.1104  144 SER A N   
1113 C CA  . SER A 144 ? 0.2629 0.7189 0.6178 0.0267  0.0129  0.1102  144 SER A CA  
1114 C C   . SER A 144 ? 0.3029 0.7222 0.6605 0.0315  0.0233  0.1095  144 SER A C   
1115 O O   . SER A 144 ? 0.2321 0.6215 0.5846 0.0352  0.0276  0.1094  144 SER A O   
1116 C CB  . SER A 144 ? 0.2915 0.7463 0.6403 0.0076  0.0063  0.0981  144 SER A CB  
1117 O OG  . SER A 144 ? 0.2607 0.7134 0.6126 -0.0096 0.0068  0.0869  144 SER A OG  
1118 N N   . CYS A 145 ? 0.2988 0.7207 0.6637 0.0311  0.0274  0.1083  145 CYS A N   
1119 C CA  . CYS A 145 ? 0.2893 0.6775 0.6552 0.0342  0.0367  0.1062  145 CYS A CA  
1120 C C   . CYS A 145 ? 0.2419 0.6036 0.6032 0.0515  0.0448  0.1156  145 CYS A C   
1121 O O   . CYS A 145 ? 0.2284 0.6012 0.5892 0.0654  0.0465  0.1274  145 CYS A O   
1122 C CB  . CYS A 145 ? 0.3130 0.7139 0.6873 0.0328  0.0397  0.1051  145 CYS A CB  
1123 S SG  . CYS A 145 ? 0.3915 0.8060 0.7695 0.0078  0.0355  0.0908  145 CYS A SG  
1124 N N   . GLY A 146 ? 0.2412 0.5673 0.5987 0.0503  0.0510  0.1101  146 GLY A N   
1125 C CA  . GLY A 146 ? 0.2854 0.5842 0.6376 0.0623  0.0594  0.1162  146 GLY A CA  
1126 C C   . GLY A 146 ? 0.2807 0.5735 0.6273 0.0620  0.0575  0.1165  146 GLY A C   
1127 O O   . GLY A 146 ? 0.2758 0.5446 0.6184 0.0695  0.0658  0.1200  146 GLY A O   
1128 N N   . SER A 147 ? 0.2487 0.5623 0.5948 0.0525  0.0476  0.1122  147 SER A N   
1129 C CA  . SER A 147 ? 0.2647 0.5706 0.6051 0.0502  0.0457  0.1099  147 SER A CA  
1130 C C   . SER A 147 ? 0.2268 0.5016 0.5642 0.0444  0.0500  0.0984  147 SER A C   
1131 O O   . SER A 147 ? 0.2342 0.5015 0.5732 0.0372  0.0499  0.0899  147 SER A O   
1132 C CB  . SER A 147 ? 0.2074 0.5416 0.5464 0.0397  0.0339  0.1063  147 SER A CB  
1133 O OG  . SER A 147 ? 0.2118 0.5782 0.5519 0.0447  0.0287  0.1153  147 SER A OG  
1134 N N   . VAL A 148 ? 0.2252 0.4824 0.5576 0.0474  0.0542  0.0974  148 VAL A N   
1135 C CA  . VAL A 148 ? 0.1951 0.4218 0.5208 0.0433  0.0586  0.0849  148 VAL A CA  
1136 C C   . VAL A 148 ? 0.1943 0.4137 0.5050 0.0361  0.0522  0.0744  148 VAL A C   
1137 O O   . VAL A 148 ? 0.1961 0.4276 0.5017 0.0363  0.0477  0.0786  148 VAL A O   
1138 C CB  . VAL A 148 ? 0.2234 0.4291 0.5520 0.0519  0.0715  0.0891  148 VAL A CB  
1139 C CG1 . VAL A 148 ? 0.2139 0.4196 0.5462 0.0596  0.0765  0.0984  148 VAL A CG1 
1140 C CG2 . VAL A 148 ? 0.2326 0.4386 0.5587 0.0572  0.0756  0.0968  148 VAL A CG2 
1141 N N   . GLY A 149 ? 0.1751 0.3754 0.4774 0.0307  0.0518  0.0607  149 GLY A N   
1142 C CA  . GLY A 149 ? 0.2431 0.4336 0.5303 0.0265  0.0475  0.0494  149 GLY A CA  
1143 C C   . GLY A 149 ? 0.3157 0.4890 0.6029 0.0297  0.0558  0.0435  149 GLY A C   
1144 O O   . GLY A 149 ? 0.2465 0.4096 0.5419 0.0328  0.0638  0.0436  149 GLY A O   
1145 N N   . PHE A 150 ? 0.2660 0.4377 0.5439 0.0284  0.0543  0.0377  150 PHE A N   
1146 C CA  . PHE A 150 ? 0.3094 0.4707 0.5892 0.0297  0.0631  0.0328  150 PHE A CA  
1147 C C   . PHE A 150 ? 0.3220 0.4844 0.5893 0.0270  0.0590  0.0218  150 PHE A C   
1148 O O   . PHE A 150 ? 0.3124 0.4830 0.5697 0.0255  0.0506  0.0216  150 PHE A O   
1149 C CB  . PHE A 150 ? 0.2848 0.4470 0.5735 0.0333  0.0723  0.0457  150 PHE A CB  
1150 C CG  . PHE A 150 ? 0.2972 0.4727 0.5813 0.0342  0.0679  0.0542  150 PHE A CG  
1151 C CD1 . PHE A 150 ? 0.3263 0.5182 0.6126 0.0366  0.0611  0.0650  150 PHE A CD1 
1152 C CD2 . PHE A 150 ? 0.2939 0.4683 0.5712 0.0321  0.0704  0.0510  150 PHE A CD2 
1153 C CE1 . PHE A 150 ? 0.3016 0.5080 0.5825 0.0378  0.0564  0.0724  150 PHE A CE1 
1154 C CE2 . PHE A 150 ? 0.3164 0.5029 0.5879 0.0334  0.0663  0.0591  150 PHE A CE2 
1155 C CZ  . PHE A 150 ? 0.3395 0.5417 0.6124 0.0367  0.0591  0.0698  150 PHE A CZ  
1156 N N   . ASN A 151 ? 0.3704 0.5260 0.6384 0.0263  0.0656  0.0121  151 ASN A N   
1157 C CA  . ASN A 151 ? 0.4049 0.5654 0.6644 0.0243  0.0645  0.0019  151 ASN A CA  
1158 C C   . ASN A 151 ? 0.4571 0.6157 0.7245 0.0213  0.0765  0.0033  151 ASN A C   
1159 O O   . ASN A 151 ? 0.4093 0.5578 0.6864 0.0209  0.0865  0.0067  151 ASN A O   
1160 C CB  . ASN A 151 ? 0.3631 0.5213 0.6142 0.0259  0.0610  -0.0140 151 ASN A CB  
1161 C CG  . ASN A 151 ? 0.3867 0.5428 0.6233 0.0287  0.0504  -0.0163 151 ASN A CG  
1162 O OD1 . ASN A 151 ? 0.3995 0.5467 0.6347 0.0302  0.0490  -0.0165 151 ASN A OD1 
1163 N ND2 . ASN A 151 ? 0.3885 0.5507 0.6124 0.0290  0.0441  -0.0188 151 ASN A ND2 
1164 N N   . ILE A 152 ? 0.4978 0.6644 0.7599 0.0187  0.0769  0.0009  152 ILE A N   
1165 C CA  . ILE A 152 ? 0.5584 0.7220 0.8254 0.0136  0.0896  0.0008  152 ILE A CA  
1166 C C   . ILE A 152 ? 0.7527 0.9265 1.0157 0.0092  0.0897  -0.0170 152 ILE A C   
1167 O O   . ILE A 152 ? 0.7204 0.9066 0.9738 0.0112  0.0806  -0.0225 152 ILE A O   
1168 C CB  . ILE A 152 ? 0.5903 0.7564 0.8542 0.0141  0.0918  0.0140  152 ILE A CB  
1169 C CG1 . ILE A 152 ? 0.5111 0.6731 0.7786 0.0205  0.0908  0.0318  152 ILE A CG1 
1170 C CG2 . ILE A 152 ? 0.6706 0.8288 0.9371 0.0077  0.1076  0.0135  152 ILE A CG2 
1171 C CD1 . ILE A 152 ? 0.5437 0.7028 0.8095 0.0227  0.0990  0.0464  152 ILE A CD1 
1172 N N   . ASP A 153 ? 1.1399 1.3103 1.4098 0.0035  0.1000  -0.0267 153 ASP A N   
1173 C CA  . ASP A 153 ? 1.1569 1.3432 1.4249 -0.0014 0.1009  -0.0445 153 ASP A CA  
1174 C C   . ASP A 153 ? 1.2212 1.4050 1.4946 -0.0127 0.1165  -0.0461 153 ASP A C   
1175 O O   . ASP A 153 ? 1.2092 1.3807 1.4897 -0.0192 0.1287  -0.0488 153 ASP A O   
1176 C CB  . ASP A 153 ? 1.2266 1.4177 1.4954 0.0009  0.0977  -0.0591 153 ASP A CB  
1177 C CG  . ASP A 153 ? 1.2955 1.4757 1.5731 -0.0064 0.1100  -0.0639 153 ASP A CG  
1178 O OD1 . ASP A 153 ? 1.2449 1.4062 1.5294 -0.0084 0.1196  -0.0519 153 ASP A OD1 
1179 O OD2 . ASP A 153 ? 1.3634 1.5515 1.6352 -0.0093 0.1084  -0.0787 153 ASP A OD2 
1180 N N   . TYR A 154 ? 1.2996 1.4929 1.5683 -0.0155 0.1172  -0.0446 154 TYR A N   
1181 C CA  . TYR A 154 ? 1.3542 1.5420 1.6257 -0.0271 0.1335  -0.0449 154 TYR A CA  
1182 C C   . TYR A 154 ? 1.3388 1.4984 1.6119 -0.0267 0.1452  -0.0274 154 TYR A C   
1183 O O   . TYR A 154 ? 1.3508 1.5045 1.6187 -0.0203 0.1431  -0.0110 154 TYR A O   
1184 C CB  . TYR A 154 ? 1.3568 1.5556 1.6326 -0.0373 0.1395  -0.0653 154 TYR A CB  
1185 C CG  . TYR A 154 ? 1.4876 1.7131 1.7562 -0.0312 0.1237  -0.0789 154 TYR A CG  
1186 C CD1 . TYR A 154 ? 1.4813 1.7234 1.7457 -0.0242 0.1151  -0.0767 154 TYR A CD1 
1187 C CD2 . TYR A 154 ? 1.4505 1.6825 1.7148 -0.0299 0.1174  -0.0926 154 TYR A CD2 
1188 C CE1 . TYR A 154 ? 1.4558 1.7176 1.7100 -0.0161 0.1017  -0.0875 154 TYR A CE1 
1189 C CE2 . TYR A 154 ? 1.4612 1.7140 1.7156 -0.0212 0.1037  -0.1025 154 TYR A CE2 
1190 C CZ  . TYR A 154 ? 1.5163 1.7822 1.7648 -0.0140 0.0963  -0.0997 154 TYR A CZ  
1191 O OH  . TYR A 154 ? 1.5572 1.8396 1.7929 -0.0039 0.0841  -0.1088 154 TYR A OH  
1192 N N   . ASP A 155 ? 1.1193 1.2615 1.3981 -0.0322 0.1576  -0.0301 155 ASP A N   
1193 C CA  . ASP A 155 ? 1.0593 1.1723 1.3370 -0.0301 0.1710  -0.0131 155 ASP A CA  
1194 C C   . ASP A 155 ? 0.8942 0.9946 1.1764 -0.0204 0.1675  -0.0050 155 ASP A C   
1195 O O   . ASP A 155 ? 0.7675 0.8450 1.0484 -0.0155 0.1778  0.0101  155 ASP A O   
1196 C CB  . ASP A 155 ? 1.0385 1.1331 1.3156 -0.0447 0.1931  -0.0199 155 ASP A CB  
1197 C CG  . ASP A 155 ? 0.9987 1.0938 1.2787 -0.0534 0.1944  -0.0390 155 ASP A CG  
1198 O OD1 . ASP A 155 ? 0.9480 1.0590 1.2323 -0.0473 0.1798  -0.0467 155 ASP A OD1 
1199 O OD2 . ASP A 155 ? 0.9627 1.0390 1.2368 -0.0659 0.2092  -0.0459 155 ASP A OD2 
1200 N N   . CYS A 156 ? 0.8429 0.9570 1.1291 -0.0164 0.1540  -0.0140 156 CYS A N   
1201 C CA  . CYS A 156 ? 0.7351 0.8384 1.0263 -0.0099 0.1525  -0.0104 156 CYS A CA  
1202 C C   . CYS A 156 ? 0.6153 0.7281 0.9059 0.0018  0.1361  -0.0005 156 CYS A C   
1203 O O   . CYS A 156 ? 0.5945 0.7247 0.8813 0.0034  0.1225  -0.0081 156 CYS A O   
1204 C CB  . CYS A 156 ? 0.7158 0.8255 1.0109 -0.0159 0.1524  -0.0303 156 CYS A CB  
1205 S SG  . CYS A 156 ? 0.7010 0.7951 0.9999 -0.0092 0.1523  -0.0276 156 CYS A SG  
1206 N N   . VAL A 157 ? 0.5189 0.6203 0.8122 0.0099  0.1382  0.0159  157 VAL A N   
1207 C CA  . VAL A 157 ? 0.4767 0.5887 0.7707 0.0187  0.1240  0.0241  157 VAL A CA  
1208 C C   . VAL A 157 ? 0.4520 0.5624 0.7502 0.0199  0.1198  0.0154  157 VAL A C   
1209 O O   . VAL A 157 ? 0.4599 0.5558 0.7636 0.0205  0.1297  0.0160  157 VAL A O   
1210 C CB  . VAL A 157 ? 0.4211 0.5280 0.7172 0.0276  0.1274  0.0448  157 VAL A CB  
1211 C CG1 . VAL A 157 ? 0.3838 0.5046 0.6828 0.0342  0.1138  0.0512  157 VAL A CG1 
1212 C CG2 . VAL A 157 ? 0.4145 0.5231 0.7039 0.0282  0.1311  0.0544  157 VAL A CG2 
1213 N N   . SER A 158 ? 0.4111 0.5339 0.7047 0.0208  0.1063  0.0073  158 SER A N   
1214 C CA  . SER A 158 ? 0.4077 0.5282 0.7023 0.0235  0.1016  0.0011  158 SER A CA  
1215 C C   . SER A 158 ? 0.3996 0.5241 0.6950 0.0288  0.0934  0.0132  158 SER A C   
1216 O O   . SER A 158 ? 0.3133 0.4477 0.6010 0.0289  0.0823  0.0130  158 SER A O   
1217 C CB  . SER A 158 ? 0.3666 0.4955 0.6522 0.0224  0.0935  -0.0157 158 SER A CB  
1218 O OG  . SER A 158 ? 0.4732 0.6015 0.7610 0.0175  0.1016  -0.0288 158 SER A OG  
1219 N N   . PHE A 159 ? 0.3629 0.4802 0.6670 0.0327  0.0992  0.0226  159 PHE A N   
1220 C CA  . PHE A 159 ? 0.3571 0.4817 0.6641 0.0366  0.0924  0.0323  159 PHE A CA  
1221 C C   . PHE A 159 ? 0.3730 0.4948 0.6753 0.0356  0.0864  0.0224  159 PHE A C   
1222 O O   . PHE A 159 ? 0.3699 0.4787 0.6682 0.0353  0.0903  0.0140  159 PHE A O   
1223 C CB  . PHE A 159 ? 0.3122 0.4298 0.6253 0.0420  0.1003  0.0456  159 PHE A CB  
1224 C CG  . PHE A 159 ? 0.3371 0.4568 0.6548 0.0461  0.1081  0.0585  159 PHE A CG  
1225 C CD1 . PHE A 159 ? 0.3005 0.4386 0.6184 0.0493  0.1011  0.0696  159 PHE A CD1 
1226 C CD2 . PHE A 159 ? 0.3630 0.4645 0.6816 0.0468  0.1229  0.0595  159 PHE A CD2 
1227 C CE1 . PHE A 159 ? 0.2994 0.4372 0.6163 0.0550  0.1079  0.0825  159 PHE A CE1 
1228 C CE2 . PHE A 159 ? 0.3776 0.4752 0.6951 0.0517  0.1317  0.0726  159 PHE A CE2 
1229 C CZ  . PHE A 159 ? 0.3578 0.4735 0.6737 0.0568  0.1238  0.0847  159 PHE A CZ  
1230 N N   . CYS A 160 ? 0.3461 0.4765 0.6419 0.0342  0.0760  0.0227  160 CYS A N   
1231 C CA  . CYS A 160 ? 0.3205 0.4444 0.6085 0.0335  0.0717  0.0142  160 CYS A CA  
1232 C C   . CYS A 160 ? 0.3196 0.4493 0.6096 0.0319  0.0675  0.0215  160 CYS A C   
1233 O O   . CYS A 160 ? 0.3646 0.4855 0.6477 0.0309  0.0663  0.0155  160 CYS A O   
1234 C CB  . CYS A 160 ? 0.3875 0.5096 0.6580 0.0322  0.0643  0.0022  160 CYS A CB  
1235 S SG  . CYS A 160 ? 0.3709 0.5052 0.6324 0.0284  0.0548  0.0065  160 CYS A SG  
1236 N N   . TYR A 161 ? 0.2815 0.4270 0.5798 0.0312  0.0656  0.0336  161 TYR A N   
1237 C CA  . TYR A 161 ? 0.2342 0.3905 0.5336 0.0270  0.0605  0.0378  161 TYR A CA  
1238 C C   . TYR A 161 ? 0.2458 0.4222 0.5612 0.0306  0.0626  0.0526  161 TYR A C   
1239 O O   . TYR A 161 ? 0.2495 0.4339 0.5682 0.0346  0.0635  0.0600  161 TYR A O   
1240 C CB  . TYR A 161 ? 0.2412 0.4012 0.5251 0.0198  0.0508  0.0322  161 TYR A CB  
1241 C CG  . TYR A 161 ? 0.3159 0.4887 0.5997 0.0119  0.0461  0.0350  161 TYR A CG  
1242 C CD1 . TYR A 161 ? 0.2949 0.4552 0.5705 0.0066  0.0469  0.0283  161 TYR A CD1 
1243 C CD2 . TYR A 161 ? 0.2318 0.4302 0.5226 0.0091  0.0412  0.0437  161 TYR A CD2 
1244 C CE1 . TYR A 161 ? 0.2925 0.4650 0.5677 -0.0036 0.0438  0.0295  161 TYR A CE1 
1245 C CE2 . TYR A 161 ? 0.2650 0.4794 0.5564 -0.0002 0.0369  0.0444  161 TYR A CE2 
1246 C CZ  . TYR A 161 ? 0.2865 0.4879 0.5706 -0.0077 0.0386  0.0370  161 TYR A CZ  
1247 O OH  . TYR A 161 ? 0.2501 0.4685 0.5350 -0.0197 0.0356  0.0367  161 TYR A OH  
1248 N N   . MET A 162 ? 0.2817 0.4670 0.6060 0.0300  0.0639  0.0571  162 MET A N   
1249 C CA  . MET A 162 ? 0.2544 0.4629 0.5895 0.0340  0.0637  0.0701  162 MET A CA  
1250 C C   . MET A 162 ? 0.2392 0.4688 0.5786 0.0247  0.0578  0.0693  162 MET A C   
1251 O O   . MET A 162 ? 0.2115 0.4292 0.5463 0.0185  0.0590  0.0615  162 MET A O   
1252 C CB  . MET A 162 ? 0.2656 0.4622 0.6015 0.0425  0.0718  0.0756  162 MET A CB  
1253 C CG  . MET A 162 ? 0.2511 0.4709 0.5936 0.0482  0.0710  0.0878  162 MET A CG  
1254 S SD  . MET A 162 ? 0.3236 0.5272 0.6662 0.0611  0.0820  0.0965  162 MET A SD  
1255 C CE  . MET A 162 ? 0.2739 0.4739 0.6140 0.0711  0.0868  0.1074  162 MET A CE  
1256 N N   . HIS A 163 ? 0.2149 0.4737 0.5584 0.0225  0.0513  0.0759  163 HIS A N   
1257 C CA  . HIS A 163 ? 0.2481 0.5266 0.5904 0.0098  0.0448  0.0720  163 HIS A CA  
1258 C C   . HIS A 163 ? 0.2410 0.5390 0.5975 0.0111  0.0484  0.0777  163 HIS A C   
1259 O O   . HIS A 163 ? 0.2205 0.5269 0.5793 0.0229  0.0503  0.0866  163 HIS A O   
1260 C CB  . HIS A 163 ? 0.2334 0.5392 0.5736 0.0060  0.0359  0.0753  163 HIS A CB  
1261 C CG  . HIS A 163 ? 0.2569 0.5825 0.5939 -0.0101 0.0295  0.0689  163 HIS A CG  
1262 N ND1 . HIS A 163 ? 0.2262 0.5277 0.5453 -0.0241 0.0283  0.0552  163 HIS A ND1 
1263 C CD2 . HIS A 163 ? 0.2308 0.5977 0.5792 -0.0151 0.0249  0.0735  163 HIS A CD2 
1264 C CE1 . HIS A 163 ? 0.2581 0.5821 0.5770 -0.0389 0.0242  0.0512  163 HIS A CE1 
1265 N NE2 . HIS A 163 ? 0.2594 0.6260 0.5971 -0.0345 0.0215  0.0616  163 HIS A NE2 
1266 N N   . HIS A 164 ? 0.1775 0.4761 0.5332 -0.0020 0.0485  0.0701  164 HIS A N   
1267 C CA  . HIS A 164 ? 0.2698 0.5867 0.6366 -0.0037 0.0520  0.0727  164 HIS A CA  
1268 C C   . HIS A 164 ? 0.3019 0.6505 0.6732 -0.0215 0.0471  0.0687  164 HIS A C   
1269 O O   . HIS A 164 ? 0.2561 0.6308 0.6345 -0.0209 0.0469  0.0713  164 HIS A O   
1270 C CB  . HIS A 164 ? 0.2274 0.5156 0.5930 -0.0034 0.0608  0.0679  164 HIS A CB  
1271 C CG  . HIS A 164 ? 0.2689 0.5322 0.6304 0.0129  0.0666  0.0716  164 HIS A CG  
1272 N ND1 . HIS A 164 ? 0.2452 0.5080 0.6097 0.0211  0.0719  0.0762  164 HIS A ND1 
1273 C CD2 . HIS A 164 ? 0.2276 0.4649 0.5813 0.0207  0.0684  0.0703  164 HIS A CD2 
1274 C CE1 . HIS A 164 ? 0.2537 0.4902 0.6120 0.0327  0.0769  0.0782  164 HIS A CE1 
1275 N NE2 . HIS A 164 ? 0.2887 0.5103 0.6405 0.0320  0.0749  0.0742  164 HIS A NE2 
1276 N N   . MET A 165 ? 0.2733 0.6065 0.6253 -0.0372 0.0426  0.0570  165 MET A N   
1277 C CA  . MET A 165 ? 0.3023 0.6560 0.6528 -0.0573 0.0406  0.0499  165 MET A CA  
1278 C C   . MET A 165 ? 0.2799 0.6146 0.6053 -0.0734 0.0354  0.0376  165 MET A C   
1279 O O   . MET A 165 ? 0.2905 0.5880 0.5967 -0.0690 0.0351  0.0328  165 MET A O   
1280 C CB  . MET A 165 ? 0.3206 0.6611 0.6727 -0.0634 0.0494  0.0460  165 MET A CB  
1281 C CG  . MET A 165 ? 0.3502 0.6375 0.6777 -0.0665 0.0544  0.0360  165 MET A CG  
1282 S SD  . MET A 165 ? 0.5395 0.8162 0.8743 -0.0666 0.0661  0.0361  165 MET A SD  
1283 C CE  . MET A 165 ? 0.4705 0.7475 0.7902 -0.0953 0.0683  0.0239  165 MET A CE  
1284 N N   . GLU A 166 ? 0.2919 0.6527 0.6167 -0.0927 0.0324  0.0316  166 GLU A N   
1285 C CA  . GLU A 166 ? 0.3574 0.6985 0.6562 -0.1110 0.0296  0.0185  166 GLU A CA  
1286 C C   . GLU A 166 ? 0.4141 0.7357 0.7001 -0.1310 0.0376  0.0076  166 GLU A C   
1287 O O   . GLU A 166 ? 0.3496 0.6968 0.6528 -0.1375 0.0421  0.0094  166 GLU A O   
1288 C CB  . GLU A 166 ? 0.3797 0.7639 0.6833 -0.1203 0.0199  0.0181  166 GLU A CB  
1289 C CG  . GLU A 166 ? 0.3849 0.7527 0.6616 -0.1425 0.0177  0.0035  166 GLU A CG  
1290 C CD  . GLU A 166 ? 0.4314 0.8386 0.7107 -0.1477 0.0070  0.0034  166 GLU A CD  
1291 O OE1 . GLU A 166 ? 0.4173 0.8336 0.7015 -0.1304 0.0008  0.0124  166 GLU A OE1 
1292 O OE2 . GLU A 166 ? 0.4806 0.9123 0.7573 -0.1703 0.0054  -0.0059 166 GLU A OE2 
1293 N N   . LEU A 167 ? 0.4079 0.6832 0.6619 -0.1400 0.0403  -0.0035 167 LEU A N   
1294 C CA  . LEU A 167 ? 0.4587 0.7051 0.6936 -0.1584 0.0500  -0.0140 167 LEU A CA  
1295 C C   . LEU A 167 ? 0.4805 0.7430 0.7049 -0.1855 0.0485  -0.0248 167 LEU A C   
1296 O O   . LEU A 167 ? 0.4964 0.7871 0.7244 -0.1886 0.0390  -0.0250 167 LEU A O   
1297 C CB  . LEU A 167 ? 0.4673 0.6505 0.6698 -0.1506 0.0558  -0.0196 167 LEU A CB  
1298 C CG  . LEU A 167 ? 0.4440 0.6110 0.6551 -0.1256 0.0577  -0.0114 167 LEU A CG  
1299 C CD1 . LEU A 167 ? 0.4835 0.5932 0.6613 -0.1178 0.0632  -0.0180 167 LEU A CD1 
1300 C CD2 . LEU A 167 ? 0.4203 0.6074 0.6558 -0.1240 0.0639  -0.0051 167 LEU A CD2 
1301 N N   . PRO A 168 ? 0.4682 0.7131 0.6786 -0.2068 0.0586  -0.0344 168 PRO A N   
1302 C CA  . PRO A 168 ? 0.4825 0.7382 0.6795 -0.2362 0.0590  -0.0471 168 PRO A CA  
1303 C C   . PRO A 168 ? 0.5454 0.7686 0.7106 -0.2394 0.0552  -0.0550 168 PRO A C   
1304 O O   . PRO A 168 ? 0.5340 0.7822 0.6962 -0.2570 0.0498  -0.0623 168 PRO A O   
1305 C CB  . PRO A 168 ? 0.5213 0.7456 0.7018 -0.2552 0.0740  -0.0557 168 PRO A CB  
1306 C CG  . PRO A 168 ? 0.5471 0.7715 0.7471 -0.2368 0.0787  -0.0451 168 PRO A CG  
1307 C CD  . PRO A 168 ? 0.5123 0.7259 0.7170 -0.2062 0.0710  -0.0347 168 PRO A CD  
1308 N N   . THR A 169 ? 0.5466 0.7151 0.6865 -0.2230 0.0582  -0.0545 169 THR A N   
1309 C CA  . THR A 169 ? 0.5880 0.7248 0.6964 -0.2238 0.0552  -0.0618 169 THR A CA  
1310 C C   . THR A 169 ? 0.5803 0.7547 0.7055 -0.2119 0.0410  -0.0554 169 THR A C   
1311 O O   . THR A 169 ? 0.5681 0.7240 0.6701 -0.2131 0.0373  -0.0612 169 THR A O   
1312 C CB  . THR A 169 ? 0.5663 0.6395 0.6441 -0.2063 0.0621  -0.0624 169 THR A CB  
1313 O OG1 . THR A 169 ? 0.5427 0.6255 0.6435 -0.1804 0.0587  -0.0505 169 THR A OG1 
1314 C CG2 . THR A 169 ? 0.6173 0.6437 0.6675 -0.2201 0.0779  -0.0704 169 THR A CG2 
1315 N N   . GLY A 170 ? 0.4834 0.7071 0.6462 -0.1992 0.0339  -0.0432 170 GLY A N   
1316 C CA  . GLY A 170 ? 0.4386 0.6926 0.6143 -0.1859 0.0222  -0.0360 170 GLY A CA  
1317 C C   . GLY A 170 ? 0.5143 0.7419 0.6867 -0.1596 0.0205  -0.0286 170 GLY A C   
1318 O O   . GLY A 170 ? 0.5113 0.7519 0.6856 -0.1497 0.0123  -0.0246 170 GLY A O   
1319 N N   . VAL A 171 ? 0.4739 0.6655 0.6403 -0.1486 0.0282  -0.0274 171 VAL A N   
1320 C CA  . VAL A 171 ? 0.4451 0.6198 0.6135 -0.1243 0.0269  -0.0206 171 VAL A CA  
1321 C C   . VAL A 171 ? 0.4406 0.6422 0.6423 -0.1114 0.0280  -0.0087 171 VAL A C   
1322 O O   . VAL A 171 ? 0.3647 0.5944 0.5852 -0.1202 0.0302  -0.0059 171 VAL A O   
1323 C CB  . VAL A 171 ? 0.4948 0.6127 0.6316 -0.1185 0.0343  -0.0281 171 VAL A CB  
1324 C CG1 . VAL A 171 ? 0.5207 0.6092 0.6210 -0.1295 0.0342  -0.0395 171 VAL A CG1 
1325 C CG2 . VAL A 171 ? 0.4573 0.5578 0.5921 -0.1246 0.0444  -0.0300 171 VAL A CG2 
1326 N N   . HIS A 172 ? 0.3766 0.5692 0.5848 -0.0911 0.0274  -0.0023 172 HIS A N   
1327 C CA  . HIS A 172 ? 0.3660 0.5839 0.6041 -0.0776 0.0282  0.0096  172 HIS A CA  
1328 C C   . HIS A 172 ? 0.3711 0.5587 0.6077 -0.0645 0.0355  0.0100  172 HIS A C   
1329 O O   . HIS A 172 ? 0.3352 0.4874 0.5496 -0.0597 0.0372  0.0030  172 HIS A O   
1330 C CB  . HIS A 172 ? 0.3411 0.5834 0.5909 -0.0667 0.0211  0.0179  172 HIS A CB  
1331 C CG  . HIS A 172 ? 0.3670 0.6407 0.6167 -0.0785 0.0133  0.0171  172 HIS A CG  
1332 N ND1 . HIS A 172 ? 0.3738 0.6393 0.6045 -0.0817 0.0075  0.0117  172 HIS A ND1 
1333 C CD2 . HIS A 172 ? 0.3405 0.6561 0.6062 -0.0883 0.0104  0.0202  172 HIS A CD2 
1334 C CE1 . HIS A 172 ? 0.3789 0.6787 0.6137 -0.0932 0.0013  0.0114  172 HIS A CE1 
1335 N NE2 . HIS A 172 ? 0.3761 0.7085 0.6323 -0.0975 0.0026  0.0163  172 HIS A NE2 
1336 N N   . ALA A 173 ? 0.3105 0.5143 0.5704 -0.0578 0.0398  0.0182  173 ALA A N   
1337 C CA  . ALA A 173 ? 0.3167 0.4967 0.5781 -0.0463 0.0471  0.0187  173 ALA A CA  
1338 C C   . ALA A 173 ? 0.2996 0.5004 0.5870 -0.0320 0.0487  0.0303  173 ALA A C   
1339 O O   . ALA A 173 ? 0.2534 0.4897 0.5604 -0.0320 0.0465  0.0391  173 ALA A O   
1340 C CB  . ALA A 173 ? 0.3573 0.5254 0.6141 -0.0559 0.0546  0.0145  173 ALA A CB  
1341 N N   . GLY A 174 ? 0.2624 0.4413 0.5486 -0.0194 0.0530  0.0299  174 GLY A N   
1342 C CA  . GLY A 174 ? 0.2517 0.4422 0.5587 -0.0063 0.0570  0.0397  174 GLY A CA  
1343 C C   . GLY A 174 ? 0.2902 0.4526 0.5927 0.0033  0.0634  0.0354  174 GLY A C   
1344 O O   . GLY A 174 ? 0.3105 0.4480 0.5958 0.0012  0.0651  0.0260  174 GLY A O   
1345 N N   . THR A 175 ? 0.2262 0.3926 0.5427 0.0143  0.0677  0.0423  175 THR A N   
1346 C CA  . THR A 175 ? 0.3088 0.4538 0.6250 0.0226  0.0750  0.0385  175 THR A CA  
1347 C C   . THR A 175 ? 0.3259 0.4628 0.6390 0.0284  0.0751  0.0361  175 THR A C   
1348 O O   . THR A 175 ? 0.2478 0.3970 0.5626 0.0282  0.0709  0.0406  175 THR A O   
1349 C CB  . THR A 175 ? 0.2850 0.4354 0.6151 0.0291  0.0821  0.0470  175 THR A CB  
1350 O OG1 . THR A 175 ? 0.2258 0.3872 0.5587 0.0347  0.0808  0.0568  175 THR A OG1 
1351 C CG2 . THR A 175 ? 0.2732 0.4382 0.6114 0.0230  0.0833  0.0499  175 THR A CG2 
1352 N N   . ASP A 176 ? 0.3121 0.4297 0.6209 0.0333  0.0804  0.0287  176 ASP A N   
1353 C CA  . ASP A 176 ? 0.3001 0.4096 0.6052 0.0373  0.0825  0.0261  176 ASP A CA  
1354 C C   . ASP A 176 ? 0.2861 0.3949 0.5956 0.0410  0.0874  0.0363  176 ASP A C   
1355 O O   . ASP A 176 ? 0.2674 0.3831 0.5829 0.0425  0.0887  0.0447  176 ASP A O   
1356 C CB  . ASP A 176 ? 0.3753 0.4663 0.6686 0.0393  0.0847  0.0129  176 ASP A CB  
1357 C CG  . ASP A 176 ? 0.3629 0.4406 0.6532 0.0413  0.0899  0.0122  176 ASP A CG  
1358 O OD1 . ASP A 176 ? 0.3195 0.3973 0.6159 0.0426  0.0939  0.0212  176 ASP A OD1 
1359 O OD2 . ASP A 176 ? 0.3994 0.4664 0.6797 0.0427  0.0900  0.0025  176 ASP A OD2 
1360 N N   . LEU A 177 ? 0.3021 0.4027 0.6094 0.0429  0.0914  0.0357  177 LEU A N   
1361 C CA  . LEU A 177 ? 0.3593 0.4577 0.6718 0.0479  0.0983  0.0471  177 LEU A CA  
1362 C C   . LEU A 177 ? 0.3615 0.4437 0.6720 0.0503  0.1052  0.0460  177 LEU A C   
1363 O O   . LEU A 177 ? 0.3094 0.3866 0.6234 0.0555  0.1125  0.0553  177 LEU A O   
1364 C CB  . LEU A 177 ? 0.3354 0.4287 0.6483 0.0490  0.1037  0.0487  177 LEU A CB  
1365 C CG  . LEU A 177 ? 0.3433 0.4548 0.6611 0.0510  0.1002  0.0592  177 LEU A CG  
1366 C CD1 . LEU A 177 ? 0.2721 0.3931 0.5957 0.0584  0.1024  0.0744  177 LEU A CD1 
1367 C CD2 . LEU A 177 ? 0.3342 0.4633 0.6512 0.0455  0.0884  0.0541  177 LEU A CD2 
1368 N N   . GLU A 178 ? 0.3840 0.4576 0.6882 0.0475  0.1037  0.0354  178 GLU A N   
1369 C CA  . GLU A 178 ? 0.4112 0.4721 0.7132 0.0495  0.1093  0.0349  178 GLU A CA  
1370 C C   . GLU A 178 ? 0.3998 0.4706 0.7063 0.0505  0.1071  0.0409  178 GLU A C   
1371 O O   . GLU A 178 ? 0.4474 0.5104 0.7534 0.0528  0.1119  0.0424  178 GLU A O   
1372 C CB  . GLU A 178 ? 0.4544 0.5019 0.7460 0.0467  0.1095  0.0204  178 GLU A CB  
1373 C CG  . GLU A 178 ? 0.4862 0.5213 0.7756 0.0455  0.1165  0.0148  178 GLU A CG  
1374 C CD  . GLU A 178 ? 0.6123 0.6448 0.8918 0.0423  0.1134  -0.0012 178 GLU A CD  
1375 O OE1 . GLU A 178 ? 0.6813 0.7166 0.9530 0.0432  0.1070  -0.0071 178 GLU A OE1 
1376 O OE2 . GLU A 178 ? 0.7288 0.7572 1.0084 0.0393  0.1182  -0.0079 178 GLU A OE2 
1377 N N   . GLY A 179 ? 0.4095 0.4989 0.7214 0.0479  0.1006  0.0439  179 GLY A N   
1378 C CA  . GLY A 179 ? 0.3595 0.4644 0.6791 0.0471  0.0992  0.0500  179 GLY A CA  
1379 C C   . GLY A 179 ? 0.3240 0.4273 0.6420 0.0418  0.0981  0.0423  179 GLY A C   
1380 O O   . GLY A 179 ? 0.2999 0.4158 0.6253 0.0392  0.0988  0.0464  179 GLY A O   
1381 N N   . ASN A 180 ? 0.2943 0.3829 0.6029 0.0407  0.0974  0.0313  180 ASN A N   
1382 C CA  . ASN A 180 ? 0.3488 0.4316 0.6543 0.0379  0.0987  0.0238  180 ASN A CA  
1383 C C   . ASN A 180 ? 0.3693 0.4611 0.6707 0.0307  0.0919  0.0221  180 ASN A C   
1384 O O   . ASN A 180 ? 0.3503 0.4416 0.6453 0.0311  0.0868  0.0187  180 ASN A O   
1385 C CB  . ASN A 180 ? 0.3999 0.4601 0.6890 0.0421  0.1002  0.0121  180 ASN A CB  
1386 C CG  . ASN A 180 ? 0.4374 0.4861 0.7213 0.0453  0.1039  0.0125  180 ASN A CG  
1387 O OD1 . ASN A 180 ? 0.4603 0.5059 0.7462 0.0461  0.1083  0.0159  180 ASN A OD1 
1388 N ND2 . ASN A 180 ? 0.4506 0.4944 0.7295 0.0464  0.1032  0.0093  180 ASN A ND2 
1389 N N   . PHE A 181 ? 0.3174 0.4142 0.6156 0.0223  0.0906  0.0235  181 PHE A N   
1390 C CA  . PHE A 181 ? 0.3359 0.4361 0.6218 0.0127  0.0830  0.0208  181 PHE A CA  
1391 C C   . PHE A 181 ? 0.3892 0.4648 0.6502 0.0150  0.0801  0.0097  181 PHE A C   
1392 O O   . PHE A 181 ? 0.3576 0.4132 0.6077 0.0217  0.0841  0.0032  181 PHE A O   
1393 C CB  . PHE A 181 ? 0.3198 0.4246 0.6030 0.0009  0.0844  0.0213  181 PHE A CB  
1394 C CG  . PHE A 181 ? 0.3305 0.4709 0.6344 -0.0054 0.0821  0.0308  181 PHE A CG  
1395 C CD1 . PHE A 181 ? 0.2967 0.4565 0.6228 -0.0002 0.0875  0.0398  181 PHE A CD1 
1396 C CD2 . PHE A 181 ? 0.3138 0.4696 0.6136 -0.0157 0.0746  0.0303  181 PHE A CD2 
1397 C CE1 . PHE A 181 ? 0.3199 0.5171 0.6648 -0.0037 0.0851  0.0487  181 PHE A CE1 
1398 C CE2 . PHE A 181 ? 0.2951 0.4890 0.6139 -0.0210 0.0718  0.0383  181 PHE A CE2 
1399 C CZ  . PHE A 181 ? 0.3055 0.5216 0.6470 -0.0144 0.0768  0.0477  181 PHE A CZ  
1400 N N   . TYR A 182 ? 0.3672 0.4459 0.6184 0.0106  0.0730  0.0075  182 TYR A N   
1401 C CA  . TYR A 182 ? 0.3395 0.3951 0.5625 0.0103  0.0705  -0.0024 182 TYR A CA  
1402 C C   . TYR A 182 ? 0.3933 0.4373 0.6019 -0.0007 0.0728  -0.0042 182 TYR A C   
1403 O O   . TYR A 182 ? 0.4016 0.4640 0.6204 -0.0123 0.0713  0.0007  182 TYR A O   
1404 C CB  . TYR A 182 ? 0.3547 0.4172 0.5716 0.0095  0.0629  -0.0041 182 TYR A CB  
1405 C CG  . TYR A 182 ? 0.3850 0.4579 0.6145 0.0184  0.0619  -0.0031 182 TYR A CG  
1406 C CD1 . TYR A 182 ? 0.3538 0.4141 0.5714 0.0275  0.0622  -0.0120 182 TYR A CD1 
1407 C CD2 . TYR A 182 ? 0.3190 0.4145 0.5707 0.0177  0.0614  0.0064  182 TYR A CD2 
1408 C CE1 . TYR A 182 ? 0.3660 0.4363 0.5947 0.0328  0.0625  -0.0127 182 TYR A CE1 
1409 C CE2 . TYR A 182 ? 0.3193 0.4200 0.5800 0.0243  0.0627  0.0069  182 TYR A CE2 
1410 C CZ  . TYR A 182 ? 0.3774 0.4652 0.6268 0.0304  0.0634  -0.0034 182 TYR A CZ  
1411 O OH  . TYR A 182 ? 0.3145 0.4079 0.5721 0.0343  0.0658  -0.0048 182 TYR A OH  
1412 N N   . GLY A 183 ? 0.3168 0.3309 0.5010 0.0029  0.0771  -0.0114 183 GLY A N   
1413 C CA  . GLY A 183 ? 0.3986 0.3939 0.5633 -0.0080 0.0816  -0.0141 183 GLY A CA  
1414 C C   . GLY A 183 ? 0.4294 0.4291 0.6075 -0.0127 0.0892  -0.0098 183 GLY A C   
1415 O O   . GLY A 183 ? 0.4093 0.4237 0.6098 -0.0053 0.0912  -0.0048 183 GLY A O   
1416 N N   . PRO A 184 ? 0.4092 0.3961 0.5734 -0.0259 0.0945  -0.0118 184 PRO A N   
1417 C CA  . PRO A 184 ? 0.4202 0.4074 0.5928 -0.0305 0.1034  -0.0089 184 PRO A CA  
1418 C C   . PRO A 184 ? 0.4728 0.4997 0.6772 -0.0416 0.1027  -0.0014 184 PRO A C   
1419 O O   . PRO A 184 ? 0.5070 0.5373 0.7171 -0.0496 0.1102  0.0002  184 PRO A O   
1420 C CB  . PRO A 184 ? 0.4310 0.3831 0.5700 -0.0408 0.1107  -0.0154 184 PRO A CB  
1421 C CG  . PRO A 184 ? 0.4921 0.4452 0.6193 -0.0516 0.1045  -0.0191 184 PRO A CG  
1422 C CD  . PRO A 184 ? 0.4637 0.4339 0.6025 -0.0386 0.0939  -0.0174 184 PRO A CD  
1423 N N   . PHE A 185 ? 0.3892 0.4474 0.6140 -0.0411 0.0944  0.0035  185 PHE A N   
1424 C CA  . PHE A 185 ? 0.3922 0.4905 0.6417 -0.0523 0.0925  0.0098  185 PHE A CA  
1425 C C   . PHE A 185 ? 0.3363 0.4588 0.6150 -0.0426 0.0961  0.0190  185 PHE A C   
1426 O O   . PHE A 185 ? 0.3245 0.4368 0.6075 -0.0269 0.0976  0.0212  185 PHE A O   
1427 C CB  . PHE A 185 ? 0.3822 0.5027 0.6372 -0.0546 0.0822  0.0114  185 PHE A CB  
1428 C CG  . PHE A 185 ? 0.3655 0.4603 0.5904 -0.0627 0.0792  0.0022  185 PHE A CG  
1429 C CD1 . PHE A 185 ? 0.3949 0.4779 0.6021 -0.0811 0.0834  -0.0045 185 PHE A CD1 
1430 C CD2 . PHE A 185 ? 0.3643 0.4428 0.5761 -0.0515 0.0739  -0.0006 185 PHE A CD2 
1431 C CE1 . PHE A 185 ? 0.4777 0.5305 0.6528 -0.0876 0.0825  -0.0133 185 PHE A CE1 
1432 C CE2 . PHE A 185 ? 0.3973 0.4497 0.5788 -0.0568 0.0721  -0.0090 185 PHE A CE2 
1433 C CZ  . PHE A 185 ? 0.4417 0.4795 0.6040 -0.0742 0.0766  -0.0151 185 PHE A CZ  
1434 N N   . VAL A 186 ? 0.2342 0.3899 0.5323 -0.0523 0.0979  0.0238  186 VAL A N   
1435 C CA  . VAL A 186 ? 0.3294 0.5139 0.6561 -0.0423 0.1010  0.0339  186 VAL A CA  
1436 C C   . VAL A 186 ? 0.3421 0.5750 0.6911 -0.0458 0.0946  0.0412  186 VAL A C   
1437 O O   . VAL A 186 ? 0.2896 0.5388 0.6344 -0.0619 0.0898  0.0370  186 VAL A O   
1438 C CB  . VAL A 186 ? 0.3550 0.5377 0.6855 -0.0468 0.1114  0.0337  186 VAL A CB  
1439 C CG1 . VAL A 186 ? 0.3758 0.5112 0.6833 -0.0401 0.1179  0.0274  186 VAL A CG1 
1440 C CG2 . VAL A 186 ? 0.3893 0.5876 0.7167 -0.0696 0.1129  0.0288  186 VAL A CG2 
1441 N N   . ASP A 187 ? 0.2738 0.5295 0.6453 -0.0302 0.0952  0.0521  187 ASP A N   
1442 C CA  . ASP A 187 ? 0.2775 0.5738 0.6595 -0.0276 0.0874  0.0588  187 ASP A CA  
1443 C C   . ASP A 187 ? 0.3174 0.6453 0.7090 -0.0338 0.0897  0.0596  187 ASP A C   
1444 O O   . ASP A 187 ? 0.2525 0.5911 0.6498 -0.0202 0.0913  0.0655  187 ASP A O   
1445 C CB  . ASP A 187 ? 0.3047 0.5953 0.6855 -0.0067 0.0845  0.0665  187 ASP A CB  
1446 C CG  . ASP A 187 ? 0.3393 0.6046 0.7168 0.0074  0.0918  0.0690  187 ASP A CG  
1447 O OD1 . ASP A 187 ? 0.3470 0.5991 0.7233 0.0031  0.0987  0.0650  187 ASP A OD1 
1448 O OD2 . ASP A 187 ? 0.2414 0.5001 0.6169 0.0222  0.0914  0.0753  187 ASP A OD2 
1449 N N   . ARG A 188 ? 0.3238 0.6661 0.7164 -0.0560 0.0907  0.0527  188 ARG A N   
1450 C CA  . ARG A 188 ? 0.3234 0.7052 0.7262 -0.0671 0.0914  0.0504  188 ARG A CA  
1451 C C   . ARG A 188 ? 0.3604 0.7655 0.7633 -0.0895 0.0860  0.0429  188 ARG A C   
1452 O O   . ARG A 188 ? 0.3250 0.7088 0.7158 -0.1022 0.0852  0.0388  188 ARG A O   
1453 C CB  . ARG A 188 ? 0.3581 0.7284 0.7598 -0.0748 0.1024  0.0472  188 ARG A CB  
1454 C CG  . ARG A 188 ? 0.4431 0.7701 0.8300 -0.0894 0.1109  0.0400  188 ARG A CG  
1455 C CD  . ARG A 188 ? 0.5336 0.8421 0.9167 -0.0896 0.1225  0.0388  188 ARG A CD  
1456 N NE  . ARG A 188 ? 0.6219 0.8904 0.9979 -0.0696 0.1264  0.0418  188 ARG A NE  
1457 C CZ  . ARG A 188 ? 0.6520 0.8842 1.0163 -0.0687 0.1370  0.0382  188 ARG A CZ  
1458 N NH1 . ARG A 188 ? 0.6142 0.8392 0.9691 -0.0860 0.1456  0.0322  188 ARG A NH1 
1459 N NH2 . ARG A 188 ? 0.6237 0.8248 0.9809 -0.0499 0.1383  0.0400  188 ARG A NH2 
1460 N N   . GLN A 189 ? 0.3767 0.8216 0.7920 -0.0931 0.0822  0.0417  189 GLN A N   
1461 C CA  . GLN A 189 ? 0.3578 0.8259 0.7711 -0.1115 0.0750  0.0360  189 GLN A CA  
1462 C C   . GLN A 189 ? 0.3703 0.8205 0.7697 -0.1388 0.0815  0.0259  189 GLN A C   
1463 O O   . GLN A 189 ? 0.3850 0.8556 0.7881 -0.1521 0.0834  0.0216  189 GLN A O   
1464 C CB  . GLN A 189 ? 0.3686 0.8838 0.7971 -0.1065 0.0694  0.0388  189 GLN A CB  
1465 C CG  . GLN A 189 ? 0.4032 0.9467 0.8273 -0.1169 0.0582  0.0352  189 GLN A CG  
1466 C CD  . GLN A 189 ? 0.4812 1.0317 0.9043 -0.0978 0.0486  0.0432  189 GLN A CD  
1467 O OE1 . GLN A 189 ? 0.3985 0.9200 0.8169 -0.0834 0.0500  0.0486  189 GLN A OE1 
1468 N NE2 . GLN A 189 ? 0.4843 1.0734 0.9098 -0.0982 0.0392  0.0439  189 GLN A NE2 
1469 N N   . THR A 190 ? 0.3886 0.7985 0.7676 -0.1472 0.0853  0.0209  190 THR A N   
1470 C CA  . THR A 190 ? 0.4945 0.8717 0.8492 -0.1716 0.0938  0.0086  190 THR A CA  
1471 C C   . THR A 190 ? 0.5183 0.8647 0.8466 -0.1839 0.0914  -0.0016 190 THR A C   
1472 O O   . THR A 190 ? 0.4595 0.7919 0.7830 -0.1665 0.0836  0.0030  190 THR A O   
1473 C CB  . THR A 190 ? 0.4942 0.8355 0.8438 -0.1668 0.1073  0.0088  190 THR A CB  
1474 O OG1 . THR A 190 ? 0.5918 0.9162 0.9249 -0.1873 0.1162  0.0006  190 THR A OG1 
1475 C CG2 . THR A 190 ? 0.4766 0.7575 0.7985 -0.1543 0.1074  0.0068  190 THR A CG2 
1476 N N   . ALA A 191 ? 0.6700 0.9921 0.9729 -0.2081 0.0966  -0.0140 191 ALA A N   
1477 C CA  . ALA A 191 ? 0.6812 0.9591 0.9503 -0.2185 0.0967  -0.0243 191 ALA A CA  
1478 C C   . ALA A 191 ? 0.6503 0.8611 0.8919 -0.2048 0.1048  -0.0245 191 ALA A C   
1479 O O   . ALA A 191 ? 0.6268 0.8137 0.8597 -0.2104 0.1169  -0.0268 191 ALA A O   
1480 C CB  . ALA A 191 ? 0.7747 1.0474 1.0228 -0.2478 0.1001  -0.0374 191 ALA A CB  
1481 N N   . GLN A 192 ? 0.5576 0.7409 0.7857 -0.1864 0.0981  -0.0222 192 GLN A N   
1482 C CA  . GLN A 192 ? 0.6017 0.7298 0.8065 -0.1688 0.1033  -0.0217 192 GLN A CA  
1483 C C   . GLN A 192 ? 0.6308 0.7168 0.8000 -0.1689 0.1009  -0.0293 192 GLN A C   
1484 O O   . GLN A 192 ? 0.6222 0.7263 0.7938 -0.1700 0.0909  -0.0299 192 GLN A O   
1485 C CB  . GLN A 192 ? 0.5336 0.6742 0.7612 -0.1412 0.0981  -0.0104 192 GLN A CB  
1486 C CG  . GLN A 192 ? 0.4707 0.6494 0.7315 -0.1377 0.1014  -0.0021 192 GLN A CG  
1487 C CD  . GLN A 192 ? 0.3829 0.5766 0.6661 -0.1124 0.0963  0.0090  192 GLN A CD  
1488 O OE1 . GLN A 192 ? 0.3639 0.5240 0.6352 -0.0960 0.0970  0.0095  192 GLN A OE1 
1489 N NE2 . GLN A 192 ? 0.3434 0.5885 0.6581 -0.1090 0.0916  0.0176  192 GLN A NE2 
1490 N N   . ALA A 193 ? 0.6239 0.6539 0.7589 -0.1664 0.1106  -0.0346 193 ALA A N   
1491 C CA  . ALA A 193 ? 0.6418 0.6256 0.7369 -0.1666 0.1114  -0.0425 193 ALA A CA  
1492 C C   . ALA A 193 ? 0.6521 0.6146 0.7399 -0.1379 0.1064  -0.0384 193 ALA A C   
1493 O O   . ALA A 193 ? 0.6339 0.5817 0.7229 -0.1224 0.1110  -0.0346 193 ALA A O   
1494 C CB  . ALA A 193 ? 0.6652 0.5983 0.7225 -0.1811 0.1268  -0.0509 193 ALA A CB  
1495 N N   . ALA A 194 ? 0.6463 0.6124 0.7293 -0.1312 0.0966  -0.0394 194 ALA A N   
1496 C CA  . ALA A 194 ? 0.6173 0.5579 0.6854 -0.1071 0.0934  -0.0387 194 ALA A CA  
1497 C C   . ALA A 194 ? 0.6818 0.5637 0.7020 -0.1058 0.1028  -0.0467 194 ALA A C   
1498 O O   . ALA A 194 ? 0.6822 0.5414 0.6794 -0.1253 0.1112  -0.0531 194 ALA A O   
1499 C CB  . ALA A 194 ? 0.5935 0.5584 0.6721 -0.1007 0.0809  -0.0370 194 ALA A CB  
1500 N N   . GLY A 195 ? 0.6563 0.5127 0.6595 -0.0827 0.1024  -0.0467 195 GLY A N   
1501 C CA  . GLY A 195 ? 0.7858 0.5861 0.7408 -0.0774 0.1117  -0.0532 195 GLY A CA  
1502 C C   . GLY A 195 ? 0.8098 0.5909 0.7365 -0.0880 0.1110  -0.0602 195 GLY A C   
1503 O O   . GLY A 195 ? 0.7380 0.5510 0.6826 -0.0987 0.1019  -0.0604 195 GLY A O   
1504 N N   . THR A 196 ? 0.8063 0.5318 0.6853 -0.0848 0.1217  -0.0660 196 THR A N   
1505 C CA  . THR A 196 ? 0.8157 0.5164 0.6626 -0.0804 0.1199  -0.0716 196 THR A CA  
1506 C C   . THR A 196 ? 0.8051 0.5371 0.6720 -0.0596 0.1056  -0.0684 196 THR A C   
1507 O O   . THR A 196 ? 0.7685 0.5157 0.6529 -0.0402 0.1018  -0.0637 196 THR A O   
1508 C CB  . THR A 196 ? 0.8350 0.4701 0.6268 -0.0678 0.1332  -0.0758 196 THR A CB  
1509 O OG1 . THR A 196 ? 0.9274 0.5301 0.6994 -0.0878 0.1486  -0.0786 196 THR A OG1 
1510 C CG2 . THR A 196 ? 0.8373 0.4459 0.5944 -0.0647 0.1324  -0.0818 196 THR A CG2 
1511 N N   . ASP A 197 ? 0.7953 0.5374 0.6594 -0.0645 0.0984  -0.0713 197 ASP A N   
1512 C CA  . ASP A 197 ? 0.7940 0.5615 0.6723 -0.0453 0.0866  -0.0690 197 ASP A CA  
1513 C C   . ASP A 197 ? 0.8997 0.6267 0.7344 -0.0255 0.0898  -0.0741 197 ASP A C   
1514 O O   . ASP A 197 ? 0.9734 0.6524 0.7653 -0.0290 0.1003  -0.0794 197 ASP A O   
1515 C CB  . ASP A 197 ? 0.7831 0.5911 0.6867 -0.0587 0.0758  -0.0681 197 ASP A CB  
1516 C CG  . ASP A 197 ? 0.7898 0.6381 0.7256 -0.0425 0.0642  -0.0625 197 ASP A CG  
1517 O OD1 . ASP A 197 ? 0.7120 0.5635 0.6573 -0.0241 0.0642  -0.0596 197 ASP A OD1 
1518 O OD2 . ASP A 197 ? 0.7562 0.6313 0.7051 -0.0484 0.0558  -0.0617 197 ASP A OD2 
1519 N N   . THR A 198 ? 0.8988 0.6461 0.7440 -0.0045 0.0813  -0.0726 198 THR A N   
1520 C CA  . THR A 198 ? 0.9459 0.6661 0.7547 0.0159  0.0821  -0.0772 198 THR A CA  
1521 C C   . THR A 198 ? 0.8337 0.5912 0.6631 0.0207  0.0699  -0.0769 198 THR A C   
1522 O O   . THR A 198 ? 0.7435 0.5459 0.6153 0.0150  0.0615  -0.0721 198 THR A O   
1523 C CB  . THR A 198 ? 0.9665 0.6707 0.7607 0.0426  0.0863  -0.0769 198 THR A CB  
1524 O OG1 . THR A 198 ? 0.9364 0.6841 0.7730 0.0488  0.0789  -0.0726 198 THR A OG1 
1525 C CG2 . THR A 198 ? 1.0140 0.6746 0.7806 0.0389  0.1000  -0.0771 198 THR A CG2 
1526 N N   . THR A 199 ? 0.8542 0.5905 0.6511 0.0316  0.0701  -0.0818 199 THR A N   
1527 C CA  . THR A 199 ? 0.8062 0.5736 0.6167 0.0389  0.0599  -0.0822 199 THR A CA  
1528 C C   . THR A 199 ? 0.8359 0.6257 0.6595 0.0635  0.0555  -0.0815 199 THR A C   
1529 O O   . THR A 199 ? 0.8873 0.6537 0.6865 0.0830  0.0610  -0.0838 199 THR A O   
1530 C CB  . THR A 199 ? 0.8208 0.5557 0.5895 0.0415  0.0628  -0.0882 199 THR A CB  
1531 O OG1 . THR A 199 ? 0.8289 0.5432 0.5856 0.0158  0.0679  -0.0904 199 THR A OG1 
1532 C CG2 . THR A 199 ? 0.8264 0.5941 0.6094 0.0461  0.0526  -0.0886 199 THR A CG2 
1533 N N   . ILE A 200 ? 0.7580 0.5935 0.6196 0.0623  0.0462  -0.0785 200 ILE A N   
1534 C CA  . ILE A 200 ? 0.7223 0.5838 0.6001 0.0813  0.0425  -0.0793 200 ILE A CA  
1535 C C   . ILE A 200 ? 0.7628 0.6180 0.6128 0.1015  0.0411  -0.0852 200 ILE A C   
1536 O O   . ILE A 200 ? 0.6709 0.5504 0.5315 0.1010  0.0349  -0.0859 200 ILE A O   
1537 C CB  . ILE A 200 ? 0.6852 0.5934 0.6102 0.0718  0.0353  -0.0743 200 ILE A CB  
1538 C CG1 . ILE A 200 ? 0.6618 0.5759 0.6113 0.0518  0.0368  -0.0676 200 ILE A CG1 
1539 C CG2 . ILE A 200 ? 0.6453 0.5782 0.5874 0.0880  0.0335  -0.0764 200 ILE A CG2 
1540 C CD1 . ILE A 200 ? 0.5346 0.4891 0.5241 0.0403  0.0304  -0.0612 200 ILE A CD1 
1541 N N   . THR A 201 ? 0.8384 0.6617 0.6517 0.1209  0.0475  -0.0892 201 THR A N   
1542 C CA  . THR A 201 ? 0.7889 0.6000 0.5683 0.1420  0.0478  -0.0946 201 THR A CA  
1543 C C   . THR A 201 ? 0.6892 0.5479 0.4938 0.1514  0.0391  -0.0967 201 THR A C   
1544 O O   . THR A 201 ? 0.6888 0.5524 0.4828 0.1548  0.0361  -0.0984 201 THR A O   
1545 C CB  . THR A 201 ? 0.8280 0.6235 0.5899 0.1521  0.0509  -0.0887 201 THR A CB  
1546 O OG1 . THR A 201 ? 0.9289 0.6824 0.6702 0.1419  0.0599  -0.0867 201 THR A OG1 
1547 C CG2 . THR A 201 ? 0.8632 0.6522 0.6002 0.1641  0.0491  -0.0867 201 THR A CG2 
1548 N N   . VAL A 202 ? 0.6354 0.5292 0.4730 0.1540  0.0358  -0.0964 202 VAL A N   
1549 C CA  . VAL A 202 ? 0.6706 0.6099 0.5329 0.1595  0.0289  -0.0985 202 VAL A CA  
1550 C C   . VAL A 202 ? 0.6429 0.6021 0.5251 0.1450  0.0245  -0.0975 202 VAL A C   
1551 O O   . VAL A 202 ? 0.6245 0.6024 0.5045 0.1522  0.0210  -0.1010 202 VAL A O   
1552 C CB  . VAL A 202 ? 0.6029 0.5725 0.4969 0.1590  0.0273  -0.0979 202 VAL A CB  
1553 C CG1 . VAL A 202 ? 0.5861 0.5772 0.5182 0.1433  0.0264  -0.0965 202 VAL A CG1 
1554 C CG2 . VAL A 202 ? 0.6398 0.6441 0.5432 0.1660  0.0216  -0.0990 202 VAL A CG2 
1555 N N   . ASN A 203 ? 0.6069 0.5651 0.5105 0.1225  0.0240  -0.0906 203 ASN A N   
1556 C CA  . ASN A 203 ? 0.6199 0.5972 0.5422 0.1067  0.0193  -0.0866 203 ASN A CA  
1557 C C   . ASN A 203 ? 0.5720 0.5280 0.4621 0.1079  0.0190  -0.0891 203 ASN A C   
1558 O O   . ASN A 203 ? 0.5352 0.5112 0.4308 0.1073  0.0147  -0.0897 203 ASN A O   
1559 C CB  . ASN A 203 ? 0.5471 0.5273 0.4944 0.0850  0.0191  -0.0787 203 ASN A CB  
1560 C CG  . ASN A 203 ? 0.5546 0.5592 0.5364 0.0828  0.0194  -0.0755 203 ASN A CG  
1561 O OD1 . ASN A 203 ? 0.5428 0.5584 0.5278 0.0964  0.0204  -0.0804 203 ASN A OD1 
1562 N ND2 . ASN A 203 ? 0.5068 0.5214 0.5143 0.0663  0.0189  -0.0676 203 ASN A ND2 
1563 N N   . VAL A 204 ? 0.5869 0.5003 0.4410 0.1096  0.0244  -0.0910 204 VAL A N   
1564 C CA  . VAL A 204 ? 0.6295 0.5181 0.4496 0.1103  0.0254  -0.0943 204 VAL A CA  
1565 C C   . VAL A 204 ? 0.6799 0.5797 0.4849 0.1327  0.0237  -0.0997 204 VAL A C   
1566 O O   . VAL A 204 ? 0.7137 0.6164 0.5087 0.1318  0.0212  -0.1013 204 VAL A O   
1567 C CB  . VAL A 204 ? 0.7008 0.5358 0.4800 0.1094  0.0342  -0.0964 204 VAL A CB  
1568 C CG1 . VAL A 204 ? 0.7733 0.5779 0.5113 0.1133  0.0370  -0.1012 204 VAL A CG1 
1569 C CG2 . VAL A 204 ? 0.7038 0.5315 0.4984 0.0836  0.0360  -0.0920 204 VAL A CG2 
1570 N N   . LEU A 205 ? 0.6850 0.5927 0.4869 0.1538  0.0251  -0.1030 205 LEU A N   
1571 C CA  . LEU A 205 ? 0.7110 0.6388 0.5080 0.1697  0.0219  -0.1041 205 LEU A CA  
1572 C C   . LEU A 205 ? 0.6209 0.5965 0.4490 0.1685  0.0164  -0.1079 205 LEU A C   
1573 O O   . LEU A 205 ? 0.6291 0.6175 0.4519 0.1729  0.0136  -0.1087 205 LEU A O   
1574 C CB  . LEU A 205 ? 0.7311 0.6641 0.5290 0.1813  0.0215  -0.0994 205 LEU A CB  
1575 C CG  . LEU A 205 ? 0.7730 0.6616 0.5388 0.1855  0.0273  -0.0946 205 LEU A CG  
1576 C CD1 . LEU A 205 ? 0.7628 0.6622 0.5338 0.1958  0.0259  -0.0906 205 LEU A CD1 
1577 C CD2 . LEU A 205 ? 0.7535 0.6157 0.4856 0.1925  0.0292  -0.0928 205 LEU A CD2 
1578 N N   . ALA A 206 ? 0.5838 0.5872 0.4515 0.1558  0.0142  -0.1050 206 ALA A N   
1579 C CA  . ALA A 206 ? 0.5609 0.6066 0.4624 0.1472  0.0099  -0.1040 206 ALA A CA  
1580 C C   . ALA A 206 ? 0.5958 0.6386 0.4953 0.1335  0.0072  -0.0999 206 ALA A C   
1581 O O   . ALA A 206 ? 0.6297 0.6987 0.5382 0.1345  0.0047  -0.1011 206 ALA A O   
1582 C CB  . ALA A 206 ? 0.4909 0.5578 0.4317 0.1338  0.0098  -0.0997 206 ALA A CB  
1583 N N   . TRP A 207 ? 0.5951 0.6073 0.4814 0.1207  0.0081  -0.0957 207 TRP A N   
1584 C CA  . TRP A 207 ? 0.5947 0.6054 0.4773 0.1075  0.0052  -0.0928 207 TRP A CA  
