data_9J2W
# 
_entry.id   9J2W 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9J2W         pdb_00009j2w 10.2210/pdb9j2w/pdb 
WWPDB D_1300050250 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-04 
_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                        9J2W 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ycxu@simm.ac.cn 
_pdbx_contact_author.name_first         Yechun 
_pdbx_contact_author.name_last          Xu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1581-6155 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhao, W.F.' 1 ? 
'Li, M.J.'   2 ? 
'Xu, Y.C.'   3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Discovery of novel cGAS inhibitors' 
_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 'Zhao, W.F.' 1 ? 
primary 'Xu, Y.C.'   2 ? 
# 
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 'Cyclic GMP-AMP synthase' 42759.270 2  2.7.7.86 ? ? ? 
2 non-polymer syn 
;2-(1~{H}-benzimidazol-2-yl)-4-[[1-(1~{H}-benzimidazol-2-yl)-3-methyl-5-oxidanyl-pyrazol-4-yl]-pyridin-2-yl-methyl]-5-methyl-pyrazol-3-ol
;
517.541   2  ?        ? ? ? 
3 non-polymer syn 'ZINC ION' 65.409    2  ?        ? ? ? 
4 water       nat water 18.015    70 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;cGAMP synthase,cGAS,h-cGAS,2'3'-cGAMP synthase,Mab-21 domain-containing protein 1
;
# 
_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       
;DAAPGASKLRAVLEKLKLSRDDISTAAGMVKGVVDHLLLRLKCDSAFRGVGLLNTGSYYEHVKISAPNEFDVMFKLEVPR
IQLEEYSNTRAYYFVKFKRNPKENPLSQFLEGEILSASKMLSKFRKIIKEEINDIKDTDVIMKRKRGGSPAVTLLISEKI
SVDITLALESKSSWPASTQEGLRIQNWLSAKVRKQLRLKPFYLVPKHAKEGNGFQEETWRLSFSHIEKEILNNHGKSKTC
CENKEEKCCRKDCLKLMKYLLEQLKERFKDKKHLDKFSSYHVKTAFFHVCTQNPQDSQWDRKDLGLCFDNCVTYFLQCLR
TEKLENYFIPEFNLFSSNLIDKRSKEFLTKQIEYERNNEFPVFDEF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;DAAPGASKLRAVLEKLKLSRDDISTAAGMVKGVVDHLLLRLKCDSAFRGVGLLNTGSYYEHVKISAPNEFDVMFKLEVPR
IQLEEYSNTRAYYFVKFKRNPKENPLSQFLEGEILSASKMLSKFRKIIKEEINDIKDTDVIMKRKRGGSPAVTLLISEKI
SVDITLALESKSSWPASTQEGLRIQNWLSAKVRKQLRLKPFYLVPKHAKEGNGFQEETWRLSFSHIEKEILNNHGKSKTC
CENKEEKCCRKDCLKLMKYLLEQLKERFKDKKHLDKFSSYHVKTAFFHVCTQNPQDSQWDRKDLGLCFDNCVTYFLQCLR
TEKLENYFIPEFNLFSSNLIDKRSKEFLTKQIEYERNNEFPVFDEF
;
_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 
;2-(1~{H}-benzimidazol-2-yl)-4-[[1-(1~{H}-benzimidazol-2-yl)-3-methyl-5-oxidanyl-pyrazol-4-yl]-pyridin-2-yl-methyl]-5-methyl-pyrazol-3-ol
;
A1EAH 
3 'ZINC ION' ZN    
4 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASP n 
1 2   ALA n 
1 3   ALA n 
1 4   PRO n 
1 5   GLY n 
1 6   ALA n 
1 7   SER n 
1 8   LYS n 
1 9   LEU n 
1 10  ARG n 
1 11  ALA n 
1 12  VAL n 
1 13  LEU n 
1 14  GLU n 
1 15  LYS n 
1 16  LEU n 
1 17  LYS n 
1 18  LEU n 
1 19  SER n 
1 20  ARG n 
1 21  ASP n 
1 22  ASP n 
1 23  ILE n 
1 24  SER n 
1 25  THR n 
1 26  ALA n 
1 27  ALA n 
1 28  GLY n 
1 29  MET n 
1 30  VAL n 
1 31  LYS n 
1 32  GLY n 
1 33  VAL n 
1 34  VAL n 
1 35  ASP n 
1 36  HIS n 
1 37  LEU n 
1 38  LEU n 
1 39  LEU n 
1 40  ARG n 
1 41  LEU n 
1 42  LYS n 
1 43  CYS n 
1 44  ASP n 
1 45  SER n 
1 46  ALA n 
1 47  PHE n 
1 48  ARG n 
1 49  GLY n 
1 50  VAL n 
1 51  GLY n 
1 52  LEU n 
1 53  LEU n 
1 54  ASN n 
1 55  THR n 
1 56  GLY n 
1 57  SER n 
1 58  TYR n 
1 59  TYR n 
1 60  GLU n 
1 61  HIS n 
1 62  VAL n 
1 63  LYS n 
1 64  ILE n 
1 65  SER n 
1 66  ALA n 
1 67  PRO n 
1 68  ASN n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  VAL n 
1 73  MET n 
1 74  PHE n 
1 75  LYS n 
1 76  LEU n 
1 77  GLU n 
1 78  VAL n 
1 79  PRO n 
1 80  ARG n 
1 81  ILE n 
1 82  GLN n 
1 83  LEU n 
1 84  GLU n 
1 85  GLU n 
1 86  TYR n 
1 87  SER n 
1 88  ASN n 
1 89  THR n 
1 90  ARG n 
1 91  ALA n 
1 92  TYR n 
1 93  TYR n 
1 94  PHE n 
1 95  VAL n 
1 96  LYS n 
1 97  PHE n 
1 98  LYS n 
1 99  ARG n 
1 100 ASN n 
1 101 PRO n 
1 102 LYS n 
1 103 GLU n 
1 104 ASN n 
1 105 PRO n 
1 106 LEU n 
1 107 SER n 
1 108 GLN n 
1 109 PHE n 
1 110 LEU n 
1 111 GLU n 
1 112 GLY n 
1 113 GLU n 
1 114 ILE n 
1 115 LEU n 
1 116 SER n 
1 117 ALA n 
1 118 SER n 
1 119 LYS n 
1 120 MET n 
1 121 LEU n 
1 122 SER n 
1 123 LYS n 
1 124 PHE n 
1 125 ARG n 
1 126 LYS n 
1 127 ILE n 
1 128 ILE n 
1 129 LYS n 
1 130 GLU n 
1 131 GLU n 
1 132 ILE n 
1 133 ASN n 
1 134 ASP n 
1 135 ILE n 
1 136 LYS n 
1 137 ASP n 
1 138 THR n 
1 139 ASP n 
1 140 VAL n 
1 141 ILE n 
1 142 MET n 
1 143 LYS n 
1 144 ARG n 
1 145 LYS n 
1 146 ARG n 
1 147 GLY n 
1 148 GLY n 
1 149 SER n 
1 150 PRO n 
1 151 ALA n 
1 152 VAL n 
1 153 THR n 
1 154 LEU n 
1 155 LEU n 
1 156 ILE n 
1 157 SER n 
1 158 GLU n 
1 159 LYS n 
1 160 ILE n 
1 161 SER n 
1 162 VAL n 
1 163 ASP n 
1 164 ILE n 
1 165 THR n 
1 166 LEU n 
1 167 ALA n 
1 168 LEU n 
1 169 GLU n 
1 170 SER n 
1 171 LYS n 
1 172 SER n 
1 173 SER n 
1 174 TRP n 
1 175 PRO n 
1 176 ALA n 
1 177 SER n 
1 178 THR n 
1 179 GLN n 
1 180 GLU n 
1 181 GLY n 
1 182 LEU n 
1 183 ARG n 
1 184 ILE n 
1 185 GLN n 
1 186 ASN n 
1 187 TRP n 
1 188 LEU n 
1 189 SER n 
1 190 ALA n 
1 191 LYS n 
1 192 VAL n 
1 193 ARG n 
1 194 LYS n 
1 195 GLN n 
1 196 LEU n 
1 197 ARG n 
1 198 LEU n 
1 199 LYS n 
1 200 PRO n 
1 201 PHE n 
1 202 TYR n 
1 203 LEU n 
1 204 VAL n 
1 205 PRO n 
1 206 LYS n 
1 207 HIS n 
1 208 ALA n 
1 209 LYS n 
1 210 GLU n 
1 211 GLY n 
1 212 ASN n 
1 213 GLY n 
1 214 PHE n 
1 215 GLN n 
1 216 GLU n 
1 217 GLU n 
1 218 THR n 
1 219 TRP n 
1 220 ARG n 
1 221 LEU n 
1 222 SER n 
1 223 PHE n 
1 224 SER n 
1 225 HIS n 
1 226 ILE n 
1 227 GLU n 
1 228 LYS n 
1 229 GLU n 
1 230 ILE n 
1 231 LEU n 
1 232 ASN n 
1 233 ASN n 
1 234 HIS n 
1 235 GLY n 
1 236 LYS n 
1 237 SER n 
1 238 LYS n 
1 239 THR n 
1 240 CYS n 
1 241 CYS n 
1 242 GLU n 
1 243 ASN n 
1 244 LYS n 
1 245 GLU n 
1 246 GLU n 
1 247 LYS n 
1 248 CYS n 
1 249 CYS n 
1 250 ARG n 
1 251 LYS n 
1 252 ASP n 
1 253 CYS n 
1 254 LEU n 
1 255 LYS n 
1 256 LEU n 
1 257 MET n 
1 258 LYS n 
1 259 TYR n 
1 260 LEU n 
1 261 LEU n 
1 262 GLU n 
1 263 GLN n 
1 264 LEU n 
1 265 LYS n 
1 266 GLU n 
1 267 ARG n 
1 268 PHE n 
1 269 LYS n 
1 270 ASP n 
1 271 LYS n 
1 272 LYS n 
1 273 HIS n 
1 274 LEU n 
1 275 ASP n 
1 276 LYS n 
1 277 PHE n 
1 278 SER n 
1 279 SER n 
1 280 TYR n 
1 281 HIS n 
1 282 VAL n 
1 283 LYS n 
1 284 THR n 
1 285 ALA n 
1 286 PHE n 
1 287 PHE n 
1 288 HIS n 
1 289 VAL n 
1 290 CYS n 
1 291 THR n 
1 292 GLN n 
1 293 ASN n 
1 294 PRO n 
1 295 GLN n 
1 296 ASP n 
1 297 SER n 
1 298 GLN n 
1 299 TRP n 
1 300 ASP n 
1 301 ARG n 
1 302 LYS n 
1 303 ASP n 
1 304 LEU n 
1 305 GLY n 
1 306 LEU n 
1 307 CYS n 
1 308 PHE n 
1 309 ASP n 
1 310 ASN n 
1 311 CYS n 
1 312 VAL n 
1 313 THR n 
1 314 TYR n 
1 315 PHE n 
1 316 LEU n 
1 317 GLN n 
1 318 CYS n 
1 319 LEU n 
1 320 ARG n 
1 321 THR n 
1 322 GLU n 
1 323 LYS n 
1 324 LEU n 
1 325 GLU n 
1 326 ASN n 
1 327 TYR n 
1 328 PHE n 
1 329 ILE n 
1 330 PRO n 
1 331 GLU n 
1 332 PHE n 
1 333 ASN n 
1 334 LEU n 
1 335 PHE n 
1 336 SER n 
1 337 SER n 
1 338 ASN n 
1 339 LEU n 
1 340 ILE n 
1 341 ASP n 
1 342 LYS n 
1 343 ARG n 
1 344 SER n 
1 345 LYS n 
1 346 GLU n 
1 347 PHE n 
1 348 LEU n 
1 349 THR n 
1 350 LYS n 
1 351 GLN n 
1 352 ILE n 
1 353 GLU n 
1 354 TYR n 
1 355 GLU n 
1 356 ARG n 
1 357 ASN n 
1 358 ASN n 
1 359 GLU n 
1 360 PHE n 
1 361 PRO n 
1 362 VAL n 
1 363 PHE n 
1 364 ASP n 
1 365 GLU n 
1 366 PHE 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                   366 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CGAS, C6orf150, MB21D1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(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 
A1EAH non-polymer         . 
;2-(1~{H}-benzimidazol-2-yl)-4-[[1-(1~{H}-benzimidazol-2-yl)-3-methyl-5-oxidanyl-pyrazol-4-yl]-pyridin-2-yl-methyl]-5-methyl-pyrazol-3-ol
;
? 'C28 H23 N9 O2'  517.541 
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 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION' ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ASP 1   157 ?   ?   ?   A . n 
A 1 2   ALA 2   158 ?   ?   ?   A . n 
A 1 3   ALA 3   159 ?   ?   ?   A . n 
A 1 4   PRO 4   160 ?   ?   ?   A . n 
A 1 5   GLY 5   161 161 GLY GLY A . n 
A 1 6   ALA 6   162 162 ALA ALA A . n 
A 1 7   SER 7   163 163 SER SER A . n 
A 1 8   LYS 8   164 164 LYS LYS A . n 
A 1 9   LEU 9   165 165 LEU LEU A . n 
A 1 10  ARG 10  166 166 ARG ARG A . n 
A 1 11  ALA 11  167 167 ALA ALA A . n 
A 1 12  VAL 12  168 168 VAL VAL A . n 
A 1 13  LEU 13  169 169 LEU LEU A . n 
A 1 14  GLU 14  170 170 GLU GLU A . n 
A 1 15  LYS 15  171 171 LYS LYS A . n 
A 1 16  LEU 16  172 172 LEU LEU A . n 
A 1 17  LYS 17  173 173 LYS LYS A . n 
A 1 18  LEU 18  174 174 LEU LEU A . n 
A 1 19  SER 19  175 175 SER SER A . n 
A 1 20  ARG 20  176 ?   ?   ?   A . n 
A 1 21  ASP 21  177 ?   ?   ?   A . n 
A 1 22  ASP 22  178 ?   ?   ?   A . n 
A 1 23  ILE 23  179 179 ILE ILE A . n 
A 1 24  SER 24  180 180 SER SER A . n 
A 1 25  THR 25  181 181 THR THR A . n 
A 1 26  ALA 26  182 182 ALA ALA A . n 
A 1 27  ALA 27  183 183 ALA ALA A . n 
A 1 28  GLY 28  184 184 GLY GLY A . n 
A 1 29  MET 29  185 185 MET MET A . n 
A 1 30  VAL 30  186 186 VAL VAL A . n 
A 1 31  LYS 31  187 187 LYS LYS A . n 
A 1 32  GLY 32  188 188 GLY GLY A . n 
A 1 33  VAL 33  189 189 VAL VAL A . n 
A 1 34  VAL 34  190 190 VAL VAL A . n 
A 1 35  ASP 35  191 191 ASP ASP A . n 
A 1 36  HIS 36  192 192 HIS HIS A . n 
A 1 37  LEU 37  193 193 LEU LEU A . n 
A 1 38  LEU 38  194 194 LEU LEU A . n 
A 1 39  LEU 39  195 195 LEU LEU A . n 
A 1 40  ARG 40  196 196 ARG ARG A . n 
A 1 41  LEU 41  197 197 LEU LEU A . n 
A 1 42  LYS 42  198 198 LYS LYS A . n 
A 1 43  CYS 43  199 199 CYS CYS A . n 
A 1 44  ASP 44  200 200 ASP ASP A . n 
A 1 45  SER 45  201 201 SER SER A . n 
A 1 46  ALA 46  202 202 ALA ALA A . n 
A 1 47  PHE 47  203 203 PHE PHE A . n 
A 1 48  ARG 48  204 204 ARG ARG A . n 
A 1 49  GLY 49  205 205 GLY GLY A . n 
A 1 50  VAL 50  206 206 VAL VAL A . n 
A 1 51  GLY 51  207 207 GLY GLY A . n 
A 1 52  LEU 52  208 208 LEU LEU A . n 
A 1 53  LEU 53  209 209 LEU LEU A . n 
A 1 54  ASN 54  210 ?   ?   ?   A . n 
A 1 55  THR 55  211 ?   ?   ?   A . n 
A 1 56  GLY 56  212 ?   ?   ?   A . n 
A 1 57  SER 57  213 ?   ?   ?   A . n 
A 1 58  TYR 58  214 ?   ?   ?   A . n 
A 1 59  TYR 59  215 215 TYR TYR A . n 
A 1 60  GLU 60  216 216 GLU GLU A . n 
A 1 61  HIS 61  217 217 HIS HIS A . n 
A 1 62  VAL 62  218 218 VAL VAL A . n 
A 1 63  LYS 63  219 219 LYS LYS A . n 
A 1 64  ILE 64  220 220 ILE ILE A . n 
A 1 65  SER 65  221 221 SER SER A . n 
A 1 66  ALA 66  222 222 ALA ALA A . n 
A 1 67  PRO 67  223 223 PRO PRO A . n 
A 1 68  ASN 68  224 224 ASN ASN A . n 
A 1 69  GLU 69  225 225 GLU GLU A . n 
A 1 70  PHE 70  226 226 PHE PHE A . n 
A 1 71  ASP 71  227 227 ASP ASP A . n 
A 1 72  VAL 72  228 228 VAL VAL A . n 
A 1 73  MET 73  229 229 MET MET A . n 
A 1 74  PHE 74  230 230 PHE PHE A . n 
A 1 75  LYS 75  231 231 LYS LYS A . n 
A 1 76  LEU 76  232 232 LEU LEU A . n 
A 1 77  GLU 77  233 233 GLU GLU A . n 
A 1 78  VAL 78  234 234 VAL VAL A . n 
A 1 79  PRO 79  235 235 PRO PRO A . n 
A 1 80  ARG 80  236 236 ARG ARG A . n 
A 1 81  ILE 81  237 237 ILE ILE A . n 
A 1 82  GLN 82  238 238 GLN GLN A . n 
A 1 83  LEU 83  239 239 LEU LEU A . n 
A 1 84  GLU 84  240 240 GLU GLU A . n 
A 1 85  GLU 85  241 241 GLU GLU A . n 
A 1 86  TYR 86  242 242 TYR TYR A . n 
A 1 87  SER 87  243 243 SER SER A . n 
A 1 88  ASN 88  244 244 ASN ASN A . n 
A 1 89  THR 89  245 245 THR THR A . n 
A 1 90  ARG 90  246 246 ARG ARG A . n 
A 1 91  ALA 91  247 247 ALA ALA A . n 
A 1 92  TYR 92  248 248 TYR TYR A . n 
A 1 93  TYR 93  249 249 TYR TYR A . n 
A 1 94  PHE 94  250 250 PHE PHE A . n 
A 1 95  VAL 95  251 251 VAL VAL A . n 
A 1 96  LYS 96  252 252 LYS LYS A . n 
A 1 97  PHE 97  253 253 PHE PHE A . n 
A 1 98  LYS 98  254 254 LYS LYS A . n 
A 1 99  ARG 99  255 ?   ?   ?   A . n 
A 1 100 ASN 100 256 ?   ?   ?   A . n 
A 1 101 PRO 101 257 ?   ?   ?   A . n 
A 1 102 LYS 102 258 ?   ?   ?   A . n 
A 1 103 GLU 103 259 259 GLU GLU A . n 
A 1 104 ASN 104 260 260 ASN ASN A . n 
A 1 105 PRO 105 261 261 PRO PRO A . n 
A 1 106 LEU 106 262 262 LEU LEU A . n 
A 1 107 SER 107 263 263 SER SER A . n 
A 1 108 GLN 108 264 264 GLN GLN A . n 
A 1 109 PHE 109 265 265 PHE PHE A . n 
A 1 110 LEU 110 266 266 LEU LEU A . n 
A 1 111 GLU 111 267 267 GLU GLU A . n 
A 1 112 GLY 112 268 268 GLY GLY A . n 
A 1 113 GLU 113 269 269 GLU GLU A . n 
A 1 114 ILE 114 270 270 ILE ILE A . n 
A 1 115 LEU 115 271 271 LEU LEU A . n 
A 1 116 SER 116 272 272 SER SER A . n 
A 1 117 ALA 117 273 273 ALA ALA A . n 
A 1 118 SER 118 274 274 SER SER A . n 
A 1 119 LYS 119 275 275 LYS LYS A . n 
A 1 120 MET 120 276 276 MET MET A . n 
A 1 121 LEU 121 277 277 LEU LEU A . n 
A 1 122 SER 122 278 278 SER SER A . n 
A 1 123 LYS 123 279 279 LYS LYS A . n 
A 1 124 PHE 124 280 280 PHE PHE A . n 
A 1 125 ARG 125 281 281 ARG ARG A . n 
A 1 126 LYS 126 282 282 LYS LYS A . n 
A 1 127 ILE 127 283 283 ILE ILE A . n 
A 1 128 ILE 128 284 284 ILE ILE A . n 
A 1 129 LYS 129 285 ?   ?   ?   A . n 
A 1 130 GLU 130 286 ?   ?   ?   A . n 
A 1 131 GLU 131 287 ?   ?   ?   A . n 
A 1 132 ILE 132 288 ?   ?   ?   A . n 
A 1 133 ASN 133 289 ?   ?   ?   A . n 
A 1 134 ASP 134 290 ?   ?   ?   A . n 
A 1 135 ILE 135 291 ?   ?   ?   A . n 
A 1 136 LYS 136 292 ?   ?   ?   A . n 
A 1 137 ASP 137 293 ?   ?   ?   A . n 
A 1 138 THR 138 294 ?   ?   ?   A . n 
A 1 139 ASP 139 295 ?   ?   ?   A . n 
A 1 140 VAL 140 296 ?   ?   ?   A . n 
A 1 141 ILE 141 297 ?   ?   ?   A . n 
A 1 142 MET 142 298 298 MET MET A . n 
A 1 143 LYS 143 299 299 LYS LYS A . n 
A 1 144 ARG 144 300 300 ARG ARG A . n 
A 1 145 LYS 145 301 ?   ?   ?   A . n 
A 1 146 ARG 146 302 ?   ?   ?   A . n 
A 1 147 GLY 147 303 ?   ?   ?   A . n 
A 1 148 GLY 148 304 304 GLY GLY A . n 
A 1 149 SER 149 305 305 SER SER A . n 
A 1 150 PRO 150 306 ?   ?   ?   A . n 
A 1 151 ALA 151 307 307 ALA ALA A . n 
A 1 152 VAL 152 308 308 VAL VAL A . n 
A 1 153 THR 153 309 309 THR THR A . n 
A 1 154 LEU 154 310 310 LEU LEU A . n 
A 1 155 LEU 155 311 311 LEU LEU A . n 
A 1 156 ILE 156 312 312 ILE ILE A . n 
A 1 157 SER 157 313 ?   ?   ?   A . n 
A 1 158 GLU 158 314 314 GLU GLU A . n 
A 1 159 LYS 159 315 315 LYS LYS A . n 
A 1 160 ILE 160 316 316 ILE ILE A . n 
A 1 161 SER 161 317 317 SER SER A . n 
A 1 162 VAL 162 318 318 VAL VAL A . n 
A 1 163 ASP 163 319 319 ASP ASP A . n 
A 1 164 ILE 164 320 320 ILE ILE A . n 
A 1 165 THR 165 321 321 THR THR A . n 
A 1 166 LEU 166 322 322 LEU LEU A . n 
A 1 167 ALA 167 323 323 ALA ALA A . n 
A 1 168 LEU 168 324 324 LEU LEU A . n 
A 1 169 GLU 169 325 325 GLU GLU A . n 
A 1 170 SER 170 326 326 SER SER A . n 
A 1 171 LYS 171 327 327 LYS LYS A . n 
A 1 172 SER 172 328 328 SER SER A . n 
A 1 173 SER 173 329 329 SER SER A . n 
A 1 174 TRP 174 330 330 TRP TRP A . n 
A 1 175 PRO 175 331 331 PRO PRO A . n 
A 1 176 ALA 176 332 332 ALA ALA A . n 
A 1 177 SER 177 333 333 SER SER A . n 
A 1 178 THR 178 334 334 THR THR A . n 
A 1 179 GLN 179 335 335 GLN GLN A . n 
A 1 180 GLU 180 336 336 GLU GLU A . n 
A 1 181 GLY 181 337 337 GLY GLY A . n 
A 1 182 LEU 182 338 338 LEU LEU A . n 
A 1 183 ARG 183 339 339 ARG ARG A . n 
A 1 184 ILE 184 340 340 ILE ILE A . n 
A 1 185 GLN 185 341 341 GLN GLN A . n 
A 1 186 ASN 186 342 342 ASN ASN A . n 
A 1 187 TRP 187 343 343 TRP TRP A . n 
A 1 188 LEU 188 344 344 LEU LEU A . n 
A 1 189 SER 189 345 345 SER SER A . n 
A 1 190 ALA 190 346 346 ALA ALA A . n 
A 1 191 LYS 191 347 347 LYS LYS A . n 
A 1 192 VAL 192 348 348 VAL VAL A . n 
A 1 193 ARG 193 349 349 ARG ARG A . n 
A 1 194 LYS 194 350 350 LYS LYS A . n 
A 1 195 GLN 195 351 351 GLN GLN A . n 
A 1 196 LEU 196 352 352 LEU LEU A . n 
A 1 197 ARG 197 353 353 ARG ARG A . n 
A 1 198 LEU 198 354 354 LEU LEU A . n 
A 1 199 LYS 199 355 355 LYS LYS A . n 
A 1 200 PRO 200 356 356 PRO PRO A . n 
A 1 201 PHE 201 357 357 PHE PHE A . n 
A 1 202 TYR 202 358 358 TYR TYR A . n 
A 1 203 LEU 203 359 359 LEU LEU A . n 
A 1 204 VAL 204 360 360 VAL VAL A . n 
A 1 205 PRO 205 361 361 PRO PRO A . n 
A 1 206 LYS 206 362 362 LYS LYS A . n 
A 1 207 HIS 207 363 363 HIS HIS A . n 
A 1 208 ALA 208 364 364 ALA ALA A . n 
A 1 209 LYS 209 365 ?   ?   ?   A . n 
A 1 210 GLU 210 366 ?   ?   ?   A . n 
A 1 211 GLY 211 367 ?   ?   ?   A . n 
A 1 212 ASN 212 368 ?   ?   ?   A . n 
A 1 213 GLY 213 369 ?   ?   ?   A . n 
A 1 214 PHE 214 370 ?   ?   ?   A . n 
A 1 215 GLN 215 371 371 GLN GLN A . n 
A 1 216 GLU 216 372 372 GLU GLU A . n 
A 1 217 GLU 217 373 373 GLU GLU A . n 
A 1 218 THR 218 374 374 THR THR A . n 
A 1 219 TRP 219 375 375 TRP TRP A . n 
A 1 220 ARG 220 376 376 ARG ARG A . n 
A 1 221 LEU 221 377 377 LEU LEU A . n 
A 1 222 SER 222 378 378 SER SER A . n 
A 1 223 PHE 223 379 379 PHE PHE A . n 
A 1 224 SER 224 380 380 SER SER A . n 
A 1 225 HIS 225 381 381 HIS HIS A . n 
A 1 226 ILE 226 382 382 ILE ILE A . n 
A 1 227 GLU 227 383 383 GLU GLU A . n 
A 1 228 LYS 228 384 384 LYS LYS A . n 
A 1 229 GLU 229 385 385 GLU GLU A . n 
A 1 230 ILE 230 386 386 ILE ILE A . n 
A 1 231 LEU 231 387 387 LEU LEU A . n 
A 1 232 ASN 232 388 388 ASN ASN A . n 
A 1 233 ASN 233 389 389 ASN ASN A . n 
A 1 234 HIS 234 390 390 HIS HIS A . n 
A 1 235 GLY 235 391 391 GLY GLY A . n 
A 1 236 LYS 236 392 392 LYS LYS A . n 
A 1 237 SER 237 393 393 SER SER A . n 
A 1 238 LYS 238 394 394 LYS LYS A . n 
A 1 239 THR 239 395 395 THR THR A . n 
A 1 240 CYS 240 396 396 CYS CYS A . n 
A 1 241 CYS 241 397 397 CYS CYS A . n 
A 1 242 GLU 242 398 398 GLU GLU A . n 
A 1 243 ASN 243 399 399 ASN ASN A . n 
A 1 244 LYS 244 400 400 LYS LYS A . n 
A 1 245 GLU 245 401 401 GLU GLU A . n 
A 1 246 GLU 246 402 402 GLU GLU A . n 
A 1 247 LYS 247 403 403 LYS LYS A . n 
A 1 248 CYS 248 404 404 CYS CYS A . n 
A 1 249 CYS 249 405 405 CYS CYS A . n 
A 1 250 ARG 250 406 406 ARG ARG A . n 
A 1 251 LYS 251 407 407 LYS LYS A . n 
A 1 252 ASP 252 408 408 ASP ASP A . n 
A 1 253 CYS 253 409 409 CYS CYS A . n 
A 1 254 LEU 254 410 410 LEU LEU A . n 
A 1 255 LYS 255 411 411 LYS LYS A . n 
A 1 256 LEU 256 412 412 LEU LEU A . n 
A 1 257 MET 257 413 413 MET MET A . n 
A 1 258 LYS 258 414 414 LYS LYS A . n 
A 1 259 TYR 259 415 415 TYR TYR A . n 
A 1 260 LEU 260 416 416 LEU LEU A . n 
A 1 261 LEU 261 417 417 LEU LEU A . n 
A 1 262 GLU 262 418 418 GLU GLU A . n 
A 1 263 GLN 263 419 419 GLN GLN A . n 
A 1 264 LEU 264 420 420 LEU LEU A . n 
A 1 265 LYS 265 421 421 LYS LYS A . n 
A 1 266 GLU 266 422 422 GLU GLU A . n 
A 1 267 ARG 267 423 423 ARG ARG A . n 
A 1 268 PHE 268 424 424 PHE PHE A . n 
A 1 269 LYS 269 425 425 LYS LYS A . n 
A 1 270 ASP 270 426 426 ASP ASP A . n 
A 1 271 LYS 271 427 427 LYS LYS A . n 
A 1 272 LYS 272 428 428 LYS LYS A . n 
A 1 273 HIS 273 429 429 HIS HIS A . n 
A 1 274 LEU 274 430 430 LEU LEU A . n 
A 1 275 ASP 275 431 431 ASP ASP A . n 
A 1 276 LYS 276 432 432 LYS LYS A . n 
A 1 277 PHE 277 433 433 PHE PHE A . n 
A 1 278 SER 278 434 434 SER SER A . n 
A 1 279 SER 279 435 435 SER SER A . n 
A 1 280 TYR 280 436 436 TYR TYR A . n 
A 1 281 HIS 281 437 437 HIS HIS A . n 
A 1 282 VAL 282 438 438 VAL VAL A . n 
A 1 283 LYS 283 439 439 LYS LYS A . n 
A 1 284 THR 284 440 440 THR THR A . n 
A 1 285 ALA 285 441 441 ALA ALA A . n 
A 1 286 PHE 286 442 442 PHE PHE A . n 
A 1 287 PHE 287 443 443 PHE PHE A . n 
A 1 288 HIS 288 444 444 HIS HIS A . n 
A 1 289 VAL 289 445 445 VAL VAL A . n 
A 1 290 CYS 290 446 446 CYS CYS A . n 
A 1 291 THR 291 447 447 THR THR A . n 
A 1 292 GLN 292 448 448 GLN GLN A . n 
A 1 293 ASN 293 449 449 ASN ASN A . n 
A 1 294 PRO 294 450 450 PRO PRO A . n 
A 1 295 GLN 295 451 451 GLN GLN A . n 
A 1 296 ASP 296 452 452 ASP ASP A . n 
A 1 297 SER 297 453 453 SER SER A . n 
A 1 298 GLN 298 454 454 GLN GLN A . n 
A 1 299 TRP 299 455 455 TRP TRP A . n 
A 1 300 ASP 300 456 456 ASP ASP A . n 
A 1 301 ARG 301 457 457 ARG ARG A . n 
A 1 302 LYS 302 458 458 LYS LYS A . n 
A 1 303 ASP 303 459 459 ASP ASP A . n 
A 1 304 LEU 304 460 460 LEU LEU A . n 
A 1 305 GLY 305 461 461 GLY GLY A . n 
A 1 306 LEU 306 462 462 LEU LEU A . n 
A 1 307 CYS 307 463 463 CYS CYS A . n 
A 1 308 PHE 308 464 464 PHE PHE A . n 
A 1 309 ASP 309 465 465 ASP ASP A . n 
A 1 310 ASN 310 466 466 ASN ASN A . n 
A 1 311 CYS 311 467 467 CYS CYS A . n 
A 1 312 VAL 312 468 468 VAL VAL A . n 
A 1 313 THR 313 469 469 THR THR A . n 
A 1 314 TYR 314 470 470 TYR TYR A . n 
A 1 315 PHE 315 471 471 PHE PHE A . n 
A 1 316 LEU 316 472 472 LEU LEU A . n 
A 1 317 GLN 317 473 473 GLN GLN A . n 
A 1 318 CYS 318 474 474 CYS CYS A . n 
A 1 319 LEU 319 475 475 LEU LEU A . n 
A 1 320 ARG 320 476 476 ARG ARG A . n 
A 1 321 THR 321 477 477 THR THR A . n 
A 1 322 GLU 322 478 478 GLU GLU A . n 
A 1 323 LYS 323 479 479 LYS LYS A . n 
A 1 324 LEU 324 480 480 LEU LEU A . n 
A 1 325 GLU 325 481 481 GLU GLU A . n 
A 1 326 ASN 326 482 482 ASN ASN A . n 
A 1 327 TYR 327 483 483 TYR TYR A . n 
A 1 328 PHE 328 484 484 PHE PHE A . n 
A 1 329 ILE 329 485 485 ILE ILE A . n 
A 1 330 PRO 330 486 486 PRO PRO A . n 
A 1 331 GLU 331 487 487 GLU GLU A . n 
A 1 332 PHE 332 488 488 PHE PHE A . n 
A 1 333 ASN 333 489 489 ASN ASN A . n 
A 1 334 LEU 334 490 490 LEU LEU A . n 
A 1 335 PHE 335 491 491 PHE PHE A . n 
A 1 336 SER 336 492 492 SER SER A . n 
A 1 337 SER 337 493 493 SER SER A . n 
A 1 338 ASN 338 494 494 ASN ASN A . n 
A 1 339 LEU 339 495 495 LEU LEU A . n 
A 1 340 ILE 340 496 496 ILE ILE A . n 
A 1 341 ASP 341 497 497 ASP ASP A . n 
A 1 342 LYS 342 498 498 LYS LYS A . n 
A 1 343 ARG 343 499 499 ARG ARG A . n 
A 1 344 SER 344 500 500 SER SER A . n 
A 1 345 LYS 345 501 501 LYS LYS A . n 
A 1 346 GLU 346 502 502 GLU GLU A . n 
A 1 347 PHE 347 503 503 PHE PHE A . n 
A 1 348 LEU 348 504 504 LEU LEU A . n 
A 1 349 THR 349 505 505 THR THR A . n 
A 1 350 LYS 350 506 506 LYS LYS A . n 
A 1 351 GLN 351 507 507 GLN GLN A . n 
A 1 352 ILE 352 508 508 ILE ILE A . n 
A 1 353 GLU 353 509 509 GLU GLU A . n 
A 1 354 TYR 354 510 510 TYR TYR A . n 
A 1 355 GLU 355 511 511 GLU GLU A . n 
A 1 356 ARG 356 512 512 ARG ARG A . n 
A 1 357 ASN 357 513 513 ASN ASN A . n 
A 1 358 ASN 358 514 514 ASN ASN A . n 
A 1 359 GLU 359 515 515 GLU GLU A . n 
A 1 360 PHE 360 516 516 PHE PHE A . n 
A 1 361 PRO 361 517 517 PRO PRO A . n 
A 1 362 VAL 362 518 518 VAL VAL A . n 
A 1 363 PHE 363 519 519 PHE PHE A . n 
A 1 364 ASP 364 520 520 ASP ASP A . n 
A 1 365 GLU 365 521 ?   ?   ?   A . n 
A 1 366 PHE 366 522 ?   ?   ?   A . n 
B 1 1   ASP 1   157 ?   ?   ?   B . n 
B 1 2   ALA 2   158 ?   ?   ?   B . n 
B 1 3   ALA 3   159 ?   ?   ?   B . n 
B 1 4   PRO 4   160 ?   ?   ?   B . n 
B 1 5   GLY 5   161 161 GLY GLY B . n 
B 1 6   ALA 6   162 162 ALA ALA B . n 
B 1 7   SER 7   163 163 SER SER B . n 
B 1 8   LYS 8   164 164 LYS LYS B . n 
B 1 9   LEU 9   165 165 LEU LEU B . n 
B 1 10  ARG 10  166 166 ARG ARG B . n 
B 1 11  ALA 11  167 167 ALA ALA B . n 
B 1 12  VAL 12  168 168 VAL VAL B . n 
B 1 13  LEU 13  169 169 LEU LEU B . n 
B 1 14  GLU 14  170 170 GLU GLU B . n 
B 1 15  LYS 15  171 171 LYS LYS B . n 
B 1 16  LEU 16  172 172 LEU LEU B . n 
B 1 17  LYS 17  173 173 LYS LYS B . n 
B 1 18  LEU 18  174 174 LEU LEU B . n 
B 1 19  SER 19  175 ?   ?   ?   B . n 
B 1 20  ARG 20  176 ?   ?   ?   B . n 
B 1 21  ASP 21  177 ?   ?   ?   B . n 
B 1 22  ASP 22  178 178 ASP ASP B . n 
B 1 23  ILE 23  179 179 ILE ILE B . n 
B 1 24  SER 24  180 ?   ?   ?   B . n 
B 1 25  THR 25  181 181 THR THR B . n 
B 1 26  ALA 26  182 182 ALA ALA B . n 
B 1 27  ALA 27  183 183 ALA ALA B . n 
B 1 28  GLY 28  184 184 GLY GLY B . n 
B 1 29  MET 29  185 185 MET MET B . n 
B 1 30  VAL 30  186 186 VAL VAL B . n 
B 1 31  LYS 31  187 187 LYS LYS B . n 
B 1 32  GLY 32  188 188 GLY GLY B . n 
B 1 33  VAL 33  189 189 VAL VAL B . n 
B 1 34  VAL 34  190 190 VAL VAL B . n 
B 1 35  ASP 35  191 191 ASP ASP B . n 
B 1 36  HIS 36  192 192 HIS HIS B . n 
B 1 37  LEU 37  193 193 LEU LEU B . n 
B 1 38  LEU 38  194 194 LEU LEU B . n 
B 1 39  LEU 39  195 195 LEU LEU B . n 
B 1 40  ARG 40  196 196 ARG ARG B . n 
B 1 41  LEU 41  197 197 LEU LEU B . n 
B 1 42  LYS 42  198 198 LYS LYS B . n 
B 1 43  CYS 43  199 199 CYS CYS B . n 
B 1 44  ASP 44  200 200 ASP ASP B . n 
B 1 45  SER 45  201 201 SER SER B . n 
B 1 46  ALA 46  202 202 ALA ALA B . n 
B 1 47  PHE 47  203 203 PHE PHE B . n 
B 1 48  ARG 48  204 204 ARG ARG B . n 
B 1 49  GLY 49  205 205 GLY GLY B . n 
B 1 50  VAL 50  206 206 VAL VAL B . n 
B 1 51  GLY 51  207 207 GLY GLY B . n 
B 1 52  LEU 52  208 208 LEU LEU B . n 
B 1 53  LEU 53  209 209 LEU LEU B . n 
B 1 54  ASN 54  210 210 ASN ASN B . n 
B 1 55  THR 55  211 ?   ?   ?   B . n 
B 1 56  GLY 56  212 ?   ?   ?   B . n 
B 1 57  SER 57  213 213 SER SER B . n 
B 1 58  TYR 58  214 214 TYR TYR B . n 
B 1 59  TYR 59  215 215 TYR TYR B . n 
B 1 60  GLU 60  216 216 GLU GLU B . n 
B 1 61  HIS 61  217 217 HIS HIS B . n 
B 1 62  VAL 62  218 218 VAL VAL B . n 
B 1 63  LYS 63  219 219 LYS LYS B . n 
B 1 64  ILE 64  220 220 ILE ILE B . n 
B 1 65  SER 65  221 221 SER SER B . n 
B 1 66  ALA 66  222 222 ALA ALA B . n 
B 1 67  PRO 67  223 223 PRO PRO B . n 
B 1 68  ASN 68  224 224 ASN ASN B . n 
B 1 69  GLU 69  225 225 GLU GLU B . n 
B 1 70  PHE 70  226 226 PHE PHE B . n 
B 1 71  ASP 71  227 227 ASP ASP B . n 
B 1 72  VAL 72  228 228 VAL VAL B . n 
B 1 73  MET 73  229 229 MET MET B . n 
B 1 74  PHE 74  230 230 PHE PHE B . n 
B 1 75  LYS 75  231 231 LYS LYS B . n 
B 1 76  LEU 76  232 232 LEU LEU B . n 
B 1 77  GLU 77  233 233 GLU GLU B . n 
B 1 78  VAL 78  234 234 VAL VAL B . n 
B 1 79  PRO 79  235 235 PRO PRO B . n 
B 1 80  ARG 80  236 236 ARG ARG B . n 
B 1 81  ILE 81  237 237 ILE ILE B . n 
B 1 82  GLN 82  238 238 GLN GLN B . n 
B 1 83  LEU 83  239 239 LEU LEU B . n 
B 1 84  GLU 84  240 240 GLU GLU B . n 
B 1 85  GLU 85  241 241 GLU GLU B . n 
B 1 86  TYR 86  242 242 TYR TYR B . n 
B 1 87  SER 87  243 243 SER SER B . n 
B 1 88  ASN 88  244 244 ASN ASN B . n 
B 1 89  THR 89  245 245 THR THR B . n 
B 1 90  ARG 90  246 246 ARG ARG B . n 
B 1 91  ALA 91  247 247 ALA ALA B . n 
B 1 92  TYR 92  248 248 TYR TYR B . n 
B 1 93  TYR 93  249 249 TYR TYR B . n 
B 1 94  PHE 94  250 250 PHE PHE B . n 
B 1 95  VAL 95  251 251 VAL VAL B . n 
B 1 96  LYS 96  252 252 LYS LYS B . n 
B 1 97  PHE 97  253 253 PHE PHE B . n 
B 1 98  LYS 98  254 254 LYS LYS B . n 
B 1 99  ARG 99  255 ?   ?   ?   B . n 
B 1 100 ASN 100 256 ?   ?   ?   B . n 
B 1 101 PRO 101 257 ?   ?   ?   B . n 
B 1 102 LYS 102 258 ?   ?   ?   B . n 
B 1 103 GLU 103 259 ?   ?   ?   B . n 
B 1 104 ASN 104 260 260 ASN ASN B . n 
B 1 105 PRO 105 261 261 PRO PRO B . n 
B 1 106 LEU 106 262 262 LEU LEU B . n 
B 1 107 SER 107 263 263 SER SER B . n 
B 1 108 GLN 108 264 264 GLN GLN B . n 
B 1 109 PHE 109 265 265 PHE PHE B . n 
B 1 110 LEU 110 266 266 LEU LEU B . n 
B 1 111 GLU 111 267 267 GLU GLU B . n 
B 1 112 GLY 112 268 268 GLY GLY B . n 
B 1 113 GLU 113 269 269 GLU GLU B . n 
B 1 114 ILE 114 270 270 ILE ILE B . n 
B 1 115 LEU 115 271 271 LEU LEU B . n 
B 1 116 SER 116 272 272 SER SER B . n 
B 1 117 ALA 117 273 273 ALA ALA B . n 
B 1 118 SER 118 274 274 SER SER B . n 
B 1 119 LYS 119 275 275 LYS LYS B . n 
B 1 120 MET 120 276 276 MET MET B . n 
B 1 121 LEU 121 277 277 LEU LEU B . n 
B 1 122 SER 122 278 278 SER SER B . n 
B 1 123 LYS 123 279 279 LYS LYS B . n 
B 1 124 PHE 124 280 280 PHE PHE B . n 
B 1 125 ARG 125 281 281 ARG ARG B . n 
B 1 126 LYS 126 282 282 LYS LYS B . n 
B 1 127 ILE 127 283 283 ILE ILE B . n 
B 1 128 ILE 128 284 284 ILE ILE B . n 
B 1 129 LYS 129 285 285 LYS LYS B . n 
B 1 130 GLU 130 286 286 GLU GLU B . n 
B 1 131 GLU 131 287 287 GLU GLU B . n 
B 1 132 ILE 132 288 288 ILE ILE B . n 
B 1 133 ASN 133 289 289 ASN ASN B . n 
B 1 134 ASP 134 290 290 ASP ASP B . n 
B 1 135 ILE 135 291 ?   ?   ?   B . n 
B 1 136 LYS 136 292 ?   ?   ?   B . n 
B 1 137 ASP 137 293 ?   ?   ?   B . n 
B 1 138 THR 138 294 ?   ?   ?   B . n 
B 1 139 ASP 139 295 ?   ?   ?   B . n 
B 1 140 VAL 140 296 296 VAL VAL B . n 
B 1 141 ILE 141 297 297 ILE ILE B . n 
B 1 142 MET 142 298 298 MET MET B . n 
B 1 143 LYS 143 299 299 LYS LYS B . n 
B 1 144 ARG 144 300 300 ARG ARG B . n 
B 1 145 LYS 145 301 ?   ?   ?   B . n 
B 1 146 ARG 146 302 ?   ?   ?   B . n 
B 1 147 GLY 147 303 ?   ?   ?   B . n 
B 1 148 GLY 148 304 304 GLY GLY B . n 
B 1 149 SER 149 305 305 SER SER B . n 
B 1 150 PRO 150 306 306 PRO PRO B . n 
B 1 151 ALA 151 307 307 ALA ALA B . n 
B 1 152 VAL 152 308 308 VAL VAL B . n 
B 1 153 THR 153 309 309 THR THR B . n 
B 1 154 LEU 154 310 310 LEU LEU B . n 
B 1 155 LEU 155 311 311 LEU LEU B . n 
B 1 156 ILE 156 312 312 ILE ILE B . n 
B 1 157 SER 157 313 313 SER SER B . n 
B 1 158 GLU 158 314 314 GLU GLU B . n 
B 1 159 LYS 159 315 ?   ?   ?   B . n 
B 1 160 ILE 160 316 316 ILE ILE B . n 
B 1 161 SER 161 317 317 SER SER B . n 
B 1 162 VAL 162 318 318 VAL VAL B . n 
B 1 163 ASP 163 319 319 ASP ASP B . n 
B 1 164 ILE 164 320 320 ILE ILE B . n 
B 1 165 THR 165 321 321 THR THR B . n 
B 1 166 LEU 166 322 322 LEU LEU B . n 
B 1 167 ALA 167 323 323 ALA ALA B . n 
B 1 168 LEU 168 324 324 LEU LEU B . n 
B 1 169 GLU 169 325 325 GLU GLU B . n 
B 1 170 SER 170 326 326 SER SER B . n 
B 1 171 LYS 171 327 327 LYS LYS B . n 
B 1 172 SER 172 328 328 SER SER B . n 
B 1 173 SER 173 329 329 SER SER B . n 
B 1 174 TRP 174 330 330 TRP TRP B . n 
B 1 175 PRO 175 331 331 PRO PRO B . n 
B 1 176 ALA 176 332 332 ALA ALA B . n 
B 1 177 SER 177 333 333 SER SER B . n 
B 1 178 THR 178 334 334 THR THR B . n 
B 1 179 GLN 179 335 335 GLN GLN B . n 
B 1 180 GLU 180 336 336 GLU GLU B . n 
B 1 181 GLY 181 337 337 GLY GLY B . n 
B 1 182 LEU 182 338 338 LEU LEU B . n 
B 1 183 ARG 183 339 339 ARG ARG B . n 
B 1 184 ILE 184 340 340 ILE ILE B . n 
B 1 185 GLN 185 341 341 GLN GLN B . n 
B 1 186 ASN 186 342 342 ASN ASN B . n 
B 1 187 TRP 187 343 343 TRP TRP B . n 
B 1 188 LEU 188 344 344 LEU LEU B . n 
B 1 189 SER 189 345 345 SER SER B . n 
B 1 190 ALA 190 346 346 ALA ALA B . n 
B 1 191 LYS 191 347 347 LYS LYS B . n 
B 1 192 VAL 192 348 348 VAL VAL B . n 
B 1 193 ARG 193 349 349 ARG ARG B . n 
B 1 194 LYS 194 350 350 LYS LYS B . n 
B 1 195 GLN 195 351 351 GLN GLN B . n 
B 1 196 LEU 196 352 352 LEU LEU B . n 
B 1 197 ARG 197 353 353 ARG ARG B . n 
B 1 198 LEU 198 354 354 LEU LEU B . n 
B 1 199 LYS 199 355 355 LYS LYS B . n 
B 1 200 PRO 200 356 356 PRO PRO B . n 
B 1 201 PHE 201 357 357 PHE PHE B . n 
B 1 202 TYR 202 358 358 TYR TYR B . n 
B 1 203 LEU 203 359 359 LEU LEU B . n 
B 1 204 VAL 204 360 360 VAL VAL B . n 
B 1 205 PRO 205 361 361 PRO PRO B . n 
B 1 206 LYS 206 362 362 LYS LYS B . n 
B 1 207 HIS 207 363 363 HIS HIS B . n 
B 1 208 ALA 208 364 364 ALA ALA B . n 
B 1 209 LYS 209 365 365 LYS LYS B . n 
B 1 210 GLU 210 366 ?   ?   ?   B . n 
B 1 211 GLY 211 367 ?   ?   ?   B . n 
B 1 212 ASN 212 368 ?   ?   ?   B . n 
B 1 213 GLY 213 369 ?   ?   ?   B . n 
B 1 214 PHE 214 370 ?   ?   ?   B . n 
B 1 215 GLN 215 371 371 GLN GLN B . n 
B 1 216 GLU 216 372 372 GLU GLU B . n 
B 1 217 GLU 217 373 373 GLU GLU B . n 
B 1 218 THR 218 374 374 THR THR B . n 
B 1 219 TRP 219 375 375 TRP TRP B . n 
B 1 220 ARG 220 376 376 ARG ARG B . n 
B 1 221 LEU 221 377 377 LEU LEU B . n 
B 1 222 SER 222 378 378 SER SER B . n 
B 1 223 PHE 223 379 379 PHE PHE B . n 
B 1 224 SER 224 380 380 SER SER B . n 
B 1 225 HIS 225 381 381 HIS HIS B . n 
B 1 226 ILE 226 382 382 ILE ILE B . n 
B 1 227 GLU 227 383 383 GLU GLU B . n 
B 1 228 LYS 228 384 384 LYS LYS B . n 
B 1 229 GLU 229 385 385 GLU GLU B . n 
B 1 230 ILE 230 386 386 ILE ILE B . n 
B 1 231 LEU 231 387 387 LEU LEU B . n 
B 1 232 ASN 232 388 388 ASN ASN B . n 
B 1 233 ASN 233 389 389 ASN ASN B . n 
B 1 234 HIS 234 390 390 HIS HIS B . n 
B 1 235 GLY 235 391 391 GLY GLY B . n 
B 1 236 LYS 236 392 392 LYS LYS B . n 
B 1 237 SER 237 393 393 SER SER B . n 
B 1 238 LYS 238 394 394 LYS LYS B . n 
B 1 239 THR 239 395 395 THR THR B . n 
B 1 240 CYS 240 396 396 CYS CYS B . n 
B 1 241 CYS 241 397 397 CYS CYS B . n 
B 1 242 GLU 242 398 398 GLU GLU B . n 
B 1 243 ASN 243 399 399 ASN ASN B . n 
B 1 244 LYS 244 400 400 LYS LYS B . n 
B 1 245 GLU 245 401 401 GLU GLU B . n 
B 1 246 GLU 246 402 402 GLU GLU B . n 
B 1 247 LYS 247 403 403 LYS LYS B . n 
B 1 248 CYS 248 404 404 CYS CYS B . n 
B 1 249 CYS 249 405 405 CYS CYS B . n 
B 1 250 ARG 250 406 406 ARG ARG B . n 
B 1 251 LYS 251 407 407 LYS LYS B . n 
B 1 252 ASP 252 408 408 ASP ASP B . n 
B 1 253 CYS 253 409 409 CYS CYS B . n 
B 1 254 LEU 254 410 410 LEU LEU B . n 
B 1 255 LYS 255 411 411 LYS LYS B . n 
B 1 256 LEU 256 412 412 LEU LEU B . n 
B 1 257 MET 257 413 413 MET MET B . n 
B 1 258 LYS 258 414 414 LYS LYS B . n 
B 1 259 TYR 259 415 415 TYR TYR B . n 
B 1 260 LEU 260 416 416 LEU LEU B . n 
B 1 261 LEU 261 417 417 LEU LEU B . n 
B 1 262 GLU 262 418 418 GLU GLU B . n 
B 1 263 GLN 263 419 419 GLN GLN B . n 
B 1 264 LEU 264 420 420 LEU LEU B . n 
B 1 265 LYS 265 421 421 LYS LYS B . n 
B 1 266 GLU 266 422 422 GLU GLU B . n 
B 1 267 ARG 267 423 423 ARG ARG B . n 
B 1 268 PHE 268 424 424 PHE PHE B . n 
B 1 269 LYS 269 425 425 LYS LYS B . n 
B 1 270 ASP 270 426 426 ASP ASP B . n 
B 1 271 LYS 271 427 427 LYS LYS B . n 
B 1 272 LYS 272 428 428 LYS LYS B . n 
B 1 273 HIS 273 429 429 HIS HIS B . n 
B 1 274 LEU 274 430 430 LEU LEU B . n 
B 1 275 ASP 275 431 431 ASP ASP B . n 
B 1 276 LYS 276 432 432 LYS LYS B . n 
B 1 277 PHE 277 433 433 PHE PHE B . n 
B 1 278 SER 278 434 434 SER SER B . n 
B 1 279 SER 279 435 435 SER SER B . n 
B 1 280 TYR 280 436 436 TYR TYR B . n 
B 1 281 HIS 281 437 437 HIS HIS B . n 
B 1 282 VAL 282 438 438 VAL VAL B . n 
B 1 283 LYS 283 439 439 LYS LYS B . n 
B 1 284 THR 284 440 440 THR THR B . n 
B 1 285 ALA 285 441 441 ALA ALA B . n 
B 1 286 PHE 286 442 442 PHE PHE B . n 
B 1 287 PHE 287 443 443 PHE PHE B . n 
B 1 288 HIS 288 444 444 HIS HIS B . n 
B 1 289 VAL 289 445 445 VAL VAL B . n 
B 1 290 CYS 290 446 446 CYS CYS B . n 
B 1 291 THR 291 447 447 THR THR B . n 
B 1 292 GLN 292 448 448 GLN GLN B . n 
B 1 293 ASN 293 449 449 ASN ASN B . n 
B 1 294 PRO 294 450 450 PRO PRO B . n 
B 1 295 GLN 295 451 451 GLN GLN B . n 
B 1 296 ASP 296 452 452 ASP ASP B . n 
B 1 297 SER 297 453 453 SER SER B . n 
B 1 298 GLN 298 454 454 GLN GLN B . n 
B 1 299 TRP 299 455 455 TRP TRP B . n 
B 1 300 ASP 300 456 456 ASP ASP B . n 
B 1 301 ARG 301 457 457 ARG ARG B . n 
B 1 302 LYS 302 458 458 LYS LYS B . n 
B 1 303 ASP 303 459 459 ASP ASP B . n 
B 1 304 LEU 304 460 460 LEU LEU B . n 
B 1 305 GLY 305 461 461 GLY GLY B . n 
B 1 306 LEU 306 462 462 LEU LEU B . n 
B 1 307 CYS 307 463 463 CYS CYS B . n 
B 1 308 PHE 308 464 464 PHE PHE B . n 
B 1 309 ASP 309 465 465 ASP ASP B . n 
B 1 310 ASN 310 466 466 ASN ASN B . n 
B 1 311 CYS 311 467 467 CYS CYS B . n 
B 1 312 VAL 312 468 468 VAL VAL B . n 
B 1 313 THR 313 469 469 THR THR B . n 
B 1 314 TYR 314 470 470 TYR TYR B . n 
B 1 315 PHE 315 471 471 PHE PHE B . n 
B 1 316 LEU 316 472 472 LEU LEU B . n 
B 1 317 GLN 317 473 473 GLN GLN B . n 
B 1 318 CYS 318 474 474 CYS CYS B . n 
B 1 319 LEU 319 475 475 LEU LEU B . n 
B 1 320 ARG 320 476 476 ARG ARG B . n 
B 1 321 THR 321 477 477 THR THR B . n 
B 1 322 GLU 322 478 478 GLU GLU B . n 
B 1 323 LYS 323 479 479 LYS LYS B . n 
B 1 324 LEU 324 480 480 LEU LEU B . n 
B 1 325 GLU 325 481 481 GLU GLU B . n 
B 1 326 ASN 326 482 482 ASN ASN B . n 
B 1 327 TYR 327 483 483 TYR TYR B . n 
B 1 328 PHE 328 484 484 PHE PHE B . n 
B 1 329 ILE 329 485 485 ILE ILE B . n 
B 1 330 PRO 330 486 486 PRO PRO B . n 
B 1 331 GLU 331 487 487 GLU GLU B . n 
B 1 332 PHE 332 488 488 PHE PHE B . n 
B 1 333 ASN 333 489 489 ASN ASN B . n 
B 1 334 LEU 334 490 490 LEU LEU B . n 
B 1 335 PHE 335 491 491 PHE PHE B . n 
B 1 336 SER 336 492 492 SER SER B . n 
B 1 337 SER 337 493 493 SER SER B . n 
B 1 338 ASN 338 494 494 ASN ASN B . n 
B 1 339 LEU 339 495 495 LEU LEU B . n 
B 1 340 ILE 340 496 496 ILE ILE B . n 
B 1 341 ASP 341 497 497 ASP ASP B . n 
B 1 342 LYS 342 498 498 LYS LYS B . n 
B 1 343 ARG 343 499 499 ARG ARG B . n 
B 1 344 SER 344 500 500 SER SER B . n 
B 1 345 LYS 345 501 501 LYS LYS B . n 
B 1 346 GLU 346 502 502 GLU GLU B . n 
B 1 347 PHE 347 503 503 PHE PHE B . n 
B 1 348 LEU 348 504 504 LEU LEU B . n 
B 1 349 THR 349 505 505 THR THR B . n 
B 1 350 LYS 350 506 506 LYS LYS B . n 
B 1 351 GLN 351 507 507 GLN GLN B . n 
B 1 352 ILE 352 508 508 ILE ILE B . n 
B 1 353 GLU 353 509 509 GLU GLU B . n 
B 1 354 TYR 354 510 510 TYR TYR B . n 
B 1 355 GLU 355 511 511 GLU GLU B . n 
B 1 356 ARG 356 512 512 ARG ARG B . n 
B 1 357 ASN 357 513 513 ASN ASN B . n 
B 1 358 ASN 358 514 514 ASN ASN B . n 
B 1 359 GLU 359 515 515 GLU GLU B . n 
B 1 360 PHE 360 516 516 PHE PHE B . n 
B 1 361 PRO 361 517 517 PRO PRO B . n 
B 1 362 VAL 362 518 518 VAL VAL B . n 
B 1 363 PHE 363 519 519 PHE PHE B . n 
B 1 364 ASP 364 520 520 ASP ASP B . n 
B 1 365 GLU 365 521 ?   ?   ?   B . n 
B 1 366 PHE 366 522 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EAH 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EAH 
_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 A1EAH 1  601 1  A1EAH DRG A . 
D 3 ZN    1  602 2  ZN    ZN  A . 
E 2 A1EAH 1  601 2  A1EAH DRG B . 
F 3 ZN    1  602 1  ZN    ZN  B . 
G 4 HOH   1  701 54 HOH   HOH A . 
G 4 HOH   2  702 70 HOH   HOH A . 
G 4 HOH   3  703 49 HOH   HOH A . 
G 4 HOH   4  704 22 HOH   HOH A . 
G 4 HOH   5  705 20 HOH   HOH A . 
G 4 HOH   6  706 3  HOH   HOH A . 
G 4 HOH   7  707 4  HOH   HOH A . 
G 4 HOH   8  708 2  HOH   HOH A . 
G 4 HOH   9  709 17 HOH   HOH A . 
G 4 HOH   10 710 24 HOH   HOH A . 
G 4 HOH   11 711 40 HOH   HOH A . 
G 4 HOH   12 712 31 HOH   HOH A . 
G 4 HOH   13 713 53 HOH   HOH A . 
G 4 HOH   14 714 28 HOH   HOH A . 
G 4 HOH   15 715 7  HOH   HOH A . 
G 4 HOH   16 716 5  HOH   HOH A . 
G 4 HOH   17 717 61 HOH   HOH A . 
G 4 HOH   18 718 26 HOH   HOH A . 
G 4 HOH   19 719 65 HOH   HOH A . 
G 4 HOH   20 720 69 HOH   HOH A . 
G 4 HOH   21 721 10 HOH   HOH A . 
G 4 HOH   22 722 13 HOH   HOH A . 
G 4 HOH   23 723 34 HOH   HOH A . 
G 4 HOH   24 724 62 HOH   HOH A . 
G 4 HOH   25 725 63 HOH   HOH A . 
G 4 HOH   26 726 32 HOH   HOH A . 
G 4 HOH   27 727 35 HOH   HOH A . 
G 4 HOH   28 728 51 HOH   HOH A . 
G 4 HOH   29 729 42 HOH   HOH A . 
G 4 HOH   30 730 64 HOH   HOH A . 
G 4 HOH   31 731 57 HOH   HOH A . 
G 4 HOH   32 732 29 HOH   HOH A . 
G 4 HOH   33 733 11 HOH   HOH A . 
G 4 HOH   34 734 60 HOH   HOH A . 
H 4 HOH   1  701 45 HOH   HOH B . 
H 4 HOH   2  702 33 HOH   HOH B . 
H 4 HOH   3  703 43 HOH   HOH B . 
H 4 HOH   4  704 8  HOH   HOH B . 
H 4 HOH   5  705 19 HOH   HOH B . 
H 4 HOH   6  706 6  HOH   HOH B . 
H 4 HOH   7  707 67 HOH   HOH B . 
H 4 HOH   8  708 39 HOH   HOH B . 
H 4 HOH   9  709 18 HOH   HOH B . 
H 4 HOH   10 710 46 HOH   HOH B . 
H 4 HOH   11 711 41 HOH   HOH B . 
H 4 HOH   12 712 50 HOH   HOH B . 
H 4 HOH   13 713 38 HOH   HOH B . 
H 4 HOH   14 714 21 HOH   HOH B . 
H 4 HOH   15 715 48 HOH   HOH B . 
H 4 HOH   16 716 59 HOH   HOH B . 
H 4 HOH   17 717 14 HOH   HOH B . 
H 4 HOH   18 718 30 HOH   HOH B . 
H 4 HOH   19 719 44 HOH   HOH B . 
H 4 HOH   20 720 37 HOH   HOH B . 
H 4 HOH   21 721 23 HOH   HOH B . 
H 4 HOH   22 722 55 HOH   HOH B . 
H 4 HOH   23 723 27 HOH   HOH B . 
H 4 HOH   24 724 9  HOH   HOH B . 
H 4 HOH   25 725 1  HOH   HOH B . 
H 4 HOH   26 726 36 HOH   HOH B . 
H 4 HOH   27 727 12 HOH   HOH B . 
H 4 HOH   28 728 16 HOH   HOH B . 
H 4 HOH   29 729 15 HOH   HOH B . 
H 4 HOH   30 730 56 HOH   HOH B . 
H 4 HOH   31 731 68 HOH   HOH B . 
H 4 HOH   32 732 58 HOH   HOH B . 
H 4 HOH   33 733 52 HOH   HOH B . 
H 4 HOH   34 734 66 HOH   HOH B . 
H 4 HOH   35 735 25 HOH   HOH B . 
H 4 HOH   36 736 47 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A ILE 179 ? CG1 ? A ILE 23  CG1 
2   1 Y 1 A ILE 179 ? CG2 ? A ILE 23  CG2 
3   1 Y 1 A ILE 179 ? CD1 ? A ILE 23  CD1 
4   1 Y 1 A ARG 204 ? CG  ? A ARG 48  CG  
5   1 Y 1 A ARG 204 ? CD  ? A ARG 48  CD  
6   1 Y 1 A ARG 204 ? NE  ? A ARG 48  NE  
7   1 Y 1 A ARG 204 ? CZ  ? A ARG 48  CZ  
8   1 Y 1 A ARG 204 ? NH1 ? A ARG 48  NH1 
9   1 Y 1 A ARG 204 ? NH2 ? A ARG 48  NH2 
10  1 Y 1 A GLU 216 ? CG  ? A GLU 60  CG  
11  1 Y 1 A GLU 216 ? CD  ? A GLU 60  CD  
12  1 Y 1 A GLU 216 ? OE1 ? A GLU 60  OE1 
13  1 Y 1 A GLU 216 ? OE2 ? A GLU 60  OE2 
14  1 Y 1 A LYS 252 ? CG  ? A LYS 96  CG  
15  1 Y 1 A LYS 252 ? CD  ? A LYS 96  CD  
16  1 Y 1 A LYS 252 ? CE  ? A LYS 96  CE  
17  1 Y 1 A LYS 252 ? NZ  ? A LYS 96  NZ  
18  1 Y 1 A LYS 254 ? CG  ? A LYS 98  CG  
19  1 Y 1 A LYS 254 ? CD  ? A LYS 98  CD  
20  1 Y 1 A LYS 254 ? CE  ? A LYS 98  CE  
21  1 Y 1 A LYS 254 ? NZ  ? A LYS 98  NZ  
22  1 Y 1 A GLU 267 ? CG  ? A GLU 111 CG  
23  1 Y 1 A GLU 267 ? CD  ? A GLU 111 CD  
24  1 Y 1 A GLU 267 ? OE1 ? A GLU 111 OE1 
25  1 Y 1 A GLU 267 ? OE2 ? A GLU 111 OE2 
26  1 Y 1 A LYS 275 ? CG  ? A LYS 119 CG  
27  1 Y 1 A LYS 275 ? CD  ? A LYS 119 CD  
28  1 Y 1 A LYS 275 ? CE  ? A LYS 119 CE  
29  1 Y 1 A LYS 275 ? NZ  ? A LYS 119 NZ  
30  1 Y 1 A LYS 279 ? CG  ? A LYS 123 CG  
31  1 Y 1 A LYS 279 ? CD  ? A LYS 123 CD  
32  1 Y 1 A LYS 279 ? CE  ? A LYS 123 CE  
33  1 Y 1 A LYS 279 ? NZ  ? A LYS 123 NZ  
34  1 Y 1 A LYS 282 ? CG  ? A LYS 126 CG  
35  1 Y 1 A LYS 282 ? CD  ? A LYS 126 CD  
36  1 Y 1 A LYS 282 ? CE  ? A LYS 126 CE  
37  1 Y 1 A LYS 282 ? NZ  ? A LYS 126 NZ  
38  1 Y 1 A LYS 299 ? CG  ? A LYS 143 CG  
39  1 Y 1 A LYS 299 ? CD  ? A LYS 143 CD  
40  1 Y 1 A LYS 299 ? CE  ? A LYS 143 CE  
41  1 Y 1 A LYS 299 ? NZ  ? A LYS 143 NZ  
42  1 Y 1 A ARG 300 ? CG  ? A ARG 144 CG  
43  1 Y 1 A ARG 300 ? CD  ? A ARG 144 CD  
44  1 Y 1 A ARG 300 ? NE  ? A ARG 144 NE  
45  1 Y 1 A ARG 300 ? CZ  ? A ARG 144 CZ  
46  1 Y 1 A ARG 300 ? NH1 ? A ARG 144 NH1 
47  1 Y 1 A ARG 300 ? NH2 ? A ARG 144 NH2 
48  1 Y 1 A VAL 308 ? CG1 ? A VAL 152 CG1 
49  1 Y 1 A VAL 308 ? CG2 ? A VAL 152 CG2 
50  1 Y 1 A ILE 312 ? CG1 ? A ILE 156 CG1 
51  1 Y 1 A ILE 312 ? CG2 ? A ILE 156 CG2 
52  1 Y 1 A ILE 312 ? CD1 ? A ILE 156 CD1 
53  1 Y 1 A GLU 314 ? CG  ? A GLU 158 CG  
54  1 Y 1 A GLU 314 ? CD  ? A GLU 158 CD  
55  1 Y 1 A GLU 314 ? OE1 ? A GLU 158 OE1 
56  1 Y 1 A GLU 314 ? OE2 ? A GLU 158 OE2 
57  1 Y 1 A LYS 315 ? CG  ? A LYS 159 CG  
58  1 Y 1 A LYS 315 ? CD  ? A LYS 159 CD  
59  1 Y 1 A LYS 315 ? CE  ? A LYS 159 CE  
60  1 Y 1 A LYS 315 ? NZ  ? A LYS 159 NZ  
61  1 Y 1 A ILE 316 ? CG1 ? A ILE 160 CG1 
62  1 Y 1 A ILE 316 ? CG2 ? A ILE 160 CG2 
63  1 Y 1 A ILE 316 ? CD1 ? A ILE 160 CD1 
64  1 Y 1 A GLN 351 ? CG  ? A GLN 195 CG  
65  1 Y 1 A GLN 351 ? CD  ? A GLN 195 CD  
66  1 Y 1 A GLN 351 ? OE1 ? A GLN 195 OE1 
67  1 Y 1 A GLN 351 ? NE2 ? A GLN 195 NE2 
68  1 Y 1 A HIS 363 ? CG  ? A HIS 207 CG  
69  1 Y 1 A HIS 363 ? ND1 ? A HIS 207 ND1 
70  1 Y 1 A HIS 363 ? CD2 ? A HIS 207 CD2 
71  1 Y 1 A HIS 363 ? CE1 ? A HIS 207 CE1 
72  1 Y 1 A HIS 363 ? NE2 ? A HIS 207 NE2 
73  1 Y 1 A GLU 372 ? CG  ? A GLU 216 CG  
74  1 Y 1 A GLU 372 ? CD  ? A GLU 216 CD  
75  1 Y 1 A GLU 372 ? OE1 ? A GLU 216 OE1 
76  1 Y 1 A GLU 372 ? OE2 ? A GLU 216 OE2 
77  1 Y 1 A LYS 439 ? CG  ? A LYS 283 CG  
78  1 Y 1 A LYS 439 ? CD  ? A LYS 283 CD  
79  1 Y 1 A LYS 439 ? CE  ? A LYS 283 CE  
80  1 Y 1 A LYS 439 ? NZ  ? A LYS 283 NZ  
81  1 Y 1 A LYS 479 ? CG  ? A LYS 323 CG  
82  1 Y 1 A LYS 479 ? CD  ? A LYS 323 CD  
83  1 Y 1 A LYS 479 ? CE  ? A LYS 323 CE  
84  1 Y 1 A LYS 479 ? NZ  ? A LYS 323 NZ  
85  1 Y 1 B GLU 170 ? CG  ? B GLU 14  CG  
86  1 Y 1 B GLU 170 ? CD  ? B GLU 14  CD  
87  1 Y 1 B GLU 170 ? OE1 ? B GLU 14  OE1 
88  1 Y 1 B GLU 170 ? OE2 ? B GLU 14  OE2 
89  1 Y 1 B LYS 171 ? CG  ? B LYS 15  CG  
90  1 Y 1 B LYS 171 ? CD  ? B LYS 15  CD  
91  1 Y 1 B LYS 171 ? CE  ? B LYS 15  CE  
92  1 Y 1 B LYS 171 ? NZ  ? B LYS 15  NZ  
93  1 Y 1 B ASP 178 ? CG  ? B ASP 22  CG  
94  1 Y 1 B ASP 178 ? OD1 ? B ASP 22  OD1 
95  1 Y 1 B ASP 178 ? OD2 ? B ASP 22  OD2 
96  1 Y 1 B ILE 179 ? CG1 ? B ILE 23  CG1 
97  1 Y 1 B ILE 179 ? CG2 ? B ILE 23  CG2 
98  1 Y 1 B ILE 179 ? CD1 ? B ILE 23  CD1 
99  1 Y 1 B LYS 187 ? CG  ? B LYS 31  CG  
100 1 Y 1 B LYS 187 ? CD  ? B LYS 31  CD  
101 1 Y 1 B LYS 187 ? CE  ? B LYS 31  CE  
102 1 Y 1 B LYS 187 ? NZ  ? B LYS 31  NZ  
103 1 Y 1 B ASP 191 ? CG  ? B ASP 35  CG  
104 1 Y 1 B ASP 191 ? OD1 ? B ASP 35  OD1 
105 1 Y 1 B ASP 191 ? OD2 ? B ASP 35  OD2 
106 1 Y 1 B ASN 210 ? CG  ? B ASN 54  CG  
107 1 Y 1 B ASN 210 ? OD1 ? B ASN 54  OD1 
108 1 Y 1 B ASN 210 ? ND2 ? B ASN 54  ND2 
109 1 Y 1 B TYR 215 ? CG  ? B TYR 59  CG  
110 1 Y 1 B TYR 215 ? CD1 ? B TYR 59  CD1 
111 1 Y 1 B TYR 215 ? CD2 ? B TYR 59  CD2 
112 1 Y 1 B TYR 215 ? CE1 ? B TYR 59  CE1 
113 1 Y 1 B TYR 215 ? CE2 ? B TYR 59  CE2 
114 1 Y 1 B TYR 215 ? CZ  ? B TYR 59  CZ  
115 1 Y 1 B TYR 215 ? OH  ? B TYR 59  OH  
116 1 Y 1 B GLU 216 ? CG  ? B GLU 60  CG  
117 1 Y 1 B GLU 216 ? CD  ? B GLU 60  CD  
118 1 Y 1 B GLU 216 ? OE1 ? B GLU 60  OE1 
119 1 Y 1 B GLU 216 ? OE2 ? B GLU 60  OE2 
120 1 Y 1 B ARG 236 ? CG  ? B ARG 80  CG  
121 1 Y 1 B ARG 236 ? CD  ? B ARG 80  CD  
122 1 Y 1 B ARG 236 ? NE  ? B ARG 80  NE  
123 1 Y 1 B ARG 236 ? CZ  ? B ARG 80  CZ  
124 1 Y 1 B ARG 236 ? NH1 ? B ARG 80  NH1 
125 1 Y 1 B ARG 236 ? NH2 ? B ARG 80  NH2 
126 1 Y 1 B LYS 254 ? CG  ? B LYS 98  CG  
127 1 Y 1 B LYS 254 ? CD  ? B LYS 98  CD  
128 1 Y 1 B LYS 254 ? CE  ? B LYS 98  CE  
129 1 Y 1 B LYS 254 ? NZ  ? B LYS 98  NZ  
130 1 Y 1 B GLU 267 ? CG  ? B GLU 111 CG  
131 1 Y 1 B GLU 267 ? CD  ? B GLU 111 CD  
132 1 Y 1 B GLU 267 ? OE1 ? B GLU 111 OE1 
133 1 Y 1 B GLU 267 ? OE2 ? B GLU 111 OE2 
134 1 Y 1 B ILE 297 ? CG1 ? B ILE 141 CG1 
135 1 Y 1 B ILE 297 ? CG2 ? B ILE 141 CG2 
136 1 Y 1 B ILE 297 ? CD1 ? B ILE 141 CD1 
137 1 Y 1 B MET 298 ? CG  ? B MET 142 CG  
138 1 Y 1 B MET 298 ? SD  ? B MET 142 SD  
139 1 Y 1 B MET 298 ? CE  ? B MET 142 CE  
140 1 Y 1 B LYS 299 ? CG  ? B LYS 143 CG  
141 1 Y 1 B LYS 299 ? CD  ? B LYS 143 CD  
142 1 Y 1 B LYS 299 ? CE  ? B LYS 143 CE  
143 1 Y 1 B LYS 299 ? NZ  ? B LYS 143 NZ  
144 1 Y 1 B ARG 300 ? CG  ? B ARG 144 CG  
145 1 Y 1 B ARG 300 ? CD  ? B ARG 144 CD  
146 1 Y 1 B ARG 300 ? NE  ? B ARG 144 NE  
147 1 Y 1 B ARG 300 ? CZ  ? B ARG 144 CZ  
148 1 Y 1 B ARG 300 ? NH1 ? B ARG 144 NH1 
149 1 Y 1 B ARG 300 ? NH2 ? B ARG 144 NH2 
150 1 Y 1 B SER 313 ? OG  ? B SER 157 OG  
151 1 Y 1 B GLU 314 ? CG  ? B GLU 158 CG  
152 1 Y 1 B GLU 314 ? CD  ? B GLU 158 CD  
153 1 Y 1 B GLU 314 ? OE1 ? B GLU 158 OE1 
154 1 Y 1 B GLU 314 ? OE2 ? B GLU 158 OE2 
155 1 Y 1 B LYS 365 ? CG  ? B LYS 209 CG  
156 1 Y 1 B LYS 365 ? CD  ? B LYS 209 CD  
157 1 Y 1 B LYS 365 ? CE  ? B LYS 209 CE  
158 1 Y 1 B LYS 365 ? NZ  ? B LYS 209 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   113.53 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9J2W 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     216.292 
_cell.length_a_esd                 ? 
_cell.length_b                     47.502 
_cell.length_b_esd                 ? 
_cell.length_c                     87.581 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9J2W 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9J2W 
_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             2.41 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.00 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '18-20% V/V PEG 3350, 0.2 M AMMONIUM CITRATE' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-11-13 
_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   0.979 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9J2W 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.20 
_reflns.d_resolution_low                               50.00 
_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                                     40994 
_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                           97.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.989 
_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                                0.110 
_reflns.pdbx_Rpim_I_all                                0.030 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       517408 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.106 
_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 2.28  ? ? ? ? ? ? 3743 ? ? ? ? ? ? ? ? ? ? ? 8.8  0.852 ? ? 0.934 0.281 ? 1  1 0.911 0.977 ? 90.1 ? 0.889 ? ? ? ? ? ? ? ? ? 
2.28 2.37  ? ? ? ? ? ? 4020 ? ? ? ? ? ? ? ? ? ? ? 10.4 0.894 ? ? 0.837 0.244 ? 2  1 0.931 0.982 ? 96.0 ? 0.799 ? ? ? ? ? ? ? ? ? 
2.37 2.48  ? ? ? ? ? ? 4111 ? ? ? ? ? ? ? ? ? ? ? 12.8 0.910 ? ? 0.708 0.193 ? 3  1 0.958 0.989 ? 99.2 ? 0.680 ? ? ? ? ? ? ? ? ? 
2.48 2.61  ? ? ? ? ? ? 4121 ? ? ? ? ? ? ? ? ? ? ? 13.6 0.911 ? ? 0.539 0.144 ? 4  1 0.968 0.992 ? 99.2 ? 0.519 ? ? ? ? ? ? ? ? ? 
2.61 2.77  ? ? ? ? ? ? 4147 ? ? ? ? ? ? ? ? ? ? ? 13.2 0.921 ? ? 0.376 0.102 ? 5  1 0.985 0.996 ? 99.1 ? 0.362 ? ? ? ? ? ? ? ? ? 
2.77 2.99  ? ? ? ? ? ? 4098 ? ? ? ? ? ? ? ? ? ? ? 13.4 0.938 ? ? 0.232 0.062 ? 6  1 0.993 0.998 ? 98.2 ? 0.223 ? ? ? ? ? ? ? ? ? 
2.99 3.29  ? ? ? ? ? ? 4161 ? ? ? ? ? ? ? ? ? ? ? 13.9 1.022 ? ? 0.143 0.038 ? 7  1 0.996 0.999 ? 99.3 ? 0.138 ? ? ? ? ? ? ? ? ? 
3.29 3.76  ? ? ? ? ? ? 4131 ? ? ? ? ? ? ? ? ? ? ? 13.0 1.131 ? ? 0.091 0.025 ? 8  1 0.998 0.999 ? 98.3 ? 0.087 ? ? ? ? ? ? ? ? ? 
3.76 4.74  ? ? ? ? ? ? 4209 ? ? ? ? ? ? ? ? ? ? ? 14.0 1.141 ? ? 0.066 0.017 ? 9  1 0.998 1.000 ? 98.8 ? 0.063 ? ? ? ? ? ? ? ? ? 
4.74 50.00 ? ? ? ? ? ? 4253 ? ? ? ? ? ? ? ? ? ? ? 12.7 1.078 ? ? 0.057 0.016 ? 10 1 0.999 1.000 ? 97.7 ? 0.055 ? ? ? ? ? ? ? ? ? 
# 
_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                                 9J2W 
_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                             32.92 
_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                     37371 
_refine.ls_number_reflns_R_free                  1805 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    88.59 
_refine.ls_percent_reflns_R_free                 4.83 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2324 
_refine.ls_R_factor_R_free                       0.2590 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2311 
_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                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4lev 
_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                 27.65 
_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                            0.24 
_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        5278 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         80 
_refine_hist.number_atoms_solvent             70 
_refine_hist.number_atoms_total               5428 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        32.92 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  ? 5462 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.857  ? 7344 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.781 ? 2072 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.058  ? 808  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 916  ? 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 2.26  . . 90  1550 51.00 . . . . 0.2912 . . . . . . . . . . . 0.3711 
'X-RAY DIFFRACTION' 2.26 2.32  . . 79  1914 62.00 . . . . 0.2924 . . . . . . . . . . . 0.3125 
'X-RAY DIFFRACTION' 2.32 2.40  . . 112 2230 73.00 . . . . 0.2742 . . . . . . . . . . . 0.3087 
'X-RAY DIFFRACTION' 2.40 2.48  . . 132 2598 85.00 . . . . 0.2684 . . . . . . . . . . . 0.3506 
'X-RAY DIFFRACTION' 2.48 2.58  . . 158 2913 96.00 . . . . 0.2653 . . . . . . . . . . . 0.2691 
'X-RAY DIFFRACTION' 2.58 2.70  . . 159 2979 98.00 . . . . 0.2586 . . . . . . . . . . . 0.2762 
'X-RAY DIFFRACTION' 2.70 2.84  . . 154 3024 98.00 . . . . 0.2460 . . . . . . . . . . . 0.2897 
'X-RAY DIFFRACTION' 2.84 3.02  . . 161 3047 99.00 . . . . 0.2498 . . . . . . . . . . . 0.3106 
'X-RAY DIFFRACTION' 3.02 3.25  . . 142 3057 99.00 . . . . 0.2448 . . . . . . . . . . . 0.2515 
'X-RAY DIFFRACTION' 3.25 3.58  . . 124 3088 99.00 . . . . 0.2275 . . . . . . . . . . . 0.2426 
'X-RAY DIFFRACTION' 3.58 4.10  . . 184 3003 98.00 . . . . 0.2000 . . . . . . . . . . . 0.2251 
'X-RAY DIFFRACTION' 4.10 5.16  . . 142 3093 98.00 . . . . 0.1875 . . . . . . . . . . . 0.2256 
'X-RAY DIFFRACTION' 5.16 32.92 . . 168 3070 96.00 . . . . 0.2330 . . . . . . . . . . . 0.2424 
# 
_struct.entry_id                     9J2W 
_struct.title                        'Human cGAS catalytic domain bound with XL-3156' 
_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        9J2W 
_struct_keywords.text            'cGAS, inhibitor, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CGAS_HUMAN 
_struct_ref.pdbx_db_accession          Q8N884 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DAAPGASKLRAVLEKLKLSRDDISTAAGMVKGVVDHLLLRLKCDSAFRGVGLLNTGSYYEHVKISAPNEFDVMFKLEVPR
IQLEEYSNTRAYYFVKFKRNPKENPLSQFLEGEILSASKMLSKFRKIIKEEINDIKDTDVIMKRKRGGSPAVTLLISEKI
SVDITLALESKSSWPASTQEGLRIQNWLSAKVRKQLRLKPFYLVPKHAKEGNGFQEETWRLSFSHIEKEILNNHGKSKTC
CENKEEKCCRKDCLKLMKYLLEQLKERFKDKKHLDKFSSYHVKTAFFHVCTQNPQDSQWDRKDLGLCFDNCVTYFLQCLR
TEKLENYFIPEFNLFSSNLIDKRSKEFLTKQIEYERNNEFPVFDEF
;
_struct_ref.pdbx_align_begin           157 
# 
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 9J2W A 1 ? 366 ? Q8N884 157 ? 522 ? 157 522 
2 1 9J2W B 1 ? 366 ? Q8N884 157 ? 522 ? 157 522 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_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,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 5   ? SER A 19  ? GLY A 161 SER A 175 1 ? 15 
HELX_P HELX_P2  AA2 SER A 24  ? CYS A 43  ? SER A 180 CYS A 199 1 ? 20 
HELX_P HELX_P3  AA3 LEU A 106 ? GLN A 108 ? LEU A 262 GLN A 264 5 ? 3  
HELX_P HELX_P4  AA4 SER A 116 ? ILE A 128 ? SER A 272 ILE A 284 1 ? 13 
HELX_P HELX_P5  AA5 PRO A 175 ? GLN A 179 ? PRO A 331 GLN A 335 5 ? 5  
HELX_P HELX_P6  AA6 SER A 189 ? LEU A 198 ? SER A 345 LEU A 354 1 ? 10 
HELX_P HELX_P7  AA7 PHE A 223 ? ASN A 232 ? PHE A 379 ASN A 388 1 ? 10 
HELX_P HELX_P8  AA8 ASN A 243 ? LYS A 247 ? ASN A 399 LYS A 403 5 ? 5  
HELX_P HELX_P9  AA9 CYS A 249 ? PHE A 268 ? CYS A 405 PHE A 424 1 ? 20 
HELX_P HELX_P10 AB1 SER A 278 ? ASN A 293 ? SER A 434 ASN A 449 1 ? 16 
HELX_P HELX_P11 AB2 GLN A 295 ? LYS A 302 ? GLN A 451 LYS A 458 5 ? 8  
HELX_P HELX_P12 AB3 ASP A 303 ? GLU A 322 ? ASP A 459 GLU A 478 1 ? 20 
HELX_P HELX_P13 AB4 ASP A 341 ? ASN A 358 ? ASP A 497 ASN A 514 1 ? 18 
HELX_P HELX_P14 AB5 GLU A 359 ? ASP A 364 ? GLU A 515 ASP A 520 5 ? 6  
HELX_P HELX_P15 AB6 ALA B 6   ? LEU B 18  ? ALA B 162 LEU B 174 1 ? 13 
HELX_P HELX_P16 AB7 ASP B 22  ? ILE B 23  ? ASP B 178 ILE B 179 5 ? 2  
HELX_P HELX_P17 AB8 THR B 25  ? THR B 25  ? THR B 181 THR B 181 5 ? 1  
HELX_P HELX_P18 AB9 ALA B 26  ? CYS B 43  ? ALA B 182 CYS B 199 1 ? 18 
HELX_P HELX_P19 AC1 LEU B 106 ? GLN B 108 ? LEU B 262 GLN B 264 5 ? 3  
HELX_P HELX_P20 AC2 SER B 116 ? ASN B 133 ? SER B 272 ASN B 289 1 ? 18 
HELX_P HELX_P21 AC3 PRO B 175 ? GLN B 179 ? PRO B 331 GLN B 335 5 ? 5  
HELX_P HELX_P22 AC4 SER B 189 ? LEU B 198 ? SER B 345 LEU B 354 1 ? 10 
HELX_P HELX_P23 AC5 PHE B 223 ? ASN B 233 ? PHE B 379 ASN B 389 1 ? 11 
HELX_P HELX_P24 AC6 ASN B 243 ? LYS B 247 ? ASN B 399 LYS B 403 5 ? 5  
HELX_P HELX_P25 AC7 CYS B 249 ? PHE B 268 ? CYS B 405 PHE B 424 1 ? 20 
HELX_P HELX_P26 AC8 SER B 278 ? ASN B 293 ? SER B 434 ASN B 449 1 ? 16 
HELX_P HELX_P27 AC9 GLN B 295 ? TRP B 299 ? GLN B 451 TRP B 455 5 ? 5  
HELX_P HELX_P28 AD1 ASP B 300 ? LYS B 302 ? ASP B 456 LYS B 458 5 ? 3  
HELX_P HELX_P29 AD2 ASP B 303 ? GLU B 322 ? ASP B 459 GLU B 478 1 ? 20 
HELX_P HELX_P30 AD3 ASP B 341 ? ASN B 358 ? ASP B 497 ASN B 514 1 ? 18 
HELX_P HELX_P31 AD4 GLU B 359 ? ASP B 364 ? GLU B 515 ASP B 520 5 ? 6  
# 
_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 
metalc1 metalc ? ? A HIS 234 NE2 ? ? ? 1_555 D ZN . ZN ? ? A HIS 390 A ZN 602 1_555 ? ? ? ? ? ? ? 2.106 ? ? 
metalc2 metalc ? ? A CYS 240 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 396 A ZN 602 1_555 ? ? ? ? ? ? ? 2.325 ? ? 
metalc3 metalc ? ? A CYS 241 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 397 A ZN 602 1_555 ? ? ? ? ? ? ? 2.308 ? ? 
metalc4 metalc ? ? A CYS 248 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 404 A ZN 602 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc5 metalc ? ? B HIS 234 NE2 ? ? ? 1_555 F ZN . ZN ? ? B HIS 390 B ZN 602 1_555 ? ? ? ? ? ? ? 2.110 ? ? 
metalc6 metalc ? ? B CYS 240 SG  ? ? ? 1_555 F ZN . ZN ? ? B CYS 396 B ZN 602 1_555 ? ? ? ? ? ? ? 2.325 ? ? 
metalc7 metalc ? ? B CYS 241 SG  ? ? ? 1_555 F ZN . ZN ? ? B CYS 397 B ZN 602 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
metalc8 metalc ? ? B CYS 248 SG  ? ? ? 1_555 F ZN . ZN ? ? B CYS 404 B ZN 602 1_555 ? ? ? ? ? ? ? 2.324 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 234 ? A HIS 390 ? 1_555 ZN ? D ZN . ? A ZN 602 ? 1_555 SG ? A CYS 240 ? A CYS 396 ? 1_555 112.3 ? 
2  NE2 ? A HIS 234 ? A HIS 390 ? 1_555 ZN ? D ZN . ? A ZN 602 ? 1_555 SG ? A CYS 241 ? A CYS 397 ? 1_555 110.2 ? 
3  SG  ? A CYS 240 ? A CYS 396 ? 1_555 ZN ? D ZN . ? A ZN 602 ? 1_555 SG ? A CYS 241 ? A CYS 397 ? 1_555 118.1 ? 
4  NE2 ? A HIS 234 ? A HIS 390 ? 1_555 ZN ? D ZN . ? A ZN 602 ? 1_555 SG ? A CYS 248 ? A CYS 404 ? 1_555 98.0  ? 
5  SG  ? A CYS 240 ? A CYS 396 ? 1_555 ZN ? D ZN . ? A ZN 602 ? 1_555 SG ? A CYS 248 ? A CYS 404 ? 1_555 108.7 ? 
6  SG  ? A CYS 241 ? A CYS 397 ? 1_555 ZN ? D ZN . ? A ZN 602 ? 1_555 SG ? A CYS 248 ? A CYS 404 ? 1_555 107.6 ? 
7  NE2 ? B HIS 234 ? B HIS 390 ? 1_555 ZN ? F ZN . ? B ZN 602 ? 1_555 SG ? B CYS 240 ? B CYS 396 ? 1_555 115.3 ? 
8  NE2 ? B HIS 234 ? B HIS 390 ? 1_555 ZN ? F ZN . ? B ZN 602 ? 1_555 SG ? B CYS 241 ? B CYS 397 ? 1_555 104.1 ? 
9  SG  ? B CYS 240 ? B CYS 396 ? 1_555 ZN ? F ZN . ? B ZN 602 ? 1_555 SG ? B CYS 241 ? B CYS 397 ? 1_555 118.8 ? 
10 NE2 ? B HIS 234 ? B HIS 390 ? 1_555 ZN ? F ZN . ? B ZN 602 ? 1_555 SG ? B CYS 248 ? B CYS 404 ? 1_555 101.1 ? 
11 SG  ? B CYS 240 ? B CYS 396 ? 1_555 ZN ? F ZN . ? B ZN 602 ? 1_555 SG ? B CYS 248 ? B CYS 404 ? 1_555 106.1 ? 
12 SG  ? B CYS 241 ? B CYS 397 ? 1_555 ZN ? F ZN . ? B ZN 602 ? 1_555 SG ? B CYS 248 ? B CYS 404 ? 1_555 110.1 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 7 ? 
AA5 ? 5 ? 
AA6 ? 2 ? 
# 
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 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? 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 GLY A 51  ? LEU A 52  ? GLY A 207 LEU A 208 
AA1 2 GLU A 69  ? GLU A 77  ? GLU A 225 GLU A 233 
AA1 3 ILE A 160 ? SER A 170 ? ILE A 316 SER A 326 
AA1 4 PHE A 201 ? PRO A 205 ? PHE A 357 PRO A 361 
AA1 5 TRP A 219 ? SER A 222 ? TRP A 375 SER A 378 
AA1 6 TYR A 92  ? PHE A 97  ? TYR A 248 PHE A 253 
AA1 7 ILE A 81  ? GLU A 85  ? ILE A 237 GLU A 241 
AA2 1 GLY A 51  ? LEU A 52  ? GLY A 207 LEU A 208 
AA2 2 GLU A 69  ? GLU A 77  ? GLU A 225 GLU A 233 
AA2 3 ILE A 160 ? SER A 170 ? ILE A 316 SER A 326 
AA2 4 VAL A 152 ? ILE A 156 ? VAL A 308 ILE A 312 
AA3 1 LEU A 110 ? GLU A 111 ? LEU A 266 GLU A 267 
AA3 2 ILE A 114 ? LEU A 115 ? ILE A 270 LEU A 271 
AA4 1 GLY B 51  ? LEU B 52  ? GLY B 207 LEU B 208 
AA4 2 GLU B 69  ? GLU B 77  ? GLU B 225 GLU B 233 
AA4 3 SER B 161 ? SER B 170 ? SER B 317 SER B 326 
AA4 4 PHE B 201 ? PRO B 205 ? PHE B 357 PRO B 361 
AA4 5 TRP B 219 ? SER B 222 ? TRP B 375 SER B 378 
AA4 6 TYR B 92  ? PHE B 97  ? TYR B 248 PHE B 253 
AA4 7 ILE B 81  ? GLU B 85  ? ILE B 237 GLU B 241 
AA5 1 GLY B 51  ? LEU B 52  ? GLY B 207 LEU B 208 
AA5 2 GLU B 69  ? GLU B 77  ? GLU B 225 GLU B 233 
AA5 3 SER B 161 ? SER B 170 ? SER B 317 SER B 326 
AA5 4 VAL B 152 ? LEU B 155 ? VAL B 308 LEU B 311 
AA5 5 ILE B 141 ? LYS B 143 ? ILE B 297 LYS B 299 
AA6 1 LEU B 110 ? GLU B 111 ? LEU B 266 GLU B 267 
AA6 2 ILE B 114 ? LEU B 115 ? ILE B 270 LEU B 271 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLY A 51  ? N GLY A 207 O LYS A 75  ? O LYS A 231 
AA1 2 3 N PHE A 70  ? N PHE A 226 O SER A 161 ? O SER A 317 
AA1 3 4 N LEU A 168 ? N LEU A 324 O LEU A 203 ? O LEU A 359 
AA1 4 5 N VAL A 204 ? N VAL A 360 O ARG A 220 ? O ARG A 376 
AA1 5 6 O TRP A 219 ? O TRP A 375 N TYR A 93  ? N TYR A 249 
AA1 6 7 O LYS A 96  ? O LYS A 252 N GLN A 82  ? N GLN A 238 
AA2 1 2 N GLY A 51  ? N GLY A 207 O LYS A 75  ? O LYS A 231 
AA2 2 3 N PHE A 70  ? N PHE A 226 O SER A 161 ? O SER A 317 
AA2 3 4 O ILE A 164 ? O ILE A 320 N VAL A 152 ? N VAL A 308 
AA3 1 2 N GLU A 111 ? N GLU A 267 O ILE A 114 ? O ILE A 270 
AA4 1 2 N GLY B 51  ? N GLY B 207 O LYS B 75  ? O LYS B 231 
AA4 2 3 N PHE B 70  ? N PHE B 226 O SER B 161 ? O SER B 317 
AA4 3 4 N LEU B 168 ? N LEU B 324 O LEU B 203 ? O LEU B 359 
AA4 4 5 N VAL B 204 ? N VAL B 360 O ARG B 220 ? O ARG B 376 
AA4 5 6 O TRP B 219 ? O TRP B 375 N TYR B 93  ? N TYR B 249 
AA4 6 7 O PHE B 94  ? O PHE B 250 N GLU B 84  ? N GLU B 240 
AA5 1 2 N GLY B 51  ? N GLY B 207 O LYS B 75  ? O LYS B 231 
AA5 2 3 N PHE B 70  ? N PHE B 226 O SER B 161 ? O SER B 317 
AA5 3 4 O ILE B 164 ? O ILE B 320 N VAL B 152 ? N VAL B 308 
AA5 4 5 O LEU B 155 ? O LEU B 311 N ILE B 141 ? N ILE B 297 
AA6 1 2 N GLU B 111 ? N GLU B 267 O ILE B 114 ? O ILE B 270 
# 
_pdbx_entry_details.entry_id                   9J2W 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 222 ? ? -118.72 78.55   
2 1 ARG A 246 ? ? 71.12   -22.92  
3 1 SER A 345 ? ? 105.15  154.67  
4 1 SER B 243 ? ? 41.21   -128.30 
5 1 ARG B 246 ? ? 63.89   -15.99  
6 1 SER B 313 ? ? 49.97   -125.85 
7 1 TRP B 343 ? ? -109.49 -65.48  
8 1 SER B 345 ? ? 97.63   158.18  
# 
_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         31.1892 
_pdbx_refine_tls.origin_y         17.7724 
_pdbx_refine_tls.origin_z         -0.4669 
_pdbx_refine_tls.T[1][1]          0.1621 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0136 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0148 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.2225 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0406 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.2959 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.6831 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.2121 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.2582 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.9188 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.6576 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.8590 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0065 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.1039 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0692 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0113 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.1648 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.3263 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0128 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.4596 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.1255 
_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 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ASP 157 ? A ASP 1   
2  1 Y 1 A ALA 158 ? A ALA 2   
3  1 Y 1 A ALA 159 ? A ALA 3   
4  1 Y 1 A PRO 160 ? A PRO 4   
5  1 Y 1 A ARG 176 ? A ARG 20  
6  1 Y 1 A ASP 177 ? A ASP 21  
7  1 Y 1 A ASP 178 ? A ASP 22  
8  1 Y 1 A ASN 210 ? A ASN 54  
9  1 Y 1 A THR 211 ? A THR 55  
10 1 Y 1 A GLY 212 ? A GLY 56  
11 1 Y 1 A SER 213 ? A SER 57  
12 1 Y 1 A TYR 214 ? A TYR 58  
13 1 Y 1 A ARG 255 ? A ARG 99  
14 1 Y 1 A ASN 256 ? A ASN 100 
15 1 Y 1 A PRO 257 ? A PRO 101 
16 1 Y 1 A LYS 258 ? A LYS 102 
17 1 Y 1 A LYS 285 ? A LYS 129 
18 1 Y 1 A GLU 286 ? A GLU 130 
19 1 Y 1 A GLU 287 ? A GLU 131 
20 1 Y 1 A ILE 288 ? A ILE 132 
21 1 Y 1 A ASN 289 ? A ASN 133 
22 1 Y 1 A ASP 290 ? A ASP 134 
23 1 Y 1 A ILE 291 ? A ILE 135 
24 1 Y 1 A LYS 292 ? A LYS 136 
25 1 Y 1 A ASP 293 ? A ASP 137 
26 1 Y 1 A THR 294 ? A THR 138 
27 1 Y 1 A ASP 295 ? A ASP 139 
28 1 Y 1 A VAL 296 ? A VAL 140 
29 1 Y 1 A ILE 297 ? A ILE 141 
30 1 Y 1 A LYS 301 ? A LYS 145 
31 1 Y 1 A ARG 302 ? A ARG 146 
32 1 Y 1 A GLY 303 ? A GLY 147 
33 1 Y 1 A PRO 306 ? A PRO 150 
34 1 Y 1 A SER 313 ? A SER 157 
35 1 Y 1 A LYS 365 ? A LYS 209 
36 1 Y 1 A GLU 366 ? A GLU 210 
37 1 Y 1 A GLY 367 ? A GLY 211 
38 1 Y 1 A ASN 368 ? A ASN 212 
39 1 Y 1 A GLY 369 ? A GLY 213 
40 1 Y 1 A PHE 370 ? A PHE 214 
41 1 Y 1 A GLU 521 ? A GLU 365 
42 1 Y 1 A PHE 522 ? A PHE 366 
43 1 Y 1 B ASP 157 ? B ASP 1   
44 1 Y 1 B ALA 158 ? B ALA 2   
45 1 Y 1 B ALA 159 ? B ALA 3   
46 1 Y 1 B PRO 160 ? B PRO 4   
47 1 Y 1 B SER 175 ? B SER 19  
48 1 Y 1 B ARG 176 ? B ARG 20  
49 1 Y 1 B ASP 177 ? B ASP 21  
50 1 Y 1 B SER 180 ? B SER 24  
51 1 Y 1 B THR 211 ? B THR 55  
52 1 Y 1 B GLY 212 ? B GLY 56  
53 1 Y 1 B ARG 255 ? B ARG 99  
54 1 Y 1 B ASN 256 ? B ASN 100 
55 1 Y 1 B PRO 257 ? B PRO 101 
56 1 Y 1 B LYS 258 ? B LYS 102 
57 1 Y 1 B GLU 259 ? B GLU 103 
58 1 Y 1 B ILE 291 ? B ILE 135 
59 1 Y 1 B LYS 292 ? B LYS 136 
60 1 Y 1 B ASP 293 ? B ASP 137 
61 1 Y 1 B THR 294 ? B THR 138 
62 1 Y 1 B ASP 295 ? B ASP 139 
63 1 Y 1 B LYS 301 ? B LYS 145 
64 1 Y 1 B ARG 302 ? B ARG 146 
65 1 Y 1 B GLY 303 ? B GLY 147 
66 1 Y 1 B LYS 315 ? B LYS 159 
67 1 Y 1 B GLU 366 ? B GLU 210 
68 1 Y 1 B GLY 367 ? B GLY 211 
69 1 Y 1 B ASN 368 ? B ASN 212 
70 1 Y 1 B GLY 369 ? B GLY 213 
71 1 Y 1 B PHE 370 ? B PHE 214 
72 1 Y 1 B GLU 521 ? B GLU 365 
73 1 Y 1 B PHE 522 ? B PHE 366 
# 
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 
A1EAH C4   C  Y N 1   
A1EAH C14  C  Y N 2   
A1EAH C5   C  Y N 3   
A1EAH C6   C  Y N 4   
A1EAH C11  C  N N 5   
A1EAH C7   C  Y N 6   
A1EAH C8   C  Y N 7   
A1EAH C9   C  Y N 8   
A1EAH C10  C  Y N 9   
A1EAH C12  C  Y N 10  
A1EAH C13  C  Y N 11  
A1EAH N1   N  Y N 12  
A1EAH N2   N  Y N 13  
A1EAH C3   C  Y N 14  
A1EAH N3   N  Y N 15  
A1EAH C1   C  Y N 16  
A1EAH C15  C  Y N 17  
A1EAH C16  C  Y N 18  
A1EAH C17  C  Y N 19  
A1EAH C18  C  Y N 20  
A1EAH C19  C  Y N 21  
A1EAH C2   C  Y N 22  
A1EAH C20  C  Y N 23  
A1EAH C21  C  Y N 24  
A1EAH C22  C  Y N 25  
A1EAH C23  C  Y N 26  
A1EAH C24  C  Y N 27  
A1EAH C25  C  Y N 28  
A1EAH C26  C  Y N 29  
A1EAH C27  C  N N 30  
A1EAH C28  C  N N 31  
A1EAH N4   N  Y N 32  
A1EAH N5   N  Y N 33  
A1EAH N6   N  Y N 34  
A1EAH N7   N  Y N 35  
A1EAH N8   N  Y N 36  
A1EAH N9   N  Y N 37  
A1EAH O1   O  N N 38  
A1EAH O2   O  N N 39  
A1EAH H1   H  N N 40  
A1EAH H2   H  N N 41  
A1EAH H5   H  N N 42  
A1EAH H7   H  N N 43  
A1EAH H8   H  N N 44  
A1EAH H9   H  N N 45  
A1EAH H10  H  N N 46  
A1EAH H11  H  N N 47  
A1EAH H12  H  N N 48  
A1EAH H13  H  N N 49  
A1EAH H14  H  N N 50  
A1EAH H15  H  N N 51  
A1EAH H16  H  N N 52  
A1EAH H17  H  N N 53  
A1EAH H18  H  N N 54  
A1EAH H19  H  N N 55  
A1EAH H20  H  N N 56  
A1EAH H21  H  N N 57  
A1EAH H22  H  N N 58  
A1EAH H23  H  N N 59  
A1EAH H24  H  N N 60  
A1EAH H3   H  N N 61  
A1EAH H4   H  N N 62  
ALA   N    N  N N 63  
ALA   CA   C  N S 64  
ALA   C    C  N N 65  
ALA   O    O  N N 66  
ALA   CB   C  N N 67  
ALA   OXT  O  N N 68  
ALA   H    H  N N 69  
ALA   H2   H  N N 70  
ALA   HA   H  N N 71  
ALA   HB1  H  N N 72  
ALA   HB2  H  N N 73  
ALA   HB3  H  N N 74  
ALA   HXT  H  N N 75  
ARG   N    N  N N 76  
ARG   CA   C  N S 77  
ARG   C    C  N N 78  
ARG   O    O  N N 79  
ARG   CB   C  N N 80  
ARG   CG   C  N N 81  
ARG   CD   C  N N 82  
ARG   NE   N  N N 83  
ARG   CZ   C  N N 84  
ARG   NH1  N  N N 85  
ARG   NH2  N  N N 86  
ARG   OXT  O  N N 87  
ARG   H    H  N N 88  
ARG   H2   H  N N 89  
ARG   HA   H  N N 90  
ARG   HB2  H  N N 91  
ARG   HB3  H  N N 92  
ARG   HG2  H  N N 93  
ARG   HG3  H  N N 94  
ARG   HD2  H  N N 95  
ARG   HD3  H  N N 96  
ARG   HE   H  N N 97  
ARG   HH11 H  N N 98  
ARG   HH12 H  N N 99  
ARG   HH21 H  N N 100 
ARG   HH22 H  N N 101 
ARG   HXT  H  N N 102 
ASN   N    N  N N 103 
ASN   CA   C  N S 104 
ASN   C    C  N N 105 
ASN   O    O  N N 106 
ASN   CB   C  N N 107 
ASN   CG   C  N N 108 
ASN   OD1  O  N N 109 
ASN   ND2  N  N N 110 
ASN   OXT  O  N N 111 
ASN   H    H  N N 112 
ASN   H2   H  N N 113 
ASN   HA   H  N N 114 
ASN   HB2  H  N N 115 
ASN   HB3  H  N N 116 
ASN   HD21 H  N N 117 
ASN   HD22 H  N N 118 
ASN   HXT  H  N N 119 
ASP   N    N  N N 120 
ASP   CA   C  N S 121 
ASP   C    C  N N 122 
ASP   O    O  N N 123 
ASP   CB   C  N N 124 
ASP   CG   C  N N 125 
ASP   OD1  O  N N 126 
ASP   OD2  O  N N 127 
ASP   OXT  O  N N 128 
ASP   H    H  N N 129 
ASP   H2   H  N N 130 
ASP   HA   H  N N 131 
ASP   HB2  H  N N 132 
ASP   HB3  H  N N 133 
ASP   HD2  H  N N 134 
ASP   HXT  H  N N 135 
CYS   N    N  N N 136 
CYS   CA   C  N R 137 
CYS   C    C  N N 138 
CYS   O    O  N N 139 
CYS   CB   C  N N 140 
CYS   SG   S  N N 141 
CYS   OXT  O  N N 142 
CYS   H    H  N N 143 
CYS   H2   H  N N 144 
CYS   HA   H  N N 145 
CYS   HB2  H  N N 146 
CYS   HB3  H  N N 147 
CYS   HG   H  N N 148 
CYS   HXT  H  N N 149 
GLN   N    N  N N 150 
GLN   CA   C  N S 151 
GLN   C    C  N N 152 
GLN   O    O  N N 153 
GLN   CB   C  N N 154 
GLN   CG   C  N N 155 
GLN   CD   C  N N 156 
GLN   OE1  O  N N 157 
GLN   NE2  N  N N 158 
GLN   OXT  O  N N 159 
GLN   H    H  N N 160 
GLN   H2   H  N N 161 
GLN   HA   H  N N 162 
GLN   HB2  H  N N 163 
GLN   HB3  H  N N 164 
GLN   HG2  H  N N 165 
GLN   HG3  H  N N 166 
GLN   HE21 H  N N 167 
GLN   HE22 H  N N 168 
GLN   HXT  H  N N 169 
GLU   N    N  N N 170 
GLU   CA   C  N S 171 
GLU   C    C  N N 172 
GLU   O    O  N N 173 
GLU   CB   C  N N 174 
GLU   CG   C  N N 175 
GLU   CD   C  N N 176 
GLU   OE1  O  N N 177 
GLU   OE2  O  N N 178 
GLU   OXT  O  N N 179 
GLU   H    H  N N 180 
GLU   H2   H  N N 181 
GLU   HA   H  N N 182 
GLU   HB2  H  N N 183 
GLU   HB3  H  N N 184 
GLU   HG2  H  N N 185 
GLU   HG3  H  N N 186 
GLU   HE2  H  N N 187 
GLU   HXT  H  N N 188 
GLY   N    N  N N 189 
GLY   CA   C  N N 190 
GLY   C    C  N N 191 
GLY   O    O  N N 192 
GLY   OXT  O  N N 193 
GLY   H    H  N N 194 
GLY   H2   H  N N 195 
GLY   HA2  H  N N 196 
GLY   HA3  H  N N 197 
GLY   HXT  H  N N 198 
HIS   N    N  N N 199 
HIS   CA   C  N S 200 
HIS   C    C  N N 201 
HIS   O    O  N N 202 
HIS   CB   C  N N 203 
HIS   CG   C  Y N 204 
HIS   ND1  N  Y N 205 
HIS   CD2  C  Y N 206 
HIS   CE1  C  Y N 207 
HIS   NE2  N  Y N 208 
HIS   OXT  O  N N 209 
HIS   H    H  N N 210 
HIS   H2   H  N N 211 
HIS   HA   H  N N 212 
HIS   HB2  H  N N 213 
HIS   HB3  H  N N 214 
HIS   HD1  H  N N 215 
HIS   HD2  H  N N 216 
HIS   HE1  H  N N 217 
HIS   HE2  H  N N 218 
HIS   HXT  H  N N 219 
HOH   O    O  N N 220 
HOH   H1   H  N N 221 
HOH   H2   H  N N 222 
ILE   N    N  N N 223 
ILE   CA   C  N S 224 
ILE   C    C  N N 225 
ILE   O    O  N N 226 
ILE   CB   C  N S 227 
ILE   CG1  C  N N 228 
ILE   CG2  C  N N 229 
ILE   CD1  C  N N 230 
ILE   OXT  O  N N 231 
ILE   H    H  N N 232 
ILE   H2   H  N N 233 
ILE   HA   H  N N 234 
ILE   HB   H  N N 235 
ILE   HG12 H  N N 236 
ILE   HG13 H  N N 237 
ILE   HG21 H  N N 238 
ILE   HG22 H  N N 239 
ILE   HG23 H  N N 240 
ILE   HD11 H  N N 241 
ILE   HD12 H  N N 242 
ILE   HD13 H  N N 243 
ILE   HXT  H  N N 244 
LEU   N    N  N N 245 
LEU   CA   C  N S 246 
LEU   C    C  N N 247 
LEU   O    O  N N 248 
LEU   CB   C  N N 249 
LEU   CG   C  N N 250 
LEU   CD1  C  N N 251 
LEU   CD2  C  N N 252 
LEU   OXT  O  N N 253 
LEU   H    H  N N 254 
LEU   H2   H  N N 255 
LEU   HA   H  N N 256 
LEU   HB2  H  N N 257 
LEU   HB3  H  N N 258 
LEU   HG   H  N N 259 
LEU   HD11 H  N N 260 
LEU   HD12 H  N N 261 
LEU   HD13 H  N N 262 
LEU   HD21 H  N N 263 
LEU   HD22 H  N N 264 
LEU   HD23 H  N N 265 
LEU   HXT  H  N N 266 
LYS   N    N  N N 267 
LYS   CA   C  N S 268 
LYS   C    C  N N 269 
LYS   O    O  N N 270 
LYS   CB   C  N N 271 
LYS   CG   C  N N 272 
LYS   CD   C  N N 273 
LYS   CE   C  N N 274 
LYS   NZ   N  N N 275 
LYS   OXT  O  N N 276 
LYS   H    H  N N 277 
LYS   H2   H  N N 278 
LYS   HA   H  N N 279 
LYS   HB2  H  N N 280 
LYS   HB3  H  N N 281 
LYS   HG2  H  N N 282 
LYS   HG3  H  N N 283 
LYS   HD2  H  N N 284 
LYS   HD3  H  N N 285 
LYS   HE2  H  N N 286 
LYS   HE3  H  N N 287 
LYS   HZ1  H  N N 288 
LYS   HZ2  H  N N 289 
LYS   HZ3  H  N N 290 
LYS   HXT  H  N N 291 
MET   N    N  N N 292 
MET   CA   C  N S 293 
MET   C    C  N N 294 
MET   O    O  N N 295 
MET   CB   C  N N 296 
MET   CG   C  N N 297 
MET   SD   S  N N 298 
MET   CE   C  N N 299 
MET   OXT  O  N N 300 
MET   H    H  N N 301 
MET   H2   H  N N 302 
MET   HA   H  N N 303 
MET   HB2  H  N N 304 
MET   HB3  H  N N 305 
MET   HG2  H  N N 306 
MET   HG3  H  N N 307 
MET   HE1  H  N N 308 
MET   HE2  H  N N 309 
MET   HE3  H  N N 310 
MET   HXT  H  N N 311 
PHE   N    N  N N 312 
PHE   CA   C  N S 313 
PHE   C    C  N N 314 
PHE   O    O  N N 315 
PHE   CB   C  N N 316 
PHE   CG   C  Y N 317 
PHE   CD1  C  Y N 318 
PHE   CD2  C  Y N 319 
PHE   CE1  C  Y N 320 
PHE   CE2  C  Y N 321 
PHE   CZ   C  Y N 322 
PHE   OXT  O  N N 323 
PHE   H    H  N N 324 
PHE   H2   H  N N 325 
PHE   HA   H  N N 326 
PHE   HB2  H  N N 327 
PHE   HB3  H  N N 328 
PHE   HD1  H  N N 329 
PHE   HD2  H  N N 330 
PHE   HE1  H  N N 331 
PHE   HE2  H  N N 332 
PHE   HZ   H  N N 333 
PHE   HXT  H  N N 334 
PRO   N    N  N N 335 
PRO   CA   C  N S 336 
PRO   C    C  N N 337 
PRO   O    O  N N 338 
PRO   CB   C  N N 339 
PRO   CG   C  N N 340 
PRO   CD   C  N N 341 
PRO   OXT  O  N N 342 
PRO   H    H  N N 343 
PRO   HA   H  N N 344 
PRO   HB2  H  N N 345 
PRO   HB3  H  N N 346 
PRO   HG2  H  N N 347 
PRO   HG3  H  N N 348 
PRO   HD2  H  N N 349 
PRO   HD3  H  N N 350 
PRO   HXT  H  N N 351 
SER   N    N  N N 352 
SER   CA   C  N S 353 
SER   C    C  N N 354 
SER   O    O  N N 355 
SER   CB   C  N N 356 
SER   OG   O  N N 357 
SER   OXT  O  N N 358 
SER   H    H  N N 359 
SER   H2   H  N N 360 
SER   HA   H  N N 361 
SER   HB2  H  N N 362 
SER   HB3  H  N N 363 
SER   HG   H  N N 364 
SER   HXT  H  N N 365 
THR   N    N  N N 366 
THR   CA   C  N S 367 
THR   C    C  N N 368 
THR   O    O  N N 369 
THR   CB   C  N R 370 
THR   OG1  O  N N 371 
THR   CG2  C  N N 372 
THR   OXT  O  N N 373 
THR   H    H  N N 374 
THR   H2   H  N N 375 
THR   HA   H  N N 376 
THR   HB   H  N N 377 
THR   HG1  H  N N 378 
THR   HG21 H  N N 379 
THR   HG22 H  N N 380 
THR   HG23 H  N N 381 
THR   HXT  H  N N 382 
TRP   N    N  N N 383 
TRP   CA   C  N S 384 
TRP   C    C  N N 385 
TRP   O    O  N N 386 
TRP   CB   C  N N 387 
TRP   CG   C  Y N 388 
TRP   CD1  C  Y N 389 
TRP   CD2  C  Y N 390 
TRP   NE1  N  Y N 391 
TRP   CE2  C  Y N 392 
TRP   CE3  C  Y N 393 
TRP   CZ2  C  Y N 394 
TRP   CZ3  C  Y N 395 
TRP   CH2  C  Y N 396 
TRP   OXT  O  N N 397 
TRP   H    H  N N 398 
TRP   H2   H  N N 399 
TRP   HA   H  N N 400 
TRP   HB2  H  N N 401 
TRP   HB3  H  N N 402 
TRP   HD1  H  N N 403 
TRP   HE1  H  N N 404 
TRP   HE3  H  N N 405 
TRP   HZ2  H  N N 406 
TRP   HZ3  H  N N 407 
TRP   HH2  H  N N 408 
TRP   HXT  H  N N 409 
TYR   N    N  N N 410 
TYR   CA   C  N S 411 
TYR   C    C  N N 412 
TYR   O    O  N N 413 
TYR   CB   C  N N 414 
TYR   CG   C  Y N 415 
TYR   CD1  C  Y N 416 
TYR   CD2  C  Y N 417 
TYR   CE1  C  Y N 418 
TYR   CE2  C  Y N 419 
TYR   CZ   C  Y N 420 
TYR   OH   O  N N 421 
TYR   OXT  O  N N 422 
TYR   H    H  N N 423 
TYR   H2   H  N N 424 
TYR   HA   H  N N 425 
TYR   HB2  H  N N 426 
TYR   HB3  H  N N 427 
TYR   HD1  H  N N 428 
TYR   HD2  H  N N 429 
TYR   HE1  H  N N 430 
TYR   HE2  H  N N 431 
TYR   HH   H  N N 432 
TYR   HXT  H  N N 433 
VAL   N    N  N N 434 
VAL   CA   C  N S 435 
VAL   C    C  N N 436 
VAL   O    O  N N 437 
VAL   CB   C  N N 438 
VAL   CG1  C  N N 439 
VAL   CG2  C  N N 440 
VAL   OXT  O  N N 441 
VAL   H    H  N N 442 
VAL   H2   H  N N 443 
VAL   HA   H  N N 444 
VAL   HB   H  N N 445 
VAL   HG11 H  N N 446 
VAL   HG12 H  N N 447 
VAL   HG13 H  N N 448 
VAL   HG21 H  N N 449 
VAL   HG22 H  N N 450 
VAL   HG23 H  N N 451 
VAL   HXT  H  N N 452 
ZN    ZN   ZN N N 453 
# 
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 
A1EAH C20 C19  doub Y N 1   
A1EAH C20 C21  sing Y N 2   
A1EAH C19 C17  sing Y N 3   
A1EAH C21 C22  doub Y N 4   
A1EAH C17 C18  doub Y N 5   
A1EAH C17 N7   sing Y N 6   
A1EAH C22 C18  sing Y N 7   
A1EAH C18 N8   sing Y N 8   
A1EAH N7  C16  sing Y N 9   
A1EAH O2  C15  sing N N 10  
A1EAH C16 N8   doub Y N 11  
A1EAH C16 N6   sing N N 12  
A1EAH C27 C8   sing N N 13  
A1EAH C15 N6   sing Y N 14  
A1EAH C15 C12  doub Y N 15  
A1EAH N6  N5   sing Y N 16  
A1EAH C12 C11  sing N N 17  
A1EAH C12 C14  sing Y N 18  
A1EAH N5  C14  doub Y N 19  
A1EAH C8  N4   doub Y N 20  
A1EAH C8  C9   sing Y N 21  
A1EAH C11 C13  sing N N 22  
A1EAH C11 C9   sing N N 23  
A1EAH C13 N9   doub Y N 24  
A1EAH C13 C26  sing Y N 25  
A1EAH C14 C28  sing N N 26  
A1EAH N4  N3   sing Y N 27  
A1EAH N9  C23  sing Y N 28  
A1EAH C9  C10  doub Y N 29  
A1EAH C26 C25  doub Y N 30  
A1EAH C23 C24  doub Y N 31  
A1EAH C25 C24  sing Y N 32  
A1EAH N3  C10  sing Y N 33  
A1EAH N3  C7   sing N N 34  
A1EAH C10 O1   sing N N 35  
A1EAH N2  C7   doub Y N 36  
A1EAH N2  C6   sing Y N 37  
A1EAH C7  N1   sing Y N 38  
A1EAH C6  C1   doub Y N 39  
A1EAH C6  C5   sing Y N 40  
A1EAH C1  C2   sing Y N 41  
A1EAH N1  C5   sing Y N 42  
A1EAH C5  C4   doub Y N 43  
A1EAH C2  C3   doub Y N 44  
A1EAH C4  C3   sing Y N 45  
A1EAH C4  H1   sing N N 46  
A1EAH C11 H2   sing N N 47  
A1EAH N1  H5   sing N N 48  
A1EAH C3  H7   sing N N 49  
A1EAH C1  H8   sing N N 50  
A1EAH C19 H9   sing N N 51  
A1EAH C2  H10  sing N N 52  
A1EAH C20 H11  sing N N 53  
A1EAH C21 H12  sing N N 54  
A1EAH C22 H13  sing N N 55  
A1EAH C23 H14  sing N N 56  
A1EAH C24 H15  sing N N 57  
A1EAH C25 H16  sing N N 58  
A1EAH C26 H17  sing N N 59  
A1EAH C27 H18  sing N N 60  
A1EAH C27 H19  sing N N 61  
A1EAH C27 H20  sing N N 62  
A1EAH C28 H21  sing N N 63  
A1EAH C28 H22  sing N N 64  
A1EAH C28 H23  sing N N 65  
A1EAH N7  H24  sing N N 66  
A1EAH O1  H3   sing N N 67  
A1EAH O2  H4   sing N N 68  
ALA   N   CA   sing N N 69  
ALA   N   H    sing N N 70  
ALA   N   H2   sing N N 71  
ALA   CA  C    sing N N 72  
ALA   CA  CB   sing N N 73  
ALA   CA  HA   sing N N 74  
ALA   C   O    doub N N 75  
ALA   C   OXT  sing N N 76  
ALA   CB  HB1  sing N N 77  
ALA   CB  HB2  sing N N 78  
ALA   CB  HB3  sing N N 79  
ALA   OXT HXT  sing N N 80  
ARG   N   CA   sing N N 81  
ARG   N   H    sing N N 82  
ARG   N   H2   sing N N 83  
ARG   CA  C    sing N N 84  
ARG   CA  CB   sing N N 85  
ARG   CA  HA   sing N N 86  
ARG   C   O    doub N N 87  
ARG   C   OXT  sing N N 88  
ARG   CB  CG   sing N N 89  
ARG   CB  HB2  sing N N 90  
ARG   CB  HB3  sing N N 91  
ARG   CG  CD   sing N N 92  
ARG   CG  HG2  sing N N 93  
ARG   CG  HG3  sing N N 94  
ARG   CD  NE   sing N N 95  
ARG   CD  HD2  sing N N 96  
ARG   CD  HD3  sing N N 97  
ARG   NE  CZ   sing N N 98  
ARG   NE  HE   sing N N 99  
ARG   CZ  NH1  sing N N 100 
ARG   CZ  NH2  doub N N 101 
ARG   NH1 HH11 sing N N 102 
ARG   NH1 HH12 sing N N 103 
ARG   NH2 HH21 sing N N 104 
ARG   NH2 HH22 sing N N 105 
ARG   OXT HXT  sing N N 106 
ASN   N   CA   sing N N 107 
ASN   N   H    sing N N 108 
ASN   N   H2   sing N N 109 
ASN   CA  C    sing N N 110 
ASN   CA  CB   sing N N 111 
ASN   CA  HA   sing N N 112 
ASN   C   O    doub N N 113 
ASN   C   OXT  sing N N 114 
ASN   CB  CG   sing N N 115 
ASN   CB  HB2  sing N N 116 
ASN   CB  HB3  sing N N 117 
ASN   CG  OD1  doub N N 118 
ASN   CG  ND2  sing N N 119 
ASN   ND2 HD21 sing N N 120 
ASN   ND2 HD22 sing N N 121 
ASN   OXT HXT  sing N N 122 
ASP   N   CA   sing N N 123 
ASP   N   H    sing N N 124 
ASP   N   H2   sing N N 125 
ASP   CA  C    sing N N 126 
ASP   CA  CB   sing N N 127 
ASP   CA  HA   sing N N 128 
ASP   C   O    doub N N 129 
ASP   C   OXT  sing N N 130 
ASP   CB  CG   sing N N 131 
ASP   CB  HB2  sing N N 132 
ASP   CB  HB3  sing N N 133 
ASP   CG  OD1  doub N N 134 
ASP   CG  OD2  sing N N 135 
ASP   OD2 HD2  sing N N 136 
ASP   OXT HXT  sing N N 137 
CYS   N   CA   sing N N 138 
CYS   N   H    sing N N 139 
CYS   N   H2   sing N N 140 
CYS   CA  C    sing N N 141 
CYS   CA  CB   sing N N 142 
CYS   CA  HA   sing N N 143 
CYS   C   O    doub N N 144 
CYS   C   OXT  sing N N 145 
CYS   CB  SG   sing N N 146 
CYS   CB  HB2  sing N N 147 
CYS   CB  HB3  sing N N 148 
CYS   SG  HG   sing N N 149 
CYS   OXT HXT  sing N N 150 
GLN   N   CA   sing N N 151 
GLN   N   H    sing N N 152 
GLN   N   H2   sing N N 153 
GLN   CA  C    sing N N 154 
GLN   CA  CB   sing N N 155 
GLN   CA  HA   sing N N 156 
GLN   C   O    doub N N 157 
GLN   C   OXT  sing N N 158 
GLN   CB  CG   sing N N 159 
GLN   CB  HB2  sing N N 160 
GLN   CB  HB3  sing N N 161 
GLN   CG  CD   sing N N 162 
GLN   CG  HG2  sing N N 163 
GLN   CG  HG3  sing N N 164 
GLN   CD  OE1  doub N N 165 
GLN   CD  NE2  sing N N 166 
GLN   NE2 HE21 sing N N 167 
GLN   NE2 HE22 sing N N 168 
GLN   OXT HXT  sing N N 169 
GLU   N   CA   sing N N 170 
GLU   N   H    sing N N 171 
GLU   N   H2   sing N N 172 
GLU   CA  C    sing N N 173 
GLU   CA  CB   sing N N 174 
GLU   CA  HA   sing N N 175 
GLU   C   O    doub N N 176 
GLU   C   OXT  sing N N 177 
GLU   CB  CG   sing N N 178 
GLU   CB  HB2  sing N N 179 
GLU   CB  HB3  sing N N 180 
GLU   CG  CD   sing N N 181 
GLU   CG  HG2  sing N N 182 
GLU   CG  HG3  sing N N 183 
GLU   CD  OE1  doub N N 184 
GLU   CD  OE2  sing N N 185 
GLU   OE2 HE2  sing N N 186 
GLU   OXT HXT  sing N N 187 
GLY   N   CA   sing N N 188 
GLY   N   H    sing N N 189 
GLY   N   H2   sing N N 190 
GLY   CA  C    sing N N 191 
GLY   CA  HA2  sing N N 192 
GLY   CA  HA3  sing N N 193 
GLY   C   O    doub N N 194 
GLY   C   OXT  sing N N 195 
GLY   OXT HXT  sing N N 196 
HIS   N   CA   sing N N 197 
HIS   N   H    sing N N 198 
HIS   N   H2   sing N N 199 
HIS   CA  C    sing N N 200 
HIS   CA  CB   sing N N 201 
HIS   CA  HA   sing N N 202 
HIS   C   O    doub N N 203 
HIS   C   OXT  sing N N 204 
HIS   CB  CG   sing N N 205 
HIS   CB  HB2  sing N N 206 
HIS   CB  HB3  sing N N 207 
HIS   CG  ND1  sing Y N 208 
HIS   CG  CD2  doub Y N 209 
HIS   ND1 CE1  doub Y N 210 
HIS   ND1 HD1  sing N N 211 
HIS   CD2 NE2  sing Y N 212 
HIS   CD2 HD2  sing N N 213 
HIS   CE1 NE2  sing Y N 214 
HIS   CE1 HE1  sing N N 215 
HIS   NE2 HE2  sing N N 216 
HIS   OXT HXT  sing N N 217 
HOH   O   H1   sing N N 218 
HOH   O   H2   sing N N 219 
ILE   N   CA   sing N N 220 
ILE   N   H    sing N N 221 
ILE   N   H2   sing N N 222 
ILE   CA  C    sing N N 223 
ILE   CA  CB   sing N N 224 
ILE   CA  HA   sing N N 225 
ILE   C   O    doub N N 226 
ILE   C   OXT  sing N N 227 
ILE   CB  CG1  sing N N 228 
ILE   CB  CG2  sing N N 229 
ILE   CB  HB   sing N N 230 
ILE   CG1 CD1  sing N N 231 
ILE   CG1 HG12 sing N N 232 
ILE   CG1 HG13 sing N N 233 
ILE   CG2 HG21 sing N N 234 
ILE   CG2 HG22 sing N N 235 
ILE   CG2 HG23 sing N N 236 
ILE   CD1 HD11 sing N N 237 
ILE   CD1 HD12 sing N N 238 
ILE   CD1 HD13 sing N N 239 
ILE   OXT HXT  sing N N 240 
LEU   N   CA   sing N N 241 
LEU   N   H    sing N N 242 
LEU   N   H2   sing N N 243 
LEU   CA  C    sing N N 244 
LEU   CA  CB   sing N N 245 
LEU   CA  HA   sing N N 246 
LEU   C   O    doub N N 247 
LEU   C   OXT  sing N N 248 
LEU   CB  CG   sing N N 249 
LEU   CB  HB2  sing N N 250 
LEU   CB  HB3  sing N N 251 
LEU   CG  CD1  sing N N 252 
LEU   CG  CD2  sing N N 253 
LEU   CG  HG   sing N N 254 
LEU   CD1 HD11 sing N N 255 
LEU   CD1 HD12 sing N N 256 
LEU   CD1 HD13 sing N N 257 
LEU   CD2 HD21 sing N N 258 
LEU   CD2 HD22 sing N N 259 
LEU   CD2 HD23 sing N N 260 
LEU   OXT HXT  sing N N 261 
LYS   N   CA   sing N N 262 
LYS   N   H    sing N N 263 
LYS   N   H2   sing N N 264 
LYS   CA  C    sing N N 265 
LYS   CA  CB   sing N N 266 
LYS   CA  HA   sing N N 267 
LYS   C   O    doub N N 268 
LYS   C   OXT  sing N N 269 
LYS   CB  CG   sing N N 270 
LYS   CB  HB2  sing N N 271 
LYS   CB  HB3  sing N N 272 
LYS   CG  CD   sing N N 273 
LYS   CG  HG2  sing N N 274 
LYS   CG  HG3  sing N N 275 
LYS   CD  CE   sing N N 276 
LYS   CD  HD2  sing N N 277 
LYS   CD  HD3  sing N N 278 
LYS   CE  NZ   sing N N 279 
LYS   CE  HE2  sing N N 280 
LYS   CE  HE3  sing N N 281 
LYS   NZ  HZ1  sing N N 282 
LYS   NZ  HZ2  sing N N 283 
LYS   NZ  HZ3  sing N N 284 
LYS   OXT HXT  sing N N 285 
MET   N   CA   sing N N 286 
MET   N   H    sing N N 287 
MET   N   H2   sing N N 288 
MET   CA  C    sing N N 289 
MET   CA  CB   sing N N 290 
MET   CA  HA   sing N N 291 
MET   C   O    doub N N 292 
MET   C   OXT  sing N N 293 
MET   CB  CG   sing N N 294 
MET   CB  HB2  sing N N 295 
MET   CB  HB3  sing N N 296 
MET   CG  SD   sing N N 297 
MET   CG  HG2  sing N N 298 
MET   CG  HG3  sing N N 299 
MET   SD  CE   sing N N 300 
MET   CE  HE1  sing N N 301 
MET   CE  HE2  sing N N 302 
MET   CE  HE3  sing N N 303 
MET   OXT HXT  sing N N 304 
PHE   N   CA   sing N N 305 
PHE   N   H    sing N N 306 
PHE   N   H2   sing N N 307 
PHE   CA  C    sing N N 308 
PHE   CA  CB   sing N N 309 
PHE   CA  HA   sing N N 310 
PHE   C   O    doub N N 311 
PHE   C   OXT  sing N N 312 
PHE   CB  CG   sing N N 313 
PHE   CB  HB2  sing N N 314 
PHE   CB  HB3  sing N N 315 
PHE   CG  CD1  doub Y N 316 
PHE   CG  CD2  sing Y N 317 
PHE   CD1 CE1  sing Y N 318 
PHE   CD1 HD1  sing N N 319 
PHE   CD2 CE2  doub Y N 320 
PHE   CD2 HD2  sing N N 321 
PHE   CE1 CZ   doub Y N 322 
PHE   CE1 HE1  sing N N 323 
PHE   CE2 CZ   sing Y N 324 
PHE   CE2 HE2  sing N N 325 
PHE   CZ  HZ   sing N N 326 
PHE   OXT HXT  sing N N 327 
PRO   N   CA   sing N N 328 
PRO   N   CD   sing N N 329 
PRO   N   H    sing N N 330 
PRO   CA  C    sing N N 331 
PRO   CA  CB   sing N N 332 
PRO   CA  HA   sing N N 333 
PRO   C   O    doub N N 334 
PRO   C   OXT  sing N N 335 
PRO   CB  CG   sing N N 336 
PRO   CB  HB2  sing N N 337 
PRO   CB  HB3  sing N N 338 
PRO   CG  CD   sing N N 339 
PRO   CG  HG2  sing N N 340 
PRO   CG  HG3  sing N N 341 
PRO   CD  HD2  sing N N 342 
PRO   CD  HD3  sing N N 343 
PRO   OXT HXT  sing N N 344 
SER   N   CA   sing N N 345 
SER   N   H    sing N N 346 
SER   N   H2   sing N N 347 
SER   CA  C    sing N N 348 
SER   CA  CB   sing N N 349 
SER   CA  HA   sing N N 350 
SER   C   O    doub N N 351 
SER   C   OXT  sing N N 352 
SER   CB  OG   sing N N 353 
SER   CB  HB2  sing N N 354 
SER   CB  HB3  sing N N 355 
SER   OG  HG   sing N N 356 
SER   OXT HXT  sing N N 357 
THR   N   CA   sing N N 358 
THR   N   H    sing N N 359 
THR   N   H2   sing N N 360 
THR   CA  C    sing N N 361 
THR   CA  CB   sing N N 362 
THR   CA  HA   sing N N 363 
THR   C   O    doub N N 364 
THR   C   OXT  sing N N 365 
THR   CB  OG1  sing N N 366 
THR   CB  CG2  sing N N 367 
THR   CB  HB   sing N N 368 
THR   OG1 HG1  sing N N 369 
THR   CG2 HG21 sing N N 370 
THR   CG2 HG22 sing N N 371 
THR   CG2 HG23 sing N N 372 
THR   OXT HXT  sing N N 373 
TRP   N   CA   sing N N 374 
TRP   N   H    sing N N 375 
TRP   N   H2   sing N N 376 
TRP   CA  C    sing N N 377 
TRP   CA  CB   sing N N 378 
TRP   CA  HA   sing N N 379 
TRP   C   O    doub N N 380 
TRP   C   OXT  sing N N 381 
TRP   CB  CG   sing N N 382 
TRP   CB  HB2  sing N N 383 
TRP   CB  HB3  sing N N 384 
TRP   CG  CD1  doub Y N 385 
TRP   CG  CD2  sing Y N 386 
TRP   CD1 NE1  sing Y N 387 
TRP   CD1 HD1  sing N N 388 
TRP   CD2 CE2  doub Y N 389 
TRP   CD2 CE3  sing Y N 390 
TRP   NE1 CE2  sing Y N 391 
TRP   NE1 HE1  sing N N 392 
TRP   CE2 CZ2  sing Y N 393 
TRP   CE3 CZ3  doub Y N 394 
TRP   CE3 HE3  sing N N 395 
TRP   CZ2 CH2  doub Y N 396 
TRP   CZ2 HZ2  sing N N 397 
TRP   CZ3 CH2  sing Y N 398 
TRP   CZ3 HZ3  sing N N 399 
TRP   CH2 HH2  sing N N 400 
TRP   OXT HXT  sing N N 401 
TYR   N   CA   sing N N 402 
TYR   N   H    sing N N 403 
TYR   N   H2   sing N N 404 
TYR   CA  C    sing N N 405 
TYR   CA  CB   sing N N 406 
TYR   CA  HA   sing N N 407 
TYR   C   O    doub N N 408 
TYR   C   OXT  sing N N 409 
TYR   CB  CG   sing N N 410 
TYR   CB  HB2  sing N N 411 
TYR   CB  HB3  sing N N 412 
TYR   CG  CD1  doub Y N 413 
TYR   CG  CD2  sing Y N 414 
TYR   CD1 CE1  sing Y N 415 
TYR   CD1 HD1  sing N N 416 
TYR   CD2 CE2  doub Y N 417 
TYR   CD2 HD2  sing N N 418 
TYR   CE1 CZ   doub Y N 419 
TYR   CE1 HE1  sing N N 420 
TYR   CE2 CZ   sing Y N 421 
TYR   CE2 HE2  sing N N 422 
TYR   CZ  OH   sing N N 423 
TYR   OH  HH   sing N N 424 
TYR   OXT HXT  sing N N 425 
VAL   N   CA   sing N N 426 
VAL   N   H    sing N N 427 
VAL   N   H2   sing N N 428 
VAL   CA  C    sing N N 429 
VAL   CA  CB   sing N N 430 
VAL   CA  HA   sing N N 431 
VAL   C   O    doub N N 432 
VAL   C   OXT  sing N N 433 
VAL   CB  CG1  sing N N 434 
VAL   CB  CG2  sing N N 435 
VAL   CB  HB   sing N N 436 
VAL   CG1 HG11 sing N N 437 
VAL   CG1 HG12 sing N N 438 
VAL   CG1 HG13 sing N N 439 
VAL   CG2 HG21 sing N N 440 
VAL   CG2 HG22 sing N N 441 
VAL   CG2 HG23 sing N N 442 
VAL   OXT HXT  sing N N 443 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4lev 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9J2W 
_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]   0.004623 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002013 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021052 
_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]   0.012453 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLY   A 1 5   ? 59.952 21.743  -25.634 1.00 50.01  ?  161 GLY   A N   1 
ATOM   2    C  CA  . GLY   A 1 5   ? 59.000 21.926  -26.714 1.00 80.22  ?  161 GLY   A CA  1 
ATOM   3    C  C   . GLY   A 1 5   ? 57.613 22.313  -26.236 1.00 65.17  ?  161 GLY   A C   1 
ATOM   4    O  O   . GLY   A 1 5   ? 56.693 22.477  -27.036 1.00 61.22  ?  161 GLY   A O   1 
ATOM   5    N  N   . ALA   A 1 6   ? 57.468 22.468  -24.917 1.00 52.18  ?  162 ALA   A N   1 
ATOM   6    C  CA  . ALA   A 1 6   ? 56.172 22.799  -24.333 1.00 46.11  ?  162 ALA   A CA  1 
ATOM   7    C  C   . ALA   A 1 6   ? 55.694 24.200  -24.701 1.00 50.24  ?  162 ALA   A C   1 
ATOM   8    O  O   . ALA   A 1 6   ? 54.503 24.493  -24.539 1.00 46.49  ?  162 ALA   A O   1 
ATOM   9    C  CB  . ALA   A 1 6   ? 56.233 22.655  -22.812 1.00 48.80  ?  162 ALA   A CB  1 
ATOM   10   N  N   . SER   A 1 7   ? 56.586 25.070  -25.182 1.00 35.39  ?  163 SER   A N   1 
ATOM   11   C  CA  . SER   A 1 7   ? 56.180 26.424  -25.549 1.00 51.05  ?  163 SER   A CA  1 
ATOM   12   C  C   . SER   A 1 7   ? 55.107 26.418  -26.634 1.00 57.99  ?  163 SER   A C   1 
ATOM   13   O  O   . SER   A 1 7   ? 54.198 27.260  -26.620 1.00 47.68  ?  163 SER   A O   1 
ATOM   14   C  CB  . SER   A 1 7   ? 57.403 27.222  -26.001 1.00 56.86  ?  163 SER   A CB  1 
ATOM   15   O  OG  . SER   A 1 7   ? 58.128 26.514  -26.991 1.00 56.64  ?  163 SER   A OG  1 
ATOM   16   N  N   . LYS   A 1 8   ? 55.179 25.468  -27.569 1.00 45.60  ?  164 LYS   A N   1 
ATOM   17   C  CA  . LYS   A 1 8   ? 54.152 25.372  -28.602 1.00 48.81  ?  164 LYS   A CA  1 
ATOM   18   C  C   . LYS   A 1 8   ? 52.813 24.941  -28.011 1.00 45.71  ?  164 LYS   A C   1 
ATOM   19   O  O   . LYS   A 1 8   ? 51.757 25.456  -28.405 1.00 38.64  ?  164 LYS   A O   1 
ATOM   20   C  CB  . LYS   A 1 8   ? 54.607 24.404  -29.692 1.00 39.20  ?  164 LYS   A CB  1 
ATOM   21   C  CG  . LYS   A 1 8   ? 53.633 24.266  -30.843 1.00 53.80  ?  164 LYS   A CG  1 
ATOM   22   C  CD  . LYS   A 1 8   ? 54.281 23.572  -32.025 1.00 45.15  ?  164 LYS   A CD  1 
ATOM   23   C  CE  . LYS   A 1 8   ? 53.286 23.366  -33.151 1.00 54.67  ?  164 LYS   A CE  1 
ATOM   24   N  NZ  . LYS   A 1 8   ? 53.923 22.716  -34.328 1.00 57.44  ?  164 LYS   A NZ  1 
ATOM   25   N  N   . LEU   A 1 9   ? 52.835 23.997  -27.065 1.00 44.71  ?  165 LEU   A N   1 
ATOM   26   C  CA  . LEU   A 1 9   ? 51.607 23.613  -26.376 1.00 45.67  ?  165 LEU   A CA  1 
ATOM   27   C  C   . LEU   A 1 9   ? 51.000 24.804  -25.644 1.00 36.77  ?  165 LEU   A C   1 
ATOM   28   O  O   . LEU   A 1 9   ? 49.775 24.987  -25.640 1.00 35.24  ?  165 LEU   A O   1 
ATOM   29   C  CB  . LEU   A 1 9   ? 51.894 22.471  -25.403 1.00 30.15  ?  165 LEU   A CB  1 
ATOM   30   C  CG  . LEU   A 1 9   ? 52.555 21.220  -25.985 1.00 30.45  ?  165 LEU   A CG  1 
ATOM   31   C  CD1 . LEU   A 1 9   ? 52.951 20.271  -24.869 1.00 24.29  ?  165 LEU   A CD1 1 
ATOM   32   C  CD2 . LEU   A 1 9   ? 51.627 20.528  -26.971 1.00 34.41  ?  165 LEU   A CD2 1 
ATOM   33   N  N   . ARG   A 1 10  ? 51.847 25.631  -25.028 1.00 47.26  ?  166 ARG   A N   1 
ATOM   34   C  CA  . ARG   A 1 10  ? 51.352 26.817  -24.335 1.00 41.00  ?  166 ARG   A CA  1 
ATOM   35   C  C   . ARG   A 1 10  ? 50.732 27.810  -25.312 1.00 36.65  ?  166 ARG   A C   1 
ATOM   36   O  O   . ARG   A 1 10  ? 49.712 28.439  -25.006 1.00 37.14  ?  166 ARG   A O   1 
ATOM   37   C  CB  . ARG   A 1 10  ? 52.487 27.470  -23.546 1.00 49.56  ?  166 ARG   A CB  1 
ATOM   38   C  CG  . ARG   A 1 10  ? 52.983 26.632  -22.375 1.00 60.86  ?  166 ARG   A CG  1 
ATOM   39   C  CD  . ARG   A 1 10  ? 52.672 27.287  -21.035 1.00 62.69  ?  166 ARG   A CD  1 
ATOM   40   N  NE  . ARG   A 1 10  ? 51.294 27.757  -20.950 1.00 66.83  ?  166 ARG   A NE  1 
ATOM   41   C  CZ  . ARG   A 1 10  ? 50.368 27.229  -20.161 1.00 69.62  ?  166 ARG   A CZ  1 
ATOM   42   N  NH1 . ARG   A 1 10  ? 50.633 26.197  -19.377 1.00 56.25  ?  166 ARG   A NH1 1 
ATOM   43   N  NH2 . ARG   A 1 10  ? 49.144 27.750  -20.159 1.00 72.37  ?  166 ARG   A NH2 1 
ATOM   44   N  N   . ALA   A 1 11  ? 51.338 27.967  -26.492 1.00 36.62  ?  167 ALA   A N   1 
ATOM   45   C  CA  . ALA   A 1 11  ? 50.746 28.818  -27.524 1.00 33.89  ?  167 ALA   A CA  1 
ATOM   46   C  C   . ALA   A 1 11  ? 49.367 28.306  -27.930 1.00 41.28  ?  167 ALA   A C   1 
ATOM   47   O  O   . ALA   A 1 11  ? 48.411 29.086  -28.081 1.00 54.81  ?  167 ALA   A O   1 
ATOM   48   C  CB  . ALA   A 1 11  ? 51.672 28.886  -28.739 1.00 29.35  ?  167 ALA   A CB  1 
ATOM   49   N  N   . VAL   A 1 12  ? 49.254 26.990  -28.124 1.00 43.83  ?  168 VAL   A N   1 
ATOM   50   C  CA  . VAL   A 1 12  ? 47.973 26.381  -28.476 1.00 41.69  ?  168 VAL   A CA  1 
ATOM   51   C  C   . VAL   A 1 12  ? 46.927 26.691  -27.414 1.00 38.39  ?  168 VAL   A C   1 
ATOM   52   O  O   . VAL   A 1 12  ? 45.791 27.077  -27.723 1.00 35.28  ?  168 VAL   A O   1 
ATOM   53   C  CB  . VAL   A 1 12  ? 48.139 24.863  -28.666 1.00 35.22  ?  168 VAL   A CB  1 
ATOM   54   C  CG1 . VAL   A 1 12  ? 46.778 24.190  -28.747 1.00 42.32  ?  168 VAL   A CG1 1 
ATOM   55   C  CG2 . VAL   A 1 12  ? 48.963 24.574  -29.907 1.00 34.55  ?  168 VAL   A CG2 1 
ATOM   56   N  N   . LEU   A 1 13  ? 47.295 26.513  -26.143 1.00 33.45  ?  169 LEU   A N   1 
ATOM   57   C  CA  . LEU   A 1 13  ? 46.348 26.765  -25.062 1.00 34.10  ?  169 LEU   A CA  1 
ATOM   58   C  C   . LEU   A 1 13  ? 45.958 28.236  -24.985 1.00 44.13  ?  169 LEU   A C   1 
ATOM   59   O  O   . LEU   A 1 13  ? 44.806 28.553  -24.668 1.00 40.89  ?  169 LEU   A O   1 
ATOM   60   C  CB  . LEU   A 1 13  ? 46.937 26.291  -23.734 1.00 41.55  ?  169 LEU   A CB  1 
ATOM   61   C  CG  . LEU   A 1 13  ? 47.089 24.773  -23.644 1.00 38.64  ?  169 LEU   A CG  1 
ATOM   62   C  CD1 . LEU   A 1 13  ? 48.068 24.387  -22.548 1.00 39.31  ?  169 LEU   A CD1 1 
ATOM   63   C  CD2 . LEU   A 1 13  ? 45.732 24.120  -23.425 1.00 33.42  ?  169 LEU   A CD2 1 
ATOM   64   N  N   . GLU   A 1 14  ? 46.895 29.141  -25.280 1.00 47.03  ?  170 GLU   A N   1 
ATOM   65   C  CA  . GLU   A 1 14  ? 46.569 30.564  -25.320 1.00 51.90  ?  170 GLU   A CA  1 
ATOM   66   C  C   . GLU   A 1 14  ? 45.510 30.852  -26.378 1.00 44.40  ?  170 GLU   A C   1 
ATOM   67   O  O   . GLU   A 1 14  ? 44.518 31.545  -26.112 1.00 54.94  ?  170 GLU   A O   1 
ATOM   68   C  CB  . GLU   A 1 14  ? 47.835 31.382  -25.586 1.00 55.53  ?  170 GLU   A CB  1 
ATOM   69   C  CG  . GLU   A 1 14  ? 47.743 32.842  -25.163 1.00 61.29  ?  170 GLU   A CG  1 
ATOM   70   C  CD  . GLU   A 1 14  ? 48.844 33.699  -25.764 1.00 73.05  ?  170 GLU   A CD  1 
ATOM   71   O  OE1 . GLU   A 1 14  ? 50.012 33.254  -25.766 1.00 76.14  ?  170 GLU   A OE1 1 
ATOM   72   O  OE2 . GLU   A 1 14  ? 48.543 34.819  -26.229 1.00 66.71  -1 170 GLU   A OE2 1 
ATOM   73   N  N   . LYS   A 1 15  ? 45.706 30.324  -27.590 1.00 47.39  ?  171 LYS   A N   1 
ATOM   74   C  CA  . LYS   A 1 15  ? 44.726 30.549  -28.652 1.00 47.13  ?  171 LYS   A CA  1 
ATOM   75   C  C   . LYS   A 1 15  ? 43.367 29.956  -28.285 1.00 56.17  ?  171 LYS   A C   1 
ATOM   76   O  O   . LYS   A 1 15  ? 42.317 30.591  -28.489 1.00 60.52  ?  171 LYS   A O   1 
ATOM   77   C  CB  . LYS   A 1 15  ? 45.245 29.969  -29.970 1.00 43.43  ?  171 LYS   A CB  1 
ATOM   78   C  CG  . LYS   A 1 15  ? 44.196 29.274  -30.827 1.00 55.97  ?  171 LYS   A CG  1 
ATOM   79   C  CD  . LYS   A 1 15  ? 44.795 28.795  -32.144 1.00 58.51  ?  171 LYS   A CD  1 
ATOM   80   C  CE  . LYS   A 1 15  ? 45.340 27.381  -32.029 1.00 43.84  ?  171 LYS   A CE  1 
ATOM   81   N  NZ  . LYS   A 1 15  ? 46.020 26.937  -33.278 1.00 59.90  ?  171 LYS   A NZ  1 
ATOM   82   N  N   . LEU   A 1 16  ? 43.370 28.744  -27.720 1.00 52.83  ?  172 LEU   A N   1 
ATOM   83   C  CA  . LEU   A 1 16  ? 42.118 28.104  -27.327 1.00 64.49  ?  172 LEU   A CA  1 
ATOM   84   C  C   . LEU   A 1 16  ? 41.383 28.925  -26.277 1.00 55.59  ?  172 LEU   A C   1 
ATOM   85   O  O   . LEU   A 1 16  ? 40.160 29.089  -26.355 1.00 61.05  ?  172 LEU   A O   1 
ATOM   86   C  CB  . LEU   A 1 16  ? 42.386 26.692  -26.807 1.00 51.59  ?  172 LEU   A CB  1 
ATOM   87   C  CG  . LEU   A 1 16  ? 42.792 25.639  -27.837 1.00 48.65  ?  172 LEU   A CG  1 
ATOM   88   C  CD1 . LEU   A 1 16  ? 43.219 24.361  -27.136 1.00 39.38  ?  172 LEU   A CD1 1 
ATOM   89   C  CD2 . LEU   A 1 16  ? 41.650 25.369  -28.803 1.00 42.55  ?  172 LEU   A CD2 1 
ATOM   90   N  N   . LYS   A 1 17  ? 42.127 29.607  -25.406 1.00 56.06  ?  173 LYS   A N   1 
ATOM   91   C  CA  . LYS   A 1 17  ? 41.502 30.398  -24.307 1.00 56.66  ?  173 LYS   A CA  1 
ATOM   92   C  C   . LYS   A 1 17  ? 40.933 31.723  -24.849 1.00 63.58  ?  173 LYS   A C   1 
ATOM   93   O  O   . LYS   A 1 17  ? 39.831 32.107  -24.421 1.00 68.03  ?  173 LYS   A O   1 
ATOM   94   C  CB  . LYS   A 1 17  ? 42.457 30.663  -23.137 1.00 50.19  ?  173 LYS   A CB  1 
ATOM   95   C  CG  . LYS   A 1 17  ? 43.150 32.014  -23.069 1.00 62.49  ?  173 LYS   A CG  1 
ATOM   96   C  CD  . LYS   A 1 17  ? 43.880 32.237  -21.752 1.00 59.22  ?  173 LYS   A CD  1 
ATOM   97   C  CE  . LYS   A 1 17  ? 43.380 31.320  -20.684 1.00 62.43  ?  173 LYS   A CE  1 
ATOM   98   N  NZ  . LYS   A 1 17  ? 44.193 31.413  -19.469 1.00 58.68  ?  173 LYS   A NZ  1 
ATOM   99   N  N   . LEU   A 1 18  ? 41.643 32.381  -25.763 1.00 62.31  ?  174 LEU   A N   1 
ATOM   100  C  CA  . LEU   A 1 18  ? 41.176 33.688  -26.283 1.00 60.36  ?  174 LEU   A CA  1 
ATOM   101  C  C   . LEU   A 1 18  ? 39.811 33.487  -26.955 1.00 80.13  ?  174 LEU   A C   1 