1585 C C   . TRP A 207 ? 0.6370 0.6304 0.4818 0.1213  0.0061  -0.0991 207 TRP A C   
1586 O O   . TRP A 207 ? 0.6104 0.6204 0.4573 0.1191  0.0029  -0.0991 207 TRP A O   
1587 C CB  . TRP A 207 ? 0.5914 0.5796 0.4732 0.0880  0.0059  -0.0880 207 TRP A CB  
1588 C CG  . TRP A 207 ? 0.6628 0.6460 0.5364 0.0722  0.0030  -0.0862 207 TRP A CG  
1589 C CD1 . TRP A 207 ? 0.6133 0.6260 0.5127 0.0588  -0.0022 -0.0802 207 TRP A CD1 
1590 C CD2 . TRP A 207 ? 0.6731 0.6187 0.5081 0.0683  0.0059  -0.0910 207 TRP A CD2 
1591 N NE1 . TRP A 207 ? 0.6292 0.6287 0.5097 0.0473  -0.0038 -0.0814 207 TRP A NE1 
1592 C CE2 . TRP A 207 ? 0.6638 0.6217 0.5050 0.0516  0.0013  -0.0886 207 TRP A CE2 
1593 C CE3 . TRP A 207 ? 0.6873 0.5884 0.4813 0.0776  0.0128  -0.0971 207 TRP A CE3 
1594 C CZ2 . TRP A 207 ? 0.7316 0.6607 0.5409 0.0421  0.0030  -0.0934 207 TRP A CZ2 
1595 C CZ3 . TRP A 207 ? 0.7305 0.5987 0.4912 0.0684  0.0158  -0.1013 207 TRP A CZ3 
1596 C CH2 . TRP A 207 ? 0.7344 0.6173 0.5034 0.0496  0.0107  -0.1002 207 TRP A CH2 
1597 N N   . LEU A 208 ? 0.6752 0.6355 0.4841 0.1378  0.0111  -0.1043 208 LEU A N   
1598 C CA  . LEU A 208 ? 0.6740 0.6182 0.4453 0.1554  0.0131  -0.1102 208 LEU A CA  
1599 C C   . LEU A 208 ? 0.5973 0.5841 0.3838 0.1697  0.0096  -0.1133 208 LEU A C   
1600 O O   . LEU A 208 ? 0.6663 0.6577 0.4420 0.1732  0.0082  -0.1140 208 LEU A O   
1601 C CB  . LEU A 208 ? 0.7281 0.6333 0.4674 0.1687  0.0192  -0.1095 208 LEU A CB  
1602 C CG  . LEU A 208 ? 0.7664 0.6211 0.4770 0.1570  0.0256  -0.1101 208 LEU A CG  
1603 C CD1 . LEU A 208 ? 0.8422 0.6640 0.5307 0.1659  0.0315  -0.1048 208 LEU A CD1 
1604 C CD2 . LEU A 208 ? 0.7384 0.5725 0.4250 0.1451  0.0260  -0.1139 208 LEU A CD2 
1605 N N   . TYR A 209 ? 0.6589 0.6786 0.4757 0.1736  0.0081  -0.1130 209 TYR A N   
1606 C CA  . TYR A 209 ? 0.6234 0.6869 0.4625 0.1788  0.0045  -0.1137 209 TYR A CA  
1607 C C   . TYR A 209 ? 0.6082 0.6975 0.4687 0.1646  0.0024  -0.1133 209 TYR A C   
1608 O O   . TYR A 209 ? 0.6327 0.7391 0.4885 0.1700  0.0013  -0.1159 209 TYR A O   
1609 C CB  . TYR A 209 ? 0.6360 0.7272 0.5029 0.1807  0.0033  -0.1133 209 TYR A CB  
1610 C CG  . TYR A 209 ? 0.7038 0.7853 0.5557 0.1941  0.0018  -0.1099 209 TYR A CG  
1611 C CD1 . TYR A 209 ? 0.7360 0.8291 0.5775 0.2063  -0.0015 -0.1091 209 TYR A CD1 
1612 C CD2 . TYR A 209 ? 0.6869 0.7510 0.5360 0.1953  0.0036  -0.1074 209 TYR A CD2 
1613 C CE1 . TYR A 209 ? 0.7687 0.8572 0.5964 0.2205  -0.0036 -0.1061 209 TYR A CE1 
1614 C CE2 . TYR A 209 ? 0.7386 0.7967 0.5732 0.2084  0.0019  -0.1042 209 TYR A CE2 
1615 C CZ  . TYR A 209 ? 0.7829 0.8543 0.6068 0.2216  -0.0020 -0.1035 209 TYR A CZ  
1616 O OH  . TYR A 209 ? 0.7558 0.8237 0.5640 0.2370  -0.0043 -0.1001 209 TYR A OH  
1617 N N   . ALA A 210 ? 0.5791 0.6699 0.4663 0.1431  0.0010  -0.1057 210 ALA A N   
1618 C CA  . ALA A 210 ? 0.5957 0.7048 0.5035 0.1261  -0.0018 -0.0996 210 ALA A CA  
1619 C C   . ALA A 210 ? 0.5974 0.6900 0.4767 0.1269  -0.0032 -0.1006 210 ALA A C   
1620 O O   . ALA A 210 ? 0.5780 0.6926 0.4632 0.1257  -0.0048 -0.1002 210 ALA A O   
1621 C CB  . ALA A 210 ? 0.5453 0.6499 0.4763 0.1059  -0.0027 -0.0908 210 ALA A CB  
1622 N N   . ALA A 211 ? 0.6211 0.6732 0.4667 0.1290  -0.0016 -0.1026 211 ALA A N   
1623 C CA  . ALA A 211 ? 0.6220 0.6530 0.4353 0.1300  -0.0017 -0.1052 211 ALA A CA  
1624 C C   . ALA A 211 ? 0.7128 0.7569 0.5098 0.1508  -0.0008 -0.1115 211 ALA A C   
1625 O O   . ALA A 211 ? 0.7098 0.7632 0.5014 0.1488  -0.0026 -0.1116 211 ALA A O   
1626 C CB  . ALA A 211 ? 0.6992 0.6798 0.4754 0.1301  0.0025  -0.1080 211 ALA A CB  
1627 N N   . VAL A 212 ? 0.6962 0.7417 0.4831 0.1721  0.0022  -0.1169 212 VAL A N   
1628 C CA  . VAL A 212 ? 0.6991 0.7614 0.4858 0.1850  0.0010  -0.1155 212 VAL A CA  
1629 C C   . VAL A 212 ? 0.6295 0.7415 0.4460 0.1814  -0.0012 -0.1174 212 VAL A C   
1630 O O   . VAL A 212 ? 0.6841 0.8081 0.4960 0.1844  -0.0022 -0.1174 212 VAL A O   
1631 C CB  . VAL A 212 ? 0.7492 0.8103 0.5370 0.1989  0.0011  -0.1126 212 VAL A CB  
1632 C CG1 . VAL A 212 ? 0.7235 0.8091 0.5131 0.2125  -0.0017 -0.1118 212 VAL A CG1 
1633 C CG2 . VAL A 212 ? 0.7507 0.7609 0.5070 0.2023  0.0051  -0.1098 212 VAL A CG2 
1634 N N   . ILE A 213 ? 0.6316 0.7721 0.4793 0.1741  -0.0009 -0.1188 213 ILE A N   
1635 C CA  . ILE A 213 ? 0.6087 0.7918 0.4897 0.1646  -0.0016 -0.1172 213 ILE A CA  
1636 C C   . ILE A 213 ? 0.6301 0.8105 0.5083 0.1520  -0.0035 -0.1117 213 ILE A C   
1637 O O   . ILE A 213 ? 0.6855 0.8932 0.5709 0.1531  -0.0030 -0.1129 213 ILE A O   
1638 C CB  . ILE A 213 ? 0.5954 0.7947 0.5141 0.1496  -0.0011 -0.1127 213 ILE A CB  
1639 C CG1 . ILE A 213 ? 0.6212 0.8178 0.5391 0.1612  0.0004  -0.1181 213 ILE A CG1 
1640 C CG2 . ILE A 213 ? 0.5321 0.7737 0.4819 0.1417  0.0009  -0.1127 213 ILE A CG2 
1641 C CD1 . ILE A 213 ? 0.6451 0.8782 0.5806 0.1667  0.0003  -0.1224 213 ILE A CD1 
1642 N N   . ASN A 214 ? 0.6242 0.7725 0.4899 0.1403  -0.0056 -0.1064 214 ASN A N   
1643 C CA  . ASN A 214 ? 0.6544 0.8027 0.5201 0.1261  -0.0083 -0.1007 214 ASN A CA  
1644 C C   . ASN A 214 ? 0.7068 0.8285 0.5320 0.1336  -0.0086 -0.1053 214 ASN A C   
1645 O O   . ASN A 214 ? 0.7048 0.8143 0.5217 0.1204  -0.0112 -0.1018 214 ASN A O   
1646 C CB  . ASN A 214 ? 0.6292 0.7674 0.5113 0.1061  -0.0108 -0.0922 214 ASN A CB  
1647 C CG  . ASN A 214 ? 0.6492 0.8181 0.5723 0.0956  -0.0102 -0.0849 214 ASN A CG  
1648 O OD1 . ASN A 214 ? 0.6827 0.8668 0.6199 0.0847  -0.0115 -0.0776 214 ASN A OD1 
1649 N ND2 . ASN A 214 ? 0.6099 0.7864 0.5501 0.0995  -0.0075 -0.0867 214 ASN A ND2 
1650 N N   . GLY A 215 ? 0.7302 0.8434 0.5285 0.1553  -0.0056 -0.1134 215 GLY A N   
1651 C CA  . GLY A 215 ? 0.7759 0.8651 0.5344 0.1648  -0.0044 -0.1181 215 GLY A CA  
1652 C C   . GLY A 215 ? 0.8547 0.8905 0.5780 0.1641  -0.0019 -0.1192 215 GLY A C   
1653 O O   . GLY A 215 ? 0.9189 0.9301 0.6168 0.1690  0.0003  -0.1193 215 GLY A O   
1654 N N   . ASP A 216 ? 0.8574 0.8735 0.5826 0.1545  -0.0016 -0.1183 216 ASP A N   
1655 C CA  . ASP A 216 ? 0.8949 0.8584 0.5825 0.1531  0.0027  -0.1214 216 ASP A CA  
1656 C C   . ASP A 216 ? 0.8884 0.8345 0.5706 0.1692  0.0075  -0.1183 216 ASP A C   
1657 O O   . ASP A 216 ? 0.9008 0.8636 0.6043 0.1751  0.0070  -0.1165 216 ASP A O   
1658 C CB  . ASP A 216 ? 0.8669 0.8199 0.5714 0.1294  0.0011  -0.1167 216 ASP A CB  
1659 C CG  . ASP A 216 ? 1.0383 1.0081 0.7607 0.1055  -0.0046 -0.1121 216 ASP A CG  
1660 O OD1 . ASP A 216 ? 0.9961 0.9415 0.7073 0.0877  -0.0044 -0.1126 216 ASP A OD1 
1661 O OD2 . ASP A 216 ? 0.9809 0.9887 0.7270 0.1043  -0.0089 -0.1083 216 ASP A OD2 
1662 N N   . ARG A 217 ? 0.9772 0.8921 0.6313 0.1767  0.0118  -0.1175 217 ARG A N   
1663 C CA  . ARG A 217 ? 0.9730 0.8745 0.6197 0.1943  0.0150  -0.1134 217 ARG A CA  
1664 C C   . ARG A 217 ? 0.9957 0.8431 0.6039 0.1955  0.0222  -0.1128 217 ARG A C   
1665 O O   . ARG A 217 ? 1.0330 0.8664 0.6310 0.2113  0.0249  -0.1083 217 ARG A O   
1666 C CB  . ARG A 217 ? 0.9207 0.8561 0.5794 0.2117  0.0118  -0.1112 217 ARG A CB  
1667 C CG  . ARG A 217 ? 0.9413 0.9310 0.6392 0.2107  0.0061  -0.1119 217 ARG A CG  
1668 C CD  . ARG A 217 ? 1.0018 1.0244 0.7092 0.2241  0.0033  -0.1113 217 ARG A CD  
1669 N NE  . ARG A 217 ? 1.0120 1.0237 0.7053 0.2436  0.0039  -0.1078 217 ARG A NE  
1670 C CZ  . ARG A 217 ? 0.9856 1.0202 0.6946 0.2543  0.0007  -0.1058 217 ARG A CZ  
1671 N NH1 . ARG A 217 ? 0.8691 0.9395 0.6105 0.2467  -0.0025 -0.1078 217 ARG A NH1 
1672 N NH2 . ARG A 217 ? 1.0091 1.0317 0.6998 0.2733  0.0006  -0.1020 217 ARG A NH2 
1673 N N   . TRP A 218 ? 1.0458 0.8629 0.6315 0.1789  0.0254  -0.1173 218 TRP A N   
1674 C CA  . TRP A 218 ? 1.0418 0.8067 0.5900 0.1779  0.0334  -0.1177 218 TRP A CA  
1675 C C   . TRP A 218 ? 1.0485 0.7845 0.5872 0.1833  0.0388  -0.1136 218 TRP A C   
1676 O O   . TRP A 218 ? 1.0522 0.7475 0.5600 0.1897  0.0459  -0.1113 218 TRP A O   
1677 C CB  . TRP A 218 ? 1.0803 0.8221 0.6111 0.1530  0.0352  -0.1248 218 TRP A CB  
1678 C CG  . TRP A 218 ? 1.0811 0.8175 0.6194 0.1319  0.0344  -0.1280 218 TRP A CG  
1679 C CD1 . TRP A 218 ? 1.0658 0.8322 0.6240 0.1177  0.0269  -0.1310 218 TRP A CD1 
1680 C CD2 . TRP A 218 ? 1.1583 0.8567 0.6824 0.1231  0.0413  -0.1281 218 TRP A CD2 
1681 N NE1 . TRP A 218 ? 1.0639 0.8140 0.6215 0.1010  0.0282  -0.1332 218 TRP A NE1 
1682 C CE2 . TRP A 218 ? 1.1403 0.8492 0.6784 0.1030  0.0375  -0.1318 218 TRP A CE2 
1683 C CE3 . TRP A 218 ? 1.1710 0.8276 0.6711 0.1308  0.0504  -0.1246 218 TRP A CE3 
1684 C CZ2 . TRP A 218 ? 1.1566 0.8367 0.6876 0.0889  0.0430  -0.1328 218 TRP A CZ2 
1685 C CZ3 . TRP A 218 ? 1.1953 0.8228 0.6877 0.1172  0.0562  -0.1251 218 TRP A CZ3 
1686 C CH2 . TRP A 218 ? 1.2182 0.8584 0.7274 0.0959  0.0527  -0.1295 218 TRP A CH2 
1687 N N   . PHE A 219 ? 1.0273 0.7824 0.5902 0.1815  0.0361  -0.1120 219 PHE A N   
1688 C CA  . PHE A 219 ? 1.0636 0.7916 0.6175 0.1846  0.0413  -0.1081 219 PHE A CA  
1689 C C   . PHE A 219 ? 1.0122 0.7566 0.5735 0.2089  0.0392  -0.1009 219 PHE A C   
1690 O O   . PHE A 219 ? 1.0753 0.8013 0.6299 0.2136  0.0426  -0.0966 219 PHE A O   
1691 C CB  . PHE A 219 ? 0.9994 0.7355 0.5732 0.1680  0.0400  -0.1107 219 PHE A CB  
1692 C CG  . PHE A 219 ? 0.9605 0.7492 0.5722 0.1693  0.0314  -0.1116 219 PHE A CG  
1693 C CD1 . PHE A 219 ? 0.9600 0.7715 0.5828 0.1570  0.0263  -0.1165 219 PHE A CD1 
1694 C CD2 . PHE A 219 ? 0.9172 0.7336 0.5526 0.1828  0.0284  -0.1074 219 PHE A CD2 
1695 C CE1 . PHE A 219 ? 0.8515 0.7111 0.5084 0.1590  0.0193  -0.1167 219 PHE A CE1 
1696 C CE2 . PHE A 219 ? 0.8671 0.7313 0.5375 0.1828  0.0216  -0.1087 219 PHE A CE2 
1697 C CZ  . PHE A 219 ? 0.8192 0.7043 0.5003 0.1714  0.0176  -0.1132 219 PHE A CZ  
1698 N N   . LEU A 220 ? 0.9873 0.7680 0.5626 0.2237  0.0331  -0.0996 220 LEU A N   
1699 C CA  . LEU A 220 ? 1.0374 0.8412 0.6221 0.2455  0.0293  -0.0938 220 LEU A CA  
1700 C C   . LEU A 220 ? 1.1399 0.9073 0.6875 0.2641  0.0341  -0.0879 220 LEU A C   
1701 O O   . LEU A 220 ? 1.1203 0.8757 0.6486 0.2706  0.0358  -0.0882 220 LEU A O   
1702 C CB  . LEU A 220 ? 1.0048 0.8626 0.6179 0.2530  0.0211  -0.0954 220 LEU A CB  
1703 C CG  . LEU A 220 ? 0.9433 0.8424 0.5947 0.2394  0.0161  -0.0995 220 LEU A CG  
1704 C CD1 . LEU A 220 ? 0.8869 0.8384 0.5641 0.2478  0.0092  -0.1006 220 LEU A CD1 
1705 C CD2 . LEU A 220 ? 0.9570 0.8575 0.6215 0.2370  0.0160  -0.0977 220 LEU A CD2 
1706 N N   . ASN A 221 ? 1.1616 0.9105 0.6977 0.2733  0.0367  -0.0821 221 ASN A N   
1707 C CA  . ASN A 221 ? 1.2670 0.9786 0.7646 0.2926  0.0418  -0.0749 221 ASN A CA  
1708 C C   . ASN A 221 ? 1.2949 1.0410 0.7973 0.3192  0.0344  -0.0702 221 ASN A C   
1709 O O   . ASN A 221 ? 1.2929 1.0915 0.8296 0.3210  0.0256  -0.0728 221 ASN A O   
1710 C CB  . ASN A 221 ? 1.2616 0.9377 0.7419 0.2913  0.0482  -0.0699 221 ASN A CB  
1711 C CG  . ASN A 221 ? 1.2104 0.9228 0.7184 0.2969  0.0416  -0.0677 221 ASN A CG  
1712 O OD1 . ASN A 221 ? 1.1456 0.9099 0.6848 0.3027  0.0323  -0.0698 221 ASN A OD1 
1713 N ND2 . ASN A 221 ? 1.2429 0.9277 0.7390 0.2940  0.0470  -0.0638 221 ASN A ND2 
1714 N N   . ARG A 222 ? 1.4457 1.1608 0.9112 0.3400  0.0382  -0.0632 222 ARG A N   
1715 C CA  . ARG A 222 ? 1.5296 1.2700 0.9919 0.3681  0.0316  -0.0569 222 ARG A CA  
1716 C C   . ARG A 222 ? 1.4674 1.1964 0.9209 0.3759  0.0325  -0.0505 222 ARG A C   
1717 O O   . ARG A 222 ? 1.4505 1.2200 0.9212 0.3892  0.0240  -0.0488 222 ARG A O   
1718 C CB  . ARG A 222 ? 1.6897 1.4016 1.1126 0.3900  0.0353  -0.0513 222 ARG A CB  
1719 C CG  . ARG A 222 ? 1.6976 1.3385 1.0729 0.3906  0.0479  -0.0454 222 ARG A CG  
1720 C CD  . ARG A 222 ? 1.7733 1.3787 1.1409 0.3643  0.0564  -0.0521 222 ARG A CD  
1721 N NE  . ARG A 222 ? 1.7566 1.3846 1.1369 0.3603  0.0529  -0.0586 222 ARG A NE  
1722 C CZ  . ARG A 222 ? 1.8203 1.4221 1.1701 0.3712  0.0574  -0.0571 222 ARG A CZ  
1723 N NH1 . ARG A 222 ? 1.8451 1.3954 1.1485 0.3871  0.0659  -0.0489 222 ARG A NH1 
1724 N NH2 . ARG A 222 ? 1.8239 1.4502 1.1881 0.3665  0.0538  -0.0634 222 ARG A NH2 
1725 N N   . PHE A 223 ? 1.4162 1.0914 0.8433 0.3659  0.0429  -0.0477 223 PHE A N   
1726 C CA  . PHE A 223 ? 1.4246 1.0809 0.8380 0.3721  0.0458  -0.0410 223 PHE A CA  
1727 C C   . PHE A 223 ? 1.2975 1.0042 0.7539 0.3649  0.0370  -0.0448 223 PHE A C   
1728 O O   . PHE A 223 ? 1.2599 1.0022 0.7540 0.3476  0.0322  -0.0530 223 PHE A O   
1729 C CB  . PHE A 223 ? 1.4202 1.0164 0.8077 0.3535  0.0589  -0.0405 223 PHE A CB  
1730 C CG  . PHE A 223 ? 1.5828 1.1202 0.9155 0.3698  0.0693  -0.0310 223 PHE A CG  
1731 C CD1 . PHE A 223 ? 1.6852 1.1715 0.9881 0.3572  0.0805  -0.0327 223 PHE A CD1 
1732 C CD2 . PHE A 223 ? 1.6038 1.1366 0.9123 0.3977  0.0681  -0.0207 223 PHE A CD2 
1733 C CE1 . PHE A 223 ? 1.7575 1.1862 1.0070 0.3716  0.0915  -0.0239 223 PHE A CE1 
1734 C CE2 . PHE A 223 ? 1.7040 1.1786 0.9568 0.4144  0.0789  -0.0108 223 PHE A CE2 
1735 C CZ  . PHE A 223 ? 1.8208 1.2418 1.0440 0.4007  0.0912  -0.0123 223 PHE A CZ  
1736 N N   . THR A 224 ? 1.2524 0.9622 0.7017 0.3788  0.0351  -0.0387 224 THR A N   
1737 C CA  . THR A 224 ? 1.1801 0.9293 0.6659 0.3699  0.0287  -0.0423 224 THR A CA  
1738 C C   . THR A 224 ? 1.2300 0.9413 0.6968 0.3665  0.0363  -0.0369 224 THR A C   
1739 O O   . THR A 224 ? 1.2962 0.9526 0.7224 0.3703  0.0466  -0.0306 224 THR A O   
1740 C CB  . THR A 224 ? 1.1905 0.9952 0.6944 0.3890  0.0165  -0.0423 224 THR A CB  
1741 O OG1 . THR A 224 ? 1.0535 0.8973 0.5976 0.3740  0.0110  -0.0483 224 THR A OG1 
1742 C CG2 . THR A 224 ? 1.2262 1.0148 0.6956 0.4153  0.0164  -0.0328 224 THR A CG2 
1743 N N   . THR A 225 ? 1.1491 0.8880 0.6437 0.3588  0.0322  -0.0393 225 THR A N   
1744 C CA  . THR A 225 ? 1.1917 0.8974 0.6704 0.3550  0.0394  -0.0344 225 THR A CA  
1745 C C   . THR A 225 ? 1.1914 0.9384 0.6945 0.3603  0.0312  -0.0350 225 THR A C   
1746 O O   . THR A 225 ? 1.1359 0.9344 0.6634 0.3684  0.0203  -0.0389 225 THR A O   
1747 C CB  . THR A 225 ? 1.2654 0.9420 0.7515 0.3263  0.0484  -0.0390 225 THR A CB  
1748 O OG1 . THR A 225 ? 1.3027 0.9414 0.7674 0.3237  0.0571  -0.0333 225 THR A OG1 
1749 C CG2 . THR A 225 ? 1.1999 0.9216 0.7357 0.3068  0.0419  -0.0483 225 THR A CG2 
1750 N N   . THR A 226 ? 1.1787 0.9032 0.6746 0.3548  0.0369  -0.0317 226 THR A N   
1751 C CA  . THR A 226 ? 1.1925 0.9503 0.7083 0.3584  0.0305  -0.0324 226 THR A CA  
1752 C C   . THR A 226 ? 1.1614 0.9197 0.7059 0.3323  0.0342  -0.0378 226 THR A C   
1753 O O   . THR A 226 ? 1.2223 0.9410 0.7565 0.3165  0.0441  -0.0375 226 THR A O   
1754 C CB  . THR A 226 ? 1.2470 0.9787 0.7238 0.3808  0.0334  -0.0219 226 THR A CB  
1755 O OG1 . THR A 226 ? 1.2892 0.9759 0.7505 0.3680  0.0450  -0.0183 226 THR A OG1 
1756 C CG2 . THR A 226 ? 1.1874 0.8919 0.6208 0.4048  0.0356  -0.0138 226 THR A CG2 
1757 N N   . LEU A 227 ? 1.0756 0.8785 0.6547 0.3281  0.0266  -0.0429 227 LEU A N   
1758 C CA  . LEU A 227 ? 1.0995 0.9044 0.7059 0.3057  0.0300  -0.0475 227 LEU A CA  
1759 C C   . LEU A 227 ? 1.1737 0.9314 0.7542 0.3028  0.0404  -0.0411 227 LEU A C   
1760 O O   . LEU A 227 ? 1.2190 0.9615 0.8120 0.2826  0.0467  -0.0439 227 LEU A O   
1761 C CB  . LEU A 227 ? 1.0131 0.8690 0.6543 0.3046  0.0210  -0.0528 227 LEU A CB  
1762 C CG  . LEU A 227 ? 1.0662 0.9204 0.7312 0.2850  0.0253  -0.0559 227 LEU A CG  
1763 C CD1 . LEU A 227 ? 1.0533 0.9117 0.7447 0.2632  0.0275  -0.0624 227 LEU A CD1 
1764 C CD2 . LEU A 227 ? 0.9370 0.8318 0.6265 0.2869  0.0182  -0.0596 227 LEU A CD2 
1765 N N   . ASN A 228 ? 1.1761 0.9101 0.7191 0.3234  0.0427  -0.0323 228 ASN A N   
1766 C CA  . ASN A 228 ? 1.1918 0.8804 0.7075 0.3216  0.0535  -0.0255 228 ASN A CA  
1767 C C   . ASN A 228 ? 1.2774 0.9121 0.7645 0.3114  0.0657  -0.0229 228 ASN A C   
1768 O O   . ASN A 228 ? 1.3453 0.9528 0.8324 0.2929  0.0748  -0.0237 228 ASN A O   
1769 C CB  . ASN A 228 ? 1.2246 0.9064 0.7076 0.3486  0.0520  -0.0164 228 ASN A CB  
1770 C CG  . ASN A 228 ? 1.0643 0.7713 0.5657 0.3489  0.0480  -0.0174 228 ASN A CG  
1771 O OD1 . ASN A 228 ? 1.0062 0.7398 0.5471 0.3300  0.0455  -0.0253 228 ASN A OD1 
1772 N ND2 . ASN A 228 ? 1.1160 0.8151 0.5873 0.3718  0.0472  -0.0094 228 ASN A ND2 
1773 N N   . ASP A 229 ? 1.2939 0.9135 0.7572 0.3221  0.0663  -0.0205 229 ASP A N   
1774 C CA  . ASP A 229 ? 1.4067 0.9728 0.8397 0.3118  0.0786  -0.0186 229 ASP A CA  
1775 C C   . ASP A 229 ? 1.4051 0.9789 0.8672 0.2853  0.0791  -0.0286 229 ASP A C   
1776 O O   . ASP A 229 ? 1.3852 0.9180 0.8312 0.2681  0.0900  -0.0294 229 ASP A O   
1777 C CB  . ASP A 229 ? 1.4070 0.9515 0.8030 0.3317  0.0797  -0.0129 229 ASP A CB  
1778 C CG  . ASP A 229 ? 1.4223 0.9587 0.7840 0.3622  0.0787  -0.0021 229 ASP A CG  
1779 O OD1 . ASP A 229 ? 1.3835 0.9274 0.7467 0.3676  0.0777  0.0013  229 ASP A OD1 
1780 O OD2 . ASP A 229 ? 1.4980 1.0189 0.8287 0.3816  0.0791  0.0034  229 ASP A OD2 
1781 N N   . PHE A 230 ? 1.4347 1.0588 0.9364 0.2818  0.0680  -0.0363 230 PHE A N   
1782 C CA  . PHE A 230 ? 1.4160 1.0491 0.9457 0.2574  0.0683  -0.0453 230 PHE A CA  
1783 C C   . PHE A 230 ? 1.3811 1.0046 0.9248 0.2384  0.0739  -0.0473 230 PHE A C   
1784 O O   . PHE A 230 ? 1.4027 1.0026 0.9450 0.2182  0.0806  -0.0513 230 PHE A O   
1785 C CB  . PHE A 230 ? 1.3493 1.0389 0.9195 0.2569  0.0564  -0.0523 230 PHE A CB  
1786 C CG  . PHE A 230 ? 1.3908 1.0906 0.9892 0.2334  0.0566  -0.0606 230 PHE A CG  
1787 C CD1 . PHE A 230 ? 1.3857 1.0579 0.9692 0.2214  0.0619  -0.0638 230 PHE A CD1 
1788 C CD2 . PHE A 230 ? 1.2965 1.0293 0.9325 0.2231  0.0525  -0.0651 230 PHE A CD2 
1789 C CE1 . PHE A 230 ? 1.2575 0.9379 0.8628 0.2008  0.0617  -0.0713 230 PHE A CE1 
1790 C CE2 . PHE A 230 ? 1.2109 0.9501 0.8685 0.2038  0.0530  -0.0718 230 PHE A CE2 
1791 C CZ  . PHE A 230 ? 1.2149 0.9284 0.8566 0.1931  0.0573  -0.0749 230 PHE A CZ  
1792 N N   . ASN A 231 ? 1.2949 0.9373 0.8521 0.2440  0.0710  -0.0450 231 ASN A N   
1793 C CA  . ASN A 231 ? 1.2599 0.8946 0.8316 0.2266  0.0763  -0.0468 231 ASN A CA  
1794 C C   . ASN A 231 ? 1.3551 0.9321 0.8895 0.2187  0.0903  -0.0420 231 ASN A C   
1795 O O   . ASN A 231 ? 1.3769 0.9393 0.9194 0.1980  0.0967  -0.0455 231 ASN A O   
1796 C CB  . ASN A 231 ? 1.1729 0.8384 0.7642 0.2351  0.0707  -0.0453 231 ASN A CB  
1797 C CG  . ASN A 231 ? 1.1972 0.9141 0.8356 0.2276  0.0613  -0.0531 231 ASN A CG  
1798 O OD1 . ASN A 231 ? 1.1578 0.9115 0.8128 0.2384  0.0531  -0.0537 231 ASN A OD1 
1799 N ND2 . ASN A 231 ? 1.1940 0.9131 0.8523 0.2091  0.0626  -0.0592 231 ASN A ND2 
1800 N N   . LEU A 232 ? 1.3754 0.9183 0.8673 0.2346  0.0959  -0.0338 232 LEU A N   
1801 C CA  . LEU A 232 ? 1.4233 0.9069 0.8751 0.2256  0.1112  -0.0294 232 LEU A CA  
1802 C C   . LEU A 232 ? 1.4141 0.8787 0.8636 0.2048  0.1160  -0.0362 232 LEU A C   
1803 O O   . LEU A 232 ? 1.4558 0.8845 0.8912 0.1846  0.1276  -0.0375 232 LEU A O   
1804 C CB  . LEU A 232 ? 1.4954 0.9437 0.8983 0.2485  0.1169  -0.0186 232 LEU A CB  
1805 C CG  . LEU A 232 ? 1.6170 1.0593 1.0028 0.2657  0.1189  -0.0095 232 LEU A CG  
1806 C CD1 . LEU A 232 ? 1.6035 1.0347 0.9988 0.2479  0.1266  -0.0103 232 LEU A CD1 
1807 C CD2 . LEU A 232 ? 1.5745 1.0702 0.9845 0.2865  0.1035  -0.0095 232 LEU A CD2 
1808 N N   . VAL A 233 ? 1.4031 0.8927 0.8665 0.2082  0.1072  -0.0412 233 VAL A N   
1809 C CA  . VAL A 233 ? 1.3614 0.8393 0.8260 0.1881  0.1099  -0.0488 233 VAL A CA  
1810 C C   . VAL A 233 ? 1.3273 0.8344 0.8328 0.1669  0.1056  -0.0576 233 VAL A C   
1811 O O   . VAL A 233 ? 1.3156 0.8035 0.8182 0.1440  0.1113  -0.0635 233 VAL A O   
1812 C CB  . VAL A 233 ? 1.4129 0.9068 0.8754 0.2011  0.1025  -0.0503 233 VAL A CB  
1813 C CG1 . VAL A 233 ? 1.3899 0.8879 0.8649 0.1806  0.1014  -0.0600 233 VAL A CG1 
1814 C CG2 . VAL A 233 ? 1.4001 0.8522 0.8143 0.2184  0.1099  -0.0419 233 VAL A CG2 
1815 N N   . ALA A 234 ? 1.3331 0.8857 0.8752 0.1735  0.0959  -0.0587 234 ALA A N   
1816 C CA  . ALA A 234 ? 1.2745 0.8524 0.8534 0.1558  0.0927  -0.0657 234 ALA A CA  
1817 C C   . ALA A 234 ? 1.3090 0.8560 0.8804 0.1375  0.1034  -0.0652 234 ALA A C   
1818 O O   . ALA A 234 ? 1.2829 0.8195 0.8594 0.1147  0.1073  -0.0714 234 ALA A O   
1819 C CB  . ALA A 234 ? 1.1594 0.7879 0.7752 0.1675  0.0821  -0.0659 234 ALA A CB  
1820 N N   . MET A 235 ? 1.3269 0.8601 0.8855 0.1465  0.1084  -0.0580 235 MET A N   
1821 C CA  . MET A 235 ? 1.3605 0.8666 0.9127 0.1299  0.1192  -0.0570 235 MET A CA  
1822 C C   . MET A 235 ? 1.3402 0.7984 0.8604 0.1094  0.1322  -0.0589 235 MET A C   
1823 O O   . MET A 235 ? 1.3102 0.7564 0.8363 0.0857  0.1394  -0.0629 235 MET A O   
1824 C CB  . MET A 235 ? 1.4689 0.9663 1.0070 0.1457  0.1227  -0.0482 235 MET A CB  
1825 C CG  . MET A 235 ? 1.5473 1.0499 1.1057 0.1335  0.1265  -0.0488 235 MET A CG  
1826 S SD  . MET A 235 ? 1.6812 1.2287 1.2922 0.1185  0.1168  -0.0586 235 MET A SD  
1827 C CE  . MET A 235 ? 1.3347 0.9307 0.9676 0.1400  0.1007  -0.0603 235 MET A CE  
1828 N N   . LYS A 236 ? 1.3270 0.7577 0.8130 0.1166  0.1359  -0.0564 236 LYS A N   
1829 C CA  . LYS A 236 ? 1.3377 0.7230 0.7931 0.0945  0.1491  -0.0592 236 LYS A CA  
1830 C C   . LYS A 236 ? 1.3726 0.7725 0.8499 0.0692  0.1456  -0.0703 236 LYS A C   
1831 O O   . LYS A 236 ? 1.4267 0.7981 0.8888 0.0431  0.1561  -0.0750 236 LYS A O   
1832 C CB  . LYS A 236 ? 1.4458 0.7979 0.8595 0.1077  0.1539  -0.0545 236 LYS A CB  
1833 C CG  . LYS A 236 ? 1.5064 0.8065 0.8829 0.0849  0.1700  -0.0568 236 LYS A CG  
1834 C CD  . LYS A 236 ? 1.5512 0.8194 0.8879 0.0979  0.1742  -0.0530 236 LYS A CD  
1835 C CE  . LYS A 236 ? 1.5876 0.8078 0.8768 0.1120  0.1882  -0.0415 236 LYS A CE  
1836 N NZ  . LYS A 236 ? 1.6391 0.8017 0.8847 0.0912  0.2072  -0.0425 236 LYS A NZ  
1837 N N   . TYR A 237 ? 1.3368 0.7813 0.8482 0.0756  0.1316  -0.0748 237 TYR A N   
1838 C CA  . TYR A 237 ? 1.2999 0.7622 0.8310 0.0551  0.1264  -0.0849 237 TYR A CA  
1839 C C   . TYR A 237 ? 1.2428 0.7413 0.8152 0.0460  0.1199  -0.0891 237 TYR A C   
1840 O O   . TYR A 237 ? 1.2296 0.7471 0.8192 0.0312  0.1142  -0.0968 237 TYR A O   
1841 C CB  . TYR A 237 ? 1.2214 0.7018 0.7522 0.0696  0.1169  -0.0868 237 TYR A CB  
1842 C CG  . TYR A 237 ? 1.2623 0.7052 0.7534 0.0705  0.1238  -0.0856 237 TYR A CG  
1843 C CD1 . TYR A 237 ? 1.2567 0.6833 0.7362 0.0461  0.1274  -0.0937 237 TYR A CD1 
1844 C CD2 . TYR A 237 ? 1.2690 0.6913 0.7325 0.0942  0.1274  -0.0766 237 TYR A CD2 
1845 C CE1 . TYR A 237 ? 1.3429 0.7336 0.7855 0.0460  0.1346  -0.0931 237 TYR A CE1 
1846 C CE2 . TYR A 237 ? 1.3275 0.7111 0.7518 0.0952  0.1351  -0.0751 237 TYR A CE2 
1847 C CZ  . TYR A 237 ? 1.3610 0.7282 0.7754 0.0710  0.1390  -0.0835 237 TYR A CZ  
1848 O OH  . TYR A 237 ? 1.4217 0.7500 0.7974 0.0707  0.1472  -0.0828 237 TYR A OH  
1849 N N   . ASN A 238 ? 1.2939 0.8011 0.8813 0.0529  0.1211  -0.0843 238 ASN A N   
1850 C CA  . ASN A 238 ? 1.2435 0.7813 0.8691 0.0437  0.1165  -0.0878 238 ASN A CA  
1851 C C   . ASN A 238 ? 1.1704 0.7524 0.8254 0.0613  0.1035  -0.0888 238 ASN A C   
1852 O O   . ASN A 238 ? 1.1405 0.7592 0.8338 0.0486  0.0963  -0.0896 238 ASN A O   
1853 C CB  . ASN A 238 ? 1.3173 0.8496 0.9501 0.0096  0.1203  -0.0965 238 ASN A CB  
1854 C CG  . ASN A 238 ? 1.2965 0.8573 0.9687 -0.0057 0.1195  -0.0919 238 ASN A CG  
1855 O OD1 . ASN A 238 ? 1.3630 0.9308 1.0484 -0.0348 0.1220  -0.0934 238 ASN A OD1 
1856 N ND2 . ASN A 238 ? 1.2947 0.8793 0.9898 0.0139  0.1147  -0.0866 238 ASN A ND2 
1857 N N   . TYR A 239 ? 1.1360 0.7322 0.7867 0.0865  0.0971  -0.0845 239 TYR A N   
1858 C CA  . TYR A 239 ? 1.0772 0.7192 0.7589 0.1002  0.0857  -0.0860 239 TYR A CA  
1859 C C   . TYR A 239 ? 1.1064 0.7704 0.8085 0.1136  0.0834  -0.0811 239 TYR A C   
1860 O O   . TYR A 239 ? 1.1584 0.8065 0.8421 0.1235  0.0871  -0.0751 239 TYR A O   
1861 C CB  . TYR A 239 ? 0.9990 0.6509 0.6686 0.1166  0.0796  -0.0855 239 TYR A CB  
1862 C CG  . TYR A 239 ? 0.9997 0.6498 0.6631 0.1059  0.0774  -0.0919 239 TYR A CG  
1863 C CD1 . TYR A 239 ? 1.0362 0.6504 0.6768 0.0834  0.0849  -0.0959 239 TYR A CD1 
1864 C CD2 . TYR A 239 ? 0.9391 0.6254 0.6194 0.1162  0.0678  -0.0945 239 TYR A CD2 
1865 C CE1 . TYR A 239 ? 0.9977 0.6124 0.6315 0.0715  0.0820  -0.1026 239 TYR A CE1 
1866 C CE2 . TYR A 239 ? 0.9673 0.6528 0.6400 0.1068  0.0653  -0.1003 239 TYR A CE2 
1867 C CZ  . TYR A 239 ? 0.9402 0.5946 0.5939 0.0832  0.0710  -0.1028 239 TYR A CZ  
1868 O OH  . TYR A 239 ? 0.9254 0.5938 0.5834 0.0703  0.0652  -0.1050 239 TYR A OH  
1869 N N   . GLU A 240 ? 1.1193 0.8182 0.8574 0.1138  0.0780  -0.0832 240 GLU A N   
1870 C CA  . GLU A 240 ? 1.1042 0.8281 0.8625 0.1261  0.0747  -0.0794 240 GLU A CA  
1871 C C   . GLU A 240 ? 1.1348 0.8733 0.8828 0.1457  0.0688  -0.0765 240 GLU A C   
1872 O O   . GLU A 240 ? 1.1194 0.8700 0.8640 0.1517  0.0637  -0.0786 240 GLU A O   
1873 C CB  . GLU A 240 ? 1.0291 0.7896 0.8281 0.1241  0.0702  -0.0819 240 GLU A CB  
1874 C CG  . GLU A 240 ? 1.0622 0.8664 0.8842 0.1353  0.0603  -0.0842 240 GLU A CG  
1875 C CD  . GLU A 240 ? 1.1497 0.9931 1.0196 0.1204  0.0547  -0.0818 240 GLU A CD  
1876 O OE1 . GLU A 240 ? 1.1129 0.9521 0.9977 0.0992  0.0567  -0.0767 240 GLU A OE1 
1877 O OE2 . GLU A 240 ? 1.1344 1.0157 1.0290 0.1272  0.0483  -0.0840 240 GLU A OE2 
1878 N N   . PRO A 241 ? 1.1699 0.9069 0.9112 0.1558  0.0697  -0.0715 241 PRO A N   
1879 C CA  . PRO A 241 ? 1.1046 0.8532 0.8325 0.1746  0.0646  -0.0682 241 PRO A CA  
1880 C C   . PRO A 241 ? 1.0451 0.8415 0.8012 0.1810  0.0544  -0.0722 241 PRO A C   
1881 O O   . PRO A 241 ? 1.0404 0.8668 0.8300 0.1751  0.0511  -0.0757 241 PRO A O   
1882 C CB  . PRO A 241 ? 1.1058 0.8478 0.8271 0.1812  0.0673  -0.0631 241 PRO A CB  
1883 C CG  . PRO A 241 ? 1.1926 0.8999 0.9057 0.1660  0.0775  -0.0619 241 PRO A CG  
1884 C CD  . PRO A 241 ? 1.1361 0.8548 0.8754 0.1500  0.0767  -0.0682 241 PRO A CD  
1885 N N   . LEU A 242 ? 1.0699 0.8714 0.8109 0.1926  0.0502  -0.0715 242 LEU A N   
1886 C CA  . LEU A 242 ? 1.0293 0.8746 0.7911 0.1999  0.0410  -0.0748 242 LEU A CA  
1887 C C   . LEU A 242 ? 1.0245 0.8911 0.7885 0.2128  0.0364  -0.0726 242 LEU A C   
1888 O O   . LEU A 242 ? 1.0514 0.9002 0.7859 0.2272  0.0372  -0.0672 242 LEU A O   
1889 C CB  . LEU A 242 ? 0.9687 0.8100 0.7112 0.2081  0.0385  -0.0746 242 LEU A CB  
1890 C CG  . LEU A 242 ? 0.8898 0.7675 0.6539 0.2072  0.0316  -0.0799 242 LEU A CG  
1891 C CD1 . LEU A 242 ? 0.9973 0.8590 0.7351 0.2151  0.0316  -0.0785 242 LEU A CD1 
1892 C CD2 . LEU A 242 ? 0.9144 0.8387 0.7018 0.2145  0.0234  -0.0821 242 LEU A CD2 
1893 N N   . THR A 243 ? 0.9519 0.8551 0.7487 0.2079  0.0319  -0.0769 243 THR A N   
1894 C CA  . THR A 243 ? 0.9578 0.8871 0.7604 0.2176  0.0266  -0.0771 243 THR A CA  
1895 C C   . THR A 243 ? 0.9480 0.9166 0.7609 0.2250  0.0177  -0.0813 243 THR A C   
1896 O O   . THR A 243 ? 0.9219 0.9028 0.7458 0.2196  0.0160  -0.0846 243 THR A O   
1897 C CB  . THR A 243 ? 0.9174 0.8612 0.7486 0.2062  0.0281  -0.0799 243 THR A CB  
1898 O OG1 . THR A 243 ? 0.9281 0.9079 0.7917 0.1976  0.0239  -0.0861 243 THR A OG1 
1899 C CG2 . THR A 243 ? 0.9714 0.8833 0.8029 0.1939  0.0366  -0.0778 243 THR A CG2 
1900 N N   . GLN A 244 ? 1.0036 0.9932 0.8119 0.2377  0.0120  -0.0816 244 GLN A N   
1901 C CA  . GLN A 244 ? 0.9582 0.9898 0.7770 0.2449  0.0030  -0.0868 244 GLN A CA  
1902 C C   . GLN A 244 ? 0.8833 0.9484 0.7403 0.2285  0.0014  -0.0946 244 GLN A C   
1903 O O   . GLN A 244 ? 0.8749 0.9704 0.7440 0.2281  -0.0038 -0.0996 244 GLN A O   
1904 C CB  . GLN A 244 ? 0.9864 1.0349 0.7923 0.2621  -0.0031 -0.0863 244 GLN A CB  
1905 C CG  . GLN A 244 ? 0.9513 1.0522 0.7765 0.2651  -0.0128 -0.0947 244 GLN A CG  
1906 C CD  . GLN A 244 ? 0.9416 1.0616 0.7704 0.2668  -0.0169 -0.0977 244 GLN A CD  
1907 O OE1 . GLN A 244 ? 0.8829 0.9909 0.6863 0.2822  -0.0186 -0.0928 244 GLN A OE1 
1908 N NE2 . GLN A 244 ? 0.8814 1.0315 0.7415 0.2514  -0.0182 -0.1056 244 GLN A NE2 
1909 N N   . ASP A 245 ? 0.8871 0.9464 0.7627 0.2149  0.0064  -0.0954 245 ASP A N   
1910 C CA  . ASP A 245 ? 0.8561 0.9404 0.7658 0.1991  0.0067  -0.1014 245 ASP A CA  
1911 C C   . ASP A 245 ? 0.8553 0.9349 0.7706 0.1921  0.0084  -0.1014 245 ASP A C   
1912 O O   . ASP A 245 ? 0.8528 0.9607 0.7896 0.1847  0.0060  -0.1065 245 ASP A O   
1913 C CB  . ASP A 245 ? 0.8814 0.9549 0.8074 0.1876  0.0127  -0.1007 245 ASP A CB  
1914 C CG  . ASP A 245 ? 0.9671 1.0737 0.9209 0.1790  0.0108  -0.1074 245 ASP A CG  
1915 O OD1 . ASP A 245 ? 0.9867 1.1172 0.9600 0.1709  0.0092  -0.1122 245 ASP A OD1 
1916 O OD2 . ASP A 245 ? 1.0439 1.1518 0.9992 0.1798  0.0115  -0.1081 245 ASP A OD2 
1917 N N   . HIS A 246 ? 0.8722 0.9158 0.7672 0.1938  0.0128  -0.0961 246 HIS A N   
1918 C CA  . HIS A 246 ? 0.8682 0.9053 0.7640 0.1887  0.0140  -0.0966 246 HIS A CA  
1919 C C   . HIS A 246 ? 0.8357 0.8916 0.7226 0.1981  0.0081  -0.0984 246 HIS A C   
1920 O O   . HIS A 246 ? 0.7749 0.8502 0.6774 0.1918  0.0066  -0.1020 246 HIS A O   
1921 C CB  . HIS A 246 ? 0.8402 0.8323 0.7119 0.1882  0.0204  -0.0918 246 HIS A CB  
1922 C CG  . HIS A 246 ? 0.8416 0.8167 0.7248 0.1770  0.0264  -0.0908 246 HIS A CG  
1923 N ND1 . HIS A 246 ? 0.8711 0.8070 0.7319 0.1770  0.0326  -0.0867 246 HIS A ND1 
1924 C CD2 . HIS A 246 ? 0.7562 0.7486 0.6710 0.1661  0.0275  -0.0931 246 HIS A CD2 
1925 C CE1 . HIS A 246 ? 0.8192 0.7502 0.6977 0.1665  0.0368  -0.0869 246 HIS A CE1 
1926 N NE2 . HIS A 246 ? 0.7432 0.7081 0.6548 0.1607  0.0337  -0.0903 246 HIS A NE2 
1927 N N   . VAL A 247 ? 0.8578 0.9102 0.7201 0.2141  0.0047  -0.0958 247 VAL A N   
1928 C CA  . VAL A 247 ? 0.8031 0.8765 0.6578 0.2249  -0.0014 -0.0975 247 VAL A CA  
1929 C C   . VAL A 247 ? 0.7936 0.9148 0.6785 0.2181  -0.0066 -0.1052 247 VAL A C   
1930 O O   . VAL A 247 ? 0.7821 0.9212 0.6744 0.2159  -0.0088 -0.1082 247 VAL A O   
1931 C CB  . VAL A 247 ? 0.8731 0.9394 0.6986 0.2454  -0.0048 -0.0932 247 VAL A CB  
1932 C CG1 . VAL A 247 ? 0.8782 0.9649 0.6948 0.2581  -0.0109 -0.0943 247 VAL A CG1 
1933 C CG2 . VAL A 247 ? 0.9004 0.9157 0.6949 0.2500  0.0022  -0.0855 247 VAL A CG2 
1934 N N   . ASP A 248 ? 0.8007 0.9422 0.7030 0.2132  -0.0080 -0.1090 248 ASP A N   
1935 C CA  . ASP A 248 ? 0.7740 0.9598 0.7027 0.2055  -0.0121 -0.1176 248 ASP A CA  
1936 C C   . ASP A 248 ? 0.7646 0.9566 0.7197 0.1872  -0.0075 -0.1203 248 ASP A C   
1937 O O   . ASP A 248 ? 0.6996 0.9230 0.6715 0.1808  -0.0096 -0.1264 248 ASP A O   
1938 C CB  . ASP A 248 ? 0.8492 1.0529 0.7866 0.2053  -0.0143 -0.1218 248 ASP A CB  
1939 C CG  . ASP A 248 ? 0.8326 1.0680 0.7594 0.2207  -0.0233 -0.1263 248 ASP A CG  
1940 O OD1 . ASP A 248 ? 0.7839 1.0252 0.6960 0.2326  -0.0275 -0.1249 248 ASP A OD1 
1941 O OD2 . ASP A 248 ? 0.7753 1.0310 0.7088 0.2213  -0.0264 -0.1314 248 ASP A OD2 
1942 N N   . ILE A 249 ? 0.7650 0.9292 0.7247 0.1788  -0.0011 -0.1159 249 ILE A N   
1943 C CA  . ILE A 249 ? 0.7743 0.9434 0.7568 0.1643  0.0029  -0.1170 249 ILE A CA  
1944 C C   . ILE A 249 ? 0.7364 0.9050 0.7094 0.1677  0.0016  -0.1164 249 ILE A C   
1945 O O   . ILE A 249 ? 0.6789 0.8724 0.6694 0.1601  0.0013  -0.1202 249 ILE A O   
1946 C CB  . ILE A 249 ? 0.7639 0.9052 0.7522 0.1572  0.0091  -0.1124 249 ILE A CB  
1947 C CG1 . ILE A 249 ? 0.7775 0.9329 0.7975 0.1420  0.0129  -0.1137 249 ILE A CG1 
1948 C CG2 . ILE A 249 ? 0.7776 0.8826 0.7402 0.1636  0.0112  -0.1073 249 ILE A CG2 
1949 C CD1 . ILE A 249 ? 0.8249 0.9715 0.8611 0.1343  0.0176  -0.1115 249 ILE A CD1 
1950 N N   . LEU A 250 ? 0.7140 0.8530 0.6574 0.1789  0.0015  -0.1117 250 LEU A N   
1951 C CA  . LEU A 250 ? 0.7571 0.8907 0.6859 0.1839  0.0004  -0.1110 250 LEU A CA  
1952 C C   . LEU A 250 ? 0.7670 0.9330 0.6958 0.1913  -0.0055 -0.1147 250 LEU A C   
1953 O O   . LEU A 250 ? 0.7610 0.9251 0.6766 0.1974  -0.0069 -0.1140 250 LEU A O   
1954 C CB  . LEU A 250 ? 0.7457 0.8368 0.6393 0.1941  0.0025  -0.1054 250 LEU A CB  
1955 C CG  . LEU A 250 ? 0.7317 0.7859 0.6178 0.1865  0.0088  -0.1028 250 LEU A CG  
1956 C CD1 . LEU A 250 ? 0.7226 0.7352 0.5714 0.1963  0.0116  -0.0978 250 LEU A CD1 
1957 C CD2 . LEU A 250 ? 0.6522 0.7086 0.5467 0.1776  0.0100  -0.1054 250 LEU A CD2 
1958 N N   . GLY A 251 ? 0.8519 1.0477 0.7941 0.1911  -0.0091 -0.1192 251 GLY A N   
1959 C CA  . GLY A 251 ? 0.7879 1.0141 0.7259 0.2008  -0.0156 -0.1231 251 GLY A CA  
1960 C C   . GLY A 251 ? 0.7469 1.0011 0.6984 0.1947  -0.0166 -0.1278 251 GLY A C   
1961 O O   . GLY A 251 ? 0.7655 1.0271 0.7027 0.2061  -0.0204 -0.1274 251 GLY A O   
1962 N N   . PRO A 252 ? 0.6801 0.9499 0.6589 0.1769  -0.0125 -0.1318 252 PRO A N   
1963 C CA  . PRO A 252 ? 0.6435 0.9391 0.6349 0.1697  -0.0121 -0.1358 252 PRO A CA  
1964 C C   . PRO A 252 ? 0.6757 0.9518 0.6531 0.1742  -0.0107 -0.1308 252 PRO A C   
1965 O O   . PRO A 252 ? 0.6674 0.9619 0.6439 0.1760  -0.0123 -0.1329 252 PRO A O   
1966 C CB  . PRO A 252 ? 0.6436 0.9517 0.6656 0.1494  -0.0060 -0.1391 252 PRO A CB  
1967 C CG  . PRO A 252 ? 0.6331 0.9342 0.6596 0.1476  -0.0056 -0.1398 252 PRO A CG  
1968 C CD  . PRO A 252 ? 0.6890 0.9574 0.6891 0.1630  -0.0080 -0.1330 252 PRO A CD  
1969 N N   . LEU A 253 ? 0.6901 0.9298 0.6559 0.1753  -0.0074 -0.1251 253 LEU A N   
1970 C CA  . LEU A 253 ? 0.6702 0.8887 0.6183 0.1796  -0.0061 -0.1217 253 LEU A CA  
1971 C C   . LEU A 253 ? 0.6938 0.8980 0.6111 0.1975  -0.0099 -0.1189 253 LEU A C   
1972 O O   . LEU A 253 ? 0.6556 0.8627 0.5628 0.2026  -0.0110 -0.1188 253 LEU A O   
1973 C CB  . LEU A 253 ? 0.6270 0.8108 0.5697 0.1747  -0.0016 -0.1181 253 LEU A CB  
1974 C CG  . LEU A 253 ? 0.5866 0.7785 0.5564 0.1594  0.0030  -0.1188 253 LEU A CG  
1975 C CD1 . LEU A 253 ? 0.5253 0.6821 0.4839 0.1586  0.0059  -0.1161 253 LEU A CD1 
1976 C CD2 . LEU A 253 ? 0.5619 0.7726 0.5403 0.1541  0.0041  -0.1202 253 LEU A CD2 
1977 N N   . SER A 254 ? 0.7134 0.9002 0.6150 0.2076  -0.0114 -0.1160 254 SER A N   
1978 C CA  . SER A 254 ? 0.7250 0.9029 0.5995 0.2264  -0.0149 -0.1128 254 SER A CA  
1979 C C   . SER A 254 ? 0.6936 0.9138 0.5769 0.2325  -0.0207 -0.1174 254 SER A C   
1980 O O   . SER A 254 ? 0.7087 0.9260 0.5730 0.2464  -0.0229 -0.1152 254 SER A O   
1981 C CB  . SER A 254 ? 0.7488 0.9123 0.6108 0.2355  -0.0159 -0.1097 254 SER A CB  
1982 O OG  . SER A 254 ? 0.7670 0.9278 0.6045 0.2557  -0.0198 -0.1065 254 SER A OG  
1983 N N   . ALA A 255 ? 0.6564 0.9155 0.5681 0.2212  -0.0224 -0.1241 255 ALA A N   
1984 C CA  . ALA A 255 ? 0.6429 0.9457 0.5642 0.2244  -0.0277 -0.1303 255 ALA A CA  
1985 C C   . ALA A 255 ? 0.6615 0.9771 0.5908 0.2175  -0.0256 -0.1321 255 ALA A C   
1986 O O   . ALA A 255 ? 0.6856 1.0148 0.6048 0.2288  -0.0291 -0.1324 255 ALA A O   
1987 C CB  . ALA A 255 ? 0.6689 1.0053 0.6152 0.2123  -0.0289 -0.1382 255 ALA A CB  
1988 N N   . GLN A 256 ? 0.6601 0.9715 0.6067 0.1999  -0.0198 -0.1327 256 GLN A N   
1989 C CA  . GLN A 256 ? 0.6529 0.9748 0.6065 0.1927  -0.0170 -0.1336 256 GLN A CA  
1990 C C   . GLN A 256 ? 0.6135 0.9113 0.5400 0.2066  -0.0178 -0.1286 256 GLN A C   
1991 O O   . GLN A 256 ? 0.6644 0.9800 0.5893 0.2102  -0.0190 -0.1301 256 GLN A O   
1992 C CB  . GLN A 256 ? 0.7222 1.0352 0.6934 0.1753  -0.0103 -0.1327 256 GLN A CB  
1993 C CG  . GLN A 256 ? 0.7566 1.0957 0.7466 0.1625  -0.0065 -0.1355 256 GLN A CG  
1994 C CD  . GLN A 256 ? 0.8673 1.1946 0.8703 0.1495  0.0001  -0.1320 256 GLN A CD  
1995 O OE1 . GLN A 256 ? 0.8713 1.1865 0.8854 0.1428  0.0027  -0.1303 256 GLN A OE1 
1996 N NE2 . GLN A 256 ? 0.8781 1.2134 0.8825 0.1456  0.0030  -0.1308 256 GLN A NE2 
1997 N N   . THR A 257 ? 0.6536 0.9090 0.5579 0.2135  -0.0163 -0.1230 257 THR A N   
1998 C CA  . THR A 257 ? 0.6885 0.9130 0.5639 0.2242  -0.0153 -0.1186 257 THR A CA  
1999 C C   . THR A 257 ? 0.7067 0.9280 0.5603 0.2447  -0.0194 -0.1161 257 THR A C   
2000 O O   . THR A 257 ? 0.6767 0.8721 0.5053 0.2545  -0.0180 -0.1126 257 THR A O   
2001 C CB  . THR A 257 ? 0.7145 0.8911 0.5719 0.2204  -0.0107 -0.1147 257 THR A CB  
2002 O OG1 . THR A 257 ? 0.6869 0.8464 0.5380 0.2250  -0.0108 -0.1122 257 THR A OG1 
2003 C CG2 . THR A 257 ? 0.7151 0.8948 0.5909 0.2024  -0.0071 -0.1169 257 THR A CG2 
2004 N N   . GLY A 258 ? 0.6816 0.9271 0.5420 0.2520  -0.0243 -0.1179 258 GLY A N   
2005 C CA  . GLY A 258 ? 0.7186 0.9610 0.5557 0.2741  -0.0284 -0.1147 258 GLY A CA  
2006 C C   . GLY A 258 ? 0.7730 0.9637 0.5774 0.2853  -0.0250 -0.1072 258 GLY A C   
2007 O O   . GLY A 258 ? 0.7627 0.9396 0.5415 0.3038  -0.0260 -0.1031 258 GLY A O   
2008 N N   . ILE A 259 ? 0.7871 0.9472 0.5903 0.2745  -0.0202 -0.1053 259 ILE A N   
2009 C CA  . ILE A 259 ? 0.8189 0.9264 0.5900 0.2816  -0.0153 -0.0988 259 ILE A CA  
2010 C C   . ILE A 259 ? 0.7851 0.8861 0.5586 0.2809  -0.0153 -0.0971 259 ILE A C   
2011 O O   . ILE A 259 ? 0.7578 0.8637 0.5526 0.2647  -0.0135 -0.0999 259 ILE A O   
2012 C CB  . ILE A 259 ? 0.7989 0.8685 0.5601 0.2679  -0.0083 -0.0983 259 ILE A CB  
2013 C CG1 . ILE A 259 ? 0.7741 0.8430 0.5247 0.2714  -0.0078 -0.0991 259 ILE A CG1 
2014 C CG2 . ILE A 259 ? 0.8221 0.8380 0.5525 0.2706  -0.0021 -0.0931 259 ILE A CG2 
2015 C CD1 . ILE A 259 ? 0.8535 0.8974 0.5997 0.2551  -0.0027 -0.1009 259 ILE A CD1 
2016 N N   . ALA A 260 ? 0.8148 0.9044 0.5656 0.2994  -0.0171 -0.0923 260 ALA A N   
2017 C CA  . ALA A 260 ? 0.8527 0.9398 0.6050 0.3004  -0.0177 -0.0907 260 ALA A CA  
2018 C C   . ALA A 260 ? 0.8270 0.8698 0.5717 0.2872  -0.0094 -0.0880 260 ALA A C   
2019 O O   . ALA A 260 ? 0.8850 0.8849 0.6050 0.2866  -0.0030 -0.0844 260 ALA A O   
2020 C CB  . ALA A 260 ? 0.8607 0.9425 0.5856 0.3252  -0.0211 -0.0852 260 ALA A CB  
2021 N N   . VAL A 261 ? 0.8124 0.8660 0.5779 0.2761  -0.0094 -0.0902 261 VAL A N   
2022 C CA  . VAL A 261 ? 0.8148 0.8324 0.5767 0.2636  -0.0022 -0.0882 261 VAL A CA  
2023 C C   . VAL A 261 ? 0.9268 0.8936 0.6492 0.2736  0.0038  -0.0811 261 VAL A C   
2024 O O   . VAL A 261 ? 0.8950 0.8239 0.6041 0.2635  0.0110  -0.0802 261 VAL A O   
2025 C CB  . VAL A 261 ? 0.7817 0.8179 0.5643 0.2581  -0.0038 -0.0899 261 VAL A CB  
2026 C CG1 . VAL A 261 ? 0.8776 0.8835 0.6637 0.2426  0.0035  -0.0891 261 VAL A CG1 
2027 C CG2 . VAL A 261 ? 0.7753 0.8634 0.5930 0.2505  -0.0098 -0.0973 261 VAL A CG2 
2028 N N   . LEU A 262 ? 0.8943 0.8605 0.5962 0.2939  0.0009  -0.0763 262 LEU A N   
2029 C CA  . LEU A 262 ? 0.9481 0.8654 0.6094 0.3058  0.0071  -0.0685 262 LEU A CA  
2030 C C   . LEU A 262 ? 0.9489 0.8359 0.5880 0.3059  0.0119  -0.0674 262 LEU A C   
2031 O O   . LEU A 262 ? 0.9743 0.8125 0.5873 0.3011  0.0208  -0.0641 262 LEU A O   
2032 C CB  . LEU A 262 ? 1.0091 0.9376 0.6516 0.3311  0.0017  -0.0635 262 LEU A CB  
2033 C CG  . LEU A 262 ? 1.0035 0.9582 0.6600 0.3343  -0.0032 -0.0642 262 LEU A CG  
2034 C CD1 . LEU A 262 ? 1.0701 0.9886 0.7199 0.3234  0.0049  -0.0610 262 LEU A CD1 
2035 C CD2 . LEU A 262 ? 0.9226 0.9318 0.6226 0.3216  -0.0104 -0.0735 262 LEU A CD2 
2036 N N   . ASP A 263 ? 0.9361 0.8513 0.5839 0.3112  0.0066  -0.0705 263 ASP A N   
2037 C CA  . ASP A 263 ? 0.9930 0.8811 0.6201 0.3113  0.0110  -0.0701 263 ASP A CA  
2038 C C   . ASP A 263 ? 0.9774 0.8433 0.6115 0.2870  0.0173  -0.0745 263 ASP A C   
2039 O O   . ASP A 263 ? 0.9551 0.7744 0.5611 0.2822  0.0253  -0.0728 263 ASP A O   
2040 C CB  . ASP A 263 ? 1.0008 0.9290 0.6403 0.3205  0.0038  -0.0731 263 ASP A CB  
2041 C CG  . ASP A 263 ? 1.0562 0.9983 0.6785 0.3476  -0.0017 -0.0683 263 ASP A CG  
2042 O OD1 . ASP A 263 ? 1.0732 0.9961 0.6752 0.3595  -0.0004 -0.0624 263 ASP A OD1 
2043 O OD2 . ASP A 263 ? 1.0515 1.0242 0.6797 0.3575  -0.0073 -0.0704 263 ASP A OD2 
2044 N N   . MET A 264 ? 0.9448 0.8434 0.6149 0.2712  0.0140  -0.0804 264 MET A N   
2045 C CA  . MET A 264 ? 0.9105 0.7914 0.5874 0.2494  0.0190  -0.0845 264 MET A CA  
2046 C C   . MET A 264 ? 0.9324 0.7677 0.5893 0.2421  0.0270  -0.0818 264 MET A C   
2047 O O   . MET A 264 ? 0.9486 0.7487 0.5879 0.2300  0.0333  -0.0835 264 MET A O   
2048 C CB  . MET A 264 ? 0.8582 0.7818 0.5758 0.2370  0.0143  -0.0899 264 MET A CB  
2049 C CG  . MET A 264 ? 0.8691 0.7824 0.5932 0.2178  0.0174  -0.0946 264 MET A CG  
2050 S SD  . MET A 264 ? 0.8696 0.7871 0.5846 0.2175  0.0160  -0.0975 264 MET A SD  
2051 C CE  . MET A 264 ? 0.7931 0.7726 0.5512 0.2134  0.0088  -0.1021 264 MET A CE  
2052 N N   . CYS A 265 ? 0.9305 0.7649 0.5870 0.2492  0.0271  -0.0776 265 CYS A N   
2053 C CA  . CYS A 265 ? 0.9849 0.7757 0.6212 0.2427  0.0354  -0.0744 265 CYS A CA  
2054 C C   . CYS A 265 ? 1.0230 0.7631 0.6170 0.2466  0.0433  -0.0707 265 CYS A C   
2055 O O   . CYS A 265 ? 1.0267 0.7274 0.6044 0.2322  0.0517  -0.0713 265 CYS A O   
2056 C CB  . CYS A 265 ? 0.9830 0.7809 0.6202 0.2539  0.0340  -0.0695 265 CYS A CB  