ATOM   102  O  O   . LEU   A 1 18  ? 39.070 34.478  -27.088 1.00 81.61  ?  174 LEU   A O   1 
ATOM   103  C  CB  . LEU   A 1 18  ? 42.203 34.314  -27.223 1.00 67.65  ?  174 LEU   A CB  1 
ATOM   104  C  CG  . LEU   A 1 18  ? 43.573 34.599  -26.602 1.00 69.75  ?  174 LEU   A CG  1 
ATOM   105  C  CD1 . LEU   A 1 18  ? 44.444 35.448  -27.506 1.00 68.52  ?  174 LEU   A CD1 1 
ATOM   106  C  CD2 . LEU   A 1 18  ? 43.452 35.235  -25.231 1.00 65.83  ?  174 LEU   A CD2 1 
ATOM   107  N  N   . SER   A 1 19  ? 39.477 32.252  -27.333 1.00 78.94  ?  175 SER   A N   1 
ATOM   108  C  CA  . SER   A 1 19  ? 38.139 31.974  -27.911 1.00 75.45  ?  175 SER   A CA  1 
ATOM   109  C  C   . SER   A 1 19  ? 37.178 31.536  -26.798 1.00 65.94  ?  175 SER   A C   1 
ATOM   110  O  O   . SER   A 1 19  ? 36.268 30.753  -27.118 1.00 74.29  ?  175 SER   A O   1 
ATOM   111  C  CB  . SER   A 1 19  ? 38.235 30.945  -29.002 1.00 74.96  ?  175 SER   A CB  1 
ATOM   112  O  OG  . SER   A 1 19  ? 39.482 31.039  -29.675 1.00 79.96  ?  175 SER   A OG  1 
ATOM   113  N  N   . ILE   A 1 23  ? 30.971 34.514  -25.664 1.00 64.81  ?  179 ILE   A N   1 
ATOM   114  C  CA  . ILE   A 1 23  ? 31.392 33.513  -24.642 1.00 65.90  ?  179 ILE   A CA  1 
ATOM   115  C  C   . ILE   A 1 23  ? 30.282 33.421  -23.589 1.00 81.09  ?  179 ILE   A C   1 
ATOM   116  O  O   . ILE   A 1 23  ? 29.352 32.615  -23.782 1.00 81.94  ?  179 ILE   A O   1 
ATOM   117  C  CB  . ILE   A 1 23  ? 32.739 33.917  -24.023 1.00 67.63  ?  179 ILE   A CB  1 
ATOM   118  N  N   . SER   A 1 24  ? 30.380 34.208  -22.517 1.00 74.21  ?  180 SER   A N   1 
ATOM   119  C  CA  . SER   A 1 24  ? 29.265 34.246  -21.540 1.00 74.83  ?  180 SER   A CA  1 
ATOM   120  C  C   . SER   A 1 24  ? 28.071 34.921  -22.224 1.00 69.64  ?  180 SER   A C   1 
ATOM   121  O  O   . SER   A 1 24  ? 26.943 34.779  -21.722 1.00 82.02  ?  180 SER   A O   1 
ATOM   122  C  CB  . SER   A 1 24  ? 29.665 34.963  -20.274 1.00 86.28  ?  180 SER   A CB  1 
ATOM   123  O  OG  . SER   A 1 24  ? 31.074 34.954  -20.091 1.00 89.42  ?  180 SER   A OG  1 
ATOM   124  N  N   . THR   A 1 25  ? 28.328 35.630  -23.325 1.00 65.61  ?  181 THR   A N   1 
ATOM   125  C  CA  . THR   A 1 25  ? 27.236 36.270  -24.085 1.00 81.60  ?  181 THR   A CA  1 
ATOM   126  C  C   . THR   A 1 25  ? 26.399 35.175  -24.684 1.00 78.91  ?  181 THR   A C   1 
ATOM   127  O  O   . THR   A 1 25  ? 25.223 35.039  -24.293 1.00 75.29  ?  181 THR   A O   1 
ATOM   128  C  CB  . THR   A 1 25  ? 27.823 37.185  -25.159 1.00 75.10  ?  181 THR   A CB  1 
ATOM   129  O  OG1 . THR   A 1 25  ? 28.059 36.347  -26.286 1.00 83.34  ?  181 THR   A OG1 1 
ATOM   130  C  CG2 . THR   A 1 25  ? 29.114 37.849  -24.719 1.00 65.88  ?  181 THR   A CG2 1 
ATOM   131  N  N   . ALA   A 1 26  ? 26.998 34.393  -25.575 1.00 71.41  ?  182 ALA   A N   1 
ATOM   132  C  CA  . ALA   A 1 26  ? 26.296 33.286  -26.212 1.00 67.85  ?  182 ALA   A CA  1 
ATOM   133  C  C   . ALA   A 1 26  ? 25.586 32.425  -25.178 1.00 67.33  ?  182 ALA   A C   1 
ATOM   134  O  O   . ALA   A 1 26  ? 24.443 32.001  -25.391 1.00 79.71  ?  182 ALA   A O   1 
ATOM   135  C  CB  . ALA   A 1 26  ? 27.273 32.448  -27.034 1.00 68.30  ?  182 ALA   A CB  1 
ATOM   136  N  N   . ALA   A 1 27  ? 26.237 32.179  -24.040 1.00 66.59  ?  183 ALA   A N   1 
ATOM   137  C  CA  . ALA   A 1 27  ? 25.632 31.360  -23.000 1.00 69.17  ?  183 ALA   A CA  1 
ATOM   138  C  C   . ALA   A 1 27  ? 24.411 32.044  -22.407 1.00 68.71  ?  183 ALA   A C   1 
ATOM   139  O  O   . ALA   A 1 27  ? 23.470 31.375  -21.980 1.00 82.93  ?  183 ALA   A O   1 
ATOM   140  C  CB  . ALA   A 1 27  ? 26.652 31.042  -21.907 1.00 68.43  ?  183 ALA   A CB  1 
ATOM   141  N  N   . GLY   A 1 28  ? 24.409 33.377  -22.366 1.00 69.77  ?  184 GLY   A N   1 
ATOM   142  C  CA  . GLY   A 1 28  ? 23.207 34.081  -21.948 1.00 77.29  ?  184 GLY   A CA  1 
ATOM   143  C  C   . GLY   A 1 28  ? 22.040 33.816  -22.879 1.00 64.67  ?  184 GLY   A C   1 
ATOM   144  O  O   . GLY   A 1 28  ? 20.915 33.550  -22.436 1.00 84.93  ?  184 GLY   A O   1 
ATOM   145  N  N   . MET   A 1 29  ? 22.295 33.883  -24.188 1.00 67.98  ?  185 MET   A N   1 
ATOM   146  C  CA  . MET   A 1 29  ? 21.240 33.545  -25.150 1.00 59.00  ?  185 MET   A CA  1 
ATOM   147  C  C   . MET   A 1 29  ? 20.743 32.110  -24.941 1.00 71.11  ?  185 MET   A C   1 
ATOM   148  O  O   . MET   A 1 29  ? 19.525 31.847  -24.880 1.00 75.26  ?  185 MET   A O   1 
ATOM   149  C  CB  . MET   A 1 29  ? 21.753 33.735  -26.580 1.00 57.12  ?  185 MET   A CB  1 
ATOM   150  C  CG  . MET   A 1 29  ? 22.517 35.029  -26.817 1.00 65.26  ?  185 MET   A CG  1 
ATOM   151  S  SD  . MET   A 1 29  ? 21.458 36.466  -27.086 1.00 97.08  ?  185 MET   A SD  1 
ATOM   152  C  CE  . MET   A 1 29  ? 20.161 35.755  -28.096 1.00 63.44  ?  185 MET   A CE  1 
ATOM   153  N  N   . VAL   A 1 30  ? 21.685 31.169  -24.824 1.00 64.38  ?  186 VAL   A N   1 
ATOM   154  C  CA  . VAL   A 1 30  ? 21.331 29.766  -24.613 1.00 69.73  ?  186 VAL   A CA  1 
ATOM   155  C  C   . VAL   A 1 30  ? 20.508 29.611  -23.338 1.00 73.67  ?  186 VAL   A C   1 
ATOM   156  O  O   . VAL   A 1 30  ? 19.533 28.853  -23.296 1.00 76.26  ?  186 VAL   A O   1 
ATOM   157  C  CB  . VAL   A 1 30  ? 22.596 28.886  -24.579 1.00 71.37  ?  186 VAL   A CB  1 
ATOM   158  C  CG1 . VAL   A 1 30  ? 22.212 27.416  -24.527 1.00 65.96  ?  186 VAL   A CG1 1 
ATOM   159  C  CG2 . VAL   A 1 30  ? 23.472 29.146  -25.797 1.00 67.65  ?  186 VAL   A CG2 1 
ATOM   160  N  N   . LYS   A 1 31  ? 20.885 30.338  -22.283 1.00 59.68  ?  187 LYS   A N   1 
ATOM   161  C  CA  . LYS   A 1 31  ? 20.186 30.249  -21.004 1.00 67.45  ?  187 LYS   A CA  1 
ATOM   162  C  C   . LYS   A 1 31  ? 18.741 30.723  -21.124 1.00 79.24  ?  187 LYS   A C   1 
ATOM   163  O  O   . LYS   A 1 31  ? 17.818 30.095  -20.585 1.00 79.05  ?  187 LYS   A O   1 
ATOM   164  C  CB  . LYS   A 1 31  ? 20.950 31.054  -19.947 1.00 78.48  ?  187 LYS   A CB  1 
ATOM   165  C  CG  . LYS   A 1 31  ? 20.661 30.667  -18.494 1.00 74.31  ?  187 LYS   A CG  1 
ATOM   166  C  CD  . LYS   A 1 31  ? 20.832 29.172  -18.256 1.00 77.68  ?  187 LYS   A CD  1 
ATOM   167  C  CE  . LYS   A 1 31  ? 19.782 28.698  -17.248 1.00 89.76  ?  187 LYS   A CE  1 
ATOM   168  N  NZ  . LYS   A 1 31  ? 19.415 27.282  -17.481 1.00 69.38  ?  187 LYS   A NZ  1 
ATOM   169  N  N   . GLY   A 1 32  ? 18.524 31.835  -21.828 1.00 71.01  ?  188 GLY   A N   1 
ATOM   170  C  CA  . GLY   A 1 32  ? 17.155 32.257  -22.089 1.00 68.04  ?  188 GLY   A CA  1 
ATOM   171  C  C   . GLY   A 1 32  ? 16.333 31.147  -22.716 1.00 78.80  ?  188 GLY   A C   1 
ATOM   172  O  O   . GLY   A 1 32  ? 15.260 30.773  -22.211 1.00 79.85  ?  188 GLY   A O   1 
ATOM   173  N  N   . VAL   A 1 33  ? 16.855 30.568  -23.801 1.00 70.52  ?  189 VAL   A N   1 
ATOM   174  C  CA  . VAL   A 1 33  ? 16.100 29.529  -24.508 1.00 65.26  ?  189 VAL   A CA  1 
ATOM   175  C  C   . VAL   A 1 33  ? 15.839 28.321  -23.603 1.00 72.06  ?  189 VAL   A C   1 
ATOM   176  O  O   . VAL   A 1 33  ? 14.731 27.762  -23.595 1.00 73.94  ?  189 VAL   A O   1 
ATOM   177  C  CB  . VAL   A 1 33  ? 16.829 29.138  -25.808 1.00 74.52  ?  189 VAL   A CB  1 
ATOM   178  C  CG1 . VAL   A 1 33  ? 16.133 27.976  -26.485 1.00 69.63  ?  189 VAL   A CG1 1 
ATOM   179  C  CG2 . VAL   A 1 33  ? 16.886 30.335  -26.747 1.00 69.63  ?  189 VAL   A CG2 1 
ATOM   180  N  N   . VAL   A 1 34  ? 16.838 27.908  -22.812 1.00 71.22  ?  190 VAL   A N   1 
ATOM   181  C  CA  . VAL   A 1 34  ? 16.682 26.674  -22.041 1.00 78.59  ?  190 VAL   A CA  1 
ATOM   182  C  C   . VAL   A 1 34  ? 15.694 26.876  -20.896 1.00 73.16  ?  190 VAL   A C   1 
ATOM   183  O  O   . VAL   A 1 34  ? 14.902 25.977  -20.581 1.00 77.79  ?  190 VAL   A O   1 
ATOM   184  C  CB  . VAL   A 1 34  ? 18.039 26.145  -21.529 1.00 68.79  ?  190 VAL   A CB  1 
ATOM   185  C  CG1 . VAL   A 1 34  ? 18.972 25.805  -22.692 1.00 80.16  ?  190 VAL   A CG1 1 
ATOM   186  C  CG2 . VAL   A 1 34  ? 18.681 27.081  -20.524 1.00 68.55  ?  190 VAL   A CG2 1 
ATOM   187  N  N   . ASP   A 1 35  ? 15.718 28.048  -20.255 1.00 68.67  ?  191 ASP   A N   1 
ATOM   188  C  CA  . ASP   A 1 35  ? 14.721 28.313  -19.224 1.00 69.24  ?  191 ASP   A CA  1 
ATOM   189  C  C   . ASP   A 1 35  ? 13.319 28.263  -19.806 1.00 77.21  ?  191 ASP   A C   1 
ATOM   190  O  O   . ASP   A 1 35  ? 12.403 27.680  -19.203 1.00 76.89  ?  191 ASP   A O   1 
ATOM   191  C  CB  . ASP   A 1 35  ? 14.973 29.666  -18.562 1.00 61.46  ?  191 ASP   A CB  1 
ATOM   192  C  CG  . ASP   A 1 35  ? 16.163 29.647  -17.629 1.00 78.62  ?  191 ASP   A CG  1 
ATOM   193  O  OD1 . ASP   A 1 35  ? 16.625 28.542  -17.276 1.00 82.67  ?  191 ASP   A OD1 1 
ATOM   194  O  OD2 . ASP   A 1 35  ? 16.648 30.737  -17.261 1.00 79.84  -1 191 ASP   A OD2 1 
ATOM   195  N  N   . HIS   A 1 36  ? 13.136 28.856  -20.992 1.00 70.77  ?  192 HIS   A N   1 
ATOM   196  C  CA  . HIS   A 1 36  ? 11.825 28.812  -21.635 1.00 76.19  ?  192 HIS   A CA  1 
ATOM   197  C  C   . HIS   A 1 36  ? 11.372 27.370  -21.877 1.00 85.28  ?  192 HIS   A C   1 
ATOM   198  O  O   . HIS   A 1 36  ? 10.242 26.983  -21.524 1.00 88.04  ?  192 HIS   A O   1 
ATOM   199  C  CB  . HIS   A 1 36  ? 11.875 29.593  -22.946 1.00 74.20  ?  192 HIS   A CB  1 
ATOM   200  C  CG  . HIS   A 1 36  ? 10.533 30.029  -23.440 1.00 74.62  ?  192 HIS   A CG  1 
ATOM   201  N  ND1 . HIS   A 1 36  ? 9.565  29.136  -23.843 1.00 85.01  ?  192 HIS   A ND1 1 
ATOM   202  C  CD2 . HIS   A 1 36  ? 9.998  31.263  -23.597 1.00 86.03  ?  192 HIS   A CD2 1 
ATOM   203  C  CE1 . HIS   A 1 36  ? 8.490  29.801  -24.228 1.00 93.19  ?  192 HIS   A CE1 1 
ATOM   204  N  NE2 . HIS   A 1 36  ? 8.727  31.093  -24.089 1.00 95.21  ?  192 HIS   A NE2 1 
ATOM   205  N  N   . LEU   A 1 37  ? 12.246 26.562  -22.487 1.00 89.96  ?  193 LEU   A N   1 
ATOM   206  C  CA  . LEU   A 1 37  ? 11.876 25.183  -22.794 1.00 82.56  ?  193 LEU   A CA  1 
ATOM   207  C  C   . LEU   A 1 37  ? 11.542 24.409  -21.528 1.00 74.36  ?  193 LEU   A C   1 
ATOM   208  O  O   . LEU   A 1 37  ? 10.603 23.602  -21.513 1.00 74.71  ?  193 LEU   A O   1 
ATOM   209  C  CB  . LEU   A 1 37  ? 12.995 24.468  -23.548 1.00 75.60  ?  193 LEU   A CB  1 
ATOM   210  C  CG  . LEU   A 1 37  ? 13.307 24.862  -24.987 1.00 85.64  ?  193 LEU   A CG  1 
ATOM   211  C  CD1 . LEU   A 1 37  ? 14.802 25.065  -25.134 1.00 72.71  ?  193 LEU   A CD1 1 
ATOM   212  C  CD2 . LEU   A 1 37  ? 12.797 23.826  -25.963 1.00 80.51  ?  193 LEU   A CD2 1 
ATOM   213  N  N   . LEU   A 1 38  ? 12.310 24.628  -20.456 1.00 71.53  ?  194 LEU   A N   1 
ATOM   214  C  CA  . LEU   A 1 38  ? 12.067 23.887  -19.225 1.00 74.76  ?  194 LEU   A CA  1 
ATOM   215  C  C   . LEU   A 1 38  ? 10.729 24.262  -18.608 1.00 75.81  ?  194 LEU   A C   1 
ATOM   216  O  O   . LEU   A 1 38  ? 10.038 23.400  -18.058 1.00 71.69  ?  194 LEU   A O   1 
ATOM   217  C  CB  . LEU   A 1 38  ? 13.198 24.118  -18.226 1.00 50.86  ?  194 LEU   A CB  1 
ATOM   218  C  CG  . LEU   A 1 38  ? 14.514 23.429  -18.586 1.00 69.18  ?  194 LEU   A CG  1 
ATOM   219  C  CD1 . LEU   A 1 38  ? 15.646 23.960  -17.726 1.00 65.11  ?  194 LEU   A CD1 1 
ATOM   220  C  CD2 . LEU   A 1 38  ? 14.378 21.921  -18.444 1.00 74.34  ?  194 LEU   A CD2 1 
ATOM   221  N  N   . LEU   A 1 39  ? 10.341 25.536  -18.690 1.00 78.50  ?  195 LEU   A N   1 
ATOM   222  C  CA  . LEU   A 1 39  ? 9.014  25.914  -18.209 1.00 75.91  ?  195 LEU   A CA  1 
ATOM   223  C  C   . LEU   A 1 39  ? 7.922  25.185  -18.988 1.00 70.21  ?  195 LEU   A C   1 
ATOM   224  O  O   . LEU   A 1 39  ? 7.006  24.580  -18.399 1.00 82.68  ?  195 LEU   A O   1 
ATOM   225  C  CB  . LEU   A 1 39  ? 8.841  27.429  -18.302 1.00 69.84  ?  195 LEU   A CB  1 
ATOM   226  C  CG  . LEU   A 1 39  ? 9.654  28.197  -17.258 1.00 80.10  ?  195 LEU   A CG  1 
ATOM   227  C  CD1 . LEU   A 1 39  ? 9.577  29.696  -17.497 1.00 76.66  ?  195 LEU   A CD1 1 
ATOM   228  C  CD2 . LEU   A 1 39  ? 9.188  27.838  -15.853 1.00 67.63  ?  195 LEU   A CD2 1 
ATOM   229  N  N   . ARG   A 1 40  ? 8.016  25.215  -20.322 1.00 75.60  ?  196 ARG   A N   1 
ATOM   230  C  CA  . ARG   A 1 40  ? 7.009  24.530  -21.133 1.00 71.45  ?  196 ARG   A CA  1 
ATOM   231  C  C   . ARG   A 1 40  ? 6.933  23.047  -20.781 1.00 78.45  ?  196 ARG   A C   1 
ATOM   232  O  O   . ARG   A 1 40  ? 5.839  22.491  -20.628 1.00 80.32  ?  196 ARG   A O   1 
ATOM   233  C  CB  . ARG   A 1 40  ? 7.294  24.711  -22.623 1.00 72.35  ?  196 ARG   A CB  1 
ATOM   234  C  CG  . ARG   A 1 40  ? 6.074  24.446  -23.501 1.00 63.44  ?  196 ARG   A CG  1 
ATOM   235  C  CD  . ARG   A 1 40  ? 5.150  25.653  -23.544 1.00 65.66  ?  196 ARG   A CD  1 
ATOM   236  N  NE  . ARG   A 1 40  ? 3.739  25.281  -23.550 1.00 75.73  ?  196 ARG   A NE  1 
ATOM   237  C  CZ  . ARG   A 1 40  ? 2.862  25.661  -22.630 1.00 92.85  ?  196 ARG   A CZ  1 
ATOM   238  N  NH1 . ARG   A 1 40  ? 3.219  26.417  -21.604 1.00 70.35  ?  196 ARG   A NH1 1 
ATOM   239  N  NH2 . ARG   A 1 40  ? 1.593  25.278  -22.746 1.00 84.56  ?  196 ARG   A NH2 1 
ATOM   240  N  N   . LEU   A 1 41  ? 8.089  22.393  -20.634 1.00 71.05  ?  197 LEU   A N   1 
ATOM   241  C  CA  . LEU   A 1 41  ? 8.098  20.975  -20.276 1.00 74.80  ?  197 LEU   A CA  1 
ATOM   242  C  C   . LEU   A 1 41  ? 7.497  20.747  -18.895 1.00 65.64  ?  197 LEU   A C   1 
ATOM   243  O  O   . LEU   A 1 41  ? 6.769  19.770  -18.681 1.00 72.04  ?  197 LEU   A O   1 
ATOM   244  C  CB  . LEU   A 1 41  ? 9.521  20.423  -20.326 1.00 54.16  ?  197 LEU   A CB  1 
ATOM   245  C  CG  . LEU   A 1 41  ? 10.132 20.151  -21.699 1.00 66.80  ?  197 LEU   A CG  1 
ATOM   246  C  CD1 . LEU   A 1 41  ? 11.647 20.212  -21.615 1.00 66.67  ?  197 LEU   A CD1 1 
ATOM   247  C  CD2 . LEU   A 1 41  ? 9.674  18.801  -22.231 1.00 57.06  ?  197 LEU   A CD2 1 
ATOM   248  N  N   . LYS   A 1 42  ? 7.797  21.633  -17.942 1.00 58.45  ?  198 LYS   A N   1 
ATOM   249  C  CA  . LYS   A 1 42  ? 7.267  21.502  -16.591 1.00 70.51  ?  198 LYS   A CA  1 
ATOM   250  C  C   . LYS   A 1 42  ? 5.753  21.596  -16.560 1.00 76.18  ?  198 LYS   A C   1 
ATOM   251  O  O   . LYS   A 1 42  ? 5.132  21.070  -15.628 1.00 71.53  ?  198 LYS   A O   1 
ATOM   252  C  CB  . LYS   A 1 42  ? 7.869  22.573  -15.681 1.00 59.68  ?  198 LYS   A CB  1 
ATOM   253  C  CG  . LYS   A 1 42  ? 9.276  22.260  -15.211 1.00 79.34  ?  198 LYS   A CG  1 
ATOM   254  C  CD  . LYS   A 1 42  ? 10.016 23.517  -14.786 1.00 71.41  ?  198 LYS   A CD  1 
ATOM   255  C  CE  . LYS   A 1 42  ? 10.613 23.358  -13.399 1.00 81.28  ?  198 LYS   A CE  1 
ATOM   256  N  NZ  . LYS   A 1 42  ? 10.601 21.938  -12.949 1.00 64.99  ?  198 LYS   A NZ  1 
ATOM   257  N  N   . CYS   A 1 43  ? 5.140  22.258  -17.545 1.00 59.81  ?  199 CYS   A N   1 
ATOM   258  C  CA  . CYS   A 1 43  ? 3.679  22.252  -17.588 1.00 76.08  ?  199 CYS   A CA  1 
ATOM   259  C  C   . CYS   A 1 43  ? 3.086  20.872  -17.878 1.00 85.62  ?  199 CYS   A C   1 
ATOM   260  O  O   . CYS   A 1 43  ? 1.893  20.666  -17.628 1.00 82.92  ?  199 CYS   A O   1 
ATOM   261  C  CB  . CYS   A 1 43  ? 3.172  23.267  -18.613 1.00 75.84  ?  199 CYS   A CB  1 
ATOM   262  S  SG  . CYS   A 1 43  ? 3.407  24.987  -18.109 1.00 96.20  ?  199 CYS   A SG  1 
ATOM   263  N  N   . ASP   A 1 44  ? 3.875  19.922  -18.380 1.00 75.64  ?  200 ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 44  ? 3.362  18.597  -18.706 1.00 70.53  ?  200 ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 44  ? 3.435  17.669  -17.497 1.00 67.99  ?  200 ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 44  ? 4.343  17.766  -16.667 1.00 83.67  ?  200 ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 44  ? 4.136  17.985  -19.875 1.00 78.14  ?  200 ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 44  ? 3.443  16.768  -20.461 1.00 73.34  ?  200 ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 44  ? 3.537  15.680  -19.854 1.00 79.73  ?  200 ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 44  ? 2.807  16.898  -21.527 1.00 69.02  -1 200 ASP   A OD2 1 
ATOM   271  N  N   . SER   A 1 45  ? 2.465  16.752  -17.414 1.00 75.66  ?  201 SER   A N   1 
ATOM   272  C  CA  . SER   A 1 45  ? 2.392  15.841  -16.275 1.00 73.07  ?  201 SER   A CA  1 
ATOM   273  C  C   . SER   A 1 45  ? 3.597  14.910  -16.226 1.00 63.61  ?  201 SER   A C   1 
ATOM   274  O  O   . SER   A 1 45  ? 4.088  14.575  -15.141 1.00 71.02  ?  201 SER   A O   1 
ATOM   275  C  CB  . SER   A 1 45  ? 1.098  15.027  -16.335 1.00 66.81  ?  201 SER   A CB  1 
ATOM   276  O  OG  . SER   A 1 45  ? 1.337  13.728  -16.852 1.00 76.02  ?  201 SER   A OG  1 
ATOM   277  N  N   . ALA   A 1 46  ? 4.088  14.481  -17.389 1.00 63.98  ?  202 ALA   A N   1 
ATOM   278  C  CA  . ALA   A 1 46  ? 5.174  13.509  -17.426 1.00 75.75  ?  202 ALA   A CA  1 
ATOM   279  C  C   . ALA   A 1 46  ? 6.537  14.146  -17.189 1.00 62.40  ?  202 ALA   A C   1 
ATOM   280  O  O   . ALA   A 1 46  ? 7.423  13.502  -16.617 1.00 75.05  ?  202 ALA   A O   1 
ATOM   281  C  CB  . ALA   A 1 46  ? 5.171  12.768  -18.764 1.00 67.19  ?  202 ALA   A CB  1 
ATOM   282  N  N   . PHE   A 1 47  ? 6.728  15.395  -17.616 1.00 66.07  ?  203 PHE   A N   1 
ATOM   283  C  CA  . PHE   A 1 47  ? 8.011  16.078  -17.510 1.00 53.75  ?  203 PHE   A CA  1 
ATOM   284  C  C   . PHE   A 1 47  ? 7.969  17.214  -16.492 1.00 68.12  ?  203 PHE   A C   1 
ATOM   285  O  O   . PHE   A 1 47  ? 8.707  18.195  -16.618 1.00 78.89  ?  203 PHE   A O   1 
ATOM   286  C  CB  . PHE   A 1 47  ? 8.448  16.603  -18.876 1.00 60.87  ?  203 PHE   A CB  1 
ATOM   287  C  CG  . PHE   A 1 47  ? 8.595  15.532  -19.917 1.00 54.26  ?  203 PHE   A CG  1 
ATOM   288  C  CD1 . PHE   A 1 47  ? 9.714  14.717  -19.942 1.00 59.90  ?  203 PHE   A CD1 1 
ATOM   289  C  CD2 . PHE   A 1 47  ? 7.609  15.335  -20.871 1.00 69.47  ?  203 PHE   A CD2 1 
ATOM   290  C  CE1 . PHE   A 1 47  ? 9.849  13.727  -20.899 1.00 62.21  ?  203 PHE   A CE1 1 
ATOM   291  C  CE2 . PHE   A 1 47  ? 7.737  14.349  -21.830 1.00 63.71  ?  203 PHE   A CE2 1 
ATOM   292  C  CZ  . PHE   A 1 47  ? 8.859  13.544  -21.845 1.00 64.66  ?  203 PHE   A CZ  1 
ATOM   293  N  N   . ARG   A 1 48  ? 7.110  17.090  -15.478 1.00 75.40  ?  204 ARG   A N   1 
ATOM   294  C  CA  . ARG   A 1 48  ? 6.972  18.151  -14.484 1.00 66.82  ?  204 ARG   A CA  1 
ATOM   295  C  C   . ARG   A 1 48  ? 8.255  18.332  -13.684 1.00 62.02  ?  204 ARG   A C   1 
ATOM   296  O  O   . ARG   A 1 48  ? 8.637  19.462  -13.356 1.00 67.05  ?  204 ARG   A O   1 
ATOM   297  C  CB  . ARG   A 1 48  ? 5.796  17.844  -13.554 1.00 70.94  ?  204 ARG   A CB  1 
ATOM   298  N  N   . GLY   A 1 49  ? 8.929  17.234  -13.356 1.00 65.25  ?  205 GLY   A N   1 
ATOM   299  C  CA  . GLY   A 1 49  ? 10.172 17.294  -12.623 1.00 49.33  ?  205 GLY   A CA  1 
ATOM   300  C  C   . GLY   A 1 49  ? 11.389 17.598  -13.458 1.00 53.51  ?  205 GLY   A C   1 
ATOM   301  O  O   . GLY   A 1 49  ? 12.513 17.478  -12.960 1.00 50.64  ?  205 GLY   A O   1 
ATOM   302  N  N   . VAL   A 1 50  ? 11.198 17.997  -14.719 1.00 60.39  ?  206 VAL   A N   1 
ATOM   303  C  CA  . VAL   A 1 50  ? 12.338 18.247  -15.589 1.00 52.12  ?  206 VAL   A CA  1 
ATOM   304  C  C   . VAL   A 1 50  ? 13.204 19.356  -15.004 1.00 57.52  ?  206 VAL   A C   1 
ATOM   305  O  O   . VAL   A 1 50  ? 12.716 20.272  -14.335 1.00 62.76  ?  206 VAL   A O   1 
ATOM   306  C  CB  . VAL   A 1 50  ? 11.865 18.598  -17.010 1.00 63.18  ?  206 VAL   A CB  1 
ATOM   307  C  CG1 . VAL   A 1 50  ? 11.442 20.063  -17.081 1.00 60.65  ?  206 VAL   A CG1 1 
ATOM   308  C  CG2 . VAL   A 1 50  ? 12.962 18.307  -18.026 1.00 65.71  ?  206 VAL   A CG2 1 
ATOM   309  N  N   . GLY   A 1 51  ? 14.506 19.256  -15.231 1.00 48.45  ?  207 GLY   A N   1 
ATOM   310  C  CA  . GLY   A 1 51  ? 15.418 20.221  -14.662 1.00 47.94  ?  207 GLY   A CA  1 
ATOM   311  C  C   . GLY   A 1 51  ? 16.782 20.064  -15.280 1.00 58.00  ?  207 GLY   A C   1 
ATOM   312  O  O   . GLY   A 1 51  ? 17.023 19.175  -16.102 1.00 58.42  ?  207 GLY   A O   1 
ATOM   313  N  N   . LEU   A 1 52  ? 17.668 20.967  -14.874 1.00 61.30  ?  208 LEU   A N   1 
ATOM   314  C  CA  . LEU   A 1 52  ? 19.054 20.931  -15.296 1.00 48.89  ?  208 LEU   A CA  1 
ATOM   315  C  C   . LEU   A 1 52  ? 19.874 20.235  -14.227 1.00 53.57  ?  208 LEU   A C   1 
ATOM   316  O  O   . LEU   A 1 52  ? 19.571 20.325  -13.034 1.00 59.86  ?  208 LEU   A O   1 
ATOM   317  C  CB  . LEU   A 1 52  ? 19.586 22.344  -15.531 1.00 46.00  ?  208 LEU   A CB  1 
ATOM   318  C  CG  . LEU   A 1 52  ? 19.342 22.933  -16.917 1.00 55.44  ?  208 LEU   A CG  1 
ATOM   319  C  CD1 . LEU   A 1 52  ? 20.163 24.188  -17.074 1.00 54.79  ?  208 LEU   A CD1 1 
ATOM   320  C  CD2 . LEU   A 1 52  ? 19.644 21.936  -18.040 1.00 58.35  ?  208 LEU   A CD2 1 
ATOM   321  N  N   . LEU   A 1 53  ? 20.919 19.542  -14.664 1.00 64.27  ?  209 LEU   A N   1 
ATOM   322  C  CA  . LEU   A 1 53  ? 21.760 18.789  -13.738 1.00 66.88  ?  209 LEU   A CA  1 
ATOM   323  C  C   . LEU   A 1 53  ? 22.466 19.699  -12.743 1.00 58.29  ?  209 LEU   A C   1 
ATOM   324  O  O   . LEU   A 1 53  ? 22.414 19.454  -11.536 1.00 74.20  ?  209 LEU   A O   1 
ATOM   325  C  CB  . LEU   A 1 53  ? 22.788 17.945  -14.492 1.00 63.26  ?  209 LEU   A CB  1 
ATOM   326  C  CG  . LEU   A 1 53  ? 22.434 16.464  -14.604 1.00 57.41  ?  209 LEU   A CG  1 
ATOM   327  C  CD1 . LEU   A 1 53  ? 21.342 16.244  -15.629 1.00 48.39  ?  209 LEU   A CD1 1 
ATOM   328  C  CD2 . LEU   A 1 53  ? 23.665 15.631  -14.928 1.00 43.63  ?  209 LEU   A CD2 1 
ATOM   329  N  N   . TYR   A 1 59  ? 25.487 24.620  -19.475 1.00 84.92  ?  215 TYR   A N   1 
ATOM   330  C  CA  . TYR   A 1 59  ? 26.255 24.650  -20.711 1.00 61.47  ?  215 TYR   A CA  1 
ATOM   331  C  C   . TYR   A 1 59  ? 27.557 23.857  -20.611 1.00 56.56  ?  215 TYR   A C   1 
ATOM   332  O  O   . TYR   A 1 59  ? 28.240 23.873  -19.592 1.00 65.55  ?  215 TYR   A O   1 
ATOM   333  C  CB  . TYR   A 1 59  ? 26.562 26.106  -21.103 1.00 69.37  ?  215 TYR   A CB  1 
ATOM   334  C  CG  . TYR   A 1 59  ? 27.817 26.680  -20.482 1.00 72.16  ?  215 TYR   A CG  1 
ATOM   335  C  CD1 . TYR   A 1 59  ? 27.797 27.184  -19.190 1.00 61.85  ?  215 TYR   A CD1 1 
ATOM   336  C  CD2 . TYR   A 1 59  ? 29.007 26.745  -21.195 1.00 73.73  ?  215 TYR   A CD2 1 
ATOM   337  C  CE1 . TYR   A 1 59  ? 28.930 27.718  -18.613 1.00 71.65  ?  215 TYR   A CE1 1 
ATOM   338  C  CE2 . TYR   A 1 59  ? 30.145 27.280  -20.627 1.00 70.21  ?  215 TYR   A CE2 1 
ATOM   339  C  CZ  . TYR   A 1 59  ? 30.099 27.764  -19.339 1.00 77.88  ?  215 TYR   A CZ  1 
ATOM   340  O  OH  . TYR   A 1 59  ? 31.242 28.296  -18.783 1.00 85.64  ?  215 TYR   A OH  1 
ATOM   341  N  N   . GLU   A 1 60  ? 27.880 23.159  -21.697 1.00 64.55  ?  216 GLU   A N   1 
ATOM   342  C  CA  . GLU   A 1 60  ? 29.142 22.452  -21.837 1.00 57.06  ?  216 GLU   A CA  1 
ATOM   343  C  C   . GLU   A 1 60  ? 29.511 22.427  -23.311 1.00 51.06  ?  216 GLU   A C   1 
ATOM   344  O  O   . GLU   A 1 60  ? 28.641 22.406  -24.188 1.00 51.79  ?  216 GLU   A O   1 
ATOM   345  C  CB  . GLU   A 1 60  ? 29.064 21.022  -21.288 1.00 50.93  ?  216 GLU   A CB  1 
ATOM   346  N  N   . HIS   A 1 61  ? 30.807 22.411  -23.578 1.00 49.23  ?  217 HIS   A N   1 
ATOM   347  C  CA  . HIS   A 1 61  ? 31.322 22.392  -24.941 1.00 46.03  ?  217 HIS   A CA  1 
ATOM   348  C  C   . HIS   A 1 61  ? 32.028 21.061  -25.153 1.00 52.16  ?  217 HIS   A C   1 
ATOM   349  O  O   . HIS   A 1 61  ? 33.145 20.851  -24.673 1.00 63.02  ?  217 HIS   A O   1 
ATOM   350  C  CB  . HIS   A 1 61  ? 32.236 23.583  -25.190 1.00 45.46  ?  217 HIS   A CB  1 
ATOM   351  C  CG  . HIS   A 1 61  ? 31.511 24.892  -25.213 1.00 46.08  ?  217 HIS   A CG  1 
ATOM   352  N  ND1 . HIS   A 1 61  ? 31.276 25.635  -24.077 1.00 61.84  ?  217 HIS   A ND1 1 
ATOM   353  C  CD2 . HIS   A 1 61  ? 30.936 25.574  -26.234 1.00 58.86  ?  217 HIS   A CD2 1 
ATOM   354  C  CE1 . HIS   A 1 61  ? 30.611 26.729  -24.402 1.00 58.66  ?  217 HIS   A CE1 1 
ATOM   355  N  NE2 . HIS   A 1 61  ? 30.390 26.716  -25.704 1.00 59.22  ?  217 HIS   A NE2 1 
ATOM   356  N  N   . VAL   A 1 62  ? 31.351 20.159  -25.864 1.00 47.37  ?  218 VAL   A N   1 
ATOM   357  C  CA  . VAL   A 1 62  ? 31.890 18.830  -26.124 1.00 44.03  ?  218 VAL   A CA  1 
ATOM   358  C  C   . VAL   A 1 62  ? 33.201 18.930  -26.890 1.00 54.54  ?  218 VAL   A C   1 
ATOM   359  O  O   . VAL   A 1 62  ? 34.174 18.234  -26.579 1.00 46.63  ?  218 VAL   A O   1 
ATOM   360  C  CB  . VAL   A 1 62  ? 30.848 17.988  -26.879 1.00 48.64  ?  218 VAL   A CB  1 
ATOM   361  C  CG1 . VAL   A 1 62  ? 31.481 16.720  -27.379 1.00 43.03  ?  218 VAL   A CG1 1 
ATOM   362  C  CG2 . VAL   A 1 62  ? 29.671 17.685  -25.972 1.00 56.19  ?  218 VAL   A CG2 1 
ATOM   363  N  N   . LYS   A 1 63  ? 33.251 19.797  -27.895 1.00 49.87  ?  219 LYS   A N   1 
ATOM   364  C  CA  . LYS   A 1 63  ? 34.467 20.054  -28.652 1.00 54.04  ?  219 LYS   A CA  1 
ATOM   365  C  C   . LYS   A 1 63  ? 35.053 21.381  -28.193 1.00 48.12  ?  219 LYS   A C   1 
ATOM   366  O  O   . LYS   A 1 63  ? 34.377 22.414  -28.248 1.00 55.42  ?  219 LYS   A O   1 
ATOM   367  C  CB  . LYS   A 1 63  ? 34.179 20.082  -30.152 1.00 48.75  ?  219 LYS   A CB  1 
ATOM   368  C  CG  . LYS   A 1 63  ? 33.354 18.910  -30.655 1.00 54.55  ?  219 LYS   A CG  1 
ATOM   369  C  CD  . LYS   A 1 63  ? 32.882 19.133  -32.088 1.00 47.67  ?  219 LYS   A CD  1 
ATOM   370  C  CE  . LYS   A 1 63  ? 33.826 20.045  -32.860 1.00 57.40  ?  219 LYS   A CE  1 
ATOM   371  N  NZ  . LYS   A 1 63  ? 33.561 20.028  -34.326 1.00 56.49  ?  219 LYS   A NZ  1 
ATOM   372  N  N   . ILE   A 1 64  ? 36.310 21.350  -27.742 1.00 48.92  ?  220 ILE   A N   1 
ATOM   373  C  CA  . ILE   A 1 64  ? 36.953 22.563  -27.254 1.00 54.68  ?  220 ILE   A CA  1 
ATOM   374  C  C   . ILE   A 1 64  ? 37.143 23.594  -28.361 1.00 52.01  ?  220 ILE   A C   1 
ATOM   375  O  O   . ILE   A 1 64  ? 37.278 24.787  -28.069 1.00 73.85  ?  220 ILE   A O   1 
ATOM   376  C  CB  . ILE   A 1 64  ? 38.297 22.214  -26.585 1.00 50.07  ?  220 ILE   A CB  1 
ATOM   377  C  CG1 . ILE   A 1 64  ? 38.498 23.046  -25.316 1.00 63.04  ?  220 ILE   A CG1 1 
ATOM   378  C  CG2 . ILE   A 1 64  ? 39.461 22.420  -27.544 1.00 50.18  ?  220 ILE   A CG2 1 
ATOM   379  C  CD1 . ILE   A 1 64  ? 37.588 22.647  -24.176 1.00 58.54  ?  220 ILE   A CD1 1 
ATOM   380  N  N   . SER   A 1 65  ? 37.130 23.174  -29.626 1.00 55.44  ?  221 SER   A N   1 
ATOM   381  C  CA  . SER   A 1 65  ? 37.381 24.061  -30.754 1.00 56.66  ?  221 SER   A CA  1 
ATOM   382  C  C   . SER   A 1 65  ? 36.118 24.696  -31.317 1.00 64.50  ?  221 SER   A C   1 
ATOM   383  O  O   . SER   A 1 65  ? 36.213 25.504  -32.247 1.00 76.94  ?  221 SER   A O   1 
ATOM   384  C  CB  . SER   A 1 65  ? 38.100 23.297  -31.872 1.00 49.32  ?  221 SER   A CB  1 
ATOM   385  O  OG  . SER   A 1 65  ? 37.284 22.257  -32.384 1.00 60.44  ?  221 SER   A OG  1 
ATOM   386  N  N   . ALA   A 1 66  ? 34.941 24.355  -30.786 1.00 63.33  ?  222 ALA   A N   1 
ATOM   387  C  CA  . ALA   A 1 66  ? 33.659 24.824  -31.308 1.00 60.24  ?  222 ALA   A CA  1 
ATOM   388  C  C   . ALA   A 1 66  ? 32.958 25.627  -30.218 1.00 58.70  ?  222 ALA   A C   1 
ATOM   389  O  O   . ALA   A 1 66  ? 32.030 25.127  -29.563 1.00 58.78  ?  222 ALA   A O   1 
ATOM   390  C  CB  . ALA   A 1 66  ? 32.795 23.656  -31.780 1.00 47.96  ?  222 ALA   A CB  1 
ATOM   391  N  N   . PRO   A 1 67  ? 33.360 26.883  -30.010 1.00 59.39  ?  223 PRO   A N   1 
ATOM   392  C  CA  . PRO   A 1 67  ? 32.804 27.653  -28.886 1.00 50.19  ?  223 PRO   A CA  1 
ATOM   393  C  C   . PRO   A 1 67  ? 31.313 27.919  -28.997 1.00 62.59  ?  223 PRO   A C   1 
ATOM   394  O  O   . PRO   A 1 67  ? 30.689 28.268  -27.988 1.00 66.44  ?  223 PRO   A O   1 
ATOM   395  C  CB  . PRO   A 1 67  ? 33.608 28.961  -28.924 1.00 59.91  ?  223 PRO   A CB  1 
ATOM   396  C  CG  . PRO   A 1 67  ? 34.077 29.073  -30.337 1.00 56.73  ?  223 PRO   A CG  1 
ATOM   397  C  CD  . PRO   A 1 67  ? 34.325 27.668  -30.799 1.00 61.21  ?  223 PRO   A CD  1 
ATOM   398  N  N   . ASN   A 1 68  ? 30.715 27.762  -30.177 1.00 56.74  ?  224 ASN   A N   1 
ATOM   399  C  CA  . ASN   A 1 68  ? 29.308 28.082  -30.378 1.00 60.89  ?  224 ASN   A CA  1 
ATOM   400  C  C   . ASN   A 1 68  ? 28.412 26.852  -30.458 1.00 65.35  ?  224 ASN   A C   1 
ATOM   401  O  O   . ASN   A 1 68  ? 27.221 26.990  -30.753 1.00 73.68  ?  224 ASN   A O   1 
ATOM   402  C  CB  . ASN   A 1 68  ? 29.129 28.932  -31.637 1.00 64.07  ?  224 ASN   A CB  1 
ATOM   403  C  CG  . ASN   A 1 68  ? 29.656 30.343  -31.467 1.00 69.55  ?  224 ASN   A CG  1 
ATOM   404  O  OD1 . ASN   A 1 68  ? 30.416 30.837  -32.297 1.00 79.58  ?  224 ASN   A OD1 1 
ATOM   405  N  ND2 . ASN   A 1 68  ? 29.251 31.000  -30.385 1.00 66.13  ?  224 ASN   A ND2 1 
ATOM   406  N  N   . GLU   A 1 69  ? 28.946 25.660  -30.207 1.00 70.76  ?  225 GLU   A N   1 
ATOM   407  C  CA  . GLU   A 1 69  ? 28.142 24.443  -30.172 1.00 54.18  ?  225 GLU   A CA  1 
ATOM   408  C  C   . GLU   A 1 69  ? 28.050 23.975  -28.725 1.00 57.81  ?  225 GLU   A C   1 
ATOM   409  O  O   . GLU   A 1 69  ? 29.054 23.563  -28.130 1.00 58.77  ?  225 GLU   A O   1 
ATOM   410  C  CB  . GLU   A 1 69  ? 28.722 23.366  -31.086 1.00 50.23  ?  225 GLU   A CB  1 
ATOM   411  C  CG  . GLU   A 1 69  ? 27.856 23.142  -32.317 1.00 78.07  ?  225 GLU   A CG  1 
ATOM   412  C  CD  . GLU   A 1 69  ? 28.235 21.911  -33.110 1.00 97.99  ?  225 GLU   A CD  1 
ATOM   413  O  OE1 . GLU   A 1 69  ? 29.322 21.899  -33.722 1.00 92.40  ?  225 GLU   A OE1 1 
ATOM   414  O  OE2 . GLU   A 1 69  ? 27.426 20.959  -33.134 1.00 101.10 -1 225 GLU   A OE2 1 
ATOM   415  N  N   . PHE   A 1 70  ? 26.846 24.050  -28.166 1.00 59.95  ?  226 PHE   A N   1 
ATOM   416  C  CA  . PHE   A 1 70  ? 26.586 23.816  -26.755 1.00 48.78  ?  226 PHE   A CA  1 
ATOM   417  C  C   . PHE   A 1 70  ? 25.949 22.448  -26.547 1.00 44.23  ?  226 PHE   A C   1 
ATOM   418  O  O   . PHE   A 1 70  ? 25.342 21.873  -27.456 1.00 53.97  ?  226 PHE   A O   1 
ATOM   419  C  CB  . PHE   A 1 70  ? 25.675 24.912  -26.187 1.00 55.20  ?  226 PHE   A CB  1 
ATOM   420  C  CG  . PHE   A 1 70  ? 26.391 26.199  -25.883 1.00 55.03  ?  226 PHE   A CG  1 
ATOM   421  C  CD1 . PHE   A 1 70  ? 26.798 27.035  -26.909 1.00 59.36  ?  226 PHE   A CD1 1 
ATOM   422  C  CD2 . PHE   A 1 70  ? 26.646 26.583  -24.577 1.00 60.00  ?  226 PHE   A CD2 1 
ATOM   423  C  CE1 . PHE   A 1 70  ? 27.459 28.221  -26.638 1.00 59.85  ?  226 PHE   A CE1 1 
ATOM   424  C  CE2 . PHE   A 1 70  ? 27.303 27.771  -24.302 1.00 64.78  ?  226 PHE   A CE2 1 
ATOM   425  C  CZ  . PHE   A 1 70  ? 27.709 28.589  -25.334 1.00 55.49  ?  226 PHE   A CZ  1 
ATOM   426  N  N   . ASP   A 1 71  ? 26.091 21.937  -25.327 1.00 47.21  ?  227 ASP   A N   1 
ATOM   427  C  CA  . ASP   A 1 71  ? 25.574 20.621  -24.959 1.00 46.35  ?  227 ASP   A CA  1 
ATOM   428  C  C   . ASP   A 1 71  ? 24.992 20.726  -23.557 1.00 54.73  ?  227 ASP   A C   1 
ATOM   429  O  O   . ASP   A 1 71  ? 25.730 20.962  -22.595 1.00 45.66  ?  227 ASP   A O   1 
ATOM   430  C  CB  . ASP   A 1 71  ? 26.674 19.562  -25.018 1.00 50.43  ?  227 ASP   A CB  1 
ATOM   431  C  CG  . ASP   A 1 71  ? 26.158 18.209  -25.463 1.00 70.22  ?  227 ASP   A CG  1 
ATOM   432  O  OD1 . ASP   A 1 71  ? 25.721 17.425  -24.597 1.00 90.03  ?  227 ASP   A OD1 1 
ATOM   433  O  OD2 . ASP   A 1 71  ? 26.194 17.932  -26.680 1.00 71.36  -1 227 ASP   A OD2 1 
ATOM   434  N  N   . VAL   A 1 72  ? 23.673 20.562  -23.439 1.00 61.08  ?  228 VAL   A N   1 
ATOM   435  C  CA  . VAL   A 1 72  ? 22.999 20.605  -22.150 1.00 56.96  ?  228 VAL   A CA  1 
ATOM   436  C  C   . VAL   A 1 72  ? 22.190 19.327  -21.979 1.00 51.68  ?  228 VAL   A C   1 
ATOM   437  O  O   . VAL   A 1 72  ? 21.918 18.600  -22.938 1.00 45.23  ?  228 VAL   A O   1 
ATOM   438  C  CB  . VAL   A 1 72  ? 22.089 21.845  -21.996 1.00 55.45  ?  228 VAL   A CB  1 
ATOM   439  C  CG1 . VAL   A 1 72  ? 22.866 23.118  -22.293 1.00 68.90  ?  228 VAL   A CG1 1 
ATOM   440  C  CG2 . VAL   A 1 72  ? 20.879 21.731  -22.894 1.00 49.06  ?  228 VAL   A CG2 1 
ATOM   441  N  N   . MET   A 1 73  ? 21.809 19.058  -20.733 1.00 45.44  ?  229 MET   A N   1 
ATOM   442  C  CA  . MET   A 1 73  ? 21.116 17.828  -20.372 1.00 54.16  ?  229 MET   A CA  1 
ATOM   443  C  C   . MET   A 1 73  ? 19.902 18.168  -19.521 1.00 58.81  ?  229 MET   A C   1 
ATOM   444  O  O   . MET   A 1 73  ? 20.037 18.810  -18.474 1.00 51.66  ?  229 MET   A O   1 
ATOM   445  C  CB  . MET   A 1 73  ? 22.050 16.876  -19.618 1.00 35.22  ?  229 MET   A CB  1 
ATOM   446  C  CG  . MET   A 1 73  ? 21.384 15.596  -19.142 1.00 55.75  ?  229 MET   A CG  1 
ATOM   447  S  SD  . MET   A 1 73  ? 22.549 14.433  -18.402 1.00 62.40  ?  229 MET   A SD  1 
ATOM   448  C  CE  . MET   A 1 73  ? 24.023 14.770  -19.362 1.00 48.21  ?  229 MET   A CE  1 
ATOM   449  N  N   . PHE   A 1 74  ? 18.724 17.742  -19.971 1.00 53.85  ?  230 PHE   A N   1 
ATOM   450  C  CA  . PHE   A 1 74  ? 17.496 17.879  -19.198 1.00 51.06  ?  230 PHE   A CA  1 
ATOM   451  C  C   . PHE   A 1 74  ? 17.264 16.588  -18.421 1.00 52.91  ?  230 PHE   A C   1 
ATOM   452  O  O   . PHE   A 1 74  ? 17.052 15.528  -19.019 1.00 58.11  ?  230 PHE   A O   1 
ATOM   453  C  CB  . PHE   A 1 74  ? 16.296 18.173  -20.100 1.00 52.89  ?  230 PHE   A CB  1 
ATOM   454  C  CG  . PHE   A 1 74  ? 16.315 19.541  -20.736 1.00 57.25  ?  230 PHE   A CG  1 
ATOM   455  C  CD1 . PHE   A 1 74  ? 17.407 20.382  -20.603 1.00 51.22  ?  230 PHE   A CD1 1 
ATOM   456  C  CD2 . PHE   A 1 74  ? 15.224 19.983  -21.468 1.00 52.05  ?  230 PHE   A CD2 1 
ATOM   457  C  CE1 . PHE   A 1 74  ? 17.413 21.632  -21.193 1.00 54.81  ?  230 PHE   A CE1 1 
ATOM   458  C  CE2 . PHE   A 1 74  ? 15.225 21.232  -22.058 1.00 56.85  ?  230 PHE   A CE2 1 
ATOM   459  C  CZ  . PHE   A 1 74  ? 16.319 22.057  -21.920 1.00 59.88  ?  230 PHE   A CZ  1 
ATOM   460  N  N   . LYS   A 1 75  ? 17.309 16.674  -17.095 1.00 59.73  ?  231 LYS   A N   1 
ATOM   461  C  CA  . LYS   A 1 75  ? 17.121 15.507  -16.247 1.00 56.50  ?  231 LYS   A CA  1 
ATOM   462  C  C   . LYS   A 1 75  ? 15.666 15.373  -15.814 1.00 45.88  ?  231 LYS   A C   1 
ATOM   463  O  O   . LYS   A 1 75  ? 14.883 16.325  -15.859 1.00 55.12  ?  231 LYS   A O   1 
ATOM   464  C  CB  . LYS   A 1 75  ? 18.010 15.578  -15.006 1.00 47.52  ?  231 LYS   A CB  1 
ATOM   465  C  CG  . LYS   A 1 75  ? 17.774 16.820  -14.163 1.00 51.01  ?  231 LYS   A CG  1 
ATOM   466  C  CD  . LYS   A 1 75  ? 18.555 16.791  -12.862 1.00 55.76  ?  231 LYS   A CD  1 
ATOM   467  C  CE  . LYS   A 1 75  ? 17.713 17.353  -11.729 1.00 55.07  ?  231 LYS   A CE  1 
ATOM   468  N  NZ  . LYS   A 1 75  ? 16.958 16.284  -11.023 1.00 58.27  ?  231 LYS   A NZ  1 
ATOM   469  N  N   . LEU   A 1 76  ? 15.319 14.167  -15.376 1.00 50.12  ?  232 LEU   A N   1 
ATOM   470  C  CA  . LEU   A 1 76  ? 13.993 13.880  -14.842 1.00 60.84  ?  232 LEU   A CA  1 
ATOM   471  C  C   . LEU   A 1 76  ? 14.144 12.772  -13.814 1.00 53.62  ?  232 LEU   A C   1 
ATOM   472  O  O   . LEU   A 1 76  ? 14.638 11.691  -14.145 1.00 54.88  ?  232 LEU   A O   1 
ATOM   473  C  CB  . LEU   A 1 76  ? 13.029 13.464  -15.955 1.00 46.81  ?  232 LEU   A CB  1 
ATOM   474  C  CG  . LEU   A 1 76  ? 11.568 13.252  -15.558 1.00 58.41  ?  232 LEU   A CG  1 
ATOM   475  C  CD1 . LEU   A 1 76  ? 10.663 13.940  -16.555 1.00 63.57  ?  232 LEU   A CD1 1 
ATOM   476  C  CD2 . LEU   A 1 76  ? 11.229 11.773  -15.472 1.00 50.68  ?  232 LEU   A CD2 1 
ATOM   477  N  N   . GLU   A 1 77  ? 13.738 13.035  -12.575 1.00 54.87  ?  233 GLU   A N   1 
ATOM   478  C  CA  . GLU   A 1 77  ? 13.905 12.034  -11.531 1.00 46.20  ?  233 GLU   A CA  1 
ATOM   479  C  C   . GLU   A 1 77  ? 12.913 10.893  -11.706 1.00 52.76  ?  233 GLU   A C   1 
ATOM   480  O  O   . GLU   A 1 77  ? 11.727 11.107  -11.970 1.00 58.94  ?  233 GLU   A O   1 
ATOM   481  C  CB  . GLU   A 1 77  ? 13.736 12.642  -10.140 1.00 53.74  ?  233 GLU   A CB  1 
ATOM   482  C  CG  . GLU   A 1 77  ? 13.954 11.603  -9.040  1.00 52.56  ?  233 GLU   A CG  1 
ATOM   483  C  CD  . GLU   A 1 77  ? 13.881 12.168  -7.638  1.00 75.67  ?  233 GLU   A CD  1 
ATOM   484  O  OE1 . GLU   A 1 77  ? 13.607 13.376  -7.487  1.00 93.41  ?  233 GLU   A OE1 1 
ATOM   485  O  OE2 . GLU   A 1 77  ? 14.100 11.393  -6.683  1.00 76.28  -1 233 GLU   A OE2 1 
ATOM   486  N  N   . VAL   A 1 78  ? 13.412 9.674   -11.550 1.00 52.93  ?  234 VAL   A N   1 
ATOM   487  C  CA  . VAL   A 1 78  ? 12.608 8.461   -11.575 1.00 52.62  ?  234 VAL   A CA  1 
ATOM   488  C  C   . VAL   A 1 78  ? 12.759 7.765   -10.227 1.00 61.99  ?  234 VAL   A C   1 
ATOM   489  O  O   . VAL   A 1 78  ? 13.722 7.031   -9.995  1.00 57.32  ?  234 VAL   A O   1 
ATOM   490  C  CB  . VAL   A 1 78  ? 13.032 7.532   -12.727 1.00 56.83  ?  234 VAL   A CB  1 
ATOM   491  C  CG1 . VAL   A 1 78  ? 12.061 6.376   -12.861 1.00 61.22  ?  234 VAL   A CG1 1 
ATOM   492  C  CG2 . VAL   A 1 78  ? 13.122 8.313   -14.028 1.00 62.62  ?  234 VAL   A CG2 1 
ATOM   493  N  N   . PRO   A 1 79  ? 11.828 7.982   -9.302  1.00 70.28  ?  235 PRO   A N   1 
ATOM   494  C  CA  . PRO   A 1 79  ? 11.934 7.343   -7.984  1.00 59.75  ?  235 PRO   A CA  1 
ATOM   495  C  C   . PRO   A 1 79  ? 11.632 5.855   -8.050  1.00 61.28  ?  235 PRO   A C   1 
ATOM   496  O  O   . PRO   A 1 79  ? 10.834 5.395   -8.869  1.00 65.59  ?  235 PRO   A O   1 
ATOM   497  C  CB  . PRO   A 1 79  ? 10.893 8.075   -7.127  1.00 59.27  ?  235 PRO   A CB  1 
ATOM   498  C  CG  . PRO   A 1 79  ? 10.117 8.951   -8.045  1.00 64.61  ?  235 PRO   A CG  1 
ATOM   499  C  CD  . PRO   A 1 79  ? 10.718 8.939   -9.403  1.00 59.39  ?  235 PRO   A CD  1 
ATOM   500  N  N   . ARG   A 1 80  ? 12.284 5.107   -7.158  1.00 66.30  ?  236 ARG   A N   1 
ATOM   501  C  CA  . ARG   A 1 80  ? 12.139 3.653   -7.038  1.00 64.41  ?  236 ARG   A CA  1 
ATOM   502  C  C   . ARG   A 1 80  ? 12.217 2.970   -8.404  1.00 65.47  ?  236 ARG   A C   1 
ATOM   503  O  O   . ARG   A 1 80  ? 11.291 2.292   -8.853  1.00 67.10  ?  236 ARG   A O   1 
ATOM   504  C  CB  . ARG   A 1 80  ? 10.843 3.293   -6.305  1.00 75.34  ?  236 ARG   A CB  1 
ATOM   505  C  CG  . ARG   A 1 80  ? 10.921 3.494   -4.798  1.00 73.11  ?  236 ARG   A CG  1 
ATOM   506  C  CD  . ARG   A 1 80  ? 11.133 2.175   -4.067  1.00 68.10  ?  236 ARG   A CD  1 
ATOM   507  N  NE  . ARG   A 1 80  ? 9.894  1.421   -3.914  1.00 75.82  ?  236 ARG   A NE  1 
ATOM   508  C  CZ  . ARG   A 1 80  ? 9.712  0.462   -3.017  1.00 82.38  ?  236 ARG   A CZ  1 
ATOM   509  N  NH1 . ARG   A 1 80  ? 10.668 0.116   -2.171  1.00 76.44  ?  236 ARG   A NH1 1 
ATOM   510  N  NH2 . ARG   A 1 80  ? 8.540  -0.166  -2.967  1.00 80.11  ?  236 ARG   A NH2 1 
ATOM   511  N  N   . ILE   A 1 81  ? 13.358 3.162   -9.059  1.00 78.59  ?  237 ILE   A N   1 
ATOM   512  C  CA  . ILE   A 1 81  ? 13.598 2.608   -10.386 1.00 63.24  ?  237 ILE   A CA  1 
ATOM   513  C  C   . ILE   A 1 81  ? 14.072 1.166   -10.253 1.00 60.53  ?  237 ILE   A C   1 
ATOM   514  O  O   . ILE   A 1 81  ? 14.686 0.780   -9.252  1.00 69.03  ?  237 ILE   A O   1 
ATOM   515  C  CB  . ILE   A 1 81  ? 14.617 3.480   -11.149 1.00 64.17  ?  237 ILE   A CB  1 
ATOM   516  C  CG1 . ILE   A 1 81  ? 14.651 3.116   -12.634 1.00 66.75  ?  237 ILE   A CG1 1 
ATOM   517  C  CG2 . ILE   A 1 81  ? 16.009 3.369   -10.533 1.00 52.17  ?  237 ILE   A CG2 1 
ATOM   518  C  CD1 . ILE   A 1 81  ? 15.262 4.190   -13.499 1.00 67.66  ?  237 ILE   A CD1 1 
ATOM   519  N  N   . GLN   A 1 82  ? 13.782 0.349   -11.266 1.00 72.19  ?  238 GLN   A N   1 
ATOM   520  C  CA  . GLN   A 1 82  ? 14.204 -1.047  -11.297 1.00 56.24  ?  238 GLN   A CA  1 
ATOM   521  C  C   . GLN   A 1 82  ? 14.924 -1.285  -12.617 1.00 50.42  ?  238 GLN   A C   1 
ATOM   522  O  O   . GLN   A 1 82  ? 14.313 -1.217  -13.686 1.00 67.57  ?  238 GLN   A O   1 
ATOM   523  C  CB  . GLN   A 1 82  ? 13.011 -1.989  -11.137 1.00 61.25  ?  238 GLN   A CB  1 
ATOM   524  C  CG  . GLN   A 1 82  ? 13.347 -3.449  -11.366 1.00 72.54  ?  238 GLN   A CG  1 
ATOM   525  C  CD  . GLN   A 1 82  ? 14.303 -3.992  -10.321 1.00 70.53  ?  238 GLN   A CD  1 
ATOM   526  O  OE1 . GLN   A 1 82  ? 15.509 -4.077  -10.554 1.00 77.21  ?  238 GLN   A OE1 1 
ATOM   527  N  NE2 . GLN   A 1 82  ? 13.767 -4.375  -9.167  1.00 74.79  ?  238 GLN   A NE2 1 
ATOM   528  N  N   . LEU   A 1 83  ? 16.221 -1.555  -12.553 1.00 59.66  ?  239 LEU   A N   1 
ATOM   529  C  CA  . LEU   A 1 83  ? 17.023 -1.704  -13.757 1.00 50.67  ?  239 LEU   A CA  1 
ATOM   530  C  C   . LEU   A 1 83  ? 17.159 -3.172  -14.135 1.00 46.99  ?  239 LEU   A C   1 
ATOM   531  O  O   . LEU   A 1 83  ? 17.315 -4.039  -13.270 1.00 60.90  ?  239 LEU   A O   1 
ATOM   532  C  CB  . LEU   A 1 83  ? 18.406 -1.078  -13.575 1.00 46.79  ?  239 LEU   A CB  1 
ATOM   533  C  CG  . LEU   A 1 83  ? 18.393 0.446   -13.441 1.00 50.01  ?  239 LEU   A CG  1 
ATOM   534  C  CD1 . LEU   A 1 83  ? 19.809 1.006   -13.419 1.00 38.10  ?  239 LEU   A CD1 1 
ATOM   535  C  CD2 . LEU   A 1 83  ? 17.566 1.082   -14.554 1.00 52.24  ?  239 LEU   A CD2 1 
ATOM   536  N  N   . GLU   A 1 84  ? 17.090 -3.441  -15.437 1.00 51.22  ?  240 GLU   A N   1 
ATOM   537  C  CA  . GLU   A 1 84  ? 17.295 -4.771  -15.996 1.00 62.49  ?  240 GLU   A CA  1 
ATOM   538  C  C   . GLU   A 1 84  ? 18.480 -4.704  -16.945 1.00 55.08  ?  240 GLU   A C   1 
ATOM   539  O  O   . GLU   A 1 84  ? 18.401 -4.044  -17.983 1.00 46.38  ?  240 GLU   A O   1 
ATOM   540  C  CB  . GLU   A 1 84  ? 16.045 -5.252  -16.735 1.00 65.02  ?  240 GLU   A CB  1 
ATOM   541  C  CG  . GLU   A 1 84  ? 16.203 -6.588  -17.441 1.00 75.83  ?  240 GLU   A CG  1 
ATOM   542  C  CD  . GLU   A 1 84  ? 14.881 -7.306  -17.631 1.00 69.29  ?  240 GLU   A CD  1 
ATOM   543  O  OE1 . GLU   A 1 84  ? 13.902 -6.948  -16.941 1.00 79.41  ?  240 GLU   A OE1 1 
ATOM   544  O  OE2 . GLU   A 1 84  ? 14.818 -8.223  -18.479 1.00 79.10  -1 240 GLU   A OE2 1 
ATOM   545  N  N   . GLU   A 1 85  ? 19.575 -5.375  -16.599 1.00 54.87  ?  241 GLU   A N   1 
ATOM   546  C  CA  . GLU   A 1 85  ? 20.761 -5.301  -17.439 1.00 45.64  ?  241 GLU   A CA  1 
ATOM   547  C  C   . GLU   A 1 85  ? 20.516 -6.001  -18.769 1.00 44.23  ?  241 GLU   A C   1 
ATOM   548  O  O   . GLU   A 1 85  ? 20.094 -7.161  -18.805 1.00 48.19  ?  241 GLU   A O   1 
ATOM   549  C  CB  . GLU   A 1 85  ? 21.969 -5.917  -16.739 1.00 44.79  ?  241 GLU   A CB  1 
ATOM   550  C  CG  . GLU   A 1 85  ? 23.256 -5.718  -17.524 1.00 42.24  ?  241 GLU   A CG  1 
ATOM   551  C  CD  . GLU   A 1 85  ? 24.472 -6.298  -16.836 1.00 55.26  ?  241 GLU   A CD  1 
ATOM   552  O  OE1 . GLU   A 1 85  ? 24.348 -6.758  -15.682 1.00 67.12  ?  241 GLU   A OE1 1 
ATOM   553  O  OE2 . GLU   A 1 85  ? 25.557 -6.288  -17.453 1.00 52.41  -1 241 GLU   A OE2 1 
ATOM   554  N  N   . TYR   A 1 86  ? 20.782 -5.292  -19.862 1.00 47.60  ?  242 TYR   A N   1 
ATOM   555  C  CA  . TYR   A 1 86  ? 20.616 -5.852  -21.198 1.00 46.64  ?  242 TYR   A CA  1 
ATOM   556  C  C   . TYR   A 1 86  ? 21.870 -6.625  -21.582 1.00 54.74  ?  242 TYR   A C   1 
ATOM   557  O  O   . TYR   A 1 86  ? 22.953 -6.043  -21.707 1.00 50.99  ?  242 TYR   A O   1 
ATOM   558  C  CB  . TYR   A 1 86  ? 20.336 -4.755  -22.218 1.00 46.95  ?  242 TYR   A CB  1 
ATOM   559  C  CG  . TYR   A 1 86  ? 20.474 -5.238  -23.643 1.00 45.78  ?  242 TYR   A CG  1 
ATOM   560  C  CD1 . TYR   A 1 86  ? 19.623 -6.209  -24.152 1.00 54.85  ?  242 TYR   A CD1 1 
ATOM   561  C  CD2 . TYR   A 1 86  ? 21.481 -4.751  -24.465 1.00 46.68  ?  242 TYR   A CD2 1 
ATOM   562  C  CE1 . TYR   A 1 86  ? 19.754 -6.664  -25.452 1.00 65.60  ?  242 TYR   A CE1 1 
ATOM   563  C  CE2 . TYR   A 1 86  ? 21.622 -5.203  -25.764 1.00 55.55  ?  242 TYR   A CE2 1 
ATOM   564  C  CZ  . TYR   A 1 86  ? 20.756 -6.157  -26.253 1.00 57.74  ?  242 TYR   A CZ  1 
ATOM   565  O  OH  . TYR   A 1 86  ? 20.895 -6.607  -27.545 1.00 62.11  ?  242 TYR   A OH  1 
ATOM   566  N  N   . SER   A 1 87  ? 21.725 -7.940  -21.754 1.00 54.16  ?  243 SER   A N   1 
ATOM   567  C  CA  . SER   A 1 87  ? 22.722 -8.777  -22.423 1.00 59.32  ?  243 SER   A CA  1 
ATOM   568  C  C   . SER   A 1 87  ? 24.091 -8.728  -21.748 1.00 56.72  ?  243 SER   A C   1 
ATOM   569  O  O   . SER   A 1 87  ? 25.119 -8.890  -22.412 1.00 59.61  ?  243 SER   A O   1 
ATOM   570  C  CB  . SER   A 1 87  ? 22.855 -8.391  -23.899 1.00 53.34  ?  243 SER   A CB  1 
ATOM   571  O  OG  . SER   A 1 87  ? 23.619 -9.352  -24.605 1.00 68.45  ?  243 SER   A OG  1 
ATOM   572  N  N   . ASN   A 1 88  ? 24.116 -8.509  -20.432 1.00 52.32  ?  244 ASN   A N   1 
ATOM   573  C  CA  . ASN   A 1 88  ? 25.365 -8.414  -19.672 1.00 52.40  ?  244 ASN   A CA  1 
ATOM   574  C  C   . ASN   A 1 88  ? 26.330 -7.404  -20.292 1.00 44.15  ?  244 ASN   A C   1 
ATOM   575  O  O   . ASN   A 1 88  ? 27.548 -7.586  -20.260 1.00 49.39  ?  244 ASN   A O   1 
ATOM   576  C  CB  . ASN   A 1 88  ? 26.035 -9.785  -19.533 1.00 48.81  ?  244 ASN   A CB  1 
ATOM   577  C  CG  . ASN   A 1 88  ? 25.494 -10.583 -18.360 1.00 79.61  ?  244 ASN   A CG  1 
ATOM   578  O  OD1 . ASN   A 1 88  ? 25.191 -10.027 -17.304 1.00 80.80  ?  244 ASN   A OD1 1 
ATOM   579  N  ND2 . ASN   A 1 88  ? 25.372 -11.894 -18.541 1.00 60.24  ?  244 ASN   A ND2 1 
ATOM   580  N  N   . THR   A 1 89  ? 25.785 -6.329  -20.869 1.00 43.76  ?  245 THR   A N   1 
ATOM   581  C  CA  . THR   A 1 89  ? 26.598 -5.281  -21.475 1.00 48.91  ?  245 THR   A CA  1 
ATOM   582  C  C   . THR   A 1 89  ? 27.209 -4.336  -20.450 1.00 42.85  ?  245 THR   A C   1 
ATOM   583  O  O   . THR   A 1 89  ? 28.042 -3.503  -20.828 1.00 43.13  ?  245 THR   A O   1 
ATOM   584  C  CB  . THR   A 1 89  ? 25.764 -4.472  -22.472 1.00 42.23  ?  245 THR   A CB  1 
ATOM   585  O  OG1 . THR   A 1 89  ? 24.598 -3.956  -21.815 1.00 45.16  ?  245 THR   A OG1 1 
ATOM   586  C  CG2 . THR   A 1 89  ? 25.343 -5.343  -23.646 1.00 47.43  ?  245 THR   A CG2 1 
ATOM   587  N  N   . ARG   A 1 90  ? 26.798 -4.435  -19.182 1.00 42.00  ?  246 ARG   A N   1 
ATOM   588  C  CA  . ARG   A 1 90  ? 27.336 -3.665  -18.062 1.00 42.44  ?  246 ARG   A CA  1 
ATOM   589  C  C   . ARG   A 1 90  ? 26.938 -2.194  -18.110 1.00 36.87  ?  246 ARG   A C   1 
ATOM   590  O  O   . ARG   A 1 90  ? 26.925 -1.523  -17.073 1.00 40.42  ?  246 ARG   A O   1 
ATOM   591  C  CB  . ARG   A 1 90  ? 28.863 -3.791  -17.992 1.00 38.75  ?  246 ARG   A CB  1 
ATOM   592  C  CG  . ARG   A 1 90  ? 29.369 -5.219  -18.079 1.00 33.12  ?  246 ARG   A CG  1 
ATOM   593  C  CD  . ARG   A 1 90  ? 28.703 -6.097  -17.034 1.00 40.20  ?  246 ARG   A CD  1 
ATOM   594  N  NE  . ARG   A 1 90  ? 29.610 -6.451  -15.949 1.00 65.98  ?  246 ARG   A NE  1 
ATOM   595  C  CZ  . ARG   A 1 90  ? 29.260 -6.533  -14.672 1.00 71.37  ?  246 ARG   A CZ  1 
ATOM   596  N  NH1 . ARG   A 1 90  ? 28.021 -6.287  -14.276 1.00 64.14  ?  246 ARG   A NH1 1 
ATOM   597  N  NH2 . ARG   A 1 90  ? 30.175 -6.875  -13.770 1.00 67.34  ?  246 ARG   A NH2 1 
ATOM   598  N  N   . ALA   A 1 91  ? 26.599 -1.678  -19.291 1.00 33.76  ?  247 ALA   A N   1 
ATOM   599  C  CA  . ALA   A 1 91  ? 26.300 -0.262  -19.437 1.00 33.24  ?  247 ALA   A CA  1 
ATOM   600  C  C   . ALA   A 1 91  ? 24.894 0.038   -19.931 1.00 39.51  ?  247 ALA   A C   1 
ATOM   601  O  O   . ALA   A 1 91  ? 24.421 1.160   -19.720 1.00 36.35  ?  247 ALA   A O   1 
ATOM   602  C  CB  . ALA   A 1 91  ? 27.308 0.401   -20.389 1.00 32.21  ?  247 ALA   A CB  1 
ATOM   603  N  N   . TYR   A 1 92  ? 24.215 -0.913  -20.567 1.00 36.49  ?  248 TYR   A N   1 
ATOM   604  C  CA  . TYR   A 1 92  ? 22.893 -0.694  -21.139 1.00 40.17  ?  248 TYR   A CA  1 
ATOM   605  C  C   . TYR   A 1 92  ? 21.836 -1.421  -20.316 1.00 39.64  ?  248 TYR   A C   1 
ATOM   606  O  O   . TYR   A 1 92  ? 22.049 -2.556  -19.879 1.00 43.02  ?  248 TYR   A O   1 
ATOM   607  C  CB  . TYR   A 1 92  ? 22.844 -1.163  -22.595 1.00 45.10  ?  248 TYR   A CB  1 
ATOM   608  C  CG  . TYR   A 1 92  ? 23.681 -0.317  -23.524 1.00 39.44  ?  248 TYR   A CG  1 
ATOM   609  C  CD1 . TYR   A 1 92  ? 25.039 -0.563  -23.690 1.00 37.40  ?  248 TYR   A CD1 1 
ATOM   610  C  CD2 . TYR   A 1 92  ? 23.117 0.741   -24.225 1.00 38.74  ?  248 TYR   A CD2 1 
ATOM   611  C  CE1 . TYR   A 1 92  ? 25.808 0.214   -24.536 1.00 38.48  ?  248 TYR   A CE1 1 
ATOM   612  C  CE2 . TYR   A 1 92  ? 23.879 1.524   -25.073 1.00 42.20  ?  248 TYR   A CE2 1 
ATOM   613  C  CZ  . TYR   A 1 92  ? 25.224 1.255   -25.224 1.00 39.91  ?  248 TYR   A CZ  1 
ATOM   614  O  OH  . TYR   A 1 92  ? 25.990 2.029   -26.065 1.00 40.94  ?  248 TYR   A OH  1 
ATOM   615  N  N   . TYR   A 1 93  ? 20.697 -0.761  -20.106 1.00 41.64  ?  249 TYR   A N   1 
ATOM   616  C  CA  . TYR   A 1 93  ? 19.670 -1.277  -19.213 1.00 41.94  ?  249 TYR   A CA  1 
ATOM   617  C  C   . TYR   A 1 93  ? 18.279 -0.980  -19.754 1.00 43.94  ?  249 TYR   A C   1 
ATOM   618  O  O   . TYR   A 1 93  ? 18.065 -0.004  -20.478 1.00 43.98  ?  249 TYR   A O   1 
ATOM   619  C  CB  . TYR   A 1 93  ? 19.790 -0.677  -17.803 1.00 40.78  ?  249 TYR   A CB  1 
ATOM   620  C  CG  . TYR   A 1 93  ? 21.087 -0.986  -17.093 1.00 39.66  ?  249 TYR   A CG  1 
ATOM   621  C  CD1 . TYR   A 1 93  ? 22.243 -0.259  -17.357 1.00 37.13  ?  249 TYR   A CD1 1 
ATOM   622  C  CD2 . TYR   A 1 93  ? 21.154 -1.999  -16.149 1.00 47.51  ?  249 TYR   A CD2 1 
ATOM   623  C  CE1 . TYR   A 1 93  ? 23.428 -0.542  -16.708 1.00 35.62  ?  249 TYR   A CE1 1 
ATOM   624  C  CE2 . TYR   A 1 93  ? 22.332 -2.288  -15.494 1.00 45.16  ?  249 TYR   A CE2 1 
ATOM   625  C  CZ  . TYR   A 1 93  ? 23.465 -1.557  -15.776 1.00 35.94  ?  249 TYR   A CZ  1 
ATOM   626  O  OH  . TYR   A 1 93  ? 24.637 -1.851  -15.118 1.00 46.91  ?  249 TYR   A OH  1 
ATOM   627  N  N   . PHE   A 1 94  ? 17.338 -1.850  -19.394 1.00 46.38  ?  250 PHE   A N   1 
ATOM   628  C  CA  . PHE   A 1 94  ? 15.914 -1.573  -19.485 1.00 48.57  ?  250 PHE   A CA  1 
ATOM   629  C  C   . PHE   A 1 94  ? 15.454 -0.942  -18.178 1.00 55.31  ?  250 PHE   A C   1 
ATOM   630  O  O   . PHE   A 1 94  ? 15.908 -1.329  -17.094 1.00 46.58  ?  250 PHE   A O   1 
ATOM   631  C  CB  . PHE   A 1 94  ? 15.116 -2.852  -19.744 1.00 59.57  ?  250 PHE   A CB  1 
ATOM   632  C  CG  . PHE   A 1 94  ? 15.480 -3.554  -21.018 1.00 57.56  ?  250 PHE   A CG  1 
ATOM   633  C  CD1 . PHE   A 1 94  ? 15.205 -2.981  -22.249 1.00 65.76  ?  250 PHE   A CD1 1 
ATOM   634  C  CD2 . PHE   A 1 94  ? 16.096 -4.794  -20.981 1.00 53.38  ?  250 PHE   A CD2 1 
ATOM   635  C  CE1 . PHE   A 1 94  ? 15.538 -3.633  -23.419 1.00 63.78  ?  250 PHE   A CE1 1 
ATOM   636  C  CE2 . PHE   A 1 94  ? 16.433 -5.449  -22.147 1.00 52.54  ?  250 PHE   A CE2 1 
ATOM   637  C  CZ  . PHE   A 1 94  ? 16.156 -4.867  -23.366 1.00 59.97  ?  250 PHE   A CZ  1 
ATOM   638  N  N   . VAL   A 1 95  ? 14.544 0.017   -18.287 1.00 53.64  ?  251 VAL   A N   1 
ATOM   639  C  CA  . VAL   A 1 95  ? 14.035 0.762   -17.142 1.00 48.15  ?  251 VAL   A CA  1 
ATOM   640  C  C   . VAL   A 1 95  ? 12.630 0.266   -16.833 1.00 55.42  ?  251 VAL   A C   1 
ATOM   641  O  O   . VAL   A 1 95  ? 11.700 0.464   -17.623 1.00 66.04  ?  251 VAL   A O   1 
ATOM   642  C  CB  . VAL   A 1 95  ? 14.039 2.273   -17.403 1.00 48.55  ?  251 VAL   A CB  1 
ATOM   643  C  CG1 . VAL   A 1 95  ? 13.328 3.000   -16.273 1.00 51.83  ?  251 VAL   A CG1 1 
ATOM   644  C  CG2 . VAL   A 1 95  ? 15.465 2.775   -17.548 1.00 50.41  ?  251 VAL   A CG2 1 
ATOM   645  N  N   . LYS   A 1 96  ? 12.560 -0.478  -15.728 1.00 51.85  ?  252 LYS   A N   1 
ATOM   646  C  CA  . LYS   A 1 96  ? 11.249 -0.941  -15.229 1.00 58.78  ?  252 LYS   A CA  1 
ATOM   647  C  C   . LYS   A 1 96  ? 10.945 -0.097  -13.992 1.00 55.48  ?  252 LYS   A C   1 
ATOM   648  O  O   . LYS   A 1 96  ? 11.785 0.743   -13.629 1.00 63.48  ?  252 LYS   A O   1 
ATOM   649  C  CB  . LYS   A 1 96  ? 11.281 -2.421  -14.855 1.00 55.16  ?  252 LYS   A CB  1 
ATOM   650  N  N   . PHE   A 1 97  ? 9.794  -0.312  -13.370 1.00 66.40  ?  253 PHE   A N   1 
ATOM   651  C  CA  . PHE   A 1 97  ? 9.392  0.545   -12.224 1.00 75.36  ?  253 PHE   A CA  1 
ATOM   652  C  C   . PHE   A 1 97  ? 8.982  -0.337  -11.044 1.00 69.47  ?  253 PHE   A C   1 
ATOM   653  O  O   . PHE   A 1 97  ? 8.333  -1.378  -11.241 1.00 57.48  ?  253 PHE   A O   1 
ATOM   654  C  CB  . PHE   A 1 97  ? 8.282  1.492   -12.676 1.00 59.91  ?  253 PHE   A CB  1 
ATOM   655  C  CG  . PHE   A 1 97  ? 8.641  2.547   -13.710 1.00 54.96  ?  253 PHE   A CG  1 
ATOM   656  C  CD1 . PHE   A 1 97  ? 8.583  2.262   -15.067 1.00 55.78  ?  253 PHE   A CD1 1 
ATOM   657  C  CD2 . PHE   A 1 97  ? 8.998  3.829   -13.321 1.00 53.41  ?  253 PHE   A CD2 1 
ATOM   658  C  CE1 . PHE   A 1 97  ? 8.895  3.229   -16.005 1.00 69.46  ?  253 PHE   A CE1 1 
ATOM   659  C  CE2 . PHE   A 1 97  ? 9.305  4.791   -14.264 1.00 66.96  ?  253 PHE   A CE2 1 
ATOM   660  C  CZ  . PHE   A 1 97  ? 9.254  4.489   -15.602 1.00 62.68  ?  253 PHE   A CZ  1 
ATOM   661  N  N   . LYS   A 1 98  ? 9.390  0.063   -9.840  1.00 67.85  ?  254 LYS   A N   1 
ATOM   662  C  CA  . LYS   A 1 98  ? 9.038  -0.700  -8.621  1.00 66.10  ?  254 LYS   A CA  1 
ATOM   663  C  C   . LYS   A 1 98  ? 7.926  0.048   -7.861  1.00 88.96  ?  254 LYS   A C   1 
ATOM   664  O  O   . LYS   A 1 98  ? 6.962  0.496   -8.530  1.00 81.38  ?  254 LYS   A O   1 
ATOM   665  C  CB  . LYS   A 1 98  ? 10.280 -0.892  -7.750  1.00 73.66  ?  254 LYS   A CB  1 
ATOM   666  N  N   . GLU   A 1 103 ? 0.389  6.763   -9.849  1.00 74.20  ?  259 GLU   A N   1 
ATOM   667  C  CA  . GLU   A 1 103 ? 1.598  6.669   -9.039  1.00 84.60  ?  259 GLU   A CA  1 
ATOM   668  C  C   . GLU   A 1 103 ? 2.855  6.674   -9.905  1.00 70.74  ?  259 GLU   A C   1 
ATOM   669  O  O   . GLU   A 1 103 ? 3.972  6.674   -9.389  1.00 78.03  ?  259 GLU   A O   1 
ATOM   670  C  CB  . GLU   A 1 103 ? 1.566  5.407   -8.173  1.00 92.08  ?  259 GLU   A CB  1 
ATOM   671  C  CG  . GLU   A 1 103 ? 0.443  5.378   -7.149  1.00 98.54  ?  259 GLU   A CG  1 
ATOM   672  C  CD  . GLU   A 1 103 ? 0.416  4.086   -6.358  1.00 97.44  ?  259 GLU   A CD  1 
ATOM   673  O  OE1 . GLU   A 1 103 ? 1.255  3.203   -6.637  1.00 106.82 ?  259 GLU   A OE1 1 
ATOM   674  O  OE2 . GLU   A 1 103 ? -0.438 3.953   -5.457  1.00 95.22  -1 259 GLU   A OE2 1 
ATOM   675  N  N   . ASN   A 1 104 ? 2.667  6.680   -11.224 1.00 79.75  ?  260 ASN   A N   1 
ATOM   676  C  CA  . ASN   A 1 104 ? 3.777  6.682   -12.174 1.00 78.26  ?  260 ASN   A CA  1 
ATOM   677  C  C   . ASN   A 1 104 ? 3.453  7.682   -13.278 1.00 69.52  ?  260 ASN   A C   1 
ATOM   678  O  O   . ASN   A 1 104 ? 2.701  7.363   -14.212 1.00 70.15  ?  260 ASN   A O   1 
ATOM   679  C  CB  . ASN   A 1 104 ? 4.022  5.288   -12.747 1.00 76.55  ?  260 ASN   A CB  1 
ATOM   680  C  CG  . ASN   A 1 104 ? 5.192  5.245   -13.722 1.00 73.74  ?  260 ASN   A CG  1 
ATOM   681  O  OD1 . ASN   A 1 104 ? 5.884  6.241   -13.934 1.00 60.85  ?  260 ASN   A OD1 1 
ATOM   682  N  ND2 . ASN   A 1 104 ? 5.421  4.078   -14.311 1.00 71.85  ?  260 ASN   A ND2 1 
ATOM   683  N  N   . PRO   A 1 105 ? 4.007  8.897   -13.210 1.00 65.84  ?  261 PRO   A N   1 
ATOM   684  C  CA  . PRO   A 1 105 ? 3.716  9.898   -14.251 1.00 61.29  ?  261 PRO   A CA  1 
ATOM   685  C  C   . PRO   A 1 105 ? 4.293  9.558   -15.619 1.00 70.43  ?  261 PRO   A C   1 
ATOM   686  O  O   . PRO   A 1 105 ? 3.945  10.235  -16.596 1.00 80.47  ?  261 PRO   A O   1 
ATOM   687  C  CB  . PRO   A 1 105 ? 4.342  11.181  -13.688 1.00 68.90  ?  261 PRO   A CB  1 
ATOM   688  C  CG  . PRO   A 1 105 ? 5.411  10.700  -12.759 1.00 74.96  ?  261 PRO   A CG  1 
ATOM   689  C  CD  . PRO   A 1 105 ? 4.882  9.432   -12.152 1.00 65.27  ?  261 PRO   A CD  1 
ATOM   690  N  N   . LEU   A 1 106 ? 5.161  8.553   -15.722 1.00 73.39  ?  262 LEU   A N   1 
ATOM   691  C  CA  . LEU   A 1 106 ? 5.694  8.102   -17.003 1.00 62.76  ?  262 LEU   A CA  1 
ATOM   692  C  C   . LEU   A 1 106 ? 4.928  6.916   -17.564 1.00 73.56  ?  262 LEU   A C   1 
ATOM   693  O  O   . LEU   A 1 106 ? 5.391  6.285   -18.520 1.00 71.44  ?  262 LEU   A O   1 
ATOM   694  C  CB  . LEU   A 1 106 ? 7.185  7.749   -16.872 1.00 56.55  ?  262 LEU   A CB  1 
ATOM   695  C  CG  . LEU   A 1 106 ? 8.103  8.914   -16.501 1.00 63.28  ?  262 LEU   A CG  1 
ATOM   696  C  CD1 . LEU   A 1 106 ? 9.563  8.479   -16.393 1.00 51.67  ?  262 LEU   A CD1 1 
ATOM   697  C  CD2 . LEU   A 1 106 ? 7.948  10.046  -17.504 1.00 58.93  ?  262 LEU   A CD2 1 
ATOM   698  N  N   . SER   A 1 107 ? 3.771  6.597   -16.978 1.00 73.34  ?  263 SER   A N   1 
ATOM   699  C  CA  . SER   A 1 107 ? 2.982  5.457   -17.431 1.00 66.18  ?  263 SER   A CA  1 
ATOM   700  C  C   . SER   A 1 107 ? 2.563  5.626   -18.880 1.00 67.77  ?  263 SER   A C   1 
ATOM   701  O  O   . SER   A 1 107 ? 2.332  4.636   -19.582 1.00 69.13  ?  263 SER   A O   1 
ATOM   702  C  CB  . SER   A 1 107 ? 1.754  5.278   -16.539 1.00 78.82  ?  263 SER   A CB  1 
ATOM   703  O  OG  . SER   A 1 107 ? 1.009  6.484   -16.480 1.00 73.43  ?  263 SER   A OG  1 
ATOM   704  N  N   . GLN   A 1 108 ? 2.467  6.870   -19.349 1.00 70.67  ?  264 GLN   A N   1 
ATOM   705  C  CA  . GLN   A 1 108 ? 2.086  7.115   -20.736 1.00 73.82  ?  264 GLN   A CA  1 
ATOM   706  C  C   . GLN   A 1 108 ? 3.074  6.521   -21.729 1.00 76.01  ?  264 GLN   A C   1 
ATOM   707  O  O   . GLN   A 1 108 ? 2.724  6.327   -22.896 1.00 69.65  ?  264 GLN   A O   1 
ATOM   708  C  CB  . GLN   A 1 108 ? 1.965  8.616   -20.960 1.00 80.22  ?  264 GLN   A CB  1 
ATOM   709  C  CG  . GLN   A 1 108 ? 1.813  9.404   -19.677 1.00 81.28  ?  264 GLN   A CG  1 
ATOM   710  C  CD  . GLN   A 1 108 ? 1.715  10.892  -19.923 1.00 84.78  ?  264 GLN   A CD  1 
ATOM   711  O  OE1 . GLN   A 1 108 ? 2.076  11.377  -20.992 1.00 81.93  ?  264 GLN   A OE1 1 
ATOM   712  N  NE2 . GLN   A 1 108 ? 1.251  11.630  -18.921 1.00 82.72  ?  264 GLN   A NE2 1 
ATOM   713  N  N   . PHE   A 1 109 ? 4.300  6.235   -21.292 1.00 78.44  ?  265 PHE   A N   1 
ATOM   714  C  CA  . PHE   A 1 109 ? 5.383  5.816   -22.175 1.00 72.46  ?  265 PHE   A CA  1 
ATOM   715  C  C   . PHE   A 1 109 ? 5.760  4.345   -22.001 1.00 68.32  ?  265 PHE   A C   1 
ATOM   716  O  O   . PHE   A 1 109 ? 6.812  3.919   -22.495 1.00 71.20  ?  265 PHE   A O   1 
ATOM   717  C  CB  . PHE   A 1 109 ? 6.620  6.693   -21.962 1.00 61.03  ?  265 PHE   A CB  1 
ATOM   718  C  CG  . PHE   A 1 109 ? 6.336  8.162   -22.030 1.00 70.48  ?  265 PHE   A CG  1 
ATOM   719  C  CD1 . PHE   A 1 109 ? 5.701  8.710   -23.131 1.00 81.74  ?  265 PHE   A CD1 1 
ATOM   720  C  CD2 . PHE   A 1 109 ? 6.715  9.000   -20.999 1.00 70.54  ?  265 PHE   A CD2 1 
ATOM   721  C  CE1 . PHE   A 1 109 ? 5.448  10.059  -23.199 1.00 77.88  ?  265 PHE   A CE1 1 
ATOM   722  C  CE2 . PHE   A 1 109 ? 6.466  10.350  -21.060 1.00 70.15  ?  265 PHE   A CE2 1 
ATOM   723  C  CZ  . PHE   A 1 109 ? 5.830  10.882  -22.163 1.00 69.70  ?  265 PHE   A CZ  1 
ATOM   724  N  N   . LEU   A 1 110 ? 4.944  3.564   -21.297 1.00 66.36  ?  266 LEU   A N   1 
ATOM   725  C  CA  . LEU   A 1 110 ? 5.259  2.157   -21.106 1.00 68.29  ?  266 LEU   A CA  1 
ATOM   726  C  C   . LEU   A 1 110 ? 4.927  1.332   -22.344 1.00 69.98  ?  266 LEU   A C   1 
ATOM   727  O  O   . LEU   A 1 110 ? 3.956  1.593   -23.060 1.00 69.44  ?  266 LEU   A O   1 
ATOM   728  C  CB  . LEU   A 1 110 ? 4.511  1.577   -19.907 1.00 66.42  ?  266 LEU   A CB  1 
ATOM   729  C  CG  . LEU   A 1 110 ? 4.813  2.115   -18.512 1.00 64.74  ?  266 LEU   A CG  1 
ATOM   730  C  CD1 . LEU   A 1 110 ? 3.801  1.562   -17.525 1.00 66.66  ?  266 LEU   A CD1 1 
ATOM   731  C  CD2 . LEU   A 1 110 ? 6.228  1.766   -18.091 1.00 74.95  ?  266 LEU   A CD2 1 
ATOM   732  N  N   . GLU   A 1 111 ? 5.759  0.325   -22.585 1.00 71.47  ?  267 GLU   A N   1 
ATOM   733  C  CA  . GLU   A 1 111 ? 5.513  -0.729  -23.561 1.00 69.46  ?  267 GLU   A CA  1 
ATOM   734  C  C   . GLU   A 1 111 ? 5.630  -2.015  -22.754 1.00 75.10  ?  267 GLU   A C   1 
ATOM   735  O  O   . GLU   A 1 111 ? 6.725  -2.550  -22.571 1.00 73.96  ?  267 GLU   A O   1 
ATOM   736  C  CB  . GLU   A 1 111 ? 6.504  -0.677  -24.730 1.00 73.51  ?  267 GLU   A CB  1 
ATOM   737  N  N   . GLY   A 1 112 ? 4.499  -2.499  -22.252 1.00 70.46  ?  268 GLY   A N   1 
ATOM   738  C  CA  . GLY   A 1 112 ? 4.537  -3.527  -21.236 1.00 70.62  ?  268 GLY   A CA  1 
ATOM   739  C  C   . GLY   A 1 112 ? 4.947  -2.931  -19.905 1.00 68.63  ?  268 GLY   A C   1 
ATOM   740  O  O   . GLY   A 1 112 ? 4.292  -2.008  -19.411 1.00 77.43  ?  268 GLY   A O   1 
ATOM   741  N  N   . GLU   A 1 113 ? 6.036  -3.430  -19.321 1.00 73.09  ?  269 GLU   A N   1 
ATOM   742  C  CA  . GLU   A 1 113 ? 6.553  -2.898  -18.066 1.00 83.98  ?  269 GLU   A CA  1 
ATOM   743  C  C   . GLU   A 1 113 ? 7.789  -2.024  -18.246 1.00 70.27  ?  269 GLU   A C   1 
ATOM   744  O  O   . GLU   A 1 113 ? 8.291  -1.477  -17.259 1.00 73.52  ?  269 GLU   A O   1 
ATOM   745  C  CB  . GLU   A 1 113 ? 6.881  -4.036  -17.094 1.00 88.08  ?  269 GLU   A CB  1 
ATOM   746  C  CG  . GLU   A 1 113 ? 5.777  -5.060  -16.909 1.00 81.96  ?  269 GLU   A CG  1 
ATOM   747  C  CD  . GLU   A 1 113 ? 6.286  -6.483  -17.024 1.00 95.63  ?  269 GLU   A CD  1 
ATOM   748  O  OE1 . GLU   A 1 113 ? 6.945  -6.805  -18.036 1.00 89.07  ?  269 GLU   A OE1 1 
ATOM   749  O  OE2 . GLU   A 1 113 ? 6.038  -7.277  -16.093 1.00 110.37 -1 269 GLU   A OE2 1 
ATOM   750  N  N   . ILE   A 1 114 ? 8.288  -1.873  -19.470 1.00 69.97  ?  270 ILE   A N   1 
ATOM   751  C  CA  . ILE   A 1 114 ? 9.522  -1.141  -19.735 1.00 63.20  ?  270 ILE   A CA  1 
ATOM   752  C  C   . ILE   A 1 114 ? 9.165  0.266   -20.195 1.00 67.47  ?  270 ILE   A C   1 
ATOM   753  O  O   . ILE   A 1 114 ? 8.256  0.447   -21.015 1.00 65.27  ?  270 ILE   A O   1 
ATOM   754  C  CB  . ILE   A 1 114 ? 10.389 -1.872  -20.780 1.00 70.69  ?  270 ILE   A CB  1 
ATOM   755  C  CG1 . ILE   A 1 114 ? 11.465 -2.724  -20.097 1.00 73.83  ?  270 ILE   A CG1 1 
ATOM   756  C  CG2 . ILE   A 1 114 ? 11.033 -0.897  -21.765 1.00 76.73  ?  270 ILE   A CG2 1 
ATOM   757  C  CD1 . ILE   A 1 114 ? 10.938 -3.659  -19.032 1.00 59.57  ?  270 ILE   A CD1 1 
ATOM   758  N  N   . LEU   A 1 115 ? 9.852  1.263   -19.641 1.00 58.15  ?  271 LEU   A N   1 
ATOM   759  C  CA  . LEU   A 1 115 ? 9.765  2.616   -20.171 1.00 64.07  ?  271 LEU   A CA  1 
ATOM   760  C  C   . LEU   A 1 115 ? 10.325 2.629   -21.587 1.00 56.99  ?  271 LEU   A C   1 
ATOM   761  O  O   . LEU   A 1 115 ? 11.490 2.283   -21.805 1.00 64.38  ?  271 LEU   A O   1 
ATOM   762  C  CB  . LEU   A 1 115 ? 10.540 3.584   -19.276 1.00 53.48  ?  271 LEU   A CB  1 
ATOM   763  C  CG  . LEU   A 1 115 ? 10.262 5.095   -19.301 1.00 70.95  ?  271 LEU   A CG  1 
ATOM   764  C  CD1 . LEU   A 1 115 ? 11.270 5.829   -18.431 1.00 53.91  ?  271 LEU   A CD1 1 
ATOM   765  C  CD2 . LEU   A 1 115 ? 10.269 5.687   -20.704 1.00 75.42  ?  271 LEU   A CD2 1 
ATOM   766  N  N   . SER   A 1 116 ? 9.501  3.032   -22.549 1.00 62.86  ?  272 SER   A N   1 
ATOM   767  C  CA  . SER   A 1 116 ? 9.945  3.103   -23.934 1.00 64.19  ?  272 SER   A CA  1 
ATOM   768  C  C   . SER   A 1 116 ? 10.688 4.413   -24.167 1.00 64.26  ?  272 SER   A C   1 
ATOM   769  O  O   . SER   A 1 116 ? 10.103 5.495   -24.045 1.00 65.64  ?  272 SER   A O   1 
ATOM   770  C  CB  . SER   A 1 116 ? 8.759  2.983   -24.888 1.00 64.41  ?  272 SER   A CB  1 
ATOM   771  O  OG  . SER   A 1 116 ? 9.101  3.424   -26.192 1.00 61.81  ?  272 SER   A OG  1 
ATOM   772  N  N   . ALA   A 1 117 ? 11.977 4.318   -24.506 1.00 54.71  ?  273 ALA   A N   1 
ATOM   773  C  CA  . ALA   A 1 117 ? 12.715 5.511   -24.906 1.00 58.79  ?  273 ALA   A CA  1 
ATOM   774  C  C   . ALA   A 1 117 ? 12.106 6.145   -26.149 1.00 66.62  ?  273 ALA   A C   1 
ATOM   775  O  O   . ALA   A 1 117 ? 12.116 7.373   -26.290 1.00 65.02  ?  273 ALA   A O   1 
ATOM   776  C  CB  . ALA   A 1 117 ? 14.184 5.167   -25.150 1.00 52.80  ?  273 ALA   A CB  1 
ATOM   777  N  N   . SER   A 1 118 ? 11.544 5.326   -27.041 1.00 61.58  ?  274 SER   A N   1 
ATOM   778  C  CA  . SER   A 1 118 ? 10.961 5.841   -28.276 1.00 63.29  ?  274 SER   A CA  1 
ATOM   779  C  C   . SER   A 1 118 ? 9.801  6.791   -27.993 1.00 59.26  ?  274 SER   A C   1 
ATOM   780  O  O   . SER   A 1 118 ? 9.787  7.929   -28.476 1.00 66.13  ?  274 SER   A O   1 
ATOM   781  C  CB  . SER   A 1 118 ? 10.507 4.679   -29.159 1.00 66.46  ?  274 SER   A CB  1 
ATOM   782  O  OG  . SER   A 1 118 ? 10.039 3.595   -28.375 1.00 81.97  ?  274 SER   A OG  1 
ATOM   783  N  N   . LYS   A 1 119 ? 8.820  6.343   -27.206 1.00 61.26  ?  275 LYS   A N   1 
ATOM   784  C  CA  . LYS   A 1 119 ? 7.640  7.167   -26.943 1.00 62.38  ?  275 LYS   A CA  1 
ATOM   785  C  C   . LYS   A 1 119 ? 7.999  8.400   -26.121 1.00 60.74  ?  275 LYS   A C   1 
ATOM   786  O  O   . LYS   A 1 119 ? 7.538  9.516   -26.412 1.00 74.18  ?  275 LYS   A O   1 
ATOM   787  C  CB  . LYS   A 1 119 ? 6.575  6.336   -26.227 1.00 64.16  ?  275 LYS   A CB  1 
ATOM   788  N  N   . MET   A 1 120 ? 8.813  8.212   -25.079 1.00 72.68  ?  276 MET   A N   1 
ATOM   789  C  CA  . MET   A 1 120 ? 9.221  9.331   -24.240 1.00 62.72  ?  276 MET   A CA  1 
ATOM   790  C  C   . MET   A 1 120 ? 9.944  10.392  -25.056 1.00 61.01  ?  276 MET   A C   1 
ATOM   791  O  O   . MET   A 1 120 ? 9.651  11.586  -24.932 1.00 76.48  ?  276 MET   A O   1 
ATOM   792  C  CB  . MET   A 1 120 ? 10.108 8.834   -23.097 1.00 62.47  ?  276 MET   A CB  1 
ATOM   793  C  CG  . MET   A 1 120 ? 10.417 9.890   -22.048 1.00 59.99  ?  276 MET   A CG  1 
ATOM   794  S  SD  . MET   A 1 120 ? 11.100 9.184   -20.535 1.00 58.94  ?  276 MET   A SD  1 
ATOM   795  C  CE  . MET   A 1 120 ? 11.179 10.630  -19.479 1.00 50.38  ?  276 MET   A CE  1 
ATOM   796  N  N   . LEU   A 1 121 ? 10.879 9.973   -25.914 1.00 63.26  ?  277 LEU   A N   1 
ATOM   797  C  CA  . LEU   A 1 121 ? 11.601 10.933  -26.741 1.00 69.41  ?  277 LEU   A CA  1 
ATOM   798  C  C   . LEU   A 1 121 ? 10.699 11.573  -27.787 1.00 69.22  ?  277 LEU   A C   1 
ATOM   799  O  O   . LEU   A 1 121 ? 10.875 12.755  -28.104 1.00 71.44  ?  277 LEU   A O   1 
ATOM   800  C  CB  . LEU   A 1 121 ? 12.795 10.258  -27.414 1.00 69.97  ?  277 LEU   A CB  1 
ATOM   801  C  CG  . LEU   A 1 121 ? 14.029 9.996   -26.550 1.00 55.17  ?  277 LEU   A CG  1 
ATOM   802  C  CD1 . LEU   A 1 121 ? 15.103 9.304   -27.371 1.00 59.07  ?  277 LEU   A CD1 1 
ATOM   803  C  CD2 . LEU   A 1 121 ? 14.554 11.295  -25.967 1.00 58.71  ?  277 LEU   A CD2 1 
ATOM   804  N  N   . SER   A 1 122 ? 9.741  10.820  -28.339 1.00 75.58  ?  278 SER   A N   1 
ATOM   805  C  CA  . SER   A 1 122 ? 8.792  11.401  -29.285 1.00 63.38  ?  278 SER   A CA  1 
ATOM   806  C  C   . SER   A 1 122 ? 8.035  12.557  -28.647 1.00 67.37  ?  278 SER   A C   1 
ATOM   807  O  O   . SER   A 1 122 ? 7.954  13.655  -29.214 1.00 68.40  ?  278 SER   A O   1 
ATOM   808  C  CB  . SER   A 1 122 ? 7.817  10.328  -29.776 1.00 65.25  ?  278 SER   A CB  1 
ATOM   809  O  OG  . SER   A 1 122 ? 8.480  9.339   -30.544 1.00 84.04  ?  278 SER   A OG  1 
ATOM   810  N  N   . LYS   A 1 123 ? 7.491  12.328  -27.448 1.00 63.69  ?  279 LYS   A N   1 
ATOM   811  C  CA  . LYS   A 1 123 ? 6.774  13.387  -26.740 1.00 65.28  ?  279 LYS   A CA  1 
ATOM   812  C  C   . LYS   A 1 123 ? 7.704  14.536  -26.359 1.00 74.13  ?  279 LYS   A C   1 
ATOM   813  O  O   . LYS   A 1 123 ? 7.332  15.710  -26.489 1.00 67.00  ?  279 LYS   A O   1 
ATOM   814  C  CB  . LYS   A 1 123 ? 6.092  12.817  -25.497 1.00 72.44  ?  279 LYS   A CB  1 
ATOM   815  N  N   . PHE   A 1 124 ? 8.908  14.217  -25.873 1.00 78.07  ?  280 PHE   A N   1 
ATOM   816  C  CA  . PHE   A 1 124 ? 9.881  15.243  -25.508 1.00 58.88  ?  280 PHE   A CA  1 
ATOM   817  C  C   . PHE   A 1 124 ? 10.167 16.170  -26.684 1.00 62.54  ?  280 PHE   A C   1 
ATOM   818  O  O   . PHE   A 1 124 ? 10.137 17.397  -26.546 1.00 64.95  ?  280 PHE   A O   1 
ATOM   819  C  CB  . PHE   A 1 124 ? 11.162 14.565  -25.007 1.00 75.95  ?  280 PHE   A CB  1 
ATOM   820  C  CG  . PHE   A 1 124 ? 12.234 15.520  -24.550 1.00 60.05  ?  280 PHE   A CG  1 
ATOM   821  C  CD1 . PHE   A 1 124 ? 12.190 16.080  -23.284 1.00 66.80  ?  280 PHE   A CD1 1 
ATOM   822  C  CD2 . PHE   A 1 124 ? 13.306 15.825  -25.374 1.00 71.08  ?  280 PHE   A CD2 1 
ATOM   823  C  CE1 . PHE   A 1 124 ? 13.182 16.948  -22.857 1.00 64.70  ?  280 PHE   A CE1 1 
ATOM   824  C  CE2 . PHE   A 1 124 ? 14.300 16.690  -24.954 1.00 63.80  ?  280 PHE   A CE2 1 
ATOM   825  C  CZ  . PHE   A 1 124 ? 14.238 17.253  -23.694 1.00 64.72  ?  280 PHE   A CZ  1 
ATOM   826  N  N   . ARG   A 1 125 ? 10.430 15.591  -27.858 1.00 64.45  ?  281 ARG   A N   1 
ATOM   827  C  CA  . ARG   A 1 125 ? 10.648 16.387  -29.062 1.00 69.26  ?  281 ARG   A CA  1 
ATOM   828  C  C   . ARG   A 1 125 ? 9.410  17.201  -29.416 1.00 83.30  ?  281 ARG   A C   1 
ATOM   829  O  O   . ARG   A 1 125 ? 9.509  18.388  -29.762 1.00 90.42  ?  281 ARG   A O   1 
ATOM   830  C  CB  . ARG   A 1 125 ? 11.024 15.461  -30.216 1.00 66.91  ?  281 ARG   A CB  1 
ATOM   831  C  CG  . ARG   A 1 125 ? 12.187 15.921  -31.067 1.00 74.62  ?  281 ARG   A CG  1 
ATOM   832  C  CD  . ARG   A 1 125 ? 12.548 14.834  -32.063 1.00 73.04  ?  281 ARG   A CD  1 
ATOM   833  N  NE  . ARG   A 1 125 ? 12.235 13.509  -31.538 1.00 85.77  ?  281 ARG   A NE  1 
ATOM   834  C  CZ  . ARG   A 1 125 ? 13.057 12.782  -30.792 1.00 82.66  ?  281 ARG   A CZ  1 
ATOM   835  N  NH1 . ARG   A 1 125 ? 14.267 13.212  -30.474 1.00 71.14  ?  281 ARG   A NH1 1 
ATOM   836  N  NH2 . ARG   A 1 125 ? 12.653 11.592  -30.356 1.00 88.92  ?  281 ARG   A NH2 1 
ATOM   837  N  N   . LYS   A 1 126 ? 8.235  16.583  -29.291 1.00 79.87  ?  282 LYS   A N   1 
ATOM   838  C  CA  . LYS   A 1 126 ? 6.968  17.306  -29.576 1.00 69.66  ?  282 LYS   A CA  1 
ATOM   839  C  C   . LYS   A 1 126 ? 6.953  18.643  -28.824 1.00 80.82  ?  282 LYS   A C   1 
ATOM   840  O  O   . LYS   A 1 126 ? 6.787  19.680  -29.487 1.00 81.63  ?  282 LYS   A O   1 
ATOM   841  C  CB  . LYS   A 1 126 ? 5.754  16.476  -29.153 1.00 77.43  ?  282 LYS   A CB  1 
ATOM   842  N  N   . ILE   A 1 127 ? 7.107  18.611  -27.497 1.00 77.47  ?  283 ILE   A N   1 
ATOM   843  C  CA  . ILE   A 1 127 ? 7.015  19.875  -26.711 1.00 71.83  ?  283 ILE   A CA  1 
ATOM   844  C  C   . ILE   A 1 127 ? 8.074  20.833  -27.259 1.00 74.05  ?  283 ILE   A C   1 
ATOM   845  O  O   . ILE   A 1 127 ? 7.709  21.936  -27.703 1.00 74.38  ?  283 ILE   A O   1 
ATOM   846  C  CB  . ILE   A 1 127 ? 7.198  19.631  -25.206 1.00 67.77  ?  283 ILE   A CB  1 
ATOM   847  C  CG1 . ILE   A 1 127 ? 6.791  18.217  -24.799 1.00 67.18  ?  283 ILE   A CG1 1 
ATOM   848  C  CG2 . ILE   A 1 127 ? 6.456  20.688  -24.391 1.00 62.54  ?  283 ILE   A CG2 1 
ATOM   849  C  CD1 . ILE   A 1 127 ? 5.298  18.018  -24.629 1.00 73.24  ?  283 ILE   A CD1 1 
ATOM   850  N  N   . ILE   A 1 128 ? 9.331  20.410  -27.233 1.00 72.44  ?  284 ILE   A N   1 
ATOM   851  C  CA  . ILE   A 1 128 ? 10.411 21.257  -27.807 1.00 81.21  ?  284 ILE   A CA  1 
ATOM   852  C  C   . ILE   A 1 128 ? 9.827  21.972  -29.036 1.00 71.79  ?  284 ILE   A C   1 
ATOM   853  O  O   . ILE   A 1 128 ? 10.099 23.181  -29.172 1.00 74.35  ?  284 ILE   A O   1 
ATOM   854  C  CB  . ILE   A 1 128 ? 11.656 20.417  -28.162 1.00 79.84  ?  284 ILE   A CB  1 
ATOM   855  C  CG1 . ILE   A 1 128 ? 12.169 19.578  -26.987 1.00 72.89  ?  284 ILE   A CG1 1 
ATOM   856  C  CG2 . ILE   A 1 128 ? 12.765 21.296  -28.740 1.00 85.54  ?  284 ILE   A CG2 1 
ATOM   857  C  CD1 . ILE   A 1 128 ? 12.368 20.339  -25.691 1.00 68.80  ?  284 ILE   A CD1 1 
ATOM   858  N  N   . MET   A 1 142 ? 15.240 24.427  -35.197 1.00 69.00  ?  298 MET   A N   1 
ATOM   859  C  CA  . MET   A 1 142 ? 15.263 23.101  -34.530 1.00 74.57  ?  298 MET   A CA  1 
ATOM   860  C  C   . MET   A 1 142 ? 15.608 22.023  -35.564 1.00 82.44  ?  298 MET   A C   1 
ATOM   861  O  O   . MET   A 1 142 ? 15.444 22.296  -36.771 1.00 75.74  ?  298 MET   A O   1 
ATOM   862  C  CB  . MET   A 1 142 ? 13.915 22.782  -33.875 1.00 65.83  ?  298 MET   A CB  1 
ATOM   863  C  CG  . MET   A 1 142 ? 13.965 21.670  -32.856 1.00 79.36  ?  298 MET   A CG  1 
ATOM   864  S  SD  . MET   A 1 142 ? 12.526 20.596  -32.983 1.00 105.38 ?  298 MET   A SD  1 
ATOM   865  C  CE  . MET   A 1 142 ? 13.164 19.247  -33.986 1.00 76.73  ?  298 MET   A CE  1 
ATOM   866  N  N   . LYS   A 1 143 ? 16.066 20.855  -35.107 1.00 78.99  ?  299 LYS   A N   1 
ATOM   867  C  CA  . LYS   A 1 143 ? 16.468 19.763  -36.034 1.00 82.13  ?  299 LYS   A CA  1 
ATOM   868  C  C   . LYS   A 1 143 ? 16.498 18.425  -35.287 1.00 86.43  ?  299 LYS   A C   1 
ATOM   869  O  O   . LYS   A 1 143 ? 16.445 18.443  -34.042 1.00 86.28  ?  299 LYS   A O   1 
ATOM   870  C  CB  . LYS   A 1 143 ? 17.831 20.035  -36.681 1.00 70.71  ?  299 LYS   A CB  1 
ATOM   871  N  N   . ARG   A 1 144 ? 16.582 17.319  -36.025 1.00 82.30  ?  300 ARG   A N   1 
ATOM   872  C  CA  . ARG   A 1 144 ? 16.579 15.996  -35.441 1.00 71.38  ?  300 ARG   A CA  1 
ATOM   873  C  C   . ARG   A 1 144 ? 17.521 15.858  -34.235 1.00 75.97  ?  300 ARG   A C   1 
ATOM   874  O  O   . ARG   A 1 144 ? 17.913 14.743  -33.853 1.00 91.08  ?  300 ARG   A O   1 
ATOM   875  C  CB  . ARG   A 1 144 ? 16.956 14.985  -36.522 1.00 66.27  ?  300 ARG   A CB  1 
ATOM   876  N  N   . GLY   A 1 148 ? 18.979 9.212   -30.899 1.00 57.64  ?  304 GLY   A N   1 
ATOM   877  C  CA  . GLY   A 1 148 ? 18.725 8.910   -29.513 1.00 58.54  ?  304 GLY   A CA  1 
ATOM   878  C  C   . GLY   A 1 148 ? 19.108 10.031  -28.564 1.00 55.08  ?  304 GLY   A C   1 
ATOM   879  O  O   . GLY   A 1 148 ? 18.283 10.881  -28.237 1.00 52.72  ?  304 GLY   A O   1 
ATOM   880  N  N   . SER   A 1 149 ? 20.365 10.033  -28.131 1.00 52.45  ?  305 SER   A N   1 
ATOM   881  C  CA  . SER   A 1 149 ? 20.865 11.045  -27.210 1.00 57.43  ?  305 SER   A CA  1 
ATOM   882  C  C   . SER   A 1 149 ? 21.820 12.000  -27.925 1.00 74.69  ?  305 SER   A C   1 
ATOM   883  O  O   . SER   A 1 149 ? 21.494 13.175  -28.141 1.00 86.86  ?  305 SER   A O   1 
ATOM   884  C  CB  . SER   A 1 149 ? 21.569 10.399  -26.010 1.00 48.20  ?  305 SER   A CB  1 
ATOM   885  O  OG  . SER   A 1 149 ? 20.635 9.842   -25.100 1.00 53.66  ?  305 SER   A OG  1 
ATOM   886  N  N   . ALA   A 1 151 ? 19.084 14.267  -28.710 1.00 59.84  ?  307 ALA   A N   1 
ATOM   887  C  CA  . ALA   A 1 151 ? 17.694 14.135  -29.084 1.00 74.78  ?  307 ALA   A CA  1 
ATOM   888  C  C   . ALA   A 1 151 ? 17.234 15.361  -29.864 1.00 79.46  ?  307 ALA   A C   1 
ATOM   889  O  O   . ALA   A 1 151 ? 16.471 15.223  -30.808 1.00 75.35  ?  307 ALA   A O   1 
ATOM   890  C  CB  . ALA   A 1 151 ? 16.822 13.910  -27.853 1.00 57.03  ?  307 ALA   A CB  1 
ATOM   891  N  N   . VAL   A 1 152 ? 17.689 16.563  -29.523 1.00 67.95  ?  308 VAL   A N   1 
ATOM   892  C  CA  . VAL   A 1 152 ? 17.262 17.687  -30.352 1.00 75.42  ?  308 VAL   A CA  1 
ATOM   893  C  C   . VAL   A 1 152 ? 18.400 18.683  -30.517 1.00 79.77  ?  308 VAL   A C   1 
ATOM   894  O  O   . VAL   A 1 152 ? 19.129 18.975  -29.569 1.00 80.07  ?  308 VAL   A O   1 
ATOM   895  C  CB  . VAL   A 1 152 ? 15.998 18.355  -29.779 1.00 66.32  ?  308 VAL   A CB  1 
ATOM   896  N  N   . THR   A 1 153 ? 18.542 19.210  -31.732 1.00 81.28  ?  309 THR   A N   1 
ATOM   897  C  CA  . THR   A 1 153 ? 19.510 20.259  -32.036 1.00 67.79  ?  309 THR   A CA  1 
ATOM   898  C  C   . THR   A 1 153 ? 18.766 21.533  -32.403 1.00 67.51  ?  309 THR   A C   1 
ATOM   899  O  O   . THR   A 1 153 ? 18.117 21.593  -33.454 1.00 80.07  ?  309 THR   A O   1 
ATOM   900  C  CB  . THR   A 1 153 ? 20.433 19.880  -33.191 1.00 71.38  ?  309 THR   A CB  1 
ATOM   901  O  OG1 . THR   A 1 153 ? 21.101 18.659  -32.887 1.00 78.23  ?  309 THR   A OG1 1 
ATOM   902  C  CG2 . THR   A 1 153 ? 21.458 20.960  -33.389 1.00 68.45  ?  309 THR   A CG2 1 
ATOM   903  N  N   . LEU   A 1 154 ? 18.886 22.549  -31.553 1.00 59.11  ?  310 LEU   A N   1 
ATOM   904  C  CA  . LEU   A 1 154 ? 18.247 23.840  -31.749 1.00 67.21  ?  310 LEU   A CA  1 
ATOM   905  C  C   . LEU   A 1 154 ? 19.286 24.845  -32.221 1.00 64.70  ?  310 LEU   A C   1 
ATOM   906  O  O   . LEU   A 1 154 ? 20.457 24.765  -31.839 1.00 62.01  ?  310 LEU   A O   1 
ATOM   907  C  CB  . LEU   A 1 154 ? 17.610 24.331  -30.447 1.00 68.48  ?  310 LEU   A CB  1 
ATOM   908  C  CG  . LEU   A 1 154 ? 17.059 23.306  -29.454 1.00 70.05  ?  310 LEU   A CG  1 
ATOM   909  C  CD1 . LEU   A 1 154 ? 16.438 24.025  -28.277 1.00 70.59  ?  310 LEU   A CD1 1 
ATOM   910  C  CD2 . LEU   A 1 154 ? 16.037 22.377  -30.098 1.00 85.48  ?  310 LEU   A CD2 1 
ATOM   911  N  N   . LEU   A 1 155 ? 18.876 25.828  -33.031 1.00 81.58  ?  311 LEU   A N   1 
ATOM   912  C  CA  . LEU   A 1 155 ? 19.814 26.904  -33.476 1.00 77.39  ?  311 LEU   A CA  1 
ATOM   913  C  C   . LEU   A 1 155 ? 19.341 28.250  -32.898 1.00 70.57  ?  311 LEU   A C   1 
ATOM   914  O  O   . LEU   A 1 155 ? 18.120 28.476  -32.875 1.00 71.97  ?  311 LEU   A O   1 
ATOM   915  C  CB  . LEU   A 1 155 ? 19.991 26.972  -34.992 1.00 66.05  ?  311 LEU   A CB  1 
ATOM   916  C  CG  . LEU   A 1 155 ? 21.016 27.991  -35.495 1.00 80.24  ?  311 LEU   A CG  1 
ATOM   917  C  CD1 . LEU   A 1 155 ? 22.033 27.344  -36.414 1.00 74.51  ?  311 LEU   A CD1 1 
ATOM   918  C  CD2 . LEU   A 1 155 ? 20.338 29.163  -36.181 1.00 69.64  ?  311 LEU   A CD2 1 
ATOM   919  N  N   . ILE   A 1 156 ? 20.264 29.100  -32.455 1.00 73.07  ?  312 ILE   A N   1 
ATOM   920  C  CA  . ILE   A 1 156 ? 19.860 30.351  -31.752 1.00 65.69  ?  312 ILE   A CA  1 
ATOM   921  C  C   . ILE   A 1 156 ? 21.000 31.365  -31.853 1.00 73.94  ?  312 ILE   A C   1 
ATOM   922  O  O   . ILE   A 1 156 ? 21.976 31.044  -32.553 1.00 95.86  ?  312 ILE   A O   1 
ATOM   923  C  CB  . ILE   A 1 156 ? 19.540 30.034  -30.283 1.00 58.48  ?  312 ILE   A CB  1 
ATOM   924  N  N   . GLU   A 1 158 ? 21.871 32.641  -35.556 1.00 70.15  ?  314 GLU   A N   1 
ATOM   925  C  CA  . GLU   A 1 158 ? 22.383 32.013  -36.800 1.00 66.58  ?  314 GLU   A CA  1 
ATOM   926  C  C   . GLU   A 1 158 ? 23.624 31.161  -36.522 1.00 72.78  ?  314 GLU   A C   1 
ATOM   927  O  O   . GLU   A 1 158 ? 23.875 30.223  -37.303 1.00 82.74  ?  314 GLU   A O   1 
ATOM   928  C  CB  . GLU   A 1 158 ? 22.826 33.064  -37.814 1.00 79.57  ?  314 GLU   A CB  1 
ATOM   929  N  N   . LYS   A 1 159 ? 24.361 31.458  -35.456 1.00 70.60  ?  315 LYS   A N   1 
ATOM   930  C  CA  . LYS   A 1 159 ? 25.642 30.745  -35.219 1.00 78.39  ?  315 LYS   A CA  1 
ATOM   931  C  C   . LYS   A 1 159 ? 25.588 29.731  -34.069 1.00 80.28  ?  315 LYS   A C   1 
ATOM   932  O  O   . LYS   A 1 159 ? 26.398 28.786  -34.086 1.00 77.91  ?  315 LYS   A O   1 
ATOM   933  C  CB  . LYS   A 1 159 ? 26.691 31.790  -34.829 1.00 75.00  ?  315 LYS   A CB  1 
ATOM   934  N  N   . ILE   A 1 160 ? 24.694 29.911  -33.104 1.00 75.43  ?  316 ILE   A N   1 
ATOM   935  C  CA  . ILE   A 1 160 ? 24.752 29.032  -31.902 1.00 69.51  ?  316 ILE   A CA  1 
ATOM   936  C  C   . ILE   A 1 160 ? 23.935 27.758  -32.093 1.00 70.89  ?  316 ILE   A C   1 
ATOM   937  O  O   . ILE   A 1 160 ? 22.774 27.866  -32.502 1.00 72.28  ?  316 ILE   A O   1 
ATOM   938  C  CB  . ILE   A 1 160 ? 24.300 29.796  -30.646 1.00 57.39  ?  316 ILE   A CB  1 
ATOM   939  N  N   . SER   A 1 161 ? 24.537 26.606  -31.799 1.00 73.43  ?  317 SER   A N   1 
ATOM   940  C  CA  . SER   A 1 161 ? 23.798 25.354  -31.794 1.00 76.61  ?  317 SER   A CA  1 
ATOM   941  C  C   . SER   A 1 161 ? 23.761 24.785  -30.382 1.00 70.17  ?  317 SER   A C   1 
ATOM   942  O  O   . SER   A 1 161 ? 24.692 24.969  -29.593 1.00 65.10  ?  317 SER   A O   1 
ATOM   943  C  CB  . SER   A 1 161 ? 24.402 24.327  -32.759 1.00 73.07  ?  317 SER   A CB  1 
ATOM   944  O  OG  . SER   A 1 161 ? 24.913 24.945  -33.930 1.00 83.75  ?  317 SER   A OG  1 
ATOM   945  N  N   . VAL   A 1 162 ? 22.658 24.108  -30.067 1.00 64.27  ?  318 VAL   A N   1 
ATOM   946  C  CA  . VAL   A 1 162 ? 22.409 23.550  -28.742 1.00 64.18  ?  318 VAL   A CA  1 
ATOM   947  C  C   . VAL   A 1 162 ? 21.855 22.146  -28.915 1.00 66.12  ?  318 VAL   A C   1 
ATOM   948  O  O   . VAL   A 1 162 ? 20.731 21.978  -29.400 1.00 67.02  ?  318 VAL   A O   1 
ATOM   949  C  CB  . VAL   A 1 162 ? 21.416 24.399  -27.927 1.00 65.50  ?  318 VAL   A CB  1 
ATOM   950  C  CG1 . VAL   A 1 162 ? 21.262 23.827  -26.521 1.00 53.26  ?  318 VAL   A CG1 1 
ATOM   951  C  CG2 . VAL   A 1 162 ? 21.850 25.850  -27.875 1.00 73.44  ?  318 VAL   A CG2 1 
ATOM   952  N  N   . ASP   A 1 163 ? 22.624 21.146  -28.505 1.00 59.19  ?  319 ASP   A N   1 
ATOM   953  C  CA  . ASP   A 1 163 ? 22.135 19.775  -28.484 1.00 64.46  ?  319 ASP   A CA  1 
ATOM   954  C  C   . ASP   A 1 163 ? 21.563 19.479  -27.104 1.00 52.61  ?  319 ASP   A C   1 
ATOM   955  O  O   . ASP   A 1 163 ? 22.248 19.652  -26.091 1.00 61.96  ?  319 ASP   A O   1 
ATOM   956  C  CB  . ASP   A 1 163 ? 23.249 18.795  -28.843 1.00 61.67  ?  319 ASP   A CB  1 
ATOM   957  C  CG  . ASP   A 1 163 ? 23.899 19.117  -30.174 1.00 78.32  ?  319 ASP   A CG  1 
ATOM   958  O  OD1 . ASP   A 1 163 ? 24.522 20.195  -30.288 1.00 80.08  ?  319 ASP   A OD1 1 
ATOM   959  O  OD2 . ASP   A 1 163 ? 23.785 18.295  -31.107 1.00 75.79  -1 319 ASP   A OD2 1 
ATOM   960  N  N   . ILE   A 1 164 ? 20.305 19.048  -27.063 1.00 73.04  ?  320 ILE   A N   1 
ATOM   961  C  CA  . ILE   A 1 164 ? 19.639 18.661  -25.828 1.00 51.98  ?  320 ILE   A CA  1 
ATOM   962  C  C   . ILE   A 1 164 ? 19.464 17.149  -25.807 1.00 51.47  ?  320 ILE   A C   1 
ATOM   963  O  O   . ILE   A 1 164 ? 18.962 16.545  -26.774 1.00 66.26  ?  320 ILE   A O   1 
ATOM   964  C  CB  . ILE   A 1 164 ? 18.291 19.375  -25.641 1.00 58.14  ?  320 ILE   A CB  1 
ATOM   965  C  CG1 . ILE   A 1 164 ? 18.525 20.834  -25.276 1.00 61.50  ?  320 ILE   A CG1 1 
ATOM   966  C  CG2 . ILE   A 1 164 ? 17.517 18.734  -24.510 1.00 63.02  ?  320 ILE   A CG2 1 
ATOM   967  C  CD1 . ILE   A 1 164 ? 17.484 21.760  -25.810 1.00 61.03  ?  320 ILE   A CD1 1 
ATOM   968  N  N   . THR   A 1 165 ? 19.886 16.560  -24.686 1.00 49.24  ?  321 THR   A N   1 
ATOM   969  C  CA  . THR   A 1 165 ? 19.788 15.152  -24.335 1.00 64.56  ?  321 THR   A CA  1 
ATOM   970  C  C   . THR   A 1 165 ? 18.862 15.013  -23.135 1.00 51.47  ?  321 THR   A C   1 
ATOM   971  O  O   . THR   A 1 165 ? 18.984 15.766  -22.164 1.00 44.50  ?  321 THR   A O   1 
ATOM   972  C  CB  . THR   A 1 165 ? 21.164 14.599  -23.944 1.00 54.52  ?  321 THR   A CB  1 
ATOM   973  O  OG1 . THR   A 1 165 ? 22.054 14.627  -25.063 1.00 51.52  ?  321 THR   A OG1 1 
ATOM   974  C  CG2 . THR   A 1 165 ? 21.066 13.177  -23.392 1.00 40.30  ?  321 THR   A CG2 1 
ATOM   975  N  N   . LEU   A 1 166 ? 17.969 14.028  -23.185 1.00 63.71  ?  322 LEU   A N   1 
ATOM   976  C  CA  . LEU   A 1 166 ? 17.097 13.692  -22.066 1.00 51.98  ?  322 LEU   A CA  1 
ATOM   977  C  C   . LEU   A 1 166 ? 17.755 12.627  -21.194 1.00 47.60  ?  322 LEU   A C   1 
ATOM   978  O  O   . LEU   A 1 166 ? 18.439 11.735  -21.702 1.00 52.93  ?  322 LEU   A O   1 
ATOM   979  C  CB  . LEU   A 1 166 ? 15.750 13.192  -22.594 1.00 55.68  ?  322 LEU   A CB  1 
ATOM   980  C  CG  . LEU   A 1 166 ? 14.821 12.382  -21.690 1.00 62.86  ?  322 LEU   A CG  1 
ATOM   981  C  CD1 . LEU   A 1 166 ? 14.354 13.224  -20.519 1.00 58.77  ?  322 LEU   A CD1 1 
ATOM   982  C  CD2 . LEU   A 1 166 ? 13.637 11.858  -22.486 1.00 62.67  ?  322 LEU   A CD2 1 
ATOM   983  N  N   . ALA   A 1 167 ? 17.554 12.723  -19.879 1.00 45.95  ?  323 ALA   A N   1 
ATOM   984  C  CA  . ALA   A 1 167 ? 18.193 11.791  -18.958 1.00 38.83  ?  323 ALA   A CA  1 
ATOM   985  C  C   . ALA   A 1 167 ? 17.303 11.551  -17.747 1.00 46.54  ?  323 ALA   A C   1 
ATOM   986  O  O   . ALA   A 1 167 ? 16.707 12.486  -17.206 1.00 51.51  ?  323 ALA   A O   1 
ATOM   987  C  CB  . ALA   A 1 167 ? 19.565 12.306  -18.503 1.00 39.20  ?  323 ALA   A CB  1 
ATOM   988  N  N   . LEU   A 1 168 ? 17.214 10.288  -17.338 1.00 44.52  ?  324 LEU   A N   1 
ATOM   989  C  CA  . LEU   A 1 168 ? 16.574 9.906   -16.089 1.00 39.72  ?  324 LEU   A CA  1 
ATOM   990  C  C   . LEU   A 1 168 ? 17.577 10.018  -14.952 1.00 38.38  ?  324 LEU   A C   1 
ATOM   991  O  O   . LEU   A 1 168 ? 18.732 9.606   -15.089 1.00 47.34  ?  324 LEU   A O   1 
ATOM   992  C  CB  . LEU   A 1 168 ? 16.043 8.473   -16.162 1.00 41.73  ?  324 LEU   A CB  1 
ATOM   993  C  CG  . LEU   A 1 168 ? 15.471 7.962   -17.485 1.00 53.03  ?  324 LEU   A CG  1 
ATOM   994  C  CD1 . LEU   A 1 168 ? 15.109 6.488   -17.373 1.00 55.78  ?  324 LEU   A CD1 1 
ATOM   995  C  CD2 . LEU   A 1 168 ? 14.261 8.777   -17.911 1.00 55.06  ?  324 LEU   A CD2 1 
ATOM   996  N  N   . GLU   A 1 169 ? 17.128 10.574  -13.830 1.00 50.17  ?  325 GLU   A N   1 
ATOM   997  C  CA  . GLU   A 1 169 ? 17.932 10.702  -12.623 1.00 41.51  ?  325 GLU   A CA  1 
ATOM   998  C  C   . GLU   A 1 169 ? 17.473 9.671   -11.605 1.00 47.56  ?  325 GLU   A C   1 
ATOM   999  O  O   . GLU   A 1 169 ? 16.270 9.547   -11.344 1.00 48.57  ?  325 GLU   A O   1 
ATOM   1000 C  CB  . GLU   A 1 169 ? 17.812 12.107  -12.029 1.00 45.34  ?  325 GLU   A CB  1 
ATOM   1001 C  CG  . GLU   A 1 169 ? 18.570 12.294  -10.724 1.00 41.97  ?  325 GLU   A CG  1 
ATOM   1002 C  CD  . GLU   A 1 169 ? 18.384 13.677  -10.136 1.00 50.48  ?  325 GLU   A CD  1 
ATOM   1003 O  OE1 . GLU   A 1 169 ? 17.313 13.939  -9.546  1.00 48.24  ?  325 GLU   A OE1 1 
ATOM   1004 O  OE2 . GLU   A 1 169 ? 19.308 14.506  -10.266 1.00 47.11  -1 325 GLU   A OE2 1 
ATOM   1005 N  N   . SER   A 1 170 ? 18.421 8.936   -11.026 1.00 42.83  ?  326 SER   A N   1 
ATOM   1006 C  CA  . SER   A 1 170 ? 18.094 7.988   -9.971  1.00 47.06  ?  326 SER   A CA  1 
ATOM   1007 C  C   . SER   A 1 170 ? 18.974 8.259   -8.764  1.00 49.18  ?  326 SER   A C   1 
ATOM   1008 O  O   . SER   A 1 170 ? 20.193 8.427   -8.901  1.00 42.45  ?  326 SER   A O   1 
ATOM   1009 C  CB  . SER   A 1 170 ? 18.264 6.539   -10.434 1.00 39.45  ?  326 SER   A CB  1 
ATOM   1010 O  OG  . SER   A 1 170 ? 18.076 5.648   -9.348  1.00 58.40  ?  326 SER   A OG  1 
ATOM   1011 N  N   . LYS   A 1 171 ? 18.348 8.305   -7.590  1.00 56.41  ?  327 LYS   A N   1 
ATOM   1012 C  CA  . LYS   A 1 171 ? 19.043 8.475   -6.325  1.00 56.80  ?  327 LYS   A CA  1 
ATOM   1013 C  C   . LYS   A 1 171 ? 19.229 7.153   -5.592  1.00 38.00  ?  327 LYS   A C   1 
ATOM   1014 O  O   . LYS   A 1 171 ? 19.658 7.151   -4.434  1.00 53.04  ?  327 LYS   A O   1 
ATOM   1015 C  CB  . LYS   A 1 171 ? 18.292 9.481   -5.453  1.00 44.84  ?  327 LYS   A CB  1 
ATOM   1016 C  CG  . LYS   A 1 171 ? 17.941 10.751  -6.209  1.00 45.66  ?  327 LYS   A CG  1 
ATOM   1017 C  CD  . LYS   A 1 171 ? 17.325 11.814  -5.320  1.00 72.32  ?  327 LYS   A CD  1 
ATOM   1018 C  CE  . LYS   A 1 171 ? 17.149 13.109  -6.098  1.00 59.91  ?  327 LYS   A CE  1 
ATOM   1019 N  NZ  . LYS   A 1 171 ? 16.561 14.204  -5.280  1.00 74.52  ?  327 LYS   A NZ  1 
ATOM   1020 N  N   . SER   A 1 172 ? 18.910 6.036   -6.242  1.00 43.27  ?  328 SER   A N   1 
ATOM   1021 C  CA  . SER   A 1 172 ? 19.263 4.725   -5.726  1.00 49.40  ?  328 SER   A CA  1 
ATOM   1022 C  C   . SER   A 1 172 ? 20.771 4.509   -5.845  1.00 43.57  ?  328 SER   A C   1 
ATOM   1023 O  O   . SER   A 1 172 ? 21.491 5.282   -6.484  1.00 43.67  ?  328 SER   A O   1 
ATOM   1024 C  CB  . SER   A 1 172 ? 18.505 3.630   -6.479  1.00 41.86  ?  328 SER   A CB  1 
ATOM   1025 O  OG  . SER   A 1 172 ? 18.880 3.591   -7.847  1.00 49.19  ?  328 SER   A OG  1 
ATOM   1026 N  N   . SER   A 1 173 ? 21.251 3.443   -5.212  1.00 42.95  ?  329 SER   A N   1 
ATOM   1027 C  CA  . SER   A 1 173 ? 22.664 3.109   -5.298  1.00 43.99  ?  329 SER   A CA  1 
ATOM   1028 C  C   . SER   A 1 173 ? 23.049 2.796   -6.742  1.00 51.39  ?  329 SER   A C   1 
ATOM   1029 O  O   . SER   A 1 173 ? 22.216 2.413   -7.570  1.00 36.92  ?  329 SER   A O   1 
ATOM   1030 C  CB  . SER   A 1 173 ? 22.992 1.924   -4.391  1.00 57.43  ?  329 SER   A CB  1 
ATOM   1031 O  OG  . SER   A 1 173 ? 22.432 2.104   -3.102  1.00 81.68  ?  329 SER   A OG  1 
ATOM   1032 N  N   . TRP   A 1 174 ? 24.331 2.977   -7.042  1.00 45.88  ?  330 TRP   A N   1 
ATOM   1033 C  CA  . TRP   A 1 174 ? 24.814 2.765   -8.396  1.00 38.15  ?  330 TRP   A CA  1 
ATOM   1034 C  C   . TRP   A 1 174 ? 24.738 1.283   -8.763  1.00 33.80  ?  330 TRP   A C   1 
ATOM   1035 O  O   . TRP   A 1 174 ? 24.822 0.416   -7.890  1.00 39.43  ?  330 TRP   A O   1 
ATOM   1036 C  CB  . TRP   A 1 174 ? 26.249 3.269   -8.536  1.00 31.51  ?  330 TRP   A CB  1 
ATOM   1037 C  CG  . TRP   A 1 174 ? 26.374 4.762   -8.454  1.00 38.00  ?  330 TRP   A CG  1 
ATOM   1038 C  CD1 . TRP   A 1 174 ? 25.395 5.651   -8.116  1.00 35.45  ?  330 TRP   A CD1 1 
ATOM   1039 C  CD2 . TRP   A 1 174 ? 27.545 5.542   -8.728  1.00 34.97  ?  330 TRP   A CD2 1 
ATOM   1040 N  NE1 . TRP   A 1 174 ? 25.885 6.934   -8.155  1.00 29.95  ?  330 TRP   A NE1 1 
ATOM   1041 C  CE2 . TRP   A 1 174 ? 27.202 6.894   -8.530  1.00 27.61  ?  330 TRP   A CE2 1 
ATOM   1042 C  CE3 . TRP   A 1 174 ? 28.849 5.227   -9.120  1.00 29.95  ?  330 TRP   A CE3 1 
ATOM   1043 C  CZ2 . TRP   A 1 174 ? 28.116 7.929   -8.710  1.00 31.00  ?  330 TRP   A CZ2 1 
ATOM   1044 C  CZ3 . TRP   A 1 174 ? 29.755 6.255   -9.297  1.00 28.92  ?  330 TRP   A CZ3 1 
ATOM   1045 C  CH2 . TRP   A 1 174 ? 29.385 7.590   -9.093  1.00 32.03  ?  330 TRP   A CH2 1 
ATOM   1046 N  N   . PRO   A 1 175 ? 24.567 0.969   -10.048 1.00 37.61  ?  331 PRO   A N   1 
ATOM   1047 C  CA  . PRO   A 1 175 ? 24.473 -0.437  -10.460 1.00 35.04  ?  331 PRO   A CA  1 
ATOM   1048 C  C   . PRO   A 1 175 ? 25.726 -1.223  -10.092 1.00 38.75  ?  331 PRO   A C   1 
ATOM   1049 O  O   . PRO   A 1 175 ? 26.812 -0.670  -9.900  1.00 37.93  ?  331 PRO   A O   1 
ATOM   1050 C  CB  . PRO   A 1 175 ? 24.296 -0.348  -11.980 1.00 34.62  ?  331 PRO   A CB  1 
ATOM   1051 C  CG  . PRO   A 1 175 ? 23.689 1.001   -12.202 1.00 39.19  ?  331 PRO   A CG  1 
ATOM   1052 C  CD  . PRO   A 1 175 ? 24.335 1.887   -11.176 1.00 35.79  ?  331 PRO   A CD  1 
ATOM   1053 N  N   . ALA   A 1 176 ? 25.556 -2.545  -9.997  1.00 37.73  ?  332 ALA   A N   1 
ATOM   1054 C  CA  . ALA   A 1 176 ? 26.644 -3.422  -9.575  1.00 41.19  ?  332 ALA   A CA  1 
ATOM   1055 C  C   . ALA   A 1 176 ? 27.807 -3.433  -10.558 1.00 44.21  ?  332 ALA   A C   1 
ATOM   1056 O  O   . ALA   A 1 176 ? 28.909 -3.850  -10.187 1.00 37.80  ?  332 ALA   A O   1 
ATOM   1057 C  CB  . ALA   A 1 176 ? 26.125 -4.847  -9.376  1.00 34.15  ?  332 ALA   A CB  1 
ATOM   1058 N  N   . SER   A 1 177 ? 27.594 -2.990  -11.797 1.00 42.80  ?  333 SER   A N   1 
ATOM   1059 C  CA  . SER   A 1 177 ? 28.683 -2.926  -12.762 1.00 39.69  ?  333 SER   A CA  1 
ATOM   1060 C  C   . SER   A 1 177 ? 29.668 -1.805  -12.462 1.00 42.74  ?  333 SER   A C   1 
ATOM   1061 O  O   . SER   A 1 177 ? 30.722 -1.744  -13.103 1.00 32.28  ?  333 SER   A O   1 
ATOM   1062 C  CB  . SER   A 1 177 ? 28.121 -2.757  -14.173 1.00 42.19  ?  333 SER   A CB  1 
ATOM   1063 O  OG  . SER   A 1 177 ? 27.296 -1.609  -14.253 1.00 33.30  ?  333 SER   A OG  1 
ATOM   1064 N  N   . THR   A 1 178 ? 29.357 -0.925  -11.513 1.00 37.80  ?  334 THR   A N   1 
ATOM   1065 C  CA  . THR   A 1 178 ? 30.244 0.166   -11.131 1.00 41.02  ?  334 THR   A CA  1 
ATOM   1066 C  C   . THR   A 1 178 ? 31.049 -0.134  -9.876  1.00 28.50  ?  334 THR   A C   1 
ATOM   1067 O  O   . THR   A 1 178 ? 31.845 0.711   -9.456  1.00 35.57  ?  334 THR   A O   1 
ATOM   1068 C  CB  . THR   A 1 178 ? 29.439 1.451   -10.910 1.00 32.67  ?  334 THR   A CB  1 
ATOM   1069 O  OG1 . THR   A 1 178 ? 28.632 1.311   -9.733  1.00 41.35  ?  334 THR   A OG1 1 
ATOM   1070 C  CG2 . THR   A 1 178 ? 28.541 1.731   -12.101 1.00 35.16  ?  334 THR   A CG2 1 
ATOM   1071 N  N   . GLN   A 1 179 ? 30.869 -1.316  -9.277  1.00 47.30  ?  335 GLN   A N   1 
ATOM   1072 C  CA  . GLN   A 1 179 ? 31.415 -1.576  -7.948  1.00 39.17  ?  335 GLN   A CA  1 
ATOM   1073 C  C   . GLN   A 1 179 ? 32.924 -1.365  -7.897  1.00 40.64  ?  335 GLN   A C   1 
ATOM   1074 O  O   . GLN   A 1 179 ? 33.456 -0.870  -6.896  1.00 37.97  ?  335 GLN   A O   1 
ATOM   1075 C  CB  . GLN   A 1 179 ? 31.052 -2.994  -7.504  1.00 41.97  ?  335 GLN   A CB  1 
ATOM   1076 C  CG  . GLN   A 1 179 ? 31.250 -3.240  -6.020  1.00 45.78  ?  335 GLN   A CG  1 
ATOM   1077 C  CD  . GLN   A 1 179 ? 32.333 -4.262  -5.744  1.00 75.17  ?  335 GLN   A CD  1 
ATOM   1078 O  OE1 . GLN   A 1 179 ? 32.694 -5.051  -6.618  1.00 85.78  ?  335 GLN   A OE1 1 
ATOM   1079 N  NE2 . GLN   A 1 179 ? 32.874 -4.240  -4.531  1.00 60.02  ?  335 GLN   A NE2 1 
ATOM   1080 N  N   . GLU   A 1 180 ? 33.628 -1.712  -8.972  1.00 42.35  ?  336 GLU   A N   1 
ATOM   1081 C  CA  . GLU   A 1 180 ? 35.079 -1.595  -9.021  1.00 35.71  ?  336 GLU   A CA  1 
ATOM   1082 C  C   . GLU   A 1 180 ? 35.551 -0.418  -9.870  1.00 32.10  ?  336 GLU   A C   1 
ATOM   1083 O  O   . GLU   A 1 180 ? 36.743 -0.332  -10.183 1.00 32.77  ?  336 GLU   A O   1 
ATOM   1084 C  CB  . GLU   A 1 180 ? 35.694 -2.898  -9.536  1.00 46.91  ?  336 GLU   A CB  1 
ATOM   1085 C  CG  . GLU   A 1 180 ? 35.249 -4.142  -8.778  1.00 49.81  ?  336 GLU   A CG  1 
ATOM   1086 C  CD  . GLU   A 1 180 ? 35.824 -4.205  -7.376  1.00 63.28  ?  336 GLU   A CD  1 
ATOM   1087 O  OE1 . GLU   A 1 180 ? 36.935 -3.671  -7.169  1.00 71.26  ?  336 GLU   A OE1 1 
ATOM   1088 O  OE2 . GLU   A 1 180 ? 35.180 -4.803  -6.488  1.00 81.22  -1 336 GLU   A OE2 1 
ATOM   1089 N  N   . GLY   A 1 181 ? 34.651 0.493   -10.244 1.00 33.07  ?  337 GLY   A N   1 
ATOM   1090 C  CA  . GLY   A 1 181 ? 35.026 1.669   -10.998 1.00 26.88  ?  337 GLY   A CA  1 
ATOM   1091 C  C   . GLY   A 1 181 ? 35.341 2.854   -10.101 1.00 30.30  ?  337 GLY   A C   1 
ATOM   1092 O  O   . GLY   A 1 181 ? 35.294 2.775   -8.874  1.00 27.40  ?  337 GLY   A O   1 
ATOM   1093 N  N   . LEU   A 1 182 ? 35.671 3.973   -10.749 1.00 25.76  ?  338 LEU   A N   1 
ATOM   1094 C  CA  . LEU   A 1 182 ? 35.970 5.233   -10.067 1.00 27.46  ?  338 LEU   A CA  1 
ATOM   1095 C  C   . LEU   A 1 182 ? 37.069 5.037   -9.022  1.00 27.98  ?  338 LEU   A C   1 
ATOM   1096 O  O   . LEU   A 1 182 ? 36.934 5.406   -7.854  1.00 28.72  ?  338 LEU   A O   1 
ATOM   1097 C  CB  . LEU   A 1 182 ? 34.702 5.826   -9.443  1.00 19.76  ?  338 LEU   A CB  1 
ATOM   1098 C  CG  . LEU   A 1 182 ? 34.738 7.265   -8.918  1.00 23.03  ?  338 LEU   A CG  1 
ATOM   1099 C  CD1 . LEU   A 1 182 ? 35.042 8.251   -10.035 1.00 20.42  ?  338 LEU   A CD1 1 
ATOM   1100 C  CD2 . LEU   A 1 182 ? 33.426 7.610   -8.227  1.00 26.45  ?  338 LEU   A CD2 1 
ATOM   1101 N  N   . ARG   A 1 183 ? 38.174 4.433   -9.458  1.00 22.93  ?  339 ARG   A N   1 
ATOM   1102 C  CA  . ARG   A 1 183 ? 39.260 4.057   -8.553  1.00 29.24  ?  339 ARG   A CA  1 
ATOM   1103 C  C   . ARG   A 1 183 ? 40.142 5.277   -8.283  1.00 25.87  ?  339 ARG   A C   1 
ATOM   1104 O  O   . ARG   A 1 183 ? 41.261 5.416   -8.782  1.00 34.94  ?  339 ARG   A O   1 
ATOM   1105 C  CB  . ARG   A 1 183 ? 40.049 2.889   -9.129  1.00 33.47  ?  339 ARG   A CB  1 
ATOM   1106 C  CG  . ARG   A 1 183 ? 39.178 1.683   -9.451  1.00 35.73  ?  339 ARG   A CG  1 
ATOM   1107 C  CD  . ARG   A 1 183 ? 40.005 0.441   -9.737  1.00 55.16  ?  339 ARG   A CD  1 
ATOM   1108 N  NE  . ARG   A 1 183 ? 40.707 0.543   -11.011 1.00 68.08  ?  339 ARG   A NE  1 
ATOM   1109 C  CZ  . ARG   A 1 183 ? 40.144 0.339   -12.195 1.00 65.93  ?  339 ARG   A CZ  1 
ATOM   1110 N  NH1 . ARG   A 1 183 ? 38.862 0.028   -12.308 1.00 56.56  ?  339 ARG   A NH1 1 
ATOM   1111 N  NH2 . ARG   A 1 183 ? 40.885 0.453   -13.294 1.00 62.08  ?  339 ARG   A NH2 1 
ATOM   1112 N  N   . ILE   A 1 184 ? 39.604 6.174   -7.457  1.00 29.01  ?  340 ILE   A N   1 
ATOM   1113 C  CA  . ILE   A 1 184 ? 40.260 7.430   -7.123  1.00 22.19  ?  340 ILE   A CA  1 
ATOM   1114 C  C   . ILE   A 1 184 ? 40.839 7.414   -5.712  1.00 21.00  ?  340 ILE   A C   1 
ATOM   1115 O  O   . ILE   A 1 184 ? 41.317 8.448   -5.234  1.00 21.68  ?  340 ILE   A O   1 
ATOM   1116 C  CB  . ILE   A 1 184 ? 39.292 8.612   -7.293  1.00 24.47  ?  340 ILE   A CB  1 
ATOM   1117 C  CG1 . ILE   A 1 184 ? 38.065 8.421   -6.393  1.00 23.57  ?  340 ILE   A CG1 1 
ATOM   1118 C  CG2 . ILE   A 1 184 ? 38.886 8.763   -8.751  1.00 22.95  ?  340 ILE   A CG2 1 
ATOM   1119 C  CD1 . ILE   A 1 184 ? 37.124 9.609   -6.368  1.00 18.30  ?  340 ILE   A CD1 1 
ATOM   1120 N  N   . GLN   A 1 185 ? 40.764 6.288   -5.018  1.00 20.55  ?  341 GLN   A N   1 
ATOM   1121 C  CA  . GLN   A 1 185 ? 41.148 6.246   -3.581  1.00 26.78  ?  341 GLN   A CA  1 
ATOM   1122 C  C   . GLN   A 1 185 ? 42.591 6.726   -3.343  1.00 28.57  ?  341 GLN   A C   1 
ATOM   1123 O  O   . GLN   A 1 185 ? 42.806 7.375   -2.320  1.00 28.54  ?  341 GLN   A O   1 
ATOM   1124 C  CB  . GLN   A 1 185 ? 40.877 4.852   -3.017  1.00 23.84  ?  341 GLN   A CB  1 
ATOM   1125 C  CG  . GLN   A 1 185 ? 39.451 4.365   -3.236  1.00 28.50  ?  341 GLN   A CG  1 
ATOM   1126 C  CD  . GLN   A 1 185 ? 39.320 3.447   -4.430  1.00 36.18  ?  341 GLN   A CD  1 
ATOM   1127 O  OE1 . GLN   A 1 185 ? 39.948 3.657   -5.470  1.00 22.77  ?  341 GLN   A OE1 1 
ATOM   1128 N  NE2 . GLN   A 1 185 ? 38.509 2.411   -4.282  1.00 29.41  ?  341 GLN   A NE2 1 
ATOM   1129 N  N   . ASN   A 1 186 ? 43.521 6.435   -4.247  1.00 18.67  ?  342 ASN   A N   1 
ATOM   1130 C  CA  . ASN   A 1 186 ? 44.940 6.793   -3.999  1.00 27.84  ?  342 ASN   A CA  1 
ATOM   1131 C  C   . ASN   A 1 186 ? 45.196 8.230   -4.464  1.00 26.86  ?  342 ASN   A C   1 
ATOM   1132 O  O   . ASN   A 1 186 ? 46.274 8.751   -4.175  1.00 25.13  ?  342 ASN   A O   1 
ATOM   1133 C  CB  . ASN   A 1 186 ? 45.881 5.766   -4.618  1.00 37.86  ?  342 ASN   A CB  1 
ATOM   1134 C  CG  . ASN   A 1 186 ? 45.988 4.509   -3.790  1.00 47.70  ?  342 ASN   A CG  1 
ATOM   1135 O  OD1 . ASN   A 1 186 ? 45.096 4.206   -2.991  1.00 59.72  ?  342 ASN   A OD1 1 
ATOM   1136 N  ND2 . ASN   A 1 186 ? 47.065 3.761   -3.968  1.00 81.55  ?  342 ASN   A ND2 1 
ATOM   1137 N  N   . TRP   A 1 187 ? 44.213 8.845   -5.107  1.00 24.41  ?  343 TRP   A N   1 
ATOM   1138 C  CA  . TRP   A 1 187 ? 44.374 10.193  -5.696  1.00 17.47  ?  343 TRP   A CA  1 
ATOM   1139 C  C   . TRP   A 1 187 ? 43.455 11.180  -4.974  1.00 24.33  ?  343 TRP   A C   1 
ATOM   1140 O  O   . TRP   A 1 187 ? 43.986 12.064  -4.297  1.00 23.58  ?  343 TRP   A O   1 
ATOM   1141 C  CB  . TRP   A 1 187 ? 44.088 10.106  -7.201  1.00 18.92  ?  343 TRP   A CB  1 
ATOM   1142 C  CG  . TRP   A 1 187 ? 43.816 11.390  -7.936  1.00 14.48  ?  343 TRP   A CG  1 
ATOM   1143 C  CD1 . TRP   A 1 187 ? 44.366 12.621  -7.751  1.00 18.54  ?  343 TRP   A CD1 1 
ATOM   1144 C  CD2 . TRP   A 1 187 ? 42.902 11.523  -9.042  1.00 16.39  ?  343 TRP   A CD2 1 
ATOM   1145 N  NE1 . TRP   A 1 187 ? 43.848 13.512  -8.650  1.00 21.64  ?  343 TRP   A NE1 1 
ATOM   1146 C  CE2 . TRP   A 1 187 ? 42.948 12.868  -9.456  1.00 20.11  ?  343 TRP   A CE2 1 
ATOM   1147 C  CE3 . TRP   A 1 187 ? 42.050 10.638  -9.709  1.00 20.37  ?  343 TRP   A CE3 1 
ATOM   1148 C  CZ2 . TRP   A 1 187 ? 42.171 13.346  -10.508 1.00 23.19  ?  343 TRP   A CZ2 1 
ATOM   1149 C  CZ3 . TRP   A 1 187 ? 41.282 11.111  -10.746 1.00 18.72  ?  343 TRP   A CZ3 1 
ATOM   1150 C  CH2 . TRP   A 1 187 ? 41.348 12.445  -11.140 1.00 19.14  ?  343 TRP   A CH2 1 
ATOM   1151 N  N   . LEU   A 1 188 ? 42.141 11.029  -5.128  1.00 19.32  ?  344 LEU   A N   1 
ATOM   1152 C  CA  . LEU   A 1 188 ? 41.235 11.970  -4.483  1.00 23.03  ?  344 LEU   A CA  1 
ATOM   1153 C  C   . LEU   A 1 188 ? 40.717 11.489  -3.130  1.00 20.40  ?  344 LEU   A C   1 
ATOM   1154 O  O   . LEU   A 1 188 ? 40.093 12.287  -2.423  1.00 24.61  ?  344 LEU   A O   1 
ATOM   1155 C  CB  . LEU   A 1 188 ? 40.045 12.276  -5.403  1.00 16.07  ?  344 LEU   A CB  1 
ATOM   1156 C  CG  . LEU   A 1 188 ? 40.415 12.760  -6.807  1.00 15.99  ?  344 LEU   A CG  1 
ATOM   1157 C  CD1 . LEU   A 1 188 ? 39.188 12.847  -7.701  1.00 25.95  ?  344 LEU   A CD1 1 
ATOM   1158 C  CD2 . LEU   A 1 188 ? 41.125 14.104  -6.739  1.00 20.03  ?  344 LEU   A CD2 1 
ATOM   1159 N  N   . SER   A 1 189 ? 40.929 10.206  -2.792  1.00 16.86  ?  345 SER   A N   1 
ATOM   1160 C  CA  . SER   A 1 189 ? 40.710 9.555   -1.491  1.00 24.62  ?  345 SER   A CA  1 
ATOM   1161 C  C   . SER   A 1 189 ? 39.469 8.668   -1.476  1.00 21.22  ?  345 SER   A C   1 
ATOM   1162 O  O   . SER   A 1 189 ? 38.530 8.875   -2.253  1.00 24.55  ?  345 SER   A O   1 
ATOM   1163 C  CB  . SER   A 1 189 ? 40.622 10.553  -0.330  1.00 21.87  ?  345 SER   A CB  1 
ATOM   1164 O  OG  . SER   A 1 189 ? 39.355 11.187  -0.292  1.00 24.35  ?  345 SER   A OG  1 
ATOM   1165 N  N   . ALA   A 1 190 ? 39.469 7.668   -0.585  1.00 22.25  ?  346 ALA   A N   1 
ATOM   1166 C  CA  . ALA   A 1 190 ? 38.319 6.780   -0.440  1.00 25.74  ?  346 ALA   A CA  1 
ATOM   1167 C  C   . ALA   A 1 190 ? 37.110 7.519   0.115   1.00 23.90  ?  346 ALA   A C   1 
ATOM   1168 O  O   . ALA   A 1 190 ? 35.966 7.188   -0.223  1.00 30.40  ?  346 ALA   A O   1 
ATOM   1169 C  CB  . ALA   A 1 190 ? 38.683 5.602   0.466   1.00 24.41  ?  346 ALA   A CB  1 
ATOM   1170 N  N   . LYS   A 1 191 ? 37.349 8.517   0.967   1.00 18.63  ?  347 LYS   A N   1 
ATOM   1171 C  CA  . LYS   A 1 191 ? 36.268 9.339   1.496   1.00 28.20  ?  347 LYS   A CA  1 
ATOM   1172 C  C   . LYS   A 1 191 ? 35.546 10.077  0.373   1.00 23.23  ?  347 LYS   A C   1 
ATOM   1173 O  O   . LYS   A 1 191 ? 34.306 10.090  0.311   1.00 24.51  ?  347 LYS   A O   1 
ATOM   1174 C  CB  . LYS   A 1 191 ? 36.858 10.309  2.521   1.00 28.11  ?  347 LYS   A CB  1 
ATOM   1175 C  CG  . LYS   A 1 191 ? 35.874 11.057  3.387   1.00 30.98  ?  347 LYS   A CG  1 
ATOM   1176 C  CD  . LYS   A 1 191 ? 36.549 12.253  4.050   1.00 47.09  ?  347 LYS   A CD  1 
ATOM   1177 C  CE  . LYS   A 1 191 ? 37.936 11.885  4.570   1.00 32.19  ?  347 LYS   A CE  1 
ATOM   1178 N  NZ  . LYS   A 1 191 ? 37.907 11.297  5.942   1.00 53.50  ?  347 LYS   A NZ  1 
ATOM   1179 N  N   . VAL   A 1 192 ? 36.312 10.675  -0.543  1.00 31.63  ?  348 VAL   A N   1 
ATOM   1180 C  CA  . VAL   A 1 192 ? 35.714 11.358  -1.685  1.00 22.97  ?  348 VAL   A CA  1 
ATOM   1181 C  C   . VAL   A 1 192 ? 34.985 10.364  -2.580  1.00 24.94  ?  348 VAL   A C   1 
ATOM   1182 O  O   . VAL   A 1 192 ? 33.917 10.668  -3.121  1.00 22.89  ?  348 VAL   A O   1 
ATOM   1183 C  CB  . VAL   A 1 192 ? 36.791 12.147  -2.454  1.00 26.26  ?  348 VAL   A CB  1 
ATOM   1184 C  CG1 . VAL   A 1 192 ? 36.264 12.612  -3.804  1.00 17.82  ?  348 VAL   A CG1 1 
ATOM   1185 C  CG2 . VAL   A 1 192 ? 37.241 13.342  -1.627  1.00 15.23  ?  348 VAL   A CG2 1 
ATOM   1186 N  N   . ARG   A 1 193 ? 35.536 9.159   -2.742  1.00 25.87  ?  349 ARG   A N   1 
ATOM   1187 C  CA  . ARG   A 1 193 ? 34.863 8.149   -3.556  1.00 27.94  ?  349 ARG   A CA  1 
ATOM   1188 C  C   . ARG   A 1 193 ? 33.503 7.797   -2.975  1.00 27.63  ?  349 ARG   A C   1 
ATOM   1189 O  O   . ARG   A 1 193 ? 32.510 7.689   -3.706  1.00 28.77  ?  349 ARG   A O   1 
ATOM   1190 C  CB  . ARG   A 1 193 ? 35.726 6.893   -3.678  1.00 19.57  ?  349 ARG   A CB  1 
ATOM   1191 C  CG  . ARG   A 1 193 ? 35.139 5.854   -4.623  1.00 21.87  ?  349 ARG   A CG  1 
ATOM   1192 C  CD  . ARG   A 1 193 ? 36.066 4.669   -4.832  1.00 24.51  ?  349 ARG   A CD  1 
ATOM   1193 N  NE  . ARG   A 1 193 ? 35.516 3.735   -5.807  1.00 21.82  ?  349 ARG   A NE  1 
ATOM   1194 C  CZ  . ARG   A 1 193 ? 34.666 2.760   -5.514  1.00 33.46  ?  349 ARG   A CZ  1 
ATOM   1195 N  NH1 . ARG   A 1 193 ? 34.259 2.550   -4.272  1.00 24.42  ?  349 ARG   A NH1 1 
ATOM   1196 N  NH2 . ARG   A 1 193 ? 34.211 1.979   -6.490  1.00 27.95  ?  349 ARG   A NH2 1 
ATOM   1197 N  N   . LYS   A 1 194 ? 33.441 7.612   -1.654  1.00 23.97  ?  350 LYS   A N   1 
ATOM   1198 C  CA  . LYS   A 1 194 ? 32.167 7.308   -1.011  1.00 22.44  ?  350 LYS   A CA  1 
ATOM   1199 C  C   . LYS   A 1 194 ? 31.170 8.444   -1.206  1.00 27.99  ?  350 LYS   A C   1 
ATOM   1200 O  O   . LYS   A 1 194 ? 30.024 8.216   -1.624  1.00 34.34  ?  350 LYS   A O   1 
ATOM   1201 C  CB  . LYS   A 1 194 ? 32.397 7.027   0.476   1.00 31.42  ?  350 LYS   A CB  1 
ATOM   1202 C  CG  . LYS   A 1 194 ? 31.131 6.733   1.267   1.00 39.11  ?  350 LYS   A CG  1 
ATOM   1203 C  CD  . LYS   A 1 194 ? 31.358 6.860   2.767   1.00 45.21  ?  350 LYS   A CD  1 
ATOM   1204 C  CE  . LYS   A 1 194 ? 30.972 5.575   3.480   1.00 66.32  ?  350 LYS   A CE  1 
ATOM   1205 N  NZ  . LYS   A 1 194 ? 29.964 5.826   4.547   1.00 76.30  ?  350 LYS   A NZ  1 
ATOM   1206 N  N   . GLN   A 1 195 ? 31.601 9.680   -0.921  1.00 25.85  ?  351 GLN   A N   1 
ATOM   1207 C  CA  . GLN   A 1 195 ? 30.725 10.836  -1.091  1.00 30.87  ?  351 GLN   A CA  1 
ATOM   1208 C  C   . GLN   A 1 195 ? 30.218 10.952  -2.526  1.00 30.48  ?  351 GLN   A C   1 
ATOM   1209 O  O   . GLN   A 1 195 ? 29.049 11.286  -2.751  1.00 28.55  ?  351 GLN   A O   1 
ATOM   1210 C  CB  . GLN   A 1 195 ? 31.460 12.110  -0.680  1.00 25.28  ?  351 GLN   A CB  1 
ATOM   1211 N  N   . LEU   A 1 196 ? 31.080 10.686  -3.512  1.00 30.13  ?  352 LEU   A N   1 
ATOM   1212 C  CA  . LEU   A 1 196 ? 30.650 10.749  -4.905  1.00 28.86  ?  352 LEU   A CA  1 
ATOM   1213 C  C   . LEU   A 1 196 ? 29.652 9.646   -5.222  1.00 32.23  ?  352 LEU   A C   1 
ATOM   1214 O  O   . LEU   A 1 196 ? 28.679 9.871   -5.951  1.00 29.98  ?  352 LEU   A O   1 
ATOM   1215 C  CB  . LEU   A 1 196 ? 31.856 10.653  -5.839  1.00 27.55  ?  352 LEU   A CB  1 
ATOM   1216 C  CG  . LEU   A 1 196 ? 32.807 11.846  -5.887  1.00 24.95  ?  352 LEU   A CG  1 
ATOM   1217 C  CD1 . LEU   A 1 196 ? 33.952 11.556  -6.840  1.00 26.70  ?  352 LEU   A CD1 1 
ATOM   1218 C  CD2 . LEU   A 1 196 ? 32.061 13.098  -6.305  1.00 38.52  ?  352 LEU   A CD2 1 
ATOM   1219 N  N   . ARG   A 1 197 ? 29.874 8.445   -4.686  1.00 22.33  ?  353 ARG   A N   1 
ATOM   1220 C  CA  . ARG   A 1 197 ? 28.965 7.344   -4.956  1.00 22.74  ?  353 ARG   A CA  1 
ATOM   1221 C  C   . ARG   A 1 197 ? 27.650 7.476   -4.199  1.00 27.36  ?  353 ARG   A C   1 
ATOM   1222 O  O   . ARG   A 1 197 ? 26.711 6.727   -4.486  1.00 25.06  ?  353 ARG   A O   1 
ATOM   1223 C  CB  . ARG   A 1 197 ? 29.653 6.017   -4.632  1.00 35.96  ?  353 ARG   A CB  1 
ATOM   1224 C  CG  . ARG   A 1 197 ? 30.814 5.691   -5.570  1.00 27.93  ?  353 ARG   A CG  1 
ATOM   1225 C  CD  . ARG   A 1 197 ? 31.447 4.365   -5.210  1.00 29.12  ?  353 ARG   A CD  1 
ATOM   1226 N  NE  . ARG   A 1 197 ? 30.534 3.260   -5.476  1.00 46.43  ?  353 ARG   A NE  1 
ATOM   1227 C  CZ  . ARG   A 1 197 ? 30.375 2.702   -6.667  1.00 43.27  ?  353 ARG   A CZ  1 
ATOM   1228 N  NH1 . ARG   A 1 197 ? 31.049 3.127   -7.724  1.00 40.36  ?  353 ARG   A NH1 1 
ATOM   1229 N  NH2 . ARG   A 1 197 ? 29.516 1.695   -6.804  1.00 38.61  ?  353 ARG   A NH2 1 
ATOM   1230 N  N   . LEU   A 1 198 ? 27.552 8.400   -3.247  1.00 27.89  ?  354 LEU   A N   1 
ATOM   1231 C  CA  . LEU   A 1 198 ? 26.257 8.723   -2.660  1.00 33.74  ?  354 LEU   A CA  1 
ATOM   1232 C  C   . LEU   A 1 198 ? 25.405 9.629   -3.543  1.00 34.32  ?  354 LEU   A C   1 
ATOM   1233 O  O   . LEU   A 1 198 ? 24.244 9.877   -3.201  1.00 37.44  ?  354 LEU   A O   1 
ATOM   1234 C  CB  . LEU   A 1 198 ? 26.429 9.368   -1.282  1.00 31.49  ?  354 LEU   A CB  1 
ATOM   1235 C  CG  . LEU   A 1 198 ? 26.944 8.391   -0.233  1.00 38.58  ?  354 LEU   A CG  1 
ATOM   1236 C  CD1 . LEU   A 1 198 ? 27.224 9.138   1.048   1.00 39.89  ?  354 LEU   A CD1 1 
ATOM   1237 C  CD2 . LEU   A 1 198 ? 25.948 7.252   -0.006  1.00 33.54  ?  354 LEU   A CD2 1 
ATOM   1238 N  N   . LYS   A 1 199 ? 25.936 10.116  -4.683  1.00 39.66  ?  355 LYS   A N   1 
ATOM   1239 C  CA  . LYS   A 1 199 ? 25.224 11.057  -5.541  1.00 40.98  ?  355 LYS   A CA  1 
ATOM   1240 C  C   . LYS   A 1 199 ? 24.369 10.317  -6.565  1.00 35.93  ?  355 LYS   A C   1 
ATOM   1241 O  O   . LYS   A 1 199 ? 24.560 9.118   -6.795  1.00 36.88  ?  355 LYS   A O   1 
ATOM   1242 C  CB  . LYS   A 1 199 ? 26.223 11.970  -6.246  1.00 38.05  ?  355 LYS   A CB  1 
ATOM   1243 C  CG  . LYS   A 1 199 ? 27.050 12.797  -5.281  1.00 43.12  ?  355 LYS   A CG  1 
ATOM   1244 C  CD  . LYS   A 1 199 ? 27.780 13.937  -5.961  1.00 55.48  ?  355 LYS   A CD  1 
ATOM   1245 C  CE  . LYS   A 1 199 ? 28.529 14.777  -4.938  1.00 68.13  ?  355 LYS   A CE  1 
ATOM   1246 N  NZ  . LYS   A 1 199 ? 28.951 16.088  -5.491  1.00 70.93  ?  355 LYS   A NZ  1 
ATOM   1247 N  N   . PRO   A 1 200 ? 23.398 10.992  -7.195  1.00 41.36  ?  356 PRO   A N   1 
ATOM   1248 C  CA  . PRO   A 1 200 ? 22.576 10.308  -8.203  1.00 34.79  ?  356 PRO   A CA  1 
ATOM   1249 C  C   . PRO   A 1 200 ? 23.401 9.859   -9.403  1.00 42.65  ?  356 PRO   A C   1 
ATOM   1250 O  O   . PRO   A 1 200 ? 24.523 10.317  -9.632  1.00 37.53  ?  356 PRO   A O   1 
ATOM   1251 C  CB  . PRO   A 1 200 ? 21.545 11.371  -8.610  1.00 41.18  ?  356 PRO   A CB  1 
ATOM   1252 C  CG  . PRO   A 1 200 ? 22.147 12.673  -8.212  1.00 34.88  ?  356 PRO   A CG  1 
ATOM   1253 C  CD  . PRO   A 1 200 ? 22.940 12.378  -6.973  1.00 40.85  ?  356 PRO   A CD  1 
ATOM   1254 N  N   . PHE   A 1 201 ? 22.826 8.934   -10.172 1.00 38.73  ?  357 PHE   A N   1 
ATOM   1255 C  CA  . PHE   A 1 201 ? 23.383 8.529   -11.457 1.00 35.99  ?  357 PHE   A CA  1 
ATOM   1256 C  C   . PHE   A 1 201 ? 22.327 8.733   -12.537 1.00 39.26  ?  357 PHE   A C   1 
ATOM   1257 O  O   . PHE   A 1 201 ? 21.133 8.880   -12.236 1.00 35.74  ?  357 PHE   A O   1 
ATOM   1258 C  CB  . PHE   A 1 201 ? 23.885 7.068   -11.430 1.00 37.03  ?  357 PHE   A CB  1 
ATOM   1259 C  CG  . PHE   A 1 201 ? 22.794 6.034   -11.307 1.00 36.39  ?  357 PHE   A CG  1 
ATOM   1260 C  CD1 . PHE   A 1 201 ? 22.178 5.518   -12.439 1.00 36.75  ?  357 PHE   A CD1 1 
ATOM   1261 C  CD2 . PHE   A 1 201 ? 22.410 5.551   -10.066 1.00 39.35  ?  357 PHE   A CD2 1 
ATOM   1262 C  CE1 . PHE   A 1 201 ? 21.184 4.561   -12.335 1.00 37.81  ?  357 PHE   A CE1 1 
ATOM   1263 C  CE2 . PHE   A 1 201 ? 21.416 4.590   -9.956  1.00 51.81  ?  357 PHE   A CE2 1 
ATOM   1264 C  CZ  . PHE   A 1 201 ? 20.804 4.095   -11.092 1.00 43.66  ?  357 PHE   A CZ  1 
ATOM   1265 N  N   . TYR   A 1 202 ? 22.751 8.766   -13.808 1.00 37.95  ?  358 TYR   A N   1 
ATOM   1266 C  CA  . TYR   A 1 202 ? 21.808 9.127   -14.853 1.00 32.32  ?  358 TYR   A CA  1 
ATOM   1267 C  C   . TYR   A 1 202 ? 21.738 8.050   -15.927 1.00 35.55  ?  358 TYR   A C   1 
ATOM   1268 O  O   . TYR   A 1 202 ? 22.629 7.210   -16.060 1.00 34.81  ?  358 TYR   A O   1 
ATOM   1269 C  CB  . TYR   A 1 202 ? 22.170 10.496  -15.451 1.00 32.12  ?  358 TYR   A CB  1 
ATOM   1270 C  CG  . TYR   A 1 202 ? 22.063 11.602  -14.420 1.00 36.83  ?  358 TYR   A CG  1 
ATOM   1271 C  CD1 . TYR   A 1 202 ? 23.122 11.893  -13.565 1.00 33.08  ?  358 TYR   A CD1 1 
ATOM   1272 C  CD2 . TYR   A 1 202 ? 20.887 12.325  -14.269 1.00 40.69  ?  358 TYR   A CD2 1 
ATOM   1273 C  CE1 . TYR   A 1 202 ? 23.019 12.889  -12.608 1.00 34.80  ?  358 TYR   A CE1 1 
ATOM   1274 C  CE2 . TYR   A 1 202 ? 20.776 13.323  -13.315 1.00 43.71  ?  358 TYR   A CE2 1 
ATOM   1275 C  CZ  . TYR   A 1 202 ? 21.844 13.600  -12.486 1.00 35.90  ?  358 TYR   A CZ  1 
ATOM   1276 O  OH  . TYR   A 1 202 ? 21.738 14.590  -11.535 1.00 41.56  ?  358 TYR   A OH  1 
ATOM   1277 N  N   . LEU   A 1 203 ? 20.642 8.076   -16.681 1.00 36.65  ?  359 LEU   A N   1 
ATOM   1278 C  CA  . LEU   A 1 203 ? 20.383 7.111   -17.745 1.00 39.36  ?  359 LEU   A CA  1 
ATOM   1279 C  C   . LEU   A 1 203 ? 19.902 7.869   -18.973 1.00 43.82  ?  359 LEU   A C   1 
ATOM   1280 O  O   . LEU   A 1 203 ? 18.891 8.573   -18.909 1.00 48.07  ?  359 LEU   A O   1 
ATOM   1281 C  CB  . LEU   A 1 203 ? 19.339 6.080   -17.309 1.00 44.10  ?  359 LEU   A CB  1 
ATOM   1282 C  CG  . LEU   A 1 203 ? 19.795 5.015   -16.313 1.00 37.57  ?  359 LEU   A CG  1 
ATOM   1283 C  CD1 . LEU   A 1 203 ? 18.600 4.447   -15.570 1.00 48.74  ?  359 LEU   A CD1 1 
ATOM   1284 C  CD2 . LEU   A 1 203 ? 20.553 3.912   -17.028 1.00 40.67  ?  359 LEU   A CD2 1 
ATOM   1285 N  N   . VAL   A 1 204 ? 20.621 7.730   -20.082 1.00 36.76  ?  360 VAL   A N   1 
ATOM   1286 C  CA  . VAL   A 1 204 ? 20.264 8.434   -21.313 1.00 37.74  ?  360 VAL   A CA  1 
ATOM   1287 C  C   . VAL   A 1 204 ? 19.759 7.420   -22.335 1.00 43.31  ?  360 VAL   A C   1 
ATOM   1288 O  O   . VAL   A 1 204 ? 20.261 6.292   -22.382 1.00 46.73  ?  360 VAL   A O   1 
ATOM   1289 C  CB  . VAL   A 1 204 ? 21.453 9.246   -21.854 1.00 41.51  ?  360 VAL   A CB  1 
ATOM   1290 C  CG1 . VAL   A 1 204 ? 21.924 10.248  -20.810 1.00 34.93  ?  360 VAL   A CG1 1 
ATOM   1291 C  CG2 . VAL   A 1 204 ? 22.599 8.328   -22.261 1.00 41.14  ?  360 VAL   A CG2 1 
ATOM   1292 N  N   . PRO   A 1 205 ? 18.770 7.759   -23.160 1.00 41.08  ?  361 PRO   A N   1 
ATOM   1293 C  CA  . PRO   A 1 205 ? 18.265 6.784   -24.138 1.00 46.50  ?  361 PRO   A CA  1 
ATOM   1294 C  C   . PRO   A 1 205 ? 19.297 6.529   -25.228 1.00 47.03  ?  361 PRO   A C   1 
ATOM   1295 O  O   . PRO   A 1 205 ? 19.801 7.464   -25.852 1.00 41.52  ?  361 PRO   A O   1 
ATOM   1296 C  CB  . PRO   A 1 205 ? 17.005 7.456   -24.693 1.00 44.72  ?  361 PRO   A CB  1 
ATOM   1297 C  CG  . PRO   A 1 205 ? 17.245 8.918   -24.506 1.00 51.15  ?  361 PRO   A CG  1 
ATOM   1298 C  CD  . PRO   A 1 205 ? 18.117 9.074   -23.291 1.00 41.78  ?  361 PRO   A CD  1 
ATOM   1299 N  N   . LYS   A 1 206 ? 19.615 5.254   -25.452 1.00 42.43  ?  362 LYS   A N   1 
ATOM   1300 C  CA  . LYS   A 1 206 ? 20.644 4.924   -26.431 1.00 50.37  ?  362 LYS   A CA  1 
ATOM   1301 C  C   . LYS   A 1 206 ? 20.483 3.487   -26.900 1.00 44.88  ?  362 LYS   A C   1 
ATOM   1302 O  O   . LYS   A 1 206 ? 20.272 2.582   -26.086 1.00 42.70  ?  362 LYS   A O   1 
ATOM   1303 C  CB  . LYS   A 1 206 ? 22.044 5.137   -25.847 1.00 46.99  ?  362 LYS   A CB  1 
ATOM   1304 C  CG  . LYS   A 1 206 ? 23.108 5.307   -26.911 1.00 47.67  ?  362 LYS   A CG  1 
ATOM   1305 C  CD  . LYS   A 1 206 ? 23.665 6.717   -26.898 1.00 52.60  ?  362 LYS   A CD  1 
ATOM   1306 C  CE  . LYS   A 1 206 ? 24.191 7.102   -28.269 1.00 62.85  ?  362 LYS   A CE  1 
ATOM   1307 N  NZ  . LYS   A 1 206 ? 24.288 8.580   -28.421 1.00 55.56  ?  362 LYS   A NZ  1 
ATOM   1308 N  N   . HIS   A 1 207 ? 20.600 3.285   -28.211 1.00 54.09  ?  363 HIS   A N   1 
ATOM   1309 C  CA  . HIS   A 1 207 ? 20.458 1.953   -28.778 1.00 51.24  ?  363 HIS   A CA  1 
ATOM   1310 C  C   . HIS   A 1 207 ? 21.634 1.074   -28.379 1.00 45.21  ?  363 HIS   A C   1 
ATOM   1311 O  O   . HIS   A 1 207 ? 22.782 1.523   -28.333 1.00 49.23  ?  363 HIS   A O   1 
ATOM   1312 C  CB  . HIS   A 1 207 ? 20.361 2.029   -30.303 1.00 51.12  ?  363 HIS   A CB  1 
ATOM   1313 N  N   . ALA   A 1 208 ? 21.339 -0.184  -28.080 1.00 47.82  ?  364 ALA   A N   1 
ATOM   1314 C  CA  . ALA   A 1 208 ? 22.375 -1.178  -27.851 1.00 53.95  ?  364 ALA   A CA  1 
ATOM   1315 C  C   . ALA   A 1 208 ? 22.338 -2.200  -28.977 1.00 56.99  ?  364 ALA   A C   1 
ATOM   1316 O  O   . ALA   A 1 208 ? 21.297 -2.396  -29.605 1.00 75.93  ?  364 ALA   A O   1 
ATOM   1317 C  CB  . ALA   A 1 208 ? 22.187 -1.853  -26.503 1.00 51.93  ?  364 ALA   A CB  1 
ATOM   1318 N  N   . GLN   A 1 215 ? 18.700 -3.393  -30.077 1.00 64.32  ?  371 GLN   A N   1 
ATOM   1319 C  CA  . GLN   A 1 215 ? 17.521 -3.277  -29.224 1.00 74.26  ?  371 GLN   A CA  1 
ATOM   1320 C  C   . GLN   A 1 215 ? 17.262 -1.807  -28.858 1.00 70.97  ?  371 GLN   A C   1 
ATOM   1321 O  O   . GLN   A 1 215 ? 18.133 -1.139  -28.304 1.00 69.58  ?  371 GLN   A O   1 
ATOM   1322 C  CB  . GLN   A 1 215 ? 17.697 -4.139  -27.974 1.00 70.14  ?  371 GLN   A CB  1 
ATOM   1323 C  CG  . GLN   A 1 215 ? 16.393 -4.478  -27.285 1.00 77.40  ?  371 GLN   A CG  1 
ATOM   1324 C  CD  . GLN   A 1 215 ? 16.279 -5.959  -26.991 1.00 75.58  ?  371 GLN   A CD  1 
ATOM   1325 O  OE1 . GLN   A 1 215 ? 16.902 -6.784  -27.660 1.00 76.01  ?  371 GLN   A OE1 1 
ATOM   1326 N  NE2 . GLN   A 1 215 ? 15.467 -6.307  -26.003 1.00 70.50  ?  371 GLN   A NE2 1 
ATOM   1327 N  N   . GLU   A 1 216 ? 16.053 -1.318  -29.153 1.00 57.90  ?  372 GLU   A N   1 
ATOM   1328 C  CA  . GLU   A 1 216 ? 15.785 0.114   -29.262 1.00 76.05  ?  372 GLU   A CA  1 
ATOM   1329 C  C   . GLU   A 1 216 ? 15.264 0.774   -27.989 1.00 66.63  ?  372 GLU   A C   1 
ATOM   1330 O  O   . GLU   A 1 216 ? 15.117 2.002   -27.975 1.00 66.75  ?  372 GLU   A O   1 
ATOM   1331 C  CB  . GLU   A 1 216 ? 14.779 0.374   -30.392 1.00 55.01  ?  372 GLU   A CB  1 
ATOM   1332 N  N   . GLU   A 1 217 ? 14.968 0.020   -26.932 1.00 66.33  ?  373 GLU   A N   1 
ATOM   1333 C  CA  . GLU   A 1 217 ? 14.386 0.603   -25.728 1.00 52.26  ?  373 GLU   A CA  1 
ATOM   1334 C  C   . GLU   A 1 217 ? 15.342 0.572   -24.541 1.00 52.84  ?  373 GLU   A C   1 
ATOM   1335 O  O   . GLU   A 1 217 ? 14.903 0.528   -23.389 1.00 52.74  ?  373 GLU   A O   1 
ATOM   1336 C  CB  . GLU   A 1 217 ? 13.077 -0.095  -25.362 1.00 54.60  ?  373 GLU   A CB  1 
ATOM   1337 C  CG  . GLU   A 1 217 ? 11.961 0.022   -26.393 1.00 57.12  ?  373 GLU   A CG  1 
ATOM   1338 C  CD  . GLU   A 1 217 ? 11.775 1.433   -26.926 1.00 70.48  ?  373 GLU   A CD  1 
ATOM   1339 O  OE1 . GLU   A 1 217 ? 11.972 2.403   -26.166 1.00 64.18  ?  373 GLU   A OE1 1 
ATOM   1340 O  OE2 . GLU   A 1 217 ? 11.411 1.571   -28.113 1.00 74.78  -1 373 GLU   A OE2 1 
ATOM   1341 N  N   . THR   A 1 218 ? 16.645 0.606   -24.797 1.00 48.11  ?  374 THR   A N   1 
ATOM   1342 C  CA  . THR   A 1 218 ? 17.634 0.545   -23.733 1.00 46.05  ?  374 THR   A CA  1 
ATOM   1343 C  C   . THR   A 1 218 ? 18.097 1.942   -23.337 1.00 44.37  ?  374 THR   A C   1 
ATOM   1344 O  O   . THR   A 1 218 ? 18.071 2.881   -24.136 1.00 44.44  ?  374 THR   A O   1 
ATOM   1345 C  CB  . THR   A 1 218 ? 18.843 -0.302  -24.143 1.00 44.98  ?  374 THR   A CB  1 
ATOM   1346 O  OG1 . THR   A 1 218 ? 19.361 0.160   -25.398 1.00 44.72  ?  374 THR   A OG1 1 
ATOM   1347 C  CG2 . THR   A 1 218 ? 18.460 -1.775  -24.255 1.00 46.49  ?  374 THR   A CG2 1 
ATOM   1348 N  N   . TRP   A 1 219 ? 18.518 2.064   -22.081 1.00 43.00  ?  375 TRP   A N   1 
ATOM   1349 C  CA  . TRP   A 1 219 ? 19.086 3.288   -21.536 1.00 41.30  ?  375 TRP   A CA  1 
ATOM   1350 C  C   . TRP   A 1 219 ? 20.509 2.998   -21.076 1.00 40.02  ?  375 TRP   A C   1 
ATOM   1351 O  O   . TRP   A 1 219 ? 20.797 1.906   -20.576 1.00 40.63  ?  375 TRP   A O   1 
ATOM   1352 C  CB  . TRP   A 1 219 ? 18.237 3.817   -20.370 1.00 41.94  ?  375 TRP   A CB  1 
ATOM   1353 C  CG  . TRP   A 1 219 ? 16.800 4.097   -20.735 1.00 45.67  ?  375 TRP   A CG  1 
ATOM   1354 C  CD1 . TRP   A 1 219 ? 15.810 3.175   -20.926 1.00 50.43  ?  375 TRP   A CD1 1 
ATOM   1355 C  CD2 . TRP   A 1 219 ? 16.187 5.382   -20.919 1.00 50.95  ?  375 TRP   A CD2 1 
ATOM   1356 N  NE1 . TRP   A 1 219 ? 14.628 3.802   -21.233 1.00 47.57  ?  375 TRP   A NE1 1 
ATOM   1357 C  CE2 . TRP   A 1 219 ? 14.830 5.156   -21.233 1.00 48.47  ?  375 TRP   A CE2 1 
ATOM   1358 C  CE3 . TRP   A 1 219 ? 16.653 6.699   -20.856 1.00 48.08  ?  375 TRP   A CE3 1 
ATOM   1359 C  CZ2 . TRP   A 1 219 ? 13.938 6.197   -21.483 1.00 47.84  ?  375 TRP   A CZ2 1 
ATOM   1360 C  CZ3 . TRP   A 1 219 ? 15.763 7.732   -21.104 1.00 44.24  ?  375 TRP   A CZ3 1 
ATOM   1361 C  CH2 . TRP   A 1 219 ? 14.422 7.474   -21.415 1.00 48.45  ?  375 TRP   A CH2 1 
ATOM   1362 N  N   . ARG   A 1 220 ? 21.399 3.971   -21.249 1.00 37.74  ?  376 ARG   A N   1 
ATOM   1363 C  CA  . ARG   A 1 220 ? 22.818 3.808   -20.970 1.00 35.87  ?  376 ARG   A CA  1 
ATOM   1364 C  C   . ARG   A 1 220 ? 23.231 4.687   -19.799 1.00 34.94  ?  376 ARG   A C   1 
ATOM   1365 O  O   . ARG   A 1 220 ? 22.797 5.838   -19.689 1.00 36.06  ?  376 ARG   A O   1 
ATOM   1366 C  CB  . ARG   A 1 220 ? 23.670 4.150   -22.195 1.00 40.93  ?  376 ARG   A CB  1 
ATOM   1367 C  CG  . ARG   A 1 220 ? 25.152 3.868   -22.004 1.00 41.08  ?  376 ARG   A CG  1 
ATOM   1368 C  CD  . ARG   A 1 220 ? 25.937 4.084   -23.284 1.00 33.39  ?  376 ARG   A CD  1 
ATOM   1369 N  NE  . ARG   A 1 220 ? 26.099 5.499   -23.594 1.00 40.81  ?  376 ARG   A NE  1 
ATOM   1370 C  CZ  . ARG   A 1 220 ? 26.541 5.964   -24.754 1.00 50.58  ?  376 ARG   A CZ  1 
ATOM   1371 N  NH1 . ARG   A 1 220 ? 26.883 5.150   -25.740 1.00 44.97  ?  376 ARG   A NH1 1 
ATOM   1372 N  NH2 . ARG   A 1 220 ? 26.649 7.279   -24.927 1.00 40.56  ?  376 ARG   A NH2 1 
ATOM   1373 N  N   . LEU   A 1 221 ? 24.084 4.131   -18.939 1.00 33.22  ?  377 LEU   A N   1 
ATOM   1374 C  CA  . LEU   A 1 221 ? 24.546 4.837   -17.752 1.00 40.09  ?  377 LEU   A CA  1 
ATOM   1375 C  C   . LEU   A 1 221 ? 25.351 6.073   -18.127 1.00 49.19  ?  377 LEU   A C   1 
ATOM   1376 O  O   . LEU   A 1 221 ? 26.145 6.064   -19.073 1.00 37.02  ?  377 LEU   A O   1 
ATOM   1377 C  CB  . LEU   A 1 221 ? 25.394 3.904   -16.887 1.00 33.19  ?  377 LEU   A CB  1 
ATOM   1378 C  CG  . LEU   A 1 221 ? 24.612 2.870   -16.077 1.00 42.33  ?  377 LEU   A CG  1 
ATOM   1379 C  CD1 . LEU   A 1 221 ? 25.561 1.975   -15.304 1.00 31.16  ?  377 LEU   A CD1 1 
ATOM   1380 C  CD2 . LEU   A 1 221 ? 23.650 3.567   -15.133 1.00 41.40  ?  377 LEU   A CD2 1 
ATOM   1381 N  N   . SER   A 1 222 ? 25.142 7.145   -17.369 1.00 39.54  ?  378 SER   A N   1 
ATOM   1382 C  CA  . SER   A 1 222 ? 25.860 8.393   -17.554 1.00 40.79  ?  378 SER   A CA  1 
ATOM   1383 C  C   . SER   A 1 222 ? 26.310 8.905   -16.195 1.00 33.96  ?  378 SER   A C   1 
ATOM   1384 O  O   . SER   A 1 222 ? 25.514 8.966   -15.239 1.00 31.66  ?  378 SER   A O   1 
ATOM   1385 C  CB  . SER   A 1 222 ? 25.004 9.443   -18.267 1.00 39.06  ?  378 SER   A CB  1 
ATOM   1386 O  OG  . SER   A 1 222 ? 25.727 10.653  -18.425 1.00 36.77  ?  378 SER   A OG  1 
ATOM   1387 N  N   . PHE   A 1 223 ? 27.602 9.248   -16.129 1.00 31.88  ?  379 PHE   A N   1 
ATOM   1388 C  CA  . PHE   A 1 223 ? 28.259 9.818   -14.960 1.00 31.19  ?  379 PHE   A CA  1 
ATOM   1389 C  C   . PHE   A 1 223 ? 28.968 11.123  -15.306 1.00 29.30  ?  379 PHE   A C   1 
ATOM   1390 O  O   . PHE   A 1 223 ? 29.962 11.469  -14.661 1.00 35.05  ?  379 PHE   A O   1 
ATOM   1391 C  CB  . PHE   A 1 223 ? 29.264 8.823   -14.376 1.00 37.60  ?  379 PHE   A CB  1 
ATOM   1392 C  CG  . PHE   A 1 223 ? 28.637 7.570   -13.844 1.00 31.75  ?  379 PHE   A CG  1 
ATOM   1393 C  CD1 . PHE   A 1 223 ? 28.031 7.559   -12.601 1.00 29.63  ?  379 PHE   A CD1 1 
ATOM   1394 C  CD2 . PHE   A 1 223 ? 28.640 6.407   -14.596 1.00 30.23  ?  379 PHE   A CD2 1 
ATOM   1395 C  CE1 . PHE   A 1 223 ? 27.453 6.406   -12.108 1.00 28.95  ?  379 PHE   A CE1 1 
ATOM   1396 C  CE2 . PHE   A 1 223 ? 28.062 5.253   -14.112 1.00 36.67  ?  379 PHE   A CE2 1 
ATOM   1397 C  CZ  . PHE   A 1 223 ? 27.467 5.252   -12.865 1.00 32.49  ?  379 PHE   A CZ  1 
ATOM   1398 N  N   . SER   A 1 224 ? 28.486 11.842  -16.322 1.00 36.90  ?  380 SER   A N   1 
ATOM   1399 C  CA  . SER   A 1 224 ? 29.158 13.061  -16.765 1.00 44.19  ?  380 SER   A CA  1 
ATOM   1400 C  C   . SER   A 1 224 ? 29.284 14.085  -15.645 1.00 32.51  ?  380 SER   A C   1 
ATOM   1401 O  O   . SER   A 1 224 ? 30.254 14.854  -15.603 1.00 31.19  ?  380 SER   A O   1 
ATOM   1402 C  CB  . SER   A 1 224 ? 28.405 13.657  -17.957 1.00 43.14  ?  380 SER   A CB  1 
ATOM   1403 O  OG  . SER   A 1 224 ? 27.199 14.272  -17.540 1.00 62.60  ?  380 SER   A OG  1 
ATOM   1404 N  N   . HIS   A 1 225 ? 28.320 14.103  -14.725 1.00 32.03  ?  381 HIS   A N   1 
ATOM   1405 C  CA  . HIS   A 1 225 ? 28.394 15.015  -13.591 1.00 28.04  ?  381 HIS   A CA  1 
ATOM   1406 C  C   . HIS   A 1 225 ? 29.592 14.697  -12.702 1.00 26.50  ?  381 HIS   A C   1 
ATOM   1407 O  O   . HIS   A 1 225 ? 30.281 15.608  -12.225 1.00 29.75  ?  381 HIS   A O   1 
ATOM   1408 C  CB  . HIS   A 1 225 ? 27.086 14.961  -12.799 1.00 36.50  ?  381 HIS   A CB  1 
ATOM   1409 C  CG  . HIS   A 1 225 ? 26.721 13.590  -12.315 1.00 31.43  ?  381 HIS   A CG  1 
ATOM   1410 N  ND1 . HIS   A 1 225 ? 26.632 12.499  -13.153 1.00 27.98  ?  381 HIS   A ND1 1 
ATOM   1411 C  CD2 . HIS   A 1 225 ? 26.407 13.138  -11.078 1.00 26.98  ?  381 HIS   A CD2 1 
ATOM   1412 C  CE1 . HIS   A 1 225 ? 26.290 11.433  -12.452 1.00 35.50  ?  381 HIS   A CE1 1 
ATOM   1413 N  NE2 . HIS   A 1 225 ? 26.146 11.794  -11.189 1.00 33.49  ?  381 HIS   A NE2 1 
ATOM   1414 N  N   . ILE   A 1 226 ? 29.874 13.410  -12.488 1.00 25.02  ?  382 ILE   A N   1 
ATOM   1415 C  CA  . ILE   A 1 226 ? 31.025 13.040  -11.672 1.00 20.98  ?  382 ILE   A CA  1 
ATOM   1416 C  C   . ILE   A 1 226 ? 32.322 13.408  -12.379 1.00 29.72  ?  382 ILE   A C   1 
ATOM   1417 O  O   . ILE   A 1 226 ? 33.278 13.879  -11.747 1.00 28.28  ?  382 ILE   A O   1 
ATOM   1418 C  CB  . ILE   A 1 226 ? 30.979 11.543  -11.323 1.00 23.30  ?  382 ILE   A CB  1 
ATOM   1419 C  CG1 . ILE   A 1 226 ? 29.617 11.170  -10.735 1.00 22.16  ?  382 ILE   A CG1 1 
ATOM   1420 C  CG2 . ILE   A 1 226 ? 32.097 11.201  -10.354 1.00 20.05  ?  382 ILE   A CG2 1 
ATOM   1421 C  CD1 . ILE   A 1 226 ? 29.302 11.867  -9.431  1.00 23.37  ?  382 ILE   A CD1 1 
ATOM   1422 N  N   . GLU   A 1 227 ? 32.380 13.190  -13.697 1.00 27.38  ?  383 GLU   A N   1 
ATOM   1423 C  CA  . GLU   A 1 227 ? 33.553 13.591  -14.465 1.00 31.16  ?  383 GLU   A CA  1 
ATOM   1424 C  C   . GLU   A 1 227 ? 33.815 15.079  -14.292 1.00 26.94  ?  383 GLU   A C   1 
ATOM   1425 O  O   . GLU   A 1 227 ? 34.949 15.503  -14.036 1.00 29.40  ?  383 GLU   A O   1 
ATOM   1426 C  CB  . GLU   A 1 227 ? 33.362 13.263  -15.949 1.00 32.12  ?  383 GLU   A CB  1 
ATOM   1427 C  CG  . GLU   A 1 227 ? 33.021 11.816  -16.264 1.00 47.82  ?  383 GLU   A CG  1 
ATOM   1428 C  CD  . GLU   A 1 227 ? 32.299 11.669  -17.595 1.00 47.91  ?  383 GLU   A CD  1 
ATOM   1429 O  OE1 . GLU   A 1 227 ? 31.938 12.700  -18.202 1.00 56.01  ?  383 GLU   A OE1 1 
ATOM   1430 O  OE2 . GLU   A 1 227 ? 32.084 10.516  -18.027 1.00 51.41  -1 383 GLU   A OE2 1 
ATOM   1431 N  N   . LYS   A 1 228 ? 32.762 15.888  -14.423 1.00 28.81  ?  384 LYS   A N   1 
ATOM   1432 C  CA  . LYS   A 1 228 ? 32.908 17.331  -14.261 1.00 28.89  ?  384 LYS   A CA  1 
ATOM   1433 C  C   . LYS   A 1 228 ? 33.395 17.689  -12.862 1.00 33.44  ?  384 LYS   A C   1 
ATOM   1434 O  O   . LYS   A 1 228 ? 34.325 18.487  -12.702 1.00 34.06  ?  384 LYS   A O   1 
ATOM   1435 C  CB  . LYS   A 1 228 ? 31.583 18.033  -14.557 1.00 36.97  ?  384 LYS   A CB  1 
ATOM   1436 C  CG  . LYS   A 1 228 ? 31.720 19.540  -14.652 1.00 43.45  ?  384 LYS   A CG  1 
ATOM   1437 C  CD  . LYS   A 1 228 ? 30.577 20.242  -13.943 1.00 57.43  ?  384 LYS   A CD  1 
ATOM   1438 C  CE  . LYS   A 1 228 ? 29.729 21.037  -14.918 1.00 62.34  ?  384 LYS   A CE  1 
ATOM   1439 N  NZ  . LYS   A 1 228 ? 28.799 21.971  -14.222 1.00 58.02  ?  384 LYS   A NZ  1 
ATOM   1440 N  N   . GLU   A 1 229 ? 32.772 17.111  -11.830 1.00 25.63  ?  385 GLU   A N   1 
ATOM   1441 C  CA  . GLU   A 1 229 ? 33.163 17.446  -10.463 1.00 29.04  ?  385 GLU   A CA  1 
ATOM   1442 C  C   . GLU   A 1 229 ? 34.617 17.082  -10.192 1.00 33.15  ?  385 GLU   A C   1 
ATOM   1443 O  O   . GLU   A 1 229 ? 35.319 17.791  -9.461  1.00 23.56  ?  385 GLU   A O   1 
ATOM   1444 C  CB  . GLU   A 1 229 ? 32.250 16.750  -9.456  1.00 31.67  ?  385 GLU   A CB  1 
ATOM   1445 C  CG  . GLU   A 1 229 ? 32.462 17.258  -8.033  1.00 50.50  ?  385 GLU   A CG  1 
ATOM   1446 C  CD  . GLU   A 1 229 ? 31.366 16.831  -7.081  1.00 58.13  ?  385 GLU   A CD  1 
ATOM   1447 O  OE1 . GLU   A 1 229 ? 30.317 16.347  -7.550  1.00 51.29  ?  385 GLU   A OE1 1 
ATOM   1448 O  OE2 . GLU   A 1 229 ? 31.556 16.980  -5.853  1.00 81.14  -1 385 GLU   A OE2 1 
ATOM   1449 N  N   . ILE   A 1 230 ? 35.089 15.979  -10.772 1.00 30.10  ?  386 ILE   A N   1 
ATOM   1450 C  CA  . ILE   A 1 230 ? 36.484 15.604  -10.573 1.00 26.56  ?  386 ILE   A CA  1 
ATOM   1451 C  C   . ILE   A 1 230 ? 37.406 16.562  -11.316 1.00 39.56  ?  386 ILE   A C   1 
ATOM   1452 O  O   . ILE   A 1 230 ? 38.434 16.991  -10.781 1.00 44.67  ?  386 ILE   A O   1 
ATOM   1453 C  CB  . ILE   A 1 230 ? 36.713 14.144  -10.996 1.00 33.87  ?  386 ILE   A CB  1 
ATOM   1454 C  CG1 . ILE   A 1 230 ? 36.138 13.194  -9.948  1.00 22.77  ?  386 ILE   A CG1 1 
ATOM   1455 C  CG2 . ILE   A 1 230 ? 38.186 13.872  -11.193 1.00 37.30  ?  386 ILE   A CG2 1 
ATOM   1456 C  CD1 . ILE   A 1 230 ? 36.262 11.745  -10.328 1.00 33.25  ?  386 ILE   A CD1 1 
ATOM   1457 N  N   . LEU   A 1 231 ? 37.047 16.932  -12.548 1.00 30.10  ?  387 LEU   A N   1 
ATOM   1458 C  CA  . LEU   A 1 231 ? 37.923 17.795  -13.335 1.00 28.64  ?  387 LEU   A CA  1 
ATOM   1459 C  C   . LEU   A 1 231 ? 38.112 19.165  -12.698 1.00 27.75  ?  387 LEU   A C   1 
ATOM   1460 O  O   . LEU   A 1 231 ? 39.185 19.763  -12.827 1.00 33.30  ?  387 LEU   A O   1 
ATOM   1461 C  CB  . LEU   A 1 231 ? 37.375 17.951  -14.748 1.00 27.91  ?  387 LEU   A CB  1 
ATOM   1462 C  CG  . LEU   A 1 231 ? 38.100 17.093  -15.775 1.00 38.85  ?  387 LEU   A CG  1 
ATOM   1463 C  CD1 . LEU   A 1 231 ? 37.214 16.910  -16.989 1.00 40.33  ?  387 LEU   A CD1 1 
ATOM   1464 C  CD2 . LEU   A 1 231 ? 39.433 17.732  -16.135 1.00 37.19  ?  387 LEU   A CD2 1 
ATOM   1465 N  N   . ASN   A 1 232 ? 37.091 19.679  -12.017 1.00 25.83  ?  388 ASN   A N   1 
ATOM   1466 C  CA  . ASN   A 1 232 ? 37.156 20.995  -11.394 1.00 39.41  ?  388 ASN   A CA  1 
ATOM   1467 C  C   . ASN   A 1 232 ? 37.591 20.941  -9.934  1.00 28.29  ?  388 ASN   A C   1 
ATOM   1468 O  O   . ASN   A 1 232 ? 37.671 21.990  -9.286  1.00 30.69  ?  388 ASN   A O   1 
ATOM   1469 C  CB  . ASN   A 1 232 ? 35.796 21.691  -11.505 1.00 22.85  ?  388 ASN   A CB  1 
ATOM   1470 C  CG  . ASN   A 1 232 ? 35.491 22.149  -12.920 1.00 37.62  ?  388 ASN   A CG  1 
ATOM   1471 O  OD1 . ASN   A 1 232 ? 36.327 22.764  -13.580 1.00 49.87  ?  388 ASN   A OD1 1 
ATOM   1472 N  ND2 . ASN   A 1 232 ? 34.290 21.840  -13.395 1.00 48.83  ?  388 ASN   A ND2 1 
ATOM   1473 N  N   . ASN   A 1 233 ? 37.869 19.747  -9.408  1.00 24.97  ?  389 ASN   A N   1 
ATOM   1474 C  CA  . ASN   A 1 233 ? 38.335 19.503  -8.046  1.00 22.12  ?  389 ASN   A CA  1 
ATOM   1475 C  C   . ASN   A 1 233 ? 39.248 18.278  -8.150  1.00 19.71  ?  389 ASN   A C   1 
ATOM   1476 O  O   . ASN   A 1 233 ? 38.918 17.168  -7.733  1.00 19.59  ?  389 ASN   A O   1 
ATOM   1477 C  CB  . ASN   A 1 233 ? 37.168 19.286  -7.078  1.00 21.02  ?  389 ASN   A CB  1 
ATOM   1478 C  CG  . ASN   A 1 233 ? 37.599 19.277  -5.623  1.00 17.27  ?  389 ASN   A CG  1 
ATOM   1479 O  OD1 . ASN   A 1 233 ? 38.789 19.334  -5.314  1.00 22.02  ?  389 ASN   A OD1 1 
ATOM   1480 N  ND2 . ASN   A 1 233 ? 36.627 19.213  -4.721  1.00 15.34  ?  389 ASN   A ND2 1 
ATOM   1481 N  N   . HIS   A 1 234 ? 40.433 18.493  -8.726  1.00 22.34  ?  390 HIS   A N   1 
ATOM   1482 C  CA  . HIS   A 1 234 ? 41.197 17.437  -9.376  1.00 19.14  ?  390 HIS   A CA  1 
ATOM   1483 C  C   . HIS   A 1 234 ? 42.495 17.061  -8.675  1.00 21.68  ?  390 HIS   A C   1 
ATOM   1484 O  O   . HIS   A 1 234 ? 43.160 16.116  -9.113  1.00 19.60  ?  390 HIS   A O   1 
ATOM   1485 C  CB  . HIS   A 1 234 ? 41.516 17.855  -10.817 1.00 17.00  ?  390 HIS   A CB  1 
ATOM   1486 C  CG  . HIS   A 1 234 ? 42.255 19.155  -10.913 1.00 17.61  ?  390 HIS   A CG  1 
ATOM   1487 N  ND1 . HIS   A 1 234 ? 41.749 20.250  -11.580 1.00 18.12  ?  390 HIS   A ND1 1 
ATOM   1488 C  CD2 . HIS   A 1 234 ? 43.461 19.536  -10.427 1.00 17.94  ?  390 HIS   A CD2 1 
ATOM   1489 C  CE1 . HIS   A 1 234 ? 42.610 21.249  -11.499 1.00 21.58  ?  390 HIS   A CE1 1 
ATOM   1490 N  NE2 . HIS   A 1 234 ? 43.658 20.842  -10.805 1.00 23.42  ?  390 HIS   A NE2 1 
ATOM   1491 N  N   . GLY   A 1 235 ? 42.892 17.773  -7.629  1.00 18.93  ?  391 GLY   A N   1 
ATOM   1492 C  CA  . GLY   A 1 235 ? 44.170 17.536  -6.999  1.00 18.71  ?  391 GLY   A CA  1 
ATOM   1493 C  C   . GLY   A 1 235 ? 44.068 16.652  -5.771  1.00 23.43  ?  391 GLY   A C   1 
ATOM   1494 O  O   . GLY   A 1 235 ? 42.994 16.455  -5.209  1.00 19.51  ?  391 GLY   A O   1 
ATOM   1495 N  N   . LYS   A 1 236 ? 45.213 16.097  -5.368  1.00 23.29  ?  392 LYS   A N   1 
ATOM   1496 C  CA  . LYS   A 1 236 ? 45.286 15.467  -4.054  1.00 15.10  ?  392 LYS   A CA  1 
ATOM   1497 C  C   . LYS   A 1 236 ? 45.238 16.521  -2.957  1.00 20.35  ?  392 LYS   A C   1 
ATOM   1498 O  O   . LYS   A 1 236 ? 44.632 16.304  -1.900  1.00 23.38  ?  392 LYS   A O   1 
ATOM   1499 C  CB  . LYS   A 1 236 ? 46.551 14.617  -3.937  1.00 19.95  ?  392 LYS   A CB  1 
ATOM   1500 C  CG  . LYS   A 1 236 ? 46.804 14.085  -2.528  1.00 26.31  ?  392 LYS   A CG  1 
ATOM   1501 C  CD  . LYS   A 1 236 ? 48.054 13.223  -2.460  1.00 24.25  ?  392 LYS   A CD  1 
ATOM   1502 C  CE  . LYS   A 1 236 ? 47.797 11.846  -3.053  1.00 21.58  ?  392 LYS   A CE  1 
ATOM   1503 N  NZ  . LYS   A 1 236 ? 46.571 11.218  -2.485  1.00 31.09  ?  392 LYS   A NZ  1 
ATOM   1504 N  N   . SER   A 1 237 ? 45.863 17.671  -3.196  1.00 21.56  ?  393 SER   A N   1 
ATOM   1505 C  CA  . SER   A 1 237 ? 45.739 18.809  -2.299  1.00 29.44  ?  393 SER   A CA  1 
ATOM   1506 C  C   . SER   A 1 237 ? 44.455 19.569  -2.601  1.00 23.20  ?  393 SER   A C   1 
ATOM   1507 O  O   . SER   A 1 237 ? 44.102 19.783  -3.764  1.00 17.37  ?  393 SER   A O   1 
ATOM   1508 C  CB  . SER   A 1 237 ? 46.942 19.740  -2.442  1.00 17.99  ?  393 SER   A CB  1 
ATOM   1509 O  OG  . SER   A 1 237 ? 46.687 20.995  -1.833  1.00 18.92  ?  393 SER   A OG  1 
ATOM   1510 N  N   . LYS   A 1 238 ? 43.752 19.973  -1.541  1.00 21.83  ?  394 LYS   A N   1 
ATOM   1511 C  CA  . LYS   A 1 238 ? 42.499 20.694  -1.727  1.00 18.47  ?  394 LYS   A CA  1 
ATOM   1512 C  C   . LYS   A 1 238 ? 42.732 22.075  -2.328  1.00 18.47  ?  394 LYS   A C   1 
ATOM   1513 O  O   . LYS   A 1 238 ? 41.846 22.610  -3.006  1.00 18.00  ?  394 LYS   A O   1 
ATOM   1514 C  CB  . LYS   A 1 238 ? 41.755 20.803  -0.395  1.00 20.65  ?  394 LYS   A CB  1 
ATOM   1515 C  CG  . LYS   A 1 238 ? 41.166 19.488  0.087   1.00 20.70  ?  394 LYS   A CG  1 
ATOM   1516 C  CD  . LYS   A 1 238 ? 40.802 19.542  1.562   1.00 14.55  ?  394 LYS   A CD  1 
ATOM   1517 C  CE  . LYS   A 1 238 ? 40.327 18.185  2.056   1.00 15.20  ?  394 LYS   A CE  1 
ATOM   1518 N  NZ  . LYS   A 1 238 ? 40.113 18.178  3.528   1.00 24.60  ?  394 LYS   A NZ  1 
ATOM   1519 N  N   . THR   A 1 239 ? 43.908 22.664  -2.097  1.00 16.59  ?  395 THR   A N   1 
ATOM   1520 C  CA  . THR   A 1 239 ? 44.256 23.965  -2.651  1.00 27.41  ?  395 THR   A CA  1 
ATOM   1521 C  C   . THR   A 1 239 ? 45.013 23.856  -3.969  1.00 25.56  ?  395 THR   A C   1 
ATOM   1522 O  O   . THR   A 1 239 ? 45.684 24.814  -4.367  1.00 14.51  ?  395 THR   A O   1 
ATOM   1523 C  CB  . THR   A 1 239 ? 45.085 24.774  -1.650  1.00 21.83  ?  395 THR   A CB  1 
ATOM   1524 O  OG1 . THR   A 1 239 ? 46.101 23.940  -1.077  1.00 23.60  ?  395 THR   A OG1 1 
ATOM   1525 C  CG2 . THR   A 1 239 ? 44.207 25.338  -0.546  1.00 19.57  ?  395 THR   A CG2 1 
ATOM   1526 N  N   . CYS   A 1 240 ? 44.936 22.709  -4.643  1.00 19.95  ?  396 CYS   A N   1 
ATOM   1527 C  CA  . CYS   A 1 240 ? 45.563 22.575  -5.951  1.00 24.23  ?  396 CYS   A CA  1 
ATOM   1528 C  C   . CYS   A 1 240 ? 45.033 23.641  -6.896  1.00 24.25  ?  396 CYS   A C   1 
ATOM   1529 O  O   . CYS   A 1 240 ? 43.819 23.792  -7.062  1.00 30.67  ?  396 CYS   A O   1 
ATOM   1530 C  CB  . CYS   A 1 240 ? 45.308 21.184  -6.531  1.00 30.23  ?  396 CYS   A CB  1 
ATOM   1531 S  SG  . CYS   A 1 240 ? 46.159 20.881  -8.104  1.00 23.72  ?  396 CYS   A SG  1 
ATOM   1532 N  N   . CYS   A 1 241 ? 45.957 24.398  -7.488  1.00 20.48  ?  397 CYS   A N   1 
ATOM   1533 C  CA  . CYS   A 1 241 ? 45.674 25.442  -8.468  1.00 21.57  ?  397 CYS   A CA  1 
ATOM   1534 C  C   . CYS   A 1 241 ? 45.017 26.674  -7.856  1.00 26.90  ?  397 CYS   A C   1 
ATOM   1535 O  O   . CYS   A 1 241 ? 44.478 27.511  -8.586  1.00 25.27  ?  397 CYS   A O   1 
ATOM   1536 C  CB  . CYS   A 1 241 ? 44.814 24.904  -9.619  1.00 31.38  ?  397 CYS   A CB  1 
ATOM   1537 S  SG  . CYS   A 1 241 ? 45.715 23.823  -10.735 1.00 26.14  ?  397 CYS   A SG  1 
ATOM   1538 N  N   . GLU   A 1 242 ? 45.050 26.816  -6.532  1.00 21.36  ?  398 GLU   A N   1 
ATOM   1539 C  CA  . GLU   A 1 242 ? 44.571 28.024  -5.875  1.00 22.16  ?  398 GLU   A CA  1 
ATOM   1540 C  C   . GLU   A 1 242 ? 45.696 28.984  -5.510  1.00 20.84  ?  398 GLU   A C   1 
ATOM   1541 O  O   . GLU   A 1 242 ? 45.418 30.083  -5.020  1.00 32.18  ?  398 GLU   A O   1 
ATOM   1542 C  CB  . GLU   A 1 242 ? 43.768 27.670  -4.617  1.00 28.13  ?  398 GLU   A CB  1 
ATOM   1543 C  CG  . GLU   A 1 242 ? 42.431 27.014  -4.905  1.00 31.73  ?  398 GLU   A CG  1 
ATOM   1544 C  CD  . GLU   A 1 242 ? 41.549 26.924  -3.678  1.00 30.56  ?  398 GLU   A CD  1 
ATOM   1545 O  OE1 . GLU   A 1 242 ? 42.045 27.204  -2.567  1.00 39.03  ?  398 GLU   A OE1 1 
ATOM   1546 O  OE2 . GLU   A 1 242 ? 40.360 26.573  -3.824  1.00 27.38  -1 398 GLU   A OE2 1 
ATOM   1547 N  N   . ASN   A 1 243 ? 46.951 28.601  -5.741  1.00 26.40  ?  399 ASN   A N   1 
ATOM   1548 C  CA  . ASN   A 1 243 ? 48.091 29.458  -5.447  1.00 24.61  ?  399 ASN   A CA  1 
ATOM   1549 C  C   . ASN   A 1 243 ? 49.225 29.126  -6.407  1.00 24.85  ?  399 ASN   A C   1 
ATOM   1550 O  O   . ASN   A 1 243 ? 49.209 28.094  -7.083  1.00 30.85  ?  399 ASN   A O   1 
ATOM   1551 C  CB  . ASN   A 1 243 ? 48.539 29.308  -3.986  1.00 15.59  ?  399 ASN   A CB  1 
ATOM   1552 C  CG  . ASN   A 1 243 ? 48.949 27.888  -3.639  1.00 27.50  ?  399 ASN   A CG  1 
ATOM   1553 O  OD1 . ASN   A 1 243 ? 49.857 27.321  -4.246  1.00 26.66  ?  399 ASN   A OD1 1 
ATOM   1554 N  ND2 . ASN   A 1 243 ? 48.272 27.302  -2.658  1.00 22.53  ?  399 ASN   A ND2 1 
ATOM   1555 N  N   . LYS   A 1 244 ? 50.217 30.023  -6.457  1.00 24.78  ?  400 LYS   A N   1 
ATOM   1556 C  CA  . LYS   A 1 244 ? 51.342 29.837  -7.372  1.00 27.79  ?  400 LYS   A CA  1 
ATOM   1557 C  C   . LYS   A 1 244 ? 52.156 28.600  -7.025  1.00 28.16  ?  400 LYS   A C   1 
ATOM   1558 O  O   . LYS   A 1 244 ? 52.710 27.949  -7.920  1.00 29.42  ?  400 LYS   A O   1 
ATOM   1559 C  CB  . LYS   A 1 244 ? 52.259 31.059  -7.358  1.00 28.07  ?  400 LYS   A CB  1 
ATOM   1560 C  CG  . LYS   A 1 244 ? 51.729 32.289  -8.063  1.00 35.87  ?  400 LYS   A CG  1 
ATOM   1561 C  CD  . LYS   A 1 244 ? 52.770 33.395  -7.987  1.00 39.92  ?  400 LYS   A CD  1 
ATOM   1562 C  CE  . LYS   A 1 244 ? 52.342 34.649  -8.718  1.00 31.37  ?  400 LYS   A CE  1 
ATOM   1563 N  NZ  . LYS   A 1 244 ? 53.233 35.784  -8.347  1.00 55.20  ?  400 LYS   A NZ  1 
ATOM   1564 N  N   . GLU   A 1 245 ? 52.260 28.273  -5.737  1.00 24.57  ?  401 GLU   A N   1 
ATOM   1565 C  CA  . GLU   A 1 245 ? 53.043 27.119  -5.317  1.00 33.36  ?  401 GLU   A CA  1 
ATOM   1566 C  C   . GLU   A 1 245 ? 52.448 25.804  -5.805  1.00 26.95  ?  401 GLU   A C   1 
ATOM   1567 O  O   . GLU   A 1 245 ? 53.183 24.821  -5.938  1.00 33.69  ?  401 GLU   A O   1 
ATOM   1568 C  CB  . GLU   A 1 245 ? 53.163 27.102  -3.792  1.00 28.85  ?  401 GLU   A CB  1 
ATOM   1569 C  CG  . GLU   A 1 245 ? 54.271 26.216  -3.245  1.00 34.92  ?  401 GLU   A CG  1 
ATOM   1570 C  CD  . GLU   A 1 245 ? 55.657 26.746  -3.568  1.00 64.67  ?  401 GLU   A CD  1 
ATOM   1571 O  OE1 . GLU   A 1 245 ? 55.908 27.945  -3.324  1.00 44.00  ?  401 GLU   A OE1 1 
ATOM   1572 O  OE2 . GLU   A 1 245 ? 56.495 25.964  -4.065  1.00 66.07  -1 401 GLU   A OE2 1 
ATOM   1573 N  N   . GLU   A 1 246 ? 51.149 25.765  -6.090  1.00 23.76  ?  402 GLU   A N   1 
ATOM   1574 C  CA  . GLU   A 1 246 ? 50.444 24.521  -6.385  1.00 28.73  ?  402 GLU   A CA  1 
ATOM   1575 C  C   . GLU   A 1 246 ? 49.715 24.591  -7.717  1.00 24.72  ?  402 GLU   A C   1 
ATOM   1576 O  O   . GLU   A 1 246 ? 48.559 24.178  -7.827  1.00 25.31  ?  402 GLU   A O   1 
ATOM   1577 C  CB  . GLU   A 1 246 ? 49.451 24.180  -5.278  1.00 23.90  ?  402 GLU   A CB  1 
ATOM   1578 C  CG  . GLU   A 1 246 ? 50.039 24.074  -3.891  1.00 24.69  ?  402 GLU   A CG  1 
ATOM   1579 C  CD  . GLU   A 1 246 ? 48.995 23.679  -2.868  1.00 25.83  ?  402 GLU   A CD  1 
ATOM   1580 O  OE1 . GLU   A 1 246 ? 48.654 22.482  -2.798  1.00 30.25  ?  402 GLU   A OE1 1 
ATOM   1581 O  OE2 . GLU   A 1 246 ? 48.505 24.571  -2.144  1.00 27.22  -1 402 GLU   A OE2 1 
ATOM   1582 N  N   . LYS   A 1 247 ? 50.365 25.103  -8.757  1.00 26.70  ?  403 LYS   A N   1 
ATOM   1583 C  CA  . LYS   A 1 247 ? 49.776 25.099  -10.089 1.00 32.62  ?  403 LYS   A CA  1 
ATOM   1584 C  C   . LYS   A 1 247 ? 50.119 23.788  -10.787 1.00 25.71  ?  403 LYS   A C   1 
ATOM   1585 O  O   . LYS   A 1 247 ? 51.294 23.424  -10.889 1.00 23.06  ?  403 LYS   A O   1 
ATOM   1586 C  CB  . LYS   A 1 247 ? 50.266 26.291  -10.914 1.00 27.14  ?  403 LYS   A CB  1 
ATOM   1587 C  CG  . LYS   A 1 247 ? 49.522 27.595  -10.639 1.00 26.15  ?  403 LYS   A CG  1 
ATOM   1588 C  CD  . LYS   A 1 247 ? 48.010 27.398  -10.683 1.00 38.95  ?  403 LYS   A CD  1 
ATOM   1589 C  CE  . LYS   A 1 247 ? 47.268 28.727  -10.673 1.00 30.27  ?  403 LYS   A CE  1 
ATOM   1590 N  NZ  . LYS   A 1 247 ? 48.036 29.788  -9.966  1.00 32.49  ?  403 LYS   A NZ  1 
ATOM   1591 N  N   . CYS   A 1 248 ? 49.093 23.075  -11.245 1.00 24.41  ?  404 CYS   A N   1 
ATOM   1592 C  CA  . CYS   A 1 248 ? 49.270 21.826  -11.974 1.00 19.90  ?  404 CYS   A CA  1 
ATOM   1593 C  C   . CYS   A 1 248 ? 48.762 22.000  -13.400 1.00 25.43  ?  404 CYS   A C   1 
ATOM   1594 O  O   . CYS   A 1 248 ? 48.173 23.024  -13.752 1.00 28.42  ?  404 CYS   A O   1 
ATOM   1595 C  CB  . CYS   A 1 248 ? 48.547 20.661  -11.282 1.00 21.83  ?  404 CYS   A CB  1 
ATOM   1596 S  SG  . CYS   A 1 248 ? 46.824 20.418  -11.788 1.00 19.96  ?  404 CYS   A SG  1 
ATOM   1597 N  N   . CYS   A 1 249 ? 48.993 20.980  -14.231 1.00 21.46  ?  405 CYS   A N   1 
ATOM   1598 C  CA  . CYS   A 1 249 ? 48.660 21.054  -15.651 1.00 26.99  ?  405 CYS   A CA  1 
ATOM   1599 C  C   . CYS   A 1 249 ? 47.675 19.971  -16.078 1.00 28.58  ?  405 CYS   A C   1 
ATOM   1600 O  O   . CYS   A 1 249 ? 47.626 19.621  -17.262 1.00 24.74  ?  405 CYS   A O   1 
ATOM   1601 C  CB  . CYS   A 1 249 ? 49.927 20.970  -16.504 1.00 26.65  ?  405 CYS   A CB  1 
ATOM   1602 S  SG  . CYS   A 1 249 ? 50.886 19.455  -16.273 1.00 24.21  ?  405 CYS   A SG  1 
ATOM   1603 N  N   . ARG   A 1 250 ? 46.889 19.438  -15.141 1.00 16.75  ?  406 ARG   A N   1 
ATOM   1604 C  CA  . ARG   A 1 250 ? 45.925 18.392  -15.475 1.00 24.74  ?  406 ARG   A CA  1 
ATOM   1605 C  C   . ARG   A 1 250 ? 44.936 18.872  -16.537 1.00 16.95  ?  406 ARG   A C   1 
ATOM   1606 O  O   . ARG   A 1 250 ? 44.777 18.243  -17.596 1.00 27.75  ?  406 ARG   A O   1 
ATOM   1607 C  CB  . ARG   A 1 250 ? 45.189 17.950  -14.205 1.00 21.39  ?  406 ARG   A CB  1 
ATOM   1608 C  CG  . ARG   A 1 250 ? 45.991 17.045  -13.257 1.00 14.69  ?  406 ARG   A CG  1 
ATOM   1609 C  CD  . ARG   A 1 250 ? 45.130 16.609  -12.067 1.00 21.08  ?  406 ARG   A CD  1 
ATOM   1610 N  NE  . ARG   A 1 250 ? 45.806 15.696  -11.147 1.00 17.31  ?  406 ARG   A NE  1 
ATOM   1611 C  CZ  . ARG   A 1 250 ? 46.524 16.070  -10.097 1.00 18.33  ?  406 ARG   A CZ  1 
ATOM   1612 N  NH1 . ARG   A 1 250 ? 46.718 17.347  -9.809  1.00 15.43  ?  406 ARG   A NH1 1 
ATOM   1613 N  NH2 . ARG   A 1 250 ? 47.060 15.139  -9.312  1.00 28.05  ?  406 ARG   A NH2 1 
ATOM   1614 N  N   . LYS   A 1 251 ? 44.272 20.001  -16.272 1.00 20.89  ?  407 LYS   A N   1 
ATOM   1615 C  CA  . LYS   A 1 251 ? 43.267 20.521  -17.196 1.00 21.46  ?  407 LYS   A CA  1 
ATOM   1616 C  C   . LYS   A 1 251 ? 43.876 20.851  -18.554 1.00 24.02  ?  407 LYS   A C   1 
ATOM   1617 O  O   . LYS   A 1 251 ? 43.268 20.581  -19.599 1.00 22.99  ?  407 LYS   A O   1 
ATOM   1618 C  CB  . LYS   A 1 251 ? 42.601 21.761  -16.597 1.00 20.86  ?  407 LYS   A CB  1 
ATOM   1619 C  CG  . LYS   A 1 251 ? 41.680 21.487  -15.415 1.00 31.19  ?  407 LYS   A CG  1 
ATOM   1620 C  CD  . LYS   A 1 251 ? 41.064 22.783  -14.899 1.00 27.60  ?  407 LYS   A CD  1 
ATOM   1621 C  CE  . LYS   A 1 251 ? 39.689 22.547  -14.292 1.00 46.27  ?  407 LYS   A CE  1 
ATOM   1622 N  NZ  . LYS   A 1 251 ? 38.974 23.819  -13.988 1.00 44.73  ?  407 LYS   A NZ  1 
ATOM   1623 N  N   . ASP   A 1 252 ? 45.071 21.446  -18.560 1.00 28.29  ?  408 ASP   A N   1 
ATOM   1624 C  CA  . ASP   A 1 252 ? 45.736 21.763  -19.821 1.00 18.94  ?  408 ASP   A CA  1 
ATOM   1625 C  C   . ASP   A 1 252 ? 46.029 20.501  -20.620 1.00 24.18  ?  408 ASP   A C   1 
ATOM   1626 O  O   . ASP   A 1 252 ? 45.841 20.475  -21.842 1.00 25.03  ?  408 ASP   A O   1 
ATOM   1627 C  CB  . ASP   A 1 252 ? 47.028 22.535  -19.554 1.00 33.96  ?  408 ASP   A CB  1 
ATOM   1628 C  CG  . ASP   A 1 252 ? 46.777 23.989  -19.206 1.00 42.78  ?  408 ASP   A CG  1 
ATOM   1629 O  OD1 . ASP   A 1 252 ? 45.699 24.511  -19.560 1.00 50.10  ?  408 ASP   A OD1 1 
ATOM   1630 O  OD2 . ASP   A 1 252 ? 47.663 24.610  -18.582 1.00 71.57  -1 408 ASP   A OD2 1 
ATOM   1631 N  N   . CYS   A 1 253 ? 46.504 19.450  -19.949 1.00 21.84  ?  409 CYS   A N   1 
ATOM   1632 C  CA  . CYS   A 1 253 ? 46.770 18.192  -20.635 1.00 26.15  ?  409 CYS   A CA  1 
ATOM   1633 C  C   . CYS   A 1 253 ? 45.506 17.639  -21.274 1.00 26.42  ?  409 CYS   A C   1 
ATOM   1634 O  O   . CYS   A 1 253 ? 45.527 17.180  -22.426 1.00 21.48  ?  409 CYS   A O   1 
ATOM   1635 C  CB  . CYS   A 1 253 ? 47.357 17.179  -19.655 1.00 28.45  ?  409 CYS   A CB  1 
ATOM   1636 S  SG  . CYS   A 1 253 ? 49.097 17.454  -19.299 1.00 29.52  ?  409 CYS   A SG  1 
ATOM   1637 N  N   . LEU   A 1 254 ? 44.390 17.681  -20.540 1.00 18.62  ?  410 LEU   A N   1 
ATOM   1638 C  CA  . LEU   A 1 254 ? 43.131 17.194  -21.095 1.00 22.42  ?  410 LEU   A CA  1 
ATOM   1639 C  C   . LEU   A 1 254 ? 42.708 18.012  -22.311 1.00 22.54  ?  410 LEU   A C   1 
ATOM   1640 O  O   . LEU   A 1 254 ? 42.268 17.457  -23.328 1.00 29.20  ?  410 LEU   A O   1 
ATOM   1641 C  CB  . LEU   A 1 254 ? 42.035 17.222  -20.034 1.00 26.64  ?  410 LEU   A CB  1 
ATOM   1642 C  CG  . LEU   A 1 254 ? 40.689 16.766  -20.599 1.00 39.11  ?  410 LEU   A CG  1 
ATOM   1643 C  CD1 . LEU   A 1 254 ? 40.794 15.361  -21.179 1.00 23.93  ?  410 LEU   A CD1 1 
ATOM   1644 C  CD2 . LEU   A 1 254 ? 39.603 16.840  -19.558 1.00 26.59  ?  410 LEU   A CD2 1 
ATOM   1645 N  N   . LYS   A 1 255 ? 42.807 19.342  -22.210 1.00 22.86  ?  411 LYS   A N   1 
ATOM   1646 C  CA  . LYS   A 1 255 ? 42.427 20.195  -23.332 1.00 21.46  ?  411 LYS   A CA  1 
ATOM   1647 C  C   . LYS   A 1 255 ? 43.289 19.911  -24.555 1.00 26.22  ?  411 LYS   A C   1 
ATOM   1648 O  O   . LYS   A 1 255 ? 42.782 19.867  -25.682 1.00 22.78  ?  411 LYS   A O   1 
ATOM   1649 C  CB  . LYS   A 1 255 ? 42.524 21.670  -22.942 1.00 21.58  ?  411 LYS   A CB  1 
ATOM   1650 C  CG  . LYS   A 1 255 ? 41.430 22.143  -22.000 1.00 32.62  ?  411 LYS   A CG  1 
ATOM   1651 C  CD  . LYS   A 1 255 ? 41.758 23.506  -21.416 1.00 44.52  ?  411 LYS   A CD  1 
ATOM   1652 C  CE  . LYS   A 1 255 ? 40.497 24.247  -21.021 1.00 54.31  ?  411 LYS   A CE  1 
ATOM   1653 N  NZ  . LYS   A 1 255 ? 39.653 23.409  -20.127 1.00 56.25  ?  411 LYS   A NZ  1 
ATOM   1654 N  N   . LEU   A 1 256 ? 44.594 19.714  -24.355 1.00 21.65  ?  412 LEU   A N   1 
ATOM   1655 C  CA  . LEU   A 1 256 ? 45.473 19.431  -25.485 1.00 24.10  ?  412 LEU   A CA  1 
ATOM   1656 C  C   . LEU   A 1 256 ? 45.132 18.092  -26.125 1.00 22.53  ?  412 LEU   A C   1 
ATOM   1657 O  O   . LEU   A 1 256 ? 45.162 17.959  -27.353 1.00 24.43  ?  412 LEU   A O   1 
ATOM   1658 C  CB  . LEU   A 1 256 ? 46.933 19.459  -25.039 1.00 26.84  ?  412 LEU   A CB  1 
ATOM   1659 C  CG  . LEU   A 1 256 ? 47.481 20.825  -24.627 1.00 23.64  ?  412 LEU   A CG  1 
ATOM   1660 C  CD1 . LEU   A 1 256 ? 48.787 20.671  -23.868 1.00 23.44  ?  412 LEU   A CD1 1 
ATOM   1661 C  CD2 . LEU   A 1 256 ? 47.667 21.704  -25.852 1.00 25.44  ?  412 LEU   A CD2 1 
ATOM   1662 N  N   . MET   A 1 257 ? 44.797 17.090  -25.309 1.00 21.20  ?  413 MET   A N   1 
ATOM   1663 C  CA  . MET   A 1 257 ? 44.403 15.795  -25.856 1.00 23.60  ?  413 MET   A CA  1 
ATOM   1664 C  C   . MET   A 1 257 ? 43.127 15.915  -26.688 1.00 22.35  ?  413 MET   A C   1 
ATOM   1665 O  O   . MET   A 1 257 ? 43.049 15.406  -27.819 1.00 26.93  ?  413 MET   A O   1 
ATOM   1666 C  CB  . MET   A 1 257 ? 44.221 14.794  -24.714 1.00 20.53  ?  413 MET   A CB  1 
ATOM   1667 C  CG  . MET   A 1 257 ? 45.503 14.115  -24.262 1.00 30.39  ?  413 MET   A CG  1 
ATOM   1668 S  SD  . MET   A 1 257 ? 46.294 13.166  -25.576 1.00 47.81  ?  413 MET   A SD  1 
ATOM   1669 C  CE  . MET   A 1 257 ? 44.940 12.106  -26.090 1.00 42.62  ?  413 MET   A CE  1 
ATOM   1670 N  N   . LYS   A 1 258 ? 42.111 16.593  -26.139 1.00 22.92  ?  414 LYS   A N   1 
ATOM   1671 C  CA  . LYS   A 1 258 ? 40.861 16.775  -26.872 1.00 25.92  ?  414 LYS   A CA  1 
ATOM   1672 C  C   . LYS   A 1 258 ? 41.089 17.541  -28.171 1.00 25.45  ?  414 LYS   A C   1 
ATOM   1673 O  O   . LYS   A 1 258 ? 40.530 17.186  -29.216 1.00 29.67  ?  414 LYS   A O   1 
ATOM   1674 C  CB  . LYS   A 1 258 ? 39.836 17.493  -25.993 1.00 26.64  ?  414 LYS   A CB  1 
ATOM   1675 C  CG  . LYS   A 1 258 ? 39.252 16.624  -24.884 1.00 27.31  ?  414 LYS   A CG  1 
ATOM   1676 C  CD  . LYS   A 1 258 ? 38.506 17.452  -23.842 1.00 32.81  ?  414 LYS   A CD  1 
ATOM   1677 C  CE  . LYS   A 1 258 ? 37.197 18.000  -24.392 1.00 48.38  ?  414 LYS   A CE  1 
ATOM   1678 N  NZ  . LYS   A 1 258 ? 36.394 18.679  -23.335 1.00 62.77  ?  414 LYS   A NZ  1 
ATOM   1679 N  N   . TYR   A 1 259 ? 41.920 18.586  -28.129 1.00 27.95  ?  415 TYR   A N   1 
ATOM   1680 C  CA  . TYR   A 1 259 ? 42.183 19.377  -29.326 1.00 26.93  ?  415 TYR   A CA  1 
ATOM   1681 C  C   . TYR   A 1 259 ? 42.944 18.570  -30.369 1.00 30.11  ?  415 TYR   A C   1 
ATOM   1682 O  O   . TYR   A 1 259 ? 42.692 18.708  -31.571 1.00 33.36  ?  415 TYR   A O   1 
ATOM   1683 C  CB  . TYR   A 1 259 ? 42.955 20.640  -28.946 1.00 29.83  ?  415 TYR   A CB  1 
ATOM   1684 C  CG  . TYR   A 1 259 ? 43.152 21.626  -30.073 1.00 36.63  ?  415 TYR   A CG  1 
ATOM   1685 C  CD1 . TYR   A 1 259 ? 42.074 22.094  -30.815 1.00 39.17  ?  415 TYR   A CD1 1 
ATOM   1686 C  CD2 . TYR   A 1 259 ? 44.416 22.107  -30.380 1.00 40.56  ?  415 TYR   A CD2 1 
ATOM   1687 C  CE1 . TYR   A 1 259 ? 42.256 23.005  -31.841 1.00 48.46  ?  415 TYR   A CE1 1 
ATOM   1688 C  CE2 . TYR   A 1 259 ? 44.607 23.016  -31.399 1.00 44.54  ?  415 TYR   A CE2 1 
ATOM   1689 C  CZ  . TYR   A 1 259 ? 43.527 23.462  -32.127 1.00 37.14  ?  415 TYR   A CZ  1 
ATOM   1690 O  OH  . TYR   A 1 259 ? 43.726 24.367  -33.143 1.00 40.73  ?  415 TYR   A OH  1 
ATOM   1691 N  N   . LEU   A 1 260 ? 43.880 17.726  -29.930 1.00 30.70  ?  416 LEU   A N   1 
ATOM   1692 C  CA  . LEU   A 1 260 ? 44.581 16.840  -30.853 1.00 25.35  ?  416 LEU   A CA  1 
ATOM   1693 C  C   . LEU   A 1 260 ? 43.599 15.932  -31.580 1.00 25.99  ?  416 LEU   A C   1 
ATOM   1694 O  O   . LEU   A 1 260 ? 43.637 15.811  -32.814 1.00 29.97  ?  416 LEU   A O   1 
ATOM   1695 C  CB  . LEU   A 1 260 ? 45.620 16.021  -30.085 1.00 26.80  ?  416 LEU   A CB  1 
ATOM   1696 C  CG  . LEU   A 1 260 ? 46.448 14.978  -30.838 1.00 38.99  ?  416 LEU   A CG  1 
ATOM   1697 C  CD1 . LEU   A 1 260 ? 47.255 15.621  -31.955 1.00 25.40  ?  416 LEU   A CD1 1 
ATOM   1698 C  CD2 . LEU   A 1 260 ? 47.362 14.235  -29.872 1.00 26.76  ?  416 LEU   A CD2 1 
ATOM   1699 N  N   . LEU   A 1 261 ? 42.695 15.294  -30.829 1.00 29.22  ?  417 LEU   A N   1 
ATOM   1700 C  CA  . LEU   A 1 261 ? 41.727 14.410  -31.476 1.00 26.24  ?  417 LEU   A CA  1 
ATOM   1701 C  C   . LEU   A 1 261 ? 40.806 15.185  -32.411 1.00 27.55  ?  417 LEU   A C   1 
ATOM   1702 O  O   . LEU   A 1 261 ? 40.481 14.708  -33.504 1.00 28.55  ?  417 LEU   A O   1 
ATOM   1703 C  CB  . LEU   A 1 261 ? 40.905 13.644  -30.441 1.00 25.62  ?  417 LEU   A CB  1 
ATOM   1704 C  CG  . LEU   A 1 261 ? 39.893 12.700  -31.101 1.00 26.50  ?  417 LEU   A CG  1 
ATOM   1705 C  CD1 . LEU   A 1 261 ? 40.600 11.666  -31.973 1.00 26.80  ?  417 LEU   A CD1 1 
ATOM   1706 C  CD2 . LEU   A 1 261 ? 39.010 12.020  -30.072 1.00 28.30  ?  417 LEU   A CD2 1 
ATOM   1707 N  N   . GLU   A 1 262 ? 40.374 16.382  -32.004 1.00 27.67  ?  418 GLU   A N   1 
ATOM   1708 C  CA  . GLU   A 1 262 ? 39.472 17.160  -32.849 1.00 29.05  ?  418 GLU   A CA  1 
ATOM   1709 C  C   . GLU   A 1 262 ? 40.147 17.571  -34.153 1.00 30.05  ?  418 GLU   A C   1 
ATOM   1710 O  O   . GLU   A 1 262 ? 39.550 17.454  -35.232 1.00 31.32  ?  418 GLU   A O   1 
ATOM   1711 C  CB  . GLU   A 1 262 ? 38.969 18.386  -32.087 1.00 31.30  ?  418 GLU   A CB  1 
ATOM   1712 C  CG  . GLU   A 1 262 ? 38.018 18.056  -30.947 1.00 32.47  ?  418 GLU   A CG  1 
ATOM   1713 C  CD  . GLU   A 1 262 ? 37.769 19.242  -30.039 1.00 50.95  ?  418 GLU   A CD  1 
ATOM   1714 O  OE1 . GLU   A 1 262 ? 37.870 20.388  -30.522 1.00 56.93  ?  418 GLU   A OE1 1 
ATOM   1715 O  OE2 . GLU   A 1 262 ? 37.480 19.028  -28.842 1.00 54.07  -1 418 GLU   A OE2 1 
ATOM   1716 N  N   . GLN   A 1 263 ? 41.393 18.046  -34.077 1.00 30.98  ?  419 GLN   A N   1 
ATOM   1717 C  CA  . GLN   A 1 263 ? 42.115 18.432  -35.286 1.00 30.60  ?  419 GLN   A CA  1 
ATOM   1718 C  C   . GLN   A 1 263 ? 42.333 17.236  -36.202 1.00 41.76  ?  419 GLN   A C   1 
ATOM   1719 O  O   . GLN   A 1 263 ? 42.182 17.347  -37.427 1.00 39.81  ?  419 GLN   A O   1 
ATOM   1720 C  CB  . GLN   A 1 263 ? 43.452 19.073  -34.917 1.00 39.21  ?  419 GLN   A CB  1 
ATOM   1721 C  CG  . GLN   A 1 263 ? 43.331 20.406  -34.195 1.00 40.05  ?  419 GLN   A CG  1 
ATOM   1722 C  CD  . GLN   A 1 263 ? 42.853 21.519  -35.103 1.00 54.26  ?  419 GLN   A CD  1 
ATOM   1723 O  OE1 . GLN   A 1 263 ? 41.656 21.783  -35.206 1.00 47.82  ?  419 GLN   A OE1 1 
ATOM   1724 N  NE2 . GLN   A 1 263 ? 43.792 22.185  -35.766 1.00 52.25  ?  419 GLN   A NE2 1 
ATOM   1725 N  N   . LEU   A 1 264 ? 42.686 16.078  -35.631 1.00 29.93  ?  420 LEU   A N   1 
ATOM   1726 C  CA  . LEU   A 1 264 ? 42.893 14.896  -36.463 1.00 30.33  ?  420 LEU   A CA  1 
ATOM   1727 C  C   . LEU   A 1 264 ? 41.591 14.437  -37.109 1.00 34.21  ?  420 LEU   A C   1 
ATOM   1728 O  O   . LEU   A 1 264 ? 41.587 14.001  -38.266 1.00 34.48  ?  420 LEU   A O   1 
ATOM   1729 C  CB  . LEU   A 1 264 ? 43.513 13.769  -35.638 1.00 32.50  ?  420 LEU   A CB  1 
ATOM   1730 C  CG  . LEU   A 1 264 ? 44.993 13.944  -35.294 1.00 32.20  ?  420 LEU   A CG  1 
ATOM   1731 C  CD1 . LEU   A 1 264 ? 45.467 12.837  -34.364 1.00 27.23  ?  420 LEU   A CD1 1 
ATOM   1732 C  CD2 . LEU   A 1 264 ? 45.833 13.984  -36.560 1.00 36.23  ?  420 LEU   A CD2 1 
ATOM   1733 N  N   . LYS   A 1 265 ? 40.475 14.530  -36.380 1.00 31.17  ?  421 LYS   A N   1 
ATOM   1734 C  CA  . LYS   A 1 265 ? 39.186 14.153  -36.951 1.00 34.45  ?  421 LYS   A CA  1 
ATOM   1735 C  C   . LYS   A 1 265 ? 38.791 15.090  -38.084 1.00 38.33  ?  421 LYS   A C   1 
ATOM   1736 O  O   . LYS   A 1 265 ? 38.241 14.649  -39.100 1.00 40.28  ?  421 LYS   A O   1 
ATOM   1737 C  CB  . LYS   A 1 265 ? 38.112 14.141  -35.862 1.00 31.82  ?  421 LYS   A CB  1 
ATOM   1738 C  CG  . LYS   A 1 265 ? 38.130 12.902  -34.976 1.00 32.85  ?  421 LYS   A CG  1 
ATOM   1739 C  CD  . LYS   A 1 265 ? 37.233 13.081  -33.761 1.00 30.63  ?  421 LYS   A CD  1 
ATOM   1740 C  CE  . LYS   A 1 265 ? 35.764 12.948  -34.133 1.00 31.49  ?  421 LYS   A CE  1 
ATOM   1741 N  NZ  . LYS   A 1 265 ? 35.374 11.528  -34.331 1.00 31.80  ?  421 LYS   A NZ  1 
ATOM   1742 N  N   . GLU   A 1 266 ? 39.063 16.387  -37.929 1.00 38.89  ?  422 GLU   A N   1 
ATOM   1743 C  CA  . GLU   A 1 266 ? 38.766 17.335  -38.999 1.00 35.49  ?  422 GLU   A CA  1 
ATOM   1744 C  C   . GLU   A 1 266 ? 39.619 17.060  -40.233 1.00 37.79  ?  422 GLU   A C   1 
ATOM   1745 O  O   . GLU   A 1 266 ? 39.106 17.013  -41.358 1.00 37.75  ?  422 GLU   A O   1 
ATOM   1746 C  CB  . GLU   A 1 266 ? 38.976 18.768  -38.508 1.00 39.90  ?  422 GLU   A CB  1 
ATOM   1747 C  CG  . GLU   A 1 266 ? 38.767 19.835  -39.578 1.00 49.57  ?  422 GLU   A CG  1 
ATOM   1748 C  CD  . GLU   A 1 266 ? 37.354 19.851  -40.133 1.00 66.27  ?  422 GLU   A CD  1 
ATOM   1749 O  OE1 . GLU   A 1 266 ? 36.469 19.191  -39.547 1.00 73.86  ?  422 GLU   A OE1 1 
ATOM   1750 O  OE2 . GLU   A 1 266 ? 37.127 20.539  -41.153 1.00 54.71  -1 422 GLU   A OE2 1 
ATOM   1751 N  N   . ARG   A 1 267 ? 40.928 16.871  -40.041 1.00 37.75  ?  423 ARG   A N   1 
ATOM   1752 C  CA  . ARG   A 1 267 ? 41.828 16.723  -41.182 1.00 36.14  ?  423 ARG   A CA  1 
ATOM   1753 C  C   . ARG   A 1 267 ? 41.478 15.497  -42.019 1.00 42.52  ?  423 ARG   A C   1 
ATOM   1754 O  O   . ARG   A 1 267 ? 41.589 15.525  -43.251 1.00 59.75  ?  423 ARG   A O   1 
ATOM   1755 C  CB  . ARG   A 1 267 ? 43.279 16.647  -40.707 1.00 38.83  ?  423 ARG   A CB  1 
ATOM   1756 C  CG  . ARG   A 1 267 ? 44.288 16.654  -41.845 1.00 58.52  ?  423 ARG   A CG  1 
ATOM   1757 C  CD  . ARG   A 1 267 ? 45.484 15.768  -41.552 1.00 63.57  ?  423 ARG   A CD  1 
ATOM   1758 N  NE  . ARG   A 1 267 ? 46.625 16.531  -41.061 1.00 65.40  ?  423 ARG   A NE  1 
ATOM   1759 C  CZ  . ARG   A 1 267 ? 47.883 16.115  -41.116 1.00 69.47  ?  423 ARG   A CZ  1 
ATOM   1760 N  NH1 . ARG   A 1 267 ? 48.200 14.941  -41.637 1.00 62.44  ?  423 ARG   A NH1 1 
ATOM   1761 N  NH2 . ARG   A 1 267 ? 48.847 16.896  -40.636 1.00 63.56  ?  423 ARG   A NH2 1 
ATOM   1762 N  N   . PHE   A 1 268 ? 41.050 14.413  -41.374 1.00 40.29  ?  424 PHE   A N   1 
ATOM   1763 C  CA  . PHE   A 1 268 ? 40.689 13.180  -42.061 1.00 42.30  ?  424 PHE   A CA  1 
ATOM   1764 C  C   . PHE   A 1 268 ? 39.178 12.955  -42.074 1.00 48.84  ?  424 PHE   A C   1 
ATOM   1765 O  O   . PHE   A 1 268 ? 38.713 11.812  -42.081 1.00 37.72  ?  424 PHE   A O   1 
ATOM   1766 C  CB  . PHE   A 1 268 ? 41.407 11.989  -41.427 1.00 42.09  ?  424 PHE   A CB  1 
ATOM   1767 C  CG  . PHE   A 1 268 ? 42.907 12.095  -41.473 1.00 36.12  ?  424 PHE   A CG  1 
ATOM   1768 C  CD1 . PHE   A 1 268 ? 43.586 12.012  -42.679 1.00 47.15  ?  424 PHE   A CD1 1 
ATOM   1769 C  CD2 . PHE   A 1 268 ? 43.638 12.289  -40.312 1.00 33.69  ?  424 PHE   A CD2 1 
ATOM   1770 C  CE1 . PHE   A 1 268 ? 44.966 12.116  -42.725 1.00 43.72  ?  424 PHE   A CE1 1 
ATOM   1771 C  CE2 . PHE   A 1 268 ? 45.018 12.394  -40.352 1.00 32.91  ?  424 PHE   A CE2 1 
ATOM   1772 C  CZ  . PHE   A 1 268 ? 45.682 12.305  -41.560 1.00 35.72  ?  424 PHE   A CZ  1 
ATOM   1773 N  N   . LYS   A 1 269 ? 38.400 14.040  -42.087 1.00 45.52  ?  425 LYS   A N   1 
ATOM   1774 C  CA  . LYS   A 1 269 ? 36.947 13.917  -42.134 1.00 40.67  ?  425 LYS   A CA  1 
ATOM   1775 C  C   . LYS   A 1 269 ? 36.459 13.298  -43.437 1.00 49.03  ?  425 LYS   A C   1 
ATOM   1776 O  O   . LYS   A 1 269 ? 35.331 12.797  -43.483 1.00 56.55  ?  425 LYS   A O   1 
ATOM   1777 C  CB  . LYS   A 1 269 ? 36.292 15.286  -41.935 1.00 50.60  ?  425 LYS   A CB  1 
ATOM   1778 C  CG  . LYS   A 1 269 ? 36.145 16.100  -43.212 1.00 49.47  ?  425 LYS   A CG  1 
ATOM   1779 C  CD  . LYS   A 1 269 ? 36.000 17.582  -42.913 1.00 54.31  ?  425 LYS   A CD  1 
ATOM   1780 C  CE  . LYS   A 1 269 ? 36.007 18.403  -44.192 1.00 57.72  ?  425 LYS   A CE  1 
ATOM   1781 N  NZ  . LYS   A 1 269 ? 34.633 18.791  -44.618 1.00 83.78  ?  425 LYS   A NZ  1 
ATOM   1782 N  N   . ASP   A 1 270 ? 37.277 13.321  -44.492 1.00 46.57  ?  426 ASP   A N   1 
ATOM   1783 C  CA  . ASP   A 1 270 ? 36.880 12.717  -45.758 1.00 51.24  ?  426 ASP   A CA  1 
ATOM   1784 C  C   . ASP   A 1 270 ? 37.024 11.202  -45.727 1.00 59.38  ?  426 ASP   A C   1 
ATOM   1785 O  O   . ASP   A 1 270 ? 36.326 10.500  -46.468 1.00 76.05  ?  426 ASP   A O   1 
ATOM   1786 C  CB  . ASP   A 1 270 ? 37.704 13.313  -46.901 1.00 66.28  ?  426 ASP   A CB  1 
ATOM   1787 C  CG  . ASP   A 1 270 ? 37.454 14.799  -47.082 1.00 85.80  ?  426 ASP   A CG  1 
ATOM   1788 O  OD1 . ASP   A 1 270 ? 36.279 15.216  -47.031 1.00 86.92  ?  426 ASP   A OD1 1 
ATOM   1789 O  OD2 . ASP   A 1 270 ? 38.434 15.551  -47.264 1.00 88.27  -1 426 ASP   A OD2 1 
ATOM   1790 N  N   . LYS   A 1 271 ? 37.919 10.687  -44.893 1.00 49.83  ?  427 LYS   A N   1 
ATOM   1791 C  CA  . LYS   A 1 271 ? 38.003 9.261   -44.633 1.00 53.15  ?  427 LYS   A CA  1 
ATOM   1792 C  C   . LYS   A 1 271 ? 37.111 8.906   -43.446 1.00 56.42  ?  427 LYS   A C   1 
ATOM   1793 O  O   . LYS   A 1 271 ? 36.637 9.774   -42.710 1.00 59.23  ?  427 LYS   A O   1 
ATOM   1794 C  CB  . LYS   A 1 271 ? 39.454 8.853   -44.376 1.00 59.69  ?  427 LYS   A CB  1 
ATOM   1795 C  CG  . LYS   A 1 271 ? 40.459 9.626   -45.221 1.00 65.23  ?  427 LYS   A CG  1 
ATOM   1796 C  CD  . LYS   A 1 271 ? 41.806 8.923   -45.290 1.00 61.09  ?  427 LYS   A CD  1 
ATOM   1797 C  CE  . LYS   A 1 271 ? 42.568 9.311   -46.551 1.00 76.04  ?  427 LYS   A CE  1 
ATOM   1798 N  NZ  . LYS   A 1 271 ? 42.409 8.316   -47.647 1.00 76.15  ?  427 LYS   A NZ  1 
ATOM   1799 N  N   . LYS   A 1 272 ? 36.876 7.610   -43.265 1.00 57.00  ?  428 LYS   A N   1 
ATOM   1800 C  CA  . LYS   A 1 272 ? 35.987 7.128   -42.218 1.00 52.14  ?  428 LYS   A CA  1 
ATOM   1801 C  C   . LYS   A 1 272 ? 36.729 6.540   -41.026 1.00 53.91  ?  428 LYS   A C   1 
ATOM   1802 O  O   . LYS   A 1 272 ? 36.085 6.058   -40.090 1.00 39.64  ?  428 LYS   A O   1 
ATOM   1803 C  CB  . LYS   A 1 272 ? 35.023 6.082   -42.789 1.00 56.20  ?  428 LYS   A CB  1 
ATOM   1804 C  CG  . LYS   A 1 272 ? 34.023 6.637   -43.791 1.00 67.33  ?  428 LYS   A CG  1 
ATOM   1805 C  CD  . LYS   A 1 272 ? 33.544 5.557   -44.749 1.00 75.71  ?  428 LYS   A CD  1 
ATOM   1806 C  CE  . LYS   A 1 272 ? 32.994 6.160   -46.032 1.00 54.57  ?  428 LYS   A CE  1 
ATOM   1807 N  NZ  . LYS   A 1 272 ? 33.478 5.437   -47.241 1.00 56.15  ?  428 LYS   A NZ  1 
ATOM   1808 N  N   . HIS   A 1 273 ? 38.064 6.585   -41.028 1.00 44.16  ?  429 HIS   A N   1 
ATOM   1809 C  CA  . HIS   A 1 273 ? 38.836 5.860   -40.023 1.00 43.81  ?  429 HIS   A CA  1 
ATOM   1810 C  C   . HIS   A 1 273 ? 38.606 6.413   -38.621 1.00 44.93  ?  429 HIS   A C   1 
ATOM   1811 O  O   . HIS   A 1 273 ? 38.524 5.648   -37.652 1.00 42.31  ?  429 HIS   A O   1 
ATOM   1812 C  CB  . HIS   A 1 273 ? 40.323 5.904   -40.377 1.00 40.02  ?  429 HIS   A CB  1 
ATOM   1813 C  CG  . HIS   A 1 273 ? 40.672 5.144   -41.619 1.00 45.77  ?  429 HIS   A CG  1 
ATOM   1814 N  ND1 . HIS   A 1 273 ? 40.467 5.652   -42.884 1.00 68.72  ?  429 HIS   A ND1 1 
ATOM   1815 C  CD2 . HIS   A 1 273 ? 41.214 3.915   -41.791 1.00 53.35  ?  429 HIS   A CD2 1 
ATOM   1816 C  CE1 . HIS   A 1 273 ? 40.866 4.768   -43.782 1.00 65.98  ?  429 HIS   A CE1 1 
ATOM   1817 N  NE2 . HIS   A 1 273 ? 41.324 3.705   -43.144 1.00 57.66  ?  429 HIS   A NE2 1 
ATOM   1818 N  N   . LEU   A 1 274 ? 38.495 7.734   -38.489 1.00 33.57  ?  430 LEU   A N   1 
ATOM   1819 C  CA  . LEU   A 1 274 ? 38.425 8.387   -37.189 1.00 35.83  ?  430 LEU   A CA  1 
ATOM   1820 C  C   . LEU   A 1 274 ? 37.008 8.771   -36.783 1.00 32.86  ?  430 LEU   A C   1 
ATOM   1821 O  O   . LEU   A 1 274 ? 36.837 9.545   -35.837 1.00 38.05  ?  430 LEU   A O   1 
ATOM   1822 C  CB  . LEU   A 1 274 ? 39.318 9.628   -37.178 1.00 31.87  ?  430 LEU   A CB  1 
ATOM   1823 C  CG  . LEU   A 1 274 ? 40.784 9.385   -37.539 1.00 38.24  ?  430 LEU   A CG  1 
ATOM   1824 C  CD1 . LEU   A 1 274 ? 41.595 10.669  -37.430 1.00 31.27  ?  430 LEU   A CD1 1 
ATOM   1825 C  CD2 . LEU   A 1 274 ? 41.366 8.294   -36.655 1.00 30.45  ?  430 LEU   A CD2 1 
ATOM   1826 N  N   . ASP   A 1 275 ? 35.989 8.241   -37.465 1.00 34.19  ?  431 ASP   A N   1 
ATOM   1827 C  CA  . ASP   A 1 275 ? 34.621 8.678   -37.200 1.00 34.92  ?  431 ASP   A CA  1 
ATOM   1828 C  C   . ASP   A 1 275 ? 34.111 8.193   -35.849 1.00 39.06  ?  431 ASP   A C   1 
ATOM   1829 O  O   . ASP   A 1 275 ? 33.223 8.824   -35.264 1.00 41.64  ?  431 ASP   A O   1 
ATOM   1830 C  CB  . ASP   A 1 275 ? 33.692 8.200   -38.316 1.00 44.17  ?  431 ASP   A CB  1 
ATOM   1831 C  CG  . ASP   A 1 275 ? 33.879 8.977   -39.605 1.00 57.78  ?  431 ASP   A CG  1 
ATOM   1832 O  OD1 . ASP   A 1 275 ? 34.513 10.053  -39.565 1.00 68.93  ?  431 ASP   A OD1 1 
ATOM   1833 O  OD2 . ASP   A 1 275 ? 33.394 8.513   -40.658 1.00 62.89  -1 431 ASP   A OD2 1 
ATOM   1834 N  N   . LYS   A 1 276 ? 34.654 7.091   -35.332 1.00 40.82  ?  432 LYS   A N   1 
ATOM   1835 C  CA  . LYS   A 1 276 ? 34.136 6.487   -34.111 1.00 39.19  ?  432 LYS   A CA  1 
ATOM   1836 C  C   . LYS   A 1 276 ? 34.831 6.972   -32.846 1.00 38.84  ?  432 LYS   A C   1 
ATOM   1837 O  O   . LYS   A 1 276 ? 34.358 6.666   -31.746 1.00 36.98  ?  432 LYS   A O   1 
ATOM   1838 C  CB  . LYS   A 1 276 ? 34.240 4.960   -34.197 1.00 37.96  ?  432 LYS   A CB  1 
ATOM   1839 C  CG  . LYS   A 1 276 ? 33.799 4.389   -35.534 1.00 46.19  ?  432 LYS   A CG  1 
ATOM   1840 C  CD  . LYS   A 1 276 ? 32.646 3.410   -35.371 1.00 53.57  ?  432 LYS   A CD  1 
ATOM   1841 C  CE  . LYS   A 1 276 ? 32.623 2.394   -36.503 1.00 45.84  ?  432 LYS   A CE  1 
ATOM   1842 N  NZ  . LYS   A 1 276 ? 31.978 1.114   -36.097 1.00 67.68  ?  432 LYS   A NZ  1 
ATOM   1843 N  N   . PHE   A 1 277 ? 35.927 7.715   -32.966 1.00 34.35  ?  433 PHE   A N   1 
ATOM   1844 C  CA  . PHE   A 1 277 ? 36.630 8.237   -31.804 1.00 35.35  ?  433 PHE   A CA  1 
ATOM   1845 C  C   . PHE   A 1 277 ? 35.997 9.545   -31.349 1.00 34.73  ?  433 PHE   A C   1 
ATOM   1846 O  O   . PHE   A 1 277 ? 35.507 10.337  -32.158 1.00 33.56  ?  433 PHE   A O   1 
ATOM   1847 C  CB  . PHE   A 1 277 ? 38.112 8.449   -32.118 1.00 28.21  ?  433 PHE   A CB  1 
ATOM   1848 C  CG  . PHE   A 1 277 ? 38.833 7.186   -32.489 1.00 28.22  ?  433 PHE   A CG  1 
ATOM   1849 C  CD1 . PHE   A 1 277 ? 39.244 6.294   -31.513 1.00 30.43  ?  433 PHE   A CD1 1 
ATOM   1850 C  CD2 . PHE   A 1 277 ? 39.092 6.886   -33.817 1.00 29.18  ?  433 PHE   A CD2 1 
ATOM   1851 C  CE1 . PHE   A 1 277 ? 39.903 5.127   -31.855 1.00 31.49  ?  433 PHE   A CE1 1 
ATOM   1852 C  CE2 . PHE   A 1 277 ? 39.751 5.723   -34.166 1.00 30.92  ?  433 PHE   A CE2 1 
ATOM   1853 C  CZ  . PHE   A 1 277 ? 40.157 4.841   -33.184 1.00 32.05  ?  433 PHE   A CZ  1 
ATOM   1854 N  N   . SER   A 1 278 ? 36.010 9.766   -30.036 1.00 27.81  ?  434 SER   A N   1 
ATOM   1855 C  CA  . SER   A 1 278 ? 35.348 10.926  -29.457 1.00 31.94  ?  434 SER   A CA  1 
ATOM   1856 C  C   . SER   A 1 278 ? 36.125 11.401  -28.239 1.00 30.60  ?  434 SER   A C   1 
ATOM   1857 O  O   . SER   A 1 278 ? 37.051 10.738  -27.764 1.00 25.45  ?  434 SER   A O   1 
ATOM   1858 C  CB  . SER   A 1 278 ? 33.900 10.608  -29.074 1.00 39.39  ?  434 SER   A CB  1 
ATOM   1859 O  OG  . SER   A 1 278 ? 33.838 9.987   -27.801 1.00 31.31  ?  434 SER   A OG  1 
ATOM   1860 N  N   . SER   A 1 279 ? 35.722 12.570  -27.734 1.00 34.73  ?  435 SER   A N   1 
ATOM   1861 C  CA  . SER   A 1 279 ? 36.333 13.121  -26.531 1.00 29.55  ?  435 SER   A CA  1 
ATOM   1862 C  C   . SER   A 1 279 ? 36.059 12.263  -25.305 1.00 28.61  ?  435 SER   A C   1 
ATOM   1863 O  O   . SER   A 1 279 ? 36.738 12.427  -24.285 1.00 28.70  ?  435 SER   A O   1 
ATOM   1864 C  CB  . SER   A 1 279 ? 35.832 14.547  -26.291 1.00 35.26  ?  435 SER   A CB  1 
ATOM   1865 O  OG  . SER   A 1 279 ? 34.494 14.550  -25.826 1.00 38.25  ?  435 SER   A OG  1 
ATOM   1866 N  N   . TYR   A 1 280 ? 35.082 11.355  -25.375 1.00 25.04  ?  436 TYR   A N   1 
ATOM   1867 C  CA  . TYR   A 1 280 ? 34.858 10.443  -24.260 1.00 33.11  ?  436 TYR   A CA  1 
ATOM   1868 C  C   . TYR   A 1 280 ? 36.038 9.498   -24.078 1.00 26.63  ?  436 TYR   A C   1 
ATOM   1869 O  O   . TYR   A 1 280 ? 36.463 9.240   -22.946 1.00 27.57  ?  436 TYR   A O   1 
ATOM   1870 C  CB  . TYR   A 1 280 ? 33.569 9.648   -24.460 1.00 29.70  ?  436 TYR   A CB  1 
ATOM   1871 C  CG  . TYR   A 1 280 ? 33.118 8.975   -23.189 1.00 34.46  ?  436 TYR   A CG  1 
ATOM   1872 C  CD1 . TYR   A 1 280 ? 32.696 9.726   -22.100 1.00 31.60  ?  436 TYR   A CD1 1 
ATOM   1873 C  CD2 . TYR   A 1 280 ? 33.144 7.593   -23.063 1.00 29.27  ?  436 TYR   A CD2 1 
ATOM   1874 C  CE1 . TYR   A 1 280 ? 32.293 9.120   -20.927 1.00 27.65  ?  436 TYR   A CE1 1 
ATOM   1875 C  CE2 . TYR   A 1 280 ? 32.743 6.977   -21.892 1.00 34.25  ?  436 TYR   A CE2 1 
ATOM   1876 C  CZ  . TYR   A 1 280 ? 32.319 7.746   -20.828 1.00 26.88  ?  436 TYR   A CZ  1 
ATOM   1877 O  OH  . TYR   A 1 280 ? 31.918 7.142   -19.658 1.00 38.08  ?  436 TYR   A OH  1 
ATOM   1878 N  N   . HIS   A 1 281 ? 36.577 8.966   -25.177 1.00 29.65  ?  437 HIS   A N   1 
ATOM   1879 C  CA  . HIS   A 1 281 ? 37.772 8.135   -25.082 1.00 23.51  ?  437 HIS   A CA  1 
ATOM   1880 C  C   . HIS   A 1 281 ? 38.935 8.922   -24.495 1.00 22.42  ?  437 HIS   A C   1 
ATOM   1881 O  O   . HIS   A 1 281 ? 39.670 8.419   -23.633 1.00 23.76  ?  437 HIS   A O   1 
ATOM   1882 C  CB  . HIS   A 1 281 ? 38.141 7.594   -26.464 1.00 24.26  ?  437 HIS   A CB  1 
ATOM   1883 C  CG  . HIS   A 1 281 ? 37.052 6.797   -27.110 1.00 25.45  ?  437 HIS   A CG  1 
ATOM   1884 N  ND1 . HIS   A 1 281 ? 36.564 7.086   -28.366 1.00 26.54  ?  437 HIS   A ND1 1 
ATOM   1885 C  CD2 . HIS   A 1 281 ? 36.358 5.719   -26.675 1.00 25.85  ?  437 HIS   A CD2 1 
ATOM   1886 C  CE1 . HIS   A 1 281 ? 35.613 6.223   -28.676 1.00 27.55  ?  437 HIS   A CE1 1 
ATOM   1887 N  NE2 . HIS   A 1 281 ? 35.469 5.382   -27.667 1.00 27.16  ?  437 HIS   A NE2 1 
ATOM   1888 N  N   . VAL   A 1 282 ? 39.107 10.166  -24.948 1.00 24.18  ?  438 VAL   A N   1 
ATOM   1889 C  CA  . VAL   A 1 282 ? 40.186 11.017  -24.454 1.00 21.62  ?  438 VAL   A CA  1 
ATOM   1890 C  C   . VAL   A 1 282 ? 40.044 11.243  -22.955 1.00 20.78  ?  438 VAL   A C   1 
ATOM   1891 O  O   . VAL   A 1 282 ? 41.012 11.121  -22.195 1.00 19.95  ?  438 VAL   A O   1 
ATOM   1892 C  CB  . VAL   A 1 282 ? 40.206 12.348  -25.227 1.00 28.01  ?  438 VAL   A CB  1 
ATOM   1893 C  CG1 . VAL   A 1 282 ? 41.086 13.352  -24.521 1.00 29.20  ?  438 VAL   A CG1 1 
ATOM   1894 C  CG2 . VAL   A 1 282 ? 40.687 12.127  -26.657 1.00 30.17  ?  438 VAL   A CG2 1 
ATOM   1895 N  N   . LYS   A 1 283 ? 38.829 11.562  -22.504 1.00 21.76  ?  439 LYS   A N   1 
ATOM   1896 C  CA  . LYS   A 1 283 ? 38.607 11.839  -21.088 1.00 28.07  ?  439 LYS   A CA  1 
ATOM   1897 C  C   . LYS   A 1 283 ? 38.797 10.586  -20.240 1.00 19.94  ?  439 LYS   A C   1 
ATOM   1898 O  O   . LYS   A 1 283 ? 39.369 10.651  -19.145 1.00 24.18  ?  439 LYS   A O   1 
ATOM   1899 C  CB  . LYS   A 1 283 ? 37.211 12.425  -20.884 1.00 24.62  ?  439 LYS   A CB  1 
ATOM   1900 N  N   . THR   A 1 284 ? 38.327 9.435   -20.729 1.00 24.30  ?  440 THR   A N   1 
ATOM   1901 C  CA  . THR   A 1 284 ? 38.510 8.185   -19.996 1.00 24.32  ?  440 THR   A CA  1 
ATOM   1902 C  C   . THR   A 1 284 ? 39.993 7.862   -19.831 1.00 23.09  ?  440 THR   A C   1 
ATOM   1903 O  O   . THR   A 1 284 ? 40.455 7.531   -18.728 1.00 27.79  ?  440 THR   A O   1 
ATOM   1904 C  CB  . THR   A 1 284 ? 37.781 7.053   -20.722 1.00 22.87  ?  440 THR   A CB  1 
ATOM   1905 O  OG1 . THR   A 1 284 ? 36.428 7.445   -20.983 1.00 26.33  ?  440 THR   A OG1 1 
ATOM   1906 C  CG2 . THR   A 1 284 ? 37.777 5.794   -19.882 1.00 28.05  ?  440 THR   A CG2 1 
ATOM   1907 N  N   . ALA   A 1 285 ? 40.760 7.966   -20.921 1.00 21.35  ?  441 ALA   A N   1 
ATOM   1908 C  CA  . ALA   A 1 285 ? 42.197 7.722   -20.835 1.00 26.66  ?  441 ALA   A CA  1 
ATOM   1909 C  C   . ALA   A 1 285 ? 42.872 8.721   -19.902 1.00 18.41  ?  441 ALA   A C   1 
ATOM   1910 O  O   . ALA   A 1 285 ? 43.783 8.359   -19.146 1.00 17.97  ?  441 ALA   A O   1 
ATOM   1911 C  CB  . ALA   A 1 285 ? 42.822 7.780   -22.230 1.00 21.07  ?  441 ALA   A CB  1 
ATOM   1912 N  N   . PHE   A 1 286 ? 42.434 9.982   -19.937 1.00 18.37  ?  442 PHE   A N   1 
ATOM   1913 C  CA  . PHE   A 1 286 ? 43.016 10.996  -19.064 1.00 19.23  ?  442 PHE   A CA  1 
ATOM   1914 C  C   . PHE   A 1 286 ? 42.769 10.670  -17.596 1.00 18.17  ?  442 PHE   A C   1 
ATOM   1915 O  O   . PHE   A 1 286 ? 43.663 10.830  -16.757 1.00 23.61  ?  442 PHE   A O   1 
ATOM   1916 C  CB  . PHE   A 1 286 ? 42.442 12.370  -19.411 1.00 17.93  ?  442 PHE   A CB  1 
ATOM   1917 C  CG  . PHE   A 1 286 ? 42.816 13.443  -18.431 1.00 18.61  ?  442 PHE   A CG  1 
ATOM   1918 C  CD1 . PHE   A 1 286 ? 44.088 13.991  -18.436 1.00 22.81  ?  442 PHE   A CD1 1 
ATOM   1919 C  CD2 . PHE   A 1 286 ? 41.899 13.895  -17.497 1.00 26.25  ?  442 PHE   A CD2 1 
ATOM   1920 C  CE1 . PHE   A 1 286 ? 44.437 14.975  -17.532 1.00 25.76  ?  442 PHE   A CE1 1 
ATOM   1921 C  CE2 . PHE   A 1 286 ? 42.241 14.878  -16.589 1.00 24.78  ?  442 PHE   A CE2 1 
ATOM   1922 C  CZ  . PHE   A 1 286 ? 43.512 15.419  -16.607 1.00 31.95  ?  442 PHE   A CZ  1 
ATOM   1923 N  N   . PHE   A 1 287 ? 41.557 10.217  -17.266 1.00 18.57  ?  443 PHE   A N   1 
ATOM   1924 C  CA  . PHE   A 1 287 ? 41.270 9.838   -15.886 1.00 21.26  ?  443 PHE   A CA  1 
ATOM   1925 C  C   . PHE   A 1 287 ? 42.098 8.629   -15.465 1.00 24.42  ?  443 PHE   A C   1 
ATOM   1926 O  O   . PHE   A 1 287 ? 42.559 8.553   -14.317 1.00 22.69  ?  443 PHE   A O   1 
ATOM   1927 C  CB  . PHE   A 1 287 ? 39.777 9.560   -15.713 1.00 17.65  ?  443 PHE   A CB  1 
ATOM   1928 C  CG  . PHE   A 1 287 ? 38.923 10.794  -15.762 1.00 22.55  ?  443 PHE   A CG  1 
ATOM   1929 C  CD1 . PHE   A 1 287 ? 39.288 11.931  -15.059 1.00 25.30  ?  443 PHE   A CD1 1 
ATOM   1930 C  CD2 . PHE   A 1 287 ? 37.755 10.817  -16.506 1.00 32.54  ?  443 PHE   A CD2 1 
ATOM   1931 C  CE1 . PHE   A 1 287 ? 38.506 13.069  -15.101 1.00 29.75  ?  443 PHE   A CE1 1 
ATOM   1932 C  CE2 . PHE   A 1 287 ? 36.969 11.952  -16.552 1.00 29.98  ?  443 PHE   A CE2 1 
ATOM   1933 C  CZ  . PHE   A 1 287 ? 37.345 13.079  -15.849 1.00 31.68  ?  443 PHE   A CZ  1 
ATOM   1934 N  N   . HIS   A 1 288 ? 42.305 7.676   -16.378 1.00 17.36  ?  444 HIS   A N   1 
ATOM   1935 C  CA  . HIS   A 1 288 ? 43.191 6.558   -16.060 1.00 17.29  ?  444 HIS   A CA  1 
ATOM   1936 C  C   . HIS   A 1 288 ? 44.607 7.043   -15.762 1.00 23.98  ?  444 HIS   A C   1 
ATOM   1937 O  O   . HIS   A 1 288 ? 45.262 6.550   -14.833 1.00 17.23  ?  444 HIS   A O   1 
ATOM   1938 C  CB  . HIS   A 1 288 ? 43.198 5.544   -17.201 1.00 22.14  ?  444 HIS   A CB  1 
ATOM   1939 C  CG  . HIS   A 1 288 ? 41.961 4.705   -17.267 1.00 26.91  ?  444 HIS   A CG  1 
ATOM   1940 N  ND1 . HIS   A 1 288 ? 41.522 3.949   -16.202 1.00 23.37  ?  444 HIS   A ND1 1 
ATOM   1941 C  CD2 . HIS   A 1 288 ? 41.072 4.499   -18.267 1.00 22.52  ?  444 HIS   A CD2 1 
ATOM   1942 C  CE1 . HIS   A 1 288 ? 40.413 3.317   -16.543 1.00 24.54  ?  444 HIS   A CE1 1 
ATOM   1943 N  NE2 . HIS   A 1 288 ? 40.119 3.633   -17.791 1.00 26.04  ?  444 HIS   A NE2 1 
ATOM   1944 N  N   . VAL   A 1 289 ? 45.094 8.014   -16.540 1.00 19.31  ?  445 VAL   A N   1 
ATOM   1945 C  CA  . VAL   A 1 289 ? 46.423 8.569   -16.288 1.00 18.33  ?  445 VAL   A CA  1 
ATOM   1946 C  C   . VAL   A 1 289 ? 46.465 9.270   -14.934 1.00 18.28  ?  445 VAL   A C   1 
ATOM   1947 O  O   . VAL   A 1 289 ? 47.460 9.182   -14.204 1.00 25.67  ?  445 VAL   A O   1 
ATOM   1948 C  CB  . VAL   A 1 289 ? 46.834 9.520   -17.427 1.00 23.78  ?  445 VAL   A CB  1 
ATOM   1949 C  CG1 . VAL   A 1 289 ? 48.177 10.169  -17.120 1.00 17.25  ?  445 VAL   A CG1 1 
ATOM   1950 C  CG2 . VAL   A 1 289 ? 46.899 8.771   -18.746 1.00 21.41  ?  445 VAL   A CG2 1 
ATOM   1951 N  N   . CYS   A 1 290 ? 45.393 9.985   -14.582 1.00 15.69  ?  446 CYS   A N   1 
ATOM   1952 C  CA  . CYS   A 1 290 ? 45.324 10.608  -13.262 1.00 22.52  ?  446 CYS   A CA  1 
ATOM   1953 C  C   . CYS   A 1 290 ? 45.400 9.562   -12.159 1.00 20.04  ?  446 CYS   A C   1 
ATOM   1954 O  O   . CYS   A 1 290 ? 46.048 9.779   -11.128 1.00 23.79  ?  446 CYS   A O   1 
ATOM   1955 C  CB  . CYS   A 1 290 ? 44.044 11.430  -13.125 1.00 17.25  ?  446 CYS   A CB  1 
ATOM   1956 S  SG  . CYS   A 1 290 ? 44.041 12.970  -14.055 1.00 25.28  ?  446 CYS   A SG  1 
ATOM   1957 N  N   . THR   A 1 291 ? 44.740 8.421   -12.357 1.00 17.42  ?  447 THR   A N   1 
ATOM   1958 C  CA  . THR   A 1 291 ? 44.835 7.344   -11.377 1.00 22.14  ?  447 THR   A CA  1 
ATOM   1959 C  C   . THR   A 1 291 ? 46.260 6.809   -11.283 1.00 25.86  ?  447 THR   A C   1 
ATOM   1960 O  O   . THR   A 1 291 ? 46.751 6.522   -10.185 1.00 21.51  ?  447 THR   A O   1 
ATOM   1961 C  CB  . THR   A 1 291 ? 43.857 6.224   -11.727 1.00 24.53  ?  447 THR   A CB  1 
ATOM   1962 O  OG1 . THR   A 1 291 ? 42.517 6.727   -11.668 1.00 29.98  ?  447 THR   A OG1 1 
ATOM   1963 C  CG2 . THR   A 1 291 ? 43.997 5.067   -10.750 1.00 24.37  ?  447 THR   A CG2 1 
ATOM   1964 N  N   . GLN   A 1 292 ? 46.946 6.678   -12.424 1.00 23.72  ?  448 GLN   A N   1 
ATOM   1965 C  CA  . GLN   A 1 292 ? 48.317 6.172   -12.394 1.00 21.08  ?  448 GLN   A CA  1 
ATOM   1966 C  C   . GLN   A 1 292 ? 49.279 7.166   -11.752 1.00 16.43  ?  448 GLN   A C   1 
ATOM   1967 O  O   . GLN   A 1 292 ? 50.296 6.759   -11.177 1.00 29.19  ?  448 GLN   A O   1 
ATOM   1968 C  CB  . GLN   A 1 292 ? 48.804 5.836   -13.804 1.00 24.83  ?  448 GLN   A CB  1 
ATOM   1969 C  CG  . GLN   A 1 292 ? 48.034 4.742   -14.519 1.00 30.83  ?  448 GLN   A CG  1 
ATOM   1970 C  CD  . GLN   A 1 292 ? 48.660 4.397   -15.857 1.00 45.39  ?  448 GLN   A CD  1 
ATOM   1971 O  OE1 . GLN   A 1 292 ? 49.405 5.195   -16.426 1.00 34.56  ?  448 GLN   A OE1 1 
ATOM   1972 N  NE2 . GLN   A 1 292 ? 48.370 3.203   -16.360 1.00 48.26  ?  448 GLN   A NE2 1 
ATOM   1973 N  N   . ASN   A 1 293 ? 48.988 8.466   -11.846 1.00 19.98  ?  449 ASN   A N   1 
ATOM   1974 C  CA  . ASN   A 1 293 ? 49.873 9.527   -11.368 1.00 16.41  ?  449 ASN   A CA  1 
ATOM   1975 C  C   . ASN   A 1 293 ? 49.119 10.371  -10.346 1.00 21.46  ?  449 ASN   A C   1 
ATOM   1976 O  O   . ASN   A 1 293 ? 48.699 11.497  -10.641 1.00 15.80  ?  449 ASN   A O   1 
ATOM   1977 C  CB  . ASN   A 1 293 ? 50.370 10.381  -12.532 1.00 17.36  ?  449 ASN   A CB  1 
ATOM   1978 C  CG  . ASN   A 1 293 ? 51.340 9.632   -13.425 1.00 25.64  ?  449 ASN   A CG  1 
ATOM   1979 O  OD1 . ASN   A 1 293 ? 50.983 8.635   -14.051 1.00 37.64  ?  449 ASN   A OD1 1 
ATOM   1980 N  ND2 . ASN   A 1 293 ? 52.576 10.112  -13.487 1.00 28.33  ?  449 ASN   A ND2 1 
ATOM   1981 N  N   . PRO   A 1 294 ? 48.940 9.855   -9.126  1.00 24.09  ?  450 PRO   A N   1 
ATOM   1982 C  CA  . PRO   A 1 294 ? 48.006 10.486  -8.183  1.00 17.08  ?  450 PRO   A CA  1 
ATOM   1983 C  C   . PRO   A 1 294 ? 48.551 11.706  -7.459  1.00 25.71  ?  450 PRO   A C   1 
ATOM   1984 O  O   . PRO   A 1 294 ? 47.758 12.441  -6.854  1.00 28.31  ?  450 PRO   A O   1 
ATOM   1985 C  CB  . PRO   A 1 294 ? 47.715 9.354   -7.191  1.00 26.40  ?  450 PRO   A CB  1 
ATOM   1986 C  CG  . PRO   A 1 294 ? 48.996 8.585   -7.158  1.00 23.90  ?  450 PRO   A CG  1 
ATOM   1987 C  CD  . PRO   A 1 294 ? 49.541 8.629   -8.568  1.00 18.24  ?  450 PRO   A CD  1 
ATOM   1988 N  N   . GLN   A 1 295 ? 49.857 11.950  -7.484  1.00 26.89  ?  451 GLN   A N   1 
ATOM   1989 C  CA  . GLN   A 1 295 ? 50.437 13.055  -6.732  1.00 20.39  ?  451 GLN   A CA  1 
ATOM   1990 C  C   . GLN   A 1 295 ? 50.423 14.331  -7.561  1.00 25.23  ?  451 GLN   A C   1 
ATOM   1991 O  O   . GLN   A 1 295 ? 50.596 14.295  -8.782  1.00 22.96  ?  451 GLN   A O   1 
ATOM   1992 C  CB  . GLN   A 1 295 ? 51.868 12.723  -6.302  1.00 19.66  ?  451 GLN   A CB  1 
ATOM   1993 C  CG  . GLN   A 1 295 ? 52.000 11.436  -5.502  1.00 20.58  ?  451 GLN   A CG  1 
ATOM   1994 C  CD  . GLN   A 1 295 ? 51.364 11.521  -4.126  1.00 31.80  ?  451 GLN   A CD  1 
ATOM   1995 O  OE1 . GLN   A 1 295 ? 51.106 12.609  -3.608  1.00 30.09  ?  451 GLN   A OE1 1 
ATOM   1996 N  NE2 . GLN   A 1 295 ? 51.112 10.366  -3.523  1.00 30.27  ?  451 GLN   A NE2 1 
ATOM   1997 N  N   . ASP   A 1 296 ? 50.216 15.463  -6.886  1.00 19.03  ?  452 ASP   A N   1 
ATOM   1998 C  CA  . ASP   A 1 296 ? 50.181 16.745  -7.583  1.00 17.39  ?  452 ASP   A CA  1 
ATOM   1999 C  C   . ASP   A 1 296 ? 51.535 17.092  -8.189  1.00 25.17  ?  452 ASP   A C   1 
ATOM   2000 O  O   . ASP   A 1 296 ? 51.596 17.760  -9.228  1.00 20.08  ?  452 ASP   A O   1 
ATOM   2001 C  CB  . ASP   A 1 296 ? 49.730 17.850  -6.628  1.00 21.34  ?  452 ASP   A CB  1 
ATOM   2002 C  CG  . ASP   A 1 296 ? 48.285 17.692  -6.195  1.00 22.44  ?  452 ASP   A CG  1 
ATOM   2003 O  OD1 . ASP   A 1 296 ? 47.541 16.938  -6.857  1.00 22.55  ?  452 ASP   A OD1 1 
ATOM   2004 O  OD2 . ASP   A 1 296 ? 47.892 18.323  -5.190  1.00 22.39  -1 452 ASP   A OD2 1 
ATOM   2005 N  N   . SER   A 1 297 ? 52.626 16.648  -7.562  1.00 21.68  ?  453 SER   A N   1 
ATOM   2006 C  CA  . SER   A 1 297 ? 53.958 16.953  -8.074  1.00 17.89  ?  453 SER   A CA  1 
ATOM   2007 C  C   . SER   A 1 297 ? 54.264 16.217  -9.373  1.00 28.62  ?  453 SER   A C   1 
ATOM   2008 O  O   . SER   A 1 297 ? 55.212 16.591  -10.072 1.00 25.39  ?  453 SER   A O   1 
ATOM   2009 C  CB  . SER   A 1 297 ? 55.015 16.616  -7.023  1.00 17.45  ?  453 SER   A CB  1 
ATOM   2010 O  OG  . SER   A 1 297 ? 54.862 15.288  -6.554  1.00 32.02  ?  453 SER   A OG  1 
ATOM   2011 N  N   . GLN   A 1 298 ? 53.499 15.179  -9.705  1.00 25.78  ?  454 GLN   A N   1 
ATOM   2012 C  CA  . GLN   A 1 298 ? 53.602 14.540  -11.010 1.00 17.35  ?  454 GLN   A CA  1 
ATOM   2013 C  C   . GLN   A 1 298 ? 52.879 15.322  -12.096 1.00 23.34  ?  454 GLN   A C   1 
ATOM   2014 O  O   . GLN   A 1 298 ? 52.900 14.906  -13.260 1.00 19.41  ?  454 GLN   A O   1 
ATOM   2015 C  CB  . GLN   A 1 298 ? 53.046 13.117  -10.948 1.00 18.41  ?  454 GLN   A CB  1 
ATOM   2016 C  CG  . GLN   A 1 298 ? 53.838 12.178  -10.059 1.00 16.15  ?  454 GLN   A CG  1 
ATOM   2017 C  CD  . GLN   A 1 298 ? 53.145 10.847  -9.868  1.00 27.82  ?  454 GLN   A CD  1 
ATOM   2018 O  OE1 . GLN   A 1 298 ? 52.116 10.763  -9.199  1.00 24.32  ?  454 GLN   A OE1 1 
ATOM   2019 N  NE2 . GLN   A 1 298 ? 53.704 9.796   -10.459 1.00 25.09  ?  454 GLN   A NE2 1 
ATOM   2020 N  N   . TRP   A 1 299 ? 52.240 16.438  -11.740 1.00 26.86  ?  455 TRP   A N   1 
ATOM   2021 C  CA  . TRP   A 1 299 ? 51.511 17.264  -12.694 1.00 29.60  ?  455 TRP   A CA  1 
ATOM   2022 C  C   . TRP   A 1 299 ? 51.955 18.719  -12.629 1.00 27.82  ?  455 TRP   A C   1 
ATOM   2023 O  O   . TRP   A 1 299 ? 51.188 19.608  -13.012 1.00 27.10  ?  455 TRP   A O   1 
ATOM   2024 C  CB  . TRP   A 1 299 ? 50.005 17.153  -12.453 1.00 22.35  ?  455 TRP   A CB  1 
ATOM   2025 C  CG  . TRP   A 1 299 ? 49.482 15.787  -12.734 1.00 17.03  ?  455 TRP   A CG  1 
ATOM   2026 C  CD1 . TRP   A 1 299 ? 49.322 14.771  -11.838 1.00 18.40  ?  455 TRP   A CD1 1 
ATOM   2027 C  CD2 . TRP   A 1 299 ? 49.048 15.281  -14.000 1.00 14.65  ?  455 TRP   A CD2 1 
ATOM   2028 N  NE1 . TRP   A 1 299 ? 48.816 13.660  -12.470 1.00 21.51  ?  455 TRP   A NE1 1 
ATOM   2029 C  CE2 . TRP   A 1 299 ? 48.637 13.949  -13.797 1.00 15.68  ?  455 TRP   A CE2 1 
ATOM   2030 C  CE3 . TRP   A 1 299 ? 48.965 15.826  -15.284 1.00 15.17  ?  455 TRP   A CE3 1 
ATOM   2031 C  CZ2 . TRP   A 1 299 ? 48.152 13.153  -14.832 1.00 14.94  ?  455 TRP   A CZ2 1 
ATOM   2032 C  CZ3 . TRP   A 1 299 ? 48.483 15.036  -16.309 1.00 16.04  ?  455 TRP   A CZ3 1 
ATOM   2033 C  CH2 . TRP   A 1 299 ? 48.083 13.714  -16.078 1.00 18.48  ?  455 TRP   A CH2 1 
ATOM   2034 N  N   . ASP   A 1 300 ? 53.175 18.974  -12.153 1.00 22.22  ?  456 ASP   A N   1 
ATOM   2035 C  CA  . ASP   A 1 300 ? 53.701 20.332  -12.071 1.00 25.28  ?  456 ASP   A CA  1 
ATOM   2036 C  C   . ASP   A 1 300 ? 53.596 21.028  -13.421 1.00 34.84  ?  456 ASP   A C   1 
ATOM   2037 O  O   . ASP   A 1 300 ? 53.854 20.427  -14.467 1.00 29.71  ?  456 ASP   A O   1 
ATOM   2038 C  CB  . ASP   A 1 300 ? 55.159 20.300  -11.602 1.00 33.88  ?  456 ASP   A CB  1 
ATOM   2039 C  CG  . ASP   A 1 300 ? 55.638 21.642  -11.075 1.00 43.14  ?  456 ASP   A CG  1 
ATOM   2040 O  OD1 . ASP   A 1 300 ? 55.670 22.621  -11.851 1.00 49.83  ?  456 ASP   A OD1 1 
ATOM   2041 O  OD2 . ASP   A 1 300 ? 55.991 21.715  -9.880  1.00 59.07  -1 456 ASP   A OD2 1 
ATOM   2042 N  N   . ARG   A 1 301 ? 53.204 22.304  -13.387 1.00 26.88  ?  457 ARG   A N   1 
ATOM   2043 C  CA  . ARG   A 1 301 ? 52.954 23.037  -14.623 1.00 39.70  ?  457 ARG   A CA  1 
ATOM   2044 C  C   . ARG   A 1 301 ? 54.214 23.116  -15.476 1.00 42.84  ?  457 ARG   A C   1 
ATOM   2045 O  O   . ARG   A 1 301 ? 54.153 22.981  -16.706 1.00 35.05  ?  457 ARG   A O   1 
ATOM   2046 C  CB  . ARG   A 1 301 ? 52.422 24.431  -14.289 1.00 32.34  ?  457 ARG   A CB  1 
ATOM   2047 C  CG  . ARG   A 1 301 ? 52.119 25.320  -15.477 1.00 47.10  ?  457 ARG   A CG  1 
ATOM   2048 C  CD  . ARG   A 1 301 ? 51.161 26.422  -15.050 1.00 58.28  ?  457 ARG   A CD  1 
ATOM   2049 N  NE  . ARG   A 1 301 ? 50.954 27.428  -16.084 1.00 77.82  ?  457 ARG   A NE  1 
ATOM   2050 C  CZ  . ARG   A 1 301 ? 51.794 28.421  -16.335 1.00 72.40  ?  457 ARG   A CZ  1 
ATOM   2051 N  NH1 . ARG   A 1 301 ? 52.907 28.577  -15.636 1.00 53.47  ?  457 ARG   A NH1 1 
ATOM   2052 N  NH2 . ARG   A 1 301 ? 51.509 29.283  -17.308 1.00 73.75  ?  457 ARG   A NH2 1 
ATOM   2053 N  N   . LYS   A 1 302 ? 55.372 23.291  -14.829 1.00 38.86  ?  458 LYS   A N   1 
ATOM   2054 C  CA  . LYS   A 1 302 ? 56.648 23.347  -15.535 1.00 36.06  ?  458 LYS   A CA  1 
ATOM   2055 C  C   . LYS   A 1 302 ? 56.889 22.122  -16.410 1.00 35.80  ?  458 LYS   A C   1 
ATOM   2056 O  O   . LYS   A 1 302 ? 57.660 22.205  -17.371 1.00 31.59  ?  458 LYS   A O   1 
ATOM   2057 C  CB  . LYS   A 1 302 ? 57.796 23.497  -14.527 1.00 41.86  ?  458 LYS   A CB  1 
ATOM   2058 C  CG  . LYS   A 1 302 ? 58.403 22.170  -14.079 1.00 46.55  ?  458 LYS   A CG  1 
ATOM   2059 C  CD  . LYS   A 1 302 ? 59.368 22.331  -12.914 1.00 49.82  ?  458 LYS   A CD  1 
ATOM   2060 C  CE  . LYS   A 1 302 ? 60.141 21.042  -12.653 1.00 59.63  ?  458 LYS   A CE  1 
ATOM   2061 N  NZ  . LYS   A 1 302 ? 60.045 20.613  -11.228 1.00 54.90  ?  458 LYS   A NZ  1 
ATOM   2062 N  N   . ASP   A 1 303 ? 56.238 20.995  -16.113 1.00 27.64  ?  459 ASP   A N   1 
ATOM   2063 C  CA  . ASP   A 1 303 ? 56.448 19.744  -16.828 1.00 33.38  ?  459 ASP   A CA  1 
ATOM   2064 C  C   . ASP   A 1 303 ? 55.346 19.444  -17.832 1.00 27.13  ?  459 ASP   A C   1 
ATOM   2065 O  O   . ASP   A 1 303 ? 55.188 18.279  -18.223 1.00 27.38  ?  459 ASP   A O   1 
ATOM   2066 C  CB  . ASP   A 1 303 ? 56.566 18.582  -15.843 1.00 29.32  ?  459 ASP   A CB  1 
ATOM   2067 C  CG  . ASP   A 1 303 ? 57.722 18.745  -14.890 1.00 38.03  ?  459 ASP   A CG  1 
ATOM   2068 O  OD1 . ASP   A 1 303 ? 58.796 19.200  -15.334 1.00 47.62  ?  459 ASP   A OD1 1 
ATOM   2069 O  OD2 . ASP   A 1 303 ? 57.554 18.420  -13.696 1.00 40.70  -1 459 ASP   A OD2 1 
ATOM   2070 N  N   . LEU   A 1 304 ? 54.583 20.462  -18.250 1.00 23.19  ?  460 LEU   A N   1 
ATOM   2071 C  CA  . LEU   A 1 304 ? 53.503 20.251  -19.213 1.00 25.26  ?  460 LEU   A CA  1 
ATOM   2072 C  C   . LEU   A 1 304 ? 53.943 19.342  -20.359 1.00 22.42  ?  460 LEU   A C   1 
ATOM   2073 O  O   . LEU   A 1 304 ? 53.290 18.333  -20.655 1.00 31.39  ?  460 LEU   A O   1 
ATOM   2074 C  CB  . LEU   A 1 304 ? 53.012 21.601  -19.745 1.00 24.20  ?  460 LEU   A CB  1 
ATOM   2075 C  CG  . LEU   A 1 304 ? 51.923 21.593  -20.823 1.00 33.29  ?  460 LEU   A CG  1 
ATOM   2076 C  CD1 . LEU   A 1 304 ? 50.634 21.011  -20.276 1.00 29.72  ?  460 LEU   A CD1 1 
ATOM   2077 C  CD2 . LEU   A 1 304 ? 51.685 22.992  -21.383 1.00 33.35  ?  460 LEU   A CD2 1 
ATOM   2078 N  N   . GLY   A 1 305 ? 55.091 19.660  -20.968 1.00 19.45  ?  461 GLY   A N   1 
ATOM   2079 C  CA  . GLY   A 1 305 ? 55.597 18.857  -22.072 1.00 23.52  ?  461 GLY   A CA  1 
ATOM   2080 C  C   . GLY   A 1 305 ? 55.626 17.373  -21.768 1.00 26.01  ?  461 GLY   A C   1 
ATOM   2081 O  O   . GLY   A 1 305 ? 55.075 16.565  -22.518 1.00 29.81  ?  461 GLY   A O   1 
ATOM   2082 N  N   . LEU   A 1 306 ? 56.256 16.990  -20.656 1.00 24.78  ?  462 LEU   A N   1 
ATOM   2083 C  CA  . LEU   A 1 306 ? 56.265 15.575  -20.298 1.00 34.21  ?  462 LEU   A CA  1 
ATOM   2084 C  C   . LEU   A 1 306 ? 54.857 15.079  -20.015 1.00 30.52  ?  462 LEU   A C   1 
ATOM   2085 O  O   . LEU   A 1 306 ? 54.437 14.045  -20.553 1.00 30.72  ?  462 LEU   A O   1 
ATOM   2086 C  CB  . LEU   A 1 306 ? 57.172 15.319  -19.094 1.00 27.94  ?  462 LEU   A CB  1 
ATOM   2087 C  CG  . LEU   A 1 306 ? 58.612 15.818  -19.166 1.00 49.05  ?  462 LEU   A CG  1 
ATOM   2088 C  CD1 . LEU   A 1 306 ? 59.113 16.190  -17.778 1.00 39.09  ?  462 LEU   A CD1 1 
ATOM   2089 C  CD2 . LEU   A 1 306 ? 59.499 14.759  -19.805 1.00 41.82  ?  462 LEU   A CD2 1 
ATOM   2090 N  N   . CYS   A 1 307 ? 54.099 15.826  -19.205 1.00 19.35  ?  463 CYS   A N   1 
ATOM   2091 C  CA  . CYS   A 1 307 ? 52.788 15.351  -18.779 1.00 29.44  ?  463 CYS   A CA  1 
ATOM   2092 C  C   . CYS   A 1 307 ? 51.905 15.060  -19.983 1.00 24.13  ?  463 CYS   A C   1 
ATOM   2093 O  O   . CYS   A 1 307 ? 51.378 13.948  -20.128 1.00 24.27  ?  463 CYS   A O   1 
ATOM   2094 C  CB  . CYS   A 1 307 ? 52.136 16.377  -17.854 1.00 27.61  ?  463 CYS   A CB  1 
ATOM   2095 S  SG  . CYS   A 1 307 ? 52.969 16.572  -16.261 1.00 28.01  ?  463 CYS   A SG  1 
ATOM   2096 N  N   . PHE   A 1 308 ? 51.774 16.039  -20.882 1.00 22.56  ?  464 PHE   A N   1 
ATOM   2097 C  CA  . PHE   A 1 308 ? 51.031 15.813  -22.117 1.00 27.54  ?  464 PHE   A CA  1 
ATOM   2098 C  C   . PHE   A 1 308 ? 51.563 14.595  -22.858 1.00 25.40  ?  464 PHE   A C   1 
ATOM   2099 O  O   . PHE   A 1 308 ? 50.789 13.715  -23.256 1.00 27.14  ?  464 PHE   A O   1 
ATOM   2100 C  CB  . PHE   A 1 308 ? 51.077 17.048  -23.019 1.00 21.68  ?  464 PHE   A CB  1 
ATOM   2101 C  CG  . PHE   A 1 308 ? 50.355 16.858  -24.329 1.00 25.34  ?  464 PHE   A CG  1 
ATOM   2102 C  CD1 . PHE   A 1 308 ? 49.011 16.519  -24.345 1.00 22.42  ?  464 PHE   A CD1 1 
ATOM   2103 C  CD2 . PHE   A 1 308 ? 51.014 17.008  -25.541 1.00 23.42  ?  464 PHE   A CD2 1 
ATOM   2104 C  CE1 . PHE   A 1 308 ? 48.336 16.332  -25.539 1.00 21.59  ?  464 PHE   A CE1 1 
ATOM   2105 C  CE2 . PHE   A 1 308 ? 50.340 16.826  -26.744 1.00 24.58  ?  464 PHE   A CE2 1 
ATOM   2106 C  CZ  . PHE   A 1 308 ? 48.999 16.489  -26.739 1.00 23.49  ?  464 PHE   A CZ  1 
ATOM   2107 N  N   . ASP   A 1 309 ? 52.887 14.514  -23.030 1.00 26.47  ?  465 ASP   A N   1 
ATOM   2108 C  CA  . ASP   A 1 309 ? 53.463 13.347  -23.689 1.00 26.43  ?  465 ASP   A CA  1 
ATOM   2109 C  C   . ASP   A 1 309 ? 52.976 12.069  -23.023 1.00 30.84  ?  465 ASP   A C   1 
ATOM   2110 O  O   . ASP   A 1 309 ? 52.488 11.150  -23.697 1.00 34.96  ?  465 ASP   A O   1 
ATOM   2111 C  CB  . ASP   A 1 309 ? 54.992 13.414  -23.671 1.00 22.35  ?  465 ASP   A CB  1 
ATOM   2112 C  CG  . ASP   A 1 309 ? 55.627 12.318  -24.511 1.00 35.94  ?  465 ASP   A CG  1 
ATOM   2113 O  OD1 . ASP   A 1 309 ? 55.161 12.112  -25.650 1.00 37.18  ?  465 ASP   A OD1 1 
ATOM   2114 O  OD2 . ASP   A 1 309 ? 56.583 11.662  -24.043 1.00 35.42  -1 465 ASP   A OD2 1 
ATOM   2115 N  N   . ASN   A 1 310 ? 53.047 12.023  -21.687 1.00 30.15  ?  466 ASN   A N   1 
ATOM   2116 C  CA  . ASN   A 1 310 ? 52.585 10.847  -20.960 1.00 29.20  ?  466 ASN   A CA  1 
ATOM   2117 C  C   . ASN   A 1 310 ? 51.148 10.520  -21.339 1.00 23.85  ?  466 ASN   A C   1 
ATOM   2118 O  O   . ASN   A 1 310 ? 50.836 9.379   -21.702 1.00 26.03  ?  466 ASN   A O   1 
ATOM   2119 C  CB  . ASN   A 1 310 ? 52.718 11.071  -19.451 1.00 26.14  ?  466 ASN   A CB  1 
ATOM   2120 C  CG  . ASN   A 1 310 ? 54.166 11.094  -18.978 1.00 36.18  ?  466 ASN   A CG  1 
ATOM   2121 O  OD1 . ASN   A 1 310 ? 55.065 10.592  -19.653 1.00 42.14  ?  466 ASN   A OD1 1 
ATOM   2122 N  ND2 . ASN   A 1 310 ? 54.393 11.686  -17.811 1.00 43.34  ?  466 ASN   A ND2 1 
ATOM   2123 N  N   . CYS   A 1 311 ? 50.271 11.532  -21.312 1.00 24.52  ?  467 CYS   A N   1 
ATOM   2124 C  CA  . CYS   A 1 311 ? 48.890 11.322  -21.729 1.00 23.09  ?  467 CYS   A CA  1 
ATOM   2125 C  C   . CYS   A 1 311 ? 48.847 10.662  -23.097 1.00 23.69  ?  467 CYS   A C   1 
ATOM   2126 O  O   . CYS   A 1 311 ? 48.295 9.564   -23.250 1.00 29.69  ?  467 CYS   A O   1 
ATOM   2127 C  CB  . CYS   A 1 311 ? 48.122 12.647  -21.736 1.00 24.05  ?  467 CYS   A CB  1 
ATOM   2128 S  SG  . CYS   A 1 311 ? 47.849 13.376  -20.103 1.00 31.29  ?  467 CYS   A SG  1 
ATOM   2129 N  N   . VAL   A 1 312 ? 49.495 11.290  -24.086 1.00 19.87  ?  468 VAL   A N   1 
ATOM   2130 C  CA  . VAL   A 1 312 ? 49.516 10.731  -25.435 1.00 22.67  ?  468 VAL   A CA  1 
ATOM   2131 C  C   . VAL   A 1 312 ? 49.916 9.268   -25.375 1.00 22.06  ?  468 VAL   A C   1 
ATOM   2132 O  O   . VAL   A 1 312 ? 49.194 8.385   -25.858 1.00 20.68  ?  468 VAL   A O   1 
ATOM   2133 C  CB  . VAL   A 1 312 ? 50.465 11.537  -26.342 1.00 26.52  ?  468 VAL   A CB  1 
ATOM   2134 C  CG1 . VAL   A 1 312 ? 50.654 10.818  -27.665 1.00 25.99  ?  468 VAL   A CG1 1 
ATOM   2135 C  CG2 . VAL   A 1 312 ? 49.923 12.945  -26.578 1.00 23.85  ?  468 VAL   A CG2 1 
ATOM   2136 N  N   . THR   A 1 313 ? 51.035 8.991   -24.694 1.00 19.65  ?  469 THR   A N   1 
ATOM   2137 C  CA  . THR   A 1 313 ? 51.564 7.634   -24.642 1.00 22.99  ?  469 THR   A CA  1 
ATOM   2138 C  C   . THR   A 1 313 ? 50.493 6.664   -24.179 1.00 20.83  ?  469 THR   A C   1 
ATOM   2139 O  O   . THR   A 1 313 ? 50.198 5.675   -24.864 1.00 25.31  ?  469 THR   A O   1 
ATOM   2140 C  CB  . THR   A 1 313 ? 52.782 7.567   -23.715 1.00 35.60  ?  469 THR   A CB  1 
ATOM   2141 O  OG1 . THR   A 1 313 ? 53.890 8.248   -24.319 1.00 38.11  ?  469 THR   A OG1 1 
ATOM   2142 C  CG2 . THR   A 1 313 ? 53.166 6.114   -23.440 1.00 19.60  ?  469 THR   A CG2 1 
ATOM   2143 N  N   . TYR   A 1 314 ? 49.852 6.968   -23.044 1.00 19.06  ?  470 TYR   A N   1 
ATOM   2144 C  CA  . TYR   A 1 314 ? 48.864 6.035   -22.520 1.00 19.70  ?  470 TYR   A CA  1 
ATOM   2145 C  C   . TYR   A 1 314 ? 47.764 5.806   -23.539 1.00 22.99  ?  470 TYR   A C   1 
ATOM   2146 O  O   . TYR   A 1 314 ? 47.429 4.655   -23.848 1.00 20.45  ?  470 TYR   A O   1 
ATOM   2147 C  CB  . TYR   A 1 314 ? 48.280 6.530   -21.195 1.00 18.82  ?  470 TYR   A CB  1 
ATOM   2148 C  CG  . TYR   A 1 314 ? 47.280 5.549   -20.601 1.00 22.59  ?  470 TYR   A CG  1 
ATOM   2149 C  CD1 . TYR   A 1 314 ? 47.712 4.393   -19.962 1.00 25.11  ?  470 TYR   A CD1 1 
ATOM   2150 C  CD2 . TYR   A 1 314 ? 45.909 5.775   -20.680 1.00 18.66  ?  470 TYR   A CD2 1 
ATOM   2151 C  CE1 . TYR   A 1 314 ? 46.811 3.486   -19.421 1.00 27.16  ?  470 TYR   A CE1 1 
ATOM   2152 C  CE2 . TYR   A 1 314 ? 44.997 4.872   -20.134 1.00 20.09  ?  470 TYR   A CE2 1 
ATOM   2153 C  CZ  . TYR   A 1 314 ? 45.456 3.729   -19.510 1.00 23.94  ?  470 TYR   A CZ  1 
ATOM   2154 O  OH  . TYR   A 1 314 ? 44.566 2.825   -18.968 1.00 36.11  ?  470 TYR   A OH  1 
ATOM   2155 N  N   . PHE   A 1 315 ? 47.240 6.891   -24.121 1.00 19.84  ?  471 PHE   A N   1 
ATOM   2156 C  CA  . PHE   A 1 315 ? 46.198 6.739   -25.129 1.00 20.60  ?  471 PHE   A CA  1 
ATOM   2157 C  C   . PHE   A 1 315 ? 46.673 5.816   -26.240 1.00 24.01  ?  471 PHE   A C   1 
ATOM   2158 O  O   . PHE   A 1 315 ? 45.983 4.851   -26.593 1.00 22.64  ?  471 PHE   A O   1 
ATOM   2159 C  CB  . PHE   A 1 315 ? 45.788 8.107   -25.679 1.00 20.78  ?  471 PHE   A CB  1 
ATOM   2160 C  CG  . PHE   A 1 315 ? 44.522 8.086   -26.503 1.00 26.38  ?  471 PHE   A CG  1 
ATOM   2161 C  CD1 . PHE   A 1 315 ? 43.282 8.013   -25.888 1.00 27.05  ?  471 PHE   A CD1 1 
ATOM   2162 C  CD2 . PHE   A 1 315 ? 44.571 8.171   -27.888 1.00 22.44  ?  471 PHE   A CD2 1 
ATOM   2163 C  CE1 . PHE   A 1 315 ? 42.115 8.002   -26.634 1.00 22.45  ?  471 PHE   A CE1 1 
ATOM   2164 C  CE2 . PHE   A 1 315 ? 43.402 8.162   -28.641 1.00 24.22  ?  471 PHE   A CE2 1 
ATOM   2165 C  CZ  . PHE   A 1 315 ? 42.175 8.078   -28.011 1.00 23.31  ?  471 PHE   A CZ  1 
ATOM   2166 N  N   . LEU   A 1 316 ? 47.892 6.050   -26.737 1.00 22.76  ?  472 LEU   A N   1 
ATOM   2167 C  CA  . LEU   A 1 316 ? 48.426 5.204   -27.798 1.00 22.13  ?  472 LEU   A CA  1 
ATOM   2168 C  C   . LEU   A 1 316 ? 48.496 3.753   -27.353 1.00 22.22  ?  472 LEU   A C   1 
ATOM   2169 O  O   . LEU   A 1 316 ? 48.110 2.847   -28.103 1.00 22.97  ?  472 LEU   A O   1 
ATOM   2170 C  CB  . LEU   A 1 316 ? 49.805 5.704   -28.225 1.00 22.83  ?  472 LEU   A CB  1 
ATOM   2171 C  CG  . LEU   A 1 316 ? 49.801 6.938   -29.125 1.00 24.42  ?  472 LEU   A CG  1 
ATOM   2172 C  CD1 . LEU   A 1 316 ? 51.213 7.472   -29.319 1.00 22.60  ?  472 LEU   A CD1 1 
ATOM   2173 C  CD2 . LEU   A 1 316 ? 49.153 6.602   -30.457 1.00 23.53  ?  472 LEU   A CD2 1 
ATOM   2174 N  N   . GLN   A 1 317 ? 48.960 3.515   -26.124 1.00 21.56  ?  473 GLN   A N   1 
ATOM   2175 C  CA  . GLN   A 1 317 ? 48.999 2.152   -25.613 1.00 21.74  ?  473 GLN   A CA  1 
ATOM   2176 C  C   . GLN   A 1 317 ? 47.609 1.533   -25.667 1.00 22.16  ?  473 GLN   A C   1 
ATOM   2177 O  O   . GLN   A 1 317 ? 47.429 0.419   -26.180 1.00 25.65  ?  473 GLN   A O   1 
ATOM   2178 C  CB  . GLN   A 1 317 ? 49.562 2.149   -24.190 1.00 21.00  ?  473 GLN   A CB  1 
ATOM   2179 C  CG  . GLN   A 1 317 ? 49.898 0.771   -23.643 1.00 21.29  ?  473 GLN   A CG  1 
ATOM   2180 C  CD  . GLN   A 1 317 ? 50.519 0.831   -22.258 1.00 28.01  ?  473 GLN   A CD  1 
ATOM   2181 O  OE1 . GLN   A 1 317 ? 49.868 1.221   -21.288 1.00 28.75  ?  473 GLN   A OE1 1 
ATOM   2182 N  NE2 . GLN   A 1 317 ? 51.790 0.450   -22.163 1.00 20.82  ?  473 GLN   A NE2 1 
ATOM   2183 N  N   . CYS   A 1 318 ? 46.600 2.289   -25.220 1.00 21.82  ?  474 CYS   A N   1 