2057 S SG  . CYS A 265 ? 0.9399 0.7809 0.6218 0.2430  0.0288  -0.0742 265 CYS A SG  
2058 N N   . ALA A 266 ? 1.0476 0.7870 0.6218 0.2658  0.0412  -0.0668 266 ALA A N   
2059 C CA  . ALA A 266 ? 1.0607 0.7497 0.5921 0.2711  0.0495  -0.0627 266 ALA A CA  
2060 C C   . ALA A 266 ? 1.1018 0.7738 0.6293 0.2530  0.0533  -0.0692 266 ALA A C   
2061 O O   . ALA A 266 ? 1.0858 0.7096 0.5845 0.2427  0.0629  -0.0689 266 ALA A O   
2062 C CB  . ALA A 266 ? 1.1334 0.8283 0.6451 0.2982  0.0458  -0.0567 266 ALA A CB  
2063 N N   . SER A 267 ? 1.0646 0.7758 0.6196 0.2480  0.0461  -0.0754 267 SER A N   
2064 C CA  . SER A 267 ? 1.0945 0.7953 0.6485 0.2294  0.0484  -0.0823 267 SER A CA  
2065 C C   . SER A 267 ? 1.0283 0.7110 0.5876 0.2057  0.0532  -0.0865 267 SER A C   
2066 O O   . SER A 267 ? 1.0491 0.6966 0.5875 0.1899  0.0596  -0.0901 267 SER A O   
2067 C CB  . SER A 267 ? 1.0629 0.8129 0.6470 0.2290  0.0396  -0.0872 267 SER A CB  
2068 O OG  . SER A 267 ? 1.0333 0.8031 0.6142 0.2503  0.0350  -0.0837 267 SER A OG  
2069 N N   . LEU A 268 ? 0.9818 0.6886 0.5685 0.2023  0.0500  -0.0866 268 LEU A N   
2070 C CA  . LEU A 268 ? 1.0288 0.7169 0.6189 0.1820  0.0548  -0.0897 268 LEU A CA  
2071 C C   . LEU A 268 ? 1.1265 0.7597 0.6802 0.1782  0.0657  -0.0859 268 LEU A C   
2072 O O   . LEU A 268 ? 1.1579 0.7609 0.6981 0.1577  0.0721  -0.0902 268 LEU A O   
2073 C CB  . LEU A 268 ? 0.9505 0.6709 0.5733 0.1832  0.0505  -0.0888 268 LEU A CB  
2074 C CG  . LEU A 268 ? 0.9454 0.6551 0.5785 0.1637  0.0542  -0.0921 268 LEU A CG  
2075 C CD1 . LEU A 268 ? 0.9397 0.6394 0.5684 0.1438  0.0549  -0.0993 268 LEU A CD1 
2076 C CD2 . LEU A 268 ? 0.8821 0.6325 0.5523 0.1661  0.0483  -0.0924 268 LEU A CD2 
2077 N N   . LYS A 269 ? 1.1444 0.7633 0.6788 0.1974  0.0682  -0.0778 269 LYS A N   
2078 C CA  . LYS A 269 ? 1.1609 0.7253 0.6570 0.1958  0.0797  -0.0727 269 LYS A CA  
2079 C C   . LYS A 269 ? 1.1803 0.7051 0.6467 0.1827  0.0873  -0.0763 269 LYS A C   
2080 O O   . LYS A 269 ? 1.2294 0.7166 0.6782 0.1633  0.0968  -0.0783 269 LYS A O   
2081 C CB  . LYS A 269 ? 1.2073 0.7630 0.6813 0.2226  0.0803  -0.0627 269 LYS A CB  
2082 C CG  . LYS A 269 ? 1.3442 0.8563 0.7892 0.2231  0.0909  -0.0557 269 LYS A CG  
2083 C CD  . LYS A 269 ? 1.3980 0.8846 0.8044 0.2491  0.0943  -0.0455 269 LYS A CD  
2084 C CE  . LYS A 269 ? 1.4552 0.9789 0.8762 0.2718  0.0852  -0.0399 269 LYS A CE  
2085 N NZ  . LYS A 269 ? 1.4761 0.9711 0.8543 0.2981  0.0891  -0.0290 269 LYS A NZ  
2086 N N   . GLU A 270 ? 1.1706 0.7025 0.6294 0.1929  0.0838  -0.0773 270 GLU A N   
2087 C CA  . GLU A 270 ? 1.2360 0.7308 0.6654 0.1812  0.0908  -0.0810 270 GLU A CA  
2088 C C   . GLU A 270 ? 1.2731 0.7722 0.7171 0.1515  0.0905  -0.0913 270 GLU A C   
2089 O O   . GLU A 270 ? 1.3066 0.7661 0.7258 0.1320  0.0995  -0.0950 270 GLU A O   
2090 C CB  . GLU A 270 ? 1.2798 0.7880 0.7028 0.1988  0.0859  -0.0804 270 GLU A CB  
2091 C CG  . GLU A 270 ? 1.3450 0.8114 0.7329 0.1907  0.0939  -0.0832 270 GLU A CG  
2092 C CD  . GLU A 270 ? 1.4534 0.9380 0.8391 0.2080  0.0884  -0.0830 270 GLU A CD  
2093 O OE1 . GLU A 270 ? 1.5508 1.0746 0.9566 0.2287  0.0797  -0.0788 270 GLU A OE1 
2094 O OE2 . GLU A 270 ? 1.4614 0.9224 0.8255 0.2002  0.0926  -0.0873 270 GLU A OE2 
2095 N N   . LEU A 271 ? 1.1949 0.7419 0.6772 0.1472  0.0803  -0.0961 271 LEU A N   
2096 C CA  . LEU A 271 ? 1.1806 0.7341 0.6761 0.1201  0.0789  -0.1050 271 LEU A CA  
2097 C C   . LEU A 271 ? 1.1896 0.7132 0.6777 0.1003  0.0873  -0.1057 271 LEU A C   
2098 O O   . LEU A 271 ? 1.2183 0.7205 0.6947 0.0745  0.0921  -0.1122 271 LEU A O   
2099 C CB  . LEU A 271 ? 1.0991 0.7071 0.6348 0.1222  0.0674  -0.1078 271 LEU A CB  
2100 C CG  . LEU A 271 ? 1.0621 0.7031 0.6076 0.1316  0.0593  -0.1100 271 LEU A CG  
2101 C CD1 . LEU A 271 ? 1.0009 0.6944 0.5855 0.1345  0.0494  -0.1114 271 LEU A CD1 
2102 C CD2 . LEU A 271 ? 1.0912 0.7159 0.6182 0.1140  0.0605  -0.1169 271 LEU A CD2 
2103 N N   . LEU A 272 ? 1.1629 0.6848 0.6564 0.1111  0.0896  -0.0990 272 LEU A N   
2104 C CA  . LEU A 272 ? 1.2296 0.7250 0.7175 0.0935  0.0982  -0.0988 272 LEU A CA  
2105 C C   . LEU A 272 ? 1.2990 0.7379 0.7439 0.0856  0.1120  -0.0965 272 LEU A C   
2106 O O   . LEU A 272 ? 1.3308 0.7448 0.7667 0.0597  0.1203  -0.1006 272 LEU A O   
2107 C CB  . LEU A 272 ? 1.2264 0.7384 0.7324 0.1086  0.0965  -0.0919 272 LEU A CB  
2108 C CG  . LEU A 272 ? 1.1708 0.7347 0.7202 0.1121  0.0855  -0.0943 272 LEU A CG  
2109 C CD1 . LEU A 272 ? 1.1245 0.7207 0.6876 0.1401  0.0780  -0.0883 272 LEU A CD1 
2110 C CD2 . LEU A 272 ? 1.0931 0.6566 0.6587 0.0987  0.0886  -0.0946 272 LEU A CD2 
2111 N N   . GLN A 273 ? 1.3117 0.7294 0.7287 0.1069  0.1153  -0.0898 273 GLN A N   
2112 C CA  . GLN A 273 ? 1.3738 0.7336 0.7454 0.1016  0.1299  -0.0865 273 GLN A CA  
2113 C C   . GLN A 273 ? 1.4084 0.7484 0.7614 0.0838  0.1334  -0.0944 273 GLN A C   
2114 O O   . GLN A 273 ? 1.4856 0.7788 0.8055 0.0674  0.1467  -0.0953 273 GLN A O   
2115 C CB  . GLN A 273 ? 1.3737 0.7153 0.7184 0.1328  0.1327  -0.0752 273 GLN A CB  
2116 C CG  . GLN A 273 ? 1.4020 0.7703 0.7659 0.1532  0.1269  -0.0675 273 GLN A CG  
2117 C CD  . GLN A 273 ? 1.4129 0.7586 0.7443 0.1822  0.1308  -0.0556 273 GLN A CD  
2118 O OE1 . GLN A 273 ? 1.3675 0.7414 0.7136 0.2024  0.1236  -0.0498 273 GLN A OE1 
2119 N NE2 . GLN A 273 ? 1.3810 0.6766 0.6671 0.1843  0.1420  -0.0522 273 GLN A NE2 
2120 N N   . ASN A 274 ? 1.3620 0.7377 0.7356 0.0851  0.1222  -0.1005 274 ASN A N   
2121 C CA  . ASN A 274 ? 1.3781 0.7393 0.7329 0.0753  0.1237  -0.1068 274 ASN A CA  
2122 C C   . ASN A 274 ? 1.3859 0.7777 0.7655 0.0497  0.1159  -0.1183 274 ASN A C   
2123 O O   . ASN A 274 ? 1.3777 0.7633 0.7448 0.0390  0.1158  -0.1247 274 ASN A O   
2124 C CB  . ASN A 274 ? 1.4481 0.8215 0.7972 0.1049  0.1181  -0.1021 274 ASN A CB  
2125 C CG  . ASN A 274 ? 1.4973 0.8341 0.8126 0.1292  0.1266  -0.0906 274 ASN A CG  
2126 O OD1 . ASN A 274 ? 1.4951 0.8551 0.8200 0.1565  0.1201  -0.0832 274 ASN A OD1 
2127 N ND2 . ASN A 274 ? 1.5299 0.8096 0.8031 0.1192  0.1412  -0.0893 274 ASN A ND2 
2128 N N   . GLY A 275 ? 1.3368 0.7606 0.7493 0.0392  0.1096  -0.1208 275 GLY A N   
2129 C CA  . GLY A 275 ? 1.3366 0.7892 0.7685 0.0158  0.1017  -0.1307 275 GLY A CA  
2130 C C   . GLY A 275 ? 1.2730 0.7601 0.7166 0.0307  0.0905  -0.1322 275 GLY A C   
2131 O O   . GLY A 275 ? 1.2363 0.7333 0.6807 0.0591  0.0876  -0.1260 275 GLY A O   
2132 N N   . MET A 276 ? 1.2861 0.7947 0.7395 0.0093  0.0839  -0.1406 276 MET A N   
2133 C CA  . MET A 276 ? 1.2749 0.8203 0.7413 0.0196  0.0729  -0.1423 276 MET A CA  
2134 C C   . MET A 276 ? 1.3227 0.8545 0.7662 0.0112  0.0741  -0.1479 276 MET A C   
2135 O O   . MET A 276 ? 1.3198 0.8792 0.7705 0.0207  0.0661  -0.1489 276 MET A O   
2136 C CB  . MET A 276 ? 1.2083 0.7961 0.7053 0.0051  0.0623  -0.1458 276 MET A CB  
2137 C CG  . MET A 276 ? 1.1876 0.8089 0.7107 0.0297  0.0555  -0.1396 276 MET A CG  
2138 S SD  . MET A 276 ? 1.0675 0.7655 0.6581 0.0133  0.0393  -0.1320 276 MET A SD  
2139 C CE  . MET A 276 ? 0.8611 0.5772 0.4858 0.0241  0.0389  -0.1236 276 MET A CE  
2140 N N   . ASN A 277 ? 1.3575 0.8470 0.7730 -0.0058 0.0847  -0.1513 277 ASN A N   
2141 C CA  . ASN A 277 ? 1.4397 0.9109 0.8301 -0.0122 0.0876  -0.1565 277 ASN A CA  
2142 C C   . ASN A 277 ? 1.4178 0.9232 0.8218 -0.0351 0.0776  -0.1654 277 ASN A C   
2143 O O   . ASN A 277 ? 1.4659 0.9736 0.8581 -0.0326 0.0753  -0.1687 277 ASN A O   
2144 C CB  . ASN A 277 ? 1.4924 0.9611 0.8718 0.0204  0.0871  -0.1506 277 ASN A CB  
2145 C CG  . ASN A 277 ? 1.6063 1.0255 0.9538 0.0354  0.0999  -0.1439 277 ASN A CG  
2146 O OD1 . ASN A 277 ? 1.6723 1.0588 1.0066 0.0239  0.1095  -0.1425 277 ASN A OD1 
2147 N ND2 . ASN A 277 ? 1.6706 1.0831 1.0034 0.0606  0.1006  -0.1393 277 ASN A ND2 
2148 N N   . GLY A 278 ? 1.3669 0.9013 0.7956 -0.0571 0.0712  -0.1686 278 GLY A N   
2149 C CA  . GLY A 278 ? 1.3382 0.9130 0.7823 -0.0773 0.0598  -0.1751 278 GLY A CA  
2150 C C   . GLY A 278 ? 1.2449 0.8584 0.7046 -0.0564 0.0483  -0.1712 278 GLY A C   
2151 O O   . GLY A 278 ? 1.2250 0.8663 0.6889 -0.0668 0.0398  -0.1750 278 GLY A O   
2152 N N   . ARG A 279 ? 1.2173 0.8351 0.6860 -0.0271 0.0480  -0.1633 279 ARG A N   
2153 C CA  . ARG A 279 ? 1.1920 0.8487 0.6790 -0.0057 0.0382  -0.1585 279 ARG A CA  
2154 C C   . ARG A 279 ? 1.0868 0.7975 0.6320 -0.0090 0.0285  -0.1478 279 ARG A C   
2155 O O   . ARG A 279 ? 1.0912 0.8020 0.6516 -0.0266 0.0300  -0.1467 279 ARG A O   
2156 C CB  . ARG A 279 ? 1.2557 0.8999 0.7350 0.0284  0.0433  -0.1525 279 ARG A CB  
2157 C CG  . ARG A 279 ? 1.3953 0.9966 0.8416 0.0313  0.0534  -0.1543 279 ARG A CG  
2158 C CD  . ARG A 279 ? 1.4166 1.0133 0.8580 0.0640  0.0565  -0.1470 279 ARG A CD  
2159 N NE  . ARG A 279 ? 1.4682 1.1065 0.9266 0.0782  0.0479  -0.1456 279 ARG A NE  
2160 C CZ  . ARG A 279 ? 1.4255 1.0730 0.8859 0.1047  0.0482  -0.1398 279 ARG A CZ  
2161 N NH1 . ARG A 279 ? 1.4334 1.0511 0.8776 0.1215  0.0558  -0.1343 279 ARG A NH1 
2162 N NH2 . ARG A 279 ? 1.3441 1.0322 0.8225 0.1140  0.0407  -0.1388 279 ARG A NH2 
2163 N N   . THR A 280 ? 1.0333 0.7883 0.6099 0.0084  0.0199  -0.1400 280 THR A N   
2164 C CA  . THR A 280 ? 0.9423 0.7465 0.5723 0.0053  0.0117  -0.1300 280 THR A CA  
2165 C C   . THR A 280 ? 0.8991 0.7246 0.5458 0.0328  0.0098  -0.1243 280 THR A C   
2166 O O   . THR A 280 ? 0.9395 0.7618 0.5676 0.0518  0.0105  -0.1268 280 THR A O   
2167 C CB  . THR A 280 ? 0.8998 0.7521 0.5631 -0.0137 0.0010  -0.1257 280 THR A CB  
2168 O OG1 . THR A 280 ? 0.9251 0.7939 0.5830 -0.0034 -0.0033 -0.1260 280 THR A OG1 
2169 C CG2 . THR A 280 ? 0.8661 0.7035 0.5141 -0.0426 0.0024  -0.1330 280 THR A CG2 
2170 N N   . ILE A 281 ? 0.8439 0.6943 0.5274 0.0333  0.0072  -0.1171 281 ILE A N   
2171 C CA  . ILE A 281 ? 0.8202 0.6977 0.5268 0.0547  0.0051  -0.1122 281 ILE A CA  
2172 C C   . ILE A 281 ? 0.7659 0.6940 0.5231 0.0437  -0.0030 -0.1032 281 ILE A C   
2173 O O   . ILE A 281 ? 0.7110 0.6455 0.4895 0.0291  -0.0039 -0.0990 281 ILE A O   
2174 C CB  . ILE A 281 ? 0.7992 0.6529 0.4974 0.0686  0.0118  -0.1129 281 ILE A CB  
2175 C CG1 . ILE A 281 ? 0.8578 0.6528 0.5012 0.0755  0.0217  -0.1208 281 ILE A CG1 
2176 C CG2 . ILE A 281 ? 0.7418 0.6218 0.4563 0.0917  0.0102  -0.1109 281 ILE A CG2 
2177 C CD1 . ILE A 281 ? 0.9227 0.6920 0.5463 0.0994  0.0291  -0.1219 281 ILE A CD1 
2178 N N   . LEU A 282 ? 0.7323 0.6954 0.5078 0.0513  -0.0079 -0.0998 282 LEU A N   
2179 C CA  . LEU A 282 ? 0.6550 0.6624 0.4751 0.0420  -0.0139 -0.0904 282 LEU A CA  
2180 C C   . LEU A 282 ? 0.6808 0.6951 0.5111 0.0186  -0.0178 -0.0869 282 LEU A C   
2181 O O   . LEU A 282 ? 0.6709 0.7068 0.5331 0.0098  -0.0200 -0.0794 282 LEU A O   
2182 C CB  . LEU A 282 ? 0.6068 0.6278 0.4551 0.0490  -0.0123 -0.0860 282 LEU A CB  
2183 C CG  . LEU A 282 ? 0.6712 0.7041 0.5202 0.0703  -0.0104 -0.0888 282 LEU A CG  
2184 C CD1 . LEU A 282 ? 0.5660 0.6173 0.4454 0.0747  -0.0090 -0.0854 282 LEU A CD1 
2185 C CD2 . LEU A 282 ? 0.6506 0.7118 0.5072 0.0720  -0.0137 -0.0870 282 LEU A CD2 
2186 N N   . GLY A 283 ? 0.6543 0.6500 0.4559 0.0088  -0.0182 -0.0930 283 GLY A N   
2187 C CA  . GLY A 283 ? 0.6800 0.6880 0.4892 -0.0136 -0.0226 -0.0916 283 GLY A CA  
2188 C C   . GLY A 283 ? 0.7919 0.7826 0.6007 -0.0290 -0.0195 -0.0938 283 GLY A C   
2189 O O   . GLY A 283 ? 0.8296 0.8412 0.6537 -0.0477 -0.0238 -0.0915 283 GLY A O   
2190 N N   . SER A 284 ? 0.7260 0.6809 0.5171 -0.0217 -0.0118 -0.0981 284 SER A N   
2191 C CA  . SER A 284 ? 0.7380 0.6725 0.5252 -0.0367 -0.0071 -0.1007 284 SER A CA  
2192 C C   . SER A 284 ? 0.8128 0.6909 0.5506 -0.0372 0.0025  -0.1118 284 SER A C   
2193 O O   . SER A 284 ? 0.8664 0.7186 0.5767 -0.0176 0.0068  -0.1154 284 SER A O   
2194 C CB  . SER A 284 ? 0.7513 0.6931 0.5649 -0.0282 -0.0051 -0.0940 284 SER A CB  
2195 O OG  . SER A 284 ? 0.7733 0.6881 0.5766 -0.0401 0.0014  -0.0975 284 SER A OG  
2196 N N   . ALA A 285 ? 0.8027 0.6613 0.5282 -0.0594 0.0068  -0.1173 285 ALA A N   
2197 C CA  . ALA A 285 ? 0.8394 0.6381 0.5172 -0.0618 0.0189  -0.1273 285 ALA A CA  
2198 C C   . ALA A 285 ? 0.8609 0.6344 0.5374 -0.0568 0.0272  -0.1254 285 ALA A C   
2199 O O   . ALA A 285 ? 0.9362 0.6597 0.5756 -0.0635 0.0386  -0.1328 285 ALA A O   
2200 C CB  . ALA A 285 ? 0.8632 0.6494 0.5217 -0.0913 0.0212  -0.1368 285 ALA A CB  
2201 N N   . LEU A 286 ? 0.7942 0.5990 0.5084 -0.0454 0.0226  -0.1160 286 LEU A N   
2202 C CA  . LEU A 286 ? 0.8230 0.6073 0.5375 -0.0381 0.0298  -0.1137 286 LEU A CA  
2203 C C   . LEU A 286 ? 0.8318 0.6328 0.5623 -0.0101 0.0267  -0.1077 286 LEU A C   
2204 O O   . LEU A 286 ? 0.8234 0.6597 0.5745 -0.0012 0.0185  -0.1040 286 LEU A O   
2205 C CB  . LEU A 286 ? 0.8199 0.6297 0.5691 -0.0582 0.0281  -0.1092 286 LEU A CB  
2206 C CG  . LEU A 286 ? 0.8524 0.6643 0.5979 -0.0890 0.0287  -0.1149 286 LEU A CG  
2207 C CD1 . LEU A 286 ? 0.7863 0.6476 0.5791 -0.1029 0.0220  -0.1075 286 LEU A CD1 
2208 C CD2 . LEU A 286 ? 0.8744 0.6278 0.5771 -0.1001 0.0430  -0.1242 286 LEU A CD2 
2209 N N   . LEU A 287 ? 0.7847 0.5619 0.5064 0.0025  0.0337  -0.1070 287 LEU A N   
2210 C CA  . LEU A 287 ? 0.7811 0.5771 0.5198 0.0270  0.0312  -0.1025 287 LEU A CA  
2211 C C   . LEU A 287 ? 0.7284 0.5689 0.5181 0.0195  0.0250  -0.0944 287 LEU A C   
2212 O O   . LEU A 287 ? 0.7448 0.5808 0.5453 0.0065  0.0282  -0.0922 287 LEU A O   
2213 C CB  . LEU A 287 ? 0.7735 0.5256 0.4780 0.0452  0.0414  -0.1056 287 LEU A CB  
2214 C CG  . LEU A 287 ? 0.8253 0.5289 0.4754 0.0532  0.0491  -0.1131 287 LEU A CG  
2215 C CD1 . LEU A 287 ? 0.9172 0.5666 0.5256 0.0670  0.0620  -0.1156 287 LEU A CD1 
2216 C CD2 . LEU A 287 ? 0.8534 0.5756 0.4991 0.0739  0.0436  -0.1143 287 LEU A CD2 
2217 N N   . GLU A 288 ? 0.6812 0.5631 0.5010 0.0272  0.0171  -0.0899 288 GLU A N   
2218 C CA  . GLU A 288 ? 0.6583 0.5808 0.5245 0.0209  0.0120  -0.0817 288 GLU A CA  
2219 C C   . GLU A 288 ? 0.6153 0.5411 0.4939 0.0367  0.0147  -0.0801 288 GLU A C   
2220 O O   . GLU A 288 ? 0.6309 0.5592 0.5019 0.0560  0.0147  -0.0832 288 GLU A O   
2221 C CB  . GLU A 288 ? 0.6734 0.6355 0.5635 0.0208  0.0042  -0.0775 288 GLU A CB  
2222 C CG  . GLU A 288 ? 0.6951 0.6629 0.5800 0.0038  0.0002  -0.0778 288 GLU A CG  
2223 C CD  . GLU A 288 ? 0.7619 0.7459 0.6704 -0.0164 -0.0014 -0.0726 288 GLU A CD  
2224 O OE1 . GLU A 288 ? 0.7534 0.7603 0.6946 -0.0151 -0.0022 -0.0652 288 GLU A OE1 
2225 O OE2 . GLU A 288 ? 0.8254 0.7990 0.7183 -0.0333 -0.0013 -0.0767 288 GLU A OE2 
2226 N N   . ASP A 289 ? 0.5944 0.5253 0.4945 0.0282  0.0165  -0.0756 289 ASP A N   
2227 C CA  . ASP A 289 ? 0.6065 0.5402 0.5186 0.0412  0.0193  -0.0745 289 ASP A CA  
2228 C C   . ASP A 289 ? 0.5543 0.5258 0.5113 0.0349  0.0158  -0.0668 289 ASP A C   
2229 O O   . ASP A 289 ? 0.5549 0.5277 0.5254 0.0387  0.0189  -0.0650 289 ASP A O   
2230 C CB  . ASP A 289 ? 0.6005 0.4963 0.4897 0.0407  0.0275  -0.0770 289 ASP A CB  
2231 C CG  . ASP A 289 ? 0.6256 0.5270 0.5360 0.0202  0.0290  -0.0719 289 ASP A CG  
2232 O OD1 . ASP A 289 ? 0.6362 0.5654 0.5710 0.0051  0.0237  -0.0673 289 ASP A OD1 
2233 O OD2 . ASP A 289 ? 0.7004 0.5797 0.6026 0.0200  0.0357  -0.0722 289 ASP A OD2 
2234 N N   . GLU A 290 ? 0.4923 0.4936 0.4713 0.0266  0.0102  -0.0618 290 GLU A N   
2235 C CA  . GLU A 290 ? 0.5184 0.5514 0.5365 0.0225  0.0085  -0.0536 290 GLU A CA  
2236 C C   . GLU A 290 ? 0.4794 0.5377 0.5132 0.0318  0.0062  -0.0527 290 GLU A C   
2237 O O   . GLU A 290 ? 0.4107 0.4944 0.4722 0.0269  0.0049  -0.0453 290 GLU A O   
2238 C CB  . GLU A 290 ? 0.4942 0.5431 0.5287 0.0049  0.0056  -0.0465 290 GLU A CB  
2239 C CG  . GLU A 290 ? 0.5312 0.5603 0.5556 -0.0074 0.0091  -0.0479 290 GLU A CG  
2240 C CD  . GLU A 290 ? 0.5342 0.5869 0.5896 -0.0186 0.0088  -0.0393 290 GLU A CD  
2241 O OE1 . GLU A 290 ? 0.5219 0.6060 0.6013 -0.0209 0.0045  -0.0316 290 GLU A OE1 
2242 O OE2 . GLU A 290 ? 0.4894 0.5289 0.5432 -0.0248 0.0136  -0.0400 290 GLU A OE2 
2243 N N   . PHE A 291 ? 0.4872 0.5387 0.5022 0.0458  0.0066  -0.0603 291 PHE A N   
2244 C CA  . PHE A 291 ? 0.5110 0.5867 0.5395 0.0548  0.0059  -0.0619 291 PHE A CA  
2245 C C   . PHE A 291 ? 0.4757 0.5478 0.4995 0.0694  0.0093  -0.0690 291 PHE A C   
2246 O O   . PHE A 291 ? 0.4598 0.5112 0.4541 0.0812  0.0103  -0.0759 291 PHE A O   
2247 C CB  . PHE A 291 ? 0.4652 0.5439 0.4757 0.0589  0.0027  -0.0655 291 PHE A CB  
2248 C CG  . PHE A 291 ? 0.4793 0.5678 0.4959 0.0457  -0.0012 -0.0589 291 PHE A CG  
2249 C CD1 . PHE A 291 ? 0.5040 0.6203 0.5487 0.0401  -0.0021 -0.0512 291 PHE A CD1 
2250 C CD2 . PHE A 291 ? 0.4995 0.5687 0.4924 0.0388  -0.0031 -0.0605 291 PHE A CD2 
2251 C CE1 . PHE A 291 ? 0.4842 0.6113 0.5330 0.0301  -0.0058 -0.0446 291 PHE A CE1 
2252 C CE2 . PHE A 291 ? 0.5905 0.6726 0.5886 0.0268  -0.0074 -0.0553 291 PHE A CE2 
2253 C CZ  . PHE A 291 ? 0.5414 0.6538 0.5677 0.0235  -0.0092 -0.0470 291 PHE A CZ  
2254 N N   . THR A 292 ? 0.4652 0.5574 0.5159 0.0697  0.0115  -0.0679 292 THR A N   
2255 C CA  . THR A 292 ? 0.5074 0.6033 0.5551 0.0834  0.0140  -0.0763 292 THR A CA  
2256 C C   . THR A 292 ? 0.5122 0.6265 0.5521 0.0944  0.0124  -0.0841 292 THR A C   
2257 O O   . THR A 292 ? 0.4675 0.5947 0.5117 0.0893  0.0104  -0.0818 292 THR A O   
2258 C CB  . THR A 292 ? 0.4487 0.5612 0.5262 0.0791  0.0175  -0.0747 292 THR A CB  
2259 O OG1 . THR A 292 ? 0.4946 0.6307 0.5950 0.0708  0.0180  -0.0708 292 THR A OG1 
2260 C CG2 . THR A 292 ? 0.4836 0.5804 0.5698 0.0705  0.0198  -0.0674 292 THR A CG2 
2261 N N   . PRO A 293 ? 0.5127 0.6307 0.5406 0.1104  0.0135  -0.0935 293 PRO A N   
2262 C CA  . PRO A 293 ? 0.5175 0.6623 0.5439 0.1205  0.0124  -0.1017 293 PRO A CA  
2263 C C   . PRO A 293 ? 0.4764 0.6521 0.5347 0.1081  0.0139  -0.1003 293 PRO A C   
2264 O O   . PRO A 293 ? 0.4317 0.6247 0.4905 0.1079  0.0128  -0.1020 293 PRO A O   
2265 C CB  . PRO A 293 ? 0.5219 0.6718 0.5382 0.1378  0.0137  -0.1113 293 PRO A CB  
2266 C CG  . PRO A 293 ? 0.5515 0.6637 0.5458 0.1421  0.0150  -0.1079 293 PRO A CG  
2267 C CD  . PRO A 293 ? 0.5326 0.6324 0.5461 0.1211  0.0158  -0.0971 293 PRO A CD  
2268 N N   . PHE A 294 ? 0.4300 0.6103 0.5136 0.0975  0.0173  -0.0967 294 PHE A N   
2269 C CA  . PHE A 294 ? 0.4589 0.6630 0.5700 0.0855  0.0211  -0.0950 294 PHE A CA  
2270 C C   . PHE A 294 ? 0.5106 0.7113 0.6264 0.0746  0.0200  -0.0842 294 PHE A C   
2271 O O   . PHE A 294 ? 0.5178 0.7375 0.6433 0.0698  0.0220  -0.0843 294 PHE A O   
2272 C CB  . PHE A 294 ? 0.5314 0.7356 0.6644 0.0780  0.0262  -0.0935 294 PHE A CB  
2273 C CG  . PHE A 294 ? 0.6492 0.8712 0.8082 0.0651  0.0327  -0.0915 294 PHE A CG  
2274 C CD1 . PHE A 294 ? 0.6716 0.8864 0.8427 0.0537  0.0349  -0.0784 294 PHE A CD1 
2275 C CD2 . PHE A 294 ? 0.7317 0.9775 0.9015 0.0644  0.0373  -0.1030 294 PHE A CD2 
2276 C CE1 . PHE A 294 ? 0.6678 0.8938 0.8588 0.0431  0.0429  -0.0761 294 PHE A CE1 
2277 C CE2 . PHE A 294 ? 0.7253 0.9828 0.9161 0.0510  0.0455  -0.1021 294 PHE A CE2 
2278 C CZ  . PHE A 294 ? 0.6706 0.9155 0.8707 0.0410  0.0488  -0.0880 294 PHE A CZ  
2279 N N   . ASP A 295 ? 0.4871 0.6654 0.5952 0.0703  0.0170  -0.0751 295 ASP A N   
2280 C CA  . ASP A 295 ? 0.4891 0.6680 0.5998 0.0612  0.0150  -0.0656 295 ASP A CA  
2281 C C   . ASP A 295 ? 0.4862 0.6715 0.5786 0.0670  0.0116  -0.0701 295 ASP A C   
2282 O O   . ASP A 295 ? 0.4828 0.6814 0.5828 0.0613  0.0121  -0.0656 295 ASP A O   
2283 C CB  . ASP A 295 ? 0.4703 0.6287 0.5743 0.0552  0.0118  -0.0574 295 ASP A CB  
2284 C CG  . ASP A 295 ? 0.5136 0.6643 0.6324 0.0512  0.0150  -0.0533 295 ASP A CG  
2285 O OD1 . ASP A 295 ? 0.5390 0.7014 0.6790 0.0492  0.0201  -0.0524 295 ASP A OD1 
2286 O OD2 . ASP A 295 ? 0.4680 0.6002 0.5765 0.0493  0.0132  -0.0512 295 ASP A OD2 
2287 N N   . VAL A 296 ? 0.5085 0.6823 0.5749 0.0793  0.0089  -0.0782 296 VAL A N   
2288 C CA  . VAL A 296 ? 0.5039 0.6837 0.5513 0.0869  0.0064  -0.0831 296 VAL A CA  
2289 C C   . VAL A 296 ? 0.5290 0.7413 0.5929 0.0875  0.0095  -0.0878 296 VAL A C   
2290 O O   . VAL A 296 ? 0.5532 0.7771 0.6177 0.0838  0.0092  -0.0854 296 VAL A O   
2291 C CB  . VAL A 296 ? 0.4955 0.6571 0.5105 0.1036  0.0049  -0.0916 296 VAL A CB  
2292 C CG1 . VAL A 296 ? 0.4983 0.6698 0.4947 0.1142  0.0033  -0.0974 296 VAL A CG1 
2293 C CG2 . VAL A 296 ? 0.5021 0.6279 0.4962 0.1003  0.0034  -0.0874 296 VAL A CG2 
2294 N N   . VAL A 297 ? 0.5200 0.7480 0.5974 0.0907  0.0132  -0.0949 297 VAL A N   
2295 C CA  . VAL A 297 ? 0.5261 0.7871 0.6180 0.0900  0.0171  -0.1022 297 VAL A CA  
2296 C C   . VAL A 297 ? 0.5678 0.8374 0.6831 0.0733  0.0222  -0.0937 297 VAL A C   
2297 O O   . VAL A 297 ? 0.6038 0.8906 0.7217 0.0702  0.0243  -0.0943 297 VAL A O   
2298 C CB  . VAL A 297 ? 0.5242 0.8015 0.6246 0.0959  0.0199  -0.1132 297 VAL A CB  
2299 C CG1 . VAL A 297 ? 0.4856 0.7908 0.6065 0.0849  0.0255  -0.1176 297 VAL A CG1 
2300 C CG2 . VAL A 297 ? 0.5143 0.7887 0.5867 0.1139  0.0146  -0.1209 297 VAL A CG2 
2301 N N   . ARG A 298 ? 0.5307 0.7873 0.6615 0.0635  0.0249  -0.0851 298 ARG A N   
2302 C CA  . ARG A 298 ? 0.5651 0.8258 0.7151 0.0501  0.0310  -0.0755 298 ARG A CA  
2303 C C   . ARG A 298 ? 0.5719 0.8300 0.7128 0.0479  0.0277  -0.0666 298 ARG A C   
2304 O O   . ARG A 298 ? 0.5790 0.8492 0.7277 0.0416  0.0328  -0.0631 298 ARG A O   
2305 C CB  . ARG A 298 ? 0.6386 0.8832 0.8027 0.0433  0.0337  -0.0664 298 ARG A CB  
2306 C CG  . ARG A 298 ? 0.6978 0.9346 0.8673 0.0357  0.0344  -0.0509 298 ARG A CG  
2307 C CD  . ARG A 298 ? 0.7948 1.0231 0.9830 0.0291  0.0410  -0.0423 298 ARG A CD  
2308 N NE  . ARG A 298 ? 0.7898 1.0026 0.9756 0.0316  0.0362  -0.0390 298 ARG A NE  
2309 C CZ  . ARG A 298 ? 0.7537 0.9578 0.9367 0.0301  0.0314  -0.0284 298 ARG A CZ  
2310 N NH1 . ARG A 298 ? 0.7432 0.9525 0.9255 0.0272  0.0300  -0.0184 298 ARG A NH1 
2311 N NH2 . ARG A 298 ? 0.5944 0.7859 0.7745 0.0316  0.0280  -0.0283 298 ARG A NH2 
2312 N N   . GLN A 299 ? 0.5668 0.8082 0.6899 0.0521  0.0200  -0.0629 299 GLN A N   
2313 C CA  . GLN A 299 ? 0.5739 0.8142 0.6866 0.0499  0.0163  -0.0559 299 GLN A CA  
2314 C C   . GLN A 299 ? 0.5926 0.8473 0.6919 0.0568  0.0157  -0.0643 299 GLN A C   
2315 O O   . GLN A 299 ? 0.6307 0.8971 0.7325 0.0527  0.0179  -0.0602 299 GLN A O   
2316 C CB  . GLN A 299 ? 0.5137 0.7329 0.6097 0.0504  0.0089  -0.0519 299 GLN A CB  
2317 C CG  . GLN A 299 ? 0.5289 0.7493 0.6161 0.0462  0.0050  -0.0447 299 GLN A CG  
2318 C CD  . GLN A 299 ? 0.4989 0.7030 0.5756 0.0416  -0.0010 -0.0398 299 GLN A CD  
2319 O OE1 . GLN A 299 ? 0.4964 0.7001 0.5596 0.0391  -0.0055 -0.0375 299 GLN A OE1 
2320 N NE2 . GLN A 299 ? 0.4399 0.6313 0.5215 0.0398  -0.0009 -0.0394 299 GLN A NE2 
2321 N N   . CYS A 300 ? 0.6143 0.8689 0.6983 0.0685  0.0133  -0.0758 300 CYS A N   
2322 C CA  . CYS A 300 ? 0.6315 0.9004 0.7004 0.0778  0.0123  -0.0839 300 CYS A CA  
2323 C C   . CYS A 300 ? 0.6473 0.9478 0.7335 0.0756  0.0192  -0.0906 300 CYS A C   
2324 O O   . CYS A 300 ? 0.6649 0.9826 0.7419 0.0819  0.0194  -0.0968 300 CYS A O   
2325 C CB  . CYS A 300 ? 0.5762 0.8329 0.6196 0.0938  0.0081  -0.0930 300 CYS A CB  
2326 S SG  . CYS A 300 ? 0.6392 0.8581 0.6545 0.0939  0.0018  -0.0869 300 CYS A SG  
2327 N N   . SER A 301 ? 0.7679 1.0763 0.8784 0.0657  0.0257  -0.0898 301 SER A N   
2328 C CA  . SER A 301 ? 0.7452 1.0817 0.8730 0.0590  0.0343  -0.0963 301 SER A CA  
2329 C C   . SER A 301 ? 0.7808 1.1143 0.9280 0.0428  0.0430  -0.0860 301 SER A C   
2330 O O   . SER A 301 ? 0.7526 1.1050 0.9142 0.0343  0.0524  -0.0916 301 SER A O   
2331 C CB  . SER A 301 ? 0.7642 1.1164 0.9002 0.0630  0.0363  -0.1096 301 SER A CB  
2332 O OG  . SER A 301 ? 0.8423 1.1946 0.9566 0.0807  0.0287  -0.1176 301 SER A OG  
2333 N N   . GLY A 302 ? 0.7198 1.0306 0.8670 0.0386  0.0410  -0.0716 302 GLY A N   
2334 C CA  . GLY A 302 ? 0.6594 0.9662 0.8185 0.0275  0.0490  -0.0594 302 GLY A CA  
2335 C C   . GLY A 302 ? 0.7074 1.0092 0.8863 0.0180  0.0592  -0.0575 302 GLY A C   
2336 O O   . GLY A 302 ? 0.6812 0.9844 0.8690 0.0087  0.0702  -0.0524 302 GLY A O   
2337 N N   . VAL A 303 ? 0.6838 0.9772 0.8677 0.0202  0.0570  -0.0611 303 VAL A N   
2338 C CA  . VAL A 303 ? 0.8291 1.1168 1.0304 0.0115  0.0672  -0.0609 303 VAL A CA  
2339 C C   . VAL A 303 ? 0.8538 1.1233 1.0609 0.0060  0.0732  -0.0432 303 VAL A C   
2340 O O   . VAL A 303 ? 0.8250 1.0838 1.0254 0.0109  0.0657  -0.0314 303 VAL A O   
2341 C CB  . VAL A 303 ? 0.8041 1.0852 1.0071 0.0168  0.0624  -0.0672 303 VAL A CB  
2342 C CG1 . VAL A 303 ? 0.8461 1.1147 1.0651 0.0088  0.0719  -0.0636 303 VAL A CG1 
2343 C CG2 . VAL A 303 ? 0.7918 1.0944 0.9902 0.0230  0.0594  -0.0852 303 VAL A CG2 
2344 N N   . THR A 304 ? 0.8733 1.1397 1.0917 -0.0039 0.0875  -0.0416 304 THR A N   
2345 C CA  . THR A 304 ? 0.8994 1.1460 1.1221 -0.0071 0.0959  -0.0247 304 THR A CA  
2346 C C   . THR A 304 ? 1.0088 1.2412 1.2437 -0.0117 0.1048  -0.0256 304 THR A C   
2347 O O   . THR A 304 ? 1.0609 1.2998 1.3010 -0.0131 0.1037  -0.0395 304 THR A O   
2348 C CB  . THR A 304 ? 0.8344 1.0817 1.0545 -0.0136 0.1075  -0.0187 304 THR A CB  
2349 O OG1 . THR A 304 ? 0.8806 1.1308 1.1089 -0.0259 0.1226  -0.0296 304 THR A OG1 
2350 C CG2 . THR A 304 ? 0.7379 1.0021 0.9458 -0.0094 0.0992  -0.0204 304 THR A CG2 
2351 N N   . PHE A 305 ? 0.9831 1.1957 1.2209 -0.0127 0.1140  -0.0104 305 PHE A N   
2352 C CA  . PHE A 305 ? 1.1408 1.3361 1.3880 -0.0150 0.1224  -0.0090 305 PHE A CA  
2353 C C   . PHE A 305 ? 1.2306 1.4053 1.4784 -0.0204 0.1408  0.0022  305 PHE A C   
2354 O O   . PHE A 305 ? 1.1245 1.2930 1.3650 -0.0159 0.1429  0.0175  305 PHE A O   
2355 C CB  . PHE A 305 ? 1.0687 1.2571 1.3171 -0.0049 0.1114  0.0003  305 PHE A CB  
2356 C CG  . PHE A 305 ? 0.9703 1.1727 1.2138 0.0007  0.0948  -0.0088 305 PHE A CG  
2357 C CD1 . PHE A 305 ? 1.0168 1.2258 1.2629 -0.0003 0.0923  -0.0251 305 PHE A CD1 
2358 C CD2 . PHE A 305 ? 0.8875 1.0959 1.1214 0.0071  0.0825  -0.0018 305 PHE A CD2 
2359 C CE1 . PHE A 305 ? 1.0168 1.2345 1.2545 0.0067  0.0788  -0.0326 305 PHE A CE1 
2360 C CE2 . PHE A 305 ? 0.9108 1.1267 1.1364 0.0119  0.0694  -0.0104 305 PHE A CE2 
2361 C CZ  . PHE A 305 ? 0.9483 1.1672 1.1750 0.0125  0.0679  -0.0252 305 PHE A CZ  
2362 N N   . GLN A 306 ? 1.3661 1.5292 1.6206 -0.0299 0.1548  -0.0060 306 GLN A N   
2363 C CA  . GLN A 306 ? 1.4084 1.5452 1.6608 -0.0360 0.1754  0.0030  306 GLN A CA  
2364 C C   . GLN A 306 ? 1.3630 1.4763 1.6197 -0.0309 0.1809  0.0112  306 GLN A C   
2365 O O   . GLN A 306 ? 1.3335 1.4268 1.5918 -0.0398 0.1977  0.0070  306 GLN A O   
2366 C CB  . GLN A 306 ? 1.4626 1.6014 1.7170 -0.0538 0.1908  -0.0138 306 GLN A CB  
2367 C CG  . GLN A 306 ? 1.5074 1.6605 1.7551 -0.0598 0.1936  -0.0160 306 GLN A CG  
2368 C CD  . GLN A 306 ? 1.6109 1.7573 1.8588 -0.0792 0.2151  -0.0275 306 GLN A CD  
2369 O OE1 . GLN A 306 ? 1.6078 1.7480 1.8562 -0.0879 0.2172  -0.0408 306 GLN A OE1 
2370 N NE2 . GLN A 306 ? 1.6334 1.7765 1.8723 -0.0841 0.2250  -0.0216 306 GLN A NE2 
2371 N N   . SER B 1   ? 0.3211 0.8297 0.6167 -0.1299 -0.0207 0.0192  1   SER B N   
2372 C CA  . SER B 1   ? 0.4121 0.8916 0.6784 -0.1495 -0.0220 0.0035  1   SER B CA  
2373 C C   . SER B 1   ? 0.3757 0.8027 0.6210 -0.1368 -0.0205 0.0034  1   SER B C   
2374 O O   . SER B 1   ? 0.3480 0.7575 0.6013 -0.1167 -0.0170 0.0132  1   SER B O   
2375 C CB  . SER B 1   ? 0.4884 0.9480 0.7444 -0.1731 -0.0142 -0.0101 1   SER B CB  
2376 O OG  . SER B 1   ? 0.5616 0.9892 0.7859 -0.1919 -0.0138 -0.0252 1   SER B OG  
2377 N N   . GLY B 2   ? 0.3996 0.8027 0.6174 -0.1489 -0.0227 -0.0082 2   GLY B N   
2378 C CA  . GLY B 2   ? 0.4226 0.7816 0.6193 -0.1373 -0.0220 -0.0095 2   GLY B CA  
2379 C C   . GLY B 2   ? 0.4445 0.8253 0.6404 -0.1285 -0.0307 -0.0042 2   GLY B C   
2380 O O   . GLY B 2   ? 0.4352 0.8629 0.6518 -0.1221 -0.0365 0.0058  2   GLY B O   
2381 N N   . PHE B 3   ? 0.4690 0.8155 0.6396 -0.1264 -0.0313 -0.0104 3   PHE B N   
2382 C CA  . PHE B 3   ? 0.4376 0.8030 0.6032 -0.1214 -0.0393 -0.0076 3   PHE B CA  
2383 C C   . PHE B 3   ? 0.4600 0.7856 0.6075 -0.1081 -0.0372 -0.0084 3   PHE B C   
2384 O O   . PHE B 3   ? 0.4927 0.7791 0.6133 -0.1148 -0.0340 -0.0202 3   PHE B O   
2385 C CB  . PHE B 3   ? 0.4490 0.8302 0.5984 -0.1431 -0.0446 -0.0197 3   PHE B CB  
2386 C CG  . PHE B 3   ? 0.3996 0.8186 0.5526 -0.1382 -0.0540 -0.0142 3   PHE B CG  
2387 C CD1 . PHE B 3   ? 0.3878 0.8612 0.5671 -0.1320 -0.0593 -0.0028 3   PHE B CD1 
2388 C CD2 . PHE B 3   ? 0.4349 0.8346 0.5645 -0.1360 -0.0569 -0.0188 3   PHE B CD2 
2389 C CE1 . PHE B 3   ? 0.3867 0.8954 0.5676 -0.1251 -0.0677 0.0034  3   PHE B CE1 
2390 C CE2 . PHE B 3   ? 0.4540 0.8881 0.5860 -0.1303 -0.0652 -0.0131 3   PHE B CE2 
2391 C CZ  . PHE B 3   ? 0.4383 0.9269 0.5956 -0.1248 -0.0706 -0.0018 3   PHE B CZ  
2392 N N   . ARG B 4   ? 0.4477 0.7842 0.6087 -0.0892 -0.0385 0.0039  4   ARG B N   
2393 C CA  . ARG B 4   ? 0.4240 0.7298 0.5736 -0.0755 -0.0358 0.0042  4   ARG B CA  
2394 C C   . ARG B 4   ? 0.4074 0.7338 0.5567 -0.0672 -0.0413 0.0110  4   ARG B C   
2395 O O   . ARG B 4   ? 0.4195 0.7846 0.5844 -0.0648 -0.0457 0.0206  4   ARG B O   
2396 C CB  . ARG B 4   ? 0.4087 0.7018 0.5752 -0.0607 -0.0288 0.0121  4   ARG B CB  
2397 C CG  . ARG B 4   ? 0.4058 0.6889 0.5792 -0.0668 -0.0236 0.0092  4   ARG B CG  
2398 C CD  . ARG B 4   ? 0.5584 0.7964 0.7069 -0.0696 -0.0190 -0.0031 4   ARG B CD  
2399 N NE  . ARG B 4   ? 0.4997 0.7190 0.6348 -0.0580 -0.0191 -0.0049 4   ARG B NE  
2400 C CZ  . ARG B 4   ? 0.5394 0.7426 0.6792 -0.0444 -0.0143 -0.0030 4   ARG B CZ  
2401 N NH1 . ARG B 4   ? 0.5168 0.7164 0.6724 -0.0402 -0.0089 0.0007  4   ARG B NH1 
2402 N NH2 . ARG B 4   ? 0.5401 0.7323 0.6684 -0.0352 -0.0147 -0.0055 4   ARG B NH2 
2403 N N   . LYS B 5   ? 0.4458 0.7471 0.5766 -0.0615 -0.0406 0.0063  5   LYS B N   
2404 C CA  . LYS B 5   ? 0.4168 0.7317 0.5498 -0.0498 -0.0428 0.0146  5   LYS B CA  
2405 C C   . LYS B 5   ? 0.3822 0.7046 0.5393 -0.0351 -0.0373 0.0282  5   LYS B C   
2406 O O   . LYS B 5   ? 0.4381 0.7365 0.5989 -0.0289 -0.0306 0.0270  5   LYS B O   
2407 C CB  . LYS B 5   ? 0.4284 0.7138 0.5379 -0.0460 -0.0416 0.0061  5   LYS B CB  
2408 C CG  . LYS B 5   ? 0.4605 0.7573 0.5530 -0.0502 -0.0480 0.0030  5   LYS B CG  
2409 C CD  . LYS B 5   ? 0.6359 0.8990 0.6981 -0.0529 -0.0471 -0.0108 5   LYS B CD  
2410 C CE  . LYS B 5   ? 0.5863 0.8607 0.6292 -0.0607 -0.0537 -0.0157 5   LYS B CE  
2411 N NZ  . LYS B 5   ? 0.7245 0.9629 0.7342 -0.0657 -0.0520 -0.0304 5   LYS B NZ  
2412 N N   . MET B 6   ? 0.3402 0.6957 0.5122 -0.0292 -0.0396 0.0410  6   MET B N   
2413 C CA  . MET B 6   ? 0.3365 0.6990 0.5296 -0.0156 -0.0333 0.0550  6   MET B CA  
2414 C C   . MET B 6   ? 0.2903 0.6640 0.4831 -0.0035 -0.0324 0.0662  6   MET B C   
2415 O O   . MET B 6   ? 0.3172 0.7191 0.5068 -0.0034 -0.0388 0.0711  6   MET B O   
2416 C CB  . MET B 6   ? 0.3283 0.7203 0.5400 -0.0166 -0.0347 0.0624  6   MET B CB  
2417 C CG  . MET B 6   ? 0.3568 0.7354 0.5845 -0.0106 -0.0264 0.0666  6   MET B CG  
2418 S SD  . MET B 6   ? 0.4705 0.8877 0.7172 -0.0142 -0.0293 0.0724  6   MET B SD  
2419 C CE  . MET B 6   ? 0.3832 0.8398 0.6363 0.0003  -0.0327 0.0892  6   MET B CE  
2420 N N   . ALA B 7   ? 0.2736 0.6265 0.4696 0.0062  -0.0237 0.0702  7   ALA B N   
2421 C CA  . ALA B 7   ? 0.2842 0.6432 0.4807 0.0178  -0.0195 0.0822  7   ALA B CA  
2422 C C   . ALA B 7   ? 0.3228 0.6984 0.5363 0.0294  -0.0144 0.0990  7   ALA B C   
2423 O O   . ALA B 7   ? 0.3452 0.7195 0.5724 0.0300  -0.0111 0.1007  7   ALA B O   
2424 C CB  . ALA B 7   ? 0.2972 0.6269 0.4896 0.0211  -0.0108 0.0779  7   ALA B CB  
2425 N N   . PHE B 8   ? 0.3102 0.6990 0.5210 0.0403  -0.0123 0.1120  8   PHE B N   
2426 C CA  . PHE B 8   ? 0.3112 0.7071 0.5336 0.0551  -0.0041 0.1292  8   PHE B CA  
2427 C C   . PHE B 8   ? 0.3339 0.6959 0.5626 0.0594  0.0100  0.1306  8   PHE B C   
2428 O O   . PHE B 8   ? 0.2539 0.5914 0.4757 0.0537  0.0141  0.1210  8   PHE B O   
2429 C CB  . PHE B 8   ? 0.3413 0.7531 0.5547 0.0670  -0.0035 0.1429  8   PHE B CB  
2430 C CG  . PHE B 8   ? 0.3797 0.8329 0.5898 0.0666  -0.0165 0.1452  8   PHE B CG  
2431 C CD1 . PHE B 8   ? 0.4713 0.9561 0.6932 0.0752  -0.0191 0.1556  8   PHE B CD1 
2432 C CD2 . PHE B 8   ? 0.3810 0.8429 0.5761 0.0574  -0.0260 0.1359  8   PHE B CD2 
2433 C CE1 . PHE B 8   ? 0.5396 1.0675 0.7593 0.0737  -0.0314 0.1561  8   PHE B CE1 
2434 C CE2 . PHE B 8   ? 0.4334 0.9342 0.6250 0.0551  -0.0378 0.1362  8   PHE B CE2 
2435 C CZ  . PHE B 8   ? 0.5096 1.0453 0.7140 0.0628  -0.0408 0.1459  8   PHE B CZ  
2436 N N   . PRO B 9   ? 0.3364 0.6977 0.5773 0.0697  0.0181  0.1420  9   PRO B N   
2437 C CA  . PRO B 9   ? 0.3121 0.6405 0.5569 0.0739  0.0334  0.1442  9   PRO B CA  
2438 C C   . PRO B 9   ? 0.2870 0.5996 0.5198 0.0788  0.0427  0.1498  9   PRO B C   
2439 O O   . PRO B 9   ? 0.3341 0.6606 0.5591 0.0887  0.0428  0.1626  9   PRO B O   
2440 C CB  . PRO B 9   ? 0.3497 0.6854 0.6065 0.0869  0.0398  0.1584  9   PRO B CB  
2441 C CG  . PRO B 9   ? 0.4019 0.7783 0.6590 0.0936  0.0291  0.1676  9   PRO B CG  
2442 C CD  . PRO B 9   ? 0.3646 0.7572 0.6155 0.0783  0.0142  0.1533  9   PRO B CD  
2443 N N   . SER B 10  ? 0.3075 0.5927 0.5381 0.0714  0.0506  0.1397  10  SER B N   
2444 C CA  . SER B 10  ? 0.3130 0.5855 0.5316 0.0709  0.0579  0.1401  10  SER B CA  
2445 C C   . SER B 10  ? 0.3732 0.6215 0.5908 0.0787  0.0770  0.1513  10  SER B C   
2446 O O   . SER B 10  ? 0.3671 0.6016 0.5750 0.0765  0.0860  0.1511  10  SER B O   
2447 C CB  . SER B 10  ? 0.3087 0.5704 0.5243 0.0576  0.0552  0.1209  10  SER B CB  
2448 O OG  . SER B 10  ? 0.3582 0.6006 0.5833 0.0526  0.0623  0.1119  10  SER B OG  
2449 N N   . GLY B 11  ? 0.3660 0.6081 0.5921 0.0877  0.0843  0.1613  11  GLY B N   
2450 C CA  . GLY B 11  ? 0.3279 0.5404 0.5508 0.0943  0.1045  0.1708  11  GLY B CA  
2451 C C   . GLY B 11  ? 0.3520 0.5578 0.5590 0.1039  0.1144  0.1853  11  GLY B C   
2452 O O   . GLY B 11  ? 0.4624 0.6427 0.6613 0.0981  0.1284  0.1826  11  GLY B O   
2453 N N   . LYS B 12  ? 0.3773 0.6071 0.5789 0.1183  0.1075  0.2003  12  LYS B N   
2454 C CA  . LYS B 12  ? 0.3812 0.6057 0.5651 0.1304  0.1167  0.2162  12  LYS B CA  
2455 C C   . LYS B 12  ? 0.3611 0.5797 0.5340 0.1186  0.1172  0.2071  12  LYS B C   
2456 O O   . LYS B 12  ? 0.4212 0.6205 0.5789 0.1235  0.1316  0.2166  12  LYS B O   
2457 C CB  . LYS B 12  ? 0.4172 0.6791 0.5983 0.1467  0.1044  0.2305  12  LYS B CB  
2458 C CG  . LYS B 12  ? 0.4212 0.6870 0.6072 0.1651  0.1097  0.2460  12  LYS B CG  
2459 C CD  . LYS B 12  ? 0.5543 0.8646 0.7554 0.1659  0.0900  0.2430  12  LYS B CD  
2460 C CE  . LYS B 12  ? 0.6077 0.9112 0.8274 0.1508  0.0863  0.2266  12  LYS B CE  
2461 N NZ  . LYS B 12  ? 0.5887 0.9328 0.8226 0.1467  0.0679  0.2205  12  LYS B NZ  
2462 N N   . VAL B 13  ? 0.3367 0.5719 0.5152 0.1042  0.1021  0.1897  13  VAL B N   
2463 C CA  . VAL B 13  ? 0.4173 0.6491 0.5858 0.0940  0.1024  0.1805  13  VAL B CA  
2464 C C   . VAL B 13  ? 0.4477 0.6500 0.6191 0.0811  0.1171  0.1684  13  VAL B C   
2465 O O   . VAL B 13  ? 0.4390 0.6295 0.6002 0.0760  0.1271  0.1667  13  VAL B O   
2466 C CB  . VAL B 13  ? 0.3880 0.6473 0.5581 0.0853  0.0816  0.1667  13  VAL B CB  
2467 C CG1 . VAL B 13  ? 0.3575 0.6140 0.5161 0.0762  0.0822  0.1570  13  VAL B CG1 
2468 C CG2 . VAL B 13  ? 0.3135 0.6049 0.4807 0.0957  0.0676  0.1771  13  VAL B CG2 
2469 N N   . GLU B 14  ? 0.4011 0.5935 0.5864 0.0750  0.1186  0.1590  14  GLU B N   
2470 C CA  . GLU B 14  ? 0.4255 0.5957 0.6146 0.0615  0.1309  0.1451  14  GLU B CA  
2471 C C   . GLU B 14  ? 0.4340 0.5748 0.6123 0.0628  0.1542  0.1548  14  GLU B C   
2472 O O   . GLU B 14  ? 0.4477 0.5788 0.6213 0.0512  0.1637  0.1456  14  GLU B O   
2473 C CB  . GLU B 14  ? 0.4050 0.5685 0.6093 0.0575  0.1300  0.1362  14  GLU B CB  
2474 C CG  . GLU B 14  ? 0.3829 0.5689 0.5957 0.0529  0.1101  0.1233  14  GLU B CG  
2475 C CD  . GLU B 14  ? 0.4018 0.5807 0.6283 0.0510  0.1100  0.1170  14  GLU B CD  
2476 O OE1 . GLU B 14  ? 0.5001 0.6609 0.7309 0.0432  0.1209  0.1073  14  GLU B OE1 
2477 O OE2 . GLU B 14  ? 0.3492 0.5415 0.5819 0.0565  0.0993  0.1208  14  GLU B OE2 
2478 N N   . GLY B 15  ? 0.4081 0.5348 0.5810 0.0773  0.1643  0.1735  15  GLY B N   
2479 C CA  . GLY B 15  ? 0.5079 0.6006 0.6664 0.0795  0.1886  0.1839  15  GLY B CA  
2480 C C   . GLY B 15  ? 0.5432 0.6363 0.6843 0.0806  0.1935  0.1905  15  GLY B C   
2481 O O   . GLY B 15  ? 0.5182 0.5812 0.6438 0.0833  0.2149  0.2011  15  GLY B O   
2482 N N   . CYS B 16  ? 0.4970 0.6214 0.6383 0.0788  0.1751  0.1851  16  CYS B N   
2483 C CA  . CYS B 16  ? 0.4639 0.5922 0.5883 0.0810  0.1779  0.1917  16  CYS B CA  
2484 C C   . CYS B 16  ? 0.4680 0.6050 0.5943 0.0631  0.1750  0.1725  16  CYS B C   
2485 O O   . CYS B 16  ? 0.4810 0.6205 0.5934 0.0630  0.1786  0.1762  16  CYS B O   
2486 C CB  . CYS B 16  ? 0.4996 0.6590 0.6183 0.0966  0.1599  0.2037  16  CYS B CB  
2487 S SG  . CYS B 16  ? 0.5555 0.7165 0.6700 0.1222  0.1613  0.2286  16  CYS B SG  
2488 N N   . MET B 17  ? 0.3901 0.5327 0.5321 0.0493  0.1691  0.1525  17  MET B N   
2489 C CA  . MET B 17  ? 0.4483 0.6041 0.5924 0.0349  0.1648  0.1339  17  MET B CA  
2490 C C   . MET B 17  ? 0.5172 0.6515 0.6604 0.0203  0.1867  0.1254  17  MET B C   
2491 O O   . MET B 17  ? 0.5535 0.6708 0.7059 0.0128  0.1970  0.1187  17  MET B O   
2492 C CB  . MET B 17  ? 0.4162 0.5920 0.5751 0.0296  0.1464  0.1166  17  MET B CB  
2493 C CG  . MET B 17  ? 0.4179 0.6107 0.5785 0.0414  0.1280  0.1245  17  MET B CG  
2494 S SD  . MET B 17  ? 0.4301 0.6460 0.5746 0.0484  0.1154  0.1314  17  MET B SD  
2495 C CE  . MET B 17  ? 0.3588 0.5803 0.4982 0.0351  0.1179  0.1136  17  MET B CE  
2496 N N   . VAL B 18  ? 0.5037 0.6401 0.6356 0.0151  0.1939  0.1246  18  VAL B N   
2497 C CA  . VAL B 18  ? 0.5493 0.6722 0.6804 -0.0019 0.2137  0.1137  18  VAL B CA  
2498 C C   . VAL B 18  ? 0.5549 0.7075 0.6904 -0.0119 0.2036  0.0952  18  VAL B C   
2499 O O   . VAL B 18  ? 0.4858 0.6637 0.6219 -0.0047 0.1829  0.0924  18  VAL B O   
2500 C CB  . VAL B 18  ? 0.5692 0.6636 0.6806 0.0001  0.2365  0.1302  18  VAL B CB  
2501 C CG1 . VAL B 18  ? 0.6124 0.6790 0.7163 0.0152  0.2448  0.1508  18  VAL B CG1 
2502 C CG2 . VAL B 18  ? 0.5331 0.6437 0.6300 0.0072  0.2301  0.1381  18  VAL B CG2 
2503 N N   . GLN B 19  ? 0.5964 0.7463 0.7347 -0.0291 0.2191  0.0813  19  GLN B N   
2504 C CA  . GLN B 19  ? 0.5539 0.7335 0.6959 -0.0382 0.2128  0.0636  19  GLN B CA  
2505 C C   . GLN B 19  ? 0.5903 0.7636 0.7180 -0.0446 0.2297  0.0687  19  GLN B C   
2506 O O   . GLN B 19  ? 0.6390 0.7838 0.7603 -0.0532 0.2532  0.0744  19  GLN B O   
2507 C CB  . GLN B 19  ? 0.5861 0.7781 0.7452 -0.0533 0.2149  0.0404  19  GLN B CB  
2508 C CG  . GLN B 19  ? 0.7321 0.9065 0.8923 -0.0723 0.2410  0.0335  19  GLN B CG  
2509 C CD  . GLN B 19  ? 0.7836 0.9874 0.9577 -0.0888 0.2417  0.0073  19  GLN B CD  
2510 O OE1 . GLN B 19  ? 0.7516 0.9769 0.9383 -0.0859 0.2258  -0.0057 19  GLN B OE1 
2511 N NE2 . GLN B 19  ? 0.7433 0.9495 0.9145 -0.1058 0.2606  -0.0006 19  GLN B NE2 
2512 N N   . VAL B 20  ? 0.5772 0.7738 0.6977 -0.0399 0.2190  0.0677  20  VAL B N   
2513 C CA  . VAL B 20  ? 0.5445 0.7377 0.6506 -0.0452 0.2340  0.0725  20  VAL B CA  
2514 C C   . VAL B 20  ? 0.5544 0.7788 0.6687 -0.0583 0.2331  0.0506  20  VAL B C   
2515 O O   . VAL B 20  ? 0.4949 0.7484 0.6157 -0.0528 0.2130  0.0393  20  VAL B O   
2516 C CB  . VAL B 20  ? 0.5434 0.7379 0.6315 -0.0279 0.2247  0.0911  20  VAL B CB  
2517 C CG1 . VAL B 20  ? 0.5160 0.7070 0.5883 -0.0334 0.2409  0.0956  20  VAL B CG1 
2518 C CG2 . VAL B 20  ? 0.5674 0.7361 0.6484 -0.0137 0.2259  0.1124  20  VAL B CG2 
2519 N N   . THR B 21  ? 0.5894 0.8072 0.7023 -0.0757 0.2559  0.0443  21  THR B N   
2520 C CA  . THR B 21  ? 0.5813 0.8318 0.7025 -0.0896 0.2584  0.0233  21  THR B CA  
2521 C C   . THR B 21  ? 0.5751 0.8229 0.6808 -0.0954 0.2745  0.0294  21  THR B C   
2522 O O   . THR B 21  ? 0.6051 0.8195 0.6991 -0.1026 0.2973  0.0409  21  THR B O   
2523 C CB  . THR B 21  ? 0.5982 0.8515 0.7361 -0.1097 0.2714  0.0044  21  THR B CB  
2524 O OG1 . THR B 21  ? 0.5948 0.8395 0.7434 -0.1034 0.2604  0.0036  21  THR B OG1 
2525 C CG2 . THR B 21  ? 0.5775 0.8742 0.7263 -0.1170 0.2626  -0.0186 21  THR B CG2 
2526 N N   . CYS B 22  ? 0.5712 0.8519 0.6748 -0.0913 0.2634  0.0222  22  CYS B N   
2527 C CA  . CYS B 22  ? 0.6134 0.8996 0.7045 -0.0979 0.2775  0.0241  22  CYS B CA  