ATOM   2184 C  CA  . CYS   A 1 318 ? 45.228 1.798   -25.261 1.00 22.33  ?  474 CYS   A CA  1 
ATOM   2185 C  C   . CYS   A 1 318 ? 44.825 1.423   -26.678 1.00 23.34  ?  474 CYS   A C   1 
ATOM   2186 O  O   . CYS   A 1 318 ? 44.139 0.417   -26.891 1.00 24.08  ?  474 CYS   A O   1 
ATOM   2187 C  CB  . CYS   A 1 318 ? 44.279 2.854   -24.695 1.00 21.90  ?  474 CYS   A CB  1 
ATOM   2188 S  SG  . CYS   A 1 318 ? 44.434 3.118   -22.917 1.00 24.63  ?  474 CYS   A SG  1 
ATOM   2189 N  N   . LEU   A 1 319 ? 45.261 2.210   -27.664 1.00 23.49  ?  475 LEU   A N   1 
ATOM   2190 C  CA  . LEU   A 1 319 ? 44.931 1.897   -29.049 1.00 24.52  ?  475 LEU   A CA  1 
ATOM   2191 C  C   . LEU   A 1 319 ? 45.591 0.596   -29.482 1.00 29.65  ?  475 LEU   A C   1 
ATOM   2192 O  O   . LEU   A 1 319 ? 44.955 -0.256  -30.113 1.00 26.01  ?  475 LEU   A O   1 
ATOM   2193 C  CB  . LEU   A 1 319 ? 45.356 3.044   -29.967 1.00 26.62  ?  475 LEU   A CB  1 
ATOM   2194 C  CG  . LEU   A 1 319 ? 44.533 4.329   -29.905 1.00 24.82  ?  475 LEU   A CG  1 
ATOM   2195 C  CD1 . LEU   A 1 319 ? 45.260 5.470   -30.603 1.00 24.48  ?  475 LEU   A CD1 1 
ATOM   2196 C  CD2 . LEU   A 1 319 ? 43.166 4.102   -30.525 1.00 25.38  ?  475 LEU   A CD2 1 
ATOM   2197 N  N   . ARG   A 1 320 ? 46.869 0.416   -29.133 1.00 24.66  ?  476 ARG   A N   1 
ATOM   2198 C  CA  . ARG   A 1 320 ? 47.609 -0.722  -29.668 1.00 25.32  ?  476 ARG   A CA  1 
ATOM   2199 C  C   . ARG   A 1 320 ? 47.111 -2.031  -29.077 1.00 26.75  ?  476 ARG   A C   1 
ATOM   2200 O  O   . ARG   A 1 320 ? 46.969 -3.029  -29.793 1.00 26.64  ?  476 ARG   A O   1 
ATOM   2201 C  CB  . ARG   A 1 320 ? 49.105 -0.555  -29.411 1.00 24.88  ?  476 ARG   A CB  1 
ATOM   2202 C  CG  . ARG   A 1 320 ? 49.759 0.527   -30.248 1.00 31.37  ?  476 ARG   A CG  1 
ATOM   2203 C  CD  . ARG   A 1 320 ? 51.258 0.309   -30.360 1.00 31.46  ?  476 ARG   A CD  1 
ATOM   2204 N  NE  . ARG   A 1 320 ? 51.979 1.566   -30.524 1.00 24.63  ?  476 ARG   A NE  1 
ATOM   2205 C  CZ  . ARG   A 1 320 ? 52.287 2.383   -29.527 1.00 38.24  ?  476 ARG   A CZ  1 
ATOM   2206 N  NH1 . ARG   A 1 320 ? 51.954 2.105   -28.278 1.00 27.07  ?  476 ARG   A NH1 1 
ATOM   2207 N  NH2 . ARG   A 1 320 ? 52.953 3.505   -29.790 1.00 32.16  ?  476 ARG   A NH2 1 
ATOM   2208 N  N   . THR   A 1 321 ? 46.839 -2.045  -27.776 1.00 25.03  ?  477 THR   A N   1 
ATOM   2209 C  CA  . THR   A 1 321 ? 46.360 -3.237  -27.095 1.00 25.44  ?  477 THR   A CA  1 
ATOM   2210 C  C   . THR   A 1 321 ? 44.844 -3.377  -27.150 1.00 25.94  ?  477 THR   A C   1 
ATOM   2211 O  O   . THR   A 1 321 ? 44.313 -4.370  -26.642 1.00 33.72  ?  477 THR   A O   1 
ATOM   2212 C  CB  . THR   A 1 321 ? 46.825 -3.235  -25.633 1.00 24.63  ?  477 THR   A CB  1 
ATOM   2213 O  OG1 . THR   A 1 321 ? 46.218 -2.140  -24.935 1.00 23.80  ?  477 THR   A OG1 1 
ATOM   2214 C  CG2 . THR   A 1 321 ? 48.343 -3.103  -25.551 1.00 24.26  ?  477 THR   A CG2 1 
ATOM   2215 N  N   . GLU   A 1 322 ? 44.143 -2.409  -27.749 1.00 25.93  ?  478 GLU   A N   1 
ATOM   2216 C  CA  . GLU   A 1 322 ? 42.690 -2.456  -27.923 1.00 27.96  ?  478 GLU   A CA  1 
ATOM   2217 C  C   . GLU   A 1 322 ? 41.974 -2.603  -26.580 1.00 33.74  ?  478 GLU   A C   1 
ATOM   2218 O  O   . GLU   A 1 322 ? 41.073 -3.428  -26.415 1.00 28.56  ?  478 GLU   A O   1 
ATOM   2219 C  CB  . GLU   A 1 322 ? 42.288 -3.579  -28.885 1.00 27.91  ?  478 GLU   A CB  1 
ATOM   2220 C  CG  . GLU   A 1 322 ? 43.123 -3.641  -30.156 1.00 34.46  ?  478 GLU   A CG  1 
ATOM   2221 C  CD  . GLU   A 1 322 ? 42.729 -4.797  -31.054 1.00 55.18  ?  478 GLU   A CD  1 
ATOM   2222 O  OE1 . GLU   A 1 322 ? 41.524 -4.938  -31.349 1.00 52.77  ?  478 GLU   A OE1 1 
ATOM   2223 O  OE2 . GLU   A 1 322 ? 43.625 -5.564  -31.467 1.00 56.02  -1 478 GLU   A OE2 1 
ATOM   2224 N  N   . LYS   A 1 323 ? 42.382 -1.783  -25.612 1.00 28.20  ?  479 LYS   A N   1 
ATOM   2225 C  CA  . LYS   A 1 323 ? 41.838 -1.848  -24.260 1.00 30.09  ?  479 LYS   A CA  1 
ATOM   2226 C  C   . LYS   A 1 323 ? 41.729 -0.441  -23.697 1.00 24.48  ?  479 LYS   A C   1 
ATOM   2227 O  O   . LYS   A 1 323 ? 42.743 0.244   -23.530 1.00 22.93  ?  479 LYS   A O   1 
ATOM   2228 C  CB  . LYS   A 1 323 ? 42.712 -2.720  -23.355 1.00 26.34  ?  479 LYS   A CB  1 
ATOM   2229 N  N   . LEU   A 1 324 ? 40.499 -0.010  -23.413 1.00 29.12  ?  480 LEU   A N   1 
ATOM   2230 C  CA  . LEU   A 1 324 ? 40.251 1.256   -22.718 1.00 25.53  ?  480 LEU   A CA  1 
ATOM   2231 C  C   . LEU   A 1 324 ? 39.013 1.042   -21.846 1.00 26.28  ?  480 LEU   A C   1 
ATOM   2232 O  O   . LEU   A 1 324 ? 37.881 1.192   -22.310 1.00 25.00  ?  480 LEU   A O   1 
ATOM   2233 C  CB  . LEU   A 1 324 ? 40.062 2.416   -23.686 1.00 23.65  ?  480 LEU   A CB  1 
ATOM   2234 C  CG  . LEU   A 1 324 ? 39.796 3.771   -23.020 1.00 22.44  ?  480 LEU   A CG  1 
ATOM   2235 C  CD1 . LEU   A 1 324 ? 40.947 4.163   -22.101 1.00 26.34  ?  480 LEU   A CD1 1 
ATOM   2236 C  CD2 . LEU   A 1 324 ? 39.542 4.855   -24.056 1.00 27.19  ?  480 LEU   A CD2 1 
ATOM   2237 N  N   . GLU   A 1 325 ? 39.248 0.684   -20.587 1.00 27.93  ?  481 GLU   A N   1 
ATOM   2238 C  CA  . GLU   A 1 325 ? 38.151 0.449   -19.658 1.00 28.86  ?  481 GLU   A CA  1 
ATOM   2239 C  C   . GLU   A 1 325 ? 37.391 1.740   -19.398 1.00 24.34  ?  481 GLU   A C   1 
ATOM   2240 O  O   . GLU   A 1 325 ? 37.996 2.787   -19.148 1.00 22.01  ?  481 GLU   A O   1 
ATOM   2241 C  CB  . GLU   A 1 325 ? 38.672 -0.105  -18.334 1.00 27.99  ?  481 GLU   A CB  1 
ATOM   2242 C  CG  . GLU   A 1 325 ? 39.368 -1.444  -18.420 1.00 39.08  ?  481 GLU   A CG  1 
ATOM   2243 C  CD  . GLU   A 1 325 ? 39.853 -1.924  -17.065 1.00 54.06  ?  481 GLU   A CD  1 
ATOM   2244 O  OE1 . GLU   A 1 325 ? 39.607 -1.224  -16.058 1.00 41.29  ?  481 GLU   A OE1 1 
ATOM   2245 O  OE2 . GLU   A 1 325 ? 40.476 -3.003  -17.006 1.00 68.59  -1 481 GLU   A OE2 1 
ATOM   2246 N  N   . ASN   A 1 326 ? 36.063 1.665   -19.453 1.00 27.70  ?  482 ASN   A N   1 
ATOM   2247 C  CA  . ASN   A 1 326 ? 35.240 2.760   -18.959 1.00 29.28  ?  482 ASN   A CA  1 
ATOM   2248 C  C   . ASN   A 1 326 ? 35.606 3.043   -17.508 1.00 24.16  ?  482 ASN   A C   1 
ATOM   2249 O  O   . ASN   A 1 326 ? 35.662 2.127   -16.682 1.00 28.02  ?  482 ASN   A O   1 
ATOM   2250 C  CB  . ASN   A 1 326 ? 33.757 2.407   -19.089 1.00 28.06  ?  482 ASN   A CB  1 
ATOM   2251 C  CG  . ASN   A 1 326 ? 32.841 3.538   -18.652 1.00 35.56  ?  482 ASN   A CG  1 
ATOM   2252 O  OD1 . ASN   A 1 326 ? 32.758 3.867   -17.467 1.00 25.26  ?  482 ASN   A OD1 1 
ATOM   2253 N  ND2 . ASN   A 1 326 ? 32.144 4.138   -19.610 1.00 28.72  ?  482 ASN   A ND2 1 
ATOM   2254 N  N   . TYR   A 1 327 ? 35.872 4.317   -17.205 1.00 24.16  ?  483 TYR   A N   1 
ATOM   2255 C  CA  . TYR   A 1 327 ? 36.402 4.673   -15.890 1.00 30.08  ?  483 TYR   A CA  1 
ATOM   2256 C  C   . TYR   A 1 327 ? 35.444 4.299   -14.767 1.00 23.38  ?  483 TYR   A C   1 
ATOM   2257 O  O   . TYR   A 1 327 ? 35.884 4.000   -13.651 1.00 21.64  ?  483 TYR   A O   1 
ATOM   2258 C  CB  . TYR   A 1 327 ? 36.716 6.168   -15.840 1.00 23.85  ?  483 TYR   A CB  1 
ATOM   2259 C  CG  . TYR   A 1 327 ? 37.638 6.556   -14.707 1.00 24.53  ?  483 TYR   A CG  1 
ATOM   2260 C  CD1 . TYR   A 1 327 ? 38.985 6.221   -14.739 1.00 18.57  ?  483 TYR   A CD1 1 
ATOM   2261 C  CD2 . TYR   A 1 327 ? 37.161 7.252   -13.604 1.00 25.99  ?  483 TYR   A CD2 1 
ATOM   2262 C  CE1 . TYR   A 1 327 ? 39.833 6.571   -13.705 1.00 23.05  ?  483 TYR   A CE1 1 
ATOM   2263 C  CE2 . TYR   A 1 327 ? 38.001 7.606   -12.565 1.00 17.95  ?  483 TYR   A CE2 1 
ATOM   2264 C  CZ  . TYR   A 1 327 ? 39.335 7.262   -12.621 1.00 27.00  ?  483 TYR   A CZ  1 
ATOM   2265 O  OH  . TYR   A 1 327 ? 40.175 7.612   -11.590 1.00 24.56  ?  483 TYR   A OH  1 
ATOM   2266 N  N   . PHE   A 1 328 ? 34.140 4.308   -15.038 1.00 25.64  ?  484 PHE   A N   1 
ATOM   2267 C  CA  . PHE   A 1 328 ? 33.128 3.956   -14.050 1.00 29.34  ?  484 PHE   A CA  1 
ATOM   2268 C  C   . PHE   A 1 328 ? 32.651 2.517   -14.169 1.00 36.81  ?  484 PHE   A C   1 
ATOM   2269 O  O   . PHE   A 1 328 ? 32.206 1.939   -13.172 1.00 34.64  ?  484 PHE   A O   1 
ATOM   2270 C  CB  . PHE   A 1 328 ? 31.920 4.892   -14.179 1.00 30.33  ?  484 PHE   A CB  1 
ATOM   2271 C  CG  . PHE   A 1 328 ? 32.242 6.335   -13.914 1.00 26.90  ?  484 PHE   A CG  1 
ATOM   2272 C  CD1 . PHE   A 1 328 ? 32.702 7.149   -14.936 1.00 28.47  ?  484 PHE   A CD1 1 
ATOM   2273 C  CD2 . PHE   A 1 328 ? 32.086 6.878   -12.649 1.00 33.01  ?  484 PHE   A CD2 1 
ATOM   2274 C  CE1 . PHE   A 1 328 ? 33.005 8.475   -14.703 1.00 35.87  ?  484 PHE   A CE1 1 
ATOM   2275 C  CE2 . PHE   A 1 328 ? 32.385 8.207   -12.410 1.00 34.37  ?  484 PHE   A CE2 1 
ATOM   2276 C  CZ  . PHE   A 1 328 ? 32.846 9.004   -13.439 1.00 31.96  ?  484 PHE   A CZ  1 
ATOM   2277 N  N   . ILE   A 1 329 ? 32.735 1.932   -15.360 1.00 34.03  ?  485 ILE   A N   1 
ATOM   2278 C  CA  . ILE   A 1 329 ? 32.256 0.578   -15.632 1.00 29.76  ?  485 ILE   A CA  1 
ATOM   2279 C  C   . ILE   A 1 329 ? 33.438 -0.235  -16.145 1.00 28.64  ?  485 ILE   A C   1 
ATOM   2280 O  O   . ILE   A 1 329 ? 33.584 -0.411  -17.363 1.00 30.74  ?  485 ILE   A O   1 
ATOM   2281 C  CB  . ILE   A 1 329 ? 31.101 0.596   -16.647 1.00 28.00  ?  485 ILE   A CB  1 
ATOM   2282 C  CG1 . ILE   A 1 329 ? 30.102 1.699   -16.287 1.00 27.74  ?  485 ILE   A CG1 1 
ATOM   2283 C  CG2 . ILE   A 1 329 ? 30.402 -0.760  -16.698 1.00 32.25  ?  485 ILE   A CG2 1 
ATOM   2284 C  CD1 . ILE   A 1 329 ? 29.059 1.957   -17.348 1.00 34.55  ?  485 ILE   A CD1 1 
ATOM   2285 N  N   . PRO   A 1 330 ? 34.293 -0.757  -15.261 1.00 29.69  ?  486 PRO   A N   1 
ATOM   2286 C  CA  . PRO   A 1 330 ? 35.592 -1.285  -15.716 1.00 34.17  ?  486 PRO   A CA  1 
ATOM   2287 C  C   . PRO   A 1 330 ? 35.493 -2.477  -16.654 1.00 40.60  ?  486 PRO   A C   1 
ATOM   2288 O  O   . PRO   A 1 330 ? 36.441 -2.722  -17.411 1.00 35.32  ?  486 PRO   A O   1 
ATOM   2289 C  CB  . PRO   A 1 330 ? 36.302 -1.658  -14.406 1.00 34.24  ?  486 PRO   A CB  1 
ATOM   2290 C  CG  . PRO   A 1 330 ? 35.212 -1.825  -13.403 1.00 36.98  ?  486 PRO   A CG  1 
ATOM   2291 C  CD  . PRO   A 1 330 ? 34.099 -0.906  -13.809 1.00 32.49  ?  486 PRO   A CD  1 
ATOM   2292 N  N   . GLU   A 1 331 ? 34.390 -3.221  -16.641 1.00 35.55  ?  487 GLU   A N   1 
ATOM   2293 C  CA  . GLU   A 1 331 ? 34.252 -4.336  -17.568 1.00 35.19  ?  487 GLU   A CA  1 
ATOM   2294 C  C   . GLU   A 1 331 ? 33.732 -3.910  -18.935 1.00 39.01  ?  487 GLU   A C   1 
ATOM   2295 O  O   . GLU   A 1 331 ? 33.579 -4.763  -19.816 1.00 34.37  ?  487 GLU   A O   1 
ATOM   2296 C  CB  . GLU   A 1 331 ? 33.345 -5.415  -16.971 1.00 42.70  ?  487 GLU   A CB  1 
ATOM   2297 C  CG  . GLU   A 1 331 ? 34.094 -6.428  -16.112 1.00 54.13  ?  487 GLU   A CG  1 
ATOM   2298 C  CD  . GLU   A 1 331 ? 33.176 -7.451  -15.475 1.00 66.97  ?  487 GLU   A CD  1 
ATOM   2299 O  OE1 . GLU   A 1 331 ? 31.945 -7.296  -15.595 1.00 58.07  ?  487 GLU   A OE1 1 
ATOM   2300 O  OE2 . GLU   A 1 331 ? 33.684 -8.408  -14.854 1.00 65.59  -1 487 GLU   A OE2 1 
ATOM   2301 N  N   . PHE   A 1 332 ? 33.462 -2.623  -19.136 1.00 29.06  ?  488 PHE   A N   1 
ATOM   2302 C  CA  . PHE   A 1 332 ? 33.103 -2.101  -20.448 1.00 32.49  ?  488 PHE   A CA  1 
ATOM   2303 C  C   . PHE   A 1 332 ? 34.367 -1.595  -21.134 1.00 27.46  ?  488 PHE   A C   1 
ATOM   2304 O  O   . PHE   A 1 332 ? 35.039 -0.693  -20.622 1.00 28.87  ?  488 PHE   A O   1 
ATOM   2305 C  CB  . PHE   A 1 332 ? 32.066 -0.986  -20.323 1.00 30.29  ?  488 PHE   A CB  1 
ATOM   2306 C  CG  . PHE   A 1 332 ? 31.359 -0.666  -21.611 1.00 29.52  ?  488 PHE   A CG  1 
ATOM   2307 C  CD1 . PHE   A 1 332 ? 31.944 0.170   -22.548 1.00 36.38  ?  488 PHE   A CD1 1 
ATOM   2308 C  CD2 . PHE   A 1 332 ? 30.110 -1.198  -21.882 1.00 31.07  ?  488 PHE   A CD2 1 
ATOM   2309 C  CE1 . PHE   A 1 332 ? 31.295 0.468   -23.733 1.00 29.99  ?  488 PHE   A CE1 1 
ATOM   2310 C  CE2 . PHE   A 1 332 ? 29.458 -0.903  -23.063 1.00 35.14  ?  488 PHE   A CE2 1 
ATOM   2311 C  CZ  . PHE   A 1 332 ? 30.051 -0.069  -23.990 1.00 31.52  ?  488 PHE   A CZ  1 
ATOM   2312 N  N   . ASN   A 1 333 ? 34.688 -2.176  -22.287 1.00 28.08  ?  489 ASN   A N   1 
ATOM   2313 C  CA  . ASN   A 1 333 ? 35.896 -1.836  -23.036 1.00 28.28  ?  489 ASN   A CA  1 
ATOM   2314 C  C   . ASN   A 1 333 ? 35.494 -0.926  -24.194 1.00 27.68  ?  489 ASN   A C   1 
ATOM   2315 O  O   . ASN   A 1 333 ? 34.906 -1.380  -25.178 1.00 28.85  ?  489 ASN   A O   1 
ATOM   2316 C  CB  . ASN   A 1 333 ? 36.596 -3.099  -23.529 1.00 27.91  ?  489 ASN   A CB  1 
ATOM   2317 C  CG  . ASN   A 1 333 ? 37.921 -2.809  -24.207 1.00 30.53  ?  489 ASN   A CG  1 
ATOM   2318 O  OD1 . ASN   A 1 333 ? 38.304 -1.652  -24.387 1.00 26.75  ?  489 ASN   A OD1 1 
ATOM   2319 N  ND2 . ASN   A 1 333 ? 38.632 -3.864  -24.586 1.00 27.66  ?  489 ASN   A ND2 1 
ATOM   2320 N  N   . LEU   A 1 334 ? 35.822 0.363   -24.075 1.00 26.72  ?  490 LEU   A N   1 
ATOM   2321 C  CA  . LEU   A 1 334 ? 35.467 1.312   -25.124 1.00 30.99  ?  490 LEU   A CA  1 
ATOM   2322 C  C   . LEU   A 1 334 ? 36.220 1.031   -26.417 1.00 27.41  ?  490 LEU   A C   1 
ATOM   2323 O  O   . LEU   A 1 334 ? 35.752 1.400   -27.500 1.00 28.21  ?  490 LEU   A O   1 
ATOM   2324 C  CB  . LEU   A 1 334 ? 35.742 2.743   -24.654 1.00 26.02  ?  490 LEU   A CB  1 
ATOM   2325 C  CG  . LEU   A 1 334 ? 35.019 3.202   -23.386 1.00 25.65  ?  490 LEU   A CG  1 
ATOM   2326 C  CD1 . LEU   A 1 334 ? 35.693 4.434   -22.806 1.00 24.44  ?  490 LEU   A CD1 1 
ATOM   2327 C  CD2 . LEU   A 1 334 ? 33.557 3.485   -23.684 1.00 26.77  ?  490 LEU   A CD2 1 
ATOM   2328 N  N   . PHE   A 1 335 ? 37.385 0.388   -26.329 1.00 26.91  ?  491 PHE   A N   1 
ATOM   2329 C  CA  . PHE   A 1 335 ? 38.195 0.075   -27.498 1.00 27.24  ?  491 PHE   A CA  1 
ATOM   2330 C  C   . PHE   A 1 335 ? 38.073 -1.384  -27.922 1.00 36.27  ?  491 PHE   A C   1 
ATOM   2331 O  O   . PHE   A 1 335 ? 38.988 -1.919  -28.557 1.00 37.60  ?  491 PHE   A O   1 
ATOM   2332 C  CB  . PHE   A 1 335 ? 39.659 0.430   -27.234 1.00 27.21  ?  491 PHE   A CB  1 
ATOM   2333 C  CG  . PHE   A 1 335 ? 39.973 1.886   -27.421 1.00 27.85  ?  491 PHE   A CG  1 
ATOM   2334 C  CD1 . PHE   A 1 335 ? 39.003 2.765   -27.875 1.00 25.92  ?  491 PHE   A CD1 1 
ATOM   2335 C  CD2 . PHE   A 1 335 ? 41.241 2.373   -27.154 1.00 29.03  ?  491 PHE   A CD2 1 
ATOM   2336 C  CE1 . PHE   A 1 335 ? 39.292 4.106   -28.053 1.00 25.45  ?  491 PHE   A CE1 1 
ATOM   2337 C  CE2 . PHE   A 1 335 ? 41.536 3.712   -27.330 1.00 24.06  ?  491 PHE   A CE2 1 
ATOM   2338 C  CZ  . PHE   A 1 335 ? 40.560 4.580   -27.780 1.00 24.52  ?  491 PHE   A CZ  1 
ATOM   2339 N  N   . SER   A 1 336 ? 36.966 -2.038  -27.578 1.00 33.56  ?  492 SER   A N   1 
ATOM   2340 C  CA  . SER   A 1 336 ? 36.751 -3.410  -28.010 1.00 33.19  ?  492 SER   A CA  1 
ATOM   2341 C  C   . SER   A 1 336 ? 36.662 -3.479  -29.530 1.00 39.72  ?  492 SER   A C   1 
ATOM   2342 O  O   . SER   A 1 336 ? 36.225 -2.535  -30.195 1.00 38.01  ?  492 SER   A O   1 
ATOM   2343 C  CB  . SER   A 1 336 ? 35.473 -3.969  -27.384 1.00 34.39  ?  492 SER   A CB  1 
ATOM   2344 O  OG  . SER   A 1 336 ? 35.266 -5.316  -27.770 1.00 41.52  ?  492 SER   A OG  1 
ATOM   2345 N  N   . SER   A 1 337 ? 37.091 -4.616  -30.084 1.00 38.94  ?  493 SER   A N   1 
ATOM   2346 C  CA  . SER   A 1 337 ? 36.961 -4.825  -31.522 1.00 48.17  ?  493 SER   A CA  1 
ATOM   2347 C  C   . SER   A 1 337 ? 35.504 -4.876  -31.959 1.00 41.74  ?  493 SER   A C   1 
ATOM   2348 O  O   . SER   A 1 337 ? 35.216 -4.694  -33.147 1.00 39.83  ?  493 SER   A O   1 
ATOM   2349 C  CB  . SER   A 1 337 ? 37.683 -6.108  -31.938 1.00 40.39  ?  493 SER   A CB  1 
ATOM   2350 O  OG  . SER   A 1 337 ? 37.100 -7.241  -31.320 1.00 54.53  ?  493 SER   A OG  1 
ATOM   2351 N  N   . ASN   A 1 338 ? 34.581 -5.119  -31.025 1.00 45.57  ?  494 ASN   A N   1 
ATOM   2352 C  CA  . ASN   A 1 338 ? 33.155 -5.071  -31.321 1.00 56.11  ?  494 ASN   A CA  1 
ATOM   2353 C  C   . ASN   A 1 338 ? 32.646 -3.648  -31.513 1.00 50.41  ?  494 ASN   A C   1 
ATOM   2354 O  O   . ASN   A 1 338 ? 31.529 -3.471  -32.011 1.00 57.77  ?  494 ASN   A O   1 
ATOM   2355 C  CB  . ASN   A 1 338 ? 32.367 -5.751  -30.198 1.00 53.98  ?  494 ASN   A CB  1 
ATOM   2356 C  CG  . ASN   A 1 338 ? 32.816 -7.179  -29.948 1.00 69.61  ?  494 ASN   A CG  1 
ATOM   2357 O  OD1 . ASN   A 1 338 ? 33.441 -7.805  -30.804 1.00 70.13  ?  494 ASN   A OD1 1 
ATOM   2358 N  ND2 . ASN   A 1 338 ? 32.504 -7.700  -28.766 1.00 62.88  ?  494 ASN   A ND2 1 
ATOM   2359 N  N   . LEU   A 1 339 ? 33.428 -2.641  -31.132 1.00 40.48  ?  495 LEU   A N   1 
ATOM   2360 C  CA  . LEU   A 1 339 ? 33.036 -1.242  -31.256 1.00 49.97  ?  495 LEU   A CA  1 
ATOM   2361 C  C   . LEU   A 1 339 ? 33.861 -0.474  -32.276 1.00 41.81  ?  495 LEU   A C   1 
ATOM   2362 O  O   . LEU   A 1 339 ? 33.306 0.317   -33.042 1.00 35.93  ?  495 LEU   A O   1 
ATOM   2363 C  CB  . LEU   A 1 339 ? 33.139 -0.545  -29.894 1.00 37.00  ?  495 LEU   A CB  1 
ATOM   2364 C  CG  . LEU   A 1 339 ? 32.259 -1.131  -28.786 1.00 34.84  ?  495 LEU   A CG  1 
ATOM   2365 C  CD1 . LEU   A 1 339 ? 32.524 -0.441  -27.455 1.00 32.88  ?  495 LEU   A CD1 1 
ATOM   2366 C  CD2 . LEU   A 1 339 ? 30.785 -1.034  -29.159 1.00 38.26  ?  495 LEU   A CD2 1 
ATOM   2367 N  N   . ILE   A 1 340 ? 35.176 -0.682  -32.302 1.00 37.31  ?  496 ILE   A N   1 
ATOM   2368 C  CA  . ILE   A 1 340 ? 36.075 -0.026  -33.244 1.00 33.09  ?  496 ILE   A CA  1 
ATOM   2369 C  C   . ILE   A 1 340 ? 36.996 -1.091  -33.821 1.00 42.70  ?  496 ILE   A C   1 
ATOM   2370 O  O   . ILE   A 1 340 ? 37.571 -1.888  -33.071 1.00 37.76  ?  496 ILE   A O   1 
ATOM   2371 C  CB  . ILE   A 1 340 ? 36.894 1.094   -32.572 1.00 37.89  ?  496 ILE   A CB  1 
ATOM   2372 C  CG1 . ILE   A 1 340 ? 35.972 2.094   -31.866 1.00 33.84  ?  496 ILE   A CG1 1 
ATOM   2373 C  CG2 . ILE   A 1 340 ? 37.773 1.801   -33.594 1.00 34.23  ?  496 ILE   A CG2 1 
ATOM   2374 C  CD1 . ILE   A 1 340 ? 36.702 3.086   -30.982 1.00 30.06  ?  496 ILE   A CD1 1 
ATOM   2375 N  N   . ASP   A 1 341 ? 37.134 -1.113  -35.144 1.00 36.69  ?  497 ASP   A N   1 
ATOM   2376 C  CA  . ASP   A 1 341 ? 37.933 -2.163  -35.754 1.00 34.05  ?  497 ASP   A CA  1 
ATOM   2377 C  C   . ASP   A 1 341 ? 39.424 -1.867  -35.605 1.00 39.98  ?  497 ASP   A C   1 
ATOM   2378 O  O   . ASP   A 1 341 ? 39.836 -0.753  -35.268 1.00 35.58  ?  497 ASP   A O   1 
ATOM   2379 C  CB  . ASP   A 1 341 ? 37.547 -2.363  -37.227 1.00 45.52  ?  497 ASP   A CB  1 
ATOM   2380 C  CG  . ASP   A 1 341 ? 37.811 -1.138  -38.100 1.00 44.32  ?  497 ASP   A CG  1 
ATOM   2381 O  OD1 . ASP   A 1 341 ? 38.638 -0.279  -37.744 1.00 49.31  ?  497 ASP   A OD1 1 
ATOM   2382 O  OD2 . ASP   A 1 341 ? 37.175 -1.041  -39.172 1.00 60.50  -1 497 ASP   A OD2 1 
ATOM   2383 N  N   . LYS   A 1 342 ? 40.234 -2.896  -35.863 1.00 37.74  ?  498 LYS   A N   1 
ATOM   2384 C  CA  . LYS   A 1 342 ? 41.678 -2.780  -35.683 1.00 39.87  ?  498 LYS   A CA  1 
ATOM   2385 C  C   . LYS   A 1 342 ? 42.272 -1.698  -36.578 1.00 38.97  ?  498 LYS   A C   1 
ATOM   2386 O  O   . LYS   A 1 342 ? 43.143 -0.933  -36.145 1.00 37.72  ?  498 LYS   A O   1 
ATOM   2387 C  CB  . LYS   A 1 342 ? 42.342 -4.128  -35.962 1.00 50.16  ?  498 LYS   A CB  1 
ATOM   2388 C  CG  . LYS   A 1 342 ? 43.847 -4.145  -35.761 1.00 60.15  ?  498 LYS   A CG  1 
ATOM   2389 C  CD  . LYS   A 1 342 ? 44.211 -4.246  -34.290 1.00 42.33  ?  498 LYS   A CD  1 
ATOM   2390 C  CE  . LYS   A 1 342 ? 45.719 -4.265  -34.098 1.00 44.40  ?  498 LYS   A CE  1 
ATOM   2391 N  NZ  . LYS   A 1 342 ? 46.181 -3.167  -33.206 1.00 47.57  ?  498 LYS   A NZ  1 
ATOM   2392 N  N   . ARG   A 1 343 ? 41.812 -1.618  -37.830 1.00 35.57  ?  499 ARG   A N   1 
ATOM   2393 C  CA  . ARG   A 1 343 ? 42.417 -0.698  -38.790 1.00 36.39  ?  499 ARG   A CA  1 
ATOM   2394 C  C   . ARG   A 1 343 ? 42.229 0.756   -38.374 1.00 39.70  ?  499 ARG   A C   1 
ATOM   2395 O  O   . ARG   A 1 343 ? 43.139 1.576   -38.539 1.00 38.80  ?  499 ARG   A O   1 
ATOM   2396 C  CB  . ARG   A 1 343 ? 41.831 -0.934  -40.181 1.00 47.95  ?  499 ARG   A CB  1 
ATOM   2397 C  CG  . ARG   A 1 343 ? 42.227 0.115   -41.214 1.00 66.61  ?  499 ARG   A CG  1 
ATOM   2398 C  CD  . ARG   A 1 343 ? 43.667 -0.064  -41.679 1.00 74.66  ?  499 ARG   A CD  1 
ATOM   2399 N  NE  . ARG   A 1 343 ? 44.563 0.975   -41.183 1.00 66.65  ?  499 ARG   A NE  1 
ATOM   2400 C  CZ  . ARG   A 1 343 ? 44.802 2.119   -41.809 1.00 70.58  ?  499 ARG   A CZ  1 
ATOM   2401 N  NH1 . ARG   A 1 343 ? 44.176 2.437   -42.931 1.00 55.14  ?  499 ARG   A NH1 1 
ATOM   2402 N  NH2 . ARG   A 1 343 ? 45.695 2.965   -41.300 1.00 64.09  ?  499 ARG   A NH2 1 
ATOM   2403 N  N   . SER   A 1 344 ? 41.050 1.099   -37.847 1.00 34.43  ?  500 SER   A N   1 
ATOM   2404 C  CA  . SER   A 1 344 ? 40.814 2.469   -37.401 1.00 32.09  ?  500 SER   A CA  1 
ATOM   2405 C  C   . SER   A 1 344 ? 41.782 2.857   -36.289 1.00 30.60  ?  500 SER   A C   1 
ATOM   2406 O  O   . SER   A 1 344 ? 42.353 3.958   -36.299 1.00 30.11  ?  500 SER   A O   1 
ATOM   2407 C  CB  . SER   A 1 344 ? 39.367 2.625   -36.929 1.00 32.56  ?  500 SER   A CB  1 
ATOM   2408 O  OG  . SER   A 1 344 ? 38.451 2.388   -37.986 1.00 42.55  ?  500 SER   A OG  1 
ATOM   2409 N  N   . LYS   A 1 345 ? 41.986 1.956   -35.326 1.00 31.34  ?  501 LYS   A N   1 
ATOM   2410 C  CA  . LYS   A 1 345 ? 42.897 2.243   -34.225 1.00 28.66  ?  501 LYS   A CA  1 
ATOM   2411 C  C   . LYS   A 1 345 ? 44.340 2.314   -34.704 1.00 28.48  ?  501 LYS   A C   1 
ATOM   2412 O  O   . LYS   A 1 345 ? 45.115 3.142   -34.219 1.00 27.95  ?  501 LYS   A O   1 
ATOM   2413 C  CB  . LYS   A 1 345 ? 42.738 1.193   -33.127 1.00 33.84  ?  501 LYS   A CB  1 
ATOM   2414 C  CG  . LYS   A 1 345 ? 41.385 1.256   -32.440 1.00 39.14  ?  501 LYS   A CG  1 
ATOM   2415 C  CD  . LYS   A 1 345 ? 41.347 0.387   -31.201 1.00 42.29  ?  501 LYS   A CD  1 
ATOM   2416 C  CE  . LYS   A 1 345 ? 41.127 -1.069  -31.566 1.00 47.78  ?  501 LYS   A CE  1 
ATOM   2417 N  NZ  . LYS   A 1 345 ? 39.732 -1.341  -32.013 1.00 40.42  ?  501 LYS   A NZ  1 
ATOM   2418 N  N   . GLU   A 1 346 ? 44.721 1.462   -35.663 1.00 29.34  ?  502 GLU   A N   1 
ATOM   2419 C  CA  . GLU   A 1 346 ? 46.068 1.552   -36.222 1.00 31.62  ?  502 GLU   A CA  1 
ATOM   2420 C  C   . GLU   A 1 346 ? 46.274 2.871   -36.959 1.00 34.07  ?  502 GLU   A C   1 
ATOM   2421 O  O   . GLU   A 1 346 ? 47.350 3.478   -36.874 1.00 34.58  ?  502 GLU   A O   1 
ATOM   2422 C  CB  . GLU   A 1 346 ? 46.333 0.369   -37.156 1.00 36.58  ?  502 GLU   A CB  1 
ATOM   2423 C  CG  . GLU   A 1 346 ? 46.584 -0.949  -36.439 1.00 37.97  ?  502 GLU   A CG  1 
ATOM   2424 C  CD  . GLU   A 1 346 ? 46.746 -2.118  -37.396 1.00 45.38  ?  502 GLU   A CD  1 
ATOM   2425 O  OE1 . GLU   A 1 346 ? 46.338 -1.991  -38.570 1.00 52.34  ?  502 GLU   A OE1 1 
ATOM   2426 O  OE2 . GLU   A 1 346 ? 47.285 -3.162  -36.974 1.00 66.11  -1 502 GLU   A OE2 1 
ATOM   2427 N  N   . PHE   A 1 347 ? 45.251 3.334   -37.680 1.00 30.36  ?  503 PHE   A N   1 
ATOM   2428 C  CA  . PHE   A 1 347 ? 45.354 4.607   -38.385 1.00 32.57  ?  503 PHE   A CA  1 
ATOM   2429 C  C   . PHE   A 1 347 ? 45.523 5.759   -37.405 1.00 31.12  ?  503 PHE   A C   1 
ATOM   2430 O  O   . PHE   A 1 347 ? 46.383 6.631   -37.593 1.00 37.15  ?  503 PHE   A O   1 
ATOM   2431 C  CB  . PHE   A 1 347 ? 44.120 4.820   -39.263 1.00 39.02  ?  503 PHE   A CB  1 
ATOM   2432 C  CG  . PHE   A 1 347 ? 44.159 6.089   -40.065 1.00 35.04  ?  503 PHE   A CG  1 
ATOM   2433 C  CD1 . PHE   A 1 347 ? 44.835 6.139   -41.273 1.00 33.99  ?  503 PHE   A CD1 1 
ATOM   2434 C  CD2 . PHE   A 1 347 ? 43.518 7.232   -39.614 1.00 32.24  ?  503 PHE   A CD2 1 
ATOM   2435 C  CE1 . PHE   A 1 347 ? 44.872 7.302   -42.016 1.00 43.20  ?  503 PHE   A CE1 1 
ATOM   2436 C  CE2 . PHE   A 1 347 ? 43.551 8.399   -40.352 1.00 50.22  ?  503 PHE   A CE2 1 
ATOM   2437 C  CZ  . PHE   A 1 347 ? 44.230 8.435   -41.554 1.00 42.09  ?  503 PHE   A CZ  1 
ATOM   2438 N  N   . LEU   A 1 348 ? 44.701 5.784   -36.350 1.00 29.01  ?  504 LEU   A N   1 
ATOM   2439 C  CA  . LEU   A 1 348 ? 44.831 6.845   -35.357 1.00 28.03  ?  504 LEU   A CA  1 
ATOM   2440 C  C   . LEU   A 1 348 ? 46.182 6.770   -34.654 1.00 27.99  ?  504 LEU   A C   1 
ATOM   2441 O  O   . LEU   A 1 348 ? 46.813 7.802   -34.391 1.00 36.30  ?  504 LEU   A O   1 
ATOM   2442 C  CB  . LEU   A 1 348 ? 43.687 6.771   -34.346 1.00 27.58  ?  504 LEU   A CB  1 
ATOM   2443 C  CG  . LEU   A 1 348 ? 43.704 7.892   -33.305 1.00 36.00  ?  504 LEU   A CG  1 
ATOM   2444 C  CD1 . LEU   A 1 348 ? 43.707 9.252   -33.992 1.00 27.15  ?  504 LEU   A CD1 1 
ATOM   2445 C  CD2 . LEU   A 1 348 ? 42.531 7.773   -32.343 1.00 26.32  ?  504 LEU   A CD2 1 
ATOM   2446 N  N   . THR   A 1 349 ? 46.644 5.553   -34.355 1.00 26.91  ?  505 THR   A N   1 
ATOM   2447 C  CA  . THR   A 1 349 ? 47.960 5.362   -33.761 1.00 27.17  ?  505 THR   A CA  1 
ATOM   2448 C  C   . THR   A 1 349 ? 49.047 5.994   -34.619 1.00 29.83  ?  505 THR   A C   1 
ATOM   2449 O  O   . THR   A 1 349 ? 49.878 6.768   -34.125 1.00 27.80  ?  505 THR   A O   1 
ATOM   2450 C  CB  . THR   A 1 349 ? 48.227 3.867   -33.581 1.00 31.75  ?  505 THR   A CB  1 
ATOM   2451 O  OG1 . THR   A 1 349 ? 47.327 3.327   -32.604 1.00 34.29  ?  505 THR   A OG1 1 
ATOM   2452 C  CG2 . THR   A 1 349 ? 49.658 3.630   -33.146 1.00 26.57  ?  505 THR   A CG2 1 
ATOM   2453 N  N   . LYS   A 1 350 ? 49.055 5.665   -35.914 1.00 34.32  ?  506 LYS   A N   1 
ATOM   2454 C  CA  . LYS   A 1 350 ? 50.080 6.188   -36.813 1.00 35.13  ?  506 LYS   A CA  1 
ATOM   2455 C  C   . LYS   A 1 350 ? 50.000 7.707   -36.904 1.00 31.96  ?  506 LYS   A C   1 
ATOM   2456 O  O   . LYS   A 1 350 ? 51.024 8.395   -36.821 1.00 35.68  ?  506 LYS   A O   1 
ATOM   2457 C  CB  . LYS   A 1 350 ? 49.952 5.516   -38.193 1.00 33.10  ?  506 LYS   A CB  1 
ATOM   2458 C  CG  . LYS   A 1 350 ? 50.608 6.163   -39.463 1.00 49.06  ?  506 LYS   A CG  1 
ATOM   2459 C  CD  . LYS   A 1 350 ? 51.916 6.967   -39.297 1.00 67.09  ?  506 LYS   A CD  1 
ATOM   2460 C  CE  . LYS   A 1 350 ? 53.001 6.263   -38.492 1.00 60.78  ?  506 LYS   A CE  1 
ATOM   2461 N  NZ  . LYS   A 1 350 ? 54.018 7.249   -38.019 1.00 54.59  ?  506 LYS   A NZ  1 
ATOM   2462 N  N   . GLN   A 1 351 ? 48.793 8.256   -37.058 1.00 28.74  ?  507 GLN   A N   1 
ATOM   2463 C  CA  . GLN   A 1 351 ? 48.678 9.707   -37.183 1.00 30.38  ?  507 GLN   A CA  1 
ATOM   2464 C  C   . GLN   A 1 351 ? 49.185 10.416  -35.930 1.00 27.67  ?  507 GLN   A C   1 
ATOM   2465 O  O   . GLN   A 1 351 ? 49.909 11.418  -36.023 1.00 29.23  ?  507 GLN   A O   1 
ATOM   2466 C  CB  . GLN   A 1 351 ? 47.233 10.096  -37.497 1.00 29.68  ?  507 GLN   A CB  1 
ATOM   2467 C  CG  . GLN   A 1 351 ? 46.795 9.675   -38.892 1.00 37.18  ?  507 GLN   A CG  1 
ATOM   2468 C  CD  . GLN   A 1 351 ? 47.816 10.045  -39.954 1.00 37.50  ?  507 GLN   A CD  1 
ATOM   2469 O  OE1 . GLN   A 1 351 ? 48.247 11.195  -40.046 1.00 47.08  ?  507 GLN   A OE1 1 
ATOM   2470 N  NE2 . GLN   A 1 351 ? 48.220 9.063   -40.753 1.00 36.56  ?  507 GLN   A NE2 1 
ATOM   2471 N  N   . ILE   A 1 352 ? 48.851 9.890   -34.746 1.00 30.06  ?  508 ILE   A N   1 
ATOM   2472 C  CA  . ILE   A 1 352 ? 49.283 10.522  -33.501 1.00 25.65  ?  508 ILE   A CA  1 
ATOM   2473 C  C   . ILE   A 1 352 ? 50.797 10.425  -33.341 1.00 27.61  ?  508 ILE   A C   1 
ATOM   2474 O  O   . ILE   A 1 352 ? 51.454 11.389  -32.923 1.00 25.20  ?  508 ILE   A O   1 
ATOM   2475 C  CB  . ILE   A 1 352 ? 48.554 9.898   -32.297 1.00 26.29  ?  508 ILE   A CB  1 
ATOM   2476 C  CG1 . ILE   A 1 352 ? 47.067 10.257  -32.306 1.00 31.93  ?  508 ILE   A CG1 1 
ATOM   2477 C  CG2 . ILE   A 1 352 ? 49.196 10.343  -30.992 1.00 23.71  ?  508 ILE   A CG2 1 
ATOM   2478 C  CD1 . ILE   A 1 352 ? 46.244 9.461   -31.308 1.00 24.36  ?  508 ILE   A CD1 1 
ATOM   2479 N  N   . GLU   A 1 353 ? 51.371 9.255   -33.638 1.00 25.64  ?  509 GLU   A N   1 
ATOM   2480 C  CA  . GLU   A 1 353 ? 52.822 9.108   -33.558 1.00 25.95  ?  509 GLU   A CA  1 
ATOM   2481 C  C   . GLU   A 1 353 ? 53.524 10.059  -34.519 1.00 26.50  ?  509 GLU   A C   1 
ATOM   2482 O  O   . GLU   A 1 353 ? 54.555 10.654  -34.177 1.00 26.40  ?  509 GLU   A O   1 
ATOM   2483 C  CB  . GLU   A 1 353 ? 53.228 7.665   -33.849 1.00 25.90  ?  509 GLU   A CB  1 
ATOM   2484 C  CG  . GLU   A 1 353 ? 53.028 6.716   -32.686 1.00 25.08  ?  509 GLU   A CG  1 
ATOM   2485 C  CD  . GLU   A 1 353 ? 53.216 5.270   -33.088 1.00 33.78  ?  509 GLU   A CD  1 
ATOM   2486 O  OE1 . GLU   A 1 353 ? 53.137 4.971   -34.299 1.00 31.74  ?  509 GLU   A OE1 1 
ATOM   2487 O  OE2 . GLU   A 1 353 ? 53.446 4.431   -32.193 1.00 31.23  -1 509 GLU   A OE2 1 
ATOM   2488 N  N   . TYR   A 1 354 ? 52.983 10.212  -35.731 1.00 29.82  ?  510 TYR   A N   1 
ATOM   2489 C  CA  . TYR   A 1 354 ? 53.532 11.192  -36.661 1.00 28.41  ?  510 TYR   A CA  1 
ATOM   2490 C  C   . TYR   A 1 354 ? 53.514 12.580  -36.042 1.00 32.33  ?  510 TYR   A C   1 
ATOM   2491 O  O   . TYR   A 1 354 ? 54.522 13.295  -36.062 1.00 32.20  ?  510 TYR   A O   1 
ATOM   2492 C  CB  . TYR   A 1 354 ? 52.748 11.189  -37.975 1.00 29.52  ?  510 TYR   A CB  1 
ATOM   2493 C  CG  . TYR   A 1 354 ? 53.121 12.337  -38.894 1.00 37.98  ?  510 TYR   A CG  1 
ATOM   2494 C  CD1 . TYR   A 1 354 ? 54.146 12.199  -39.815 1.00 35.18  ?  510 TYR   A CD1 1 
ATOM   2495 C  CD2 . TYR   A 1 354 ? 52.458 13.564  -38.829 1.00 30.78  ?  510 TYR   A CD2 1 
ATOM   2496 C  CE1 . TYR   A 1 354 ? 54.500 13.238  -40.651 1.00 45.22  ?  510 TYR   A CE1 1 
ATOM   2497 C  CE2 . TYR   A 1 354 ? 52.812 14.613  -39.659 1.00 46.92  ?  510 TYR   A CE2 1 
ATOM   2498 C  CZ  . TYR   A 1 354 ? 53.834 14.445  -40.572 1.00 54.37  ?  510 TYR   A CZ  1 
ATOM   2499 O  OH  . TYR   A 1 354 ? 54.191 15.473  -41.406 1.00 64.27  ?  510 TYR   A OH  1 
ATOM   2500 N  N   . GLU   A 1 355 ? 52.367 12.977  -35.486 1.00 28.15  ?  511 GLU   A N   1 
ATOM   2501 C  CA  . GLU   A 1 355 ? 52.256 14.300  -34.880 1.00 27.35  ?  511 GLU   A CA  1 
ATOM   2502 C  C   . GLU   A 1 355 ? 53.309 14.504  -33.800 1.00 29.50  ?  511 GLU   A C   1 
ATOM   2503 O  O   . GLU   A 1 355 ? 54.012 15.520  -33.783 1.00 31.93  ?  511 GLU   A O   1 
ATOM   2504 C  CB  . GLU   A 1 355 ? 50.854 14.504  -34.303 1.00 26.86  ?  511 GLU   A CB  1 
ATOM   2505 C  CG  . GLU   A 1 355 ? 49.759 14.542  -35.344 1.00 29.49  ?  511 GLU   A CG  1 
ATOM   2506 C  CD  . GLU   A 1 355 ? 49.933 15.692  -36.311 1.00 37.54  ?  511 GLU   A CD  1 
ATOM   2507 O  OE1 . GLU   A 1 355 ? 50.134 16.830  -35.839 1.00 39.55  ?  511 GLU   A OE1 1 
ATOM   2508 O  OE2 . GLU   A 1 355 ? 49.874 15.462  -37.537 1.00 48.46  -1 511 GLU   A OE2 1 
ATOM   2509 N  N   . ARG   A 1 356 ? 53.441 13.533  -32.894 1.00 28.62  ?  512 ARG   A N   1 
ATOM   2510 C  CA  . ARG   A 1 356 ? 54.375 13.695  -31.784 1.00 24.93  ?  512 ARG   A CA  1 
ATOM   2511 C  C   . ARG   A 1 356 ? 55.815 13.766  -32.275 1.00 27.69  ?  512 ARG   A C   1 
ATOM   2512 O  O   . ARG   A 1 356 ? 56.614 14.563  -31.766 1.00 34.43  ?  512 ARG   A O   1 
ATOM   2513 C  CB  . ARG   A 1 356 ? 54.220 12.561  -30.774 1.00 26.67  ?  512 ARG   A CB  1 
ATOM   2514 C  CG  . ARG   A 1 356 ? 55.335 12.563  -29.750 1.00 29.81  ?  512 ARG   A CG  1 
ATOM   2515 C  CD  . ARG   A 1 356 ? 55.120 11.555  -28.654 1.00 32.51  ?  512 ARG   A CD  1 
ATOM   2516 N  NE  . ARG   A 1 356 ? 54.994 10.194  -29.154 1.00 28.04  ?  512 ARG   A NE  1 
ATOM   2517 C  CZ  . ARG   A 1 356 ? 54.685 9.154   -28.393 1.00 26.07  ?  512 ARG   A CZ  1 
ATOM   2518 N  NH1 . ARG   A 1 356 ? 54.475 9.290   -27.094 1.00 23.17  ?  512 ARG   A NH1 1 
ATOM   2519 N  NH2 . ARG   A 1 356 ? 54.587 7.950   -28.947 1.00 22.62  ?  512 ARG   A NH2 1 
ATOM   2520 N  N   . ASN   A 1 357 ? 56.167 12.945  -33.266 1.00 27.31  ?  513 ASN   A N   1 
ATOM   2521 C  CA  . ASN   A 1 357 ? 57.529 12.970  -33.787 1.00 34.40  ?  513 ASN   A CA  1 
ATOM   2522 C  C   . ASN   A 1 357 ? 57.876 14.289  -34.469 1.00 41.99  ?  513 ASN   A C   1 
ATOM   2523 O  O   . ASN   A 1 357 ? 59.062 14.626  -34.565 1.00 37.37  ?  513 ASN   A O   1 
ATOM   2524 C  CB  . ASN   A 1 357 ? 57.735 11.808  -34.759 1.00 28.10  ?  513 ASN   A CB  1 
ATOM   2525 C  CG  . ASN   A 1 357 ? 57.955 10.489  -34.045 1.00 28.05  ?  513 ASN   A CG  1 
ATOM   2526 O  OD1 . ASN   A 1 357 ? 58.613 10.439  -33.008 1.00 28.71  ?  513 ASN   A OD1 1 
ATOM   2527 N  ND2 . ASN   A 1 357 ? 57.411 9.412   -34.602 1.00 27.26  ?  513 ASN   A ND2 1 
ATOM   2528 N  N   . ASN   A 1 358 ? 56.877 15.044  -34.929 1.00 41.27  ?  514 ASN   A N   1 
ATOM   2529 C  CA  . ASN   A 1 358 ? 57.088 16.282  -35.670 1.00 40.59  ?  514 ASN   A CA  1 
ATOM   2530 C  C   . ASN   A 1 358 ? 56.598 17.505  -34.905 1.00 37.83  ?  514 ASN   A C   1 
ATOM   2531 O  O   . ASN   A 1 358 ? 56.312 18.541  -35.516 1.00 39.81  ?  514 ASN   A O   1 
ATOM   2532 C  CB  . ASN   A 1 358 ? 56.403 16.203  -37.035 1.00 30.48  ?  514 ASN   A CB  1 
ATOM   2533 C  CG  . ASN   A 1 358 ? 57.088 15.228  -37.973 1.00 31.20  ?  514 ASN   A CG  1 
ATOM   2534 O  OD1 . ASN   A 1 358 ? 58.067 15.571  -38.634 1.00 37.44  ?  514 ASN   A OD1 1 
ATOM   2535 N  ND2 . ASN   A 1 358 ? 56.573 14.006  -38.038 1.00 40.40  ?  514 ASN   A ND2 1 
ATOM   2536 N  N   . GLU   A 1 359 ? 56.493 17.396  -33.578 1.00 39.78  ?  515 GLU   A N   1 
ATOM   2537 C  CA  . GLU   A 1 359 ? 56.080 18.500  -32.709 1.00 42.87  ?  515 GLU   A CA  1 
ATOM   2538 C  C   . GLU   A 1 359 ? 54.692 19.026  -33.072 1.00 35.14  ?  515 GLU   A C   1 
ATOM   2539 O  O   . GLU   A 1 359 ? 54.452 20.235  -33.094 1.00 43.24  ?  515 GLU   A O   1 
ATOM   2540 C  CB  . GLU   A 1 359 ? 57.115 19.626  -32.715 1.00 62.94  ?  515 GLU   A CB  1 
ATOM   2541 C  CG  . GLU   A 1 359 ? 58.371 19.290  -31.926 1.00 64.76  ?  515 GLU   A CG  1 
ATOM   2542 C  CD  . GLU   A 1 359 ? 59.527 20.217  -32.238 1.00 77.27  ?  515 GLU   A CD  1 
ATOM   2543 O  OE1 . GLU   A 1 359 ? 59.366 21.102  -33.103 1.00 79.80  ?  515 GLU   A OE1 1 
ATOM   2544 O  OE2 . GLU   A 1 359 ? 60.601 20.054  -31.619 1.00 84.76  -1 515 GLU   A OE2 1 
ATOM   2545 N  N   . PHE   A 1 360 ? 53.776 18.102  -33.364 1.00 34.54  ?  516 PHE   A N   1 
ATOM   2546 C  CA  . PHE   A 1 360 ? 52.346 18.360  -33.505 1.00 33.98  ?  516 PHE   A CA  1 
ATOM   2547 C  C   . PHE   A 1 360 ? 52.038 19.456  -34.523 1.00 37.80  ?  516 PHE   A C   1 
ATOM   2548 O  O   . PHE   A 1 360 ? 51.544 20.528  -34.149 1.00 41.66  ?  516 PHE   A O   1 
ATOM   2549 C  CB  . PHE   A 1 360 ? 51.763 18.710  -32.135 1.00 29.93  ?  516 PHE   A CB  1 
ATOM   2550 C  CG  . PHE   A 1 360 ? 52.036 17.666  -31.093 1.00 31.90  ?  516 PHE   A CG  1 
ATOM   2551 C  CD1 . PHE   A 1 360 ? 51.265 16.517  -31.028 1.00 24.87  ?  516 PHE   A CD1 1 
ATOM   2552 C  CD2 . PHE   A 1 360 ? 53.089 17.811  -30.205 1.00 31.79  ?  516 PHE   A CD2 1 
ATOM   2553 C  CE1 . PHE   A 1 360 ? 51.524 15.544  -30.083 1.00 25.46  ?  516 PHE   A CE1 1 
ATOM   2554 C  CE2 . PHE   A 1 360 ? 53.353 16.840  -29.257 1.00 31.79  ?  516 PHE   A CE2 1 
ATOM   2555 C  CZ  . PHE   A 1 360 ? 52.570 15.707  -29.197 1.00 26.24  ?  516 PHE   A CZ  1 
ATOM   2556 N  N   . PRO   A 1 361 ? 52.296 19.222  -35.813 1.00 41.18  ?  517 PRO   A N   1 
ATOM   2557 C  CA  . PRO   A 1 361 ? 51.942 20.232  -36.824 1.00 45.36  ?  517 PRO   A CA  1 
ATOM   2558 C  C   . PRO   A 1 361 ? 50.447 20.445  -36.980 1.00 40.80  ?  517 PRO   A C   1 
ATOM   2559 O  O   . PRO   A 1 361 ? 50.039 21.488  -37.505 1.00 43.06  ?  517 PRO   A O   1 
ATOM   2560 C  CB  . PRO   A 1 361 ? 52.562 19.672  -38.112 1.00 41.14  ?  517 PRO   A CB  1 
ATOM   2561 C  CG  . PRO   A 1 361 ? 52.664 18.201  -37.872 1.00 38.29  ?  517 PRO   A CG  1 
ATOM   2562 C  CD  . PRO   A 1 361 ? 52.969 18.055  -36.411 1.00 38.01  ?  517 PRO   A CD  1 
ATOM   2563 N  N   . VAL   A 1 362 ? 49.616 19.495  -36.543 1.00 41.82  ?  518 VAL   A N   1 
ATOM   2564 C  CA  . VAL   A 1 362 ? 48.175 19.662  -36.678 1.00 53.98  ?  518 VAL   A CA  1 
ATOM   2565 C  C   . VAL   A 1 362 ? 47.644 20.723  -35.723 1.00 43.40  ?  518 VAL   A C   1 
ATOM   2566 O  O   . VAL   A 1 362 ? 46.520 21.207  -35.900 1.00 51.73  ?  518 VAL   A O   1 
ATOM   2567 C  CB  . VAL   A 1 362 ? 47.455 18.318  -36.458 1.00 44.60  ?  518 VAL   A CB  1 
ATOM   2568 C  CG1 . VAL   A 1 362 ? 47.223 18.073  -34.975 1.00 46.12  ?  518 VAL   A CG1 1 
ATOM   2569 C  CG2 . VAL   A 1 362 ? 46.145 18.281  -37.229 1.00 51.13  ?  518 VAL   A CG2 1 
ATOM   2570 N  N   . PHE   A 1 363 ? 48.424 21.101  -34.708 1.00 40.56  ?  519 PHE   A N   1 
ATOM   2571 C  CA  . PHE   A 1 363 ? 47.979 22.149  -33.796 1.00 39.55  ?  519 PHE   A CA  1 
ATOM   2572 C  C   . PHE   A 1 363 ? 47.919 23.499  -34.499 1.00 63.47  ?  519 PHE   A C   1 
ATOM   2573 O  O   . PHE   A 1 363 ? 47.018 24.304  -34.233 1.00 70.19  ?  519 PHE   A O   1 
ATOM   2574 C  CB  . PHE   A 1 363 ? 48.902 22.217  -32.581 1.00 36.20  ?  519 PHE   A CB  1 
ATOM   2575 C  CG  . PHE   A 1 363 ? 48.566 21.222  -31.508 1.00 36.95  ?  519 PHE   A CG  1 
ATOM   2576 C  CD1 . PHE   A 1 363 ? 47.327 20.603  -31.478 1.00 34.55  ?  519 PHE   A CD1 1 
ATOM   2577 C  CD2 . PHE   A 1 363 ? 49.488 20.912  -30.522 1.00 33.95  ?  519 PHE   A CD2 1 
ATOM   2578 C  CE1 . PHE   A 1 363 ? 47.016 19.688  -30.489 1.00 28.28  ?  519 PHE   A CE1 1 
ATOM   2579 C  CE2 . PHE   A 1 363 ? 49.183 19.999  -29.530 1.00 30.00  ?  519 PHE   A CE2 1 
ATOM   2580 C  CZ  . PHE   A 1 363 ? 47.946 19.387  -29.513 1.00 28.17  ?  519 PHE   A CZ  1 
ATOM   2581 N  N   . ASP   A 1 364 ? 48.865 23.758  -35.400 1.00 53.57  ?  520 ASP   A N   1 
ATOM   2582 C  CA  . ASP   A 1 364 ? 48.912 25.000  -36.167 1.00 56.07  ?  520 ASP   A CA  1 
ATOM   2583 C  C   . ASP   A 1 364 ? 47.593 25.279  -36.879 1.00 55.39  ?  520 ASP   A C   1 
ATOM   2584 O  O   . ASP   A 1 364 ? 47.558 25.444  -38.098 1.00 72.30  ?  520 ASP   A O   1 
ATOM   2585 C  CB  . ASP   A 1 364 ? 50.048 24.947  -37.192 1.00 41.47  ?  520 ASP   A CB  1 
ATOM   2586 C  CG  . ASP   A 1 364 ? 51.398 24.697  -36.554 1.00 59.28  ?  520 ASP   A CG  1 
ATOM   2587 O  OD1 . ASP   A 1 364 ? 51.510 24.862  -35.322 1.00 65.10  ?  520 ASP   A OD1 1 
ATOM   2588 O  OD2 . ASP   A 1 364 ? 52.343 24.323  -37.279 1.00 63.25  -1 520 ASP   A OD2 1 
ATOM   2589 N  N   . GLY   B 1 5   ? 57.555 13.324  27.108  1.00 85.10  ?  161 GLY   B N   1 
ATOM   2590 C  CA  . GLY   B 1 5   ? 56.361 12.870  27.797  1.00 64.98  ?  161 GLY   B CA  1 
ATOM   2591 C  C   . GLY   B 1 5   ? 55.192 12.600  26.869  1.00 75.10  ?  161 GLY   B C   1 
ATOM   2592 O  O   . GLY   B 1 5   ? 54.069 12.386  27.324  1.00 64.75  ?  161 GLY   B O   1 
ATOM   2593 N  N   . ALA   B 1 6   ? 55.457 12.609  25.558  1.00 61.66  ?  162 ALA   B N   1 
ATOM   2594 C  CA  . ALA   B 1 6   ? 54.405 12.319  24.588  1.00 54.32  ?  162 ALA   B CA  1 
ATOM   2595 C  C   . ALA   B 1 6   ? 53.833 10.920  24.780  1.00 59.02  ?  162 ALA   B C   1 
ATOM   2596 O  O   . ALA   B 1 6   ? 52.681 10.656  24.403  1.00 54.10  ?  162 ALA   B O   1 
ATOM   2597 C  CB  . ALA   B 1 6   ? 54.942 12.483  23.166  1.00 49.00  ?  162 ALA   B CB  1 
ATOM   2598 N  N   . SER   B 1 7   ? 54.621 10.011  25.358  1.00 48.18  ?  163 SER   B N   1 
ATOM   2599 C  CA  . SER   B 1 7   ? 54.129 8.664   25.617  1.00 52.69  ?  163 SER   B CA  1 
ATOM   2600 C  C   . SER   B 1 7   ? 52.947 8.684   26.577  1.00 50.04  ?  163 SER   B C   1 
ATOM   2601 O  O   . SER   B 1 7   ? 52.008 7.893   26.435  1.00 46.86  ?  163 SER   B O   1 
ATOM   2602 C  CB  . SER   B 1 7   ? 55.261 7.795   26.160  1.00 61.00  ?  163 SER   B CB  1 
ATOM   2603 O  OG  . SER   B 1 7   ? 55.771 8.333   27.366  1.00 66.87  ?  163 SER   B OG  1 
ATOM   2604 N  N   . LYS   B 1 8   ? 52.960 9.598   27.554  1.00 50.03  ?  164 LYS   B N   1 
ATOM   2605 C  CA  . LYS   B 1 8   ? 51.809 9.721   28.443  1.00 40.19  ?  164 LYS   B CA  1 
ATOM   2606 C  C   . LYS   B 1 8   ? 50.587 10.242  27.694  1.00 40.29  ?  164 LYS   B C   1 
ATOM   2607 O  O   . LYS   B 1 8   ? 49.460 9.800   27.951  1.00 42.13  ?  164 LYS   B O   1 
ATOM   2608 C  CB  . LYS   B 1 8   ? 52.142 10.627  29.629  1.00 47.94  ?  164 LYS   B CB  1 
ATOM   2609 C  CG  . LYS   B 1 8   ? 50.902 11.122  30.361  1.00 57.98  ?  164 LYS   B CG  1 
ATOM   2610 C  CD  . LYS   B 1 8   ? 51.230 11.878  31.632  1.00 51.08  ?  164 LYS   B CD  1 
ATOM   2611 C  CE  . LYS   B 1 8   ? 50.205 11.563  32.708  1.00 49.93  ?  164 LYS   B CE  1 
ATOM   2612 N  NZ  . LYS   B 1 8   ? 49.023 12.458  32.605  1.00 63.97  ?  164 LYS   B NZ  1 
ATOM   2613 N  N   . LEU   B 1 9   ? 50.789 11.183  26.767  1.00 42.79  ?  165 LEU   B N   1 
ATOM   2614 C  CA  . LEU   B 1 9   ? 49.684 11.654  25.935  1.00 42.06  ?  165 LEU   B CA  1 
ATOM   2615 C  C   . LEU   B 1 9   ? 49.042 10.496  25.177  1.00 41.07  ?  165 LEU   B C   1 
ATOM   2616 O  O   . LEU   B 1 9   ? 47.809 10.361  25.146  1.00 29.17  ?  165 LEU   B O   1 
ATOM   2617 C  CB  . LEU   B 1 9   ? 50.181 12.728  24.963  1.00 31.96  ?  165 LEU   B CB  1 
ATOM   2618 C  CG  . LEU   B 1 9   ? 50.685 14.061  25.513  1.00 33.97  ?  165 LEU   B CG  1 
ATOM   2619 C  CD1 . LEU   B 1 9   ? 51.030 14.996  24.365  1.00 28.28  ?  165 LEU   B CD1 1 
ATOM   2620 C  CD2 . LEU   B 1 9   ? 49.639 14.692  26.416  1.00 25.84  ?  165 LEU   B CD2 1 
ATOM   2621 N  N   . ARG   B 1 10  ? 49.877 9.642   24.569  1.00 42.08  ?  166 ARG   B N   1 
ATOM   2622 C  CA  . ARG   B 1 10  ? 49.356 8.513   23.804  1.00 40.84  ?  166 ARG   B CA  1 
ATOM   2623 C  C   . ARG   B 1 10  ? 48.692 7.482   24.714  1.00 38.00  ?  166 ARG   B C   1 
ATOM   2624 O  O   . ARG   B 1 10  ? 47.725 6.821   24.313  1.00 46.80  ?  166 ARG   B O   1 
ATOM   2625 C  CB  . ARG   B 1 10  ? 50.464 7.861   22.979  1.00 44.15  ?  166 ARG   B CB  1 
ATOM   2626 C  CG  . ARG   B 1 10  ? 50.862 8.635   21.734  1.00 52.42  ?  166 ARG   B CG  1 
ATOM   2627 C  CD  . ARG   B 1 10  ? 49.769 8.574   20.669  1.00 65.22  ?  166 ARG   B CD  1 
ATOM   2628 N  NE  . ARG   B 1 10  ? 48.788 7.515   20.896  1.00 66.29  ?  166 ARG   B NE  1 
ATOM   2629 C  CZ  . ARG   B 1 10  ? 47.580 7.492   20.345  1.00 71.74  ?  166 ARG   B CZ  1 
ATOM   2630 N  NH1 . ARG   B 1 10  ? 47.177 8.448   19.521  1.00 61.53  ?  166 ARG   B NH1 1 
ATOM   2631 N  NH2 . ARG   B 1 10  ? 46.757 6.485   20.622  1.00 60.64  ?  166 ARG   B NH2 1 
ATOM   2632 N  N   . ALA   B 1 11  ? 49.185 7.341   25.948  1.00 33.39  ?  167 ALA   B N   1 
ATOM   2633 C  CA  . ALA   B 1 11  ? 48.516 6.484   26.927  1.00 43.31  ?  167 ALA   B CA  1 
ATOM   2634 C  C   . ALA   B 1 11  ? 47.122 7.005   27.243  1.00 41.87  ?  167 ALA   B C   1 
ATOM   2635 O  O   . ALA   B 1 11  ? 46.154 6.237   27.330  1.00 42.21  ?  167 ALA   B O   1 
ATOM   2636 C  CB  . ALA   B 1 11  ? 49.351 6.398   28.207  1.00 34.26  ?  167 ALA   B CB  1 
ATOM   2637 N  N   . VAL   B 1 12  ? 47.015 8.320   27.442  1.00 43.75  ?  168 VAL   B N   1 
ATOM   2638 C  CA  . VAL   B 1 12  ? 45.721 8.948   27.686  1.00 41.10  ?  168 VAL   B CA  1 
ATOM   2639 C  C   . VAL   B 1 12  ? 44.778 8.690   26.520  1.00 33.93  ?  168 VAL   B C   1 
ATOM   2640 O  O   . VAL   B 1 12  ? 43.604 8.349   26.713  1.00 33.62  ?  168 VAL   B O   1 
ATOM   2641 C  CB  . VAL   B 1 12  ? 45.907 10.455  27.942  1.00 30.63  ?  168 VAL   B CB  1 
ATOM   2642 C  CG1 . VAL   B 1 12  ? 44.572 11.173  27.901  1.00 29.05  ?  168 VAL   B CG1 1 
ATOM   2643 C  CG2 . VAL   B 1 12  ? 46.612 10.689  29.271  1.00 34.42  ?  168 VAL   B CG2 1 
ATOM   2644 N  N   . LEU   B 1 13  ? 45.277 8.840   25.291  1.00 26.26  ?  169 LEU   B N   1 
ATOM   2645 C  CA  . LEU   B 1 13  ? 44.425 8.614   24.124  1.00 37.91  ?  169 LEU   B CA  1 
ATOM   2646 C  C   . LEU   B 1 13  ? 43.981 7.158   24.035  1.00 41.48  ?  169 LEU   B C   1 
ATOM   2647 O  O   . LEU   B 1 13  ? 42.825 6.873   23.694  1.00 49.54  ?  169 LEU   B O   1 
ATOM   2648 C  CB  . LEU   B 1 13  ? 45.153 9.030   22.850  1.00 31.65  ?  169 LEU   B CB  1 
ATOM   2649 C  CG  . LEU   B 1 13  ? 45.399 10.534  22.746  1.00 37.17  ?  169 LEU   B CG  1 
ATOM   2650 C  CD1 . LEU   B 1 13  ? 46.474 10.840  21.719  1.00 37.16  ?  169 LEU   B CD1 1 
ATOM   2651 C  CD2 . LEU   B 1 13  ? 44.109 11.266  22.415  1.00 36.56  ?  169 LEU   B CD2 1 
ATOM   2652 N  N   . GLU   B 1 14  ? 44.890 6.227   24.333  1.00 35.26  ?  170 GLU   B N   1 
ATOM   2653 C  CA  . GLU   B 1 14  ? 44.542 4.810   24.348  1.00 38.42  ?  170 GLU   B CA  1 
ATOM   2654 C  C   . GLU   B 1 14  ? 43.411 4.535   25.330  1.00 45.36  ?  170 GLU   B C   1 
ATOM   2655 O  O   . GLU   B 1 14  ? 42.426 3.869   24.990  1.00 51.52  ?  170 GLU   B O   1 
ATOM   2656 C  CB  . GLU   B 1 14  ? 45.771 3.975   24.703  1.00 50.97  ?  170 GLU   B CB  1 
ATOM   2657 N  N   . LYS   B 1 15  ? 43.539 5.042   26.560  1.00 41.46  ?  171 LYS   B N   1 
ATOM   2658 C  CA  . LYS   B 1 15  ? 42.491 4.829   27.556  1.00 47.31  ?  171 LYS   B CA  1 
ATOM   2659 C  C   . LYS   B 1 15  ? 41.177 5.473   27.121  1.00 48.02  ?  171 LYS   B C   1 
ATOM   2660 O  O   . LYS   B 1 15  ? 40.097 4.916   27.356  1.00 52.78  ?  171 LYS   B O   1 
ATOM   2661 C  CB  . LYS   B 1 15  ? 42.931 5.376   28.913  1.00 38.14  ?  171 LYS   B CB  1 
ATOM   2662 N  N   . LEU   B 1 16  ? 41.250 6.650   26.483  1.00 49.76  ?  172 LEU   B N   1 
ATOM   2663 C  CA  . LEU   B 1 16  ? 40.040 7.316   26.007  1.00 41.29  ?  172 LEU   B CA  1 
ATOM   2664 C  C   . LEU   B 1 16  ? 39.358 6.506   24.915  1.00 56.14  ?  172 LEU   B C   1 
ATOM   2665 O  O   . LEU   B 1 16  ? 38.126 6.540   24.794  1.00 60.43  ?  172 LEU   B O   1 
ATOM   2666 C  CB  . LEU   B 1 16  ? 40.366 8.726   25.502  1.00 41.28  ?  172 LEU   B CB  1 
ATOM   2667 C  CG  . LEU   B 1 16  ? 40.705 9.742   26.595  1.00 38.55  ?  172 LEU   B CG  1 
ATOM   2668 C  CD1 . LEU   B 1 16  ? 41.017 11.105  25.993  1.00 29.21  ?  172 LEU   B CD1 1 
ATOM   2669 C  CD2 . LEU   B 1 16  ? 39.571 9.839   27.602  1.00 40.23  ?  172 LEU   B CD2 1 
ATOM   2670 N  N   . LYS   B 1 17  ? 40.132 5.790   24.100  1.00 55.41  ?  173 LYS   B N   1 
ATOM   2671 C  CA  . LYS   B 1 17  ? 39.522 4.937   23.084  1.00 51.25  ?  173 LYS   B CA  1 
ATOM   2672 C  C   . LYS   B 1 17  ? 38.741 3.786   23.715  1.00 57.81  ?  173 LYS   B C   1 
ATOM   2673 O  O   . LYS   B 1 17  ? 37.552 3.593   23.427  1.00 48.86  ?  173 LYS   B O   1 
ATOM   2674 C  CB  . LYS   B 1 17  ? 40.586 4.397   22.129  1.00 46.27  ?  173 LYS   B CB  1 
ATOM   2675 C  CG  . LYS   B 1 17  ? 40.032 4.140   20.737  1.00 56.99  ?  173 LYS   B CG  1 
ATOM   2676 C  CD  . LYS   B 1 17  ? 41.108 3.670   19.778  1.00 61.11  ?  173 LYS   B CD  1 
ATOM   2677 C  CE  . LYS   B 1 17  ? 42.288 4.627   19.744  1.00 55.57  ?  173 LYS   B CE  1 
ATOM   2678 N  NZ  . LYS   B 1 17  ? 43.194 4.333   18.597  1.00 57.56  ?  173 LYS   B NZ  1 
ATOM   2679 N  N   . LEU   B 1 18  ? 39.403 3.010   24.574  1.00 57.57  ?  174 LEU   B N   1 
ATOM   2680 C  CA  . LEU   B 1 18  ? 38.855 1.776   25.156  1.00 67.45  ?  174 LEU   B CA  1 
ATOM   2681 C  C   . LEU   B 1 18  ? 37.448 1.908   25.741  1.00 71.42  ?  174 LEU   B C   1 
ATOM   2682 O  O   . LEU   B 1 18  ? 36.526 1.196   25.329  1.00 73.13  ?  174 LEU   B O   1 
ATOM   2683 C  CB  . LEU   B 1 18  ? 39.787 1.244   26.250  1.00 63.18  ?  174 LEU   B CB  1 
ATOM   2684 C  CG  . LEU   B 1 18  ? 40.883 0.237   25.906  1.00 67.69  ?  174 LEU   B CG  1 
ATOM   2685 C  CD1 . LEU   B 1 18  ? 41.522 0.545   24.554  1.00 68.28  ?  174 LEU   B CD1 1 
ATOM   2686 C  CD2 . LEU   B 1 18  ? 41.924 0.227   27.012  1.00 75.28  ?  174 LEU   B CD2 1 
ATOM   2687 N  N   . ASP   B 1 22  ? 31.228 -0.246  23.744  1.00 72.77  ?  178 ASP   B N   1 
ATOM   2688 C  CA  . ASP   B 1 22  ? 29.985 0.043   24.439  1.00 77.75  ?  178 ASP   B CA  1 
ATOM   2689 C  C   . ASP   B 1 22  ? 29.097 1.033   23.683  1.00 75.51  ?  178 ASP   B C   1 
ATOM   2690 O  O   . ASP   B 1 22  ? 27.886 1.040   23.848  1.00 68.30  ?  178 ASP   B O   1 
ATOM   2691 C  CB  . ASP   B 1 22  ? 30.270 0.611   25.836  1.00 69.08  ?  178 ASP   B CB  1 
ATOM   2692 N  N   . ILE   B 1 23  ? 29.730 1.852   22.852  1.00 76.21  ?  179 ILE   B N   1 
ATOM   2693 C  CA  . ILE   B 1 23  ? 29.035 2.866   22.076  1.00 66.77  ?  179 ILE   B CA  1 
ATOM   2694 C  C   . ILE   B 1 23  ? 28.713 2.335   20.684  1.00 72.86  ?  179 ILE   B C   1 
ATOM   2695 O  O   . ILE   B 1 23  ? 27.559 2.326   20.269  1.00 89.10  ?  179 ILE   B O   1 
ATOM   2696 C  CB  . ILE   B 1 23  ? 29.848 4.173   22.004  1.00 67.98  ?  179 ILE   B CB  1 
ATOM   2697 N  N   . THR   B 1 25  ? 26.353 -0.124  21.279  1.00 67.80  ?  181 THR   B N   1 
ATOM   2698 C  CA  . THR   B 1 25  ? 25.228 -0.742  21.974  1.00 60.30  ?  181 THR   B CA  1 
ATOM   2699 C  C   . THR   B 1 25  ? 24.348 0.312   22.640  1.00 85.61  ?  181 THR   B C   1 
ATOM   2700 O  O   . THR   B 1 25  ? 23.134 0.342   22.423  1.00 92.52  ?  181 THR   B O   1 
ATOM   2701 C  CB  . THR   B 1 25  ? 25.709 -1.753  23.033  1.00 89.86  ?  181 THR   B CB  1 
ATOM   2702 O  OG1 . THR   B 1 25  ? 26.369 -2.847  22.385  1.00 88.08  ?  181 THR   B OG1 1 
ATOM   2703 C  CG2 . THR   B 1 25  ? 24.539 -2.277  23.853  1.00 80.54  ?  181 THR   B CG2 1 
ATOM   2704 N  N   . ALA   B 1 26  ? 24.974 1.170   23.452  1.00 86.02  ?  182 ALA   B N   1 
ATOM   2705 C  CA  . ALA   B 1 26  ? 24.252 2.258   24.105  1.00 82.22  ?  182 ALA   B CA  1 
ATOM   2706 C  C   . ALA   B 1 26  ? 23.447 3.067   23.097  1.00 61.61  ?  182 ALA   B C   1 
ATOM   2707 O  O   . ALA   B 1 26  ? 22.252 3.328   23.296  1.00 67.42  ?  182 ALA   B O   1 
ATOM   2708 C  CB  . ALA   B 1 26  ? 25.237 3.161   24.850  1.00 67.86  ?  182 ALA   B CB  1 
ATOM   2709 N  N   . ALA   B 1 27  ? 24.093 3.452   21.990  1.00 55.29  ?  183 ALA   B N   1 
ATOM   2710 C  CA  . ALA   B 1 27  ? 23.418 4.227   20.953  1.00 67.90  ?  183 ALA   B CA  1 
ATOM   2711 C  C   . ALA   B 1 27  ? 22.118 3.565   20.524  1.00 58.60  ?  183 ALA   B C   1 
ATOM   2712 O  O   . ALA   B 1 27  ? 21.122 4.251   20.262  1.00 68.33  ?  183 ALA   B O   1 
ATOM   2713 C  CB  . ALA   B 1 27  ? 24.344 4.416   19.748  1.00 56.55  ?  183 ALA   B CB  1 
ATOM   2714 N  N   . GLY   B 1 28  ? 22.110 2.230   20.459  1.00 71.90  ?  184 GLY   B N   1 
ATOM   2715 C  CA  . GLY   B 1 28  ? 20.918 1.469   20.137  1.00 61.70  ?  184 GLY   B CA  1 
ATOM   2716 C  C   . GLY   B 1 28  ? 19.733 1.960   20.931  1.00 69.22  ?  184 GLY   B C   1 
ATOM   2717 O  O   . GLY   B 1 28  ? 18.750 2.459   20.371  1.00 72.80  ?  184 GLY   B O   1 
ATOM   2718 N  N   . MET   B 1 29  ? 19.865 1.872   22.253  1.00 72.16  ?  185 MET   B N   1 
ATOM   2719 C  CA  . MET   B 1 29  ? 18.852 2.388   23.162  1.00 73.39  ?  185 MET   B CA  1 
ATOM   2720 C  C   . MET   B 1 29  ? 18.469 3.823   22.804  1.00 67.68  ?  185 MET   B C   1 
ATOM   2721 O  O   . MET   B 1 29  ? 17.287 4.136   22.603  1.00 59.11  ?  185 MET   B O   1 
ATOM   2722 C  CB  . MET   B 1 29  ? 19.407 2.270   24.578  1.00 84.14  ?  185 MET   B CB  1 
ATOM   2723 C  CG  . MET   B 1 29  ? 20.229 0.989   24.749  1.00 84.36  ?  185 MET   B CG  1 
ATOM   2724 S  SD  . MET   B 1 29  ? 20.602 0.623   26.463  1.00 100.03 ?  185 MET   B SD  1 
ATOM   2725 C  CE  . MET   B 1 29  ? 19.163 1.246   27.271  1.00 74.39  ?  185 MET   B CE  1 
ATOM   2726 N  N   . VAL   B 1 30  ? 19.476 4.694   22.661  1.00 68.33  ?  186 VAL   B N   1 
ATOM   2727 C  CA  . VAL   B 1 30  ? 19.239 6.078   22.251  1.00 57.22  ?  186 VAL   B CA  1 
ATOM   2728 C  C   . VAL   B 1 30  ? 18.368 6.116   21.008  1.00 57.92  ?  186 VAL   B C   1 
ATOM   2729 O  O   . VAL   B 1 30  ? 17.291 6.731   20.994  1.00 52.41  ?  186 VAL   B O   1 
ATOM   2730 C  CB  . VAL   B 1 30  ? 20.578 6.801   22.014  1.00 59.14  ?  186 VAL   B CB  1 
ATOM   2731 C  CG1 . VAL   B 1 30  ? 20.337 8.195   21.463  1.00 57.61  ?  186 VAL   B CG1 1 
ATOM   2732 C  CG2 . VAL   B 1 30  ? 21.385 6.868   23.300  1.00 60.82  ?  186 VAL   B CG2 1 
ATOM   2733 N  N   . LYS   B 1 31  ? 18.810 5.417   19.955  1.00 49.89  ?  187 LYS   B N   1 
ATOM   2734 C  CA  . LYS   B 1 31  ? 18.071 5.408   18.701  1.00 62.25  ?  187 LYS   B CA  1 
ATOM   2735 C  C   . LYS   B 1 31  ? 16.621 5.031   18.936  1.00 63.71  ?  187 LYS   B C   1 
ATOM   2736 O  O   . LYS   B 1 31  ? 15.708 5.706   18.445  1.00 64.06  ?  187 LYS   B O   1 
ATOM   2737 C  CB  . LYS   B 1 31  ? 18.725 4.441   17.712  1.00 52.92  ?  187 LYS   B CB  1 
ATOM   2738 N  N   . GLY   B 1 32  ? 16.398 3.990   19.744  1.00 59.81  ?  188 GLY   B N   1 
ATOM   2739 C  CA  . GLY   B 1 32  ? 15.041 3.525   19.979  1.00 47.23  ?  188 GLY   B CA  1 
ATOM   2740 C  C   . GLY   B 1 32  ? 14.137 4.628   20.478  1.00 61.89  ?  188 GLY   B C   1 
ATOM   2741 O  O   . GLY   B 1 32  ? 13.007 4.785   20.010  1.00 62.97  ?  188 GLY   B O   1 
ATOM   2742 N  N   . VAL   B 1 33  ? 14.632 5.431   21.421  1.00 64.06  ?  189 VAL   B N   1 
ATOM   2743 C  CA  . VAL   B 1 33  ? 13.848 6.567   21.894  1.00 62.69  ?  189 VAL   B CA  1 
ATOM   2744 C  C   . VAL   B 1 33  ? 13.709 7.596   20.783  1.00 51.46  ?  189 VAL   B C   1 
ATOM   2745 O  O   . VAL   B 1 33  ? 12.596 8.023   20.441  1.00 63.56  ?  189 VAL   B O   1 
ATOM   2746 C  CB  . VAL   B 1 33  ? 14.486 7.181   23.155  1.00 59.23  ?  189 VAL   B CB  1 
ATOM   2747 C  CG1 . VAL   B 1 33  ? 13.724 8.436   23.585  1.00 66.84  ?  189 VAL   B CG1 1 
ATOM   2748 C  CG2 . VAL   B 1 33  ? 14.528 6.161   24.279  1.00 69.86  ?  189 VAL   B CG2 1 
ATOM   2749 N  N   . VAL   B 1 34  ? 14.835 7.962   20.166  1.00 55.39  ?  190 VAL   B N   1 
ATOM   2750 C  CA  . VAL   B 1 34  ? 14.854 9.080   19.224  1.00 57.40  ?  190 VAL   B CA  1 
ATOM   2751 C  C   . VAL   B 1 34  ? 13.806 8.892   18.131  1.00 59.40  ?  190 VAL   B C   1 
ATOM   2752 O  O   . VAL   B 1 34  ? 12.892 9.713   17.983  1.00 61.33  ?  190 VAL   B O   1 
ATOM   2753 C  CB  . VAL   B 1 34  ? 16.257 9.255   18.624  1.00 61.87  ?  190 VAL   B CB  1 
ATOM   2754 C  CG1 . VAL   B 1 34  ? 16.209 10.281  17.505  1.00 59.52  ?  190 VAL   B CG1 1 
ATOM   2755 C  CG2 . VAL   B 1 34  ? 17.226 9.691   19.693  1.00 63.78  ?  190 VAL   B CG2 1 
ATOM   2756 N  N   . ASP   B 1 35  ? 13.930 7.803   17.356  1.00 51.90  ?  191 ASP   B N   1 
ATOM   2757 C  CA  . ASP   B 1 35  ? 12.944 7.439   16.341  1.00 61.46  ?  191 ASP   B CA  1 
ATOM   2758 C  C   . ASP   B 1 35  ? 11.535 7.668   16.850  1.00 69.15  ?  191 ASP   B C   1 
ATOM   2759 O  O   . ASP   B 1 35  ? 10.747 8.395   16.229  1.00 82.29  ?  191 ASP   B O   1 
ATOM   2760 C  CB  . ASP   B 1 35  ? 13.096 5.971   15.941  1.00 68.03  ?  191 ASP   B CB  1 
ATOM   2761 N  N   . HIS   B 1 36  ? 11.202 7.056   17.992  1.00 61.51  ?  192 HIS   B N   1 
ATOM   2762 C  CA  . HIS   B 1 36  ? 9.833  7.147   18.468  1.00 67.00  ?  192 HIS   B CA  1 
ATOM   2763 C  C   . HIS   B 1 36  ? 9.425  8.598   18.638  1.00 70.32  ?  192 HIS   B C   1 
ATOM   2764 O  O   . HIS   B 1 36  ? 8.404  9.032   18.092  1.00 63.58  ?  192 HIS   B O   1 
ATOM   2765 C  CB  . HIS   B 1 36  ? 9.676  6.369   19.762  1.00 72.05  ?  192 HIS   B CB  1 
ATOM   2766 C  CG  . HIS   B 1 36  ? 9.636  4.885   19.569  1.00 73.96  ?  192 HIS   B CG  1 
ATOM   2767 N  ND1 . HIS   B 1 36  ? 10.656 4.182   18.970  1.00 68.03  ?  192 HIS   B ND1 1 
ATOM   2768 C  CD2 . HIS   B 1 36  ? 8.676  3.976   19.869  1.00 67.41  ?  192 HIS   B CD2 1 
ATOM   2769 C  CE1 . HIS   B 1 36  ? 10.337 2.900   18.930  1.00 71.10  ?  192 HIS   B CE1 1 
ATOM   2770 N  NE2 . HIS   B 1 36  ? 9.140  2.748   19.469  1.00 67.62  ?  192 HIS   B NE2 1 
ATOM   2771 N  N   . LEU   B 1 37  ? 10.254 9.384   19.327  1.00 62.87  ?  193 LEU   B N   1 
ATOM   2772 C  CA  . LEU   B 1 37  ? 9.967  10.806  19.458  1.00 55.85  ?  193 LEU   B CA  1 
ATOM   2773 C  C   . LEU   B 1 37  ? 9.721  11.425  18.092  1.00 48.57  ?  193 LEU   B C   1 
ATOM   2774 O  O   . LEU   B 1 37  ? 8.687  12.065  17.869  1.00 59.24  ?  193 LEU   B O   1 
ATOM   2775 C  CB  . LEU   B 1 37  ? 11.111 11.515  20.188  1.00 53.83  ?  193 LEU   B CB  1 
ATOM   2776 C  CG  . LEU   B 1 37  ? 11.383 11.015  21.604  1.00 46.37  ?  193 LEU   B CG  1 
ATOM   2777 C  CD1 . LEU   B 1 37  ? 12.568 11.738  22.226  1.00 48.47  ?  193 LEU   B CD1 1 
ATOM   2778 C  CD2 . LEU   B 1 37  ? 10.136 11.178  22.452  1.00 48.60  ?  193 LEU   B CD2 1 
ATOM   2779 N  N   . LEU   B 1 38  ? 10.624 11.174  17.138  1.00 47.47  ?  194 LEU   B N   1 
ATOM   2780 C  CA  . LEU   B 1 38  ? 10.463 11.759  15.812  1.00 51.67  ?  194 LEU   B CA  1 
ATOM   2781 C  C   . LEU   B 1 38  ? 9.157  11.320  15.167  1.00 60.69  ?  194 LEU   B C   1 
ATOM   2782 O  O   . LEU   B 1 38  ? 8.482  12.127  14.522  1.00 58.23  ?  194 LEU   B O   1 
ATOM   2783 C  CB  . LEU   B 1 38  ? 11.655 11.410  14.926  1.00 43.29  ?  194 LEU   B CB  1 
ATOM   2784 C  CG  . LEU   B 1 38  ? 12.945 12.147  15.289  1.00 52.43  ?  194 LEU   B CG  1 
ATOM   2785 C  CD1 . LEU   B 1 38  ? 14.128 11.575  14.528  1.00 43.16  ?  194 LEU   B CD1 1 
ATOM   2786 C  CD2 . LEU   B 1 38  ? 12.787 13.636  15.013  1.00 49.84  ?  194 LEU   B CD2 1 
ATOM   2787 N  N   . LEU   B 1 39  ? 8.766  10.057  15.350  1.00 66.95  ?  195 LEU   B N   1 
ATOM   2788 C  CA  . LEU   B 1 39  ? 7.466  9.632   14.844  1.00 63.54  ?  195 LEU   B CA  1 
ATOM   2789 C  C   . LEU   B 1 39  ? 6.356  10.503  15.420  1.00 57.59  ?  195 LEU   B C   1 
ATOM   2790 O  O   . LEU   B 1 39  ? 5.583  11.123  14.674  1.00 61.58  ?  195 LEU   B O   1 
ATOM   2791 C  CB  . LEU   B 1 39  ? 7.233  8.155   15.164  1.00 67.86  ?  195 LEU   B CB  1 
ATOM   2792 C  CG  . LEU   B 1 39  ? 7.631  7.191   14.038  1.00 61.38  ?  195 LEU   B CG  1 
ATOM   2793 C  CD1 . LEU   B 1 39  ? 9.119  6.860   14.043  1.00 65.27  ?  195 LEU   B CD1 1 
ATOM   2794 C  CD2 . LEU   B 1 39  ? 6.788  5.933   14.101  1.00 69.98  ?  195 LEU   B CD2 1 
ATOM   2795 N  N   . ARG   B 1 40  ? 6.309  10.619  16.749  1.00 62.81  ?  196 ARG   B N   1 
ATOM   2796 C  CA  . ARG   B 1 40  ? 5.224  11.355  17.387  1.00 54.91  ?  196 ARG   B CA  1 
ATOM   2797 C  C   . ARG   B 1 40  ? 5.215  12.809  16.935  1.00 53.97  ?  196 ARG   B C   1 
ATOM   2798 O  O   . ARG   B 1 40  ? 4.176  13.338  16.521  1.00 67.07  ?  196 ARG   B O   1 
ATOM   2799 C  CB  . ARG   B 1 40  ? 5.353  11.253  18.904  1.00 59.04  ?  196 ARG   B CB  1 
ATOM   2800 C  CG  . ARG   B 1 40  ? 4.385  12.135  19.656  1.00 69.31  ?  196 ARG   B CG  1 
ATOM   2801 C  CD  . ARG   B 1 40  ? 2.969  11.597  19.581  1.00 74.55  ?  196 ARG   B CD  1 
ATOM   2802 N  NE  . ARG   B 1 40  ? 2.435  11.300  20.906  1.00 81.37  ?  196 ARG   B NE  1 
ATOM   2803 C  CZ  . ARG   B 1 40  ? 1.789  12.175  21.665  1.00 74.53  ?  196 ARG   B CZ  1 
ATOM   2804 N  NH1 . ARG   B 1 40  ? 1.571  13.415  21.258  1.00 75.97  ?  196 ARG   B NH1 1 
ATOM   2805 N  NH2 . ARG   B 1 40  ? 1.352  11.797  22.862  1.00 84.41  ?  196 ARG   B NH2 1 
ATOM   2806 N  N   . LEU   B 1 41  ? 6.379  13.461  16.983  1.00 51.56  ?  197 LEU   B N   1 
ATOM   2807 C  CA  . LEU   B 1 41  ? 6.468  14.856  16.568  1.00 57.72  ?  197 LEU   B CA  1 
ATOM   2808 C  C   . LEU   B 1 41  ? 6.010  15.040  15.128  1.00 63.34  ?  197 LEU   B C   1 
ATOM   2809 O  O   . LEU   B 1 41  ? 5.426  16.075  14.785  1.00 60.50  ?  197 LEU   B O   1 
ATOM   2810 C  CB  . LEU   B 1 41  ? 7.898  15.373  16.740  1.00 48.00  ?  197 LEU   B CB  1 
ATOM   2811 C  CG  . LEU   B 1 41  ? 8.397  15.639  18.159  1.00 49.65  ?  197 LEU   B CG  1 
ATOM   2812 C  CD1 . LEU   B 1 41  ? 9.917  15.564  18.222  1.00 45.02  ?  197 LEU   B CD1 1 
ATOM   2813 C  CD2 . LEU   B 1 41  ? 7.906  16.998  18.635  1.00 47.89  ?  197 LEU   B CD2 1 
ATOM   2814 N  N   . LYS   B 1 42  ? 6.251  14.040  14.271  1.00 52.33  ?  198 LYS   B N   1 
ATOM   2815 C  CA  . LYS   B 1 42  ? 5.870  14.201  12.872  1.00 61.26  ?  198 LYS   B CA  1 
ATOM   2816 C  C   . LYS   B 1 42  ? 4.365  14.176  12.669  1.00 60.21  ?  198 LYS   B C   1 
ATOM   2817 O  O   . LYS   B 1 42  ? 3.898  14.584  11.601  1.00 66.53  ?  198 LYS   B O   1 
ATOM   2818 C  CB  . LYS   B 1 42  ? 6.527  13.127  12.000  1.00 56.71  ?  198 LYS   B CB  1 
ATOM   2819 C  CG  . LYS   B 1 42  ? 8.006  13.361  11.732  1.00 57.24  ?  198 LYS   B CG  1 
ATOM   2820 C  CD  . LYS   B 1 42  ? 8.736  12.048  11.498  1.00 64.90  ?  198 LYS   B CD  1 
ATOM   2821 C  CE  . LYS   B 1 42  ? 9.724  12.146  10.353  1.00 73.88  ?  198 LYS   B CE  1 
ATOM   2822 N  NZ  . LYS   B 1 42  ? 10.547 10.910  10.257  1.00 74.97  ?  198 LYS   B NZ  1 
ATOM   2823 N  N   . CYS   B 1 43  ? 3.601  13.721  13.662  1.00 56.16  ?  199 CYS   B N   1 
ATOM   2824 C  CA  . CYS   B 1 43  ? 2.150  13.764  13.558  1.00 58.94  ?  199 CYS   B CA  1 
ATOM   2825 C  C   . CYS   B 1 43  ? 1.596  15.168  13.756  1.00 70.86  ?  199 CYS   B C   1 
ATOM   2826 O  O   . CYS   B 1 43  ? 0.439  15.420  13.401  1.00 81.15  ?  199 CYS   B O   1 
ATOM   2827 C  CB  . CYS   B 1 43  ? 1.521  12.813  14.578  1.00 70.30  ?  199 CYS   B CB  1 
ATOM   2828 S  SG  . CYS   B 1 43  ? 2.099  11.103  14.455  1.00 69.09  ?  199 CYS   B SG  1 
ATOM   2829 N  N   . ASP   B 1 44  ? 2.391  16.081  14.304  1.00 71.36  ?  200 ASP   B N   1 
ATOM   2830 C  CA  . ASP   B 1 44  ? 1.958  17.451  14.536  1.00 59.50  ?  200 ASP   B CA  1 
ATOM   2831 C  C   . ASP   B 1 44  ? 2.230  18.307  13.306  1.00 61.01  ?  200 ASP   B C   1 
ATOM   2832 O  O   . ASP   B 1 44  ? 3.228  18.112  12.606  1.00 66.52  ?  200 ASP   B O   1 
ATOM   2833 C  CB  . ASP   B 1 44  ? 2.671  18.036  15.754  1.00 63.14  ?  200 ASP   B CB  1 
ATOM   2834 C  CG  . ASP   B 1 44  ? 1.967  19.250  16.312  1.00 66.70  ?  200 ASP   B CG  1 
ATOM   2835 O  OD1 . ASP   B 1 44  ? 2.158  20.356  15.764  1.00 70.40  ?  200 ASP   B OD1 1 
ATOM   2836 O  OD2 . ASP   B 1 44  ? 1.216  19.095  17.296  1.00 60.69  -1 200 ASP   B OD2 1 
ATOM   2837 N  N   . SER   B 1 45  ? 1.330  19.258  13.044  1.00 64.67  ?  201 SER   B N   1 
ATOM   2838 C  CA  . SER   B 1 45  ? 1.507  20.150  11.901  1.00 73.51  ?  201 SER   B CA  1 
ATOM   2839 C  C   . SER   B 1 45  ? 2.698  21.078  12.102  1.00 60.31  ?  201 SER   B C   1 
ATOM   2840 O  O   . SER   B 1 45  ? 3.447  21.350  11.157  1.00 79.52  ?  201 SER   B O   1 
ATOM   2841 C  CB  . SER   B 1 45  ? 0.234  20.962  11.666  1.00 68.09  ?  201 SER   B CB  1 
ATOM   2842 O  OG  . SER   B 1 45  ? -0.176 21.611  12.857  1.00 68.90  ?  201 SER   B OG  1 
ATOM   2843 N  N   . ALA   B 1 46  ? 2.891  21.572  13.328  1.00 64.29  ?  202 ALA   B N   1 
ATOM   2844 C  CA  . ALA   B 1 46  ? 3.980  22.504  13.596  1.00 59.73  ?  202 ALA   B CA  1 
ATOM   2845 C  C   . ALA   B 1 46  ? 5.347  21.858  13.406  1.00 57.34  ?  202 ALA   B C   1 
ATOM   2846 O  O   . ALA   B 1 46  ? 6.292  22.528  12.974  1.00 65.47  ?  202 ALA   B O   1 
ATOM   2847 C  CB  . ALA   B 1 46  ? 3.851  23.060  15.012  1.00 62.57  ?  202 ALA   B CB  1 
ATOM   2848 N  N   . PHE   B 1 47  ? 5.473  20.567  13.715  1.00 52.47  ?  203 PHE   B N   1 
ATOM   2849 C  CA  . PHE   B 1 47  ? 6.742  19.852  13.643  1.00 55.96  ?  203 PHE   B CA  1 
ATOM   2850 C  C   . PHE   B 1 47  ? 6.739  18.792  12.544  1.00 60.12  ?  203 PHE   B C   1 
ATOM   2851 O  O   . PHE   B 1 47  ? 7.421  17.771  12.658  1.00 47.70  ?  203 PHE   B O   1 
ATOM   2852 C  CB  . PHE   B 1 47  ? 7.068  19.209  14.992  1.00 50.06  ?  203 PHE   B CB  1 
ATOM   2853 C  CG  . PHE   B 1 47  ? 7.196  20.192  16.121  1.00 47.80  ?  203 PHE   B CG  1 
ATOM   2854 C  CD1 . PHE   B 1 47  ? 8.355  20.934  16.289  1.00 56.77  ?  203 PHE   B CD1 1 
ATOM   2855 C  CD2 . PHE   B 1 47  ? 6.154  20.376  17.016  1.00 49.75  ?  203 PHE   B CD2 1 
ATOM   2856 C  CE1 . PHE   B 1 47  ? 8.470  21.838  17.329  1.00 50.51  ?  203 PHE   B CE1 1 
ATOM   2857 C  CE2 . PHE   B 1 47  ? 6.265  21.279  18.056  1.00 49.60  ?  203 PHE   B CE2 1 
ATOM   2858 C  CZ  . PHE   B 1 47  ? 7.422  22.011  18.213  1.00 47.52  ?  203 PHE   B CZ  1 
ATOM   2859 N  N   . ARG   B 1 48  ? 5.980  19.034  11.470  1.00 70.98  ?  204 ARG   B N   1 
ATOM   2860 C  CA  . ARG   B 1 48  ? 5.766  18.009  10.450  1.00 53.70  ?  204 ARG   B CA  1 
ATOM   2861 C  C   . ARG   B 1 48  ? 7.075  17.559  9.811   1.00 55.22  ?  204 ARG   B C   1 
ATOM   2862 O  O   . ARG   B 1 48  ? 7.260  16.368  9.530   1.00 56.92  ?  204 ARG   B O   1 
ATOM   2863 C  CB  . ARG   B 1 48  ? 4.803  18.534  9.384   1.00 64.99  ?  204 ARG   B CB  1 
ATOM   2864 C  CG  . ARG   B 1 48  ? 4.482  17.546  8.268   1.00 73.06  ?  204 ARG   B CG  1 
ATOM   2865 C  CD  . ARG   B 1 48  ? 3.688  16.346  8.770   1.00 85.77  ?  204 ARG   B CD  1 
ATOM   2866 N  NE  . ARG   B 1 48  ? 3.217  15.515  7.665   1.00 99.62  ?  204 ARG   B NE  1 
ATOM   2867 C  CZ  . ARG   B 1 48  ? 2.687  14.307  7.802   1.00 100.40 ?  204 ARG   B CZ  1 
ATOM   2868 N  NH1 . ARG   B 1 48  ? 2.548  13.743  8.991   1.00 93.61  ?  204 ARG   B NH1 1 
ATOM   2869 N  NH2 . ARG   B 1 48  ? 2.283  13.650  6.719   1.00 88.00  ?  204 ARG   B NH2 1 
ATOM   2870 N  N   . GLY   B 1 49  ? 7.995  18.491  9.574   1.00 52.19  ?  205 GLY   B N   1 
ATOM   2871 C  CA  . GLY   B 1 49  ? 9.228  18.172  8.883   1.00 53.88  ?  205 GLY   B CA  1 
ATOM   2872 C  C   . GLY   B 1 49  ? 10.424 17.967  9.791   1.00 50.63  ?  205 GLY   B C   1 
ATOM   2873 O  O   . GLY   B 1 49  ? 11.568 18.145  9.365   1.00 45.76  ?  205 GLY   B O   1 
ATOM   2874 N  N   . VAL   B 1 50  ? 10.177 17.584  11.045  1.00 42.44  ?  206 VAL   B N   1 
ATOM   2875 C  CA  . VAL   B 1 50  ? 11.270 17.420  11.996  1.00 45.87  ?  206 VAL   B CA  1 
ATOM   2876 C  C   . VAL   B 1 50  ? 12.113 16.208  11.611  1.00 39.86  ?  206 VAL   B C   1 
ATOM   2877 O  O   . VAL   B 1 50  ? 11.615 15.214  11.062  1.00 58.02  ?  206 VAL   B O   1 
ATOM   2878 C  CB  . VAL   B 1 50  ? 10.728 17.298  13.433  1.00 41.97  ?  206 VAL   B CB  1 
ATOM   2879 C  CG1 . VAL   B 1 50  ? 9.980  15.985  13.626  1.00 54.14  ?  206 VAL   B CG1 1 
ATOM   2880 C  CG2 . VAL   B 1 50  ? 11.862 17.432  14.446  1.00 43.46  ?  206 VAL   B CG2 1 
ATOM   2881 N  N   . GLY   B 1 51  ? 13.410 16.305  11.879  1.00 37.93  ?  207 GLY   B N   1 
ATOM   2882 C  CA  . GLY   B 1 51  ? 14.311 15.207  11.602  1.00 40.66  ?  207 GLY   B CA  1 
ATOM   2883 C  C   . GLY   B 1 51  ? 15.640 15.417  12.284  1.00 47.98  ?  207 GLY   B C   1 
ATOM   2884 O  O   . GLY   B 1 51  ? 15.856 16.394  13.010  1.00 49.73  ?  207 GLY   B O   1 
ATOM   2885 N  N   . LEU   B 1 52  ? 16.530 14.469  12.030  1.00 38.57  ?  208 LEU   B N   1 
ATOM   2886 C  CA  . LEU   B 1 52  ? 17.886 14.508  12.546  1.00 42.53  ?  208 LEU   B CA  1 
ATOM   2887 C  C   . LEU   B 1 52  ? 18.767 15.239  11.546  1.00 54.00  ?  208 LEU   B C   1 
ATOM   2888 O  O   . LEU   B 1 52  ? 18.676 15.001  10.340  1.00 57.23  ?  208 LEU   B O   1 
ATOM   2889 C  CB  . LEU   B 1 52  ? 18.410 13.087  12.781  1.00 55.02  ?  208 LEU   B CB  1 
ATOM   2890 C  CG  . LEU   B 1 52  ? 17.916 12.370  14.041  1.00 63.24  ?  208 LEU   B CG  1 
ATOM   2891 C  CD1 . LEU   B 1 52  ? 17.802 10.877  13.798  1.00 64.95  ?  208 LEU   B CD1 1 
ATOM   2892 C  CD2 . LEU   B 1 52  ? 18.817 12.629  15.232  1.00 61.62  ?  208 LEU   B CD2 1 
ATOM   2893 N  N   . LEU   B 1 53  ? 19.607 16.140  12.060  1.00 53.86  ?  209 LEU   B N   1 
ATOM   2894 C  CA  . LEU   B 1 53  ? 20.572 16.848  11.226  1.00 59.63  ?  209 LEU   B CA  1 
ATOM   2895 C  C   . LEU   B 1 53  ? 21.306 15.893  10.286  1.00 78.11  ?  209 LEU   B C   1 
ATOM   2896 O  O   . LEU   B 1 53  ? 21.418 16.149  9.083   1.00 86.68  ?  209 LEU   B O   1 
ATOM   2897 C  CB  . LEU   B 1 53  ? 21.588 17.570  12.107  1.00 68.61  ?  209 LEU   B CB  1 
ATOM   2898 C  CG  . LEU   B 1 53  ? 22.020 18.918  11.556  1.00 62.01  ?  209 LEU   B CG  1 
ATOM   2899 C  CD1 . LEU   B 1 53  ? 20.981 19.927  12.032  1.00 60.30  ?  209 LEU   B CD1 1 
ATOM   2900 C  CD2 . LEU   B 1 53  ? 23.401 19.265  12.058  1.00 55.67  ?  209 LEU   B CD2 1 
ATOM   2901 N  N   . ASN   B 1 54  ? 21.827 14.792  10.831  1.00 74.19  ?  210 ASN   B N   1 
ATOM   2902 C  CA  . ASN   B 1 54  ? 22.494 13.742  10.063  1.00 77.10  ?  210 ASN   B CA  1 
ATOM   2903 C  C   . ASN   B 1 54  ? 23.475 14.308  9.023   1.00 79.27  ?  210 ASN   B C   1 
ATOM   2904 O  O   . ASN   B 1 54  ? 24.680 14.411  9.296   1.00 72.97  ?  210 ASN   B O   1 
ATOM   2905 C  CB  . ASN   B 1 54  ? 21.447 12.855  9.378   1.00 60.05  ?  210 ASN   B CB  1 
ATOM   2906 N  N   . SER   B 1 57  ? 23.950 10.088  11.374  1.00 81.38  ?  213 SER   B N   1 
ATOM   2907 C  CA  . SER   B 1 57  ? 24.460 10.245  12.762  1.00 76.46  ?  213 SER   B CA  1 
ATOM   2908 C  C   . SER   B 1 57  ? 23.339 10.749  13.675  1.00 74.43  ?  213 SER   B C   1 
ATOM   2909 O  O   . SER   B 1 57  ? 22.959 11.928  13.558  1.00 71.65  ?  213 SER   B O   1 
ATOM   2910 C  CB  . SER   B 1 57  ? 25.663 11.152  12.817  1.00 60.65  ?  213 SER   B CB  1 
ATOM   2911 O  OG  . SER   B 1 57  ? 26.562 10.862  11.758  1.00 76.60  ?  213 SER   B OG  1 
ATOM   2912 N  N   . TYR   B 1 58  ? 22.831 9.873   14.536  1.00 71.18  ?  214 TYR   B N   1 
ATOM   2913 C  CA  . TYR   B 1 58  ? 21.780 10.279  15.495  1.00 61.14  ?  214 TYR   B CA  1 
ATOM   2914 C  C   . TYR   B 1 58  ? 22.425 10.927  16.682  1.00 79.94  ?  214 TYR   B C   1 
ATOM   2915 O  O   . TYR   B 1 58  ? 21.922 11.959  17.159  1.00 83.93  ?  214 TYR   B O   1 
ATOM   2916 C  CB  . TYR   B 1 58  ? 21.125 9.065   16.147  1.00 54.61  ?  214 TYR   B CB  1 
ATOM   2917 C  CG  . TYR   B 1 58  ? 19.979 8.389   15.410  1.00 56.48  ?  214 TYR   B CG  1 
ATOM   2918 C  CD1 . TYR   B 1 58  ? 20.135 7.884   14.124  1.00 64.72  ?  214 TYR   B CD1 1 
ATOM   2919 C  CD2 . TYR   B 1 58  ? 18.748 8.222   16.025  1.00 60.58  ?  214 TYR   B CD2 1 
ATOM   2920 C  CE1 . TYR   B 1 58  ? 19.089 7.260   13.466  1.00 57.78  ?  214 TYR   B CE1 1 
ATOM   2921 C  CE2 . TYR   B 1 58  ? 17.694 7.600   15.378  1.00 59.44  ?  214 TYR   B CE2 1 
ATOM   2922 C  CZ  . TYR   B 1 58  ? 17.865 7.119   14.095  1.00 59.11  ?  214 TYR   B CZ  1 
ATOM   2923 O  OH  . TYR   B 1 58  ? 16.815 6.511   13.475  1.00 73.51  ?  214 TYR   B OH  1 
ATOM   2924 N  N   . TYR   B 1 59  ? 23.569 10.398  17.110  1.00 82.66  ?  215 TYR   B N   1 
ATOM   2925 C  CA  . TYR   B 1 59  ? 24.129 10.867  18.391  1.00 45.40  ?  215 TYR   B CA  1 
ATOM   2926 C  C   . TYR   B 1 59  ? 25.547 11.359  18.362  1.00 69.78  ?  215 TYR   B C   1 
ATOM   2927 O  O   . TYR   B 1 59  ? 26.393 10.792  17.653  1.00 69.74  ?  215 TYR   B O   1 
ATOM   2928 C  CB  . TYR   B 1 59  ? 24.098 9.606   19.246  1.00 62.02  ?  215 TYR   B CB  1 
ATOM   2929 N  N   . GLU   B 1 60  ? 25.807 12.380  19.164  1.00 71.08  ?  216 GLU   B N   1 
ATOM   2930 C  CA  . GLU   B 1 60  ? 27.133 12.953  19.397  1.00 52.39  ?  216 GLU   B CA  1 
ATOM   2931 C  C   . GLU   B 1 60  ? 27.419 12.944  20.895  1.00 50.93  ?  216 GLU   B C   1 
ATOM   2932 O  O   . GLU   B 1 60  ? 26.547 12.633  21.712  1.00 42.50  ?  216 GLU   B O   1 
ATOM   2933 C  CB  . GLU   B 1 60  ? 27.238 14.374  18.833  1.00 49.08  ?  216 GLU   B CB  1 
ATOM   2934 N  N   . HIS   B 1 61  ? 28.652 13.308  21.244  1.00 45.57  ?  217 HIS   B N   1 
ATOM   2935 C  CA  . HIS   B 1 61  ? 29.107 13.363  22.627  1.00 42.83  ?  217 HIS   B CA  1 
ATOM   2936 C  C   . HIS   B 1 61  ? 29.837 14.674  22.857  1.00 39.71  ?  217 HIS   B C   1 
ATOM   2937 O  O   . HIS   B 1 61  ? 30.898 14.897  22.273  1.00 51.37  ?  217 HIS   B O   1 
ATOM   2938 C  CB  . HIS   B 1 61  ? 30.023 12.187  22.963  1.00 41.34  ?  217 HIS   B CB  1 
ATOM   2939 C  CG  . HIS   B 1 61  ? 29.322 10.868  22.976  1.00 44.35  ?  217 HIS   B CG  1 
ATOM   2940 N  ND1 . HIS   B 1 61  ? 28.974 10.199  21.824  1.00 49.48  ?  217 HIS   B ND1 1 
ATOM   2941 C  CD2 . HIS   B 1 61  ? 28.888 10.101  24.005  1.00 50.88  ?  217 HIS   B CD2 1 
ATOM   2942 C  CE1 . HIS   B 1 61  ? 28.370 9.070   22.144  1.00 47.68  ?  217 HIS   B CE1 1 
ATOM   2943 N  NE2 . HIS   B 1 61  ? 28.303 8.987   23.460  1.00 57.63  ?  217 HIS   B NE2 1 
ATOM   2944 N  N   . VAL   B 1 62  ? 29.288 15.529  23.724  1.00 43.00  ?  218 VAL   B N   1 
ATOM   2945 C  CA  . VAL   B 1 62  ? 29.964 16.782  24.041  1.00 46.59  ?  218 VAL   B CA  1 
ATOM   2946 C  C   . VAL   B 1 62  ? 31.144 16.564  24.977  1.00 50.91  ?  218 VAL   B C   1 
ATOM   2947 O  O   . VAL   B 1 62  ? 32.033 17.422  25.052  1.00 53.01  ?  218 VAL   B O   1 
ATOM   2948 C  CB  . VAL   B 1 62  ? 28.990 17.799  24.660  1.00 42.09  ?  218 VAL   B CB  1 
ATOM   2949 C  CG1 . VAL   B 1 62  ? 27.753 17.957  23.793  1.00 47.21  ?  218 VAL   B CG1 1 
ATOM   2950 C  CG2 . VAL   B 1 62  ? 28.621 17.381  26.083  1.00 49.07  ?  218 VAL   B CG2 1 
ATOM   2951 N  N   . LYS   B 1 63  ? 31.185 15.439  25.691  1.00 46.37  ?  219 LYS   B N   1 
ATOM   2952 C  CA  . LYS   B 1 63  ? 32.250 15.140  26.642  1.00 41.19  ?  219 LYS   B CA  1 
ATOM   2953 C  C   . LYS   B 1 63  ? 32.894 13.817  26.265  1.00 49.79  ?  219 LYS   B C   1 
ATOM   2954 O  O   . LYS   B 1 63  ? 32.210 12.791  26.216  1.00 45.33  ?  219 LYS   B O   1 
ATOM   2955 C  CB  . LYS   B 1 63  ? 31.707 15.079  28.072  1.00 43.19  ?  219 LYS   B CB  1 
ATOM   2956 C  CG  . LYS   B 1 63  ? 31.297 16.410  28.664  1.00 43.61  ?  219 LYS   B CG  1 
ATOM   2957 C  CD  . LYS   B 1 63  ? 30.917 16.237  30.129  1.00 40.86  ?  219 LYS   B CD  1 
ATOM   2958 C  CE  . LYS   B 1 63  ? 32.022 15.528  30.904  1.00 50.49  ?  219 LYS   B CE  1 
ATOM   2959 N  NZ  . LYS   B 1 63  ? 31.623 15.212  32.306  1.00 51.60  ?  219 LYS   B NZ  1 
ATOM   2960 N  N   . ILE   B 1 64  ? 34.213 13.840  26.028  1.00 42.05  ?  220 ILE   B N   1 
ATOM   2961 C  CA  . ILE   B 1 64  ? 34.920 12.640  25.581  1.00 43.24  ?  220 ILE   B CA  1 
ATOM   2962 C  C   . ILE   B 1 64  ? 34.932 11.570  26.656  1.00 33.33  ?  220 ILE   B C   1 
ATOM   2963 O  O   . ILE   B 1 64  ? 35.070 10.381  26.347  1.00 60.38  ?  220 ILE   B O   1 
ATOM   2964 C  CB  . ILE   B 1 64  ? 36.343 13.005  25.046  1.00 39.71  ?  220 ILE   B CB  1 
ATOM   2965 C  CG1 . ILE   B 1 64  ? 37.249 13.786  26.023  1.00 37.75  ?  220 ILE   B CG1 1 
ATOM   2966 C  CG2 . ILE   B 1 64  ? 36.215 13.774  23.780  1.00 55.15  ?  220 ILE   B CG2 1 
ATOM   2967 C  CD1 . ILE   B 1 64  ? 37.642 13.091  27.276  1.00 49.50  ?  220 ILE   B CD1 1 
ATOM   2968 N  N   . SER   B 1 65  ? 34.711 11.956  27.912  1.00 42.24  ?  221 SER   B N   1 
ATOM   2969 C  CA  . SER   B 1 65  ? 34.822 11.051  29.041  1.00 51.30  ?  221 SER   B CA  1 
ATOM   2970 C  C   . SER   B 1 65  ? 33.465 10.680  29.632  1.00 42.40  ?  221 SER   B C   1 
ATOM   2971 O  O   . SER   B 1 65  ? 33.404 10.179  30.762  1.00 49.39  ?  221 SER   B O   1 
ATOM   2972 C  CB  . SER   B 1 65  ? 35.713 11.672  30.113  1.00 57.53  ?  221 SER   B CB  1 
ATOM   2973 O  OG  . SER   B 1 65  ? 35.209 12.941  30.486  1.00 42.88  ?  221 SER   B OG  1 
ATOM   2974 N  N   . ALA   B 1 66  ? 32.378 10.920  28.895  1.00 51.86  ?  222 ALA   B N   1 
ATOM   2975 C  CA  . ALA   B 1 66  ? 31.024 10.553  29.309  1.00 51.57  ?  222 ALA   B CA  1 
ATOM   2976 C  C   . ALA   B 1 66  ? 30.371 9.800   28.157  1.00 47.68  ?  222 ALA   B C   1 
ATOM   2977 O  O   . ALA   B 1 66  ? 29.490 10.329  27.468  1.00 55.34  ?  222 ALA   B O   1 
ATOM   2978 C  CB  . ALA   B 1 66  ? 30.211 11.788  29.700  1.00 37.70  ?  222 ALA   B CB  1 
ATOM   2979 N  N   . PRO   B 1 67  ? 30.806 8.562   27.903  1.00 52.24  ?  223 PRO   B N   1 
ATOM   2980 C  CA  . PRO   B 1 67  ? 30.278 7.821   26.745  1.00 56.49  ?  223 PRO   B CA  1 
ATOM   2981 C  C   . PRO   B 1 67  ? 28.789 7.541   26.831  1.00 46.66  ?  223 PRO   B C   1 
ATOM   2982 O  O   . PRO   B 1 67  ? 28.170 7.252   25.800  1.00 68.29  ?  223 PRO   B O   1 
ATOM   2983 C  CB  . PRO   B 1 67  ? 31.094 6.522   26.764  1.00 64.13  ?  223 PRO   B CB  1 
ATOM   2984 C  CG  . PRO   B 1 67  ? 31.459 6.344   28.200  1.00 51.81  ?  223 PRO   B CG  1 
ATOM   2985 C  CD  . PRO   B 1 67  ? 31.719 7.737   28.713  1.00 51.20  ?  223 PRO   B CD  1 
ATOM   2986 N  N   . ASN   B 1 68  ? 28.194 7.619   28.020  1.00 40.83  ?  224 ASN   B N   1 
ATOM   2987 C  CA  . ASN   B 1 68  ? 26.768 7.393   28.203  1.00 53.59  ?  224 ASN   B CA  1 
ATOM   2988 C  C   . ASN   B 1 68  ? 25.965 8.688   28.202  1.00 55.28  ?  224 ASN   B C   1 
ATOM   2989 O  O   . ASN   B 1 68  ? 24.782 8.673   28.556  1.00 50.50  ?  224 ASN   B O   1 
ATOM   2990 C  CB  . ASN   B 1 68  ? 26.521 6.626   29.502  1.00 48.61  ?  224 ASN   B CB  1 
ATOM   2991 C  CG  . ASN   B 1 68  ? 27.060 5.210   29.453  1.00 61.27  ?  224 ASN   B CG  1 
ATOM   2992 O  OD1 . ASN   B 1 68  ? 26.870 4.493   28.470  1.00 56.32  ?  224 ASN   B OD1 1 
ATOM   2993 N  ND2 . ASN   B 1 68  ? 27.743 4.799   30.517  1.00 64.10  ?  224 ASN   B ND2 1 
ATOM   2994 N  N   . GLU   B 1 69  ? 26.578 9.804   27.815  1.00 53.47  ?  225 GLU   B N   1 
ATOM   2995 C  CA  . GLU   B 1 69  ? 25.912 11.103  27.760  1.00 42.88  ?  225 GLU   B CA  1 
ATOM   2996 C  C   . GLU   B 1 69  ? 25.894 11.545  26.301  1.00 37.96  ?  225 GLU   B C   1 
ATOM   2997 O  O   . GLU   B 1 69  ? 26.919 11.974  25.758  1.00 43.29  ?  225 GLU   B O   1 
ATOM   2998 C  CB  . GLU   B 1 69  ? 26.613 12.112  28.666  1.00 32.80  ?  225 GLU   B CB  1 
ATOM   2999 C  CG  . GLU   B 1 69  ? 26.456 11.785  30.147  1.00 44.19  ?  225 GLU   B CG  1 
ATOM   3000 C  CD  . GLU   B 1 69  ? 27.117 12.801  31.059  1.00 61.16  ?  225 GLU   B CD  1 
ATOM   3001 O  OE1 . GLU   B 1 69  ? 27.348 13.946  30.617  1.00 52.47  ?  225 GLU   B OE1 1 
ATOM   3002 O  OE2 . GLU   B 1 69  ? 27.406 12.451  32.224  1.00 57.03  -1 225 GLU   B OE2 1 
ATOM   3003 N  N   . PHE   B 1 70  ? 24.730 11.433  25.673  1.00 37.57  ?  226 PHE   B N   1 
ATOM   3004 C  CA  . PHE   B 1 70  ? 24.562 11.667  24.247  1.00 36.69  ?  226 PHE   B CA  1 
ATOM   3005 C  C   . PHE   B 1 70  ? 23.955 13.043  23.992  1.00 40.25  ?  226 PHE   B C   1 
ATOM   3006 O  O   . PHE   B 1 70  ? 23.378 13.670  24.884  1.00 46.26  ?  226 PHE   B O   1 
ATOM   3007 C  CB  . PHE   B 1 70  ? 23.681 10.578  23.629  1.00 46.05  ?  226 PHE   B CB  1 
ATOM   3008 C  CG  . PHE   B 1 70  ? 24.340 9.225   23.561  1.00 51.52  ?  226 PHE   B CG  1 
ATOM   3009 C  CD1 . PHE   B 1 70  ? 24.399 8.409   24.680  1.00 55.72  ?  226 PHE   B CD1 1 
ATOM   3010 C  CD2 . PHE   B 1 70  ? 24.888 8.766   22.377  1.00 55.05  ?  226 PHE   B CD2 1 
ATOM   3011 C  CE1 . PHE   B 1 70  ? 25.001 7.164   24.617  1.00 61.93  ?  226 PHE   B CE1 1 
ATOM   3012 C  CE2 . PHE   B 1 70  ? 25.488 7.521   22.307  1.00 55.70  ?  226 PHE   B CE2 1 
ATOM   3013 C  CZ  . PHE   B 1 70  ? 25.546 6.721   23.429  1.00 55.48  ?  226 PHE   B CZ  1 
ATOM   3014 N  N   . ASP   B 1 71  ? 24.092 13.502  22.749  1.00 38.98  ?  227 ASP   B N   1 
ATOM   3015 C  CA  . ASP   B 1 71  ? 23.630 14.827  22.349  1.00 42.55  ?  227 ASP   B CA  1 
ATOM   3016 C  C   . ASP   B 1 71  ? 23.014 14.730  20.962  1.00 41.69  ?  227 ASP   B C   1 
ATOM   3017 O  O   . ASP   B 1 71  ? 23.684 14.318  20.011  1.00 42.17  ?  227 ASP   B O   1 
ATOM   3018 C  CB  . ASP   B 1 71  ? 24.780 15.838  22.361  1.00 51.68  ?  227 ASP   B CB  1 
ATOM   3019 C  CG  . ASP   B 1 71  ? 24.306 17.260  22.147  1.00 63.62  ?  227 ASP   B CG  1 
ATOM   3020 O  OD1 . ASP   B 1 71  ? 23.990 17.935  23.150  1.00 49.72  ?  227 ASP   B OD1 1 
ATOM   3021 O  OD2 . ASP   B 1 71  ? 24.246 17.704  20.981  1.00 71.69  -1 227 ASP   B OD2 1 
ATOM   3022 N  N   . VAL   B 1 72  ? 21.745 15.116  20.852  1.00 50.47  ?  228 VAL   B N   1 
ATOM   3023 C  CA  . VAL   B 1 72  ? 20.964 14.952  19.632  1.00 55.91  ?  228 VAL   B CA  1 
ATOM   3024 C  C   . VAL   B 1 72  ? 20.353 16.294  19.254  1.00 48.18  ?  228 VAL   B C   1 
ATOM   3025 O  O   . VAL   B 1 72  ? 19.902 17.047  20.124  1.00 35.64  ?  228 VAL   B O   1 
ATOM   3026 C  CB  . VAL   B 1 72  ? 19.862 13.887  19.813  1.00 55.23  ?  228 VAL   B CB  1 
ATOM   3027 C  CG1 . VAL   B 1 72  ? 19.131 13.664  18.518  1.00 57.65  ?  228 VAL   B CG1 1 
ATOM   3028 C  CG2 . VAL   B 1 72  ? 20.455 12.581  20.320  1.00 52.06  ?  228 VAL   B CG2 1 
ATOM   3029 N  N   . MET   B 1 73  ? 20.330 16.592  17.955  1.00 43.97  ?  229 MET   B N   1 
ATOM   3030 C  CA  . MET   B 1 73  ? 19.692 17.795  17.432  1.00 46.33  ?  229 MET   B CA  1 
ATOM   3031 C  C   . MET   B 1 73  ? 18.550 17.403  16.504  1.00 39.08  ?  229 MET   B C   1 
ATOM   3032 O  O   . MET   B 1 73  ? 18.767 16.712  15.501  1.00 44.81  ?  229 MET   B O   1 
ATOM   3033 C  CB  . MET   B 1 73  ? 20.690 18.686  16.690  1.00 34.83  ?  229 MET   B CB  1 
ATOM   3034 C  CG  . MET   B 1 73  ? 20.052 19.944  16.107  1.00 54.13  ?  229 MET   B CG  1 
ATOM   3035 S  SD  . MET   B 1 73  ? 21.223 21.209  15.569  1.00 55.93  ?  229 MET   B SD  1 
ATOM   3036 C  CE  . MET   B 1 73  ? 22.474 21.081  16.841  1.00 49.36  ?  229 MET   B CE  1 
ATOM   3037 N  N   . PHE   B 1 74  ? 17.341 17.846  16.838  1.00 42.21  ?  230 PHE   B N   1 
ATOM   3038 C  CA  . PHE   B 1 74  ? 16.187 17.723  15.956  1.00 41.06  ?  230 PHE   B CA  1 
ATOM   3039 C  C   . PHE   B 1 74  ? 16.067 19.009  15.147  1.00 47.90  ?  230 PHE   B C   1 
ATOM   3040 O  O   . PHE   B 1 74  ? 15.889 20.089  15.721  1.00 52.68  ?  230 PHE   B O   1 
ATOM   3041 C  CB  . PHE   B 1 74  ? 14.904 17.479  16.750  1.00 45.27  ?  230 PHE   B CB  1 
ATOM   3042 C  CG  . PHE   B 1 74  ? 14.818 16.124  17.407  1.00 40.07  ?  230 PHE   B CG  1 
ATOM   3043 C  CD1 . PHE   B 1 74  ? 15.856 15.211  17.322  1.00 39.02  ?  230 PHE   B CD1 1 
ATOM   3044 C  CD2 . PHE   B 1 74  ? 13.683 15.772  18.120  1.00 39.19  ?  230 PHE   B CD2 1 
ATOM   3045 C  CE1 . PHE   B 1 74  ? 15.759 13.971  17.934  1.00 44.30  ?  230 PHE   B CE1 1 
ATOM   3046 C  CE2 . PHE   B 1 74  ? 13.583 14.538  18.734  1.00 44.87  ?  230 PHE   B CE2 1 
ATOM   3047 C  CZ  . PHE   B 1 74  ? 14.621 13.637  18.641  1.00 39.40  ?  230 PHE   B CZ  1 
ATOM   3048 N  N   . LYS   B 1 75  ? 16.167 18.902  13.827  1.00 48.68  ?  231 LYS   B N   1 
ATOM   3049 C  CA  . LYS   B 1 75  ? 16.077 20.068  12.960  1.00 38.60  ?  231 LYS   B CA  1 
ATOM   3050 C  C   . LYS   B 1 75  ? 14.680 20.185  12.358  1.00 41.76  ?  231 LYS   B C   1 
ATOM   3051 O  O   . LYS   B 1 75  ? 13.948 19.201  12.227  1.00 43.79  ?  231 LYS   B O   1 
ATOM   3052 C  CB  . LYS   B 1 75  ? 17.121 20.002  11.842  1.00 37.10  ?  231 LYS   B CB  1 
ATOM   3053 C  CG  . LYS   B 1 75  ? 17.062 18.732  11.012  1.00 52.59  ?  231 LYS   B CG  1 
ATOM   3054 C  CD  . LYS   B 1 75  ? 17.394 19.009  9.555   1.00 50.53  ?  231 LYS   B CD  1 
ATOM   3055 C  CE  . LYS   B 1 75  ? 16.142 19.338  8.755   1.00 55.89  ?  231 LYS   B CE  1 
ATOM   3056 N  NZ  . LYS   B 1 75  ? 16.254 18.901  7.336   1.00 56.07  ?  231 LYS   B NZ  1 
ATOM   3057 N  N   . LEU   B 1 76  ? 14.319 21.414  11.991  1.00 35.63  ?  232 LEU   B N   1 
ATOM   3058 C  CA  . LEU   B 1 76  ? 13.034 21.685  11.353  1.00 38.77  ?  232 LEU   B CA  1 
ATOM   3059 C  C   . LEU   B 1 76  ? 13.209 22.849  10.393  1.00 40.80  ?  232 LEU   B C   1 
ATOM   3060 O  O   . LEU   B 1 76  ? 13.575 23.948  10.818  1.00 45.28  ?  232 LEU   B O   1 
ATOM   3061 C  CB  . LEU   B 1 76  ? 11.955 22.004  12.391  1.00 39.16  ?  232 LEU   B CB  1 
ATOM   3062 C  CG  . LEU   B 1 76  ? 10.591 22.378  11.809  1.00 47.37  ?  232 LEU   B CG  1 
ATOM   3063 C  CD1 . LEU   B 1 76  ? 9.978  21.187  11.090  1.00 51.72  ?  232 LEU   B CD1 1 
ATOM   3064 C  CD2 . LEU   B 1 76  ? 9.661  22.888  12.896  1.00 45.10  ?  232 LEU   B CD2 1 
ATOM   3065 N  N   . GLU   B 1 77  ? 12.948 22.617  9.110   1.00 52.50  ?  233 GLU   B N   1 
ATOM   3066 C  CA  . GLU   B 1 77  ? 13.175 23.657  8.117   1.00 50.98  ?  233 GLU   B CA  1 
ATOM   3067 C  C   . GLU   B 1 77  ? 12.161 24.782  8.258   1.00 46.19  ?  233 GLU   B C   1 
ATOM   3068 O  O   . GLU   B 1 77  ? 10.961 24.543  8.423   1.00 46.20  ?  233 GLU   B O   1 
ATOM   3069 C  CB  . GLU   B 1 77  ? 13.094 23.087  6.704   1.00 50.74  ?  233 GLU   B CB  1 
ATOM   3070 C  CG  . GLU   B 1 77  ? 13.382 24.129  5.627   1.00 59.54  ?  233 GLU   B CG  1 
ATOM   3071 C  CD  . GLU   B 1 77  ? 13.322 23.582  4.216   1.00 66.28  ?  233 GLU   B CD  1 
ATOM   3072 O  OE1 . GLU   B 1 77  ? 13.040 22.378  4.050   1.00 79.96  ?  233 GLU   B OE1 1 
ATOM   3073 O  OE2 . GLU   B 1 77  ? 13.551 24.366  3.270   1.00 59.51  -1 233 GLU   B OE2 1 
ATOM   3074 N  N   . VAL   B 1 78  ? 12.645 26.012  8.193   1.00 44.93  ?  234 VAL   B N   1 
ATOM   3075 C  CA  . VAL   B 1 78  ? 11.789 27.190  8.116   1.00 45.81  ?  234 VAL   B CA  1 
ATOM   3076 C  C   . VAL   B 1 78  ? 12.052 27.880  6.773   1.00 61.75  ?  234 VAL   B C   1 
ATOM   3077 O  O   . VAL   B 1 78  ? 13.011 28.627  6.634   1.00 63.88  ?  234 VAL   B O   1 
ATOM   3078 C  CB  . VAL   B 1 78  ? 12.063 28.153  9.287   1.00 55.37  ?  234 VAL   B CB  1 
ATOM   3079 C  CG1 . VAL   B 1 78  ? 11.250 29.431  9.135   1.00 53.26  ?  234 VAL   B CG1 1 
ATOM   3080 C  CG2 . VAL   B 1 78  ? 11.720 27.475  10.608  1.00 58.43  ?  234 VAL   B CG2 1 
ATOM   3081 N  N   . PRO   B 1 79  ? 11.218 27.630  5.755   1.00 65.35  ?  235 PRO   B N   1 
ATOM   3082 C  CA  . PRO   B 1 79  ? 11.441 28.293  4.468   1.00 62.58  ?  235 PRO   B CA  1 
ATOM   3083 C  C   . PRO   B 1 79  ? 11.064 29.765  4.557   1.00 49.24  ?  235 PRO   B C   1 
ATOM   3084 O  O   . PRO   B 1 79  ? 10.215 30.169  5.364   1.00 47.32  ?  235 PRO   B O   1 
ATOM   3085 C  CB  . PRO   B 1 79  ? 10.530 27.528  3.519   1.00 61.69  ?  235 PRO   B CB  1 
ATOM   3086 C  CG  . PRO   B 1 79  ? 9.647  26.668  4.333   1.00 66.42  ?  235 PRO   B CG  1 
ATOM   3087 C  CD  . PRO   B 1 79  ? 10.012 26.798  5.769   1.00 44.84  ?  235 PRO   B CD  1 
ATOM   3088 N  N   . ARG   B 1 80  ? 11.732 30.569  3.727   1.00 54.50  ?  236 ARG   B N   1 
ATOM   3089 C  CA  . ARG   B 1 80  ? 11.460 31.990  3.611   1.00 43.11  ?  236 ARG   B CA  1 
ATOM   3090 C  C   . ARG   B 1 80  ? 11.531 32.689  4.973   1.00 50.52  ?  236 ARG   B C   1 
ATOM   3091 O  O   . ARG   B 1 80  ? 10.641 33.457  5.370   1.00 61.22  ?  236 ARG   B O   1 
ATOM   3092 C  CB  . ARG   B 1 80  ? 10.109 32.246  2.940   1.00 51.25  ?  236 ARG   B CB  1 
ATOM   3093 N  N   . ILE   B 1 81  ? 12.597 32.403  5.700   1.00 49.90  ?  237 ILE   B N   1 
ATOM   3094 C  CA  . ILE   B 1 81  ? 12.809 32.963  7.028   1.00 55.70  ?  237 ILE   B CA  1 
ATOM   3095 C  C   . ILE   B 1 81  ? 13.258 34.411  6.880   1.00 54.89  ?  237 ILE   B C   1 
ATOM   3096 O  O   . ILE   B 1 81  ? 13.851 34.789  5.864   1.00 56.50  ?  237 ILE   B O   1 
ATOM   3097 C  CB  . ILE   B 1 81  ? 13.845 32.108  7.792   1.00 57.74  ?  237 ILE   B CB  1 
ATOM   3098 C  CG1 . ILE   B 1 81  ? 14.104 32.660  9.191   1.00 62.18  ?  237 ILE   B CG1 1 
ATOM   3099 C  CG2 . ILE   B 1 81  ? 15.152 32.029  7.006   1.00 73.16  ?  237 ILE   B CG2 1 
ATOM   3100 C  CD1 . ILE   B 1 81  ? 14.547 31.603  10.185  1.00 57.10  ?  237 ILE   B CD1 1 
ATOM   3101 N  N   . GLN   B 1 82  ? 12.966 35.241  7.881   1.00 55.38  ?  238 GLN   B N   1 
ATOM   3102 C  CA  . GLN   B 1 82  ? 13.446 36.618  7.917   1.00 53.70  ?  238 GLN   B CA  1 
ATOM   3103 C  C   . GLN   B 1 82  ? 14.064 36.863  9.286   1.00 51.96  ?  238 GLN   B C   1 
ATOM   3104 O  O   . GLN   B 1 82  ? 13.358 36.882  10.296  1.00 54.51  ?  238 GLN   B O   1 
ATOM   3105 C  CB  . GLN   B 1 82  ? 12.321 37.616  7.638   1.00 66.25  ?  238 GLN   B CB  1 
ATOM   3106 C  CG  . GLN   B 1 82  ? 12.698 39.056  7.945   1.00 75.44  ?  238 GLN   B CG  1 
ATOM   3107 C  CD  . GLN   B 1 82  ? 13.804 39.572  7.042   1.00 80.91  ?  238 GLN   B CD  1 
ATOM   3108 O  OE1 . GLN   B 1 82  ? 14.807 40.108  7.514   1.00 75.76  ?  238 GLN   B OE1 1 
ATOM   3109 N  NE2 . GLN   B 1 82  ? 13.625 39.414  5.735   1.00 66.71  ?  238 GLN   B NE2 1 
ATOM   3110 N  N   . LEU   B 1 83  ? 15.375 37.046  9.328   1.00 56.64  ?  239 LEU   B N   1 
ATOM   3111 C  CA  . LEU   B 1 83  ? 16.062 37.284  10.585  1.00 46.93  ?  239 LEU   B CA  1 
ATOM   3112 C  C   . LEU   B 1 83  ? 16.191 38.776  10.856  1.00 49.36  ?  239 LEU   B C   1 
ATOM   3113 O  O   . LEU   B 1 83  ? 16.342 39.584  9.935   1.00 55.32  ?  239 LEU   B O   1 
ATOM   3114 C  CB  . LEU   B 1 83  ? 17.446 36.635  10.574  1.00 49.71  ?  239 LEU   B CB  1 
ATOM   3115 C  CG  . LEU   B 1 83  ? 17.438 35.133  10.299  1.00 45.36  ?  239 LEU   B CG  1 
ATOM   3116 C  CD1 . LEU   B 1 83  ? 18.804 34.518  10.547  1.00 34.32  ?  239 LEU   B CD1 1 
ATOM   3117 C  CD2 . LEU   B 1 83  ? 16.404 34.493  11.201  1.00 54.71  ?  239 LEU   B CD2 1 
ATOM   3118 N  N   . GLU   B 1 84  ? 16.112 39.140  12.135  1.00 38.04  ?  240 GLU   B N   1 
ATOM   3119 C  CA  . GLU   B 1 84  ? 16.495 40.483  12.559  1.00 53.71  ?  240 GLU   B CA  1 
ATOM   3120 C  C   . GLU   B 1 84  ? 17.436 40.367  13.748  1.00 55.25  ?  240 GLU   B C   1 
ATOM   3121 O  O   . GLU   B 1 84  ? 17.077 39.779  14.771  1.00 46.17  ?  240 GLU   B O   1 
ATOM   3122 C  CB  . GLU   B 1 84  ? 15.285 41.352  12.916  1.00 45.53  ?  240 GLU   B CB  1 
ATOM   3123 C  CG  . GLU   B 1 84  ? 15.700 42.606  13.675  1.00 45.00  ?  240 GLU   B CG  1 
ATOM   3124 C  CD  . GLU   B 1 84  ? 14.567 43.585  13.893  1.00 70.25  ?  240 GLU   B CD  1 
ATOM   3125 O  OE1 . GLU   B 1 84  ? 13.510 43.178  14.419  1.00 73.82  ?  240 GLU   B OE1 1 
ATOM   3126 O  OE2 . GLU   B 1 84  ? 14.740 44.769  13.535  1.00 72.98  -1 240 GLU   B OE2 1 
ATOM   3127 N  N   . GLU   B 1 85  ? 18.630 40.933  13.615  1.00 46.63  ?  241 GLU   B N   1 
ATOM   3128 C  CA  . GLU   B 1 85  ? 19.649 40.778  14.640  1.00 43.39  ?  241 GLU   B CA  1 
ATOM   3129 C  C   . GLU   B 1 85  ? 19.287 41.548  15.902  1.00 40.93  ?  241 GLU   B C   1 
ATOM   3130 O  O   . GLU   B 1 85  ? 18.804 42.683  15.847  1.00 52.79  ?  241 GLU   B O   1 
ATOM   3131 C  CB  . GLU   B 1 85  ? 20.997 41.250  14.106  1.00 51.21  ?  241 GLU   B CB  1 
ATOM   3132 C  CG  . GLU   B 1 85  ? 22.128 41.206  15.116  1.00 60.23  ?  241 GLU   B CG  1 
ATOM   3133 C  CD  . GLU   B 1 85  ? 23.424 41.760  14.559  1.00 56.29  ?  241 GLU   B CD  1 
ATOM   3134 O  OE1 . GLU   B 1 85  ? 23.433 42.199  13.390  1.00 57.40  ?  241 GLU   B OE1 1 
ATOM   3135 O  OE2 . GLU   B 1 85  ? 24.432 41.770  15.294  1.00 47.75  -1 241 GLU   B OE2 1 
ATOM   3136 N  N   . TYR   B 1 86  ? 19.462 40.875  17.040  1.00 40.94  ?  242 TYR   B N   1 
ATOM   3137 C  CA  . TYR   B 1 86  ? 19.191 41.494  18.358  1.00 39.06  ?  242 TYR   B CA  1 
ATOM   3138 C  C   . TYR   B 1 86  ? 20.328 42.410  18.704  1.00 46.29  ?  242 TYR   B C   1 
ATOM   3139 O  O   . TYR   B 1 86  ? 21.490 41.976  18.657  1.00 42.16  ?  242 TYR   B O   1 
ATOM   3140 C  CB  . TYR   B 1 86  ? 19.084 40.435  19.449  1.00 39.41  ?  242 TYR   B CB  1 
ATOM   3141 C  CG  . TYR   B 1 86  ? 19.020 40.996  20.860  1.00 53.33  ?  242 TYR   B CG  1 
ATOM   3142 C  CD1 . TYR   B 1 86  ? 17.991 41.844  21.247  1.00 49.31  ?  242 TYR   B CD1 1 
ATOM   3143 C  CD2 . TYR   B 1 86  ? 19.990 40.681  21.799  1.00 53.95  ?  242 TYR   B CD2 1 
ATOM   3144 C  CE1 . TYR   B 1 86  ? 17.928 42.358  22.529  1.00 54.45  ?  242 TYR   B CE1 1 
ATOM   3145 C  CE2 . TYR   B 1 86  ? 19.941 41.190  23.083  1.00 51.57  ?  242 TYR   B CE2 1 
ATOM   3146 C  CZ  . TYR   B 1 86  ? 18.906 42.031  23.447  1.00 58.12  ?  242 TYR   B CZ  1 
ATOM   3147 O  OH  . TYR   B 1 86  ? 18.853 42.533  24.713  1.00 63.43  ?  242 TYR   B OH  1 
ATOM   3148 N  N   . SER   B 1 87  ? 19.998 43.644  19.080  1.00 48.54  ?  243 SER   B N   1 
ATOM   3149 C  CA  . SER   B 1 87  ? 21.053 44.653  19.327  1.00 54.03  ?  243 SER   B CA  1 
ATOM   3150 C  C   . SER   B 1 87  ? 22.096 44.482  18.226  1.00 56.15  ?  243 SER   B C   1 
ATOM   3151 O  O   . SER   B 1 87  ? 21.713 44.488  17.037  1.00 56.93  ?  243 SER   B O   1 
ATOM   3152 C  CB  . SER   B 1 87  ? 21.647 44.537  20.693  1.00 62.61  ?  243 SER   B CB  1 
ATOM   3153 O  OG  . SER   B 1 87  ? 20.699 44.895  21.687  1.00 50.74  ?  243 SER   B OG  1 
ATOM   3154 N  N   . ASN   B 1 88  ? 23.356 44.352  18.593  1.00 47.99  ?  244 ASN   B N   1 
ATOM   3155 C  CA  . ASN   B 1 88  ? 24.371 44.067  17.545  1.00 55.40  ?  244 ASN   B CA  1 
ATOM   3156 C  C   . ASN   B 1 88  ? 25.128 42.831  18.024  1.00 41.40  ?  244 ASN   B C   1 
ATOM   3157 O  O   . ASN   B 1 88  ? 26.361 42.839  18.006  1.00 44.64  ?  244 ASN   B O   1 
ATOM   3158 C  CB  . ASN   B 1 88  ? 25.201 45.309  17.250  1.00 64.44  ?  244 ASN   B CB  1 
ATOM   3159 C  CG  . ASN   B 1 88  ? 24.364 46.410  16.643  1.00 71.44  ?  244 ASN   B CG  1 
ATOM   3160 O  OD1 . ASN   B 1 88  ? 23.996 46.337  15.467  1.00 75.08  ?  244 ASN   B OD1 1 
ATOM   3161 N  ND2 . ASN   B 1 88  ? 24.045 47.428  17.428  1.00 59.88  ?  244 ASN   B ND2 1 
ATOM   3162 N  N   . THR   B 1 89  ? 24.385 41.809  18.430  1.00 46.43  ?  245 THR   B N   1 
ATOM   3163 C  CA  . THR   B 1 89  ? 25.034 40.629  19.044  1.00 54.21  ?  245 THR   B CA  1 
ATOM   3164 C  C   . THR   B 1 89  ? 25.733 39.806  17.972  1.00 41.05  ?  245 THR   B C   1 
ATOM   3165 O  O   . THR   B 1 89  ? 26.610 39.032  18.351  1.00 37.02  ?  245 THR   B O   1 
ATOM   3166 C  CB  . THR   B 1 89  ? 23.983 39.817  19.804  1.00 43.74  ?  245 THR   B CB  1 
ATOM   3167 O  OG1 . THR   B 1 89  ? 22.915 39.571  18.895  1.00 45.16  ?  245 THR   B OG1 1 
ATOM   3168 C  CG2 . THR   B 1 89  ? 23.489 40.549  21.037  1.00 43.57  ?  245 THR   B CG2 1 
ATOM   3169 N  N   . ARG   B 1 90  ? 25.347 39.963  16.705  1.00 38.06  ?  246 ARG   B N   1 
ATOM   3170 C  CA  . ARG   B 1 90  ? 25.900 39.242  15.559  1.00 42.77  ?  246 ARG   B CA  1 
ATOM   3171 C  C   . ARG   B 1 90  ? 25.645 37.738  15.618  1.00 36.12  ?  246 ARG   B C   1 
ATOM   3172 O  O   . ARG   B 1 90  ? 25.782 37.049  14.601  1.00 38.39  ?  246 ARG   B O   1 
ATOM   3173 C  CB  . ARG   B 1 90  ? 27.402 39.518  15.423  1.00 38.54  ?  246 ARG   B CB  1 
ATOM   3174 C  CG  . ARG   B 1 90  ? 27.780 40.992  15.492  1.00 40.92  ?  246 ARG   B CG  1 
ATOM   3175 C  CD  . ARG   B 1 90  ? 27.956 41.593  14.105  1.00 51.84  ?  246 ARG   B CD  1 
ATOM   3176 N  NE  . ARG   B 1 90  ? 28.676 42.861  14.146  1.00 69.58  ?  246 ARG   B NE  1 
ATOM   3177 C  CZ  . ARG   B 1 90  ? 28.118 44.047  13.937  1.00 66.74  ?  246 ARG   B CZ  1 
ATOM   3178 N  NH1 . ARG   B 1 90  ? 26.829 44.167  13.664  1.00 50.96  ?  246 ARG   B NH1 1 
ATOM   3179 N  NH2 . ARG   B 1 90  ? 28.874 45.140  14.007  1.00 57.45  ?  246 ARG   B NH2 1 
ATOM   3180 N  N   . ALA   B 1 91  ? 25.273 37.214  16.789  1.00 39.96  ?  247 ALA   B N   1 
ATOM   3181 C  CA  . ALA   B 1 91  ? 24.979 35.796  16.936  1.00 34.65  ?  247 ALA   B CA  1 
ATOM   3182 C  C   . ALA   B 1 91  ? 23.528 35.500  17.285  1.00 31.06  ?  247 ALA   B C   1 
ATOM   3183 O  O   . ALA   B 1 91  ? 23.057 34.396  16.995  1.00 28.67  ?  247 ALA   B O   1 
ATOM   3184 C  CB  . ALA   B 1 91  ? 25.882 35.171  18.011  1.00 30.24  ?  247 ALA   B CB  1 
ATOM   3185 N  N   . TYR   B 1 92  ? 22.812 36.447  17.885  1.00 29.26  ?  248 TYR   B N   1 
ATOM   3186 C  CA  . TYR   B 1 92  ? 21.439 36.249  18.332  1.00 30.58  ?  248 TYR   B CA  1 
ATOM   3187 C  C   . TYR   B 1 92  ? 20.478 37.008  17.426  1.00 43.22  ?  248 TYR   B C   1 
ATOM   3188 O  O   . TYR   B 1 92  ? 20.760 38.138  17.014  1.00 41.54  ?  248 TYR   B O   1 
ATOM   3189 C  CB  . TYR   B 1 92  ? 21.266 36.709  19.782  1.00 39.28  ?  248 TYR   B CB  1 
ATOM   3190 C  CG  . TYR   B 1 92  ? 22.037 35.876  20.780  1.00 33.55  ?  248 TYR   B CG  1 
ATOM   3191 C  CD1 . TYR   B 1 92  ? 23.377 36.137  21.045  1.00 36.40  ?  248 TYR   B CD1 1 
ATOM   3192 C  CD2 . TYR   B 1 92  ? 21.428 34.829  21.457  1.00 38.14  ?  248 TYR   B CD2 1 
ATOM   3193 C  CE1 . TYR   B 1 92  ? 24.086 35.376  21.956  1.00 38.18  ?  248 TYR   B CE1 1 
ATOM   3194 C  CE2 . TYR   B 1 92  ? 22.130 34.063  22.370  1.00 33.81  ?  248 TYR   B CE2 1 
ATOM   3195 C  CZ  . TYR   B 1 92  ? 23.458 34.342  22.615  1.00 33.94  ?  248 TYR   B CZ  1 
ATOM   3196 O  OH  . TYR   B 1 92  ? 24.162 33.583  23.522  1.00 45.20  ?  248 TYR   B OH  1 
ATOM   3197 N  N   . TYR   B 1 93  ? 19.340 36.383  17.121  1.00 34.23  ?  249 TYR   B N   1 
ATOM   3198 C  CA  . TYR   B 1 93  ? 18.390 36.933  16.164  1.00 35.14  ?  249 TYR   B CA  1 
ATOM   3199 C  C   . TYR   B 1 93  ? 16.962 36.659  16.611  1.00 47.75  ?  249 TYR   B C   1 
ATOM   3200 O  O   . TYR   B 1 93  ? 16.690 35.691  17.327  1.00 44.18  ?  249 TYR   B O   1 
ATOM   3201 C  CB  . TYR   B 1 93  ? 18.589 36.339  14.757  1.00 39.73  ?  249 TYR   B CB  1 
ATOM   3202 C  CG  . TYR   B 1 93  ? 19.944 36.608  14.141  1.00 42.76  ?  249 TYR   B CG  1 
ATOM   3203 C  CD1 . TYR   B 1 93  ? 21.055 35.851  14.492  1.00 31.15  ?  249 TYR   B CD1 1 
ATOM   3204 C  CD2 . TYR   B 1 93  ? 20.108 37.612  13.197  1.00 36.75  ?  249 TYR   B CD2 1 
ATOM   3205 C  CE1 . TYR   B 1 93  ? 22.293 36.096  13.929  1.00 30.55  ?  249 TYR   B CE1 1 
ATOM   3206 C  CE2 . TYR   B 1 93  ? 21.340 37.862  12.628  1.00 42.58  ?  249 TYR   B CE2 1 
ATOM   3207 C  CZ  . TYR   B 1 93  ? 22.429 37.103  12.997  1.00 38.15  ?  249 TYR   B CZ  1 
ATOM   3208 O  OH  . TYR   B 1 93  ? 23.656 37.352  12.429  1.00 34.16  ?  249 TYR   B OH  1 
ATOM   3209 N  N   . PHE   B 1 94  ? 16.054 37.534  16.182  1.00 45.66  ?  250 PHE   B N   1 
ATOM   3210 C  CA  . PHE   B 1 94  ? 14.628 37.251  16.179  1.00 44.20  ?  250 PHE   B CA  1 
ATOM   3211 C  C   . PHE   B 1 94  ? 14.258 36.619  14.846  1.00 47.53  ?  250 PHE   B C   1 
ATOM   3212 O  O   . PHE   B 1 94  ? 14.744 37.041  13.788  1.00 50.33  ?  250 PHE   B O   1 
ATOM   3213 C  CB  . PHE   B 1 94  ? 13.800 38.522  16.375  1.00 51.20  ?  250 PHE   B CB  1 
ATOM   3214 C  CG  . PHE   B 1 94  ? 14.079 39.252  17.653  1.00 40.95  ?  250 PHE   B CG  1 
ATOM   3215 C  CD1 . PHE   B 1 94  ? 13.695 38.719  18.871  1.00 45.31  ?  250 PHE   B CD1 1 
ATOM   3216 C  CD2 . PHE   B 1 94  ? 14.699 40.490  17.633  1.00 47.54  ?  250 PHE   B CD2 1 
ATOM   3217 C  CE1 . PHE   B 1 94  ? 13.943 39.399  20.049  1.00 46.59  ?  250 PHE   B CE1 1 
ATOM   3218 C  CE2 . PHE   B 1 94  ? 14.948 41.176  18.804  1.00 54.61  ?  250 PHE   B CE2 1 
ATOM   3219 C  CZ  . PHE   B 1 94  ? 14.570 40.629  20.014  1.00 56.94  ?  250 PHE   B CZ  1 
ATOM   3220 N  N   . VAL   B 1 95  ? 13.383 35.619  14.905  1.00 42.18  ?  251 VAL   B N   1 
ATOM   3221 C  CA  . VAL   B 1 95  ? 12.896 34.917  13.725  1.00 44.35  ?  251 VAL   B CA  1 
ATOM   3222 C  C   . VAL   B 1 95  ? 11.527 35.477  13.362  1.00 60.61  ?  251 VAL   B C   1 
ATOM   3223 O  O   . VAL   B 1 95  ? 10.585 35.407  14.161  1.00 49.69  ?  251 VAL   B O   1 