2528 C C   . CYS B 22  ? 0.6271 0.9583 0.7313 -0.1082 0.2744  -0.0001 22  CYS B C   
2529 O O   . CYS B 22  ? 0.6228 0.9832 0.7318 -0.0960 0.2523  -0.0085 22  CYS B O   
2530 C CB  . CYS B 22  ? 0.5838 0.8662 0.6549 -0.0784 0.2661  0.0426  22  CYS B CB  
2531 S SG  . CYS B 22  ? 0.6775 0.9578 0.7296 -0.0851 0.2861  0.0492  22  CYS B SG  
2532 N N   . GLY B 23  ? 0.7178 1.0451 0.8252 -0.1245 0.2879  -0.0089 23  GLY B N   
2533 C CA  . GLY B 23  ? 0.6590 1.0213 0.7777 -0.1293 0.2780  -0.0299 23  GLY B CA  
2534 C C   . GLY B 23  ? 0.6075 0.9888 0.7431 -0.1249 0.2594  -0.0453 23  GLY B C   
2535 O O   . GLY B 23  ? 0.5680 0.9316 0.7119 -0.1312 0.2617  -0.0475 23  GLY B O   
2536 N N   . THR B 24  ? 0.6026 1.0175 0.7405 -0.1122 0.2405  -0.0550 24  THR B N   
2537 C CA  . THR B 24  ? 0.6708 1.1026 0.8205 -0.1047 0.2217  -0.0681 24  THR B CA  
2538 C C   . THR B 24  ? 0.6455 1.0694 0.7943 -0.0905 0.2109  -0.0584 24  THR B C   
2539 O O   . THR B 24  ? 0.6530 1.0801 0.8115 -0.0862 0.1992  -0.0664 24  THR B O   
2540 C CB  . THR B 24  ? 0.8294 1.2978 0.9786 -0.0956 0.2062  -0.0828 24  THR B CB  
2541 O OG1 . THR B 24  ? 0.9261 1.4080 1.0853 -0.0917 0.1917  -0.0972 24  THR B OG1 
2542 C CG2 . THR B 24  ? 0.7832 1.2623 0.9193 -0.0770 0.1947  -0.0748 24  THR B CG2 
2543 N N   . THR B 25  ? 0.6029 1.0174 0.7395 -0.0834 0.2145  -0.0413 25  THR B N   
2544 C CA  . THR B 25  ? 0.5590 0.9576 0.6898 -0.0654 0.1951  -0.0299 25  THR B CA  
2545 C C   . THR B 25  ? 0.5280 0.8906 0.6625 -0.0681 0.2008  -0.0178 25  THR B C   
2546 O O   . THR B 25  ? 0.5394 0.8767 0.6696 -0.0776 0.2199  -0.0072 25  THR B O   
2547 C CB  . THR B 25  ? 0.5732 0.9655 0.6838 -0.0515 0.1866  -0.0148 25  THR B CB  
2548 O OG1 . THR B 25  ? 0.6561 1.0810 0.7618 -0.0466 0.1797  -0.0266 25  THR B OG1 
2549 C CG2 . THR B 25  ? 0.5135 0.8897 0.6185 -0.0357 0.1674  -0.0042 25  THR B CG2 
2550 N N   . THR B 26  ? 0.5080 0.8672 0.6493 -0.0591 0.1852  -0.0194 26  THR B N   
2551 C CA  . THR B 26  ? 0.4897 0.8168 0.6337 -0.0576 0.1872  -0.0067 26  THR B CA  
2552 C C   . THR B 26  ? 0.4580 0.7803 0.5969 -0.0400 0.1653  0.0018  26  THR B C   
2553 O O   . THR B 26  ? 0.4377 0.7776 0.5805 -0.0335 0.1496  -0.0099 26  THR B O   
2554 C CB  . THR B 26  ? 0.5060 0.8318 0.6675 -0.0701 0.1952  -0.0200 26  THR B CB  
2555 O OG1 . THR B 26  ? 0.6105 0.9343 0.7753 -0.0895 0.2188  -0.0263 26  THR B OG1 
2556 C CG2 . THR B 26  ? 0.4872 0.7816 0.6511 -0.0652 0.1942  -0.0074 26  THR B CG2 
2557 N N   . LEU B 27  ? 0.4756 0.7739 0.6052 -0.0324 0.1653  0.0219  27  LEU B N   
2558 C CA  . LEU B 27  ? 0.4262 0.7198 0.5525 -0.0184 0.1466  0.0302  27  LEU B CA  
2559 C C   . LEU B 27  ? 0.4422 0.7080 0.5692 -0.0154 0.1533  0.0478  27  LEU B C   
2560 O O   . LEU B 27  ? 0.4507 0.6972 0.5786 -0.0233 0.1729  0.0534  27  LEU B O   
2561 C CB  . LEU B 27  ? 0.4091 0.7145 0.5191 -0.0079 0.1336  0.0356  27  LEU B CB  
2562 C CG  . LEU B 27  ? 0.4255 0.7291 0.5219 -0.0094 0.1459  0.0451  27  LEU B CG  
2563 C CD1 . LEU B 27  ? 0.4292 0.7070 0.5198 -0.0066 0.1571  0.0657  27  LEU B CD1 
2564 C CD2 . LEU B 27  ? 0.4049 0.7241 0.4854 0.0002  0.1321  0.0462  27  LEU B CD2 
2565 N N   . ASN B 28  ? 0.3719 0.6353 0.4966 -0.0036 0.1380  0.0569  28  ASN B N   
2566 C CA  . ASN B 28  ? 0.3977 0.6395 0.5241 0.0018  0.1425  0.0731  28  ASN B CA  
2567 C C   . ASN B 28  ? 0.4118 0.6452 0.5219 0.0110  0.1471  0.0935  28  ASN B C   
2568 O O   . ASN B 28  ? 0.4006 0.6478 0.4982 0.0153  0.1404  0.0954  28  ASN B O   
2569 C CB  . ASN B 28  ? 0.3983 0.6445 0.5319 0.0091  0.1248  0.0722  28  ASN B CB  
2570 C CG  . ASN B 28  ? 0.4254 0.6830 0.5702 0.0032  0.1171  0.0518  28  ASN B CG  
2571 O OD1 . ASN B 28  ? 0.4999 0.7499 0.6570 -0.0042 0.1257  0.0441  28  ASN B OD1 
2572 N ND2 . ASN B 28  ? 0.3881 0.6632 0.5267 0.0070  0.1015  0.0427  28  ASN B ND2 
2573 N N   . GLY B 29  ? 0.3987 0.6086 0.5075 0.0148  0.1602  0.1087  29  GLY B N   
2574 C CA  . GLY B 29  ? 0.4065 0.6075 0.4988 0.0271  0.1648  0.1302  29  GLY B CA  
2575 C C   . GLY B 29  ? 0.4636 0.6528 0.5589 0.0390  0.1633  0.1450  29  GLY B C   
2576 O O   . GLY B 29  ? 0.4141 0.5959 0.5238 0.0354  0.1634  0.1390  29  GLY B O   
2577 N N   . LEU B 30  ? 0.4472 0.6368 0.5281 0.0542  0.1620  0.1644  30  LEU B N   
2578 C CA  . LEU B 30  ? 0.4780 0.6643 0.5606 0.0688  0.1584  0.1798  30  LEU B CA  
2579 C C   . LEU B 30  ? 0.4741 0.6315 0.5408 0.0792  0.1803  0.2004  30  LEU B C   
2580 O O   . LEU B 30  ? 0.4973 0.6543 0.5452 0.0870  0.1854  0.2123  30  LEU B O   
2581 C CB  . LEU B 30  ? 0.4911 0.7090 0.5704 0.0799  0.1356  0.1845  30  LEU B CB  
2582 C CG  . LEU B 30  ? 0.4319 0.6584 0.5149 0.0952  0.1277  0.1986  30  LEU B CG  
2583 C CD1 . LEU B 30  ? 0.4028 0.6392 0.5055 0.0889  0.1148  0.1859  30  LEU B CD1 
2584 C CD2 . LEU B 30  ? 0.4299 0.6842 0.5002 0.1083  0.1139  0.2096  30  LEU B CD2 
2585 N N   . TRP B 31  ? 0.5145 0.6460 0.5865 0.0805  0.1937  0.2052  31  TRP B N   
2586 C CA  . TRP B 31  ? 0.5369 0.6311 0.5918 0.0881  0.2193  0.2225  31  TRP B CA  
2587 C C   . TRP B 31  ? 0.5432 0.6379 0.5915 0.1125  0.2164  0.2443  31  TRP B C   
2588 O O   . TRP B 31  ? 0.5321 0.6256 0.5934 0.1166  0.2127  0.2445  31  TRP B O   
2589 C CB  . TRP B 31  ? 0.5756 0.6374 0.6383 0.0719  0.2391  0.2117  31  TRP B CB  
2590 C CG  . TRP B 31  ? 0.6723 0.6870 0.7150 0.0758  0.2695  0.2268  31  TRP B CG  
2591 C CD1 . TRP B 31  ? 0.6992 0.6957 0.7158 0.0885  0.2838  0.2463  31  TRP B CD1 
2592 C CD2 . TRP B 31  ? 0.7199 0.6977 0.7652 0.0672  0.2899  0.2233  31  TRP B CD2 
2593 N NE1 . TRP B 31  ? 0.7444 0.6915 0.7456 0.0883  0.3132  0.2555  31  TRP B NE1 
2594 C CE2 . TRP B 31  ? 0.8023 0.7372 0.8210 0.0746  0.3173  0.2410  31  TRP B CE2 
2595 C CE3 . TRP B 31  ? 0.6805 0.6559 0.7462 0.0540  0.2884  0.2066  31  TRP B CE3 
2596 C CZ2 . TRP B 31  ? 0.8277 0.7159 0.8394 0.0684  0.3435  0.2421  31  TRP B CZ2 
2597 C CZ3 . TRP B 31  ? 0.7604 0.6931 0.8205 0.0476  0.3131  0.2072  31  TRP B CZ3 
2598 C CH2 . TRP B 31  ? 0.7658 0.6544 0.7989 0.0543  0.3406  0.2245  31  TRP B CH2 
2599 N N   . LEU B 32  ? 0.5698 0.6673 0.5969 0.1294  0.2188  0.2629  32  LEU B N   
2600 C CA  . LEU B 32  ? 0.5979 0.7011 0.6154 0.1557  0.2165  0.2852  32  LEU B CA  
2601 C C   . LEU B 32  ? 0.6721 0.7398 0.6599 0.1701  0.2414  0.3066  32  LEU B C   
2602 O O   . LEU B 32  ? 0.6583 0.7237 0.6294 0.1680  0.2470  0.3092  32  LEU B O   
2603 C CB  . LEU B 32  ? 0.5653 0.7182 0.5855 0.1653  0.1892  0.2866  32  LEU B CB  
2604 C CG  . LEU B 32  ? 0.5447 0.7295 0.5908 0.1506  0.1654  0.2654  32  LEU B CG  
2605 C CD1 . LEU B 32  ? 0.5036 0.7309 0.5476 0.1524  0.1422  0.2617  32  LEU B CD1 
2606 C CD2 . LEU B 32  ? 0.5169 0.7064 0.5794 0.1573  0.1602  0.2675  32  LEU B CD2 
2607 N N   . ASP B 33  ? 0.6713 0.7098 0.6508 0.1857  0.2574  0.3223  33  ASP B N   
2608 C CA  . ASP B 33  ? 0.7583 0.7522 0.7065 0.1998  0.2857  0.3430  33  ASP B CA  
2609 C C   . ASP B 33  ? 0.7439 0.7050 0.6851 0.1745  0.3057  0.3304  33  ASP B C   
2610 O O   . ASP B 33  ? 0.7317 0.6859 0.6925 0.1502  0.3075  0.3093  33  ASP B O   
2611 C CB  . ASP B 33  ? 0.7987 0.8149 0.7254 0.2272  0.2787  0.3648  33  ASP B CB  
2612 C CG  . ASP B 33  ? 0.8184 0.8760 0.7560 0.2492  0.2571  0.3738  33  ASP B CG  
2613 O OD1 . ASP B 33  ? 0.9059 0.9475 0.8465 0.2612  0.2649  0.3820  33  ASP B OD1 
2614 O OD2 . ASP B 33  ? 0.8251 0.9321 0.7683 0.2537  0.2329  0.3719  33  ASP B OD2 
2615 N N   . ASP B 34  ? 0.7820 0.7242 0.6960 0.1791  0.3213  0.3420  34  ASP B N   
2616 C CA  . ASP B 34  ? 0.8566 0.7700 0.7644 0.1542  0.3398  0.3281  34  ASP B CA  
2617 C C   . ASP B 34  ? 0.8019 0.7527 0.7174 0.1393  0.3251  0.3148  34  ASP B C   
2618 O O   . ASP B 34  ? 0.8054 0.7389 0.7069 0.1268  0.3413  0.3119  34  ASP B O   
2619 C CB  . ASP B 34  ? 0.8836 0.7492 0.7610 0.1639  0.3614  0.3377  34  ASP B CB  
2620 C CG  . ASP B 34  ? 0.9209 0.8019 0.7757 0.1912  0.3546  0.3580  34  ASP B CG  
2621 O OD1 . ASP B 34  ? 0.8750 0.8023 0.7370 0.2075  0.3323  0.3670  34  ASP B OD1 
2622 O OD2 . ASP B 34  ? 0.9356 0.7824 0.7649 0.1961  0.3719  0.3640  34  ASP B OD2 
2623 N N   . VAL B 35  ? 0.7654 0.7661 0.7038 0.1387  0.2938  0.3033  35  VAL B N   
2624 C CA  . VAL B 35  ? 0.6877 0.7240 0.6327 0.1267  0.2769  0.2888  35  VAL B CA  
2625 C C   . VAL B 35  ? 0.6358 0.6991 0.6120 0.1082  0.2575  0.2636  35  VAL B C   
2626 O O   . VAL B 35  ? 0.6510 0.7275 0.6435 0.1139  0.2435  0.2620  35  VAL B O   
2627 C CB  . VAL B 35  ? 0.6852 0.7569 0.6186 0.1475  0.2572  0.3018  35  VAL B CB  
2628 C CG1 . VAL B 35  ? 0.6566 0.7614 0.5961 0.1337  0.2407  0.2850  35  VAL B CG1 
2629 C CG2 . VAL B 35  ? 0.7397 0.7866 0.6389 0.1695  0.2759  0.3285  35  VAL B CG2 
2630 N N   . VAL B 36  ? 0.6195 0.6918 0.6032 0.0871  0.2572  0.2442  36  VAL B N   
2631 C CA  . VAL B 36  ? 0.5724 0.6729 0.5820 0.0718  0.2381  0.2204  36  VAL B CA  
2632 C C   . VAL B 36  ? 0.5507 0.6888 0.5587 0.0729  0.2171  0.2139  36  VAL B C   
2633 O O   . VAL B 36  ? 0.5686 0.7065 0.5609 0.0712  0.2245  0.2164  36  VAL B O   
2634 C CB  . VAL B 36  ? 0.5697 0.6545 0.5907 0.0473  0.2537  0.2010  36  VAL B CB  
2635 C CG1 . VAL B 36  ? 0.5223 0.6401 0.5673 0.0343  0.2329  0.1763  36  VAL B CG1 
2636 C CG2 . VAL B 36  ? 0.6092 0.6578 0.6325 0.0457  0.2721  0.2055  36  VAL B CG2 
2637 N N   . TYR B 37  ? 0.5149 0.6831 0.5375 0.0753  0.1920  0.2052  37  TYR B N   
2638 C CA  . TYR B 37  ? 0.4957 0.6976 0.5155 0.0770  0.1709  0.1985  37  TYR B CA  
2639 C C   . TYR B 37  ? 0.4628 0.6794 0.4992 0.0603  0.1610  0.1737  37  TYR B C   
2640 O O   . TYR B 37  ? 0.4411 0.6577 0.4952 0.0551  0.1552  0.1640  37  TYR B O   
2641 C CB  . TYR B 37  ? 0.4849 0.7100 0.5052 0.0925  0.1503  0.2075  37  TYR B CB  
2642 C CG  . TYR B 37  ? 0.5175 0.7339 0.5210 0.1126  0.1585  0.2326  37  TYR B CG  
2643 C CD1 . TYR B 37  ? 0.5350 0.7256 0.5402 0.1203  0.1730  0.2450  37  TYR B CD1 
2644 C CD2 . TYR B 37  ? 0.5343 0.7669 0.5181 0.1250  0.1530  0.2441  37  TYR B CD2 
2645 C CE1 . TYR B 37  ? 0.5687 0.7503 0.5559 0.1417  0.1817  0.2689  37  TYR B CE1 
2646 C CE2 . TYR B 37  ? 0.5668 0.7930 0.5332 0.1460  0.1609  0.2678  37  TYR B CE2 
2647 C CZ  . TYR B 37  ? 0.5844 0.7849 0.5522 0.1551  0.1753  0.2805  37  TYR B CZ  
2648 O OH  . TYR B 37  ? 0.6202 0.8136 0.5682 0.1790  0.1839  0.3051  37  TYR B OH  
2649 N N   . CYS B 38  ? 0.4604 0.6901 0.4901 0.0534  0.1591  0.1639  38  CYS B N   
2650 C CA  . CYS B 38  ? 0.4317 0.6772 0.4747 0.0407  0.1496  0.1408  38  CYS B CA  
2651 C C   . CYS B 38  ? 0.4277 0.6956 0.4590 0.0415  0.1387  0.1341  38  CYS B C   
2652 O O   . CYS B 38  ? 0.4496 0.7180 0.4630 0.0482  0.1432  0.1459  38  CYS B O   
2653 C CB  . CYS B 38  ? 0.4359 0.6676 0.4895 0.0247  0.1682  0.1289  38  CYS B CB  
2654 S SG  . CYS B 38  ? 0.4826 0.7119 0.5224 0.0156  0.1873  0.1273  38  CYS B SG  
2655 N N   . PRO B 39  ? 0.4024 0.6877 0.4415 0.0358  0.1251  0.1155  39  PRO B N   
2656 C CA  . PRO B 39  ? 0.4004 0.7049 0.4267 0.0373  0.1152  0.1081  39  PRO B CA  
2657 C C   . PRO B 39  ? 0.4248 0.7281 0.4433 0.0309  0.1322  0.1066  39  PRO B C   
2658 O O   . PRO B 39  ? 0.4268 0.7224 0.4558 0.0197  0.1477  0.0993  39  PRO B O   
2659 C CB  . PRO B 39  ? 0.3731 0.6898 0.4098 0.0328  0.1013  0.0881  39  PRO B CB  
2660 C CG  . PRO B 39  ? 0.3620 0.6676 0.4163 0.0313  0.0995  0.0883  39  PRO B CG  
2661 C CD  . PRO B 39  ? 0.3775 0.6635 0.4355 0.0291  0.1192  0.1008  39  PRO B CD  
2662 N N   . ARG B 40  ? 0.4327 0.7445 0.4323 0.0373  0.1298  0.1132  40  ARG B N   
2663 C CA  . ARG B 40  ? 0.4527 0.7628 0.4432 0.0318  0.1472  0.1138  40  ARG B CA  
2664 C C   . ARG B 40  ? 0.4378 0.7635 0.4379 0.0206  0.1491  0.0923  40  ARG B C   
2665 O O   . ARG B 40  ? 0.4515 0.7760 0.4513 0.0112  0.1671  0.0893  40  ARG B O   
2666 C CB  . ARG B 40  ? 0.4721 0.7894 0.4389 0.0422  0.1434  0.1254  40  ARG B CB  
2667 C CG  . ARG B 40  ? 0.4590 0.7995 0.4171 0.0461  0.1244  0.1138  40  ARG B CG  
2668 C CD  . ARG B 40  ? 0.4825 0.8287 0.4165 0.0543  0.1252  0.1246  40  ARG B CD  
2669 N NE  . ARG B 40  ? 0.4747 0.8397 0.3967 0.0593  0.1065  0.1155  40  ARG B NE  
2670 C CZ  . ARG B 40  ? 0.4931 0.8661 0.3931 0.0672  0.1032  0.1231  40  ARG B CZ  
2671 N NH1 . ARG B 40  ? 0.5200 0.8849 0.4072 0.0720  0.1172  0.1401  40  ARG B NH1 
2672 N NH2 . ARG B 40  ? 0.4871 0.8747 0.3758 0.0707  0.0861  0.1135  40  ARG B NH2 
2673 N N   . HIS B 41  ? 0.4345 0.7751 0.4423 0.0216  0.1323  0.0772  41  HIS B N   
2674 C CA  . HIS B 41  ? 0.4609 0.8199 0.4745 0.0148  0.1339  0.0579  41  HIS B CA  
2675 C C   . HIS B 41  ? 0.4504 0.8075 0.4843 0.0016  0.1478  0.0477  41  HIS B C   
2676 O O   . HIS B 41  ? 0.4399 0.8171 0.4810 -0.0042 0.1497  0.0307  41  HIS B O   
2677 C CB  . HIS B 41  ? 0.4165 0.7900 0.4272 0.0221  0.1130  0.0450  41  HIS B CB  
2678 C CG  . HIS B 41  ? 0.4399 0.8078 0.4647 0.0222  0.1030  0.0388  41  HIS B CG  
2679 N ND1 . HIS B 41  ? 0.4900 0.8622 0.5329 0.0147  0.1084  0.0256  41  HIS B ND1 
2680 C CD2 . HIS B 41  ? 0.4527 0.8127 0.4759 0.0284  0.0883  0.0433  41  HIS B CD2 
2681 C CE1 . HIS B 41  ? 0.4503 0.8153 0.5010 0.0174  0.0974  0.0231  41  HIS B CE1 
2682 N NE2 . HIS B 41  ? 0.4725 0.8297 0.5118 0.0252  0.0853  0.0335  41  HIS B NE2 
2683 N N   . VAL B 42  ? 0.4024 0.7374 0.4443 -0.0030 0.1585  0.0576  42  VAL B N   
2684 C CA  . VAL B 42  ? 0.5042 0.8351 0.5622 -0.0181 0.1757  0.0484  42  VAL B CA  
2685 C C   . VAL B 42  ? 0.5151 0.8514 0.5680 -0.0294 0.1959  0.0456  42  VAL B C   
2686 O O   . VAL B 42  ? 0.5154 0.8605 0.5818 -0.0443 0.2085  0.0315  42  VAL B O   
2687 C CB  . VAL B 42  ? 0.4128 0.7141 0.4765 -0.0197 0.1846  0.0608  42  VAL B CB  
2688 C CG1 . VAL B 42  ? 0.4458 0.7235 0.4923 -0.0159 0.1990  0.0823  42  VAL B CG1 
2689 C CG2 . VAL B 42  ? 0.4907 0.7887 0.5721 -0.0362 0.1995  0.0476  42  VAL B CG2 
2690 N N   . ILE B 43  ? 0.4702 0.8036 0.5037 -0.0231 0.1989  0.0581  43  ILE B N   
2691 C CA  . ILE B 43  ? 0.5179 0.8575 0.5435 -0.0325 0.2171  0.0564  43  ILE B CA  
2692 C C   . ILE B 43  ? 0.5219 0.8984 0.5536 -0.0363 0.2117  0.0357  43  ILE B C   
2693 O O   . ILE B 43  ? 0.5095 0.8974 0.5405 -0.0476 0.2281  0.0295  43  ILE B O   
2694 C CB  . ILE B 43  ? 0.5072 0.8335 0.5082 -0.0211 0.2191  0.0769  43  ILE B CB  
2695 C CG1 . ILE B 43  ? 0.5675 0.8576 0.5599 -0.0240 0.2402  0.0954  43  ILE B CG1 
2696 C CG2 . ILE B 43  ? 0.5499 0.8967 0.5392 -0.0217 0.2222  0.0720  43  ILE B CG2 
2697 C CD1 . ILE B 43  ? 0.5920 0.8622 0.5965 -0.0244 0.2398  0.0988  43  ILE B CD1 
2698 N N   . CYS B 44  ? 0.4924 0.8875 0.5281 -0.0263 0.1901  0.0253  44  CYS B N   
2699 C CA  . CYS B 44  ? 0.5802 1.0084 0.6148 -0.0236 0.1833  0.0092  44  CYS B CA  
2700 C C   . CYS B 44  ? 0.6712 1.1226 0.7270 -0.0321 0.1841  -0.0119 44  CYS B C   
2701 O O   . CYS B 44  ? 0.6233 1.0663 0.6925 -0.0340 0.1797  -0.0152 44  CYS B O   
2702 C CB  . CYS B 44  ? 0.5706 1.0032 0.5910 -0.0057 0.1602  0.0105  44  CYS B CB  
2703 S SG  . CYS B 44  ? 0.4819 0.8950 0.4767 0.0052  0.1563  0.0332  44  CYS B SG  
2704 N N   . THR B 45  ? 0.7471 1.2308 0.8053 -0.0361 0.1894  -0.0264 45  THR B N   
2705 C CA  . THR B 45  ? 0.8287 1.3382 0.9045 -0.0409 0.1869  -0.0474 45  THR B CA  
2706 C C   . THR B 45  ? 0.8834 1.4103 0.9537 -0.0222 0.1651  -0.0564 45  THR B C   
2707 O O   . THR B 45  ? 0.8871 1.4010 0.9418 -0.0082 0.1521  -0.0468 45  THR B O   
2708 C CB  . THR B 45  ? 0.7994 1.3203 0.8779 -0.0520 0.1974  -0.0567 45  THR B CB  
2709 O OG1 . THR B 45  ? 0.8782 1.4181 0.9421 -0.0396 0.1894  -0.0586 45  THR B OG1 
2710 C CG2 . THR B 45  ? 0.7646 1.2631 0.8408 -0.0681 0.2206  -0.0450 45  THR B CG2 
2711 N N   . SER B 46  ? 0.9781 1.5216 1.0575 -0.0211 0.1572  -0.0736 46  SER B N   
2712 C CA  . SER B 46  ? 1.0094 1.5652 1.0803 -0.0023 0.1381  -0.0819 46  SER B CA  
2713 C C   . SER B 46  ? 1.0240 1.5889 1.0735 0.0109  0.1332  -0.0791 46  SER B C   
2714 O O   . SER B 46  ? 0.9710 1.5327 1.0050 0.0274  0.1205  -0.0776 46  SER B O   
2715 C CB  . SER B 46  ? 0.9465 1.5192 1.0289 -0.0032 0.1317  -0.0991 46  SER B CB  
2716 O OG  . SER B 46  ? 1.0092 1.5900 1.0805 0.0164  0.1146  -0.1059 46  SER B OG  
2717 N N   . GLU B 47  ? 0.9861 1.5604 1.0330 0.0038  0.1435  -0.0788 47  GLU B N   
2718 C CA  . GLU B 47  ? 0.9712 1.5540 0.9976 0.0159  0.1394  -0.0767 47  GLU B CA  
2719 C C   . GLU B 47  ? 0.8923 1.4601 0.9017 0.0172  0.1453  -0.0592 47  GLU B C   
2720 O O   . GLU B 47  ? 0.8837 1.4520 0.8716 0.0317  0.1364  -0.0562 47  GLU B O   
2721 C CB  . GLU B 47  ? 1.0600 1.6626 1.0903 0.0093  0.1468  -0.0849 47  GLU B CB  
2722 C CG  . GLU B 47  ? 1.0708 1.6670 1.1090 -0.0109 0.1674  -0.0785 47  GLU B CG  
2723 C CD  . GLU B 47  ? 1.1495 1.7497 1.2107 -0.0282 0.1751  -0.0885 47  GLU B CD  
2724 O OE1 . GLU B 47  ? 1.1339 1.7421 1.2049 -0.0239 0.1635  -0.0991 47  GLU B OE1 
2725 O OE2 . GLU B 47  ? 1.1445 1.7382 1.2118 -0.0458 0.1930  -0.0857 47  GLU B OE2 
2726 N N   . ASP B 48  ? 0.8626 1.4158 0.8787 0.0031  0.1602  -0.0472 48  ASP B N   
2727 C CA  . ASP B 48  ? 0.7998 1.3266 0.7977 0.0058  0.1611  -0.0275 48  ASP B CA  
2728 C C   . ASP B 48  ? 0.7049 1.2130 0.6865 0.0218  0.1399  -0.0211 48  ASP B C   
2729 O O   . ASP B 48  ? 0.6208 1.1185 0.5817 0.0290  0.1356  -0.0101 48  ASP B O   
2730 C CB  . ASP B 48  ? 0.8034 1.3039 0.8102 -0.0082 0.1754  -0.0142 48  ASP B CB  
2731 C CG  . ASP B 48  ? 0.8169 1.3259 0.8297 -0.0254 0.2002  -0.0153 48  ASP B CG  
2732 O OD1 . ASP B 48  ? 0.7903 1.2856 0.8169 -0.0404 0.2144  -0.0137 48  ASP B OD1 
2733 O OD2 . ASP B 48  ? 0.8009 1.3263 0.8032 -0.0245 0.2059  -0.0175 48  ASP B OD2 
2734 N N   . MET B 49  ? 0.7664 1.2721 0.7556 0.0272  0.1269  -0.0292 49  MET B N   
2735 C CA  . MET B 49  ? 0.6673 1.1509 0.6443 0.0378  0.1090  -0.0230 49  MET B CA  
2736 C C   . MET B 49  ? 0.6310 1.1182 0.5827 0.0517  0.0973  -0.0263 49  MET B C   
2737 O O   . MET B 49  ? 0.5670 1.0354 0.5036 0.0578  0.0853  -0.0185 49  MET B O   
2738 C CB  . MET B 49  ? 0.7072 1.1875 0.6979 0.0393  0.1003  -0.0323 49  MET B CB  
2739 C CG  . MET B 49  ? 0.7175 1.1840 0.7295 0.0275  0.1072  -0.0264 49  MET B CG  
2740 S SD  . MET B 49  ? 0.7796 1.2144 0.7861 0.0249  0.1077  -0.0030 49  MET B SD  
2741 C CE  . MET B 49  ? 0.5750 1.0031 0.5549 0.0391  0.0889  0.0016  49  MET B CE  
2742 N N   . LEU B 50  ? 0.6776 1.1895 0.6239 0.0567  0.1010  -0.0380 50  LEU B N   
2743 C CA  . LEU B 50  ? 0.6886 1.2016 0.6091 0.0713  0.0904  -0.0426 50  LEU B CA  
2744 C C   . LEU B 50  ? 0.6968 1.1932 0.5967 0.0725  0.0874  -0.0282 50  LEU B C   
2745 O O   . LEU B 50  ? 0.7247 1.2056 0.6049 0.0808  0.0738  -0.0273 50  LEU B O   
2746 C CB  . LEU B 50  ? 0.7383 1.2837 0.6574 0.0766  0.0977  -0.0560 50  LEU B CB  
2747 C CG  . LEU B 50  ? 0.8659 1.4142 0.7613 0.0949  0.0868  -0.0663 50  LEU B CG  
2748 C CD1 . LEU B 50  ? 0.8701 1.4035 0.7382 0.0999  0.0824  -0.0576 50  LEU B CD1 
2749 C CD2 . LEU B 50  ? 0.8629 1.3937 0.7554 0.1030  0.0737  -0.0722 50  LEU B CD2 
2750 N N   . ASN B 51  ? 0.6929 1.1920 0.5956 0.0641  0.1004  -0.0172 51  ASN B N   
2751 C CA  . ASN B 51  ? 0.6945 1.1790 0.5788 0.0657  0.0983  -0.0016 51  ASN B CA  
2752 C C   . ASN B 51  ? 0.6036 1.0855 0.4978 0.0546  0.1159  0.0117  51  ASN B C   
2753 O O   . ASN B 51  ? 0.5832 1.0759 0.4700 0.0526  0.1282  0.0141  51  ASN B O   
2754 C CB  . ASN B 51  ? 0.7791 1.2713 0.6366 0.0759  0.0940  -0.0049 51  ASN B CB  
2755 C CG  . ASN B 51  ? 0.9055 1.4244 0.7650 0.0777  0.1041  -0.0174 51  ASN B CG  
2756 O OD1 . ASN B 51  ? 0.8676 1.4015 0.7476 0.0679  0.1183  -0.0201 51  ASN B OD1 
2757 N ND2 . ASN B 51  ? 0.9578 1.4836 0.7948 0.0899  0.0976  -0.0252 51  ASN B ND2 
2758 N N   . PRO B 52  ? 0.5884 1.0541 0.4975 0.0476  0.1187  0.0208  52  PRO B N   
2759 C CA  . PRO B 52  ? 0.5352 0.9945 0.4528 0.0367  0.1385  0.0319  52  PRO B CA  
2760 C C   . PRO B 52  ? 0.5239 0.9714 0.4205 0.0413  0.1422  0.0502  52  PRO B C   
2761 O O   . PRO B 52  ? 0.5401 0.9800 0.4217 0.0509  0.1277  0.0578  52  PRO B O   
2762 C CB  . PRO B 52  ? 0.5727 1.0157 0.5100 0.0305  0.1385  0.0352  52  PRO B CB  
2763 C CG  . PRO B 52  ? 0.5447 0.9798 0.4765 0.0404  0.1167  0.0350  52  PRO B CG  
2764 C CD  . PRO B 52  ? 0.6018 1.0525 0.5189 0.0493  0.1052  0.0214  52  PRO B CD  
2765 N N   . ASN B 53  ? 0.5096 0.9576 0.4039 0.0342  0.1620  0.0564  53  ASN B N   
2766 C CA  . ASN B 53  ? 0.5694 1.0005 0.4458 0.0379  0.1697  0.0770  53  ASN B CA  
2767 C C   . ASN B 53  ? 0.6061 1.0136 0.4950 0.0305  0.1822  0.0887  53  ASN B C   
2768 O O   . ASN B 53  ? 0.6015 1.0035 0.4991 0.0178  0.2035  0.0884  53  ASN B O   
2769 C CB  . ASN B 53  ? 0.5597 1.0002 0.4223 0.0353  0.1857  0.0786  53  ASN B CB  
2770 C CG  . ASN B 53  ? 0.5899 1.0144 0.4283 0.0431  0.1911  0.0999  53  ASN B CG  
2771 O OD1 . ASN B 53  ? 0.6377 1.0397 0.4752 0.0443  0.1964  0.1161  53  ASN B OD1 
2772 N ND2 . ASN B 53  ? 0.6048 1.0412 0.4222 0.0500  0.1900  0.1005  53  ASN B ND2 
2773 N N   . TYR B 54  ? 0.5360 0.9295 0.4250 0.0381  0.1697  0.0987  54  TYR B N   
2774 C CA  . TYR B 54  ? 0.5388 0.9097 0.4404 0.0329  0.1798  0.1084  54  TYR B CA  
2775 C C   . TYR B 54  ? 0.6151 0.9647 0.5033 0.0315  0.2027  0.1269  54  TYR B C   
2776 O O   . TYR B 54  ? 0.6494 0.9818 0.5476 0.0200  0.2222  0.1284  54  TYR B O   
2777 C CB  . TYR B 54  ? 0.5259 0.8905 0.4294 0.0430  0.1608  0.1152  54  TYR B CB  
2778 C CG  . TYR B 54  ? 0.4930 0.8683 0.4144 0.0403  0.1446  0.0975  54  TYR B CG  
2779 C CD1 . TYR B 54  ? 0.4781 0.8481 0.4222 0.0298  0.1517  0.0888  54  TYR B CD1 
2780 C CD2 . TYR B 54  ? 0.4798 0.8690 0.3933 0.0480  0.1233  0.0890  54  TYR B CD2 
2781 C CE1 . TYR B 54  ? 0.4505 0.8295 0.4090 0.0288  0.1377  0.0735  54  TYR B CE1 
2782 C CE2 . TYR B 54  ? 0.4539 0.8486 0.3809 0.0463  0.1103  0.0735  54  TYR B CE2 
2783 C CZ  . TYR B 54  ? 0.4392 0.8293 0.3885 0.0376  0.1175  0.0664  54  TYR B CZ  
2784 O OH  . TYR B 54  ? 0.4158 0.8108 0.3767 0.0372  0.1054  0.0519  54  TYR B OH  
2785 N N   . GLU B 55  ? 0.6263 0.9746 0.4897 0.0431  0.2017  0.1411  55  GLU B N   
2786 C CA  . GLU B 55  ? 0.6833 1.0090 0.5296 0.0440  0.2244  0.1598  55  GLU B CA  
2787 C C   . GLU B 55  ? 0.6588 0.9815 0.5111 0.0260  0.2492  0.1510  55  GLU B C   
2788 O O   . GLU B 55  ? 0.6660 0.9638 0.5227 0.0160  0.2705  0.1566  55  GLU B O   
2789 C CB  . GLU B 55  ? 0.6785 1.0097 0.4959 0.0592  0.2190  0.1732  55  GLU B CB  
2790 C CG  . GLU B 55  ? 0.8158 1.1561 0.6267 0.0752  0.1940  0.1798  55  GLU B CG  
2791 C CD  . GLU B 55  ? 0.8770 1.2407 0.7016 0.0732  0.1699  0.1594  55  GLU B CD  
2792 O OE1 . GLU B 55  ? 0.8190 1.1916 0.6597 0.0614  0.1721  0.1409  55  GLU B OE1 
2793 O OE2 . GLU B 55  ? 0.9162 1.2891 0.7350 0.0834  0.1494  0.1619  55  GLU B OE2 
2794 N N   . ASP B 56  ? 0.6461 0.9952 0.4989 0.0212  0.2469  0.1358  56  ASP B N   
2795 C CA  . ASP B 56  ? 0.6844 1.0397 0.5460 0.0027  0.2689  0.1239  56  ASP B CA  
2796 C C   . ASP B 56  ? 0.6712 1.0234 0.5604 -0.0133 0.2757  0.1111  56  ASP B C   
2797 O O   . ASP B 56  ? 0.6882 1.0289 0.5826 -0.0305 0.3004  0.1089  56  ASP B O   
2798 C CB  . ASP B 56  ? 0.6496 1.0407 0.5112 0.0025  0.2608  0.1069  56  ASP B CB  
2799 C CG  . ASP B 56  ? 0.6575 1.0515 0.4909 0.0137  0.2613  0.1178  56  ASP B CG  
2800 O OD1 . ASP B 56  ? 0.6852 1.0554 0.4978 0.0229  0.2670  0.1391  56  ASP B OD1 
2801 O OD2 . ASP B 56  ? 0.7105 1.1323 0.5418 0.0145  0.2561  0.1047  56  ASP B OD2 
2802 N N   . LEU B 57  ? 0.5957 0.9584 0.5018 -0.0091 0.2546  0.1012  57  LEU B N   
2803 C CA  . LEU B 57  ? 0.6155 0.9806 0.5479 -0.0236 0.2591  0.0865  57  LEU B CA  
2804 C C   . LEU B 57  ? 0.6813 1.0093 0.6156 -0.0294 0.2749  0.0999  57  LEU B C   
2805 O O   . LEU B 57  ? 0.6847 1.0062 0.6334 -0.0474 0.2925  0.0911  57  LEU B O   
2806 C CB  . LEU B 57  ? 0.6418 1.0264 0.5888 -0.0159 0.2327  0.0731  57  LEU B CB  
2807 C CG  . LEU B 57  ? 0.6688 1.0912 0.6257 -0.0179 0.2239  0.0504  57  LEU B CG  
2808 C CD1 . LEU B 57  ? 0.6023 1.0346 0.5697 -0.0088 0.1998  0.0399  57  LEU B CD1 
2809 C CD2 . LEU B 57  ? 0.6211 1.0595 0.5955 -0.0377 0.2436  0.0349  57  LEU B CD2 
2810 N N   . LEU B 58  ? 0.6999 1.0048 0.6197 -0.0138 0.2685  0.1203  58  LEU B N   
2811 C CA  . LEU B 58  ? 0.7082 0.9751 0.6246 -0.0150 0.2844  0.1361  58  LEU B CA  
2812 C C   . LEU B 58  ? 0.6900 0.9307 0.5872 -0.0229 0.3149  0.1480  58  LEU B C   
2813 O O   . LEU B 58  ? 0.7014 0.9089 0.5976 -0.0315 0.3362  0.1549  58  LEU B O   
2814 C CB  . LEU B 58  ? 0.6303 0.8864 0.5359 0.0065  0.2674  0.1544  58  LEU B CB  
2815 C CG  . LEU B 58  ? 0.6755 0.8942 0.5758 0.0115  0.2802  0.1728  58  LEU B CG  
2816 C CD1 . LEU B 58  ? 0.6791 0.8907 0.6046 -0.0031 0.2844  0.1593  58  LEU B CD1 
2817 C CD2 . LEU B 58  ? 0.6495 0.8696 0.5406 0.0344  0.2598  0.1890  58  LEU B CD2 
2818 N N   . ILE B 59  ? 0.6927 0.9447 0.5723 -0.0196 0.3186  0.1512  59  ILE B N   
2819 C CA  . ILE B 59  ? 0.7388 0.9647 0.5993 -0.0286 0.3495  0.1617  59  ILE B CA  
2820 C C   . ILE B 59  ? 0.7759 1.0015 0.6538 -0.0565 0.3718  0.1437  59  ILE B C   
2821 O O   . ILE B 59  ? 0.8190 1.0099 0.6880 -0.0692 0.3922  0.1480  59  ILE B O   
2822 C CB  . ILE B 59  ? 0.7545 0.9946 0.5925 -0.0198 0.3488  0.1679  59  ILE B CB  
2823 C CG1 . ILE B 59  ? 0.7753 0.9970 0.5870 0.0054  0.3408  0.1936  59  ILE B CG1 
2824 C CG2 . ILE B 59  ? 0.7926 1.0187 0.6205 -0.0388 0.3779  0.1650  59  ILE B CG2 
2825 C CD1 . ILE B 59  ? 0.7786 1.0226 0.5705 0.0196  0.3283  0.1982  59  ILE B CD1 
2826 N N   . ARG B 60  ? 0.7341 0.9978 0.6383 -0.0672 0.3593  0.1190  60  ARG B N   
2827 C CA  . ARG B 60  ? 0.7022 0.9762 0.6269 -0.0937 0.3761  0.0984  60  ARG B CA  
2828 C C   . ARG B 60  ? 0.7893 1.0396 0.7300 -0.1024 0.3777  0.0954  60  ARG B C   
2829 O O   . ARG B 60  ? 0.7880 1.0400 0.7456 -0.1208 0.3838  0.0810  60  ARG B O   
2830 C CB  . ARG B 60  ? 0.7603 1.0871 0.7062 -0.0971 0.3589  0.0737  60  ARG B CB  
2831 C CG  . ARG B 60  ? 0.9049 1.2532 0.8425 -0.0961 0.3606  0.0685  60  ARG B CG  
2832 C CD  . ARG B 60  ? 0.9292 1.3175 0.8669 -0.0796 0.3333  0.0603  60  ARG B CD  
2833 N NE  . ARG B 60  ? 1.0178 1.4239 0.9458 -0.0773 0.3340  0.0553  60  ARG B NE  
2834 C CZ  . ARG B 60  ? 1.0018 1.4024 0.9030 -0.0654 0.3352  0.0708  60  ARG B CZ  
2835 N NH1 . ARG B 60  ? 0.9266 1.3039 0.8075 -0.0516 0.3340  0.0943  60  ARG B NH1 
2836 N NH2 . ARG B 60  ? 0.9475 1.3655 0.8423 -0.0648 0.3361  0.0634  60  ARG B NH2 
2837 N N   . LYS B 61  ? 0.7777 1.0065 0.7148 -0.0866 0.3694  0.1094  61  LYS B N   
2838 C CA  . LYS B 61  ? 0.7402 0.9437 0.6895 -0.0930 0.3730  0.1084  61  LYS B CA  
2839 C C   . LYS B 61  ? 0.8196 0.9696 0.7464 -0.0904 0.3887  0.1285  61  LYS B C   
2840 O O   . LYS B 61  ? 0.8183 0.9505 0.7189 -0.0765 0.3933  0.1479  61  LYS B O   
2841 C CB  . LYS B 61  ? 0.7015 0.9160 0.6633 -0.0756 0.3449  0.1092  61  LYS B CB  
2842 C CG  . LYS B 61  ? 0.6527 0.9025 0.6445 -0.0854 0.3296  0.0835  61  LYS B CG  
2843 C CD  . LYS B 61  ? 0.6728 0.9669 0.6723 -0.0930 0.3251  0.0642  61  LYS B CD  
2844 C CE  . LYS B 61  ? 0.5990 0.9289 0.6240 -0.0956 0.3066  0.0416  61  LYS B CE  
2845 N NZ  . LYS B 61  ? 0.7155 1.0366 0.7594 -0.1137 0.3182  0.0296  61  LYS B NZ  
2846 N N   . SER B 62  ? 0.7918 0.9163 0.7280 -0.1040 0.3972  0.1224  62  SER B N   
2847 C CA  . SER B 62  ? 0.8339 0.9036 0.7503 -0.1017 0.4130  0.1386  62  SER B CA  
2848 C C   . SER B 62  ? 0.8398 0.8918 0.7682 -0.0977 0.4080  0.1392  62  SER B C   
2849 O O   . SER B 62  ? 0.8256 0.9081 0.7786 -0.1004 0.3937  0.1252  62  SER B O   
2850 C CB  . SER B 62  ? 0.8427 0.8922 0.7545 -0.1241 0.4328  0.1297  62  SER B CB  
2851 O OG  . SER B 62  ? 0.8605 0.9226 0.7591 -0.1266 0.4392  0.1316  62  SER B OG  
2852 N N   . ASN B 63  ? 0.8504 0.8521 0.7603 -0.0900 0.4202  0.1556  63  ASN B N   
2853 C CA  . ASN B 63  ? 0.8729 0.8561 0.7912 -0.0820 0.4155  0.1595  63  ASN B CA  
2854 C C   . ASN B 63  ? 0.8448 0.8427 0.7912 -0.1038 0.4127  0.1343  63  ASN B C   
2855 O O   . ASN B 63  ? 0.8521 0.8669 0.8173 -0.0988 0.3987  0.1295  63  ASN B O   
2856 C CB  . ASN B 63  ? 0.9217 0.8470 0.8150 -0.0714 0.4317  0.1784  63  ASN B CB  
2857 C CG  . ASN B 63  ? 0.9344 0.8493 0.8029 -0.0417 0.4280  0.2058  63  ASN B CG  
2858 O OD1 . ASN B 63  ? 0.8822 0.8276 0.7567 -0.0242 0.4096  0.2135  63  ASN B OD1 
2859 N ND2 . ASN B 63  ? 0.9467 0.8189 0.7870 -0.0345 0.4451  0.2205  63  ASN B ND2 
2860 N N   . HIS B 64  ? 0.8866 0.8808 0.8366 -0.1275 0.4250  0.1178  64  HIS B N   
2861 C CA  . HIS B 64  ? 0.9289 0.9333 0.9028 -0.1465 0.4225  0.0948  64  HIS B CA  
2862 C C   . HIS B 64  ? 0.8596 0.9235 0.8615 -0.1511 0.4026  0.0754  64  HIS B C   
2863 O O   . HIS B 64  ? 0.8552 0.9325 0.8779 -0.1620 0.3960  0.0573  64  HIS B O   
2864 C CB  . HIS B 64  ? 0.9438 0.9241 0.9119 -0.1693 0.4420  0.0829  64  HIS B CB  
2865 C CG  . HIS B 64  ? 0.9221 0.9253 0.8873 -0.1805 0.4473  0.0763  64  HIS B CG  
2866 N ND1 . HIS B 64  ? 0.9452 1.0036 0.9330 -0.1893 0.4342  0.0574  64  HIS B ND1 
2867 C CD2 . HIS B 64  ? 1.0001 0.9780 0.9422 -0.1835 0.4648  0.0858  64  HIS B CD2 
2868 C CE1 . HIS B 64  ? 0.8333 0.9009 0.8129 -0.1973 0.4433  0.0558  64  HIS B CE1 
2869 N NE2 . HIS B 64  ? 1.0100 1.0293 0.9621 -0.1949 0.4620  0.0727  64  HIS B NE2 
2870 N N   . ASN B 65  ? 0.8348 0.9336 0.8362 -0.1416 0.3926  0.0784  65  ASN B N   
2871 C CA  . ASN B 65  ? 0.7678 0.9197 0.7932 -0.1413 0.3729  0.0612  65  ASN B CA  
2872 C C   . ASN B 65  ? 0.7379 0.8955 0.7740 -0.1268 0.3580  0.0649  65  ASN B C   
2873 O O   . ASN B 65  ? 0.6691 0.8671 0.7206 -0.1217 0.3411  0.0539  65  ASN B O   
2874 C CB  . ASN B 65  ? 0.7695 0.9543 0.7889 -0.1344 0.3677  0.0627  65  ASN B CB  
2875 C CG  . ASN B 65  ? 0.8277 1.0070 0.8353 -0.1468 0.3830  0.0616  65  ASN B CG  
2876 O OD1 . ASN B 65  ? 0.7991 0.9699 0.7853 -0.1382 0.3897  0.0769  65  ASN B OD1 
2877 N ND2 . ASN B 65  ? 0.8523 1.0353 0.8728 -0.1669 0.3891  0.0434  65  ASN B ND2 
2878 N N   . PHE B 66  ? 0.7505 0.8689 0.7781 -0.1178 0.3631  0.0806  66  PHE B N   
2879 C CA  . PHE B 66  ? 0.7559 0.8785 0.7940 -0.1023 0.3496  0.0865  66  PHE B CA  
2880 C C   . PHE B 66  ? 0.7016 0.7982 0.7485 -0.1104 0.3536  0.0807  66  PHE B C   
2881 O O   . PHE B 66  ? 0.7978 0.8506 0.8289 -0.1129 0.3695  0.0904  66  PHE B O   
2882 C CB  . PHE B 66  ? 0.7531 0.8574 0.7711 -0.0763 0.3444  0.1144  66  PHE B CB  
2883 C CG  . PHE B 66  ? 0.6879 0.8205 0.6965 -0.0643 0.3292  0.1187  66  PHE B CG  
2884 C CD1 . PHE B 66  ? 0.6974 0.8711 0.7200 -0.0574 0.3008  0.1068  66  PHE B CD1 
2885 C CD2 . PHE B 66  ? 0.7003 0.8161 0.6840 -0.0598 0.3441  0.1345  66  PHE B CD2 
2886 C CE1 . PHE B 66  ? 0.6780 0.8755 0.6901 -0.0469 0.2877  0.1098  66  PHE B CE1 
2887 C CE2 . PHE B 66  ? 0.7320 0.8740 0.7061 -0.0491 0.3303  0.1378  66  PHE B CE2 
2888 C CZ  . PHE B 66  ? 0.6696 0.8526 0.6581 -0.0429 0.3019  0.1250  66  PHE B CZ  
2889 N N   . LEU B 67  ? 0.6594 0.7810 0.7298 -0.1139 0.3397  0.0644  67  LEU B N   
2890 C CA  . LEU B 67  ? 0.7440 0.8427 0.8228 -0.1186 0.3413  0.0598  67  LEU B CA  
2891 C C   . LEU B 67  ? 0.7486 0.8491 0.8351 -0.0992 0.3291  0.0717  67  LEU B C   
2892 O O   . LEU B 67  ? 0.6848 0.8215 0.7864 -0.0928 0.3047  0.0613  67  LEU B O   
2893 C CB  . LEU B 67  ? 0.7937 0.9171 0.8925 -0.1371 0.3349  0.0322  67  LEU B CB  
2894 C CG  . LEU B 67  ? 0.9307 1.0275 1.0355 -0.1375 0.3361  0.0313  67  LEU B CG  
2895 C CD1 . LEU B 67  ? 1.0143 1.0579 1.0990 -0.1438 0.3582  0.0408  67  LEU B CD1 
2896 C CD2 . LEU B 67  ? 0.9600 1.0829 1.0866 -0.1480 0.3237  0.0069  67  LEU B CD2 
2897 N N   . VAL B 68  ? 0.7618 0.8228 0.8351 -0.0869 0.3374  0.0922  68  VAL B N   
2898 C CA  . VAL B 68  ? 0.7717 0.8322 0.8500 -0.0664 0.3187  0.1036  68  VAL B CA  
2899 C C   . VAL B 68  ? 0.8567 0.8949 0.9457 -0.0743 0.3277  0.0970  68  VAL B C   
2900 O O   . VAL B 68  ? 0.9122 0.9111 0.9882 -0.0821 0.3462  0.0991  68  VAL B O   
2901 C CB  . VAL B 68  ? 0.7801 0.8180 0.8359 -0.0435 0.3201  0.1322  68  VAL B CB  
2902 C CG1 . VAL B 68  ? 0.7428 0.7740 0.8035 -0.0249 0.3068  0.1439  68  VAL B CG1 
2903 C CG2 . VAL B 68  ? 0.7016 0.7666 0.7483 -0.0338 0.3064  0.1375  68  VAL B CG2 
2904 N N   . GLN B 69  ? 0.7735 0.8344 0.8818 -0.0699 0.3064  0.0872  69  GLN B N   
2905 C CA  . GLN B 69  ? 0.8612 0.9067 0.9815 -0.0774 0.3120  0.0786  69  GLN B CA  
2906 C C   . GLN B 69  ? 0.8448 0.8906 0.9704 -0.0567 0.2932  0.0902  69  GLN B C   
2907 O O   . GLN B 69  ? 0.7142 0.7927 0.8490 -0.0470 0.2679  0.0869  69  GLN B O   
2908 C CB  . GLN B 69  ? 0.8843 0.9627 1.0254 -0.0954 0.3046  0.0501  69  GLN B CB  
2909 C CG  . GLN B 69  ? 1.0072 1.0790 1.1425 -0.1169 0.3158  0.0335  69  GLN B CG  
2910 C CD  . GLN B 69  ? 1.0702 1.1653 1.2231 -0.1306 0.3061  0.0075  69  GLN B CD  
2911 O OE1 . GLN B 69  ? 1.0858 1.2193 1.2480 -0.1378 0.2959  -0.0095 69  GLN B OE1 
2912 N NE2 . GLN B 69  ? 1.0539 1.1260 1.2101 -0.1319 0.3088  0.0051  69  GLN B NE2 
2913 N N   . ALA B 70  ? 0.9100 0.9192 1.0296 -0.0508 0.3064  0.1025  70  ALA B N   
2914 C CA  . ALA B 70  ? 0.9201 0.9288 1.0465 -0.0332 0.2917  0.1121  70  ALA B CA  
2915 C C   . ALA B 70  ? 0.9620 0.9611 1.1029 -0.0458 0.2974  0.0964  70  ALA B C   
2916 O O   . ALA B 70  ? 1.0320 0.9926 1.1651 -0.0493 0.3190  0.1014  70  ALA B O   
2917 C CB  . ALA B 70  ? 0.8785 0.8556 0.9858 -0.0130 0.3019  0.1396  70  ALA B CB  
2918 N N   . GLY B 71  ? 0.9319 0.9647 1.0921 -0.0517 0.2786  0.0775  71  GLY B N   
2919 C CA  . GLY B 71  ? 0.9540 0.9836 1.1274 -0.0676 0.2853  0.0582  71  GLY B CA  
2920 C C   . GLY B 71  ? 1.0269 1.0457 1.1929 -0.0896 0.3022  0.0432  71  GLY B C   
2921 O O   . GLY B 71  ? 1.0385 1.0855 1.2072 -0.0994 0.2972  0.0306  71  GLY B O   
2922 N N   . ASN B 72  ? 1.0814 1.0599 1.2355 -0.0961 0.3185  0.0432  72  ASN B N   
2923 C CA  . ASN B 72  ? 1.1446 1.1091 1.2878 -0.1160 0.3322  0.0294  72  ASN B CA  
2924 C C   . ASN B 72  ? 1.1949 1.1214 1.3134 -0.1125 0.3513  0.0468  72  ASN B C   
2925 O O   . ASN B 72  ? 1.2157 1.1347 1.3246 -0.1283 0.3624  0.0372  72  ASN B O   
2926 C CB  . ASN B 72  ? 1.2049 1.1500 1.3502 -0.1286 0.3387  0.0130  72  ASN B CB  
2927 C CG  . ASN B 72  ? 1.2670 1.2430 1.4336 -0.1276 0.3205  -0.0005 72  ASN B CG  
2928 O OD1 . ASN B 72  ? 1.2369 1.2559 1.4176 -0.1255 0.3028  -0.0078 72  ASN B OD1 
2929 N ND2 . ASN B 72  ? 1.3291 1.2817 1.4966 -0.1277 0.3251  -0.0039 72  ASN B ND2 
2930 N N   . VAL B 73  ? 1.1810 1.0853 1.2887 -0.0910 0.3549  0.0724  73  VAL B N   
2931 C CA  . VAL B 73  ? 1.2035 1.0718 1.2851 -0.0837 0.3720  0.0904  73  VAL B CA  
2932 C C   . VAL B 73  ? 1.1682 1.0613 1.2460 -0.0891 0.3697  0.0899  73  VAL B C   
2933 O O   . VAL B 73  ? 1.1158 1.0483 1.2057 -0.0819 0.3538  0.0924  73  VAL B O   
2934 C CB  . VAL B 73  ? 1.1975 1.0468 1.2691 -0.0554 0.3724  0.1188  73  VAL B CB  
2935 C CG1 . VAL B 73  ? 1.2991 1.1015 1.3403 -0.0463 0.3927  0.1358  73  VAL B CG1 
2936 C CG2 . VAL B 73  ? 1.1842 1.0252 1.2672 -0.0484 0.3684  0.1182  73  VAL B CG2 
2937 N N   . GLN B 74  ? 1.1885 1.0589 1.2496 -0.1021 0.3860  0.0855  74  GLN B N   
2938 C CA  . GLN B 74  ? 1.2110 1.1006 1.2658 -0.1073 0.3866  0.0860  74  GLN B CA  
2939 C C   . GLN B 74  ? 1.2100 1.0673 1.2382 -0.0881 0.3980  0.1131  74  GLN B C   
2940 O O   . GLN B 74  ? 1.1555 0.9674 1.1620 -0.0893 0.4175  0.1187  74  GLN B O   
2941 C CB  . GLN B 74  ? 1.2736 1.1640 1.3279 -0.1338 0.3964  0.0637  74  GLN B CB  
2942 C CG  . GLN B 74  ? 1.3016 1.2221 1.3793 -0.1506 0.3856  0.0371  74  GLN B CG  
2943 C CD  . GLN B 74  ? 1.2536 1.2324 1.3503 -0.1544 0.3668  0.0248  74  GLN B CD  
2944 O OE1 . GLN B 74  ? 1.2344 1.2289 1.3256 -0.1579 0.3685  0.0256  74  GLN B OE1 
2945 N NE2 . GLN B 74  ? 1.1767 1.1870 1.2944 -0.1524 0.3491  0.0133  74  GLN B NE2 
2946 N N   . LEU B 75  ? 1.1230 1.0039 1.1518 -0.0690 0.3858  0.1298  75  LEU B N   
2947 C CA  . LEU B 75  ? 1.0974 0.9559 1.1004 -0.0495 0.3940  0.1550  75  LEU B CA  
2948 C C   . LEU B 75  ? 1.1097 0.9723 1.1008 -0.0619 0.4021  0.1504  75  LEU B C   
2949 O O   . LEU B 75  ? 1.0836 0.9869 1.0898 -0.0753 0.3923  0.1351  75  LEU B O   
2950 C CB  . LEU B 75  ? 1.0151 0.9030 1.0232 -0.0250 0.3765  0.1736  75  LEU B CB  
2951 C CG  . LEU B 75  ? 0.9155 0.8054 0.9361 -0.0099 0.3667  0.1812  75  LEU B CG  
2952 C CD1 . LEU B 75  ? 0.8839 0.8195 0.9347 -0.0186 0.3470  0.1640  75  LEU B CD1 
2953 C CD2 . LEU B 75  ? 0.9205 0.8127 0.9276 0.0202  0.3608  0.2095  75  LEU B CD2 
2954 N N   . ARG B 76  ? 1.0884 0.9091 1.0519 -0.0570 0.4204  0.1630  76  ARG B N   
2955 C CA  . ARG B 76  ? 1.0825 0.9063 1.0329 -0.0664 0.4285  0.1616  76  ARG B CA  
2956 C C   . ARG B 76  ? 1.0470 0.8850 0.9839 -0.0428 0.4208  0.1841  76  ARG B C   
2957 O O   . ARG B 76  ? 1.0553 0.8801 0.9809 -0.0168 0.4178  0.2059  76  ARG B O   
2958 C CB  . ARG B 76  ? 1.1502 0.9248 1.0785 -0.0778 0.4533  0.1593  76  ARG B CB  
2959 C CG  . ARG B 76  ? 1.1806 0.9791 1.1176 -0.1063 0.4564  0.1371  76  ARG B CG  
2960 C CD  . ARG B 76  ? 1.2267 0.9998 1.1624 -0.1319 0.4736  0.1172  76  ARG B CD  
2961 N NE  . ARG B 76  ? 1.3673 1.0777 1.2755 -0.1269 0.4965  0.1273  76  ARG B NE  
2962 C CZ  . ARG B 76  ? 1.3706 1.0509 1.2760 -0.1455 0.5120  0.1111  76  ARG B CZ  
2963 N NH1 . ARG B 76  ? 1.3337 1.0422 1.2628 -0.1689 0.5054  0.0851  76  ARG B NH1 
2964 N NH2 . ARG B 76  ? 1.2701 0.8912 1.1472 -0.1396 0.5349  0.1207  76  ARG B NH2 
2965 N N   . VAL B 77  ? 0.9875 0.8555 0.9256 -0.0514 0.4169  0.1781  77  VAL B N   
2966 C CA  . VAL B 77  ? 0.9377 0.8269 0.8645 -0.0318 0.4076  0.1957  77  VAL B CA  
2967 C C   . VAL B 77  ? 0.9599 0.8162 0.8559 -0.0272 0.4247  0.2088  77  VAL B C   
2968 O O   . VAL B 77  ? 1.0209 0.8663 0.9130 -0.0487 0.4385  0.1956  77  VAL B O   
2969 C CB  . VAL B 77  ? 0.9093 0.8528 0.8559 -0.0427 0.3926  0.1802  77  VAL B CB  
2970 C CG1 . VAL B 77  ? 0.8746 0.8413 0.8088 -0.0217 0.3819  0.1977  77  VAL B CG1 
2971 C CG2 . VAL B 77  ? 0.7908 0.7638 0.7675 -0.0467 0.3767  0.1662  77  VAL B CG2 
2972 N N   . ILE B 78  ? 0.9440 0.7851 0.8180 0.0011  0.4240  0.2343  78  ILE B N   
2973 C CA  . ILE B 78  ? 1.0234 0.8282 0.8659 0.0089  0.4412  0.2481  78  ILE B CA  
2974 C C   . ILE B 78  ? 0.9794 0.8091 0.8075 0.0272  0.4313  0.2636  78  ILE B C   
2975 O O   . ILE B 78  ? 1.0177 0.8208 0.8182 0.0403  0.4425  0.2789  78  ILE B O   
2976 C CB  . ILE B 78  ? 1.0429 0.7979 0.8663 0.0283  0.4538  0.2643  78  ILE B CB  
2977 C CG1 . ILE B 78  ? 1.0872 0.8602 0.9139 0.0587  0.4361  0.2826  78  ILE B CG1 
2978 C CG2 . ILE B 78  ? 1.0786 0.8076 0.9137 0.0100  0.4643  0.2482  78  ILE B CG2 
2979 C CD1 . ILE B 78  ? 1.1481 0.8787 0.9609 0.0793  0.4465  0.2966  78  ILE B CD1 
2980 N N   . GLY B 79  ? 0.9809 0.8613 0.8265 0.0295  0.4103  0.2597  79  GLY B N   
2981 C CA  . GLY B 79  ? 0.8952 0.8044 0.7283 0.0472  0.3979  0.2728  79  GLY B CA  
2982 C C   . GLY B 79  ? 0.8337 0.7973 0.6902 0.0479  0.3743  0.2650  79  GLY B C   
2983 O O   . GLY B 79  ? 0.8187 0.7940 0.6960 0.0481  0.3645  0.2603  79  GLY B O   
2984 N N   . HIS B 80  ? 0.8378 0.8345 0.6914 0.0468  0.3659  0.2620  80  HIS B N   
2985 C CA  . HIS B 80  ? 0.8337 0.8817 0.7098 0.0454  0.3385  0.2479  80  HIS B CA  
2986 C C   . HIS B 80  ? 0.8233 0.8976 0.6830 0.0640  0.3216  0.2587  80  HIS B C   
2987 O O   . HIS B 80  ? 0.7981 0.8597 0.6326 0.0679  0.3368  0.2702  80  HIS B O   
2988 C CB  . HIS B 80  ? 0.7477 0.8151 0.6445 0.0176  0.3405  0.2203  80  HIS B CB  
2989 C CG  . HIS B 80  ? 0.7649 0.8290 0.6456 0.0066  0.3590  0.2188  80  HIS B CG  
2990 N ND1 . HIS B 80  ? 0.8463 0.8706 0.7141 -0.0072 0.3837  0.2186  80  HIS B ND1 
2991 C CD2 . HIS B 80  ? 0.7531 0.8488 0.6306 0.0056  0.3490  0.2119  80  HIS B CD2 
2992 C CE1 . HIS B 80  ? 0.8300 0.8628 0.6872 -0.0159 0.3906  0.2140  80  HIS B CE1 
2993 N NE2 . HIS B 80  ? 0.7912 0.8671 0.6529 -0.0074 0.3736  0.2120  80  HIS B NE2 
2994 N N   . SER B 81  ? 0.7311 0.8411 0.6036 0.0749  0.2910  0.2547  81  SER B N   
2995 C CA  . SER B 81  ? 0.7523 0.8891 0.6094 0.0920  0.2735  0.2637  81  SER B CA  
2996 C C   . SER B 81  ? 0.6807 0.8597 0.5589 0.0886  0.2426  0.2451  81  SER B C   
2997 O O   . SER B 81  ? 0.6426 0.8273 0.5446 0.0808  0.2330  0.2323  81  SER B O   
2998 C CB  . SER B 81  ? 0.8045 0.9302 0.6416 0.1188  0.2733  0.2902  81  SER B CB  
2999 O OG  . SER B 81  ? 0.8351 0.9942 0.6615 0.1351  0.2517  0.2963  81  SER B OG  