ATOM   3224 C  CB  . VAL   B 1 95  ? 12.827 33.399  13.964  1.00 51.93  ?  251 VAL   B CB  1 
ATOM   3225 C  CG1 . VAL   B 1 95  ? 12.215 32.700  12.762  1.00 43.19  ?  251 VAL   B CG1 1 
ATOM   3226 C  CG2 . VAL   B 1 95  ? 14.213 32.841  14.250  1.00 41.20  ?  251 VAL   B CG2 1 
ATOM   3227 N  N   . LYS   B 1 96  ? 11.418 36.036  12.163  1.00 54.73  ?  252 LYS   B N   1 
ATOM   3228 C  CA  . LYS   B 1 96  ? 10.183 36.469  11.537  1.00 56.56  ?  252 LYS   B CA  1 
ATOM   3229 C  C   . LYS   B 1 96  ? 10.010 35.671  10.247  1.00 62.61  ?  252 LYS   B C   1 
ATOM   3230 O  O   . LYS   B 1 96  ? 10.872 34.875  9.865   1.00 54.54  ?  252 LYS   B O   1 
ATOM   3231 C  CB  . LYS   B 1 96  ? 10.213 37.974  11.251  1.00 49.80  ?  252 LYS   B CB  1 
ATOM   3232 C  CG  . LYS   B 1 96  ? 10.413 38.854  12.476  1.00 64.21  ?  252 LYS   B CG  1 
ATOM   3233 C  CD  . LYS   B 1 96  ? 10.406 40.327  12.088  1.00 71.67  ?  252 LYS   B CD  1 
ATOM   3234 C  CE  . LYS   B 1 96  ? 10.507 41.236  13.304  1.00 60.31  ?  252 LYS   B CE  1 
ATOM   3235 N  NZ  . LYS   B 1 96  ? 10.641 42.670  12.915  1.00 48.27  ?  252 LYS   B NZ  1 
ATOM   3236 N  N   . PHE   B 1 97  ? 8.912  35.918  9.542   1.00 58.07  ?  253 PHE   B N   1 
ATOM   3237 C  CA  . PHE   B 1 97  ? 8.575  35.115  8.378   1.00 66.42  ?  253 PHE   B CA  1 
ATOM   3238 C  C   . PHE   B 1 97  ? 8.257  36.001  7.184   1.00 66.62  ?  253 PHE   B C   1 
ATOM   3239 O  O   . PHE   B 1 97  ? 7.720  37.103  7.327   1.00 74.01  ?  253 PHE   B O   1 
ATOM   3240 C  CB  . PHE   B 1 97  ? 7.398  34.185  8.686   1.00 58.33  ?  253 PHE   B CB  1 
ATOM   3241 C  CG  . PHE   B 1 97  ? 7.671  33.231  9.814   1.00 59.37  ?  253 PHE   B CG  1 
ATOM   3242 C  CD1 . PHE   B 1 97  ? 7.438  33.606  11.127  1.00 50.56  ?  253 PHE   B CD1 1 
ATOM   3243 C  CD2 . PHE   B 1 97  ? 8.178  31.966  9.564   1.00 47.85  ?  253 PHE   B CD2 1 
ATOM   3244 C  CE1 . PHE   B 1 97  ? 7.694  32.737  12.168  1.00 50.47  ?  253 PHE   B CE1 1 
ATOM   3245 C  CE2 . PHE   B 1 97  ? 8.435  31.091  10.604  1.00 58.53  ?  253 PHE   B CE2 1 
ATOM   3246 C  CZ  . PHE   B 1 97  ? 8.194  31.478  11.906  1.00 50.04  ?  253 PHE   B CZ  1 
ATOM   3247 N  N   . LYS   B 1 98  ? 8.610  35.505  6.002   1.00 68.68  ?  254 LYS   B N   1 
ATOM   3248 C  CA  . LYS   B 1 98  ? 8.342  36.212  4.760   1.00 73.79  ?  254 LYS   B CA  1 
ATOM   3249 C  C   . LYS   B 1 98  ? 6.931  35.893  4.286   1.00 64.49  ?  254 LYS   B C   1 
ATOM   3250 O  O   . LYS   B 1 98  ? 6.482  36.375  3.247   1.00 82.45  ?  254 LYS   B O   1 
ATOM   3251 C  CB  . LYS   B 1 98  ? 9.365  35.834  3.689   1.00 58.48  ?  254 LYS   B CB  1 
ATOM   3252 N  N   . ASN   B 1 104 ? 1.564  28.991  7.086   1.00 59.64  ?  260 ASN   B N   1 
ATOM   3253 C  CA  . ASN   B 1 104 ? 2.679  28.965  8.023   1.00 71.41  ?  260 ASN   B CA  1 
ATOM   3254 C  C   . ASN   B 1 104 ? 2.300  28.049  9.185   1.00 69.92  ?  260 ASN   B C   1 
ATOM   3255 O  O   . ASN   B 1 104 ? 1.475  28.410  10.027  1.00 71.91  ?  260 ASN   B O   1 
ATOM   3256 C  CB  . ASN   B 1 104 ? 3.007  30.384  8.510   1.00 62.35  ?  260 ASN   B CB  1 
ATOM   3257 C  CG  . ASN   B 1 104 ? 4.295  30.460  9.333   1.00 73.82  ?  260 ASN   B CG  1 
ATOM   3258 O  OD1 . ASN   B 1 104 ? 4.833  31.547  9.541   1.00 86.04  ?  260 ASN   B OD1 1 
ATOM   3259 N  ND2 . ASN   B 1 104 ? 4.799  29.318  9.782   1.00 70.62  ?  260 ASN   B ND2 1 
ATOM   3260 N  N   . PRO   B 1 105 ? 2.902  26.857  9.229   1.00 55.26  ?  261 PRO   B N   1 
ATOM   3261 C  CA  . PRO   B 1 105 ? 2.586  25.916  10.315  1.00 61.04  ?  261 PRO   B CA  1 
ATOM   3262 C  C   . PRO   B 1 105 ? 3.088  26.368  11.675  1.00 66.02  ?  261 PRO   B C   1 
ATOM   3263 O  O   . PRO   B 1 105 ? 2.629  25.835  12.693  1.00 75.95  ?  261 PRO   B O   1 
ATOM   3264 C  CB  . PRO   B 1 105 ? 3.269  24.619  9.863   1.00 69.57  ?  261 PRO   B CB  1 
ATOM   3265 C  CG  . PRO   B 1 105 ? 4.396  25.079  8.997   1.00 78.44  ?  261 PRO   B CG  1 
ATOM   3266 C  CD  . PRO   B 1 105 ? 3.903  26.315  8.293   1.00 54.54  ?  261 PRO   B CD  1 
ATOM   3267 N  N   . LEU   B 1 106 ? 4.006  27.330  11.725  1.00 67.98  ?  262 LEU   B N   1 
ATOM   3268 C  CA  . LEU   B 1 106 ? 4.516  27.872  12.976  1.00 55.72  ?  262 LEU   B CA  1 
ATOM   3269 C  C   . LEU   B 1 106 ? 3.738  29.093  13.450  1.00 59.31  ?  262 LEU   B C   1 
ATOM   3270 O  O   . LEU   B 1 106 ? 4.131  29.714  14.442  1.00 68.76  ?  262 LEU   B O   1 
ATOM   3271 C  CB  . LEU   B 1 106 ? 5.996  28.232  12.831  1.00 51.17  ?  262 LEU   B CB  1 
ATOM   3272 C  CG  . LEU   B 1 106 ? 6.915  27.053  12.518  1.00 53.66  ?  262 LEU   B CG  1 
ATOM   3273 C  CD1 . LEU   B 1 106 ? 8.372  27.497  12.464  1.00 55.63  ?  262 LEU   B CD1 1 
ATOM   3274 C  CD2 . LEU   B 1 106 ? 6.706  25.953  13.544  1.00 64.24  ?  262 LEU   B CD2 1 
ATOM   3275 N  N   . SER   B 1 107 ? 2.643  29.443  12.768  1.00 65.95  ?  263 SER   B N   1 
ATOM   3276 C  CA  . SER   B 1 107 ? 1.879  30.633  13.120  1.00 57.07  ?  263 SER   B CA  1 
ATOM   3277 C  C   . SER   B 1 107 ? 1.221  30.522  14.488  1.00 61.96  ?  263 SER   B C   1 
ATOM   3278 O  O   . SER   B 1 107 ? 0.843  31.550  15.064  1.00 71.00  ?  263 SER   B O   1 
ATOM   3279 C  CB  . SER   B 1 107 ? 0.818  30.912  12.054  1.00 69.78  ?  263 SER   B CB  1 
ATOM   3280 O  OG  . SER   B 1 107 ? -0.210 29.936  12.087  1.00 81.64  ?  263 SER   B OG  1 
ATOM   3281 N  N   . GLN   B 1 108 ? 1.075  29.306  15.019  1.00 68.27  ?  264 GLN   B N   1 
ATOM   3282 C  CA  . GLN   B 1 108 ? 0.519  29.123  16.357  1.00 62.48  ?  264 GLN   B CA  1 
ATOM   3283 C  C   . GLN   B 1 108 ? 1.477  29.555  17.459  1.00 65.27  ?  264 GLN   B C   1 
ATOM   3284 O  O   . GLN   B 1 108 ? 1.030  29.781  18.589  1.00 64.65  ?  264 GLN   B O   1 
ATOM   3285 C  CB  . GLN   B 1 108 ? 0.123  27.659  16.567  1.00 60.23  ?  264 GLN   B CB  1 
ATOM   3286 C  CG  . GLN   B 1 108 ? 1.300  26.708  16.559  1.00 60.49  ?  264 GLN   B CG  1 
ATOM   3287 C  CD  . GLN   B 1 108 ? 0.894  25.270  16.774  1.00 65.16  ?  264 GLN   B CD  1 
ATOM   3288 O  OE1 . GLN   B 1 108 ? 0.612  24.851  17.898  1.00 71.05  ?  264 GLN   B OE1 1 
ATOM   3289 N  NE2 . GLN   B 1 108 ? 0.862  24.502  15.695  1.00 58.64  ?  264 GLN   B NE2 1 
ATOM   3290 N  N   . PHE   B 1 109 ? 2.773  29.662  17.166  1.00 60.35  ?  265 PHE   B N   1 
ATOM   3291 C  CA  . PHE   B 1 109 ? 3.766  30.130  18.125  1.00 54.24  ?  265 PHE   B CA  1 
ATOM   3292 C  C   . PHE   B 1 109 ? 4.120  31.598  17.930  1.00 64.20  ?  265 PHE   B C   1 
ATOM   3293 O  O   . PHE   B 1 109 ? 5.028  32.098  18.599  1.00 65.74  ?  265 PHE   B O   1 
ATOM   3294 C  CB  . PHE   B 1 109 ? 5.046  29.290  18.047  1.00 54.51  ?  265 PHE   B CB  1 
ATOM   3295 C  CG  . PHE   B 1 109 ? 4.796  27.818  18.022  1.00 55.90  ?  265 PHE   B CG  1 
ATOM   3296 C  CD1 . PHE   B 1 109 ? 4.174  27.199  19.089  1.00 53.94  ?  265 PHE   B CD1 1 
ATOM   3297 C  CD2 . PHE   B 1 109 ? 5.183  27.050  16.939  1.00 60.06  ?  265 PHE   B CD2 1 
ATOM   3298 C  CE1 . PHE   B 1 109 ? 3.932  25.860  19.077  1.00 53.78  ?  265 PHE   B CE1 1 
ATOM   3299 C  CE2 . PHE   B 1 109 ? 4.946  25.703  16.922  1.00 54.28  ?  265 PHE   B CE2 1 
ATOM   3300 C  CZ  . PHE   B 1 109 ? 4.317  25.105  17.994  1.00 57.42  ?  265 PHE   B CZ  1 
ATOM   3301 N  N   . LEU   B 1 110 ? 3.439  32.300  17.027  1.00 69.44  ?  266 LEU   B N   1 
ATOM   3302 C  CA  . LEU   B 1 110 ? 3.802  33.675  16.699  1.00 69.01  ?  266 LEU   B CA  1 
ATOM   3303 C  C   . LEU   B 1 110 ? 3.318  34.638  17.783  1.00 65.08  ?  266 LEU   B C   1 
ATOM   3304 O  O   . LEU   B 1 110 ? 2.120  34.691  18.083  1.00 80.48  ?  266 LEU   B O   1 
ATOM   3305 C  CB  . LEU   B 1 110 ? 3.209  34.064  15.346  1.00 63.14  ?  266 LEU   B CB  1 
ATOM   3306 C  CG  . LEU   B 1 110 ? 4.136  34.046  14.121  1.00 75.40  ?  266 LEU   B CG  1 
ATOM   3307 C  CD1 . LEU   B 1 110 ? 3.330  34.198  12.840  1.00 68.58  ?  266 LEU   B CD1 1 
ATOM   3308 C  CD2 . LEU   B 1 110 ? 5.203  35.129  14.214  1.00 74.94  ?  266 LEU   B CD2 1 
ATOM   3309 N  N   . GLU   B 1 111 ? 4.248  35.419  18.347  1.00 69.81  ?  267 GLU   B N   1 
ATOM   3310 C  CA  . GLU   B 1 111 ? 3.931  36.536  19.240  1.00 73.69  ?  267 GLU   B CA  1 
ATOM   3311 C  C   . GLU   B 1 111 ? 4.124  37.813  18.431  1.00 79.98  ?  267 GLU   B C   1 
ATOM   3312 O  O   . GLU   B 1 111 ? 5.239  38.325  18.303  1.00 75.16  ?  267 GLU   B O   1 
ATOM   3313 C  CB  . GLU   B 1 111 ? 4.814  36.512  20.485  1.00 64.17  ?  267 GLU   B CB  1 
ATOM   3314 N  N   . GLY   B 1 112 ? 3.023  38.324  17.873  1.00 72.51  ?  268 GLY   B N   1 
ATOM   3315 C  CA  . GLY   B 1 112 ? 3.097  39.416  16.915  1.00 67.85  ?  268 GLY   B CA  1 
ATOM   3316 C  C   . GLY   B 1 112 ? 3.675  38.959  15.591  1.00 71.36  ?  268 GLY   B C   1 
ATOM   3317 O  O   . GLY   B 1 112 ? 3.075  38.134  14.888  1.00 71.19  ?  268 GLY   B O   1 
ATOM   3318 N  N   . GLU   B 1 113 ? 4.861  39.463  15.246  1.00 73.44  ?  269 GLU   B N   1 
ATOM   3319 C  CA  . GLU   B 1 113 ? 5.521  39.105  13.996  1.00 75.98  ?  269 GLU   B CA  1 
ATOM   3320 C  C   . GLU   B 1 113 ? 6.764  38.264  14.223  1.00 71.60  ?  269 GLU   B C   1 
ATOM   3321 O  O   . GLU   B 1 113 ? 7.502  37.989  13.269  1.00 68.07  ?  269 GLU   B O   1 
ATOM   3322 C  CB  . GLU   B 1 113 ? 5.885  40.378  13.222  1.00 70.83  ?  269 GLU   B CB  1 
ATOM   3323 C  CG  . GLU   B 1 113 ? 4.686  41.072  12.588  1.00 80.99  ?  269 GLU   B CG  1 
ATOM   3324 C  CD  . GLU   B 1 113 ? 4.622  40.928  11.080  1.00 94.69  ?  269 GLU   B CD  1 
ATOM   3325 O  OE1 . GLU   B 1 113 ? 5.660  41.086  10.404  1.00 82.64  ?  269 GLU   B OE1 1 
ATOM   3326 O  OE2 . GLU   B 1 113 ? 3.517  40.651  10.571  1.00 84.40  -1 269 GLU   B OE2 1 
ATOM   3327 N  N   . ILE   B 1 114 ? 7.002  37.847  15.464  1.00 63.87  ?  270 ILE   B N   1 
ATOM   3328 C  CA  . ILE   B 1 114 ? 8.225  37.170  15.870  1.00 70.20  ?  270 ILE   B CA  1 
ATOM   3329 C  C   . ILE   B 1 114 ? 7.877  35.781  16.386  1.00 68.44  ?  270 ILE   B C   1 
ATOM   3330 O  O   . ILE   B 1 114 ? 6.899  35.607  17.124  1.00 64.99  ?  270 ILE   B O   1 
ATOM   3331 C  CB  . ILE   B 1 114 ? 8.980  37.988  16.941  1.00 61.13  ?  270 ILE   B CB  1 
ATOM   3332 C  CG1 . ILE   B 1 114 ? 9.836  39.088  16.294  1.00 61.01  ?  270 ILE   B CG1 1 
ATOM   3333 C  CG2 . ILE   B 1 114 ? 9.791  37.088  17.867  1.00 59.40  ?  270 ILE   B CG2 1 
ATOM   3334 C  CD1 . ILE   B 1 114 ? 9.872  40.376  17.086  1.00 61.73  ?  270 ILE   B CD1 1 
ATOM   3335 N  N   . LEU   B 1 115 ? 8.676  34.792  15.994  1.00 61.59  ?  271 LEU   B N   1 
ATOM   3336 C  CA  . LEU   B 1 115 ? 8.469  33.424  16.454  1.00 57.12  ?  271 LEU   B CA  1 
ATOM   3337 C  C   . LEU   B 1 115 ? 8.890  33.297  17.916  1.00 58.24  ?  271 LEU   B C   1 
ATOM   3338 O  O   . LEU   B 1 115 ? 10.025 33.629  18.274  1.00 64.91  ?  271 LEU   B O   1 
ATOM   3339 C  CB  . LEU   B 1 115 ? 9.255  32.445  15.580  1.00 44.66  ?  271 LEU   B CB  1 
ATOM   3340 C  CG  . LEU   B 1 115 ? 9.178  30.956  15.923  1.00 62.09  ?  271 LEU   B CG  1 
ATOM   3341 C  CD1 . LEU   B 1 115 ? 7.784  30.394  15.679  1.00 61.87  ?  271 LEU   B CD1 1 
ATOM   3342 C  CD2 . LEU   B 1 115 ? 10.227 30.170  15.144  1.00 45.28  ?  271 LEU   B CD2 1 
ATOM   3343 N  N   . SER   B 1 116 ? 7.979  32.815  18.759  1.00 52.62  ?  272 SER   B N   1 
ATOM   3344 C  CA  . SER   B 1 116 ? 8.257  32.692  20.186  1.00 54.63  ?  272 SER   B CA  1 
ATOM   3345 C  C   . SER   B 1 116 ? 9.025  31.406  20.462  1.00 54.86  ?  272 SER   B C   1 
ATOM   3346 O  O   . SER   B 1 116 ? 8.505  30.306  20.244  1.00 52.90  ?  272 SER   B O   1 
ATOM   3347 C  CB  . SER   B 1 116 ? 6.962  32.721  20.994  1.00 63.07  ?  272 SER   B CB  1 
ATOM   3348 O  OG  . SER   B 1 116 ? 7.203  32.368  22.345  1.00 57.17  ?  272 SER   B OG  1 
ATOM   3349 N  N   . ALA   B 1 117 ? 10.264 31.546  20.937  1.00 52.16  ?  273 ALA   B N   1 
ATOM   3350 C  CA  . ALA   B 1 117 ? 11.015 30.377  21.381  1.00 48.57  ?  273 ALA   B CA  1 
ATOM   3351 C  C   . ALA   B 1 117 ? 10.307 29.686  22.539  1.00 58.45  ?  273 ALA   B C   1 
ATOM   3352 O  O   . ALA   B 1 117 ? 10.308 28.453  22.630  1.00 49.39  ?  273 ALA   B O   1 
ATOM   3353 C  CB  . ALA   B 1 117 ? 12.433 30.783  21.783  1.00 50.90  ?  273 ALA   B CB  1 
ATOM   3354 N  N   . SER   B 1 118 ? 9.671  30.467  23.417  1.00 50.26  ?  274 SER   B N   1 
ATOM   3355 C  CA  . SER   B 1 118 ? 9.021  29.896  24.593  1.00 59.23  ?  274 SER   B CA  1 
ATOM   3356 C  C   . SER   B 1 118 ? 7.859  28.988  24.204  1.00 61.19  ?  274 SER   B C   1 
ATOM   3357 O  O   . SER   B 1 118 ? 7.758  27.858  24.687  1.00 62.69  ?  274 SER   B O   1 
ATOM   3358 C  CB  . SER   B 1 118 ? 8.546  31.015  25.523  1.00 51.28  ?  274 SER   B CB  1 
ATOM   3359 O  OG  . SER   B 1 118 ? 9.644  31.704  26.094  1.00 61.83  ?  274 SER   B OG  1 
ATOM   3360 N  N   . LYS   B 1 119 ? 6.972  29.463  23.325  1.00 53.34  ?  275 LYS   B N   1 
ATOM   3361 C  CA  . LYS   B 1 119 ? 5.801  28.671  22.952  1.00 57.94  ?  275 LYS   B CA  1 
ATOM   3362 C  C   . LYS   B 1 119 ? 6.195  27.435  22.149  1.00 57.25  ?  275 LYS   B C   1 
ATOM   3363 O  O   . LYS   B 1 119 ? 5.692  26.328  22.402  1.00 61.20  ?  275 LYS   B O   1 
ATOM   3364 C  CB  . LYS   B 1 119 ? 4.819  29.539  22.164  1.00 54.10  ?  275 LYS   B CB  1 
ATOM   3365 C  CG  . LYS   B 1 119 ? 4.365  30.791  22.908  1.00 57.86  ?  275 LYS   B CG  1 
ATOM   3366 C  CD  . LYS   B 1 119 ? 2.921  31.153  22.588  1.00 65.73  ?  275 LYS   B CD  1 
ATOM   3367 C  CE  . LYS   B 1 119 ? 2.356  32.116  23.622  1.00 59.60  ?  275 LYS   B CE  1 
ATOM   3368 N  NZ  . LYS   B 1 119 ? 1.446  33.129  23.019  1.00 72.10  ?  275 LYS   B NZ  1 
ATOM   3369 N  N   . MET   B 1 120 ? 7.087  27.607  21.167  1.00 58.62  ?  276 MET   B N   1 
ATOM   3370 C  CA  . MET   B 1 120 ? 7.558  26.472  20.382  1.00 59.59  ?  276 MET   B CA  1 
ATOM   3371 C  C   . MET   B 1 120 ? 8.220  25.428  21.270  1.00 46.99  ?  276 MET   B C   1 
ATOM   3372 O  O   . MET   B 1 120 ? 7.956  24.226  21.133  1.00 48.17  ?  276 MET   B O   1 
ATOM   3373 C  CB  . MET   B 1 120 ? 8.524  26.950  19.297  1.00 45.41  ?  276 MET   B CB  1 
ATOM   3374 C  CG  . MET   B 1 120 ? 8.423  26.176  17.994  1.00 49.16  ?  276 MET   B CG  1 
ATOM   3375 S  SD  . MET   B 1 120 ? 9.536  26.792  16.717  1.00 52.20  ?  276 MET   B SD  1 
ATOM   3376 C  CE  . MET   B 1 120 ? 9.581  25.385  15.610  1.00 43.03  ?  276 MET   B CE  1 
ATOM   3377 N  N   . LEU   B 1 121 ? 9.069  25.870  22.203  1.00 48.71  ?  277 LEU   B N   1 
ATOM   3378 C  CA  . LEU   B 1 121 ? 9.711  24.930  23.112  1.00 64.64  ?  277 LEU   B CA  1 
ATOM   3379 C  C   . LEU   B 1 121 ? 8.694  24.252  24.018  1.00 60.83  ?  277 LEU   B C   1 
ATOM   3380 O  O   . LEU   B 1 121 ? 8.796  23.050  24.278  1.00 57.93  ?  277 LEU   B O   1 
ATOM   3381 C  CB  . LEU   B 1 121 ? 10.771 25.641  23.950  1.00 55.48  ?  277 LEU   B CB  1 
ATOM   3382 C  CG  . LEU   B 1 121 ? 12.097 25.936  23.252  1.00 54.30  ?  277 LEU   B CG  1 
ATOM   3383 C  CD1 . LEU   B 1 121 ? 12.939 26.883  24.094  1.00 40.30  ?  277 LEU   B CD1 1 
ATOM   3384 C  CD2 . LEU   B 1 121 ? 12.840 24.649  22.963  1.00 46.41  ?  277 LEU   B CD2 1 
ATOM   3385 N  N   . SER   B 1 122 ? 7.721  25.011  24.529  1.00 48.28  ?  278 SER   B N   1 
ATOM   3386 C  CA  . SER   B 1 122 ? 6.706  24.427  25.399  1.00 57.44  ?  278 SER   B CA  1 
ATOM   3387 C  C   . SER   B 1 122 ? 5.986  23.288  24.696  1.00 60.94  ?  278 SER   B C   1 
ATOM   3388 O  O   . SER   B 1 122 ? 5.819  22.201  25.263  1.00 59.05  ?  278 SER   B O   1 
ATOM   3389 C  CB  . SER   B 1 122 ? 5.713  25.502  25.839  1.00 58.63  ?  278 SER   B CB  1 
ATOM   3390 O  OG  . SER   B 1 122 ? 6.093  26.072  27.079  1.00 78.50  ?  278 SER   B OG  1 
ATOM   3391 N  N   . LYS   B 1 123 ? 5.579  23.509  23.445  1.00 56.77  ?  279 LYS   B N   1 
ATOM   3392 C  CA  . LYS   B 1 123 ? 4.908  22.441  22.709  1.00 61.14  ?  279 LYS   B CA  1 
ATOM   3393 C  C   . LYS   B 1 123 ? 5.857  21.276  22.438  1.00 51.32  ?  279 LYS   B C   1 
ATOM   3394 O  O   . LYS   B 1 123 ? 5.471  20.108  22.580  1.00 56.63  ?  279 LYS   B O   1 
ATOM   3395 C  CB  . LYS   B 1 123 ? 4.327  22.984  21.406  1.00 59.61  ?  279 LYS   B CB  1 
ATOM   3396 C  CG  . LYS   B 1 123 ? 3.755  21.905  20.512  1.00 54.36  ?  279 LYS   B CG  1 
ATOM   3397 C  CD  . LYS   B 1 123 ? 2.372  22.285  20.023  1.00 56.75  ?  279 LYS   B CD  1 
ATOM   3398 C  CE  . LYS   B 1 123 ? 1.862  21.283  19.010  1.00 71.96  ?  279 LYS   B CE  1 
ATOM   3399 N  NZ  . LYS   B 1 123 ? 0.818  21.854  18.116  1.00 59.42  ?  279 LYS   B NZ  1 
ATOM   3400 N  N   . PHE   B 1 124 ? 7.098  21.578  22.042  1.00 49.61  ?  280 PHE   B N   1 
ATOM   3401 C  CA  . PHE   B 1 124 ? 8.102  20.545  21.794  1.00 52.18  ?  280 PHE   B CA  1 
ATOM   3402 C  C   . PHE   B 1 124 ? 8.237  19.607  22.994  1.00 53.09  ?  280 PHE   B C   1 
ATOM   3403 O  O   . PHE   B 1 124 ? 8.084  18.381  22.867  1.00 50.22  ?  280 PHE   B O   1 
ATOM   3404 C  CB  . PHE   B 1 124 ? 9.432  21.236  21.458  1.00 50.77  ?  280 PHE   B CB  1 
ATOM   3405 C  CG  . PHE   B 1 124 ? 10.542 20.310  21.035  1.00 47.53  ?  280 PHE   B CG  1 
ATOM   3406 C  CD1 . PHE   B 1 124 ? 10.530 19.720  19.781  1.00 43.24  ?  280 PHE   B CD1 1 
ATOM   3407 C  CD2 . PHE   B 1 124 ? 11.637 20.095  21.859  1.00 42.16  ?  280 PHE   B CD2 1 
ATOM   3408 C  CE1 . PHE   B 1 124 ? 11.561 18.893  19.376  1.00 42.68  ?  280 PHE   B CE1 1 
ATOM   3409 C  CE2 . PHE   B 1 124 ? 12.676 19.273  21.458  1.00 40.71  ?  280 PHE   B CE2 1 
ATOM   3410 C  CZ  . PHE   B 1 124 ? 12.636 18.669  20.214  1.00 53.55  ?  280 PHE   B CZ  1 
ATOM   3411 N  N   . ARG   B 1 125 ? 8.481  20.173  24.181  1.00 56.84  ?  281 ARG   B N   1 
ATOM   3412 C  CA  . ARG   B 1 125 ? 8.637  19.342  25.371  1.00 51.62  ?  281 ARG   B CA  1 
ATOM   3413 C  C   . ARG   B 1 125 ? 7.334  18.678  25.790  1.00 53.03  ?  281 ARG   B C   1 
ATOM   3414 O  O   . ARG   B 1 125 ? 7.369  17.579  26.338  1.00 54.36  ?  281 ARG   B O   1 
ATOM   3415 C  CB  . ARG   B 1 125 ? 9.190  20.134  26.556  1.00 64.84  ?  281 ARG   B CB  1 
ATOM   3416 C  CG  . ARG   B 1 125 ? 10.083 21.300  26.227  1.00 69.67  ?  281 ARG   B CG  1 
ATOM   3417 C  CD  . ARG   B 1 125 ? 10.338 22.130  27.474  1.00 62.09  ?  281 ARG   B CD  1 
ATOM   3418 N  NE  . ARG   B 1 125 ? 10.907 21.321  28.547  1.00 75.10  ?  281 ARG   B NE  1 
ATOM   3419 C  CZ  . ARG   B 1 125 ? 10.255 20.962  29.645  1.00 69.77  ?  281 ARG   B CZ  1 
ATOM   3420 N  NH1 . ARG   B 1 125 ? 8.995  21.313  29.847  1.00 73.57  ?  281 ARG   B NH1 1 
ATOM   3421 N  NH2 . ARG   B 1 125 ? 10.879 20.223  30.559  1.00 73.10  ?  281 ARG   B NH2 1 
ATOM   3422 N  N   . LYS   B 1 126 ? 6.183  19.317  25.569  1.00 52.56  ?  282 LYS   B N   1 
ATOM   3423 C  CA  . LYS   B 1 126 ? 4.919  18.673  25.915  1.00 55.16  ?  282 LYS   B CA  1 
ATOM   3424 C  C   . LYS   B 1 126 ? 4.734  17.386  25.118  1.00 57.28  ?  282 LYS   B C   1 
ATOM   3425 O  O   . LYS   B 1 126 ? 4.421  16.321  25.678  1.00 60.26  ?  282 LYS   B O   1 
ATOM   3426 C  CB  . LYS   B 1 126 ? 3.769  19.642  25.650  1.00 59.05  ?  282 LYS   B CB  1 
ATOM   3427 C  CG  . LYS   B 1 126 ? 2.594  19.507  26.569  1.00 65.68  ?  282 LYS   B CG  1 
ATOM   3428 C  CD  . LYS   B 1 126 ? 1.327  19.958  25.884  1.00 61.84  ?  282 LYS   B CD  1 
ATOM   3429 C  CE  . LYS   B 1 126 ? 0.401  20.462  26.943  1.00 79.96  ?  282 LYS   B CE  1 
ATOM   3430 N  NZ  . LYS   B 1 126 ? 0.481  19.486  28.052  1.00 80.67  ?  282 LYS   B NZ  1 
ATOM   3431 N  N   . ILE   B 1 127 ? 4.927  17.470  23.799  1.00 61.21  ?  283 ILE   B N   1 
ATOM   3432 C  CA  . ILE   B 1 127 ? 4.823  16.286  22.949  1.00 55.06  ?  283 ILE   B CA  1 
ATOM   3433 C  C   . ILE   B 1 127 ? 5.824  15.226  23.393  1.00 60.46  ?  283 ILE   B C   1 
ATOM   3434 O  O   . ILE   B 1 127 ? 5.483  14.041  23.536  1.00 63.89  ?  283 ILE   B O   1 
ATOM   3435 C  CB  . ILE   B 1 127 ? 5.026  16.666  21.471  1.00 59.65  ?  283 ILE   B CB  1 
ATOM   3436 C  CG1 . ILE   B 1 127 ? 4.145  17.862  21.091  1.00 62.39  ?  283 ILE   B CG1 1 
ATOM   3437 C  CG2 . ILE   B 1 127 ? 4.743  15.471  20.579  1.00 54.68  ?  283 ILE   B CG2 1 
ATOM   3438 C  CD1 . ILE   B 1 127 ? 3.879  17.998  19.602  1.00 75.76  ?  283 ILE   B CD1 1 
ATOM   3439 N  N   . ILE   B 1 128 ? 7.078  15.635  23.623  1.00 61.12  ?  284 ILE   B N   1 
ATOM   3440 C  CA  . ILE   B 1 128 ? 8.090  14.658  24.018  1.00 50.65  ?  284 ILE   B CA  1 
ATOM   3441 C  C   . ILE   B 1 128 ? 7.724  14.005  25.345  1.00 58.80  ?  284 ILE   B C   1 
ATOM   3442 O  O   . ILE   B 1 128 ? 7.867  12.793  25.505  1.00 52.87  ?  284 ILE   B O   1 
ATOM   3443 C  CB  . ILE   B 1 128 ? 9.488  15.302  24.065  1.00 55.73  ?  284 ILE   B CB  1 
ATOM   3444 C  CG1 . ILE   B 1 128 ? 10.098 15.323  22.667  1.00 53.81  ?  284 ILE   B CG1 1 
ATOM   3445 C  CG2 . ILE   B 1 128 ? 10.408 14.535  25.007  1.00 47.46  ?  284 ILE   B CG2 1 
ATOM   3446 C  CD1 . ILE   B 1 128 ? 10.885 16.556  22.387  1.00 45.04  ?  284 ILE   B CD1 1 
ATOM   3447 N  N   . LYS   B 1 129 ? 7.232  14.786  26.308  1.00 53.13  ?  285 LYS   B N   1 
ATOM   3448 C  CA  . LYS   B 1 129 ? 6.886  14.229  27.612  1.00 60.47  ?  285 LYS   B CA  1 
ATOM   3449 C  C   . LYS   B 1 129 ? 5.769  13.206  27.490  1.00 69.39  ?  285 LYS   B C   1 
ATOM   3450 O  O   . LYS   B 1 129 ? 5.826  12.133  28.100  1.00 74.27  ?  285 LYS   B O   1 
ATOM   3451 C  CB  . LYS   B 1 129 ? 6.486  15.347  28.574  1.00 55.32  ?  285 LYS   B CB  1 
ATOM   3452 C  CG  . LYS   B 1 129 ? 6.021  14.846  29.932  1.00 73.34  ?  285 LYS   B CG  1 
ATOM   3453 C  CD  . LYS   B 1 129 ? 6.660  15.639  31.062  1.00 82.02  ?  285 LYS   B CD  1 
ATOM   3454 C  CE  . LYS   B 1 129 ? 6.056  17.030  31.167  1.00 82.70  ?  285 LYS   B CE  1 
ATOM   3455 N  NZ  . LYS   B 1 129 ? 6.969  17.998  31.837  1.00 83.65  ?  285 LYS   B NZ  1 
ATOM   3456 N  N   . GLU   B 1 130 ? 4.739  13.518  26.700  1.00 67.27  ?  286 GLU   B N   1 
ATOM   3457 C  CA  . GLU   B 1 130 ? 3.647  12.561  26.543  1.00 71.60  ?  286 GLU   B CA  1 
ATOM   3458 C  C   . GLU   B 1 130 ? 4.121  11.290  25.848  1.00 65.43  ?  286 GLU   B C   1 
ATOM   3459 O  O   . GLU   B 1 130 ? 3.655  10.190  26.170  1.00 66.43  ?  286 GLU   B O   1 
ATOM   3460 C  CB  . GLU   B 1 130 ? 2.483  13.198  25.786  1.00 63.75  ?  286 GLU   B CB  1 
ATOM   3461 C  CG  . GLU   B 1 130 ? 1.769  14.277  26.581  1.00 74.35  ?  286 GLU   B CG  1 
ATOM   3462 C  CD  . GLU   B 1 130 ? 0.505  14.761  25.902  1.00 92.51  ?  286 GLU   B CD  1 
ATOM   3463 O  OE1 . GLU   B 1 130 ? 0.167  14.230  24.824  1.00 93.43  ?  286 GLU   B OE1 1 
ATOM   3464 O  OE2 . GLU   B 1 130 ? -0.151 15.672  26.450  1.00 88.98  -1 286 GLU   B OE2 1 
ATOM   3465 N  N   . GLU   B 1 131 ? 5.062  11.413  24.908  1.00 61.13  ?  287 GLU   B N   1 
ATOM   3466 C  CA  . GLU   B 1 131 ? 5.581  10.215  24.248  1.00 64.15  ?  287 GLU   B CA  1 
ATOM   3467 C  C   . GLU   B 1 131 ? 6.480  9.409   25.182  1.00 69.47  ?  287 GLU   B C   1 
ATOM   3468 O  O   . GLU   B 1 131 ? 6.428  8.173   25.195  1.00 83.85  ?  287 GLU   B O   1 
ATOM   3469 C  CB  . GLU   B 1 131 ? 6.334  10.603  22.976  1.00 60.93  ?  287 GLU   B CB  1 
ATOM   3470 C  CG  . GLU   B 1 131 ? 6.890  9.423   22.197  1.00 67.53  ?  287 GLU   B CG  1 
ATOM   3471 C  CD  . GLU   B 1 131 ? 5.811  8.640   21.480  1.00 77.03  ?  287 GLU   B CD  1 
ATOM   3472 O  OE1 . GLU   B 1 131 ? 4.710  9.192   21.273  1.00 82.88  ?  287 GLU   B OE1 1 
ATOM   3473 O  OE2 . GLU   B 1 131 ? 6.066  7.471   21.120  1.00 66.66  -1 287 GLU   B OE2 1 
ATOM   3474 N  N   . ILE   B 1 132 ? 7.310  10.096  25.970  1.00 70.33  ?  288 ILE   B N   1 
ATOM   3475 C  CA  . ILE   B 1 132 ? 8.228  9.457   26.910  1.00 75.85  ?  288 ILE   B CA  1 
ATOM   3476 C  C   . ILE   B 1 132 ? 7.476  8.602   27.922  1.00 78.08  ?  288 ILE   B C   1 
ATOM   3477 O  O   . ILE   B 1 132 ? 7.984  7.566   28.372  1.00 83.09  ?  288 ILE   B O   1 
ATOM   3478 C  CB  . ILE   B 1 132 ? 9.092  10.544  27.591  1.00 70.95  ?  288 ILE   B CB  1 
ATOM   3479 C  CG1 . ILE   B 1 132 ? 10.133 11.090  26.607  1.00 57.38  ?  288 ILE   B CG1 1 
ATOM   3480 C  CG2 . ILE   B 1 132 ? 9.729  10.048  28.882  1.00 72.80  ?  288 ILE   B CG2 1 
ATOM   3481 C  CD1 . ILE   B 1 132 ? 10.892 10.008  25.878  1.00 74.10  ?  288 ILE   B CD1 1 
ATOM   3482 N  N   . ASN   B 1 133 ? 6.250  8.997   28.268  1.00 86.22  ?  289 ASN   B N   1 
ATOM   3483 C  CA  . ASN   B 1 133 ? 5.491  8.300   29.301  1.00 78.84  ?  289 ASN   B CA  1 
ATOM   3484 C  C   . ASN   B 1 133 ? 5.038  6.912   28.859  1.00 84.73  ?  289 ASN   B C   1 
ATOM   3485 O  O   . ASN   B 1 133 ? 4.698  6.086   29.714  1.00 84.99  ?  289 ASN   B O   1 
ATOM   3486 C  CB  . ASN   B 1 133 ? 4.286  9.149   29.717  1.00 79.60  ?  289 ASN   B CB  1 
ATOM   3487 C  CG  . ASN   B 1 133 ? 4.676  10.337  30.594  1.00 87.85  ?  289 ASN   B CG  1 
ATOM   3488 O  OD1 . ASN   B 1 133 ? 5.718  10.325  31.252  1.00 82.97  ?  289 ASN   B OD1 1 
ATOM   3489 N  ND2 . ASN   B 1 133 ? 3.834  11.367  30.607  1.00 80.85  ?  289 ASN   B ND2 1 
ATOM   3490 N  N   . ASP   B 1 134 ? 5.030  6.634   27.559  1.00 87.87  ?  290 ASP   B N   1 
ATOM   3491 C  CA  . ASP   B 1 134 ? 4.673  5.311   27.060  1.00 89.34  ?  290 ASP   B CA  1 
ATOM   3492 C  C   . ASP   B 1 134 ? 5.932  4.467   26.881  1.00 94.50  ?  290 ASP   B C   1 
ATOM   3493 O  O   . ASP   B 1 134 ? 5.958  3.289   27.239  1.00 112.26 ?  290 ASP   B O   1 
ATOM   3494 C  CB  . ASP   B 1 134 ? 3.910  5.420   25.737  1.00 86.62  ?  290 ASP   B CB  1 
ATOM   3495 C  CG  . ASP   B 1 134 ? 3.836  4.101   24.993  1.00 95.08  ?  290 ASP   B CG  1 
ATOM   3496 O  OD1 . ASP   B 1 134 ? 3.662  3.057   25.654  1.00 95.34  ?  290 ASP   B OD1 1 
ATOM   3497 O  OD2 . ASP   B 1 134 ? 3.947  4.107   23.748  1.00 99.36  -1 290 ASP   B OD2 1 
ATOM   3498 N  N   . VAL   B 1 140 ? 12.043 5.483   30.659  1.00 67.19  ?  296 VAL   B N   1 
ATOM   3499 C  CA  . VAL   B 1 140 ? 12.667 6.774   30.420  1.00 66.08  ?  296 VAL   B CA  1 
ATOM   3500 C  C   . VAL   B 1 140 ? 12.053 7.811   31.351  1.00 67.10  ?  296 VAL   B C   1 
ATOM   3501 O  O   . VAL   B 1 140 ? 10.906 7.688   31.788  1.00 81.31  ?  296 VAL   B O   1 
ATOM   3502 C  CB  . VAL   B 1 140 ? 12.524 7.196   28.940  1.00 63.33  ?  296 VAL   B CB  1 
ATOM   3503 C  CG1 . VAL   B 1 140 ? 13.524 6.443   28.085  1.00 78.01  ?  296 VAL   B CG1 1 
ATOM   3504 C  CG2 . VAL   B 1 140 ? 11.123 6.882   28.445  1.00 65.37  ?  296 VAL   B CG2 1 
ATOM   3505 N  N   . ILE   B 1 141 ? 12.845 8.839   31.664  1.00 64.65  ?  297 ILE   B N   1 
ATOM   3506 C  CA  . ILE   B 1 141 ? 12.400 9.905   32.559  1.00 64.21  ?  297 ILE   B CA  1 
ATOM   3507 C  C   . ILE   B 1 141 ? 12.959 11.236  32.079  1.00 57.59  ?  297 ILE   B C   1 
ATOM   3508 O  O   . ILE   B 1 141 ? 14.037 11.305  31.492  1.00 68.66  ?  297 ILE   B O   1 
ATOM   3509 C  CB  . ILE   B 1 141 ? 12.817 9.642   34.024  1.00 71.95  ?  297 ILE   B CB  1 
ATOM   3510 N  N   . MET   B 1 142 ? 12.228 12.306  32.369  1.00 61.51  ?  298 MET   B N   1 
ATOM   3511 C  CA  . MET   B 1 142 ? 12.549 13.635  31.874  1.00 61.51  ?  298 MET   B CA  1 
ATOM   3512 C  C   . MET   B 1 142 ? 13.064 14.517  33.004  1.00 64.29  ?  298 MET   B C   1 
ATOM   3513 O  O   . MET   B 1 142 ? 12.506 14.520  34.106  1.00 68.17  ?  298 MET   B O   1 
ATOM   3514 C  CB  . MET   B 1 142 ? 11.319 14.278  31.228  1.00 60.71  ?  298 MET   B CB  1 
ATOM   3515 N  N   . LYS   B 1 143 ? 14.135 15.256  32.729  1.00 54.68  ?  299 LYS   B N   1 
ATOM   3516 C  CA  . LYS   B 1 143 ? 14.648 16.261  33.648  1.00 76.55  ?  299 LYS   B CA  1 
ATOM   3517 C  C   . LYS   B 1 143 ? 14.301 17.649  33.129  1.00 76.07  ?  299 LYS   B C   1 
ATOM   3518 O  O   . LYS   B 1 143 ? 14.218 17.868  31.916  1.00 85.62  ?  299 LYS   B O   1 
ATOM   3519 C  CB  . LYS   B 1 143 ? 16.163 16.132  33.827  1.00 54.58  ?  299 LYS   B CB  1 
ATOM   3520 N  N   . ARG   B 1 144 ? 14.082 18.575  34.056  1.00 80.22  ?  300 ARG   B N   1 
ATOM   3521 C  CA  . ARG   B 1 144 ? 13.814 19.968  33.722  1.00 77.74  ?  300 ARG   B CA  1 
ATOM   3522 C  C   . ARG   B 1 144 ? 15.124 20.742  33.691  1.00 74.05  ?  300 ARG   B C   1 
ATOM   3523 O  O   . ARG   B 1 144 ? 16.110 20.321  34.296  1.00 86.16  ?  300 ARG   B O   1 
ATOM   3524 C  CB  . ARG   B 1 144 ? 12.846 20.590  34.732  1.00 69.29  ?  300 ARG   B CB  1 
ATOM   3525 N  N   . GLY   B 1 148 ? 16.825 26.246  27.582  1.00 57.66  ?  304 GLY   B N   1 
ATOM   3526 C  CA  . GLY   B 1 148 ? 16.430 26.621  26.209  1.00 60.48  ?  304 GLY   B CA  1 
ATOM   3527 C  C   . GLY   B 1 148 ? 17.102 25.773  25.142  1.00 53.01  ?  304 GLY   B C   1 
ATOM   3528 O  O   . GLY   B 1 148 ? 16.386 25.064  24.419  1.00 45.23  ?  304 GLY   B O   1 
ATOM   3529 N  N   . SER   B 1 149 ? 18.429 25.851  25.039  1.00 52.81  ?  305 SER   B N   1 
ATOM   3530 C  CA  . SER   B 1 149 ? 19.136 25.155  23.933  1.00 49.55  ?  305 SER   B CA  1 
ATOM   3531 C  C   . SER   B 1 149 ? 19.028 23.646  24.131  1.00 72.01  ?  305 SER   B C   1 
ATOM   3532 O  O   . SER   B 1 149 ? 18.400 23.010  23.261  1.00 86.61  ?  305 SER   B O   1 
ATOM   3533 C  CB  . SER   B 1 149 ? 20.539 25.612  23.771  1.00 56.83  ?  305 SER   B CB  1 
ATOM   3534 O  OG  . SER   B 1 149 ? 21.178 24.893  22.729  1.00 79.63  ?  305 SER   B OG  1 
ATOM   3535 N  N   . PRO   B 1 150 ? 19.550 23.015  25.204  1.00 73.49  ?  306 PRO   B N   1 
ATOM   3536 C  CA  . PRO   B 1 150 ? 19.304 21.595  25.390  1.00 66.76  ?  306 PRO   B CA  1 
ATOM   3537 C  C   . PRO   B 1 150 ? 17.882 21.630  25.890  1.00 57.68  ?  306 PRO   B C   1 
ATOM   3538 O  O   . PRO   B 1 150 ? 17.665 21.472  27.098  1.00 78.74  ?  306 PRO   B O   1 
ATOM   3539 C  CB  . PRO   B 1 150 ? 20.320 21.098  26.404  1.00 61.50  ?  306 PRO   B CB  1 
ATOM   3540 C  CG  . PRO   B 1 150 ? 21.163 22.324  26.704  1.00 76.39  ?  306 PRO   B CG  1 
ATOM   3541 C  CD  . PRO   B 1 150 ? 20.392 23.560  26.252  1.00 63.29  ?  306 PRO   B CD  1 
ATOM   3542 N  N   . ALA   B 1 151 ? 16.930 21.836  24.986  1.00 52.74  ?  307 ALA   B N   1 
ATOM   3543 C  CA  . ALA   B 1 151 ? 15.498 21.932  25.333  1.00 55.39  ?  307 ALA   B CA  1 
ATOM   3544 C  C   . ALA   B 1 151 ? 15.083 20.851  26.326  1.00 66.45  ?  307 ALA   B C   1 
ATOM   3545 O  O   . ALA   B 1 151 ? 14.372 21.172  27.296  1.00 64.22  ?  307 ALA   B O   1 
ATOM   3546 C  CB  . ALA   B 1 151 ? 14.696 21.814  24.071  1.00 55.87  ?  307 ALA   B CB  1 
ATOM   3547 N  N   . VAL   B 1 152 ? 15.491 19.612  26.084  1.00 54.98  ?  308 VAL   B N   1 
ATOM   3548 C  CA  . VAL   B 1 152 ? 14.999 18.533  26.976  1.00 57.37  ?  308 VAL   B CA  1 
ATOM   3549 C  C   . VAL   B 1 152 ? 16.123 17.539  27.281  1.00 53.57  ?  308 VAL   B C   1 
ATOM   3550 O  O   . VAL   B 1 152 ? 16.949 17.269  26.393  1.00 52.73  ?  308 VAL   B O   1 
ATOM   3551 C  CB  . VAL   B 1 152 ? 13.757 17.857  26.362  1.00 52.58  ?  308 VAL   B CB  1 
ATOM   3552 C  CG1 . VAL   B 1 152 ? 13.843 16.337  26.356  1.00 54.87  ?  308 VAL   B CG1 1 
ATOM   3553 C  CG2 . VAL   B 1 152 ? 12.471 18.320  27.025  1.00 48.03  ?  308 VAL   B CG2 1 
ATOM   3554 N  N   . THR   B 1 153 ? 16.154 17.063  28.516  1.00 57.22  ?  309 THR   B N   1 
ATOM   3555 C  CA  . THR   B 1 153 ? 17.117 16.038  28.896  1.00 59.52  ?  309 THR   B CA  1 
ATOM   3556 C  C   . THR   B 1 153 ? 16.349 14.792  29.310  1.00 52.32  ?  309 THR   B C   1 
ATOM   3557 O  O   . THR   B 1 153 ? 15.494 14.849  30.202  1.00 60.46  ?  309 THR   B O   1 
ATOM   3558 C  CB  . THR   B 1 153 ? 18.036 16.514  30.022  1.00 69.14  ?  309 THR   B CB  1 
ATOM   3559 O  OG1 . THR   B 1 153 ? 18.758 17.675  29.589  1.00 59.85  ?  309 THR   B OG1 1 
ATOM   3560 C  CG2 . THR   B 1 153 ? 19.032 15.422  30.384  1.00 50.60  ?  309 THR   B CG2 1 
ATOM   3561 N  N   . LEU   B 1 154 ? 16.633 13.681  28.643  1.00 51.22  ?  310 LEU   B N   1 
ATOM   3562 C  CA  . LEU   B 1 154 ? 16.005 12.402  28.928  1.00 52.71  ?  310 LEU   B CA  1 
ATOM   3563 C  C   . LEU   B 1 154 ? 17.036 11.450  29.514  1.00 60.92  ?  310 LEU   B C   1 
ATOM   3564 O  O   . LEU   B 1 154 ? 18.182 11.404  29.059  1.00 65.83  ?  310 LEU   B O   1 
ATOM   3565 C  CB  . LEU   B 1 154 ? 15.397 11.790  27.665  1.00 54.29  ?  310 LEU   B CB  1 
ATOM   3566 C  CG  . LEU   B 1 154 ? 14.354 12.628  26.928  1.00 63.84  ?  310 LEU   B CG  1 
ATOM   3567 C  CD1 . LEU   B 1 154 ? 13.868 11.878  25.706  1.00 51.21  ?  310 LEU   B CD1 1 
ATOM   3568 C  CD2 . LEU   B 1 154 ? 13.193 12.972  27.850  1.00 45.75  ?  310 LEU   B CD2 1 
ATOM   3569 N  N   . LEU   B 1 155 ? 16.626 10.758  30.582  1.00 68.90  ?  311 LEU   B N   1 
ATOM   3570 C  CA  . LEU   B 1 155 ? 17.503 9.752   31.228  1.00 65.75  ?  311 LEU   B CA  1 
ATOM   3571 C  C   . LEU   B 1 155 ? 16.940 8.355   30.934  1.00 65.30  ?  311 LEU   B C   1 
ATOM   3572 O  O   . LEU   B 1 155 ? 15.900 7.997   31.509  1.00 55.66  ?  311 LEU   B O   1 
ATOM   3573 C  CB  . LEU   B 1 155 ? 17.630 10.009  32.723  1.00 67.37  ?  311 LEU   B CB  1 
ATOM   3574 C  CG  . LEU   B 1 155 ? 17.622 11.476  33.156  1.00 68.34  ?  311 LEU   B CG  1 
ATOM   3575 C  CD1 . LEU   B 1 155 ? 17.272 11.540  34.629  1.00 60.34  ?  311 LEU   B CD1 1 
ATOM   3576 C  CD2 . LEU   B 1 155 ? 18.984 12.094  32.901  1.00 53.76  ?  311 LEU   B CD2 1 
ATOM   3577 N  N   . ILE   B 1 156 ? 17.607 7.618   30.051  1.00 64.27  ?  312 ILE   B N   1 
ATOM   3578 C  CA  . ILE   B 1 156 ? 17.160 6.260   29.646  1.00 57.57  ?  312 ILE   B CA  1 
ATOM   3579 C  C   . ILE   B 1 156 ? 17.671 5.283   30.710  1.00 79.60  ?  312 ILE   B C   1 
ATOM   3580 O  O   . ILE   B 1 156 ? 18.829 5.437   31.149  1.00 80.18  ?  312 ILE   B O   1 
ATOM   3581 C  CB  . ILE   B 1 156 ? 17.721 5.939   28.253  1.00 66.09  ?  312 ILE   B CB  1 
ATOM   3582 C  CG1 . ILE   B 1 156 ? 16.889 6.577   27.144  1.00 67.87  ?  312 ILE   B CG1 1 
ATOM   3583 C  CG2 . ILE   B 1 156 ? 17.863 4.433   28.042  1.00 77.20  ?  312 ILE   B CG2 1 
ATOM   3584 C  CD1 . ILE   B 1 156 ? 17.198 8.038   26.883  1.00 51.29  ?  312 ILE   B CD1 1 
ATOM   3585 N  N   . SER   B 1 157 ? 16.820 4.349   31.132  1.00 72.49  ?  313 SER   B N   1 
ATOM   3586 C  CA  . SER   B 1 157 ? 17.211 3.389   32.189  1.00 82.46  ?  313 SER   B CA  1 
ATOM   3587 C  C   . SER   B 1 157 ? 17.801 4.165   33.371  1.00 83.19  ?  313 SER   B C   1 
ATOM   3588 O  O   . SER   B 1 157 ? 17.118 5.077   33.876  1.00 81.32  ?  313 SER   B O   1 
ATOM   3589 C  CB  . SER   B 1 157 ? 18.178 2.375   31.658  1.00 68.89  ?  313 SER   B CB  1 
ATOM   3590 N  N   . GLU   B 1 158 ? 19.013 3.803   33.790  1.00 76.67  ?  314 GLU   B N   1 
ATOM   3591 C  CA  . GLU   B 1 158 ? 19.669 4.491   34.927  1.00 82.95  ?  314 GLU   B CA  1 
ATOM   3592 C  C   . GLU   B 1 158 ? 20.541 5.638   34.401  1.00 67.40  ?  314 GLU   B C   1 
ATOM   3593 O  O   . GLU   B 1 158 ? 21.504 5.978   35.102  1.00 80.60  ?  314 GLU   B O   1 
ATOM   3594 C  CB  . GLU   B 1 158 ? 20.509 3.483   35.707  1.00 76.36  ?  314 GLU   B CB  1 
ATOM   3595 N  N   . ILE   B 1 160 ? 21.943 6.068   30.932  1.00 63.16  ?  316 ILE   B N   1 
ATOM   3596 C  CA  . ILE   B 1 160 ? 22.158 6.701   29.601  1.00 62.89  ?  316 ILE   B CA  1 
ATOM   3597 C  C   . ILE   B 1 160 ? 21.359 8.010   29.547  1.00 66.92  ?  316 ILE   B C   1 
ATOM   3598 O  O   . ILE   B 1 160 ? 20.148 7.976   29.807  1.00 53.25  ?  316 ILE   B O   1 
ATOM   3599 C  CB  . ILE   B 1 160 ? 21.795 5.733   28.458  1.00 66.76  ?  316 ILE   B CB  1 
ATOM   3600 C  CG1 . ILE   B 1 160 ? 22.736 4.544   28.415  1.00 74.73  ?  316 ILE   B CG1 1 
ATOM   3601 C  CG2 . ILE   B 1 160 ? 21.754 6.464   27.115  1.00 58.17  ?  316 ILE   B CG2 1 
ATOM   3602 C  CD1 . ILE   B 1 160 ? 22.573 3.691   27.173  1.00 82.97  ?  316 ILE   B CD1 1 
ATOM   3603 N  N   . SER   B 1 161 ? 22.033 9.121   29.237  1.00 68.35  ?  317 SER   B N   1 
ATOM   3604 C  CA  . SER   B 1 161 ? 21.365 10.443  29.158  1.00 50.16  ?  317 SER   B CA  1 
ATOM   3605 C  C   . SER   B 1 161 ? 21.368 10.970  27.715  1.00 51.98  ?  317 SER   B C   1 
ATOM   3606 O  O   . SER   B 1 161 ? 22.334 10.678  26.983  1.00 41.27  ?  317 SER   B O   1 
ATOM   3607 C  CB  . SER   B 1 161 ? 22.002 11.406  30.109  1.00 58.16  ?  317 SER   B CB  1 
ATOM   3608 O  OG  . SER   B 1 161 ? 22.818 10.729  31.053  1.00 66.64  ?  317 SER   B OG  1 
ATOM   3609 N  N   . VAL   B 1 162 ? 20.325 11.710  27.326  1.00 42.99  ?  318 VAL   B N   1 
ATOM   3610 C  CA  . VAL   B 1 162 ? 20.199 12.244  25.974  1.00 51.72  ?  318 VAL   B CA  1 
ATOM   3611 C  C   . VAL   B 1 162 ? 19.721 13.686  26.072  1.00 40.85  ?  318 VAL   B C   1 
ATOM   3612 O  O   . VAL   B 1 162 ? 18.601 13.942  26.530  1.00 47.71  ?  318 VAL   B O   1 
ATOM   3613 C  CB  . VAL   B 1 162 ? 19.232 11.418  25.107  1.00 49.88  ?  318 VAL   B CB  1 
ATOM   3614 C  CG1 . VAL   B 1 162 ? 19.151 12.002  23.706  1.00 49.23  ?  318 VAL   B CG1 1 
ATOM   3615 C  CG2 . VAL   B 1 162 ? 19.668 9.962   25.047  1.00 58.53  ?  318 VAL   B CG2 1 
ATOM   3616 N  N   . ASP   B 1 163 ? 20.566 14.621  25.645  1.00 45.34  ?  319 ASP   B N   1 
ATOM   3617 C  CA  . ASP   B 1 163 ? 20.186 16.025  25.538  1.00 44.34  ?  319 ASP   B CA  1 
ATOM   3618 C  C   . ASP   B 1 163 ? 19.690 16.289  24.123  1.00 49.34  ?  319 ASP   B C   1 
ATOM   3619 O  O   . ASP   B 1 163 ? 20.440 16.116  23.157  1.00 54.85  ?  319 ASP   B O   1 
ATOM   3620 C  CB  . ASP   B 1 163 ? 21.365 16.938  25.865  1.00 43.57  ?  319 ASP   B CB  1 
ATOM   3621 C  CG  . ASP   B 1 163 ? 21.769 16.868  27.320  1.00 58.98  ?  319 ASP   B CG  1 
ATOM   3622 O  OD1 . ASP   B 1 163 ? 21.007 17.374  28.172  1.00 48.89  ?  319 ASP   B OD1 1 
ATOM   3623 O  OD2 . ASP   B 1 163 ? 22.850 16.318  27.611  1.00 77.46  -1 319 ASP   B OD2 1 
ATOM   3624 N  N   . ILE   B 1 164 ? 18.435 16.711  23.999  1.00 56.75  ?  320 ILE   B N   1 
ATOM   3625 C  CA  . ILE   B 1 164 ? 17.817 16.968  22.704  1.00 52.26  ?  320 ILE   B CA  1 
ATOM   3626 C  C   . ILE   B 1 164 ? 17.704 18.473  22.506  1.00 42.46  ?  320 ILE   B C   1 
ATOM   3627 O  O   . ILE   B 1 164 ? 17.234 19.197  23.396  1.00 45.60  ?  320 ILE   B O   1 
ATOM   3628 C  CB  . ILE   B 1 164 ? 16.447 16.280  22.579  1.00 41.08  ?  320 ILE   B CB  1 
ATOM   3629 C  CG1 . ILE   B 1 164 ? 16.575 14.790  22.894  1.00 39.18  ?  320 ILE   B CG1 1 
ATOM   3630 C  CG2 . ILE   B 1 164 ? 15.878 16.468  21.181  1.00 50.97  ?  320 ILE   B CG2 1 
ATOM   3631 C  CD1 . ILE   B 1 164 ? 15.329 14.190  23.481  1.00 47.36  ?  320 ILE   B CD1 1 
ATOM   3632 N  N   . THR   B 1 165 ? 18.145 18.938  21.341  1.00 39.96  ?  321 THR   B N   1 
ATOM   3633 C  CA  . THR   B 1 165 ? 18.130 20.348  20.986  1.00 49.08  ?  321 THR   B CA  1 
ATOM   3634 C  C   . THR   B 1 165 ? 17.215 20.548  19.787  1.00 53.27  ?  321 THR   B C   1 
ATOM   3635 O  O   . THR   B 1 165 ? 17.300 19.801  18.805  1.00 52.56  ?  321 THR   B O   1 
ATOM   3636 C  CB  . THR   B 1 165 ? 19.547 20.846  20.670  1.00 46.68  ?  321 THR   B CB  1 
ATOM   3637 O  OG1 . THR   B 1 165 ? 20.313 20.916  21.879  1.00 44.20  ?  321 THR   B OG1 1 
ATOM   3638 C  CG2 . THR   B 1 165 ? 19.506 22.219  20.016  1.00 37.94  ?  321 THR   B CG2 1 
ATOM   3639 N  N   . LEU   B 1 166 ? 16.335 21.541  19.873  1.00 47.62  ?  322 LEU   B N   1 
ATOM   3640 C  CA  . LEU   B 1 166 ? 15.515 21.942  18.739  1.00 48.86  ?  322 LEU   B CA  1 
ATOM   3641 C  C   . LEU   B 1 166 ? 16.255 23.008  17.943  1.00 43.42  ?  322 LEU   B C   1 
ATOM   3642 O  O   . LEU   B 1 166 ? 16.833 23.931  18.523  1.00 39.61  ?  322 LEU   B O   1 
ATOM   3643 C  CB  . LEU   B 1 166 ? 14.161 22.472  19.209  1.00 40.16  ?  322 LEU   B CB  1 
ATOM   3644 C  CG  . LEU   B 1 166 ? 13.237 23.031  18.124  1.00 49.16  ?  322 LEU   B CG  1 
ATOM   3645 C  CD1 . LEU   B 1 166 ? 12.855 21.945  17.131  1.00 50.48  ?  322 LEU   B CD1 1 
ATOM   3646 C  CD2 . LEU   B 1 166 ? 12.000 23.644  18.753  1.00 47.96  ?  322 LEU   B CD2 1 
ATOM   3647 N  N   . ALA   B 1 167 ? 16.243 22.878  16.618  1.00 38.41  ?  323 ALA   B N   1 
ATOM   3648 C  CA  . ALA   B 1 167 ? 16.917 23.836  15.757  1.00 38.90  ?  323 ALA   B CA  1 
ATOM   3649 C  C   . ALA   B 1 167 ? 16.099 24.078  14.498  1.00 54.76  ?  323 ALA   B C   1 
ATOM   3650 O  O   . ALA   B 1 167 ? 15.580 23.137  13.891  1.00 42.85  ?  323 ALA   B O   1 
ATOM   3651 C  CB  . ALA   B 1 167 ? 18.323 23.355  15.376  1.00 30.76  ?  323 ALA   B CB  1 
ATOM   3652 N  N   . LEU   B 1 168 ? 15.985 25.348  14.118  1.00 42.73  ?  324 LEU   B N   1 
ATOM   3653 C  CA  . LEU   B 1 168 ? 15.426 25.715  12.826  1.00 36.80  ?  324 LEU   B CA  1 
ATOM   3654 C  C   . LEU   B 1 168 ? 16.502 25.611  11.757  1.00 35.83  ?  324 LEU   B C   1 
ATOM   3655 O  O   . LEU   B 1 168 ? 17.654 25.993  11.981  1.00 37.42  ?  324 LEU   B O   1 
ATOM   3656 C  CB  . LEU   B 1 168 ? 14.872 27.139  12.863  1.00 36.34  ?  324 LEU   B CB  1 
ATOM   3657 C  CG  . LEU   B 1 168 ? 14.003 27.516  14.063  1.00 45.91  ?  324 LEU   B CG  1 
ATOM   3658 C  CD1 . LEU   B 1 168 ? 13.680 29.001  14.042  1.00 45.76  ?  324 LEU   B CD1 1 
ATOM   3659 C  CD2 . LEU   B 1 168 ? 12.725 26.691  14.096  1.00 40.91  ?  324 LEU   B CD2 1 
ATOM   3660 N  N   . GLU   B 1 169 ? 16.120 25.094  10.594  1.00 33.04  ?  325 GLU   B N   1 
ATOM   3661 C  CA  . GLU   B 1 169 ? 17.012 24.959  9.450   1.00 40.46  ?  325 GLU   B CA  1 
ATOM   3662 C  C   . GLU   B 1 169 ? 16.654 25.998  8.403   1.00 44.65  ?  325 GLU   B C   1 
ATOM   3663 O  O   . GLU   B 1 169 ? 15.493 26.088  7.989   1.00 44.23  ?  325 GLU   B O   1 
ATOM   3664 C  CB  . GLU   B 1 169 ? 16.916 23.561  8.837   1.00 38.16  ?  325 GLU   B CB  1 
ATOM   3665 C  CG  . GLU   B 1 169 ? 17.760 23.388  7.583   1.00 48.17  ?  325 GLU   B CG  1 
ATOM   3666 C  CD  . GLU   B 1 169 ? 17.628 22.008  6.976   1.00 45.14  ?  325 GLU   B CD  1 
ATOM   3667 O  OE1 . GLU   B 1 169 ? 16.629 21.761  6.270   1.00 53.82  ?  325 GLU   B OE1 1 
ATOM   3668 O  OE2 . GLU   B 1 169 ? 18.522 21.170  7.212   1.00 44.66  -1 325 GLU   B OE2 1 
ATOM   3669 N  N   . SER   B 1 170 ? 17.642 26.776  7.965   1.00 40.87  ?  326 SER   B N   1 
ATOM   3670 C  CA  . SER   B 1 170 ? 17.433 27.714  6.872   1.00 41.26  ?  326 SER   B CA  1 
ATOM   3671 C  C   . SER   B 1 170 ? 18.417 27.407  5.756   1.00 38.75  ?  326 SER   B C   1 
ATOM   3672 O  O   . SER   B 1 170 ? 19.626 27.298  5.998   1.00 43.29  ?  326 SER   B O   1 
ATOM   3673 C  CB  . SER   B 1 170 ? 17.589 29.165  7.329   1.00 34.70  ?  326 SER   B CB  1 
ATOM   3674 O  OG  . SER   B 1 170 ? 17.528 30.038  6.214   1.00 55.26  ?  326 SER   B OG  1 
ATOM   3675 N  N   . LYS   B 1 171 ? 17.891 27.253  4.543   1.00 47.22  ?  327 LYS   B N   1 
ATOM   3676 C  CA  . LYS   B 1 171 ? 18.702 27.034  3.355   1.00 39.52  ?  327 LYS   B CA  1 
ATOM   3677 C  C   . LYS   B 1 171 ? 18.972 28.325  2.598   1.00 42.06  ?  327 LYS   B C   1 
ATOM   3678 O  O   . LYS   B 1 171 ? 19.466 28.279  1.466   1.00 48.61  ?  327 LYS   B O   1 
ATOM   3679 C  CB  . LYS   B 1 171 ? 18.033 26.004  2.443   1.00 38.54  ?  327 LYS   B CB  1 
ATOM   3680 C  CG  . LYS   B 1 171 ? 17.963 24.613  3.058   1.00 43.55  ?  327 LYS   B CG  1 
ATOM   3681 C  CD  . LYS   B 1 171 ? 16.754 23.833  2.570   1.00 61.02  ?  327 LYS   B CD  1 
ATOM   3682 C  CE  . LYS   B 1 171 ? 17.076 22.354  2.440   1.00 60.10  ?  327 LYS   B CE  1 
ATOM   3683 N  NZ  . LYS   B 1 171 ? 16.742 21.606  3.683   1.00 71.24  ?  327 LYS   B NZ  1 
ATOM   3684 N  N   . SER   B 1 172 ? 18.661 29.472  3.197   1.00 35.04  ?  328 SER   B N   1 
ATOM   3685 C  CA  . SER   B 1 172 ? 18.997 30.761  2.619   1.00 39.24  ?  328 SER   B CA  1 
ATOM   3686 C  C   . SER   B 1 172 ? 20.478 31.058  2.849   1.00 38.77  ?  328 SER   B C   1 
ATOM   3687 O  O   . SER   B 1 172 ? 21.210 30.273  3.458   1.00 42.01  ?  328 SER   B O   1 
ATOM   3688 C  CB  . SER   B 1 172 ? 18.108 31.854  3.213   1.00 35.45  ?  328 SER   B CB  1 
ATOM   3689 O  OG  . SER   B 1 172 ? 18.214 31.893  4.626   1.00 58.13  ?  328 SER   B OG  1 
ATOM   3690 N  N   . SER   B 1 173 ? 20.930 32.207  2.354   1.00 54.66  ?  329 SER   B N   1 
ATOM   3691 C  CA  . SER   B 1 173 ? 22.321 32.597  2.533   1.00 43.46  ?  329 SER   B CA  1 
ATOM   3692 C  C   . SER   B 1 173 ? 22.641 32.772  4.013   1.00 28.00  ?  329 SER   B C   1 
ATOM   3693 O  O   . SER   B 1 173 ? 21.782 33.144  4.819   1.00 28.94  ?  329 SER   B O   1 
ATOM   3694 C  CB  . SER   B 1 173 ? 22.608 33.897  1.783   1.00 52.01  ?  329 SER   B CB  1 
ATOM   3695 O  OG  . SER   B 1 173 ? 22.556 33.692  0.383   1.00 66.62  ?  329 SER   B OG  1 
ATOM   3696 N  N   . TRP   B 1 174 ? 23.892 32.488  4.371   1.00 39.31  ?  330 TRP   B N   1 
ATOM   3697 C  CA  . TRP   B 1 174 ? 24.336 32.685  5.741   1.00 34.54  ?  330 TRP   B CA  1 
ATOM   3698 C  C   . TRP   B 1 174 ? 24.260 34.169  6.099   1.00 34.94  ?  330 TRP   B C   1 
ATOM   3699 O  O   . TRP   B 1 174 ? 24.482 35.034  5.246   1.00 30.94  ?  330 TRP   B O   1 
ATOM   3700 C  CB  . TRP   B 1 174 ? 25.765 32.175  5.930   1.00 29.09  ?  330 TRP   B CB  1 
ATOM   3701 C  CG  . TRP   B 1 174 ? 25.906 30.676  5.902   1.00 31.40  ?  330 TRP   B CG  1 
ATOM   3702 C  CD1 . TRP   B 1 174 ? 24.989 29.771  5.452   1.00 31.10  ?  330 TRP   B CD1 1 
ATOM   3703 C  CD2 . TRP   B 1 174 ? 27.033 29.913  6.358   1.00 27.88  ?  330 TRP   B CD2 1 
ATOM   3704 N  NE1 . TRP   B 1 174 ? 25.477 28.493  5.592   1.00 33.20  ?  330 TRP   B NE1 1 
ATOM   3705 C  CE2 . TRP   B 1 174 ? 26.729 28.553  6.147   1.00 27.74  ?  330 TRP   B CE2 1 
ATOM   3706 C  CE3 . TRP   B 1 174 ? 28.268 30.249  6.920   1.00 25.25  ?  330 TRP   B CE3 1 
ATOM   3707 C  CZ2 . TRP   B 1 174 ? 27.615 27.530  6.478   1.00 30.33  ?  330 TRP   B CZ2 1 
ATOM   3708 C  CZ3 . TRP   B 1 174 ? 29.147 29.232  7.250   1.00 30.47  ?  330 TRP   B CZ3 1 
ATOM   3709 C  CH2 . TRP   B 1 174 ? 28.816 27.889  7.028   1.00 29.73  ?  330 TRP   B CH2 1 
ATOM   3710 N  N   . PRO   B 1 175 ? 23.935 34.491  7.352   1.00 35.00  ?  331 PRO   B N   1 
ATOM   3711 C  CA  . PRO   B 1 175 ? 23.816 35.899  7.749   1.00 36.76  ?  331 PRO   B CA  1 
ATOM   3712 C  C   . PRO   B 1 175 ? 25.108 36.671  7.515   1.00 41.32  ?  331 PRO   B C   1 
ATOM   3713 O  O   . PRO   B 1 175 ? 26.203 36.108  7.444   1.00 34.99  ?  331 PRO   B O   1 
ATOM   3714 C  CB  . PRO   B 1 175 ? 23.475 35.816  9.241   1.00 37.56  ?  331 PRO   B CB  1 
ATOM   3715 C  CG  . PRO   B 1 175 ? 22.779 34.493  9.376   1.00 37.40  ?  331 PRO   B CG  1 
ATOM   3716 C  CD  . PRO   B 1 175 ? 23.509 33.579  8.428   1.00 34.06  ?  331 PRO   B CD  1 
ATOM   3717 N  N   . ALA   B 1 176 ? 24.959 37.993  7.392   1.00 41.07  ?  332 ALA   B N   1 
ATOM   3718 C  CA  . ALA   B 1 176 ? 26.088 38.856  7.060   1.00 40.93  ?  332 ALA   B CA  1 
ATOM   3719 C  C   . ALA   B 1 176 ? 27.160 38.863  8.141   1.00 32.18  ?  332 ALA   B C   1 
ATOM   3720 O  O   . ALA   B 1 176 ? 28.313 39.199  7.852   1.00 37.54  ?  332 ALA   B O   1 
ATOM   3721 C  CB  . ALA   B 1 176 ? 25.599 40.283  6.806   1.00 42.71  ?  332 ALA   B CB  1 
ATOM   3722 N  N   . SER   B 1 177 ? 26.811 38.502  9.378   1.00 31.21  ?  333 SER   B N   1 
ATOM   3723 C  CA  . SER   B 1 177 ? 27.793 38.463  10.454  1.00 25.87  ?  333 SER   B CA  1 
ATOM   3724 C  C   . SER   B 1 177 ? 28.811 37.343  10.284  1.00 33.46  ?  333 SER   B C   1 
ATOM   3725 O  O   . SER   B 1 177 ? 29.820 37.334  10.996  1.00 32.61  ?  333 SER   B O   1 
ATOM   3726 C  CB  . SER   B 1 177 ? 27.086 38.320  11.803  1.00 29.98  ?  333 SER   B CB  1 
ATOM   3727 O  OG  . SER   B 1 177 ? 26.408 37.078  11.895  1.00 37.21  ?  333 SER   B OG  1 
ATOM   3728 N  N   . THR   B 1 178 ? 28.575 36.407  9.367   1.00 27.70  ?  334 THR   B N   1 
ATOM   3729 C  CA  . THR   B 1 178 ? 29.487 35.301  9.114   1.00 37.09  ?  334 THR   B CA  1 
ATOM   3730 C  C   . THR   B 1 178 ? 30.375 35.526  7.898   1.00 28.70  ?  334 THR   B C   1 
ATOM   3731 O  O   . THR   B 1 178 ? 31.125 34.620  7.522   1.00 29.43  ?  334 THR   B O   1 
ATOM   3732 C  CB  . THR   B 1 178 ? 28.697 34.001  8.922   1.00 39.16  ?  334 THR   B CB  1 
ATOM   3733 O  OG1 . THR   B 1 178 ? 28.020 34.036  7.660   1.00 37.18  ?  334 THR   B OG1 1 
ATOM   3734 C  CG2 . THR   B 1 178 ? 27.666 33.830  10.029  1.00 31.47  ?  334 THR   B CG2 1 
ATOM   3735 N  N   . GLN   B 1 179 ? 30.321 36.712  7.283   1.00 32.94  ?  335 GLN   B N   1 
ATOM   3736 C  CA  . GLN   B 1 179 ? 30.927 36.899  5.967   1.00 31.78  ?  335 GLN   B CA  1 
ATOM   3737 C  C   . GLN   B 1 179 ? 32.442 36.741  5.995   1.00 41.67  ?  335 GLN   B C   1 
ATOM   3738 O  O   . GLN   B 1 179 ? 33.036 36.318  4.996   1.00 38.36  ?  335 GLN   B O   1 
ATOM   3739 C  CB  . GLN   B 1 179 ? 30.547 38.268  5.404   1.00 43.08  ?  335 GLN   B CB  1 
ATOM   3740 C  CG  . GLN   B 1 179 ? 29.666 38.196  4.164   1.00 69.88  ?  335 GLN   B CG  1 
ATOM   3741 C  CD  . GLN   B 1 179 ? 28.892 39.475  3.921   1.00 68.27  ?  335 GLN   B CD  1 
ATOM   3742 O  OE1 . GLN   B 1 179 ? 29.424 40.575  4.070   1.00 67.18  ?  335 GLN   B OE1 1 
ATOM   3743 N  NE2 . GLN   B 1 179 ? 27.625 39.338  3.541   1.00 70.05  ?  335 GLN   B NE2 1 
ATOM   3744 N  N   . GLU   B 1 180 ? 33.086 37.074  7.114   1.00 36.70  ?  336 GLU   B N   1 
ATOM   3745 C  CA  . GLU   B 1 180 ? 34.534 36.961  7.241   1.00 35.29  ?  336 GLU   B CA  1 
ATOM   3746 C  C   . GLU   B 1 180 ? 34.949 35.858  8.211   1.00 32.13  ?  336 GLU   B C   1 
ATOM   3747 O  O   . GLU   B 1 180 ? 36.115 35.799  8.617   1.00 39.19  ?  336 GLU   B O   1 
ATOM   3748 C  CB  . GLU   B 1 180 ? 35.139 38.303  7.658   1.00 40.93  ?  336 GLU   B CB  1 
ATOM   3749 C  CG  . GLU   B 1 180 ? 34.574 39.497  6.896   1.00 51.08  ?  336 GLU   B CG  1 
ATOM   3750 C  CD  . GLU   B 1 180 ? 35.402 39.852  5.672   1.00 65.23  ?  336 GLU   B CD  1 
ATOM   3751 O  OE1 . GLU   B 1 180 ? 36.488 40.446  5.833   1.00 81.99  ?  336 GLU   B OE1 1 
ATOM   3752 O  OE2 . GLU   B 1 180 ? 34.964 39.532  4.545   1.00 66.21  -1 336 GLU   B OE2 1 
ATOM   3753 N  N   . GLY   B 1 181 ? 34.018 34.980  8.592   1.00 32.30  ?  337 GLY   B N   1 
ATOM   3754 C  CA  . GLY   B 1 181 ? 34.346 33.807  9.373   1.00 27.22  ?  337 GLY   B CA  1 
ATOM   3755 C  C   . GLY   B 1 181 ? 34.681 32.619  8.487   1.00 27.57  ?  337 GLY   B C   1 
ATOM   3756 O  O   . GLY   B 1 181 ? 34.664 32.697  7.259   1.00 28.96  ?  337 GLY   B O   1 
ATOM   3757 N  N   . LEU   B 1 182 ? 34.988 31.497  9.140   1.00 26.43  ?  338 LEU   B N   1 
ATOM   3758 C  CA  . LEU   B 1 182 ? 35.320 30.252  8.448   1.00 23.20  ?  338 LEU   B CA  1 
ATOM   3759 C  C   . LEU   B 1 182 ? 36.468 30.470  7.461   1.00 24.66  ?  338 LEU   B C   1 
ATOM   3760 O  O   . LEU   B 1 182 ? 36.384 30.137  6.277   1.00 23.17  ?  338 LEU   B O   1 
ATOM   3761 C  CB  . LEU   B 1 182 ? 34.083 29.676  7.750   1.00 20.16  ?  338 LEU   B CB  1 
ATOM   3762 C  CG  . LEU   B 1 182 ? 34.120 28.258  7.171   1.00 20.48  ?  338 LEU   B CG  1 
ATOM   3763 C  CD1 . LEU   B 1 182 ? 34.319 27.223  8.264   1.00 16.60  ?  338 LEU   B CD1 1 
ATOM   3764 C  CD2 . LEU   B 1 182 ? 32.851 27.974  6.375   1.00 31.09  ?  338 LEU   B CD2 1 
ATOM   3765 N  N   . ARG   B 1 183 ? 37.556 31.055  7.964   1.00 22.68  ?  339 ARG   B N   1 
ATOM   3766 C  CA  . ARG   B 1 183 ? 38.699 31.409  7.122   1.00 28.67  ?  339 ARG   B CA  1 
ATOM   3767 C  C   . ARG   B 1 183 ? 39.595 30.181  6.947   1.00 21.48  ?  339 ARG   B C   1 
ATOM   3768 O  O   . ARG   B 1 183 ? 40.703 30.080  7.478   1.00 31.95  ?  339 ARG   B O   1 
ATOM   3769 C  CB  . ARG   B 1 183 ? 39.447 32.594  7.715   1.00 31.37  ?  339 ARG   B CB  1 
ATOM   3770 C  CG  . ARG   B 1 183 ? 38.581 33.843  7.813   1.00 40.28  ?  339 ARG   B CG  1 
ATOM   3771 C  CD  . ARG   B 1 183 ? 39.363 35.065  8.269   1.00 54.81  ?  339 ARG   B CD  1 
ATOM   3772 N  NE  . ARG   B 1 183 ? 40.611 35.230  7.535   1.00 63.88  ?  339 ARG   B NE  1 
ATOM   3773 C  CZ  . ARG   B 1 183 ? 41.278 36.372  7.443   1.00 67.14  ?  339 ARG   B CZ  1 
ATOM   3774 N  NH1 . ARG   B 1 183 ? 40.835 37.480  8.016   1.00 66.29  ?  339 ARG   B NH1 1 
ATOM   3775 N  NH2 . ARG   B 1 183 ? 42.418 36.404  6.757   1.00 60.09  ?  339 ARG   B NH2 1 
ATOM   3776 N  N   . ILE   B 1 184 ? 39.079 29.230  6.168   1.00 23.44  ?  340 ILE   B N   1 
ATOM   3777 C  CA  . ILE   B 1 184 ? 39.761 27.971  5.898   1.00 20.67  ?  340 ILE   B CA  1 
ATOM   3778 C  C   . ILE   B 1 184 ? 40.433 27.971  4.530   1.00 20.46  ?  340 ILE   B C   1 
ATOM   3779 O  O   . ILE   B 1 184 ? 40.890 26.920  4.070   1.00 23.06  ?  340 ILE   B O   1 
ATOM   3780 C  CB  . ILE   B 1 184 ? 38.787 26.789  6.018   1.00 27.22  ?  340 ILE   B CB  1 
ATOM   3781 C  CG1 . ILE   B 1 184 ? 37.714 26.886  4.928   1.00 30.15  ?  340 ILE   B CG1 1 
ATOM   3782 C  CG2 . ILE   B 1 184 ? 38.150 26.762  7.398   1.00 15.20  ?  340 ILE   B CG2 1 
ATOM   3783 C  CD1 . ILE   B 1 184 ? 36.706 25.759  4.942   1.00 18.26  ?  340 ILE   B CD1 1 
ATOM   3784 N  N   . GLN   B 1 185 ? 40.509 29.130  3.870   1.00 22.43  ?  341 GLN   B N   1 
ATOM   3785 C  CA  . GLN   B 1 185 ? 40.932 29.174  2.472   1.00 22.26  ?  341 GLN   B CA  1 
ATOM   3786 C  C   . GLN   B 1 185 ? 42.339 28.615  2.292   1.00 26.88  ?  341 GLN   B C   1 
ATOM   3787 O  O   . GLN   B 1 185 ? 42.599 27.847  1.361   1.00 25.00  ?  341 GLN   B O   1 
ATOM   3788 C  CB  . GLN   B 1 185 ? 40.858 30.608  1.946   1.00 24.25  ?  341 GLN   B CB  1 
ATOM   3789 C  CG  . GLN   B 1 185 ? 39.447 31.151  1.798   1.00 30.16  ?  341 GLN   B CG  1 
ATOM   3790 C  CD  . GLN   B 1 185 ? 39.034 32.013  2.972   1.00 27.28  ?  341 GLN   B CD  1 
ATOM   3791 O  OE1 . GLN   B 1 185 ? 39.556 31.868  4.076   1.00 34.85  ?  341 GLN   B OE1 1 
ATOM   3792 N  NE2 . GLN   B 1 185 ? 38.098 32.927  2.736   1.00 24.58  ?  341 GLN   B NE2 1 
ATOM   3793 N  N   . ASN   B 1 186 ? 43.264 28.994  3.169   1.00 26.51  ?  342 ASN   B N   1 
ATOM   3794 C  CA  . ASN   B 1 186 ? 44.634 28.518  3.045   1.00 28.06  ?  342 ASN   B CA  1 
ATOM   3795 C  C   . ASN   B 1 186 ? 44.823 27.111  3.596   1.00 14.29  ?  342 ASN   B C   1 
ATOM   3796 O  O   . ASN   B 1 186 ? 45.902 26.535  3.425   1.00 23.34  ?  342 ASN   B O   1 
ATOM   3797 C  CB  . ASN   B 1 186 ? 45.584 29.485  3.753   1.00 31.26  ?  342 ASN   B CB  1 
ATOM   3798 C  CG  . ASN   B 1 186 ? 45.751 30.789  2.998   1.00 56.86  ?  342 ASN   B CG  1 
ATOM   3799 O  OD1 . ASN   B 1 186 ? 45.139 30.997  1.950   1.00 48.88  ?  342 ASN   B OD1 1 
ATOM   3800 N  ND2 . ASN   B 1 186 ? 46.576 31.680  3.533   1.00 66.86  ?  342 ASN   B ND2 1 
ATOM   3801 N  N   . TRP   B 1 187 ? 43.799 26.550  4.235   1.00 21.62  ?  343 TRP   B N   1 
ATOM   3802 C  CA  . TRP   B 1 187 ? 43.884 25.245  4.882   1.00 20.39  ?  343 TRP   B CA  1 
ATOM   3803 C  C   . TRP   B 1 187 ? 43.069 24.214  4.107   1.00 21.89  ?  343 TRP   B C   1 
ATOM   3804 O  O   . TRP   B 1 187 ? 43.641 23.284  3.532   1.00 20.04  ?  343 TRP   B O   1 
ATOM   3805 C  CB  . TRP   B 1 187 ? 43.413 25.379  6.336   1.00 14.01  ?  343 TRP   B CB  1 
ATOM   3806 C  CG  . TRP   B 1 187 ? 43.082 24.102  7.062   1.00 19.02  ?  343 TRP   B CG  1 
ATOM   3807 C  CD1 . TRP   B 1 187 ? 43.631 22.867  6.867   1.00 15.84  ?  343 TRP   B CD1 1 
ATOM   3808 C  CD2 . TRP   B 1 187 ? 42.100 23.946  8.096   1.00 20.51  ?  343 TRP   B CD2 1 
ATOM   3809 N  NE1 . TRP   B 1 187 ? 43.055 21.954  7.721   1.00 19.13  ?  343 TRP   B NE1 1 
ATOM   3810 C  CE2 . TRP   B 1 187 ? 42.112 22.592  8.485   1.00 19.06  ?  343 TRP   B CE2 1 
ATOM   3811 C  CE3 . TRP   B 1 187 ? 41.212 24.821  8.733   1.00 18.12  ?  343 TRP   B CE3 1 
ATOM   3812 C  CZ2 . TRP   B 1 187 ? 41.272 22.092  9.479   1.00 13.38  ?  343 TRP   B CZ2 1 
ATOM   3813 C  CZ3 . TRP   B 1 187 ? 40.381 24.324  9.719   1.00 18.12  ?  343 TRP   B CZ3 1 
ATOM   3814 C  CH2 . TRP   B 1 187 ? 40.414 22.971  10.081  1.00 13.73  ?  343 TRP   B CH2 1 
ATOM   3815 N  N   . LEU   B 1 188 ? 41.746 24.366  4.053   1.00 16.47  ?  344 LEU   B N   1 
ATOM   3816 C  CA  . LEU   B 1 188 ? 40.879 23.419  3.367   1.00 18.95  ?  344 LEU   B CA  1 
ATOM   3817 C  C   . LEU   B 1 188 ? 40.513 23.848  1.952   1.00 20.56  ?  344 LEU   B C   1 
ATOM   3818 O  O   . LEU   B 1 188 ? 39.867 23.066  1.246   1.00 26.65  ?  344 LEU   B O   1 
ATOM   3819 C  CB  . LEU   B 1 188 ? 39.598 23.200  4.181   1.00 17.47  ?  344 LEU   B CB  1 
ATOM   3820 C  CG  . LEU   B 1 188 ? 39.838 22.695  5.606   1.00 15.71  ?  344 LEU   B CG  1 
ATOM   3821 C  CD1 . LEU   B 1 188 ? 38.527 22.530  6.356   1.00 14.67  ?  344 LEU   B CD1 1 
ATOM   3822 C  CD2 . LEU   B 1 188 ? 40.607 21.385  5.574   1.00 19.27  ?  344 LEU   B CD2 1 
ATOM   3823 N  N   . SER   B 1 189 ? 40.891 25.070  1.550   1.00 21.54  ?  345 SER   B N   1 
ATOM   3824 C  CA  . SER   B 1 189 ? 40.740 25.677  0.221   1.00 26.29  ?  345 SER   B CA  1 
ATOM   3825 C  C   . SER   B 1 189 ? 39.513 26.579  0.145   1.00 27.21  ?  345 SER   B C   1 
ATOM   3826 O  O   . SER   B 1 189 ? 38.581 26.451  0.944   1.00 25.88  ?  345 SER   B O   1 
ATOM   3827 C  CB  . SER   B 1 189 ? 40.680 24.637  -0.904  1.00 24.53  ?  345 SER   B CB  1 
ATOM   3828 O  OG  . SER   B 1 189 ? 39.377 24.092  -1.031  1.00 21.63  ?  345 SER   B OG  1 
ATOM   3829 N  N   . ALA   B 1 190 ? 39.524 27.506  -0.818  1.00 21.44  ?  346 ALA   B N   1 
ATOM   3830 C  CA  . ALA   B 1 190 ? 38.399 28.411  -1.019  1.00 25.23  ?  346 ALA   B CA  1 
ATOM   3831 C  C   . ALA   B 1 190 ? 37.208 27.710  -1.657  1.00 24.72  ?  346 ALA   B C   1 
ATOM   3832 O  O   . ALA   B 1 190 ? 36.060 28.067  -1.370  1.00 26.48  ?  346 ALA   B O   1 
ATOM   3833 C  CB  . ALA   B 1 190 ? 38.826 29.597  -1.884  1.00 21.36  ?  346 ALA   B CB  1 
ATOM   3834 N  N   . LYS   B 1 191 ? 37.461 26.730  -2.528  1.00 18.16  ?  347 LYS   B N   1 
ATOM   3835 C  CA  . LYS   B 1 191 ? 36.372 25.946  -3.102  1.00 31.94  ?  347 LYS   B CA  1 
ATOM   3836 C  C   . LYS   B 1 191 ? 35.583 25.237  -2.009  1.00 24.64  ?  347 LYS   B C   1 
ATOM   3837 O  O   . LYS   B 1 191 ? 34.345 25.213  -2.033  1.00 34.18  ?  347 LYS   B O   1 
ATOM   3838 C  CB  . LYS   B 1 191 ? 36.936 24.943  -4.114  1.00 27.85  ?  347 LYS   B CB  1 
ATOM   3839 C  CG  . LYS   B 1 191 ? 35.997 23.803  -4.493  1.00 35.71  ?  347 LYS   B CG  1 
ATOM   3840 C  CD  . LYS   B 1 191 ? 36.673 22.794  -5.428  1.00 45.18  ?  347 LYS   B CD  1 
ATOM   3841 C  CE  . LYS   B 1 191 ? 37.716 23.442  -6.335  1.00 47.53  ?  347 LYS   B CE  1 
ATOM   3842 N  NZ  . LYS   B 1 191 ? 37.099 24.109  -7.514  1.00 52.37  ?  347 LYS   B NZ  1 
ATOM   3843 N  N   . VAL   B 1 192 ? 36.286 24.683  -1.019  1.00 22.82  ?  348 VAL   B N   1 
ATOM   3844 C  CA  . VAL   B 1 192 ? 35.615 24.012  0.087   1.00 27.13  ?  348 VAL   B CA  1 
ATOM   3845 C  C   . VAL   B 1 192 ? 34.816 25.008  0.917   1.00 23.33  ?  348 VAL   B C   1 
ATOM   3846 O  O   . VAL   B 1 192 ? 33.700 24.707  1.355   1.00 26.01  ?  348 VAL   B O   1 
ATOM   3847 C  CB  . VAL   B 1 192 ? 36.637 23.245  0.943   1.00 27.42  ?  348 VAL   B CB  1 
ATOM   3848 C  CG1 . VAL   B 1 192 ? 36.040 22.887  2.291   1.00 15.66  ?  348 VAL   B CG1 1 
ATOM   3849 C  CG2 . VAL   B 1 192 ? 37.086 21.992  0.215   1.00 16.53  ?  348 VAL   B CG2 1 
ATOM   3850 N  N   . ARG   B 1 193 ? 35.365 26.202  1.155   1.00 22.48  ?  349 ARG   B N   1 
ATOM   3851 C  CA  . ARG   B 1 193 ? 34.624 27.193  1.929   1.00 24.68  ?  349 ARG   B CA  1 
ATOM   3852 C  C   . ARG   B 1 193 ? 33.359 27.623  1.197   1.00 28.89  ?  349 ARG   B C   1 
ATOM   3853 O  O   . ARG   B 1 193 ? 32.301 27.796  1.816   1.00 23.50  ?  349 ARG   B O   1 
ATOM   3854 C  CB  . ARG   B 1 193 ? 35.501 28.406  2.236   1.00 27.05  ?  349 ARG   B CB  1 
ATOM   3855 C  CG  . ARG   B 1 193 ? 34.740 29.527  2.934   1.00 22.97  ?  349 ARG   B CG  1 
ATOM   3856 C  CD  . ARG   B 1 193 ? 35.625 30.716  3.264   1.00 20.51  ?  349 ARG   B CD  1 
ATOM   3857 N  NE  . ARG   B 1 193 ? 35.019 31.569  4.281   1.00 18.11  ?  349 ARG   B NE  1 
ATOM   3858 C  CZ  . ARG   B 1 193 ? 34.416 32.723  4.029   1.00 29.10  ?  349 ARG   B CZ  1 
ATOM   3859 N  NH1 . ARG   B 1 193 ? 34.334 33.205  2.800   1.00 33.74  ?  349 ARG   B NH1 1 
ATOM   3860 N  NH2 . ARG   B 1 193 ? 33.883 33.411  5.035   1.00 28.10  ?  349 ARG   B NH2 1 
ATOM   3861 N  N   . LYS   B 1 194 ? 33.440 27.789  -0.126  1.00 23.98  ?  350 LYS   B N   1 
ATOM   3862 C  CA  . LYS   B 1 194 ? 32.241 28.126  -0.886  1.00 22.27  ?  350 LYS   B CA  1 
ATOM   3863 C  C   . LYS   B 1 194 ? 31.211 27.008  -0.808  1.00 27.20  ?  350 LYS   B C   1 
ATOM   3864 O  O   . LYS   B 1 194 ? 30.014 27.271  -0.652  1.00 27.57  ?  350 LYS   B O   1 
ATOM   3865 C  CB  . LYS   B 1 194 ? 32.576 28.427  -2.345  1.00 30.70  ?  350 LYS   B CB  1 
ATOM   3866 C  CG  . LYS   B 1 194 ? 31.381 29.019  -3.078  1.00 47.22  ?  350 LYS   B CG  1 
ATOM   3867 C  CD  . LYS   B 1 194 ? 31.699 29.464  -4.492  1.00 40.43  ?  350 LYS   B CD  1 
ATOM   3868 C  CE  . LYS   B 1 194 ? 30.663 30.467  -4.990  1.00 60.88  ?  350 LYS   B CE  1 
ATOM   3869 N  NZ  . LYS   B 1 194 ? 30.436 30.350  -6.455  1.00 70.12  ?  350 LYS   B NZ  1 
ATOM   3870 N  N   . GLN   B 1 195 ? 31.654 25.752  -0.917  1.00 18.56  ?  351 GLN   B N   1 
ATOM   3871 C  CA  . GLN   B 1 195 ? 30.710 24.639  -0.833  1.00 28.14  ?  351 GLN   B CA  1 
ATOM   3872 C  C   . GLN   B 1 195 ? 30.074 24.553  0.549   1.00 26.57  ?  351 GLN   B C   1 
ATOM   3873 O  O   . GLN   B 1 195 ? 28.874 24.280  0.671   1.00 30.17  ?  351 GLN   B O   1 
ATOM   3874 C  CB  . GLN   B 1 195 ? 31.401 23.321  -1.187  1.00 24.47  ?  351 GLN   B CB  1 
ATOM   3875 C  CG  . GLN   B 1 195 ? 31.249 22.930  -2.648  1.00 38.56  ?  351 GLN   B CG  1 
ATOM   3876 C  CD  . GLN   B 1 195 ? 32.390 22.066  -3.153  1.00 42.20  ?  351 GLN   B CD  1 
ATOM   3877 O  OE1 . GLN   B 1 195 ? 32.770 22.148  -4.320  1.00 49.14  ?  351 GLN   B OE1 1 
ATOM   3878 N  NE2 . GLN   B 1 195 ? 32.937 21.230  -2.277  1.00 58.33  ?  351 GLN   B NE2 1 
ATOM   3879 N  N   . LEU   B 1 196 ? 30.860 24.788  1.601   1.00 24.26  ?  352 LEU   B N   1 
ATOM   3880 C  CA  . LEU   B 1 196 ? 30.321 24.750  2.956   1.00 30.22  ?  352 LEU   B CA  1 
ATOM   3881 C  C   . LEU   B 1 196 ? 29.302 25.858  3.171   1.00 27.58  ?  352 LEU   B C   1 
ATOM   3882 O  O   . LEU   B 1 196 ? 28.266 25.642  3.811   1.00 30.07  ?  352 LEU   B O   1 
ATOM   3883 C  CB  . LEU   B 1 196 ? 31.450 24.863  3.980   1.00 23.23  ?  352 LEU   B CB  1 
ATOM   3884 C  CG  . LEU   B 1 196 ? 32.368 23.648  4.101   1.00 17.16  ?  352 LEU   B CG  1 
ATOM   3885 C  CD1 . LEU   B 1 196 ? 33.477 23.902  5.112   1.00 19.98  ?  352 LEU   B CD1 1 
ATOM   3886 C  CD2 . LEU   B 1 196 ? 31.555 22.420  4.481   1.00 24.33  ?  352 LEU   B CD2 1 
ATOM   3887 N  N   . ARG   B 1 197 ? 29.574 27.053  2.642   1.00 21.48  ?  353 ARG   B N   1 
ATOM   3888 C  CA  . ARG   B 1 197 ? 28.638 28.156  2.818   1.00 30.33  ?  353 ARG   B CA  1 
ATOM   3889 C  C   . ARG   B 1 197 ? 27.356 27.967  2.014   1.00 30.83  ?  353 ARG   B C   1 
ATOM   3890 O  O   . ARG   B 1 197 ? 26.367 28.656  2.286   1.00 26.03  ?  353 ARG   B O   1 
ATOM   3891 C  CB  . ARG   B 1 197 ? 29.313 29.479  2.454   1.00 31.99  ?  353 ARG   B CB  1 
ATOM   3892 C  CG  . ARG   B 1 197 ? 30.383 29.904  3.453   1.00 34.59  ?  353 ARG   B CG  1 
ATOM   3893 C  CD  . ARG   B 1 197 ? 31.038 31.224  3.069   1.00 32.17  ?  353 ARG   B CD  1 
ATOM   3894 N  NE  . ARG   B 1 197 ? 30.067 32.304  2.947   1.00 47.18  ?  353 ARG   B NE  1 
ATOM   3895 C  CZ  . ARG   B 1 197 ? 29.578 32.995  3.968   1.00 37.72  ?  353 ARG   B CZ  1 
ATOM   3896 N  NH1 . ARG   B 1 197 ? 29.936 32.733  5.214   1.00 42.71  ?  353 ARG   B NH1 1 
ATOM   3897 N  NH2 . ARG   B 1 197 ? 28.704 33.969  3.733   1.00 41.11  ?  353 ARG   B NH2 1 
ATOM   3898 N  N   . LEU   B 1 198 ? 27.344 27.053  1.041   1.00 26.44  ?  354 LEU   B N   1 
ATOM   3899 C  CA  . LEU   B 1 198 ? 26.113 26.722  0.332   1.00 36.09  ?  354 LEU   B CA  1 
ATOM   3900 C  C   . LEU   B 1 198 ? 25.220 25.776  1.121   1.00 31.46  ?  354 LEU   B C   1 
ATOM   3901 O  O   . LEU   B 1 198 ? 24.069 25.561  0.726   1.00 31.40  ?  354 LEU   B O   1 
ATOM   3902 C  CB  . LEU   B 1 198 ? 26.424 26.110  -1.038  1.00 28.89  ?  354 LEU   B CB  1 
ATOM   3903 C  CG  . LEU   B 1 198 ? 27.025 27.060  -2.078  1.00 33.60  ?  354 LEU   B CG  1 
ATOM   3904 C  CD1 . LEU   B 1 198 ? 27.294 26.349  -3.400  1.00 47.36  ?  354 LEU   B CD1 1 
ATOM   3905 C  CD2 . LEU   B 1 198 ? 26.108 28.253  -2.282  1.00 29.85  ?  354 LEU   B CD2 1 
ATOM   3906 N  N   . LYS   B 1 199 ? 25.717 25.218  2.218   1.00 31.65  ?  355 LYS   B N   1 
ATOM   3907 C  CA  . LYS   B 1 199 ? 24.916 24.368  3.077   1.00 32.00  ?  355 LYS   B CA  1 
ATOM   3908 C  C   . LYS   B 1 199 ? 24.006 25.218  3.960   1.00 31.03  ?  355 LYS   B C   1 
ATOM   3909 O  O   . LYS   B 1 199 ? 24.225 26.423  4.115   1.00 34.53  ?  355 LYS   B O   1 
ATOM   3910 C  CB  . LYS   B 1 199 ? 25.826 23.489  3.929   1.00 32.07  ?  355 LYS   B CB  1 
ATOM   3911 C  CG  . LYS   B 1 199 ? 26.854 22.717  3.114   1.00 32.77  ?  355 LYS   B CG  1 
ATOM   3912 C  CD  . LYS   B 1 199 ? 26.873 21.243  3.483   1.00 37.84  ?  355 LYS   B CD  1 
ATOM   3913 C  CE  . LYS   B 1 199 ? 27.977 20.501  2.745   1.00 48.14  ?  355 LYS   B CE  1 
ATOM   3914 N  NZ  . LYS   B 1 199 ? 27.553 20.058  1.385   1.00 59.78  ?  355 LYS   B NZ  1 
ATOM   3915 N  N   . PRO   B 1 200 ? 22.962 24.624  4.530   1.00 29.12  ?  356 PRO   B N   1 
ATOM   3916 C  CA  . PRO   B 1 200 ? 22.074 25.387  5.417   1.00 26.02  ?  356 PRO   B CA  1 
ATOM   3917 C  C   . PRO   B 1 200 ? 22.780 25.772  6.709   1.00 34.61  ?  356 PRO   B C   1 
ATOM   3918 O  O   . PRO   B 1 200 ? 23.853 25.268  7.049   1.00 33.02  ?  356 PRO   B O   1 
ATOM   3919 C  CB  . PRO   B 1 200 ? 20.912 24.423  5.681   1.00 33.03  ?  356 PRO   B CB  1 
ATOM   3920 C  CG  . PRO   B 1 200 ? 21.436 23.071  5.334   1.00 33.81  ?  356 PRO   B CG  1 
ATOM   3921 C  CD  . PRO   B 1 200 ? 22.457 23.266  4.269   1.00 35.67  ?  356 PRO   B CD  1 
ATOM   3922 N  N   . PHE   B 1 201 ? 22.156 26.702  7.435   1.00 29.58  ?  357 PHE   B N   1 
ATOM   3923 C  CA  . PHE   B 1 201 ? 22.601 27.083  8.770   1.00 30.96  ?  357 PHE   B CA  1 
ATOM   3924 C  C   . PHE   B 1 201 ? 21.456 26.870  9.753   1.00 28.12  ?  357 PHE   B C   1 
ATOM   3925 O  O   . PHE   B 1 201 ? 20.289 26.738  9.354   1.00 29.25  ?  357 PHE   B O   1 
ATOM   3926 C  CB  . PHE   B 1 201 ? 23.097 28.541  8.816   1.00 26.65  ?  357 PHE   B CB  1 
ATOM   3927 C  CG  . PHE   B 1 201 ? 22.019 29.573  8.600   1.00 26.95  ?  357 PHE   B CG  1 
ATOM   3928 C  CD1 . PHE   B 1 201 ? 21.666 29.972  7.320   1.00 36.12  ?  357 PHE   B CD1 1 
ATOM   3929 C  CD2 . PHE   B 1 201 ? 21.381 30.164  9.679   1.00 27.79  ?  357 PHE   B CD2 1 
ATOM   3930 C  CE1 . PHE   B 1 201 ? 20.685 30.928  7.121   1.00 30.63  ?  357 PHE   B CE1 1 
ATOM   3931 C  CE2 . PHE   B 1 201 ? 20.398 31.120  9.486   1.00 34.71  ?  357 PHE   B CE2 1 
ATOM   3932 C  CZ  . PHE   B 1 201 ? 20.050 31.504  8.205   1.00 32.85  ?  357 PHE   B CZ  1 
ATOM   3933 N  N   . TYR   B 1 202 ? 21.776 26.825  11.052  1.00 38.97  ?  358 TYR   B N   1 
ATOM   3934 C  CA  . TYR   B 1 202 ? 20.747 26.462  12.011  1.00 32.64  ?  358 TYR   B CA  1 
ATOM   3935 C  C   . TYR   B 1 202 ? 20.595 27.538  13.077  1.00 28.68  ?  358 TYR   B C   1 
ATOM   3936 O  O   . TYR   B 1 202 ? 21.494 28.343  13.315  1.00 28.05  ?  358 TYR   B O   1 
ATOM   3937 C  CB  . TYR   B 1 202 ? 21.058 25.089  12.617  1.00 30.93  ?  358 TYR   B CB  1 
ATOM   3938 C  CG  . TYR   B 1 202 ? 21.007 24.037  11.539  1.00 31.91  ?  358 TYR   B CG  1 
ATOM   3939 C  CD1 . TYR   B 1 202 ? 19.804 23.450  11.182  1.00 39.44  ?  358 TYR   B CD1 1 
ATOM   3940 C  CD2 . TYR   B 1 202 ? 22.146 23.678  10.829  1.00 28.02  ?  358 TYR   B CD2 1 
ATOM   3941 C  CE1 . TYR   B 1 202 ? 19.742 22.513  10.178  1.00 40.95  ?  358 TYR   B CE1 1 
ATOM   3942 C  CE2 . TYR   B 1 202 ? 22.091 22.737  9.817   1.00 35.83  ?  358 TYR   B CE2 1 
ATOM   3943 C  CZ  . TYR   B 1 202 ? 20.880 22.162  9.492   1.00 40.69  ?  358 TYR   B CZ  1 
ATOM   3944 O  OH  . TYR   B 1 202 ? 20.801 21.217  8.495   1.00 36.25  ?  358 TYR   B OH  1 
ATOM   3945 N  N   . LEU   B 1 203 ? 19.414 27.568  13.687  1.00 29.48  ?  359 LEU   B N   1 
ATOM   3946 C  CA  . LEU   B 1 203 ? 19.088 28.548  14.717  1.00 30.88  ?  359 LEU   B CA  1 
ATOM   3947 C  C   . LEU   B 1 203 ? 18.510 27.812  15.915  1.00 39.53  ?  359 LEU   B C   1 
ATOM   3948 O  O   . LEU   B 1 203 ? 17.497 27.119  15.790  1.00 39.84  ?  359 LEU   B O   1 
ATOM   3949 C  CB  . LEU   B 1 203 ? 18.104 29.599  14.197  1.00 31.47  ?  359 LEU   B CB  1 
ATOM   3950 C  CG  . LEU   B 1 203 ? 18.727 30.837  13.552  1.00 37.52  ?  359 LEU   B CG  1 
ATOM   3951 C  CD1 . LEU   B 1 203 ? 17.650 31.728  12.972  1.00 53.30  ?  359 LEU   B CD1 1 
ATOM   3952 C  CD2 . LEU   B 1 203 ? 19.560 31.596  14.567  1.00 34.43  ?  359 LEU   B CD2 1 
ATOM   3953 N  N   . VAL   B 1 204 ? 19.152 27.964  17.065  1.00 32.54  ?  360 VAL   B N   1 
ATOM   3954 C  CA  . VAL   B 1 204 ? 18.775 27.243  18.276  1.00 36.32  ?  360 VAL   B CA  1 
ATOM   3955 C  C   . VAL   B 1 204 ? 18.187 28.248  19.259  1.00 35.51  ?  360 VAL   B C   1 
ATOM   3956 O  O   . VAL   B 1 204 ? 18.757 29.331  19.427  1.00 37.07  ?  360 VAL   B O   1 
ATOM   3957 C  CB  . VAL   B 1 204 ? 19.991 26.511  18.867  1.00 29.81  ?  360 VAL   B CB  1 
ATOM   3958 C  CG1 . VAL   B 1 204 ? 19.635 25.845  20.162  1.00 63.87  ?  360 VAL   B CG1 1 
ATOM   3959 C  CG2 . VAL   B 1 204 ? 20.534 25.495  17.874  1.00 38.96  ?  360 VAL   B CG2 1 
ATOM   3960 N  N   . PRO   B 1 205 ? 17.065 27.961  19.922  1.00 36.02  ?  361 PRO   B N   1 
ATOM   3961 C  CA  . PRO   B 1 205 ? 16.508 28.943  20.864  1.00 37.91  ?  361 PRO   B CA  1 
ATOM   3962 C  C   . PRO   B 1 205 ? 17.438 29.138  22.054  1.00 47.87  ?  361 PRO   B C   1 
ATOM   3963 O  O   . PRO   B 1 205 ? 17.858 28.172  22.694  1.00 46.21  ?  361 PRO   B O   1 
ATOM   3964 C  CB  . PRO   B 1 205 ? 15.171 28.322  21.282  1.00 36.25  ?  361 PRO   B CB  1 
ATOM   3965 C  CG  . PRO   B 1 205 ? 15.351 26.862  21.080  1.00 40.98  ?  361 PRO   B CG  1 
ATOM   3966 C  CD  . PRO   B 1 205 ? 16.316 26.693  19.936  1.00 40.94  ?  361 PRO   B CD  1 
ATOM   3967 N  N   . LYS   B 1 206 ? 17.761 30.397  22.348  1.00 44.52  ?  362 LYS   B N   1 
ATOM   3968 C  CA  . LYS   B 1 206 ? 18.742 30.709  23.379  1.00 39.13  ?  362 LYS   B CA  1 
ATOM   3969 C  C   . LYS   B 1 206 ? 18.529 32.132  23.868  1.00 41.96  ?  362 LYS   B C   1 
ATOM   3970 O  O   . LYS   B 1 206 ? 18.354 33.042  23.056  1.00 52.60  ?  362 LYS   B O   1 
ATOM   3971 C  CB  . LYS   B 1 206 ? 20.163 30.535  22.828  1.00 40.67  ?  362 LYS   B CB  1 
ATOM   3972 C  CG  . LYS   B 1 206 ? 21.247 30.714  23.863  1.00 48.91  ?  362 LYS   B CG  1 
ATOM   3973 C  CD  . LYS   B 1 206 ? 21.365 29.485  24.736  1.00 55.26  ?  362 LYS   B CD  1 
ATOM   3974 C  CE  . LYS   B 1 206 ? 22.300 29.740  25.899  1.00 68.90  ?  362 LYS   B CE  1 
ATOM   3975 N  NZ  . LYS   B 1 206 ? 22.329 28.590  26.838  1.00 78.44  ?  362 LYS   B NZ  1 
ATOM   3976 N  N   . HIS   B 1 207 ? 18.549 32.330  25.182  1.00 44.66  ?  363 HIS   B N   1 
ATOM   3977 C  CA  . HIS   B 1 207 ? 18.352 33.671  25.707  1.00 57.94  ?  363 HIS   B CA  1 
ATOM   3978 C  C   . HIS   B 1 207 ? 19.663 34.451  25.727  1.00 45.33  ?  363 HIS   B C   1 
ATOM   3979 O  O   . HIS   B 1 207 ? 20.756 33.888  25.860  1.00 56.64  ?  363 HIS   B O   1 
ATOM   3980 C  CB  . HIS   B 1 207 ? 17.735 33.645  27.108  1.00 42.96  ?  363 HIS   B CB  1 
ATOM   3981 C  CG  . HIS   B 1 207 ? 18.475 32.800  28.101  1.00 69.05  ?  363 HIS   B CG  1 
ATOM   3982 N  ND1 . HIS   B 1 207 ? 18.133 32.759  29.438  1.00 62.52  ?  363 HIS   B ND1 1 
ATOM   3983 C  CD2 . HIS   B 1 207 ? 19.521 31.953  27.953  1.00 73.40  ?  363 HIS   B CD2 1 
ATOM   3984 C  CE1 . HIS   B 1 207 ? 18.941 31.924  30.068  1.00 66.26  ?  363 HIS   B CE1 1 
ATOM   3985 N  NE2 . HIS   B 1 207 ? 19.792 31.423  29.190  1.00 78.92  ?  363 HIS   B NE2 1 
ATOM   3986 N  N   . ALA   B 1 208 ? 19.532 35.763  25.561  1.00 55.37  ?  364 ALA   B N   1 
ATOM   3987 C  CA  . ALA   B 1 208 ? 20.648 36.685  25.477  1.00 57.63  ?  364 ALA   B CA  1 
ATOM   3988 C  C   . ALA   B 1 208 ? 20.554 37.696  26.610  1.00 61.13  ?  364 ALA   B C   1 
ATOM   3989 O  O   . ALA   B 1 208 ? 19.462 38.046  27.067  1.00 70.78  ?  364 ALA   B O   1 
ATOM   3990 C  CB  . ALA   B 1 208 ? 20.668 37.411  24.125  1.00 45.02  ?  364 ALA   B CB  1 
ATOM   3991 N  N   . LYS   B 1 209 ? 21.712 38.165  27.058  1.00 78.91  ?  365 LYS   B N   1 
ATOM   3992 C  CA  . LYS   B 1 209 ? 21.773 39.126  28.150  1.00 77.49  ?  365 LYS   B CA  1 
ATOM   3993 C  C   . LYS   B 1 209 ? 21.713 40.555  27.620  1.00 60.04  ?  365 LYS   B C   1 
ATOM   3994 O  O   . LYS   B 1 209 ? 21.603 40.771  26.412  1.00 87.27  ?  365 LYS   B O   1 
ATOM   3995 C  CB  . LYS   B 1 209 ? 23.045 38.921  28.975  1.00 64.65  ?  365 LYS   B CB  1 
ATOM   3996 N  N   . GLN   B 1 215 ? 16.748 39.075  27.381  1.00 67.02  ?  371 GLN   B N   1 
ATOM   3997 C  CA  . GLN   B 1 215 ? 15.853 38.898  26.243  1.00 66.86  ?  371 GLN   B CA  1 
ATOM   3998 C  C   . GLN   B 1 215 ? 15.676 37.399  25.992  1.00 67.85  ?  371 GLN   B C   1 
ATOM   3999 O  O   . GLN   B 1 215 ? 16.656 36.679  25.790  1.00 68.41  ?  371 GLN   B O   1 
ATOM   4000 C  CB  . GLN   B 1 215 ? 16.406 39.601  25.003  1.00 54.51  ?  371 GLN   B CB  1 
ATOM   4001 C  CG  . GLN   B 1 215 ? 15.556 39.402  23.765  1.00 53.30  ?  371 GLN   B CG  1 
ATOM   4002 C  CD  . GLN   B 1 215 ? 14.290 40.230  23.815  1.00 64.93  ?  371 GLN   B CD  1 
ATOM   4003 O  OE1 . GLN   B 1 215 ? 14.342 41.451  23.954  1.00 66.68  ?  371 GLN   B OE1 1 
ATOM   4004 N  NE2 . GLN   B 1 215 ? 13.143 39.570  23.705  1.00 64.94  ?  371 GLN   B NE2 1 
ATOM   4005 N  N   . GLU   B 1 216 ? 14.422 36.946  25.992  1.00 60.28  ?  372 GLU   B N   1 
ATOM   4006 C  CA  . GLU   B 1 216 ? 14.117 35.528  26.105  1.00 70.13  ?  372 GLU   B CA  1 
ATOM   4007 C  C   . GLU   B 1 216 ? 13.375 34.973  24.890  1.00 70.14  ?  372 GLU   B C   1 
ATOM   4008 O  O   . GLU   B 1 216 ? 12.808 33.876  24.970  1.00 69.86  ?  372 GLU   B O   1 
ATOM   4009 C  CB  . GLU   B 1 216 ? 13.303 35.259  27.375  1.00 47.32  ?  372 GLU   B CB  1 
ATOM   4010 C  CG  . GLU   B 1 216 ? 14.148 34.852  28.568  1.00 62.70  ?  372 GLU   B CG  1 
ATOM   4011 C  CD  . GLU   B 1 216 ? 14.356 33.345  28.643  1.00 74.99  ?  372 GLU   B CD  1 
ATOM   4012 O  OE1 . GLU   B 1 216 ? 14.720 32.758  27.605  1.00 71.72  ?  372 GLU   B OE1 1 
ATOM   4013 O  OE2 . GLU   B 1 216 ? 14.169 32.745  29.726  1.00 89.81  -1 372 GLU   B OE2 1 
ATOM   4014 N  N   . GLU   B 1 217 ? 13.375 35.681  23.761  1.00 54.30  ?  373 GLU   B N   1 
ATOM   4015 C  CA  . GLU   B 1 217 ? 12.738 35.163  22.551  1.00 47.52  ?  373 GLU   B CA  1 
ATOM   4016 C  C   . GLU   B 1 217 ? 13.687 35.246  21.363  1.00 61.41  ?  373 GLU   B C   1 
ATOM   4017 O  O   . GLU   B 1 217 ? 13.269 35.474  20.224  1.00 53.03  ?  373 GLU   B O   1 
ATOM   4018 C  CB  . GLU   B 1 217 ? 11.429 35.893  22.261  1.00 68.63  ?  373 GLU   B CB  1 
ATOM   4019 C  CG  . GLU   B 1 217 ? 10.256 34.958  22.058  1.00 69.30  ?  373 GLU   B CG  1 
ATOM   4020 C  CD  . GLU   B 1 217 ? 9.967  34.105  23.282  1.00 74.55  ?  373 GLU   B CD  1 
ATOM   4021 O  OE1 . GLU   B 1 217 ? 9.627  34.677  24.338  1.00 65.77  ?  373 GLU   B OE1 1 
ATOM   4022 O  OE2 . GLU   B 1 217 ? 10.078 32.862  23.192  1.00 75.77  -1 373 GLU   B OE2 1 
ATOM   4023 N  N   . THR   B 1 218 ? 14.978 35.050  21.608  1.00 48.14  ?  374 THR   B N   1 
ATOM   4024 C  CA  . THR   B 1 218 ? 15.985 35.096  20.559  1.00 53.06  ?  374 THR   B CA  1 
ATOM   4025 C  C   . THR   B 1 218 ? 16.444 33.692  20.183  1.00 43.13  ?  374 THR   B C   1 
ATOM   4026 O  O   . THR   B 1 218 ? 16.261 32.727  20.929  1.00 46.66  ?  374 THR   B O   1 
ATOM   4027 C  CB  . THR   B 1 218 ? 17.188 35.940  20.991  1.00 44.24  ?  374 THR   B CB  1 
ATOM   4028 O  OG1 . THR   B 1 218 ? 17.427 35.748  22.391  1.00 46.89  ?  374 THR   B OG1 1 
ATOM   4029 C  CG2 . THR   B 1 218 ? 16.930 37.416  20.719  1.00 58.32  ?  374 THR   B CG2 1 
ATOM   4030 N  N   . TRP   B 1 219 ? 17.039 33.592  18.997  1.00 40.50  ?  375 TRP   B N   1 
ATOM   4031 C  CA  . TRP   B 1 219 ? 17.626 32.359  18.492  1.00 35.12  ?  375 TRP   B CA  1 
ATOM   4032 C  C   . TRP   B 1 219 ? 19.080 32.641  18.136  1.00 35.55  ?  375 TRP   B C   1 
ATOM   4033 O  O   . TRP   B 1 219 ? 19.407 33.730  17.658  1.00 42.51  ?  375 TRP   B O   1 
ATOM   4034 C  CB  . TRP   B 1 219 ? 16.854 31.839  17.266  1.00 37.11  ?  375 TRP   B CB  1 
ATOM   4035 C  CG  . TRP   B 1 219 ? 15.380 31.606  17.517  1.00 41.80  ?  375 TRP   B CG  1 
ATOM   4036 C  CD1 . TRP   B 1 219 ? 14.419 32.563  17.692  1.00 41.02  ?  375 TRP   B CD1 1 
ATOM   4037 C  CD2 . TRP   B 1 219 ? 14.700 30.343  17.589  1.00 36.38  ?  375 TRP   B CD2 1 
ATOM   4038 N  NE1 . TRP   B 1 219 ? 13.192 31.976  17.883  1.00 38.89  ?  375 TRP   B NE1 1 
ATOM   4039 C  CE2 . TRP   B 1 219 ? 13.336 30.615  17.823  1.00 44.64  ?  375 TRP   B CE2 1 
ATOM   4040 C  CE3 . TRP   B 1 219 ? 15.112 29.011  17.484  1.00 39.36  ?  375 TRP   B CE3 1 
ATOM   4041 C  CZ2 . TRP   B 1 219 ? 12.384 29.606  17.955  1.00 39.52  ?  375 TRP   B CZ2 1 
ATOM   4042 C  CZ3 . TRP   B 1 219 ? 14.161 28.010  17.614  1.00 38.77  ?  375 TRP   B CZ3 1 
ATOM   4043 C  CH2 . TRP   B 1 219 ? 12.815 28.314  17.848  1.00 42.20  ?  375 TRP   B CH2 1 
ATOM   4044 N  N   . ARG   B 1 220 ? 19.950 31.664  18.376  1.00 31.30  ?  376 ARG   B N   1 
ATOM   4045 C  CA  . ARG   B 1 220 ? 21.385 31.808  18.180  1.00 30.70  ?  376 ARG   B CA  1 
ATOM   4046 C  C   . ARG   B 1 220 ? 21.858 30.920  17.035  1.00 29.29  ?  376 ARG   B C   1 
ATOM   4047 O  O   . ARG   B 1 220 ? 21.383 29.792  16.874  1.00 31.22  ?  376 ARG   B O   1 
ATOM   4048 C  CB  . ARG   B 1 220 ? 22.157 31.458  19.455  1.00 28.48  ?  376 ARG   B CB  1 
ATOM   4049 C  CG  . ARG   B 1 220 ? 23.617 31.868  19.410  1.00 32.87  ?  376 ARG   B CG  1 
ATOM   4050 C  CD  . ARG   B 1 220 ? 24.328 31.589  20.720  1.00 32.22  ?  376 ARG   B CD  1 
ATOM   4051 N  NE  . ARG   B 1 220 ? 24.419 30.162  21.002  1.00 32.41  ?  376 ARG   B NE  1 
ATOM   4052 C  CZ  . ARG   B 1 220 ? 24.747 29.654  22.182  1.00 43.78  ?  376 ARG   B CZ  1 
ATOM   4053 N  NH1 . ARG   B 1 220 ? 25.047 30.433  23.208  1.00 49.55  ?  376 ARG   B NH1 1 
ATOM   4054 N  NH2 . ARG   B 1 220 ? 24.776 28.333  22.335  1.00 45.32  ?  376 ARG   B NH2 1 
ATOM   4055 N  N   . LEU   B 1 221 ? 22.805 31.440  16.255  1.00 27.07  ?  377 LEU   B N   1 
ATOM   4056 C  CA  . LEU   B 1 221 ? 23.324 30.719  15.099  1.00 28.86  ?  377 LEU   B CA  1 
ATOM   4057 C  C   . LEU   B 1 221 ? 24.083 29.468  15.524  1.00 35.62  ?  377 LEU   B C   1 
ATOM   4058 O  O   . LEU   B 1 221 ? 24.843 29.478  16.497  1.00 31.95  ?  377 LEU   B O   1 
ATOM   4059 C  CB  . LEU   B 1 221 ? 24.245 31.629  14.286  1.00 27.44  ?  377 LEU   B CB  1 
ATOM   4060 C  CG  . LEU   B 1 221 ? 23.571 32.732  13.471  1.00 33.32  ?  377 LEU   B CG  1 
ATOM   4061 C  CD1 . LEU   B 1 221 ? 24.604 33.582  12.747  1.00 36.50  ?  377 LEU   B CD1 1 
ATOM   4062 C  CD2 . LEU   B 1 221 ? 22.584 32.131  12.484  1.00 31.21  ?  377 LEU   B CD2 1 
ATOM   4063 N  N   . SER   B 1 222 ? 23.887 28.388  14.772  1.00 29.28  ?  378 SER   B N   1 
ATOM   4064 C  CA  . SER   B 1 222 ? 24.562 27.123  15.011  1.00 31.02  ?  378 SER   B CA  1 
ATOM   4065 C  C   . SER   B 1 222 ? 25.122 26.602  13.696  1.00 35.74  ?  378 SER   B C   1 
ATOM   4066 O  O   . SER   B 1 222 ? 24.424 26.585  12.665  1.00 29.06  ?  378 SER   B O   1 
ATOM   4067 C  CB  . SER   B 1 222 ? 23.626 26.087  15.642  1.00 27.18  ?  378 SER   B CB  1 
ATOM   4068 O  OG  . SER   B 1 222 ? 24.346 24.925  16.023  1.00 29.59  ?  378 SER   B OG  1 
ATOM   4069 N  N   . PHE   B 1 223 ? 26.395 26.193  13.755  1.00 28.29  ?  379 PHE   B N   1 
ATOM   4070 C  CA  . PHE   B 1 223 ? 27.157 25.655  12.636  1.00 25.66  ?  379 PHE   B CA  1 
ATOM   4071 C  C   . PHE   B 1 223 ? 27.847 24.349  13.014  1.00 25.66  ?  379 PHE   B C   1 
ATOM   4072 O  O   . PHE   B 1 223 ? 28.870 24.002  12.416  1.00 34.65  ?  379 PHE   B O   1 
ATOM   4073 C  CB  . PHE   B 1 223 ? 28.200 26.670  12.160  1.00 28.73  ?  379 PHE   B CB  1 
ATOM   4074 C  CG  . PHE   B 1 223 ? 27.613 27.925  11.590  1.00 24.26  ?  379 PHE   B CG  1 
ATOM   4075 C  CD1 . PHE   B 1 223 ? 27.058 27.928  10.322  1.00 30.95  ?  379 PHE   B CD1 1 
ATOM   4076 C  CD2 . PHE   B 1 223 ? 27.608 29.100  12.323  1.00 25.26  ?  379 PHE   B CD2 1 
ATOM   4077 C  CE1 . PHE   B 1 223 ? 26.517 29.083  9.791   1.00 36.47  ?  379 PHE   B CE1 1 
ATOM   4078 C  CE2 . PHE   B 1 223 ? 27.066 30.260  11.798  1.00 31.62  ?  379 PHE   B CE2 1 
ATOM   4079 C  CZ  . PHE   B 1 223 ? 26.519 30.250  10.529  1.00 32.91  ?  379 PHE   B CZ  1 
ATOM   4080 N  N   . SER   B 1 224 ? 27.319 23.627  14.003  1.00 28.55  ?  380 SER   B N   1 
ATOM   4081 C  CA  . SER   B 1 224 ? 27.996 22.432  14.493  1.00 27.69  ?  380 SER   B CA  1 
ATOM   4082 C  C   . SER   B 1 224 ? 28.139 21.368  13.406  1.00 32.31  ?  380 SER   B C   1 
ATOM   4083 O  O   . SER   B 1 224 ? 29.062 20.543  13.460  1.00 26.42  ?  380 SER   B O   1 
ATOM   4084 C  CB  . SER   B 1 224 ? 27.242 21.882  15.704  1.00 42.85  ?  380 SER   B CB  1 
ATOM   4085 O  OG  . SER   B 1 224 ? 25.899 21.601  15.365  1.00 57.29  ?  380 SER   B OG  1 
ATOM   4086 N  N   . HIS   B 1 225 ? 27.248 21.370  12.406  1.00 27.62  ?  381 HIS   B N   1 
ATOM   4087 C  CA  . HIS   B 1 225 ? 27.419 20.460  11.277  1.00 28.63  ?  381 HIS   B CA  1 
ATOM   4088 C  C   . HIS   B 1 225 ? 28.693 20.781  10.505  1.00 24.09  ?  381 HIS   B C   1 
ATOM   4089 O  O   . HIS   B 1 225 ? 29.449 19.873  10.129  1.00 26.79  ?  381 HIS   B O   1 
ATOM   4090 C  CB  . HIS   B 1 225 ? 26.188 20.505  10.365  1.00 25.27  ?  381 HIS   B CB  1 
ATOM   4091 C  CG  . HIS   B 1 225 ? 25.890 21.855  9.783   1.00 24.48  ?  381 HIS   B CG  1 
ATOM   4092 N  ND1 . HIS   B 1 225 ? 25.741 22.988  10.554  1.00 24.95  ?  381 HIS   B ND1 1 
ATOM   4093 C  CD2 . HIS   B 1 225 ? 25.674 22.243  8.503   1.00 30.71  ?  381 HIS   B CD2 1 
ATOM   4094 C  CE1 . HIS   B 1 225 ? 25.470 24.019  9.774   1.00 26.15  ?  381 HIS   B CE1 1 
ATOM   4095 N  NE2 . HIS   B 1 225 ? 25.420 23.593  8.524   1.00 30.59  ?  381 HIS   B NE2 1 
ATOM   4096 N  N   . ILE   B 1 226 ? 28.957 22.069  10.280  1.00 27.96  ?  382 ILE   B N   1 
ATOM   4097 C  CA  . ILE   B 1 226 ? 30.189 22.467  9.606   1.00 19.47  ?  382 ILE   B CA  1 
ATOM   4098 C  C   . ILE   B 1 226 ? 31.399 22.066  10.438  1.00 28.39  ?  382 ILE   B C   1 
ATOM   4099 O  O   . ILE   B 1 226 ? 32.424 21.635  9.896   1.00 29.89  ?  382 ILE   B O   1 
ATOM   4100 C  CB  . ILE   B 1 226 ? 30.179 23.978  9.317   1.00 28.13  ?  382 ILE   B CB  1 
ATOM   4101 C  CG1 . ILE   B 1 226 ? 28.911 24.372  8.552   1.00 27.55  ?  382 ILE   B CG1 1 
ATOM   4102 C  CG2 . ILE   B 1 226 ? 31.420 24.370  8.532   1.00 20.49  ?  382 ILE   B CG2 1 
ATOM   4103 C  CD1 . ILE   B 1 226 ? 28.780 23.710  7.201   1.00 28.33  ?  382 ILE   B CD1 1 
ATOM   4104 N  N   . GLU   B 1 227 ? 31.301 22.199  11.763  1.00 26.02  ?  383 GLU   B N   1 
ATOM   4105 C  CA  . GLU   B 1 227 ? 32.401 21.807  12.639  1.00 26.42  ?  383 GLU   B CA  1 
ATOM   4106 C  C   . GLU   B 1 227 ? 32.716 20.327  12.487  1.00 28.18  ?  383 GLU   B C   1 
ATOM   4107 O  O   . GLU   B 1 227 ? 33.883 19.933  12.362  1.00 23.08  ?  383 GLU   B O   1 
ATOM   4108 C  CB  . GLU   B 1 227 ? 32.052 22.112  14.096  1.00 27.33  ?  383 GLU   B CB  1 
ATOM   4109 C  CG  . GLU   B 1 227 ? 31.772 23.564  14.410  1.00 42.44  ?  383 GLU   B CG  1 
ATOM   4110 C  CD  . GLU   B 1 227 ? 31.183 23.743  15.799  1.00 45.54  ?  383 GLU   B CD  1 
ATOM   4111 O  OE1 . GLU   B 1 227 ? 31.405 22.866  16.663  1.00 40.95  ?  383 GLU   B OE1 1 
ATOM   4112 O  OE2 . GLU   B 1 227 ? 30.503 24.763  16.029  1.00 45.97  -1 383 GLU   B OE2 1 
ATOM   4113 N  N   . LYS   B 1 228 ? 31.679 19.490  12.528  1.00 20.82  ?  384 LYS   B N   1 
ATOM   4114 C  CA  . LYS   B 1 228 ? 31.864 18.053  12.351  1.00 26.05  ?  384 LYS   B CA  1 
ATOM   4115 C  C   . LYS   B 1 228 ? 32.518 17.749  11.010  1.00 31.35  ?  384 LYS   B C   1 
ATOM   4116 O  O   . LYS   B 1 228 ? 33.483 16.975  10.934  1.00 29.16  ?  384 LYS   B O   1 
ATOM   4117 C  CB  . LYS   B 1 228 ? 30.515 17.339  12.463  1.00 31.86  ?  384 LYS   B CB  1 
ATOM   4118 C  CG  . LYS   B 1 228 ? 30.558 15.878  12.052  1.00 31.31  ?  384 LYS   B CG  1 
ATOM   4119 C  CD  . LYS   B 1 228 ? 29.175 15.246  12.050  1.00 47.91  ?  384 LYS   B CD  1 
ATOM   4120 C  CE  . LYS   B 1 228 ? 29.240 13.808  11.558  1.00 55.47  ?  384 LYS   B CE  1 
ATOM   4121 N  NZ  . LYS   B 1 228 ? 28.821 13.694  10.133  1.00 82.95  ?  384 LYS   B NZ  1 
ATOM   4122 N  N   . GLU   B 1 229 ? 32.044 18.393  9.957   1.00 28.65  ?  385 GLU   B N   1 
ATOM   4123 C  CA  . GLU   B 1 229 ? 32.587 18.142  8.603   1.00 23.86  ?  385 GLU   B CA  1 
ATOM   4124 C  C   . GLU   B 1 229 ? 34.078 18.511  8.565   1.00 27.46  ?  385 GLU   B C   1 
ATOM   4125 O  O   . GLU   B 1 229 ? 34.858 17.721  8.026   1.00 32.09  ?  385 GLU   B O   1 
ATOM   4126 C  CB  . GLU   B 1 229 ? 31.789 18.908  7.554   1.00 24.35  ?  385 GLU   B CB  1 
ATOM   4127 C  CG  . GLU   B 1 229 ? 30.385 18.353  7.344   1.00 45.01  ?  385 GLU   B CG  1 
ATOM   4128 C  CD  . GLU   B 1 229 ? 29.847 18.590  5.949   1.00 52.43  ?  385 GLU   B CD  1 
ATOM   4129 O  OE1 . GLU   B 1 229 ? 30.663 18.836  5.041   1.00 47.39  ?  385 GLU   B OE1 1 
ATOM   4130 O  OE2 . GLU   B 1 229 ? 28.616 18.524  5.770   1.00 68.41  -1 385 GLU   B OE2 1 
ATOM   4131 N  N   . ILE   B 1 230 ? 34.462 19.646  9.139   1.00 20.64  ?  386 ILE   B N   1 
ATOM   4132 C  CA  . ILE   B 1 230 ? 35.891 20.057  9.027   1.00 22.83  ?  386 ILE   B CA  1 
ATOM   4133 C  C   . ILE   B 1 230 ? 36.761 19.134  9.899   1.00 32.74  ?  386 ILE   B C   1 
ATOM   4134 O  O   . ILE   B 1 230 ? 37.905 18.915  9.527   1.00 34.06  ?  386 ILE   B O   1 
ATOM   4135 C  CB  . ILE   B 1 230 ? 36.115 21.557  9.300   1.00 36.83  ?  386 ILE   B CB  1 
ATOM   4136 C  CG1 . ILE   B 1 230 ? 35.688 21.990  10.686  1.00 38.45  ?  386 ILE   B CG1 1 
ATOM   4137 C  CG2 . ILE   B 1 230 ? 35.430 22.402  8.226   1.00 37.06  ?  386 ILE   B CG2 1 
ATOM   4138 C  CD1 . ILE   B 1 230 ? 35.577 23.497  10.831  1.00 37.37  ?  386 ILE   B CD1 1 
ATOM   4139 N  N   . LEU   B 1 231 ? 36.209 18.573  10.970  1.00 31.08  ?  387 LEU   B N   1 
ATOM   4140 C  CA  . LEU   B 1 231 ? 37.013 17.712  11.866  1.00 29.54  ?  387 LEU   B CA  1 
ATOM   4141 C  C   . LEU   B 1 231 ? 37.210 16.334  11.217  1.00 24.16  ?  387 LEU   B C   1 
ATOM   4142 O  O   . LEU   B 1 231 ? 38.291 15.765  11.391  1.00 29.27  ?  387 LEU   B O   1 
ATOM   4143 C  CB  . LEU   B 1 231 ? 36.384 17.604  13.249  1.00 24.19  ?  387 LEU   B CB  1 
ATOM   4144 C  CG  . LEU   B 1 231 ? 36.841 18.661  14.250  1.00 40.91  ?  387 LEU   B CG  1 
ATOM   4145 C  CD1 . LEU   B 1 231 ? 35.874 18.748  15.408  1.00 41.16  ?  387 LEU   B CD1 1 
ATOM   4146 C  CD2 . LEU   B 1 231 ? 38.244 18.328  14.712  1.00 36.24  ?  387 LEU   B CD2 1 
ATOM   4147 N  N   . ASN   B 1 232 ? 36.195 15.840  10.517  1.00 21.06  ?  388 ASN   B N   1 
ATOM   4148 C  CA  . ASN   B 1 232 ? 36.307 14.520  9.907   1.00 28.93  ?  388 ASN   B CA  1 
ATOM   4149 C  C   . ASN   B 1 232 ? 36.784 14.571  8.458   1.00 30.28  ?  388 ASN   B C   1 
ATOM   4150 O  O   . ASN   B 1 232 ? 36.864 13.524  7.803   1.00 38.30  ?  388 ASN   B O   1 
ATOM   4151 C  CB  . ASN   B 1 232 ? 34.966 13.787  10.013  1.00 24.99  ?  388 ASN   B CB  1 
ATOM   4152 C  CG  . ASN   B 1 232 ? 34.611 13.442  11.453  1.00 37.68  ?  388 ASN   B CG  1 
ATOM   4153 O  OD1 . ASN   B 1 232 ? 35.418 12.865  12.183  1.00 36.24  ?  388 ASN   B OD1 1 
ATOM   4154 N  ND2 . ASN   B 1 232 ? 33.410 13.820  11.876  1.00 33.87  ?  388 ASN   B ND2 1 
ATOM   4155 N  N   . ASN   B 1 233 ? 37.118 15.763  7.950   1.00 19.04  ?  389 ASN   B N   1 
ATOM   4156 C  CA  . ASN   B 1 233 ? 37.725 15.979  6.634   1.00 23.73  ?  389 ASN   B CA  1 
ATOM   4157 C  C   . ASN   B 1 233 ? 38.658 17.180  6.825   1.00 16.30  ?  389 ASN   B C   1 
ATOM   4158 O  O   . ASN   B 1 233 ? 38.358 18.312  6.437   1.00 22.00  ?  389 ASN   B O   1 
ATOM   4159 C  CB  . ASN   B 1 233 ? 36.675 16.221  5.549   1.00 17.95  ?  389 ASN   B CB  1 
ATOM   4160 C  CG  . ASN   B 1 233 ? 37.220 16.013  4.149   1.00 25.26  ?  389 ASN   B CG  1 
ATOM   4161 O  OD1 . ASN   B 1 233 ? 38.413 15.776  3.962   1.00 23.20  ?  389 ASN   B OD1 1 
ATOM   4162 N  ND2 . ASN   B 1 233 ? 36.343 16.091  3.156   1.00 14.90  ?  389 ASN   B ND2 1 
ATOM   4163 N  N   . HIS   B 1 234 ? 39.814 16.913  7.437   1.00 22.28  ?  390 HIS   B N   1 
ATOM   4164 C  CA  . HIS   B 1 234 ? 40.541 17.920  8.198   1.00 17.43  ?  390 HIS   B CA  1 
ATOM   4165 C  C   . HIS   B 1 234 ? 41.912 18.293  7.652   1.00 19.45  ?  390 HIS   B C   1 
ATOM   4166 O  O   . HIS   B 1 234 ? 42.562 19.176  8.223   1.00 17.19  ?  390 HIS   B O   1 
ATOM   4167 C  CB  . HIS   B 1 234 ? 40.707 17.440  9.648   1.00 17.34  ?  390 HIS   B CB  1 
ATOM   4168 C  CG  . HIS   B 1 234 ? 41.432 16.133  9.772   1.00 24.07  ?  390 HIS   B CG  1 
ATOM   4169 N  ND1 . HIS   B 1 234 ? 40.823 14.987  10.235  1.00 24.79  ?  390 HIS   B ND1 1 
ATOM   4170 C  CD2 . HIS   B 1 234 ? 42.714 15.793  9.498   1.00 18.99  ?  390 HIS   B CD2 1 
ATOM   4171 C  CE1 . HIS   B 1 234 ? 41.697 13.996  10.240  1.00 31.49  ?  390 HIS   B CE1 1 
ATOM   4172 N  NE2 . HIS   B 1 234 ? 42.853 14.458  9.798   1.00 28.46  ?  390 HIS   B NE2 1 
ATOM   4173 N  N   . GLY   B 1 235 ? 42.382 17.652  6.590   1.00 21.05  ?  391 GLY   B N   1 
ATOM   4174 C  CA  . GLY   B 1 235 ? 43.710 17.910  6.084   1.00 21.95  ?  391 GLY   B CA  1 
ATOM   4175 C  C   . GLY   B 1 235 ? 43.705 18.768  4.834   1.00 17.03  ?  391 GLY   B C   1 
ATOM   4176 O  O   . GLY   B 1 235 ? 42.686 18.922  4.165   1.00 16.89  ?  391 GLY   B O   1 
ATOM   4177 N  N   . LYS   B 1 236 ? 44.868 19.351  4.538   1.00 26.44  ?  392 LYS   B N   1 
ATOM   4178 C  CA  . LYS   B 1 236 ? 45.056 19.972  3.232   1.00 15.68  ?  392 LYS   B CA  1 
ATOM   4179 C  C   . LYS   B 1 236 ? 45.021 18.919  2.132   1.00 22.24  ?  392 LYS   B C   1 
ATOM   4180 O  O   . LYS   B 1 236 ? 44.438 19.140  1.065   1.00 19.58  ?  392 LYS   B O   1 
ATOM   4181 C  CB  . LYS   B 1 236 ? 46.375 20.744  3.196   1.00 20.55  ?  392 LYS   B CB  1 
ATOM   4182 C  CG  . LYS   B 1 236 ? 46.734 21.290  1.820   1.00 13.28  ?  392 LYS   B CG  1 
ATOM   4183 C  CD  . LYS   B 1 236 ? 47.954 22.197  1.876   1.00 15.69  ?  392 LYS   B CD  1 
ATOM   4184 C  CE  . LYS   B 1 236 ? 47.608 23.559  2.458   1.00 20.44  ?  392 LYS   B CE  1 
ATOM   4185 N  NZ  . LYS   B 1 236 ? 46.434 24.174  1.781   1.00 22.55  ?  392 LYS   B NZ  1 
ATOM   4186 N  N   . SER   B 1 237 ? 45.639 17.768  2.383   1.00 17.15  ?  393 SER   B N   1 
ATOM   4187 C  CA  . SER   B 1 237 ? 45.555 16.638  1.474   1.00 24.30  ?  393 SER   B CA  1 
ATOM   4188 C  C   . SER   B 1 237 ? 44.244 15.893  1.683   1.00 21.81  ?  393 SER   B C   1 
ATOM   4189 O  O   . SER   B 1 237 ? 43.809 15.676  2.818   1.00 18.75  ?  393 SER   B O   1 
ATOM   4190 C  CB  . SER   B 1 237 ? 46.735 15.691  1.691   1.00 18.58  ?  393 SER   B CB  1 
ATOM   4191 O  OG  . SER   B 1 237 ? 46.522 14.453  1.036   1.00 23.21  ?  393 SER   B OG  1 
ATOM   4192 N  N   . LYS   B 1 238 ? 43.611 15.501  0.575   1.00 16.88  ?  394 LYS   B N   1 
ATOM   4193 C  CA  . LYS   B 1 238 ? 42.363 14.753  0.664   1.00 17.82  ?  394 LYS   B CA  1 
ATOM   4194 C  C   . LYS   B 1 238 ? 42.564 13.362  1.248   1.00 22.01  ?  394 LYS   B C   1 
ATOM   4195 O  O   . LYS   B 1 238 ? 41.616 12.794  1.802   1.00 20.66  ?  394 LYS   B O   1 
ATOM   4196 C  CB  . LYS   B 1 238 ? 41.707 14.653  -0.712  1.00 23.61  ?  394 LYS   B CB  1 
ATOM   4197 C  CG  . LYS   B 1 238 ? 41.119 15.961  -1.216  1.00 17.55  ?  394 LYS   B CG  1 
ATOM   4198 C  CD  . LYS   B 1 238 ? 40.987 15.959  -2.730  1.00 16.57  ?  394 LYS   B CD  1 
ATOM   4199 C  CE  . LYS   B 1 238 ? 40.673 17.348  -3.264  1.00 17.22  ?  394 LYS   B CE  1 
ATOM   4200 N  NZ  . LYS   B 1 238 ? 40.515 17.339  -4.745  1.00 22.92  ?  394 LYS   B NZ  1 
ATOM   4201 N  N   . THR   B 1 239 ? 43.768 12.798  1.137   1.00 18.37  ?  395 THR   B N   1 
ATOM   4202 C  CA  . THR   B 1 239 ? 44.078 11.502  1.724   1.00 26.78  ?  395 THR   B CA  1 
ATOM   4203 C  C   . THR   B 1 239 ? 44.763 11.625  3.078   1.00 23.44  ?  395 THR   B C   1 
ATOM   4204 O  O   . THR   B 1 239 ? 45.465 10.697  3.494   1.00 21.42  ?  395 THR   B O   1 
ATOM   4205 C  CB  . THR   B 1 239 ? 44.955 10.675  0.782   1.00 22.98  ?  395 THR   B CB  1 
ATOM   4206 O  OG1 . THR   B 1 239 ? 46.013 11.494  0.268   1.00 28.19  ?  395 THR   B OG1 1 
ATOM   4207 C  CG2 . THR   B 1 239 ? 44.140 10.111  -0.368  1.00 21.91  ?  395 THR   B CG2 1 
ATOM   4208 N  N   . CYS   B 1 240 ? 44.594 12.753  3.763   1.00 15.16  ?  396 CYS   B N   1 
ATOM   4209 C  CA  . CYS   B 1 240 ? 45.110 12.870  5.118   1.00 19.63  ?  396 CYS   B CA  1 
ATOM   4210 C  C   . CYS   B 1 240 ? 44.513 11.782  5.998   1.00 18.89  ?  396 CYS   B C   1 
ATOM   4211 O  O   . CYS   B 1 240 ? 43.293 11.595  6.034   1.00 28.14  ?  396 CYS   B O   1 
ATOM   4212 C  CB  . CYS   B 1 240 ? 44.796 14.249  5.699   1.00 24.97  ?  396 CYS   B CB  1 
ATOM   4213 S  SG  . CYS   B 1 240 ? 45.626 14.560  7.278   1.00 23.17  ?  396 CYS   B SG  1 
ATOM   4214 N  N   . CYS   B 1 241 ? 45.389 11.041  6.674   1.00 17.20  ?  397 CYS   B N   1 
ATOM   4215 C  CA  . CYS   B 1 241 ? 45.056 9.995   7.636   1.00 19.04  ?  397 CYS   B CA  1 
ATOM   4216 C  C   . CYS   B 1 241 ? 44.469 8.745   6.992   1.00 28.36  ?  397 CYS   B C   1 
ATOM   4217 O  O   . CYS   B 1 241 ? 43.911 7.900   7.702   1.00 23.38  ?  397 CYS   B O   1 
ATOM   4218 C  CB  . CYS   B 1 241 ? 44.097 10.512  8.714   1.00 23.36  ?  397 CYS   B CB  1 
ATOM   4219 S  SG  . CYS   B 1 241 ? 44.900 11.612  9.896   1.00 22.64  ?  397 CYS   B SG  1 
ATOM   4220 N  N   . GLU   B 1 242 ? 44.572 8.595   5.672   1.00 23.01  ?  398 GLU   B N   1 
ATOM   4221 C  CA  . GLU   B 1 242 ? 44.126 7.381   5.001   1.00 20.22  ?  398 GLU   B CA  1 
ATOM   4222 C  C   . GLU   B 1 242 ? 45.274 6.441   4.660   1.00 21.75  ?  398 GLU   B C   1 
ATOM   4223 O  O   . GLU   B 1 242 ? 45.035 5.378   4.078   1.00 28.00  ?  398 GLU   B O   1 
ATOM   4224 C  CB  . GLU   B 1 242 ? 43.342 7.721   3.727   1.00 20.51  ?  398 GLU   B CB  1 
ATOM   4225 C  CG  . GLU   B 1 242 ? 42.019 8.430   3.980   1.00 23.87  ?  398 GLU   B CG  1 
ATOM   4226 C  CD  . GLU   B 1 242 ? 41.120 8.439   2.758   1.00 29.51  ?  398 GLU   B CD  1 
ATOM   4227 O  OE1 . GLU   B 1 242 ? 41.587 8.026   1.676   1.00 37.40  ?  398 GLU   B OE1 1 
ATOM   4228 O  OE2 . GLU   B 1 242 ? 39.948 8.851   2.881   1.00 35.79  -1 398 GLU   B OE2 1 
ATOM   4229 N  N   . ASN   B 1 243 ? 46.506 6.802   5.005   1.00 26.05  ?  399 ASN   B N   1 
ATOM   4230 C  CA  . ASN   B 1 243 ? 47.654 5.928   4.807   1.00 30.74  ?  399 ASN   B CA  1 
ATOM   4231 C  C   . ASN   B 1 243 ? 48.719 6.298   5.829   1.00 23.96  ?  399 ASN   B C   1 
ATOM   4232 O  O   . ASN   B 1 243 ? 48.616 7.313   6.523   1.00 29.89  ?  399 ASN   B O   1 
ATOM   4233 C  CB  . ASN   B 1 243 ? 48.183 6.014   3.369   1.00 18.85  ?  399 ASN   B CB  1 
ATOM   4234 C  CG  . ASN   B 1 243 ? 48.677 7.402   3.003   1.00 26.35  ?  399 ASN   B CG  1 
ATOM   4235 O  OD1 . ASN   B 1 243 ? 49.620 7.920   3.601   1.00 30.71  ?  399 ASN   B OD1 1 
ATOM   4236 N  ND2 . ASN   B 1 243 ? 48.037 8.013   2.012   1.00 21.23  ?  399 ASN   B ND2 1 
ATOM   4237 N  N   . LYS   B 1 244 ? 49.752 5.455   5.912   1.00 26.08  ?  400 LYS   B N   1 
ATOM   4238 C  CA  . LYS   B 1 244 ? 50.782 5.640   6.928   1.00 24.15  ?  400 LYS   B CA  1 
ATOM   4239 C  C   . LYS   B 1 244 ? 51.611 6.895   6.685   1.00 31.34  ?  400 LYS   B C   1 
ATOM   4240 O  O   . LYS   B 1 244 ? 52.034 7.549   7.644   1.00 36.54  ?  400 LYS   B O   1 
ATOM   4241 C  CB  . LYS   B 1 244 ? 51.699 4.421   6.982   1.00 30.78  ?  400 LYS   B CB  1 
ATOM   4242 C  CG  . LYS   B 1 244 ? 51.110 3.220   7.695   1.00 32.87  ?  400 LYS   B CG  1 
ATOM   4243 C  CD  . LYS   B 1 244 ? 52.117 2.082   7.720   1.00 48.92  ?  400 LYS   B CD  1 
ATOM   4244 C  CE  . LYS   B 1 244 ? 51.617 0.897   8.524   1.00 34.55  ?  400 LYS   B CE  1 
ATOM   4245 N  NZ  . LYS   B 1 244 ? 52.506 -0.283  8.329   1.00 46.66  ?  400 LYS   B NZ  1 
ATOM   4246 N  N   . GLU   B 1 245 ? 51.864 7.238   5.422   1.00 23.61  ?  401 GLU   B N   1 
ATOM   4247 C  CA  . GLU   B 1 245 ? 52.678 8.411   5.127   1.00 25.08  ?  401 GLU   B CA  1 
ATOM   4248 C  C   . GLU   B 1 245 ? 51.982 9.712   5.507   1.00 27.23  ?  401 GLU   B C   1 
ATOM   4249 O  O   . GLU   B 1 245 ? 52.655 10.738  5.654   1.00 31.67  ?  401 GLU   B O   1 
ATOM   4250 C  CB  . GLU   B 1 245 ? 53.047 8.432   3.642   1.00 20.67  ?  401 GLU   B CB  1 
ATOM   4251 C  CG  . GLU   B 1 245 ? 54.235 9.322   3.298   1.00 45.07  ?  401 GLU   B CG  1 
ATOM   4252 C  CD  . GLU   B 1 245 ? 55.572 8.683   3.634   1.00 54.54  ?  401 GLU   B CD  1 
ATOM   4253 O  OE1 . GLU   B 1 245 ? 55.715 7.455   3.446   1.00 48.42  ?  401 GLU   B OE1 1 
ATOM   4254 O  OE2 . GLU   B 1 245 ? 56.480 9.411   4.087   1.00 53.85  -1 401 GLU   B OE2 1 
ATOM   4255 N  N   . GLU   B 1 246 ? 50.661 9.697   5.683   1.00 26.91  ?  402 GLU   B N   1 
ATOM   4256 C  CA  . GLU   B 1 246 ? 49.891 10.922  5.869   1.00 30.93  ?  402 GLU   B CA  1 
ATOM   4257 C  C   . GLU   B 1 246 ? 49.067 10.905  7.154   1.00 27.32  ?  402 GLU   B C   1 
ATOM   4258 O  O   . GLU   B 1 246 ? 47.962 11.448  7.188   1.00 32.50  ?  402 GLU   B O   1 
ATOM   4259 C  CB  . GLU   B 1 246 ? 48.980 11.169  4.668   1.00 27.19  ?  402 GLU   B CB  1 
ATOM   4260 C  CG  . GLU   B 1 246 ? 49.709 11.363  3.353   1.00 34.70  ?  402 GLU   B CG  1 
ATOM   4261 C  CD  . GLU   B 1 246 ? 48.755 11.581  2.197   1.00 35.22  ?  402 GLU   B CD  1 
ATOM   4262 O  OE1 . GLU   B 1 246 ? 48.350 12.740  1.972   1.00 23.96  ?  402 GLU   B OE1 1 
ATOM   4263 O  OE2 . GLU   B 1 246 ? 48.404 10.595  1.516   1.00 31.94  -1 402 GLU   B OE2 1 
ATOM   4264 N  N   . LYS   B 1 247 ? 49.582 10.299  8.218   1.00 26.49  ?  403 LYS   B N   1 