3000 N N   . MET B 82  ? 0.6679 0.8741 0.5353 0.0945  0.2281  0.2436  82  MET B N   
3001 C CA  . MET B 82  ? 0.6271 0.8693 0.5089 0.0913  0.2007  0.2259  82  MET B CA  
3002 C C   . MET B 82  ? 0.6290 0.8924 0.4989 0.1108  0.1804  0.2378  82  MET B C   
3003 O O   . MET B 82  ? 0.6526 0.9208 0.4988 0.1222  0.1821  0.2501  82  MET B O   
3004 C CB  . MET B 82  ? 0.6340 0.8919 0.5123 0.0802  0.2006  0.2109  82  MET B CB  
3005 C CG  . MET B 82  ? 0.6460 0.9371 0.5287 0.0824  0.1734  0.1975  82  MET B CG  
3006 S SD  . MET B 82  ? 0.5780 0.8850 0.4742 0.0643  0.1717  0.1702  82  MET B SD  
3007 C CE  . MET B 82  ? 0.5990 0.9046 0.4708 0.0648  0.1886  0.1772  82  MET B CE  
3008 N N   . GLN B 83  ? 0.6013 0.8790 0.4869 0.1139  0.1617  0.2335  83  GLN B N   
3009 C CA  . GLN B 83  ? 0.6485 0.9529 0.5262 0.1290  0.1405  0.2409  83  GLN B CA  
3010 C C   . GLN B 83  ? 0.5629 0.8941 0.4524 0.1192  0.1174  0.2193  83  GLN B C   
3011 O O   . GLN B 83  ? 0.5358 0.8677 0.4463 0.1105  0.1098  0.2070  83  GLN B O   
3012 C CB  . GLN B 83  ? 0.7039 1.0047 0.5883 0.1416  0.1382  0.2547  83  GLN B CB  
3013 C CG  . GLN B 83  ? 0.6841 1.0187 0.5611 0.1570  0.1165  0.2621  83  GLN B CG  
3014 C CD  . GLN B 83  ? 0.7084 1.0441 0.5911 0.1721  0.1153  0.2775  83  GLN B CD  
3015 O OE1 . GLN B 83  ? 0.6717 0.9823 0.5671 0.1698  0.1278  0.2801  83  GLN B OE1 
3016 N NE2 . GLN B 83  ? 0.7044 1.0705 0.5761 0.1888  0.1010  0.2882  83  GLN B NE2 
3017 N N   . ASN B 84  ? 0.5662 0.9170 0.4400 0.1208  0.1072  0.2146  84  ASN B N   
3018 C CA  . ASN B 84  ? 0.5386 0.9098 0.4190 0.1117  0.0873  0.1937  84  ASN B CA  
3019 C C   . ASN B 84  ? 0.5166 0.8751 0.4165 0.0960  0.0937  0.1761  84  ASN B C   
3020 O O   . ASN B 84  ? 0.5266 0.8708 0.4259 0.0897  0.1119  0.1752  84  ASN B O   
3021 C CB  . ASN B 84  ? 0.5260 0.9169 0.4117 0.1173  0.0670  0.1944  84  ASN B CB  
3022 C CG  . ASN B 84  ? 0.5503 0.9587 0.4164 0.1339  0.0618  0.2121  84  ASN B CG  
3023 O OD1 . ASN B 84  ? 0.5680 0.9850 0.4134 0.1385  0.0617  0.2149  84  ASN B OD1 
3024 N ND2 . ASN B 84  ? 0.5520 0.9674 0.4245 0.1440  0.0578  0.2244  84  ASN B ND2 
3025 N N   . CYS B 85  ? 0.4887 0.8530 0.4053 0.0891  0.0803  0.1617  85  CYS B N   
3026 C CA  . CYS B 85  ? 0.4686 0.8247 0.4019 0.0763  0.0849  0.1444  85  CYS B CA  
3027 C C   . CYS B 85  ? 0.4635 0.8005 0.4160 0.0720  0.0976  0.1482  85  CYS B C   
3028 O O   . CYS B 85  ? 0.4441 0.7771 0.4131 0.0619  0.0989  0.1336  85  CYS B O   
3029 C CB  . CYS B 85  ? 0.4449 0.8138 0.3827 0.0718  0.0655  0.1261  85  CYS B CB  
3030 S SG  . CYS B 85  ? 0.4556 0.8423 0.3676 0.0752  0.0536  0.1192  85  CYS B SG  
3031 N N   . VAL B 86  ? 0.4835 0.8077 0.4322 0.0801  0.1083  0.1674  86  VAL B N   
3032 C CA  . VAL B 86  ? 0.4823 0.7858 0.4467 0.0775  0.1203  0.1721  86  VAL B CA  
3033 C C   . VAL B 86  ? 0.5118 0.7909 0.4678 0.0758  0.1463  0.1828  86  VAL B C   
3034 O O   . VAL B 86  ? 0.5399 0.8157 0.4753 0.0850  0.1539  0.1975  86  VAL B O   
3035 C CB  . VAL B 86  ? 0.5312 0.8377 0.4988 0.0895  0.1112  0.1855  86  VAL B CB  
3036 C CG1 . VAL B 86  ? 0.5702 0.8498 0.5434 0.0924  0.1298  0.1983  86  VAL B CG1 
3037 C CG2 . VAL B 86  ? 0.4495 0.7706 0.4338 0.0841  0.0915  0.1705  86  VAL B CG2 
3038 N N   . LEU B 87  ? 0.5075 0.7691 0.4782 0.0633  0.1606  0.1747  87  LEU B N   
3039 C CA  . LEU B 87  ? 0.5622 0.7957 0.5255 0.0587  0.1878  0.1837  87  LEU B CA  
3040 C C   . LEU B 87  ? 0.5527 0.7609 0.5186 0.0659  0.1975  0.1985  87  LEU B C   
3041 O O   . LEU B 87  ? 0.5303 0.7393 0.5146 0.0635  0.1895  0.1918  87  LEU B O   
3042 C CB  . LEU B 87  ? 0.5291 0.7607 0.5057 0.0385  0.1995  0.1642  87  LEU B CB  
3043 C CG  . LEU B 87  ? 0.6038 0.8055 0.5772 0.0271  0.2292  0.1677  87  LEU B CG  
3044 C CD1 . LEU B 87  ? 0.5976 0.7882 0.5456 0.0312  0.2453  0.1817  87  LEU B CD1 
3045 C CD2 . LEU B 87  ? 0.6053 0.8159 0.5978 0.0061  0.2351  0.1439  87  LEU B CD2 
3046 N N   . LYS B 88  ? 0.6096 0.7943 0.5551 0.0761  0.2153  0.2191  88  LYS B N   
3047 C CA  . LYS B 88  ? 0.6517 0.8066 0.5934 0.0857  0.2293  0.2360  88  LYS B CA  
3048 C C   . LYS B 88  ? 0.6612 0.7772 0.5957 0.0729  0.2609  0.2371  88  LYS B C   
3049 O O   . LYS B 88  ? 0.6857 0.7880 0.5992 0.0729  0.2773  0.2454  88  LYS B O   
3050 C CB  . LYS B 88  ? 0.6489 0.8062 0.5689 0.1110  0.2255  0.2604  88  LYS B CB  
3051 C CG  . LYS B 88  ? 0.7054 0.8971 0.6366 0.1230  0.1967  0.2603  88  LYS B CG  
3052 C CD  . LYS B 88  ? 0.6585 0.8756 0.5702 0.1414  0.1836  0.2737  88  LYS B CD  
3053 C CE  . LYS B 88  ? 0.6923 0.8853 0.5754 0.1537  0.2050  0.2941  88  LYS B CE  
3054 N NZ  . LYS B 88  ? 0.8468 1.0559 0.7115 0.1804  0.1969  0.3156  88  LYS B NZ  
3055 N N   . LEU B 89  ? 0.6821 0.7800 0.6333 0.0609  0.2698  0.2281  89  LEU B N   
3056 C CA  . LEU B 89  ? 0.7219 0.7805 0.6676 0.0463  0.3005  0.2272  89  LEU B CA  
3057 C C   . LEU B 89  ? 0.7509 0.7720 0.6837 0.0616  0.3153  0.2482  89  LEU B C   
3058 O O   . LEU B 89  ? 0.7299 0.7506 0.6777 0.0658  0.3069  0.2470  89  LEU B O   
3059 C CB  . LEU B 89  ? 0.6805 0.7451 0.6523 0.0224  0.3012  0.2018  89  LEU B CB  
3060 C CG  . LEU B 89  ? 0.6477 0.7537 0.6350 0.0109  0.2830  0.1799  89  LEU B CG  
3061 C CD1 . LEU B 89  ? 0.5768 0.6927 0.5904 -0.0058 0.2787  0.1574  89  LEU B CD1 
3062 C CD2 . LEU B 89  ? 0.6552 0.7615 0.6288 0.0003  0.2985  0.1771  89  LEU B CD2 
3063 N N   . LYS B 90  ? 0.7585 0.7463 0.6620 0.0705  0.3383  0.2676  90  LYS B N   
3064 C CA  . LYS B 90  ? 0.8350 0.7820 0.7229 0.0864  0.3539  0.2867  90  LYS B CA  
3065 C C   . LYS B 90  ? 0.8877 0.7961 0.7831 0.0644  0.3725  0.2709  90  LYS B C   
3066 O O   . LYS B 90  ? 0.9196 0.8133 0.8115 0.0427  0.3865  0.2570  90  LYS B O   
3067 C CB  . LYS B 90  ? 0.8580 0.7825 0.7132 0.1055  0.3626  0.3061  90  LYS B CB  
3068 C CG  . LYS B 90  ? 0.9618 0.8441 0.8020 0.1241  0.3745  0.3212  90  LYS B CG  
3069 C CD  . LYS B 90  ? 0.9476 0.8345 0.7644 0.1573  0.3684  0.3454  90  LYS B CD  
3070 C CE  . LYS B 90  ? 1.0206 0.8566 0.8174 0.1733  0.3877  0.3576  90  LYS B CE  
3071 N NZ  . LYS B 90  ? 1.1457 0.9865 0.9198 0.2079  0.3833  0.3802  90  LYS B NZ  
3072 N N   . VAL B 91  ? 0.8990 0.7955 0.8059 0.0686  0.3715  0.2714  91  VAL B N   
3073 C CA  . VAL B 91  ? 0.9577 0.8185 0.8709 0.0489  0.3875  0.2560  91  VAL B CA  
3074 C C   . VAL B 91  ? 1.0531 0.8634 0.9439 0.0655  0.4036  0.2712  91  VAL B C   
3075 O O   . VAL B 91  ? 1.0367 0.8415 0.9078 0.0931  0.4022  0.2935  91  VAL B O   
3076 C CB  . VAL B 91  ? 0.9645 0.8480 0.9090 0.0374  0.3759  0.2402  91  VAL B CB  
3077 C CG1 . VAL B 91  ? 0.8996 0.8267 0.8649 0.0178  0.3647  0.2202  91  VAL B CG1 
3078 C CG2 . VAL B 91  ? 0.9277 0.8300 0.8784 0.0631  0.3599  0.2574  91  VAL B CG2 
3079 N N   . ASP B 92  ? 1.1071 0.8813 0.9998 0.0494  0.4192  0.2581  92  ASP B N   
3080 C CA  . ASP B 92  ? 1.1805 0.9016 1.0495 0.0628  0.4383  0.2695  92  ASP B CA  
3081 C C   . ASP B 92  ? 1.1683 0.8818 1.0446 0.0807  0.4339  0.2774  92  ASP B C   
3082 O O   . ASP B 92  ? 1.2073 0.8872 1.0627 0.1032  0.4451  0.2932  92  ASP B O   
3083 C CB  . ASP B 92  ? 1.1639 0.8456 1.0257 0.0358  0.4606  0.2512  92  ASP B CB  
3084 C CG  . ASP B 92  ? 1.1576 0.8486 1.0461 0.0092  0.4576  0.2259  92  ASP B CG  
3085 O OD1 . ASP B 92  ? 1.1479 0.8734 1.0608 0.0113  0.4392  0.2222  92  ASP B OD1 
3086 O OD2 . ASP B 92  ? 1.1407 0.8054 1.0254 -0.0139 0.4738  0.2090  92  ASP B OD2 
3087 N N   . THR B 93  ? 1.1146 0.8598 1.0195 0.0726  0.4181  0.2669  93  THR B N   
3088 C CA  . THR B 93  ? 1.0812 0.8227 0.9959 0.0872  0.4132  0.2726  93  THR B CA  
3089 C C   . THR B 93  ? 1.0551 0.8449 0.9824 0.1081  0.3894  0.2871  93  THR B C   
3090 O O   . THR B 93  ? 0.9581 0.7906 0.9053 0.0964  0.3732  0.2780  93  THR B O   
3091 C CB  . THR B 93  ? 1.0914 0.8308 1.0290 0.0615  0.4139  0.2485  93  THR B CB  
3092 O OG1 . THR B 93  ? 1.2457 0.9411 1.1700 0.0428  0.4359  0.2351  93  THR B OG1 
3093 C CG2 . THR B 93  ? 1.0150 0.7535 0.9639 0.0768  0.4079  0.2546  93  THR B CG2 
3094 N N   . ALA B 94  ? 1.0165 0.8019 0.9326 0.1389  0.3872  0.3084  94  ALA B N   
3095 C CA  . ALA B 94  ? 0.8403 0.6733 0.7696 0.1583  0.3640  0.3211  94  ALA B CA  
3096 C C   . ALA B 94  ? 0.8941 0.7421 0.8518 0.1482  0.3548  0.3099  94  ALA B C   
3097 O O   . ALA B 94  ? 0.8900 0.7064 0.8486 0.1485  0.3658  0.3064  94  ALA B O   
3098 C CB  . ALA B 94  ? 0.8903 0.7187 0.8007 0.1942  0.3640  0.3449  94  ALA B CB  
3099 N N   . ASN B 95  ? 0.8291 0.7260 0.8111 0.1383  0.3308  0.2983  95  ASN B N   
3100 C CA  . ASN B 95  ? 0.7669 0.6839 0.7778 0.1299  0.3146  0.2826  95  ASN B CA  
3101 C C   . ASN B 95  ? 0.8242 0.7308 0.8324 0.1541  0.3169  0.2999  95  ASN B C   
3102 O O   . ASN B 95  ? 0.8462 0.7721 0.8449 0.1799  0.3079  0.3192  95  ASN B O   
3103 C CB  . ASN B 95  ? 0.6903 0.6642 0.7230 0.1252  0.2818  0.2697  95  ASN B CB  
3104 C CG  . ASN B 95  ? 0.7355 0.7300 0.7958 0.1188  0.2647  0.2552  95  ASN B CG  
3105 O OD1 . ASN B 95  ? 0.7890 0.7577 0.8565 0.1098  0.2769  0.2477  95  ASN B OD1 
3106 N ND2 . ASN B 95  ? 0.6982 0.7385 0.7729 0.1227  0.2370  0.2507  95  ASN B ND2 
3107 N N   . PRO B 96  ? 0.8721 0.7484 0.8862 0.1479  0.3303  0.2944  96  PRO B N   
3108 C CA  . PRO B 96  ? 0.8776 0.7470 0.8899 0.1724  0.3317  0.3108  96  PRO B CA  
3109 C C   . PRO B 96  ? 0.8201 0.7423 0.8596 0.1786  0.3009  0.3055  96  PRO B C   
3110 O O   . PRO B 96  ? 0.8237 0.7582 0.8613 0.2037  0.2957  0.3223  96  PRO B O   
3111 C CB  . PRO B 96  ? 0.8930 0.7148 0.9048 0.1592  0.3527  0.2991  96  PRO B CB  
3112 C CG  . PRO B 96  ? 0.9255 0.7534 0.9541 0.1254  0.3517  0.2743  96  PRO B CG  
3113 C CD  . PRO B 96  ? 0.8504 0.7032 0.8749 0.1186  0.3428  0.2719  96  PRO B CD  
3114 N N   . LYS B 97  ? 0.8106 0.7656 0.8737 0.1574  0.2807  0.2833  97  LYS B N   
3115 C CA  . LYS B 97  ? 0.7781 0.7811 0.8648 0.1604  0.2523  0.2769  97  LYS B CA  
3116 C C   . LYS B 97  ? 0.7503 0.7976 0.8344 0.1725  0.2315  0.2851  97  LYS B C   
3117 O O   . LYS B 97  ? 0.7677 0.8559 0.8704 0.1698  0.2075  0.2763  97  LYS B O   
3118 C CB  . LYS B 97  ? 0.7587 0.7745 0.8684 0.1337  0.2407  0.2496  97  LYS B CB  
3119 C CG  . LYS B 97  ? 0.8487 0.8279 0.9637 0.1194  0.2584  0.2380  97  LYS B CG  
3120 C CD  . LYS B 97  ? 0.9408 0.8860 1.0418 0.1020  0.2805  0.2309  97  LYS B CD  
3121 C CE  . LYS B 97  ? 1.1106 1.0259 1.2191 0.0831  0.2960  0.2145  97  LYS B CE  
3122 N NZ  . LYS B 97  ? 1.2154 1.1246 1.3246 0.0567  0.3045  0.1947  97  LYS B NZ  
3123 N N   . THR B 98  ? 0.7156 0.7553 0.7761 0.1843  0.2403  0.3004  98  THR B N   
3124 C CA  . THR B 98  ? 0.7003 0.7832 0.7573 0.1939  0.2204  0.3062  98  THR B CA  
3125 C C   . THR B 98  ? 0.6668 0.7877 0.7341 0.2134  0.2031  0.3159  98  THR B C   
3126 O O   . THR B 98  ? 0.6546 0.7634 0.7113 0.2366  0.2142  0.3352  98  THR B O   
3127 C CB  . THR B 98  ? 0.6812 0.7468 0.7080 0.2080  0.2352  0.3246  98  THR B CB  
3128 O OG1 . THR B 98  ? 0.7319 0.7666 0.7503 0.1875  0.2509  0.3141  98  THR B OG1 
3129 C CG2 . THR B 98  ? 0.6241 0.7364 0.6463 0.2186  0.2143  0.3304  98  THR B CG2 
3130 N N   . PRO B 99  ? 0.6131 0.7788 0.6998 0.2048  0.1774  0.3029  99  PRO B N   
3131 C CA  . PRO B 99  ? 0.5145 0.7211 0.6114 0.2211  0.1610  0.3110  99  PRO B CA  
3132 C C   . PRO B 99  ? 0.6070 0.8448 0.6877 0.2396  0.1529  0.3262  99  PRO B C   
3133 O O   . PRO B 99  ? 0.6043 0.8323 0.6673 0.2379  0.1580  0.3287  99  PRO B O   
3134 C CB  . PRO B 99  ? 0.5418 0.7786 0.6629 0.2001  0.1389  0.2884  99  PRO B CB  
3135 C CG  . PRO B 99  ? 0.5433 0.7725 0.6589 0.1802  0.1370  0.2737  99  PRO B CG  
3136 C CD  . PRO B 99  ? 0.5399 0.7219 0.6375 0.1806  0.1627  0.2807  99  PRO B CD  
3137 N N   . LYS B 100 ? 0.6058 0.8827 0.6926 0.2581  0.1408  0.3365  100 LYS B N   
3138 C CA  . LYS B 100 ? 0.6247 0.9488 0.7031 0.2723  0.1254  0.3456  100 LYS B CA  
3139 C C   . LYS B 100 ? 0.5707 0.9224 0.6574 0.2486  0.1051  0.3251  100 LYS B C   
3140 O O   . LYS B 100 ? 0.5426 0.9070 0.6501 0.2288  0.0922  0.3061  100 LYS B O   
3141 C CB  . LYS B 100 ? 0.6661 1.0317 0.7548 0.2926  0.1156  0.3564  100 LYS B CB  
3142 C CG  . LYS B 100 ? 0.7649 1.1848 0.8451 0.3033  0.0997  0.3594  100 LYS B CG  
3143 C CD  . LYS B 100 ? 0.8799 1.2942 0.9325 0.3269  0.1124  0.3757  100 LYS B CD  
3144 C CE  . LYS B 100 ? 0.9183 1.3788 0.9625 0.3250  0.0944  0.3711  100 LYS B CE  
3145 N NZ  . LYS B 100 ? 0.7673 1.2180 0.7996 0.3151  0.0916  0.3691  100 LYS B NZ  
3146 N N   . TYR B 101 ? 0.5640 0.9198 0.6320 0.2505  0.1042  0.3288  101 TYR B N   
3147 C CA  . TYR B 101 ? 0.5842 0.9562 0.6562 0.2279  0.0888  0.3090  101 TYR B CA  
3148 C C   . TYR B 101 ? 0.5867 0.9941 0.6421 0.2383  0.0776  0.3163  101 TYR B C   
3149 O O   . TYR B 101 ? 0.5323 0.9419 0.5690 0.2623  0.0858  0.3372  101 TYR B O   
3150 C CB  . TYR B 101 ? 0.4863 0.8137 0.5543 0.2086  0.1023  0.2972  101 TYR B CB  
3151 C CG  . TYR B 101 ? 0.5219 0.8226 0.5642 0.2171  0.1194  0.3099  101 TYR B CG  
3152 C CD1 . TYR B 101 ? 0.5585 0.8190 0.5868 0.2316  0.1440  0.3272  101 TYR B CD1 
3153 C CD2 . TYR B 101 ? 0.5220 0.8350 0.5522 0.2106  0.1125  0.3047  101 TYR B CD2 
3154 C CE1 . TYR B 101 ? 0.6036 0.8359 0.6059 0.2385  0.1618  0.3391  101 TYR B CE1 
3155 C CE2 . TYR B 101 ? 0.5557 0.8442 0.5618 0.2178  0.1290  0.3164  101 TYR B CE2 
3156 C CZ  . TYR B 101 ? 0.5926 0.8403 0.5847 0.2312  0.1539  0.3336  101 TYR B CZ  
3157 O OH  . TYR B 101 ? 0.7198 0.9401 0.6858 0.2375  0.1720  0.3453  101 TYR B OH  
3158 N N   . LYS B 102 ? 0.5085 0.9422 0.5694 0.2200  0.0591  0.2983  102 LYS B N   
3159 C CA  . LYS B 102 ? 0.5107 0.9738 0.5556 0.2233  0.0480  0.2996  102 LYS B CA  
3160 C C   . LYS B 102 ? 0.4653 0.9144 0.5092 0.1991  0.0439  0.2794  102 LYS B C   
3161 O O   . LYS B 102 ? 0.4431 0.8716 0.5015 0.1811  0.0451  0.2638  102 LYS B O   
3162 C CB  . LYS B 102 ? 0.5763 1.0988 0.6287 0.2262  0.0254  0.2966  102 LYS B CB  
3163 C CG  . LYS B 102 ? 0.6745 1.2254 0.7283 0.2520  0.0257  0.3156  102 LYS B CG  
3164 C CD  . LYS B 102 ? 0.7182 1.3054 0.7942 0.2395  0.0103  0.2999  102 LYS B CD  
3165 C CE  . LYS B 102 ? 0.8054 1.4135 0.8799 0.2577  0.0143  0.3093  102 LYS B CE  
3166 N NZ  . LYS B 102 ? 0.8922 1.5086 0.9891 0.2503  0.0111  0.3017  102 LYS B NZ  
3167 N N   . PHE B 103 ? 0.4773 0.9387 0.5028 0.2006  0.0394  0.2803  103 PHE B N   
3168 C CA  . PHE B 103 ? 0.4626 0.9230 0.4843 0.1806  0.0312  0.2613  103 PHE B CA  
3169 C C   . PHE B 103 ? 0.4542 0.9625 0.4736 0.1774  0.0086  0.2534  103 PHE B C   
3170 O O   . PHE B 103 ? 0.4940 1.0329 0.5015 0.1942  0.0036  0.2668  103 PHE B O   
3171 C CB  . PHE B 103 ? 0.4859 0.9231 0.4858 0.1838  0.0443  0.2676  103 PHE B CB  
3172 C CG  . PHE B 103 ? 0.4922 0.8814 0.4936 0.1782  0.0661  0.2681  103 PHE B CG  
3173 C CD1 . PHE B 103 ? 0.4745 0.8441 0.4959 0.1690  0.0711  0.2604  103 PHE B CD1 
3174 C CD2 . PHE B 103 ? 0.5185 0.8829 0.5004 0.1818  0.0826  0.2763  103 PHE B CD2 
3175 C CE1 . PHE B 103 ? 0.4815 0.8099 0.5043 0.1622  0.0910  0.2593  103 PHE B CE1 
3176 C CE2 . PHE B 103 ? 0.5262 0.8491 0.5095 0.1742  0.1032  0.2752  103 PHE B CE2 
3177 C CZ  . PHE B 103 ? 0.5078 0.8132 0.5116 0.1641  0.1073  0.2663  103 PHE B CZ  
3178 N N   . VAL B 104 ? 0.4292 0.9436 0.4580 0.1563  -0.0041 0.2316  104 VAL B N   
3179 C CA  . VAL B 104 ? 0.4219 0.9788 0.4505 0.1492  -0.0246 0.2212  104 VAL B CA  
3180 C C   . VAL B 104 ? 0.4101 0.9582 0.4319 0.1288  -0.0322 0.1998  104 VAL B C   
3181 O O   . VAL B 104 ? 0.4127 0.9303 0.4426 0.1156  -0.0272 0.1874  104 VAL B O   
3182 C CB  . VAL B 104 ? 0.4500 1.0263 0.5005 0.1454  -0.0324 0.2173  104 VAL B CB  
3183 C CG1 . VAL B 104 ? 0.3992 1.0019 0.4529 0.1261  -0.0505 0.1971  104 VAL B CG1 
3184 C CG2 . VAL B 104 ? 0.4201 1.0284 0.4714 0.1687  -0.0323 0.2380  104 VAL B CG2 
3185 N N   . ARG B 105 ? 0.4194 0.9950 0.4255 0.1268  -0.0443 0.1951  105 ARG B N   
3186 C CA  . ARG B 105 ? 0.4458 1.0159 0.4424 0.1083  -0.0527 0.1743  105 ARG B CA  
3187 C C   . ARG B 105 ? 0.4007 0.9960 0.4054 0.0933  -0.0686 0.1588  105 ARG B C   
3188 O O   . ARG B 105 ? 0.4362 1.0721 0.4368 0.0955  -0.0802 0.1603  105 ARG B O   
3189 C CB  . ARG B 105 ? 0.4644 1.0465 0.4366 0.1139  -0.0553 0.1772  105 ARG B CB  
3190 C CG  . ARG B 105 ? 0.4299 0.9977 0.3893 0.0974  -0.0601 0.1571  105 ARG B CG  
3191 C CD  . ARG B 105 ? 0.5113 1.0848 0.4459 0.1048  -0.0591 0.1618  105 ARG B CD  
3192 N NE  . ARG B 105 ? 0.4995 1.0602 0.4209 0.0901  -0.0638 0.1423  105 ARG B NE  
3193 C CZ  . ARG B 105 ? 0.4426 0.9696 0.3639 0.0844  -0.0544 0.1343  105 ARG B CZ  
3194 N NH1 . ARG B 105 ? 0.4354 0.9380 0.3696 0.0894  -0.0397 0.1427  105 ARG B NH1 
3195 N NH2 . ARG B 105 ? 0.4443 0.9628 0.3513 0.0736  -0.0595 0.1171  105 ARG B NH2 
3196 N N   . ILE B 106 ? 0.4097 0.9824 0.4246 0.0778  -0.0687 0.1435  106 ILE B N   
3197 C CA  . ILE B 106 ? 0.4313 1.0251 0.4532 0.0630  -0.0815 0.1298  106 ILE B CA  
3198 C C   . ILE B 106 ? 0.4641 1.0661 0.4660 0.0484  -0.0924 0.1125  106 ILE B C   
3199 O O   . ILE B 106 ? 0.4480 1.0266 0.4335 0.0457  -0.0893 0.1057  106 ILE B O   
3200 C CB  . ILE B 106 ? 0.3559 0.9229 0.3949 0.0526  -0.0773 0.1206  106 ILE B CB  
3201 C CG1 . ILE B 106 ? 0.4019 0.9255 0.4346 0.0474  -0.0687 0.1114  106 ILE B CG1 
3202 C CG2 . ILE B 106 ? 0.3718 0.9446 0.4318 0.0644  -0.0709 0.1357  106 ILE B CG2 
3203 C CD1 . ILE B 106 ? 0.4525 0.9630 0.4723 0.0294  -0.0760 0.0894  106 ILE B CD1 
3204 N N   . GLN B 107 ? 0.4521 1.0883 0.4555 0.0382  -0.1047 0.1045  107 GLN B N   
3205 C CA  . GLN B 107 ? 0.4370 1.0799 0.4224 0.0200  -0.1149 0.0850  107 GLN B CA  
3206 C C   . GLN B 107 ? 0.4198 1.0218 0.4029 0.0028  -0.1121 0.0667  107 GLN B C   
3207 O O   . GLN B 107 ? 0.3757 0.9595 0.3765 0.0015  -0.1064 0.0673  107 GLN B O   
3208 C CB  . GLN B 107 ? 0.4304 1.1118 0.4212 0.0117  -0.1235 0.0798  107 GLN B CB  
3209 C CG  . GLN B 107 ? 0.5208 1.2319 0.5077 0.0265  -0.1236 0.0918  107 GLN B CG  
3210 C CD  . GLN B 107 ? 0.6047 1.3098 0.5667 0.0277  -0.1250 0.0883  107 GLN B CD  
3211 O OE1 . GLN B 107 ? 0.5948 1.3012 0.5420 0.0110  -0.1314 0.0705  107 GLN B OE1 
3212 N NE2 . GLN B 107 ? 0.5463 1.2424 0.5021 0.0471  -0.1179 0.1049  107 GLN B NE2 
3213 N N   . PRO B 108 ? 0.4053 0.9914 0.3650 -0.0090 -0.1153 0.0506  108 PRO B N   
3214 C CA  . PRO B 108 ? 0.4407 0.9915 0.3938 -0.0257 -0.1138 0.0321  108 PRO B CA  
3215 C C   . PRO B 108 ? 0.4214 0.9875 0.3873 -0.0408 -0.1188 0.0243  108 PRO B C   
3216 O O   . PRO B 108 ? 0.4785 1.0879 0.4494 -0.0453 -0.1274 0.0255  108 PRO B O   
3217 C CB  . PRO B 108 ? 0.4279 0.9702 0.3501 -0.0349 -0.1181 0.0174  108 PRO B CB  
3218 C CG  . PRO B 108 ? 0.4651 1.0528 0.3817 -0.0304 -0.1266 0.0244  108 PRO B CG  
3219 C CD  . PRO B 108 ? 0.5048 1.1078 0.4409 -0.0086 -0.1214 0.0478  108 PRO B CD  
3220 N N   . GLY B 109 ? 0.4236 0.9555 0.3944 -0.0487 -0.1133 0.0159  109 GLY B N   
3221 C CA  . GLY B 109 ? 0.4329 0.9751 0.4167 -0.0628 -0.1158 0.0094  109 GLY B CA  
3222 C C   . GLY B 109 ? 0.4730 1.0261 0.4871 -0.0519 -0.1117 0.0242  109 GLY B C   
3223 O O   . GLY B 109 ? 0.4186 0.9658 0.4442 -0.0621 -0.1103 0.0185  109 GLY B O   
3224 N N   . GLN B 110 ? 0.4710 1.0373 0.4965 -0.0314 -0.1085 0.0431  110 GLN B N   
3225 C CA  . GLN B 110 ? 0.4057 0.9798 0.4573 -0.0188 -0.1030 0.0585  110 GLN B CA  
3226 C C   . GLN B 110 ? 0.3588 0.8870 0.4169 -0.0154 -0.0921 0.0580  110 GLN B C   
3227 O O   . GLN B 110 ? 0.3613 0.8557 0.4043 -0.0170 -0.0881 0.0498  110 GLN B O   
3228 C CB  . GLN B 110 ? 0.4069 1.0077 0.4635 0.0024  -0.1019 0.0790  110 GLN B CB  
3229 C CG  . GLN B 110 ? 0.4923 1.1500 0.5498 0.0047  -0.1127 0.0843  110 GLN B CG  
3230 C CD  . GLN B 110 ? 0.6184 1.3006 0.6848 -0.0129 -0.1194 0.0721  110 GLN B CD  
3231 O OE1 . GLN B 110 ? 0.5484 1.2418 0.6350 -0.0088 -0.1163 0.0787  110 GLN B OE1 
3232 N NE2 . GLN B 110 ? 0.6279 1.3132 0.6769 -0.0325 -0.1260 0.0537  110 GLN B NE2 
3233 N N   . THR B 111 ? 0.3378 0.8667 0.4183 -0.0101 -0.0872 0.0662  111 THR B N   
3234 C CA  . THR B 111 ? 0.3580 0.8479 0.4466 -0.0076 -0.0772 0.0651  111 THR B CA  
3235 C C   . THR B 111 ? 0.2892 0.7775 0.3933 0.0109  -0.0679 0.0835  111 THR B C   
3236 O O   . THR B 111 ? 0.2926 0.8102 0.4041 0.0223  -0.0688 0.0981  111 THR B O   
3237 C CB  . THR B 111 ? 0.3628 0.8468 0.4624 -0.0197 -0.0777 0.0564  111 THR B CB  
3238 O OG1 . THR B 111 ? 0.2918 0.8127 0.4110 -0.0155 -0.0803 0.0672  111 THR B OG1 
3239 C CG2 . THR B 111 ? 0.3274 0.8038 0.4081 -0.0397 -0.0840 0.0371  111 THR B CG2 
3240 N N   . PHE B 112 ? 0.2796 0.7331 0.3881 0.0136  -0.0583 0.0820  112 PHE B N   
3241 C CA  . PHE B 112 ? 0.2952 0.7397 0.4163 0.0283  -0.0471 0.0969  112 PHE B CA  
3242 C C   . PHE B 112 ? 0.2656 0.6753 0.3936 0.0256  -0.0386 0.0897  112 PHE B C   
3243 O O   . PHE B 112 ? 0.2971 0.6888 0.4167 0.0153  -0.0412 0.0743  112 PHE B O   
3244 C CB  . PHE B 112 ? 0.3253 0.7704 0.4347 0.0390  -0.0428 0.1064  112 PHE B CB  
3245 C CG  . PHE B 112 ? 0.2976 0.7218 0.3891 0.0332  -0.0423 0.0943  112 PHE B CG  
3246 C CD1 . PHE B 112 ? 0.3009 0.7375 0.3735 0.0271  -0.0518 0.0863  112 PHE B CD1 
3247 C CD2 . PHE B 112 ? 0.2831 0.6784 0.3766 0.0350  -0.0317 0.0913  112 PHE B CD2 
3248 C CE1 . PHE B 112 ? 0.3631 0.7811 0.4183 0.0241  -0.0506 0.0760  112 PHE B CE1 
3249 C CE2 . PHE B 112 ? 0.2873 0.6681 0.3650 0.0318  -0.0308 0.0808  112 PHE B CE2 
3250 C CZ  . PHE B 112 ? 0.2988 0.6897 0.3571 0.0272  -0.0401 0.0736  112 PHE B CZ  
3251 N N   . SER B 113 ? 0.2568 0.6570 0.3989 0.0355  -0.0280 0.1009  113 SER B N   
3252 C CA  . SER B 113 ? 0.2622 0.6323 0.4118 0.0338  -0.0189 0.0948  113 SER B CA  
3253 C C   . SER B 113 ? 0.2504 0.6029 0.3925 0.0379  -0.0098 0.0952  113 SER B C   
3254 O O   . SER B 113 ? 0.2787 0.6384 0.4158 0.0460  -0.0056 0.1067  113 SER B O   
3255 C CB  . SER B 113 ? 0.2772 0.6443 0.4461 0.0402  -0.0112 0.1046  113 SER B CB  
3256 O OG  . SER B 113 ? 0.3264 0.7108 0.5040 0.0359  -0.0186 0.1035  113 SER B OG  
3257 N N   . VAL B 114 ? 0.2428 0.5737 0.3836 0.0325  -0.0065 0.0823  114 VAL B N   
3258 C CA  . VAL B 114 ? 0.2495 0.5661 0.3854 0.0340  0.0024  0.0791  114 VAL B CA  
3259 C C   . VAL B 114 ? 0.2616 0.5602 0.4120 0.0342  0.0133  0.0774  114 VAL B C   
3260 O O   . VAL B 114 ? 0.2255 0.5157 0.3816 0.0299  0.0108  0.0680  114 VAL B O   
3261 C CB  . VAL B 114 ? 0.3012 0.6124 0.4207 0.0285  -0.0036 0.0633  114 VAL B CB  
3262 C CG1 . VAL B 114 ? 0.2842 0.5850 0.4019 0.0300  0.0063  0.0591  114 VAL B CG1 
3263 C CG2 . VAL B 114 ? 0.2685 0.5956 0.3711 0.0274  -0.0135 0.0638  114 VAL B CG2 
3264 N N   . LEU B 115 ? 0.2644 0.5557 0.4190 0.0384  0.0260  0.0857  115 LEU B N   
3265 C CA  . LEU B 115 ? 0.2663 0.5399 0.4324 0.0365  0.0381  0.0819  115 LEU B CA  
3266 C C   . LEU B 115 ? 0.2508 0.5197 0.4099 0.0321  0.0428  0.0705  115 LEU B C   
3267 O O   . LEU B 115 ? 0.2610 0.5299 0.4142 0.0333  0.0509  0.0761  115 LEU B O   
3268 C CB  . LEU B 115 ? 0.2960 0.5619 0.4697 0.0429  0.0512  0.0980  115 LEU B CB  
3269 C CG  . LEU B 115 ? 0.3268 0.5724 0.5106 0.0391  0.0656  0.0933  115 LEU B CG  
3270 C CD1 . LEU B 115 ? 0.2989 0.5402 0.4948 0.0369  0.0616  0.0865  115 LEU B CD1 
3271 C CD2 . LEU B 115 ? 0.3199 0.5522 0.5040 0.0451  0.0818  0.1093  115 LEU B CD2 
3272 N N   . ALA B 116 ? 0.2459 0.5123 0.4040 0.0278  0.0376  0.0546  116 ALA B N   
3273 C CA  . ALA B 116 ? 0.3471 0.6139 0.4990 0.0250  0.0409  0.0422  116 ALA B CA  
3274 C C   . ALA B 116 ? 0.3742 0.6330 0.5382 0.0214  0.0559  0.0403  116 ALA B C   
3275 O O   . ALA B 116 ? 0.3362 0.5861 0.5123 0.0199  0.0597  0.0384  116 ALA B O   
3276 C CB  . ALA B 116 ? 0.2696 0.5360 0.4147 0.0244  0.0312  0.0264  116 ALA B CB  
3277 N N   . CYS B 117 ? 0.3319 0.5938 0.4919 0.0189  0.0651  0.0400  117 CYS B N   
3278 C CA  . CYS B 117 ? 0.4023 0.6562 0.5714 0.0128  0.0818  0.0389  117 CYS B CA  
3279 C C   . CYS B 117 ? 0.4235 0.6888 0.5899 0.0072  0.0860  0.0243  117 CYS B C   
3280 O O   . CYS B 117 ? 0.3876 0.6649 0.5421 0.0098  0.0796  0.0214  117 CYS B O   
3281 C CB  . CYS B 117 ? 0.3804 0.6247 0.5465 0.0146  0.0934  0.0565  117 CYS B CB  
3282 S SG  . CYS B 117 ? 0.4272 0.6598 0.5995 0.0224  0.0928  0.0735  117 CYS B SG  
3283 N N   . TYR B 118 ? 0.4495 0.7127 0.6271 -0.0007 0.0974  0.0146  118 TYR B N   
3284 C CA  . TYR B 118 ? 0.4722 0.7505 0.6506 -0.0079 0.1041  -0.0002 118 TYR B CA  
3285 C C   . TYR B 118 ? 0.5113 0.7795 0.6986 -0.0197 0.1244  0.0001  118 TYR B C   
3286 O O   . TYR B 118 ? 0.5215 0.7753 0.7187 -0.0232 0.1307  0.0005  118 TYR B O   
3287 C CB  . TYR B 118 ? 0.4540 0.7470 0.6358 -0.0060 0.0948  -0.0185 118 TYR B CB  
3288 C CG  . TYR B 118 ? 0.5028 0.8003 0.6714 0.0051  0.0773  -0.0190 118 TYR B CG  
3289 C CD1 . TYR B 118 ? 0.4727 0.7851 0.6280 0.0092  0.0722  -0.0242 118 TYR B CD1 
3290 C CD2 . TYR B 118 ? 0.4721 0.7571 0.6398 0.0107  0.0672  -0.0136 118 TYR B CD2 
3291 C CE1 . TYR B 118 ? 0.4346 0.7465 0.5747 0.0184  0.0579  -0.0249 118 TYR B CE1 
3292 C CE2 . TYR B 118 ? 0.4690 0.7546 0.6221 0.0184  0.0531  -0.0146 118 TYR B CE2 
3293 C CZ  . TYR B 118 ? 0.4555 0.7530 0.5941 0.0221  0.0488  -0.0203 118 TYR B CZ  
3294 O OH  . TYR B 118 ? 0.4210 0.7152 0.5425 0.0289  0.0364  -0.0219 118 TYR B OH  
3295 N N   . ASN B 119 ? 0.4667 0.7393 0.6485 -0.0259 0.1355  0.0010  119 ASN B N   
3296 C CA  . ASN B 119 ? 0.5221 0.7829 0.7086 -0.0394 0.1572  0.0005  119 ASN B CA  
3297 C C   . ASN B 119 ? 0.5624 0.7912 0.7473 -0.0373 0.1674  0.0187  119 ASN B C   
3298 O O   . ASN B 119 ? 0.5387 0.7500 0.7296 -0.0472 0.1836  0.0168  119 ASN B O   
3299 C CB  . ASN B 119 ? 0.5039 0.7770 0.7043 -0.0510 0.1626  -0.0201 119 ASN B CB  
3300 C CG  . ASN B 119 ? 0.5379 0.8454 0.7389 -0.0527 0.1565  -0.0377 119 ASN B CG  
3301 O OD1 . ASN B 119 ? 0.6422 0.9673 0.8469 -0.0462 0.1430  -0.0496 119 ASN B OD1 
3302 N ND2 . ASN B 119 ? 0.5559 0.8733 0.7516 -0.0597 0.1664  -0.0388 119 ASN B ND2 
3303 N N   . GLY B 120 ? 0.5291 0.7511 0.7048 -0.0240 0.1581  0.0361  120 GLY B N   
3304 C CA  . GLY B 120 ? 0.4936 0.6898 0.6666 -0.0175 0.1654  0.0548  120 GLY B CA  
3305 C C   . GLY B 120 ? 0.5076 0.6944 0.6921 -0.0147 0.1612  0.0542  120 GLY B C   
3306 O O   . GLY B 120 ? 0.5215 0.6852 0.7051 -0.0104 0.1711  0.0679  120 GLY B O   
3307 N N   . SER B 121 ? 0.4949 0.6979 0.6885 -0.0155 0.1475  0.0392  121 SER B N   
3308 C CA  . SER B 121 ? 0.5738 0.7693 0.7781 -0.0130 0.1430  0.0373  121 SER B CA  
3309 C C   . SER B 121 ? 0.5393 0.7470 0.7426 -0.0023 0.1220  0.0393  121 SER B C   
3310 O O   . SER B 121 ? 0.4918 0.7177 0.6923 -0.0019 0.1098  0.0275  121 SER B O   
3311 C CB  . SER B 121 ? 0.5834 0.7842 0.7986 -0.0241 0.1477  0.0171  121 SER B CB  
3312 O OG  . SER B 121 ? 0.7176 0.9005 0.9350 -0.0356 0.1692  0.0162  121 SER B OG  
3313 N N   . PRO B 122 ? 0.4997 0.6984 0.7046 0.0063  0.1182  0.0532  122 PRO B N   
3314 C CA  . PRO B 122 ? 0.4592 0.6699 0.6632 0.0136  0.0994  0.0540  122 PRO B CA  
3315 C C   . PRO B 122 ? 0.5046 0.7215 0.7141 0.0104  0.0909  0.0365  122 PRO B C   
3316 O O   . PRO B 122 ? 0.5871 0.7962 0.8061 0.0059  0.0980  0.0288  122 PRO B O   
3317 C CB  . PRO B 122 ? 0.5208 0.7212 0.7296 0.0213  0.1009  0.0699  122 PRO B CB  
3318 C CG  . PRO B 122 ? 0.5871 0.7664 0.7963 0.0202  0.1214  0.0793  122 PRO B CG  
3319 C CD  . PRO B 122 ? 0.5295 0.7077 0.7334 0.0106  0.1317  0.0707  122 PRO B CD  
3320 N N   . SER B 123 ? 0.4761 0.7058 0.6776 0.0134  0.0762  0.0305  123 SER B N   
3321 C CA  . SER B 123 ? 0.5249 0.7586 0.7266 0.0133  0.0677  0.0152  123 SER B CA  
3322 C C   . SER B 123 ? 0.5006 0.7321 0.6998 0.0180  0.0552  0.0181  123 SER B C   
3323 O O   . SER B 123 ? 0.4959 0.7226 0.6988 0.0183  0.0524  0.0099  123 SER B O   
3324 C CB  . SER B 123 ? 0.5226 0.7701 0.7135 0.0131  0.0631  0.0028  123 SER B CB  
3325 O OG  . SER B 123 ? 0.5770 0.8269 0.7598 0.0176  0.0514  -0.0073 123 SER B OG  
3326 N N   . GLY B 124 ? 0.3881 0.6241 0.5806 0.0209  0.0481  0.0289  124 GLY B N   
3327 C CA  . GLY B 124 ? 0.3316 0.5678 0.5213 0.0226  0.0369  0.0303  124 GLY B CA  
3328 C C   . GLY B 124 ? 0.3614 0.6078 0.5451 0.0245  0.0308  0.0424  124 GLY B C   
3329 O O   . GLY B 124 ? 0.2759 0.5289 0.4536 0.0259  0.0332  0.0483  124 GLY B O   
3330 N N   . VAL B 125 ? 0.3249 0.5743 0.5103 0.0244  0.0232  0.0459  125 VAL B N   
3331 C CA  . VAL B 125 ? 0.2846 0.5491 0.4660 0.0257  0.0164  0.0565  125 VAL B CA  
3332 C C   . VAL B 125 ? 0.2921 0.5599 0.4633 0.0204  0.0044  0.0482  125 VAL B C   
3333 O O   . VAL B 125 ? 0.2716 0.5287 0.4444 0.0174  0.0031  0.0400  125 VAL B O   
3334 C CB  . VAL B 125 ? 0.2756 0.5455 0.4714 0.0306  0.0212  0.0717  125 VAL B CB  
3335 C CG1 . VAL B 125 ? 0.3012 0.5672 0.5070 0.0282  0.0189  0.0684  125 VAL B CG1 
3336 C CG2 . VAL B 125 ? 0.2773 0.5679 0.4689 0.0343  0.0153  0.0836  125 VAL B CG2 
3337 N N   . TYR B 126 ? 0.3162 0.5971 0.4751 0.0187  -0.0035 0.0497  126 TYR B N   
3338 C CA  . TYR B 126 ? 0.3118 0.5943 0.4584 0.0115  -0.0136 0.0413  126 TYR B CA  
3339 C C   . TYR B 126 ? 0.2976 0.6027 0.4375 0.0101  -0.0208 0.0482  126 TYR B C   
3340 O O   . TYR B 126 ? 0.2680 0.5843 0.4087 0.0164  -0.0182 0.0581  126 TYR B O   
3341 C CB  . TYR B 126 ? 0.3328 0.5971 0.4608 0.0094  -0.0154 0.0257  126 TYR B CB  
3342 C CG  . TYR B 126 ? 0.3710 0.6371 0.4879 0.0136  -0.0137 0.0240  126 TYR B CG  
3343 C CD1 . TYR B 126 ? 0.4136 0.6890 0.5142 0.0117  -0.0202 0.0235  126 TYR B CD1 
3344 C CD2 . TYR B 126 ? 0.3893 0.6499 0.5125 0.0185  -0.0052 0.0224  126 TYR B CD2 
3345 C CE1 . TYR B 126 ? 0.3902 0.6680 0.4806 0.0158  -0.0181 0.0224  126 TYR B CE1 
3346 C CE2 . TYR B 126 ? 0.4154 0.6802 0.5295 0.0215  -0.0028 0.0205  126 TYR B CE2 
3347 C CZ  . TYR B 126 ? 0.4038 0.6768 0.5015 0.0207  -0.0092 0.0211  126 TYR B CZ  
3348 O OH  . TYR B 126 ? 0.4051 0.6827 0.4934 0.0239  -0.0064 0.0194  126 TYR B OH  
3349 N N   . GLN B 127 ? 0.2848 0.5961 0.4161 0.0013  -0.0294 0.0420  127 GLN B N   
3350 C CA  . GLN B 127 ? 0.3653 0.7020 0.4901 -0.0020 -0.0374 0.0462  127 GLN B CA  
3351 C C   . GLN B 127 ? 0.3594 0.6890 0.4591 -0.0075 -0.0428 0.0348  127 GLN B C   
3352 O O   . GLN B 127 ? 0.3678 0.6734 0.4536 -0.0120 -0.0426 0.0218  127 GLN B O   
3353 C CB  . GLN B 127 ? 0.2673 0.6212 0.4005 -0.0102 -0.0428 0.0465  127 GLN B CB  
3354 C CG  . GLN B 127 ? 0.3682 0.7576 0.5008 -0.0118 -0.0506 0.0530  127 GLN B CG  
3355 C CD  . GLN B 127 ? 0.3808 0.7950 0.5331 0.0007  -0.0477 0.0711  127 GLN B CD  
3356 O OE1 . GLN B 127 ? 0.3367 0.7377 0.4980 0.0119  -0.0385 0.0799  127 GLN B OE1 
3357 N NE2 . GLN B 127 ? 0.3707 0.8214 0.5283 -0.0010 -0.0548 0.0762  127 GLN B NE2 
3358 N N   . CYS B 128 ? 0.3385 0.6878 0.4302 -0.0057 -0.0472 0.0399  128 CYS B N   
3359 C CA  A CYS B 128 ? 0.3491 0.6930 0.4163 -0.0093 -0.0516 0.0305  128 CYS B CA  
3360 C CA  B CYS B 128 ? 0.3498 0.6927 0.4165 -0.0112 -0.0523 0.0289  128 CYS B CA  
3361 C C   . CYS B 128 ? 0.3665 0.7398 0.4270 -0.0145 -0.0605 0.0332  128 CYS B C   
3362 O O   . CYS B 128 ? 0.3394 0.7404 0.4146 -0.0096 -0.0619 0.0462  128 CYS B O   
3363 C CB  A CYS B 128 ? 0.3466 0.6839 0.4086 0.0008  -0.0459 0.0339  128 CYS B CB  
3364 C CB  B CYS B 128 ? 0.3627 0.6899 0.4201 -0.0028 -0.0467 0.0271  128 CYS B CB  
3365 S SG  A CYS B 128 ? 0.3884 0.6955 0.4497 0.0055  -0.0372 0.0251  128 CYS B SG  
3366 S SG  B CYS B 128 ? 0.3565 0.7040 0.4220 0.0084  -0.0426 0.0437  128 CYS B SG  
3367 N N   . ALA B 129 ? 0.3346 0.7027 0.3713 -0.0226 -0.0659 0.0215  129 ALA B N   
3368 C CA  . ALA B 129 ? 0.3663 0.7633 0.3937 -0.0275 -0.0743 0.0225  129 ALA B CA  
3369 C C   . ALA B 129 ? 0.3326 0.7267 0.3414 -0.0210 -0.0743 0.0224  129 ALA B C   
3370 O O   . ALA B 129 ? 0.3511 0.7175 0.3458 -0.0190 -0.0701 0.0141  129 ALA B O   
3371 C CB  . ALA B 129 ? 0.3960 0.7928 0.4097 -0.0456 -0.0808 0.0079  129 ALA B CB  
3372 N N   . MET B 130 ? 0.3434 0.7678 0.3520 -0.0162 -0.0785 0.0321  130 MET B N   
3373 C CA  . MET B 130 ? 0.3799 0.8044 0.3679 -0.0123 -0.0797 0.0306  130 MET B CA  
3374 C C   . MET B 130 ? 0.3721 0.7925 0.3353 -0.0271 -0.0872 0.0136  130 MET B C   
3375 O O   . MET B 130 ? 0.4026 0.8505 0.3639 -0.0363 -0.0954 0.0117  130 MET B O   
3376 C CB  . MET B 130 ? 0.3695 0.8267 0.3629 -0.0014 -0.0813 0.0470  130 MET B CB  
3377 C CG  . MET B 130 ? 0.3697 0.8315 0.3414 0.0032  -0.0827 0.0471  130 MET B CG  
3378 S SD  . MET B 130 ? 0.5086 0.9336 0.4746 0.0105  -0.0711 0.0441  130 MET B SD  
3379 C CE  . MET B 130 ? 0.4158 0.8427 0.4082 0.0239  -0.0598 0.0635  130 MET B CE  
3380 N N   . ARG B 131 ? 0.4188 0.8049 0.3623 -0.0294 -0.0837 0.0007  131 ARG B N   
3381 C CA  . ARG B 131 ? 0.4336 0.8069 0.3487 -0.0429 -0.0884 -0.0161 131 ARG B CA  
3382 C C   . ARG B 131 ? 0.4805 0.8808 0.3809 -0.0449 -0.0956 -0.0155 131 ARG B C   
3383 O O   . ARG B 131 ? 0.4561 0.8767 0.3629 -0.0326 -0.0954 -0.0026 131 ARG B O   
3384 C CB  . ARG B 131 ? 0.4167 0.7497 0.3100 -0.0391 -0.0823 -0.0272 131 ARG B CB  
3385 C CG  . ARG B 131 ? 0.4318 0.7378 0.3359 -0.0335 -0.0746 -0.0282 131 ARG B CG  
3386 C CD  . ARG B 131 ? 0.5190 0.8088 0.4237 -0.0458 -0.0746 -0.0365 131 ARG B CD  
3387 N NE  . ARG B 131 ? 0.5561 0.8379 0.4352 -0.0622 -0.0788 -0.0501 131 ARG B NE  
3388 C CZ  . ARG B 131 ? 0.5444 0.8267 0.4259 -0.0781 -0.0806 -0.0560 131 ARG B CZ  
3389 N NH1 . ARG B 131 ? 0.5067 0.7960 0.4144 -0.0783 -0.0789 -0.0493 131 ARG B NH1 
3390 N NH2 . ARG B 131 ? 0.5050 0.7808 0.3617 -0.0951 -0.0835 -0.0694 131 ARG B NH2 
3391 N N   . PRO B 132 ? 0.4983 0.8978 0.3771 -0.0609 -0.1013 -0.0300 132 PRO B N   
3392 C CA  . PRO B 132 ? 0.4958 0.9201 0.3576 -0.0634 -0.1083 -0.0316 132 PRO B CA  
3393 C C   . PRO B 132 ? 0.4710 0.8818 0.3157 -0.0503 -0.1046 -0.0296 132 PRO B C   
3394 O O   . PRO B 132 ? 0.4983 0.9345 0.3353 -0.0463 -0.1092 -0.0247 132 PRO B O   
3395 C CB  . PRO B 132 ? 0.5611 0.9748 0.3991 -0.0856 -0.1123 -0.0515 132 PRO B CB  
3396 C CG  . PRO B 132 ? 0.5453 0.9475 0.3975 -0.0954 -0.1097 -0.0551 132 PRO B CG  
3397 C CD  . PRO B 132 ? 0.5503 0.9268 0.4182 -0.0785 -0.1009 -0.0457 132 PRO B CD  
3398 N N   . ASN B 133 ? 0.4775 0.8515 0.3155 -0.0430 -0.0964 -0.0335 133 ASN B N   
3399 C CA  . ASN B 133 ? 0.5071 0.8702 0.3305 -0.0303 -0.0919 -0.0323 133 ASN B CA  
3400 C C   . ASN B 133 ? 0.5021 0.8745 0.3499 -0.0140 -0.0854 -0.0156 133 ASN B C   
3401 O O   . ASN B 133 ? 0.4921 0.8515 0.3330 -0.0035 -0.0789 -0.0152 133 ASN B O   
3402 C CB  . ASN B 133 ? 0.5301 0.8501 0.3289 -0.0307 -0.0864 -0.0475 133 ASN B CB  
3403 C CG  . ASN B 133 ? 0.5470 0.8443 0.3618 -0.0253 -0.0793 -0.0468 133 ASN B CG  
3404 O OD1 . ASN B 133 ? 0.4637 0.7760 0.3080 -0.0228 -0.0785 -0.0357 133 ASN B OD1 
3405 N ND2 . ASN B 133 ? 0.5944 0.8553 0.3881 -0.0224 -0.0740 -0.0586 133 ASN B ND2 
3406 N N   . PHE B 134 ? 0.4465 0.8392 0.3223 -0.0123 -0.0857 -0.0029 134 PHE B N   
3407 C CA  . PHE B 134 ? 0.4115 0.8156 0.3084 0.0015  -0.0791 0.0144  134 PHE B CA  
3408 C C   . PHE B 134 ? 0.3971 0.7754 0.3037 0.0084  -0.0689 0.0135  134 PHE B C   
3409 O O   . PHE B 134 ? 0.4317 0.8128 0.3466 0.0185  -0.0613 0.0233  134 PHE B O   
3410 C CB  . PHE B 134 ? 0.4227 0.8450 0.3082 0.0100  -0.0792 0.0228  134 PHE B CB  
3411 C CG  . PHE B 134 ? 0.4325 0.8898 0.3161 0.0076  -0.0885 0.0292  134 PHE B CG  
3412 C CD1 . PHE B 134 ? 0.4210 0.9021 0.3268 0.0125  -0.0892 0.0438  134 PHE B CD1 
3413 C CD2 . PHE B 134 ? 0.4547 0.9220 0.3134 0.0004  -0.0966 0.0194  134 PHE B CD2 
3414 C CE1 . PHE B 134 ? 0.4670 0.9859 0.3709 0.0124  -0.0983 0.0498  134 PHE B CE1 
3415 C CE2 . PHE B 134 ? 0.4786 0.9833 0.3355 -0.0020 -0.1059 0.0240  134 PHE B CE2 
3416 C CZ  . PHE B 134 ? 0.4856 1.0185 0.3658 0.0046  -0.1072 0.0395  134 PHE B CZ  
3417 N N   . THR B 135 ? 0.4033 0.7570 0.3077 0.0027  -0.0680 0.0015  135 THR B N   
3418 C CA  . THR B 135 ? 0.3931 0.7271 0.3101 0.0086  -0.0597 0.0002  135 THR B CA  
3419 C C   . THR B 135 ? 0.3642 0.6954 0.3020 0.0035  -0.0599 0.0022  135 THR B C   
3420 O O   . THR B 135 ? 0.4061 0.7481 0.3464 -0.0057 -0.0664 0.0021  135 THR B O   
3421 C CB  . THR B 135 ? 0.4643 0.7703 0.3581 0.0098  -0.0576 -0.0154 135 THR B CB  
3422 O OG1 . THR B 135 ? 0.4158 0.7052 0.2952 -0.0010 -0.0625 -0.0268 135 THR B OG1 
3423 C CG2 . THR B 135 ? 0.4870 0.7959 0.3579 0.0141  -0.0581 -0.0184 135 THR B CG2 
3424 N N   . ILE B 136 ? 0.3586 0.6767 0.3112 0.0088  -0.0525 0.0029  136 ILE B N   
3425 C CA  . ILE B 136 ? 0.4301 0.7415 0.4003 0.0047  -0.0518 0.0032  136 ILE B CA  
3426 C C   . ILE B 136 ? 0.4528 0.7367 0.4175 0.0072  -0.0472 -0.0083 136 ILE B C   
3427 O O   . ILE B 136 ? 0.3867 0.6623 0.3421 0.0149  -0.0427 -0.0132 136 ILE B O   
3428 C CB  . ILE B 136 ? 0.3644 0.6913 0.3629 0.0096  -0.0470 0.0187  136 ILE B CB  
3429 C CG1 . ILE B 136 ? 0.3920 0.7114 0.3999 0.0184  -0.0366 0.0213  136 ILE B CG1 
3430 C CG2 . ILE B 136 ? 0.3229 0.6777 0.3235 0.0107  -0.0512 0.0311  136 ILE B CG2 
3431 C CD1 . ILE B 136 ? 0.3200 0.6483 0.3525 0.0226  -0.0295 0.0358  136 ILE B CD1 
3432 N N   . LYS B 137 ? 0.4406 0.7116 0.4094 0.0011  -0.0482 -0.0130 137 LYS B N   
3433 C CA  . LYS B 137 ? 0.4649 0.7092 0.4271 0.0044  -0.0440 -0.0232 137 LYS B CA  
3434 C C   . LYS B 137 ? 0.4839 0.7317 0.4743 0.0081  -0.0386 -0.0163 137 LYS B C   
3435 O O   . LYS B 137 ? 0.5128 0.7599 0.5160 0.0023  -0.0395 -0.0137 137 LYS B O   
3436 C CB  . LYS B 137 ? 0.5382 0.7613 0.4811 -0.0055 -0.0475 -0.0337 137 LYS B CB  
3437 C CG  . LYS B 137 ? 0.6205 0.8295 0.5290 -0.0085 -0.0503 -0.0443 137 LYS B CG  
3438 C CD  . LYS B 137 ? 0.6804 0.8604 0.5671 -0.0187 -0.0505 -0.0558 137 LYS B CD  
3439 C CE  . LYS B 137 ? 0.8557 1.0291 0.7122 -0.0287 -0.0545 -0.0644 137 LYS B CE  
3440 N NZ  . LYS B 137 ? 0.8627 1.0248 0.7104 -0.0472 -0.0561 -0.0715 137 LYS B NZ  
3441 N N   . GLY B 138 ? 0.4946 0.7470 0.4947 0.0171  -0.0323 -0.0138 138 GLY B N   
3442 C CA  . GLY B 138 ? 0.4369 0.6927 0.4627 0.0194  -0.0262 -0.0078 138 GLY B CA  
3443 C C   . GLY B 138 ? 0.4565 0.7006 0.4830 0.0263  -0.0205 -0.0168 138 GLY B C   
3444 O O   . GLY B 138 ? 0.5139 0.7418 0.5207 0.0298  -0.0220 -0.0281 138 GLY B O   
3445 N N   . SER B 139 ? 0.4756 0.7280 0.5237 0.0288  -0.0132 -0.0119 139 SER B N   
3446 C CA  . SER B 139 ? 0.4346 0.6827 0.4876 0.0345  -0.0075 -0.0206 139 SER B CA  
3447 C C   . SER B 139 ? 0.3941 0.6580 0.4632 0.0350  0.0010  -0.0154 139 SER B C   
3448 O O   . SER B 139 ? 0.3616 0.6287 0.4505 0.0315  0.0065  -0.0068 139 SER B O   
3449 C CB  . SER B 139 ? 0.4579 0.6949 0.5224 0.0332  -0.0066 -0.0220 139 SER B CB  
3450 O OG  . SER B 139 ? 0.4392 0.6760 0.5095 0.0390  -0.0012 -0.0305 139 SER B OG  
3451 N N   . PHE B 140 ? 0.3607 0.6333 0.4194 0.0389  0.0028  -0.0203 140 PHE B N   
3452 C CA  . PHE B 140 ? 0.4274 0.7147 0.4978 0.0377  0.0121  -0.0165 140 PHE B CA  
3453 C C   . PHE B 140 ? 0.4489 0.7451 0.5144 0.0432  0.0156  -0.0300 140 PHE B C   
3454 O O   . PHE B 140 ? 0.3965 0.6916 0.4417 0.0499  0.0104  -0.0379 140 PHE B O   
3455 C CB  . PHE B 140 ? 0.4256 0.7209 0.4876 0.0365  0.0115  -0.0069 140 PHE B CB  
3456 C CG  . PHE B 140 ? 0.4145 0.7080 0.4806 0.0329  0.0078  0.0071  140 PHE B CG  
3457 C CD1 . PHE B 140 ? 0.3994 0.6941 0.4838 0.0306  0.0154  0.0190  140 PHE B CD1 
3458 C CD2 . PHE B 140 ? 0.3907 0.6829 0.4407 0.0323  -0.0025 0.0080  140 PHE B CD2 
3459 C CE1 . PHE B 140 ? 0.4137 0.7108 0.5011 0.0301  0.0119  0.0325  140 PHE B CE1 
3460 C CE2 . PHE B 140 ? 0.3852 0.6828 0.4396 0.0295  -0.0065 0.0201  140 PHE B CE2 
3461 C CZ  . PHE B 140 ? 0.3832 0.6847 0.4565 0.0297  0.0004  0.0328  140 PHE B CZ  
3462 N N   . LEU B 141 ? 0.4563 0.7620 0.5395 0.0406  0.0247  -0.0334 141 LEU B N   
3463 C CA  . LEU B 141 ? 0.4999 0.8226 0.5819 0.0447  0.0291  -0.0462 141 LEU B CA  
3464 C C   . LEU B 141 ? 0.5015 0.8396 0.5896 0.0389  0.0388  -0.0422 141 LEU B C   
3465 O O   . LEU B 141 ? 0.4176 0.7502 0.5093 0.0332  0.0422  -0.0289 141 LEU B O   
3466 C CB  . LEU B 141 ? 0.4489 0.7760 0.5456 0.0446  0.0330  -0.0555 141 LEU B CB  
3467 C CG  . LEU B 141 ? 0.5162 0.8257 0.6051 0.0509  0.0246  -0.0587 141 LEU B CG  
3468 C CD1 . LEU B 141 ? 0.5383 0.8503 0.6436 0.0498  0.0287  -0.0654 141 LEU B CD1 
3469 C CD2 . LEU B 141 ? 0.4691 0.7747 0.5315 0.0635  0.0169  -0.0674 141 LEU B CD2 
3470 N N   . ASN B 142 ? 0.5240 0.8827 0.6119 0.0413  0.0434  -0.0538 142 ASN B N   
3471 C CA  . ASN B 142 ? 0.4936 0.8684 0.5896 0.0334  0.0552  -0.0524 142 ASN B CA  