ATOM   4265 C  CA  . LYS   B 1 247 ? 48.892 10.340  9.501   1.00 30.59  ?  403 LYS   B CA  1 
ATOM   4266 C  C   . LYS   B 1 247 ? 49.255 11.627  10.235  1.00 28.37  ?  403 LYS   B C   1 
ATOM   4267 O  O   . LYS   B 1 247 ? 50.436 11.910  10.462  1.00 23.66  ?  403 LYS   B O   1 
ATOM   4268 C  CB  . LYS   B 1 247 ? 49.232 9.115   10.349  1.00 20.90  ?  403 LYS   B CB  1 
ATOM   4269 C  CG  . LYS   B 1 247 ? 48.677 7.806   9.805   1.00 37.93  ?  403 LYS   B CG  1 
ATOM   4270 C  CD  . LYS   B 1 247 ? 47.254 7.553   10.297  1.00 43.31  ?  403 LYS   B CD  1 
ATOM   4271 C  CE  . LYS   B 1 247 ? 46.558 6.477   9.471   1.00 32.61  ?  403 LYS   B CE  1 
ATOM   4272 N  NZ  . LYS   B 1 247 ? 46.429 5.183   10.203  1.00 52.08  ?  403 LYS   B NZ  1 
ATOM   4273 N  N   . CYS   B 1 248 ? 48.240 12.407  10.589  1.00 25.05  ?  404 CYS   B N   1 
ATOM   4274 C  CA  . CYS   B 1 248 ? 48.405 13.636  11.351  1.00 22.59  ?  404 CYS   B CA  1 
ATOM   4275 C  C   . CYS   B 1 248 ? 47.764 13.479  12.720  1.00 22.56  ?  404 CYS   B C   1 
ATOM   4276 O  O   . CYS   B 1 248 ? 47.050 12.513  12.992  1.00 23.08  ?  404 CYS   B O   1 
ATOM   4277 C  CB  . CYS   B 1 248 ? 47.793 14.832  10.611  1.00 18.12  ?  404 CYS   B CB  1 
ATOM   4278 S  SG  . CYS   B 1 248 ? 46.020 15.110  10.932  1.00 20.29  ?  404 CYS   B SG  1 
ATOM   4279 N  N   . CYS   B 1 249 ? 48.017 14.454  13.589  1.00 21.73  ?  405 CYS   B N   1 
ATOM   4280 C  CA  . CYS   B 1 249 ? 47.587 14.365  14.977  1.00 26.40  ?  405 CYS   B CA  1 
ATOM   4281 C  C   . CYS   B 1 249 ? 46.570 15.441  15.344  1.00 26.02  ?  405 CYS   B C   1 
ATOM   4282 O  O   . CYS   B 1 249 ? 46.485 15.846  16.504  1.00 30.85  ?  405 CYS   B O   1 
ATOM   4283 C  CB  . CYS   B 1 249 ? 48.794 14.437  15.912  1.00 20.97  ?  405 CYS   B CB  1 
ATOM   4284 S  SG  . CYS   B 1 249 ? 49.635 16.036  15.925  1.00 26.27  ?  405 CYS   B SG  1 
ATOM   4285 N  N   . ARG   B 1 250 ? 45.785 15.907  14.370  1.00 24.53  ?  406 ARG   B N   1 
ATOM   4286 C  CA  . ARG   B 1 250 ? 44.816 16.967  14.636  1.00 23.92  ?  406 ARG   B CA  1 
ATOM   4287 C  C   . ARG   B 1 250 ? 43.743 16.503  15.620  1.00 19.62  ?  406 ARG   B C   1 
ATOM   4288 O  O   . ARG   B 1 250 ? 43.521 17.127  16.673  1.00 30.66  ?  406 ARG   B O   1 
ATOM   4289 C  CB  . ARG   B 1 250 ? 44.181 17.429  13.319  1.00 22.01  ?  406 ARG   B CB  1 
ATOM   4290 C  CG  . ARG   B 1 250 ? 45.053 18.342  12.458  1.00 17.41  ?  406 ARG   B CG  1 
ATOM   4291 C  CD  . ARG   B 1 250 ? 44.318 18.731  11.178  1.00 24.58  ?  406 ARG   B CD  1 
ATOM   4292 N  NE  . ARG   B 1 250 ? 45.085 19.642  10.333  1.00 15.59  ?  406 ARG   B NE  1 
ATOM   4293 C  CZ  . ARG   B 1 250 ? 45.821 19.266  9.295   1.00 15.02  ?  406 ARG   B CZ  1 
ATOM   4294 N  NH1 . ARG   B 1 250 ? 45.955 17.991  8.967   1.00 17.36  ?  406 ARG   B NH1 1 
ATOM   4295 N  NH2 . ARG   B 1 250 ? 46.441 20.192  8.569   1.00 17.06  ?  406 ARG   B NH2 1 
ATOM   4296 N  N   . LYS   B 1 251 ? 43.066 15.397  15.288  1.00 21.94  ?  407 LYS   B N   1 
ATOM   4297 C  CA  . LYS   B 1 251 ? 41.970 14.906  16.118  1.00 22.97  ?  407 LYS   B CA  1 
ATOM   4298 C  C   . LYS   B 1 251 ? 42.443 14.539  17.517  1.00 27.44  ?  407 LYS   B C   1 
ATOM   4299 O  O   . LYS   B 1 251 ? 41.715 14.753  18.493  1.00 28.04  ?  407 LYS   B O   1 
ATOM   4300 C  CB  . LYS   B 1 251 ? 41.302 13.701  15.448  1.00 21.67  ?  407 LYS   B CB  1 
ATOM   4301 C  CG  . LYS   B 1 251 ? 40.638 14.009  14.115  1.00 28.16  ?  407 LYS   B CG  1 
ATOM   4302 C  CD  . LYS   B 1 251 ? 39.961 12.780  13.524  1.00 28.93  ?  407 LYS   B CD  1 
ATOM   4303 C  CE  . LYS   B 1 251 ? 38.601 12.529  14.158  1.00 64.51  ?  407 LYS   B CE  1 
ATOM   4304 N  NZ  . LYS   B 1 251 ? 37.832 11.485  13.424  1.00 50.31  ?  407 LYS   B NZ  1 
ATOM   4305 N  N   . ASP   B 1 252 ? 43.660 14.000  17.636  1.00 25.37  ?  408 ASP   B N   1 
ATOM   4306 C  CA  . ASP   B 1 252 ? 44.193 13.654  18.947  1.00 21.07  ?  408 ASP   B CA  1 
ATOM   4307 C  C   . ASP   B 1 252 ? 44.461 14.898  19.784  1.00 21.20  ?  408 ASP   B C   1 
ATOM   4308 O  O   . ASP   B 1 252 ? 44.199 14.903  20.992  1.00 27.89  ?  408 ASP   B O   1 
ATOM   4309 C  CB  . ASP   B 1 252 ? 45.464 12.825  18.802  1.00 28.32  ?  408 ASP   B CB  1 
ATOM   4310 C  CG  . ASP   B 1 252 ? 45.178 11.392  18.437  1.00 37.86  ?  408 ASP   B CG  1 
ATOM   4311 O  OD1 . ASP   B 1 252 ? 43.978 11.033  18.395  1.00 37.18  ?  408 ASP   B OD1 1 
ATOM   4312 O  OD2 . ASP   B 1 252 ? 46.136 10.637  18.202  1.00 57.12  -1 408 ASP   B OD2 1 
ATOM   4313 N  N   . CYS   B 1 253 ? 44.972 15.966  19.163  1.00 20.35  ?  409 CYS   B N   1 
ATOM   4314 C  CA  . CYS   B 1 253 ? 45.173 17.212  19.897  1.00 25.53  ?  409 CYS   B CA  1 
ATOM   4315 C  C   . CYS   B 1 253 ? 43.849 17.768  20.395  1.00 26.08  ?  409 CYS   B C   1 
ATOM   4316 O  O   . CYS   B 1 253 ? 43.754 18.242  21.535  1.00 24.50  ?  409 CYS   B O   1 
ATOM   4317 C  CB  . CYS   B 1 253 ? 45.892 18.237  19.022  1.00 25.50  ?  409 CYS   B CB  1 
ATOM   4318 S  SG  . CYS   B 1 253 ? 47.670 17.966  18.852  1.00 29.34  ?  409 CYS   B SG  1 
ATOM   4319 N  N   . LEU   B 1 254 ? 42.811 17.712  19.556  1.00 23.13  ?  410 LEU   B N   1 
ATOM   4320 C  CA  . LEU   B 1 254 ? 41.499 18.179  19.997  1.00 22.46  ?  410 LEU   B CA  1 
ATOM   4321 C  C   . LEU   B 1 254 ? 40.974 17.341  21.159  1.00 19.83  ?  410 LEU   B C   1 
ATOM   4322 O  O   . LEU   B 1 254 ? 40.451 17.881  22.144  1.00 28.79  ?  410 LEU   B O   1 
ATOM   4323 C  CB  . LEU   B 1 254 ? 40.507 18.152  18.837  1.00 21.83  ?  410 LEU   B CB  1 
ATOM   4324 C  CG  . LEU   B 1 254 ? 39.103 18.544  19.300  1.00 31.52  ?  410 LEU   B CG  1 
ATOM   4325 C  CD1 . LEU   B 1 254 ? 39.082 19.976  19.814  1.00 25.66  ?  410 LEU   B CD1 1 
ATOM   4326 C  CD2 . LEU   B 1 254 ? 38.082 18.349  18.211  1.00 31.06  ?  410 LEU   B CD2 1 
ATOM   4327 N  N   . LYS   B 1 255 ? 41.088 16.013  21.047  1.00 20.83  ?  411 LYS   B N   1 
ATOM   4328 C  CA  . LYS   B 1 255 ? 40.648 15.136  22.129  1.00 18.95  ?  411 LYS   B CA  1 
ATOM   4329 C  C   . LYS   B 1 255 ? 41.380 15.445  23.426  1.00 21.03  ?  411 LYS   B C   1 
ATOM   4330 O  O   . LYS   B 1 255 ? 40.772 15.458  24.502  1.00 26.49  ?  411 LYS   B O   1 
ATOM   4331 C  CB  . LYS   B 1 255 ? 40.864 13.671  21.753  1.00 24.83  ?  411 LYS   B CB  1 
ATOM   4332 C  CG  . LYS   B 1 255 ? 39.750 13.062  20.931  1.00 37.71  ?  411 LYS   B CG  1 
ATOM   4333 C  CD  . LYS   B 1 255 ? 39.841 11.546  20.936  1.00 49.19  ?  411 LYS   B CD  1 
ATOM   4334 C  CE  . LYS   B 1 255 ? 40.549 11.027  19.698  1.00 50.75  ?  411 LYS   B CE  1 
ATOM   4335 N  NZ  . LYS   B 1 255 ? 39.597 10.677  18.606  1.00 64.47  ?  411 LYS   B NZ  1 
ATOM   4336 N  N   . LEU   B 1 256 ? 42.690 15.690  23.345  1.00 19.09  ?  412 LEU   B N   1 
ATOM   4337 C  CA  . LEU   B 1 256 ? 43.461 15.957  24.553  1.00 20.32  ?  412 LEU   B CA  1 
ATOM   4338 C  C   . LEU   B 1 256 ? 43.060 17.284  25.182  1.00 23.76  ?  412 LEU   B C   1 
ATOM   4339 O  O   . LEU   B 1 256 ? 42.950 17.386  26.409  1.00 20.36  ?  412 LEU   B O   1 
ATOM   4340 C  CB  . LEU   B 1 256 ? 44.954 15.937  24.238  1.00 21.22  ?  412 LEU   B CB  1 
ATOM   4341 C  CG  . LEU   B 1 256 ? 45.529 14.577  23.850  1.00 24.93  ?  412 LEU   B CG  1 
ATOM   4342 C  CD1 . LEU   B 1 256 ? 46.900 14.737  23.207  1.00 19.24  ?  412 LEU   B CD1 1 
ATOM   4343 C  CD2 . LEU   B 1 256 ? 45.597 13.680  25.069  1.00 23.85  ?  412 LEU   B CD2 1 
ATOM   4344 N  N   . MET   B 1 257 ? 42.835 18.312  24.359  1.00 20.23  ?  413 MET   B N   1 
ATOM   4345 C  CA  . MET   B 1 257 ? 42.366 19.589  24.891  1.00 22.26  ?  413 MET   B CA  1 
ATOM   4346 C  C   . MET   B 1 257 ? 41.014 19.440  25.587  1.00 26.37  ?  413 MET   B C   1 
ATOM   4347 O  O   . MET   B 1 257 ? 40.806 19.963  26.696  1.00 27.40  ?  413 MET   B O   1 
ATOM   4348 C  CB  . MET   B 1 257 ? 42.284 20.613  23.760  1.00 18.43  ?  413 MET   B CB  1 
ATOM   4349 C  CG  . MET   B 1 257 ? 43.625 21.147  23.287  1.00 24.84  ?  413 MET   B CG  1 
ATOM   4350 S  SD  . MET   B 1 257 ? 44.538 21.921  24.629  1.00 46.35  ?  413 MET   B SD  1 
ATOM   4351 C  CE  . MET   B 1 257 ? 43.827 23.560  24.611  1.00 35.40  ?  413 MET   B CE  1 
ATOM   4352 N  N   . LYS   B 1 258 ? 40.084 18.718  24.954  1.00 22.72  ?  414 LYS   B N   1 
ATOM   4353 C  CA  . LYS   B 1 258 ? 38.762 18.536  25.551  1.00 21.24  ?  414 LYS   B CA  1 
ATOM   4354 C  C   . LYS   B 1 258 ? 38.841 17.727  26.841  1.00 24.72  ?  414 LYS   B C   1 
ATOM   4355 O  O   . LYS   B 1 258 ? 38.140 18.037  27.812  1.00 26.48  ?  414 LYS   B O   1 
ATOM   4356 C  CB  . LYS   B 1 258 ? 37.817 17.878  24.547  1.00 22.59  ?  414 LYS   B CB  1 
ATOM   4357 C  CG  . LYS   B 1 258 ? 37.368 18.823  23.439  1.00 33.73  ?  414 LYS   B CG  1 
ATOM   4358 C  CD  . LYS   B 1 258 ? 36.489 18.134  22.403  1.00 32.66  ?  414 LYS   B CD  1 
ATOM   4359 C  CE  . LYS   B 1 258 ? 35.347 17.368  23.048  1.00 40.33  ?  414 LYS   B CE  1 
ATOM   4360 N  NZ  . LYS   B 1 258 ? 34.023 17.873  22.589  1.00 65.52  ?  414 LYS   B NZ  1 
ATOM   4361 N  N   . TYR   B 1 259 ? 39.692 16.696  26.876  1.00 28.70  ?  415 TYR   B N   1 
ATOM   4362 C  CA  . TYR   B 1 259 ? 39.864 15.919  28.101  1.00 27.66  ?  415 TYR   B CA  1 
ATOM   4363 C  C   . TYR   B 1 259 ? 40.472 16.766  29.209  1.00 26.04  ?  415 TYR   B C   1 
ATOM   4364 O  O   . TYR   B 1 259 ? 40.082 16.645  30.377  1.00 25.05  ?  415 TYR   B O   1 
ATOM   4365 C  CB  . TYR   B 1 259 ? 40.742 14.698  27.836  1.00 24.86  ?  415 TYR   B CB  1 
ATOM   4366 C  CG  . TYR   B 1 259 ? 40.836 13.712  28.993  1.00 31.12  ?  415 TYR   B CG  1 
ATOM   4367 C  CD1 . TYR   B 1 259 ? 39.717 13.357  29.739  1.00 31.59  ?  415 TYR   B CD1 1 
ATOM   4368 C  CD2 . TYR   B 1 259 ? 42.047 13.134  29.334  1.00 29.36  ?  415 TYR   B CD2 1 
ATOM   4369 C  CE1 . TYR   B 1 259 ? 39.802 12.454  30.777  1.00 54.65  ?  415 TYR   B CE1 1 
ATOM   4370 C  CE2 . TYR   B 1 259 ? 42.146 12.237  30.376  1.00 28.81  ?  415 TYR   B CE2 1 
ATOM   4371 C  CZ  . TYR   B 1 259 ? 41.021 11.904  31.093  1.00 35.89  ?  415 TYR   B CZ  1 
ATOM   4372 O  OH  . TYR   B 1 259 ? 41.109 11.006  32.133  1.00 43.60  ?  415 TYR   B OH  1 
ATOM   4373 N  N   . LEU   B 1 260 ? 41.434 17.623  28.863  1.00 22.09  ?  416 LEU   B N   1 
ATOM   4374 C  CA  . LEU   B 1 260 ? 42.025 18.527  29.844  1.00 24.34  ?  416 LEU   B CA  1 
ATOM   4375 C  C   . LEU   B 1 260 ? 40.953 19.401  30.476  1.00 31.05  ?  416 LEU   B C   1 
ATOM   4376 O  O   . LEU   B 1 260 ? 40.863 19.511  31.707  1.00 23.63  ?  416 LEU   B O   1 
ATOM   4377 C  CB  . LEU   B 1 260 ? 43.105 19.382  29.175  1.00 22.44  ?  416 LEU   B CB  1 
ATOM   4378 C  CG  . LEU   B 1 260 ? 43.822 20.442  30.012  1.00 25.64  ?  416 LEU   B CG  1 
ATOM   4379 C  CD1 . LEU   B 1 260 ? 44.530 19.807  31.198  1.00 26.39  ?  416 LEU   B CD1 1 
ATOM   4380 C  CD2 . LEU   B 1 260 ? 44.802 21.214  29.145  1.00 21.15  ?  416 LEU   B CD2 1 
ATOM   4381 N  N   . LEU   B 1 261 ? 40.107 20.012  29.641  1.00 25.38  ?  417 LEU   B N   1 
ATOM   4382 C  CA  . LEU   B 1 261 ? 39.059 20.875  30.176  1.00 26.76  ?  417 LEU   B CA  1 
ATOM   4383 C  C   . LEU   B 1 261 ? 38.056 20.086  31.013  1.00 31.33  ?  417 LEU   B C   1 
ATOM   4384 O  O   . LEU   B 1 261 ? 37.641 20.536  32.086  1.00 29.95  ?  417 LEU   B O   1 
ATOM   4385 C  CB  . LEU   B 1 261 ? 38.342 21.617  29.051  1.00 23.01  ?  417 LEU   B CB  1 
ATOM   4386 C  CG  . LEU   B 1 261 ? 37.334 22.620  29.622  1.00 24.96  ?  417 LEU   B CG  1 
ATOM   4387 C  CD1 . LEU   B 1 261 ? 38.011 23.616  30.565  1.00 24.22  ?  417 LEU   B CD1 1 
ATOM   4388 C  CD2 . LEU   B 1 261 ? 36.575 23.340  28.523  1.00 21.94  ?  417 LEU   B CD2 1 
ATOM   4389 N  N   . GLU   B 1 262 ? 37.640 18.910  30.530  1.00 29.33  ?  418 GLU   B N   1 
ATOM   4390 C  CA  . GLU   B 1 262 ? 36.665 18.114  31.272  1.00 31.37  ?  418 GLU   B CA  1 
ATOM   4391 C  C   . GLU   B 1 262 ? 37.202 17.724  32.643  1.00 30.00  ?  418 GLU   B C   1 
ATOM   4392 O  O   . GLU   B 1 262 ? 36.491 17.833  33.652  1.00 26.77  ?  418 GLU   B O   1 
ATOM   4393 C  CB  . GLU   B 1 262 ? 36.282 16.869  30.468  1.00 29.59  ?  418 GLU   B CB  1 
ATOM   4394 C  CG  . GLU   B 1 262 ? 35.478 17.161  29.210  1.00 32.28  ?  418 GLU   B CG  1 
ATOM   4395 C  CD  . GLU   B 1 262 ? 35.289 15.935  28.338  1.00 43.04  ?  418 GLU   B CD  1 
ATOM   4396 O  OE1 . GLU   B 1 262 ? 35.265 14.811  28.883  1.00 45.69  ?  418 GLU   B OE1 1 
ATOM   4397 O  OE2 . GLU   B 1 262 ? 35.175 16.096  27.104  1.00 37.41  -1 418 GLU   B OE2 1 
ATOM   4398 N  N   . GLN   B 1 263 ? 38.464 17.292  32.705  1.00 26.49  ?  419 GLN   B N   1 
ATOM   4399 C  CA  . GLN   B 1 263 ? 39.052 16.885  33.977  1.00 29.81  ?  419 GLN   B CA  1 
ATOM   4400 C  C   . GLN   B 1 263 ? 39.213 18.067  34.922  1.00 30.80  ?  419 GLN   B C   1 
ATOM   4401 O  O   . GLN   B 1 263 ? 38.977 17.937  36.129  1.00 33.74  ?  419 GLN   B O   1 
ATOM   4402 C  CB  . GLN   B 1 263 ? 40.402 16.210  33.742  1.00 29.24  ?  419 GLN   B CB  1 
ATOM   4403 C  CG  . GLN   B 1 263 ? 40.294 14.878  33.046  1.00 40.34  ?  419 GLN   B CG  1 
ATOM   4404 C  CD  . GLN   B 1 263 ? 39.479 13.877  33.838  1.00 40.05  ?  419 GLN   B CD  1 
ATOM   4405 O  OE1 . GLN   B 1 263 ? 39.928 13.375  34.867  1.00 44.47  ?  419 GLN   B OE1 1 
ATOM   4406 N  NE2 . GLN   B 1 263 ? 38.266 13.598  33.373  1.00 46.88  ?  419 GLN   B NE2 1 
ATOM   4407 N  N   . LEU   B 1 264 ? 39.622 19.227  34.399  1.00 29.96  ?  420 LEU   B N   1 
ATOM   4408 C  CA  . LEU   B 1 264 ? 39.763 20.393  35.266  1.00 29.78  ?  420 LEU   B CA  1 
ATOM   4409 C  C   . LEU   B 1 264 ? 38.410 20.856  35.796  1.00 33.83  ?  420 LEU   B C   1 
ATOM   4410 O  O   . LEU   B 1 264 ? 38.294 21.231  36.968  1.00 28.94  ?  420 LEU   B O   1 
ATOM   4411 C  CB  . LEU   B 1 264 ? 40.470 21.527  34.528  1.00 35.88  ?  420 LEU   B CB  1 
ATOM   4412 C  CG  . LEU   B 1 264 ? 41.965 21.307  34.286  1.00 30.74  ?  420 LEU   B CG  1 
ATOM   4413 C  CD1 . LEU   B 1 264 ? 42.531 22.412  33.409  1.00 30.75  ?  420 LEU   B CD1 1 
ATOM   4414 C  CD2 . LEU   B 1 264 ? 42.721 21.210  35.609  1.00 26.05  ?  420 LEU   B CD2 1 
ATOM   4415 N  N   . LYS   B 1 265 ? 37.372 20.829  34.954  1.00 27.63  ?  421 LYS   B N   1 
ATOM   4416 C  CA  . LYS   B 1 265 ? 36.044 21.206  35.424  1.00 39.18  ?  421 LYS   B CA  1 
ATOM   4417 C  C   . LYS   B 1 265 ? 35.524 20.213  36.455  1.00 41.71  ?  421 LYS   B C   1 
ATOM   4418 O  O   . LYS   B 1 265 ? 34.815 20.596  37.392  1.00 39.07  ?  421 LYS   B O   1 
ATOM   4419 C  CB  . LYS   B 1 265 ? 35.074 21.313  34.247  1.00 29.97  ?  421 LYS   B CB  1 
ATOM   4420 C  CG  . LYS   B 1 265 ? 35.320 22.506  33.341  1.00 29.49  ?  421 LYS   B CG  1 
ATOM   4421 C  CD  . LYS   B 1 265 ? 34.307 22.545  32.211  1.00 29.34  ?  421 LYS   B CD  1 
ATOM   4422 C  CE  . LYS   B 1 265 ? 32.926 22.919  32.724  1.00 32.16  ?  421 LYS   B CE  1 
ATOM   4423 N  NZ  . LYS   B 1 265 ? 31.940 23.066  31.620  1.00 43.06  ?  421 LYS   B NZ  1 
ATOM   4424 N  N   . GLU   B 1 266 ? 35.870 18.932  36.300  1.00 36.66  ?  422 GLU   B N   1 
ATOM   4425 C  CA  . GLU   B 1 266 ? 35.462 17.935  37.285  1.00 38.61  ?  422 GLU   B CA  1 
ATOM   4426 C  C   . GLU   B 1 266 ? 36.173 18.145  38.618  1.00 42.60  ?  422 GLU   B C   1 
ATOM   4427 O  O   . GLU   B 1 266 ? 35.541 18.114  39.680  1.00 39.42  ?  422 GLU   B O   1 
ATOM   4428 C  CB  . GLU   B 1 266 ? 35.731 16.529  36.749  1.00 42.83  ?  422 GLU   B CB  1 
ATOM   4429 C  CG  . GLU   B 1 266 ? 34.679 15.504  37.137  1.00 60.21  ?  422 GLU   B CG  1 
ATOM   4430 C  CD  . GLU   B 1 266 ? 33.435 15.585  36.274  1.00 77.75  ?  422 GLU   B CD  1 
ATOM   4431 O  OE1 . GLU   B 1 266 ? 32.514 16.348  36.633  1.00 65.71  ?  422 GLU   B OE1 1 
ATOM   4432 O  OE2 . GLU   B 1 266 ? 33.374 14.879  35.244  1.00 85.48  -1 422 GLU   B OE2 1 
ATOM   4433 N  N   . ARG   B 1 267 ? 37.492 18.365  38.584  1.00 42.41  ?  423 ARG   B N   1 
ATOM   4434 C  CA  . ARG   B 1 267 ? 38.249 18.489  39.829  1.00 38.56  ?  423 ARG   B CA  1 
ATOM   4435 C  C   . ARG   B 1 267 ? 37.787 19.688  40.654  1.00 42.59  ?  423 ARG   B C   1 
ATOM   4436 O  O   . ARG   B 1 267 ? 37.803 19.635  41.889  1.00 53.08  ?  423 ARG   B O   1 
ATOM   4437 C  CB  . ARG   B 1 267 ? 39.750 18.588  39.533  1.00 44.03  ?  423 ARG   B CB  1 
ATOM   4438 C  CG  . ARG   B 1 267 ? 40.578 19.082  40.719  1.00 57.09  ?  423 ARG   B CG  1 
ATOM   4439 C  CD  . ARG   B 1 267 ? 42.043 19.315  40.380  1.00 44.96  ?  423 ARG   B CD  1 
ATOM   4440 N  NE  . ARG   B 1 267 ? 42.686 18.155  39.774  1.00 56.87  ?  423 ARG   B NE  1 
ATOM   4441 C  CZ  . ARG   B 1 267 ? 43.484 17.322  40.428  1.00 59.14  ?  423 ARG   B CZ  1 
ATOM   4442 N  NH1 . ARG   B 1 267 ? 43.720 17.465  41.722  1.00 54.96  ?  423 ARG   B NH1 1 
ATOM   4443 N  NH2 . ARG   B 1 267 ? 44.059 16.319  39.767  1.00 57.67  ?  423 ARG   B NH2 1 
ATOM   4444 N  N   . PHE   B 1 268 ? 37.345 20.763  39.997  1.00 48.29  ?  424 PHE   B N   1 
ATOM   4445 C  CA  . PHE   B 1 268 ? 36.940 21.991  40.674  1.00 41.03  ?  424 PHE   B CA  1 
ATOM   4446 C  C   . PHE   B 1 268 ? 35.440 22.252  40.560  1.00 38.90  ?  424 PHE   B C   1 
ATOM   4447 O  O   . PHE   B 1 268 ? 35.003 23.406  40.594  1.00 42.04  ?  424 PHE   B O   1 
ATOM   4448 C  CB  . PHE   B 1 268 ? 37.717 23.182  40.119  1.00 37.21  ?  424 PHE   B CB  1 
ATOM   4449 C  CG  . PHE   B 1 268 ? 39.197 23.089  40.332  1.00 46.77  ?  424 PHE   B CG  1 
ATOM   4450 C  CD1 . PHE   B 1 268 ? 39.746 23.324  41.581  1.00 38.62  ?  424 PHE   B CD1 1 
ATOM   4451 C  CD2 . PHE   B 1 268 ? 40.040 22.762  39.284  1.00 39.00  ?  424 PHE   B CD2 1 
ATOM   4452 C  CE1 . PHE   B 1 268 ? 41.110 23.235  41.781  1.00 43.10  ?  424 PHE   B CE1 1 
ATOM   4453 C  CE2 . PHE   B 1 268 ? 41.404 22.672  39.477  1.00 44.03  ?  424 PHE   B CE2 1 
ATOM   4454 C  CZ  . PHE   B 1 268 ? 41.939 22.908  40.729  1.00 40.62  ?  424 PHE   B CZ  1 
ATOM   4455 N  N   . LYS   B 1 269 ? 34.634 21.193  40.439  1.00 51.96  ?  425 LYS   B N   1 
ATOM   4456 C  CA  . LYS   B 1 269 ? 33.206 21.379  40.204  1.00 51.36  ?  425 LYS   B CA  1 
ATOM   4457 C  C   . LYS   B 1 269 ? 32.471 21.913  41.427  1.00 58.11  ?  425 LYS   B C   1 
ATOM   4458 O  O   . LYS   B 1 269 ? 31.363 22.440  41.284  1.00 52.70  ?  425 LYS   B O   1 
ATOM   4459 C  CB  . LYS   B 1 269 ? 32.567 20.067  39.741  1.00 48.97  ?  425 LYS   B CB  1 
ATOM   4460 C  CG  . LYS   B 1 269 ? 32.458 18.980  40.802  1.00 55.58  ?  425 LYS   B CG  1 
ATOM   4461 C  CD  . LYS   B 1 269 ? 31.938 17.688  40.181  1.00 66.26  ?  425 LYS   B CD  1 
ATOM   4462 C  CE  . LYS   B 1 269 ? 31.745 16.592  41.217  1.00 57.10  ?  425 LYS   B CE  1 
ATOM   4463 N  NZ  . LYS   B 1 269 ? 31.147 15.369  40.608  1.00 76.02  ?  425 LYS   B NZ  1 
ATOM   4464 N  N   . ASP   B 1 270 ? 33.053 21.798  42.621  1.00 58.53  ?  426 ASP   B N   1 
ATOM   4465 C  CA  . ASP   B 1 270 ? 32.421 22.334  43.820  1.00 61.41  ?  426 ASP   B CA  1 
ATOM   4466 C  C   . ASP   B 1 270 ? 32.681 23.823  44.003  1.00 53.99  ?  426 ASP   B C   1 
ATOM   4467 O  O   . ASP   B 1 270 ? 32.067 24.443  44.878  1.00 74.98  ?  426 ASP   B O   1 
ATOM   4468 C  CB  . ASP   B 1 270 ? 32.885 21.551  45.047  1.00 68.83  ?  426 ASP   B CB  1 
ATOM   4469 C  CG  . ASP   B 1 270 ? 32.838 20.052  44.825  1.00 84.00  ?  426 ASP   B CG  1 
ATOM   4470 O  OD1 . ASP   B 1 270 ? 31.774 19.548  44.404  1.00 75.65  ?  426 ASP   B OD1 1 
ATOM   4471 O  OD2 . ASP   B 1 270 ? 33.861 19.378  45.063  1.00 68.30  -1 426 ASP   B OD2 1 
ATOM   4472 N  N   . LYS   B 1 271 ? 33.576 24.400  43.213  1.00 65.18  ?  427 LYS   B N   1 
ATOM   4473 C  CA  . LYS   B 1 271 ? 33.669 25.838  43.033  1.00 50.78  ?  427 LYS   B CA  1 
ATOM   4474 C  C   . LYS   B 1 271 ? 32.991 26.203  41.716  1.00 54.60  ?  427 LYS   B C   1 
ATOM   4475 O  O   . LYS   B 1 271 ? 32.697 25.341  40.885  1.00 61.47  ?  427 LYS   B O   1 
ATOM   4476 C  CB  . LYS   B 1 271 ? 35.135 26.287  43.054  1.00 57.89  ?  427 LYS   B CB  1 
ATOM   4477 C  CG  . LYS   B 1 271 ? 35.905 25.756  44.261  1.00 68.53  ?  427 LYS   B CG  1 
ATOM   4478 C  CD  . LYS   B 1 271 ? 37.392 26.077  44.205  1.00 68.68  ?  427 LYS   B CD  1 
ATOM   4479 C  CE  . LYS   B 1 271 ? 38.097 25.582  45.464  1.00 70.60  ?  427 LYS   B CE  1 
ATOM   4480 N  NZ  . LYS   B 1 271 ? 39.536 25.967  45.519  1.00 81.45  ?  427 LYS   B NZ  1 
ATOM   4481 N  N   . LYS   B 1 272 ? 32.722 27.493  41.533  1.00 56.50  ?  428 LYS   B N   1 
ATOM   4482 C  CA  . LYS   B 1 272 ? 32.053 27.961  40.327  1.00 62.37  ?  428 LYS   B CA  1 
ATOM   4483 C  C   . LYS   B 1 272 ? 33.018 28.550  39.307  1.00 46.19  ?  428 LYS   B C   1 
ATOM   4484 O  O   . LYS   B 1 272 ? 32.573 29.086  38.287  1.00 40.75  ?  428 LYS   B O   1 
ATOM   4485 C  CB  . LYS   B 1 272 ? 30.981 28.997  40.676  1.00 52.77  ?  428 LYS   B CB  1 
ATOM   4486 C  CG  . LYS   B 1 272 ? 31.374 29.962  41.780  1.00 76.17  ?  428 LYS   B CG  1 
ATOM   4487 C  CD  . LYS   B 1 272 ? 30.177 30.329  42.644  1.00 71.60  ?  428 LYS   B CD  1 
ATOM   4488 C  CE  . LYS   B 1 272 ? 29.853 29.235  43.644  1.00 79.75  ?  428 LYS   B CE  1 
ATOM   4489 N  NZ  . LYS   B 1 272 ? 28.475 29.385  44.188  1.00 65.22  ?  428 LYS   B NZ  1 
ATOM   4490 N  N   . HIS   B 1 273 ? 34.326 28.448  39.551  1.00 39.21  ?  429 HIS   B N   1 
ATOM   4491 C  CA  . HIS   B 1 273 ? 35.298 29.161  38.728  1.00 34.90  ?  429 HIS   B CA  1 
ATOM   4492 C  C   . HIS   B 1 273 ? 35.298 28.681  37.282  1.00 41.77  ?  429 HIS   B C   1 
ATOM   4493 O  O   . HIS   B 1 273 ? 35.542 29.477  36.367  1.00 42.53  ?  429 HIS   B O   1 
ATOM   4494 C  CB  . HIS   B 1 273 ? 36.696 29.015  39.331  1.00 40.17  ?  429 HIS   B CB  1 
ATOM   4495 C  CG  . HIS   B 1 273 ? 36.818 29.569  40.717  1.00 52.12  ?  429 HIS   B CG  1 
ATOM   4496 N  ND1 . HIS   B 1 273 ? 36.553 30.888  41.017  1.00 55.56  ?  429 HIS   B ND1 1 
ATOM   4497 C  CD2 . HIS   B 1 273 ? 37.174 28.981  41.883  1.00 57.03  ?  429 HIS   B CD2 1 
ATOM   4498 C  CE1 . HIS   B 1 273 ? 36.743 31.089  42.309  1.00 64.23  ?  429 HIS   B CE1 1 
ATOM   4499 N  NE2 . HIS   B 1 273 ? 37.119 29.947  42.858  1.00 67.41  ?  429 HIS   B NE2 1 
ATOM   4500 N  N   . LEU   B 1 274 ? 35.027 27.398  37.048  1.00 32.54  ?  430 LEU   B N   1 
ATOM   4501 C  CA  . LEU   B 1 274 ? 35.158 26.808  35.721  1.00 39.01  ?  430 LEU   B CA  1 
ATOM   4502 C  C   . LEU   B 1 274 ? 33.817 26.453  35.089  1.00 41.16  ?  430 LEU   B C   1 
ATOM   4503 O  O   . LEU   B 1 274 ? 33.791 25.778  34.054  1.00 40.73  ?  430 LEU   B O   1 
ATOM   4504 C  CB  . LEU   B 1 274 ? 36.046 25.563  35.786  1.00 32.17  ?  430 LEU   B CB  1 
ATOM   4505 C  CG  . LEU   B 1 274 ? 37.488 25.795  36.240  1.00 36.54  ?  430 LEU   B CG  1 
ATOM   4506 C  CD1 . LEU   B 1 274 ? 38.306 24.514  36.131  1.00 29.41  ?  430 LEU   B CD1 1 
ATOM   4507 C  CD2 . LEU   B 1 274 ? 38.127 26.919  35.435  1.00 27.97  ?  430 LEU   B CD2 1 
ATOM   4508 N  N   . ASP   B 1 275 ? 32.705 26.900  35.674  1.00 47.87  ?  431 ASP   B N   1 
ATOM   4509 C  CA  . ASP   B 1 275 ? 31.391 26.492  35.191  1.00 34.38  ?  431 ASP   B CA  1 
ATOM   4510 C  C   . ASP   B 1 275 ? 31.067 27.034  33.803  1.00 40.68  ?  431 ASP   B C   1 
ATOM   4511 O  O   . ASP   B 1 275 ? 30.254 26.431  33.095  1.00 35.31  ?  431 ASP   B O   1 
ATOM   4512 C  CB  . ASP   B 1 275 ? 30.310 26.933  36.178  1.00 45.06  ?  431 ASP   B CB  1 
ATOM   4513 C  CG  . ASP   B 1 275 ? 30.238 26.041  37.400  1.00 59.18  ?  431 ASP   B CG  1 
ATOM   4514 O  OD1 . ASP   B 1 275 ? 30.922 24.996  37.416  1.00 61.43  ?  431 ASP   B OD1 1 
ATOM   4515 O  OD2 . ASP   B 1 275 ? 29.493 26.383  38.342  1.00 75.90  -1 431 ASP   B OD2 1 
ATOM   4516 N  N   . LYS   B 1 276 ? 31.679 28.145  33.394  1.00 34.05  ?  432 LYS   B N   1 
ATOM   4517 C  CA  . LYS   B 1 276 ? 31.312 28.796  32.142  1.00 28.19  ?  432 LYS   B CA  1 
ATOM   4518 C  C   . LYS   B 1 276 ? 32.155 28.352  30.953  1.00 31.34  ?  432 LYS   B C   1 
ATOM   4519 O  O   . LYS   B 1 276 ? 31.840 28.731  29.820  1.00 30.34  ?  432 LYS   B O   1 
ATOM   4520 C  CB  . LYS   B 1 276 ? 31.408 30.317  32.291  1.00 37.84  ?  432 LYS   B CB  1 
ATOM   4521 C  CG  . LYS   B 1 276 ? 30.238 30.931  33.040  1.00 34.96  ?  432 LYS   B CG  1 
ATOM   4522 C  CD  . LYS   B 1 276 ? 30.329 32.445  33.062  1.00 39.61  ?  432 LYS   B CD  1 
ATOM   4523 C  CE  . LYS   B 1 276 ? 29.028 33.063  33.546  1.00 62.31  ?  432 LYS   B CE  1 
ATOM   4524 N  NZ  . LYS   B 1 276 ? 29.100 34.548  33.598  1.00 58.74  ?  432 LYS   B NZ  1 
ATOM   4525 N  N   . PHE   B 1 277 ? 33.207 27.571  31.175  1.00 29.26  ?  433 PHE   B N   1 
ATOM   4526 C  CA  . PHE   B 1 277 ? 34.039 27.078  30.087  1.00 27.18  ?  433 PHE   B CA  1 
ATOM   4527 C  C   . PHE   B 1 277 ? 33.455 25.784  29.537  1.00 32.70  ?  433 PHE   B C   1 
ATOM   4528 O  O   . PHE   B 1 277 ? 32.941 24.951  30.289  1.00 27.24  ?  433 PHE   B O   1 
ATOM   4529 C  CB  . PHE   B 1 277 ? 35.473 26.859  30.567  1.00 29.22  ?  433 PHE   B CB  1 
ATOM   4530 C  CG  . PHE   B 1 277 ? 36.146 28.116  31.033  1.00 30.94  ?  433 PHE   B CG  1 
ATOM   4531 C  CD1 . PHE   B 1 277 ? 36.639 29.033  30.119  1.00 33.72  ?  433 PHE   B CD1 1 
ATOM   4532 C  CD2 . PHE   B 1 277 ? 36.272 28.389  32.385  1.00 28.55  ?  433 PHE   B CD2 1 
ATOM   4533 C  CE1 . PHE   B 1 277 ? 37.254 30.195  30.545  1.00 32.28  ?  433 PHE   B CE1 1 
ATOM   4534 C  CE2 . PHE   B 1 277 ? 36.885 29.550  32.817  1.00 30.01  ?  433 PHE   B CE2 1 
ATOM   4535 C  CZ  . PHE   B 1 277 ? 37.377 30.454  31.896  1.00 27.77  ?  433 PHE   B CZ  1 
ATOM   4536 N  N   . SER   B 1 278 ? 33.529 25.624  28.218  1.00 30.03  ?  434 SER   B N   1 
ATOM   4537 C  CA  . SER   B 1 278 ? 32.893 24.502  27.545  1.00 30.14  ?  434 SER   B CA  1 
ATOM   4538 C  C   . SER   B 1 278 ? 33.817 23.962  26.463  1.00 28.60  ?  434 SER   B C   1 
ATOM   4539 O  O   . SER   B 1 278 ? 34.801 24.598  26.074  1.00 22.92  ?  434 SER   B O   1 
ATOM   4540 C  CB  . SER   B 1 278 ? 31.542 24.905  26.940  1.00 30.09  ?  434 SER   B CB  1 
ATOM   4541 O  OG  . SER   B 1 278 ? 31.714 25.758  25.819  1.00 34.31  ?  434 SER   B OG  1 
ATOM   4542 N  N   . SER   B 1 279 ? 33.477 22.768  25.975  1.00 30.39  ?  435 SER   B N   1 
ATOM   4543 C  CA  . SER   B 1 279 ? 34.180 22.188  24.840  1.00 26.63  ?  435 SER   B CA  1 
ATOM   4544 C  C   . SER   B 1 279 ? 34.033 23.038  23.586  1.00 26.18  ?  435 SER   B C   1 
ATOM   4545 O  O   . SER   B 1 279 ? 34.814 22.871  22.646  1.00 31.34  ?  435 SER   B O   1 
ATOM   4546 C  CB  . SER   B 1 279 ? 33.673 20.770  24.574  1.00 28.11  ?  435 SER   B CB  1 
ATOM   4547 O  OG  . SER   B 1 279 ? 32.388 20.793  23.979  1.00 33.09  ?  435 SER   B OG  1 
ATOM   4548 N  N   . TYR   B 1 280 ? 33.049 23.943  23.551  1.00 26.03  ?  436 TYR   B N   1 
ATOM   4549 C  CA  . TYR   B 1 280 ? 32.946 24.869  22.428  1.00 24.16  ?  436 TYR   B CA  1 
ATOM   4550 C  C   . TYR   B 1 280 ? 34.134 25.819  22.389  1.00 23.08  ?  436 TYR   B C   1 
ATOM   4551 O  O   . TYR   B 1 280 ? 34.653 26.129  21.312  1.00 25.71  ?  436 TYR   B O   1 
ATOM   4552 C  CB  . TYR   B 1 280 ? 31.644 25.664  22.502  1.00 28.16  ?  436 TYR   B CB  1 
ATOM   4553 C  CG  . TYR   B 1 280 ? 31.321 26.368  21.206  1.00 29.38  ?  436 TYR   B CG  1 
ATOM   4554 C  CD1 . TYR   B 1 280 ? 30.882 25.653  20.099  1.00 29.66  ?  436 TYR   B CD1 1 
ATOM   4555 C  CD2 . TYR   B 1 280 ? 31.474 27.742  21.080  1.00 26.06  ?  436 TYR   B CD2 1 
ATOM   4556 C  CE1 . TYR   B 1 280 ? 30.594 26.287  18.906  1.00 24.75  ?  436 TYR   B CE1 1 
ATOM   4557 C  CE2 . TYR   B 1 280 ? 31.188 28.386  19.891  1.00 29.69  ?  436 TYR   B CE2 1 
ATOM   4558 C  CZ  . TYR   B 1 280 ? 30.748 27.653  18.808  1.00 30.25  ?  436 TYR   B CZ  1 
ATOM   4559 O  OH  . TYR   B 1 280 ? 30.463 28.289  17.622  1.00 33.12  ?  436 TYR   B OH  1 
ATOM   4560 N  N   . HIS   B 1 281 ? 34.573 26.299  23.553  1.00 24.59  ?  437 HIS   B N   1 
ATOM   4561 C  CA  . HIS   B 1 281 ? 35.756 27.153  23.604  1.00 27.84  ?  437 HIS   B CA  1 
ATOM   4562 C  C   . HIS   B 1 281 ? 36.986 26.394  23.122  1.00 23.22  ?  437 HIS   B C   1 
ATOM   4563 O  O   . HIS   B 1 281 ? 37.782 26.908  22.324  1.00 21.85  ?  437 HIS   B O   1 
ATOM   4564 C  CB  . HIS   B 1 281 ? 35.962 27.664  25.032  1.00 20.42  ?  437 HIS   B CB  1 
ATOM   4565 C  CG  . HIS   B 1 281 ? 34.845 28.525  25.533  1.00 25.02  ?  437 HIS   B CG  1 
ATOM   4566 N  ND1 . HIS   B 1 281 ? 34.207 28.291  26.732  1.00 27.13  ?  437 HIS   B ND1 1 
ATOM   4567 C  CD2 . HIS   B 1 281 ? 34.252 29.619  25.000  1.00 21.36  ?  437 HIS   B CD2 1 
ATOM   4568 C  CE1 . HIS   B 1 281 ? 33.269 29.202  26.915  1.00 25.22  ?  437 HIS   B CE1 1 
ATOM   4569 N  NE2 . HIS   B 1 281 ? 33.275 30.021  25.878  1.00 26.35  ?  437 HIS   B NE2 1 
ATOM   4570 N  N   . VAL   B 1 282 ? 37.147 25.160  23.603  1.00 20.40  ?  438 VAL   B N   1 
ATOM   4571 C  CA  . VAL   B 1 282 ? 38.258 24.312  23.181  1.00 20.75  ?  438 VAL   B CA  1 
ATOM   4572 C  C   . VAL   B 1 282 ? 38.240 24.119  21.670  1.00 19.62  ?  438 VAL   B C   1 
ATOM   4573 O  O   . VAL   B 1 282 ? 39.264 24.267  20.991  1.00 19.54  ?  438 VAL   B O   1 
ATOM   4574 C  CB  . VAL   B 1 282 ? 38.200 22.965  23.924  1.00 29.82  ?  438 VAL   B CB  1 
ATOM   4575 C  CG1 . VAL   B 1 282 ? 39.201 22.003  23.347  1.00 28.52  ?  438 VAL   B CG1 1 
ATOM   4576 C  CG2 . VAL   B 1 282 ? 38.448 23.170  25.412  1.00 25.72  ?  438 VAL   B CG2 1 
ATOM   4577 N  N   . LYS   B 1 283 ? 37.065 23.802  21.119  1.00 24.32  ?  439 LYS   B N   1 
ATOM   4578 C  CA  . LYS   B 1 283 ? 36.940 23.538  19.690  1.00 20.29  ?  439 LYS   B CA  1 
ATOM   4579 C  C   . LYS   B 1 283 ? 37.228 24.787  18.864  1.00 17.91  ?  439 LYS   B C   1 
ATOM   4580 O  O   . LYS   B 1 283 ? 37.900 24.712  17.827  1.00 23.37  ?  439 LYS   B O   1 
ATOM   4581 C  CB  . LYS   B 1 283 ? 35.537 23.013  19.391  1.00 26.08  ?  439 LYS   B CB  1 
ATOM   4582 C  CG  . LYS   B 1 283 ? 35.380 21.511  19.551  1.00 43.91  ?  439 LYS   B CG  1 
ATOM   4583 C  CD  . LYS   B 1 283 ? 33.991 21.064  19.127  1.00 43.12  ?  439 LYS   B CD  1 
ATOM   4584 C  CE  . LYS   B 1 283 ? 33.073 20.911  20.327  1.00 42.14  ?  439 LYS   B CE  1 
ATOM   4585 N  NZ  . LYS   B 1 283 ? 31.688 21.355  20.013  1.00 57.14  ?  439 LYS   B NZ  1 
ATOM   4586 N  N   . THR   B 1 284 ? 36.717 25.940  19.304  1.00 18.06  ?  440 THR   B N   1 
ATOM   4587 C  CA  . THR   B 1 284 ? 36.975 27.196  18.609  1.00 19.51  ?  440 THR   B CA  1 
ATOM   4588 C  C   . THR   B 1 284 ? 38.469 27.502  18.570  1.00 25.02  ?  440 THR   B C   1 
ATOM   4589 O  O   . THR   B 1 284 ? 39.031 27.807  17.507  1.00 18.53  ?  440 THR   B O   1 
ATOM   4590 C  CB  . THR   B 1 284 ? 36.206 28.327  19.297  1.00 20.19  ?  440 THR   B CB  1 
ATOM   4591 O  OG1 . THR   B 1 284 ? 34.828 27.959  19.431  1.00 25.97  ?  440 THR   B OG1 1 
ATOM   4592 C  CG2 . THR   B 1 284 ? 36.298 29.604  18.493  1.00 19.36  ?  440 THR   B CG2 1 
ATOM   4593 N  N   . ALA   B 1 285 ? 39.131 27.421  19.730  1.00 17.96  ?  441 ALA   B N   1 
ATOM   4594 C  CA  . ALA   B 1 285 ? 40.569 27.670  19.769  1.00 23.57  ?  441 ALA   B CA  1 
ATOM   4595 C  C   . ALA   B 1 285 ? 41.323 26.685  18.881  1.00 16.10  ?  441 ALA   B C   1 
ATOM   4596 O  O   . ALA   B 1 285 ? 42.277 27.062  18.186  1.00 23.40  ?  441 ALA   B O   1 
ATOM   4597 C  CB  . ALA   B 1 285 ? 41.078 27.597  21.209  1.00 17.12  ?  441 ALA   B CB  1 
ATOM   4598 N  N   . PHE   B 1 286 ? 40.896 25.420  18.876  1.00 18.94  ?  442 PHE   B N   1 
ATOM   4599 C  CA  . PHE   B 1 286 ? 41.565 24.417  18.053  1.00 21.04  ?  442 PHE   B CA  1 
ATOM   4600 C  C   . PHE   B 1 286 ? 41.431 24.738  16.569  1.00 23.12  ?  442 PHE   B C   1 
ATOM   4601 O  O   . PHE   B 1 286 ? 42.390 24.595  15.802  1.00 27.46  ?  442 PHE   B O   1 
ATOM   4602 C  CB  . PHE   B 1 286 ? 40.998 23.031  18.352  1.00 19.87  ?  442 PHE   B CB  1 
ATOM   4603 C  CG  . PHE   B 1 286 ? 41.497 21.972  17.422  1.00 18.39  ?  442 PHE   B CG  1 
ATOM   4604 C  CD1 . PHE   B 1 286 ? 42.782 21.471  17.551  1.00 22.38  ?  442 PHE   B CD1 1 
ATOM   4605 C  CD2 . PHE   B 1 286 ? 40.694 21.491  16.402  1.00 20.94  ?  442 PHE   B CD2 1 
ATOM   4606 C  CE1 . PHE   B 1 286 ? 43.252 20.502  16.689  1.00 30.95  ?  442 PHE   B CE1 1 
ATOM   4607 C  CE2 . PHE   B 1 286 ? 41.159 20.522  15.535  1.00 23.44  ?  442 PHE   B CE2 1 
ATOM   4608 C  CZ  . PHE   B 1 286 ? 42.440 20.026  15.680  1.00 22.24  ?  442 PHE   B CZ  1 
ATOM   4609 N  N   . PHE   B 1 287 ? 40.236 25.154  16.139  1.00 16.42  ?  443 PHE   B N   1 
ATOM   4610 C  CA  . PHE   B 1 287 ? 40.049 25.527  14.738  1.00 20.51  ?  443 PHE   B CA  1 
ATOM   4611 C  C   . PHE   B 1 287 ? 40.920 26.721  14.369  1.00 23.30  ?  443 PHE   B C   1 
ATOM   4612 O  O   . PHE   B 1 287 ? 41.481 26.781  13.265  1.00 21.87  ?  443 PHE   B O   1 
ATOM   4613 C  CB  . PHE   B 1 287 ? 38.576 25.834  14.460  1.00 15.37  ?  443 PHE   B CB  1 
ATOM   4614 C  CG  . PHE   B 1 287 ? 37.699 24.614  14.402  1.00 24.05  ?  443 PHE   B CG  1 
ATOM   4615 C  CD1 . PHE   B 1 287 ? 38.143 23.451  13.793  1.00 25.07  ?  443 PHE   B CD1 1 
ATOM   4616 C  CD2 . PHE   B 1 287 ? 36.424 24.635  14.943  1.00 26.03  ?  443 PHE   B CD2 1 
ATOM   4617 C  CE1 . PHE   B 1 287 ? 37.336 22.329  13.736  1.00 25.52  ?  443 PHE   B CE1 1 
ATOM   4618 C  CE2 . PHE   B 1 287 ? 35.611 23.517  14.888  1.00 26.45  ?  443 PHE   B CE2 1 
ATOM   4619 C  CZ  . PHE   B 1 287 ? 36.069 22.362  14.283  1.00 29.17  ?  443 PHE   B CZ  1 
ATOM   4620 N  N   . HIS   B 1 288 ? 41.048 27.686  15.283  1.00 17.28  ?  444 HIS   B N   1 
ATOM   4621 C  CA  . HIS   B 1 288 ? 41.952 28.805  15.027  1.00 20.21  ?  444 HIS   B CA  1 
ATOM   4622 C  C   . HIS   B 1 288 ? 43.389 28.323  14.858  1.00 20.11  ?  444 HIS   B C   1 
ATOM   4623 O  O   . HIS   B 1 288 ? 44.121 28.816  13.989  1.00 19.89  ?  444 HIS   B O   1 
ATOM   4624 C  CB  . HIS   B 1 288 ? 41.852 29.834  16.151  1.00 23.72  ?  444 HIS   B CB  1 
ATOM   4625 C  CG  . HIS   B 1 288 ? 40.634 30.698  16.062  1.00 24.36  ?  444 HIS   B CG  1 
ATOM   4626 N  ND1 . HIS   B 1 288 ? 40.354 31.472  14.957  1.00 20.60  ?  444 HIS   B ND1 1 
ATOM   4627 C  CD2 . HIS   B 1 288 ? 39.627 30.915  16.940  1.00 19.07  ?  444 HIS   B CD2 1 
ATOM   4628 C  CE1 . HIS   B 1 288 ? 39.224 32.126  15.156  1.00 21.10  ?  444 HIS   B CE1 1 
ATOM   4629 N  NE2 . HIS   B 1 288 ? 38.762 31.806  16.353  1.00 18.98  ?  444 HIS   B NE2 1 
ATOM   4630 N  N   . VAL   B 1 289 ? 43.811 27.356  15.677  1.00 19.37  ?  445 VAL   B N   1 
ATOM   4631 C  CA  . VAL   B 1 289 ? 45.157 26.805  15.525  1.00 22.01  ?  445 VAL   B CA  1 
ATOM   4632 C  C   . VAL   B 1 289 ? 45.300 26.095  14.181  1.00 19.08  ?  445 VAL   B C   1 
ATOM   4633 O  O   . VAL   B 1 289 ? 46.360 26.160  13.545  1.00 21.19  ?  445 VAL   B O   1 
ATOM   4634 C  CB  . VAL   B 1 289 ? 45.498 25.864  16.696  1.00 24.58  ?  445 VAL   B CB  1 
ATOM   4635 C  CG1 . VAL   B 1 289 ? 46.868 25.232  16.490  1.00 20.40  ?  445 VAL   B CG1 1 
ATOM   4636 C  CG2 . VAL   B 1 289 ? 45.461 26.617  18.014  1.00 20.58  ?  445 VAL   B CG2 1 
ATOM   4637 N  N   . CYS   B 1 290 ? 44.249 25.404  13.733  1.00 18.21  ?  446 CYS   B N   1 
ATOM   4638 C  CA  . CYS   B 1 290 ? 44.286 24.776  12.413  1.00 23.07  ?  446 CYS   B CA  1 
ATOM   4639 C  C   . CYS   B 1 290 ? 44.470 25.815  11.318  1.00 22.83  ?  446 CYS   B C   1 
ATOM   4640 O  O   . CYS   B 1 290 ? 45.186 25.579  10.338  1.00 25.64  ?  446 CYS   B O   1 
ATOM   4641 C  CB  . CYS   B 1 290 ? 43.009 23.973  12.167  1.00 15.18  ?  446 CYS   B CB  1 
ATOM   4642 S  SG  . CYS   B 1 290 ? 42.916 22.421  13.072  1.00 23.19  ?  446 CYS   B SG  1 
ATOM   4643 N  N   . THR   B 1 291 ? 43.821 26.971  11.461  1.00 15.90  ?  447 THR   B N   1 
ATOM   4644 C  CA  . THR   B 1 291 ? 44.031 28.045  10.494  1.00 19.63  ?  447 THR   B CA  1 
ATOM   4645 C  C   . THR   B 1 291 ? 45.464 28.569  10.554  1.00 25.91  ?  447 THR   B C   1 
ATOM   4646 O  O   . THR   B 1 291 ? 46.069 28.859  9.514   1.00 18.16  ?  447 THR   B O   1 
ATOM   4647 C  CB  . THR   B 1 291 ? 43.031 29.175  10.732  1.00 29.06  ?  447 THR   B CB  1 
ATOM   4648 O  OG1 . THR   B 1 291 ? 41.704 28.694  10.482  1.00 25.17  ?  447 THR   B OG1 1 
ATOM   4649 C  CG2 . THR   B 1 291 ? 43.320 30.351  9.808   1.00 18.40  ?  447 THR   B CG2 1 
ATOM   4650 N  N   . GLN   B 1 292 ? 46.031 28.684  11.761  1.00 22.48  ?  448 GLN   B N   1 
ATOM   4651 C  CA  . GLN   B 1 292 ? 47.402 29.178  11.885  1.00 30.01  ?  448 GLN   B CA  1 
ATOM   4652 C  C   . GLN   B 1 292 ? 48.419 28.218  11.277  1.00 21.50  ?  448 GLN   B C   1 
ATOM   4653 O  O   . GLN   B 1 292 ? 49.453 28.660  10.765  1.00 34.99  ?  448 GLN   B O   1 
ATOM   4654 C  CB  . GLN   B 1 292 ? 47.762 29.422  13.351  1.00 36.08  ?  448 GLN   B CB  1 
ATOM   4655 C  CG  . GLN   B 1 292 ? 47.110 30.629  13.990  1.00 30.39  ?  448 GLN   B CG  1 
ATOM   4656 C  CD  . GLN   B 1 292 ? 47.572 30.830  15.419  1.00 53.82  ?  448 GLN   B CD  1 
ATOM   4657 O  OE1 . GLN   B 1 292 ? 48.106 29.911  16.042  1.00 51.32  ?  448 GLN   B OE1 1 
ATOM   4658 N  NE2 . GLN   B 1 292 ? 47.377 32.033  15.943  1.00 48.47  ?  448 GLN   B NE2 1 
ATOM   4659 N  N   . ASN   B 1 293 ? 48.155 26.912  11.336  1.00 19.52  ?  449 ASN   B N   1 
ATOM   4660 C  CA  . ASN   B 1 293 ? 49.092 25.879  10.899  1.00 20.21  ?  449 ASN   B CA  1 
ATOM   4661 C  C   . ASN   B 1 293 ? 48.429 25.049  9.803   1.00 27.00  ?  449 ASN   B C   1 
ATOM   4662 O  O   . ASN   B 1 293 ? 48.022 23.902  10.032  1.00 22.91  ?  449 ASN   B O   1 
ATOM   4663 C  CB  . ASN   B 1 293 ? 49.519 24.998  12.071  1.00 23.44  ?  449 ASN   B CB  1 
ATOM   4664 C  CG  . ASN   B 1 293 ? 50.263 25.775  13.144  1.00 27.26  ?  449 ASN   B CG  1 
ATOM   4665 O  OD1 . ASN   B 1 293 ? 51.486 25.897  13.105  1.00 39.29  ?  449 ASN   B OD1 1 
ATOM   4666 N  ND2 . ASN   B 1 293 ? 49.521 26.312  14.106  1.00 34.52  ?  449 ASN   B ND2 1 
ATOM   4667 N  N   . PRO   B 1 294 ? 48.320 25.599  8.589   1.00 21.10  ?  450 PRO   B N   1 
ATOM   4668 C  CA  . PRO   B 1 294 ? 47.479 24.972  7.560   1.00 19.54  ?  450 PRO   B CA  1 
ATOM   4669 C  C   . PRO   B 1 294 ? 48.078 23.739  6.902   1.00 29.20  ?  450 PRO   B C   1 
ATOM   4670 O  O   . PRO   B 1 294 ? 47.337 23.002  6.236   1.00 24.22  ?  450 PRO   B O   1 
ATOM   4671 C  CB  . PRO   B 1 294 ? 47.303 26.099  6.535   1.00 29.09  ?  450 PRO   B CB  1 
ATOM   4672 C  CG  . PRO   B 1 294 ? 48.576 26.879  6.644   1.00 22.60  ?  450 PRO   B CG  1 
ATOM   4673 C  CD  . PRO   B 1 294 ? 48.975 26.826  8.100   1.00 25.50  ?  450 PRO   B CD  1 
ATOM   4674 N  N   . GLN   B 1 295 ? 49.375 23.487  7.052   1.00 22.66  ?  451 GLN   B N   1 
ATOM   4675 C  CA  . GLN   B 1 295 ? 50.022 22.383  6.357   1.00 20.02  ?  451 GLN   B CA  1 
ATOM   4676 C  C   . GLN   B 1 295 ? 49.925 21.103  7.177   1.00 28.01  ?  451 GLN   B C   1 
ATOM   4677 O  O   . GLN   B 1 295 ? 50.090 21.120  8.400   1.00 23.89  ?  451 GLN   B O   1 
ATOM   4678 C  CB  . GLN   B 1 295 ? 51.489 22.709  6.070   1.00 21.62  ?  451 GLN   B CB  1 
ATOM   4679 C  CG  . GLN   B 1 295 ? 51.707 23.973  5.251   1.00 25.10  ?  451 GLN   B CG  1 
ATOM   4680 C  CD  . GLN   B 1 295 ? 51.135 23.877  3.845   1.00 33.90  ?  451 GLN   B CD  1 
ATOM   4681 O  OE1 . GLN   B 1 295 ? 50.967 22.786  3.297   1.00 30.62  ?  451 GLN   B OE1 1 
ATOM   4682 N  NE2 . GLN   B 1 295 ? 50.834 25.027  3.255   1.00 23.79  ?  451 GLN   B NE2 1 
ATOM   4683 N  N   . ASP   B 1 296 ? 49.655 19.989  6.490   1.00 15.31  ?  452 ASP   B N   1 
ATOM   4684 C  CA  . ASP   B 1 296 ? 49.600 18.698  7.169   1.00 16.44  ?  452 ASP   B CA  1 
ATOM   4685 C  C   . ASP   B 1 296 ? 50.923 18.362  7.843   1.00 27.83  ?  452 ASP   B C   1 
ATOM   4686 O  O   . ASP   B 1 296 ? 50.941 17.662  8.861   1.00 18.10  ?  452 ASP   B O   1 
ATOM   4687 C  CB  . ASP   B 1 296 ? 49.222 17.596  6.177   1.00 20.01  ?  452 ASP   B CB  1 
ATOM   4688 C  CG  . ASP   B 1 296 ? 47.851 17.805  5.563   1.00 29.43  ?  452 ASP   B CG  1 
ATOM   4689 O  OD1 . ASP   B 1 296 ? 47.043 18.563  6.141   1.00 26.36  ?  452 ASP   B OD1 1 
ATOM   4690 O  OD2 . ASP   B 1 296 ? 47.582 17.209  4.499   1.00 22.76  -1 452 ASP   B OD2 1 
ATOM   4691 N  N   . SER   B 1 297 ? 52.036 18.857  7.297   1.00 22.11  ?  453 SER   B N   1 
ATOM   4692 C  CA  . SER   B 1 297 ? 53.351 18.599  7.866   1.00 17.35  ?  453 SER   B CA  1 
ATOM   4693 C  C   . SER   B 1 297 ? 53.581 19.329  9.181   1.00 22.85  ?  453 SER   B C   1 
ATOM   4694 O  O   . SER   B 1 297 ? 54.580 19.054  9.856   1.00 24.27  ?  453 SER   B O   1 
ATOM   4695 C  CB  . SER   B 1 297 ? 54.436 18.985  6.863   1.00 13.75  ?  453 SER   B CB  1 
ATOM   4696 O  OG  . SER   B 1 297 ? 54.386 20.371  6.572   1.00 30.92  ?  453 SER   B OG  1 
ATOM   4697 N  N   . GLN   B 1 298 ? 52.702 20.253  9.552   1.00 22.52  ?  454 GLN   B N   1 
ATOM   4698 C  CA  . GLN   B 1 298 ? 52.745 20.881  10.864  1.00 24.67  ?  454 GLN   B CA  1 
ATOM   4699 C  C   . GLN   B 1 298 ? 51.947 20.101  11.900  1.00 24.80  ?  454 GLN   B C   1 
ATOM   4700 O  O   . GLN   B 1 298 ? 51.853 20.539  13.050  1.00 27.26  ?  454 GLN   B O   1 
ATOM   4701 C  CB  . GLN   B 1 298 ? 52.226 22.318  10.768  1.00 23.88  ?  454 GLN   B CB  1 
ATOM   4702 C  CG  . GLN   B 1 298 ? 53.052 23.196  9.840   1.00 19.88  ?  454 GLN   B CG  1 
ATOM   4703 C  CD  . GLN   B 1 298 ? 52.402 24.536  9.580   1.00 34.29  ?  454 GLN   B CD  1 
ATOM   4704 O  OE1 . GLN   B 1 298 ? 51.394 24.623  8.878   1.00 28.44  ?  454 GLN   B OE1 1 
ATOM   4705 N  NE2 . GLN   B 1 298 ? 52.977 25.592  10.143  1.00 26.27  ?  454 GLN   B NE2 1 
ATOM   4706 N  N   . TRP   B 1 299 ? 51.377 18.955  11.515  1.00 23.57  ?  455 TRP   B N   1 
ATOM   4707 C  CA  . TRP   B 1 299 ? 50.588 18.118  12.410  1.00 28.43  ?  455 TRP   B CA  1 
ATOM   4708 C  C   . TRP   B 1 299 ? 51.037 16.663  12.361  1.00 20.75  ?  455 TRP   B C   1 
ATOM   4709 O  O   . TRP   B 1 299 ? 50.251 15.772  12.690  1.00 25.02  ?  455 TRP   B O   1 
ATOM   4710 C  CB  . TRP   B 1 299 ? 49.099 18.224  12.072  1.00 21.14  ?  455 TRP   B CB  1 
ATOM   4711 C  CG  . TRP   B 1 299 ? 48.554 19.593  12.273  1.00 16.48  ?  455 TRP   B CG  1 
ATOM   4712 C  CD1 . TRP   B 1 299 ? 48.478 20.586  11.345  1.00 21.48  ?  455 TRP   B CD1 1 
ATOM   4713 C  CD2 . TRP   B 1 299 ? 48.010 20.128  13.485  1.00 15.67  ?  455 TRP   B CD2 1 
ATOM   4714 N  NE1 . TRP   B 1 299 ? 47.917 21.710  11.901  1.00 21.41  ?  455 TRP   B NE1 1 
ATOM   4715 C  CE2 . TRP   B 1 299 ? 47.621 21.454  13.214  1.00 13.71  ?  455 TRP   B CE2 1 
ATOM   4716 C  CE3 . TRP   B 1 299 ? 47.812 19.615  14.769  1.00 15.10  ?  455 TRP   B CE3 1 
ATOM   4717 C  CZ2 . TRP   B 1 299 ? 47.047 22.275  14.182  1.00 22.75  ?  455 TRP   B CZ2 1 
ATOM   4718 C  CZ3 . TRP   B 1 299 ? 47.243 20.430  15.729  1.00 15.12  ?  455 TRP   B CZ3 1 
ATOM   4719 C  CH2 . TRP   B 1 299 ? 46.865 21.745  15.429  1.00 18.65  ?  455 TRP   B CH2 1 
ATOM   4720 N  N   . ASP   B 1 300 ? 52.280 16.412  11.954  1.00 24.89  ?  456 ASP   B N   1 
ATOM   4721 C  CA  . ASP   B 1 300 ? 52.809 15.056  11.873  1.00 26.43  ?  456 ASP   B CA  1 
ATOM   4722 C  C   . ASP   B 1 300 ? 52.597 14.318  13.188  1.00 29.16  ?  456 ASP   B C   1 
ATOM   4723 O  O   . ASP   B 1 300 ? 52.835 14.870  14.265  1.00 22.42  ?  456 ASP   B O   1 
ATOM   4724 C  CB  . ASP   B 1 300 ? 54.301 15.118  11.534  1.00 30.03  ?  456 ASP   B CB  1 
ATOM   4725 C  CG  . ASP   B 1 300 ? 54.854 13.793  11.037  1.00 41.96  ?  456 ASP   B CG  1 
ATOM   4726 O  OD1 . ASP   B 1 300 ? 54.692 12.765  11.729  1.00 49.25  ?  456 ASP   B OD1 1 
ATOM   4727 O  OD2 . ASP   B 1 300 ? 55.452 13.779  9.940   1.00 54.77  -1 456 ASP   B OD2 1 
ATOM   4728 N  N   . ARG   B 1 301 ? 52.122 13.068  13.097  1.00 28.32  ?  457 ARG   B N   1 
ATOM   4729 C  CA  . ARG   B 1 301 ? 51.846 12.293  14.305  1.00 38.02  ?  457 ARG   B CA  1 
ATOM   4730 C  C   . ARG   B 1 301 ? 53.068 12.245  15.214  1.00 34.18  ?  457 ARG   B C   1 
ATOM   4731 O  O   . ARG   B 1 301 ? 52.946 12.373  16.441  1.00 37.42  ?  457 ARG   B O   1 
ATOM   4732 C  CB  . ARG   B 1 301 ? 51.392 10.885  13.934  1.00 45.40  ?  457 ARG   B CB  1 
ATOM   4733 C  CG  . ARG   B 1 301 ? 51.228 9.926   15.106  1.00 48.68  ?  457 ARG   B CG  1 
ATOM   4734 C  CD  . ARG   B 1 301 ? 50.111 8.968   14.737  1.00 61.92  ?  457 ARG   B CD  1 
ATOM   4735 N  NE  . ARG   B 1 301 ? 48.799 9.589   14.938  1.00 51.43  ?  457 ARG   B NE  1 
ATOM   4736 C  CZ  . ARG   B 1 301 ? 48.367 10.128  16.075  1.00 68.34  ?  457 ARG   B CZ  1 
ATOM   4737 N  NH1 . ARG   B 1 301 ? 48.991 9.917   17.224  1.00 68.08  ?  457 ARG   B NH1 1 
ATOM   4738 N  NH2 . ARG   B 1 301 ? 47.268 10.878  16.060  1.00 47.33  ?  457 ARG   B NH2 1 
ATOM   4739 N  N   . LYS   B 1 302 ? 54.262 12.119  14.623  1.00 34.81  ?  458 LYS   B N   1 
ATOM   4740 C  CA  . LYS   B 1 302 ? 55.498 12.091  15.397  1.00 40.97  ?  458 LYS   B CA  1 
ATOM   4741 C  C   . LYS   B 1 302 ? 55.600 13.271  16.354  1.00 39.24  ?  458 LYS   B C   1 
ATOM   4742 O  O   . LYS   B 1 302 ? 56.182 13.141  17.435  1.00 37.20  ?  458 LYS   B O   1 
ATOM   4743 C  CB  . LYS   B 1 302 ? 56.705 12.089  14.457  1.00 39.53  ?  458 LYS   B CB  1 
ATOM   4744 C  CG  . LYS   B 1 302 ? 58.027 11.793  15.153  1.00 53.56  ?  458 LYS   B CG  1 
ATOM   4745 C  CD  . LYS   B 1 302 ? 58.930 13.021  15.178  1.00 60.76  ?  458 LYS   B CD  1 
ATOM   4746 C  CE  . LYS   B 1 302 ? 60.037 12.869  16.212  1.00 41.11  ?  458 LYS   B CE  1 
ATOM   4747 N  NZ  . LYS   B 1 302 ? 60.077 14.012  17.167  1.00 63.19  ?  458 LYS   B NZ  1 
ATOM   4748 N  N   . ASP   B 1 303 ? 55.034 14.421  15.980  1.00 32.83  ?  459 ASP   B N   1 
ATOM   4749 C  CA  . ASP   B 1 303 ? 55.147 15.650  16.751  1.00 29.75  ?  459 ASP   B CA  1 
ATOM   4750 C  C   . ASP   B 1 303 ? 53.946 15.905  17.655  1.00 27.98  ?  459 ASP   B C   1 
ATOM   4751 O  O   . ASP   B 1 303 ? 53.742 17.052  18.076  1.00 30.30  ?  459 ASP   B O   1 
ATOM   4752 C  CB  . ASP   B 1 303 ? 55.346 16.844  15.817  1.00 32.86  ?  459 ASP   B CB  1 
ATOM   4753 C  CG  . ASP   B 1 303 ? 56.654 16.783  15.067  1.00 35.56  ?  459 ASP   B CG  1 
ATOM   4754 O  OD1 . ASP   B 1 303 ? 57.674 16.415  15.687  1.00 59.64  ?  459 ASP   B OD1 1 
ATOM   4755 O  OD2 . ASP   B 1 303 ? 56.666 17.122  13.866  1.00 33.86  -1 459 ASP   B OD2 1 
ATOM   4756 N  N   . LEU   B 1 304 ? 53.153 14.869  17.960  1.00 26.08  ?  460 LEU   B N   1 
ATOM   4757 C  CA  . LEU   B 1 304 ? 52.002 15.037  18.846  1.00 28.54  ?  460 LEU   B CA  1 
ATOM   4758 C  C   . LEU   B 1 304 ? 52.358 15.911  20.040  1.00 20.98  ?  460 LEU   B C   1 
ATOM   4759 O  O   . LEU   B 1 304 ? 51.719 16.942  20.288  1.00 28.15  ?  460 LEU   B O   1 
ATOM   4760 C  CB  . LEU   B 1 304 ? 51.487 13.673  19.319  1.00 21.20  ?  460 LEU   B CB  1 
ATOM   4761 C  CG  . LEU   B 1 304 ? 50.391 13.715  20.390  1.00 31.83  ?  460 LEU   B CG  1 
ATOM   4762 C  CD1 . LEU   B 1 304 ? 49.149 14.412  19.862  1.00 24.37  ?  460 LEU   B CD1 1 
ATOM   4763 C  CD2 . LEU   B 1 304 ? 50.056 12.317  20.878  1.00 32.54  ?  460 LEU   B CD2 1 
ATOM   4764 N  N   . GLY   B 1 305 ? 53.437 15.544  20.736  1.00 19.32  ?  461 GLY   B N   1 
ATOM   4765 C  CA  . GLY   B 1 305 ? 53.828 16.259  21.941  1.00 20.64  ?  461 GLY   B CA  1 
ATOM   4766 C  C   . GLY   B 1 305 ? 53.926 17.756  21.742  1.00 23.25  ?  461 GLY   B C   1 
ATOM   4767 O  O   . GLY   B 1 305 ? 53.371 18.534  22.522  1.00 29.29  ?  461 GLY   B O   1 
ATOM   4768 N  N   . LEU   B 1 306 ? 54.618 18.185  20.684  1.00 28.79  ?  462 LEU   B N   1 
ATOM   4769 C  CA  . LEU   B 1 306 ? 54.737 19.622  20.461  1.00 25.42  ?  462 LEU   B CA  1 
ATOM   4770 C  C   . LEU   B 1 306 ? 53.413 20.210  19.999  1.00 26.82  ?  462 LEU   B C   1 
ATOM   4771 O  O   . LEU   B 1 306 ? 53.000 21.273  20.483  1.00 23.20  ?  462 LEU   B O   1 
ATOM   4772 C  CB  . LEU   B 1 306 ? 55.849 19.925  19.456  1.00 25.99  ?  462 LEU   B CB  1 
ATOM   4773 C  CG  . LEU   B 1 306 ? 57.093 20.521  20.128  1.00 45.52  ?  462 LEU   B CG  1 
ATOM   4774 C  CD1 . LEU   B 1 306 ? 57.881 19.454  20.876  1.00 62.08  ?  462 LEU   B CD1 1 
ATOM   4775 C  CD2 . LEU   B 1 306 ? 57.978 21.272  19.136  1.00 69.95  ?  462 LEU   B CD2 1 
ATOM   4776 N  N   . CYS   B 1 307 ? 52.718 19.513  19.094  1.00 21.70  ?  463 CYS   B N   1 
ATOM   4777 C  CA  . CYS   B 1 307 ? 51.464 20.039  18.571  1.00 28.43  ?  463 CYS   B CA  1 
ATOM   4778 C  C   . CYS   B 1 307 ? 50.493 20.328  19.705  1.00 25.58  ?  463 CYS   B C   1 
ATOM   4779 O  O   . CYS   B 1 307 ? 49.999 21.455  19.841  1.00 24.95  ?  463 CYS   B O   1 
ATOM   4780 C  CB  . CYS   B 1 307 ? 50.862 19.060  17.561  1.00 27.62  ?  463 CYS   B CB  1 
ATOM   4781 S  SG  . CYS   B 1 307 ? 51.836 18.846  16.048  1.00 24.56  ?  463 CYS   B SG  1 
ATOM   4782 N  N   . PHE   B 1 308 ? 50.251 19.331  20.560  1.00 20.49  ?  464 PHE   B N   1 
ATOM   4783 C  CA  . PHE   B 1 308 ? 49.400 19.542  21.727  1.00 21.53  ?  464 PHE   B CA  1 
ATOM   4784 C  C   . PHE   B 1 308 ? 49.874 20.735  22.543  1.00 22.65  ?  464 PHE   B C   1 
ATOM   4785 O  O   . PHE   B 1 308 ? 49.072 21.596  22.924  1.00 21.16  ?  464 PHE   B O   1 
ATOM   4786 C  CB  . PHE   B 1 308 ? 49.355 18.287  22.601  1.00 23.25  ?  464 PHE   B CB  1 
ATOM   4787 C  CG  . PHE   B 1 308 ? 48.523 18.457  23.846  1.00 22.31  ?  464 PHE   B CG  1 
ATOM   4788 C  CD1 . PHE   B 1 308 ? 47.199 18.850  23.755  1.00 21.94  ?  464 PHE   B CD1 1 
ATOM   4789 C  CD2 . PHE   B 1 308 ? 49.067 18.238  25.103  1.00 19.59  ?  464 PHE   B CD2 1 
ATOM   4790 C  CE1 . PHE   B 1 308 ? 46.429 19.019  24.889  1.00 21.35  ?  464 PHE   B CE1 1 
ATOM   4791 C  CE2 . PHE   B 1 308 ? 48.297 18.404  26.244  1.00 24.99  ?  464 PHE   B CE2 1 
ATOM   4792 C  CZ  . PHE   B 1 308 ? 46.977 18.794  26.136  1.00 19.81  ?  464 PHE   B CZ  1 
ATOM   4793 N  N   . ASP   B 1 309 ? 51.185 20.813  22.801  1.00 22.28  ?  465 ASP   B N   1 
ATOM   4794 C  CA  . ASP   B 1 309 ? 51.705 21.941  23.567  1.00 26.16  ?  465 ASP   B CA  1 
ATOM   4795 C  C   . ASP   B 1 309 ? 51.293 23.254  22.923  1.00 26.10  ?  465 ASP   B C   1 
ATOM   4796 O  O   . ASP   B 1 309 ? 50.761 24.150  23.595  1.00 30.32  ?  465 ASP   B O   1 
ATOM   4797 C  CB  . ASP   B 1 309 ? 53.229 21.851  23.682  1.00 24.77  ?  465 ASP   B CB  1 
ATOM   4798 C  CG  . ASP   B 1 309 ? 53.803 22.870  24.659  1.00 32.03  ?  465 ASP   B CG  1 
ATOM   4799 O  OD1 . ASP   B 1 309 ? 53.438 22.816  25.851  1.00 29.12  ?  465 ASP   B OD1 1 
ATOM   4800 O  OD2 . ASP   B 1 309 ? 54.620 23.720  24.239  1.00 34.25  -1 465 ASP   B OD2 1 
ATOM   4801 N  N   . ASN   B 1 310 ? 51.467 23.354  21.602  1.00 20.77  ?  466 ASN   B N   1 
ATOM   4802 C  CA  . ASN   B 1 310 ? 51.152 24.600  20.919  1.00 21.36  ?  466 ASN   B CA  1 
ATOM   4803 C  C   . ASN   B 1 310 ? 49.660 24.888  20.952  1.00 25.20  ?  466 ASN   B C   1 
ATOM   4804 O  O   . ASN   B 1 310 ? 49.259 26.058  20.927  1.00 25.08  ?  466 ASN   B O   1 
ATOM   4805 C  CB  . ASN   B 1 310 ? 51.669 24.554  19.482  1.00 24.06  ?  466 ASN   B CB  1 
ATOM   4806 C  CG  . ASN   B 1 310 ? 53.187 24.486  19.410  1.00 29.96  ?  466 ASN   B CG  1 
ATOM   4807 O  OD1 . ASN   B 1 310 ? 53.889 24.998  20.285  1.00 32.00  ?  466 ASN   B OD1 1 
ATOM   4808 N  ND2 . ASN   B 1 310 ? 53.698 23.852  18.363  1.00 29.37  ?  466 ASN   B ND2 1 
ATOM   4809 N  N   . CYS   B 1 311 ? 48.823 23.850  21.023  1.00 22.82  ?  467 CYS   B N   1 
ATOM   4810 C  CA  . CYS   B 1 311 ? 47.403 24.090  21.247  1.00 19.87  ?  467 CYS   B CA  1 
ATOM   4811 C  C   . CYS   B 1 311 ? 47.182 24.702  22.623  1.00 30.30  ?  467 CYS   B C   1 
ATOM   4812 O  O   . CYS   B 1 311 ? 46.553 25.761  22.752  1.00 27.44  ?  467 CYS   B O   1 
ATOM   4813 C  CB  . CYS   B 1 311 ? 46.611 22.792  21.089  1.00 27.87  ?  467 CYS   B CB  1 
ATOM   4814 S  SG  . CYS   B 1 311 ? 46.493 22.184  19.386  1.00 26.55  ?  467 CYS   B SG  1 
ATOM   4815 N  N   . VAL   B 1 312 ? 47.747 24.071  23.660  1.00 21.24  ?  468 VAL   B N   1 
ATOM   4816 C  CA  . VAL   B 1 312 ? 47.580 24.574  25.021  1.00 24.86  ?  468 VAL   B CA  1 
ATOM   4817 C  C   . VAL   B 1 312 ? 47.987 26.037  25.085  1.00 20.37  ?  468 VAL   B C   1 
ATOM   4818 O  O   . VAL   B 1 312 ? 47.195 26.906  25.475  1.00 18.90  ?  468 VAL   B O   1 
ATOM   4819 C  CB  . VAL   B 1 312 ? 48.387 23.717  26.014  1.00 25.04  ?  468 VAL   B CB  1 
ATOM   4820 C  CG1 . VAL   B 1 312 ? 48.392 24.363  27.391  1.00 20.60  ?  468 VAL   B CG1 1 
ATOM   4821 C  CG2 . VAL   B 1 312 ? 47.823 22.303  26.089  1.00 22.16  ?  468 VAL   B CG2 1 
ATOM   4822 N  N   . THR   B 1 313 ? 49.214 26.330  24.643  1.00 20.28  ?  469 THR   B N   1 
ATOM   4823 C  CA  . THR   B 1 313 ? 49.705 27.702  24.615  1.00 20.29  ?  469 THR   B CA  1 
ATOM   4824 C  C   . THR   B 1 313 ? 48.688 28.640  23.985  1.00 18.84  ?  469 THR   B C   1 
ATOM   4825 O  O   . THR   B 1 313 ? 48.316 29.657  24.583  1.00 24.74  ?  469 THR   B O   1 
ATOM   4826 C  CB  . THR   B 1 313 ? 51.036 27.776  23.862  1.00 25.98  ?  469 THR   B CB  1 
ATOM   4827 O  OG1 . THR   B 1 313 ? 52.056 27.114  24.621  1.00 31.97  ?  469 THR   B OG1 1 
ATOM   4828 C  CG2 . THR   B 1 313 ? 51.435 29.227  23.632  1.00 26.30  ?  469 THR   B CG2 1 
ATOM   4829 N  N   . TYR   B 1 314 ? 48.186 28.294  22.794  1.00 21.19  ?  470 TYR   B N   1 
ATOM   4830 C  CA  . TYR   B 1 314 ? 47.255 29.201  22.132  1.00 21.06  ?  470 TYR   B CA  1 
ATOM   4831 C  C   . TYR   B 1 314 ? 46.029 29.426  22.999  1.00 19.59  ?  470 TYR   B C   1 
ATOM   4832 O  O   . TYR   B 1 314 ? 45.619 30.572  23.224  1.00 23.81  ?  470 TYR   B O   1 
ATOM   4833 C  CB  . TYR   B 1 314 ? 46.837 28.682  20.757  1.00 20.27  ?  470 TYR   B CB  1 
ATOM   4834 C  CG  . TYR   B 1 314 ? 45.879 29.646  20.084  1.00 25.48  ?  470 TYR   B CG  1 
ATOM   4835 C  CD1 . TYR   B 1 314 ? 46.333 30.860  19.586  1.00 23.88  ?  470 TYR   B CD1 1 
ATOM   4836 C  CD2 . TYR   B 1 314 ? 44.522 29.362  19.981  1.00 21.93  ?  470 TYR   B CD2 1 
ATOM   4837 C  CE1 . TYR   B 1 314 ? 45.468 31.755  18.984  1.00 27.12  ?  470 TYR   B CE1 1 
ATOM   4838 C  CE2 . TYR   B 1 314 ? 43.649 30.252  19.375  1.00 26.67  ?  470 TYR   B CE2 1 
ATOM   4839 C  CZ  . TYR   B 1 314 ? 44.129 31.447  18.881  1.00 24.10  ?  470 TYR   B CZ  1 
ATOM   4840 O  OH  . TYR   B 1 314 ? 43.269 32.340  18.281  1.00 38.64  ?  470 TYR   B OH  1 
ATOM   4841 N  N   . PHE   B 1 315 ? 45.450 28.340  23.519  1.00 17.98  ?  471 PHE   B N   1 
ATOM   4842 C  CA  . PHE   B 1 315 ? 44.310 28.491  24.412  1.00 21.62  ?  471 PHE   B CA  1 
ATOM   4843 C  C   . PHE   B 1 315 ? 44.669 29.414  25.563  1.00 23.13  ?  471 PHE   B C   1 
ATOM   4844 O  O   . PHE   B 1 315 ? 43.938 30.370  25.857  1.00 19.67  ?  471 PHE   B O   1 
ATOM   4845 C  CB  . PHE   B 1 315 ? 43.853 27.119  24.914  1.00 20.65  ?  471 PHE   B CB  1 
ATOM   4846 C  CG  . PHE   B 1 315 ? 42.508 27.130  25.594  1.00 22.10  ?  471 PHE   B CG  1 
ATOM   4847 C  CD1 . PHE   B 1 315 ? 41.344 27.213  24.847  1.00 21.22  ?  471 PHE   B CD1 1 
ATOM   4848 C  CD2 . PHE   B 1 315 ? 42.405 27.028  26.973  1.00 19.59  ?  471 PHE   B CD2 1 
ATOM   4849 C  CE1 . PHE   B 1 315 ? 40.106 27.217  25.457  1.00 20.68  ?  471 PHE   B CE1 1 
ATOM   4850 C  CE2 . PHE   B 1 315 ? 41.163 27.028  27.591  1.00 22.21  ?  471 PHE   B CE2 1 
ATOM   4851 C  CZ  . PHE   B 1 315 ? 40.013 27.122  26.831  1.00 20.01  ?  471 PHE   B CZ  1 
ATOM   4852 N  N   . LEU   B 1 316 ? 45.843 29.196  26.165  1.00 20.82  ?  472 LEU   B N   1 
ATOM   4853 C  CA  . LEU   B 1 316 ? 46.303 30.068  27.238  1.00 20.23  ?  472 LEU   B CA  1 
ATOM   4854 C  C   . LEU   B 1 316 ? 46.328 31.520  26.784  1.00 20.34  ?  472 LEU   B C   1 
ATOM   4855 O  O   . LEU   B 1 316 ? 45.821 32.406  27.483  1.00 20.90  ?  472 LEU   B O   1 
ATOM   4856 C  CB  . LEU   B 1 316 ? 47.684 29.626  27.718  1.00 22.90  ?  472 LEU   B CB  1 
ATOM   4857 C  CG  . LEU   B 1 316 ? 47.677 28.447  28.689  1.00 23.85  ?  472 LEU   B CG  1 
ATOM   4858 C  CD1 . LEU   B 1 316 ? 49.090 27.967  28.971  1.00 21.36  ?  472 LEU   B CD1 1 
ATOM   4859 C  CD2 . LEU   B 1 316 ? 46.967 28.842  29.972  1.00 21.69  ?  472 LEU   B CD2 1 
ATOM   4860 N  N   . GLN   B 1 317 ? 46.886 31.780  25.598  1.00 19.89  ?  473 GLN   B N   1 
ATOM   4861 C  CA  . GLN   B 1 317 ? 46.919 33.145  25.087  1.00 20.11  ?  473 GLN   B CA  1 
ATOM   4862 C  C   . GLN   B 1 317 ? 45.515 33.733  25.060  1.00 22.48  ?  473 GLN   B C   1 
ATOM   4863 O  O   . GLN   B 1 317 ? 45.278 34.835  25.572  1.00 20.81  ?  473 GLN   B O   1 
ATOM   4864 C  CB  . GLN   B 1 317 ? 47.557 33.172  23.694  1.00 19.60  ?  473 GLN   B CB  1 
ATOM   4865 C  CG  . GLN   B 1 317 ? 47.768 34.575  23.133  1.00 19.98  ?  473 GLN   B CG  1 
ATOM   4866 C  CD  . GLN   B 1 317 ? 48.603 34.582  21.862  1.00 27.54  ?  473 GLN   B CD  1 
ATOM   4867 O  OE1 . GLN   B 1 317 ? 48.119 34.245  20.781  1.00 24.69  ?  473 GLN   B OE1 1 
ATOM   4868 N  NE2 . GLN   B 1 317 ? 49.868 34.967  21.989  1.00 26.63  ?  473 GLN   B NE2 1 
ATOM   4869 N  N   . CYS   B 1 318 ? 44.555 32.966  24.530  1.00 19.60  ?  474 CYS   B N   1 
ATOM   4870 C  CA  . CYS   B 1 318 ? 43.179 33.445  24.459  1.00 19.75  ?  474 CYS   B CA  1 
ATOM   4871 C  C   . CYS   B 1 318 ? 42.655 33.804  25.841  1.00 27.51  ?  474 CYS   B C   1 
ATOM   4872 O  O   . CYS   B 1 318 ? 41.947 34.806  26.002  1.00 20.99  ?  474 CYS   B O   1 
ATOM   4873 C  CB  . CYS   B 1 318 ? 42.287 32.392  23.804  1.00 19.16  ?  474 CYS   B CB  1 
ATOM   4874 S  SG  . CYS   B 1 318 ? 42.645 32.094  22.060  1.00 25.29  ?  474 CYS   B SG  1 
ATOM   4875 N  N   . LEU   B 1 319 ? 43.011 33.013  26.855  1.00 20.68  ?  475 LEU   B N   1 
ATOM   4876 C  CA  . LEU   B 1 319 ? 42.550 33.310  28.205  1.00 21.47  ?  475 LEU   B CA  1 
ATOM   4877 C  C   . LEU   B 1 319 ? 43.153 34.610  28.718  1.00 22.77  ?  475 LEU   B C   1 
ATOM   4878 O  O   . LEU   B 1 319 ? 42.458 35.418  29.345  1.00 27.77  ?  475 LEU   B O   1 
ATOM   4879 C  CB  . LEU   B 1 319 ? 42.890 32.159  29.149  1.00 24.70  ?  475 LEU   B CB  1 
ATOM   4880 C  CG  . LEU   B 1 319 ? 42.091 30.865  29.009  1.00 24.73  ?  475 LEU   B CG  1 
ATOM   4881 C  CD1 . LEU   B 1 319 ? 42.830 29.725  29.689  1.00 21.43  ?  475 LEU   B CD1 1 
ATOM   4882 C  CD2 . LEU   B 1 319 ? 40.697 31.029  29.592  1.00 21.78  ?  475 LEU   B CD2 1 
ATOM   4883 N  N   . ARG   B 1 320 ? 44.443 34.839  28.448  1.00 22.13  ?  476 ARG   B N   1 
ATOM   4884 C  CA  . ARG   B 1 320 ? 45.106 35.998  29.039  1.00 22.95  ?  476 ARG   B CA  1 
ATOM   4885 C  C   . ARG   B 1 320 ? 44.633 37.290  28.392  1.00 23.18  ?  476 ARG   B C   1 
ATOM   4886 O  O   . ARG   B 1 320 ? 44.368 38.280  29.083  1.00 32.38  ?  476 ARG   B O   1 
ATOM   4887 C  CB  . ARG   B 1 320 ? 46.623 35.873  28.911  1.00 23.00  ?  476 ARG   B CB  1 
ATOM   4888 C  CG  . ARG   B 1 320 ? 47.209 34.684  29.641  1.00 23.01  ?  476 ARG   B CG  1 
ATOM   4889 C  CD  . ARG   B 1 320 ? 48.690 34.875  29.915  1.00 34.87  ?  476 ARG   B CD  1 
ATOM   4890 N  NE  . ARG   B 1 320 ? 49.364 33.597  30.110  1.00 29.02  ?  476 ARG   B NE  1 
ATOM   4891 C  CZ  . ARG   B 1 320 ? 49.739 32.798  29.121  1.00 43.08  ?  476 ARG   B CZ  1 
ATOM   4892 N  NH1 . ARG   B 1 320 ? 49.524 33.119  27.856  1.00 28.08  ?  476 ARG   B NH1 1 
ATOM   4893 N  NH2 . ARG   B 1 320 ? 50.352 31.653  29.408  1.00 29.78  ?  476 ARG   B NH2 1 
ATOM   4894 N  N   . THR   B 1 321 ? 44.529 37.297  27.066  1.00 22.56  ?  477 THR   B N   1 
ATOM   4895 C  CA  . THR   B 1 321 ? 44.072 38.465  26.330  1.00 25.21  ?  477 THR   B CA  1 
ATOM   4896 C  C   . THR   B 1 321 ? 42.553 38.580  26.289  1.00 25.70  ?  477 THR   B C   1 
ATOM   4897 O  O   . THR   B 1 321 ? 42.041 39.528  25.686  1.00 32.35  ?  477 THR   B O   1 
ATOM   4898 C  CB  . THR   B 1 321 ? 44.635 38.438  24.904  1.00 22.27  ?  477 THR   B CB  1 
ATOM   4899 O  OG1 . THR   B 1 321 ? 44.109 37.307  24.199  1.00 31.30  ?  477 THR   B OG1 1 
ATOM   4900 C  CG2 . THR   B 1 321 ? 46.157 38.341  24.933  1.00 22.36  ?  477 THR   B CG2 1 
ATOM   4901 N  N   . GLU   B 1 322 ? 41.832 37.646  26.916  1.00 23.47  ?  478 GLU   B N   1 
ATOM   4902 C  CA  . GLU   B 1 322 ? 40.367 37.668  26.970  1.00 26.36  ?  478 GLU   B CA  1 
ATOM   4903 C  C   . GLU   B 1 322 ? 39.755 37.782  25.578  1.00 24.78  ?  478 GLU   B C   1 
ATOM   4904 O  O   . GLU   B 1 322 ? 38.793 38.522  25.358  1.00 26.96  ?  478 GLU   B O   1 
ATOM   4905 C  CB  . GLU   B 1 322 ? 39.861 38.801  27.862  1.00 25.65  ?  478 GLU   B CB  1 
ATOM   4906 C  CG  . GLU   B 1 322 ? 40.255 38.694  29.314  1.00 31.54  ?  478 GLU   B CG  1 
ATOM   4907 C  CD  . GLU   B 1 322 ? 39.528 39.706  30.172  1.00 39.30  ?  478 GLU   B CD  1 
ATOM   4908 O  OE1 . GLU   B 1 322 ? 38.383 39.427  30.584  1.00 42.61  ?  478 GLU   B OE1 1 
ATOM   4909 O  OE2 . GLU   B 1 322 ? 40.103 40.783  30.435  1.00 47.63  -1 478 GLU   B OE2 1 
ATOM   4910 N  N   . LYS   B 1 323 ? 40.312 37.041  24.622  1.00 28.99  ?  479 LYS   B N   1 
ATOM   4911 C  CA  . LYS   B 1 323 ? 39.858 37.129  23.240  1.00 31.62  ?  479 LYS   B CA  1 
ATOM   4912 C  C   . LYS   B 1 323 ? 39.829 35.743  22.618  1.00 26.44  ?  479 LYS   B C   1 
ATOM   4913 O  O   . LYS   B 1 323 ? 40.873 35.100  22.478  1.00 19.87  ?  479 LYS   B O   1 
ATOM   4914 C  CB  . LYS   B 1 323 ? 40.757 38.057  22.418  1.00 29.32  ?  479 LYS   B CB  1 
ATOM   4915 C  CG  . LYS   B 1 323 ? 40.472 37.989  20.934  1.00 48.69  ?  479 LYS   B CG  1 
ATOM   4916 C  CD  . LYS   B 1 323 ? 41.554 38.662  20.116  1.00 66.92  ?  479 LYS   B CD  1 
ATOM   4917 C  CE  . LYS   B 1 323 ? 41.231 38.563  18.638  1.00 48.92  ?  479 LYS   B CE  1 
ATOM   4918 N  NZ  . LYS   B 1 323 ? 39.876 39.112  18.365  1.00 59.33  ?  479 LYS   B NZ  1 
ATOM   4919 N  N   . LEU   B 1 324 ? 38.635 35.297  22.235  1.00 29.16  ?  480 LEU   B N   1 
ATOM   4920 C  CA  . LEU   B 1 324 ? 38.454 34.051  21.492  1.00 23.48  ?  480 LEU   B CA  1 
ATOM   4921 C  C   . LEU   B 1 324 ? 37.295 34.281  20.530  1.00 30.24  ?  480 LEU   B C   1 
ATOM   4922 O  O   . LEU   B 1 324 ? 36.129 34.123  20.905  1.00 27.93  ?  480 LEU   B O   1 
ATOM   4923 C  CB  . LEU   B 1 324 ? 38.191 32.872  22.423  1.00 19.50  ?  480 LEU   B CB  1 
ATOM   4924 C  CG  . LEU   B 1 324 ? 37.957 31.521  21.742  1.00 20.06  ?  480 LEU   B CG  1 
ATOM   4925 C  CD1 . LEU   B 1 324 ? 39.176 31.107  20.934  1.00 22.32  ?  480 LEU   B CD1 1 
ATOM   4926 C  CD2 . LEU   B 1 324 ? 37.602 30.451  22.763  1.00 25.87  ?  480 LEU   B CD2 1 
ATOM   4927 N  N   . GLU   B 1 325 ? 37.618 34.674  19.301  1.00 24.49  ?  481 GLU   B N   1 
ATOM   4928 C  CA  . GLU   B 1 325 ? 36.593 34.927  18.298  1.00 28.93  ?  481 GLU   B CA  1 
ATOM   4929 C  C   . GLU   B 1 325 ? 35.866 33.639  17.949  1.00 24.43  ?  481 GLU   B C   1 
ATOM   4930 O  O   . GLU   B 1 325 ? 36.497 32.600  17.737  1.00 19.42  ?  481 GLU   B O   1 
ATOM   4931 C  CB  . GLU   B 1 325 ? 37.210 35.514  17.031  1.00 26.64  ?  481 GLU   B CB  1 
ATOM   4932 C  CG  . GLU   B 1 325 ? 37.909 36.836  17.212  1.00 36.33  ?  481 GLU   B CG  1 
ATOM   4933 C  CD  . GLU   B 1 325 ? 38.548 37.330  15.928  1.00 54.19  ?  481 GLU   B CD  1 
ATOM   4934 O  OE1 . GLU   B 1 325 ? 38.473 36.614  14.905  1.00 30.84  ?  481 GLU   B OE1 1 
ATOM   4935 O  OE2 . GLU   B 1 325 ? 39.129 38.434  15.945  1.00 60.08  -1 481 GLU   B OE2 1 
ATOM   4936 N  N   . ASN   B 1 326 ? 34.539 33.709  17.886  1.00 21.26  ?  482 ASN   B N   1 
ATOM   4937 C  CA  . ASN   B 1 326 ? 33.770 32.624  17.295  1.00 20.53  ?  482 ASN   B CA  1 
ATOM   4938 C  C   . ASN   B 1 326 ? 34.302 32.336  15.900  1.00 21.83  ?  482 ASN   B C   1 
ATOM   4939 O  O   . ASN   B 1 326 ? 34.513 33.255  15.104  1.00 22.52  ?  482 ASN   B O   1 
ATOM   4940 C  CB  . ASN   B 1 326 ? 32.286 32.999  17.243  1.00 24.26  ?  482 ASN   B CB  1 
ATOM   4941 C  CG  . ASN   B 1 326 ? 31.425 31.900  16.651  1.00 29.93  ?  482 ASN   B CG  1 
ATOM   4942 O  OD1 . ASN   B 1 326 ? 31.472 31.635  15.449  1.00 20.18  ?  482 ASN   B OD1 1 
ATOM   4943 N  ND2 . ASN   B 1 326 ? 30.631 31.256  17.494  1.00 25.75  ?  482 ASN   B ND2 1 
ATOM   4944 N  N   . TYR   B 1 327 ? 34.543 31.057  15.612  1.00 24.59  ?  483 TYR   B N   1 
ATOM   4945 C  CA  . TYR   B 1 327 ? 35.201 30.702  14.360  1.00 22.29  ?  483 TYR   B CA  1 
ATOM   4946 C  C   . TYR   B 1 327 ? 34.360 31.077  13.146  1.00 27.27  ?  483 TYR   B C   1 
ATOM   4947 O  O   . TYR   B 1 327 ? 34.908 31.303  12.061  1.00 25.09  ?  483 TYR   B O   1 
ATOM   4948 C  CB  . TYR   B 1 327 ? 35.518 29.210  14.335  1.00 17.22  ?  483 TYR   B CB  1 
ATOM   4949 C  CG  . TYR   B 1 327 ? 36.494 28.827  13.253  1.00 28.52  ?  483 TYR   B CG  1 
ATOM   4950 C  CD1 . TYR   B 1 327 ? 37.837 29.150  13.366  1.00 18.12  ?  483 TYR   B CD1 1 
ATOM   4951 C  CD2 . TYR   B 1 327 ? 36.075 28.142  12.120  1.00 24.08  ?  483 TYR   B CD2 1 
ATOM   4952 C  CE1 . TYR   B 1 327 ? 38.739 28.803  12.386  1.00 20.14  ?  483 TYR   B CE1 1 
ATOM   4953 C  CE2 . TYR   B 1 327 ? 36.971 27.789  11.130  1.00 18.45  ?  483 TYR   B CE2 1 
ATOM   4954 C  CZ  . TYR   B 1 327 ? 38.302 28.123  11.271  1.00 26.30  ?  483 TYR   B CZ  1 
ATOM   4955 O  OH  . TYR   B 1 327 ? 39.208 27.781  10.295  1.00 21.45  ?  483 TYR   B OH  1 
ATOM   4956 N  N   . PHE   B 1 328 ? 33.039 31.149  13.306  1.00 26.58  ?  484 PHE   B N   1 
ATOM   4957 C  CA  . PHE   B 1 328 ? 32.146 31.488  12.207  1.00 28.95  ?  484 PHE   B CA  1 
ATOM   4958 C  C   . PHE   B 1 328 ? 31.634 32.919  12.268  1.00 28.23  ?  484 PHE   B C   1 
ATOM   4959 O  O   . PHE   B 1 328 ? 31.215 33.452  11.235  1.00 25.37  ?  484 PHE   B O   1 
ATOM   4960 C  CB  . PHE   B 1 328 ? 30.947 30.532  12.188  1.00 24.95  ?  484 PHE   B CB  1 
ATOM   4961 C  CG  . PHE   B 1 328 ? 31.325 29.097  11.980  1.00 28.99  ?  484 PHE   B CG  1 
ATOM   4962 C  CD1 . PHE   B 1 328 ? 31.683 28.301  13.054  1.00 31.19  ?  484 PHE   B CD1 1 
ATOM   4963 C  CD2 . PHE   B 1 328 ? 31.321 28.541  10.713  1.00 27.99  ?  484 PHE   B CD2 1 
ATOM   4964 C  CE1 . PHE   B 1 328 ? 32.035 26.981  12.870  1.00 30.77  ?  484 PHE   B CE1 1 
ATOM   4965 C  CE2 . PHE   B 1 328 ? 31.669 27.222  10.523  1.00 30.96  ?  484 PHE   B CE2 1 
ATOM   4966 C  CZ  . PHE   B 1 328 ? 32.028 26.440  11.603  1.00 25.55  ?  484 PHE   B CZ  1 
ATOM   4967 N  N   . ILE   B 1 329 ? 31.653 33.544  13.442  1.00 26.04  ?  485 ILE   B N   1 
ATOM   4968 C  CA  . ILE   B 1 329 ? 31.168 34.910  13.630  1.00 28.77  ?  485 ILE   B CA  1 
ATOM   4969 C  C   . ILE   B 1 329 ? 32.289 35.720  14.274  1.00 27.77  ?  485 ILE   B C   1 
ATOM   4970 O  O   . ILE   B 1 329 ? 32.346 35.819  15.508  1.00 27.86  ?  485 ILE   B O   1 
ATOM   4971 C  CB  . ILE   B 1 329 ? 29.889 34.926  14.485  1.00 27.76  ?  485 ILE   B CB  1 
ATOM   4972 C  CG1 . ILE   B 1 329 ? 28.902 33.876  13.968  1.00 31.99  ?  485 ILE   B CG1 1 
ATOM   4973 C  CG2 . ILE   B 1 329 ? 29.249 36.308  14.471  1.00 27.55  ?  485 ILE   B CG2 1 
ATOM   4974 C  CD1 . ILE   B 1 329 ? 27.821 33.500  14.954  1.00 31.59  ?  485 ILE   B CD1 1 
ATOM   4975 N  N   . PRO   B 1 330 ? 33.187 36.317  13.485  1.00 29.24  ?  486 PRO   B N   1 
ATOM   4976 C  CA  . PRO   B 1 330 ? 34.439 36.851  14.057  1.00 29.62  ?  486 PRO   B CA  1 
ATOM   4977 C  C   . PRO   B 1 330 ? 34.251 37.929  15.113  1.00 25.53  ?  486 PRO   B C   1 
ATOM   4978 O  O   . PRO   B 1 330 ? 35.105 38.059  15.999  1.00 28.49  ?  486 PRO   B O   1 
ATOM   4979 C  CB  . PRO   B 1 330 ? 35.174 37.402  12.827  1.00 25.39  ?  486 PRO   B CB  1 
ATOM   4980 C  CG  . PRO   B 1 330 ? 34.607 36.648  11.672  1.00 27.21  ?  486 PRO   B CG  1 
ATOM   4981 C  CD  . PRO   B 1 330 ? 33.165 36.409  12.015  1.00 24.79  ?  486 PRO   B CD  1 
ATOM   4982 N  N   . GLU   B 1 331 ? 33.174 38.711  15.057  1.00 28.90  ?  487 GLU   B N   1 
ATOM   4983 C  CA  . GLU   B 1 331 ? 32.996 39.800  16.007  1.00 31.13  ?  487 GLU   B CA  1 
ATOM   4984 C  C   . GLU   B 1 331 ? 32.340 39.366  17.311  1.00 28.92  ?  487 GLU   B C   1 
ATOM   4985 O  O   . GLU   B 1 331 ? 32.222 40.188  18.228  1.00 32.86  ?  487 GLU   B O   1 
ATOM   4986 C  CB  . GLU   B 1 331 ? 32.187 40.936  15.372  1.00 44.19  ?  487 GLU   B CB  1 
ATOM   4987 C  CG  . GLU   B 1 331 ? 32.889 41.579  14.186  1.00 37.10  ?  487 GLU   B CG  1 
ATOM   4988 C  CD  . GLU   B 1 331 ? 32.098 42.715  13.575  1.00 60.66  ?  487 GLU   B CD  1 
ATOM   4989 O  OE1 . GLU   B 1 331 ? 30.994 42.459  13.049  1.00 68.87  ?  487 GLU   B OE1 1 
ATOM   4990 O  OE2 . GLU   B 1 331 ? 32.582 43.865  13.617  1.00 77.64  -1 487 GLU   B OE2 1 
ATOM   4991 N  N   . PHE   B 1 332 ? 31.917 38.110  17.425  1.00 34.73  ?  488 PHE   B N   1 
ATOM   4992 C  CA  . PHE   B 1 332 ? 31.438 37.567  18.692  1.00 27.02  ?  488 PHE   B CA  1 
ATOM   4993 C  C   . PHE   B 1 332 ? 32.636 37.013  19.454  1.00 26.44  ?  488 PHE   B C   1 
ATOM   4994 O  O   . PHE   B 1 332 ? 33.209 35.988  19.069  1.00 22.74  ?  488 PHE   B O   1 
ATOM   4995 C  CB  . PHE   B 1 332 ? 30.382 36.488  18.470  1.00 28.84  ?  488 PHE   B CB  1 
ATOM   4996 C  CG  . PHE   B 1 332 ? 29.608 36.137  19.711  1.00 32.86  ?  488 PHE   B CG  1 
ATOM   4997 C  CD1 . PHE   B 1 332 ? 28.446 36.817  20.037  1.00 29.68  ?  488 PHE   B CD1 1 
ATOM   4998 C  CD2 . PHE   B 1 332 ? 30.051 35.135  20.560  1.00 32.76  ?  488 PHE   B CD2 1 
ATOM   4999 C  CE1 . PHE   B 1 332 ? 27.735 36.497  21.181  1.00 31.17  ?  488 PHE   B CE1 1 
ATOM   5000 C  CE2 . PHE   B 1 332 ? 29.346 34.813  21.704  1.00 29.80  ?  488 PHE   B CE2 1 
ATOM   5001 C  CZ  . PHE   B 1 332 ? 28.186 35.494  22.015  1.00 25.21  ?  488 PHE   B CZ  1 
ATOM   5002 N  N   . ASN   B 1 333 ? 33.014 37.692  20.534  1.00 27.51  ?  489 ASN   B N   1 
ATOM   5003 C  CA  . ASN   B 1 333 ? 34.145 37.282  21.360  1.00 30.32  ?  489 ASN   B CA  1 
ATOM   5004 C  C   . ASN   B 1 333 ? 33.626 36.352  22.451  1.00 24.89  ?  489 ASN   B C   1 
ATOM   5005 O  O   . ASN   B 1 333 ? 32.909 36.786  23.358  1.00 33.17  ?  489 ASN   B O   1 
ATOM   5006 C  CB  . ASN   B 1 333 ? 34.842 38.504  21.953  1.00 23.03  ?  489 ASN   B CB  1 
ATOM   5007 C  CG  . ASN   B 1 333 ? 36.040 38.138  22.811  1.00 26.57  ?  489 ASN   B CG  1 
ATOM   5008 O  OD1 . ASN   B 1 333 ? 36.397 36.967  22.943  1.00 29.47  ?  489 ASN   B OD1 1 
ATOM   5009 N  ND2 . ASN   B 1 333 ? 36.672 39.148  23.398  1.00 27.26  ?  489 ASN   B ND2 1 
ATOM   5010 N  N   . LEU   B 1 334 ? 33.994 35.070  22.364  1.00 28.08  ?  490 LEU   B N   1 
ATOM   5011 C  CA  . LEU   B 1 334 ? 33.528 34.097  23.348  1.00 30.27  ?  490 LEU   B CA  1 
ATOM   5012 C  C   . LEU   B 1 334 ? 34.116 34.360  24.729  1.00 28.20  ?  490 LEU   B C   1 
ATOM   5013 O  O   . LEU   B 1 334 ? 33.497 34.015  25.741  1.00 26.30  ?  490 LEU   B O   1 
ATOM   5014 C  CB  . LEU   B 1 334 ? 33.871 32.679  22.891  1.00 24.78  ?  490 LEU   B CB  1 
ATOM   5015 C  CG  . LEU   B 1 334 ? 33.188 32.183  21.614  1.00 28.07  ?  490 LEU   B CG  1 
ATOM   5016 C  CD1 . LEU   B 1 334 ? 33.922 30.977  21.048  1.00 20.08  ?  490 LEU   B CD1 1 
ATOM   5017 C  CD2 . LEU   B 1 334 ? 31.732 31.845  21.884  1.00 23.56  ?  490 LEU   B CD2 1 
ATOM   5018 N  N   . PHE   B 1 335 ? 35.304 34.963  24.793  1.00 25.59  ?  491 PHE   B N   1 
ATOM   5019 C  CA  . PHE   B 1 335 ? 35.976 35.250  26.055  1.00 25.43  ?  491 PHE   B CA  1 
ATOM   5020 C  C   . PHE   B 1 335 ? 35.765 36.690  26.509  1.00 29.65  ?  491 PHE   B C   1 
ATOM   5021 O  O   . PHE   B 1 335 ? 36.595 37.237  27.243  1.00 32.11  ?  491 PHE   B O   1 
ATOM   5022 C  CB  . PHE   B 1 335 ? 37.469 34.947  25.941  1.00 27.35  ?  491 PHE   B CB  1 
ATOM   5023 C  CG  . PHE   B 1 335 ? 37.810 33.495  26.110  1.00 28.87  ?  491 PHE   B CG  1 
ATOM   5024 C  CD1 . PHE   B 1 335 ? 36.841 32.577  26.481  1.00 22.72  ?  491 PHE   B CD1 1 
ATOM   5025 C  CD2 . PHE   B 1 335 ? 39.106 33.049  25.911  1.00 24.56  ?  491 PHE   B CD2 1 
ATOM   5026 C  CE1 . PHE   B 1 335 ? 37.158 31.240  26.642  1.00 24.60  ?  491 PHE   B CE1 1 
ATOM   5027 C  CE2 . PHE   B 1 335 ? 39.429 31.714  26.069  1.00 21.00  ?  491 PHE   B CE2 1 
ATOM   5028 C  CZ  . PHE   B 1 335 ? 38.454 30.808  26.436  1.00 22.59  ?  491 PHE   B CZ  1 
ATOM   5029 N  N   . SER   B 1 336 ? 34.670 37.316  26.084  1.00 24.23  ?  492 SER   B N   1 
ATOM   5030 C  CA  . SER   B 1 336 ? 34.407 38.698  26.457  1.00 30.06  ?  492 SER   B CA  1 
ATOM   5031 C  C   . SER   B 1 336 ? 34.213 38.820  27.964  1.00 33.07  ?  492 SER   B C   1 
ATOM   5032 O  O   . SER   B 1 336 ? 33.711 37.907  28.626  1.00 34.01  ?  492 SER   B O   1 
ATOM   5033 C  CB  . SER   B 1 336 ? 33.170 39.220  25.728  1.00 29.06  ?  492 SER   B CB  1 
ATOM   5034 O  OG  . SER   B 1 336 ? 32.788 40.489  26.225  1.00 44.21  ?  492 SER   B OG  1 
ATOM   5035 N  N   . SER   B 1 337 ? 34.622 39.970  28.508  1.00 32.47  ?  493 SER   B N   1 
ATOM   5036 C  CA  . SER   B 1 337 ? 34.428 40.231  29.930  1.00 42.70  ?  493 SER   B CA  1 
ATOM   5037 C  C   . SER   B 1 337 ? 32.956 40.245  30.313  1.00 40.81  ?  493 SER   B C   1 
ATOM   5038 O  O   . SER   B 1 337 ? 32.630 40.046  31.488  1.00 34.89  ?  493 SER   B O   1 
ATOM   5039 C  CB  . SER   B 1 337 ? 35.077 41.560  30.317  1.00 27.74  ?  493 SER   B CB  1 
ATOM   5040 O  OG  . SER   B 1 337 ? 36.380 41.662  29.773  1.00 63.11  ?  493 SER   B OG  1 
ATOM   5041 N  N   . ASN   B 1 338 ? 32.064 40.479  29.351  1.00 42.93  ?  494 ASN   B N   1 
ATOM   5042 C  CA  . ASN   B 1 338 ? 30.630 40.471  29.600  1.00 37.86  ?  494 ASN   B CA  1 
ATOM   5043 C  C   . ASN   B 1 338 ? 30.053 39.064  29.681  1.00 40.21  ?  494 ASN   B C   1 
ATOM   5044 O  O   . ASN   B 1 338 ? 28.921 38.904  30.149  1.00 37.47  ?  494 ASN   B O   1 
ATOM   5045 C  CB  . ASN   B 1 338 ? 29.910 41.262  28.506  1.00 48.36  ?  494 ASN   B CB  1 
ATOM   5046 C  CG  . ASN   B 1 338 ? 30.321 42.726  28.478  1.00 62.40  ?  494 ASN   B CG  1 
ATOM   5047 O  OD1 . ASN   B 1 338 ? 31.011 43.207  29.376  1.00 60.01  ?  494 ASN   B OD1 1 
ATOM   5048 N  ND2 . ASN   B 1 338 ? 29.898 43.440  27.439  1.00 70.00  ?  494 ASN   B ND2 1 
ATOM   5049 N  N   . LEU   B 1 339 ? 30.793 38.051  29.239  1.00 41.97  ?  495 LEU   B N   1 
ATOM   5050 C  CA  . LEU   B 1 339 ? 30.367 36.658  29.313  1.00 36.77  ?  495 LEU   B CA  1 
ATOM   5051 C  C   . LEU   B 1 339 ? 31.090 35.873  30.393  1.00 36.35  ?  495 LEU   B C   1 
ATOM   5052 O  O   . LEU   B 1 339 ? 30.468 35.080  31.101  1.00 38.91  ?  495 LEU   B O   1 
ATOM   5053 C  CB  . LEU   B 1 339 ? 30.586 35.964  27.964  1.00 38.93  ?  495 LEU   B CB  1 
ATOM   5054 C  CG  . LEU   B 1 339 ? 29.805 36.510  26.766  1.00 36.35  ?  495 LEU   B CG  1 
ATOM   5055 C  CD1 . LEU   B 1 339 ? 30.192 35.779  25.488  1.00 25.13  ?  495 LEU   B CD1 1 
ATOM   5056 C  CD2 . LEU   B 1 339 ? 28.307 36.409  27.010  1.00 34.98  ?  495 LEU   B CD2 1 
ATOM   5057 N  N   . ILE   B 1 340 ? 32.398 36.067  30.520  1.00 34.89  ?  496 ILE   B N   1 
ATOM   5058 C  CA  . ILE   B 1 340 ? 33.212 35.389  31.520  1.00 33.66  ?  496 ILE   B CA  1 
ATOM   5059 C  C   . ILE   B 1 340 ? 34.106 36.435  32.161  1.00 40.35  ?  496 ILE   B C   1 
ATOM   5060 O  O   . ILE   B 1 340 ? 34.792 37.185  31.459  1.00 34.92  ?  496 ILE   B O   1 
ATOM   5061 C  CB  . ILE   B 1 340 ? 34.059 34.255  30.907  1.00 31.31  ?  496 ILE   B CB  1 
ATOM   5062 C  CG1 . ILE   B 1 340 ? 33.179 33.293  30.102  1.00 25.83  ?  496 ILE   B CG1 1 
ATOM   5063 C  CG2 . ILE   B 1 340 ? 34.815 33.512  31.995  1.00 36.91  ?  496 ILE   B CG2 1 
ATOM   5064 C  CD1 . ILE   B 1 340 ? 33.959 32.326  29.237  1.00 26.23  ?  496 ILE   B CD1 1 
ATOM   5065 N  N   . ASP   B 1 341 ? 34.088 36.506  33.485  1.00 38.27  ?  497 ASP   B N   1 
ATOM   5066 C  CA  . ASP   B 1 341 ? 34.881 37.519  34.154  1.00 32.25  ?  497 ASP   B CA  1 
ATOM   5067 C  C   . ASP   B 1 341 ? 36.337 37.062  34.257  1.00 39.90  ?  497 ASP   B C   1 
ATOM   5068 O  O   . ASP   B 1 341 ? 36.655 35.880  34.100  1.00 33.05  ?  497 ASP   B O   1 
ATOM   5069 C  CB  . ASP   B 1 341 ? 34.291 37.826  35.529  1.00 42.39  ?  497 ASP   B CB  1 
ATOM   5070 C  CG  . ASP   B 1 341 ? 34.806 36.904  36.598  1.00 49.87  ?  497 ASP   B CG  1 
ATOM   5071 O  OD1 . ASP   B 1 341 ? 34.236 35.807  36.788  1.00 64.41  ?  497 ASP   B OD1 1 
ATOM   5072 O  OD2 . ASP   B 1 341 ? 35.789 37.291  37.250  1.00 67.33  -1 497 ASP   B OD2 1 
ATOM   5073 N  N   . LYS   B 1 342 ? 37.229 38.024  34.519  1.00 38.41  ?  498 LYS   B N   1 
ATOM   5074 C  CA  . LYS   B 1 342 ? 38.665 37.749  34.457  1.00 44.82  ?  498 LYS   B CA  1 
ATOM   5075 C  C   . LYS   B 1 342 ? 39.123 36.790  35.552  1.00 34.62  ?  498 LYS   B C   1 
ATOM   5076 O  O   . LYS   B 1 342 ? 40.109 36.071  35.360  1.00 38.24  ?  498 LYS   B O   1 
ATOM   5077 C  CB  . LYS   B 1 342 ? 39.458 39.057  34.537  1.00 48.10  ?  498 LYS   B CB  1 
ATOM   5078 C  CG  . LYS   B 1 342 ? 40.961 38.906  34.299  1.00 56.63  ?  498 LYS   B CG  1 
ATOM   5079 C  CD  . LYS   B 1 342 ? 41.310 39.174  32.847  1.00 47.61  ?  498 LYS   B CD  1 
ATOM   5080 C  CE  . LYS   B 1 342 ? 42.729 39.689  32.670  1.00 55.02  ?  498 LYS   B CE  1 
ATOM   5081 N  NZ  . LYS   B 1 342 ? 43.736 38.754  33.238  1.00 61.60  ?  498 LYS   B NZ  1 
ATOM   5082 N  N   . ARG   B 1 343 ? 38.443 36.772  36.701  1.00 32.75  ?  499 ARG   B N   1 
ATOM   5083 C  CA  . ARG   B 1 343 ? 38.814 35.849  37.772  1.00 39.19  ?  499 ARG   B CA  1 
ATOM   5084 C  C   . ARG   B 1 343 ? 38.769 34.401  37.293  1.00 34.35  ?  499 ARG   B C   1 
ATOM   5085 O  O   . ARG   B 1 343 ? 39.687 33.617  37.570  1.00 34.11  ?  499 ARG   B O   1 
ATOM   5086 C  CB  . ARG   B 1 343 ? 37.886 36.054  38.969  1.00 44.22  ?  499 ARG   B CB  1 
ATOM   5087 C  CG  . ARG   B 1 343 ? 38.297 35.402  40.269  1.00 50.56  ?  499 ARG   B CG  1 
ATOM   5088 C  CD  . ARG   B 1 343 ? 37.192 35.600  41.301  1.00 51.14  ?  499 ARG   B CD  1 
ATOM   5089 N  NE  . ARG   B 1 343 ? 37.707 35.846  42.643  1.00 54.00  ?  499 ARG   B NE  1 
ATOM   5090 C  CZ  . ARG   B 1 343 ? 36.949 36.048  43.712  1.00 68.78  ?  499 ARG   B CZ  1 
ATOM   5091 N  NH1 . ARG   B 1 343 ? 35.628 36.048  43.633  1.00 62.17  ?  499 ARG   B NH1 1 
ATOM   5092 N  NH2 . ARG   B 1 343 ? 37.530 36.260  44.889  1.00 65.06  ?  499 ARG   B NH2 1 
ATOM   5093 N  N   . SER   B 1 344 ? 37.716 34.033  36.557  1.00 32.63  ?  500 SER   B N   1 
ATOM   5094 C  CA  . SER   B 1 344 ? 37.598 32.671  36.042  1.00 38.12  ?  500 SER   B CA  1 
ATOM   5095 C  C   . SER   B 1 344 ? 38.713 32.349  35.052  1.00 29.10  ?  500 SER   B C   1 
ATOM   5096 O  O   . SER   B 1 344 ? 39.302 31.260  35.098  1.00 30.22  ?  500 SER   B O   1 
ATOM   5097 C  CB  . SER   B 1 344 ? 36.230 32.481  35.386  1.00 29.25  ?  500 SER   B CB  1 
ATOM   5098 O  OG  . SER   B 1 344 ? 35.177 32.725  36.303  1.00 32.38  ?  500 SER   B OG  1 
ATOM   5099 N  N   . LYS   B 1 345 ? 39.007 33.281  34.141  1.00 25.32  ?  501 LYS   B N   1 
ATOM   5100 C  CA  . LYS   B 1 345 ? 40.065 33.057  33.160  1.00 28.97  ?  501 LYS   B CA  1 
ATOM   5101 C  C   . LYS   B 1 345 ? 41.423 32.915  33.835  1.00 28.70  ?  501 LYS   B C   1 
ATOM   5102 O  O   . LYS   B 1 345 ? 42.237 32.078  33.432  1.00 35.85  ?  501 LYS   B O   1 
ATOM   5103 C  CB  . LYS   B 1 345 ? 40.084 34.195  32.141  1.00 25.14  ?  501 LYS   B CB  1 
ATOM   5104 C  CG  . LYS   B 1 345 ? 38.815 34.299  31.314  1.00 40.17  ?  501 LYS   B CG  1 
ATOM   5105 C  CD  . LYS   B 1 345 ? 38.742 35.618  30.568  1.00 40.56  ?  501 LYS   B CD  1 
ATOM   5106 C  CE  . LYS   B 1 345 ? 37.313 35.929  30.158  1.00 39.14  ?  501 LYS   B CE  1 
ATOM   5107 N  NZ  . LYS   B 1 345 ? 37.145 37.343  29.722  1.00 29.00  ?  501 LYS   B NZ  1 
ATOM   5108 N  N   . GLU   B 1 346 ? 41.682 33.713  34.873  1.00 27.61  ?  502 GLU   B N   1 
ATOM   5109 C  CA  . GLU   B 1 346 ? 42.943 33.600  35.601  1.00 32.31  ?  502 GLU   B CA  1 
ATOM   5110 C  C   . GLU   B 1 346 ? 43.032 32.277  36.348  1.00 33.90  ?  502 GLU   B C   1 
ATOM   5111 O  O   . GLU   B 1 346 ? 44.102 31.657  36.396  1.00 32.95  ?  502 GLU   B O   1 
ATOM   5112 C  CB  . GLU   B 1 346 ? 43.099 34.768  36.575  1.00 30.85  ?  502 GLU   B CB  1 
ATOM   5113 C  CG  . GLU   B 1 346 ? 43.238 36.125  35.911  1.00 35.45  ?  502 GLU   B CG  1 
ATOM   5114 C  CD  . GLU   B 1 346 ? 43.109 37.271  36.897  1.00 51.66  ?  502 GLU   B CD  1 
ATOM   5115 O  OE1 . GLU   B 1 346 ? 42.705 37.025  38.054  1.00 50.31  ?  502 GLU   B OE1 1 
ATOM   5116 O  OE2 . GLU   B 1 346 ? 43.408 38.421  36.514  1.00 48.76  -1 502 GLU   B OE2 1 
ATOM   5117 N  N   . PHE   B 1 347 ? 41.926 31.832  36.946  1.00 29.07  ?  503 PHE   B N   1 
ATOM   5118 C  CA  . PHE   B 1 347 ? 41.928 30.536  37.618  1.00 30.14  ?  503 PHE   B CA  1 
ATOM   5119 C  C   . PHE   B 1 347 ? 42.239 29.416  36.631  1.00 30.07  ?  503 PHE   B C   1 
ATOM   5120 O  O   . PHE   B 1 347 ? 43.086 28.549  36.897  1.00 33.73  ?  503 PHE   B O   1 
ATOM   5121 C  CB  . PHE   B 1 347 ? 40.580 30.299  38.304  1.00 30.48  ?  503 PHE   B CB  1 
ATOM   5122 C  CG  . PHE   B 1 347 ? 40.527 29.038  39.120  1.00 33.28  ?  503 PHE   B CG  1 
ATOM   5123 C  CD1 . PHE   B 1 347 ? 41.047 29.000  40.404  1.00 36.96  ?  503 PHE   B CD1 1 
ATOM   5124 C  CD2 . PHE   B 1 347 ? 39.961 27.887  38.598  1.00 32.85  ?  503 PHE   B CD2 1 
ATOM   5125 C  CE1 . PHE   B 1 347 ? 40.998 27.836  41.153  1.00 42.68  ?  503 PHE   B CE1 1 
ATOM   5126 C  CE2 . PHE   B 1 347 ? 39.909 26.723  39.340  1.00 38.35  ?  503 PHE   B CE2 1 
ATOM   5127 C  CZ  . PHE   B 1 347 ? 40.429 26.697  40.618  1.00 35.09  ?  503 PHE   B CZ  1 
ATOM   5128 N  N   . LEU   B 1 348 ? 41.571 29.428  35.474  1.00 25.30  ?  504 LEU   B N   1 
ATOM   5129 C  CA  . LEU   B 1 348 ? 41.805 28.381  34.485  1.00 24.50  ?  504 LEU   B CA  1 
ATOM   5130 C  C   . LEU   B 1 348 ? 43.226 28.450  33.942  1.00 26.36  ?  504 LEU   B C   1 
ATOM   5131 O  O   . LEU   B 1 348 ? 43.852 27.414  33.687  1.00 28.07  ?  504 LEU   B O   1 
ATOM   5132 C  CB  . LEU   B 1 348 ? 40.787 28.486  33.351  1.00 23.80  ?  504 LEU   B CB  1 
ATOM   5133 C  CG  . LEU   B 1 348 ? 40.893 27.402  32.275  1.00 25.96  ?  504 LEU   B CG  1 
ATOM   5134 C  CD1 . LEU   B 1 348 ? 40.951 26.019  32.914  1.00 23.44  ?  504 LEU   B CD1 1 
ATOM   5135 C  CD2 . LEU   B 1 348 ? 39.731 27.497  31.302  1.00 26.34  ?  504 LEU   B CD2 1 
ATOM   5136 N  N   . THR   B 1 349 ? 43.759 29.662  33.772  1.00 24.05  ?  505 THR   B N   1 
ATOM   5137 C  CA  . THR   B 1 349 ? 45.133 29.814  33.312  1.00 33.51  ?  505 THR   B CA  1 
ATOM   5138 C  C   . THR   B 1 349 ? 46.111 29.216  34.313  1.00 25.31  ?  505 THR   B C   1 
ATOM   5139 O  O   . THR   B 1 349 ? 47.030 28.480  33.936  1.00 24.35  ?  505 THR   B O   1 
ATOM   5140 C  CB  . THR   B 1 349 ? 45.440 31.293  33.075  1.00 28.44  ?  505 THR   B CB  1 
ATOM   5141 O  OG1 . THR   B 1 349 ? 44.621 31.788  32.009  1.00 28.01  ?  505 THR   B OG1 1 
ATOM   5142 C  CG2 . THR   B 1 349 ? 46.905 31.485  32.717  1.00 34.12  ?  505 THR   B CG2 1 
ATOM   5143 N  N   . LYS   B 1 350 ? 45.929 29.526  35.599  1.00 27.13  ?  506 LYS   B N   1 
ATOM   5144 C  CA  . LYS   B 1 350 ? 46.805 28.968  36.623  1.00 28.60  ?  506 LYS   B CA  1 
ATOM   5145 C  C   . LYS   B 1 350 ? 46.745 27.446  36.625  1.00 26.33  ?  506 LYS   B C   1 
ATOM   5146 O  O   . LYS   B 1 350 ? 47.786 26.774  36.665  1.00 28.45  ?  506 LYS   B O   1 
ATOM   5147 C  CB  . LYS   B 1 350 ? 46.426 29.526  37.997  1.00 30.47  ?  506 LYS   B CB  1 
ATOM   5148 C  CG  . LYS   B 1 350 ? 47.248 28.963  39.146  1.00 46.65  ?  506 LYS   B CG  1 
ATOM   5149 C  CD  . LYS   B 1 350 ? 46.824 29.561  40.481  1.00 58.83  ?  506 LYS   B CD  1 
ATOM   5150 C  CE  . LYS   B 1 350 ? 46.546 28.478  41.511  1.00 71.91  ?  506 LYS   B CE  1 
ATOM   5151 N  NZ  . LYS   B 1 350 ? 45.093 28.181  41.628  1.00 80.64  ?  506 LYS   B NZ  1 
ATOM   5152 N  N   . GLN   B 1 351 ? 45.535 26.882  36.552  1.00 27.14  ?  507 GLN   B N   1 
ATOM   5153 C  CA  . GLN   B 1 351 ? 45.400 25.427  36.564  1.00 26.20  ?  507 GLN   B CA  1 
ATOM   5154 C  C   . GLN   B 1 351 ? 46.088 24.796  35.358  1.00 25.34  ?  507 GLN   B C   1 
ATOM   5155 O  O   . GLN   B 1 351 ? 46.859 23.836  35.498  1.00 25.66  ?  507 GLN   B O   1 
ATOM   5156 C  CB  . GLN   B 1 351 ? 43.923 25.036  36.613  1.00 29.62  ?  507 GLN   B CB  1 
ATOM   5157 C  CG  . GLN   B 1 351 ? 43.209 25.465  37.887  1.00 31.73  ?  507 GLN   B CG  1 
ATOM   5158 C  CD  . GLN   B 1 351 ? 43.990 25.112  39.141  1.00 34.45  ?  507 GLN   B CD  1 
ATOM   5159 O  OE1 . GLN   B 1 351 ? 44.159 25.943  40.033  1.00 42.63  ?  507 GLN   B OE1 1 
ATOM   5160 N  NE2 . GLN   B 1 351 ? 44.474 23.877  39.211  1.00 41.08  ?  507 GLN   B NE2 1 
ATOM   5161 N  N   . ILE   B 1 352 ? 45.826 25.331  34.160  1.00 24.33  ?  508 ILE   B N   1 
ATOM   5162 C  CA  . ILE   B 1 352 ? 46.392 24.760  32.940  1.00 23.51  ?  508 ILE   B CA  1 
ATOM   5163 C  C   . ILE   B 1 352 ? 47.912 24.880  32.942  1.00 23.74  ?  508 ILE   B C   1 
ATOM   5164 O  O   . ILE   B 1 352 ? 48.620 23.950  32.538  1.00 23.64  ?  508 ILE   B O   1 
ATOM   5165 C  CB  . ILE   B 1 352 ? 45.769 25.426  31.697  1.00 27.41  ?  508 ILE   B CB  1 
ATOM   5166 C  CG1 . ILE   B 1 352 ? 44.331 24.952  31.487  1.00 23.86  ?  508 ILE   B CG1 1 
ATOM   5167 C  CG2 . ILE   B 1 352 ? 46.584 25.124  30.456  1.00 21.76  ?  508 ILE   B CG2 1 
ATOM   5168 C  CD1 . ILE   B 1 352 ? 43.601 25.706  30.395  1.00 22.97  ?  508 ILE   B CD1 1 
ATOM   5169 N  N   . GLU   B 1 353 ? 48.440 26.025  33.387  1.00 24.13  ?  509 GLU   B N   1 
ATOM   5170 C  CA  . GLU   B 1 353 ? 49.889 26.201  33.412  1.00 27.82  ?  509 GLU   B CA  1 
ATOM   5171 C  C   . GLU   B 1 353 ? 50.547 25.250  34.403  1.00 26.60  ?  509 GLU   B C   1 
ATOM   5172 O  O   . GLU   B 1 353 ? 51.616 24.694  34.118  1.00 29.28  ?  509 GLU   B O   1 
ATOM   5173 C  CB  . GLU   B 1 353 ? 50.247 27.647  33.749  1.00 24.90  ?  509 GLU   B CB  1 
ATOM   5174 C  CG  . GLU   B 1 353 ? 50.122 28.588  32.570  1.00 26.86  ?  509 GLU   B CG  1 
ATOM   5175 C  CD  . GLU   B 1 353 ? 50.547 30.000  32.901  1.00 28.77  ?  509 GLU   B CD  1 
ATOM   5176 O  OE1 . GLU   B 1 353 ? 50.352 30.428  34.059  1.00 34.81  ?  509 GLU   B OE1 1 
ATOM   5177 O  OE2 . GLU   B 1 353 ? 51.078 30.681  32.001  1.00 32.49  -1 509 GLU   B OE2 1 
ATOM   5178 N  N   . TYR   B 1 354 ? 49.926 25.045  35.570  1.00 26.26  ?  510 TYR   B N   1 
ATOM   5179 C  CA  . TYR   B 1 354 ? 50.436 24.040  36.497  1.00 27.29  ?  510 TYR   B CA  1 
ATOM   5180 C  C   . TYR   B 1 354 ? 50.475 22.667  35.834  1.00 26.93  ?  510 TYR   B C   1 
ATOM   5181 O  O   . TYR   B 1 354 ? 51.501 21.971  35.863  1.00 31.84  ?  510 TYR   B O   1 
ATOM   5182 C  CB  . TYR   B 1 354 ? 49.575 24.001  37.761  1.00 31.08  ?  510 TYR   B CB  1 
ATOM   5183 C  CG  . TYR   B 1 354 ? 49.966 22.883  38.702  1.00 50.25  ?  510 TYR   B CG  1 
ATOM   5184 C  CD1 . TYR   B 1 354 ? 50.978 23.060  39.633  1.00 43.14  ?  510 TYR   B CD1 1 
ATOM   5185 C  CD2 . TYR   B 1 354 ? 49.336 21.644  38.645  1.00 36.98  ?  510 TYR   B CD2 1 
ATOM   5186 C  CE1 . TYR   B 1 354 ? 51.350 22.041  40.489  1.00 41.33  ?  510 TYR   B CE1 1 
ATOM   5187 C  CE2 . TYR   B 1 354 ? 49.702 20.616  39.495  1.00 49.98  ?  510 TYR   B CE2 1 
ATOM   5188 C  CZ  . TYR   B 1 354 ? 50.709 20.821  40.416  1.00 39.08  ?  510 TYR   B CZ  1 
ATOM   5189 O  OH  . TYR   B 1 354 ? 51.072 19.800  41.262  1.00 48.85  ?  510 TYR   B OH  1 
ATOM   5190 N  N   . GLU   B 1 355 ? 49.352 22.264  35.230  1.00 26.18  ?  511 GLU   B N   1 
ATOM   5191 C  CA  . GLU   B 1 355 ? 49.281 20.971  34.556  1.00 27.95  ?  511 GLU   B CA  1 
ATOM   5192 C  C   . GLU   B 1 355 ? 50.390 20.818  33.524  1.00 33.39  ?  511 GLU   B C   1 
ATOM   5193 O  O   . GLU   B 1 355 ? 51.094 19.803  33.494  1.00 28.43  ?  511 GLU   B O   1 
ATOM   5194 C  CB  . GLU   B 1 355 ? 47.913 20.796  33.895  1.00 27.76  ?  511 GLU   B CB  1 
ATOM   5195 C  CG  . GLU   B 1 355 ? 46.769 20.721  34.877  1.00 34.07  ?  511 GLU   B CG  1 
ATOM   5196 C  CD  . GLU   B 1 355 ? 46.887 19.512  35.775  1.00 38.74  ?  511 GLU   B CD  1 
ATOM   5197 O  OE1 . GLU   B 1 355 ? 47.227 18.425  35.262  1.00 35.42  ?  511 GLU   B OE1 1 
ATOM   5198 O  OE2 . GLU   B 1 355 ? 46.646 19.645  36.992  1.00 40.15  -1 511 GLU   B OE2 1 
ATOM   5199 N  N   . ARG   B 1 356 ? 50.561 21.829  32.671  1.00 24.51  ?  512 ARG   B N   1 
ATOM   5200 C  CA  . ARG   B 1 356 ? 51.568 21.756  31.620  1.00 24.42  ?  512 ARG   B CA  1 
ATOM   5201 C  C   . ARG   B 1 356 ? 52.978 21.708  32.192  1.00 24.99  ?  512 ARG   B C   1 
ATOM   5202 O  O   . ARG   B 1 356 ? 53.856 21.051  31.620  1.00 33.38  ?  512 ARG   B O   1 
ATOM   5203 C  CB  . ARG   B 1 356 ? 51.407 22.943  30.670  1.00 23.11  ?  512 ARG   B CB  1 
ATOM   5204 C  CG  . ARG   B 1 356 ? 52.080 22.766  29.321  1.00 22.40  ?  512 ARG   B CG  1 
ATOM   5205 C  CD  . ARG   B 1 356 ? 53.294 23.661  29.201  1.00 23.60  ?  512 ARG   B CD  1 
ATOM   5206 N  NE  . ARG   B 1 356 ? 52.928 25.069  29.290  1.00 23.95  ?  512 ARG   B NE  1 
ATOM   5207 C  CZ  . ARG   B 1 356 ? 52.553 25.812  28.258  1.00 30.42  ?  512 ARG   B CZ  1 
ATOM   5208 N  NH1 . ARG   B 1 356 ? 52.481 25.310  27.036  1.00 27.87  ?  512 ARG   B NH1 1 
ATOM   5209 N  NH2 . ARG   B 1 356 ? 52.244 27.090  28.458  1.00 22.20  ?  512 ARG   B NH2 1 
ATOM   5210 N  N   . ASN   B 1 357 ? 53.217 22.379  33.321  1.00 30.84  ?  513 ASN   B N   1 
ATOM   5211 C  CA  . ASN   B 1 357 ? 54.542 22.342  33.924  1.00 28.13  ?  513 ASN   B CA  1 
ATOM   5212 C  C   . ASN   B 1 357 ? 54.820 21.029  34.642  1.00 34.28  ?  513 ASN   B C   1 
ATOM   5213 O  O   . ASN   B 1 357 ? 55.988 20.725  34.911  1.00 30.66  ?  513 ASN   B O   1 
ATOM   5214 C  CB  . ASN   B 1 357 ? 54.716 23.512  34.894  1.00 27.70  ?  513 ASN   B CB  1 
ATOM   5215 C  CG  . ASN   B 1 357 ? 54.976 24.824  34.182  1.00 33.75  ?  513 ASN   B CG  1 
ATOM   5216 O  OD1 . ASN   B 1 357 ? 55.706 24.874  33.194  1.00 29.95  ?  513 ASN   B OD1 1 
ATOM   5217 N  ND2 . ASN   B 1 357 ? 54.378 25.898  34.685  1.00 27.22  ?  513 ASN   B ND2 1 
ATOM   5218 N  N   . ASN   B 1 358 ? 53.790 20.243  34.963  1.00 35.85  ?  514 ASN   B N   1 
ATOM   5219 C  CA  . ASN   B 1 358 ? 53.995 18.995  35.693  1.00 41.13  ?  514 ASN   B CA  1 
ATOM   5220 C  C   . ASN   B 1 358 ? 53.539 17.767  34.905  1.00 43.16  ?  514 ASN   B C   1 
ATOM   5221 O  O   . ASN   B 1 358 ? 53.177 16.745  35.493  1.00 46.80  ?  514 ASN   B O   1 
ATOM   5222 C  CB  . ASN   B 1 358 ? 53.297 19.052  37.049  1.00 29.93  ?  514 ASN   B CB  1 
ATOM   5223 C  CG  . ASN   B 1 358 ? 53.905 20.092  37.967  1.00 36.27  ?  514 ASN   B CG  1 
ATOM   5224 O  OD1 . ASN   B 1 358 ? 54.857 19.812  38.694  1.00 35.85  ?  514 ASN   B OD1 1 
ATOM   5225 N  ND2 . ASN   B 1 358 ? 53.362 21.304  37.933  1.00 43.72  ?  514 ASN   B ND2 1 
ATOM   5226 N  N   . GLU   B 1 359 ? 53.567 17.850  33.572  1.00 35.03  ?  515 GLU   B N   1 
ATOM   5227 C  CA  . GLU   B 1 359 ? 53.243 16.725  32.686  1.00 43.62  ?  515 GLU   B CA  1 
ATOM   5228 C  C   . GLU   B 1 359 ? 51.819 16.211  32.903  1.00 34.52  ?  515 GLU   B C   1 
ATOM   5229 O  O   . GLU   B 1 359 ? 51.567 15.005  32.888  1.00 41.88  ?  515 GLU   B O   1 
ATOM   5230 C  CB  . GLU   B 1 359 ? 54.259 15.588  32.833  1.00 50.20  ?  515 GLU   B CB  1 
ATOM   5231 C  CG  . GLU   B 1 359 ? 55.711 16.034  32.744  1.00 58.23  ?  515 GLU   B CG  1 
ATOM   5232 C  CD  . GLU   B 1 359 ? 56.682 14.870  32.765  1.00 73.30  ?  515 GLU   B CD  1 
ATOM   5233 O  OE1 . GLU   B 1 359 ? 56.756 14.169  33.795  1.00 80.97  ?  515 GLU   B OE1 1 
ATOM   5234 O  OE2 . GLU   B 1 359 ? 57.371 14.653  31.744  1.00 80.84  -1 515 GLU   B OE2 1 
ATOM   5235 N  N   . PHE   B 1 360 ? 50.888 17.138  33.108  1.00 35.02  ?  516 PHE   B N   1 
ATOM   5236 C  CA  . PHE   B 1 360 ? 49.455 16.857  33.116  1.00 35.10  ?  516 PHE   B CA  1 
ATOM   5237 C  C   . PHE   B 1 360 ? 49.047 15.711  34.053  1.00 41.65  ?  516 PHE   B C   1 
ATOM   5238 O  O   . PHE   B 1 360 ? 48.543 14.682  33.592  1.00 45.62  ?  516 PHE   B O   1 
ATOM   5239 C  CB  . PHE   B 1 360 ? 48.975 16.588  31.702  1.00 29.37  ?  516 PHE   B CB  1 
ATOM   5240 C  CG  . PHE   B 1 360 ? 49.292 17.696  30.735  1.00 29.77  ?  516 PHE   B CG  1 
ATOM   5241 C  CD1 . PHE   B 1 360 ? 48.461 18.799  30.629  1.00 28.45  ?  516 PHE   B CD1 1 
ATOM   5242 C  CD2 . PHE   B 1 360 ? 50.430 17.641  29.947  1.00 28.04  ?  516 PHE   B CD2 1 
ATOM   5243 C  CE1 . PHE   B 1 360 ? 48.757 19.826  29.749  1.00 30.33  ?  516 PHE   B CE1 1 
ATOM   5244 C  CE2 . PHE   B 1 360 ? 50.731 18.664  29.064  1.00 29.04  ?  516 PHE   B CE2 1 
ATOM   5245 C  CZ  . PHE   B 1 360 ? 49.893 19.758  28.966  1.00 28.67  ?  516 PHE   B CZ  1 
ATOM   5246 N  N   . PRO   B 1 361 ? 49.228 15.865  35.369  1.00 33.20  ?  517 PRO   B N   1 
ATOM   5247 C  CA  . PRO   B 1 361 ? 48.752 14.820  36.290  1.00 41.48  ?  517 PRO   B CA  1 
ATOM   5248 C  C   . PRO   B 1 361 ? 47.237 14.712  36.358  1.00 36.96  ?  517 PRO   B C   1 
ATOM   5249 O  O   . PRO   B 1 361 ? 46.731 13.670  36.795  1.00 47.42  ?  517 PRO   B O   1 
ATOM   5250 C  CB  . PRO   B 1 361 ? 49.339 15.241  37.644  1.00 35.56  ?  517 PRO   B CB  1 
ATOM   5251 C  CG  . PRO   B 1 361 ? 49.574 16.700  37.519  1.00 34.01  ?  517 PRO   B CG  1 
ATOM   5252 C  CD  . PRO   B 1 361 ? 49.939 16.942  36.083  1.00 34.03  ?  517 PRO   B CD  1 
ATOM   5253 N  N   . VAL   B 1 362 ? 46.497 15.744  35.941  1.00 42.55  ?  518 VAL   B N   1 
ATOM   5254 C  CA  . VAL   B 1 362 ? 45.039 15.677  35.955  1.00 41.61  ?  518 VAL   B CA  1 
ATOM   5255 C  C   . VAL   B 1 362 ? 44.519 14.628  34.982  1.00 39.03  ?  518 VAL   B C   1 
ATOM   5256 O  O   . VAL   B 1 362 ? 43.375 14.181  35.108  1.00 48.72  ?  518 VAL   B O   1 
ATOM   5257 C  CB  . VAL   B 1 362 ? 44.429 17.061  35.643  1.00 40.26  ?  518 VAL   B CB  1 
ATOM   5258 C  CG1 . VAL   B 1 362 ? 44.424 17.322  34.140  1.00 34.25  ?  518 VAL   B CG1 1 
ATOM   5259 C  CG2 . VAL   B 1 362 ? 43.026 17.177  36.219  1.00 49.26  ?  518 VAL   B CG2 1 
ATOM   5260 N  N   . PHE   B 1 363 ? 45.339 14.219  34.010  1.00 36.85  ?  519 PHE   B N   1 
ATOM   5261 C  CA  . PHE   B 1 363 ? 44.911 13.197  33.062  1.00 37.82  ?  519 PHE   B CA  1 
ATOM   5262 C  C   . PHE   B 1 363 ? 44.706 11.851  33.744  1.00 56.93  ?  519 PHE   B C   1 
ATOM   5263 O  O   . PHE   B 1 363 ? 43.864 11.059  33.306  1.00 57.57  ?  519 PHE   B O   1 
ATOM   5264 C  CB  . PHE   B 1 363 ? 45.931 13.061  31.933  1.00 36.48  ?  519 PHE   B CB  1 
ATOM   5265 C  CG  . PHE   B 1 363 ? 45.785 14.088  30.850  1.00 46.92  ?  519 PHE   B CG  1 
ATOM   5266 C  CD1 . PHE   B 1 363 ? 44.605 14.798  30.700  1.00 36.19  ?  519 PHE   B CD1 1 
ATOM   5267 C  CD2 . PHE   B 1 363 ? 46.827 14.340  29.974  1.00 34.27  ?  519 PHE   B CD2 1 
ATOM   5268 C  CE1 . PHE   B 1 363 ? 44.469 15.743  29.700  1.00 32.96  ?  519 PHE   B CE1 1 
ATOM   5269 C  CE2 . PHE   B 1 363 ? 46.700 15.283  28.973  1.00 29.86  ?  519 PHE   B CE2 1 
ATOM   5270 C  CZ  . PHE   B 1 363 ? 45.518 15.986  28.834  1.00 30.68  ?  519 PHE   B CZ  1 
ATOM   5271 N  N   . ASP   B 1 364 ? 45.462 11.576  34.803  1.00 57.95  ?  520 ASP   B N   1 
ATOM   5272 C  CA  . ASP   B 1 364 ? 45.363 10.311  35.522  1.00 56.66  ?  520 ASP   B CA  1 
ATOM   5273 C  C   . ASP   B 1 364 ? 43.952 10.068  36.045  1.00 56.51  ?  520 ASP   B C   1 
ATOM   5274 O  O   . ASP   B 1 364 ? 43.768 9.633   37.180  1.00 84.64  ?  520 ASP   B O   1 
ATOM   5275 C  CB  . ASP   B 1 364 ? 46.358 10.282  36.683  1.00 51.19  ?  520 ASP   B CB  1 
ATOM   5276 C  CG  . ASP   B 1 364 ? 47.792 10.443  36.226  1.00 65.51  ?  520 ASP   B CG  1 
ATOM   5277 O  OD1 . ASP   B 1 364 ? 48.048 10.314  35.010  1.00 68.31  ?  520 ASP   B OD1 1 
ATOM   5278 O  OD2 . ASP   B 1 364 ? 48.662 10.701  37.083  1.00 59.92  -1 520 ASP   B OD2 1 
HETATM 5279 C  C4  . A1EAH C 2 .   ? 28.956 5.723   -20.929 1.00 38.99  ?  601 A1EAH A C4  1 
HETATM 5280 C  C14 . A1EAH C 2 .   ? 31.531 13.011  -26.204 1.00 42.34  ?  601 A1EAH A C14 1 
HETATM 5281 C  C5  . A1EAH C 2 .   ? 29.229 6.247   -22.182 1.00 42.11  ?  601 A1EAH A C5  1 
HETATM 5282 C  C6  . A1EAH C 2 .   ? 29.690 5.441   -23.233 1.00 35.64  ?  601 A1EAH A C6  1 
HETATM 5283 C  C11 . A1EAH C 2 .   ? 29.195 11.801  -26.702 1.00 53.90  ?  601 A1EAH A C11 1 
HETATM 5284 C  C7  . A1EAH C 2 .   ? 29.547 7.497   -23.982 1.00 39.44  ?  601 A1EAH A C7  1 
HETATM 5285 C  C8  . A1EAH C 2 .   ? 29.891 9.419   -26.884 1.00 46.06  ?  601 A1EAH A C8  1 
HETATM 5286 C  C9  . A1EAH C 2 .   ? 29.400 10.449  -26.053 1.00 45.43  ?  601 A1EAH A C9  1 
HETATM 5287 C  C10 . A1EAH C 2 .   ? 29.185 9.876   -24.798 1.00 52.28  ?  601 A1EAH A C10 1 
HETATM 5288 C  C12 . A1EAH C 2 .   ? 30.449 12.587  -27.013 1.00 50.98  ?  601 A1EAH A C12 1 
HETATM 5289 C  C13 . A1EAH C 2 .   ? 27.960 12.572  -26.251 1.00 57.92  ?  601 A1EAH A C13 1 
HETATM 5290 N  N1  . A1EAH C 2 .   ? 29.135 7.539   -22.675 1.00 36.97  ?  601 A1EAH A N1  1 
HETATM 5291 N  N2  . A1EAH C 2 .   ? 29.886 6.210   -24.375 1.00 45.96  ?  601 A1EAH A N2  1 
HETATM 5292 C  C3  . A1EAH C 2 .   ? 29.147 4.369   -20.760 1.00 41.14  ?  601 A1EAH A C3  1 
HETATM 5293 N  N3  . A1EAH C 2 .   ? 29.572 8.559   -24.902 1.00 42.98  ?  601 A1EAH A N3  1 
HETATM 5294 C  C1  . A1EAH C 2 .   ? 29.886 4.076   -23.040 1.00 34.89  ?  601 A1EAH A C1  1 
HETATM 5295 C  C15 . A1EAH C 2 .   ? 30.755 12.973  -28.297 1.00 42.25  ?  601 A1EAH A C15 1 
HETATM 5296 C  C16 . A1EAH C 2 .   ? 32.666 14.203  -29.316 1.00 35.74  ?  601 A1EAH A C16 1 
HETATM 5297 C  C17 . A1EAH C 2 .   ? 33.151 15.062  -31.318 1.00 33.66  ?  601 A1EAH A C17 1 
HETATM 5298 C  C18 . A1EAH C 2 .   ? 34.317 15.028  -30.543 1.00 29.68  ?  601 A1EAH A C18 1 
HETATM 5299 C  C19 . A1EAH C 2 .   ? 33.142 15.552  -32.612 1.00 32.45  ?  601 A1EAH A C19 1 
HETATM 5300 C  C2  . A1EAH C 2 .   ? 29.605 3.558   -21.798 1.00 30.39  ?  601 A1EAH A C2  1 
HETATM 5301 C  C20 . A1EAH C 2 .   ? 34.340 16.013  -33.111 1.00 37.38  ?  601 A1EAH A C20 1 
HETATM 5302 C  C21 . A1EAH C 2 .   ? 35.510 15.984  -32.350 1.00 36.89  ?  601 A1EAH A C21 1 
HETATM 5303 C  C22 . A1EAH C 2 .   ? 35.518 15.495  -31.065 1.00 34.93  ?  601 A1EAH A C22 1 
HETATM 5304 C  C23 . A1EAH C 2 .   ? 25.713 12.473  -25.793 1.00 68.36  ?  601 A1EAH A C23 1 
HETATM 5305 C  C24 . A1EAH C 2 .   ? 25.650 13.813  -25.503 1.00 61.99  ?  601 A1EAH A C24 1 
HETATM 5306 C  C25 . A1EAH C 2 .   ? 26.801 14.554  -25.603 1.00 63.31  ?  601 A1EAH A C25 1 
HETATM 5307 C  C26 . A1EAH C 2 .   ? 27.972 13.928  -25.989 1.00 64.93  ?  601 A1EAH A C26 1 
HETATM 5308 C  C27 . A1EAH C 2 .   ? 30.277 9.476   -28.322 1.00 49.79  ?  601 A1EAH A C27 1 
HETATM 5309 C  C28 . A1EAH C 2 .   ? 31.737 12.854  -24.736 1.00 38.82  ?  601 A1EAH A C28 1 
HETATM 5310 N  N4  . A1EAH C 2 .   ? 29.988 8.298   -26.192 1.00 43.67  ?  601 A1EAH A N4  1 
HETATM 5311 N  N5  . A1EAH C 2 .   ? 32.427 13.637  -26.957 1.00 38.31  ?  601 A1EAH A N5  1 
HETATM 5312 N  N6  . A1EAH C 2 .   ? 31.951 13.628  -28.255 1.00 47.99  ?  601 A1EAH A N6  1 
HETATM 5313 N  N7  . A1EAH C 2 .   ? 32.144 14.536  -30.535 1.00 34.30  ?  601 A1EAH A N7  1 
HETATM 5314 N  N8  . A1EAH C 2 .   ? 34.026 14.487  -29.295 1.00 28.79  ?  601 A1EAH A N8  1 
HETATM 5315 N  N9  . A1EAH C 2 .   ? 26.841 11.849  -26.166 1.00 61.88  ?  601 A1EAH A N9  1 
HETATM 5316 O  O1  . A1EAH C 2 .   ? 28.727 10.400  -23.673 1.00 42.19  ?  601 A1EAH A O1  1 
HETATM 5317 O  O2  . A1EAH C 2 .   ? 30.071 12.799  -29.414 1.00 43.36  ?  601 A1EAH A O2  1 
HETATM 5318 ZN ZN  . ZN    D 3 .   ? 45.549 21.576  -10.237 1.00 25.00  ?  602 ZN    A ZN  1 
HETATM 5319 C  C4  . A1EAH E 2 .   ? 32.980 20.200  29.057  1.00 26.42  ?  601 A1EAH B C4  1 
HETATM 5320 C  C14 . A1EAH E 2 .   ? 27.767 26.201  24.601  1.00 37.20  ?  601 A1EAH B C14 1 
HETATM 5321 C  C5  . A1EAH E 2 .   ? 31.795 20.665  28.511  1.00 33.22  ?  601 A1EAH B C5  1 
HETATM 5322 C  C6  . A1EAH E 2 .   ? 30.590 20.677  29.230  1.00 32.63  ?  601 A1EAH B C6  1 
HETATM 5323 C  C11 . A1EAH E 2 .   ? 27.427 23.739  23.618  1.00 44.74  ?  601 A1EAH B C11 1 
HETATM 5324 C  C7  . A1EAH E 2 .   ? 30.194 21.494  27.245  1.00 28.85  ?  601 A1EAH B C7  1 
HETATM 5325 C  C8  . A1EAH E 2 .   ? 29.608 22.513  23.944  1.00 31.01  ?  601 A1EAH B C8  1 
HETATM 5326 C  C9  . A1EAH E 2 .   ? 28.414 23.017  24.508  1.00 41.72  ?  601 A1EAH B C9  1 
HETATM 5327 C  C10 . A1EAH E 2 .   ? 28.461 22.699  25.861  1.00 42.18  ?  601 A1EAH B C10 1 
HETATM 5328 C  C12 . A1EAH E 2 .   ? 27.572 25.244  23.572  1.00 38.19  ?  601 A1EAH B C12 1 
HETATM 5329 C  C13 . A1EAH E 2 .   ? 25.983 23.255  23.691  1.00 37.57  ?  601 A1EAH B C13 1 
HETATM 5330 N  N1  . A1EAH E 2 .   ? 31.518 21.176  27.259  1.00 32.38  ?  601 A1EAH B N1  1 
HETATM 5331 N  N2  . A1EAH E 2 .   ? 29.560 21.195  28.443  1.00 34.66  ?  601 A1EAH B N2  1 
HETATM 5332 C  C3  . A1EAH E 2 .   ? 32.930 19.743  30.355  1.00 32.09  ?  601 A1EAH B C3  1 
HETATM 5333 N  N3  . A1EAH E 2 .   ? 29.639 22.027  26.070  1.00 43.22  ?  601 A1EAH B N3  1 
HETATM 5334 C  C1  . A1EAH E 2 .   ? 30.564 20.210  30.541  1.00 37.55  ?  601 A1EAH B C1  1 
HETATM 5335 C  C15 . A1EAH E 2 .   ? 27.558 25.950  22.394  1.00 40.41  ?  601 A1EAH B C15 1 
HETATM 5336 C  C16 . A1EAH E 2 .   ? 27.767 28.365  21.834  1.00 36.36  ?  601 A1EAH B C16 1 
HETATM 5337 C  C17 . A1EAH E 2 .   ? 27.953 30.454  21.079  1.00 32.85  ?  601 A1EAH B C17 1 
HETATM 5338 C  C18 . A1EAH E 2 .   ? 27.655 29.608  20.004  1.00 35.65  ?  601 A1EAH B C18 1 
HETATM 5339 C  C19 . A1EAH E 2 .   ? 28.130 31.816  20.916  1.00 38.64  ?  601 A1EAH B C19 1 
HETATM 5340 C  C2  . A1EAH E 2 .   ? 31.741 19.748  31.083  1.00 33.91  ?  601 A1EAH B C2  1 
HETATM 5341 C  C20 . A1EAH E 2 .   ? 27.999 32.312  19.639  1.00 40.61  ?  601 A1EAH B C20 1 
HETATM 5342 C  C21 . A1EAH E 2 .   ? 27.701 31.480  18.558  1.00 34.59  ?  601 A1EAH B C21 1 
HETATM 5343 C  C22 . A1EAH E 2 .   ? 27.527 30.126  18.720  1.00 24.93  ?  601 A1EAH B C22 1 
HETATM 5344 C  C23 . A1EAH E 2 .   ? 23.783 23.796  24.028  1.00 59.29  ?  601 A1EAH B C23 1 
HETATM 5345 C  C24 . A1EAH E 2 .   ? 23.364 22.511  23.784  1.00 69.43  ?  601 A1EAH B C24 1 
HETATM 5346 C  C25 . A1EAH E 2 .   ? 24.310 21.569  23.471  1.00 64.85  ?  601 A1EAH B C25 1 
HETATM 5347 C  C26 . A1EAH E 2 .   ? 25.637 21.947  23.415  1.00 48.86  ?  601 A1EAH B C26 1 
HETATM 5348 C  C27 . A1EAH E 2 .   ? 30.075 22.568  22.531  1.00 30.14  ?  601 A1EAH B C27 1 
HETATM 5349 C  C28 . A1EAH E 2 .   ? 27.863 26.012  26.075  1.00 45.80  ?  601 A1EAH B C28 1 
HETATM 5350 N  N4  . A1EAH E 2 .   ? 30.336 21.931  24.884  1.00 35.83  ?  601 A1EAH B N4  1 
HETATM 5351 N  N5  . A1EAH E 2 .   ? 27.851 27.413  24.068  1.00 48.95  ?  601 A1EAH B N5  1 
HETATM 5352 N  N6  . A1EAH E 2 .   ? 27.728 27.267  22.703  1.00 36.37  ?  601 A1EAH B N6  1 
HETATM 5353 N  N7  . A1EAH E 2 .   ? 28.012 29.656  22.204  1.00 48.59  ?  601 A1EAH B N7  1 
HETATM 5354 N  N8  . A1EAH E 2 .   ? 27.533 28.302  20.465  1.00 29.39  ?  601 A1EAH B N8  1 
HETATM 5355 N  N9  . A1EAH E 2 .   ? 25.067 24.183  23.977  1.00 60.88  ?  601 A1EAH B N9  1 
HETATM 5356 O  O1  . A1EAH E 2 .   ? 27.601 22.944  26.834  1.00 40.05  ?  601 A1EAH B O1  1 
HETATM 5357 O  O2  . A1EAH E 2 .   ? 27.412 25.521  21.153  1.00 39.86  ?  601 A1EAH B O2  1 
HETATM 5358 ZN ZN  . ZN    F 3 .   ? 44.834 13.881  9.356   1.00 24.29  ?  602 ZN    B ZN  1 
HETATM 5359 O  O   . HOH   G 4 .   ? 25.148 13.193  -16.661 1.00 38.54  ?  701 HOH   A O   1 
HETATM 5360 O  O   . HOH   G 4 .   ? 34.134 16.759  -24.473 1.00 52.11  ?  702 HOH   A O   1 
HETATM 5361 O  O   . HOH   G 4 .   ? 26.034 7.432   -21.267 1.00 40.09  ?  703 HOH   A O   1 
HETATM 5362 O  O   . HOH   G 4 .   ? 41.854 22.577  -5.888  1.00 28.11  ?  704 HOH   A O   1 
HETATM 5363 O  O   . HOH   G 4 .   ? 55.493 17.067  -12.854 1.00 26.24  ?  705 HOH   A O   1 
HETATM 5364 O  O   . HOH   G 4 .   ? 55.109 2.389   -31.885 1.00 25.54  ?  706 HOH   A O   1 
HETATM 5365 O  O   . HOH   G 4 .   ? 33.859 3.162   -28.111 1.00 29.60  ?  707 HOH   A O   1 
HETATM 5366 O  O   . HOH   G 4 .   ? 46.222 12.679  -10.438 1.00 20.09  ?  708 HOH   A O   1 
HETATM 5367 O  O   . HOH   G 4 .   ? 32.020 -3.523  -14.781 1.00 28.50  ?  709 HOH   A O   1 
HETATM 5368 O  O   . HOH   G 4 .   ? 34.723 6.242   -18.850 1.00 29.38  ?  710 HOH   A O   1 
HETATM 5369 O  O   . HOH   G 4 .   ? 61.192 11.451  -33.273 1.00 40.95  ?  711 HOH   A O   1 
HETATM 5370 O  O   . HOH   G 4 .   ? 43.263 5.363   -6.838  1.00 35.75  ?  712 HOH   A O   1 
HETATM 5371 O  O   . HOH   G 4 .   ? 36.766 17.747  -35.099 1.00 37.37  ?  713 HOH   A O   1 
HETATM 5372 O  O   . HOH   G 4 .   ? 41.760 25.440  -8.035  1.00 33.63  ?  714 HOH   A O   1 
HETATM 5373 O  O   . HOH   G 4 .   ? 38.539 3.900   -12.596 1.00 28.99  ?  715 HOH   A O   1 
HETATM 5374 O  O   . HOH   G 4 .   ? 41.841 19.955  -5.538  1.00 19.98  ?  716 HOH   A O   1 
HETATM 5375 O  O   . HOH   G 4 .   ? 57.523 18.126  -9.295  1.00 35.45  ?  717 HOH   A O   1 
HETATM 5376 O  O   . HOH   G 4 .   ? 42.261 1.253   -19.777 1.00 32.14  ?  718 HOH   A O   1 
HETATM 5377 O  O   . HOH   G 4 .   ? 51.440 7.382   -16.633 1.00 32.49  ?  719 HOH   A O   1 
HETATM 5378 O  O   . HOH   G 4 .   ? 32.496 7.384   -27.377 1.00 39.92  ?  720 HOH   A O   1 
HETATM 5379 O  O   . HOH   G 4 .   ? 46.173 23.042  -16.369 1.00 27.60  ?  721 HOH   A O   1 
HETATM 5380 O  O   . HOH   G 4 .   ? 37.679 19.782  3.267   1.00 23.06  ?  722 HOH   A O   1 
HETATM 5381 O  O   . HOH   G 4 .   ? 50.274 15.514  -3.960  1.00 34.22  ?  723 HOH   A O   1 
HETATM 5382 O  O   . HOH   G 4 .   ? 28.508 -9.151  -16.446 1.00 45.62  ?  724 HOH   A O   1 
HETATM 5383 O  O   . HOH   G 4 .   ? 47.464 8.402   -1.486  1.00 39.35  ?  725 HOH   A O   1 
HETATM 5384 O  O   . HOH   G 4 .   ? 36.444 15.773  -6.894  1.00 26.18  ?  726 HOH   A O   1 
HETATM 5385 O  O   . HOH   G 4 .   ? 54.637 17.243  -25.385 1.00 28.18  ?  727 HOH   A O   1 
HETATM 5386 O  O   . HOH   G 4 .   ? 53.173 6.626   -10.223 1.00 38.58  ?  728 HOH   A O   1 
HETATM 5387 O  O   . HOH   G 4 .   ? 38.072 15.477  -28.646 1.00 35.40  ?  729 HOH   A O   1 
HETATM 5388 O  O   . HOH   G 4 .   ? 55.027 15.039  -26.891 1.00 35.52  ?  730 HOH   A O   1 
HETATM 5389 O  O   . HOH   G 4 .   ? 41.066 21.647  -8.572  1.00 28.12  ?  731 HOH   A O   1 
HETATM 5390 O  O   . HOH   G 4 .   ? 51.896 7.471   -4.720  1.00 32.32  ?  732 HOH   A O   1 
HETATM 5391 O  O   . HOH   G 4 .   ? 45.111 21.981  -13.823 1.00 29.35  ?  733 HOH   A O   1 
HETATM 5392 O  O   . HOH   G 4 .   ? 38.424 20.313  -21.131 1.00 42.19  ?  734 HOH   A O   1 
HETATM 5393 O  O   . HOH   H 4 .   ? 42.966 6.782   0.170   1.00 31.77  ?  701 HOH   B O   1 
HETATM 5394 O  O   . HOH   H 4 .   ? 50.439 30.285  36.494  1.00 38.02  ?  702 HOH   B O   1 
HETATM 5395 O  O   . HOH   H 4 .   ? 12.619 20.075  7.953   1.00 44.92  ?  703 HOH   B O   1 
HETATM 5396 O  O   . HOH   H 4 .   ? 33.386 29.126  16.996  1.00 22.06  ?  704 HOH   B O   1 
HETATM 5397 O  O   . HOH   H 4 .   ? 33.562 30.106  34.720  1.00 38.50  ?  705 HOH   B O   1 
HETATM 5398 O  O   . HOH   H 4 .   ? 12.123 35.007  17.190  1.00 47.19  ?  706 HOH   B O   1 
HETATM 5399 O  O   . HOH   H 4 .   ? 49.028 33.409  18.361  1.00 36.32  ?  707 HOH   B O   1 
HETATM 5400 O  O   . HOH   H 4 .   ? 42.696 36.399  31.870  1.00 31.52  ?  708 HOH   B O   1 
HETATM 5401 O  O   . HOH   H 4 .   ? 54.603 18.444  12.680  1.00 29.95  ?  709 HOH   B O   1 
HETATM 5402 O  O   . HOH   H 4 .   ? 33.893 25.123  38.408  1.00 47.47  ?  710 HOH   B O   1 
HETATM 5403 O  O   . HOH   H 4 .   ? 42.986 29.689  5.894   1.00 34.30  ?  711 HOH   B O   1 
HETATM 5404 O  O   . HOH   H 4 .   ? 24.386 28.078  18.910  1.00 31.64  ?  712 HOH   B O   1 
HETATM 5405 O  O   . HOH   H 4 .   ? 31.857 38.576  9.431   1.00 35.29  ?  713 HOH   B O   1 
HETATM 5406 O  O   . HOH   H 4 .   ? 28.866 29.834  -1.167  1.00 33.58  ?  714 HOH   B O   1 
HETATM 5407 O  O   . HOH   H 4 .   ? 49.312 14.938  4.278   1.00 30.08  ?  715 HOH   B O   1 
HETATM 5408 O  O   . HOH   H 4 .   ? 36.757 33.869  13.415  1.00 32.26  ?  716 HOH   B O   1 
HETATM 5409 O  O   . HOH   H 4 .   ? 30.938 39.105  13.003  1.00 29.59  ?  717 HOH   B O   1 
HETATM 5410 O  O   . HOH   H 4 .   ? 26.066 31.784  2.580   1.00 33.26  ?  718 HOH   B O   1 
HETATM 5411 O  O   . HOH   H 4 .   ? 23.998 39.277  10.278  1.00 43.77  ?  719 HOH   B O   1 
HETATM 5412 O  O   . HOH   H 4 .   ? 38.140 15.644  -4.775  1.00 31.01  ?  720 HOH   B O   1 
HETATM 5413 O  O   . HOH   H 4 .   ? 33.583 17.622  33.357  1.00 29.14  ?  721 HOH   B O   1 
HETATM 5414 O  O   . HOH   H 4 .   ? 52.249 28.678  9.859   1.00 37.00  ?  722 HOH   B O   1 
HETATM 5415 O  O   . HOH   H 4 .   ? 35.947 19.623  5.362   1.00 24.21  ?  723 HOH   B O   1 
HETATM 5416 O  O   . HOH   H 4 .   ? 41.345 15.463  4.424   1.00 22.73  ?  724 HOH   B O   1 
HETATM 5417 O  O   . HOH   H 4 .   ? 45.299 22.675  9.788   1.00 15.55  ?  725 HOH   B O   1 
HETATM 5418 O  O   . HOH   H 4 .   ? 40.478 34.301  18.576  1.00 34.81  ?  726 HOH   B O   1 
HETATM 5419 O  O   . HOH   H 4 .   ? 44.738 12.425  15.349  1.00 25.86  ?  727 HOH   B O   1 
HETATM 5420 O  O   . HOH   H 4 .   ? 37.635 31.834  10.970  1.00 28.85  ?  728 HOH   B O   1 
HETATM 5421 O  O   . HOH   H 4 .   ? 44.184 13.508  12.848  1.00 26.08  ?  729 HOH   B O   1 
HETATM 5422 O  O   . HOH   H 4 .   ? 46.003 6.731   0.130   1.00 32.03  ?  730 HOH   B O   1 
HETATM 5423 O  O   . HOH   H 4 .   ? 44.437 34.795  32.523  1.00 30.91  ?  731 HOH   B O   1 
HETATM 5424 O  O   . HOH   H 4 .   ? 9.621  21.830  7.890   1.00 52.71  ?  732 HOH   B O   1 
HETATM 5425 O  O   . HOH   H 4 .   ? 30.943 32.151  -0.026  1.00 37.97  ?  733 HOH   B O   1 
HETATM 5426 O  O   . HOH   H 4 .   ? 33.517 31.288  0.387   1.00 33.24  ?  734 HOH   B O   1 
HETATM 5427 O  O   . HOH   H 4 .   ? 40.416 13.717  7.126   1.00 28.11  ?  735 HOH   B O   1 
HETATM 5428 O  O   . HOH   H 4 .   ? 52.354 27.572  7.399   1.00 33.94  ?  736 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   . GLY   A 5   ? 0.7177 0.6564 0.5260 -0.0738 0.0701  -0.0087 161 GLY   A N   
2    C  CA  . GLY   A 5   ? 1.1156 1.0332 0.8993 -0.0666 0.0660  -0.0021 161 GLY   A CA  
3    C  C   . GLY   A 5   ? 0.9320 0.8318 0.7125 -0.0583 0.0554  0.0046  161 GLY   A C   
4    O  O   . GLY   A 5   ? 0.8937 0.7772 0.6552 -0.0504 0.0499  0.0097  161 GLY   A O   
5    N  N   . ALA   A 6   ? 0.7596 0.6640 0.5591 -0.0596 0.0523  0.0040  162 ALA   A N   
6    C  CA  . ALA   A 6   ? 0.6870 0.5779 0.4869 -0.0518 0.0426  0.0092  162 ALA   A CA  
7    C  C   . ALA   A 6   ? 0.7580 0.6194 0.5316 -0.0530 0.0460  0.0181  162 ALA   A C   
8    O  O   . ALA   A 6   ? 0.7163 0.5650 0.4851 -0.0439 0.0373  0.0227  162 ALA   A O   
9    C  CB  . ALA   A 6   ? 0.7088 0.6116 0.5340 -0.0537 0.0399  0.0061  162 ALA   A CB  
10   N  N   . SER   A 7   ? 0.5796 0.4294 0.3357 -0.0639 0.0587  0.0203  163 SER   A N   
11   C  CA  . SER   A 7   ? 0.7982 0.6155 0.5257 -0.0651 0.0630  0.0293  163 SER   A CA  
12   C  C   . SER   A 7   ? 0.8994 0.7003 0.6036 -0.0518 0.0550  0.0350  163 SER   A C   
13   O  O   . SER   A 7   ? 0.7822 0.5595 0.4698 -0.0449 0.0509  0.0421  163 SER   A O   
14   C  CB  . SER   A 7   ? 0.8803 0.6883 0.5917 -0.0806 0.0794  0.0299  163 SER   A CB  
15   O  OG  . SER   A 7   ? 0.8740 0.6960 0.5820 -0.0830 0.0844  0.0257  163 SER   A OG  
16   N  N   . LYS   A 8   ? 0.7389 0.5524 0.4414 -0.0471 0.0522  0.0315  164 LYS   A N   
17   C  CA  . LYS   A 8   ? 0.7904 0.5918 0.4722 -0.0339 0.0435  0.0356  164 LYS   A CA  
18   C  C   . LYS   A 8   ? 0.7439 0.5517 0.4412 -0.0211 0.0281  0.0348  164 LYS   A C   
19   O  O   . LYS   A 8   ? 0.6658 0.4569 0.3456 -0.0103 0.0207  0.0402  164 LYS   A O   
20   C  CB  . LYS   A 8   ? 0.6654 0.4807 0.3432 -0.0329 0.0444  0.0307  164 LYS   A CB  
21   C  CG  . LYS   A 8   ? 0.8614 0.6660 0.5166 -0.0197 0.0355  0.0338  164 LYS   A CG  
22   C  CD  . LYS   A 8   ? 0.7527 0.5656 0.3970 -0.0209 0.0399  0.0299  164 LYS   A CD  
23   C  CE  . LYS   A 8   ? 0.8835 0.6878 0.5060 -0.0072 0.0297  0.0319  164 LYS   A CE  
24   N  NZ  . LYS   A 8   ? 0.9205 0.7318 0.5304 -0.0084 0.0344  0.0279  164 LYS   A NZ  
25   N  N   . LEU   A 9   ? 0.7124 0.5445 0.4418 -0.0219 0.0233  0.0279  165 LEU   A N   
26   C  CA  . LEU   A 9   ? 0.7169 0.5556 0.4626 -0.0121 0.0106  0.0266  165 LEU   A CA  
27   C  C   . LEU   A 9   ? 0.6124 0.4326 0.3523 -0.0103 0.0099  0.0330  165 LEU   A C   
28   O  O   . LEU   A 9   ? 0.5958 0.4105 0.3326 0.0010  0.0000  0.0352  165 LEU   A O   
29   C  CB  . LEU   A 9   ? 0.5010 0.3652 0.2794 -0.0151 0.0081  0.0188  165 LEU   A CB  
30   C  CG  . LEU   A 9   ? 0.4960 0.3787 0.2822 -0.0164 0.0089  0.0116  165 LEU   A CG  
31   C  CD1 . LEU   A 9   ? 0.4015 0.3045 0.2170 -0.0194 0.0078  0.0051  165 LEU   A CD1 
32   C  CD2 . LEU   A 9   ? 0.5482 0.4326 0.3266 -0.0061 -0.0009 0.0098  165 LEU   A CD2 
33   N  N   . ARG   A 10  ? 0.7487 0.5598 0.4872 -0.0211 0.0204  0.0352  166 ARG   A N   
34   C  CA  . ARG   A 10  ? 0.6786 0.4695 0.4097 -0.0201 0.0209  0.0409  166 ARG   A CA  
35   C  C   . ARG   A 10  ? 0.6450 0.4063 0.3412 -0.0120 0.0202  0.0492  166 ARG   A C   
36   O  O   . ARG   A 10  ? 0.6576 0.4057 0.3477 -0.0022 0.0135  0.0532  166 ARG   A O   
37   C  CB  . ARG   A 10  ? 0.7867 0.5741 0.5224 -0.0350 0.0330  0.0405  166 ARG   A CB  
38   C  CG  . ARG   A 10  ? 0.9094 0.7243 0.6788 -0.0406 0.0322  0.0328  166 ARG   A CG  
39   C  CD  . ARG   A 10  ? 0.9306 0.7404 0.7108 -0.0421 0.0314  0.0337  166 ARG   A CD  
40   N  NE  . ARG   A 10  ? 0.9906 0.7859 0.7629 -0.0297 0.0225  0.0386  166 ARG   A NE  
41   C  CZ  . ARG   A 10  ? 1.0152 0.8231 0.8070 -0.0218 0.0128  0.0362  166 ARG   A CZ  
42   N  NH1 . ARG   A 10  ? 0.8288 0.6612 0.6473 -0.0246 0.0106  0.0298  166 ARG   A NH1 
43   N  NH2 . ARG   A 10  ? 1.0569 0.8525 0.8404 -0.0105 0.0055  0.0401  166 ARG   A NH2 
44   N  N   . ALA   A 11  ? 0.6563 0.4067 0.3283 -0.0152 0.0271  0.0517  167 ALA   A N   
45   C  CA  . ALA   A 11  ? 0.6437 0.3649 0.2791 -0.0060 0.0259  0.0598  167 ALA   A CA  
46   C  C   . ALA   A 11  ? 0.7345 0.4631 0.3708 0.0120  0.0099  0.0591  167 ALA   A C   
47   O  O   . ALA   A 11  ? 0.9184 0.6275 0.5366 0.0241  0.0037  0.0647  167 ALA   A O   
48   C  CB  . ALA   A 11  ? 0.5977 0.3092 0.2083 -0.0130 0.0364  0.0618  167 ALA   A CB  
49   N  N   . VAL   A 12  ? 0.7504 0.5074 0.4075 0.0141  0.0031  0.0515  168 VAL   A N   
50   C  CA  . VAL   A 12  ? 0.7179 0.4864 0.3797 0.0291  -0.0119 0.0486  168 VAL   A CA  
51   C  C   . VAL   A 12  ? 0.6699 0.4411 0.3478 0.0364  -0.0202 0.0486  168 VAL   A C   
52   O  O   . VAL   A 12  ? 0.6364 0.4007 0.3033 0.0506  -0.0300 0.0508  168 VAL   A O   
53   C  CB  . VAL   A 12  ? 0.6184 0.4167 0.3031 0.0271  -0.0162 0.0393  168 VAL   A CB  
54   C  CG1 . VAL   A 12  ? 0.6993 0.5130 0.3958 0.0399  -0.0314 0.0345  168 VAL   A CG1 
55   C  CG2 . VAL   A 12  ? 0.6174 0.4128 0.2824 0.0235  -0.0098 0.0391  168 VAL   A CG2 
56   N  N   . LEU   A 13  ? 0.5948 0.3773 0.2991 0.0274  -0.0166 0.0455  169 LEU   A N   
57   C  CA  . LEU   A 13  ? 0.5961 0.3825 0.3170 0.0333  -0.0234 0.0449  169 LEU   A CA  
58   C  C   . LEU   A 13  ? 0.7410 0.4977 0.4378 0.0393  -0.0218 0.0530  169 LEU   A C   
59   O  O   . LEU   A 13  ? 0.6995 0.4556 0.3986 0.0514  -0.0309 0.0534  169 LEU   A O   
60   C  CB  . LEU   A 13  ? 0.6751 0.4777 0.4259 0.0220  -0.0189 0.0403  169 LEU   A CB  
61   C  CG  . LEU   A 13  ? 0.6204 0.4514 0.3962 0.0189  -0.0225 0.0320  169 LEU   A CG  
62   C  CD1 . LEU   A 13  ? 0.6178 0.4603 0.4153 0.0068  -0.0152 0.0286  169 LEU   A CD1 
63   C  CD2 . LEU   A 13  ? 0.5438 0.3905 0.3356 0.0291  -0.0350 0.0275  169 LEU   A CD2 
64   N  N   . GLU   A 14  ? 0.7941 0.5257 0.4672 0.0311  -0.0099 0.0591  170 GLU   A N   
65   C  CA  . GLU   A 14  ? 0.8764 0.5742 0.5214 0.0368  -0.0074 0.0673  170 GLU   A CA  
66   C  C   . GLU   A 14  ? 0.7940 0.4795 0.4137 0.0552  -0.0175 0.0713  170 GLU   A C   
67   O  O   . GLU   A 14  ? 0.9336 0.6077 0.5461 0.0684  -0.0246 0.0742  170 GLU   A O   
68   C  CB  . GLU   A 14  ? 0.9384 0.6109 0.5607 0.0226  0.0084  0.0725  170 GLU   A CB  
69   C  CG  . GLU   A 14  ? 1.0304 0.6678 0.6307 0.0229  0.0142  0.0796  170 GLU   A CG  
70   C  CD  . GLU   A 14  ? 1.1973 0.8078 0.7706 0.0102  0.0294  0.0843  170 GLU   A CD  
71   O  OE1 . GLU   A 14  ? 1.2308 0.8513 0.8110 -0.0062 0.0396  0.0815  170 GLU   A OE1 
72   O  OE2 . GLU   A 14  ? 1.1315 0.7183 0.6849 0.0162  0.0311  0.0877  170 GLU   A OE2 
73   N  N   . LYS   A 15  ? 0.8354 0.5240 0.4412 0.0572  -0.0186 0.0710  171 LYS   A N   
74   C  CA  . LYS   A 15  ? 0.8438 0.5225 0.4244 0.0754  -0.0290 0.0742  171 LYS   A CA  
75   C  C   . LYS   A 15  ? 0.9416 0.6464 0.5460 0.0894  -0.0450 0.0676  171 LYS   A C   
76   O  O   . LYS   A 15  ? 1.0050 0.6996 0.5950 0.1063  -0.0542 0.0704  171 LYS   A O   
77   C  CB  . LYS   A 15  ? 0.8020 0.4826 0.3656 0.0737  -0.0270 0.0738  171 LYS   A CB  
78   C  CG  . LYS   A 15  ? 0.9557 0.6532 0.5179 0.0897  -0.0422 0.0695  171 LYS   A CG  
79   C  CD  . LYS   A 15  ? 0.9951 0.6910 0.5369 0.0875  -0.0390 0.0695  171 LYS   A CD  
80   C  CE  . LYS   A 15  ? 0.7878 0.5169 0.3608 0.0764  -0.0382 0.0597  171 LYS   A CE  
81   N  NZ  . LYS   A 15  ? 0.9985 0.7257 0.5516 0.0735  -0.0336 0.0593  171 LYS   A NZ  
82   N  N   . LEU   A 16  ? 0.8758 0.6146 0.5169 0.0825  -0.0482 0.0585  172 LEU   A N   
83   C  CA  . LEU   A 16  ? 1.0063 0.7717 0.6723 0.0928  -0.0619 0.0513  172 LEU   A CA  
84   C  C   . LEU   A 16  ? 0.8933 0.6525 0.5664 0.0993  -0.0646 0.0531  172 LEU   A C   
85   O  O   . LEU   A 16  ? 0.9598 0.7260 0.6337 0.1149  -0.0761 0.0511  172 LEU   A O   
86   C  CB  . LEU   A 16  ? 0.8203 0.6179 0.5220 0.0819  -0.0623 0.0419  172 LEU   A CB  
87   C  CG  . LEU   A 16  ? 0.7794 0.5899 0.4793 0.0788  -0.0633 0.0372  172 LEU   A CG  
88   C  CD1 . LEU   A 16  ? 0.6423 0.4784 0.3755 0.0669  -0.0614 0.0291  172 LEU   A CD1 
89   C  CD2 . LEU   A 16  ? 0.7020 0.5217 0.3931 0.0942  -0.0769 0.0337  172 LEU   A CD2 
90   N  N   . LYS   A 17  ? 0.9046 0.6476 0.5780 0.0889  -0.0537 0.0573  173 LYS   A N   
91   C  CA  . LYS   A 17  ? 0.9119 0.6482 0.5926 0.0941  -0.0551 0.0587  173 LYS   A CA  
92   C  C   . LYS   A 17  ? 1.0222 0.7261 0.6673 0.1096  -0.0577 0.0666  173 LYS   A C   
93   O  O   . LYS   A 17  ? 1.0757 0.7832 0.7259 0.1235  -0.0664 0.0654  173 LYS   A O   
94   C  CB  . LYS   A 17  ? 0.8276 0.5584 0.5211 0.0778  -0.0433 0.0594  173 LYS   A CB  
95   C  CG  . LYS   A 17  ? 1.0052 0.6985 0.6706 0.0733  -0.0324 0.0678  173 LYS   A CG  
96   C  CD  . LYS   A 17  ? 0.9578 0.6514 0.6410 0.0587  -0.0231 0.0663  173 LYS   A CD  
97   C  CE  . LYS   A 17  ? 0.9747 0.7013 0.6961 0.0578  -0.0293 0.0585  173 LYS   A CE  
98   N  NZ  . LYS   A 17  ? 0.9210 0.6499 0.6589 0.0435  -0.0205 0.0566  173 LYS   A NZ  
99   N  N   . LEU   A 18  ? 1.0272 0.7018 0.6384 0.1075  -0.0500 0.0740  174 LEU   A N   
100  C  CA  . LEU   A 18  ? 1.0179 0.6690 0.6068 0.1177  -0.0488 0.0775  174 LEU   A CA  
101  C  C   . LEU   A 18  ? 1.2620 0.9299 0.8525 0.1376  -0.0636 0.0732  174 LEU   A C   
102  O  O   . LEU   A 18  ? 1.2889 0.9441 0.8679 0.1499  -0.0661 0.0743  174 LEU   A O   
103  C  CB  . LEU   A 18  ? 1.1289 0.7527 0.6887 0.1089  -0.0366 0.0832  174 LEU   A CB  
104  C  CG  . LEU   A 18  ? 1.1605 0.7699 0.7199 0.0880  -0.0210 0.0860  174 LEU   A CG  
105  C  CD1 . LEU   A 18  ? 1.1639 0.7452 0.6945 0.0804  -0.0088 0.0908  174 LEU   A CD1 
106  C  CD2 . LEU   A 18  ? 1.1079 0.7123 0.6811 0.0848  -0.0183 0.0854  174 LEU   A CD2 
107  N  N   . SER   A 19  ? 1.2326 0.9291 0.8375 0.1403  -0.0730 0.0676  175 SER   A N   
108  C  CA  . SER   A 19  ? 1.1790 0.8972 0.7905 0.1577  -0.0873 0.0613  175 SER   A CA  
109  C  C   . SER   A 19  ? 1.0385 0.7845 0.6824 0.1627  -0.0963 0.0542  175 SER   A C   
110  O  O   . SER   A 19  ? 1.1289 0.9047 0.7891 0.1708  -0.1080 0.0461  175 SER   A O   
111  C  CB  . SER   A 19  ? 1.1680 0.9027 0.7774 0.1577  -0.0925 0.0576  175 SER   A CB  
112  O  OG  . SER   A 19  ? 1.2461 0.9591 0.8327 0.1464  -0.0812 0.0637  175 SER   A OG  
113  N  N   . ILE   A 23  ? 0.9993 0.7906 0.6724 0.2390  -0.1321 0.0322  179 ILE   A N   
114  C  CA  . ILE   A 23  ? 0.9966 0.8079 0.6995 0.2241  -0.1301 0.0295  179 ILE   A CA  
115  C  C   . ILE   A 23  ? 1.1696 1.0092 0.9022 0.2300  -0.1356 0.0211  179 ILE   A C   
116  O  O   . ILE   A 23  ? 1.1610 1.0367 0.9158 0.2346  -0.1450 0.0111  179 ILE   A O   
117  C  CB  . ILE   A 23  ? 1.0329 0.8127 0.7241 0.2094  -0.1171 0.0389  179 ILE   A CB  
118  N  N   . SER   A 24  ? 1.0871 0.9118 0.8206 0.2288  -0.1295 0.0244  180 SER   A N   
119  C  CA  . SER   A 24  ? 1.0778 0.9283 0.8372 0.2358  -0.1341 0.0163  180 SER   A CA  
120  C  C   . SER   A 24  ? 1.0134 0.8698 0.7627 0.2550  -0.1420 0.0118  180 SER   A C   
121  O  O   . SER   A 24  ? 1.1528 1.0388 0.9249 0.2626  -0.1481 0.0027  180 SER   A O   
122  C  CB  . SER   A 24  ? 1.2286 1.0605 0.9892 0.2305  -0.1256 0.0208  180 SER   A CB  
123  O  OG  . SER   A 24  ? 1.2812 1.0863 1.0300 0.2152  -0.1156 0.0293  180 SER   A OG  
124  N  N   . THR   A 25  ? 0.9827 0.8117 0.6986 0.2625  -0.1414 0.0177  181 THR   A N   
125  C  CA  . THR   A 25  ? 1.1883 1.0207 0.8912 0.2821  -0.1494 0.0137  181 THR   A CA  
126  C  C   . THR   A 25  ? 1.1333 1.0069 0.8579 0.2859  -0.1601 0.0030  181 THR   A C   
127  O  O   . THR   A 25  ? 1.0699 0.9745 0.8164 0.2943  -0.1669 -0.0069 181 THR   A O   
128  C  CB  . THR   A 25  ? 1.1335 0.9254 0.7947 0.2877  -0.1455 0.0228  181 THR   A CB  
129  O  OG1 . THR   A 25  ? 1.2359 1.0374 0.8934 0.2854  -0.1495 0.0217  181 THR   A OG1 
130  C  CG2 . THR   A 25  ? 1.0365 0.7883 0.6785 0.2749  -0.1324 0.0338  181 THR   A CG2 
131  N  N   . ALA   A 26  ? 1.0396 0.9145 0.7591 0.2786  -0.1608 0.0043  182 ALA   A N   
132  C  CA  . ALA   A 26  ? 0.9753 0.8883 0.7146 0.2801  -0.1703 -0.0063 182 ALA   A CA  
133  C  C   . ALA   A 26  ? 0.9414 0.8949 0.7220 0.2738  -0.1735 -0.0169 182 ALA   A C   
134  O  O   . ALA   A 26  ? 1.0806 1.0682 0.8797 0.2810  -0.1819 -0.0283 182 ALA   A O   
135  C  CB  . ALA   A 26  ? 0.9854 0.8929 0.7168 0.2686  -0.1685 -0.0028 182 ALA   A CB  
136  N  N   . ALA   A 27  ? 0.9282 0.8784 0.7235 0.2603  -0.1664 -0.0138 183 ALA   A N   
137  C  CA  . ALA   A 27  ? 0.9361 0.9225 0.7698 0.2531  -0.1680 -0.0234 183 ALA   A CA  
138  C  C   . ALA   A 27  ? 0.9218 0.9230 0.7660 0.2658  -0.1713 -0.0298 183 ALA   A C   
139  O  O   . ALA   A 27  ? 1.0791 1.1183 0.9537 0.2646  -0.1755 -0.0413 183 ALA   A O   
140  C  CB  . ALA   A 27  ? 0.9268 0.9026 0.7705 0.2372  -0.1594 -0.0179 183 ALA   A CB  
141  N  N   . GLY   A 28  ? 0.9536 0.9249 0.7723 0.2775  -0.1687 -0.0229 184 GLY   A N   
142  C  CA  . GLY   A 28  ? 1.0423 1.0270 0.8674 0.2919  -0.1727 -0.0294 184 GLY   A CA  
143  C  C   . GLY   A 28  ? 0.8712 0.8848 0.7012 0.3046  -0.1833 -0.0400 184 GLY   A C   
144  O  O   . GLY   A 28  ? 1.1076 1.1563 0.9630 0.3088  -0.1880 -0.0514 184 GLY   A O   
145  N  N   . MET   A 29  ? 0.9260 0.9255 0.7314 0.3105  -0.1869 -0.0368 185 MET   A N   
146  C  CA  . MET   A 29  ? 0.8013 0.8291 0.6112 0.3221  -0.1973 -0.0473 185 MET   A CA  
147  C  C   . MET   A 29  ? 0.9266 1.0001 0.7750 0.3099  -0.2008 -0.0597 185 MET   A C   
148  O  O   . MET   A 29  ? 0.9603 1.0696 0.8298 0.3163  -0.2073 -0.0724 185 MET   A O   
149  C  CB  . MET   A 29  ? 0.7964 0.8002 0.5736 0.3282  -0.1996 -0.0411 185 MET   A CB  
150  C  CG  . MET   A 29  ? 0.9297 0.8830 0.6668 0.3351  -0.1934 -0.0275 185 MET   A CG  
151  S  SD  . MET   A 29  ? 1.3446 1.2858 1.0582 0.3613  -0.1988 -0.0290 185 MET   A SD  
152  C  CE  . MET   A 29  ? 0.8993 0.8844 0.6268 0.3738  -0.2125 -0.0438 185 MET   A CE  
153  N  N   . VAL   A 30  ? 0.8387 0.9111 0.6962 0.2918  -0.1963 -0.0567 186 VAL   A N   
154  C  CA  . VAL   A 30  ? 0.8818 0.9935 0.7742 0.2780  -0.1983 -0.0680 186 VAL   A CA  
155  C  C   . VAL   A 30  ? 0.9116 1.0515 0.8361 0.2745  -0.1967 -0.0765 186 VAL   A C   
156  O  O   . VAL   A 30  ? 0.9225 1.1012 0.8739 0.2717  -0.2009 -0.0898 186 VAL   A O   
157  C  CB  . VAL   A 30  ? 0.9058 1.0063 0.7996 0.2596  -0.1928 -0.0621 186 VAL   A CB  
158  C  CG1 . VAL   A 30  ? 0.8137 0.9524 0.7400 0.2457  -0.1951 -0.0743 186 VAL   A CG1 
159  C  CG2 . VAL   A 30  ? 0.8803 0.9502 0.7399 0.2631  -0.1930 -0.0528 186 VAL   A CG2 
160  N  N   . LYS   A 31  ? 0.7419 0.8622 0.6633 0.2739  -0.1901 -0.0692 187 LYS   A N   
161  C  CA  . LYS   A 31  ? 0.8228 0.9672 0.7730 0.2703  -0.1874 -0.0763 187 LYS   A CA  
162  C  C   . LYS   A 31  ? 0.9615 1.1307 0.9185 0.2860  -0.1940 -0.0868 187 LYS   A C   
163  O  O   . LYS   A 31  ? 0.9362 1.1432 0.9242 0.2811  -0.1950 -0.0991 187 LYS   A O   
164  C  CB  . LYS   A 31  ? 0.9757 1.0896 0.9165 0.2682  -0.1790 -0.0655 187 LYS   A CB  
165  C  CG  . LYS   A 31  ? 0.9054 1.0404 0.8775 0.2580  -0.1736 -0.0707 187 LYS   A CG  
166  C  CD  . LYS   A 31  ? 0.9297 1.0914 0.9305 0.2390  -0.1719 -0.0775 187 LYS   A CD  
167  C  CE  . LYS   A 31  ? 1.0585 1.2579 1.0940 0.2337  -0.1702 -0.0896 187 LYS   A CE  
168  N  NZ  . LYS   A 31  ? 0.7806 1.0134 0.8421 0.2194  -0.1715 -0.1006 187 LYS   A NZ  
169  N  N   . GLY   A 32  ? 0.8741 1.0222 0.8018 0.3048  -0.1983 -0.0826 188 GLY   A N   
170  C  CA  . GLY   A 32  ? 0.8269 0.9993 0.7590 0.3214  -0.2059 -0.0932 188 GLY   A CA  
171  C  C   . GLY   A 32  ? 0.9415 1.1559 0.8967 0.3176  -0.2125 -0.1074 188 GLY   A C   
172  O  O   . GLY   A 32  ? 0.9329 1.1848 0.9161 0.3168  -0.2144 -0.1203 188 GLY   A O   
173  N  N   . VAL   A 33  ? 0.8423 1.0507 0.7865 0.3138  -0.2154 -0.1054 189 VAL   A N   
174  C  CA  . VAL   A 33  ? 0.7567 1.0027 0.7203 0.3103  -0.2219 -0.1190 189 VAL   A CA  
175  C  C   . VAL   A 33  ? 0.8185 1.0980 0.8215 0.2898  -0.2173 -0.1286 189 VAL   A C   
176  O  O   . VAL   A 33  ? 0.8212 1.1397 0.8486 0.2888  -0.2209 -0.1432 189 VAL   A O   
177  C  CB  . VAL   A 33  ? 0.8862 1.1162 0.8290 0.3092  -0.2250 -0.1141 189 VAL   A CB  
178  C  CG1 . VAL   A 33  ? 0.8046 1.0725 0.7684 0.3032  -0.2308 -0.1283 189 VAL   A CG1 
179  C  CG2 . VAL   A 33  ? 0.8472 1.0472 0.7513 0.3305  -0.2297 -0.1065 189 VAL   A CG2 
180  N  N   . VAL   A 34  ? 0.8106 1.0754 0.8200 0.2731  -0.2088 -0.1210 190 VAL   A N   
181  C  CA  . VAL   A 34  ? 0.8829 1.1762 0.9269 0.2526  -0.2039 -0.1296 190 VAL   A CA  
182  C  C   . VAL   A 34  ? 0.7977 1.1160 0.8660 0.2530  -0.2011 -0.1379 190 VAL   A C   
183  O  O   . VAL   A 34  ? 0.8348 1.1886 0.9324 0.2422  -0.2001 -0.1509 190 VAL   A O   
184  C  CB  . VAL   A 34  ? 0.7666 1.0374 0.8099 0.2354  -0.1960 -0.1196 190 VAL   A CB  
185  C  CG1 . VAL   A 34  ? 0.9246 1.1750 0.9462 0.2335  -0.1986 -0.1131 190 VAL   A CG1 
186  C  CG2 . VAL   A 34  ? 0.7763 1.0191 0.8093 0.2381  -0.1896 -0.1081 190 VAL   A CG2 
187  N  N   . ASP   A 35  ? 0.7513 1.0507 0.8073 0.2647  -0.1991 -0.1309 191 ASP   A N   
188  C  CA  . ASP   A 35  ? 0.7433 1.0670 0.8207 0.2670  -0.1969 -0.1393 191 ASP   A CA  
189  C  C   . ASP   A 35  ? 0.8289 1.1879 0.9167 0.2777  -0.2048 -0.1540 191 ASP   A C   
190  O  O   . ASP   A 35  ? 0.8031 1.1981 0.9204 0.2698  -0.2028 -0.1667 191 ASP   A O   
191  C  CB  . ASP   A 35  ? 0.6606 0.9555 0.7192 0.2798  -0.1942 -0.1293 191 ASP   A CB  
192  C  CG  . ASP   A 35  ? 0.8872 1.1557 0.9442 0.2671  -0.1848 -0.1178 191 ASP   A CG  
193  O  OD1 . ASP   A 35  ? 0.9290 1.2073 1.0047 0.2479  -0.1800 -0.1193 191 ASP   A OD1 
194  O  OD2 . ASP   A 35  ? 0.9203 1.1570 0.9562 0.2761  -0.1822 -0.1074 191 ASP   A OD2 
195  N  N   . HIS   A 36  ? 0.7587 1.1081 0.8220 0.2954  -0.2135 -0.1529 192 HIS   A N   
196  C  CA  . HIS   A 36  ? 0.8132 1.1966 0.8850 0.3070  -0.2221 -0.1674 192 HIS   A CA  
197  C  C   . HIS   A 36  ? 0.9065 1.3267 1.0072 0.2899  -0.2221 -0.1807 192 HIS   A C   
198  O  O   . HIS   A 36  ? 0.9200 1.3786 1.0466 0.2874  -0.2227 -0.1954 192 HIS   A O   
199  C  CB  . HIS   A 36  ? 0.8060 1.1692 0.8442 0.3278  -0.2311 -0.1629 192 HIS   A CB  
200  C  CG  . HIS   A 36  ? 0.8016 1.1922 0.8414 0.3467  -0.2402 -0.1755 192 HIS   A CG  
201  N  ND1 . HIS   A 36  ? 0.9108 1.3445 0.9748 0.3426  -0.2449 -0.1920 192 HIS   A ND1 
202  C  CD2 . HIS   A 36  ? 0.9560 1.3370 0.9756 0.3702  -0.2456 -0.1746 192 HIS   A CD2 
203  C  CE1 . HIS   A 36  ? 1.0100 1.4613 1.0695 0.3631  -0.2531 -0.2010 192 HIS   A CE1 
204  N  NE2 . HIS   A 36  ? 1.0552 1.4748 1.0875 0.3805  -0.2538 -0.1906 192 HIS   A NE2 
205  N  N   . LEU   A 37  ? 0.9713 1.3796 1.0671 0.2775  -0.2212 -0.1761 193 LEU   A N   
206  C  CA  . LEU   A 37  ? 0.8592 1.2983 0.9793 0.2608  -0.2210 -0.1883 193 LEU   A CA  
207  C  C   . LEU   A 37  ? 0.7367 1.1988 0.8899 0.2411  -0.2118 -0.1956 193 LEU   A C   
208  O  O   . LEU   A 37  ? 0.7207 1.2191 0.8989 0.2324  -0.2118 -0.2105 193 LEU   A O   
209  C  CB  . LEU   A 37  ? 0.7821 1.2005 0.8900 0.2500  -0.2205 -0.1809 193 LEU   A CB  
210  C  CG  . LEU   A 37  ? 0.9252 1.3257 1.0031 0.2649  -0.2291 -0.1761 193 LEU   A CG  
211  C  CD1 . LEU   A 37  ? 0.7838 1.1418 0.8369 0.2611  -0.2251 -0.1592 193 LEU   A CD1 
212  C  CD2 . LEU   A 37  ? 0.8476 1.2751 0.9364 0.2592  -0.2344 -0.1886 193 LEU   A CD2 
213  N  N   . LEU   A 38  ? 0.7078 1.1489 0.8613 0.2332  -0.2033 -0.1853 194 LEU   A N   
214  C  CA  . LEU   A 38  ? 0.7326 1.1924 0.9155 0.2141  -0.1937 -0.1912 194 LEU   A CA  
215  C  C   . LEU   A 38  ? 0.7294 1.2207 0.9304 0.2208  -0.1938 -0.2031 194 LEU   A C   
216  O  O   . LEU   A 38  ? 0.6580 1.1792 0.8867 0.2057  -0.1885 -0.2148 194 LEU   A O   
217  C  CB  . LEU   A 38  ? 0.4418 0.8715 0.6191 0.2062  -0.1851 -0.1775 194 LEU   A CB  
218  C  CG  . LEU   A 38  ? 0.6854 1.0903 0.8527 0.1933  -0.1826 -0.1682 194 LEU   A CG  
219  C  CD1 . LEU   A 38  ? 0.6484 1.0207 0.8046 0.1913  -0.1761 -0.1538 194 LEU   A CD1 
220  C  CD2 . LEU   A 38  ? 0.7354 1.1618 0.9272 0.1703  -0.1773 -0.1777 194 LEU   A CD2 
221  N  N   . LEU   A 39  ? 0.7710 1.2554 0.9562 0.2432  -0.1995 -0.2005 195 LEU   A N   
222  C  CA  . LEU   A 39  ? 0.7221 1.2385 0.9236 0.2516  -0.2008 -0.2130 195 LEU   A CA  
223  C  C   . LEU   A 39  ? 0.6314 1.1870 0.8491 0.2504  -0.2066 -0.2301 195 LEU   A C   
224  O  O   . LEU   A 39  ? 0.7684 1.3589 1.0141 0.2397  -0.2024 -0.2436 195 LEU   A O   
225  C  CB  . LEU   A 39  ? 0.6592 1.1578 0.8366 0.2774  -0.2068 -0.2069 195 LEU   A CB  
226  C  CG  . LEU   A 39  ? 0.8034 1.2697 0.9703 0.2778  -0.1996 -0.1930 195 LEU   A CG  
227  C  CD1 . LEU   A 39  ? 0.7772 1.2200 0.9157 0.3032  -0.2056 -0.1860 195 LEU   A CD1 
228  C  CD2 . LEU   A 39  ? 0.6286 1.1169 0.8243 0.2642  -0.1902 -0.1994 195 LEU   A CD2 
229  N  N   . ARG   A 40  ? 0.7072 1.2576 0.9074 0.2609  -0.2160 -0.2300 196 ARG   A N   
230  C  CA  . ARG   A 40  ? 0.6375 1.2250 0.8521 0.2606  -0.2221 -0.2466 196 ARG   A CA  
231  C  C   . ARG   A 40  ? 0.7096 1.3185 0.9525 0.2330  -0.2140 -0.2554 196 ARG   A C   
232  O  O   . ARG   A 40  ? 0.7125 1.3597 0.9797 0.2266  -0.2132 -0.2716 196 ARG   A O   
233  C  CB  . ARG   A 40  ? 0.6615 1.2361 0.8513 0.2743  -0.2325 -0.2437 196 ARG   A CB  
234  C  CG  . ARG   A 40  ? 0.5326 1.1456 0.7322 0.2830  -0.2415 -0.2611 196 ARG   A CG  
235  C  CD  . ARG   A 40  ? 0.5602 1.1836 0.7510 0.3089  -0.2491 -0.2658 196 ARG   A CD  
236  N  NE  . ARG   A 40  ? 0.6628 1.3353 0.8793 0.3099  -0.2523 -0.2862 196 ARG   A NE  
237  C  CZ  . ARG   A 40  ? 0.8663 1.5621 1.0996 0.3132  -0.2498 -0.2945 196 ARG   A CZ  
238  N  NH1 . ARG   A 40  ? 0.5900 1.2649 0.8180 0.3158  -0.2440 -0.2843 196 ARG   A NH1 
239  N  NH2 . ARG   A 40  ? 0.7384 1.4801 0.9945 0.3138  -0.2531 -0.3139 196 ARG   A NH2 
240  N  N   . LEU   A 41  ? 0.6256 1.2092 0.8647 0.2162  -0.2075 -0.2451 197 LEU   A N   
241  C  CA  . LEU   A 41  ? 0.6603 1.2589 0.9230 0.1896  -0.1991 -0.2523 197 LEU   A CA  
242  C  C   . LEU   A 41  ? 0.5294 1.1472 0.8175 0.1769  -0.1888 -0.2587 197 LEU   A C   
243  O  O   . LEU   A 41  ? 0.5929 1.2395 0.9048 0.1607  -0.1839 -0.2721 197 LEU   A O   
244  C  CB  . LEU   A 41  ? 0.4140 0.9787 0.6652 0.1760  -0.1942 -0.2390 197 LEU   A CB  
245  C  CG  . LEU   A 41  ? 0.5853 1.1356 0.8172 0.1800  -0.2018 -0.2354 197 LEU   A CG  
246  C  CD1 . LEU   A 41  ? 0.6037 1.1132 0.8162 0.1753  -0.1983 -0.2183 197 LEU   A CD1 
247  C  CD2 . LEU   A 41  ? 0.4479 1.0227 0.6974 0.1634  -0.2011 -0.2487 197 LEU   A CD2 
248  N  N   . LYS   A 42  ? 0.4457 1.0470 0.7282 0.1835  -0.1850 -0.2493 198 LYS   A N   
249  C  CA  . LYS   A 42  ? 0.5856 1.2032 0.8901 0.1726  -0.1749 -0.2545 198 LYS   A CA  
250  C  C   . LYS   A 42  ? 0.6373 1.2969 0.9603 0.1786  -0.1778 -0.2719 198 LYS   A C   
251  O  O   . LYS   A 42  ? 0.5633 1.2449 0.9095 0.1639  -0.1687 -0.2807 198 LYS   A O   
252  C  CB  . LYS   A 42  ? 0.4614 1.0525 0.7536 0.1819  -0.1717 -0.2410 198 LYS   A CB  
253  C  CG  . LYS   A 42  ? 0.7249 1.2812 1.0084 0.1688  -0.1644 -0.2263 198 LYS   A CG  
254  C  CD  . LYS   A 42  ? 0.6422 1.1665 0.9046 0.1840  -0.1652 -0.2116 198 LYS   A CD  
255  C  CE  . LYS   A 42  ? 0.7684 1.2802 1.0397 0.1698  -0.1533 -0.2049 198 LYS   A CE  
256  N  NZ  . LYS   A 42  ? 0.5501 1.0759 0.8433 0.1437  -0.1438 -0.2113 198 LYS   A NZ  
257  N  N   . CYS   A 43  ? 0.4296 1.1008 0.7421 0.2001  -0.1899 -0.2774 199 CYS   A N   
258  C  CA  . CYS   A 43  ? 0.6148 1.3294 0.9463 0.2054  -0.1931 -0.2957 199 CYS   A CA  
259  C  C   . CYS   A 43  ? 0.7177 1.4629 1.0724 0.1849  -0.1896 -0.3109 199 CYS   A C   
260  O  O   . CYS   A 43  ? 0.6638 1.4472 1.0397 0.1828  -0.1886 -0.3272 199 CYS   A O   
261  C  CB  . CYS   A 43  ? 0.6163 1.3357 0.9296 0.2341  -0.2073 -0.2984 199 CYS   A CB  
262  S  SG  . CYS   A 43  ? 0.8910 1.5834 1.1808 0.2597  -0.2108 -0.2856 199 CYS   A SG  
263  N  N   . ASP   A 44  ? 0.5977 1.3273 0.9490 0.1695  -0.1873 -0.3065 200 ASP   A N   
264  C  CA  . ASP   A 44  ? 0.5179 1.2729 0.8889 0.1497  -0.1838 -0.3205 200 ASP   A CA  
265  C  C   . ASP   A 44  ? 0.4787 1.2350 0.8695 0.1227  -0.1682 -0.3218 200 ASP   A C   
266  O  O   . ASP   A 44  ? 0.6891 1.4164 1.0735 0.1156  -0.1606 -0.3083 200 ASP   A O   
267  C  CB  . ASP   A 44  ? 0.6250 1.3623 0.9818 0.1463  -0.1889 -0.3159 200 ASP   A CB  
268  C  CG  . ASP   A 44  ? 0.5485 1.3150 0.9233 0.1310  -0.1882 -0.3323 200 ASP   A CG  
269  O  OD1 . ASP   A 44  ? 0.6239 1.3916 1.0140 0.1059  -0.1767 -0.3354 200 ASP   A OD1 
270  O  OD2 . ASP   A 44  ? 0.4875 1.2747 0.8601 0.1441  -0.1990 -0.3422 200 ASP   A OD2 
271  N  N   . SER   A 45  ? 0.5569 1.3468 0.9709 0.1073  -0.1634 -0.3387 201 SER   A N   
272  C  CA  . SER   A 45  ? 0.5172 1.3098 0.9494 0.0813  -0.1479 -0.3415 201 SER   A CA  
273  C  C   . SER   A 45  ? 0.4114 1.1700 0.8353 0.0621  -0.1406 -0.3302 201 SER   A C   
274  O  O   . SER   A 45  ? 0.5100 1.2513 0.9371 0.0468  -0.1285 -0.3229 201 SER   A O   
275  C  CB  . SER   A 45  ? 0.4156 1.2504 0.8724 0.0688  -0.1445 -0.3626 201 SER   A CB  
276  O  OG  . SER   A 45  ? 0.5321 1.3637 0.9927 0.0486  -0.1405 -0.3667 201 SER   A OG  
277  N  N   . ALA   A 46  ? 0.4232 1.1717 0.8358 0.0631  -0.1477 -0.3286 202 ALA   A N   
278  C  CA  . ALA   A 46  ? 0.5848 1.3034 0.9901 0.0447  -0.1411 -0.3196 202 ALA   A CA  
279  C  C   . ALA   A 46  ? 0.4363 1.1143 0.8201 0.0522  -0.1418 -0.2996 202 ALA   A C   
280  O  O   . ALA   A 46  ? 0.6061 1.2586 0.9869 0.0357  -0.1325 -0.2908 202 ALA   A O   
281  C  CB  . ALA   A 46  ? 0.4759 1.1998 0.8774 0.0422  -0.1482 -0.3264 202 ALA   A CB  
282  N  N   . PHE   A 47  ? 0.4907 1.1614 0.8584 0.0768  -0.1524 -0.2924 203 PHE   A N   
283  C  CA  . PHE   A 47  ? 0.3547 0.9873 0.7005 0.0854  -0.1540 -0.2740 203 PHE   A CA  
284  C  C   . PHE   A 47  ? 0.5389 1.1662 0.8830 0.0970  -0.1518 -0.2672 203 PHE   A C   
285  O  O   . PHE   A 47  ? 0.6903 1.2928 1.0143 0.1130  -0.1571 -0.2543 203 PHE   A O   
286  C  CB  . PHE   A 47  ? 0.4563 1.0769 0.7797 0.1039  -0.1672 -0.2689 203 PHE   A CB  
287  C  CG  . PHE   A 47  ? 0.3719 0.9950 0.6947 0.0935  -0.1698 -0.2745 203 PHE   A CG  
288  C  CD1 . PHE   A 47  ? 0.4548 1.0508 0.7703 0.0780  -0.1645 -0.2661 203 PHE   A CD1 
289  C  CD2 . PHE   A 47  ? 0.5525 1.2053 0.8818 0.0997  -0.1777 -0.2889 203 PHE   A CD2 
290  C  CE1 . PHE   A 47  ? 0.4840 1.0814 0.7982 0.0687  -0.1668 -0.2715 203 PHE   A CE1 
291  C  CE2 . PHE   A 47  ? 0.4790 1.1341 0.8076 0.0901  -0.1801 -0.2944 203 PHE   A CE2 
292  C  CZ  . PHE   A 47  ? 0.5031 1.1298 0.8238 0.0745  -0.1745 -0.2856 203 PHE   A CZ  
293  N  N   . ARG   A 48  ? 0.6169 1.2667 0.9813 0.0888  -0.1437 -0.2758 204 ARG   A N   
294  C  CA  . ARG   A 48  ? 0.5092 1.1564 0.8732 0.0998  -0.1414 -0.2708 204 ARG   A CA  
295  C  C   . ARG   A 48  ? 0.4643 1.0750 0.8170 0.0944  -0.1346 -0.2541 204 ARG   A C   
296  O  O   . ARG   A 48  ? 0.5378 1.1322 0.8776 0.1103  -0.1374 -0.2443 204 ARG   A O   
297  C  CB  . ARG   A 48  ? 0.5423 1.2219 0.9311 0.0896  -0.1330 -0.2843 204 ARG   A CB  
298  N  N   . GLY   A 49  ? 0.5087 1.1054 0.8652 0.0724  -0.1254 -0.2509 205 GLY   A N   
299  C  CA  . GLY   A 49  ? 0.3214 0.8849 0.6679 0.0662  -0.1188 -0.2361 205 GLY   A CA  
300  C  C   . GLY   A 49  ? 0.3922 0.9253 0.7156 0.0751  -0.1263 -0.2235 205 GLY   A C   
301  O  O   . GLY   A 49  ? 0.3679 0.8734 0.6830 0.0679  -0.1210 -0.2120 205 GLY   A O   
302  N  N   . VAL   A 50  ? 0.4818 1.0192 0.7936 0.0907  -0.1385 -0.2255 206 VAL   A N   
303  C  CA  . VAL   A 50  ? 0.3945 0.9029 0.6828 0.0987  -0.1453 -0.2139 206 VAL   A CA  
304  C  C   . VAL   A 50  ? 0.4776 0.9580 0.7499 0.1104  -0.1450 -0.1993 206 VAL   A C   
305  O  O   . VAL   A 50  ? 0.5414 1.0273 0.8158 0.1213  -0.1445 -0.1990 206 VAL   A O   
306  C  CB  . VAL   A 50  ? 0.5350 1.0534 0.8122 0.1153  -0.1581 -0.2189 206 VAL   A CB  
307  C  CG1 . VAL   A 50  ? 0.5069 1.0254 0.7722 0.1404  -0.1656 -0.2160 206 VAL   A CG1 
308  C  CG2 . VAL   A 50  ? 0.5821 1.0753 0.8394 0.1154  -0.1629 -0.2105 206 VAL   A CG2 
309  N  N   . GLY   A 51  ? 0.3782 0.8283 0.6343 0.1075  -0.1449 -0.1874 207 GLY   A N   
310  C  CA  . GLY   A 51  ? 0.3861 0.8082 0.6270 0.1165  -0.1438 -0.1737 207 GLY   A CA  
311  C  C   . GLY   A 51  ? 0.5303 0.9221 0.7513 0.1151  -0.1461 -0.1626 207 GLY   A C   
312  O  O   . GLY   A 51  ? 0.5358 0.9284 0.7554 0.1066  -0.1481 -0.1656 207 GLY   A O   
313  N  N   . LEU   A 52  ? 0.5864 0.9512 0.7914 0.1238  -0.1456 -0.1500 208 LEU   A N   
314  C  CA  . LEU   A 52  ? 0.4460 0.7801 0.6314 0.1225  -0.1467 -0.1385 208 LEU   A CA  
315  C  C   . LEU   A 52  ? 0.5048 0.8296 0.7009 0.1045  -0.1368 -0.1350 208 LEU   A C   
316  O  O   . LEU   A 52  ? 0.5772 0.9092 0.7880 0.0993  -0.1294 -0.1365 208 LEU   A O   
317  C  CB  . LEU   A 52  ? 0.4272 0.7344 0.5862 0.1425  -0.1515 -0.1266 208 LEU   A CB  
318  C  CG  . LEU   A 52  ? 0.5558 0.8578 0.6930 0.1594  -0.1616 -0.1256 208 LEU   A CG  
319  C  CD1 . LEU   A 52  ? 0.5693 0.8356 0.6767 0.1744  -0.1635 -0.1116 208 LEU   A CD1 
320  C  CD2 . LEU   A 52  ? 0.5928 0.8976 0.7266 0.1514  -0.1654 -0.1290 208 LEU   A CD2 
321  N  N   . LEU   A 53  ? 0.6487 0.9568 0.8364 0.0951  -0.1366 -0.1306 209 LEU   A N   
322  C  CA  . LEU   A 53  ? 0.6823 0.9801 0.8787 0.0776  -0.1275 -0.1277 209 LEU   A CA  
323  C  C   . LEU   A 53  ? 0.5831 0.8598 0.7721 0.0830  -0.1231 -0.1170 209 LEU   A C   
324  O  O   . LEU   A 53  ? 0.7801 1.0574 0.9817 0.0721  -0.1128 -0.1170 209 LEU   A O   
325  C  CB  . LEU   A 53  ? 0.6453 0.9272 0.8310 0.0685  -0.1290 -0.1250 209 LEU   A CB  
326  C  CG  . LEU   A 53  ? 0.5617 0.8570 0.7625 0.0490  -0.1240 -0.1350 209 LEU   A CG  
327  C  CD1 . LEU   A 53  ? 0.4390 0.7565 0.6430 0.0536  -0.1303 -0.1448 209 LEU   A CD1 
328  C  CD2 . LEU   A 53  ? 0.3983 0.6711 0.5884 0.0379  -0.1219 -0.1304 209 LEU   A CD2 
329  N  N   . TYR   A 59  ? 1.0286 1.1647 1.0333 0.1718  -0.1629 -0.0656 215 TYR   A N   
330  C  CA  . TYR   A 59  ? 0.7478 0.8627 0.7251 0.1746  -0.1656 -0.0592 215 TYR   A CA  
331  C  C   . TYR   A 59  ? 0.6911 0.7920 0.6659 0.1593  -0.1605 -0.0545 215 TYR   A C   
332  O  O   . TYR   A 59  ? 0.8080 0.8946 0.7881 0.1474  -0.1494 -0.0489 215 TYR   A O   
333  C  CB  . TYR   A 59  ? 0.8704 0.9513 0.8141 0.1898  -0.1649 -0.0475 215 TYR   A CB  
334  C  CG  . TYR   A 59  ? 0.9230 0.9689 0.8500 0.1857  -0.1572 -0.0347 215 TYR   A CG  
335  C  CD1 . TYR   A 59  ? 0.7906 0.8320 0.7276 0.1849  -0.1520 -0.0325 215 TYR   A CD1 
336  C  CD2 . TYR   A 59  ? 0.9613 0.9784 0.8617 0.1825  -0.1545 -0.0253 215 TYR   A CD2 
337  C  CE1 . TYR   A 59  ? 0.9305 0.9388 0.8532 0.1773  -0.1415 -0.0215 215 TYR   A CE1 
338  C  CE2 . TYR   A 59  ? 0.9320 0.9169 0.8187 0.1743  -0.1434 -0.0145 215 TYR   A CE2 
339  C  CZ  . TYR   A 59  ? 1.0267 1.0074 0.9249 0.1713  -0.1369 -0.0129 215 TYR   A CZ  
340  O  OH  . TYR   A 59  ? 1.1396 1.0895 1.0248 0.1619  -0.1255 -0.0032 215 TYR   A OH  
341  N  N   . GLU   A 60  ? 0.7946 0.8971 0.7608 0.1561  -0.1642 -0.0566 216 GLU   A N   
342  C  CA  . GLU   A 60  ? 0.7080 0.7923 0.6676 0.1398  -0.1553 -0.0515 216 GLU   A CA  
343  C  C   . GLU   A 60  ? 0.6438 0.7183 0.5778 0.1466  -0.1613 -0.0495 216 GLU   A C   
344  O  O   . GLU   A 60  ? 0.6482 0.7393 0.5802 0.1571  -0.1709 -0.0562 216 GLU   A O   
345  C  CB  . GLU   A 60  ? 0.6136 0.7193 0.6023 0.1213  -0.1510 -0.0609 216 GLU   A CB  
346  N  N   . HIS   A 61  ? 0.6359 0.6831 0.5514 0.1385  -0.1530 -0.0404 217 HIS   A N   
347  C  CA  . HIS   A 61  ? 0.6085 0.6430 0.4975 0.1432  -0.1564 -0.0373 217 HIS   A CA  
348  C  C   . HIS   A 61  ? 0.6809 0.7210 0.5797 0.1264  -0.1515 -0.0418 217 HIS   A C   
349  O  O   . HIS   A 61  ? 0.8244 0.8478 0.7222 0.1139  -0.1404 -0.0359 217 HIS   A O   
350  C  CB  . HIS   A 61  ? 0.6248 0.6218 0.4808 0.1489  -0.1504 -0.0231 217 HIS   A CB  
351  C  CG  . HIS   A 61  ? 0.6409 0.6286 0.4812 0.1680  -0.1565 -0.0188 217 HIS   A CG  
352  N  ND1 . HIS   A 61  ? 0.8396 0.8218 0.6883 0.1699  -0.1525 -0.0156 217 HIS   A ND1 
353  C  CD2 . HIS   A 61  ? 0.8111 0.7934 0.6319 0.1821  -0.1613 -0.0178 217 HIS   A CD2 
354  C  CE1 . HIS   A 61  ? 0.8076 0.7805 0.6408 0.1855  -0.1558 -0.0129 217 HIS   A CE1 
355  N  NE2 . HIS   A 61  ? 0.8201 0.7929 0.6371 0.1924  -0.1603 -0.0142 217 HIS   A NE2 
356  N  N   . VAL   A 62  ? 0.6090 0.6734 0.5174 0.1268  -0.1602 -0.0532 218 VAL   A N   
357  C  CA  . VAL   A 62  ? 0.5616 0.6320 0.4791 0.1121  -0.1566 -0.0590 218 VAL   A CA  
358  C  C   . VAL   A 62  ? 0.7126 0.7564 0.6031 0.1098  -0.1506 -0.0502 218 VAL   A C   
359  O  O   . VAL   A 62  ? 0.6136 0.6493 0.5088 0.0961  -0.1413 -0.0488 218 VAL   A O   
360  C  CB  . VAL   A 62  ? 0.6061 0.7065 0.5354 0.1145  -0.1681 -0.0734 218 VAL   A CB  
361  C  CG1 . VAL   A 62  ? 0.5344 0.6352 0.4656 0.1015  -0.1649 -0.0787 218 VAL   A CG1 
362  C  CG2 . VAL   A 62  ? 0.6817 0.8106 0.6426 0.1118  -0.1711 -0.0835 218 VAL   A CG2 
363  N  N   . LYS   A 63  ? 0.6679 0.6980 0.5291 0.1235  -0.1554 -0.0444 219 LYS   A N   
364  C  CA  . LYS   A 63  ? 0.7389 0.7426 0.5718 0.1219  -0.1488 -0.0354 219 LYS   A CA  
365  C  C   . LYS   A 63  ? 0.6793 0.6548 0.4940 0.1256  -0.1413 -0.0221 219 LYS   A C   
366  O  O   . LYS   A 63  ? 0.7777 0.7474 0.5805 0.1399  -0.1469 -0.0184 219 LYS   A O   
367  C  CB  . LYS   A 63  ? 0.6795 0.6843 0.4884 0.1337  -0.1584 -0.0377 219 LYS   A CB  
368  C  CG  . LYS   A 63  ? 0.7369 0.7722 0.5634 0.1324  -0.1682 -0.0525 219 LYS   A CG  
369  C  CD  . LYS   A 63  ? 0.6557 0.6922 0.4634 0.1435  -0.1741 -0.0539 219 LYS   A CD  
370  C  CE  . LYS   A 63  ? 0.8023 0.8062 0.5722 0.1497  -0.1688 -0.0409 219 LYS   A CE  
371  N  NZ  . LYS   A 63  ? 0.7969 0.8012 0.5484 0.1577  -0.1731 -0.0428 219 LYS   A NZ  
372  N  N   . ILE   A 64  ? 0.6961 0.6542 0.5085 0.1129  -0.1286 -0.0155 220 ILE   A N   
373  C  CA  . ILE   A 64  ? 0.7834 0.7145 0.5798 0.1135  -0.1201 -0.0039 220 ILE   A CA  
374  C  C   . ILE   A 64  ? 0.7707 0.6770 0.5285 0.1253  -0.1214 0.0046  220 ILE   A C   
375  O  O   . ILE   A 64  ? 1.0606 0.9439 0.8016 0.1304  -0.1174 0.0135  220 ILE   A O   
376  C  CB  . ILE   A 64  ? 0.7257 0.6473 0.5293 0.0967  -0.1066 -0.0005 220 ILE   A CB  
377  C  CG1 . ILE   A 64  ? 0.8915 0.8018 0.7019 0.0934  -0.0997 0.0055  220 ILE   A CG1 
378  C  CG2 . ILE   A 64  ? 0.7429 0.6443 0.5194 0.0934  -0.0995 0.0057  220 ILE   A CG2 
379  C  CD1 . ILE   A 64  ? 0.8172 0.7487 0.6583 0.0923  -0.1035 -0.0011 220 ILE   A CD1 
380  N  N   . SER   A 65  ? 0.8185 0.7276 0.5603 0.1300  -0.1267 0.0019  221 SER   A N   
381  C  CA  . SER   A 65  ? 0.8556 0.7395 0.5576 0.1406  -0.1271 0.0102  221 SER   A CA  
382  C  C   . SER   A 65  ? 0.9569 0.8448 0.6489 0.1596  -0.1389 0.0088  221 SER   A C   
383  O  O   . SER   A 65  ? 1.1304 0.9978 0.7950 0.1671  -0.1365 0.0152  221 SER   A O   
384  C  CB  . SER   A 65  ? 0.7670 0.6509 0.4558 0.1354  -0.1250 0.0080  221 SER   A CB  
385  O  OG  . SER   A 65  ? 0.8936 0.8060 0.5969 0.1391  -0.1365 -0.0039 221 SER   A OG  
386  N  N   . ALA   A 66  ? 0.9234 0.8393 0.6434 0.1645  -0.1480 -0.0004 222 ALA   A N   
387  C  CA  . ALA   A 66  ? 0.8801 0.8076 0.6013 0.1794  -0.1565 -0.0047 222 ALA   A CA  
388  C  C   . ALA   A 66  ? 0.8561 0.7844 0.5899 0.1854  -0.1572 -0.0036 222 ALA   A C   
389  O  O   . ALA   A 66  ? 0.8373 0.7951 0.6011 0.1857  -0.1633 -0.0132 222 ALA   A O   
390  C  CB  . ALA   A 66  ? 0.7050 0.6685 0.4489 0.1792  -0.1663 -0.0188 222 ALA   A CB  
391  N  N   . PRO   A 67  ? 0.8828 0.7793 0.5943 0.1898  -0.1501 0.0075  223 PRO   A N   
392  C  CA  . PRO   A 67  ? 0.7630 0.6581 0.4858 0.1945  -0.1495 0.0087  223 PRO   A CA  
393  C  C   . PRO   A 67  ? 0.9087 0.8258 0.6436 0.2091  -0.1592 0.0006  223 PRO   A C   
394  O  O   . PRO   A 67  ? 0.9487 0.8747 0.7009 0.2120  -0.1600 -0.0018 223 PRO   A O   
395  C  CB  . PRO   A 67  ? 0.9109 0.7636 0.6018 0.1956  -0.1392 0.0218  223 PRO   A CB  
396  C  CG  . PRO   A 67  ? 0.8858 0.7221 0.5476 0.1981  -0.1377 0.0258  223 PRO   A CG  
397  C  CD  . PRO   A 67  ? 0.9302 0.7903 0.6051 0.1897  -0.1416 0.0187  223 PRO   A CD  
398  N  N   . ASN   A 68  ? 0.8340 0.7612 0.5607 0.2183  -0.1663 -0.0043 224 ASN   A N   
399  C  CA  . ASN   A 68  ? 0.8770 0.8242 0.6123 0.2333  -0.1754 -0.0122 224 ASN   A CA  
400  C  C   . ASN   A 68  ? 0.9085 0.8991 0.6756 0.2303  -0.1842 -0.0268 224 ASN   A C   
401  O  O   . ASN   A 68  ? 1.0044 1.0157 0.7795 0.2420  -0.1920 -0.0350 224 ASN   A O   
402  C  CB  . ASN   A 68  ? 0.9351 0.8620 0.6371 0.2481  -0.1777 -0.0078 224 ASN   A CB  
403  C  CG  . ASN   A 68  ? 1.0282 0.9138 0.7006 0.2534  -0.1696 0.0047  224 ASN   A CG  
404  O  OD1 . ASN   A 68  ? 1.1757 1.0311 0.8167 0.2540  -0.1644 0.0133  224 ASN   A OD1 
405  N  ND2 . ASN   A 68  ? 0.9821 0.8659 0.6645 0.2565  -0.1680 0.0052  224 ASN   A ND2 
406  N  N   . GLU   A 69  ? 0.9663 0.9710 0.7512 0.2147  -0.1826 -0.0310 225 GLU   A N   
407  C  CA  . GLU   A 69  ? 0.7326 0.7769 0.5492 0.2088  -0.1891 -0.0454 225 GLU   A CA  
408  C  C   . GLU   A 69  ? 0.7629 0.8231 0.6106 0.1975  -0.1859 -0.0494 225 GLU   A C   
409  O  O   . GLU   A 69  ? 0.7777 0.8273 0.6279 0.1849  -0.1797 -0.0450 225 GLU   A O   
410  C  CB  . GLU   A 69  ? 0.6823 0.7311 0.4952 0.1997  -0.1899 -0.0489 225 GLU   A CB  
411  C  CG  . GLU   A 69  ? 1.0306 1.0962 0.8395 0.2094  -0.1986 -0.0571 225 GLU   A CG  
412  C  CD  . GLU   A 69  ? 1.2784 1.3549 1.0901 0.1992  -0.2000 -0.0635 225 GLU   A CD  
413  O  OE1 . GLU   A 69  ? 1.2232 1.2763 1.0111 0.1959  -0.1955 -0.0558 225 GLU   A OE1 
414  O  OE2 . GLU   A 69  ? 1.2986 1.4068 1.1360 0.1942  -0.2052 -0.0768 225 GLU   A OE2 
415  N  N   . PHE   A 70  ? 0.7738 0.8595 0.6446 0.2023  -0.1900 -0.0580 226 PHE   A N   
416  C  CA  . PHE   A 70  ? 0.6179 0.7183 0.5171 0.1940  -0.1866 -0.0616 226 PHE   A CA  
417  C  C   . PHE   A 70  ? 0.5370 0.6740 0.4695 0.1816  -0.1891 -0.0759 226 PHE   A C   
418  O  O   . PHE   A 70  ? 0.6529 0.8085 0.5891 0.1830  -0.1948 -0.0848 226 PHE   A O   
419  C  CB  . PHE   A 70  ? 0.6980 0.8003 0.5992 0.2074  -0.1879 -0.0613 226 PHE   A CB  
420  C  CG  . PHE   A 70  ? 0.7173 0.7816 0.5918 0.2147  -0.1823 -0.0472 226 PHE   A CG  
421  C  CD1 . PHE   A 70  ? 0.7936 0.8288 0.6329 0.2253  -0.1825 -0.0385 226 PHE   A CD1 
422  C  CD2 . PHE   A 70  ? 0.7797 0.8364 0.6638 0.2103  -0.1762 -0.0430 226 PHE   A CD2 
423  C  CE1 . PHE   A 70  ? 0.8205 0.8188 0.6345 0.2300  -0.1759 -0.0260 226 PHE   A CE1 
424  C  CE2 . PHE   A 70  ? 0.8606 0.8811 0.7197 0.2158  -0.1703 -0.0306 226 PHE   A CE2 
425  C  CZ  . PHE   A 70  ? 0.7645 0.7554 0.5886 0.2250  -0.1698 -0.0222 226 PHE   A CZ  
426  N  N   . ASP   A 71  ? 0.5638 0.7098 0.5201 0.1689  -0.1840 -0.0783 227 ASP   A N   
427  C  CA  . ASP   A 71  ? 0.5322 0.7089 0.5201 0.1540  -0.1837 -0.0912 227 ASP   A CA  
428  C  C   . ASP   A 71  ? 0.6249 0.8162 0.6383 0.1498  -0.1797 -0.0946 227 ASP   A C   
429  O  O   . ASP   A 71  ? 0.5150 0.6910 0.5290 0.1449  -0.1739 -0.0874 227 ASP   A O   
430  C  CB  . ASP   A 71  ? 0.5866 0.7547 0.5746 0.1382  -0.1798 -0.0905 227 ASP   A CB  
431  C  CG  . ASP   A 71  ? 0.8227 1.0157 0.8295 0.1265  -0.1815 -0.1038 227 ASP   A CG  
432  O  OD1 . ASP   A 71  ? 1.0583 1.2699 1.0925 0.1134  -0.1777 -0.1120 227 ASP   A OD1 
433  O  OD2 . ASP   A 71  ? 0.8420 1.0344 0.8351 0.1298  -0.1860 -0.1060 227 ASP   A OD2 
434  N  N   . VAL   A 72  ? 0.6885 0.9097 0.7226 0.1517  -0.1825 -0.1059 228 VAL   A N   
435  C  CA  . VAL   A 72  ? 0.6222 0.8605 0.6815 0.1472  -0.1781 -0.1106 228 VAL   A CA  
436  C  C   . VAL   A 72  ? 0.5349 0.8051 0.6236 0.1321  -0.1765 -0.1251 228 VAL   A C   
437  O  O   . VAL   A 72  ? 0.4493 0.7307 0.5384 0.1291  -0.1805 -0.1323 228 VAL   A O   
438  C  CB  . VAL   A 72  ? 0.6032 0.8454 0.6582 0.1652  -0.1814 -0.1101 228 VAL   A CB  
439  C  CG1 . VAL   A 72  ? 0.7965 1.0028 0.8186 0.1797  -0.1821 -0.0956 228 VAL   A CG1 
440  C  CG2 . VAL   A 72  ? 0.5122 0.7799 0.5719 0.1735  -0.1888 -0.1212 228 VAL   A CG2 
441  N  N   . MET   A 73  ? 0.4436 0.7271 0.5560 0.1222  -0.1700 -0.1291 229 MET   A N   
442  C  CA  . MET   A 73  ? 0.5362 0.8456 0.6758 0.1050  -0.1656 -0.1418 229 MET   A CA  
443  C  C   . MET   A 73  ? 0.5802 0.9138 0.7403 0.1072  -0.1633 -0.1491 229 MET   A C   
444  O  O   . MET   A 73  ? 0.4909 0.8179 0.6542 0.1095  -0.1588 -0.1436 229 MET   A O   
445  C  CB  . MET   A 73  ? 0.2976 0.5953 0.4452 0.0854  -0.1570 -0.1395 229 MET   A CB  
446  C  CG  . MET   A 73  ? 0.5423 0.8608 0.7152 0.0661  -0.1503 -0.1512 229 MET   A CG  
447  S  SD  . MET   A 73  ? 0.6317 0.9307 0.8086 0.0439  -0.1401 -0.1480 229 MET   A SD  
448  C  CE  . MET   A 73  ? 0.4719 0.7409 0.6191 0.0524  -0.1461 -0.1370 229 MET   A CE  
449  N  N   . PHE   A 74  ? 0.5035 0.8655 0.6772 0.1067  -0.1663 -0.1618 230 PHE   A N   
450  C  CA  . PHE   A 74  ? 0.4519 0.8409 0.6473 0.1065  -0.1635 -0.1710 230 PHE   A CA  
451  C  C   . PHE   A 74  ? 0.4630 0.8652 0.6823 0.0828  -0.1535 -0.1791 230 PHE   A C   
452  O  O   . PHE   A 74  ? 0.5235 0.9354 0.7491 0.0714  -0.1534 -0.1872 230 PHE   A O   
453  C  CB  . PHE   A 74  ? 0.4664 0.8800 0.6631 0.1196  -0.1722 -0.1812 230 PHE   A CB  
454  C  CG  . PHE   A 74  ? 0.5337 0.9347 0.7066 0.1442  -0.1810 -0.1740 230 PHE   A CG  
455  C  CD1 . PHE   A 74  ? 0.4761 0.8435 0.6265 0.1523  -0.1807 -0.1590 230 PHE   A CD1 
456  C  CD2 . PHE   A 74  ? 0.4612 0.8831 0.6334 0.1591  -0.1892 -0.1826 230 PHE   A CD2 
457  C  CE1 . PHE   A 74  ? 0.5347 0.8868 0.6608 0.1740  -0.1876 -0.1520 230 PHE   A CE1 
458  C  CE2 . PHE   A 74  ? 0.5348 0.9423 0.6829 0.1818  -0.1967 -0.1759 230 PHE   A CE2 
459  C  CZ  . PHE   A 74  ? 0.5931 0.9644 0.7175 0.1889  -0.1955 -0.1603 230 PHE   A CZ  
460  N  N   . LYS   A 75  ? 0.5459 0.9466 0.7770 0.0753  -0.1447 -0.1767 231 LYS   A N   
461  C  CA  . LYS   A 75  ? 0.4958 0.9045 0.7466 0.0527  -0.1337 -0.1829 231 LYS   A CA  
462  C  C   . LYS   A 75  ? 0.3433 0.7845 0.6156 0.0498  -0.1307 -0.1957 231 LYS   A C   
463  O  O   . LYS   A 75  ? 0.4548 0.9112 0.7282 0.0658  -0.1361 -0.1986 231 LYS   A O   
464  C  CB  . LYS   A 75  ? 0.3888 0.7770 0.6400 0.0445  -0.1245 -0.1733 231 LYS   A CB  
465  C  CG  . LYS   A 75  ? 0.4324 0.8217 0.6842 0.0578  -0.1242 -0.1686 231 LYS   A CG  
466  C  CD  . LYS   A 75  ? 0.4972 0.8695 0.7521 0.0481  -0.1143 -0.1609 231 LYS   A CD  
467  C  CE  . LYS   A 75  ? 0.4786 0.8663 0.7476 0.0505  -0.1086 -0.1641 231 LYS   A CE  
468  N  NZ  . LYS   A 75  ? 0.5064 0.9118 0.7957 0.0310  -0.0982 -0.1738 231 LYS   A NZ  
469  N  N   . LEU   A 76  ? 0.3886 0.8390 0.6767 0.0290  -0.1216 -0.2035 232 LEU   A N   
470  C  CA  . LEU   A 76  ? 0.5074 0.9876 0.8167 0.0224  -0.1165 -0.2161 232 LEU   A CA  
471  C  C   . LEU   A 76  ? 0.4147 0.8879 0.7348 -0.0016 -0.1022 -0.2171 232 LEU   A C   
472  O  O   . LEU   A 76  ? 0.4360 0.8964 0.7528 -0.0160 -0.0988 -0.2174 232 LEU   A O   
473  C  CB  . LEU   A 76  ? 0.3192 0.8250 0.6345 0.0244  -0.1235 -0.2294 232 LEU   A CB  
474  C  CG  . LEU   A 76  ? 0.4471 0.9880 0.7843 0.0197  -0.1199 -0.2442 232 LEU   A CG  
475  C  CD1 . LEU   A 76  ? 0.5042 1.0701 0.8410 0.0388  -0.1323 -0.2527 232 LEU   A CD1 
476  C  CD2 . LEU   A 76  ? 0.3426 0.8904 0.6925 -0.0042 -0.1109 -0.2537 232 LEU   A CD2 
477  N  N   . GLU   A 77  ? 0.4247 0.9042 0.7559 -0.0056 -0.0936 -0.2174 233 GLU   A N   
478  C  CA  . GLU   A 77  ? 0.3159 0.7852 0.6542 -0.0277 -0.0792 -0.2171 233 GLU   A CA  
479  C  C   . GLU   A 77  ? 0.3878 0.8769 0.7400 -0.0438 -0.0737 -0.2308 233 GLU   A C   
480  O  O   . GLU   A 77  ? 0.4516 0.9716 0.8164 -0.0388 -0.0772 -0.2425 233 GLU   A O   
481  C  CB  . GLU   A 77  ? 0.4089 0.8791 0.7540 -0.0275 -0.0710 -0.2135 233 GLU   A CB  
482  C  CG  . GLU   A 77  ? 0.3973 0.8535 0.7464 -0.0500 -0.0554 -0.2121 233 GLU   A CG  
483  C  CD  . GLU   A 77  ? 0.6889 1.1435 1.0428 -0.0504 -0.0467 -0.2078 233 GLU   A CD  
484  O  OE1 . GLU   A 77  ? 0.9092 1.3750 1.2648 -0.0332 -0.0525 -0.2066 233 GLU   A OE1 
485  O  OE2 . GLU   A 77  ? 0.7012 1.1416 1.0555 -0.0675 -0.0337 -0.2054 233 GLU   A OE2 
486  N  N   . VAL   A 78  ? 0.3974 0.8675 0.7464 -0.0629 -0.0651 -0.2295 234 VAL   A N   
487  C  CA  . VAL   A 78  ? 0.3858 0.8679 0.7456 -0.0812 -0.0575 -0.2412 234 VAL   A CA  
488  C  C   . VAL   A 78  ? 0.5095 0.9749 0.8709 -0.0996 -0.0414 -0.2377 234 VAL   A C   
489  O  O   . VAL   A 78  ? 0.4647 0.8992 0.8140 -0.1104 -0.0353 -0.2296 234 VAL   A O   
490  C  CB  . VAL   A 78  ? 0.4454 0.9171 0.7968 -0.0872 -0.0618 -0.2434 234 VAL   A CB  
491  C  CG1 . VAL   A 78  ? 0.4916 0.9795 0.8551 -0.1043 -0.0553 -0.2573 234 VAL   A CG1 
492  C  CG2 . VAL   A 78  ? 0.5177 0.9992 0.8624 -0.0673 -0.0779 -0.2438 234 VAL   A CG2 
493  N  N   . PRO   A 79  ? 0.6036 1.0881 0.9786 -0.1031 -0.0340 -0.2436 235 PRO   A N   
494  C  CA  . PRO   A 79  ? 0.4759 0.9437 0.8505 -0.1203 -0.0182 -0.2400 235 PRO   A CA  
495  C  C   . PRO   A 79  ? 0.4973 0.9586 0.8726 -0.1417 -0.0086 -0.2469 235 PRO   A C   
496  O  O   . PRO   A 79  ? 0.5416 1.0246 0.9260 -0.1450 -0.0122 -0.2593 235 PRO   A O   
497  C  CB  . PRO   A 79  ? 0.4559 0.9506 0.8454 -0.1162 -0.0144 -0.2461 235 PRO   A CB  
498  C  CG  . PRO   A 79  ? 0.5095 1.0369 0.9084 -0.0982 -0.0280 -0.2549 235 PRO   A CG  
499  C  CD  . PRO   A 79  ? 0.4492 0.9694 0.8381 -0.0892 -0.0406 -0.2527 235 PRO   A CD  
500  N  N   . ARG   A 80  ? 0.5749 1.0050 0.9394 -0.1559 0.0037  -0.2387 236 ARG   A N   
501  C  CA  . ARG   A 80  ? 0.5570 0.9725 0.9177 -0.1768 0.0147  -0.2428 236 ARG   A CA  
502  C  C   . ARG   A 80  ? 0.5710 0.9873 0.9291 -0.1785 0.0069  -0.2488 236 ARG   A C   
503  O  O   . ARG   A 80  ? 0.5819 1.0173 0.9502 -0.1880 0.0086  -0.2619 236 ARG   A O   
504  C  CB  . ARG   A 80  ? 0.6832 1.1211 1.0585 -0.1894 0.0256  -0.2544 236 ARG   A CB  
505  C  CG  . ARG   A 80  ? 0.6600 1.0853 1.0323 -0.1944 0.0380  -0.2474 236 ARG   A CG  
506  C  CD  . ARG   A 80  ? 0.6108 1.0059 0.9709 -0.2152 0.0535  -0.2445 236 ARG   A CD  
507  N  NE  . ARG   A 80  ? 0.6979 1.1130 1.0700 -0.2307 0.0625  -0.2589 236 ARG   A NE  
508  C  CZ  . ARG   A 80  ? 0.7895 1.1862 1.1544 -0.2488 0.0781  -0.2588 236 ARG   A CZ  
509  N  NH1 . ARG   A 80  ? 0.7340 1.0912 1.0790 -0.2530 0.0864  -0.2450 236 ARG   A NH1 
510  N  NH2 . ARG   A 80  ? 0.7496 1.1675 1.1268 -0.2628 0.0858  -0.2731 236 ARG   A NH2 
511  N  N   . ILE   A 81  ? 0.7489 1.1442 1.0931 -0.1693 -0.0017 -0.2392 237 ILE   A N   
512  C  CA  . ILE   A 81  ? 0.5567 0.9501 0.8960 -0.1688 -0.0101 -0.2433 237 ILE   A CA  
513  C  C   . ILE   A 81  ? 0.5370 0.8990 0.8638 -0.1870 0.0000  -0.2415 237 ILE   A C   
514  O  O   . ILE   A 81  ? 0.6581 0.9910 0.9738 -0.1949 0.0105  -0.2321 237 ILE   A O   
515  C  CB  . ILE   A 81  ? 0.5751 0.9596 0.9036 -0.1506 -0.0234 -0.2341 237 ILE   A CB  
516  C  CG1 . ILE   A 81  ? 0.6067 0.9974 0.9323 -0.1471 -0.0341 -0.2403 237 ILE   A CG1 
517  C  CG2 . ILE   A 81  ? 0.4422 0.7873 0.7528 -0.1521 -0.0187 -0.2189 237 ILE   A CG2 
518  C  CD1 . ILE   A 81  ? 0.6196 1.0130 0.9382 -0.1266 -0.0487 -0.2347 237 ILE   A CD1 
519  N  N   . GLN   A 82  ? 0.6827 1.0497 1.0104 -0.1933 -0.0032 -0.2506 238 GLN   A N   
520  C  CA  . GLN   A 82  ? 0.4949 0.8321 0.8100 -0.2094 0.0051  -0.2499 238 GLN   A CA  
521  C  C   . GLN   A 82  ? 0.4278 0.7554 0.7327 -0.2032 -0.0059 -0.2492 238 GLN   A C   
522  O  O   . GLN   A 82  ? 0.6333 0.9867 0.9474 -0.1991 -0.0150 -0.2598 238 GLN   A O   
523  C  CB  . GLN   A 82  ? 0.5495 0.9019 0.8759 -0.2270 0.0147  -0.2637 238 GLN   A CB  
524  C  CG  . GLN   A 82  ? 0.7065 1.0298 1.0198 -0.2430 0.0220  -0.2648 238 GLN   A CG  
525  C  CD  . GLN   A 82  ? 0.7022 0.9818 0.9958 -0.2498 0.0332  -0.2511 238 GLN   A CD  
526  O  OE1 . GLN   A 82  ? 0.8023 1.0525 1.0787 -0.2436 0.0294  -0.2404 238 GLN   A OE1 
527  N  NE2 . GLN   A 82  ? 0.7572 1.0323 1.0522 -0.2622 0.0472  -0.2519 238 GLN   A NE2 
528  N  N   . LEU   A 83  ? 0.5633 0.8544 0.8489 -0.2018 -0.0053 -0.2371 239 LEU   A N   
529  C  CA  . LEU   A 83  ? 0.4569 0.7370 0.7312 -0.1947 -0.0157 -0.2355 239 LEU   A CA  
530  C  C   . LEU   A 83  ? 0.4209 0.6792 0.6855 -0.2095 -0.0100 -0.2398 239 LEU   A C   
531  O  O   . LEU   A 83  ? 0.6082 0.8411 0.8647 -0.2226 0.0026  -0.2363 239 LEU   A O   
532  C  CB  . LEU   A 83  ? 0.4215 0.6763 0.6803 -0.1830 -0.0195 -0.2207 239 LEU   A CB  
533  C  CG  . LEU   A 83  ? 0.4529 0.7281 0.7192 -0.1662 -0.0275 -0.2164 239 LEU   A CG  
534  C  CD1 . LEU   A 83  ? 0.3157 0.5659 0.5662 -0.1555 -0.0318 -0.2031 239 LEU   A CD1 
535  C  CD2 . LEU   A 83  ? 0.4650 0.7763 0.7435 -0.1555 -0.0400 -0.2266 239 LEU   A CD2 
536  N  N   . GLU   A 84  ? 0.4714 0.7390 0.7357 -0.2069 -0.0193 -0.2473 240 GLU   A N   
537  C  CA  . GLU   A 84  ? 0.6244 0.8714 0.8785 -0.2189 -0.0161 -0.2519 240 GLU   A CA  
538  C  C   . GLU   A 84  ? 0.5424 0.7705 0.7800 -0.2082 -0.0258 -0.2457 240 GLU   A C   
539  O  O   . GLU   A 84  ? 0.4239 0.6732 0.6653 -0.1962 -0.0384 -0.2495 240 GLU   A O   
540  C  CB  . GLU   A 84  ? 0.6413 0.9186 0.9107 -0.2270 -0.0178 -0.2687 240 GLU   A CB  
541  C  CG  . GLU   A 84  ? 0.7877 1.0461 1.0472 -0.2389 -0.0157 -0.2749 240 GLU   A CG  
542  C  CD  . GLU   A 84  ? 0.6919 0.9741 0.9667 -0.2537 -0.0108 -0.2912 240 GLU   A CD  
543  O  OE1 . GLU   A 84  ? 0.8063 1.1134 1.0976 -0.2577 -0.0055 -0.2965 240 GLU   A OE1 
544  O  OE2 . GLU   A 84  ? 0.8195 1.0961 1.0899 -0.2613 -0.0122 -0.2993 240 GLU   A OE2 
545  N  N   . GLU   A 85  ? 0.5594 0.7477 0.7778 -0.2118 -0.0202 -0.2364 241 GLU   A N   
546  C  CA  . GLU   A 85  ? 0.4541 0.6237 0.6562 -0.2016 -0.0287 -0.2306 241 GLU   A CA  
547  C  C   . GLU   A 85  ? 0.4348 0.6105 0.6352 -0.2044 -0.0351 -0.2414 241 GLU   A C   
548  O  O   . GLU   A 85  ? 0.4883 0.6549 0.6877 -0.2187 -0.0283 -0.2487 241 GLU   A O   
549  C  CB  . GLU   A 85  ? 0.4648 0.5906 0.6466 -0.2043 -0.0208 -0.2191 241 GLU   A CB  
550  C  CG  . GLU   A 85  ? 0.4439 0.5519 0.6093 -0.1925 -0.0292 -0.2129 241 GLU   A CG  
551  C  CD  . GLU   A 85  ? 0.6293 0.6953 0.7748 -0.1934 -0.0219 -0.2021 241 GLU   A CD  
552  O  OE1 . GLU   A 85  ? 0.7856 0.8355 0.9290 -0.2020 -0.0106 -0.1978 241 GLU   A OE1 
553  O  OE2 . GLU   A 85  ? 0.6037 0.6528 0.7347 -0.1849 -0.0274 -0.1980 241 GLU   A OE2 
554  N  N   . TYR   A 86  ? 0.4729 0.6634 0.6721 -0.1907 -0.0481 -0.2426 242 TYR   A N   
555  C  CA  . TYR   A 86  ? 0.4597 0.6567 0.6558 -0.1914 -0.0556 -0.2525 242 TYR   A CA  
556  C  C   . TYR   A 86  ? 0.5824 0.7416 0.7560 -0.1918 -0.0549 -0.2471 242 TYR   A C   
557  O  O   . TYR   A 86  ? 0.5436 0.6891 0.7049 -0.1799 -0.0593 -0.2376 242 TYR   A O   
558  C  CB  . TYR   A 86  ? 0.4510 0.6796 0.6533 -0.1756 -0.0697 -0.2558 242 TYR   A CB  
559  C  CG  . TYR   A 86  ? 0.4387 0.6684 0.6325 -0.1733 -0.0783 -0.2634 242 TYR   A CG  
560  C  CD1 . TYR   A 86  ? 0.5479 0.7875 0.7485 -0.1855 -0.0769 -0.2767 242 TYR   A CD1 
561  C  CD2 . TYR   A 86  ? 0.4585 0.6785 0.6366 -0.1595 -0.0873 -0.2573 242 TYR   A CD2 
562  C  CE1 . TYR   A 86  ? 0.6866 0.9269 0.8789 -0.1835 -0.0848 -0.2839 242 TYR   A CE1 
563  C  CE2 . TYR   A 86  ? 0.5738 0.7941 0.7428 -0.1574 -0.0947 -0.2642 242 TYR   A CE2 
564  C  CZ  . TYR   A 86  ? 0.5957 0.8261 0.7719 -0.1692 -0.0937 -0.2774 242 TYR   A CZ  
565  O  OH  . TYR   A 86  ? 0.6542 0.8849 0.8209 -0.1670 -0.1012 -0.2845 242 TYR   A OH  
566  N  N   . SER   A 87  ? 0.5826 0.7248 0.7506 -0.2053 -0.0489 -0.2537 243 SER   A N   
567  C  CA  . SER   A 87  ? 0.6650 0.7761 0.8126 -0.2051 -0.0501 -0.2525 243 SER   A CA  
568  C  C   . SER   A 87  ? 0.6499 0.7256 0.7797 -0.1992 -0.0459 -0.2386 243 SER   A C   
569  O  O   . SER   A 87  ? 0.6983 0.7551 0.8116 -0.1918 -0.0504 -0.2356 243 SER   A O   
570  C  CB  . SER   A 87  ? 0.5848 0.7126 0.7293 -0.1943 -0.0636 -0.2580 243 SER   A CB  
571  O  OG  . SER   A 87  ? 0.7914 0.8917 0.9176 -0.1963 -0.0640 -0.2598 243 SER   A OG  
572  N  N   . ASN   A 88  ? 0.5959 0.6632 0.7288 -0.2021 -0.0371 -0.2304 244 ASN   A N   
573  C  CA  . ASN   A 88  ? 0.6127 0.6483 0.7300 -0.1961 -0.0327 -0.2172 244 ASN   A CA  
574  C  C   . ASN   A 88  ? 0.5093 0.5486 0.6198 -0.1796 -0.0428 -0.2114 244 ASN   A C   
575  O  O   . ASN   A 88  ? 0.5906 0.6021 0.6838 -0.1738 -0.0420 -0.2042 244 ASN   A O   
576  C  CB  . ASN   A 88  ? 0.5870 0.5823 0.6853 -0.2032 -0.0253 -0.2159 244 ASN   A CB  
577  C  CG  . ASN   A 88  ? 0.9818 0.9620 1.0811 -0.2170 -0.0120 -0.2149 244 ASN   A CG  
578  O  OD1 . ASN   A 88  ? 0.9918 0.9789 1.0992 -0.2180 -0.0066 -0.2092 244 ASN   A OD1 
579  N  ND2 . ASN   A 88  ? 0.7466 0.7053 0.8367 -0.2276 -0.0063 -0.2204 244 ASN   A ND2 
580  N  N   . THR   A 89  ? 0.4886 0.5622 0.6119 -0.1715 -0.0521 -0.2147 245 THR   A N   
581  C  CA  . THR   A 89  ? 0.5540 0.6334 0.6709 -0.1557 -0.0616 -0.2094 245 THR   A CA  
582  C  C   . THR   A 89  ? 0.4791 0.5530 0.5961 -0.1487 -0.0589 -0.1977 245 THR   A C   
583  O  O   . THR   A 89  ? 0.4851 0.5589 0.5949 -0.1361 -0.0653 -0.1922 245 THR   A O   
584  C  CB  . THR   A 89  ? 0.4531 0.5697 0.5816 -0.1481 -0.0729 -0.2167 245 THR   A CB  
585  O  OG1 . THR   A 89  ? 0.4748 0.6179 0.6232 -0.1512 -0.0710 -0.2195 245 THR   A OG1 
586  C  CG2 . THR   A 89  ? 0.5183 0.6395 0.6442 -0.1530 -0.0770 -0.2282 245 THR   A CG2 
587  N  N   . ARG   A 90  ? 0.4671 0.5371 0.5918 -0.1565 -0.0496 -0.1942 246 ARG   A N   
588  C  CA  . ARG   A 90  ? 0.4752 0.5376 0.5997 -0.1516 -0.0455 -0.1833 246 ARG   A CA  
589  C  C   . ARG   A 90  ? 0.3900 0.4831 0.5277 -0.1409 -0.0531 -0.1820 246 ARG   A C   
590  O  O   . ARG   A 90  ? 0.4325 0.5274 0.5760 -0.1393 -0.0491 -0.1755 246 ARG   A O   
591  C  CB  . ARG   A 90  ? 0.4454 0.4765 0.5506 -0.1452 -0.0445 -0.1747 246 ARG   A CB  
592  C  CG  . ARG   A 90  ? 0.3899 0.3889 0.4794 -0.1525 -0.0384 -0.1759 246 ARG   A CG  
593  C  CD  . ARG   A 90  ? 0.4826 0.4697 0.5750 -0.1658 -0.0271 -0.1759 246 ARG   A CD  
594  N  NE  . ARG   A 90  ? 0.8246 0.7791 0.9032 -0.1653 -0.0186 -0.1657 246 ARG   A NE  
595  C  CZ  . ARG   A 90  ? 0.8942 0.8421 0.9757 -0.1713 -0.0094 -0.1605 246 ARG   A CZ  
596  N  NH1 . ARG   A 90  ? 0.7890 0.7607 0.8875 -0.1790 -0.0067 -0.1650 246 ARG   A NH1 
597  N  NH2 . ARG   A 90  ? 0.8584 0.7755 0.9248 -0.1689 -0.0027 -0.1509 246 ARG   A NH2 
598  N  N   . ALA   A 91  ? 0.3418 0.4580 0.4828 -0.1328 -0.0641 -0.1880 247 ALA   A N   
599  C  CA  . ALA   A 91  ? 0.3236 0.4659 0.4736 -0.1200 -0.0724 -0.1861 247 ALA   A CA  
600  C  C   . ALA   A 91  ? 0.3859 0.5632 0.5521 -0.1191 -0.0779 -0.1959 247 ALA   A C   
601  O  O   . ALA   A 91  ? 0.3354 0.5342 0.5114 -0.1098 -0.0824 -0.1944 247 ALA   A O   
602  C  CB  . ALA   A 91  ? 0.3166 0.4545 0.4525 -0.1059 -0.0819 -0.1821 247 ALA   A CB  
603  N  N   . TYR   A 92  ? 0.3445 0.5281 0.5139 -0.1279 -0.0777 -0.2062 248 TYR   A N   
604  C  CA  . TYR   A 92  ? 0.3745 0.5926 0.5593 -0.1268 -0.0835 -0.2169 248 TYR   A CA  
605  C  C   . TYR   A 92  ? 0.3601 0.5860 0.5599 -0.1423 -0.0735 -0.2237 248 TYR   A C   
606  O  O   . TYR   A 92  ? 0.4126 0.6152 0.6068 -0.1561 -0.0639 -0.2239 248 TYR   A O   
607  C  CB  . TYR   A 92  ? 0.4376 0.6609 0.6153 -0.1246 -0.0918 -0.2249 248 TYR   A CB  
608  C  CG  . TYR   A 92  ? 0.3712 0.5927 0.5347 -0.1078 -0.1024 -0.2194 248 TYR   A CG  
609  C  CD1 . TYR   A 92  ? 0.3615 0.5535 0.5062 -0.1059 -0.1014 -0.2121 248 TYR   A CD1 
610  C  CD2 . TYR   A 92  ? 0.3519 0.6006 0.5196 -0.0934 -0.1133 -0.2216 248 TYR   A CD2 
611  C  CE1 . TYR   A 92  ? 0.3803 0.5706 0.5110 -0.0910 -0.1102 -0.2072 248 TYR   A CE1 
612  C  CE2 . TYR   A 92  ? 0.4021 0.6470 0.5543 -0.0779 -0.1224 -0.2158 248 TYR   A CE2 
613  C  CZ  . TYR   A 92  ? 0.3889 0.6048 0.5227 -0.0774 -0.1206 -0.2087 248 TYR   A CZ  
614  O  OH  . TYR   A 92  ? 0.4088 0.6206 0.5262 -0.0625 -0.1287 -0.2031 248 TYR   A OH  
615  N  N   . TYR   A 93  ? 0.3688 0.6268 0.5864 -0.1394 -0.0754 -0.2292 249 TYR   A N   
616  C  CA  . TYR   A 93  ? 0.3642 0.6324 0.5969 -0.1532 -0.0653 -0.2354 249 TYR   A CA  
617  C  C   . TYR   A 93  ? 0.3701 0.6785 0.6210 -0.1510 -0.0710 -0.2485 249 TYR   A C   
618  O  O   . TYR   A 93  ? 0.3624 0.6926 0.6159 -0.1354 -0.0825 -0.2498 249 TYR   A O   
619  C  CB  . TYR   A 93  ? 0.3501 0.6126 0.5869 -0.1531 -0.0575 -0.2265 249 TYR   A CB  
620  C  CG  . TYR   A 93  ? 0.3544 0.5782 0.5744 -0.1559 -0.0506 -0.2140 249 TYR   A CG  
621  C  CD1 . TYR   A 93  ? 0.3310 0.5413 0.5383 -0.1429 -0.0571 -0.2043 249 TYR   A CD1 
622  C  CD2 . TYR   A 93  ? 0.4629 0.6634 0.6789 -0.1709 -0.0375 -0.2121 249 TYR   A CD2 
623  C  CE1 . TYR   A 93  ? 0.3281 0.5045 0.5206 -0.1450 -0.0509 -0.1938 249 TYR   A CE1 
624  C  CE2 . TYR   A 93  ? 0.4504 0.6153 0.6500 -0.1720 -0.0315 -0.2008 249 TYR   A CE2 
625  C  CZ  . TYR   A 93  ? 0.3410 0.4949 0.5297 -0.1590 -0.0384 -0.1920 249 TYR   A CZ  
626  O  OH  . TYR   A 93  ? 0.4967 0.6164 0.6694 -0.1596 -0.0324 -0.1816 249 TYR   A OH  
627  N  N   . PHE   A 94  ? 0.3942 0.7114 0.6566 -0.1667 -0.0626 -0.2583 250 PHE   A N   
628  C  CA  . PHE   A 94  ? 0.4020 0.7585 0.6850 -0.1671 -0.0643 -0.2708 250 PHE   A CA  
629  C  C   . PHE   A 94  ? 0.4806 0.8461 0.7749 -0.1676 -0.0568 -0.2674 250 PHE   A C   
630  O  O   . PHE   A 94  ? 0.3801 0.7208 0.6689 -0.1771 -0.0455 -0.2596 250 PHE   A O   
631  C  CB  . PHE   A 94  ? 0.5370 0.8993 0.8271 -0.1850 -0.0582 -0.2842 250 PHE   A CB  
632  C  CG  . PHE   A 94  ? 0.5178 0.8719 0.7974 -0.1858 -0.0650 -0.2891 250 PHE   A CG  
633  C  CD1 . PHE   A 94  ? 0.6128 0.9913 0.8945 -0.1721 -0.0790 -0.2951 250 PHE   A CD1 
634  C  CD2 . PHE   A 94  ? 0.4803 0.8012 0.7467 -0.1996 -0.0574 -0.2876 250 PHE   A CD2 
635  C  CE1 . PHE   A 94  ? 0.5938 0.9646 0.8651 -0.1730 -0.0851 -0.2998 250 PHE   A CE1 
636  C  CE2 . PHE   A 94  ? 0.4758 0.7886 0.7321 -0.2003 -0.0636 -0.2925 250 PHE   A CE2 
637  C  CZ  . PHE   A 94  ? 0.5605 0.8987 0.8195 -0.1873 -0.0774 -0.2987 250 PHE   A CZ  
638  N  N   . VAL   A 95  ? 0.4428 0.8434 0.7519 -0.1567 -0.0633 -0.2734 251 VAL   A N   
639  C  CA  . VAL   A 95  ? 0.3652 0.7786 0.6857 -0.1545 -0.0578 -0.2712 251 VAL   A CA  
640  C  C   . VAL   A 95  ? 0.4415 0.8831 0.7812 -0.1668 -0.0510 -0.2859 251 VAL   A C   
641  O  O   . VAL   A 95  ? 0.5610 1.0355 0.9126 -0.1616 -0.0587 -0.2983 251 VAL   A O   
642  C  CB  . VAL   A 95  ? 0.3638 0.7949 0.6858 -0.1320 -0.0695 -0.2670 251 VAL   A CB  
643  C  CG1 . VAL   A 95  ? 0.3951 0.8435 0.7308 -0.1300 -0.0641 -0.2673 251 VAL   A CG1 
644  C  CG2 . VAL   A 95  ? 0.4036 0.8053 0.7064 -0.1215 -0.0743 -0.2520 251 VAL   A CG2 
645  N  N   . LYS   A 96  ? 0.4013 0.8269 0.7418 -0.1839 -0.0362 -0.2844 252 LYS   A N   
646  C  CA  . LYS   A 96  ? 0.4750 0.9254 0.8331 -0.1973 -0.0272 -0.2978 252 LYS   A CA  
647  C  C   . LYS   A 96  ? 0.4278 0.8864 0.7937 -0.1935 -0.0214 -0.2932 252 LYS   A C   
648  O  O   . LYS   A 96  ? 0.5373 0.9808 0.8941 -0.1812 -0.0247 -0.2801 252 LYS   A O   
649  C  CB  . LYS   A 96  ? 0.4390 0.8655 0.7913 -0.2201 -0.0137 -0.3004 252 LYS   A CB  
650  N  N   . PHE   A 97  ? 0.5531 1.0348 0.9349 -0.2038 -0.0129 -0.3041 253 PHE   A N   
651  C  CA  . PHE   A 97  ? 0.6599 1.1533 1.0502 -0.1993 -0.0078 -0.3013 253 PHE   A CA  
652  C  C   . PHE   A 97  ? 0.5882 1.0710 0.9804 -0.2204 0.0101  -0.3034 253 PHE   A C   
653  O  O   . PHE   A 97  ? 0.4327 0.9212 0.8300 -0.2368 0.0169  -0.3148 253 PHE   A O   
654  C  CB  . PHE   A 97  ? 0.4427 0.9819 0.8516 -0.1857 -0.0175 -0.3131 253 PHE   A CB  
655  C  CG  . PHE   A 97  ? 0.3780 0.9272 0.7831 -0.1623 -0.0350 -0.3098 253 PHE   A CG  
656  C  CD1 . PHE   A 97  ? 0.3857 0.9442 0.7893 -0.1581 -0.0455 -0.3167 253 PHE   A CD1 
657  C  CD2 . PHE   A 97  ? 0.3594 0.9085 0.7616 -0.1444 -0.0406 -0.3001 253 PHE   A CD2 
658  C  CE1 . PHE   A 97  ? 0.5585 1.1245 0.9563 -0.1363 -0.0610 -0.3133 253 PHE   A CE1 
659  C  CE2 . PHE   A 97  ? 0.5306 1.0866 0.9271 -0.1229 -0.0559 -0.2968 253 PHE   A CE2 
660  C  CZ  . PHE   A 97  ? 0.4746 1.0386 0.8683 -0.1188 -0.0660 -0.3032 253 PHE   A CZ  
661  N  N   . LYS   A 98  ? 0.5752 1.0410 0.9617 -0.2200 0.0179  -0.2925 254 LYS   A N   
662  C  CA  . LYS   A 98  ? 0.5576 1.0108 0.9432 -0.2389 0.0354  -0.2932 254 LYS   A CA  
663  C  C   . LYS   A 98  ? 0.8296 1.3169 1.2335 -0.2367 0.0390  -0.3011 254 LYS   A C   
664  O  O   . LYS   A 98  ? 0.7146 1.2416 1.1361 -0.2298 0.0309  -0.3145 254 LYS   A O   
665  C  CB  . LYS   A 98  ? 0.6754 1.0835 1.0399 -0.2410 0.0427  -0.2756 254 LYS   A CB  
666  N  N   . GLU   A 103 ? 0.4963 1.2963 1.0267 -0.1344 -0.0230 -0.3860 259 GLU   A N   
667  C  CA  . GLU   A 103 ? 0.6485 1.4042 1.1619 -0.1401 -0.0151 -0.3670 259 GLU   A CA  
668  C  C   . GLU   A 103 ? 0.4898 1.2138 0.9842 -0.1318 -0.0245 -0.3535 259 GLU   A C   
669  O  O   . GLU   A 103 ? 0.5996 1.2867 1.0786 -0.1337 -0.0203 -0.3374 259 GLU   A O   
670  C  CB  . GLU   A 103 ? 0.7486 1.4876 1.2623 -0.1682 0.0034  -0.3682 259 GLU   A CB  
671  C  CG  . GLU   A 103 ? 0.8163 1.5814 1.3465 -0.1784 0.0150  -0.3797 259 GLU   A CG  
672  C  CD  . GLU   A 103 ? 0.8095 1.5554 1.3372 -0.2065 0.0336  -0.3808 259 GLU   A CD  
673  O  OE1 . GLU   A 103 ? 0.9444 1.6568 1.4575 -0.2173 0.0368  -0.3729 259 GLU   A OE1 
674  O  OE2 . GLU   A 103 ? 0.7718 1.5350 1.3109 -0.2175 0.0450  -0.3895 259 GLU   A OE2 
675  N  N   . ASN   A 104 ? 0.5986 1.3379 1.0938 -0.1225 -0.0372 -0.3606 260 ASN   A N   
676  C  CA  . ASN   A 104 ? 0.5944 1.3071 1.0719 -0.1141 -0.0470 -0.3495 260 ASN   A CA  
677  C  C   . ASN   A 104 ? 0.4760 1.2120 0.9537 -0.0891 -0.0647 -0.3537 260 ASN   A C   
678  O  O   . ASN   A 104 ? 0.4721 1.2349 0.9585 -0.0883 -0.0710 -0.3679 260 ASN   A O   
679  C  CB  . ASN   A 104 ? 0.5785 1.2777 1.0524 -0.1334 -0.0423 -0.3532 260 ASN   A CB  
680  C  CG  . ASN   A 104 ? 0.5583 1.2298 1.0136 -0.1254 -0.0519 -0.3421 260 ASN   A CG  
681  O  OD1 . ASN   A 104 ? 0.4027 1.0628 0.8467 -0.1064 -0.0613 -0.3307 260 ASN   A OD1 
682  N  ND2 . ASN   A 104 ? 0.5396 1.1993 0.9909 -0.1403 -0.0492 -0.3455 260 ASN   A ND2 
683  N  N   . PRO   A 105 ? 0.4364 1.1618 0.9034 -0.0681 -0.0729 -0.3419 261 PRO   A N   
684  C  CA  . PRO   A 105 ? 0.3737 1.1175 0.8374 -0.0428 -0.0896 -0.3449 261 PRO   A CA  
685  C  C   . PRO   A 105 ? 0.4974 1.2303 0.9484 -0.0383 -0.0998 -0.3430 261 PRO   A C   
686  O  O   . PRO   A 105 ? 0.6199 1.3697 1.0678 -0.0188 -0.1134 -0.3475 261 PRO   A O   
687  C  CB  . PRO   A 105 ? 0.4798 1.2061 0.9318 -0.0247 -0.0931 -0.3303 261 PRO   A CB  
688  C  CG  . PRO   A 105 ? 0.5717 1.2613 1.0152 -0.0400 -0.0813 -0.3164 261 PRO   A CG  
689  C  CD  . PRO   A 105 ? 0.4422 1.1385 0.8991 -0.0663 -0.0669 -0.3257 261 PRO   A CD  
690  N  N   . LEU   A 106 ? 0.5472 1.2516 0.9895 -0.0548 -0.0938 -0.3366 262 LEU   A N   
691  C  CA  . LEU   A 106 ? 0.4199 1.1140 0.8507 -0.0528 -0.1024 -0.3358 262 LEU   A CA  
692  C  C   . LEU   A 106 ? 0.5457 1.2603 0.9891 -0.0692 -0.0995 -0.3521 262 LEU   A C   
693  O  O   . LEU   A 106 ? 0.5255 1.2290 0.9600 -0.0726 -0.1040 -0.3521 262 LEU   A O   
694  C  CB  . LEU   A 106 ? 0.3624 1.0119 0.7743 -0.0592 -0.0988 -0.3188 262 LEU   A CB  
695  C  CG  . LEU   A 106 ? 0.4602 1.0870 0.8572 -0.0424 -0.1029 -0.3023 262 LEU   A CG  
696  C  CD1 . LEU   A 106 ? 0.3329 0.9180 0.7125 -0.0500 -0.0991 -0.2872 262 LEU   A CD1 
697  C  CD2 . LEU   A 106 ? 0.4038 1.0428 0.7927 -0.0163 -0.1189 -0.3021 262 LEU   A CD2 
698  N  N   . SER   A 107 ? 0.5264 1.2703 0.9898 -0.0799 -0.0918 -0.3663 263 SER   A N   
699  C  CA  . SER   A 107 ? 0.4244 1.1891 0.9009 -0.0971 -0.0879 -0.3829 263 SER   A CA  
700  C  C   . SER   A 107 ? 0.4367 1.2249 0.9135 -0.0833 -0.1029 -0.3929 263 SER   A C   
701  O  O   . SER   A 107 ? 0.4504 1.2452 0.9310 -0.0957 -0.1025 -0.4029 263 SER   A O   
702  C  CB  . SER   A 107 ? 0.5669 1.3626 1.0652 -0.1085 -0.0777 -0.3970 263 SER   A CB  
703  O  OG  . SER   A 107 ? 0.4859 1.3116 0.9924 -0.0878 -0.0860 -0.4020 263 SER   A OG  
704  N  N   . GLN   A 108 ? 0.4713 1.2710 0.9428 -0.0572 -0.1162 -0.3903 264 GLN   A N   
705  C  CA  . GLN   A 108 ? 0.5050 1.3256 0.9741 -0.0417 -0.1311 -0.3989 264 GLN   A CA  
706  C  C   . GLN   A 108 ? 0.5476 1.3411 0.9994 -0.0443 -0.1359 -0.3918 264 GLN   A C   
707  O  O   . GLN   A 108 ? 0.4615 1.2720 0.9129 -0.0383 -0.1456 -0.4013 264 GLN   A O   
708  C  CB  . GLN   A 108 ? 0.5858 1.4151 1.0472 -0.0122 -0.1435 -0.3942 264 GLN   A CB  
709  C  CG  . GLN   A 108 ? 0.5977 1.4264 1.0641 -0.0083 -0.1371 -0.3885 264 GLN   A CG  
710  C  CD  . GLN   A 108 ? 0.6435 1.4777 1.1001 0.0213  -0.1494 -0.3834 264 GLN   A CD  
711  O  OE1 . GLN   A 108 ? 0.6150 1.4422 1.0555 0.0389  -0.1620 -0.3792 264 GLN   A OE1 
712  N  NE2 . GLN   A 108 ? 0.6114 1.4557 1.0758 0.0270  -0.1455 -0.3834 264 GLN   A NE2 
713  N  N   . PHE   A 109 ? 0.5970 1.3493 1.0342 -0.0526 -0.1294 -0.3755 265 PHE   A N   
714  C  CA  . PHE   A 109 ? 0.5374 1.2603 0.9554 -0.0527 -0.1343 -0.3666 265 PHE   A CA  
715  C  C   . PHE   A 109 ? 0.4911 1.1949 0.9100 -0.0792 -0.1229 -0.3681 265 PHE   A C   
716  O  O   . PHE   A 109 ? 0.5433 1.2167 0.9453 -0.0819 -0.1244 -0.3588 265 PHE   A O   
717  C  CB  . PHE   A 109 ? 0.4111 1.0996 0.8083 -0.0390 -0.1375 -0.3463 265 PHE   A CB  
718  C  CG  . PHE   A 109 ? 0.5279 1.2290 0.9212 -0.0132 -0.1475 -0.3430 265 PHE   A CG  
719  C  CD1 . PHE   A 109 ? 0.6628 1.3883 1.0545 0.0054  -0.1611 -0.3514 265 PHE   A CD1 
720  C  CD2 . PHE   A 109 ? 0.5344 1.2213 0.9243 -0.0070 -0.1435 -0.3313 265 PHE   A CD2 
721  C  CE1 . PHE   A 109 ? 0.6133 1.3471 0.9988 0.0298  -0.1701 -0.3479 265 PHE   A CE1 
722  C  CE2 . PHE   A 109 ? 0.5284 1.2241 0.9130 0.0169  -0.1524 -0.3280 265 PHE   A CE2 
723  C  CZ  . PHE   A 109 ? 0.5160 1.2343 0.8978 0.0356  -0.1657 -0.3361 265 PHE   A CZ  
724  N  N   . LEU   A 110 ? 0.4551 1.1744 0.8919 -0.0988 -0.1112 -0.3795 266 LEU   A N   
725  C  CA  . LEU   A 110 ? 0.4867 1.1856 0.9226 -0.1239 -0.0996 -0.3810 266 LEU   A CA  
726  C  C   . LEU   A 110 ? 0.5032 1.2150 0.9408 -0.1294 -0.1055 -0.3939 266 LEU   A C   
727  O  O   . LEU   A 110 ? 0.4801 1.2290 0.9293 -0.1208 -0.1141 -0.4083 266 LEU   A O   
728  C  CB  . LEU   A 110 ? 0.4544 1.1626 0.9066 -0.1439 -0.0839 -0.3885 266 LEU   A CB  
729  C  CG  . LEU   A 110 ? 0.4386 1.1315 0.8899 -0.1444 -0.0746 -0.3768 266 LEU   A CG  
730  C  CD1 . LEU   A 110 ? 0.4507 1.1619 0.9201 -0.1629 -0.0604 -0.3883 266 LEU   A CD1 
731  C  CD2 . LEU   A 110 ? 0.5907 1.2351 1.0220 -0.1505 -0.0687 -0.3587 266 LEU   A CD2 
732  N  N   . GLU   A 111 ? 0.5368 1.2168 0.9619 -0.1433 -0.1009 -0.3888 267 GLU   A N   
733  C  CA  . GLU   A 111 ? 0.5091 1.1949 0.9354 -0.1545 -0.1028 -0.4008 267 GLU   A CA  
734  C  C   . GLU   A 111 ? 0.5875 1.2508 1.0151 -0.1817 -0.0859 -0.4017 267 GLU   A C   
735  O  O   . GLU   A 111 ? 0.5923 1.2151 1.0028 -0.1889 -0.0809 -0.3893 267 GLU   A O   
736  C  CB  . GLU   A 111 ? 0.5740 1.2390 0.9799 -0.1431 -0.1143 -0.3929 267 GLU   A CB  
737  N  N   . GLY   A 112 ? 0.5138 1.2029 0.9607 -0.1964 -0.0769 -0.4163 268 GLY   A N   
738  C  CA  . GLY   A 112 ? 0.5228 1.1901 0.9704 -0.2208 -0.0593 -0.4156 268 GLY   A CA  
739  C  C   . GLY   A 112 ? 0.5047 1.1541 0.9487 -0.2187 -0.0510 -0.4015 268 GLY   A C   
740  O  O   . GLY   A 112 ? 0.6032 1.2790 1.0596 -0.2088 -0.0525 -0.4041 268 GLY   A O   
741  N  N   . GLU   A 113 ? 0.5821 1.1867 1.0086 -0.2272 -0.0426 -0.3868 269 GLU   A N   
742  C  CA  . GLU   A 113 ? 0.7286 1.3127 1.1494 -0.2250 -0.0349 -0.3724 269 GLU   A CA  
743  C  C   . GLU   A 113 ? 0.5688 1.1289 0.9724 -0.2061 -0.0442 -0.3547 269 GLU   A C   
744  O  O   . GLU   A 113 ? 0.6171 1.1606 1.0156 -0.2023 -0.0393 -0.3423 269 GLU   A O   
745  C  CB  . GLU   A 113 ? 0.7946 1.3447 1.2073 -0.2478 -0.0174 -0.3679 269 GLU   A CB  
746  C  CG  . GLU   A 113 ? 0.7069 1.2740 1.1332 -0.2695 -0.0062 -0.3846 269 GLU   A CG  
747  C  CD  . GLU   A 113 ? 0.8966 1.4282 1.3088 -0.2887 0.0028  -0.3838 269 GLU   A CD  
748  O  OE1 . GLU   A 113 ? 0.8221 1.3393 1.2229 -0.2845 -0.0058 -0.3817 269 GLU   A OE1 
749  O  OE2 . GLU   A 113 ? 1.0887 1.6053 1.4997 -0.3077 0.0187  -0.3849 269 GLU   A OE2 
750  N  N   . ILE   A 114 ? 0.5688 1.1268 0.9632 -0.1943 -0.0573 -0.3536 270 ILE   A N   
751  C  CA  . ILE   A 114 ? 0.4973 1.0305 0.8735 -0.1778 -0.0657 -0.3374 270 ILE   A CA  
752  C  C   . ILE   A 114 ? 0.5402 1.1018 0.9217 -0.1540 -0.0793 -0.3378 270 ILE   A C   
753  O  O   . ILE   A 114 ? 0.4974 1.0929 0.8899 -0.1475 -0.0877 -0.3511 270 ILE   A O   
754  C  CB  . ILE   A 114 ? 0.6058 1.1149 0.9654 -0.1798 -0.0709 -0.3349 270 ILE   A CB  
755  C  CG1 . ILE   A 114 ? 0.6661 1.1296 1.0095 -0.1933 -0.0597 -0.3232 270 ILE   A CG1 
756  C  CG2 . ILE   A 114 ? 0.6859 1.1956 1.0340 -0.1571 -0.0865 -0.3280 270 ILE   A CG2 
757  C  CD1 . ILE   A 114 ? 0.4854 0.9421 0.8359 -0.2150 -0.0432 -0.3277 270 ILE   A CD1 
758  N  N   . LEU   A 115 ? 0.4294 0.9773 0.8028 -0.1408 -0.0812 -0.3238 271 LEU   A N   
759  C  CA  . LEU   A 115 ? 0.4988 1.0645 0.8709 -0.1164 -0.0948 -0.3213 271 LEU   A CA  
760  C  C   . LEU   A 115 ? 0.4160 0.9756 0.7739 -0.1057 -0.1075 -0.3202 271 LEU   A C   
761  O  O   . LEU   A 115 ? 0.5263 1.0530 0.8668 -0.1079 -0.1072 -0.3097 271 LEU   A O   
762  C  CB  . LEU   A 115 ? 0.3740 0.9202 0.7377 -0.1064 -0.0932 -0.3054 271 LEU   A CB  
763  C  CG  . LEU   A 115 ? 0.5888 1.1531 0.9539 -0.0830 -0.1030 -0.3024 271 LEU   A CG  
764  C  CD1 . LEU   A 115 ? 0.3858 0.9229 0.7397 -0.0768 -0.1001 -0.2856 271 LEU   A CD1 
765  C  CD2 . LEU   A 115 ? 0.6447 1.2199 1.0010 -0.0638 -0.1189 -0.3044 271 LEU   A CD2 
766  N  N   . SER   A 116 ? 0.4775 1.0688 0.8419 -0.0936 -0.1186 -0.3312 272 SER   A N   
767  C  CA  . SER   A 116 ? 0.5004 1.0881 0.8506 -0.0821 -0.1311 -0.3308 272 SER   A CA  
768  C  C   . SER   A 116 ? 0.5106 1.0864 0.8446 -0.0590 -0.1407 -0.3170 272 SER   A C   
769  O  O   . SER   A 116 ? 0.5195 1.1157 0.8586 -0.0427 -0.1464 -0.3178 272 SER   A O   
770  C  CB  . SER   A 116 ? 0.4862 1.1123 0.8488 -0.0781 -0.1392 -0.3484 272 SER   A CB  
771  O  OG  . SER   A 116 ? 0.4581 1.0843 0.8059 -0.0609 -0.1532 -0.3469 272 SER   A OG  
772  N  N   . ALA   A 117 ? 0.4075 0.9499 0.7211 -0.0573 -0.1423 -0.3046 273 ALA   A N   
773  C  CA  . ALA   A 117 ? 0.4693 0.9995 0.7651 -0.0357 -0.1518 -0.2922 273 ALA   A CA  
774  C  C   . ALA   A 117 ? 0.5619 1.1156 0.8538 -0.0168 -0.1659 -0.2991 273 ALA   A C   
775  O  O   . ALA   A 117 ? 0.5434 1.0999 0.8271 0.0037  -0.1736 -0.2928 273 ALA   A O   
776  C  CB  . ALA   A 117 ? 0.4131 0.9051 0.6878 -0.0389 -0.1506 -0.2797 273 ALA   A CB  
777  N  N   . SER   A 118 ? 0.4908 1.0610 0.7880 -0.0231 -0.1692 -0.3122 274 SER   A N   
778  C  CA  . SER   A 118 ? 0.5064 1.0991 0.7992 -0.0054 -0.1828 -0.3195 274 SER   A CA  
779  C  C   . SER   A 118 ? 0.4400 1.0653 0.7464 0.0085  -0.1871 -0.3265 274 SER   A C   
780  O  O   . SER   A 118 ? 0.5300 1.1582 0.8245 0.0312  -0.1971 -0.3216 274 SER   A O   
781  C  CB  . SER   A 118 ? 0.5401 1.1463 0.8388 -0.0175 -0.1843 -0.3339 274 SER   A CB  
782  O  OG  . SER   A 118 ? 0.7283 1.3402 1.0458 -0.0413 -0.1722 -0.3426 274 SER   A OG  
783  N  N   . LYS   A 119 ? 0.4494 1.0986 0.7796 -0.0046 -0.1792 -0.3381 275 LYS   A N   
784  C  CA  . LYS   A 119 ? 0.4474 1.1307 0.7920 0.0079  -0.1830 -0.3469 275 LYS   A CA  
785  C  C   . LYS   A 119 ? 0.4333 1.1038 0.7708 0.0222  -0.1826 -0.3334 275 LYS   A C   
786  O  O   . LYS   A 119 ? 0.6001 1.2846 0.9335 0.0441  -0.1919 -0.3337 275 LYS   A O   
787  C  CB  . LYS   A 119 ? 0.4521 1.1622 0.8234 -0.0117 -0.1731 -0.3622 275 LYS   A CB  
788  N  N   . MET   A 120 ? 0.5943 1.2375 0.9298 0.0102  -0.1719 -0.3219 276 MET   A N   
789  C  CA  . MET   A 120 ? 0.4749 1.1043 0.8038 0.0221  -0.1708 -0.3090 276 MET   A CA  
790  C  C   . MET   A 120 ? 0.4675 1.0791 0.7715 0.0452  -0.1823 -0.2972 276 MET   A C   
791  O  O   . MET   A 120 ? 0.6631 1.2804 0.9625 0.0645  -0.1879 -0.2938 276 MET   A O   
792  C  CB  . MET   A 120 ? 0.4814 1.0820 0.8101 0.0045  -0.1577 -0.2984 276 MET   A CB  
793  C  CG  . MET   A 120 ? 0.4547 1.0441 0.7805 0.0137  -0.1548 -0.2870 276 MET   A CG  
794  S  SD  . MET   A 120 ? 0.4475 1.0125 0.7793 -0.0093 -0.1379 -0.2790 276 MET   A SD  
795  C  CE  . MET   A 120 ? 0.3409 0.9022 0.6711 0.0061  -0.1374 -0.2688 276 MET   A CE  
796  N  N   . LEU   A 121 ? 0.5093 1.0984 0.7958 0.0438  -0.1857 -0.2912 277 LEU   A N   
797  C  CA  . LEU   A 121 ? 0.6021 1.1724 0.8628 0.0648  -0.1958 -0.2798 277 LEU   A CA  
798  C  C   . LEU   A 121 ? 0.5926 1.1877 0.8497 0.0849  -0.2084 -0.2885 277 LEU   A C   
799  O  O   . LEU   A 121 ? 0.6296 1.2157 0.8692 0.1065  -0.2158 -0.2802 277 LEU   A O   
800  C  CB  . LEU   A 121 ? 0.6246 1.1662 0.8678 0.0573  -0.1957 -0.2724 277 LEU   A CB  
801  C  CG  . LEU   A 121 ? 0.4504 0.9587 0.6871 0.0451  -0.1861 -0.2592 277 LEU   A CG  
802  C  CD1 . LEU   A 121 ? 0.5138 0.9977 0.7330 0.0393  -0.1872 -0.2543 277 LEU   A CD1 
803  C  CD2 . LEU   A 121 ? 0.5047 0.9965 0.7296 0.0602  -0.1870 -0.2454 277 LEU   A CD2 
804  N  N   . SER   A 122 ? 0.6581 1.2832 0.9304 0.0785  -0.2108 -0.3051 278 SER   A N   
805  C  CA  . SER   A 122 ? 0.4951 1.1473 0.7659 0.0978  -0.2228 -0.3150 278 SER   A CA  
806  C  C   . SER   A 122 ? 0.5386 1.2063 0.8150 0.1140  -0.2248 -0.3157 278 SER   A C   
807  O  O   . SER   A 122 ? 0.5581 1.2234 0.8174 0.1379  -0.2346 -0.3113 278 SER   A O   
808  C  CB  . SER   A 122 ? 0.5012 1.1863 0.7919 0.0853  -0.2233 -0.3344 278 SER   A CB  
809  O  OG  . SER   A 122 ? 0.7468 1.4172 1.0291 0.0735  -0.2233 -0.3343 278 SER   A OG  
810  N  N   . LYS   A 123 ? 0.4797 1.1617 0.7786 0.1013  -0.2152 -0.3209 279 LYS   A N   
811  C  CA  . LYS   A 123 ? 0.4928 1.1896 0.7981 0.1155  -0.2162 -0.3220 279 LYS   A CA  
812  C  C   . LYS   A 123 ? 0.6234 1.2865 0.9067 0.1300  -0.2170 -0.3032 279 LYS   A C   
813  O  O   . LYS   A 123 ? 0.5352 1.2019 0.8087 0.1524  -0.2243 -0.3011 279 LYS   A O   
814  C  CB  . LYS   A 123 ? 0.5677 1.2842 0.9006 0.0966  -0.2043 -0.3309 279 LYS   A CB  
815  N  N   . PHE   A 124 ? 0.6871 1.3170 0.9621 0.1177  -0.2094 -0.2897 280 PHE   A N   
816  C  CA  . PHE   A 124 ? 0.4621 1.0588 0.7162 0.1295  -0.2095 -0.2718 280 PHE   A CA  
817  C  C   . PHE   A 124 ? 0.5221 1.1056 0.7485 0.1535  -0.2216 -0.2652 280 PHE   A C   
818  O  O   . PHE   A 124 ? 0.5602 1.1346 0.7731 0.1727  -0.2256 -0.2580 280 PHE   A O   
819  C  CB  . PHE   A 124 ? 0.6903 1.2558 0.9397 0.1113  -0.2004 -0.2605 280 PHE   A CB  
820  C  CG  . PHE   A 124 ? 0.5069 1.0384 0.7365 0.1207  -0.1992 -0.2426 280 PHE   A CG  
821  C  CD1 . PHE   A 124 ? 0.5907 1.1192 0.8282 0.1202  -0.1926 -0.2379 280 PHE   A CD1 
822  C  CD2 . PHE   A 124 ? 0.6652 1.1675 0.8681 0.1289  -0.2042 -0.2309 280 PHE   A CD2 
823  C  CE1 . PHE   A 124 ? 0.5805 1.0778 0.7999 0.1283  -0.1914 -0.2220 280 PHE   A CE1 
824  C  CE2 . PHE   A 124 ? 0.5895 1.0605 0.7740 0.1366  -0.2026 -0.2149 280 PHE   A CE2 
825  C  CZ  . PHE   A 124 ? 0.5992 1.0677 0.7922 0.1363  -0.1963 -0.2106 280 PHE   A CZ  
826  N  N   . ARG   A 125 ? 0.5503 1.1315 0.7668 0.1525  -0.2271 -0.2677 281 ARG   A N   
827  C  CA  . ARG   A 125 ? 0.6243 1.1936 0.8136 0.1746  -0.2383 -0.2623 281 ARG   A CA  
828  C  C   . ARG   A 125 ? 0.7923 1.3890 0.9837 0.1953  -0.2473 -0.2722 281 ARG   A C   
829  O  O   . ARG   A 125 ? 0.8949 1.4769 1.0638 0.2176  -0.2538 -0.2641 281 ARG   A O   
830  C  CB  . ARG   A 125 ? 0.5978 1.1648 0.7798 0.1674  -0.2420 -0.2658 281 ARG   A CB  
831  C  CG  . ARG   A 125 ? 0.7182 1.2497 0.8672 0.1778  -0.2462 -0.2512 281 ARG   A CG  
832  C  CD  . ARG   A 125 ? 0.6996 1.2305 0.8450 0.1671  -0.2482 -0.2559 281 ARG   A CD  
833  N  NE  . ARG   A 125 ? 0.8458 1.3946 1.0185 0.1426  -0.2406 -0.2671 281 ARG   A NE  
834  C  CZ  . ARG   A 125 ? 0.8105 1.3413 0.9888 0.1229  -0.2305 -0.2614 281 ARG   A CZ  
835  N  NH1 . ARG   A 125 ? 0.6821 1.1786 0.8424 0.1241  -0.2269 -0.2453 281 ARG   A NH1 
836  N  NH2 . ARG   A 125 ? 0.8767 1.4235 1.0784 0.1014  -0.2235 -0.2724 281 ARG   A NH2 
837  N  N   . LYS   A 126 ? 0.7269 1.3628 0.9448 0.1880  -0.2472 -0.2900 282 LYS   A N   
838  C  CA  . LYS   A 126 ? 0.5858 1.2525 0.8085 0.2075  -0.2557 -0.3016 282 LYS   A CA  
839  C  C   . LYS   A 126 ? 0.7347 1.3885 0.9476 0.2244  -0.2555 -0.2922 282 LYS   A C   
840  O  O   . LYS   A 126 ? 0.7543 1.4016 0.9456 0.2488  -0.2649 -0.2888 282 LYS   A O   
841  C  CB  . LYS   A 126 ? 0.6583 1.3687 0.9149 0.1937  -0.2522 -0.3214 282 LYS   A CB  
842  N  N   . ILE   A 127 ? 0.6889 1.3384 0.9161 0.2119  -0.2452 -0.2883 283 ILE   A N   
843  C  CA  . ILE   A 127 ? 0.6235 1.2626 0.8429 0.2274  -0.2447 -0.2806 283 ILE   A CA  
844  C  C   . ILE   A 127 ? 0.6776 1.2746 0.8612 0.2438  -0.2492 -0.2626 283 ILE   A C   
845  O  O   . ILE   A 127 ? 0.6891 1.2825 0.8545 0.2678  -0.2573 -0.2608 283 ILE   A O   
846  C  CB  . ILE   A 127 ? 0.5667 1.2033 0.8049 0.2098  -0.2321 -0.2775 283 ILE   A CB  
847  C  CG1 . ILE   A 127 ? 0.5411 1.2028 0.8089 0.1835  -0.2240 -0.2901 283 ILE   A CG1 
848  C  CG2 . ILE   A 127 ? 0.4953 1.1428 0.7380 0.2241  -0.2323 -0.2793 283 ILE   A CG2 
849  C  CD1 . ILE   A 127 ? 0.5941 1.3015 0.8871 0.1835  -0.2251 -0.3097 283 ILE   A CD1 
850  N  N   . ILE   A 128 ? 0.6710 1.2370 0.8442 0.2311  -0.2437 -0.2501 284 ILE   A N   
851  C  CA  . ILE   A 128 ? 0.8076 1.3323 0.9456 0.2448  -0.2471 -0.2329 284 ILE   A CA  
852  C  C   . ILE   A 128 ? 0.6932 1.2231 0.8112 0.2692  -0.2593 -0.2367 284 ILE   A C   
853  O  O   . ILE   A 128 ? 0.7428 1.2475 0.8348 0.2884  -0.2625 -0.2259 284 ILE   A O   
854  C  CB  . ILE   A 128 ? 0.8012 1.3017 0.9307 0.2286  -0.2429 -0.2244 284 ILE   A CB  
855  C  CG1 . ILE   A 128 ? 0.7072 1.2050 0.8574 0.2040  -0.2311 -0.2226 284 ILE   A CG1 
856  C  CG2 . ILE   A 128 ? 0.8996 1.3581 0.9926 0.2419  -0.2454 -0.2072 284 ILE   A CG2 
857  C  CD1 . ILE   A 128 ? 0.6587 1.1440 0.8114 0.2053  -0.2245 -0.2143 284 ILE   A CD1 
858  N  N   . MET   A 142 ? 0.7952 1.1223 0.7043 0.3247  -0.2774 -0.1644 298 MET   A N   
859  C  CA  . MET   A 142 ? 0.8458 1.1975 0.7898 0.3003  -0.2723 -0.1729 298 MET   A CA  
860  C  C   . MET   A 142 ? 0.9441 1.3016 0.8865 0.2906  -0.2749 -0.1775 298 MET   A C   
861  O  O   . MET   A 142 ? 0.8676 1.2217 0.7884 0.3051  -0.2826 -0.1783 298 MET   A O   
862  C  CB  . MET   A 142 ? 0.7094 1.1041 0.6877 0.2986  -0.2745 -0.1893 298 MET   A CB  
863  C  CG  . MET   A 142 ? 0.8633 1.2764 0.8756 0.2736  -0.2665 -0.1954 298 MET   A CG  
864  S  SD  . MET   A 142 ? 1.1627 1.6300 1.2112 0.2658  -0.2709 -0.2188 298 MET   A SD  
865  C  CE  . MET   A 142 ? 0.8007 1.2671 0.8477 0.2497  -0.2714 -0.2220 298 MET   A CE  
866  N  N   . LYS   A 143 ? 0.8910 1.2559 0.8543 0.2676  -0.2687 -0.1806 299 LYS   A N   
867  C  CA  . LYS   A 143 ? 0.9301 1.2986 0.8919 0.2567  -0.2703 -0.1850 299 LYS   A CA  
868  C  C   . LYS   A 143 ? 0.9675 1.3548 0.9615 0.2314  -0.2637 -0.1936 299 LYS   A C   
869  O  O   . LYS   A 143 ? 0.9583 1.3489 0.9711 0.2225  -0.2570 -0.1927 299 LYS   A O   
870  C  CB  . LYS   A 143 ? 0.8101 1.1385 0.7382 0.2581  -0.2677 -0.1697 299 LYS   A CB  
871  N  N   . ARG   A 144 ? 0.9102 1.3079 0.9091 0.2204  -0.2654 -0.2015 300 ARG   A N   
872  C  CA  . ARG   A 144 ? 0.7574 1.1708 0.7841 0.1966  -0.2592 -0.2103 300 ARG   A CA  
873  C  C   . ARG   A 144 ? 0.8205 1.2131 0.8529 0.1818  -0.2483 -0.2004 300 ARG   A C   
874  O  O   . ARG   A 144 ? 1.0066 1.4004 1.0536 0.1615  -0.2420 -0.2039 300 ARG   A O   
875  C  CB  . ARG   A 144 ? 0.6950 1.1081 0.7149 0.1884  -0.2616 -0.2152 300 ARG   A CB  
876  N  N   . GLY   A 148 ? 0.5546 0.9520 0.6833 0.0584  -0.2033 -0.2265 304 GLY   A N   
877  C  CA  . GLY   A 148 ? 0.5575 0.9591 0.7076 0.0447  -0.1937 -0.2277 304 GLY   A CA  
878  C  C   . GLY   A 148 ? 0.5188 0.9086 0.6654 0.0536  -0.1913 -0.2156 304 GLY   A C   
879  O  O   . GLY   A 148 ? 0.4808 0.8873 0.6349 0.0646  -0.1941 -0.2171 304 GLY   A O   
880  N  N   . SER   A 149 ? 0.4992 0.8601 0.6337 0.0491  -0.1860 -0.2042 305 SER   A N   
881  C  CA  . SER   A 149 ? 0.5684 0.9154 0.6984 0.0563  -0.1832 -0.1923 305 SER   A CA  
882  C  C   . SER   A 149 ? 0.8044 1.1282 0.9051 0.0725  -0.1889 -0.1799 305 SER   A C   
883  O  O   . SER   A 149 ? 0.9613 1.2869 1.0523 0.0903  -0.1946 -0.1753 305 SER   A O   
884  C  CB  . SER   A 149 ? 0.4534 0.7852 0.5926 0.0388  -0.1721 -0.1886 305 SER   A CB  
885  O  OG  . SER   A 149 ? 0.5077 0.8586 0.6724 0.0261  -0.1655 -0.1974 305 SER   A OG  
886  N  N   . ALA   A 151 ? 0.5990 0.9716 0.7032 0.1147  -0.2072 -0.1894 307 ALA   A N   
887  C  CA  . ALA   A 151 ? 0.7720 1.1778 0.8917 0.1190  -0.2125 -0.2035 307 ALA   A CA  
888  C  C   . ALA   A 151 ? 0.8367 1.2442 0.9383 0.1437  -0.2223 -0.2009 307 ALA   A C   
889  O  O   . ALA   A 151 ? 0.7782 1.2050 0.8798 0.1509  -0.2298 -0.2105 307 ALA   A O   
890  C  CB  . ALA   A 151 ? 0.5301 0.9580 0.6788 0.1090  -0.2061 -0.2112 307 ALA   A CB  
891  N  N   . VAL   A 152 ? 0.7035 1.0900 0.7882 0.1573  -0.2224 -0.1882 308 VAL   A N   
892  C  CA  . VAL   A 152 ? 0.8056 1.1902 0.8699 0.1809  -0.2313 -0.1858 308 VAL   A CA  
893  C  C   . VAL   A 152 ? 0.8842 1.2299 0.9167 0.1918  -0.2307 -0.1683 308 VAL   A C   
894  O  O   . VAL   A 152 ? 0.8946 1.2213 0.9263 0.1863  -0.2237 -0.1587 308 VAL   A O   
895  C  CB  . VAL   A 152 ? 0.6769 1.0862 0.7567 0.1914  -0.2337 -0.1933 308 VAL   A CB  
896  N  N   . THR   A 153 ? 0.9164 1.2499 0.9220 0.2071  -0.2376 -0.1644 309 THR   A N   
897  C  CA  . THR   A 153 ? 0.7695 1.0651 0.7413 0.2191  -0.2370 -0.1482 309 THR   A CA  
898  C  C   . THR   A 153 ? 0.7718 1.0657 0.7276 0.2425  -0.2434 -0.1466 309 THR   A C   
899  O  O   . THR   A 153 ? 0.9295 1.2355 0.8773 0.2543  -0.2517 -0.1532 309 THR   A O   
900  C  CB  . THR   A 153 ? 0.8292 1.1055 0.7773 0.2175  -0.2383 -0.1431 309 THR   A CB  
901  O  OG1 . THR   A 153 ? 0.9107 1.1887 0.8729 0.1963  -0.2325 -0.1456 309 THR   A OG1 
902  C  CG2 . THR   A 153 ? 0.8169 1.0531 0.7308 0.2275  -0.2355 -0.1261 309 THR   A CG2 
903  N  N   . LEU   A 154 ? 0.6729 0.9504 0.6228 0.2495  -0.2398 -0.1380 310 LEU   A N   
904  C  CA  . LEU   A 154 ? 0.7832 1.0544 0.7163 0.2718  -0.2447 -0.1355 310 LEU   A CA  
905  C  C   . LEU   A 154 ? 0.7793 1.0057 0.6732 0.2818  -0.2425 -0.1188 310 LEU   A C   
906  O  O   . LEU   A 154 ? 0.7563 0.9574 0.6422 0.2707  -0.2349 -0.1081 310 LEU   A O   
907  C  CB  . LEU   A 154 ? 0.7888 1.0716 0.7414 0.2729  -0.2415 -0.1379 310 LEU   A CB  
908  C  CG  . LEU   A 154 ? 0.7842 1.1008 0.7767 0.2550  -0.2376 -0.1497 310 LEU   A CG  
909  C  CD1 . LEU   A 154 ? 0.7842 1.1082 0.7896 0.2600  -0.2348 -0.1506 310 LEU   A CD1 
910  C  CD2 . LEU   A 154 ? 0.9601 1.3151 0.9726 0.2520  -0.2438 -0.1666 310 LEU   A CD2 
911  N  N   . LEU   A 155 ? 1.0054 1.2206 0.8738 0.3027  -0.2485 -0.1164 311 LEU   A N   
912  C  CA  . LEU   A 155 ? 0.9810 1.1503 0.8093 0.3126  -0.2453 -0.1001 311 LEU   A CA  
913  C  C   . LEU   A 155 ? 0.9028 1.0583 0.7201 0.3287  -0.2450 -0.0956 311 LEU   A C   
914  O  O   . LEU   A 155 ? 0.9080 1.0895 0.7369 0.3409  -0.2518 -0.1062 311 LEU   A O   
915  C  CB  . LEU   A 155 ? 0.8508 1.0081 0.6506 0.3227  -0.2508 -0.0982 311 LEU   A CB  
916  C  CG  . LEU   A 155 ? 1.0608 1.1695 0.8186 0.3303  -0.2459 -0.0815 311 LEU   A CG  
917  C  CD1 . LEU   A 155 ? 0.9982 1.0925 0.7403 0.3208  -0.2436 -0.0765 311 LEU   A CD1 
918  C  CD2 . LEU   A 155 ? 0.9396 1.0359 0.6705 0.3546  -0.2520 -0.0801 311 LEU   A CD2 
919  N  N   . ILE   A 156 ? 0.9547 1.0713 0.7504 0.3284  -0.2372 -0.0812 312 ILE   A N   
920  C  CA  . ILE   A 156 ? 0.8690 0.9712 0.6558 0.3416  -0.2357 -0.0772 312 ILE   A CA  
921  C  C   . ILE   A 156 ? 1.0029 1.0537 0.7527 0.3438  -0.2279 -0.0601 312 ILE   A C   
922  O  O   . ILE   A 156 ? 1.2927 1.3241 1.0256 0.3363  -0.2247 -0.0530 312 ILE   A O   
923  C  CB  . ILE   A 156 ? 0.7590 0.8829 0.5802 0.3305  -0.2316 -0.0823 312 ILE   A CB  
924  N  N   . GLU   A 158 ? 1.0123 0.9924 0.6608 0.3748  -0.2339 -0.0433 314 GLU   A N   
925  C  CA  . GLU   A 158 ? 0.9731 0.9497 0.6071 0.3716  -0.2358 -0.0422 314 GLU   A CA  
926  C  C   . GLU   A 158 ? 1.0511 1.0210 0.6933 0.3485  -0.2271 -0.0366 314 GLU   A C   
927  O  O   . GLU   A 158 ? 1.1721 1.1546 0.8171 0.3417  -0.2298 -0.0403 314 GLU   A O   
928  C  CB  . GLU   A 158 ? 1.1673 1.1014 0.7546 0.3851  -0.2338 -0.0312 314 GLU   A CB  
929  N  N   . LYS   A 159 ? 1.0284 0.9800 0.6741 0.3371  -0.2175 -0.0286 315 LYS   A N   
930  C  CA  . LYS   A 159 ? 1.1293 1.0707 0.7785 0.3163  -0.2087 -0.0224 315 LYS   A CA  
931  C  C   . LYS   A 159 ? 1.1296 1.1014 0.8194 0.3001  -0.2077 -0.0297 315 LYS   A C   
932  O  O   . LYS   A 159 ? 1.0956 1.0711 0.7935 0.2842  -0.2040 -0.0292 315 LYS   A O   
933  C  CB  . LYS   A 159 ? 1.1106 1.0063 0.7329 0.3130  -0.1971 -0.0076 315 LYS   A CB  
934  N  N   . ILE   A 160 ? 1.0535 1.0456 0.7668 0.3040  -0.2104 -0.0362 316 ILE   A N   
935  C  CA  . ILE   A 160 ? 0.9585 0.9746 0.7081 0.2875  -0.2075 -0.0415 316 ILE   A CA  
936  C  C   . ILE   A 160 ? 0.9505 1.0113 0.7317 0.2822  -0.2151 -0.0567 316 ILE   A C   
937  O  O   . ILE   A 160 ? 0.9586 1.0419 0.7459 0.2949  -0.2235 -0.0662 316 ILE   A O   
938  C  CB  . ILE   A 160 ? 0.8015 0.8168 0.5623 0.2913  -0.2049 -0.0408 316 ILE   A CB  
939  N  N   . SER   A 161 ? 0.9726 1.0449 0.7724 0.2638  -0.2119 -0.0593 317 SER   A N   
940  C  CA  . SER   A 161 ? 0.9884 1.1017 0.8206 0.2555  -0.2172 -0.0741 317 SER   A CA  
941  C  C   . SER   A 161 ? 0.8903 1.0206 0.7551 0.2409  -0.2124 -0.0781 317 SER   A C   
942  O  O   . SER   A 161 ? 0.8341 0.9435 0.6957 0.2326  -0.2047 -0.0690 317 SER   A O   
943  C  CB  . SER   A 161 ? 0.9446 1.0600 0.7719 0.2461  -0.2182 -0.0762 317 SER   A CB  
944  O  OG  . SER   A 161 ? 1.1010 1.1890 0.8919 0.2564  -0.2189 -0.0677 317 SER   A OG  
945  N  N   . VAL   A 162 ? 0.7927 0.9609 0.6885 0.2379  -0.2167 -0.0922 318 VAL   A N   
946  C  CA  . VAL   A 162 ? 0.7740 0.9621 0.7026 0.2246  -0.2123 -0.0978 318 VAL   A CA  
947  C  C   . VAL   A 162 ? 0.7778 1.0003 0.7342 0.2115  -0.2147 -0.1123 318 VAL   A C   
948  O  O   . VAL   A 162 ? 0.7768 1.0260 0.7436 0.2180  -0.2212 -0.1236 318 VAL   A O   
949  C  CB  . VAL   A 162 ? 0.7835 0.9826 0.7227 0.2353  -0.2132 -0.1007 318 VAL   A CB  
950  C  CG1 . VAL   A 162 ? 0.6117 0.8288 0.5832 0.2204  -0.2073 -0.1055 318 VAL   A CG1 
951  C  CG2 . VAL   A 162 ? 0.9060 1.0694 0.8151 0.2497  -0.2112 -0.0874 318 VAL   A CG2 
952  N  N   . ASP   A 163 ? 0.6864 0.9079 0.6544 0.1929  -0.2091 -0.1123 319 ASP   A N   
953  C  CA  . ASP   A 163 ? 0.7343 0.9853 0.7297 0.1777  -0.2093 -0.1259 319 ASP   A CA  
954  C  C   . ASP   A 163 ? 0.5673 0.8380 0.5938 0.1675  -0.2042 -0.1320 319 ASP   A C   
955  O  O   . ASP   A 163 ? 0.6897 0.9457 0.7187 0.1609  -0.1975 -0.1245 319 ASP   A O   
956  C  CB  . ASP   A 163 ? 0.7051 0.9432 0.6948 0.1632  -0.2059 -0.1236 319 ASP   A CB  
957  C  CG  . ASP   A 163 ? 0.9338 1.1508 0.8912 0.1727  -0.2097 -0.1168 319 ASP   A CG  
958  O  OD1 . ASP   A 163 ? 0.9742 1.1630 0.9056 0.1837  -0.2085 -0.1041 319 ASP   A OD1 