3472 C C   . ASN B 142 ? 0.4913 0.8577 0.6070 0.0213  0.0661  -0.0442 142 ASN B C   
3473 O O   . ASN B 142 ? 0.4412 0.8021 0.5694 0.0188  0.0671  -0.0478 142 ASN B O   
3474 C CB  . ASN B 142 ? 0.5239 0.9267 0.6227 0.0360  0.0595  -0.0688 142 ASN B CB  
3475 C CG  . ASN B 142 ? 0.6527 1.0742 0.7493 0.0318  0.0682  -0.0690 142 ASN B CG  
3476 O OD1 . ASN B 142 ? 0.6752 1.1046 0.7863 0.0191  0.0816  -0.0680 142 ASN B OD1 
3477 N ND2 . ASN B 142 ? 0.6775 1.1046 0.7545 0.0420  0.0618  -0.0708 142 ASN B ND2 
3478 N N   . GLY B 143 ? 0.4426 0.8050 0.5584 0.0149  0.0747  -0.0323 143 GLY B N   
3479 C CA  . GLY B 143 ? 0.4368 0.7858 0.5664 0.0051  0.0869  -0.0225 143 GLY B CA  
3480 C C   . GLY B 143 ? 0.4519 0.7787 0.5811 0.0080  0.0818  -0.0069 143 GLY B C   
3481 O O   . GLY B 143 ? 0.4381 0.7513 0.5761 0.0023  0.0925  0.0032  143 GLY B O   
3482 N N   . SER B 144 ? 0.4516 0.7743 0.5699 0.0165  0.0668  -0.0045 144 SER B N   
3483 C CA  . SER B 144 ? 0.3882 0.6959 0.5067 0.0187  0.0617  0.0099  144 SER B CA  
3484 C C   . SER B 144 ? 0.3936 0.6998 0.5032 0.0203  0.0641  0.0258  144 SER B C   
3485 O O   . SER B 144 ? 0.3514 0.6492 0.4624 0.0229  0.0617  0.0391  144 SER B O   
3486 C CB  . SER B 144 ? 0.3795 0.6842 0.4889 0.0248  0.0457  0.0054  144 SER B CB  
3487 O OG  . SER B 144 ? 0.3586 0.6704 0.4489 0.0294  0.0377  0.0017  144 SER B OG  
3488 N N   . CYS B 145 ? 0.3828 0.6984 0.4829 0.0197  0.0694  0.0250  145 CYS B N   
3489 C CA  . CYS B 145 ? 0.3961 0.7113 0.4846 0.0226  0.0714  0.0397  145 CYS B CA  
3490 C C   . CYS B 145 ? 0.3914 0.6924 0.4870 0.0215  0.0837  0.0560  145 CYS B C   
3491 O O   . CYS B 145 ? 0.3359 0.6279 0.4433 0.0147  0.0976  0.0543  145 CYS B O   
3492 C CB  . CYS B 145 ? 0.4141 0.7411 0.4930 0.0209  0.0783  0.0347  145 CYS B CB  
3493 S SG  . CYS B 145 ? 0.5128 0.8538 0.5744 0.0275  0.0625  0.0215  145 CYS B SG  
3494 N N   . GLY B 146 ? 0.3391 0.6386 0.4252 0.0286  0.0796  0.0718  146 GLY B N   
3495 C CA  . GLY B 146 ? 0.3623 0.6481 0.4525 0.0317  0.0893  0.0887  146 GLY B CA  
3496 C C   . GLY B 146 ? 0.3151 0.5954 0.4171 0.0345  0.0826  0.0919  146 GLY B C   
3497 O O   . GLY B 146 ? 0.3353 0.6063 0.4389 0.0402  0.0889  0.1075  146 GLY B O   
3498 N N   . SER B 147 ? 0.3108 0.5962 0.4196 0.0317  0.0707  0.0783  147 SER B N   
3499 C CA  . SER B 147 ? 0.3377 0.6211 0.4553 0.0346  0.0621  0.0817  147 SER B CA  
3500 C C   . SER B 147 ? 0.3192 0.6144 0.4273 0.0422  0.0515  0.0941  147 SER B C   
3501 O O   . SER B 147 ? 0.2988 0.6055 0.3924 0.0438  0.0447  0.0934  147 SER B O   
3502 C CB  . SER B 147 ? 0.2968 0.5827 0.4183 0.0307  0.0512  0.0649  147 SER B CB  
3503 O OG  . SER B 147 ? 0.2588 0.5385 0.3897 0.0249  0.0596  0.0528  147 SER B OG  
3504 N N   . VAL B 148 ? 0.2927 0.5872 0.4089 0.0473  0.0505  0.1054  148 VAL B N   
3505 C CA  . VAL B 148 ? 0.3024 0.6130 0.4107 0.0556  0.0423  0.1186  148 VAL B CA  
3506 C C   . VAL B 148 ? 0.2895 0.6121 0.4047 0.0546  0.0281  0.1152  148 VAL B C   
3507 O O   . VAL B 148 ? 0.2761 0.5899 0.4041 0.0503  0.0282  0.1084  148 VAL B O   
3508 C CB  . VAL B 148 ? 0.3218 0.6257 0.4295 0.0659  0.0554  0.1387  148 VAL B CB  
3509 C CG1 . VAL B 148 ? 0.3384 0.6279 0.4368 0.0648  0.0711  0.1412  148 VAL B CG1 
3510 C CG2 . VAL B 148 ? 0.3173 0.6078 0.4408 0.0675  0.0627  0.1429  148 VAL B CG2 
3511 N N   . GLY B 149 ? 0.2950 0.6389 0.4007 0.0574  0.0161  0.1190  149 GLY B N   
3512 C CA  . GLY B 149 ? 0.2875 0.6479 0.3985 0.0556  0.0034  0.1174  149 GLY B CA  
3513 C C   . GLY B 149 ? 0.2981 0.6769 0.4125 0.0672  0.0036  0.1359  149 GLY B C   
3514 O O   . GLY B 149 ? 0.3147 0.6977 0.4197 0.0769  0.0092  0.1488  149 GLY B O   
3515 N N   . PHE B 150 ? 0.2899 0.6807 0.4170 0.0672  -0.0021 0.1374  150 PHE B N   
3516 C CA  . PHE B 150 ? 0.3225 0.7312 0.4548 0.0810  -0.0001 0.1556  150 PHE B CA  
3517 C C   . PHE B 150 ? 0.2902 0.7239 0.4343 0.0780  -0.0114 0.1533  150 PHE B C   
3518 O O   . PHE B 150 ? 0.2755 0.7028 0.4267 0.0654  -0.0164 0.1391  150 PHE B O   
3519 C CB  . PHE B 150 ? 0.3058 0.6895 0.4461 0.0903  0.0173  0.1673  150 PHE B CB  
3520 C CG  . PHE B 150 ? 0.2892 0.6538 0.4451 0.0824  0.0211  0.1578  150 PHE B CG  
3521 C CD1 . PHE B 150 ? 0.3069 0.6478 0.4628 0.0711  0.0251  0.1429  150 PHE B CD1 
3522 C CD2 . PHE B 150 ? 0.2841 0.6564 0.4542 0.0870  0.0205  0.1634  150 PHE B CD2 
3523 C CE1 . PHE B 150 ? 0.3019 0.6267 0.4711 0.0646  0.0281  0.1337  150 PHE B CE1 
3524 C CE2 . PHE B 150 ? 0.2697 0.6243 0.4532 0.0800  0.0240  0.1546  150 PHE B CE2 
3525 C CZ  . PHE B 150 ? 0.3109 0.6414 0.4935 0.0689  0.0276  0.1398  150 PHE B CZ  
3526 N N   . ASN B 151 ? 0.3096 0.7720 0.4551 0.0906  -0.0141 0.1679  151 ASN B N   
3527 C CA  . ASN B 151 ? 0.4065 0.8978 0.5658 0.0921  -0.0216 0.1704  151 ASN B CA  
3528 C C   . ASN B 151 ? 0.4492 0.9404 0.6167 0.1119  -0.0103 0.1903  151 ASN B C   
3529 O O   . ASN B 151 ? 0.4270 0.9097 0.5838 0.1271  -0.0006 0.2053  151 ASN B O   
3530 C CB  . ASN B 151 ? 0.3724 0.9082 0.5246 0.0893  -0.0373 0.1679  151 ASN B CB  
3531 C CG  . ASN B 151 ? 0.3586 0.8915 0.5025 0.0680  -0.0477 0.1466  151 ASN B CG  
3532 O OD1 . ASN B 151 ? 0.3650 0.8950 0.4917 0.0648  -0.0509 0.1418  151 ASN B OD1 
3533 N ND2 . ASN B 151 ? 0.3597 0.8892 0.5138 0.0542  -0.0516 0.1340  151 ASN B ND2 
3534 N N   . ILE B 152 ? 0.4753 0.9752 0.6600 0.1122  -0.0109 0.1907  152 ILE B N   
3535 C CA  . ILE B 152 ? 0.5608 1.0643 0.7538 0.1318  -0.0013 0.2089  152 ILE B CA  
3536 C C   . ILE B 152 ? 0.7205 1.2775 0.9207 0.1385  -0.0136 0.2142  152 ILE B C   
3537 O O   . ILE B 152 ? 0.6618 1.2398 0.8732 0.1234  -0.0245 0.2009  152 ILE B O   
3538 C CB  . ILE B 152 ? 0.5570 1.0290 0.7642 0.1282  0.0090  0.2054  152 ILE B CB  
3539 C CG1 . ILE B 152 ? 0.5036 0.9286 0.7043 0.1194  0.0200  0.1974  152 ILE B CG1 
3540 C CG2 . ILE B 152 ? 0.6832 1.1560 0.8958 0.1502  0.0203  0.2250  152 ILE B CG2 
3541 C CD1 . ILE B 152 ? 0.5122 0.9037 0.7233 0.1208  0.0341  0.1982  152 ILE B CD1 
3542 N N   . ASP B 153 ? 1.0089 1.5868 1.2000 0.1599  -0.0112 0.2321  153 ASP B N   
3543 C CA  . ASP B 153 ? 1.0425 1.6577 1.2306 0.1618  -0.0195 0.2310  153 ASP B CA  
3544 C C   . ASP B 153 ? 1.1598 1.7725 1.3597 0.1689  -0.0128 0.2357  153 ASP B C   
3545 O O   . ASP B 153 ? 1.3010 1.9329 1.5114 0.1557  -0.0210 0.2236  153 ASP B O   
3546 C CB  . ASP B 153 ? 1.0932 1.7242 1.2622 0.1825  -0.0166 0.2467  153 ASP B CB  
3547 C CG  . ASP B 153 ? 1.2253 1.8638 1.3793 0.1776  -0.0236 0.2432  153 ASP B CG  
3548 O OD1 . ASP B 153 ? 1.0805 1.6926 1.2333 0.1723  -0.0206 0.2416  153 ASP B OD1 
3549 O OD2 . ASP B 153 ? 1.1823 1.8541 1.3249 0.1809  -0.0312 0.2429  153 ASP B OD2 
3550 N N   . TYR B 154 ? 1.3071 1.8933 1.5046 0.1888  0.0031  0.2526  154 TYR B N   
3551 C CA  . TYR B 154 ? 1.3131 1.8876 1.5213 0.1952  0.0117  0.2566  154 TYR B CA  
3552 C C   . TYR B 154 ? 1.3185 1.8470 1.5236 0.2098  0.0310  0.2707  154 TYR B C   
3553 O O   . TYR B 154 ? 1.3030 1.8018 1.5209 0.2021  0.0378  0.2654  154 TYR B O   
3554 C CB  . TYR B 154 ? 1.3557 1.9648 1.5600 0.2074  0.0090  0.2627  154 TYR B CB  
3555 C CG  . TYR B 154 ? 1.4066 2.0534 1.6209 0.1865  -0.0078 0.2444  154 TYR B CG  
3556 C CD1 . TYR B 154 ? 1.3536 1.9937 1.5849 0.1707  -0.0102 0.2320  154 TYR B CD1 
3557 C CD2 . TYR B 154 ? 1.3660 2.0527 1.5718 0.1818  -0.0202 0.2389  154 TYR B CD2 
3558 C CE1 . TYR B 154 ? 1.3501 2.0203 1.5891 0.1504  -0.0236 0.2150  154 TYR B CE1 
3559 C CE2 . TYR B 154 ? 1.3230 2.0408 1.5371 0.1607  -0.0338 0.2211  154 TYR B CE2 
3560 C CZ  . TYR B 154 ? 1.3545 2.0631 1.5850 0.1450  -0.0350 0.2096  154 TYR B CZ  
3561 O OH  . TYR B 154 ? 1.3435 2.0797 1.5807 0.1235  -0.0465 0.1922  154 TYR B OH  
3562 N N   . ASP B 155 ? 1.0706 1.5924 1.2573 0.2310  0.0410  0.2883  155 ASP B N   
3563 C CA  . ASP B 155 ? 1.0410 1.5163 1.2189 0.2449  0.0612  0.3026  155 ASP B CA  
3564 C C   . ASP B 155 ? 0.9130 1.3755 1.0818 0.2419  0.0620  0.3041  155 ASP B C   
3565 O O   . ASP B 155 ? 0.8233 1.2353 0.9824 0.2404  0.0795  0.3062  155 ASP B O   
3566 C CB  . ASP B 155 ? 0.9466 1.4142 1.1063 0.2714  0.0758  0.3220  155 ASP B CB  
3567 C CG  . ASP B 155 ? 0.9318 1.4347 1.0739 0.2833  0.0689  0.3288  155 ASP B CG  
3568 O OD1 . ASP B 155 ? 0.9597 1.4897 1.1019 0.2710  0.0537  0.3193  155 ASP B OD1 
3569 O OD2 . ASP B 155 ? 0.9248 1.4283 1.0520 0.3055  0.0795  0.3432  155 ASP B OD2 
3570 N N   . CYS B 156 ? 0.8564 1.3526 1.0212 0.2323  0.0454  0.2956  156 CYS B N   
3571 C CA  . CYS B 156 ? 0.7463 1.2316 0.8916 0.2311  0.0468  0.2972  156 CYS B CA  
3572 C C   . CYS B 156 ? 0.6288 1.1042 0.7781 0.2020  0.0378  0.2737  156 CYS B C   
3573 O O   . CYS B 156 ? 0.6249 1.1336 0.7835 0.1877  0.0200  0.2596  156 CYS B O   
3574 C CB  . CYS B 156 ? 0.6972 1.2259 0.8287 0.2431  0.0364  0.3043  156 CYS B CB  
3575 S SG  . CYS B 156 ? 0.6858 1.2052 0.7925 0.2493  0.0393  0.3128  156 CYS B SG  
3576 N N   . VAL B 157 ? 0.5522 0.9823 0.6929 0.1935  0.0509  0.2695  157 VAL B N   
3577 C CA  . VAL B 157 ? 0.4916 0.9113 0.6322 0.1697  0.0441  0.2490  157 VAL B CA  
3578 C C   . VAL B 157 ? 0.4704 0.9105 0.5935 0.1706  0.0356  0.2497  157 VAL B C   
3579 O O   . VAL B 157 ? 0.4548 0.8845 0.5603 0.1848  0.0460  0.2645  157 VAL B O   
3580 C CB  . VAL B 157 ? 0.4362 0.8054 0.5754 0.1606  0.0614  0.2434  157 VAL B CB  
3581 C CG1 . VAL B 157 ? 0.4116 0.7738 0.5485 0.1396  0.0549  0.2236  157 VAL B CG1 
3582 C CG2 . VAL B 157 ? 0.4693 0.8192 0.6253 0.1582  0.0689  0.2406  157 VAL B CG2 
3583 N N   . SER B 158 ? 0.4431 0.9114 0.5692 0.1559  0.0174  0.2342  158 SER B N   
3584 C CA  . SER B 158 ? 0.3945 0.8794 0.5036 0.1533  0.0087  0.2312  158 SER B CA  
3585 C C   . SER B 158 ? 0.4023 0.8588 0.5083 0.1338  0.0101  0.2132  158 SER B C   
3586 O O   . SER B 158 ? 0.3417 0.7980 0.4574 0.1169  0.0013  0.1954  158 SER B O   
3587 C CB  . SER B 158 ? 0.3686 0.9036 0.4797 0.1496  -0.0114 0.2252  158 SER B CB  
3588 O OG  . SER B 158 ? 0.4356 1.0035 0.5426 0.1713  -0.0128 0.2437  158 SER B OG  
3589 N N   . PHE B 159 ? 0.3806 0.8118 0.4725 0.1371  0.0225  0.2183  159 PHE B N   
3590 C CA  . PHE B 159 ? 0.4022 0.8120 0.4896 0.1210  0.0240  0.2022  159 PHE B CA  
3591 C C   . PHE B 159 ? 0.3713 0.8056 0.4442 0.1164  0.0100  0.1950  159 PHE B C   
3592 O O   . PHE B 159 ? 0.3905 0.8428 0.4492 0.1286  0.0086  0.2074  159 PHE B O   
3593 C CB  . PHE B 159 ? 0.4274 0.8019 0.5065 0.1245  0.0445  0.2095  159 PHE B CB  
3594 C CG  . PHE B 159 ? 0.3865 0.7312 0.4782 0.1255  0.0600  0.2131  159 PHE B CG  
3595 C CD1 . PHE B 159 ? 0.3649 0.6933 0.4710 0.1103  0.0607  0.1965  159 PHE B CD1 
3596 C CD2 . PHE B 159 ? 0.4115 0.7430 0.4980 0.1425  0.0748  0.2333  159 PHE B CD2 
3597 C CE1 . PHE B 159 ? 0.3662 0.6680 0.4828 0.1103  0.0750  0.1988  159 PHE B CE1 
3598 C CE2 . PHE B 159 ? 0.4149 0.7160 0.5106 0.1426  0.0903  0.2359  159 PHE B CE2 
3599 C CZ  . PHE B 159 ? 0.3919 0.6790 0.5031 0.1259  0.0902  0.2184  159 PHE B CZ  
3600 N N   . CYS B 160 ? 0.3539 0.7875 0.4285 0.0996  0.0002  0.1751  160 CYS B N   
3601 C CA  . CYS B 160 ? 0.3571 0.8108 0.4166 0.0937  -0.0129 0.1661  160 CYS B CA  
3602 C C   . CYS B 160 ? 0.3524 0.7853 0.4027 0.0821  -0.0112 0.1505  160 CYS B C   
3603 O O   . CYS B 160 ? 0.3863 0.8311 0.4205 0.0790  -0.0193 0.1444  160 CYS B O   
3604 C CB  . CYS B 160 ? 0.3463 0.8275 0.4118 0.0849  -0.0298 0.1559  160 CYS B CB  
3605 S SG  . CYS B 160 ? 0.3370 0.7972 0.4190 0.0688  -0.0312 0.1382  160 CYS B SG  
3606 N N   . TYR B 161 ? 0.3417 0.7463 0.4010 0.0762  -0.0012 0.1434  161 TYR B N   
3607 C CA  . TYR B 161 ? 0.3358 0.7262 0.3878 0.0662  -0.0013 0.1271  161 TYR B CA  
3608 C C   . TYR B 161 ? 0.3414 0.7060 0.4006 0.0652  0.0151  0.1268  161 TYR B C   
3609 O O   . TYR B 161 ? 0.3258 0.6779 0.4007 0.0653  0.0224  0.1294  161 TYR B O   
3610 C CB  . TYR B 161 ? 0.3200 0.7096 0.3761 0.0546  -0.0126 0.1095  161 TYR B CB  
3611 C CG  . TYR B 161 ? 0.3154 0.6893 0.3627 0.0469  -0.0124 0.0925  161 TYR B CG  
3612 C CD1 . TYR B 161 ? 0.3259 0.7060 0.3530 0.0451  -0.0187 0.0853  161 TYR B CD1 
3613 C CD2 . TYR B 161 ? 0.3018 0.6563 0.3602 0.0426  -0.0064 0.0832  161 TYR B CD2 
3614 C CE1 . TYR B 161 ? 0.3234 0.6898 0.3415 0.0406  -0.0181 0.0701  161 TYR B CE1 
3615 C CE2 . TYR B 161 ? 0.2988 0.6426 0.3489 0.0383  -0.0064 0.0682  161 TYR B CE2 
3616 C CZ  . TYR B 161 ? 0.3190 0.6683 0.3487 0.0380  -0.0120 0.0620  161 TYR B CZ  
3617 O OH  . TYR B 161 ? 0.3282 0.6669 0.3487 0.0360  -0.0114 0.0472  161 TYR B OH  
3618 N N   . MET B 162 ? 0.3553 0.7132 0.4033 0.0629  0.0204  0.1212  162 MET B N   
3619 C CA  . MET B 162 ? 0.3361 0.6744 0.3906 0.0582  0.0345  0.1153  162 MET B CA  
3620 C C   . MET B 162 ? 0.3278 0.6667 0.3751 0.0509  0.0288  0.0967  162 MET B C   
3621 O O   . MET B 162 ? 0.3364 0.6854 0.3670 0.0520  0.0224  0.0939  162 MET B O   
3622 C CB  . MET B 162 ? 0.3571 0.6875 0.4039 0.0635  0.0508  0.1286  162 MET B CB  
3623 C CG  . MET B 162 ? 0.3563 0.6701 0.4087 0.0555  0.0665  0.1205  162 MET B CG  
3624 S SD  . MET B 162 ? 0.4175 0.7146 0.4620 0.0600  0.0897  0.1383  162 MET B SD  
3625 C CE  . MET B 162 ? 0.3840 0.6604 0.4464 0.0603  0.1003  0.1449  162 MET B CE  
3626 N N   . HIS B 163 ? 0.3133 0.6416 0.3718 0.0448  0.0318  0.0841  163 HIS B N   
3627 C CA  . HIS B 163 ? 0.3132 0.6423 0.3642 0.0408  0.0262  0.0666  163 HIS B CA  
3628 C C   . HIS B 163 ? 0.3840 0.7150 0.4278 0.0403  0.0361  0.0632  163 HIS B C   
3629 O O   . HIS B 163 ? 0.3562 0.6812 0.4088 0.0382  0.0508  0.0677  163 HIS B O   
3630 C CB  . HIS B 163 ? 0.3276 0.6472 0.3921 0.0365  0.0261  0.0549  163 HIS B CB  
3631 C CG  . HIS B 163 ? 0.3978 0.7174 0.4524 0.0355  0.0201  0.0377  163 HIS B CG  
3632 N ND1 . HIS B 163 ? 0.3403 0.6623 0.3771 0.0366  0.0078  0.0319  163 HIS B ND1 
3633 C CD2 . HIS B 163 ? 0.3772 0.6954 0.4354 0.0344  0.0252  0.0249  163 HIS B CD2 
3634 C CE1 . HIS B 163 ? 0.3949 0.7133 0.4230 0.0377  0.0062  0.0172  163 HIS B CE1 
3635 N NE2 . HIS B 163 ? 0.3788 0.6973 0.4203 0.0372  0.0161  0.0129  163 HIS B NE2 
3636 N N   . HIS B 164 ? 0.3196 0.6581 0.3462 0.0414  0.0288  0.0540  164 HIS B N   
3637 C CA  . HIS B 164 ? 0.3682 0.7124 0.3862 0.0416  0.0367  0.0492  164 HIS B CA  
3638 C C   . HIS B 164 ? 0.4672 0.8144 0.4787 0.0417  0.0324  0.0308  164 HIS B C   
3639 O O   . HIS B 164 ? 0.4526 0.8060 0.4666 0.0404  0.0419  0.0244  164 HIS B O   
3640 C CB  . HIS B 164 ? 0.3566 0.7091 0.3561 0.0459  0.0345  0.0578  164 HIS B CB  
3641 C CG  . HIS B 164 ? 0.3582 0.7093 0.3595 0.0486  0.0439  0.0765  164 HIS B CG  
3642 N ND1 . HIS B 164 ? 0.3735 0.7250 0.3686 0.0492  0.0573  0.0831  164 HIS B ND1 
3643 C CD2 . HIS B 164 ? 0.3610 0.7100 0.3677 0.0522  0.0423  0.0906  164 HIS B CD2 
3644 C CE1 . HIS B 164 ? 0.3873 0.7338 0.3816 0.0538  0.0641  0.1011  164 HIS B CE1 
3645 N NE2 . HIS B 164 ? 0.3795 0.7255 0.3813 0.0565  0.0550  0.1060  164 HIS B NE2 
3646 N N   . MET B 165 ? 0.4420 0.7853 0.4430 0.0436  0.0193  0.0223  165 MET B N   
3647 C CA  . MET B 165 ? 0.4475 0.7917 0.4362 0.0471  0.0162  0.0064  165 MET B CA  
3648 C C   . MET B 165 ? 0.4444 0.7761 0.4239 0.0484  0.0048  -0.0029 165 MET B C   
3649 O O   . MET B 165 ? 0.4516 0.7770 0.4296 0.0452  -0.0029 0.0023  165 MET B O   
3650 C CB  . MET B 165 ? 0.4579 0.8105 0.4258 0.0510  0.0155  0.0057  165 MET B CB  
3651 C CG  . MET B 165 ? 0.4520 0.8025 0.4024 0.0514  0.0050  0.0108  165 MET B CG  
3652 S SD  . MET B 165 ? 0.6971 1.0597 0.6270 0.0555  0.0080  0.0141  165 MET B SD  
3653 C CE  . MET B 165 ? 0.6598 1.0186 0.5711 0.0617  0.0050  -0.0055 165 MET B CE  
3654 N N   . GLU B 166 ? 0.4231 0.7518 0.3944 0.0536  0.0043  -0.0170 166 GLU B N   
3655 C CA  . GLU B 166 ? 0.4649 0.7772 0.4195 0.0565  -0.0047 -0.0267 166 GLU B CA  
3656 C C   . GLU B 166 ? 0.5522 0.8615 0.4775 0.0629  -0.0084 -0.0346 166 GLU B C   
3657 O O   . GLU B 166 ? 0.5098 0.8323 0.4308 0.0681  -0.0030 -0.0372 166 GLU B O   
3658 C CB  . GLU B 166 ? 0.5094 0.8160 0.4729 0.0604  -0.0023 -0.0363 166 GLU B CB  
3659 C CG  . GLU B 166 ? 0.5134 0.7990 0.4556 0.0656  -0.0091 -0.0466 166 GLU B CG  
3660 C CD  . GLU B 166 ? 0.5725 0.8522 0.5255 0.0693  -0.0069 -0.0532 166 GLU B CD  
3661 O OE1 . GLU B 166 ? 0.7637 1.0380 0.7005 0.0803  -0.0068 -0.0642 166 GLU B OE1 
3662 O OE2 . GLU B 166 ? 0.5972 0.8778 0.5730 0.0629  -0.0050 -0.0476 166 GLU B OE2 
3663 N N   . LEU B 167 ? 0.5529 0.8446 0.4574 0.0617  -0.0167 -0.0387 167 LEU B N   
3664 C CA  . LEU B 167 ? 0.5886 0.8719 0.4616 0.0670  -0.0200 -0.0466 167 LEU B CA  
3665 C C   . LEU B 167 ? 0.5986 0.8638 0.4539 0.0773  -0.0193 -0.0602 167 LEU B C   
3666 O O   . LEU B 167 ? 0.6056 0.8634 0.4718 0.0789  -0.0181 -0.0632 167 LEU B O   
3667 C CB  . LEU B 167 ? 0.5499 0.8237 0.4071 0.0581  -0.0284 -0.0443 167 LEU B CB  
3668 C CG  . LEU B 167 ? 0.5086 0.8025 0.3768 0.0511  -0.0303 -0.0308 167 LEU B CG  
3669 C CD1 . LEU B 167 ? 0.5064 0.7957 0.3566 0.0427  -0.0395 -0.0315 167 LEU B CD1 
3670 C CD2 . LEU B 167 ? 0.5199 0.8310 0.3868 0.0572  -0.0243 -0.0268 167 LEU B CD2 
3671 N N   . PRO B 168 ? 0.5846 0.8416 0.4103 0.0860  -0.0196 -0.0684 168 PRO B N   
3672 C CA  . PRO B 168 ? 0.6252 0.8624 0.4293 0.0990  -0.0181 -0.0806 168 PRO B CA  
3673 C C   . PRO B 168 ? 0.6563 0.8624 0.4496 0.0948  -0.0216 -0.0842 168 PRO B C   
3674 O O   . PRO B 168 ? 0.6336 0.8282 0.4250 0.1038  -0.0190 -0.0900 168 PRO B O   
3675 C CB  . PRO B 168 ? 0.6350 0.8649 0.4055 0.1072  -0.0180 -0.0868 168 PRO B CB  
3676 C CG  . PRO B 168 ? 0.7118 0.9606 0.4882 0.0982  -0.0196 -0.0784 168 PRO B CG  
3677 C CD  . PRO B 168 ? 0.6860 0.9520 0.4962 0.0858  -0.0204 -0.0663 168 PRO B CD  
3678 N N   . THR B 169 ? 0.6522 0.8459 0.4377 0.0810  -0.0270 -0.0814 169 THR B N   
3679 C CA  . THR B 169 ? 0.6654 0.8306 0.4416 0.0739  -0.0294 -0.0851 169 THR B CA  
3680 C C   . THR B 169 ? 0.6581 0.8298 0.4653 0.0707  -0.0284 -0.0800 169 THR B C   
3681 O O   . THR B 169 ? 0.6752 0.8234 0.4762 0.0665  -0.0290 -0.0833 169 THR B O   
3682 C CB  . THR B 169 ? 0.6543 0.8137 0.4204 0.0572  -0.0354 -0.0834 169 THR B CB  
3683 O OG1 . THR B 169 ? 0.6567 0.8488 0.4521 0.0488  -0.0385 -0.0713 169 THR B OG1 
3684 C CG2 . THR B 169 ? 0.6741 0.8192 0.4023 0.0597  -0.0360 -0.0913 169 THR B CG2 
3685 N N   . GLY B 170 ? 0.6034 0.8043 0.4424 0.0719  -0.0259 -0.0724 170 GLY B N   
3686 C CA  . GLY B 170 ? 0.5753 0.7812 0.4429 0.0679  -0.0246 -0.0677 170 GLY B CA  
3687 C C   . GLY B 170 ? 0.5988 0.8133 0.4867 0.0530  -0.0284 -0.0571 170 GLY B C   
3688 O O   . GLY B 170 ? 0.5931 0.8061 0.5006 0.0489  -0.0278 -0.0537 170 GLY B O   
3689 N N   . VAL B 171 ? 0.5618 0.7863 0.4445 0.0461  -0.0324 -0.0518 171 VAL B N   
3690 C CA  . VAL B 171 ? 0.5323 0.7721 0.4351 0.0350  -0.0359 -0.0404 171 VAL B CA  
3691 C C   . VAL B 171 ? 0.5359 0.8016 0.4587 0.0378  -0.0317 -0.0294 171 VAL B C   
3692 O O   . VAL B 171 ? 0.4816 0.7538 0.4024 0.0458  -0.0263 -0.0318 171 VAL B O   
3693 C CB  . VAL B 171 ? 0.5325 0.7685 0.4155 0.0250  -0.0432 -0.0422 171 VAL B CB  
3694 C CG1 . VAL B 171 ? 0.5772 0.7825 0.4387 0.0198  -0.0450 -0.0539 171 VAL B CG1 
3695 C CG2 . VAL B 171 ? 0.4848 0.7267 0.3470 0.0288  -0.0442 -0.0443 171 VAL B CG2 
3696 N N   . HIS B 172 ? 0.4629 0.7437 0.4033 0.0315  -0.0333 -0.0171 172 HIS B N   
3697 C CA  . HIS B 172 ? 0.4111 0.7099 0.3721 0.0343  -0.0267 -0.0052 172 HIS B CA  
3698 C C   . HIS B 172 ? 0.4134 0.7292 0.3709 0.0324  -0.0299 0.0058  172 HIS B C   
3699 O O   . HIS B 172 ? 0.3643 0.6834 0.3133 0.0266  -0.0383 0.0063  172 HIS B O   
3700 C CB  . HIS B 172 ? 0.3927 0.6906 0.3802 0.0324  -0.0225 0.0006  172 HIS B CB  
3701 C CG  . HIS B 172 ? 0.4406 0.7240 0.4311 0.0351  -0.0195 -0.0102 172 HIS B CG  
3702 N ND1 . HIS B 172 ? 0.4571 0.7263 0.4491 0.0318  -0.0231 -0.0146 172 HIS B ND1 
3703 C CD2 . HIS B 172 ? 0.4320 0.7155 0.4241 0.0414  -0.0131 -0.0175 172 HIS B CD2 
3704 C CE1 . HIS B 172 ? 0.4468 0.7062 0.4398 0.0371  -0.0192 -0.0235 172 HIS B CE1 
3705 N NE2 . HIS B 172 ? 0.4412 0.7110 0.4351 0.0431  -0.0135 -0.0258 172 HIS B NE2 
3706 N N   . ALA B 173 ? 0.3448 0.6723 0.3071 0.0371  -0.0226 0.0138  173 ALA B N   
3707 C CA  . ALA B 173 ? 0.3716 0.7152 0.3282 0.0381  -0.0241 0.0253  173 ALA B CA  
3708 C C   . ALA B 173 ? 0.3539 0.7050 0.3290 0.0416  -0.0134 0.0400  173 ALA B C   
3709 O O   . ALA B 173 ? 0.3319 0.6771 0.3191 0.0425  -0.0033 0.0382  173 ALA B O   
3710 C CB  . ALA B 173 ? 0.4287 0.7750 0.3609 0.0413  -0.0253 0.0194  173 ALA B CB  
3711 N N   . GLY B 174 ? 0.3772 0.7413 0.3524 0.0437  -0.0148 0.0541  174 GLY B N   
3712 C CA  . GLY B 174 ? 0.3481 0.7147 0.3360 0.0483  -0.0032 0.0695  174 GLY B CA  
3713 C C   . GLY B 174 ? 0.3626 0.7451 0.3430 0.0539  -0.0060 0.0847  174 GLY B C   
3714 O O   . GLY B 174 ? 0.3818 0.7768 0.3457 0.0537  -0.0167 0.0822  174 GLY B O   
3715 N N   . THR B 175 ? 0.3660 0.7472 0.3567 0.0596  0.0045  0.1004  175 THR B N   
3716 C CA  . THR B 175 ? 0.3838 0.7788 0.3653 0.0687  0.0051  0.1173  175 THR B CA  
3717 C C   . THR B 175 ? 0.3816 0.7826 0.3765 0.0741  0.0042  0.1304  175 THR B C   
3718 O O   . THR B 175 ? 0.3669 0.7572 0.3797 0.0706  0.0068  0.1278  175 THR B O   
3719 C CB  . THR B 175 ? 0.3992 0.7853 0.3744 0.0741  0.0216  0.1277  175 THR B CB  
3720 O OG1 . THR B 175 ? 0.3945 0.7622 0.3864 0.0732  0.0362  0.1328  175 THR B OG1 
3721 C CG2 . THR B 175 ? 0.4015 0.7848 0.3645 0.0693  0.0237  0.1148  175 THR B CG2 
3722 N N   . ASP B 176 ? 0.3974 0.8175 0.3828 0.0838  0.0004  0.1442  176 ASP B N   
3723 C CA  . ASP B 176 ? 0.4025 0.8288 0.3973 0.0943  0.0039  0.1614  176 ASP B CA  
3724 C C   . ASP B 176 ? 0.4153 0.8178 0.4114 0.1017  0.0246  0.1752  176 ASP B C   
3725 O O   . ASP B 176 ? 0.4213 0.8078 0.4104 0.0980  0.0352  0.1717  176 ASP B O   
3726 C CB  . ASP B 176 ? 0.4177 0.8760 0.3998 0.1040  -0.0071 0.1714  176 ASP B CB  
3727 C CG  . ASP B 176 ? 0.4417 0.9027 0.4022 0.1135  -0.0011 0.1815  176 ASP B CG  
3728 O OD1 . ASP B 176 ? 0.4507 0.8873 0.4078 0.1156  0.0153  0.1869  176 ASP B OD1 
3729 O OD2 . ASP B 176 ? 0.4535 0.9418 0.3994 0.1183  -0.0123 0.1838  176 ASP B OD2 
3730 N N   . LEU B 177 ? 0.4293 0.8291 0.4330 0.1123  0.0314  0.1909  177 LEU B N   
3731 C CA  . LEU B 177 ? 0.4376 0.8079 0.4415 0.1172  0.0533  0.2023  177 LEU B CA  
3732 C C   . LEU B 177 ? 0.4676 0.8347 0.4493 0.1277  0.0636  0.2165  177 LEU B C   
3733 O O   . LEU B 177 ? 0.4859 0.8257 0.4632 0.1304  0.0838  0.2257  177 LEU B O   
3734 C CB  . LEU B 177 ? 0.4402 0.8025 0.4565 0.1263  0.0600  0.2150  177 LEU B CB  
3735 C CG  . LEU B 177 ? 0.4201 0.7632 0.4575 0.1143  0.0640  0.2029  177 LEU B CG  
3736 C CD1 . LEU B 177 ? 0.4238 0.7350 0.4619 0.1053  0.0830  0.1980  177 LEU B CD1 
3737 C CD2 . LEU B 177 ? 0.3904 0.7496 0.4372 0.1006  0.0456  0.1821  177 LEU B CD2 
3738 N N   . GLU B 178 ? 0.4756 0.8688 0.4419 0.1335  0.0512  0.2186  178 GLU B N   
3739 C CA  . GLU B 178 ? 0.5028 0.8938 0.4461 0.1417  0.0598  0.2290  178 GLU B CA  
3740 C C   . GLU B 178 ? 0.4976 0.8823 0.4341 0.1284  0.0610  0.2134  178 GLU B C   
3741 O O   . GLU B 178 ? 0.5195 0.9009 0.4373 0.1333  0.0693  0.2205  178 GLU B O   
3742 C CB  . GLU B 178 ? 0.5158 0.9410 0.4447 0.1556  0.0457  0.2389  178 GLU B CB  
3743 C CG  . GLU B 178 ? 0.5589 0.9854 0.4806 0.1772  0.0541  0.2632  178 GLU B CG  
3744 C CD  . GLU B 178 ? 0.7386 1.2091 0.6564 0.1891  0.0353  0.2687  178 GLU B CD  
3745 O OE1 . GLU B 178 ? 0.7901 1.2690 0.7092 0.2065  0.0379  0.2855  178 GLU B OE1 
3746 O OE2 . GLU B 178 ? 0.7524 1.2504 0.6654 0.1811  0.0181  0.2558  178 GLU B OE2 
3747 N N   . GLY B 179 ? 0.4708 0.8547 0.4209 0.1131  0.0532  0.1929  179 GLY B N   
3748 C CA  . GLY B 179 ? 0.4814 0.8596 0.4265 0.1019  0.0553  0.1775  179 GLY B CA  
3749 C C   . GLY B 179 ? 0.4618 0.8614 0.3936 0.0991  0.0382  0.1656  179 GLY B C   
3750 O O   . GLY B 179 ? 0.4603 0.8563 0.3854 0.0924  0.0403  0.1538  179 GLY B O   
3751 N N   . ASN B 180 ? 0.4626 0.8853 0.3893 0.1040  0.0222  0.1680  180 ASN B N   
3752 C CA  . ASN B 180 ? 0.4630 0.9043 0.3750 0.0998  0.0066  0.1559  180 ASN B CA  
3753 C C   . ASN B 180 ? 0.4398 0.8788 0.3634 0.0871  -0.0046 0.1365  180 ASN B C   
3754 O O   . ASN B 180 ? 0.4271 0.8690 0.3664 0.0852  -0.0097 0.1369  180 ASN B O   
3755 C CB  . ASN B 180 ? 0.4782 0.9480 0.3779 0.1098  -0.0046 0.1666  180 ASN B CB  
3756 C CG  . ASN B 180 ? 0.5043 0.9745 0.3897 0.1248  0.0070  0.1869  180 ASN B CG  
3757 O OD1 . ASN B 180 ? 0.5186 0.9838 0.3873 0.1261  0.0132  0.1871  180 ASN B OD1 
3758 N ND2 . ASN B 180 ? 0.5129 0.9864 0.4037 0.1373  0.0117  0.2047  180 ASN B ND2 
3759 N N   . PHE B 181 ? 0.4359 0.8679 0.3512 0.0793  -0.0069 0.1201  181 PHE B N   
3760 C CA  . PHE B 181 ? 0.4183 0.8434 0.3409 0.0688  -0.0156 0.1022  181 PHE B CA  
3761 C C   . PHE B 181 ? 0.4189 0.8618 0.3379 0.0651  -0.0320 0.0985  181 PHE B C   
3762 O O   . PHE B 181 ? 0.4342 0.8978 0.3387 0.0688  -0.0395 0.1034  181 PHE B O   
3763 C CB  . PHE B 181 ? 0.4198 0.8357 0.3287 0.0642  -0.0155 0.0860  181 PHE B CB  
3764 C CG  . PHE B 181 ? 0.4067 0.8049 0.3284 0.0616  -0.0038 0.0791  181 PHE B CG  
3765 C CD1 . PHE B 181 ? 0.4131 0.8074 0.3352 0.0647  0.0109  0.0852  181 PHE B CD1 
3766 C CD2 . PHE B 181 ? 0.3905 0.7773 0.3220 0.0555  -0.0074 0.0656  181 PHE B CD2 
3767 C CE1 . PHE B 181 ? 0.4019 0.7855 0.3361 0.0608  0.0213  0.0769  181 PHE B CE1 
3768 C CE2 . PHE B 181 ? 0.3790 0.7545 0.3220 0.0538  0.0025  0.0582  181 PHE B CE2 
3769 C CZ  . PHE B 181 ? 0.4007 0.7765 0.3459 0.0559  0.0165  0.0632  181 PHE B CZ  
3770 N N   . TYR B 182 ? 0.4034 0.8392 0.3351 0.0571  -0.0371 0.0889  182 TYR B N   
3771 C CA  . TYR B 182 ? 0.4059 0.8528 0.3298 0.0484  -0.0517 0.0778  182 TYR B CA  
3772 C C   . TYR B 182 ? 0.4227 0.8554 0.3262 0.0423  -0.0546 0.0602  182 TYR B C   
3773 O O   . TYR B 182 ? 0.4139 0.8245 0.3202 0.0412  -0.0480 0.0516  182 TYR B O   
3774 C CB  . TYR B 182 ? 0.3893 0.8310 0.3324 0.0417  -0.0546 0.0739  182 TYR B CB  
3775 C CG  . TYR B 182 ? 0.3833 0.8399 0.3458 0.0490  -0.0521 0.0910  182 TYR B CG  
3776 C CD1 . TYR B 182 ? 0.3906 0.8774 0.3524 0.0504  -0.0617 0.0974  182 TYR B CD1 
3777 C CD2 . TYR B 182 ? 0.3721 0.8130 0.3527 0.0546  -0.0396 0.1000  182 TYR B CD2 
3778 C CE1 . TYR B 182 ? 0.4103 0.9121 0.3879 0.0596  -0.0592 0.1133  182 TYR B CE1 
3779 C CE2 . TYR B 182 ? 0.3704 0.8217 0.3659 0.0628  -0.0362 0.1159  182 TYR B CE2 
3780 C CZ  . TYR B 182 ? 0.4140 0.8962 0.4077 0.0664  -0.0463 0.1230  182 TYR B CZ  
3781 O OH  . TYR B 182 ? 0.3877 0.8833 0.3947 0.0772  -0.0432 0.1395  182 TYR B OH  
3782 N N   . GLY B 183 ? 0.4309 0.8766 0.3132 0.0389  -0.0640 0.0545  183 GLY B N   
3783 C CA  . GLY B 183 ? 0.4428 0.8734 0.3023 0.0336  -0.0666 0.0378  183 GLY B CA  
3784 C C   . GLY B 183 ? 0.4944 0.9246 0.3375 0.0418  -0.0607 0.0402  183 GLY B C   
3785 O O   . GLY B 183 ? 0.4664 0.9105 0.3126 0.0506  -0.0555 0.0553  183 GLY B O   
3786 N N   . PRO B 184 ? 0.4702 0.8839 0.2932 0.0397  -0.0608 0.0254  184 PRO B N   
3787 C CA  . PRO B 184 ? 0.5017 0.9169 0.3071 0.0471  -0.0556 0.0263  184 PRO B CA  
3788 C C   . PRO B 184 ? 0.4861 0.8895 0.3022 0.0539  -0.0425 0.0277  184 PRO B C   
3789 O O   . PRO B 184 ? 0.5686 0.9717 0.3701 0.0592  -0.0373 0.0254  184 PRO B O   
3790 C CB  . PRO B 184 ? 0.5270 0.9294 0.3040 0.0414  -0.0624 0.0082  184 PRO B CB  
3791 C CG  . PRO B 184 ? 0.5041 0.8837 0.2896 0.0357  -0.0624 -0.0027 184 PRO B CG  
3792 C CD  . PRO B 184 ? 0.4943 0.8846 0.3086 0.0322  -0.0638 0.0079  184 PRO B CD  
3793 N N   . PHE B 185 ? 0.4472 0.8440 0.2884 0.0534  -0.0366 0.0315  185 PHE B N   
3794 C CA  . PHE B 185 ? 0.4354 0.8218 0.2879 0.0568  -0.0252 0.0284  185 PHE B CA  
3795 C C   . PHE B 185 ? 0.4364 0.8322 0.2966 0.0623  -0.0127 0.0418  185 PHE B C   
3796 O O   . PHE B 185 ? 0.4425 0.8492 0.3051 0.0648  -0.0114 0.0570  185 PHE B O   
3797 C CB  . PHE B 185 ? 0.4601 0.8359 0.3351 0.0529  -0.0244 0.0261  185 PHE B CB  
3798 C CG  . PHE B 185 ? 0.4951 0.8598 0.3618 0.0467  -0.0351 0.0144  185 PHE B CG  
3799 C CD1 . PHE B 185 ? 0.5349 0.8848 0.3795 0.0471  -0.0378 -0.0012 185 PHE B CD1 
3800 C CD2 . PHE B 185 ? 0.4688 0.8376 0.3467 0.0405  -0.0418 0.0191  185 PHE B CD2 
3801 C CE1 . PHE B 185 ? 0.5892 0.9240 0.4222 0.0405  -0.0457 -0.0121 185 PHE B CE1 
3802 C CE2 . PHE B 185 ? 0.4918 0.8497 0.3607 0.0326  -0.0504 0.0076  185 PHE B CE2 
3803 C CZ  . PHE B 185 ? 0.5481 0.8869 0.3937 0.0320  -0.0519 -0.0080 185 PHE B CZ  
3804 N N   . VAL B 186 ? 0.4329 0.8248 0.2954 0.0646  -0.0026 0.0357  186 VAL B N   
3805 C CA  . VAL B 186 ? 0.4345 0.8323 0.3055 0.0668  0.0120  0.0459  186 VAL B CA  
3806 C C   . VAL B 186 ? 0.4485 0.8407 0.3410 0.0637  0.0218  0.0398  186 VAL B C   
3807 O O   . VAL B 186 ? 0.4253 0.8118 0.3196 0.0632  0.0175  0.0257  186 VAL B O   
3808 C CB  . VAL B 186 ? 0.4523 0.8582 0.3030 0.0714  0.0166  0.0446  186 VAL B CB  
3809 C CG1 . VAL B 186 ? 0.4718 0.8857 0.3007 0.0746  0.0075  0.0518  186 VAL B CG1 
3810 C CG2 . VAL B 186 ? 0.5148 0.9179 0.3563 0.0732  0.0152  0.0263  186 VAL B CG2 
3811 N N   . ASP B 187 ? 0.4157 0.8087 0.3229 0.0618  0.0358  0.0504  187 ASP B N   
3812 C CA  . ASP B 187 ? 0.4293 0.8191 0.3581 0.0568  0.0464  0.0446  187 ASP B CA  
3813 C C   . ASP B 187 ? 0.4785 0.8789 0.4033 0.0567  0.0563  0.0352  187 ASP B C   
3814 O O   . ASP B 187 ? 0.4369 0.8414 0.3644 0.0538  0.0709  0.0419  187 ASP B O   
3815 C CB  . ASP B 187 ? 0.3998 0.7819 0.3456 0.0531  0.0575  0.0590  187 ASP B CB  
3816 C CG  . ASP B 187 ? 0.4216 0.8041 0.3571 0.0560  0.0676  0.0758  187 ASP B CG  
3817 O OD1 . ASP B 187 ? 0.4556 0.8464 0.3713 0.0606  0.0654  0.0774  187 ASP B OD1 
3818 O OD2 . ASP B 187 ? 0.4263 0.7987 0.3720 0.0543  0.0790  0.0881  187 ASP B OD2 
3819 N N   . ARG B 188 ? 0.5064 0.9111 0.4222 0.0607  0.0486  0.0195  188 ARG B N   
3820 C CA  . ARG B 188 ? 0.5039 0.9225 0.4187 0.0624  0.0561  0.0072  188 ARG B CA  
3821 C C   . ARG B 188 ? 0.5799 0.9975 0.4948 0.0671  0.0477  -0.0091 188 ARG B C   
3822 O O   . ARG B 188 ? 0.5686 0.9723 0.4743 0.0700  0.0351  -0.0114 188 ARG B O   
3823 C CB  . ARG B 188 ? 0.5455 0.9731 0.4375 0.0678  0.0571  0.0079  188 ARG B CB  
3824 C CG  . ARG B 188 ? 0.5851 1.0056 0.4510 0.0747  0.0425  0.0061  188 ARG B CG  
3825 C CD  . ARG B 188 ? 0.6121 1.0416 0.4566 0.0789  0.0459  0.0102  188 ARG B CD  
3826 N NE  . ARG B 188 ? 0.6200 1.0463 0.4587 0.0774  0.0452  0.0271  188 ARG B NE  
3827 C CZ  . ARG B 188 ? 0.7049 1.1347 0.5204 0.0819  0.0415  0.0321  188 ARG B CZ  
3828 N NH1 . ARG B 188 ? 0.7306 1.1653 0.5255 0.0875  0.0391  0.0217  188 ARG B NH1 
3829 N NH2 . ARG B 188 ? 0.7089 1.1381 0.5207 0.0819  0.0406  0.0480  188 ARG B NH2 
3830 N N   . GLN B 189 ? 0.6206 1.0537 0.5462 0.0675  0.0557  -0.0205 189 GLN B N   
3831 C CA  . GLN B 189 ? 0.5911 1.0264 0.5175 0.0743  0.0501  -0.0358 189 GLN B CA  
3832 C C   . GLN B 189 ? 0.6426 1.0735 0.5404 0.0867  0.0408  -0.0441 189 GLN B C   
3833 O O   . GLN B 189 ? 0.6913 1.1381 0.5820 0.0951  0.0440  -0.0550 189 GLN B O   
3834 C CB  . GLN B 189 ? 0.5730 1.0331 0.5172 0.0724  0.0614  -0.0461 189 GLN B CB  
3835 C CG  . GLN B 189 ? 0.6100 1.0727 0.5632 0.0774  0.0569  -0.0588 189 GLN B CG  
3836 C CD  . GLN B 189 ? 0.7398 1.1927 0.7169 0.0670  0.0589  -0.0543 189 GLN B CD  
3837 O OE1 . GLN B 189 ? 0.6306 1.0658 0.6117 0.0594  0.0587  -0.0408 189 GLN B OE1 
3838 N NE2 . GLN B 189 ? 0.7189 1.1840 0.7105 0.0680  0.0606  -0.0659 189 GLN B NE2 
3839 N N   . THR B 190 ? 0.6524 1.0625 0.5328 0.0876  0.0300  -0.0394 190 THR B N   
3840 C CA  . THR B 190 ? 0.7387 1.1380 0.5883 0.0972  0.0217  -0.0469 190 THR B CA  
3841 C C   . THR B 190 ? 0.7745 1.1482 0.6152 0.0974  0.0108  -0.0503 190 THR B C   
3842 O O   . THR B 190 ? 0.7044 1.0703 0.5617 0.0890  0.0082  -0.0438 190 THR B O   
3843 C CB  . THR B 190 ? 0.7235 1.1238 0.5553 0.0959  0.0207  -0.0388 190 THR B CB  
3844 O OG1 . THR B 190 ? 0.8372 1.2355 0.6404 0.1066  0.0183  -0.0485 190 THR B OG1 
3845 C CG2 . THR B 190 ? 0.6993 1.0833 0.5260 0.0891  0.0111  -0.0303 190 THR B CG2 
3846 N N   . ALA B 191 ? 0.9525 1.3116 0.7649 0.1070  0.0056  -0.0607 191 ALA B N   
3847 C CA  . ALA B 191 ? 0.9482 1.2786 0.7451 0.1061  -0.0034 -0.0650 191 ALA B CA  
3848 C C   . ALA B 191 ? 0.8721 1.1931 0.6528 0.0978  -0.0103 -0.0590 191 ALA B C   
3849 O O   . ALA B 191 ? 0.8785 1.2034 0.6390 0.1013  -0.0101 -0.0598 191 ALA B O   
3850 C CB  . ALA B 191 ? 1.0264 1.3406 0.7964 0.1205  -0.0041 -0.0788 191 ALA B CB  
3851 N N   . GLN B 192 ? 0.7462 1.0583 0.5368 0.0870  -0.0163 -0.0531 192 GLN B N   
3852 C CA  . GLN B 192 ? 0.7511 1.0622 0.5315 0.0780  -0.0233 -0.0468 192 GLN B CA  
3853 C C   . GLN B 192 ? 0.7051 0.9931 0.4746 0.0705  -0.0314 -0.0524 192 GLN B C   
3854 O O   . GLN B 192 ? 0.7072 0.9852 0.4904 0.0687  -0.0314 -0.0542 192 GLN B O   
3855 C CB  . GLN B 192 ? 0.6814 1.0133 0.4875 0.0713  -0.0214 -0.0309 192 GLN B CB  
3856 C CG  . GLN B 192 ? 0.6490 1.0008 0.4638 0.0764  -0.0114 -0.0250 192 GLN B CG  
3857 C CD  . GLN B 192 ? 0.5418 0.9075 0.3815 0.0709  -0.0064 -0.0092 192 GLN B CD  
3858 O OE1 . GLN B 192 ? 0.4642 0.8340 0.3017 0.0669  -0.0113 0.0009  192 GLN B OE1 
3859 N NE2 . GLN B 192 ? 0.4569 0.8295 0.3194 0.0710  0.0037  -0.0073 192 GLN B NE2 
3860 N N   . ALA B 193 ? 0.7088 0.9886 0.4525 0.0656  -0.0376 -0.0561 193 ALA B N   
3861 C CA  . ALA B 193 ? 0.7096 0.9653 0.4358 0.0566  -0.0440 -0.0646 193 ALA B CA  
3862 C C   . ALA B 193 ? 0.6753 0.9461 0.4161 0.0426  -0.0512 -0.0559 193 ALA B C   
3863 O O   . ALA B 193 ? 0.6009 0.8912 0.3381 0.0397  -0.0547 -0.0496 193 ALA B O   
3864 C CB  . ALA B 193 ? 0.7095 0.9453 0.3948 0.0586  -0.0453 -0.0765 193 ALA B CB  
3865 N N   . ALA B 194 ? 0.6445 0.9084 0.4014 0.0352  -0.0533 -0.0552 194 ALA B N   
3866 C CA  . ALA B 194 ? 0.6332 0.9093 0.3984 0.0215  -0.0609 -0.0506 194 ALA B CA  
3867 C C   . ALA B 194 ? 0.6769 0.9364 0.4092 0.0108  -0.0665 -0.0636 194 ALA B C   
3868 O O   . ALA B 194 ? 0.7356 0.9654 0.4397 0.0140  -0.0633 -0.0762 194 ALA B O   
3869 C CB  . ALA B 194 ? 0.5863 0.8593 0.3773 0.0168  -0.0606 -0.0471 194 ALA B CB  
3870 N N   . GLY B 195 ? 0.6629 0.9419 0.3973 -0.0017 -0.0743 -0.0610 195 GLY B N   
3871 C CA  . GLY B 195 ? 0.7418 1.0059 0.4452 -0.0151 -0.0789 -0.0752 195 GLY B CA  
3872 C C   . GLY B 195 ? 0.7590 0.9874 0.4508 -0.0241 -0.0764 -0.0876 195 GLY B C   
3873 O O   . GLY B 195 ? 0.6872 0.9036 0.3961 -0.0188 -0.0718 -0.0849 195 GLY B O   
3874 N N   . THR B 196 ? 0.8205 1.0294 0.4807 -0.0378 -0.0783 -0.1020 196 THR B N   
3875 C CA  . THR B 196 ? 0.8048 0.9876 0.4573 -0.0528 -0.0769 -0.1123 196 THR B CA  
3876 C C   . THR B 196 ? 0.7450 0.9583 0.4357 -0.0611 -0.0818 -0.1022 196 THR B C   
3877 O O   . THR B 196 ? 0.7398 0.9951 0.4501 -0.0639 -0.0890 -0.0927 196 THR B O   
3878 C CB  . THR B 196 ? 0.8182 0.9871 0.4356 -0.0721 -0.0794 -0.1282 196 THR B CB  
3879 O OG1 . THR B 196 ? 0.8066 0.9504 0.3876 -0.0633 -0.0751 -0.1366 196 THR B OG1 
3880 C CG2 . THR B 196 ? 0.7994 0.9336 0.4042 -0.0881 -0.0750 -0.1400 196 THR B CG2 
3881 N N   . ASP B 197 ? 0.7534 0.9458 0.4528 -0.0643 -0.0776 -0.1041 197 ASP B N   
3882 C CA  . ASP B 197 ? 0.7758 0.9965 0.5079 -0.0741 -0.0822 -0.0964 197 ASP B CA  
3883 C C   . ASP B 197 ? 0.8505 1.0711 0.5694 -0.0990 -0.0859 -0.1087 197 ASP B C   
3884 O O   . ASP B 197 ? 0.9559 1.1462 0.6387 -0.1098 -0.0831 -0.1242 197 ASP B O   
3885 C CB  . ASP B 197 ? 0.7287 0.9343 0.4821 -0.0664 -0.0764 -0.0910 197 ASP B CB  
3886 C CG  . ASP B 197 ? 0.7332 0.9782 0.5288 -0.0656 -0.0804 -0.0757 197 ASP B CG  
3887 O OD1 . ASP B 197 ? 0.6493 0.9341 0.4574 -0.0687 -0.0876 -0.0680 197 ASP B OD1 
3888 O OD2 . ASP B 197 ? 0.6941 0.9292 0.5082 -0.0612 -0.0761 -0.0716 197 ASP B OD2 
3889 N N   . THR B 198 ? 0.8320 1.0879 0.5801 -0.1084 -0.0914 -0.1020 198 THR B N   
3890 C CA  . THR B 198 ? 0.8545 1.1151 0.5970 -0.1332 -0.0941 -0.1134 198 THR B CA  
3891 C C   . THR B 198 ? 0.7545 1.0288 0.5308 -0.1353 -0.0936 -0.1052 198 THR B C   
3892 O O   . THR B 198 ? 0.6660 0.9551 0.4711 -0.1182 -0.0933 -0.0896 198 THR B O   
3893 C CB  . THR B 198 ? 0.8853 1.1919 0.6268 -0.1456 -0.1044 -0.1155 198 THR B CB  
3894 O OG1 . THR B 198 ? 0.8797 1.2340 0.6528 -0.1307 -0.1108 -0.0968 198 THR B OG1 
3895 C CG2 . THR B 198 ? 0.9306 1.2200 0.6344 -0.1468 -0.1043 -0.1264 198 THR B CG2 
3896 N N   . THR B 199 ? 0.7763 1.0423 0.5471 -0.1569 -0.0922 -0.1166 199 THR B N   
3897 C CA  . THR B 199 ? 0.7238 1.0043 0.5248 -0.1618 -0.0917 -0.1106 199 THR B CA  
3898 C C   . THR B 199 ? 0.7082 1.0526 0.5369 -0.1688 -0.1021 -0.1034 199 THR B C   
3899 O O   . THR B 199 ? 0.6971 1.0666 0.5136 -0.1839 -0.1085 -0.1123 199 THR B O   
3900 C CB  . THR B 199 ? 0.7138 0.9542 0.4942 -0.1819 -0.0839 -0.1264 199 THR B CB  
3901 O OG1 . THR B 199 ? 0.7219 0.9039 0.4736 -0.1706 -0.0742 -0.1315 199 THR B OG1 
3902 C CG2 . THR B 199 ? 0.6820 0.9339 0.4923 -0.1858 -0.0822 -0.1203 199 THR B CG2 
3903 N N   . ILE B 200 ? 0.6265 0.9981 0.4915 -0.1563 -0.1035 -0.0871 200 ILE B N   
3904 C CA  . ILE B 200 ? 0.5994 1.0324 0.4909 -0.1581 -0.1127 -0.0779 200 ILE B CA  
3905 C C   . ILE B 200 ? 0.5898 1.0395 0.4862 -0.1834 -0.1141 -0.0895 200 ILE B C   
3906 O O   . ILE B 200 ? 0.5286 0.9808 0.4472 -0.1845 -0.1109 -0.0849 200 ILE B O   
3907 C CB  . ILE B 200 ? 0.5546 1.0075 0.4802 -0.1352 -0.1121 -0.0564 200 ILE B CB  
3908 C CG1 . ILE B 200 ? 0.5202 0.9466 0.4390 -0.1134 -0.1075 -0.0479 200 ILE B CG1 
3909 C CG2 . ILE B 200 ? 0.4737 0.9905 0.4210 -0.1319 -0.1215 -0.0452 200 ILE B CG2 
3910 C CD1 . ILE B 200 ? 0.4310 0.8477 0.3750 -0.0960 -0.1011 -0.0336 200 ILE B CD1 
3911 N N   . THR B 201 ? 0.6174 1.0819 0.4935 -0.2044 -0.1189 -0.1047 201 THR B N   
3912 C CA  . THR B 201 ? 0.5838 1.0556 0.4598 -0.2314 -0.1170 -0.1188 201 THR B CA  
3913 C C   . THR B 201 ? 0.5561 1.0761 0.4721 -0.2289 -0.1197 -0.1071 201 THR B C   
3914 O O   . THR B 201 ? 0.5748 1.0860 0.4993 -0.2425 -0.1145 -0.1125 201 THR B O   
3915 C CB  . THR B 201 ? 0.6672 1.1472 0.5238 -0.2460 -0.1179 -0.1310 201 THR B CB  
3916 O OG1 . THR B 201 ? 0.7575 1.1921 0.5772 -0.2441 -0.1149 -0.1397 201 THR B OG1 
3917 C CG2 . THR B 201 ? 0.6721 1.1479 0.5252 -0.2741 -0.1116 -0.1464 201 THR B CG2 
3918 N N   . VAL B 202 ? 0.5197 1.0878 0.4585 -0.2102 -0.1265 -0.0906 202 VAL B N   
3919 C CA  . VAL B 202 ? 0.4883 1.1007 0.4618 -0.2044 -0.1278 -0.0789 202 VAL B CA  
3920 C C   . VAL B 202 ? 0.4828 1.0791 0.4756 -0.1973 -0.1239 -0.0707 202 VAL B C   
3921 O O   . VAL B 202 ? 0.4905 1.1013 0.5026 -0.2044 -0.1209 -0.0704 202 VAL B O   
3922 C CB  . VAL B 202 ? 0.4694 1.1281 0.4582 -0.1816 -0.1340 -0.0614 202 VAL B CB  
3923 C CG1 . VAL B 202 ? 0.4390 1.0940 0.4425 -0.1545 -0.1340 -0.0414 202 VAL B CG1 
3924 C CG2 . VAL B 202 ? 0.4700 1.1771 0.4814 -0.1831 -0.1351 -0.0574 202 VAL B CG2 
3925 N N   . ASN B 203 ? 0.4384 0.9996 0.4257 -0.1816 -0.1213 -0.0638 203 ASN B N   
3926 C CA  . ASN B 203 ? 0.4854 1.0187 0.4904 -0.1707 -0.1130 -0.0549 203 ASN B CA  
3927 C C   . ASN B 203 ? 0.4866 0.9792 0.4789 -0.1914 -0.1049 -0.0706 203 ASN B C   
3928 O O   . ASN B 203 ? 0.4282 0.9214 0.4403 -0.1927 -0.1006 -0.0670 203 ASN B O   
3929 C CB  . ASN B 203 ? 0.4124 0.9086 0.4132 -0.1467 -0.1078 -0.0440 203 ASN B CB  
3930 C CG  . ASN B 203 ? 0.4186 0.9500 0.4351 -0.1243 -0.1125 -0.0253 203 ASN B CG  
3931 O OD1 . ASN B 203 ? 0.3872 0.9702 0.4132 -0.1248 -0.1207 -0.0207 203 ASN B OD1 
3932 N ND2 . ASN B 203 ? 0.3739 0.8776 0.3915 -0.1046 -0.1068 -0.0151 203 ASN B ND2 
3933 N N   . VAL B 204 ? 0.5041 0.9586 0.4616 -0.2068 -0.1018 -0.0877 204 VAL B N   
3934 C CA  . VAL B 204 ? 0.5427 0.9540 0.4824 -0.2271 -0.0925 -0.1031 204 VAL B CA  
3935 C C   . VAL B 204 ? 0.4958 0.9462 0.4521 -0.2504 -0.0943 -0.1099 204 VAL B C   
3936 O O   . VAL B 204 ? 0.5464 0.9800 0.5108 -0.2578 -0.0869 -0.1118 204 VAL B O   
3937 C CB  . VAL B 204 ? 0.5934 0.9598 0.4891 -0.2397 -0.0886 -0.1204 204 VAL B CB  
3938 C CG1 . VAL B 204 ? 0.6785 0.9975 0.5514 -0.2621 -0.0773 -0.1366 204 VAL B CG1 
3939 C CG2 . VAL B 204 ? 0.5365 0.8630 0.4168 -0.2147 -0.0855 -0.1135 204 VAL B CG2 
3940 N N   . LEU B 205 ? 0.4977 1.0009 0.4605 -0.2594 -0.1027 -0.1124 205 LEU B N   
3941 C CA  . LEU B 205 ? 0.5089 1.0448 0.4894 -0.2735 -0.1002 -0.1152 205 LEU B CA  
3942 C C   . LEU B 205 ? 0.4985 1.0646 0.5170 -0.2576 -0.1011 -0.0984 205 LEU B C   
3943 O O   . LEU B 205 ? 0.4920 1.0573 0.5213 -0.2692 -0.0949 -0.1019 205 LEU B O   
3944 C CB  . LEU B 205 ? 0.5212 1.1009 0.5010 -0.2768 -0.1059 -0.1173 205 LEU B CB  
3945 C CG  . LEU B 205 ? 0.6298 1.1804 0.5728 -0.2972 -0.1028 -0.1363 205 LEU B CG  
3946 C CD1 . LEU B 205 ? 0.5764 1.1758 0.5213 -0.2981 -0.1095 -0.1372 205 LEU B CD1 
3947 C CD2 . LEU B 205 ? 0.6488 1.1606 0.5730 -0.3258 -0.0909 -0.1544 205 LEU B CD2 
3948 N N   . ALA B 206 ? 0.4633 1.0529 0.5007 -0.2304 -0.1074 -0.0797 206 ALA B N   
3949 C CA  . ALA B 206 ? 0.4096 1.0222 0.4806 -0.2133 -0.1065 -0.0629 206 ALA B CA  
3950 C C   . ALA B 206 ? 0.4452 1.0193 0.5203 -0.2178 -0.0992 -0.0650 206 ALA B C   
3951 O O   . ALA B 206 ? 0.4228 1.0086 0.5208 -0.2154 -0.0950 -0.0588 206 ALA B O   
3952 C CB  . ALA B 206 ? 0.3858 1.0191 0.4706 -0.1830 -0.1118 -0.0425 206 ALA B CB  
3953 N N   . TRP B 207 ? 0.4430 0.9547 0.4914 -0.2160 -0.0925 -0.0709 207 TRP B N   
3954 C CA  . TRP B 207 ? 0.4288 0.8886 0.4742 -0.2136 -0.0815 -0.0715 207 TRP B CA  
3955 C C   . TRP B 207 ? 0.5031 0.9496 0.5385 -0.2426 -0.0750 -0.0880 207 TRP B C   
3956 O O   . TRP B 207 ? 0.4758 0.9128 0.5252 -0.2433 -0.0684 -0.0853 207 TRP B O   
3957 C CB  . TRP B 207 ? 0.4838 0.8856 0.5023 -0.2008 -0.0767 -0.0729 207 TRP B CB  
3958 C CG  . TRP B 207 ? 0.5500 0.8938 0.5579 -0.1961 -0.0656 -0.0751 207 TRP B CG  
3959 C CD1 . TRP B 207 ? 0.5359 0.8680 0.5630 -0.1770 -0.0613 -0.0629 207 TRP B CD1 
3960 C CD2 . TRP B 207 ? 0.5753 0.8640 0.5479 -0.2099 -0.0570 -0.0907 207 TRP B CD2 
3961 N NE1 . TRP B 207 ? 0.5428 0.8196 0.5495 -0.1777 -0.0515 -0.0701 207 TRP B NE1 
3962 C CE2 . TRP B 207 ? 0.5975 0.8457 0.5699 -0.1967 -0.0484 -0.0865 207 TRP B CE2 
3963 C CE3 . TRP B 207 ? 0.5887 0.8568 0.5275 -0.2320 -0.0549 -0.1081 207 TRP B CE3 
3964 C CZ2 . TRP B 207 ? 0.6438 0.8329 0.5832 -0.2025 -0.0381 -0.0978 207 TRP B CZ2 
3965 C CZ3 . TRP B 207 ? 0.6342 0.8399 0.5394 -0.2387 -0.0435 -0.1195 207 TRP B CZ3 
3966 C CH2 . TRP B 207 ? 0.5955 0.7623 0.5008 -0.2228 -0.0353 -0.1137 207 TRP B CH2 
3967 N N   . LEU B 208 ? 0.4658 0.9121 0.4766 -0.2677 -0.0761 -0.1055 208 LEU B N   
3968 C CA  . LEU B 208 ? 0.5165 0.9551 0.5178 -0.2987 -0.0690 -0.1221 208 LEU B CA  
3969 C C   . LEU B 208 ? 0.5038 0.9936 0.5396 -0.2986 -0.0697 -0.1143 208 LEU B C   
3970 O O   . LEU B 208 ? 0.5748 1.0513 0.6132 -0.3120 -0.0606 -0.1196 208 LEU B O   
3971 C CB  . LEU B 208 ? 0.5334 0.9625 0.5030 -0.3202 -0.0675 -0.1393 208 LEU B CB  
3972 C CG  . LEU B 208 ? 0.5657 0.9332 0.4923 -0.3241 -0.0636 -0.1509 208 LEU B CG  
3973 C CD1 . LEU B 208 ? 0.6428 0.9989 0.5395 -0.3441 -0.0597 -0.1665 208 LEU B CD1 
3974 C CD2 . LEU B 208 ? 0.5885 0.8851 0.4963 -0.3207 -0.0493 -0.1526 208 LEU B CD2 
3975 N N   . TYR B 209 ? 0.5122 1.0578 0.5711 -0.2823 -0.0790 -0.1017 209 TYR B N   
3976 C CA  . TYR B 209 ? 0.4607 1.0511 0.5497 -0.2767 -0.0791 -0.0927 209 TYR B CA  
3977 C C   . TYR B 209 ? 0.4427 1.0232 0.5550 -0.2600 -0.0757 -0.0792 209 TYR B C   
3978 O O   . TYR B 209 ? 0.4875 1.0718 0.6128 -0.2659 -0.0696 -0.0795 209 TYR B O   
3979 C CB  . TYR B 209 ? 0.4372 1.0844 0.5408 -0.2603 -0.0888 -0.0819 209 TYR B CB  
3980 C CG  . TYR B 209 ? 0.4896 1.1632 0.5791 -0.2790 -0.0907 -0.0952 209 TYR B CG  
3981 C CD1 . TYR B 209 ? 0.5372 1.2386 0.6341 -0.2949 -0.0869 -0.1029 209 TYR B CD1 
3982 C CD2 . TYR B 209 ? 0.4910 1.1635 0.5602 -0.2805 -0.0960 -0.1004 209 TYR B CD2 
3983 C CE1 . TYR B 209 ? 0.5612 1.2896 0.6460 -0.3129 -0.0881 -0.1158 209 TYR B CE1 
3984 C CE2 . TYR B 209 ? 0.5266 1.2237 0.5835 -0.2978 -0.0972 -0.1130 209 TYR B CE2 
3985 C CZ  . TYR B 209 ? 0.5816 1.3076 0.6467 -0.3144 -0.0931 -0.1209 209 TYR B CZ  
3986 O OH  . TYR B 209 ? 0.5635 1.3170 0.6171 -0.3327 -0.0937 -0.1342 209 TYR B OH  
3987 N N   . ALA B 210 ? 0.3893 0.9566 0.5066 -0.2394 -0.0790 -0.0676 210 ALA B N   
3988 C CA  . ALA B 210 ? 0.4934 1.0463 0.6306 -0.2254 -0.0742 -0.0564 210 ALA B CA  
3989 C C   . ALA B 210 ? 0.5023 1.0072 0.6258 -0.2430 -0.0625 -0.0684 210 ALA B C   
3990 O O   . ALA B 210 ? 0.4567 0.9655 0.5996 -0.2410 -0.0571 -0.0633 210 ALA B O   
3991 C CB  . ALA B 210 ? 0.4238 0.9413 0.5545 -0.1981 -0.0736 -0.0445 210 ALA B CB  
3992 N N   . ALA B 211 ? 0.5267 0.9845 0.6143 -0.2596 -0.0577 -0.0841 211 ALA B N   
3993 C CA  . ALA B 211 ? 0.5369 0.9446 0.6046 -0.2775 -0.0452 -0.0965 211 ALA B CA  
3994 C C   . ALA B 211 ? 0.5622 1.0046 0.6455 -0.3007 -0.0421 -0.1034 211 ALA B C   
3995 O O   . ALA B 211 ? 0.5735 0.9975 0.6633 -0.3044 -0.0331 -0.1030 211 ALA B O   
3996 C CB  . ALA B 211 ? 0.5761 0.9340 0.5997 -0.2927 -0.0408 -0.1129 211 ALA B CB  
3997 N N   . VAL B 212 ? 0.5194 1.0005 0.6030 -0.3091 -0.0468 -0.1077 212 VAL B N   
3998 C CA  . VAL B 212 ? 0.5417 1.0482 0.6346 -0.3232 -0.0418 -0.1125 212 VAL B CA  
3999 C C   . VAL B 212 ? 0.4747 1.0167 0.6044 -0.3038 -0.0436 -0.0962 212 VAL B C   
4000 O O   . VAL B 212 ? 0.5527 1.0914 0.6900 -0.3119 -0.0356 -0.0983 212 VAL B O   
4001 C CB  . VAL B 212 ? 0.5131 1.0587 0.5991 -0.3348 -0.0473 -0.1206 212 VAL B CB  
4002 C CG1 . VAL B 212 ? 0.5121 1.0906 0.6088 -0.3496 -0.0427 -0.1262 212 VAL B CG1 
4003 C CG2 . VAL B 212 ? 0.5681 1.0706 0.6150 -0.3538 -0.0435 -0.1369 212 VAL B CG2 
4004 N N   . ILE B 213 ? 0.4576 1.0313 0.6086 -0.2772 -0.0530 -0.0796 213 ILE B N   
4005 C CA  . ILE B 213 ? 0.5016 1.1011 0.6842 -0.2558 -0.0533 -0.0631 213 ILE B CA  
4006 C C   . ILE B 213 ? 0.4861 1.0452 0.6724 -0.2561 -0.0435 -0.0620 213 ILE B C   
4007 O O   . ILE B 213 ? 0.5279 1.0984 0.7316 -0.2538 -0.0387 -0.0577 213 ILE B O   
4008 C CB  . ILE B 213 ? 0.4884 1.1111 0.6861 -0.2258 -0.0620 -0.0451 213 ILE B CB  
4009 C CG1 . ILE B 213 ? 0.4521 1.0984 0.6367 -0.2271 -0.0708 -0.0484 213 ILE B CG1 
4010 C CG2 . ILE B 213 ? 0.4609 1.1204 0.6867 -0.2049 -0.0628 -0.0295 213 ILE B CG2 
4011 C CD1 . ILE B 213 ? 0.4298 1.1258 0.6214 -0.2314 -0.0742 -0.0502 213 ILE B CD1 
4012 N N   . ASN B 214 ? 0.4850 0.9961 0.6533 -0.2594 -0.0400 -0.0665 214 ASN B N   
4013 C CA  . ASN B 214 ? 0.5213 0.9921 0.6913 -0.2563 -0.0307 -0.0644 214 ASN B CA  
4014 C C   . ASN B 214 ? 0.5461 0.9695 0.6890 -0.2823 -0.0187 -0.0811 214 ASN B C   
4015 O O   . ASN B 214 ? 0.5551 0.9182 0.6791 -0.2743 -0.0097 -0.0811 214 ASN B O   
4016 C CB  . ASN B 214 ? 0.5061 0.9330 0.6627 -0.2310 -0.0314 -0.0562 214 ASN B CB  
4017 C CG  . ASN B 214 ? 0.5430 1.0012 0.7281 -0.2023 -0.0375 -0.0370 214 ASN B CG  
4018 O OD1 . ASN B 214 ? 0.5546 0.9927 0.7504 -0.1847 -0.0323 -0.0273 214 ASN B OD1 
4019 N ND2 . ASN B 214 ? 0.5006 1.0071 0.6963 -0.1974 -0.0478 -0.0316 214 ASN B ND2 
4020 N N   . GLY B 215 ? 0.5579 0.9936 0.6900 -0.3040 -0.0165 -0.0930 215 GLY B N   
4021 C CA  . GLY B 215 ? 0.6462 1.0398 0.7542 -0.3276 -0.0029 -0.1071 215 GLY B CA  
4022 C C   . GLY B 215 ? 0.7166 1.0535 0.7803 -0.3464 0.0038  -0.1233 215 GLY B C   
4023 O O   . GLY B 215 ? 0.7654 1.0686 0.8052 -0.3668 0.0162  -0.1354 215 GLY B O   
4024 N N   . ASP B 216 ? 0.6880 1.0095 0.7375 -0.3392 -0.0027 -0.1238 216 ASP B N   
4025 C CA  . ASP B 216 ? 0.7255 0.9883 0.7286 -0.3527 0.0040  -0.1385 216 ASP B CA  
4026 C C   . ASP B 216 ? 0.7367 1.0253 0.7285 -0.3717 0.0015  -0.1495 216 ASP B C   
4027 O O   . ASP B 216 ? 0.7829 1.1245 0.7931 -0.3644 -0.0114 -0.1444 216 ASP B O   
4028 C CB  . ASP B 216 ? 0.7034 0.9339 0.6912 -0.3243 -0.0009 -0.1306 216 ASP B CB  
4029 C CG  . ASP B 216 ? 0.8514 1.0442 0.8422 -0.2964 0.0041  -0.1182 216 ASP B CG  
4030 O OD1 . ASP B 216 ? 0.8446 1.0548 0.8622 -0.2918 0.0066  -0.1101 216 ASP B OD1 
4031 O OD2 . ASP B 216 ? 0.8268 0.9745 0.7931 -0.2787 0.0056  -0.1169 216 ASP B OD2 
4032 N N   . ARG B 217 ? 0.7988 1.0493 0.7593 -0.3941 0.0147  -0.1637 217 ARG B N   
4033 C CA  . ARG B 217 ? 0.8116 1.0873 0.7618 -0.4134 0.0142  -0.1749 217 ARG B CA  
4034 C C   . ARG B 217 ? 0.8435 1.0534 0.7434 -0.4328 0.0285  -0.1910 217 ARG B C   
4035 O O   . ARG B 217 ? 0.8443 1.0682 0.7321 -0.4529 0.0318  -0.2022 217 ARG B O   
4036 C CB  . ARG B 217 ? 0.7189 1.0442 0.6952 -0.4235 0.0159  -0.1746 217 ARG B CB  
4037 C CG  . ARG B 217 ? 0.7557 1.1497 0.7781 -0.4030 0.0020  -0.1588 217 ARG B CG  
4038 C CD  . ARG B 217 ? 0.7447 1.1783 0.7899 -0.4104 0.0055  -0.1582 217 ARG B CD  
4039 N NE  . ARG B 217 ? 0.7171 1.1646 0.7452 -0.4361 0.0099  -0.1739 217 ARG B NE  
4040 C CZ  . ARG B 217 ? 0.7300 1.2373 0.7713 -0.4371 -0.0002 -0.1749 217 ARG B CZ  
4041 N NH1 . ARG B 217 ? 0.6655 1.2218 0.7357 -0.4127 -0.0147 -0.1601 217 ARG B NH1 
4042 N NH2 . ARG B 217 ? 0.7272 1.2462 0.7520 -0.4628 0.0054  -0.1906 217 ARG B NH2 
4043 N N   . TRP B 218 ? 0.9150 1.0529 0.7838 -0.4260 0.0377  -0.1922 218 TRP B N   
4044 C CA  . TRP B 218 ? 0.9481 1.0164 0.7662 -0.4403 0.0541  -0.2051 218 TRP B CA  
4045 C C   . TRP B 218 ? 0.9348 1.0046 0.7312 -0.4478 0.0500  -0.2139 218 TRP B C   
4046 O O   . TRP B 218 ? 0.9480 0.9776 0.7079 -0.4653 0.0636  -0.2256 218 TRP B O   
4047 C CB  . TRP B 218 ? 0.9990 0.9909 0.7874 -0.4239 0.0635  -0.2021 218 TRP B CB  
4048 C CG  . TRP B 218 ? 0.9418 0.9182 0.7234 -0.4001 0.0527  -0.1970 218 TRP B CG  
4049 C CD1 . TRP B 218 ? 0.9495 0.9393 0.7564 -0.3761 0.0435  -0.1844 218 TRP B CD1 
4050 C CD2 . TRP B 218 ? 1.0112 0.9541 0.7573 -0.3953 0.0521  -0.2032 218 TRP B CD2 
4051 N NE1 . TRP B 218 ? 0.9665 0.9372 0.7585 -0.3508 0.0374  -0.1792 218 TRP B NE1 
4052 C CE2 . TRP B 218 ? 0.9780 0.9187 0.7301 -0.3675 0.0416  -0.1942 218 TRP B CE2 
4053 C CE3 . TRP B 218 ? 1.0701 0.9868 0.7812 -0.4096 0.0599  -0.2142 218 TRP B CE3 
4054 C CZ2 . TRP B 218 ? 0.9959 0.9102 0.7203 -0.3524 0.0386  -0.1957 218 TRP B CZ2 
4055 C CZ3 . TRP B 218 ? 1.0477 0.9361 0.7308 -0.3967 0.0565  -0.2165 218 TRP B CZ3 
4056 C CH2 . TRP B 218 ? 1.0651 0.9523 0.7532 -0.3701 0.0456  -0.2089 218 TRP B CH2 
4057 N N   . PHE B 219 ? 0.9055 1.0231 0.7239 -0.4355 0.0323  -0.2082 219 PHE B N   
4058 C CA  . PHE B 219 ? 0.8908 1.0104 0.6892 -0.4398 0.0275  -0.2155 219 PHE B CA  
4059 C C   . PHE B 219 ? 0.8483 1.0317 0.6644 -0.4576 0.0221  -0.2212 219 PHE B C   
4060 O O   . PHE B 219 ? 0.9421 1.1291 0.7413 -0.4639 0.0192  -0.2285 219 PHE B O   
4061 C CB  . PHE B 219 ? 0.8960 1.0295 0.7039 -0.4151 0.0118  -0.2064 219 PHE B CB  
4062 C CG  . PHE B 219 ? 0.8307 1.0306 0.6884 -0.3998 -0.0028 -0.1916 219 PHE B CG  
4063 C CD1 . PHE B 219 ? 0.8262 1.0141 0.7000 -0.3846 -0.0025 -0.1816 219 PHE B CD1 
4064 C CD2 . PHE B 219 ? 0.8019 1.0754 0.6896 -0.3995 -0.0156 -0.1872 219 PHE B CD2 
4065 C CE1 . PHE B 219 ? 0.7621 1.0094 0.6817 -0.3695 -0.0143 -0.1668 219 PHE B CE1 
4066 C CE2 . PHE B 219 ? 0.7310 1.0617 0.6622 -0.3816 -0.0272 -0.1715 219 PHE B CE2 
4067 C CZ  . PHE B 219 ? 0.7003 1.0177 0.6478 -0.3670 -0.0262 -0.1612 219 PHE B CZ  
4068 N N   . LEU B 220 ? 0.8309 1.0637 0.6784 -0.4651 0.0213  -0.2186 220 LEU B N   
4069 C CA  . LEU B 220 ? 0.8091 1.1086 0.6747 -0.4787 0.0151  -0.2235 220 LEU B CA  
4070 C C   . LEU B 220 ? 0.9641 1.2358 0.7960 -0.5088 0.0304  -0.2414 220 LEU B C   
4071 O O   . LEU B 220 ? 0.9744 1.2087 0.7907 -0.5233 0.0464  -0.2475 220 LEU B O   
4072 C CB  . LEU B 220 ? 0.8117 1.1712 0.7194 -0.4748 0.0102  -0.2149 220 LEU B CB  
4073 C CG  . LEU B 220 ? 0.7827 1.1801 0.7281 -0.4452 -0.0045 -0.1959 220 LEU B CG  
4074 C CD1 . LEU B 220 ? 0.6885 1.1457 0.6717 -0.4426 -0.0078 -0.1887 220 LEU B CD1 
4075 C CD2 . LEU B 220 ? 0.7928 1.2213 0.7436 -0.4300 -0.0196 -0.1902 220 LEU B CD2 
4076 N N   . ASN B 221 ? 0.9497 1.2411 0.7707 -0.5182 0.0261  -0.2497 221 ASN B N   
4077 C CA  . ASN B 221 ? 1.0436 1.3128 0.8332 -0.5474 0.0401  -0.2671 221 ASN B CA  
4078 C C   . ASN B 221 ? 1.0837 1.4268 0.8972 -0.5650 0.0367  -0.2737 221 ASN B C   
4079 O O   . ASN B 221 ? 1.1082 1.5207 0.9601 -0.5516 0.0218  -0.2642 221 ASN B O   
4080 C CB  . ASN B 221 ? 1.1334 1.3737 0.8928 -0.5472 0.0386  -0.2732 221 ASN B CB  
4081 C CG  . ASN B 221 ? 1.0246 1.3350 0.8087 -0.5376 0.0193  -0.2694 221 ASN B CG  
4082 O OD1 . ASN B 221 ? 0.9350 1.3163 0.7576 -0.5307 0.0076  -0.2619 221 ASN B OD1 
4083 N ND2 . ASN B 221 ? 1.0212 1.3099 0.7813 -0.5353 0.0166  -0.2738 221 ASN B ND2 
4084 N N   . ARG B 222 ? 1.2056 1.5326 0.9939 -0.5946 0.0516  -0.2902 222 ARG B N   
4085 C CA  . ARG B 222 ? 1.2755 1.6707 1.0784 -0.6139 0.0485  -0.3002 222 ARG B CA  
4086 C C   . ARG B 222 ? 1.2368 1.6473 1.0269 -0.6184 0.0416  -0.3073 222 ARG B C   
4087 O O   . ARG B 222 ? 1.2360 1.7158 1.0447 -0.6260 0.0333  -0.3121 222 ARG B O   
4088 C CB  . ARG B 222 ? 1.4256 1.8016 1.2088 -0.6464 0.0686  -0.3159 222 ARG B CB  
4089 C CG  . ARG B 222 ? 1.4360 1.7593 1.1732 -0.6709 0.0841  -0.3323 222 ARG B CG  
4090 C CD  . ARG B 222 ? 1.5050 1.7355 1.2060 -0.6588 0.0934  -0.3277 222 ARG B CD  
4091 N NE  . ARG B 222 ? 1.5213 1.7069 1.2192 -0.6508 0.1035  -0.3202 222 ARG B NE  
4092 C CZ  . ARG B 222 ? 1.5788 1.7104 1.2464 -0.6696 0.1256  -0.3284 222 ARG B CZ  
4093 N NH1 . ARG B 222 ? 1.6038 1.7190 1.2416 -0.6994 0.1409  -0.3449 222 ARG B NH1 
4094 N NH2 . ARG B 222 ? 1.5436 1.6362 1.2097 -0.6582 0.1331  -0.3197 222 ARG B NH2 
4095 N N   . PHE B 223 ? 1.1436 1.4915 0.9019 -0.6123 0.0449  -0.3080 223 PHE B N   
4096 C CA  . PHE B 223 ? 1.1791 1.5364 0.9232 -0.6155 0.0387  -0.3146 223 PHE B CA  
4097 C C   . PHE B 223 ? 1.0502 1.4765 0.8301 -0.5904 0.0159  -0.3017 223 PHE B C   
4098 O O   . PHE B 223 ? 1.0444 1.4840 0.8498 -0.5652 0.0061  -0.2856 223 PHE B O   
4099 C CB  . PHE B 223 ? 1.1777 1.4506 0.8799 -0.6100 0.0467  -0.3164 223 PHE B CB  
4100 C CG  . PHE B 223 ? 1.3259 1.5523 0.9863 -0.6394 0.0654  -0.3342 223 PHE B CG  
4101 C CD1 . PHE B 223 ? 1.3163 1.5830 0.9738 -0.6601 0.0639  -0.3474 223 PHE B CD1 
4102 C CD2 . PHE B 223 ? 1.3854 1.5264 1.0078 -0.6454 0.0852  -0.3374 223 PHE B CD2 
4103 C CE1 . PHE B 223 ? 1.3728 1.5951 0.9906 -0.6889 0.0825  -0.3644 223 PHE B CE1 
4104 C CE2 . PHE B 223 ? 1.4487 1.5437 1.0305 -0.6717 0.1041  -0.3527 223 PHE B CE2 
4105 C CZ  . PHE B 223 ? 1.5077 1.6427 1.0871 -0.6946 0.1030  -0.3667 223 PHE B CZ  
4106 N N   . THR B 224 ? 1.0443 1.5147 0.8254 -0.5972 0.0083  -0.3085 224 THR B N   
4107 C CA  . THR B 224 ? 0.9828 1.5125 0.7904 -0.5730 -0.0118 -0.2966 224 THR B CA  
4108 C C   . THR B 224 ? 1.0148 1.5213 0.7963 -0.5713 -0.0153 -0.3018 224 THR B C   
4109 O O   . THR B 224 ? 1.0845 1.5417 0.8303 -0.5923 -0.0025 -0.3165 224 THR B O   
4110 C CB  . THR B 224 ? 0.9521 1.5717 0.7910 -0.5786 -0.0199 -0.2980 224 THR B CB  
4111 O OG1 . THR B 224 ? 0.9031 1.5755 0.7716 -0.5477 -0.0384 -0.2807 224 THR B OG1 
4112 C CG2 . THR B 224 ? 1.0011 1.6404 0.8216 -0.6055 -0.0156 -0.3167 224 THR B CG2 
4113 N N   . THR B 225 ? 0.9634 1.5047 0.7614 -0.5455 -0.0321 -0.2895 225 THR B N   
4114 C CA  . THR B 225 ? 0.9613 1.4875 0.7364 -0.5423 -0.0367 -0.2940 225 THR B CA  
4115 C C   . THR B 225 ? 0.9560 1.5620 0.7566 -0.5295 -0.0533 -0.2877 225 THR B C   
4116 O O   . THR B 225 ? 0.9222 1.5946 0.7530 -0.5290 -0.0587 -0.2839 225 THR B O   
4117 C CB  . THR B 225 ? 0.9788 1.4406 0.7355 -0.5202 -0.0376 -0.2850 225 THR B CB  
4118 O OG1 . THR B 225 ? 1.0361 1.4922 0.7748 -0.5123 -0.0444 -0.2870 225 THR B OG1 
4119 C CG2 . THR B 225 ? 0.9257 1.4082 0.7139 -0.4902 -0.0484 -0.2645 225 THR B CG2 
4120 N N   . THR B 226 ? 0.9549 1.5533 0.7410 -0.5179 -0.0608 -0.2865 226 THR B N   
4121 C CA  . THR B 226 ? 0.9446 1.6103 0.7499 -0.5024 -0.0760 -0.2792 226 THR B CA  
4122 C C   . THR B 226 ? 0.8868 1.5370 0.6932 -0.4695 -0.0865 -0.2625 226 THR B C   
4123 O O   . THR B 226 ? 0.9635 1.5476 0.7462 -0.4642 -0.0816 -0.2625 226 THR B O   
4124 C CB  . THR B 226 ? 0.9963 1.6736 0.7806 -0.5228 -0.0746 -0.2961 226 THR B CB  
4125 O OG1 . THR B 226 ? 1.0197 1.6353 0.7707 -0.5184 -0.0726 -0.2995 226 THR B OG1 
4126 C CG2 . THR B 226 ? 1.0152 1.6858 0.7874 -0.5602 -0.0597 -0.3160 226 THR B CG2 
4127 N N   . LEU B 227 ? 0.8546 1.5660 0.6871 -0.4466 -0.1001 -0.2482 227 LEU B N   
4128 C CA  . LEU B 227 ? 0.8492 1.5501 0.6833 -0.4151 -0.1094 -0.2315 227 LEU B CA  
4129 C C   . LEU B 227 ? 0.9019 1.5569 0.7010 -0.4163 -0.1086 -0.2397 227 LEU B C   
4130 O O   . LEU B 227 ? 0.9517 1.5639 0.7391 -0.3981 -0.1096 -0.2316 227 LEU B O   
4131 C CB  . LEU B 227 ? 0.7926 1.5660 0.6561 -0.3914 -0.1222 -0.2154 227 LEU B CB  
4132 C CG  . LEU B 227 ? 0.7998 1.5664 0.6623 -0.3602 -0.1309 -0.1988 227 LEU B CG  
4133 C CD1 . LEU B 227 ? 0.7638 1.4951 0.6354 -0.3418 -0.1295 -0.1845 227 LEU B CD1 
4134 C CD2 . LEU B 227 ? 0.7515 1.5874 0.6352 -0.3400 -0.1415 -0.1858 227 LEU B CD2 
4135 N N   . ASN B 228 ? 0.9145 1.5780 0.6958 -0.4376 -0.1062 -0.2561 228 ASN B N   
4136 C CA  . ASN B 228 ? 0.9382 1.5569 0.6844 -0.4393 -0.1047 -0.2647 228 ASN B CA  
4137 C C   . ASN B 228 ? 1.0241 1.5573 0.7387 -0.4487 -0.0915 -0.2731 228 ASN B C   
4138 O O   . ASN B 228 ? 1.0531 1.5400 0.7481 -0.4316 -0.0919 -0.2683 228 ASN B O   
4139 C CB  . ASN B 228 ? 0.9756 1.6236 0.7105 -0.4622 -0.1041 -0.2814 228 ASN B CB  
4140 C CG  . ASN B 228 ? 0.9503 1.6592 0.6984 -0.4445 -0.1180 -0.2732 228 ASN B CG  
4141 O OD1 . ASN B 228 ? 0.9113 1.6372 0.6750 -0.4147 -0.1273 -0.2544 228 ASN B OD1 
4142 N ND2 . ASN B 228 ? 0.9857 1.7274 0.7265 -0.4632 -0.1186 -0.2873 228 ASN B ND2 
4143 N N   . ASP B 229 ? 1.0683 1.5792 0.7761 -0.4749 -0.0787 -0.2855 229 ASP B N   
4144 C CA  . ASP B 229 ? 1.1235 1.5503 0.7976 -0.4845 -0.0638 -0.2939 229 ASP B CA  
4145 C C   . ASP B 229 ? 1.1196 1.5115 0.7994 -0.4616 -0.0640 -0.2796 229 ASP B C   
4146 O O   . ASP B 229 ? 1.1434 1.4683 0.7935 -0.4532 -0.0574 -0.2807 229 ASP B O   
4147 C CB  . ASP B 229 ? 1.1790 1.5931 0.8449 -0.5179 -0.0490 -0.3094 229 ASP B CB  
4148 C CG  . ASP B 229 ? 1.2333 1.6663 0.8841 -0.5429 -0.0460 -0.3265 229 ASP B CG  
4149 O OD1 . ASP B 229 ? 1.2377 1.7426 0.9134 -0.5523 -0.0525 -0.3289 229 ASP B OD1 
4150 O OD2 . ASP B 229 ? 1.2569 1.6329 0.8697 -0.5511 -0.0373 -0.3372 229 ASP B OD2 
4151 N N   . PHE B 230 ? 1.0780 1.5132 0.7944 -0.4509 -0.0705 -0.2666 230 PHE B N   
4152 C CA  . PHE B 230 ? 1.1017 1.5068 0.8244 -0.4292 -0.0710 -0.2532 230 PHE B CA  
4153 C C   . PHE B 230 ? 1.0673 1.4558 0.7788 -0.4024 -0.0789 -0.2440 230 PHE B C   
4154 O O   . PHE B 230 ? 1.1080 1.4440 0.8039 -0.3887 -0.0747 -0.2399 230 PHE B O   
4155 C CB  . PHE B 230 ? 1.0253 1.4859 0.7911 -0.4187 -0.0784 -0.2389 230 PHE B CB  
4156 C CG  . PHE B 230 ? 1.0909 1.5313 0.8666 -0.3931 -0.0818 -0.2234 230 PHE B CG  
4157 C CD1 . PHE B 230 ? 1.0873 1.4649 0.8461 -0.3954 -0.0710 -0.2263 230 PHE B CD1 
4158 C CD2 . PHE B 230 ? 1.0274 1.5090 0.8268 -0.3660 -0.0948 -0.2060 230 PHE B CD2 
4159 C CE1 . PHE B 230 ? 0.9793 1.3397 0.7463 -0.3726 -0.0740 -0.2133 230 PHE B CE1 
4160 C CE2 . PHE B 230 ? 0.9533 1.4166 0.7611 -0.3439 -0.0971 -0.1925 230 PHE B CE2 
4161 C CZ  . PHE B 230 ? 0.9435 1.3478 0.7356 -0.3478 -0.0871 -0.1968 230 PHE B CZ  
4162 N N   . ASN B 231 ? 1.0266 1.4604 0.7455 -0.3934 -0.0900 -0.2401 231 ASN B N   
4163 C CA  . ASN B 231 ? 1.0564 1.4776 0.7659 -0.3671 -0.0970 -0.2302 231 ASN B CA  
4164 C C   . ASN B 231 ? 1.1001 1.4519 0.7648 -0.3705 -0.0883 -0.2422 231 ASN B C   
4165 O O   . ASN B 231 ? 1.1119 1.4268 0.7623 -0.3496 -0.0881 -0.2356 231 ASN B O   
4166 C CB  . ASN B 231 ? 0.9792 1.4655 0.7069 -0.3557 -0.1100 -0.2221 231 ASN B CB  
4167 C CG  . ASN B 231 ? 0.9310 1.4680 0.6972 -0.3327 -0.1194 -0.2013 231 ASN B CG  
4168 O OD1 . ASN B 231 ? 0.8590 1.4587 0.6499 -0.3304 -0.1267 -0.1954 231 ASN B OD1 
4169 N ND2 . ASN B 231 ? 0.9190 1.4280 0.6896 -0.3154 -0.1184 -0.1903 231 ASN B ND2 
4170 N N   . LEU B 232 ? 1.1110 1.4430 0.7522 -0.3958 -0.0799 -0.2597 232 LEU B N   
4171 C CA  . LEU B 232 ? 1.1769 1.4355 0.7735 -0.3989 -0.0689 -0.2709 232 LEU B CA  
4172 C C   . LEU B 232 ? 1.1872 1.3825 0.7694 -0.3936 -0.0574 -0.2695 232 LEU B C   
4173 O O   . LEU B 232 ? 1.2388 1.3738 0.7883 -0.3813 -0.0505 -0.2714 232 LEU B O   
4174 C CB  . LEU B 232 ? 1.2263 1.4748 0.8008 -0.4287 -0.0605 -0.2899 232 LEU B CB  
4175 C CG  . LEU B 232 ? 1.3129 1.6058 0.8868 -0.4333 -0.0695 -0.2952 232 LEU B CG  
4176 C CD1 . LEU B 232 ? 1.2710 1.5638 0.8380 -0.4040 -0.0794 -0.2850 232 LEU B CD1 
4177 C CD2 . LEU B 232 ? 1.2311 1.6077 0.8426 -0.4439 -0.0789 -0.2933 232 LEU B CD2 
4178 N N   . VAL B 233 ? 1.1706 1.3803 0.7770 -0.4001 -0.0554 -0.2652 233 VAL B N   
4179 C CA  . VAL B 233 ? 1.1636 1.3181 0.7594 -0.3927 -0.0455 -0.2621 233 VAL B CA  
4180 C C   . VAL B 233 ? 1.1298 1.2971 0.7446 -0.3627 -0.0550 -0.2453 233 VAL B C   
4181 O O   . VAL B 233 ? 1.1242 1.2390 0.7206 -0.3477 -0.0484 -0.2425 233 VAL B O   
4182 C CB  . VAL B 233 ? 1.1625 1.3230 0.7734 -0.4148 -0.0374 -0.2661 233 VAL B CB  
4183 C CG1 . VAL B 233 ? 1.1704 1.2979 0.7855 -0.4014 -0.0326 -0.2576 233 VAL B CG1 
4184 C CG2 . VAL B 233 ? 1.2094 1.3298 0.7893 -0.4433 -0.0216 -0.2834 233 VAL B CG2 
4185 N N   . ALA B 234 ? 1.1301 1.3661 0.7808 -0.3525 -0.0696 -0.2335 234 ALA B N   
4186 C CA  . ALA B 234 ? 1.0579 1.3059 0.7247 -0.3240 -0.0778 -0.2171 234 ALA B CA  
4187 C C   . ALA B 234 ? 1.0728 1.2857 0.7102 -0.3049 -0.0777 -0.2165 234 ALA B C   
4188 O O   . ALA B 234 ? 1.0781 1.2565 0.7056 -0.2860 -0.0746 -0.2107 234 ALA B O   
4189 C CB  . ALA B 234 ? 0.9785 1.3052 0.6870 -0.3155 -0.0919 -0.2033 234 ALA B CB  
4190 N N   . MET B 235 ? 1.0753 1.2974 0.6979 -0.3092 -0.0806 -0.2229 235 MET B N   
4191 C CA  . MET B 235 ? 1.1439 1.3371 0.7396 -0.2903 -0.0806 -0.2221 235 MET B CA  
4192 C C   . MET B 235 ? 1.1724 1.2864 0.7284 -0.2864 -0.0665 -0.2305 235 MET B C   
4193 O O   . MET B 235 ? 1.1004 1.1884 0.6435 -0.2625 -0.0653 -0.2242 235 MET B O   
4194 C CB  . MET B 235 ? 1.2127 1.4310 0.7998 -0.2976 -0.0860 -0.2284 235 MET B CB  
4195 C CG  . MET B 235 ? 1.2838 1.5167 0.8689 -0.2720 -0.0939 -0.2177 235 MET B CG  
4196 S SD  . MET B 235 ? 1.4663 1.7355 1.0878 -0.2450 -0.1021 -0.1947 235 MET B SD  
4197 C CE  . MET B 235 ? 1.0554 1.3801 0.7200 -0.2600 -0.1074 -0.1896 235 MET B CE  
4198 N N   . LYS B 236 ? 1.1704 1.2452 0.7062 -0.3082 -0.0547 -0.2441 236 LYS B N   
4199 C CA  . LYS B 236 ? 1.2038 1.2013 0.7016 -0.3011 -0.0400 -0.2499 236 LYS B CA  
4200 C C   . LYS B 236 ? 1.2124 1.1900 0.7172 -0.2811 -0.0375 -0.2396 236 LYS B C   
4201 O O   . LYS B 236 ? 1.3464 1.2664 0.8221 -0.2650 -0.0273 -0.2404 236 LYS B O   
4202 C CB  . LYS B 236 ? 1.3549 1.3133 0.8314 -0.3281 -0.0259 -0.2641 236 LYS B CB  
4203 C CG  . LYS B 236 ? 1.4237 1.3020 0.8654 -0.3190 -0.0090 -0.2667 236 LYS B CG  
4204 C CD  . LYS B 236 ? 1.4152 1.2644 0.8512 -0.3432 0.0046  -0.2737 236 LYS B CD  
4205 C CE  . LYS B 236 ? 1.4064 1.1861 0.7966 -0.3520 0.0224  -0.2848 236 LYS B CE  
4206 N NZ  . LYS B 236 ? 1.3941 1.1696 0.7619 -0.3502 0.0202  -0.2918 236 LYS B NZ  
4207 N N   . TYR B 237 ? 1.1836 1.2092 0.7267 -0.2798 -0.0465 -0.2293 237 TYR B N   
4208 C CA  . TYR B 237 ? 1.1696 1.1796 0.7218 -0.2643 -0.0439 -0.2205 237 TYR B CA  
4209 C C   . TYR B 237 ? 1.1243 1.1798 0.7038 -0.2423 -0.0562 -0.2054 237 TYR B C   
4210 O O   . TYR B 237 ? 1.0346 1.0886 0.6276 -0.2306 -0.0558 -0.1974 237 TYR B O   
4211 C CB  . TYR B 237 ? 1.1196 1.1358 0.6912 -0.2830 -0.0402 -0.2218 237 TYR B CB  
4212 C CG  . TYR B 237 ? 1.1549 1.1113 0.6968 -0.2996 -0.0236 -0.2338 237 TYR B CG  
4213 C CD1 . TYR B 237 ? 1.1668 1.0699 0.6934 -0.2894 -0.0121 -0.2321 237 TYR B CD1 
4214 C CD2 . TYR B 237 ? 1.1231 1.0758 0.6518 -0.3245 -0.0186 -0.2459 237 TYR B CD2 
4215 C CE1 . TYR B 237 ? 1.2394 1.0859 0.7383 -0.3021 0.0043  -0.2406 237 TYR B CE1 
4216 C CE2 . TYR B 237 ? 1.2029 1.0985 0.7032 -0.3398 -0.0016 -0.2556 237 TYR B CE2 
4217 C CZ  . TYR B 237 ? 1.2860 1.1280 0.7715 -0.3278 0.0099  -0.2521 237 TYR B CZ  
4218 O OH  . TYR B 237 ? 1.3439 1.1274 0.8002 -0.3406 0.0279  -0.2593 237 TYR B OH  
4219 N N   . ASN B 238 ? 1.1717 1.2670 0.7592 -0.2360 -0.0662 -0.2009 238 ASN B N   
4220 C CA  . ASN B 238 ? 1.1114 1.2454 0.7220 -0.2135 -0.0757 -0.1854 238 ASN B CA  
4221 C C   . ASN B 238 ? 1.0252 1.2168 0.6807 -0.2163 -0.0849 -0.1737 238 ASN B C   
4222 O O   . ASN B 238 ? 1.0225 1.2230 0.7055 -0.1945 -0.0854 -0.1573 238 ASN B O   
4223 C CB  . ASN B 238 ? 1.1816 1.2713 0.7763 -0.1898 -0.0678 -0.1813 238 ASN B CB  
4224 C CG  . ASN B 238 ? 1.2542 1.3714 0.8685 -0.1628 -0.0735 -0.1654 238 ASN B CG  
4225 O OD1 . ASN B 238 ? 1.2832 1.3710 0.8888 -0.1407 -0.0674 -0.1609 238 ASN B OD1 
4226 N ND2 . ASN B 238 ? 1.2272 1.4016 0.8664 -0.1641 -0.0847 -0.1570 238 ASN B ND2 
4227 N N   . TYR B 239 ? 0.9861 1.2120 0.6592 -0.2364 -0.0889 -0.1770 239 TYR B N   
4228 C CA  . TYR B 239 ? 0.8812 1.1650 0.5976 -0.2373 -0.0973 -0.1652 239 TYR B CA  
4229 C C   . TYR B 239 ? 0.9529 1.2938 0.6872 -0.2315 -0.1080 -0.1567 239 TYR B C   
4230 O O   . TYR B 239 ? 0.9603 1.3077 0.6819 -0.2447 -0.1086 -0.1664 239 TYR B O   
4231 C CB  . TYR B 239 ? 0.8173 1.1028 0.5429 -0.2620 -0.0928 -0.1740 239 TYR B CB  
4232 C CG  . TYR B 239 ? 0.8517 1.1041 0.5790 -0.2630 -0.0854 -0.1743 239 TYR B CG  
4233 C CD1 . TYR B 239 ? 0.8786 1.0662 0.5782 -0.2505 -0.0749 -0.1766 239 TYR B CD1 
4234 C CD2 . TYR B 239 ? 0.7652 1.0489 0.5250 -0.2719 -0.0870 -0.1697 239 TYR B CD2 
4235 C CE1 . TYR B 239 ? 0.8501 1.0037 0.5560 -0.2451 -0.0658 -0.1729 239 TYR B CE1 
4236 C CE2 . TYR B 239 ? 0.7822 1.0309 0.5479 -0.2683 -0.0779 -0.1667 239 TYR B CE2 
4237 C CZ  . TYR B 239 ? 0.8033 0.9865 0.5420 -0.2546 -0.0673 -0.1681 239 TYR B CZ  
4238 O OH  . TYR B 239 ? 0.7911 0.9414 0.5357 -0.2490 -0.0583 -0.1644 239 TYR B OH  
4239 N N   . GLU B 240 ? 0.9796 1.3587 0.7413 -0.2108 -0.1153 -0.1385 240 GLU B N   
4240 C CA  . GLU B 240 ? 0.9491 1.3851 0.7325 -0.2021 -0.1244 -0.1267 240 GLU B CA  
4241 C C   . GLU B 240 ? 0.9241 1.3903 0.7154 -0.2237 -0.1262 -0.1357 240 GLU B C   
4242 O O   . GLU B 240 ? 0.9091 1.3833 0.7168 -0.2366 -0.1240 -0.1384 240 GLU B O   
4243 C CB  . GLU B 240 ? 0.9518 1.4212 0.7700 -0.1819 -0.1286 -0.1059 240 GLU B CB  
4244 C CG  . GLU B 240 ? 0.9613 1.4838 0.8025 -0.1672 -0.1356 -0.0898 240 GLU B CG  
4245 C CD  . GLU B 240 ? 0.9978 1.5363 0.8675 -0.1465 -0.1362 -0.0698 240 GLU B CD  
4246 O OE1 . GLU B 240 ? 0.8957 1.4068 0.7596 -0.1304 -0.1320 -0.0630 240 GLU B OE1 
4247 O OE2 . GLU B 240 ? 0.9966 1.5690 0.8952 -0.1453 -0.1381 -0.0610 240 GLU B OE2 
4248 N N   . PRO B 241 ? 0.9507 1.4343 0.7306 -0.2288 -0.1296 -0.1414 241 PRO B N   
4249 C CA  . PRO B 241 ? 0.8671 1.3844 0.6551 -0.2497 -0.1310 -0.1507 241 PRO B CA  
4250 C C   . PRO B 241 ? 0.8581 1.4312 0.6855 -0.2443 -0.1358 -0.1376 241 PRO B C   
4251 O O   . PRO B 241 ? 0.8779 1.4776 0.7260 -0.2207 -0.1407 -0.1188 241 PRO B O   
4252 C CB  . PRO B 241 ? 0.8280 1.3629 0.6010 -0.2480 -0.1358 -0.1540 241 PRO B CB  
4253 C CG  . PRO B 241 ? 0.9365 1.4356 0.6878 -0.2298 -0.1349 -0.1496 241 PRO B CG  
4254 C CD  . PRO B 241 ? 0.9190 1.3820 0.6715 -0.2194 -0.1300 -0.1437 241 PRO B CD  
4255 N N   . LEU B 242 ? 0.8644 1.4531 0.7006 -0.2660 -0.1331 -0.1477 242 LEU B N   
4256 C CA  . LEU B 242 ? 0.8048 1.4458 0.6761 -0.2631 -0.1361 -0.1378 242 LEU B CA  
4257 C C   . LEU B 242 ? 0.8023 1.5009 0.6820 -0.2624 -0.1426 -0.1367 242 LEU B C   
4258 O O   . LEU B 242 ? 0.7984 1.5006 0.6621 -0.2834 -0.1413 -0.1532 242 LEU B O   
4259 C CB  . LEU B 242 ? 0.7704 1.3989 0.6458 -0.2871 -0.1286 -0.1498 242 LEU B CB  
4260 C CG  . LEU B 242 ? 0.7088 1.3655 0.6175 -0.2827 -0.1281 -0.1394 242 LEU B CG  
4261 C CD1 . LEU B 242 ? 0.7471 1.3755 0.6496 -0.3088 -0.1185 -0.1543 242 LEU B CD1 
4262 C CD2 . LEU B 242 ? 0.7197 1.4453 0.6541 -0.2754 -0.1342 -0.1308 242 LEU B CD2 
4263 N N   . THR B 243 ? 0.7800 1.5227 0.6838 -0.2383 -0.1486 -0.1176 243 THR B N   
4264 C CA  . THR B 243 ? 0.7598 1.5598 0.6722 -0.2332 -0.1545 -0.1142 243 THR B CA  
4265 C C   . THR B 243 ? 0.6942 1.5415 0.6331 -0.2377 -0.1544 -0.1120 243 THR B C   
4266 O O   . THR B 243 ? 0.6666 1.5043 0.6209 -0.2388 -0.1505 -0.1084 243 THR B O   
4267 C CB  . THR B 243 ? 0.7756 1.5926 0.6931 -0.2017 -0.1597 -0.0939 243 THR B CB  
4268 O OG1 . THR B 243 ? 0.7648 1.6083 0.7105 -0.1816 -0.1599 -0.0749 243 THR B OG1 
4269 C CG2 . THR B 243 ? 0.8086 1.5733 0.7067 -0.1921 -0.1579 -0.0911 243 THR B CG2 
4270 N N   . GLN B 244 ? 0.7330 1.6337 0.6769 -0.2388 -0.1588 -0.1140 244 GLN B N   
4271 C CA  . GLN B 244 ? 0.6976 1.6515 0.6657 -0.2392 -0.1593 -0.1108 244 GLN B CA  
4272 C C   . GLN B 244 ? 0.6809 1.6509 0.6726 -0.2085 -0.1605 -0.0868 244 GLN B C   
4273 O O   . GLN B 244 ? 0.6632 1.6555 0.6754 -0.2078 -0.1583 -0.0827 244 GLN B O   
4274 C CB  . GLN B 244 ? 0.6847 1.6943 0.6508 -0.2441 -0.1641 -0.1177 244 GLN B CB  
4275 C CG  . GLN B 244 ? 0.6943 1.7688 0.6853 -0.2331 -0.1663 -0.1087 244 GLN B CG  
4276 C CD  . GLN B 244 ? 0.7353 1.8114 0.7438 -0.2447 -0.1608 -0.1115 244 GLN B CD  
4277 O OE1 . GLN B 244 ? 0.7066 1.7756 0.7097 -0.2748 -0.1561 -0.1306 244 GLN B OE1 
4278 N NE2 . GLN B 244 ? 0.6789 1.7602 0.7073 -0.2206 -0.1604 -0.0922 244 GLN B NE2 
4279 N N   . ASP B 245 ? 0.6793 1.6361 0.6673 -0.1830 -0.1628 -0.0708 245 ASP B N   
4280 C CA  . ASP B 245 ? 0.6836 1.6468 0.6913 -0.1547 -0.1618 -0.0480 245 ASP B CA  
4281 C C   . ASP B 245 ? 0.6773 1.6004 0.6940 -0.1594 -0.1564 -0.0470 245 ASP B C   
4282 O O   . ASP B 245 ? 0.6605 1.5960 0.6983 -0.1460 -0.1542 -0.0341 245 ASP B O   
4283 C CB  . ASP B 245 ? 0.7751 1.7274 0.7741 -0.1287 -0.1636 -0.0320 245 ASP B CB  
4284 C CG  . ASP B 245 ? 0.8393 1.8255 0.8547 -0.0984 -0.1635 -0.0094 245 ASP B CG  
4285 O OD1 . ASP B 245 ? 0.8430 1.8303 0.8773 -0.0899 -0.1598 0.0005  245 ASP B OD1 
4286 O OD2 . ASP B 245 ? 0.8857 1.8965 0.8937 -0.0829 -0.1664 -0.0018 245 ASP B OD2 
4287 N N   . HIS B 246 ? 0.6818 1.5554 0.6813 -0.1772 -0.1539 -0.0604 246 HIS B N   
4288 C CA  . HIS B 246 ? 0.6590 1.4939 0.6644 -0.1852 -0.1484 -0.0627 246 HIS B CA  
4289 C C   . HIS B 246 ? 0.6351 1.4896 0.6545 -0.2037 -0.1452 -0.0719 246 HIS B C   
4290 O O   . HIS B 246 ? 0.5631 1.4150 0.6016 -0.1972 -0.1420 -0.0634 246 HIS B O   
4291 C CB  . HIS B 246 ? 0.6555 1.4346 0.6344 -0.2013 -0.1458 -0.0774 246 HIS B CB  
4292 C CG  . HIS B 246 ? 0.6743 1.4267 0.6405 -0.1823 -0.1474 -0.0678 246 HIS B CG  
4293 N ND1 . HIS B 246 ? 0.7243 1.4427 0.6611 -0.1912 -0.1474 -0.0798 246 HIS B ND1 
4294 C CD2 . HIS B 246 ? 0.6357 1.3889 0.6134 -0.1550 -0.1480 -0.0475 246 HIS B CD2 
4295 C CE1 . HIS B 246 ? 0.6764 1.3781 0.6078 -0.1701 -0.1483 -0.0676 246 HIS B CE1 
4296 N NE2 . HIS B 246 ? 0.6292 1.3513 0.5853 -0.1487 -0.1484 -0.0479 246 HIS B NE2 
4297 N N   . VAL B 247 ? 0.6349 1.5096 0.6449 -0.2274 -0.1454 -0.0894 247 VAL B N   
4298 C CA  . VAL B 247 ? 0.5725 1.4695 0.5951 -0.2457 -0.1415 -0.0986 247 VAL B CA  
4299 C C   . VAL B 247 ? 0.5671 1.5094 0.6177 -0.2241 -0.1433 -0.0812 247 VAL B C   
4300 O O   . VAL B 247 ? 0.5695 1.5095 0.6359 -0.2263 -0.1390 -0.0789 247 VAL B O   
4301 C CB  . VAL B 247 ? 0.6769 1.5984 0.6861 -0.2717 -0.1415 -0.1184 247 VAL B CB  
4302 C CG1 . VAL B 247 ? 0.6212 1.5660 0.6427 -0.2918 -0.1364 -0.1284 247 VAL B CG1 
4303 C CG2 . VAL B 247 ? 0.7204 1.5896 0.6990 -0.2922 -0.1381 -0.1352 247 VAL B CG2 
4304 N N   . ASP B 248 ? 0.5817 1.5623 0.6369 -0.2011 -0.1489 -0.0679 248 ASP B N   
4305 C CA  . ASP B 248 ? 0.5710 1.5959 0.6488 -0.1791 -0.1499 -0.0515 248 ASP B CA  
4306 C C   . ASP B 248 ? 0.5545 1.5524 0.6464 -0.1562 -0.1467 -0.0325 248 ASP B C   
4307 O O   . ASP B 248 ? 0.5241 1.5428 0.6351 -0.1458 -0.1445 -0.0231 248 ASP B O   
4308 C CB  . ASP B 248 ? 0.6259 1.6960 0.7009 -0.1604 -0.1556 -0.0429 248 ASP B CB  
4309 C CG  . ASP B 248 ? 0.5881 1.7196 0.6695 -0.1704 -0.1576 -0.0519 248 ASP B CG  
4310 O OD1 . ASP B 248 ? 0.5828 1.7225 0.6727 -0.1905 -0.1542 -0.0632 248 ASP B OD1 
4311 O OD2 . ASP B 248 ? 0.5974 1.7698 0.6750 -0.1586 -0.1623 -0.0480 248 ASP B OD2 
4312 N N   . ILE B 249 ? 0.5493 1.5020 0.6318 -0.1479 -0.1460 -0.0268 249 ILE B N   
4313 C CA  . ILE B 249 ? 0.6160 1.5417 0.7117 -0.1284 -0.1421 -0.0102 249 ILE B CA  
4314 C C   . ILE B 249 ? 0.5898 1.4898 0.6945 -0.1460 -0.1369 -0.0190 249 ILE B C   
4315 O O   . ILE B 249 ? 0.5020 1.4040 0.6258 -0.1339 -0.1334 -0.0078 249 ILE B O   
4316 C CB  . ILE B 249 ? 0.6107 1.4979 0.6931 -0.1164 -0.1424 -0.0032 249 ILE B CB  
4317 C CG1 . ILE B 249 ? 0.6229 1.4869 0.7190 -0.0937 -0.1378 0.0156  249 ILE B CG1 
4318 C CG2 . ILE B 249 ? 0.6150 1.4580 0.6797 -0.1403 -0.1415 -0.0211 249 ILE B CG2 
4319 C CD1 . ILE B 249 ? 0.6906 1.5448 0.7777 -0.0704 -0.1382 0.0306  249 ILE B CD1 
4320 N N   . LEU B 250 ? 0.5672 1.4413 0.6568 -0.1745 -0.1356 -0.0392 250 LEU B N   
4321 C CA  . LEU B 250 ? 0.5922 1.4416 0.6861 -0.1947 -0.1296 -0.0502 250 LEU B CA  
4322 C C   . LEU B 250 ? 0.5652 1.4569 0.6752 -0.2020 -0.1281 -0.0530 250 LEU B C   
4323 O O   . LEU B 250 ? 0.5740 1.4517 0.6899 -0.2179 -0.1225 -0.0609 250 LEU B O   
4324 C CB  . LEU B 250 ? 0.5519 1.3641 0.6204 -0.2239 -0.1271 -0.0720 250 LEU B CB  
4325 C CG  . LEU B 250 ? 0.5143 1.2732 0.5643 -0.2220 -0.1263 -0.0734 250 LEU B CG  
4326 C CD1 . LEU B 250 ? 0.5162 1.2484 0.5358 -0.2487 -0.1244 -0.0952 250 LEU B CD1 
4327 C CD2 . LEU B 250 ? 0.4671 1.1879 0.5259 -0.2181 -0.1210 -0.0685 250 LEU B CD2 
4328 N N   . GLY B 251 ? 0.5235 1.4673 0.6399 -0.1903 -0.1327 -0.0467 251 GLY B N   
4329 C CA  . GLY B 251 ? 0.5388 1.5285 0.6669 -0.1997 -0.1320 -0.0524 251 GLY B CA  
4330 C C   . GLY B 251 ? 0.4880 1.4804 0.6372 -0.1947 -0.1273 -0.0455 251 GLY B C   
4331 O O   . GLY B 251 ? 0.4981 1.5001 0.6508 -0.2164 -0.1234 -0.0585 251 GLY B O   
4332 N N   . PRO B 252 ? 0.5038 1.4889 0.6668 -0.1663 -0.1266 -0.0251 252 PRO B N   
4333 C CA  . PRO B 252 ? 0.5002 1.4875 0.6832 -0.1609 -0.1217 -0.0185 252 PRO B CA  
4334 C C   . PRO B 252 ? 0.4953 1.4333 0.6780 -0.1797 -0.1153 -0.0281 252 PRO B C   
4335 O O   . PRO B 252 ? 0.4940 1.4369 0.6895 -0.1867 -0.1107 -0.0305 252 PRO B O   
4336 C CB  . PRO B 252 ? 0.4944 1.4820 0.6885 -0.1249 -0.1216 0.0059  252 PRO B CB  
4337 C CG  . PRO B 252 ? 0.4990 1.4859 0.6793 -0.1119 -0.1261 0.0122  252 PRO B CG  
4338 C CD  . PRO B 252 ? 0.5150 1.4992 0.6761 -0.1372 -0.1298 -0.0069 252 PRO B CD  
4339 N N   . LEU B 253 ? 0.5387 1.4296 0.7064 -0.1870 -0.1146 -0.0333 253 LEU B N   
4340 C CA  . LEU B 253 ? 0.4998 1.3437 0.6628 -0.2066 -0.1079 -0.0444 253 LEU B CA  
4341 C C   . LEU B 253 ? 0.5411 1.3888 0.6917 -0.2401 -0.1046 -0.0664 253 LEU B C   
4342 O O   . LEU B 253 ? 0.4623 1.2996 0.6185 -0.2546 -0.0978 -0.0733 253 LEU B O   
4343 C CB  . LEU B 253 ? 0.4197 1.2149 0.5667 -0.2053 -0.1081 -0.0451 253 LEU B CB  
4344 C CG  . LEU B 253 ? 0.3897 1.1604 0.5465 -0.1794 -0.1076 -0.0273 253 LEU B CG  
4345 C CD1 . LEU B 253 ? 0.3881 1.1155 0.5249 -0.1842 -0.1081 -0.0332 253 LEU B CD1 
4346 C CD2 . LEU B 253 ? 0.4151 1.1709 0.5909 -0.1749 -0.1009 -0.0212 253 LEU B CD2 
4347 N N   . SER B 254 ? 0.5505 1.4108 0.6828 -0.2531 -0.1082 -0.0778 254 SER B N   
4348 C CA  . SER B 254 ? 0.5163 1.3881 0.6365 -0.2842 -0.1045 -0.0984 254 SER B CA  
4349 C C   . SER B 254 ? 0.5517 1.4720 0.6915 -0.2862 -0.1032 -0.0978 254 SER B C   
4350 O O   . SER B 254 ? 0.5947 1.5146 0.7299 -0.3125 -0.0966 -0.1134 254 SER B O   
4351 C CB  . SER B 254 ? 0.5396 1.4293 0.6414 -0.2915 -0.1098 -0.1071 254 SER B CB  
4352 O OG  . SER B 254 ? 0.5730 1.4894 0.6676 -0.3180 -0.1069 -0.1248 254 SER B OG  
4353 N N   . ALA B 255 ? 0.5045 1.4655 0.6644 -0.2586 -0.1085 -0.0802 255 ALA B N   
4354 C CA  . ALA B 255 ? 0.5112 1.5216 0.6888 -0.2580 -0.1078 -0.0790 255 ALA B CA  
4355 C C   . ALA B 255 ? 0.4944 1.4838 0.6877 -0.2558 -0.1012 -0.0739 255 ALA B C   
4356 O O   . ALA B 255 ? 0.5191 1.5236 0.7176 -0.2737 -0.0963 -0.0840 255 ALA B O   
4357 C CB  . ALA B 255 ? 0.5112 1.5728 0.7006 -0.2283 -0.1151 -0.0623 255 ALA B CB  
4358 N N   . GLN B 256 ? 0.4874 1.4435 0.6886 -0.2337 -0.1007 -0.0582 256 GLN B N   
4359 C CA  . GLN B 256 ? 0.5148 1.4479 0.7311 -0.2303 -0.0941 -0.0528 256 GLN B CA  
4360 C C   . GLN B 256 ? 0.5072 1.4055 0.7123 -0.2624 -0.0857 -0.0715 256 GLN B C   
4361 O O   . GLN B 256 ? 0.5291 1.4351 0.7444 -0.2718 -0.0800 -0.0754 256 GLN B O   
4362 C CB  . GLN B 256 ? 0.5429 1.4361 0.7642 -0.2070 -0.0936 -0.0368 256 GLN B CB  
4363 C CG  . GLN B 256 ? 0.5988 1.4921 0.8423 -0.1877 -0.0895 -0.0223 256 GLN B CG  
4364 C CD  . GLN B 256 ? 0.6759 1.5221 0.9221 -0.1714 -0.0866 -0.0108 256 GLN B CD  
4365 O OE1 . GLN B 256 ? 0.6414 1.4738 0.8787 -0.1603 -0.0904 -0.0049 256 GLN B OE1 
4366 N NE2 . GLN B 256 ? 0.7081 1.5384 0.9698 -0.1642 -0.0803 -0.0042 256 GLN B NE2 
4367 N N   . THR B 257 ? 0.4992 1.3573 0.6811 -0.2793 -0.0841 -0.0833 257 THR B N   
4368 C CA  . THR B 257 ? 0.5604 1.3741 0.7253 -0.3085 -0.0744 -0.1005 257 THR B CA  
4369 C C   . THR B 257 ? 0.5322 1.3669 0.6840 -0.3388 -0.0706 -0.1202 257 THR B C   
4370 O O   . THR B 257 ? 0.5546 1.3499 0.6887 -0.3642 -0.0607 -0.1350 257 THR B O   
4371 C CB  . THR B 257 ? 0.5682 1.3259 0.7097 -0.3130 -0.0733 -0.1052 257 THR B CB  
4372 O OG1 . THR B 257 ? 0.5068 1.2808 0.6338 -0.3142 -0.0803 -0.1094 257 THR B OG1 
4373 C CG2 . THR B 257 ? 0.4992 1.2300 0.6523 -0.2870 -0.0749 -0.0882 257 THR B CG2 
4374 N N   . GLY B 258 ? 0.5438 1.4372 0.7017 -0.3372 -0.0771 -0.1211 258 GLY B N   
4375 C CA  . GLY B 258 ? 0.5826 1.4980 0.7277 -0.3673 -0.0729 -0.1409 258 GLY B CA  
4376 C C   . GLY B 258 ? 0.6114 1.4852 0.7247 -0.3921 -0.0681 -0.1581 258 GLY B C   
4377 O O   . GLY B 258 ? 0.6477 1.5212 0.7463 -0.4217 -0.0602 -0.1764 258 GLY B O   
4378 N N   . ILE B 259 ? 0.6016 1.4409 0.7024 -0.3809 -0.0722 -0.1530 259 ILE B N   
4379 C CA  . ILE B 259 ? 0.6635 1.4563 0.7315 -0.4018 -0.0672 -0.1684 259 ILE B CA  
4380 C C   . ILE B 259 ? 0.6294 1.4457 0.6900 -0.3924 -0.0773 -0.1667 259 ILE B C   
4381 O O   . ILE B 259 ? 0.5999 1.4162 0.6684 -0.3657 -0.0856 -0.1511 259 ILE B O   
4382 C CB  . ILE B 259 ? 0.6162 1.3369 0.6705 -0.3987 -0.0613 -0.1661 259 ILE B CB  
4383 C CG1 . ILE B 259 ? 0.6240 1.3141 0.6785 -0.4129 -0.0491 -0.1712 259 ILE B CG1 
4384 C CG2 . ILE B 259 ? 0.6611 1.3350 0.6800 -0.4137 -0.0579 -0.1792 259 ILE B CG2 
4385 C CD1 . ILE B 259 ? 0.6076 1.2335 0.6535 -0.4041 -0.0442 -0.1657 259 ILE B CD1 
4386 N N   . ALA B 260 ? 0.6661 1.4990 0.7099 -0.4149 -0.0755 -0.1831 260 ALA B N   
4387 C CA  . ALA B 260 ? 0.6707 1.5295 0.7076 -0.4068 -0.0849 -0.1822 260 ALA B CA  
4388 C C   . ALA B 260 ? 0.6795 1.4839 0.6967 -0.3973 -0.0868 -0.1789 260 ALA B C   
4389 O O   . ALA B 260 ? 0.6772 1.4193 0.6713 -0.4121 -0.0778 -0.1884 260 ALA B O   
4390 C CB  . ALA B 260 ? 0.7154 1.5963 0.7358 -0.4360 -0.0810 -0.2026 260 ALA B CB  
4391 N N   . VAL B 261 ? 0.6448 1.4725 0.6698 -0.3714 -0.0978 -0.1649 261 VAL B N   
4392 C CA  . VAL B 261 ? 0.6323 1.4185 0.6395 -0.3602 -0.1011 -0.1612 261 VAL B CA  
4393 C C   . VAL B 261 ? 0.6951 1.4360 0.6672 -0.3876 -0.0937 -0.1818 261 VAL B C   
4394 O O   . VAL B 261 ? 0.7056 1.3847 0.6567 -0.3893 -0.0888 -0.1848 261 VAL B O   
4395 C CB  . VAL B 261 ? 0.6184 1.4460 0.6334 -0.3355 -0.1128 -0.1483 261 VAL B CB  
4396 C CG1 . VAL B 261 ? 0.6504 1.4344 0.6499 -0.3203 -0.1159 -0.1417 261 VAL B CG1 
4397 C CG2 . VAL B 261 ? 0.5899 1.4678 0.6366 -0.3104 -0.1182 -0.1294 261 VAL B CG2 
4398 N N   . LEU B 262 ? 0.7066 1.4780 0.6711 -0.4086 -0.0921 -0.1961 262 LEU B N   
4399 C CA  . LEU B 262 ? 0.7753 1.5063 0.7057 -0.4362 -0.0836 -0.2163 262 LEU B CA  
4400 C C   . LEU B 262 ? 0.7778 1.4443 0.6901 -0.4554 -0.0690 -0.2262 262 LEU B C   
4401 O O   . LEU B 262 ? 0.7902 1.3927 0.6716 -0.4622 -0.0623 -0.2336 262 LEU B O   
4402 C CB  . LEU B 262 ? 0.7988 1.5819 0.7297 -0.4569 -0.0832 -0.2298 262 LEU B CB  
4403 C CG  . LEU B 262 ? 0.8404 1.6749 0.7756 -0.4444 -0.0952 -0.2261 262 LEU B CG  
4404 C CD1 . LEU B 262 ? 0.8730 1.6629 0.7786 -0.4445 -0.0961 -0.2313 262 LEU B CD1 
4405 C CD2 . LEU B 262 ? 0.7379 1.6164 0.7035 -0.4090 -0.1069 -0.2029 262 LEU B CD2 
4406 N N   . ASP B 263 ? 0.7653 1.4463 0.6949 -0.4632 -0.0632 -0.2260 263 ASP B N   
4407 C CA  . ASP B 263 ? 0.8080 1.4283 0.7201 -0.4808 -0.0482 -0.2346 263 ASP B CA  
4408 C C   . ASP B 263 ? 0.7854 1.3472 0.6895 -0.4623 -0.0478 -0.2246 263 ASP B C   
4409 O O   . ASP B 263 ? 0.7883 1.2813 0.6602 -0.4730 -0.0368 -0.2335 263 ASP B O   
4410 C CB  . ASP B 263 ? 0.7797 1.4319 0.7152 -0.4885 -0.0436 -0.2339 263 ASP B CB  
4411 C CG  . ASP B 263 ? 0.8142 1.5132 0.7500 -0.5131 -0.0402 -0.2485 263 ASP B CG  
4412 O OD1 . ASP B 263 ? 0.8454 1.5448 0.7607 -0.5268 -0.0398 -0.2603 263 ASP B OD1 
4413 O OD2 . ASP B 263 ? 0.8146 1.5504 0.7706 -0.5187 -0.0378 -0.2485 263 ASP B OD2 
4414 N N   . MET B 264 ? 0.7527 1.3401 0.6842 -0.4334 -0.0589 -0.2059 264 MET B N   
4415 C CA  . MET B 264 ? 0.7051 1.2424 0.6305 -0.4157 -0.0590 -0.1967 264 MET B CA  
4416 C C   . MET B 264 ? 0.7327 1.2259 0.6252 -0.4138 -0.0596 -0.2024 264 MET B C   
4417 O O   . MET B 264 ? 0.7533 1.1825 0.6222 -0.4123 -0.0525 -0.2050 264 MET B O   
4418 C CB  . MET B 264 ? 0.6566 1.2329 0.6172 -0.3852 -0.0705 -0.1754 264 MET B CB  
4419 C CG  . MET B 264 ? 0.6657 1.1919 0.6219 -0.3702 -0.0688 -0.1676 264 MET B CG  
4420 S SD  . MET B 264 ? 0.7282 1.2269 0.6935 -0.3792 -0.0570 -0.1683 264 MET B SD  
4421 C CE  . MET B 264 ? 0.6051 1.1646 0.6198 -0.3535 -0.0659 -0.1465 264 MET B CE  
4422 N N   . CYS B 265 ? 0.7208 1.2464 0.6097 -0.4125 -0.0675 -0.2045 265 CYS B N   
4423 C CA  . CYS B 265 ? 0.8181 1.3012 0.6735 -0.4119 -0.0672 -0.2113 265 CYS B CA  
4424 C C   . CYS B 265 ? 0.8689 1.2830 0.6853 -0.4360 -0.0510 -0.2287 265 CYS B C   
4425 O O   . CYS B 265 ? 0.8649 1.2179 0.6517 -0.4297 -0.0464 -0.2311 265 CYS B O   
4426 C CB  . CYS B 265 ? 0.8584 1.3895 0.7153 -0.4114 -0.0764 -0.2132 265 CYS B CB  
4427 S SG  . CYS B 265 ? 0.7766 1.3624 0.6645 -0.3752 -0.0935 -0.1902 265 CYS B SG  
4428 N N   . ALA B 266 ? 0.8809 1.3030 0.6953 -0.4624 -0.0412 -0.2408 266 ALA B N   
4429 C CA  . ALA B 266 ? 0.8718 1.2274 0.6479 -0.4859 -0.0235 -0.2566 266 ALA B CA  
4430 C C   . ALA B 266 ? 0.9230 1.2135 0.6862 -0.4789 -0.0134 -0.2526 266 ALA B C   
4431 O O   . ALA B 266 ? 0.9256 1.1453 0.6509 -0.4789 -0.0035 -0.2583 266 ALA B O   
4432 C CB  . ALA B 266 ? 0.9067 1.2914 0.6864 -0.5153 -0.0150 -0.2692 266 ALA B CB  
4433 N N   . SER B 267 ? 0.8529 1.1657 0.6465 -0.4706 -0.0155 -0.2422 267 SER B N   
4434 C CA  . SER B 267 ? 0.9113 1.1673 0.6957 -0.4609 -0.0075 -0.2372 267 SER B CA  
4435 C C   . SER B 267 ? 0.9003 1.1203 0.6698 -0.4363 -0.0135 -0.2302 267 SER B C   
4436 O O   . SER B 267 ? 0.9265 1.0778 0.6672 -0.4309 -0.0031 -0.2319 267 SER B O   
4437 C CB  . SER B 267 ? 0.8607 1.1557 0.6848 -0.4534 -0.0113 -0.2257 267 SER B CB  
4438 O OG  . SER B 267 ? 0.8656 1.2023 0.7048 -0.4738 -0.0072 -0.2320 267 SER B OG  
4439 N N   . LEU B 268 ? 0.8882 1.1551 0.6771 -0.4189 -0.0297 -0.2212 268 LEU B N   
4440 C CA  . LEU B 268 ? 0.8917 1.1282 0.6647 -0.3962 -0.0351 -0.2157 268 LEU B CA  
4441 C C   . LEU B 268 ? 0.9484 1.1272 0.6744 -0.4032 -0.0263 -0.2284 268 LEU B C   
4442 O O   . LEU B 268 ? 0.9982 1.1166 0.6951 -0.3900 -0.0203 -0.2286 268 LEU B O   
4443 C CB  . LEU B 268 ? 0.8028 1.1035 0.6052 -0.3770 -0.0529 -0.2030 268 LEU B CB  
4444 C CG  . LEU B 268 ? 0.7586 1.0372 0.5477 -0.3525 -0.0593 -0.1960 268 LEU B CG  
4445 C CD1 . LEU B 268 ? 0.7686 0.9958 0.5476 -0.3396 -0.0533 -0.1923 268 LEU B CD1 
4446 C CD2 . LEU B 268 ? 0.7082 1.0509 0.5309 -0.3337 -0.0744 -0.1809 268 LEU B CD2 
4447 N N   . LYS B 269 ? 0.9567 1.1516 0.6732 -0.4232 -0.0242 -0.2393 269 LYS B N   
4448 C CA  . LYS B 269 ? 1.0218 1.1601 0.6933 -0.4312 -0.0142 -0.2516 269 LYS B CA  
4449 C C   . LYS B 269 ? 1.0774 1.1334 0.7145 -0.4334 0.0040  -0.2562 269 LYS B C   
4450 O O   . LYS B 269 ? 1.1190 1.1166 0.7223 -0.4189 0.0095  -0.2569 269 LYS B O   
4451 C CB  . LYS B 269 ? 0.9346 1.1005 0.6020 -0.4578 -0.0115 -0.2643 269 LYS B CB  
4452 C CG  . LYS B 269 ? 1.0681 1.1869 0.6936 -0.4633 -0.0045 -0.2754 269 LYS B CG  
4453 C CD  . LYS B 269 ? 1.0855 1.2102 0.6984 -0.4959 0.0054  -0.2910 269 LYS B CD  
4454 C CE  . LYS B 269 ? 1.0649 1.2711 0.7053 -0.5033 -0.0084 -0.2927 269 LYS B CE  
4455 N NZ  . LYS B 269 ? 1.0733 1.2776 0.6934 -0.5340 0.0017  -0.3101 269 LYS B NZ  
4456 N N   . GLU B 270 ? 1.0401 1.0908 0.6843 -0.4499 0.0143  -0.2587 270 GLU B N   
4457 C CA  . GLU B 270 ? 1.0728 1.0451 0.6825 -0.4524 0.0333  -0.2624 270 GLU B CA  
4458 C C   . GLU B 270 ? 1.1350 1.0717 0.7414 -0.4235 0.0320  -0.2514 270 GLU B C   
4459 O O   . GLU B 270 ? 1.1803 1.0460 0.7487 -0.4121 0.0440  -0.2524 270 GLU B O   
4460 C CB  . GLU B 270 ? 1.0970 1.0790 0.7178 -0.4763 0.0442  -0.2668 270 GLU B CB  
4461 C CG  . GLU B 270 ? 1.2000 1.1118 0.7947 -0.4758 0.0627  -0.2664 270 GLU B CG  
4462 C CD  . GLU B 270 ? 1.2479 1.1681 0.8456 -0.5045 0.0756  -0.2742 270 GLU B CD  
4463 O OE1 . GLU B 270 ? 1.2719 1.2369 0.8786 -0.5263 0.0732  -0.2832 270 GLU B OE1 
4464 O OE2 . GLU B 270 ? 1.2737 1.1580 0.8643 -0.5049 0.0882  -0.2714 270 GLU B OE2 
4465 N N   . LEU B 271 ? 1.0717 1.0575 0.7171 -0.4099 0.0181  -0.2404 271 LEU B N   
4466 C CA  . LEU B 271 ? 1.0496 1.0072 0.6927 -0.3825 0.0158  -0.2308 271 LEU B CA  
4467 C C   . LEU B 271 ? 1.1023 1.0276 0.7158 -0.3621 0.0135  -0.2308 271 LEU B C   
4468 O O   . LEU B 271 ? 1.1351 1.0045 0.7227 -0.3418 0.0209  -0.2280 271 LEU B O   
4469 C CB  . LEU B 271 ? 0.9878 1.0115 0.6793 -0.3724 -0.0001 -0.2189 271 LEU B CB  
4470 C CG  . LEU B 271 ? 0.9694 1.0155 0.6915 -0.3815 0.0026  -0.2146 271 LEU B CG  
4471 C CD1 . LEU B 271 ? 0.8690 0.9818 0.6386 -0.3668 -0.0143 -0.2008 271 LEU B CD1 
4472 C CD2 . LEU B 271 ? 0.9994 0.9761 0.6969 -0.3757 0.0177  -0.2151 271 LEU B CD2 
4473 N N   . LEU B 272 ? 1.0326 0.9933 0.6490 -0.3656 0.0038  -0.2336 272 LEU B N   
4474 C CA  . LEU B 272 ? 1.1465 1.0821 0.7367 -0.3460 0.0011  -0.2334 272 LEU B CA  
4475 C C   . LEU B 272 ? 1.1994 1.0636 0.7414 -0.3506 0.0177  -0.2433 272 LEU B C   
4476 O O   . LEU B 272 ? 1.2133 1.0290 0.7266 -0.3277 0.0226  -0.2410 272 LEU B O   
4477 C CB  . LEU B 272 ? 1.2033 1.2022 0.8133 -0.3474 -0.0146 -0.2322 272 LEU B CB  
4478 C CG  . LEU B 272 ? 1.0911 1.1631 0.7463 -0.3360 -0.0323 -0.2192 272 LEU B CG  
4479 C CD1 . LEU B 272 ? 1.0283 1.1692 0.7136 -0.3543 -0.0409 -0.2203 272 LEU B CD1 
4480 C CD2 . LEU B 272 ? 1.0333 1.1123 0.6839 -0.3106 -0.0417 -0.2117 272 LEU B CD2 
4481 N N   . GLN B 273 ? 1.2092 1.0679 0.7422 -0.3788 0.0270  -0.2536 273 GLN B N   
4482 C CA  . GLN B 273 ? 1.2581 1.0494 0.7452 -0.3853 0.0440  -0.2624 273 GLN B CA  
4483 C C   . GLN B 273 ? 1.3042 1.0293 0.7678 -0.3777 0.0610  -0.2594 273 GLN B C   
4484 O O   . GLN B 273 ? 1.3612 1.0220 0.7842 -0.3686 0.0742  -0.2613 273 GLN B O   
4485 C CB  . GLN B 273 ? 1.2198 1.0296 0.7048 -0.4198 0.0493  -0.2747 273 GLN B CB  
4486 C CG  . GLN B 273 ? 1.2208 1.0932 0.7246 -0.4264 0.0338  -0.2782 273 GLN B CG  
4487 C CD  . GLN B 273 ? 1.3105 1.1928 0.8042 -0.4589 0.0410  -0.2922 273 GLN B CD  
4488 O OE1 . GLN B 273 ? 1.2630 1.2134 0.7860 -0.4738 0.0305  -0.2949 273 GLN B OE1 
4489 N NE2 . GLN B 273 ? 1.3767 1.1918 0.8284 -0.4695 0.0598  -0.3006 273 GLN B NE2 
4490 N N   . ASN B 274 ? 1.2746 1.0148 0.7629 -0.3793 0.0609  -0.2538 274 ASN B N   
4491 C CA  . ASN B 274 ? 1.2646 0.9477 0.7327 -0.3774 0.0781  -0.2516 274 ASN B CA  
4492 C C   . ASN B 274 ? 1.2886 0.9608 0.7667 -0.3487 0.0749  -0.2400 274 ASN B C   
4493 O O   . ASN B 274 ? 1.2894 0.9172 0.7530 -0.3439 0.0883  -0.2366 274 ASN B O   
4494 C CB  . ASN B 274 ? 1.2728 0.9777 0.7571 -0.4092 0.0853  -0.2569 274 ASN B CB  
4495 C CG  . ASN B 274 ? 1.3224 1.0263 0.7892 -0.4387 0.0936  -0.2696 274 ASN B CG  
4496 O OD1 . ASN B 274 ? 1.3432 1.1060 0.8371 -0.4624 0.0872  -0.2755 274 ASN B OD1 
4497 N ND2 . ASN B 274 ? 1.3775 1.0154 0.7984 -0.4367 0.1085  -0.2737 274 ASN B ND2 
4498 N N   . GLY B 275 ? 1.2529 0.9644 0.7544 -0.3295 0.0582  -0.2337 275 GLY B N   
4499 C CA  . GLY B 275 ? 1.2061 0.9072 0.7170 -0.3050 0.0569  -0.2238 275 GLY B CA  
4500 C C   . GLY B 275 ? 1.1811 0.9054 0.7211 -0.3207 0.0582  -0.2219 275 GLY B C   
4501 O O   . GLY B 275 ? 1.1586 0.9179 0.7172 -0.3485 0.0576  -0.2271 275 GLY B O   
4502 N N   . MET B 276 ? 1.1289 0.8338 0.6725 -0.3007 0.0606  -0.2141 276 MET B N   
4503 C CA  . MET B 276 ? 1.1916 0.9198 0.7657 -0.3099 0.0603  -0.2105 276 MET B CA  
4504 C C   . MET B 276 ? 1.2902 0.9583 0.8399 -0.3074 0.0791  -0.2090 276 MET B C   
4505 O O   . MET B 276 ? 1.2632 0.9421 0.8345 -0.3113 0.0808  -0.2052 276 MET B O   
4506 C CB  . MET B 276 ? 1.0997 0.8694 0.7135 -0.2844 0.0467  -0.1963 276 MET B CB  
4507 C CG  . MET B 276 ? 1.0099 0.8604 0.6715 -0.2880 0.0286  -0.1897 276 MET B CG  
4508 S SD  . MET B 276 ? 1.0134 0.9060 0.7265 -0.2545 0.0180  -0.1675 276 MET B SD  
4509 C CE  . MET B 276 ? 0.8392 0.8073 0.5866 -0.2530 -0.0011 -0.1613 276 MET B CE  
4510 N N   . ASN B 277 ? 1.3533 0.9599 0.8592 -0.2997 0.0933  -0.2106 277 ASN B N   
4511 C CA  . ASN B 277 ? 1.3869 0.9378 0.8669 -0.2990 0.1122  -0.2082 277 ASN B CA  
4512 C C   . ASN B 277 ? 1.3859 0.9217 0.8725 -0.2721 0.1131  -0.1980 277 ASN B C   
4513 O O   . ASN B 277 ? 1.4204 0.9299 0.9007 -0.2753 0.1254  -0.1949 277 ASN B O   
4514 C CB  . ASN B 277 ? 1.4080 0.9762 0.9001 -0.3346 0.1198  -0.2144 277 ASN B CB  
4515 C CG  . ASN B 277 ? 1.5427 1.0839 1.0034 -0.3564 0.1324  -0.2233 277 ASN B CG  
4516 O OD1 . ASN B 277 ? 1.5915 1.0964 1.0197 -0.3448 0.1361  -0.2243 277 ASN B OD1 
4517 N ND2 . ASN B 277 ? 1.6129 1.1719 1.0823 -0.3881 0.1399  -0.2300 277 ASN B ND2 
4518 N N   . GLY B 278 ? 1.3439 0.8976 0.8431 -0.2455 0.1006  -0.1927 278 GLY B N   
4519 C CA  . GLY B 278 ? 1.2935 0.8398 0.8024 -0.2206 0.1005  -0.1839 278 GLY B CA  
4520 C C   . GLY B 278 ? 1.2407 0.8320 0.7928 -0.2341 0.0937  -0.1820 278 GLY B C   
4521 O O   . GLY B 278 ? 1.2315 0.8180 0.7962 -0.2149 0.0958  -0.1723 278 GLY B O   
4522 N N   . ARG B 279 ? 1.2054 0.8516 0.7902 -0.2613 0.0846  -0.1855 279 ARG B N   
4523 C CA  . ARG B 279 ? 1.1659 0.8714 0.8038 -0.2707 0.0766  -0.1779 279 ARG B CA  
4524 C C   . ARG B 279 ? 1.0990 0.8713 0.7843 -0.2516 0.0573  -0.1652 279 ARG B C   
4525 O O   . ARG B 279 ? 1.1066 0.8788 0.7835 -0.2330 0.0507  -0.1630 279 ARG B O   
4526 C CB  . ARG B 279 ? 1.2292 0.9551 0.8709 -0.3120 0.0797  -0.1903 279 ARG B CB  
4527 C CG  . ARG B 279 ? 1.3078 0.9716 0.9057 -0.3258 0.1002  -0.1978 279 ARG B CG  
4528 C CD  . ARG B 279 ? 1.3257 1.0226 0.9354 -0.3604 0.1029  -0.2055 279 ARG B CD  
4529 N NE  . ARG B 279 ? 1.3714 1.1150 1.0228 -0.3729 0.0997  -0.2022 279 ARG B NE  
4530 C CZ  . ARG B 279 ? 1.3295 1.1128 0.9992 -0.4002 0.1015  -0.2074 279 ARG B CZ  
4531 N NH1 . ARG B 279 ? 1.3008 1.0828 0.9509 -0.4201 0.1066  -0.2173 279 ARG B NH1 
4532 N NH2 . ARG B 279 ? 1.2354 1.0637 0.9448 -0.4064 0.0979  -0.2025 279 ARG B NH2 
4533 N N   . THR B 280 ? 1.0163 0.8457 0.7506 -0.2563 0.0490  -0.1568 280 THR B N   
4534 C CA  . THR B 280 ? 0.9121 0.7999 0.6897 -0.2372 0.0330  -0.1435 280 THR B CA  
4535 C C   . THR B 280 ? 0.8529 0.8096 0.6721 -0.2565 0.0231  -0.1415 280 THR B C   
4536 O O   . THR B 280 ? 0.8849 0.8499 0.7093 -0.2811 0.0285  -0.1477 280 THR B O   
4537 C CB  . THR B 280 ? 0.8751 0.7609 0.6730 -0.2087 0.0327  -0.1302 280 THR B CB  
4538 O OG1 . THR B 280 ? 0.8656 0.7564 0.6811 -0.2188 0.0387  -0.1280 280 THR B OG1 
4539 C CG2 . THR B 280 ? 0.8793 0.7046 0.6373 -0.1867 0.0413  -0.1320 280 THR B CG2 
4540 N N   . ILE B 281 ? 0.7838 0.7904 0.6312 -0.2445 0.0090  -0.1327 281 ILE B N   
4541 C CA  . ILE B 281 ? 0.6984 0.7755 0.5869 -0.2546 -0.0019 -0.1273 281 ILE B CA  
4542 C C   . ILE B 281 ? 0.6764 0.7863 0.6026 -0.2270 -0.0099 -0.1094 281 ILE B C   
4543 O O   . ILE B 281 ? 0.6609 0.7656 0.5842 -0.2056 -0.0145 -0.1033 281 ILE B O   
4544 C CB  . ILE B 281 ? 0.7292 0.8346 0.6100 -0.2679 -0.0104 -0.1347 281 ILE B CB  
4545 C CG1 . ILE B 281 ? 0.7480 0.8054 0.5820 -0.2915 -0.0005 -0.1536 281 ILE B CG1 
4546 C CG2 . ILE B 281 ? 0.6511 0.8247 0.5659 -0.2829 -0.0194 -0.1329 281 ILE B CG2 
4547 C CD1 . ILE B 281 ? 0.7895 0.8797 0.6181 -0.3152 -0.0068 -0.1647 281 ILE B CD1 
4548 N N   . LEU B 282 ? 0.6224 0.7636 0.5823 -0.2275 -0.0104 -0.1014 282 LEU B N   
4549 C CA  . LEU B 282 ? 0.5582 0.7243 0.5514 -0.2023 -0.0155 -0.0850 282 LEU B CA  
4550 C C   . LEU B 282 ? 0.6287 0.7505 0.6064 -0.1782 -0.0115 -0.0814 282 LEU B C   
4551 O O   . LEU B 282 ? 0.6011 0.7381 0.5931 -0.1580 -0.0173 -0.0717 282 LEU B O   
4552 C CB  . LEU B 282 ? 0.5241 0.7461 0.5420 -0.1960 -0.0280 -0.0762 282 LEU B CB  
4553 C CG  . LEU B 282 ? 0.5832 0.8621 0.6258 -0.2138 -0.0333 -0.0762 282 LEU B CG  
4554 C CD1 . LEU B 282 ? 0.5181 0.8519 0.5844 -0.2021 -0.0451 -0.0650 282 LEU B CD1 
4555 C CD2 . LEU B 282 ? 0.5684 0.8572 0.6358 -0.2143 -0.0279 -0.0706 282 LEU B CD2 
4556 N N   . GLY B 283 ? 0.6227 0.6899 0.5691 -0.1803 -0.0008 -0.0898 283 GLY B N   
4557 C CA  . GLY B 283 ? 0.6145 0.6435 0.5467 -0.1565 0.0035  -0.0869 283 GLY B CA  
4558 C C   . GLY B 283 ? 0.7370 0.7469 0.6436 -0.1445 0.0009  -0.0904 283 GLY B C   
4559 O O   . GLY B 283 ? 0.7943 0.7910 0.6993 -0.1216 0.0012  -0.0858 283 GLY B O   
4560 N N   . SER B 284 ? 0.6935 0.7025 0.5794 -0.1593 -0.0013 -0.0991 284 SER B N   
4561 C CA  . SER B 284 ? 0.7320 0.7207 0.5907 -0.1481 -0.0029 -0.1031 284 SER B CA  
4562 C C   . SER B 284 ? 0.7588 0.7058 0.5729 -0.1659 0.0045  -0.1181 284 SER B C   
4563 O O   . SER B 284 ? 0.7960 0.7495 0.6079 -0.1919 0.0066  -0.1255 284 SER B O   
4564 C CB  . SER B 284 ? 0.7280 0.7655 0.6094 -0.1442 -0.0150 -0.0964 284 SER B CB  
4565 O OG  . SER B 284 ? 0.7489 0.7714 0.6004 -0.1448 -0.0165 -0.1041 284 SER B OG  
4566 N N   . ALA B 285 ? 0.7842 0.6888 0.5618 -0.1520 0.0091  -0.1231 285 ALA B N   
4567 C CA  . ALA B 285 ? 0.8404 0.7023 0.5715 -0.1667 0.0166  -0.1372 285 ALA B CA  
4568 C C   . ALA B 285 ? 0.8529 0.7371 0.5784 -0.1719 0.0082  -0.1410 285 ALA B C   
4569 O O   . ALA B 285 ? 0.9045 0.7515 0.5886 -0.1805 0.0141  -0.1528 285 ALA B O   
4570 C CB  . ALA B 285 ? 0.8921 0.6898 0.5799 -0.1480 0.0282  -0.1412 285 ALA B CB  
4571 N N   . LEU B 286 ? 0.7812 0.7233 0.5451 -0.1668 -0.0046 -0.1313 286 LEU B N   
4572 C CA  . LEU B 286 ? 0.8249 0.7933 0.5860 -0.1709 -0.0133 -0.1336 286 LEU B CA  
4573 C C   . LEU B 286 ? 0.7711 0.8005 0.5679 -0.1883 -0.0231 -0.1299 286 LEU B C   
4574 O O   . LEU B 286 ? 0.7433 0.8005 0.5736 -0.1897 -0.0248 -0.1218 286 LEU B O   
4575 C CB  . LEU B 286 ? 0.8218 0.8012 0.5907 -0.1432 -0.0187 -0.1244 286 LEU B CB  
4576 C CG  . LEU B 286 ? 0.8121 0.7390 0.5479 -0.1226 -0.0099 -0.1276 286 LEU B CG  
4577 C CD1 . LEU B 286 ? 0.7765 0.7240 0.5335 -0.0957 -0.0146 -0.1167 286 LEU B CD1 
4578 C CD2 . LEU B 286 ? 0.7990 0.6885 0.4874 -0.1283 -0.0053 -0.1405 286 LEU B CD2 
4579 N N   . LEU B 287 ? 0.7362 0.7876 0.5247 -0.2003 -0.0296 -0.1358 287 LEU B N   
4580 C CA  . LEU B 287 ? 0.6797 0.7960 0.5013 -0.2114 -0.0408 -0.1309 287 LEU B CA  
4581 C C   . LEU B 287 ? 0.6691 0.8242 0.5224 -0.1866 -0.0498 -0.1138 287 LEU B C   
4582 O O   . LEU B 287 ? 0.6749 0.8208 0.5158 -0.1710 -0.0517 -0.1116 287 LEU B O   
4583 C CB  . LEU B 287 ? 0.6738 0.7977 0.4715 -0.2327 -0.0440 -0.1445 287 LEU B CB  
4584 C CG  . LEU B 287 ? 0.7243 0.8049 0.4873 -0.2594 -0.0329 -0.1627 287 LEU B CG  
4585 C CD1 . LEU B 287 ? 0.7578 0.8401 0.4921 -0.2805 -0.0349 -0.1781 287 LEU B CD1 
4586 C CD2 . LEU B 287 ? 0.7296 0.8339 0.5172 -0.2783 -0.0310 -0.1634 287 LEU B CD2 
4587 N N   . GLU B 288 ? 0.6005 0.7967 0.4935 -0.1828 -0.0541 -0.1016 288 GLU B N   
4588 C CA  . GLU B 288 ? 0.5845 0.8117 0.5071 -0.1599 -0.0599 -0.0847 288 GLU B CA  
4589 C C   . GLU B 288 ? 0.5079 0.7892 0.4449 -0.1623 -0.0706 -0.0793 288 GLU B C   
4590 O O   . GLU B 288 ? 0.5066 0.8254 0.4574 -0.1781 -0.0751 -0.0810 288 GLU B O   
4591 C CB  . GLU B 288 ? 0.5941 0.8334 0.5492 -0.1529 -0.0574 -0.0739 288 GLU B CB  
4592 C CG  . GLU B 288 ? 0.6655 0.8562 0.6096 -0.1445 -0.0477 -0.0762 288 GLU B CG  
4593 C CD  . GLU B 288 ? 0.7447 0.9171 0.6836 -0.1209 -0.0465 -0.0708 288 GLU B CD  
4594 O OE1 . GLU B 288 ? 0.7222 0.9261 0.6799 -0.1089 -0.0522 -0.0601 288 GLU B OE1 
4595 O OE2 . GLU B 288 ? 0.7768 0.9041 0.6917 -0.1145 -0.0392 -0.0774 288 GLU B OE2 
4596 N N   . ASP B 289 ? 0.5093 0.7971 0.4434 -0.1461 -0.0743 -0.0726 289 ASP B N   
4597 C CA  . ASP B 289 ? 0.5049 0.8415 0.4491 -0.1453 -0.0839 -0.0665 289 ASP B CA  
4598 C C   . ASP B 289 ? 0.4627 0.8243 0.4341 -0.1219 -0.0859 -0.0472 289 ASP B C   
4599 O O   . ASP B 289 ? 0.4486 0.8388 0.4217 -0.1148 -0.0918 -0.0405 289 ASP B O   
4600 C CB  . ASP B 289 ? 0.4695 0.7940 0.3805 -0.1505 -0.0865 -0.0771 289 ASP B CB  
4601 C CG  . ASP B 289 ? 0.4765 0.7768 0.3763 -0.1289 -0.0837 -0.0718 289 ASP B CG  
4602 O OD1 . ASP B 289 ? 0.4742 0.7545 0.3843 -0.1136 -0.0780 -0.0648 289 ASP B OD1 
4603 O OD2 . ASP B 289 ? 0.5856 0.8880 0.4655 -0.1281 -0.0871 -0.0757 289 ASP B OD2 
4604 N N   . GLU B 290 ? 0.3843 0.7342 0.3755 -0.1101 -0.0802 -0.0383 290 GLU B N   
4605 C CA  . GLU B 290 ? 0.4200 0.7898 0.4355 -0.0899 -0.0800 -0.0208 290 GLU B CA  
4606 C C   . GLU B 290 ? 0.3847 0.7894 0.4319 -0.0881 -0.0813 -0.0092 290 GLU B C   
4607 O O   . GLU B 290 ? 0.3591 0.7658 0.4261 -0.0725 -0.0772 0.0039  290 GLU B O   
4608 C CB  . GLU B 290 ? 0.4051 0.7375 0.4182 -0.0751 -0.0721 -0.0189 290 GLU B CB  
4609 C CG  . GLU B 290 ? 0.4648 0.7690 0.4476 -0.0726 -0.0710 -0.0284 290 GLU B CG  
4610 C CD  . GLU B 290 ? 0.4964 0.7945 0.4825 -0.0537 -0.0672 -0.0205 290 GLU B CD  
4611 O OE1 . GLU B 290 ? 0.4843 0.7781 0.4898 -0.0431 -0.0617 -0.0127 290 GLU B OE1 
4612 O OE2 . GLU B 290 ? 0.4733 0.7697 0.4410 -0.0504 -0.0689 -0.0234 290 GLU B OE2 
4613 N N   . PHE B 291 ? 0.3616 0.7948 0.4133 -0.1042 -0.0863 -0.0144 291 PHE B N   
4614 C CA  . PHE B 291 ? 0.3834 0.8595 0.4641 -0.1017 -0.0889 -0.0034 291 PHE B CA  
4615 C C   . PHE B 291 ? 0.3609 0.8885 0.4423 -0.1076 -0.0989 -0.0028 291 PHE B C   
4616 O O   . PHE B 291 ? 0.3548 0.8892 0.4205 -0.1284 -0.1031 -0.0179 291 PHE B O   
4617 C CB  . PHE B 291 ? 0.3796 0.8486 0.4690 -0.1160 -0.0851 -0.0107 291 PHE B CB  
4618 C CG  . PHE B 291 ? 0.3705 0.7949 0.4620 -0.1087 -0.0756 -0.0100 291 PHE B CG  
4619 C CD1 . PHE B 291 ? 0.4193 0.8477 0.5348 -0.0911 -0.0714 0.0047  291 PHE B CD1 
4620 C CD2 . PHE B 291 ? 0.3948 0.7726 0.4622 -0.1183 -0.0704 -0.0240 291 PHE B CD2 
4621 C CE1 . PHE B 291 ? 0.4074 0.7975 0.5245 -0.0849 -0.0631 0.0043  291 PHE B CE1 
4622 C CE2 . PHE B 291 ? 0.5160 0.8561 0.5844 -0.1102 -0.0623 -0.0235 291 PHE B CE2 
4623 C CZ  . PHE B 291 ? 0.4733 0.8212 0.5674 -0.0940 -0.0591 -0.0097 291 PHE B CZ  
4624 N N   . THR B 292 ? 0.3389 0.9026 0.4368 -0.0896 -0.1020 0.0142  292 THR B N   
4625 C CA  . THR B 292 ? 0.3793 0.9986 0.4796 -0.0926 -0.1120 0.0160  292 THR B CA  
4626 C C   . THR B 292 ? 0.3311 0.9861 0.4500 -0.1040 -0.1141 0.0133  292 THR B C   
4627 O O   . THR B 292 ? 0.3220 0.9660 0.4571 -0.1047 -0.1087 0.0151  292 THR B O   
4628 C CB  . THR B 292 ? 0.3710 1.0171 0.4807 -0.0675 -0.1135 0.0362  292 THR B CB  
4629 O OG1 . THR B 292 ? 0.4040 1.0526 0.5381 -0.0518 -0.1072 0.0515  292 THR B OG1 
4630 C CG2 . THR B 292 ? 0.3565 0.9677 0.4477 -0.0563 -0.1097 0.0393  292 THR B CG2 
4631 N N   . PRO B 293 ? 0.3487 1.0358 0.4623 -0.1112 -0.1183 0.0084  293 PRO B N   
4632 C CA  . PRO B 293 ? 0.3522 1.0684 0.4824 -0.1155 -0.1168 0.0088  293 PRO B CA  
4633 C C   . PRO B 293 ? 0.4028 1.1285 0.5568 -0.0915 -0.1123 0.0286  293 PRO B C   
4634 O O   . PRO B 293 ? 0.3309 1.0587 0.5004 -0.0951 -0.1082 0.0284  293 PRO B O   
4635 C CB  . PRO B 293 ? 0.3754 1.1304 0.4963 -0.1192 -0.1226 0.0048  293 PRO B CB  
4636 C CG  . PRO B 293 ? 0.3893 1.1241 0.4844 -0.1312 -0.1261 -0.0076 293 PRO B CG  
4637 C CD  . PRO B 293 ? 0.3702 1.0697 0.4624 -0.1164 -0.1242 0.0014  293 PRO B CD  
4638 N N   . PHE B 294 ? 0.3735 1.1007 0.5288 -0.0671 -0.1116 0.0455  294 PHE B N   
4639 C CA  . PHE B 294 ? 0.3647 1.0966 0.5385 -0.0435 -0.1056 0.0647  294 PHE B CA  
4640 C C   . PHE B 294 ? 0.3805 1.0767 0.5667 -0.0426 -0.0986 0.0666  294 PHE B C   
4641 O O   . PHE B 294 ? 0.3935 1.0915 0.5966 -0.0348 -0.0931 0.0740  294 PHE B O   
4642 C CB  . PHE B 294 ? 0.4758 1.2135 0.6436 -0.0192 -0.1049 0.0817  294 PHE B CB  
4643 C CG  . PHE B 294 ? 0.5455 1.2829 0.7277 0.0062  -0.0969 0.1021  294 PHE B CG  
4644 C CD1 . PHE B 294 ? 0.5858 1.2880 0.7754 0.0167  -0.0888 0.1111  294 PHE B CD1 
4645 C CD2 . PHE B 294 ? 0.6192 1.3906 0.8052 0.0202  -0.0965 0.1123  294 PHE B CD2 
4646 C CE1 . PHE B 294 ? 0.5919 1.2894 0.7920 0.0390  -0.0799 0.1292  294 PHE B CE1 
4647 C CE2 . PHE B 294 ? 0.5971 1.3642 0.7925 0.0441  -0.0880 0.1311  294 PHE B CE2 
4648 C CZ  . PHE B 294 ? 0.5711 1.2996 0.7729 0.0529  -0.0794 0.1394  294 PHE B CZ  
4649 N N   . ASP B 295 ? 0.3688 1.0329 0.5462 -0.0500 -0.0983 0.0595  295 ASP B N   
4650 C CA  . ASP B 295 ? 0.3760 1.0035 0.5629 -0.0504 -0.0906 0.0590  295 ASP B CA  
4651 C C   . ASP B 295 ? 0.3958 1.0281 0.5930 -0.0682 -0.0898 0.0484  295 ASP B C   
4652 O O   . ASP B 295 ? 0.3679 0.9868 0.5808 -0.0619 -0.0826 0.0541  295 ASP B O   
4653 C CB  . ASP B 295 ? 0.3815 0.9562 0.5459 -0.0556 -0.0869 0.0488  295 ASP B CB  
4654 C CG  . ASP B 295 ? 0.4342 1.0039 0.5872 -0.0407 -0.0871 0.0574  295 ASP B CG  
4655 O OD1 . ASP B 295 ? 0.4705 1.0702 0.6329 -0.0238 -0.0881 0.0734  295 ASP B OD1 
4656 O OD2 . ASP B 295 ? 0.4162 0.9512 0.5495 -0.0452 -0.0856 0.0483  295 ASP B OD2 
4657 N N   . VAL B 296 ? 0.4062 1.0483 0.5908 -0.0911 -0.0948 0.0317  296 VAL B N   
4658 C CA  . VAL B 296 ? 0.3876 1.0295 0.5784 -0.1094 -0.0919 0.0209  296 VAL B CA  
4659 C C   . VAL B 296 ? 0.3953 1.0650 0.6064 -0.0965 -0.0891 0.0326  296 VAL B C   
4660 O O   . VAL B 296 ? 0.3893 1.0480 0.6148 -0.0957 -0.0829 0.0347  296 VAL B O   
4661 C CB  . VAL B 296 ? 0.3615 1.0098 0.5328 -0.1366 -0.0962 0.0011  296 VAL B CB  
4662 C CG1 . VAL B 296 ? 0.3492 1.0030 0.5278 -0.1544 -0.0919 -0.0083 296 VAL B CG1 
4663 C CG2 . VAL B 296 ? 0.3709 0.9766 0.5170 -0.1503 -0.0958 -0.0126 296 VAL B CG2 
4664 N N   . VAL B 297 ? 0.3969 1.1026 0.6080 -0.0849 -0.0935 0.0406  297 VAL B N   
4665 C CA  . VAL B 297 ? 0.3752 1.1106 0.6022 -0.0719 -0.0914 0.0511  297 VAL B CA  
4666 C C   . VAL B 297 ? 0.4560 1.1723 0.6975 -0.0484 -0.0838 0.0683  297 VAL B C   
4667 O O   . VAL B 297 ? 0.4924 1.2107 0.7484 -0.0449 -0.0788 0.0718  297 VAL B O   
4668 C CB  . VAL B 297 ? 0.3860 1.1637 0.6071 -0.0626 -0.0973 0.0564  297 VAL B CB  
4669 C CG1 . VAL B 297 ? 0.3674 1.1718 0.6030 -0.0422 -0.0941 0.0712  297 VAL B CG1 
4670 C CG2 . VAL B 297 ? 0.3766 1.1793 0.5869 -0.0878 -0.1031 0.0380  297 VAL B CG2 
4671 N N   . ARG B 298 ? 0.4341 1.1307 0.6711 -0.0322 -0.0820 0.0790  298 ARG B N   
4672 C CA  . ARG B 298 ? 0.4571 1.1322 0.7057 -0.0109 -0.0731 0.0947  298 ARG B CA  
4673 C C   . ARG B 298 ? 0.4465 1.0929 0.7062 -0.0196 -0.0669 0.0887  298 ARG B C   
4674 O O   . ARG B 298 ? 0.4729 1.1153 0.7459 -0.0088 -0.0601 0.0969  298 ARG B O   
4675 C CB  . ARG B 298 ? 0.5110 1.1653 0.7516 0.0032  -0.0709 0.1042  298 ARG B CB  
4676 C CG  . ARG B 298 ? 0.6124 1.2280 0.8620 0.0121  -0.0610 0.1105  298 ARG B CG  
4677 C CD  . ARG B 298 ? 0.7170 1.3184 0.9612 0.0314  -0.0560 0.1247  298 ARG B CD  
4678 N NE  . ARG B 298 ? 0.6877 1.2857 0.9162 0.0246  -0.0618 0.1183  298 ARG B NE  
4679 C CZ  . ARG B 298 ? 0.6285 1.1807 0.8457 0.0174  -0.0573 0.1087  298 ARG B CZ  
4680 N NH1 . ARG B 298 ? 0.6484 1.1671 0.8733 0.0162  -0.0489 0.1058  298 ARG B NH1 
4681 N NH2 . ARG B 298 ? 0.5121 1.0542 0.7097 0.0112  -0.0615 0.1010  298 ARG B NH2 
4682 N N   . GLN B 299 ? 0.4396 1.0650 0.6923 -0.0385 -0.0686 0.0746  299 GLN B N   
4683 C CA  . GLN B 299 ? 0.4679 1.0653 0.7285 -0.0474 -0.0624 0.0682  299 GLN B CA  
4684 C C   . GLN B 299 ? 0.4700 1.0825 0.7382 -0.0606 -0.0617 0.0607  299 GLN B C   
4685 O O   . GLN B 299 ? 0.4991 1.0995 0.7803 -0.0562 -0.0546 0.0641  299 GLN B O   
4686 C CB  . GLN B 299 ? 0.4147 0.9738 0.6554 -0.0627 -0.0627 0.0535  299 GLN B CB  
4687 C CG  . GLN B 299 ? 0.4131 0.9265 0.6533 -0.0659 -0.0537 0.0478  299 GLN B CG  
4688 C CD  . GLN B 299 ? 0.3941 0.8573 0.6098 -0.0714 -0.0512 0.0365  299 GLN B CD  
4689 O OE1 . GLN B 299 ? 0.4152 0.8441 0.6245 -0.0786 -0.0455 0.0278  299 GLN B OE1 
4690 N NE2 . GLN B 299 ? 0.3707 0.8300 0.5714 -0.0672 -0.0552 0.0365  299 GLN B NE2 
4691 N N   . CYS B 300 ? 0.4817 1.1205 0.7416 -0.0771 -0.0682 0.0500  300 CYS B N   
4692 C CA  . CYS B 300 ? 0.5162 1.1692 0.7821 -0.0928 -0.0668 0.0409  300 CYS B CA  
4693 C C   . CYS B 300 ? 0.5336 1.2204 0.8138 -0.0776 -0.0662 0.0520  300 CYS B C   
4694 O O   . CYS B 300 ? 0.5568 1.2594 0.8438 -0.0888 -0.0647 0.0455  300 CYS B O   
4695 C CB  . CYS B 300 ? 0.4363 1.1004 0.6857 -0.1195 -0.0722 0.0229  300 CYS B CB  
4696 S SG  . CYS B 300 ? 0.4960 1.1124 0.7258 -0.1413 -0.0700 0.0067  300 CYS B SG  
4697 N N   . SER B 301 ? 0.6464 1.3432 0.9298 -0.0523 -0.0663 0.0685  301 SER B N   
4698 C CA  . SER B 301 ? 0.5829 1.3063 0.8777 -0.0341 -0.0641 0.0810  301 SER B CA  
4699 C C   . SER B 301 ? 0.6218 1.3219 0.9240 -0.0085 -0.0561 0.0982  301 SER B C   
4700 O O   . SER B 301 ? 0.5752 1.2933 0.8843 0.0088  -0.0531 0.1098  301 SER B O   
4701 C CB  . SER B 301 ? 0.6396 1.4055 0.9267 -0.0278 -0.0713 0.0846  301 SER B CB  
4702 O OG  . SER B 301 ? 0.6956 1.4819 0.9748 -0.0529 -0.0778 0.0675  301 SER B OG  
4703 N N   . GLY B 302 ? 0.5859 1.2469 0.8856 -0.0058 -0.0518 0.0998  302 GLY B N   
4704 C CA  . GLY B 302 ? 0.5543 1.1867 0.8611 0.0135  -0.0421 0.1126  302 GLY B CA  
4705 C C   . GLY B 302 ? 0.5887 1.2242 0.8909 0.0384  -0.0389 0.1303  302 GLY B C   
4706 O O   . GLY B 302 ? 0.5853 1.2132 0.8935 0.0560  -0.0308 0.1425  302 GLY B O   
4707 N N   . VAL B 303 ? 0.6162 1.2612 0.9063 0.0405  -0.0443 0.1323  303 VAL B N   
4708 C CA  . VAL B 303 ? 0.7536 1.4024 1.0370 0.0642  -0.0405 0.1498  303 VAL B CA  
4709 C C   . VAL B 303 ? 0.7672 1.3735 1.0527 0.0769  -0.0288 0.1592  303 VAL B C   
4710 O O   . VAL B 303 ? 0.7147 1.2923 1.0019 0.0662  -0.0271 0.1511  303 VAL B O   
4711 C CB  . VAL B 303 ? 0.7569 1.4242 1.0258 0.0618  -0.0488 0.1483  303 VAL B CB  
4712 C CG1 . VAL B 303 ? 0.8587 1.5201 1.1185 0.0856  -0.0429 0.1664  303 VAL B CG1 
4713 C CG2 . VAL B 303 ? 0.7156 1.4283 0.9817 0.0526  -0.0585 0.1409  303 VAL B CG2 
4714 N N   . THR B 304 ? 0.7874 1.3896 1.0718 0.0997  -0.0198 0.1764  304 THR B N   
4715 C CA  . THR B 304 ? 0.7790 1.3409 1.0644 0.1125  -0.0065 0.1863  304 THR B CA  
4716 C C   . THR B 304 ? 0.9117 1.4698 1.1842 0.1308  -0.0011 0.2018  304 THR B C   
4717 O O   . THR B 304 ? 0.9541 1.5421 1.2167 0.1372  -0.0073 0.2069  304 THR B O   
4718 C CB  . THR B 304 ? 0.6932 1.2437 0.9866 0.1235  0.0034  0.1934  304 THR B CB  
4719 O OG1 . THR B 304 ? 0.7318 1.3176 1.0233 0.1345  0.0007  0.2009  304 THR B OG1 
4720 C CG2 . THR B 304 ? 0.5650 1.1030 0.8710 0.1062  0.0025  0.1788  304 THR B CG2 
4721 N N   . PHE B 305 ? 0.8849 1.4051 1.1571 0.1393  0.0116  0.2093  305 PHE B N   
4722 C CA  . PHE B 305 ? 1.0005 1.5099 1.2602 0.1565  0.0199  0.2246  305 PHE B CA  
4723 C C   . PHE B 305 ? 0.9813 1.4527 1.2411 0.1725  0.0388  0.2377  305 PHE B C   
4724 O O   . PHE B 305 ? 1.0864 1.5541 1.3343 0.1932  0.0484  0.2547  305 PHE B O   
4725 C CB  . PHE B 305 ? 0.9714 1.4733 1.2276 0.1458  0.0158  0.2176  305 PHE B CB  
4726 C CG  . PHE B 305 ? 0.8874 1.4169 1.1434 0.1256  -0.0014 0.2009  305 PHE B CG  
4727 C CD1 . PHE B 305 ? 0.9457 1.5112 1.1910 0.1269  -0.0120 0.2019  305 PHE B CD1 
4728 C CD2 . PHE B 305 ? 0.8115 1.3294 1.0761 0.1053  -0.0059 0.1837  305 PHE B CD2 
4729 C CE1 . PHE B 305 ? 0.9081 1.4962 1.1516 0.1070  -0.0263 0.1856  305 PHE B CE1 
4730 C CE2 . PHE B 305 ? 0.7833 1.3224 1.0449 0.0865  -0.0199 0.1684  305 PHE B CE2 
4731 C CZ  . PHE B 305 ? 0.8537 1.4273 1.1048 0.0867  -0.0299 0.1691  305 PHE B CZ  
4732 C C14 . V8X C .   ? 0.3475 0.8184 0.7259 -0.1326 0.0489  0.0258  401 V8X A C14 
4733 C C10 . V8X C .   ? 0.3520 0.7339 0.7427 -0.0388 0.0616  0.0628  401 V8X A C10 
4734 C C12 . V8X C .   ? 0.3322 0.7867 0.7102 -0.0980 0.0401  0.0408  401 V8X A C12 
4735 C C13 . V8X C .   ? 0.3472 0.8024 0.7165 -0.1255 0.0437  0.0280  401 V8X A C13 
4736 C C15 . V8X C .   ? 0.3944 0.8509 0.7545 -0.1608 0.0524  0.0121  401 V8X A C15 
4737 C C16 . V8X C .   ? 0.3988 0.8584 0.7549 -0.1807 0.0586  0.0037  401 V8X A C16 
4738 C C17 . V8X C .   ? 0.4605 0.8924 0.7896 -0.2069 0.0625  -0.0106 401 V8X A C17 
4739 F F18 . V8X C .   ? 0.4947 0.9256 0.8171 -0.2263 0.0696  -0.0190 401 V8X A F18 
4740 C C02 . V8X C .   ? 0.3849 0.8489 0.7676 -0.0051 0.0261  0.0875  401 V8X A C02 
4741 C C03 . V8X C .   ? 0.3448 0.8154 0.7241 -0.0307 0.0221  0.0742  401 V8X A C03 
4742 C C05 . V8X C .   ? 0.3712 0.8525 0.7651 -0.0465 0.0328  0.0656  401 V8X A C05 
4743 C C06 . V8X C .   ? 0.3281 0.7841 0.7233 -0.0533 0.0428  0.0607  401 V8X A C06 
4744 C C07 . V8X C .   ? 0.3432 0.8028 0.7483 -0.0377 0.0492  0.0672  401 V8X A C07 
4745 C C08 . V8X C .   ? 0.3611 0.7785 0.7614 -0.0273 0.0579  0.0695  401 V8X A C08 
4746 C C09 . V8X C .   ? 0.3548 0.7579 0.7550 -0.0407 0.0662  0.0624  401 V8X A C09 
4747 C C19 . V8X C .   ? 0.4327 0.8345 0.7392 -0.2137 0.0603  -0.0172 401 V8X A C19 
4748 C C20 . V8X C .   ? 0.4362 0.8402 0.7494 -0.1946 0.0533  -0.0090 401 V8X A C20 
4749 C C22 . V8X C .   ? 0.4019 0.8338 0.7422 -0.1682 0.0494  0.0062  401 V8X A C22 
4750 C C26 . V8X C .   ? 0.4198 0.9279 0.7990 -0.0456 0.0142  0.0684  401 V8X A C26 
4751 C C27 . V8X C .   ? 0.3574 0.8625 0.7233 -0.0667 0.0083  0.0574  401 V8X A C27 
4752 C C28 . V8X C .   ? 0.3951 0.9333 0.7599 -0.0819 0.0026  0.0505  401 V8X A C28 
4753 C C29 . V8X C .   ? 0.3654 0.9046 0.7155 -0.1027 -0.0027 0.0391  401 V8X A C29 
4754 C C30 . V8X C .   ? 0.3481 0.8565 0.6851 -0.1073 -0.0026 0.0353  401 V8X A C30 
4755 C C32 . V8X C .   ? 0.3681 0.8448 0.7217 -0.0728 0.0078  0.0532  401 V8X A C32 
4756 F F21 . V8X C .   ? 0.4705 0.8411 0.7596 -0.1963 0.0501  -0.0145 401 V8X A F21 
4757 N N01 . V8X C .   ? 0.3275 0.8122 0.7094 0.0063  0.0215  0.0959  401 V8X A N01 
4758 N N04 . V8X C .   ? 0.3413 0.7996 0.7254 -0.0395 0.0299  0.0685  401 V8X A N04 
4759 N N11 . V8X C .   ? 0.3575 0.8220 0.7505 -0.0783 0.0439  0.0498  401 V8X A N11 
4760 N N23 . V8X C .   ? 0.3311 0.7660 0.6794 -0.1466 0.0437  0.0164  401 V8X A N23 
4761 N N31 . V8X C .   ? 0.3634 0.8442 0.7033 -0.0924 0.0022  0.0425  401 V8X A N31 
4762 O O24 . V8X C .   ? 0.3255 0.7665 0.6955 -0.0932 0.0360  0.0427  401 V8X A O24 
4763 O O25 . V8X C .   ? 0.3841 0.9010 0.7842 -0.0470 0.0283  0.0667  401 V8X A O25 
4764 O O33 . V8X C .   ? 0.3818 0.8278 0.7332 -0.0620 0.0120  0.0571  401 V8X A O33 
4785 C C14 . V8X D .   ? 0.6063 0.9974 0.5436 0.0788  0.0268  -0.0483 401 V8X B C14 
4786 C C10 . V8X D .   ? 0.5194 0.8983 0.4959 0.0477  0.0472  0.0168  401 V8X B C10 
4787 C C12 . V8X D .   ? 0.5329 0.9056 0.5043 0.0618  0.0272  -0.0301 401 V8X B C12 
4788 C C13 . V8X D .   ? 0.5973 0.9709 0.5441 0.0729  0.0216  -0.0422 401 V8X B C13 
4789 C C15 . V8X D .   ? 0.6839 1.0648 0.5944 0.0905  0.0190  -0.0580 401 V8X B C15 
4790 C C16 . V8X D .   ? 0.6980 1.0868 0.5870 0.1026  0.0195  -0.0673 401 V8X B C16 
4791 C C17 . V8X D .   ? 0.7343 1.1021 0.5951 0.1133  0.0118  -0.0751 401 V8X B C17 
4792 F F18 . V8X D .   ? 0.7778 1.1508 0.6157 0.1266  0.0130  -0.0836 401 V8X B F18 
4793 C C02 . V8X D .   ? 0.5136 0.8667 0.5795 0.0276  0.0610  -0.0005 401 V8X B C02 
4794 C C03 . V8X D .   ? 0.4930 0.8476 0.5426 0.0364  0.0462  -0.0110 401 V8X B C03 
4795 C C05 . V8X D .   ? 0.5488 0.9285 0.5715 0.0429  0.0499  -0.0176 401 V8X B C05 
4796 C C06 . V8X D .   ? 0.4902 0.8727 0.4922 0.0468  0.0472  -0.0118 401 V8X B C06 
4797 C C07 . V8X D .   ? 0.4845 0.8785 0.4901 0.0416  0.0616  -0.0058 401 V8X B C07 
4798 C C08 . V8X D .   ? 0.5055 0.8922 0.5002 0.0415  0.0624  0.0116  401 V8X B C08 
4799 C C09 . V8X D .   ? 0.5097 0.9035 0.4805 0.0482  0.0570  0.0109  401 V8X B C09 
4800 C C19 . V8X D .   ? 0.7285 1.0682 0.5821 0.1105  0.0041  -0.0745 401 V8X B C19 
4801 C C20 . V8X D .   ? 0.7015 1.0374 0.5784 0.0980  0.0029  -0.0657 401 V8X B C20 
4802 C C22 . V8X D .   ? 0.6724 1.0291 0.5775 0.0891  0.0104  -0.0572 401 V8X B C22 
4803 C C26 . V8X D .   ? 0.5719 0.9353 0.6191 0.0418  0.0432  -0.0283 401 V8X B C26 
4804 C C27 . V8X D .   ? 0.5276 0.8772 0.5636 0.0490  0.0302  -0.0344 401 V8X B C27 
4805 C C28 . V8X D .   ? 0.5826 0.9413 0.6147 0.0565  0.0296  -0.0493 401 V8X B C28 
4806 C C29 . V8X D .   ? 0.5740 0.9189 0.5936 0.0646  0.0208  -0.0565 401 V8X B C29 
4807 C C30 . V8X D .   ? 0.5621 0.8848 0.5745 0.0625  0.0129  -0.0497 401 V8X B C30 
4808 C C32 . V8X D .   ? 0.5376 0.8684 0.5667 0.0490  0.0204  -0.0281 401 V8X B C32 
4809 F F21 . V8X D .   ? 0.6768 0.9882 0.5486 0.0940  -0.0041 -0.0651 401 V8X B F21 
4810 N N01 . V8X D .   ? 0.4670 0.8181 0.5503 0.0221  0.0679  -0.0049 401 V8X B N01 
4811 N N04 . V8X D .   ? 0.5010 0.8628 0.5315 0.0404  0.0443  -0.0088 401 V8X B N04 
4812 N N11 . V8X D .   ? 0.5359 0.9237 0.5196 0.0559  0.0398  -0.0242 401 V8X B N11 
4813 N N23 . V8X D .   ? 0.5741 0.9294 0.5027 0.0784  0.0119  -0.0477 401 V8X B N23 
4814 N N31 . V8X D .   ? 0.5399 0.8585 0.5583 0.0543  0.0126  -0.0366 401 V8X B N31 
4815 O O24 . V8X D .   ? 0.4927 0.8516 0.4705 0.0583  0.0221  -0.0252 401 V8X B O24 
4816 O O25 . V8X D .   ? 0.5727 0.9667 0.6036 0.0423  0.0560  -0.0290 401 V8X B O25 
4817 O O33 . V8X D .   ? 0.4978 0.8231 0.5288 0.0445  0.0188  -0.0160 401 V8X B O33 
4838 O O   . HOH E .   ? 0.9367 1.0900 0.9119 0.1716  0.0043  -0.1158 501 HOH A O   
4839 O O   . HOH E .   ? 0.7019 0.8882 0.5671 0.1073  -0.0130 -0.0904 502 HOH A O   
4840 O O   . HOH E .   ? 0.7141 0.8586 0.9982 0.0066  0.1078  -0.0311 503 HOH A O   
4841 O O   . HOH E .   ? 0.6204 0.6396 0.7673 -0.1601 0.1271  -0.0288 504 HOH A O   
4842 O O   . HOH E .   ? 0.3453 0.5379 0.7055 -0.0017 0.1088  0.0517  505 HOH A O   
4843 O O   . HOH E .   ? 0.4971 0.6259 0.6026 -0.0432 -0.0018 -0.0214 506 HOH A O   
4844 O O   . HOH E .   ? 0.5162 0.5066 0.4520 0.0611  0.0097  -0.0753 507 HOH A O   
4845 O O   . HOH E .   ? 0.4935 0.6495 0.6482 0.0541  0.0277  -0.0599 508 HOH A O   
4846 O O   . HOH E .   ? 0.9648 0.8434 0.5728 0.1668  0.0148  -0.1223 509 HOH A O   
4847 O O   . HOH E .   ? 0.5236 0.7712 0.5619 0.0602  0.0009  -0.0560 510 HOH A O   
4848 O O   . HOH E .   ? 0.3759 0.5111 0.6351 0.0308  0.0641  -0.0145 511 HOH A O   
4849 O O   . HOH E .   ? 0.4535 0.6540 0.5972 -0.1260 0.0051  -0.0255 512 HOH A O   
4850 O O   . HOH E .   ? 0.5124 0.5480 0.5306 0.1035  0.0252  -0.0827 513 HOH A O   
4851 O O   . HOH E .   ? 0.3853 0.4741 0.6795 0.0392  0.0913  0.0133  514 HOH A O   
4852 O O   . HOH E .   ? 0.3129 0.4271 0.6241 -0.0005 0.1076  0.0308  515 HOH A O   
4853 O O   . HOH E .   ? 0.3131 0.4227 0.5460 -0.0244 0.0563  0.0076  516 HOH A O   
4854 O O   . HOH E .   ? 0.5487 0.5283 0.5961 -0.1027 0.0549  -0.0466 517 HOH A O   
4855 O O   . HOH E .   ? 0.6241 0.5217 0.6751 -0.0458 0.0918  -0.0359 518 HOH A O   
4856 O O   . HOH E .   ? 0.2880 0.5661 0.6182 0.0669  0.0582  0.1228  519 HOH A O   
4857 O O   . HOH E .   ? 0.3989 0.4863 0.5132 -0.0352 0.0149  -0.0233 520 HOH A O   
4858 O O   . HOH E .   ? 0.8817 0.9930 0.6534 0.2999  -0.0225 -0.0918 521 HOH A O   
4859 O O   . HOH E .   ? 0.4475 0.7650 0.4630 0.0835  0.0114  -0.0795 522 HOH A O   
4860 O O   . HOH E .   ? 0.3717 0.8512 0.8330 0.0347  0.1203  0.0906  523 HOH A O   
4861 O O   . HOH E .   ? 0.4339 0.5675 0.6056 0.0480  0.0328  -0.0495 524 HOH A O   
4862 O O   . HOH E .   ? 0.5224 0.5662 0.8310 0.0679  0.1363  0.0575  525 HOH A O   
4863 O O   . HOH E .   ? 0.7811 0.7485 0.7493 0.1222  0.0369  -0.0853 526 HOH A O   
4864 O O   . HOH E .   ? 0.7808 0.6541 1.0535 0.0244  0.2785  0.0599  527 HOH A O   
4865 O O   . HOH E .   ? 0.3557 0.4479 0.6632 0.0207  0.1052  0.0272  528 HOH A O   
4866 O O   . HOH E .   ? 0.4487 0.5562 0.7841 0.0627  0.1272  0.0689  529 HOH A O   
4867 O O   . HOH E .   ? 0.5947 0.7305 0.7043 0.0289  0.0057  -0.0342 530 HOH A O   
4868 O O   . HOH E .   ? 0.5498 0.5306 0.7112 0.0323  0.0824  -0.0239 531 HOH A O   
4869 O O   . HOH E .   ? 0.5688 0.5539 0.7096 -0.1114 0.1203  -0.0211 532 HOH A O   
4870 O O   . HOH E .   ? 0.6439 0.5921 0.4602 -0.0939 -0.0049 -0.1021 533 HOH A O   
4871 O O   . HOH E .   ? 0.6347 0.8049 0.9612 -0.0992 0.1728  0.0241  534 HOH A O   
4872 O O   . HOH E .   ? 1.2682 0.6209 0.7249 -0.0243 0.1647  -0.0960 535 HOH A O   
4873 O O   . HOH E .   ? 0.4941 0.5760 0.7355 0.0438  0.0829  -0.0537 536 HOH A O   
4874 O O   . HOH E .   ? 0.4861 0.5357 0.6867 -0.0971 0.1144  -0.0067 537 HOH A O   
4875 O O   . HOH E .   ? 0.4572 0.6956 0.6129 -0.0076 -0.0148 0.0182  538 HOH A O   
4876 O O   . HOH E .   ? 0.6166 0.5790 0.9128 -0.0001 0.2295  0.0169  539 HOH A O   
4877 O O   . HOH E .   ? 0.5343 0.7163 0.7500 0.0334  0.0484  -0.0471 540 HOH A O   
4878 O O   . HOH E .   ? 0.4529 0.9904 0.7489 -0.0040 -0.0353 0.0972  541 HOH A O   
4879 O O   . HOH E .   ? 0.6299 0.7089 0.9064 0.2517  0.2369  0.2302  542 HOH A O   
4880 O O   . HOH E .   ? 0.5137 0.6497 0.8560 0.1541  0.1750  0.1471  543 HOH A O   
4881 O O   . HOH E .   ? 0.6742 0.6967 0.9490 0.2200  0.2414  0.2036  544 HOH A O   
4882 O O   . HOH E .   ? 0.3559 0.8315 0.8209 0.0645  0.1339  0.1026  545 HOH A O   
4883 O O   . HOH E .   ? 1.0989 1.1956 0.7608 0.3843  -0.0263 -0.0811 546 HOH A O   
4884 O O   . HOH E .   ? 0.6198 0.7079 0.9529 0.1060  0.1590  0.1027  547 HOH A O   
4885 O O   . HOH E .   ? 0.6816 0.7764 0.9475 -0.1344 0.1950  0.0071  548 HOH A O   
4886 O O   . HOH F .   ? 0.5178 0.9224 0.7126 -0.2383 -0.0040 -0.0510 501 HOH B O   
4887 O O   . HOH F .   ? 0.4549 0.8566 0.3396 0.0709  0.0435  0.0854  502 HOH B O   
4888 O O   . HOH F .   ? 0.7395 1.0449 0.4634 0.0711  -0.0359 -0.0501 503 HOH B O   
4889 O O   . HOH F .   ? 0.4936 0.7508 0.5025 -0.0238 -0.0500 -0.0138 504 HOH B O   
4890 O O   . HOH F .   ? 0.3862 0.9217 0.4910 0.0922  -0.0412 0.1679  505 HOH B O   
4891 O O   . HOH F .   ? 0.4274 0.8293 0.4360 -0.1502 -0.0860 -0.0502 506 HOH B O   
4892 O O   . HOH F .   ? 0.4216 1.0704 0.5695 -0.0013 -0.0962 0.0917  507 HOH B O   
4893 O O   . HOH F .   ? 0.4666 0.9140 0.5899 -0.0454 -0.0711 0.0368  508 HOH B O   
4894 O O   . HOH F .   ? 0.7977 0.9352 0.7130 -0.4084 0.0463  -0.1730 509 HOH B O   
4895 O O   . HOH F .   ? 0.3243 0.5850 0.4697 0.0425  0.0726  0.1045  510 HOH B O   
4896 O O   . HOH F .   ? 0.3863 1.0399 0.4178 -0.0954 -0.1312 0.0033  511 HOH B O   
4897 O O   . HOH F .   ? 0.4640 0.8847 0.3257 0.0763  0.0062  0.0898  512 HOH B O   
4898 O O   . HOH F .   ? 0.3709 0.7493 0.3110 0.0357  -0.0400 0.0422  513 HOH B O   
4899 O O   . HOH F .   ? 0.3828 0.6846 0.3628 -0.0209 -0.0609 -0.0073 514 HOH B O   
4900 O O   . HOH F .   ? 0.3000 0.8887 0.6124 -0.1318 -0.0284 0.0215  515 HOH B O   
4901 O O   . HOH F .   ? 0.5132 0.7132 0.4373 0.0276  -0.0342 -0.0468 516 HOH B O   
4902 O O   . HOH F .   ? 0.5605 0.9098 0.3434 0.0001  -0.0807 -0.0302 517 HOH B O   
4903 O O   . HOH F .   ? 0.3663 0.9762 0.4812 0.0158  -0.0904 0.0996  518 HOH B O   
4904 O O   . HOH F .   ? 0.5781 0.8022 0.3985 -0.0043 -0.0601 -0.0575 519 HOH B O   
4905 O O   . HOH F .   ? 0.6714 1.0160 0.4935 0.1395  0.1294  0.2420  520 HOH B O   
4906 O O   . HOH F .   ? 0.8602 0.9811 0.8274 0.2998  0.2295  0.3966  521 HOH B O   
4907 O O   . HOH F .   ? 0.5748 1.2139 0.5390 -0.1116 -0.1393 -0.0220 522 HOH B O   
4908 O O   . HOH F .   ? 0.7451 1.1925 0.4854 0.1002  0.0379  0.0179  523 HOH B O   
4909 O O   . HOH F .   ? 0.6506 0.9847 0.3911 0.0542  -0.0471 -0.0311 524 HOH B O   
4910 O O   . HOH F .   ? 0.5619 0.9247 0.3448 0.0633  -0.0318 -0.0089 525 HOH B O   
4911 O O   . HOH F .   ? 0.4694 0.9026 0.3457 0.0857  0.0047  0.1205  526 HOH B O   
4912 O O   . HOH F .   ? 0.5872 0.9455 0.4380 0.1004  0.1201  0.1859  527 HOH B O   
4913 O O   . HOH F .   ? 0.5674 1.0526 0.4963 0.0065  0.1962  0.0285  528 HOH B O   
4914 O O   . HOH F .   ? 0.4121 0.6894 0.5518 -0.0084 -0.0259 0.0270  529 HOH B O   
4915 O O   . HOH F .   ? 0.6395 1.2104 0.8964 -0.1613 -0.0458 -0.0013 530 HOH B O   
4916 O O   . HOH F .   ? 0.9392 0.8713 0.7755 -0.0594 0.4469  0.2031  531 HOH B O   
4917 O O   . HOH F .   ? 0.6613 1.0746 0.5314 0.0692  0.0615  0.0657  532 HOH B O   
4918 O O   . HOH F .   ? 0.6541 1.0244 0.6987 0.0712  0.0282  -0.0790 533 HOH B O   
4919 O O   . HOH F .   ? 0.5618 0.8227 0.7047 0.0300  0.0299  -0.0271 534 HOH B O   
4920 O O   . HOH F .   ? 0.4925 1.1566 0.4793 0.1640  -0.0570 0.2252  535 HOH B O   
4921 O O   . HOH F .   ? 0.6570 0.9354 0.6654 0.3019  0.1562  0.3805  536 HOH B O   
4922 O O   . HOH F .   ? 0.4930 1.1338 0.6710 0.0651  -0.0694 0.1496  537 HOH B O   
4923 O O   . HOH F .   ? 0.6702 1.2501 0.9302 -0.1891 -0.0375 -0.0155 538 HOH B O   
4924 O O   . HOH F .   ? 0.8788 1.3757 1.0169 -0.0431 0.1522  -0.0869 539 HOH B O   
4925 O O   . HOH F .   ? 0.5572 1.0388 0.4715 -0.0132 0.2416  0.0418  540 HOH B O   
4926 O O   . HOH F .   ? 0.7957 1.0464 0.5930 0.0965  0.2361  0.2421  541 HOH B O   
4927 O O   . HOH F .   ? 0.7186 1.0748 0.4119 0.0505  -0.0579 -0.0306 542 HOH B O   
# 