959  O  OD2 . ASP   A 163 ? 0.8983 1.1257 0.8556 0.1689  -0.2133 -0.1242 319 ASP   A OD2 
960  N  N   . ILE   A 164 ? 0.8073 1.1111 0.8568 0.1661  -0.2070 -0.1457 320 ILE   A N   
961  C  CA  . ILE   A 164 ? 0.5232 0.8487 0.6030 0.1551  -0.2014 -0.1532 320 ILE   A CA  
962  C  C   . ILE   A 164 ? 0.5033 0.8474 0.6051 0.1346  -0.1979 -0.1643 320 ILE   A C   
963  O  O   . ILE   A 164 ? 0.6848 1.0444 0.7882 0.1340  -0.2030 -0.1736 320 ILE   A O   
964  C  CB  . ILE   A 164 ? 0.5901 0.9392 0.6800 0.1684  -0.2056 -0.1607 320 ILE   A CB  
965  C  CG1 . ILE   A 164 ? 0.6463 0.9733 0.7172 0.1855  -0.2062 -0.1490 320 ILE   A CG1 
966  C  CG2 . ILE   A 164 ? 0.6320 1.0077 0.7549 0.1543  -0.1993 -0.1709 320 ILE   A CG2 
967  C  CD1 . ILE   A 164 ? 0.6391 0.9775 0.7023 0.2062  -0.2140 -0.1533 320 ILE   A CD1 
968  N  N   . THR   A 165 ? 0.4709 0.8117 0.5883 0.1178  -0.1889 -0.1633 321 THR   A N   
969  C  CA  . THR   A 165 ? 0.6539 1.0067 0.7922 0.0961  -0.1825 -0.1723 321 THR   A CA  
970  C  C   . THR   A 165 ? 0.4720 0.8464 0.6371 0.0881  -0.1763 -0.1795 321 THR   A C   
971  O  O   . THR   A 165 ? 0.3853 0.7531 0.5522 0.0921  -0.1727 -0.1730 321 THR   A O   
972  C  CB  . THR   A 165 ? 0.5380 0.8643 0.6692 0.0831  -0.1759 -0.1639 321 THR   A CB  
973  O  OG1 . THR   A 165 ? 0.5147 0.8216 0.6212 0.0888  -0.1808 -0.1579 321 THR   A OG1 
974  C  CG2 . THR   A 165 ? 0.3483 0.6828 0.5002 0.0602  -0.1677 -0.1723 321 THR   A CG2 
975  N  N   . LEU   A 166 ? 0.6122 1.0112 0.7973 0.0759  -0.1742 -0.1930 322 LEU   A N   
976  C  CA  . LEU   A 166 ? 0.4483 0.8677 0.6590 0.0648  -0.1665 -0.2009 322 LEU   A CA  
977  C  C   . LEU   A 166 ? 0.3943 0.8004 0.6139 0.0424  -0.1551 -0.1993 322 LEU   A C   
978  O  O   . LEU   A 166 ? 0.4685 0.8611 0.6813 0.0321  -0.1538 -0.1989 322 LEU   A O   
979  C  CB  . LEU   A 166 ? 0.4787 0.9316 0.7054 0.0631  -0.1697 -0.2169 322 LEU   A CB  
980  C  CG  . LEU   A 166 ? 0.5531 1.0286 0.8067 0.0458  -0.1606 -0.2283 322 LEU   A CG  
981  C  CD1 . LEU   A 166 ? 0.4954 0.9787 0.7590 0.0511  -0.1565 -0.2263 322 LEU   A CD1 
982  C  CD2 . LEU   A 166 ? 0.5362 1.0431 0.8019 0.0449  -0.1653 -0.2442 322 LEU   A CD2 
983  N  N   . ALA   A 167 ? 0.3680 0.7766 0.6015 0.0352  -0.1465 -0.1982 323 ALA   A N   
984  C  CA  . ALA   A 167 ? 0.2808 0.6739 0.5207 0.0150  -0.1349 -0.1956 323 ALA   A CA  
985  C  C   . ALA   A 167 ? 0.3656 0.7755 0.6271 0.0042  -0.1253 -0.2019 323 ALA   A C   
986  O  O   . ALA   A 167 ? 0.4222 0.8450 0.6899 0.0147  -0.1263 -0.2018 323 ALA   A O   
987  C  CB  . ALA   A 167 ? 0.3007 0.6635 0.5252 0.0182  -0.1333 -0.1811 323 ALA   A CB  
988  N  N   . LEU   A 168 ? 0.3374 0.7455 0.6086 -0.0166 -0.1157 -0.2072 324 LEU   A N   
989  C  CA  . LEU   A 168 ? 0.2679 0.6849 0.5563 -0.0300 -0.1041 -0.2113 324 LEU   A CA  
990  C  C   . LEU   A 168 ? 0.2615 0.6524 0.5445 -0.0357 -0.0956 -0.1996 324 LEU   A C   
991  O  O   . LEU   A 168 ? 0.3883 0.7525 0.6580 -0.0406 -0.0943 -0.1919 324 LEU   A O   
992  C  CB  . LEU   A 168 ? 0.2881 0.7111 0.5863 -0.0501 -0.0966 -0.2217 324 LEU   A CB  
993  C  CG  . LEU   A 168 ? 0.4254 0.8650 0.7245 -0.0491 -0.1044 -0.2325 324 LEU   A CG  
994  C  CD1 . LEU   A 168 ? 0.4577 0.8969 0.7649 -0.0712 -0.0950 -0.2412 324 LEU   A CD1 
995  C  CD2 . LEU   A 168 ? 0.4362 0.9101 0.7457 -0.0345 -0.1128 -0.2417 324 LEU   A CD2 
996  N  N   . GLU   A 169 ? 0.4047 0.8037 0.6979 -0.0349 -0.0898 -0.1987 325 GLU   A N   
997  C  CA  . GLU   A 169 ? 0.3032 0.6807 0.5934 -0.0406 -0.0809 -0.1887 325 GLU   A CA  
998  C  C   . GLU   A 169 ? 0.3762 0.7535 0.6775 -0.0611 -0.0667 -0.1932 325 GLU   A C   
999  O  O   . GLU   A 169 ? 0.3757 0.7778 0.6919 -0.0649 -0.0634 -0.2032 325 GLU   A O   
1000 C  CB  . GLU   A 169 ? 0.3491 0.7330 0.6407 -0.0245 -0.0840 -0.1837 325 GLU   A CB  
1001 C  CG  . GLU   A 169 ? 0.3135 0.6778 0.6035 -0.0301 -0.0747 -0.1743 325 GLU   A CG  
1002 C  CD  . GLU   A 169 ? 0.4184 0.7896 0.7101 -0.0140 -0.0775 -0.1702 325 GLU   A CD  
1003 O  OE1 . GLU   A 169 ? 0.3783 0.7712 0.6836 -0.0133 -0.0740 -0.1768 325 GLU   A OE1 
1004 O  OE2 . GLU   A 169 ? 0.3855 0.7400 0.6643 -0.0019 -0.0832 -0.1605 325 GLU   A OE2 
1005 N  N   . SER   A 170 ? 0.3287 0.6774 0.6214 -0.0740 -0.0580 -0.1860 326 SER   A N   
1006 C  CA  . SER   A 170 ? 0.3824 0.7247 0.6809 -0.0927 -0.0435 -0.1880 326 SER   A CA  
1007 C  C   . SER   A 170 ? 0.4195 0.7381 0.7110 -0.0950 -0.0355 -0.1767 326 SER   A C   
1008 O  O   . SER   A 170 ? 0.3466 0.6416 0.6246 -0.0910 -0.0383 -0.1674 326 SER   A O   
1009 C  CB  . SER   A 170 ? 0.2929 0.6205 0.5854 -0.1084 -0.0389 -0.1916 326 SER   A CB  
1010 O  OG  . SER   A 170 ? 0.5367 0.8519 0.8305 -0.1256 -0.0243 -0.1914 326 SER   A OG  
1011 N  N   . LYS   A 171 ? 0.5058 0.8312 0.8064 -0.1014 -0.0255 -0.1780 327 LYS   A N   
1012 C  CA  . LYS   A 171 ? 0.5199 0.8240 0.8144 -0.1051 -0.0163 -0.1683 327 LYS   A CA  
1013 C  C   . LYS   A 171 ? 0.2921 0.5727 0.5792 -0.1243 -0.0025 -0.1665 327 LYS   A C   
1014 O  O   . LYS   A 171 ? 0.4905 0.7533 0.7716 -0.1290 0.0070  -0.1591 327 LYS   A O   
1015 C  CB  . LYS   A 171 ? 0.3573 0.6823 0.6640 -0.0979 -0.0141 -0.1700 327 LYS   A CB  
1016 C  CG  . LYS   A 171 ? 0.3580 0.7063 0.6706 -0.0775 -0.0279 -0.1726 327 LYS   A CG  
1017 C  CD  . LYS   A 171 ? 0.6869 1.0519 1.0091 -0.0684 -0.0261 -0.1732 327 LYS   A CD  
1018 C  CE  . LYS   A 171 ? 0.5243 0.9051 0.8470 -0.0459 -0.0403 -0.1736 327 LYS   A CE  
1019 N  NZ  . LYS   A 171 ? 0.7018 1.0974 1.0323 -0.0349 -0.0392 -0.1741 327 LYS   A NZ  
1020 N  N   . SER   A 172 ? 0.3599 0.6387 0.6456 -0.1348 -0.0011 -0.1729 328 SER   A N   
1021 C  CA  . SER   A 172 ? 0.4509 0.7012 0.7248 -0.1511 0.0105  -0.1700 328 SER   A CA  
1022 C  C   . SER   A 172 ? 0.3951 0.6106 0.6496 -0.1489 0.0090  -0.1586 328 SER   A C   
1023 O  O   . SER   A 172 ? 0.3974 0.6130 0.6489 -0.1363 -0.0013 -0.1546 328 SER   A O   
1024 C  CB  . SER   A 172 ? 0.3512 0.6099 0.6293 -0.1620 0.0116  -0.1807 328 SER   A CB  
1025 O  OG  . SER   A 172 ? 0.4444 0.7052 0.7192 -0.1552 -0.0002 -0.1830 328 SER   A OG  
1026 N  N   . SER   A 173 ? 0.4022 0.5872 0.6425 -0.1607 0.0196  -0.1536 329 SER   A N   
1027 C  CA  . SER   A 173 ? 0.4332 0.5841 0.6541 -0.1587 0.0189  -0.1435 329 SER   A CA  
1028 C  C   . SER   A 173 ? 0.5282 0.6789 0.7454 -0.1550 0.0086  -0.1471 329 SER   A C   
1029 O  O   . SER   A 173 ? 0.3356 0.5052 0.5619 -0.1584 0.0051  -0.1572 329 SER   A O   
1030 C  CB  . SER   A 173 ? 0.6197 0.7379 0.8245 -0.1710 0.0319  -0.1382 329 SER   A CB  
1031 O  OG  . SER   A 173 ? 0.9247 1.0457 1.1330 -0.1759 0.0420  -0.1366 329 SER   A OG  
1032 N  N   . TRP   A 174 ? 0.4700 0.5996 0.6737 -0.1478 0.0039  -0.1391 330 TRP   A N   
1033 C  CA  . TRP   A 174 ? 0.3743 0.5024 0.5728 -0.1431 -0.0059 -0.1419 330 TRP   A CA  
1034 C  C   . TRP   A 174 ? 0.3278 0.4389 0.5174 -0.1550 -0.0009 -0.1459 330 TRP   A C   
1035 O  O   . TRP   A 174 ? 0.4097 0.4982 0.5901 -0.1647 0.0101  -0.1424 330 TRP   A O   
1036 C  CB  . TRP   A 174 ? 0.3014 0.4093 0.4866 -0.1334 -0.0107 -0.1327 330 TRP   A CB  
1037 C  CG  . TRP   A 174 ? 0.3750 0.5001 0.5686 -0.1206 -0.0179 -0.1299 330 TRP   A CG  
1038 C  CD1 . TRP   A 174 ? 0.3280 0.4811 0.5377 -0.1165 -0.0194 -0.1335 330 TRP   A CD1 
1039 C  CD2 . TRP   A 174 ? 0.3433 0.4575 0.5277 -0.1090 -0.0245 -0.1224 330 TRP   A CD2 
1040 N  NE1 . TRP   A 174 ? 0.2556 0.4151 0.4671 -0.1031 -0.0269 -0.1291 330 TRP   A NE1 
1041 C  CE2 . TRP   A 174 ? 0.2414 0.3743 0.4333 -0.0967 -0.0294 -0.1195 330 TRP   A CE2 
1042 C  CE3 . TRP   A 174 ? 0.2956 0.3824 0.4601 -0.1042 -0.0258 -0.1143 330 TRP   A CE3 
1043 C  CZ2 . TRP   A 174 ? 0.2920 0.4149 0.4711 -0.0813 -0.0350 -0.1085 330 TRP   A CZ2 
1044 C  CZ3 . TRP   A 174 ? 0.2882 0.3685 0.4420 -0.0891 -0.0313 -0.1039 330 TRP   A CZ3 
1045 C  CH2 . TRP   A 174 ? 0.3197 0.4170 0.4804 -0.0785 -0.0355 -0.1010 330 TRP   A CH2 
1046 N  N   . PRO   A 175 ? 0.3725 0.4932 0.5635 -0.1538 -0.0089 -0.1533 331 PRO   A N   
1047 C  CA  . PRO   A 175 ? 0.3478 0.4528 0.5307 -0.1650 -0.0046 -0.1580 331 PRO   A CA  
1048 C  C   . PRO   A 175 ? 0.4157 0.4799 0.5769 -0.1668 0.0009  -0.1489 331 PRO   A C   
1049 O  O   . PRO   A 175 ? 0.4131 0.4631 0.5649 -0.1579 -0.0016 -0.1402 331 PRO   A O   
1050 C  CB  . PRO   A 175 ? 0.3351 0.4581 0.5220 -0.1595 -0.0164 -0.1661 331 PRO   A CB  
1051 C  CG  . PRO   A 175 ? 0.3765 0.5334 0.5790 -0.1484 -0.0249 -0.1688 331 PRO   A CG  
1052 C  CD  . PRO   A 175 ? 0.3373 0.4852 0.5373 -0.1420 -0.0222 -0.1583 331 PRO   A CD  
1053 N  N   . ALA   A 176 ? 0.4119 0.4571 0.5646 -0.1783 0.0085  -0.1515 332 ALA   A N   
1054 C  CA  . ALA   A 176 ? 0.4764 0.4815 0.6072 -0.1796 0.0145  -0.1433 332 ALA   A CA  
1055 C  C   . ALA   A 176 ? 0.5232 0.5148 0.6419 -0.1703 0.0060  -0.1412 332 ALA   A C   
1056 O  O   . ALA   A 176 ? 0.4583 0.4189 0.5591 -0.1670 0.0091  -0.1332 332 ALA   A O   
1057 C  CB  . ALA   A 176 ? 0.3950 0.3835 0.5191 -0.1934 0.0238  -0.1477 332 ALA   A CB  
1058 N  N   . SER   A 177 ? 0.4949 0.5092 0.6221 -0.1653 -0.0046 -0.1483 333 SER   A N   
1059 C  CA  . SER   A 177 ? 0.4630 0.4665 0.5786 -0.1562 -0.0126 -0.1469 333 SER   A CA  
1060 C  C   . SER   A 177 ? 0.5035 0.5046 0.6158 -0.1442 -0.0163 -0.1382 333 SER   A C   
1061 O  O   . SER   A 177 ? 0.3788 0.3678 0.4798 -0.1364 -0.0212 -0.1360 333 SER   A O   
1062 C  CB  . SER   A 177 ? 0.4832 0.5122 0.6074 -0.1539 -0.0228 -0.1571 333 SER   A CB  
1063 O  OG  . SER   A 177 ? 0.3533 0.4168 0.4953 -0.1489 -0.0286 -0.1601 333 SER   A OG  
1064 N  N   . THR   A 178 ? 0.4339 0.4463 0.5558 -0.1425 -0.0137 -0.1337 334 THR   A N   
1065 C  CA  . THR   A 178 ? 0.4763 0.4864 0.5960 -0.1320 -0.0165 -0.1257 334 THR   A CA  
1066 C  C   . THR   A 178 ? 0.3317 0.3125 0.4385 -0.1330 -0.0071 -0.1156 334 THR   A C   
1067 O  O   . THR   A 178 ? 0.4235 0.4001 0.5278 -0.1249 -0.0084 -0.1088 334 THR   A O   
1068 C  CB  . THR   A 178 ? 0.3538 0.3956 0.4919 -0.1275 -0.0207 -0.1272 334 THR   A CB  
1069 O  OG1 . THR   A 178 ? 0.4604 0.5049 0.6056 -0.1355 -0.0114 -0.1262 334 THR   A OG1 
1070 C  CG2 . THR   A 178 ? 0.3714 0.4431 0.5213 -0.1250 -0.0302 -0.1371 334 THR   A CG2 
1071 N  N   . GLN   A 179 ? 0.5799 0.5399 0.6775 -0.1420 0.0020  -0.1146 335 GLN   A N   
1072 C  CA  . GLN   A 179 ? 0.4894 0.4241 0.5747 -0.1424 0.0111  -0.1049 335 GLN   A CA  
1073 C  C   . GLN   A 179 ? 0.5204 0.4333 0.5904 -0.1318 0.0090  -0.0970 335 GLN   A C   
1074 O  O   . GLN   A 179 ? 0.4912 0.3949 0.5565 -0.1274 0.0126  -0.0888 335 GLN   A O   
1075 C  CB  . GLN   A 179 ? 0.5355 0.4488 0.6103 -0.1525 0.0202  -0.1056 335 GLN   A CB  
1076 C  CG  . GLN   A 179 ? 0.5943 0.4868 0.6583 -0.1540 0.0302  -0.0967 335 GLN   A CG  
1077 C  CD  . GLN   A 179 ? 0.9870 0.8420 1.0270 -0.1503 0.0339  -0.0902 335 GLN   A CD  
1078 O  OE1 . GLN   A 179 ? 1.1280 0.9713 1.1601 -0.1500 0.0310  -0.0939 335 GLN   A OE1 
1079 N  NE2 . GLN   A 179 ? 0.8055 0.6419 0.8332 -0.1464 0.0398  -0.0807 335 GLN   A NE2 
1080 N  N   . GLU   A 180 ? 0.5471 0.4527 0.6094 -0.1273 0.0033  -0.1000 336 GLU   A N   
1081 C  CA  . GLU   A 180 ? 0.4742 0.3606 0.5219 -0.1166 0.0015  -0.0935 336 GLU   A CA  
1082 C  C   . GLU   A 180 ? 0.4196 0.3276 0.4724 -0.1034 -0.0088 -0.0908 336 GLU   A C   
1083 O  O   . GLU   A 180 ? 0.4355 0.3333 0.4764 -0.0927 -0.0118 -0.0852 336 GLU   A O   
1084 C  CB  . GLU   A 180 ? 0.6305 0.4908 0.6610 -0.1169 0.0029  -0.0955 336 GLU   A CB  
1085 C  CG  . GLU   A 180 ? 0.6773 0.5167 0.6984 -0.1248 0.0116  -0.0939 336 GLU   A CG  
1086 C  CD  . GLU   A 180 ? 0.8590 0.6775 0.8679 -0.1208 0.0186  -0.0833 336 GLU   A CD  
1087 O  OE1 . GLU   A 180 ? 0.9651 0.7758 0.9664 -0.1101 0.0164  -0.0772 336 GLU   A OE1 
1088 O  OE2 . GLU   A 180 ? 1.0899 0.8998 1.0961 -0.1282 0.0263  -0.0813 336 GLU   A OE2 
1089 N  N   . GLY   A 181 ? 0.4165 0.3539 0.4862 -0.1038 -0.0140 -0.0949 337 GLY   A N   
1090 C  CA  . GLY   A 181 ? 0.3313 0.2865 0.4035 -0.0915 -0.0230 -0.0916 337 GLY   A CA  
1091 C  C   . GLY   A 181 ? 0.3724 0.3323 0.4466 -0.0837 -0.0224 -0.0818 337 GLY   A C   
1092 O  O   . GLY   A 181 ? 0.3389 0.2895 0.4126 -0.0871 -0.0153 -0.0773 337 GLY   A O   
1093 N  N   . LEU   A 182 ? 0.3101 0.2835 0.3850 -0.0731 -0.0297 -0.0785 338 LEU   A N   
1094 C  CA  . LEU   A 182 ? 0.3295 0.3081 0.4058 -0.0653 -0.0299 -0.0699 338 LEU   A CA  
1095 C  C   . LEU   A 182 ? 0.3468 0.3044 0.4119 -0.0630 -0.0239 -0.0613 338 LEU   A C   
1096 O  O   . LEU   A 182 ? 0.3560 0.3118 0.4236 -0.0640 -0.0193 -0.0568 338 LEU   A O   
1097 C  CB  . LEU   A 182 ? 0.2207 0.2175 0.3125 -0.0692 -0.0289 -0.0727 338 LEU   A CB  
1098 C  CG  . LEU   A 182 ? 0.2581 0.2639 0.3530 -0.0607 -0.0306 -0.0660 338 LEU   A CG  
1099 C  CD1 . LEU   A 182 ? 0.2232 0.2382 0.3145 -0.0501 -0.0391 -0.0643 338 LEU   A CD1 
1100 C  CD2 . LEU   A 182 ? 0.2905 0.3135 0.4011 -0.0654 -0.0284 -0.0703 338 LEU   A CD2 
1101 N  N   . ARG   A 183 ? 0.2921 0.2347 0.3443 -0.0593 -0.0242 -0.0596 339 ARG   A N   
1102 C  CA  . ARG   A 183 ? 0.3824 0.3054 0.4231 -0.0562 -0.0193 -0.0529 339 ARG   A CA  
1103 C  C   . ARG   A 183 ? 0.3386 0.2670 0.3773 -0.0469 -0.0214 -0.0452 339 ARG   A C   
1104 O  O   . ARG   A 183 ? 0.4572 0.3825 0.4879 -0.0401 -0.0236 -0.0427 339 ARG   A O   
1105 C  CB  . ARG   A 183 ? 0.4457 0.3518 0.4741 -0.0551 -0.0189 -0.0553 339 ARG   A CB  
1106 C  CG  . ARG   A 183 ? 0.4765 0.3754 0.5058 -0.0654 -0.0165 -0.0637 339 ARG   A CG  
1107 C  CD  . ARG   A 183 ? 0.7352 0.6112 0.7494 -0.0638 -0.0145 -0.0652 339 ARG   A CD  
1108 N  NE  . ARG   A 183 ? 0.8983 0.7800 0.9084 -0.0568 -0.0205 -0.0675 339 ARG   A NE  
1109 C  CZ  . ARG   A 183 ? 0.8666 0.7578 0.8806 -0.0602 -0.0249 -0.0754 339 ARG   A CZ  
1110 N  NH1 . ARG   A 183 ? 0.7423 0.6407 0.7659 -0.0708 -0.0244 -0.0827 339 ARG   A NH1 
1111 N  NH2 . ARG   A 183 ? 0.8185 0.7136 0.8266 -0.0530 -0.0297 -0.0766 339 ARG   A NH2 
1112 N  N   . ILE   A 184 ? 0.3731 0.3099 0.4194 -0.0474 -0.0200 -0.0422 340 ILE   A N   
1113 C  CA  . ILE   A 184 ? 0.2853 0.2273 0.3306 -0.0402 -0.0215 -0.0357 340 ILE   A CA  
1114 C  C   . ILE   A 184 ? 0.2755 0.2065 0.3158 -0.0392 -0.0163 -0.0301 340 ILE   A C   
1115 O  O   . ILE   A 184 ? 0.2829 0.2178 0.3230 -0.0347 -0.0167 -0.0254 340 ILE   A O   
1116 C  CB  . ILE   A 184 ? 0.3049 0.2642 0.3608 -0.0395 -0.0247 -0.0365 340 ILE   A CB  
1117 C  CG1 . ILE   A 184 ? 0.2885 0.2525 0.3545 -0.0463 -0.0207 -0.0392 340 ILE   A CG1 
1118 C  CG2 . ILE   A 184 ? 0.2812 0.2515 0.3392 -0.0378 -0.0311 -0.0413 340 ILE   A CG2 
1119 C  CD1 . ILE   A 184 ? 0.2124 0.1938 0.2890 -0.0439 -0.0234 -0.0400 340 ILE   A CD1 
1120 N  N   . GLN   A 185 ? 0.2763 0.1928 0.3116 -0.0435 -0.0113 -0.0307 341 GLN   A N   
1121 C  CA  . GLN   A 185 ? 0.3609 0.2665 0.3901 -0.0424 -0.0063 -0.0254 341 GLN   A CA  
1122 C  C   . GLN   A 185 ? 0.3870 0.2902 0.4083 -0.0334 -0.0082 -0.0204 341 GLN   A C   
1123 O  O   . GLN   A 185 ? 0.3866 0.2905 0.4073 -0.0313 -0.0065 -0.0163 341 GLN   A O   
1124 C  CB  . GLN   A 185 ? 0.3327 0.2192 0.3539 -0.0481 -0.0004 -0.0267 341 GLN   A CB  
1125 C  CG  . GLN   A 185 ? 0.3874 0.2778 0.4176 -0.0590 0.0025  -0.0328 341 GLN   A CG  
1126 C  CD  . GLN   A 185 ? 0.4863 0.3732 0.5152 -0.0625 0.0003  -0.0393 341 GLN   A CD  
1127 O  OE1 . GLN   A 185 ? 0.3149 0.2075 0.3429 -0.0566 -0.0056 -0.0403 341 GLN   A OE1 
1128 N  NE2 . GLN   A 185 ? 0.4041 0.2810 0.4324 -0.0727 0.0056  -0.0440 341 GLN   A NE2 
1129 N  N   . ASN   A 186 ? 0.2639 0.1658 0.2799 -0.0286 -0.0115 -0.0215 342 ASN   A N   
1130 C  CA  . ASN   A 186 ? 0.3821 0.2840 0.3916 -0.0207 -0.0128 -0.0181 342 ASN   A CA  
1131 C  C   . ASN   A 186 ? 0.3623 0.2800 0.3782 -0.0189 -0.0160 -0.0168 342 ASN   A C   
1132 O  O   . ASN   A 186 ? 0.3404 0.2612 0.3533 -0.0142 -0.0165 -0.0146 342 ASN   A O   
1133 C  CB  . ASN   A 186 ? 0.5149 0.4081 0.5153 -0.0159 -0.0139 -0.0203 342 ASN   A CB  
1134 C  CG  . ASN   A 186 ? 0.6500 0.5231 0.6394 -0.0149 -0.0103 -0.0196 342 ASN   A CG  
1135 O  OD1 . ASN   A 186 ? 0.8052 0.6697 0.7943 -0.0205 -0.0063 -0.0186 342 ASN   A OD1 
1136 N  ND2 . ASN   A 186 ? 1.0848 0.9496 1.0643 -0.0073 -0.0113 -0.0203 342 ASN   A ND2 
1137 N  N   . TRP   A 187 ? 0.3256 0.2525 0.3493 -0.0224 -0.0178 -0.0185 343 TRP   A N   
1138 C  CA  . TRP   A 187 ? 0.2330 0.1712 0.2597 -0.0203 -0.0207 -0.0170 343 TRP   A CA  
1139 C  C   . TRP   A 187 ? 0.3158 0.2593 0.3494 -0.0221 -0.0199 -0.0152 343 TRP   A C   
1140 O  O   . TRP   A 187 ? 0.3065 0.2508 0.3388 -0.0201 -0.0188 -0.0118 343 TRP   A O   
1141 C  CB  . TRP   A 187 ? 0.2495 0.1929 0.2765 -0.0204 -0.0246 -0.0206 343 TRP   A CB  
1142 C  CG  . TRP   A 187 ? 0.1899 0.1422 0.2183 -0.0187 -0.0276 -0.0194 343 TRP   A CG  
1143 C  CD1 . TRP   A 187 ? 0.2413 0.1956 0.2674 -0.0164 -0.0272 -0.0155 343 TRP   A CD1 
1144 C  CD2 . TRP   A 187 ? 0.2110 0.1700 0.2418 -0.0189 -0.0318 -0.0226 343 TRP   A CD2 
1145 N  NE1 . TRP   A 187 ? 0.2794 0.2384 0.3046 -0.0148 -0.0303 -0.0152 343 TRP   A NE1 
1146 C  CE2 . TRP   A 187 ? 0.2576 0.2206 0.2857 -0.0155 -0.0337 -0.0195 343 TRP   A CE2 
1147 C  CE3 . TRP   A 187 ? 0.2593 0.2210 0.2936 -0.0215 -0.0341 -0.0282 343 TRP   A CE3 
1148 C  CZ2 . TRP   A 187 ? 0.2949 0.2640 0.3224 -0.0131 -0.0383 -0.0213 343 TRP   A CZ2 
1149 C  CZ3 . TRP   A 187 ? 0.2349 0.2057 0.2706 -0.0199 -0.0391 -0.0308 343 TRP   A CZ3 
1150 C  CH2 . TRP   A 187 ? 0.2404 0.2146 0.2722 -0.0149 -0.0415 -0.0271 343 TRP   A CH2 
1151 N  N   . LEU   A 188 ? 0.2484 0.1963 0.2892 -0.0257 -0.0203 -0.0181 344 LEU   A N   
1152 C  CA  . LEU   A 188 ? 0.2908 0.2456 0.3388 -0.0263 -0.0196 -0.0172 344 LEU   A CA  
1153 C  C   . LEU   A 188 ? 0.2581 0.2083 0.3086 -0.0302 -0.0144 -0.0168 344 LEU   A C   
1154 O  O   . LEU   A 188 ? 0.3080 0.2634 0.3637 -0.0302 -0.0129 -0.0158 344 LEU   A O   
1155 C  CB  . LEU   A 188 ? 0.1962 0.1624 0.2518 -0.0267 -0.0235 -0.0213 344 LEU   A CB  
1156 C  CG  . LEU   A 188 ? 0.1957 0.1654 0.2466 -0.0224 -0.0288 -0.0215 344 LEU   A CG  
1157 C  CD1 . LEU   A 188 ? 0.3156 0.2972 0.3733 -0.0220 -0.0335 -0.0265 344 LEU   A CD1 
1158 C  CD2 . LEU   A 188 ? 0.2494 0.2172 0.2945 -0.0176 -0.0292 -0.0164 344 LEU   A CD2 
1159 N  N   . SER   A 189 ? 0.2185 0.1580 0.2642 -0.0334 -0.0112 -0.0176 345 SER   A N   
1160 C  CA  . SER   A 189 ? 0.3211 0.2505 0.3637 -0.0369 -0.0052 -0.0161 345 SER   A CA  
1161 C  C   . SER   A 189 ? 0.2763 0.2053 0.3247 -0.0451 -0.0017 -0.0208 345 SER   A C   
1162 O  O   . SER   A 189 ? 0.3107 0.2528 0.3694 -0.0480 -0.0042 -0.0256 345 SER   A O   
1163 C  CB  . SER   A 189 ? 0.2848 0.2173 0.3290 -0.0352 -0.0029 -0.0126 345 SER   A CB  
1164 O  OG  . SER   A 189 ? 0.3083 0.2530 0.3638 -0.0380 -0.0025 -0.0152 345 SER   A OG  
1165 N  N   . ALA   A 190 ? 0.2970 0.2108 0.3377 -0.0491 0.0043  -0.0197 346 ALA   A N   
1166 C  CA  . ALA   A 190 ? 0.3407 0.2518 0.3855 -0.0590 0.0096  -0.0242 346 ALA   A CA  
1167 C  C   . ALA   A 190 ? 0.3079 0.2344 0.3657 -0.0634 0.0123  -0.0263 346 ALA   A C   
1168 O  O   . ALA   A 190 ? 0.3835 0.3198 0.4520 -0.0713 0.0140  -0.0327 346 ALA   A O   
1169 C  CB  . ALA   A 190 ? 0.3369 0.2239 0.3667 -0.0617 0.0163  -0.0214 346 ALA   A CB  
1170 N  N   . LYS   A 191 ? 0.2401 0.1701 0.2976 -0.0583 0.0127  -0.0218 347 LYS   A N   
1171 C  CA  . LYS   A 191 ? 0.3522 0.2975 0.4217 -0.0605 0.0150  -0.0238 347 LYS   A CA  
1172 C  C   . LYS   A 191 ? 0.2776 0.2439 0.3612 -0.0586 0.0085  -0.0290 347 LYS   A C   
1173 O  O   . LYS   A 191 ? 0.2844 0.2658 0.3810 -0.0637 0.0101  -0.0350 347 LYS   A O   
1174 C  CB  . LYS   A 191 ? 0.3538 0.2966 0.4177 -0.0540 0.0157  -0.0181 347 LYS   A CB  
1175 C  CG  . LYS   A 191 ? 0.3835 0.3376 0.4561 -0.0557 0.0197  -0.0194 347 LYS   A CG  
1176 C  CD  . LYS   A 191 ? 0.5892 0.5428 0.6572 -0.0477 0.0179  -0.0147 347 LYS   A CD  
1177 C  CE  . LYS   A 191 ? 0.4116 0.3478 0.4636 -0.0442 0.0179  -0.0091 347 LYS   A CE  
1178 N  NZ  . LYS   A 191 ? 0.6889 0.6127 0.7312 -0.0471 0.0253  -0.0064 347 LYS   A NZ  
1179 N  N   . VAL   A 192 ? 0.3844 0.3525 0.4650 -0.0510 0.0013  -0.0271 348 VAL   A N   
1180 C  CA  . VAL   A 192 ? 0.2658 0.2508 0.3560 -0.0477 -0.0054 -0.0312 348 VAL   A CA  
1181 C  C   . VAL   A 192 ? 0.2865 0.2779 0.3832 -0.0542 -0.0066 -0.0386 348 VAL   A C   
1182 O  O   . VAL   A 192 ? 0.2502 0.2601 0.3593 -0.0548 -0.0097 -0.0447 348 VAL   A O   
1183 C  CB  . VAL   A 192 ? 0.3113 0.2930 0.3934 -0.0391 -0.0116 -0.0270 348 VAL   A CB  
1184 C  CG1 . VAL   A 192 ? 0.1982 0.1932 0.2858 -0.0354 -0.0187 -0.0309 348 VAL   A CG1 
1185 C  CG2 . VAL   A 192 ? 0.1735 0.1530 0.2521 -0.0336 -0.0107 -0.0217 348 VAL   A CG2 
1186 N  N   . ARG   A 193 ? 0.3060 0.2824 0.3944 -0.0589 -0.0043 -0.0387 349 ARG   A N   
1187 C  CA  . ARG   A 193 ? 0.3292 0.3096 0.4228 -0.0664 -0.0048 -0.0464 349 ARG   A CA  
1188 C  C   . ARG   A 193 ? 0.3175 0.3086 0.4237 -0.0763 0.0010  -0.0527 349 ARG   A C   
1189 O  O   . ARG   A 193 ? 0.3216 0.3309 0.4405 -0.0803 -0.0019 -0.0611 349 ARG   A O   
1190 C  CB  . ARG   A 193 ? 0.2350 0.1935 0.3152 -0.0694 -0.0022 -0.0452 349 ARG   A CB  
1191 C  CG  . ARG   A 193 ? 0.2623 0.2225 0.3460 -0.0771 -0.0030 -0.0536 349 ARG   A CG  
1192 C  CD  . ARG   A 193 ? 0.3087 0.2453 0.3773 -0.0781 -0.0011 -0.0524 349 ARG   A CD  
1193 N  NE  . ARG   A 193 ? 0.2733 0.2111 0.3448 -0.0855 -0.0023 -0.0612 349 ARG   A NE  
1194 C  CZ  . ARG   A 193 ? 0.4215 0.3541 0.4959 -0.0980 0.0041  -0.0672 349 ARG   A CZ  
1195 N  NH1 . ARG   A 193 ? 0.3098 0.2345 0.3835 -0.1046 0.0128  -0.0650 349 ARG   A NH1 
1196 N  NH2 . ARG   A 193 ? 0.3498 0.2848 0.4271 -0.1048 0.0023  -0.0761 349 ARG   A NH2 
1197 N  N   . LYS   A 194 ? 0.2755 0.2569 0.3783 -0.0805 0.0093  -0.0493 350 LYS   A N   
1198 C  CA  . LYS   A 194 ? 0.2489 0.2407 0.3632 -0.0909 0.0163  -0.0552 350 LYS   A CA  
1199 C  C   . LYS   A 194 ? 0.3036 0.3243 0.4355 -0.0869 0.0121  -0.0599 350 LYS   A C   
1200 O  O   . LYS   A 194 ? 0.3723 0.4130 0.5195 -0.0934 0.0120  -0.0694 350 LYS   A O   
1201 C  CB  . LYS   A 194 ? 0.3717 0.3460 0.4760 -0.0945 0.0260  -0.0493 350 LYS   A CB  
1202 C  CG  . LYS   A 194 ? 0.4625 0.4463 0.5772 -0.1061 0.0352  -0.0549 350 LYS   A CG  
1203 C  CD  . LYS   A 194 ? 0.5478 0.5176 0.6523 -0.1063 0.0436  -0.0481 350 LYS   A CD  
1204 C  CE  . LYS   A 194 ? 0.8240 0.7758 0.9202 -0.1201 0.0555  -0.0493 350 LYS   A CE  
1205 N  NZ  . LYS   A 194 ? 0.9441 0.9066 1.0483 -0.1274 0.0649  -0.0517 350 LYS   A NZ  
1206 N  N   . GLN   A 195 ? 0.2764 0.2997 0.4061 -0.0757 0.0084  -0.0540 351 GLN   A N   
1207 C  CA  . GLN   A 195 ? 0.3273 0.3749 0.4709 -0.0694 0.0039  -0.0577 351 GLN   A CA  
1208 C  C   . GLN   A 195 ? 0.3133 0.3788 0.4658 -0.0662 -0.0052 -0.0647 351 GLN   A C   
1209 O  O   . GLN   A 195 ? 0.2755 0.3656 0.4439 -0.0661 -0.0073 -0.0726 351 GLN   A O   
1210 C  CB  . GLN   A 195 ? 0.2611 0.3027 0.3968 -0.0577 0.0012  -0.0497 351 GLN   A CB  
1211 N  N   . LEU   A 196 ? 0.3159 0.3707 0.4583 -0.0628 -0.0108 -0.0623 352 LEU   A N   
1212 C  CA  . LEU   A 196 ? 0.2926 0.3629 0.4409 -0.0594 -0.0197 -0.0687 352 LEU   A CA  
1213 C  C   . LEU   A 196 ? 0.3270 0.4100 0.4875 -0.0715 -0.0175 -0.0797 352 LEU   A C   
1214 O  O   . LEU   A 196 ? 0.2859 0.3935 0.4598 -0.0700 -0.0234 -0.0884 352 LEU   A O   
1215 C  CB  . LEU   A 196 ? 0.2863 0.3408 0.4195 -0.0540 -0.0249 -0.0637 352 LEU   A CB  
1216 C  CG  . LEU   A 196 ? 0.2602 0.3058 0.3820 -0.0423 -0.0285 -0.0546 352 LEU   A CG  
1217 C  CD1 . LEU   A 196 ? 0.2914 0.3235 0.3997 -0.0394 -0.0322 -0.0512 352 LEU   A CD1 
1218 C  CD2 . LEU   A 196 ? 0.4241 0.4872 0.5523 -0.0325 -0.0350 -0.0564 352 LEU   A CD2 
1219 N  N   . ARG   A 197 ? 0.2088 0.2752 0.3644 -0.0833 -0.0092 -0.0799 353 ARG   A N   
1220 C  CA  . ARG   A 197 ? 0.2077 0.2830 0.3735 -0.0969 -0.0058 -0.0906 353 ARG   A CA  
1221 C  C   . ARG   A 197 ? 0.2527 0.3501 0.4366 -0.1044 -0.0001 -0.0979 353 ARG   A C   
1222 O  O   . ARG   A 197 ? 0.2146 0.3265 0.4110 -0.1161 0.0022  -0.1090 353 ARG   A O   
1223 C  CB  . ARG   A 197 ? 0.3895 0.4357 0.5411 -0.1068 0.0018  -0.0881 353 ARG   A CB  
1224 C  CG  . ARG   A 197 ? 0.2986 0.3275 0.4350 -0.1006 -0.0041 -0.0841 353 ARG   A CG  
1225 C  CD  . ARG   A 197 ? 0.3284 0.3279 0.4502 -0.1089 0.0034  -0.0821 353 ARG   A CD  
1226 N  NE  . ARG   A 197 ? 0.5442 0.5466 0.6731 -0.1238 0.0078  -0.0928 353 ARG   A NE  
1227 C  CZ  . ARG   A 197 ? 0.5019 0.5094 0.6328 -0.1266 0.0025  -0.1008 353 ARG   A CZ  
1228 N  NH1 . ARG   A 197 ? 0.4659 0.4760 0.5917 -0.1153 -0.0073 -0.0990 353 ARG   A NH1 
1229 N  NH2 . ARG   A 197 ? 0.4418 0.4508 0.5743 -0.1367 0.0067  -0.1069 353 ARG   A NH2 
1230 N  N   . LEU   A 198 ? 0.2576 0.3587 0.4435 -0.0985 0.0027  -0.0928 354 LEU   A N   
1231 C  CA  . LEU   A 198 ? 0.3166 0.4440 0.5215 -0.1029 0.0067  -0.1007 354 LEU   A CA  
1232 C  C   . LEU   A 198 ? 0.3076 0.4679 0.5285 -0.0929 -0.0039 -0.1084 354 LEU   A C   
1233 O  O   . LEU   A 198 ? 0.3320 0.5193 0.5713 -0.0957 -0.0017 -0.1170 354 LEU   A O   
1234 C  CB  . LEU   A 198 ? 0.2922 0.4115 0.4928 -0.0999 0.0139  -0.0930 354 LEU   A CB  
1235 C  CG  . LEU   A 198 ? 0.3959 0.4871 0.5828 -0.1112 0.0258  -0.0875 354 LEU   A CG  
1236 C  CD1 . LEU   A 198 ? 0.4173 0.5006 0.5978 -0.1060 0.0311  -0.0795 354 LEU   A CD1 
1237 C  CD2 . LEU   A 198 ? 0.3263 0.4246 0.5233 -0.1296 0.0354  -0.0973 354 LEU   A CD2 
1238 N  N   . LYS   A 199 ? 0.3780 0.5373 0.5918 -0.0810 -0.0152 -0.1060 355 LYS   A N   
1239 C  CA  . LYS   A 199 ? 0.3819 0.5686 0.6064 -0.0686 -0.0262 -0.1118 355 LYS   A CA  
1240 C  C   . LYS   A 199 ? 0.3057 0.5156 0.5437 -0.0753 -0.0312 -0.1254 355 LYS   A C   
1241 O  O   . LYS   A 199 ? 0.3222 0.5215 0.5575 -0.0885 -0.0272 -0.1287 355 LYS   A O   
1242 C  CB  . LYS   A 199 ? 0.3554 0.5272 0.5628 -0.0528 -0.0351 -0.1021 355 LYS   A CB  
1243 C  CG  . LYS   A 199 ? 0.4306 0.5820 0.6257 -0.0463 -0.0309 -0.0901 355 LYS   A CG  
1244 C  CD  . LYS   A 199 ? 0.5950 0.7370 0.7762 -0.0306 -0.0395 -0.0823 355 LYS   A CD  
1245 C  CE  . LYS   A 199 ? 0.7649 0.8885 0.9354 -0.0256 -0.0348 -0.0720 355 LYS   A CE  
1246 N  NZ  . LYS   A 199 ? 0.8060 0.9239 0.9654 -0.0105 -0.0421 -0.0661 355 LYS   A NZ  
1247 N  N   . PRO   A 200 ? 0.3591 0.6009 0.6114 -0.0663 -0.0401 -0.1341 356 PRO   A N   
1248 C  CA  . PRO   A 200 ? 0.2678 0.5275 0.5265 -0.0701 -0.0445 -0.1446 356 PRO   A CA  
1249 C  C   . PRO   A 200 ? 0.3763 0.6220 0.6220 -0.0687 -0.0520 -0.1434 356 PRO   A C   
1250 O  O   . PRO   A 200 ? 0.3236 0.5486 0.5539 -0.0604 -0.0558 -0.1337 356 PRO   A O   
1251 C  CB  . PRO   A 200 ? 0.3350 0.6254 0.6043 -0.0550 -0.0534 -0.1503 356 PRO   A CB  
1252 C  CG  . PRO   A 200 ? 0.2582 0.5435 0.5236 -0.0404 -0.0577 -0.1422 356 PRO   A CG  
1253 C  CD  . PRO   A 200 ? 0.3457 0.6034 0.6030 -0.0501 -0.0453 -0.1326 356 PRO   A CD  
1254 N  N   . PHE   A 201 ? 0.3238 0.5768 0.5711 -0.0758 -0.0527 -0.1513 357 PHE   A N   
1255 C  CA  . PHE   A 201 ? 0.2954 0.5406 0.5316 -0.0733 -0.0607 -0.1522 357 PHE   A CA  
1256 C  C   . PHE   A 201 ? 0.3251 0.5983 0.5684 -0.0656 -0.0700 -0.1616 357 PHE   A C   
1257 O  O   . PHE   A 201 ? 0.2677 0.5648 0.5255 -0.0662 -0.0682 -0.1688 357 PHE   A O   
1258 C  CB  . PHE   A 201 ? 0.3193 0.5407 0.5469 -0.0894 -0.0524 -0.1523 357 PHE   A CB  
1259 C  CG  . PHE   A 201 ? 0.3047 0.5364 0.5416 -0.1031 -0.0453 -0.1614 357 PHE   A CG  
1260 C  CD1 . PHE   A 201 ? 0.3035 0.5496 0.5432 -0.1041 -0.0511 -0.1707 357 PHE   A CD1 
1261 C  CD2 . PHE   A 201 ? 0.3425 0.5684 0.5841 -0.1151 -0.0326 -0.1607 357 PHE   A CD2 
1262 C  CE1 . PHE   A 201 ? 0.3107 0.5665 0.5594 -0.1173 -0.0444 -0.1798 357 PHE   A CE1 
1263 C  CE2 . PHE   A 201 ? 0.4950 0.7294 0.7442 -0.1281 -0.0256 -0.1693 357 PHE   A CE2 
1264 C  CZ  . PHE   A 201 ? 0.3852 0.6350 0.6386 -0.1295 -0.0316 -0.1791 357 PHE   A CZ  
1265 N  N   . TYR   A 202 ? 0.3129 0.5837 0.5455 -0.0578 -0.0799 -0.1620 358 TYR   A N   
1266 C  CA  . TYR   A 202 ? 0.2315 0.5280 0.4685 -0.0477 -0.0898 -0.1699 358 TYR   A CA  
1267 C  C   . TYR   A 202 ? 0.2741 0.5697 0.5068 -0.0550 -0.0920 -0.1769 358 TYR   A C   
1268 O  O   . TYR   A 202 ? 0.2761 0.5482 0.4982 -0.0640 -0.0883 -0.1739 358 TYR   A O   
1269 C  CB  . TYR   A 202 ? 0.2319 0.5301 0.4586 -0.0265 -0.1015 -0.1638 358 TYR   A CB  
1270 C  CG  . TYR   A 202 ? 0.2886 0.5902 0.5206 -0.0181 -0.0998 -0.1583 358 TYR   A CG  
1271 C  CD1 . TYR   A 202 ? 0.2504 0.5301 0.4765 -0.0197 -0.0950 -0.1485 358 TYR   A CD1 
1272 C  CD2 . TYR   A 202 ? 0.3253 0.6522 0.5686 -0.0089 -0.1025 -0.1636 358 TYR   A CD2 
1273 C  CE1 . TYR   A 202 ? 0.2695 0.5522 0.5007 -0.0123 -0.0932 -0.1439 358 TYR   A CE1 
1274 C  CE2 . TYR   A 202 ? 0.3613 0.6906 0.6090 -0.0009 -0.1005 -0.1589 358 TYR   A CE2 
1275 C  CZ  . TYR   A 202 ? 0.2719 0.5788 0.5134 -0.0028 -0.0958 -0.1489 358 TYR   A CZ  
1276 O  OH  . TYR   A 202 ? 0.3415 0.6504 0.5872 0.0052  -0.0938 -0.1446 358 TYR   A OH  
1277 N  N   . LEU   A 203 ? 0.2767 0.5983 0.5176 -0.0508 -0.0980 -0.1868 359 LEU   A N   
1278 C  CA  . LEU   A 203 ? 0.3103 0.6359 0.5492 -0.0570 -0.1008 -0.1952 359 LEU   A CA  
1279 C  C   . LEU   A 203 ? 0.3615 0.7068 0.5969 -0.0397 -0.1142 -0.1991 359 LEU   A C   
1280 O  O   . LEU   A 203 ? 0.4034 0.7736 0.6495 -0.0308 -0.1178 -0.2041 359 LEU   A O   
1281 C  CB  . LEU   A 203 ? 0.3606 0.6996 0.6155 -0.0738 -0.0920 -0.2059 359 LEU   A CB  
1282 C  CG  . LEU   A 203 ? 0.2863 0.6012 0.5401 -0.0927 -0.0782 -0.2028 359 LEU   A CG  
1283 C  CD1 . LEU   A 203 ? 0.4165 0.7482 0.6874 -0.1058 -0.0688 -0.2117 359 LEU   A CD1 
1284 C  CD2 . LEU   A 203 ? 0.3374 0.6298 0.5779 -0.1011 -0.0776 -0.2029 359 LEU   A CD2 
1285 N  N   . VAL   A 204 ? 0.2815 0.6148 0.5006 -0.0345 -0.1212 -0.1970 360 VAL   A N   
1286 C  CA  . VAL   A 204 ? 0.2916 0.6393 0.5032 -0.0174 -0.1338 -0.1995 360 VAL   A CA  
1287 C  C   . VAL   A 204 ? 0.3579 0.7163 0.5715 -0.0245 -0.1364 -0.2108 360 VAL   A C   
1288 O  O   . VAL   A 204 ? 0.4074 0.7500 0.6180 -0.0392 -0.1307 -0.2122 360 VAL   A O   
1289 C  CB  . VAL   A 204 ? 0.3541 0.6803 0.5428 -0.0033 -0.1405 -0.1878 360 VAL   A CB  
1290 C  CG1 . VAL   A 204 ? 0.2745 0.5906 0.4620 0.0033  -0.1377 -0.1773 360 VAL   A CG1 
1291 C  CG2 . VAL   A 204 ? 0.3621 0.6634 0.5375 -0.0129 -0.1378 -0.1848 360 VAL   A CG2 
1292 N  N   . PRO   A 205 ? 0.3196 0.7038 0.5377 -0.0145 -0.1449 -0.2193 361 PRO   A N   
1293 C  CA  . PRO   A 205 ? 0.3834 0.7792 0.6042 -0.0217 -0.1476 -0.2309 361 PRO   A CA  
1294 C  C   . PRO   A 205 ? 0.4043 0.7794 0.6034 -0.0179 -0.1531 -0.2263 361 PRO   A C   
1295 O  O   . PRO   A 205 ? 0.3423 0.7106 0.5246 -0.0010 -0.1612 -0.2188 361 PRO   A O   
1296 C  CB  . PRO   A 205 ? 0.3469 0.7758 0.5766 -0.0083 -0.1563 -0.2400 361 PRO   A CB  
1297 C  CG  . PRO   A 205 ? 0.4327 0.8580 0.6529 0.0115  -0.1618 -0.2298 361 PRO   A CG  
1298 C  CD  . PRO   A 205 ? 0.3222 0.7244 0.5409 0.0050  -0.1529 -0.2185 361 PRO   A CD  
1299 N  N   . LYS   A 206 ? 0.3502 0.7138 0.5482 -0.0337 -0.1481 -0.2308 362 LYS   A N   
1300 C  CA  . LYS   A 206 ? 0.4646 0.8075 0.6418 -0.0314 -0.1521 -0.2270 362 LYS   A CA  
1301 C  C   . LYS   A 206 ? 0.3948 0.7355 0.5747 -0.0474 -0.1486 -0.2371 362 LYS   A C   
1302 O  O   . LYS   A 206 ? 0.3650 0.7010 0.5563 -0.0645 -0.1386 -0.2408 362 LYS   A O   
1303 C  CB  . LYS   A 206 ? 0.4369 0.7484 0.6000 -0.0315 -0.1473 -0.2136 362 LYS   A CB  
1304 C  CG  . LYS   A 206 ? 0.4596 0.7531 0.5987 -0.0222 -0.1536 -0.2078 362 LYS   A CG  
1305 C  CD  . LYS   A 206 ? 0.5286 0.8155 0.6544 -0.0044 -0.1588 -0.1960 362 LYS   A CD  
1306 C  CE  . LYS   A 206 ? 0.6683 0.9485 0.7711 0.0090  -0.1677 -0.1931 362 LYS   A CE  
1307 N  NZ  . LYS   A 206 ? 0.5803 0.8600 0.6708 0.0284  -0.1741 -0.1838 362 LYS   A NZ  
1308 N  N   . HIS   A 207 ? 0.5149 0.8574 0.6828 -0.0415 -0.1567 -0.2412 363 HIS   A N   
1309 C  CA  . HIS   A 207 ? 0.4794 0.8195 0.6482 -0.0555 -0.1545 -0.2512 363 HIS   A CA  
1310 C  C   . HIS   A 207 ? 0.4182 0.7238 0.5758 -0.0676 -0.1458 -0.2453 363 HIS   A C   
1311 O  O   . HIS   A 207 ? 0.4817 0.7656 0.6233 -0.0606 -0.1460 -0.2342 363 HIS   A O   
1312 C  CB  . HIS   A 207 ? 0.4787 0.8281 0.6354 -0.0448 -0.1657 -0.2564 363 HIS   A CB  
1313 N  N   . ALA   A 208 ? 0.4505 0.7506 0.6159 -0.0857 -0.1379 -0.2529 364 ALA   A N   
1314 C  CA  . ALA   A 208 ? 0.5435 0.8099 0.6965 -0.0969 -0.1301 -0.2491 364 ALA   A CA  
1315 C  C   . ALA   A 208 ? 0.5856 0.8488 0.7309 -0.1026 -0.1331 -0.2588 364 ALA   A C   
1316 O  O   . ALA   A 208 ? 0.8138 1.1021 0.9693 -0.1040 -0.1379 -0.2702 364 ALA   A O   
1317 C  CB  . ALA   A 208 ? 0.5180 0.7731 0.6821 -0.1130 -0.1172 -0.2484 364 ALA   A CB  
1318 N  N   . GLN   A 215 ? 0.6373 0.9792 0.8273 -0.1205 -0.1393 -0.2988 371 GLN   A N   
1319 C  CA  . GLN   A 215 ? 0.7472 1.1139 0.9605 -0.1274 -0.1343 -0.3051 371 GLN   A CA  
1320 C  C   . GLN   A 215 ? 0.6971 1.0829 0.9165 -0.1105 -0.1396 -0.2985 371 GLN   A C   
1321 O  O   . GLN   A 215 ? 0.6888 1.0562 0.8988 -0.1031 -0.1380 -0.2851 371 GLN   A O   
1322 C  CB  . GLN   A 215 ? 0.7012 1.0452 0.9187 -0.1459 -0.1195 -0.3024 371 GLN   A CB  
1323 C  CG  . GLN   A 215 ? 0.7776 1.1454 1.0179 -0.1586 -0.1125 -0.3129 371 GLN   A CG  
1324 C  CD  . GLN   A 215 ? 0.7606 1.1100 1.0011 -0.1804 -0.1015 -0.3195 371 GLN   A CD  
1325 O  OE1 . GLN   A 215 ? 0.7783 1.1056 1.0041 -0.1849 -0.1023 -0.3207 371 GLN   A OE1 
1326 N  NE2 . GLN   A 215 ? 0.6883 1.0462 0.9444 -0.1939 -0.0910 -0.3242 371 GLN   A NE2 
1327 N  N   . GLU   A 216 ? 0.5141 0.9367 0.7492 -0.1043 -0.1456 -0.3085 372 GLU   A N   
1328 C  CA  . GLU   A 216 ? 0.7372 1.1791 0.9733 -0.0836 -0.1545 -0.3040 372 GLU   A CA  
1329 C  C   . GLU   A 216 ? 0.6089 1.0620 0.8606 -0.0834 -0.1484 -0.3009 372 GLU   A C   
1330 O  O   . GLU   A 216 ? 0.6066 1.0718 0.8576 -0.0658 -0.1551 -0.2959 372 GLU   A O   
1331 C  CB  . GLU   A 216 ? 0.4574 0.9334 0.6994 -0.0734 -0.1660 -0.3166 372 GLU   A CB  
1332 N  N   . GLU   A 217 ? 0.6024 1.0510 0.8668 -0.1018 -0.1359 -0.3036 373 GLU   A N   
1333 C  CA  . GLU   A 217 ? 0.4150 0.8762 0.6946 -0.1023 -0.1296 -0.3019 373 GLU   A CA  
1334 C  C   . GLU   A 217 ? 0.4353 0.8645 0.7079 -0.1089 -0.1193 -0.2882 373 GLU   A C   
1335 O  O   . GLU   A 217 ? 0.4287 0.8613 0.7138 -0.1177 -0.1096 -0.2882 373 GLU   A O   
1336 C  CB  . GLU   A 217 ? 0.4285 0.9158 0.7301 -0.1172 -0.1230 -0.3172 373 GLU   A CB  
1337 C  CG  . GLU   A 217 ? 0.4442 0.9694 0.7566 -0.1104 -0.1329 -0.3325 373 GLU   A CG  
1338 C  CD  . GLU   A 217 ? 0.6083 1.1523 0.9175 -0.0851 -0.1459 -0.3295 373 GLU   A CD  
1339 O  OE1 . GLU   A 217 ? 0.5298 1.0704 0.8384 -0.0753 -0.1451 -0.3198 373 GLU   A OE1 
1340 O  OE2 . GLU   A 217 ? 0.6577 1.2195 0.9640 -0.0749 -0.1571 -0.3371 373 GLU   A OE2 
1341 N  N   . THR   A 218 ? 0.3922 0.7908 0.6448 -0.1044 -0.1210 -0.2768 374 THR   A N   
1342 C  CA  . THR   A 218 ? 0.3792 0.7467 0.6239 -0.1100 -0.1118 -0.2641 374 THR   A CA  
1343 C  C   . THR   A 218 ? 0.3597 0.7264 0.5999 -0.0931 -0.1162 -0.2525 374 THR   A C   
1344 O  O   . THR   A 218 ? 0.3583 0.7373 0.5928 -0.0755 -0.1275 -0.2513 374 THR   A O   
1345 C  CB  . THR   A 218 ? 0.3835 0.7165 0.6089 -0.1160 -0.1098 -0.2589 374 THR   A CB  
1346 O  OG1 . THR   A 218 ? 0.3851 0.7181 0.5960 -0.1015 -0.1217 -0.2573 374 THR   A OG1 
1347 C  CG2 . THR   A 218 ? 0.4036 0.7305 0.6324 -0.1351 -0.1027 -0.2689 374 THR   A CG2 
1348 N  N   . TRP   A 219 ? 0.3472 0.6978 0.5887 -0.0984 -0.1069 -0.2439 375 TRP   A N   
1349 C  CA  . TRP   A 219 ? 0.3292 0.6742 0.5659 -0.0849 -0.1092 -0.2322 375 TRP   A CA  
1350 C  C   . TRP   A 219 ? 0.3306 0.6388 0.5514 -0.0893 -0.1036 -0.2204 375 TRP   A C   
1351 O  O   . TRP   A 219 ? 0.3453 0.6340 0.5645 -0.1050 -0.0938 -0.2207 375 TRP   A O   
1352 C  CB  . TRP   A 219 ? 0.3257 0.6881 0.5797 -0.0862 -0.1034 -0.2332 375 TRP   A CB  
1353 C  CG  . TRP   A 219 ? 0.3549 0.7549 0.6255 -0.0819 -0.1082 -0.2458 375 TRP   A CG  
1354 C  CD1 . TRP   A 219 ? 0.4049 0.8227 0.6886 -0.0947 -0.1047 -0.2593 375 TRP   A CD1 
1355 C  CD2 . TRP   A 219 ? 0.4120 0.8362 0.6876 -0.0633 -0.1171 -0.2466 375 TRP   A CD2 
1356 N  NE1 . TRP   A 219 ? 0.3521 0.8055 0.6496 -0.0852 -0.1111 -0.2690 375 TRP   A NE1 
1357 C  CE2 . TRP   A 219 ? 0.3641 0.8214 0.6563 -0.0654 -0.1188 -0.2613 375 TRP   A CE2 
1358 C  CE3 . TRP   A 219 ? 0.3801 0.8002 0.6467 -0.0448 -0.1237 -0.2365 375 TRP   A CE3 
1359 C  CZ2 . TRP   A 219 ? 0.3438 0.8301 0.6437 -0.0489 -0.1271 -0.2661 375 TRP   A CZ2 
1360 C  CZ3 . TRP   A 219 ? 0.3205 0.7670 0.5934 -0.0284 -0.1317 -0.2406 375 TRP   A CZ3 
1361 C  CH2 . TRP   A 219 ? 0.3574 0.8368 0.6467 -0.0302 -0.1335 -0.2554 375 TRP   A CH2 
1362 N  N   . ARG   A 220 ? 0.3092 0.6072 0.5173 -0.0749 -0.1097 -0.2103 376 ARG   A N   
1363 C  CA  . ARG   A 220 ? 0.3018 0.5672 0.4939 -0.0765 -0.1060 -0.1999 376 ARG   A CA  
1364 C  C   . ARG   A 220 ? 0.2918 0.5500 0.4858 -0.0722 -0.1020 -0.1899 376 ARG   A C   
1365 O  O   . ARG   A 220 ? 0.2985 0.5738 0.4977 -0.0596 -0.1074 -0.1881 376 ARG   A O   
1366 C  CB  . ARG   A 220 ? 0.3750 0.6316 0.5483 -0.0642 -0.1158 -0.1964 376 ARG   A CB  
1367 C  CG  . ARG   A 220 ? 0.3934 0.6173 0.5500 -0.0664 -0.1119 -0.1875 376 ARG   A CG  
1368 C  CD  . ARG   A 220 ? 0.3050 0.5212 0.4426 -0.0556 -0.1207 -0.1855 376 ARG   A CD  
1369 N  NE  . ARG   A 220 ? 0.3987 0.6225 0.5293 -0.0376 -0.1292 -0.1788 376 ARG   A NE  
1370 C  CZ  . ARG   A 220 ? 0.5289 0.7506 0.6424 -0.0251 -0.1379 -0.1767 376 ARG   A CZ  
1371 N  NH1 . ARG   A 220 ? 0.4638 0.6782 0.5666 -0.0283 -0.1397 -0.1812 376 ARG   A NH1 
1372 N  NH2 . ARG   A 220 ? 0.4035 0.6288 0.5089 -0.0089 -0.1446 -0.1695 376 ARG   A NH2 
1373 N  N   . LEU   A 221 ? 0.2806 0.5123 0.4692 -0.0822 -0.0925 -0.1836 377 LEU   A N   
1374 C  CA  . LEU   A 221 ? 0.3703 0.5929 0.5603 -0.0800 -0.0875 -0.1744 377 LEU   A CA  
1375 C  C   . LEU   A 221 ? 0.4902 0.7096 0.6693 -0.0630 -0.0964 -0.1662 377 LEU   A C   
1376 O  O   . LEU   A 221 ? 0.3447 0.5532 0.5086 -0.0569 -0.1025 -0.1642 377 LEU   A O   
1377 C  CB  . LEU   A 221 ? 0.2953 0.4873 0.4783 -0.0931 -0.0761 -0.1692 377 LEU   A CB  
1378 C  CG  . LEU   A 221 ? 0.4084 0.5992 0.6009 -0.1096 -0.0647 -0.1741 377 LEU   A CG  
1379 C  CD1 . LEU   A 221 ? 0.2825 0.4384 0.4629 -0.1197 -0.0543 -0.1675 377 LEU   A CD1 
1380 C  CD2 . LEU   A 221 ? 0.3840 0.5959 0.5931 -0.1091 -0.0614 -0.1750 377 LEU   A CD2 
1381 N  N   . SER   A 222 ? 0.3628 0.5909 0.5488 -0.0552 -0.0969 -0.1616 378 SER   A N   
1382 C  CA  . SER   A 222 ? 0.3837 0.6069 0.5591 -0.0393 -0.1044 -0.1531 378 SER   A CA  
1383 C  C   . SER   A 222 ? 0.2994 0.5120 0.4787 -0.0408 -0.0975 -0.1453 378 SER   A C   
1384 O  O   . SER   A 222 ? 0.2613 0.4859 0.4557 -0.0459 -0.0914 -0.1476 378 SER   A O   
1385 C  CB  . SER   A 222 ? 0.3535 0.6003 0.5305 -0.0229 -0.1149 -0.1554 378 SER   A CB  
1386 O  OG  . SER   A 222 ? 0.3320 0.5697 0.4953 -0.0072 -0.1215 -0.1460 378 SER   A OG  
1387 N  N   . PHE   A 223 ? 0.2895 0.4728 0.4489 -0.0351 -0.0947 -0.1316 379 PHE   A N   
1388 C  CA  . PHE   A 223 ? 0.2886 0.4533 0.4431 -0.0336 -0.0866 -0.1193 379 PHE   A CA  
1389 C  C   . PHE   A 223 ? 0.2740 0.4277 0.4117 -0.0174 -0.0913 -0.1079 379 PHE   A C   
1390 O  O   . PHE   A 223 ? 0.3578 0.4891 0.4848 -0.0164 -0.0852 -0.0967 379 PHE   A O   
1391 C  CB  . PHE   A 223 ? 0.3817 0.5189 0.5279 -0.0451 -0.0765 -0.1142 379 PHE   A CB  
1392 C  CG  . PHE   A 223 ? 0.3019 0.4430 0.4613 -0.0620 -0.0695 -0.1236 379 PHE   A CG  
1393 C  CD1 . PHE   A 223 ? 0.2690 0.4155 0.4413 -0.0694 -0.0616 -0.1244 379 PHE   A CD1 
1394 C  CD2 . PHE   A 223 ? 0.2842 0.4225 0.4418 -0.0709 -0.0702 -0.1320 379 PHE   A CD2 
1395 C  CE1 . PHE   A 223 ? 0.2565 0.4044 0.4391 -0.0862 -0.0538 -0.1328 379 PHE   A CE1 
1396 C  CE2 . PHE   A 223 ? 0.3621 0.5010 0.5300 -0.0876 -0.0628 -0.1407 379 PHE   A CE2 
1397 C  CZ  . PHE   A 223 ? 0.3046 0.4467 0.4832 -0.0948 -0.0539 -0.1397 379 PHE   A CZ  
1398 N  N   . SER   A 224 ? 0.3665 0.5348 0.5007 -0.0048 -0.1021 -0.1108 380 SER   A N   
1399 C  CA  . SER   A 224 ? 0.4699 0.6244 0.5849 0.0101  -0.1061 -0.1000 380 SER   A CA  
1400 C  C   . SER   A 224 ? 0.3245 0.4710 0.4397 0.0149  -0.1011 -0.0911 380 SER   A C   
1401 O  O   . SER   A 224 ? 0.3207 0.4455 0.4188 0.0210  -0.0991 -0.0799 380 SER   A O   
1402 C  CB  . SER   A 224 ? 0.4517 0.6245 0.5630 0.0236  -0.1187 -0.1054 380 SER   A CB  
1403 O  OG  . SER   A 224 ? 0.6848 0.8819 0.8117 0.0301  -0.1227 -0.1112 380 SER   A OG  
1404 N  N   . HIS   A 225 ? 0.3062 0.4702 0.4405 0.0115  -0.0985 -0.0966 381 HIS   A N   
1405 C  CA  . HIS   A 225 ? 0.2578 0.4148 0.3930 0.0154  -0.0933 -0.0893 381 HIS   A CA  
1406 C  C   . HIS   A 225 ? 0.2497 0.3802 0.3769 0.0065  -0.0829 -0.0799 381 HIS   A C   
1407 O  O   . HIS   A 225 ? 0.3002 0.4140 0.4163 0.0123  -0.0801 -0.0701 381 HIS   A O   
1408 C  CB  . HIS   A 225 ? 0.3483 0.5316 0.5068 0.0123  -0.0919 -0.0985 381 HIS   A CB  
1409 C  CG  . HIS   A 225 ? 0.2761 0.4678 0.4504 -0.0056 -0.0850 -0.1069 381 HIS   A CG  
1410 N  ND1 . HIS   A 225 ? 0.2297 0.4270 0.4063 -0.0139 -0.0875 -0.1149 381 HIS   A ND1 
1411 C  CD2 . HIS   A 225 ? 0.2147 0.4086 0.4019 -0.0170 -0.0752 -0.1086 381 HIS   A CD2 
1412 C  CE1 . HIS   A 225 ? 0.3195 0.5203 0.5091 -0.0301 -0.0792 -0.1210 381 HIS   A CE1 
1413 N  NE2 . HIS   A 225 ? 0.2926 0.4914 0.4885 -0.0323 -0.0715 -0.1171 381 HIS   A NE2 
1414 N  N   . ILE   A 226 ? 0.2312 0.3568 0.3627 -0.0073 -0.0772 -0.0832 382 ILE   A N   
1415 C  CA  . ILE   A 226 ? 0.1910 0.2922 0.3140 -0.0142 -0.0682 -0.0748 382 ILE   A CA  
1416 C  C   . ILE   A 226 ? 0.3151 0.3963 0.4179 -0.0081 -0.0700 -0.0663 382 ILE   A C   
1417 O  O   . ILE   A 226 ? 0.3058 0.3695 0.3993 -0.0070 -0.0650 -0.0573 382 ILE   A O   
1418 C  CB  . ILE   A 226 ? 0.2188 0.3175 0.3490 -0.0291 -0.0619 -0.0805 382 ILE   A CB  
1419 C  CG1 . ILE   A 226 ? 0.1902 0.3108 0.3409 -0.0367 -0.0595 -0.0903 382 ILE   A CG1 
1420 C  CG2 . ILE   A 226 ? 0.1888 0.2632 0.3099 -0.0342 -0.0530 -0.0719 382 ILE   A CG2 
1421 C  CD1 . ILE   A 226 ? 0.2026 0.3252 0.3600 -0.0357 -0.0538 -0.0864 382 ILE   A CD1 
1422 N  N   . GLU   A 227 ? 0.2867 0.3710 0.3824 -0.0046 -0.0768 -0.0696 383 GLU   A N   
1423 C  CA  . GLU   A 227 ? 0.3469 0.4140 0.4229 0.0012  -0.0781 -0.0621 383 GLU   A CA  
1424 C  C   . GLU   A 227 ? 0.2993 0.3588 0.3654 0.0117  -0.0790 -0.0536 383 GLU   A C   
1425 O  O   . GLU   A 227 ? 0.3406 0.3817 0.3946 0.0120  -0.0744 -0.0451 383 GLU   A O   
1426 C  CB  . GLU   A 227 ? 0.3589 0.4331 0.4285 0.0048  -0.0861 -0.0677 383 GLU   A CB  
1427 C  CG  . GLU   A 227 ? 0.5522 0.6341 0.6308 -0.0055 -0.0860 -0.0777 383 GLU   A CG  
1428 C  CD  . GLU   A 227 ? 0.5481 0.6462 0.6259 -0.0009 -0.0959 -0.0863 383 GLU   A CD  
1429 O  OE1 . GLU   A 227 ? 0.6505 0.7556 0.7218 0.0113  -0.1031 -0.0846 383 GLU   A OE1 
1430 O  OE2 . GLU   A 227 ? 0.5891 0.6923 0.6719 -0.0091 -0.0965 -0.0951 383 GLU   A OE2 
1431 N  N   . LYS   A 228 ? 0.3167 0.3903 0.3876 0.0204  -0.0849 -0.0563 384 LYS   A N   
1432 C  CA  . LYS   A 228 ? 0.3245 0.3887 0.3844 0.0312  -0.0858 -0.0486 384 LYS   A CA  
1433 C  C   . LYS   A 228 ? 0.3849 0.4379 0.4477 0.0267  -0.0772 -0.0427 384 LYS   A C   
1434 O  O   . LYS   A 228 ? 0.4037 0.4381 0.4525 0.0294  -0.0740 -0.0342 384 LYS   A O   
1435 C  CB  . LYS   A 228 ? 0.4185 0.5015 0.4846 0.0424  -0.0939 -0.0538 384 LYS   A CB  
1436 C  CG  . LYS   A 228 ? 0.5104 0.5801 0.5603 0.0558  -0.0960 -0.0459 384 LYS   A CG  
1437 C  CD  . LYS   A 228 ? 0.6785 0.7629 0.7405 0.0635  -0.0982 -0.0494 384 LYS   A CD  
1438 C  CE  . LYS   A 228 ? 0.7402 0.8340 0.7945 0.0802  -0.1090 -0.0519 384 LYS   A CE  
1439 N  NZ  . LYS   A 228 ? 0.6799 0.7830 0.7415 0.0908  -0.1109 -0.0535 384 LYS   A NZ  
1440 N  N   . GLU   A 229 ? 0.2764 0.3405 0.3569 0.0194  -0.0731 -0.0474 385 GLU   A N   
1441 C  CA  . GLU   A 229 ? 0.3221 0.3765 0.4048 0.0158  -0.0653 -0.0422 385 GLU   A CA  
1442 C  C   . GLU   A 229 ? 0.3844 0.4186 0.4564 0.0094  -0.0593 -0.0357 385 GLU   A C   
1443 O  O   . GLU   A 229 ? 0.2696 0.2907 0.3349 0.0102  -0.0549 -0.0291 385 GLU   A O   
1444 C  CB  . GLU   A 229 ? 0.3440 0.4134 0.4460 0.0080  -0.0612 -0.0487 385 GLU   A CB  
1445 C  CG  . GLU   A 229 ? 0.5846 0.6460 0.6883 0.0064  -0.0540 -0.0439 385 GLU   A CG  
1446 C  CD  . GLU   A 229 ? 0.6696 0.7477 0.7915 0.0007  -0.0500 -0.0505 385 GLU   A CD  
1447 O  OE1 . GLU   A 229 ? 0.5718 0.6704 0.7065 -0.0007 -0.0535 -0.0594 385 GLU   A OE1 
1448 O  OE2 . GLU   A 229 ? 0.9629 1.0342 1.0861 -0.0027 -0.0431 -0.0472 385 GLU   A OE2 
1449 N  N   . ILE   A 230 ? 0.3471 0.3793 0.4175 0.0032  -0.0591 -0.0380 386 ILE   A N   
1450 C  CA  . ILE   A 230 ? 0.3110 0.3264 0.3717 -0.0013 -0.0540 -0.0327 386 ILE   A CA  
1451 C  C   . ILE   A 230 ? 0.4852 0.4888 0.5291 0.0050  -0.0556 -0.0263 386 ILE   A C   
1452 O  O   . ILE   A 230 ? 0.5565 0.5476 0.5932 0.0038  -0.0508 -0.0205 386 ILE   A O   
1453 C  CB  . ILE   A 230 ? 0.4029 0.4184 0.4656 -0.0086 -0.0533 -0.0374 386 ILE   A CB  
1454 C  CG1 . ILE   A 230 ? 0.2568 0.2760 0.3323 -0.0173 -0.0483 -0.0415 386 ILE   A CG1 
1455 C  CG2 . ILE   A 230 ? 0.4555 0.4559 0.5059 -0.0098 -0.0502 -0.0327 386 ILE   A CG2 
1456 C  CD1 . ILE   A 230 ? 0.3901 0.4067 0.4664 -0.0247 -0.0471 -0.0467 386 ILE   A CD1 
1457 N  N   . LEU   A 231 ? 0.3665 0.3739 0.4033 0.0117  -0.0620 -0.0277 387 LEU   A N   
1458 C  CA  . LEU   A 231 ? 0.3586 0.3526 0.3769 0.0168  -0.0626 -0.0215 387 LEU   A CA  
1459 C  C   . LEU   A 231 ? 0.3532 0.3366 0.3647 0.0212  -0.0599 -0.0151 387 LEU   A C   
1460 O  O   . LEU   A 231 ? 0.4327 0.4015 0.4309 0.0205  -0.0562 -0.0094 387 LEU   A O   
1461 C  CB  . LEU   A 231 ? 0.3503 0.3497 0.3603 0.0242  -0.0703 -0.0241 387 LEU   A CB  
1462 C  CG  . LEU   A 231 ? 0.4924 0.4892 0.4946 0.0209  -0.0708 -0.0259 387 LEU   A CG  
1463 C  CD1 . LEU   A 231 ? 0.5081 0.5163 0.5078 0.0270  -0.0795 -0.0315 387 LEU   A CD1 
1464 C  CD2 . LEU   A 231 ? 0.4829 0.4626 0.4674 0.0212  -0.0663 -0.0185 387 LEU   A CD2 
1465 N  N   . ASN   A 232 ? 0.3234 0.3142 0.3438 0.0252  -0.0615 -0.0167 388 ASN   A N   
1466 C  CA  . ASN   A 232 ? 0.5013 0.4813 0.5149 0.0301  -0.0592 -0.0114 388 ASN   A CA  
1467 C  C   . ASN   A 232 ? 0.3590 0.3354 0.3805 0.0232  -0.0521 -0.0098 388 ASN   A C   
1468 O  O   . ASN   A 232 ? 0.3940 0.3613 0.4107 0.0261  -0.0497 -0.0062 388 ASN   A O   
1469 C  CB  . ASN   A 232 ? 0.2871 0.2768 0.3042 0.0406  -0.0653 -0.0142 388 ASN   A CB  
1470 C  CG  . ASN   A 232 ? 0.4795 0.4675 0.4825 0.0507  -0.0727 -0.0138 388 ASN   A CG  
1471 O  OD1 . ASN   A 232 ? 0.6472 0.6170 0.6305 0.0527  -0.0715 -0.0077 388 ASN   A OD1 
1472 N  ND2 . ASN   A 232 ? 0.6119 0.6193 0.6243 0.0567  -0.0802 -0.0207 388 ASN   A ND2 
1473 N  N   . ASN   A 233 ? 0.3116 0.2937 0.3436 0.0146  -0.0489 -0.0126 389 ASN   A N   
1474 C  CA  . ASN   A 233 ? 0.2746 0.2534 0.3126 0.0082  -0.0425 -0.0113 389 ASN   A CA  
1475 C  C   . ASN   A 233 ? 0.2446 0.2214 0.2827 0.0010  -0.0399 -0.0120 389 ASN   A C   
1476 O  O   . ASN   A 233 ? 0.2379 0.2209 0.2856 -0.0040 -0.0386 -0.0157 389 ASN   A O   
1477 C  CB  . ASN   A 233 ? 0.2516 0.2424 0.3046 0.0075  -0.0416 -0.0153 389 ASN   A CB  
1478 C  CG  . ASN   A 233 ? 0.2050 0.1904 0.2609 0.0027  -0.0351 -0.0132 389 ASN   A CG  
1479 O  OD1 . ASN   A 233 ? 0.2715 0.2457 0.3196 -0.0003 -0.0317 -0.0093 389 ASN   A OD1 
1480 N  ND2 . ASN   A 233 ? 0.1737 0.1682 0.2408 0.0020  -0.0332 -0.0162 389 ASN   A ND2 
1481 N  N   . HIS   A 234 ? 0.2851 0.2524 0.3115 0.0006  -0.0388 -0.0086 390 HIS   A N   
1482 C  CA  . HIS   A 234 ? 0.2454 0.2124 0.2693 -0.0030 -0.0386 -0.0102 390 HIS   A CA  
1483 C  C   . HIS   A 234 ? 0.2803 0.2411 0.3022 -0.0075 -0.0335 -0.0082 390 HIS   A C   
1484 O  O   . HIS   A 234 ? 0.2546 0.2153 0.2748 -0.0095 -0.0331 -0.0100 390 HIS   A O   
1485 C  CB  . HIS   A 234 ? 0.2236 0.1873 0.2352 0.0008  -0.0418 -0.0090 390 HIS   A CB  
1486 C  CG  . HIS   A 234 ? 0.2392 0.1917 0.2382 0.0026  -0.0393 -0.0035 390 HIS   A CG  
1487 N  ND1 . HIS   A 234 ? 0.2508 0.1980 0.2397 0.0089  -0.0423 -0.0010 390 HIS   A ND1 
1488 C  CD2 . HIS   A 234 ? 0.2475 0.1926 0.2417 -0.0014 -0.0339 -0.0005 390 HIS   A CD2 
1489 C  CE1 . HIS   A 234 ? 0.3027 0.2371 0.2801 0.0079  -0.0380 0.0037  390 HIS   A CE1 
1490 N  NE2 . HIS   A 234 ? 0.3247 0.2592 0.3061 0.0010  -0.0329 0.0036  390 HIS   A NE2 
1491 N  N   . GLY   A 235 ? 0.2470 0.2035 0.2688 -0.0083 -0.0299 -0.0052 391 GLY   A N   
1492 C  CA  . GLY   A 235 ? 0.2461 0.1991 0.2656 -0.0115 -0.0258 -0.0040 391 GLY   A CA  
1493 C  C   . GLY   A 235 ? 0.3030 0.2573 0.3299 -0.0138 -0.0236 -0.0053 391 GLY   A C   
1494 O  O   . GLY   A 235 ? 0.2502 0.2071 0.2841 -0.0141 -0.0238 -0.0065 391 GLY   A O   
1495 N  N   . LYS   A 236 ? 0.3026 0.2551 0.3272 -0.0151 -0.0213 -0.0053 392 LYS   A N   
1496 C  CA  . LYS   A 236 ? 0.1984 0.1492 0.2261 -0.0161 -0.0189 -0.0053 392 LYS   A CA  
1497 C  C   . LYS   A 236 ? 0.2651 0.2149 0.2934 -0.0163 -0.0168 -0.0032 392 LYS   A C   
1498 O  O   . LYS   A 236 ? 0.3025 0.2513 0.3344 -0.0168 -0.0150 -0.0030 392 LYS   A O   
1499 C  CB  . LYS   A 236 ? 0.2615 0.2112 0.2853 -0.0153 -0.0179 -0.0062 392 LYS   A CB  
1500 C  CG  . LYS   A 236 ? 0.3433 0.2896 0.3669 -0.0147 -0.0157 -0.0055 392 LYS   A CG  
1501 C  CD  . LYS   A 236 ? 0.3190 0.2647 0.3378 -0.0117 -0.0157 -0.0068 392 LYS   A CD  
1502 C  CE  . LYS   A 236 ? 0.2877 0.2278 0.3045 -0.0108 -0.0165 -0.0087 392 LYS   A CE  
1503 N  NZ  . LYS   A 236 ? 0.4100 0.3428 0.4286 -0.0135 -0.0149 -0.0084 392 LYS   A NZ  
1504 N  N   . SER   A 237 ? 0.2821 0.2311 0.3061 -0.0163 -0.0163 -0.0018 393 SER   A N   
1505 C  CA  . SER   A 237 ? 0.3829 0.3294 0.4064 -0.0166 -0.0145 -0.0003 393 SER   A CA  
1506 C  C   . SER   A 237 ? 0.3038 0.2490 0.3289 -0.0144 -0.0159 0.0004  393 SER   A C   
1507 O  O   . SER   A 237 ? 0.2308 0.1758 0.2534 -0.0125 -0.0185 0.0006  393 SER   A O   
1508 C  CB  . SER   A 237 ? 0.2404 0.1852 0.2578 -0.0187 -0.0127 0.0001  393 SER   A CB  
1509 O  OG  . SER   A 237 ? 0.2547 0.1943 0.2699 -0.0192 -0.0111 0.0013  393 SER   A OG  
1510 N  N   . LYS   A 238 ? 0.2853 0.2301 0.3141 -0.0137 -0.0145 0.0005  394 LYS   A N   
1511 C  CA  . LYS   A 238 ? 0.2417 0.1872 0.2730 -0.0101 -0.0160 0.0005  394 LYS   A CA  
1512 C  C   . LYS   A 238 ? 0.2473 0.1848 0.2696 -0.0077 -0.0166 0.0025  394 LYS   A C   
1513 O  O   . LYS   A 238 ? 0.2421 0.1790 0.2630 -0.0028 -0.0195 0.0027  394 LYS   A O   
1514 C  CB  . LYS   A 238 ? 0.2666 0.2141 0.3037 -0.0099 -0.0135 -0.0004 394 LYS   A CB  
1515 C  CG  . LYS   A 238 ? 0.2627 0.2164 0.3075 -0.0124 -0.0122 -0.0024 394 LYS   A CG  
1516 C  CD  . LYS   A 238 ? 0.1840 0.1375 0.2313 -0.0134 -0.0081 -0.0026 394 LYS   A CD  
1517 C  CE  . LYS   A 238 ? 0.1898 0.1460 0.2418 -0.0171 -0.0055 -0.0040 394 LYS   A CE  
1518 N  NZ  . LYS   A 238 ? 0.3096 0.2638 0.3611 -0.0183 -0.0008 -0.0036 394 LYS   A NZ  
1519 N  N   . THR   A 239 ? 0.2281 0.1590 0.2433 -0.0109 -0.0139 0.0038  395 THR   A N   
1520 C  CA  . THR   A 239 ? 0.3724 0.2922 0.3766 -0.0105 -0.0130 0.0058  395 THR   A CA  
1521 C  C   . THR   A 239 ? 0.3523 0.2698 0.3490 -0.0123 -0.0135 0.0069  395 THR   A C   
1522 O  O   . THR   A 239 ? 0.2193 0.1265 0.2053 -0.0147 -0.0109 0.0085  395 THR   A O   
1523 C  CB  . THR   A 239 ? 0.3051 0.2188 0.3055 -0.0147 -0.0089 0.0055  395 THR   A CB  
1524 O  OG1 . THR   A 239 ? 0.3234 0.2451 0.3284 -0.0192 -0.0075 0.0036  395 THR   A OG1 
1525 C  CG2 . THR   A 239 ? 0.2762 0.1878 0.2795 -0.0115 -0.0082 0.0050  395 THR   A CG2 
1526 N  N   . CYS   A 240 ? 0.2770 0.2028 0.2783 -0.0118 -0.0161 0.0057  396 CYS   A N   
1527 C  CA  . CYS   A 240 ? 0.3342 0.2584 0.3279 -0.0128 -0.0166 0.0063  396 CYS   A CA  
1528 C  C   . CYS   A 240 ? 0.3419 0.2554 0.3239 -0.0086 -0.0179 0.0092  396 CYS   A C   
1529 O  O   . CYS   A 240 ? 0.4225 0.3366 0.4061 -0.0022 -0.0219 0.0093  396 CYS   A O   
1530 C  CB  . CYS   A 240 ? 0.4049 0.3387 0.4050 -0.0117 -0.0198 0.0040  396 CYS   A CB  
1531 S  SG  . CYS   A 240 ? 0.3257 0.2590 0.3166 -0.0128 -0.0200 0.0040  396 CYS   A SG  
1532 N  N   . CYS   A 241 ? 0.3017 0.2051 0.2712 -0.0121 -0.0144 0.0112  397 CYS   A N   
1533 C  CA  . CYS   A 241 ? 0.3259 0.2144 0.2792 -0.0086 -0.0146 0.0149  397 CYS   A CA  
1534 C  C   . CYS   A 241 ? 0.3997 0.2752 0.3471 -0.0047 -0.0140 0.0169  397 CYS   A C   
1535 O  O   . CYS   A 241 ? 0.3882 0.2503 0.3217 0.0014  -0.0156 0.0201  397 CYS   A O   
1536 C  CB  . CYS   A 241 ? 0.4494 0.3422 0.4008 -0.0015 -0.0206 0.0150  397 CYS   A CB  
1537 S  SG  . CYS   A 241 ? 0.3808 0.2815 0.3307 -0.0056 -0.0202 0.0133  397 CYS   A SG  
1538 N  N   . GLU   A 242 ? 0.3257 0.2040 0.2818 -0.0072 -0.0120 0.0152  398 GLU   A N   
1539 C  CA  . GLU   A 242 ? 0.3425 0.2073 0.2922 -0.0041 -0.0106 0.0165  398 GLU   A CA  
1540 C  C   . GLU   A 242 ? 0.3337 0.1847 0.2734 -0.0125 -0.0038 0.0170  398 GLU   A C   
1541 O  O   . GLU   A 242 ? 0.4851 0.3211 0.4166 -0.0109 -0.0018 0.0180  398 GLU   A O   
1542 C  CB  . GLU   A 242 ? 0.4095 0.2853 0.3741 -0.0012 -0.0123 0.0137  398 GLU   A CB  
1543 C  CG  . GLU   A 242 ? 0.4480 0.3358 0.4219 0.0069  -0.0182 0.0125  398 GLU   A CG  
1544 C  CD  . GLU   A 242 ? 0.4263 0.3224 0.4124 0.0097  -0.0185 0.0099  398 GLU   A CD  
1545 O  OE1 . GLU   A 242 ? 0.5340 0.4273 0.5215 0.0052  -0.0145 0.0092  398 GLU   A OE1 
1546 O  OE2 . GLU   A 242 ? 0.3800 0.2864 0.3741 0.0161  -0.0227 0.0080  398 GLU   A OE2 
1547 N  N   . ASN   A 243 ? 0.4023 0.2583 0.3424 -0.0215 -0.0001 0.0157  399 ASN   A N   
1548 C  CA  . ASN   A 243 ? 0.3856 0.2318 0.3178 -0.0313 0.0068  0.0147  399 ASN   A CA  
1549 C  C   . ASN   A 243 ? 0.3887 0.2387 0.3167 -0.0386 0.0103  0.0142  399 ASN   A C   
1550 O  O   . ASN   A 243 ? 0.4587 0.3211 0.3923 -0.0361 0.0071  0.0140  399 ASN   A O   
1551 C  CB  . ASN   A 243 ? 0.2637 0.1203 0.2083 -0.0360 0.0083  0.0103  399 ASN   A CB  
1552 C  CG  . ASN   A 243 ? 0.4017 0.2811 0.3622 -0.0368 0.0057  0.0071  399 ASN   A CG  
1553 O  OD1 . ASN   A 243 ? 0.3878 0.2757 0.3496 -0.0412 0.0070  0.0057  399 ASN   A OD1 
1554 N  ND2 . ASN   A 243 ? 0.3320 0.2204 0.3036 -0.0322 0.0024  0.0059  399 ASN   A ND2 
1555 N  N   . LYS   A 244 ? 0.3948 0.2340 0.3128 -0.0484 0.0175  0.0135  400 LYS   A N   
1556 C  CA  . LYS   A 244 ? 0.4333 0.2762 0.3466 -0.0566 0.0223  0.0125  400 LYS   A CA  
1557 C  C   . LYS   A 244 ? 0.4229 0.2927 0.3543 -0.0596 0.0210  0.0071  400 LYS   A C   
1558 O  O   . LYS   A 244 ? 0.4359 0.3146 0.3674 -0.0611 0.0218  0.0064  400 LYS   A O   
1559 C  CB  . LYS   A 244 ? 0.4464 0.2736 0.3467 -0.0685 0.0314  0.0115  400 LYS   A CB  
1560 C  CG  . LYS   A 244 ? 0.5638 0.3594 0.4399 -0.0667 0.0346  0.0175  400 LYS   A CG  
1561 C  CD  . LYS   A 244 ? 0.6241 0.4045 0.4881 -0.0812 0.0449  0.0155  400 LYS   A CD  
1562 C  CE  . LYS   A 244 ? 0.5372 0.2814 0.3731 -0.0801 0.0494  0.0219  400 LYS   A CE  
1563 N  NZ  . LYS   A 244 ? 0.8485 0.5755 0.6735 -0.0949 0.0598  0.0191  400 LYS   A NZ  
1564 N  N   . GLU   A 245 ? 0.3688 0.2509 0.3140 -0.0597 0.0191  0.0033  401 GLU   A N   
1565 C  CA  . GLU   A 245 ? 0.4672 0.3729 0.4275 -0.0608 0.0175  -0.0017 401 GLU   A CA  
1566 C  C   . GLU   A 245 ? 0.3806 0.2959 0.3475 -0.0522 0.0115  -0.0003 401 GLU   A C   
1567 O  O   . GLU   A 245 ? 0.4579 0.3893 0.4327 -0.0526 0.0108  -0.0037 401 GLU   A O   
1568 C  CB  . GLU   A 245 ? 0.4039 0.3178 0.3744 -0.0613 0.0162  -0.0054 401 GLU   A CB  
1569 C  CG  . GLU   A 245 ? 0.4692 0.4057 0.4521 -0.0636 0.0156  -0.0115 401 GLU   A CG  
1570 C  CD  . GLU   A 245 ? 0.8441 0.7876 0.8256 -0.0746 0.0219  -0.0166 401 GLU   A CD  
1571 O  OE1 . GLU   A 245 ? 0.5882 0.5208 0.5628 -0.0827 0.0270  -0.0177 401 GLU   A OE1 
1572 O  OE2 . GLU   A 245 ? 0.8544 0.8143 0.8417 -0.0753 0.0221  -0.0199 401 GLU   A OE2 
1573 N  N   . GLU   A 246 ? 0.3443 0.2505 0.3081 -0.0444 0.0072  0.0039  402 GLU   A N   
1574 C  CA  . GLU   A 246 ? 0.4017 0.3170 0.3730 -0.0371 0.0015  0.0043  402 GLU   A CA  
1575 C  C   . GLU   A 246 ? 0.3569 0.2638 0.3186 -0.0325 -0.0008 0.0078  402 GLU   A C   
1576 O  O   . GLU   A 246 ? 0.3632 0.2706 0.3280 -0.0255 -0.0060 0.0090  402 GLU   A O   
1577 C  CB  . GLU   A 246 ? 0.3365 0.2544 0.3171 -0.0319 -0.0024 0.0043  402 GLU   A CB  
1578 C  CG  . GLU   A 246 ? 0.3414 0.2668 0.3299 -0.0348 -0.0009 0.0012  402 GLU   A CG  
1579 C  CD  . GLU   A 246 ? 0.3530 0.2798 0.3487 -0.0297 -0.0040 0.0016  402 GLU   A CD  
1580 O  OE1 . GLU   A 246 ? 0.4040 0.3386 0.4066 -0.0263 -0.0068 0.0010  402 GLU   A OE1 
1581 O  OE2 . GLU   A 246 ? 0.3738 0.2930 0.3675 -0.0293 -0.0029 0.0023  402 GLU   A OE2 
1582 N  N   . LYS   A 247 ? 0.3884 0.2882 0.3379 -0.0365 0.0031  0.0091  403 LYS   A N   
1583 C  CA  . LYS   A 247 ? 0.4696 0.3619 0.4079 -0.0316 0.0007  0.0122  403 LYS   A CA  
1584 C  C   . LYS   A 247 ? 0.3753 0.2818 0.3196 -0.0306 -0.0015 0.0094  403 LYS   A C   
1585 O  O   . LYS   A 247 ? 0.3380 0.2535 0.2849 -0.0363 0.0025  0.0064  403 LYS   A O   
1586 C  CB  . LYS   A 247 ? 0.4127 0.2871 0.3314 -0.0362 0.0066  0.0156  403 LYS   A CB  
1587 C  CG  . LYS   A 247 ? 0.4111 0.2648 0.3178 -0.0333 0.0071  0.0197  403 LYS   A CG  
1588 C  CD  . LYS   A 247 ? 0.5726 0.4257 0.4816 -0.0213 -0.0010 0.0216  403 LYS   A CD  
1589 C  CE  . LYS   A 247 ? 0.4752 0.3062 0.3688 -0.0159 -0.0009 0.0259  403 LYS   A CE  
1590 N  NZ  . LYS   A 247 ? 0.5103 0.3273 0.3970 -0.0245 0.0066  0.0261  403 LYS   A NZ  
1591 N  N   . CYS   A 248 ? 0.3570 0.2666 0.3040 -0.0233 -0.0078 0.0097  404 CYS   A N   
1592 C  CA  . CYS   A 248 ? 0.2948 0.2154 0.2459 -0.0217 -0.0103 0.0067  404 CYS   A CA  
1593 C  C   . CYS   A 248 ? 0.3718 0.2853 0.3092 -0.0174 -0.0128 0.0089  404 CYS   A C   
1594 O  O   . CYS   A 248 ? 0.4182 0.3183 0.3434 -0.0144 -0.0134 0.0130  404 CYS   A O   
1595 C  CB  . CYS   A 248 ? 0.3108 0.2418 0.2770 -0.0180 -0.0154 0.0038  404 CYS   A CB  
1596 S  SG  . CYS   A 248 ? 0.2870 0.2174 0.2541 -0.0103 -0.0229 0.0042  404 CYS   A SG  
1597 N  N   . CYS   A 249 ? 0.3185 0.2402 0.2567 -0.0164 -0.0145 0.0061  405 CYS   A N   
1598 C  CA  . CYS   A 249 ? 0.3950 0.3113 0.3190 -0.0126 -0.0168 0.0074  405 CYS   A CA  
1599 C  C   . CYS   A 249 ? 0.4101 0.3349 0.3408 -0.0066 -0.0244 0.0040  405 CYS   A C   
1600 O  O   . CYS   A 249 ? 0.3644 0.2895 0.2860 -0.0041 -0.0265 0.0030  405 CYS   A O   
1601 C  CB  . CYS   A 249 ? 0.3936 0.3105 0.3084 -0.0177 -0.0107 0.0066  405 CYS   A CB  
1602 S  SG  . CYS   A 249 ? 0.3516 0.2869 0.2814 -0.0202 -0.0097 -0.0002 405 CYS   A SG  
1603 N  N   . ARG   A 250 ? 0.2530 0.1847 0.1988 -0.0050 -0.0282 0.0018  406 ARG   A N   
1604 C  CA  . ARG   A 250 ? 0.3488 0.2891 0.3021 -0.0013 -0.0347 -0.0025 406 ARG   A CA  
1605 C  C   . ARG   A 250 ? 0.2546 0.1919 0.1974 0.0054  -0.0405 -0.0016 406 ARG   A C   
1606 O  O   . ARG   A 250 ? 0.3917 0.3328 0.3298 0.0077  -0.0440 -0.0046 406 ARG   A O   
1607 C  CB  . ARG   A 250 ? 0.2989 0.2452 0.2688 -0.0018 -0.0363 -0.0044 406 ARG   A CB  
1608 C  CG  . ARG   A 250 ? 0.2091 0.1597 0.1891 -0.0065 -0.0326 -0.0066 406 ARG   A CG  
1609 C  CD  . ARG   A 250 ? 0.2844 0.2388 0.2778 -0.0070 -0.0338 -0.0081 406 ARG   A CD  
1610 N  NE  . ARG   A 250 ? 0.2338 0.1898 0.2342 -0.0101 -0.0308 -0.0098 406 ARG   A NE  
1611 C  CZ  . ARG   A 250 ? 0.2465 0.2010 0.2488 -0.0120 -0.0269 -0.0077 406 ARG   A CZ  
1612 N  NH1 . ARG   A 250 ? 0.2125 0.1631 0.2107 -0.0126 -0.0248 -0.0043 406 ARG   A NH1 
1613 N  NH2 . ARG   A 250 ? 0.3676 0.3235 0.3748 -0.0131 -0.0252 -0.0095 406 ARG   A NH2 
1614 N  N   . LYS   A 251 ? 0.3085 0.2387 0.2466 0.0096  -0.0418 0.0023  407 LYS   A N   
1615 C  CA  . LYS   A 251 ? 0.3201 0.2477 0.2476 0.0182  -0.0483 0.0031  407 LYS   A CA  
1616 C  C   . LYS   A 251 ? 0.3628 0.2807 0.2690 0.0198  -0.0471 0.0058  407 LYS   A C   
1617 O  O   . LYS   A 251 ? 0.3510 0.2723 0.2502 0.0258  -0.0533 0.0037  407 LYS   A O   
1618 C  CB  . LYS   A 251 ? 0.3165 0.2356 0.2407 0.0233  -0.0490 0.0071  407 LYS   A CB  
1619 C  CG  . LYS   A 251 ? 0.4369 0.3673 0.3809 0.0239  -0.0514 0.0038  407 LYS   A CG  
1620 C  CD  . LYS   A 251 ? 0.3963 0.3174 0.3351 0.0301  -0.0519 0.0076  407 LYS   A CD  
1621 C  CE  . LYS   A 251 ? 0.6223 0.5583 0.5776 0.0351  -0.0575 0.0030  407 LYS   A CE  
1622 N  NZ  . LYS   A 251 ? 0.6078 0.5355 0.5564 0.0441  -0.0593 0.0059  407 LYS   A NZ  
1623 N  N   . ASP   A 252 ? 0.4244 0.3308 0.3199 0.0140  -0.0390 0.0100  408 ASP   A N   
1624 C  CA  . ASP   A 252 ? 0.3163 0.2128 0.1906 0.0140  -0.0361 0.0126  408 ASP   A CA  
1625 C  C   . ASP   A 252 ? 0.3775 0.2860 0.2551 0.0129  -0.0380 0.0072  408 ASP   A C   
1626 O  O   . ASP   A 252 ? 0.3944 0.2999 0.2568 0.0176  -0.0410 0.0073  408 ASP   A O   
1627 C  CB  . ASP   A 252 ? 0.5132 0.3982 0.3789 0.0055  -0.0257 0.0166  408 ASP   A CB  
1628 C  CG  . ASP   A 252 ? 0.6355 0.5016 0.4884 0.0073  -0.0232 0.0228  408 ASP   A CG  
1629 O  OD1 . ASP   A 252 ? 0.7338 0.5924 0.5773 0.0171  -0.0296 0.0252  408 ASP   A OD1 
1630 O  OD2 . ASP   A 252 ? 1.0030 0.8617 0.8548 -0.0009 -0.0151 0.0247  408 ASP   A OD2 
1631 N  N   . CYS   A 253 ? 0.3378 0.2587 0.2334 0.0075  -0.0362 0.0024  409 CYS   A N   
1632 C  CA  . CYS   A 253 ? 0.3881 0.3189 0.2868 0.0069  -0.0379 -0.0034 409 CYS   A CA  
1633 C  C   . CYS   A 253 ? 0.3888 0.3261 0.2889 0.0135  -0.0474 -0.0075 409 CYS   A C   
1634 O  O   . CYS   A 253 ? 0.3290 0.2680 0.2192 0.0160  -0.0499 -0.0102 409 CYS   A O   
1635 C  CB  . CYS   A 253 ? 0.4078 0.3483 0.3250 0.0016  -0.0352 -0.0076 409 CYS   A CB  
1636 S  SG  . CYS   A 253 ? 0.4222 0.3618 0.3377 -0.0057 -0.0249 -0.0062 409 CYS   A SG  
1637 N  N   . LEU   A 254 ? 0.2842 0.2266 0.1967 0.0162  -0.0525 -0.0086 410 LEU   A N   
1638 C  CA  . LEU   A 254 ? 0.3280 0.2799 0.2440 0.0219  -0.0616 -0.0138 410 LEU   A CA  
1639 C  C   . LEU   A 254 ? 0.3386 0.2840 0.2339 0.0303  -0.0663 -0.0110 410 LEU   A C   
1640 O  O   . LEU   A 254 ? 0.4226 0.3743 0.3126 0.0342  -0.0723 -0.0157 410 LEU   A O   
1641 C  CB  . LEU   A 254 ? 0.3730 0.3328 0.3064 0.0228  -0.0652 -0.0157 410 LEU   A CB  
1642 C  CG  . LEU   A 254 ? 0.5247 0.4977 0.4637 0.0281  -0.0746 -0.0223 410 LEU   A CG  
1643 C  CD1 . LEU   A 254 ? 0.3280 0.3092 0.2719 0.0239  -0.0763 -0.0300 410 LEU   A CD1 
1644 C  CD2 . LEU   A 254 ? 0.3568 0.3397 0.3136 0.0285  -0.0771 -0.0248 410 LEU   A CD2 
1645 N  N   . LYS   A 255 ? 0.3519 0.2832 0.2336 0.0337  -0.0638 -0.0035 411 LYS   A N   
1646 C  CA  . LYS   A 255 ? 0.3454 0.2664 0.2036 0.0429  -0.0679 0.0003  411 LYS   A CA  
1647 C  C   . LYS   A 255 ? 0.4136 0.3290 0.2537 0.0414  -0.0649 0.0006  411 LYS   A C   
1648 O  O   . LYS   A 255 ? 0.3745 0.2904 0.2005 0.0489  -0.0713 -0.0008 411 LYS   A O   
1649 C  CB  . LYS   A 255 ? 0.3577 0.2600 0.2022 0.0458  -0.0639 0.0087  411 LYS   A CB  
1650 C  CG  . LYS   A 255 ? 0.4919 0.3986 0.3489 0.0514  -0.0688 0.0084  411 LYS   A CG  
1651 C  CD  . LYS   A 255 ? 0.6533 0.5396 0.4985 0.0518  -0.0628 0.0163  411 LYS   A CD  
1652 C  CE  . LYS   A 255 ? 0.7768 0.6631 0.6235 0.0630  -0.0697 0.0168  411 LYS   A CE  
1653 N  NZ  . LYS   A 255 ? 0.7838 0.6938 0.6597 0.0618  -0.0743 0.0093  411 LYS   A NZ  
1654 N  N   . LEU   A 256 ? 0.3570 0.2685 0.1973 0.0320  -0.0553 0.0020  412 LEU   A N   
1655 C  CA  . LEU   A 256 ? 0.3948 0.3024 0.2187 0.0300  -0.0512 0.0018  412 LEU   A CA  
1656 C  C   . LEU   A 256 ? 0.3673 0.2900 0.1987 0.0316  -0.0575 -0.0068 412 LEU   A C   
1657 O  O   . LEU   A 256 ? 0.3978 0.3184 0.2120 0.0355  -0.0597 -0.0079 412 LEU   A O   
1658 C  CB  . LEU   A 256 ? 0.4296 0.3341 0.2559 0.0196  -0.0397 0.0035  412 LEU   A CB  
1659 C  CG  . LEU   A 256 ? 0.3988 0.2862 0.2133 0.0160  -0.0317 0.0113  412 LEU   A CG  
1660 C  CD1 . LEU   A 256 ? 0.3910 0.2828 0.2167 0.0050  -0.0218 0.0103  412 LEU   A CD1 
1661 C  CD2 . LEU   A 256 ? 0.4380 0.3073 0.2214 0.0192  -0.0289 0.0171  412 LEU   A CD2 
1662 N  N   . MET   A 257 ? 0.3377 0.2744 0.1933 0.0282  -0.0601 -0.0131 413 MET   A N   
1663 C  CA  . MET   A 257 ? 0.3616 0.3107 0.2244 0.0288  -0.0659 -0.0220 413 MET   A CA  
1664 C  C   . MET   A 257 ? 0.3464 0.3006 0.2022 0.0377  -0.0766 -0.0250 413 MET   A C   
1665 O  O   . MET   A 257 ? 0.4069 0.3643 0.2520 0.0407  -0.0806 -0.0295 413 MET   A O   
1666 C  CB  . MET   A 257 ? 0.3109 0.2702 0.1991 0.0231  -0.0658 -0.0274 413 MET   A CB  
1667 C  CG  . MET   A 257 ? 0.4341 0.3925 0.3282 0.0162  -0.0576 -0.0283 413 MET   A CG  
1668 S  SD  . MET   A 257 ? 0.6581 0.6180 0.5403 0.0162  -0.0563 -0.0339 413 MET   A SD  
1669 C  CE  . MET   A 257 ? 0.5868 0.5565 0.4760 0.0190  -0.0669 -0.0435 413 MET   A CE  
1670 N  N   . LYS   A 258 ? 0.3510 0.3072 0.2126 0.0426  -0.0817 -0.0232 414 LYS   A N   
1671 C  CA  . LYS   A 258 ? 0.3883 0.3521 0.2445 0.0525  -0.0928 -0.0267 414 LYS   A CA  
1672 C  C   . LYS   A 258 ? 0.3968 0.3478 0.2225 0.0606  -0.0942 -0.0217 414 LYS   A C   
1673 O  O   . LYS   A 258 ? 0.4508 0.4089 0.2676 0.0670  -0.1022 -0.0269 414 LYS   A O   
1674 C  CB  . LYS   A 258 ? 0.3923 0.3603 0.2595 0.0572  -0.0969 -0.0252 414 LYS   A CB  
1675 C  CG  . LYS   A 258 ? 0.3857 0.3698 0.2823 0.0505  -0.0977 -0.0321 414 LYS   A CG  
1676 C  CD  . LYS   A 258 ? 0.4512 0.4371 0.3582 0.0539  -0.0988 -0.0292 414 LYS   A CD  
1677 C  CE  . LYS   A 258 ? 0.6464 0.6422 0.5496 0.0662  -0.1097 -0.0321 414 LYS   A CE  
1678 N  NZ  . LYS   A 258 ? 0.8227 0.8234 0.7389 0.0698  -0.1108 -0.0310 414 LYS   A NZ  
1679 N  N   . TYR   A 259 ? 0.4407 0.3723 0.2491 0.0600  -0.0861 -0.0119 415 TYR   A N   
1680 C  CA  . TYR   A 259 ? 0.4439 0.3593 0.2201 0.0670  -0.0858 -0.0060 415 TYR   A CA  
1681 C  C   . TYR   A 259 ? 0.4870 0.4041 0.2528 0.0635  -0.0831 -0.0097 415 TYR   A C   
1682 O  O   . TYR   A 259 ? 0.5369 0.4500 0.2806 0.0714  -0.0880 -0.0098 415 TYR   A O   
1683 C  CB  . TYR   A 259 ? 0.4933 0.3858 0.2542 0.0645  -0.0758 0.0048  415 TYR   A CB  
1684 C  CG  . TYR   A 259 ? 0.5988 0.4696 0.3234 0.0717  -0.0744 0.0124  415 TYR   A CG  
1685 C  CD1 . TYR   A 259 ? 0.6376 0.5055 0.3454 0.0864  -0.0852 0.0132  415 TYR   A CD1 
1686 C  CD2 . TYR   A 259 ? 0.6606 0.5136 0.3669 0.0639  -0.0620 0.0187  415 TYR   A CD2 
1687 C  CE1 . TYR   A 259 ? 0.7751 0.6199 0.4463 0.0939  -0.0837 0.0209  415 TYR   A CE1 
1688 C  CE2 . TYR   A 259 ? 0.7305 0.5607 0.4012 0.0695  -0.0593 0.0262  415 TYR   A CE2 
1689 C  CZ  . TYR   A 259 ? 0.6449 0.4695 0.2969 0.0849  -0.0702 0.0278  415 TYR   A CZ  
1690 O  OH  . TYR   A 259 ? 0.7118 0.5108 0.3250 0.0913  -0.0674 0.0359  415 TYR   A OH  
1691 N  N   . LEU   A 260 ? 0.4878 0.4105 0.2682 0.0527  -0.0756 -0.0130 416 LEU   A N   
1692 C  CA  . LEU   A 260 ? 0.4212 0.3475 0.1944 0.0498  -0.0732 -0.0180 416 LEU   A CA  
1693 C  C   . LEU   A 260 ? 0.4234 0.3642 0.1999 0.0555  -0.0847 -0.0275 416 LEU   A C   
1694 O  O   . LEU   A 260 ? 0.4812 0.4199 0.2375 0.0604  -0.0874 -0.0293 416 LEU   A O   
1695 C  CB  . LEU   A 260 ? 0.4314 0.3636 0.2234 0.0390  -0.0646 -0.0211 416 LEU   A CB  
1696 C  CG  . LEU   A 260 ? 0.5851 0.5225 0.3739 0.0356  -0.0611 -0.0273 416 LEU   A CG  
1697 C  CD1 . LEU   A 260 ? 0.4265 0.3519 0.1869 0.0367  -0.0547 -0.0223 416 LEU   A CD1 
1698 C  CD2 . LEU   A 260 ? 0.4214 0.3648 0.2306 0.0271  -0.0539 -0.0301 416 LEU   A CD2 
1699 N  N   . LEU   A 261 ? 0.4511 0.4067 0.2523 0.0545  -0.0912 -0.0342 417 LEU   A N   
1700 C  CA  . LEU   A 261 ? 0.4065 0.3775 0.2129 0.0583  -0.1019 -0.0447 417 LEU   A CA  
1701 C  C   . LEU   A 261 ? 0.4298 0.4005 0.2167 0.0710  -0.1118 -0.0435 417 LEU   A C   
1702 O  O   . LEU   A 261 ? 0.4439 0.4210 0.2199 0.0757  -0.1186 -0.0499 417 LEU   A O   
1703 C  CB  . LEU   A 261 ? 0.3835 0.3699 0.2200 0.0534  -0.1059 -0.0522 417 LEU   A CB  
1704 C  CG  . LEU   A 261 ? 0.3868 0.3902 0.2299 0.0554  -0.1164 -0.0645 417 LEU   A CG  
1705 C  CD1 . LEU   A 261 ? 0.3936 0.3959 0.2286 0.0517  -0.1143 -0.0707 417 LEU   A CD1 
1706 C  CD2 . LEU   A 261 ? 0.3951 0.4132 0.2671 0.0494  -0.1193 -0.0719 417 LEU   A CD2 
1707 N  N   . GLU   A 262 ? 0.4357 0.3987 0.2170 0.0775  -0.1131 -0.0357 418 GLU   A N   
1708 C  CA  . GLU   A 262 ? 0.4603 0.4219 0.2217 0.0918  -0.1232 -0.0342 418 GLU   A CA  
1709 C  C   . GLU   A 262 ? 0.4901 0.4351 0.2166 0.0969  -0.1207 -0.0290 418 GLU   A C   
1710 O  O   . GLU   A 262 ? 0.5095 0.4598 0.2207 0.1064  -0.1302 -0.0333 418 GLU   A O   
1711 C  CB  . GLU   A 262 ? 0.4917 0.4451 0.2526 0.0983  -0.1239 -0.0264 418 GLU   A CB  
1712 C  CG  . GLU   A 262 ? 0.4893 0.4621 0.2823 0.0962  -0.1286 -0.0326 418 GLU   A CG  
1713 C  CD  . GLU   A 262 ? 0.7267 0.6891 0.5202 0.1006  -0.1265 -0.0243 418 GLU   A CD  
1714 O  OE1 . GLU   A 262 ? 0.8180 0.7608 0.5845 0.1102  -0.1263 -0.0154 418 GLU   A OE1 
1715 O  OE2 . GLU   A 262 ? 0.7543 0.7264 0.5737 0.0945  -0.1246 -0.0267 418 GLU   A OE2 
1716 N  N   . GLN   A 263 ? 0.5128 0.4383 0.2260 0.0902  -0.1078 -0.0201 419 GLN   A N   
1717 C  CA  . GLN   A 263 ? 0.5248 0.4335 0.2043 0.0932  -0.1033 -0.0149 419 GLN   A CA  
1718 C  C   . GLN   A 263 ? 0.6624 0.5834 0.3410 0.0911  -0.1057 -0.0245 419 GLN   A C   
1719 O  O   . GLN   A 263 ? 0.6479 0.5644 0.3004 0.0993  -0.1103 -0.0249 419 GLN   A O   
1720 C  CB  . GLN   A 263 ? 0.6434 0.5325 0.3138 0.0837  -0.0876 -0.0054 419 GLN   A CB  
1721 C  CG  . GLN   A 263 ? 0.6622 0.5336 0.3259 0.0860  -0.0842 0.0048  419 GLN   A CG  
1722 C  CD  . GLN   A 263 ? 0.8610 0.7120 0.4886 0.0995  -0.0884 0.0126  419 GLN   A CD  
1723 O  OE1 . GLN   A 263 ? 0.7782 0.6345 0.4044 0.1124  -0.1008 0.0110  419 GLN   A OE1 
1724 N  NE2 . GLN   A 263 ? 0.8535 0.6810 0.4509 0.0967  -0.0778 0.0208  419 GLN   A NE2 
1725 N  N   . LEU   A 264 ? 0.4990 0.4342 0.2042 0.0806  -0.1027 -0.0325 420 LEU   A N   
1726 C  CA  . LEU   A 264 ? 0.5008 0.4462 0.2053 0.0786  -0.1048 -0.0424 420 LEU   A CA  
1727 C  C   . LEU   A 264 ? 0.5443 0.5055 0.2499 0.0873  -0.1199 -0.0520 420 LEU   A C   
1728 O  O   . LEU   A 264 ? 0.5526 0.5160 0.2413 0.0914  -0.1240 -0.0573 420 LEU   A O   
1729 C  CB  . LEU   A 264 ? 0.5162 0.4707 0.2479 0.0667  -0.0985 -0.0487 420 LEU   A CB  
1730 C  CG  . LEU   A 264 ? 0.5169 0.4605 0.2460 0.0582  -0.0838 -0.0424 420 LEU   A CG  
1731 C  CD1 . LEU   A 264 ? 0.4416 0.3948 0.1983 0.0490  -0.0796 -0.0488 420 LEU   A CD1 
1732 C  CD2 . LEU   A 264 ? 0.5799 0.5152 0.2815 0.0596  -0.0784 -0.0414 420 LEU   A CD2 
1733 N  N   . LYS   A 265 ? 0.4952 0.4687 0.2206 0.0901  -0.1283 -0.0551 421 LYS   A N   
1734 C  CA  . LYS   A 265 ? 0.5295 0.5214 0.2581 0.0982  -0.1431 -0.0653 421 LYS   A CA  
1735 C  C   . LYS   A 265 ? 0.5909 0.5750 0.2906 0.1119  -0.1484 -0.0597 421 LYS   A C   
1736 O  O   . LYS   A 265 ? 0.6129 0.6076 0.3102 0.1157  -0.1544 -0.0663 421 LYS   A O   
1737 C  CB  . LYS   A 265 ? 0.4810 0.4891 0.2388 0.0975  -0.1492 -0.0694 421 LYS   A CB  
1738 C  CG  . LYS   A 265 ? 0.4792 0.5001 0.2690 0.0839  -0.1458 -0.0784 421 LYS   A CG  
1739 C  CD  . LYS   A 265 ? 0.4382 0.4710 0.2545 0.0820  -0.1486 -0.0798 421 LYS   A CD  
1740 C  CE  . LYS   A 265 ? 0.4385 0.4947 0.2633 0.0894  -0.1629 -0.0905 421 LYS   A CE  
1741 N  NZ  . LYS   A 265 ? 0.4308 0.5040 0.2736 0.0802  -0.1658 -0.1051 421 LYS   A NZ  
1742 N  N   . GLU   A 266 ? 0.6110 0.5749 0.2916 0.1179  -0.1440 -0.0467 422 GLU   A N   
1743 C  CA  . GLU   A 266 ? 0.5806 0.5326 0.2353 0.1294  -0.1456 -0.0396 422 GLU   A CA  
1744 C  C   . GLU   A 266 ? 0.6213 0.5631 0.2514 0.1279  -0.1401 -0.0386 422 GLU   A C   
1745 O  O   . GLU   A 266 ? 0.6229 0.5693 0.2423 0.1353  -0.1458 -0.0414 422 GLU   A O   
1746 C  CB  . GLU   A 266 ? 0.6496 0.5782 0.2884 0.1344  -0.1401 -0.0257 422 GLU   A CB  
1747 C  CG  . GLU   A 266 ? 0.7879 0.6988 0.3970 0.1461  -0.1402 -0.0174 422 GLU   A CG  
1748 C  CD  . GLU   A 266 ? 0.9908 0.9196 0.6074 0.1585  -0.1533 -0.0241 422 GLU   A CD  
1749 O  OE1 . GLU   A 266 ? 1.0684 1.0231 0.7149 0.1576  -0.1615 -0.0343 422 GLU   A OE1 
1750 O  OE2 . GLU   A 266 ? 0.8564 0.7733 0.4488 0.1690  -0.1548 -0.0194 422 GLU   A OE2 
1751 N  N   . ARG   A 267 ? 0.6282 0.5571 0.2493 0.1184  -0.1286 -0.0350 423 ARG   A N   
1752 C  CA  . ARG   A 267 ? 0.6195 0.5377 0.2161 0.1165  -0.1213 -0.0332 423 ARG   A CA  
1753 C  C   . ARG   A 267 ? 0.6911 0.6287 0.2960 0.1161  -0.1281 -0.0460 423 ARG   A C   
1754 O  O   . ARG   A 267 ? 0.9175 0.8508 0.5021 0.1203  -0.1279 -0.0456 423 ARG   A O   
1755 C  CB  . ARG   A 267 ? 0.6600 0.5653 0.2502 0.1055  -0.1073 -0.0290 423 ARG   A CB  
1756 C  CG  . ARG   A 267 ? 0.9221 0.8155 0.4861 0.1030  -0.0974 -0.0261 423 ARG   A CG  
1757 C  CD  . ARG   A 267 ? 0.9815 0.8792 0.5547 0.0912  -0.0871 -0.0311 423 ARG   A CD  
1758 N  NE  . ARG   A 267 ? 1.0115 0.8935 0.5798 0.0822  -0.0713 -0.0210 423 ARG   A NE  
1759 C  CZ  . ARG   A 267 ? 1.0622 0.9449 0.6326 0.0721  -0.0584 -0.0224 423 ARG   A CZ  
1760 N  NH1 . ARG   A 267 ? 0.9667 0.8628 0.5429 0.0703  -0.0590 -0.0327 423 ARG   A NH1 
1761 N  NH2 . ARG   A 267 ? 0.9926 0.8629 0.5596 0.0637  -0.0446 -0.0139 423 ARG   A NH2 
1762 N  N   . PHE   A 268 ? 0.6462 0.6041 0.2805 0.1105  -0.1337 -0.0577 424 PHE   A N   
1763 C  CA  . PHE   A 268 ? 0.6624 0.6378 0.3071 0.1083  -0.1395 -0.0708 424 PHE   A CA  
1764 C  C   . PHE   A 268 ? 0.7317 0.7279 0.3960 0.1134  -0.1525 -0.0789 424 PHE   A C   
1765 O  O   . PHE   A 268 ? 0.5783 0.5921 0.2627 0.1079  -0.1573 -0.0914 424 PHE   A O   
1766 C  CB  . PHE   A 268 ? 0.6520 0.6331 0.3142 0.0965  -0.1344 -0.0792 424 PHE   A CB  
1767 C  CG  . PHE   A 268 ? 0.5877 0.5522 0.2325 0.0916  -0.1212 -0.0733 424 PHE   A CG  
1768 C  CD1 . PHE   A 268 ? 0.7376 0.6948 0.3591 0.0928  -0.1159 -0.0724 424 PHE   A CD1 
1769 C  CD2 . PHE   A 268 ? 0.5542 0.5125 0.2133 0.0835  -0.1114 -0.0676 424 PHE   A CD2 
1770 C  CE1 . PHE   A 268 ? 0.7032 0.6477 0.3101 0.0876  -0.1027 -0.0677 424 PHE   A CE1 
1771 C  CE2 . PHE   A 268 ? 0.5510 0.4979 0.2014 0.0770  -0.0971 -0.0620 424 PHE   A CE2 
1772 C  CZ  . PHE   A 268 ? 0.5978 0.5382 0.2213 0.0792  -0.0929 -0.0625 424 PHE   A CZ  
1773 N  N   . LYS   A 269 ? 0.6925 0.6863 0.3508 0.1238  -0.1577 -0.0722 425 LYS   A N   
1774 C  CA  . LYS   A 269 ? 0.6179 0.6330 0.2943 0.1298  -0.1696 -0.0801 425 LYS   A CA  
1775 C  C   . LYS   A 269 ? 0.7220 0.7486 0.3922 0.1334  -0.1762 -0.0888 425 LYS   A C   
1776 O  O   . LYS   A 269 ? 0.8033 0.8520 0.4932 0.1346  -0.1854 -0.0992 425 LYS   A O   
1777 C  CB  . LYS   A 269 ? 0.7487 0.7569 0.4171 0.1420  -0.1729 -0.0707 425 LYS   A CB  
1778 C  CG  . LYS   A 269 ? 0.7485 0.7446 0.3865 0.1547  -0.1752 -0.0645 425 LYS   A CG  
1779 C  CD  . LYS   A 269 ? 0.8213 0.7985 0.4438 0.1650  -0.1736 -0.0518 425 LYS   A CD  
1780 C  CE  . LYS   A 269 ? 0.8815 0.8416 0.4702 0.1770  -0.1741 -0.0447 425 LYS   A CE  
1781 N  NZ  . LYS   A 269 ? 1.2060 1.1797 0.7978 0.1915  -0.1862 -0.0491 425 LYS   A NZ  
1782 N  N   . ASP   A 270 ? 0.7046 0.7170 0.3478 0.1348  -0.1714 -0.0851 426 ASP   A N   
1783 C  CA  . ASP   A 270 ? 0.7630 0.7852 0.3985 0.1382  -0.1774 -0.0933 426 ASP   A CA  
1784 C  C   . ASP   A 270 ? 0.8552 0.8914 0.5097 0.1263  -0.1773 -0.1069 426 ASP   A C   
1785 O  O   . ASP   A 270 ? 1.0594 1.1109 0.7191 0.1271  -0.1847 -0.1174 426 ASP   A O   
1786 C  CB  . ASP   A 270 ? 0.9727 0.9739 0.5716 0.1439  -0.1717 -0.0843 426 ASP   A CB  
1787 C  CG  . ASP   A 270 ? 1.2325 1.2175 0.8100 0.1563  -0.1722 -0.0715 426 ASP   A CG  
1788 O  OD1 . ASP   A 270 ? 1.2402 1.2363 0.8260 0.1660  -0.1820 -0.0735 426 ASP   A OD1 
1789 O  OD2 . ASP   A 270 ? 1.2803 1.2410 0.8328 0.1563  -0.1621 -0.0596 426 ASP   A OD2 
1790 N  N   . LYS   A 271 ? 0.7329 0.7632 0.3971 0.1154  -0.1688 -0.1069 427 LYS   A N   
1791 C  CA  . LYS   A 271 ? 0.7644 0.8058 0.4493 0.1039  -0.1681 -0.1196 427 LYS   A CA  
1792 C  C   . LYS   A 271 ? 0.7896 0.8467 0.5074 0.0982  -0.1726 -0.1260 427 LYS   A C   
1793 O  O   . LYS   A 271 ? 0.8226 0.8809 0.5471 0.1026  -0.1747 -0.1197 427 LYS   A O   
1794 C  CB  . LYS   A 271 ? 0.8546 0.8810 0.5322 0.0961  -0.1563 -0.1171 427 LYS   A CB  
1795 C  CG  . LYS   A 271 ? 0.9421 0.9498 0.5865 0.1014  -0.1489 -0.1066 427 LYS   A CG  
1796 C  CD  . LYS   A 271 ? 0.8948 0.8936 0.5330 0.0937  -0.1379 -0.1084 427 LYS   A CD  
1797 C  CE  . LYS   A 271 ? 1.0988 1.0854 0.7052 0.0981  -0.1321 -0.1030 427 LYS   A CE  
1798 N  NZ  . LYS   A 271 ? 1.0987 1.0933 0.7015 0.0977  -0.1357 -0.1138 427 LYS   A NZ  
1799 N  N   . LYS   A 272 ? 0.7866 0.8548 0.5244 0.0880  -0.1735 -0.1385 428 LYS   A N   
1800 C  CA  . LYS   A 272 ? 0.7095 0.7930 0.4786 0.0806  -0.1767 -0.1458 428 LYS   A CA  
1801 C  C   . LYS   A 272 ? 0.7297 0.8052 0.5134 0.0694  -0.1685 -0.1463 428 LYS   A C   
1802 O  O   . LYS   A 272 ? 0.5371 0.6228 0.3464 0.0616  -0.1695 -0.1522 428 LYS   A O   
1803 C  CB  . LYS   A 272 ? 0.7505 0.8518 0.5331 0.0760  -0.1833 -0.1602 428 LYS   A CB  
1804 C  CG  . LYS   A 272 ? 0.8898 1.0043 0.6642 0.0872  -0.1932 -0.1618 428 LYS   A CG  
1805 C  CD  . LYS   A 272 ? 0.9913 1.1172 0.7679 0.0832  -0.1979 -0.1751 428 LYS   A CD  
1806 C  CE  . LYS   A 272 ? 0.7277 0.8601 0.4855 0.0965  -0.2063 -0.1746 428 LYS   A CE  
1807 N  NZ  . LYS   A 272 ? 0.7554 0.8826 0.4954 0.0955  -0.2060 -0.1801 428 LYS   A NZ  
1808 N  N   . HIS   A 273 ? 0.6175 0.6751 0.3853 0.0685  -0.1599 -0.1402 429 HIS   A N   
1809 C  CA  . HIS   A 273 ? 0.6114 0.6612 0.3918 0.0585  -0.1521 -0.1424 429 HIS   A CA  
1810 C  C   . HIS   A 273 ? 0.6196 0.6705 0.4171 0.0564  -0.1513 -0.1373 429 HIS   A C   
1811 O  O   . HIS   A 273 ? 0.5788 0.6316 0.3974 0.0469  -0.1488 -0.1429 429 HIS   A O   
1812 C  CB  . HIS   A 273 ? 0.5764 0.6089 0.3353 0.0597  -0.1430 -0.1370 429 HIS   A CB  
1813 C  CG  . HIS   A 273 ? 0.6543 0.6853 0.3993 0.0598  -0.1422 -0.1435 429 HIS   A CG  
1814 N  ND1 . HIS   A 273 ? 0.9517 0.9838 0.6757 0.0681  -0.1460 -0.1411 429 HIS   A ND1 
1815 C  CD2 . HIS   A 273 ? 0.7505 0.7778 0.4986 0.0533  -0.1378 -0.1523 429 HIS   A CD2 
1816 C  CE1 . HIS   A 273 ? 0.9203 0.9507 0.6357 0.0661  -0.1442 -0.1484 429 HIS   A CE1 
1817 N  NE2 . HIS   A 273 ? 0.8112 0.8385 0.5409 0.0573  -0.1392 -0.1553 429 HIS   A NE2 
1818 N  N   . LEU   A 274 ? 0.4800 0.5279 0.2674 0.0652  -0.1530 -0.1265 430 LEU   A N   
1819 C  CA  . LEU   A 274 ? 0.5051 0.5514 0.3049 0.0642  -0.1515 -0.1203 430 LEU   A CA  
1820 C  C   . LEU   A 274 ? 0.4556 0.5192 0.2739 0.0668  -0.1595 -0.1224 430 LEU   A C   
1821 O  O   . LEU   A 274 ? 0.5193 0.5819 0.3447 0.0687  -0.1592 -0.1160 430 LEU   A O   
1822 C  CB  . LEU   A 274 ? 0.4678 0.4962 0.2468 0.0703  -0.1446 -0.1048 430 LEU   A CB  
1823 C  CG  . LEU   A 274 ? 0.5589 0.5712 0.3230 0.0665  -0.1330 -0.1003 430 LEU   A CG  
1824 C  CD1 . LEU   A 274 ? 0.4820 0.4775 0.2286 0.0701  -0.1246 -0.0851 430 LEU   A CD1 
1825 C  CD2 . LEU   A 274 ? 0.4531 0.4647 0.2392 0.0548  -0.1252 -0.1048 430 LEU   A CD2 
1826 N  N   . ASP   A 275 ? 0.4642 0.5442 0.2907 0.0669  -0.1663 -0.1318 431 ASP   A N   
1827 C  CA  . ASP   A 275 ? 0.4618 0.5604 0.3045 0.0709  -0.1737 -0.1343 431 ASP   A CA  
1828 C  C   . ASP   A 275 ? 0.5010 0.6095 0.3738 0.0604  -0.1717 -0.1394 431 ASP   A C   
1829 O  O   . ASP   A 275 ? 0.5254 0.6457 0.4113 0.0640  -0.1753 -0.1381 431 ASP   A O   
1830 C  CB  . ASP   A 275 ? 0.5735 0.6881 0.4168 0.0735  -0.1812 -0.1439 431 ASP   A CB  
1831 C  CG  . ASP   A 275 ? 0.7579 0.8654 0.5721 0.0868  -0.1848 -0.1377 431 ASP   A CG  
1832 O  OD1 . ASP   A 275 ? 0.9110 1.0021 0.7058 0.0948  -0.1818 -0.1252 431 ASP   A OD1 
1833 O  OD2 . ASP   A 275 ? 0.8209 0.9380 0.6307 0.0889  -0.1901 -0.1453 431 ASP   A OD2 
1834 N  N   . LYS   A 276 ? 0.5217 0.6244 0.4048 0.0477  -0.1656 -0.1449 432 LYS   A N   
1835 C  CA  . LYS   A 276 ? 0.4893 0.5997 0.3999 0.0362  -0.1627 -0.1504 432 LYS   A CA  
1836 C  C   . LYS   A 276 ? 0.4876 0.5860 0.4023 0.0343  -0.1569 -0.1422 432 LYS   A C   
1837 O  O   . LYS   A 276 ? 0.4545 0.5590 0.3915 0.0259  -0.1544 -0.1452 432 LYS   A O   
1838 C  CB  . LYS   A 276 ? 0.4715 0.5797 0.3909 0.0231  -0.1587 -0.1612 432 LYS   A CB  
1839 C  CG  . LYS   A 276 ? 0.5757 0.6920 0.4873 0.0245  -0.1638 -0.1695 432 LYS   A CG  
1840 C  CD  . LYS   A 276 ? 0.6566 0.7886 0.5903 0.0136  -0.1652 -0.1817 432 LYS   A CD  
1841 C  CE  . LYS   A 276 ? 0.5614 0.6932 0.4871 0.0100  -0.1669 -0.1912 432 LYS   A CE  
1842 N  NZ  . LYS   A 276 ? 0.8304 0.9662 0.7749 -0.0052 -0.1639 -0.2025 432 LYS   A NZ  
1843 N  N   . PHE   A 277 ? 0.4432 0.5236 0.3384 0.0405  -0.1520 -0.1302 433 PHE   A N   
1844 C  CA  . PHE   A 277 ? 0.4587 0.5251 0.3595 0.0376  -0.1418 -0.1181 433 PHE   A CA  
1845 C  C   . PHE   A 277 ? 0.4485 0.5200 0.3509 0.0460  -0.1454 -0.1105 433 PHE   A C   
1846 O  O   . PHE   A 277 ? 0.4367 0.5137 0.3248 0.0577  -0.1538 -0.1094 433 PHE   A O   
1847 C  CB  . PHE   A 277 ? 0.3818 0.4274 0.2628 0.0389  -0.1329 -0.1085 433 PHE   A CB  
1848 C  CG  . PHE   A 277 ? 0.3846 0.4240 0.2637 0.0319  -0.1285 -0.1154 433 PHE   A CG  
1849 C  CD1 . PHE   A 277 ? 0.4094 0.4425 0.3042 0.0219  -0.1209 -0.1172 433 PHE   A CD1 
1850 C  CD2 . PHE   A 277 ? 0.4033 0.4420 0.2633 0.0363  -0.1320 -0.1203 433 PHE   A CD2 
1851 C  CE1 . PHE   A 277 ? 0.4266 0.4520 0.3180 0.0169  -0.1170 -0.1238 433 PHE   A CE1 
1852 C  CE2 . PHE   A 277 ? 0.4283 0.4607 0.2859 0.0307  -0.1279 -0.1273 433 PHE   A CE2 
1853 C  CZ  . PHE   A 277 ? 0.4396 0.4651 0.3130 0.0213  -0.1205 -0.1290 433 PHE   A CZ  
1854 N  N   . SER   A 278 ? 0.3563 0.4251 0.2752 0.0407  -0.1392 -0.1053 434 SER   A N   
1855 C  CA  . SER   A 278 ? 0.4053 0.4793 0.3287 0.0479  -0.1421 -0.0993 434 SER   A CA  
1856 C  C   . SER   A 278 ? 0.3919 0.4506 0.3201 0.0435  -0.1313 -0.0882 434 SER   A C   
1857 O  O   . SER   A 278 ? 0.3293 0.3768 0.2608 0.0346  -0.1225 -0.0865 434 SER   A O   
1858 C  CB  . SER   A 278 ? 0.4837 0.5826 0.4302 0.0461  -0.1496 -0.1104 434 SER   A CB  
1859 O  OG  . SER   A 278 ? 0.3736 0.4733 0.3426 0.0338  -0.1422 -0.1122 434 SER   A OG  
1860 N  N   . SER   A 279 ? 0.4443 0.5029 0.3725 0.0506  -0.1326 -0.0812 435 SER   A N   
1861 C  CA  . SER   A 279 ? 0.3812 0.4269 0.3145 0.0469  -0.1233 -0.0715 435 SER   A CA  
1862 C  C   . SER   A 279 ? 0.3584 0.4112 0.3173 0.0354  -0.1187 -0.0764 435 SER   A C   
1863 O  O   . SER   A 279 ? 0.3619 0.4034 0.3253 0.0304  -0.1102 -0.0695 435 SER   A O   
1864 C  CB  . SER   A 279 ? 0.4562 0.5001 0.3834 0.0577  -0.1265 -0.0642 435 SER   A CB  
1865 O  OG  . SER   A 279 ? 0.4809 0.5454 0.4271 0.0600  -0.1332 -0.0714 435 SER   A OG  
1866 N  N   . TYR   A 280 ? 0.3019 0.3728 0.2767 0.0308  -0.1239 -0.0884 436 TYR   A N   
1867 C  CA  . TYR   A 280 ? 0.3958 0.4703 0.3920 0.0185  -0.1182 -0.0932 436 TYR   A CA  
1868 C  C   . TYR   A 280 ? 0.3208 0.3782 0.3129 0.0100  -0.1097 -0.0916 436 TYR   A C   
1869 O  O   . TYR   A 280 ? 0.3327 0.3814 0.3334 0.0033  -0.1017 -0.0878 436 TYR   A O   
1870 C  CB  . TYR   A 280 ? 0.3395 0.4366 0.3525 0.0138  -0.1248 -0.1074 436 TYR   A CB  
1871 C  CG  . TYR   A 280 ? 0.3911 0.4924 0.4259 0.0018  -0.1185 -0.1113 436 TYR   A CG  
1872 C  CD1 . TYR   A 280 ? 0.3497 0.4552 0.3956 0.0031  -0.1159 -0.1064 436 TYR   A CD1 
1873 C  CD2 . TYR   A 280 ? 0.3237 0.4224 0.3662 -0.0108 -0.1145 -0.1195 436 TYR   A CD2 
1874 C  CE1 . TYR   A 280 ? 0.2927 0.4011 0.3568 -0.0081 -0.1094 -0.1096 436 TYR   A CE1 
1875 C  CE2 . TYR   A 280 ? 0.3807 0.4802 0.4403 -0.0222 -0.1078 -0.1224 436 TYR   A CE2 
1876 C  CZ  . TYR   A 280 ? 0.2821 0.3869 0.3524 -0.0209 -0.1051 -0.1173 436 TYR   A CZ  
1877 O  OH  . TYR   A 280 ? 0.4187 0.5236 0.5044 -0.0323 -0.0978 -0.1200 436 TYR   A OH  
1878 N  N   . HIS   A 281 ? 0.3652 0.4179 0.3437 0.0110  -0.1114 -0.0948 437 HIS   A N   
1879 C  CA  . HIS   A 281 ? 0.2946 0.3313 0.2675 0.0052  -0.1036 -0.0933 437 HIS   A CA  
1880 C  C   . HIS   A 281 ? 0.2883 0.3102 0.2533 0.0076  -0.0959 -0.0808 437 HIS   A C   
1881 O  O   . HIS   A 281 ? 0.3070 0.3190 0.2770 0.0019  -0.0884 -0.0783 437 HIS   A O   
1882 C  CB  . HIS   A 281 ? 0.3096 0.3448 0.2673 0.0076  -0.1071 -0.0987 437 HIS   A CB  
1883 C  CG  . HIS   A 281 ? 0.3174 0.3677 0.2821 0.0047  -0.1149 -0.1122 437 HIS   A CG  
1884 N  ND1 . HIS   A 281 ? 0.3314 0.3922 0.2850 0.0122  -0.1242 -0.1170 437 HIS   A ND1 
1885 C  CD2 . HIS   A 281 ? 0.3150 0.3714 0.2959 -0.0054 -0.1147 -0.1224 437 HIS   A CD2 
1886 C  CE1 . HIS   A 281 ? 0.3357 0.4109 0.3001 0.0068  -0.1299 -0.1303 437 HIS   A CE1 
1887 N  NE2 . HIS   A 281 ? 0.3262 0.3985 0.3074 -0.0046 -0.1238 -0.1339 437 HIS   A NE2 
1888 N  N   . VAL   A 282 ? 0.3158 0.3356 0.2675 0.0162  -0.0979 -0.0733 438 VAL   A N   
1889 C  CA  . VAL   A 282 ? 0.2905 0.2968 0.2341 0.0175  -0.0904 -0.0623 438 VAL   A CA  
1890 C  C   . VAL   A 282 ? 0.2749 0.2803 0.2342 0.0132  -0.0859 -0.0585 438 VAL   A C   
1891 O  O   . VAL   A 282 ? 0.2669 0.2630 0.2279 0.0092  -0.0782 -0.0540 438 VAL   A O   
1892 C  CB  . VAL   A 282 ? 0.3790 0.3813 0.3040 0.0269  -0.0934 -0.0554 438 VAL   A CB  
1893 C  CG1 . VAL   A 282 ? 0.4000 0.3895 0.3198 0.0267  -0.0856 -0.0448 438 VAL   A CG1 
1894 C  CG2 . VAL   A 282 ? 0.4138 0.4129 0.3195 0.0305  -0.0953 -0.0574 438 VAL   A CG2 
1895 N  N   . LYS   A 283 ? 0.2797 0.2963 0.2509 0.0145  -0.0906 -0.0609 439 LYS   A N   
1896 C  CA  . LYS   A 283 ? 0.3549 0.3713 0.3402 0.0109  -0.0862 -0.0576 439 LYS   A CA  
1897 C  C   . LYS   A 283 ? 0.2484 0.2626 0.2465 0.0011  -0.0809 -0.0617 439 LYS   A C   
1898 O  O   . LYS   A 283 ? 0.3033 0.3095 0.3058 -0.0023 -0.0743 -0.0566 439 LYS   A O   
1899 C  CB  . LYS   A 283 ? 0.3030 0.3340 0.2984 0.0151  -0.0926 -0.0605 439 LYS   A CB  
1900 N  N   . THR   A 284 ? 0.3001 0.3202 0.3030 -0.0035 -0.0836 -0.0713 440 THR   A N   
1901 C  CA  . THR   A 284 ? 0.2996 0.3134 0.3111 -0.0128 -0.0781 -0.0752 440 THR   A CA  
1902 C  C   . THR   A 284 ? 0.2927 0.2903 0.2942 -0.0128 -0.0716 -0.0699 440 THR   A C   
1903 O  O   . THR   A 284 ? 0.3535 0.3425 0.3598 -0.0166 -0.0654 -0.0667 440 THR   A O   
1904 C  CB  . THR   A 284 ? 0.2775 0.2985 0.2930 -0.0178 -0.0823 -0.0870 440 THR   A CB  
1905 O  OG1 . THR   A 284 ? 0.3116 0.3519 0.3369 -0.0167 -0.0894 -0.0929 440 THR   A OG1 
1906 C  CG2 . THR   A 284 ? 0.3433 0.3554 0.3670 -0.0280 -0.0761 -0.0912 440 THR   A CG2 
1907 N  N   . ALA   A 285 ? 0.2765 0.2709 0.2638 -0.0081 -0.0729 -0.0692 441 ALA   A N   
1908 C  CA  . ALA   A 285 ? 0.3507 0.3332 0.3292 -0.0074 -0.0668 -0.0650 441 ALA   A CA  
1909 C  C   . ALA   A 285 ? 0.2473 0.2257 0.2263 -0.0058 -0.0618 -0.0555 441 ALA   A C   
1910 O  O   . ALA   A 285 ? 0.2439 0.2149 0.2241 -0.0074 -0.0561 -0.0530 441 ALA   A O   
1911 C  CB  . ALA   A 285 ? 0.2851 0.2672 0.2482 -0.0027 -0.0687 -0.0662 441 ALA   A CB  
1912 N  N   . PHE   A 286 ? 0.2460 0.2288 0.2234 -0.0021 -0.0642 -0.0507 442 PHE   A N   
1913 C  CA  . PHE   A 286 ? 0.2585 0.2366 0.2358 -0.0013 -0.0595 -0.0424 442 PHE   A CA  
1914 C  C   . PHE   A 286 ? 0.2408 0.2178 0.2318 -0.0057 -0.0562 -0.0417 442 PHE   A C   
1915 O  O   . PHE   A 286 ? 0.3115 0.2827 0.3029 -0.0068 -0.0508 -0.0373 442 PHE   A O   
1916 C  CB  . PHE   A 286 ? 0.2431 0.2235 0.2145 0.0040  -0.0630 -0.0379 442 PHE   A CB  
1917 C  CG  . PHE   A 286 ? 0.2533 0.2283 0.2255 0.0042  -0.0586 -0.0304 442 PHE   A CG  
1918 C  CD1 . PHE   A 286 ? 0.3123 0.2793 0.2750 0.0036  -0.0528 -0.0251 442 PHE   A CD1 
1919 C  CD2 . PHE   A 286 ? 0.3452 0.3240 0.3281 0.0043  -0.0598 -0.0294 442 PHE   A CD2 
1920 C  CE1 . PHE   A 286 ? 0.3511 0.3130 0.3145 0.0028  -0.0486 -0.0191 442 PHE   A CE1 
1921 C  CE2 . PHE   A 286 ? 0.3286 0.3015 0.3115 0.0044  -0.0557 -0.0231 442 PHE   A CE2 
1922 C  CZ  . PHE   A 286 ? 0.4257 0.3897 0.3987 0.0034  -0.0503 -0.0180 442 PHE   A CZ  
1923 N  N   . PHE   A 287 ? 0.2399 0.2234 0.2421 -0.0086 -0.0591 -0.0466 443 PHE   A N   
1924 C  CA  . PHE   A 287 ? 0.2709 0.2524 0.2846 -0.0135 -0.0551 -0.0462 443 PHE   A CA  
1925 C  C   . PHE   A 287 ? 0.3148 0.2858 0.3271 -0.0171 -0.0504 -0.0477 443 PHE   A C   
1926 O  O   . PHE   A 287 ? 0.2942 0.2588 0.3092 -0.0185 -0.0456 -0.0440 443 PHE   A O   
1927 C  CB  . PHE   A 287 ? 0.2175 0.2095 0.2435 -0.0170 -0.0585 -0.0523 443 PHE   A CB  
1928 C  CG  . PHE   A 287 ? 0.2750 0.2776 0.3044 -0.0120 -0.0627 -0.0504 443 PHE   A CG  
1929 C  CD1 . PHE   A 287 ? 0.3119 0.3103 0.3391 -0.0085 -0.0601 -0.0426 443 PHE   A CD1 
1930 C  CD2 . PHE   A 287 ? 0.3951 0.4119 0.4294 -0.0103 -0.0696 -0.0570 443 PHE   A CD2 
1931 C  CE1 . PHE   A 287 ? 0.3654 0.3710 0.3939 -0.0028 -0.0639 -0.0409 443 PHE   A CE1 
1932 C  CE2 . PHE   A 287 ? 0.3588 0.3851 0.3951 -0.0037 -0.0740 -0.0555 443 PHE   A CE2 
1933 C  CZ  . PHE   A 287 ? 0.3838 0.4034 0.4167 0.0003  -0.0710 -0.0472 443 PHE   A CZ  
1934 N  N   . HIS   A 288 ? 0.2281 0.1967 0.2350 -0.0177 -0.0519 -0.0533 444 HIS   A N   
1935 C  CA  . HIS   A 288 ? 0.2324 0.1892 0.2354 -0.0190 -0.0476 -0.0546 444 HIS   A CA  
1936 C  C   . HIS   A 288 ? 0.3206 0.2734 0.3171 -0.0143 -0.0438 -0.0485 444 HIS   A C   
1937 O  O   . HIS   A 288 ? 0.2376 0.1825 0.2344 -0.0142 -0.0397 -0.0467 444 HIS   A O   
1938 C  CB  . HIS   A 288 ? 0.2966 0.2512 0.2936 -0.0195 -0.0500 -0.0622 444 HIS   A CB  
1939 C  CG  . HIS   A 288 ? 0.3541 0.3101 0.3582 -0.0262 -0.0521 -0.0700 444 HIS   A CG  
1940 N  ND1 . HIS   A 288 ? 0.3100 0.2577 0.3203 -0.0326 -0.0479 -0.0713 444 HIS   A ND1 
1941 C  CD2 . HIS   A 288 ? 0.2950 0.2601 0.3005 -0.0281 -0.0576 -0.0775 444 HIS   A CD2 
1942 C  CE1 . HIS   A 288 ? 0.3214 0.2733 0.3377 -0.0394 -0.0501 -0.0795 444 HIS   A CE1 
1943 N  NE2 . HIS   A 288 ? 0.3371 0.3008 0.3514 -0.0366 -0.0564 -0.0838 444 HIS   A NE2 
1944 N  N   . VAL   A 289 ? 0.2617 0.2201 0.2518 -0.0105 -0.0451 -0.0455 445 VAL   A N   
1945 C  CA  . VAL   A 289 ? 0.2513 0.2085 0.2365 -0.0077 -0.0410 -0.0407 445 VAL   A CA  
1946 C  C   . VAL   A 289 ? 0.2487 0.2053 0.2406 -0.0089 -0.0381 -0.0352 445 VAL   A C   
1947 O  O   . VAL   A 289 ? 0.3430 0.2973 0.3348 -0.0078 -0.0344 -0.0331 445 VAL   A O   
1948 C  CB  . VAL   A 289 ? 0.3221 0.2837 0.2977 -0.0051 -0.0418 -0.0387 445 VAL   A CB  
1949 C  CG1 . VAL   A 289 ? 0.2404 0.2025 0.2125 -0.0042 -0.0365 -0.0344 445 VAL   A CG1 
1950 C  CG2 . VAL   A 289 ? 0.2946 0.2567 0.2623 -0.0035 -0.0442 -0.0444 445 VAL   A CG2 
1951 N  N   . CYS   A 290 ? 0.2130 0.1728 0.2105 -0.0104 -0.0402 -0.0333 446 CYS   A N   
1952 C  CA  . CYS   A 290 ? 0.2978 0.2566 0.3015 -0.0115 -0.0375 -0.0288 446 CYS   A CA  
1953 C  C   . CYS   A 290 ? 0.2669 0.2194 0.2753 -0.0136 -0.0347 -0.0300 446 CYS   A C   
1954 O  O   . CYS   A 290 ? 0.3149 0.2649 0.3241 -0.0130 -0.0314 -0.0265 446 CYS   A O   
1955 C  CB  . CYS   A 290 ? 0.2275 0.1913 0.2367 -0.0119 -0.0404 -0.0278 446 CYS   A CB  
1956 S  SG  . CYS   A 290 ? 0.3313 0.2975 0.3316 -0.0076 -0.0429 -0.0237 446 CYS   A SG  
1957 N  N   . THR   A 291 ? 0.2342 0.1834 0.2445 -0.0162 -0.0357 -0.0350 447 THR   A N   
1958 C  CA  . THR   A 291 ? 0.2971 0.2360 0.3082 -0.0182 -0.0323 -0.0359 447 THR   A CA  
1959 C  C   . THR   A 291 ? 0.3489 0.2814 0.3522 -0.0135 -0.0301 -0.0352 447 THR   A C   
1960 O  O   . THR   A 291 ? 0.2964 0.2223 0.2986 -0.0119 -0.0272 -0.0327 447 THR   A O   
1961 C  CB  . THR   A 291 ? 0.3281 0.2627 0.3411 -0.0232 -0.0332 -0.0422 447 THR   A CB  
1962 O  OG1 . THR   A 291 ? 0.3908 0.3348 0.4134 -0.0275 -0.0351 -0.0437 447 THR   A OG1 
1963 C  CG2 . THR   A 291 ? 0.3322 0.2516 0.3423 -0.0253 -0.0287 -0.0426 447 THR   A CG2 
1964 N  N   . GLN   A 292 ? 0.3229 0.2583 0.3203 -0.0103 -0.0316 -0.0377 448 GLN   A N   
1965 C  CA  . GLN   A 292 ? 0.2925 0.2249 0.2836 -0.0049 -0.0297 -0.0382 448 GLN   A CA  
1966 C  C   . GLN   A 292 ? 0.2307 0.1704 0.2233 -0.0024 -0.0277 -0.0336 448 GLN   A C   
1967 O  O   . GLN   A 292 ? 0.3935 0.3318 0.3837 0.0021  -0.0259 -0.0336 448 GLN   A O   
1968 C  CB  . GLN   A 292 ? 0.3411 0.2765 0.3259 -0.0025 -0.0312 -0.0426 448 GLN   A CB  
1969 C  CG  . GLN   A 292 ? 0.4205 0.3484 0.4026 -0.0047 -0.0332 -0.0486 448 GLN   A CG  
1970 C  CD  . GLN   A 292 ? 0.6066 0.5371 0.5810 -0.0012 -0.0344 -0.0531 448 GLN   A CD  
1971 O  OE1 . GLN   A 292 ? 0.4670 0.4071 0.4389 0.0013  -0.0339 -0.0514 448 GLN   A OE1 
1972 N  NE2 . GLN   A 292 ? 0.6474 0.5687 0.6174 -0.0017 -0.0354 -0.0593 448 GLN   A NE2 
1973 N  N   . ASN   A 293 ? 0.2720 0.2194 0.2677 -0.0050 -0.0280 -0.0302 449 ASN   A N   
1974 C  CA  . ASN   A 293 ? 0.2243 0.1785 0.2208 -0.0043 -0.0257 -0.0267 449 ASN   A CA  
1975 C  C   . ASN   A 293 ? 0.2866 0.2400 0.2887 -0.0072 -0.0254 -0.0226 449 ASN   A C   
1976 O  O   . ASN   A 293 ? 0.2137 0.1703 0.2162 -0.0093 -0.0259 -0.0201 449 ASN   A O   
1977 C  CB  . ASN   A 293 ? 0.2355 0.1968 0.2274 -0.0048 -0.0253 -0.0265 449 ASN   A CB  
1978 C  CG  . ASN   A 293 ? 0.3412 0.3054 0.3277 -0.0015 -0.0245 -0.0309 449 ASN   A CG  
1979 O  OD1 . ASN   A 293 ? 0.4957 0.4553 0.4793 0.0000  -0.0265 -0.0346 449 ASN   A OD1 
1980 N  ND2 . ASN   A 293 ? 0.3729 0.3454 0.3583 -0.0008 -0.0212 -0.0311 449 ASN   A ND2 
1981 N  N   . PRO   A 294 ? 0.3207 0.2687 0.3257 -0.0070 -0.0243 -0.0217 450 PRO   A N   
1982 C  CA  . PRO   A 294 ? 0.2306 0.1773 0.2409 -0.0099 -0.0239 -0.0186 450 PRO   A CA  
1983 C  C   . PRO   A 294 ? 0.3379 0.2893 0.3495 -0.0101 -0.0221 -0.0152 450 PRO   A C   
1984 O  O   . PRO   A 294 ? 0.3698 0.3208 0.3851 -0.0122 -0.0219 -0.0128 450 PRO   A O   
1985 C  CB  . PRO   A 294 ? 0.3518 0.2891 0.3620 -0.0098 -0.0224 -0.0191 450 PRO   A CB  
1986 C  CG  . PRO   A 294 ? 0.3230 0.2578 0.3271 -0.0045 -0.0219 -0.0206 450 PRO   A CG  
1987 C  CD  . PRO   A 294 ? 0.2501 0.1913 0.2518 -0.0032 -0.0234 -0.0235 450 PRO   A CD  
1988 N  N   . GLN   A 295 ? 0.3521 0.3086 0.3611 -0.0082 -0.0208 -0.0156 451 GLN   A N   
1989 C  CA  . GLN   A 295 ? 0.2676 0.2288 0.2781 -0.0096 -0.0188 -0.0136 451 GLN   A CA  
1990 C  C   . GLN   A 295 ? 0.3289 0.2927 0.3372 -0.0128 -0.0181 -0.0121 451 GLN   A C   
1991 O  O   . GLN   A 295 ? 0.3010 0.2662 0.3051 -0.0129 -0.0184 -0.0132 451 GLN   A O   
1992 C  CB  . GLN   A 295 ? 0.2564 0.2243 0.2662 -0.0065 -0.0177 -0.0159 451 GLN   A CB  
1993 C  CG  . GLN   A 295 ? 0.2703 0.2329 0.2788 -0.0012 -0.0186 -0.0170 451 GLN   A CG  
1994 C  CD  . GLN   A 295 ? 0.4142 0.3705 0.4237 -0.0016 -0.0182 -0.0142 451 GLN   A CD  
1995 O  OE1 . GLN   A 295 ? 0.3907 0.3495 0.4032 -0.0050 -0.0172 -0.0121 451 GLN   A OE1 
1996 N  NE2 . GLN   A 295 ? 0.3993 0.3457 0.4050 0.0018  -0.0184 -0.0140 451 GLN   A NE2 
1997 N  N   . ASP   A 296 ? 0.2503 0.2130 0.2597 -0.0153 -0.0167 -0.0095 452 ASP   A N   
1998 C  CA  . ASP   A 296 ? 0.2317 0.1926 0.2362 -0.0182 -0.0154 -0.0074 452 ASP   A CA  
1999 C  C   . ASP   A 296 ? 0.3298 0.2963 0.3301 -0.0207 -0.0121 -0.0092 452 ASP   A C   
2000 O  O   . ASP   A 296 ? 0.2688 0.2324 0.2619 -0.0228 -0.0107 -0.0080 452 ASP   A O   
2001 C  CB  . ASP   A 296 ? 0.2829 0.2395 0.2885 -0.0199 -0.0142 -0.0048 452 ASP   A CB  
2002 C  CG  . ASP   A 296 ? 0.2968 0.2494 0.3065 -0.0177 -0.0168 -0.0034 452 ASP   A CG  
2003 O  OD1 . ASP   A 296 ? 0.2976 0.2505 0.3086 -0.0159 -0.0196 -0.0044 452 ASP   A OD1 
2004 O  OD2 . ASP   A 296 ? 0.2962 0.2464 0.3083 -0.0182 -0.0158 -0.0021 452 ASP   A OD2 
2005 N  N   . SER   A 297 ? 0.2814 0.2565 0.2857 -0.0204 -0.0107 -0.0123 453 SER   A N   
2006 C  CA  . SER   A 297 ? 0.2309 0.2153 0.2335 -0.0234 -0.0071 -0.0153 453 SER   A CA  
2007 C  C   . SER   A 297 ? 0.3670 0.3544 0.3659 -0.0214 -0.0073 -0.0175 453 SER   A C   
2008 O  O   . SER   A 297 ? 0.3249 0.3191 0.3208 -0.0248 -0.0034 -0.0197 453 SER   A O   
2009 C  CB  . SER   A 297 ? 0.2194 0.2153 0.2284 -0.0221 -0.0066 -0.0193 453 SER   A CB  
2010 O  OG  . SER   A 297 ? 0.4030 0.3990 0.4147 -0.0150 -0.0102 -0.0204 453 SER   A OG  
2011 N  N   . GLN   A 298 ? 0.3327 0.3153 0.3314 -0.0167 -0.0111 -0.0174 454 GLN   A N   
2012 C  CA  . GLN   A 298 ? 0.2274 0.2107 0.2211 -0.0148 -0.0117 -0.0195 454 GLN   A CA  
2013 C  C   . GLN   A 298 ? 0.3084 0.2846 0.2939 -0.0173 -0.0117 -0.0164 454 GLN   A C   
2014 O  O   . GLN   A 298 ? 0.2605 0.2368 0.2401 -0.0159 -0.0123 -0.0180 454 GLN   A O   
2015 C  CB  . GLN   A 298 ? 0.2415 0.2210 0.2372 -0.0095 -0.0156 -0.0215 454 GLN   A CB  
2016 C  CG  . GLN   A 298 ? 0.2099 0.1940 0.2098 -0.0049 -0.0158 -0.0245 454 GLN   A CG  
2017 C  CD  . GLN   A 298 ? 0.3609 0.3357 0.3603 -0.0006 -0.0188 -0.0255 454 GLN   A CD  
2018 O  OE1 . GLN   A 298 ? 0.3188 0.2853 0.3201 -0.0018 -0.0202 -0.0229 454 GLN   A OE1 
2019 N  NE2 . GLN   A 298 ? 0.3272 0.3027 0.3234 0.0041  -0.0194 -0.0296 454 GLN   A NE2 
2020 N  N   . TRP   A 299 ? 0.3559 0.3251 0.3396 -0.0199 -0.0114 -0.0123 455 TRP   A N   
2021 C  CA  . TRP   A 299 ? 0.3968 0.3573 0.3706 -0.0204 -0.0120 -0.0088 455 TRP   A CA  
2022 C  C   . TRP   A 299 ? 0.3785 0.3334 0.3453 -0.0256 -0.0071 -0.0057 455 TRP   A C   
2023 O  O   . TRP   A 299 ? 0.3759 0.3197 0.3340 -0.0249 -0.0079 -0.0016 455 TRP   A O   
2024 C  CB  . TRP   A 299 ? 0.3058 0.2608 0.2826 -0.0168 -0.0174 -0.0070 455 TRP   A CB  
2025 C  CG  . TRP   A 299 ? 0.2357 0.1941 0.2172 -0.0135 -0.0216 -0.0106 455 TRP   A CG  
2026 C  CD1 . TRP   A 299 ? 0.2493 0.2099 0.2400 -0.0126 -0.0228 -0.0129 455 TRP   A CD1 
2027 C  CD2 . TRP   A 299 ? 0.2076 0.1657 0.1834 -0.0112 -0.0248 -0.0125 455 TRP   A CD2 
2028 N  NE1 . TRP   A 299 ? 0.2885 0.2493 0.2796 -0.0106 -0.0260 -0.0163 455 TRP   A NE1 
2029 C  CE2 . TRP   A 299 ? 0.2175 0.1779 0.2003 -0.0097 -0.0276 -0.0165 455 TRP   A CE2 
2030 C  CE3 . TRP   A 299 ? 0.2191 0.1742 0.1829 -0.0102 -0.0254 -0.0113 455 TRP   A CE3 
2031 C  CZ2 . TRP   A 299 ? 0.2089 0.1700 0.1887 -0.0078 -0.0312 -0.0202 455 TRP   A CZ2 
2032 C  CZ3 . TRP   A 299 ? 0.2307 0.1874 0.1912 -0.0073 -0.0294 -0.0147 455 TRP   A CZ3 
2033 C  CH2 . TRP   A 299 ? 0.2575 0.2179 0.2267 -0.0065 -0.0324 -0.0194 455 TRP   A CH2 
2034 N  N   . ASP   A 300 ? 0.3042 0.2662 0.2740 -0.0304 -0.0020 -0.0079 456 ASP   A N   
2035 C  CA  . ASP   A 300 ? 0.3472 0.3034 0.3101 -0.0373 0.0038  -0.0060 456 ASP   A CA  
2036 C  C   . ASP   A 300 ? 0.4774 0.4225 0.4239 -0.0391 0.0066  -0.0027 456 ASP   A C   
2037 O  O   . ASP   A 300 ? 0.4127 0.3616 0.3546 -0.0376 0.0067  -0.0043 456 ASP   A O   
2038 C  CB  . ASP   A 300 ? 0.4491 0.4194 0.4187 -0.0430 0.0089  -0.0110 456 ASP   A CB  
2039 C  CG  . ASP   A 300 ? 0.5692 0.5346 0.5355 -0.0513 0.0147  -0.0104 456 ASP   A CG  
2040 O  OD1 . ASP   A 300 ? 0.6624 0.6155 0.6154 -0.0565 0.0195  -0.0074 456 ASP   A OD1 
2041 O  OD2 . ASP   A 300 ? 0.7652 0.7380 0.7412 -0.0529 0.0145  -0.0130 456 ASP   A OD2 
2042 N  N   . ARG   A 301 ? 0.3852 0.3148 0.3213 -0.0416 0.0089  0.0018  457 ARG   A N   
2043 C  CA  . ARG   A 301 ? 0.5591 0.4736 0.4759 -0.0417 0.0111  0.0061  457 ARG   A CA  
2044 C  C   . ARG   A 301 ? 0.6000 0.5185 0.5092 -0.0490 0.0189  0.0040  457 ARG   A C   
2045 O  O   . ARG   A 301 ? 0.5070 0.4210 0.4036 -0.0472 0.0193  0.0054  457 ARG   A O   
2046 C  CB  . ARG   A 301 ? 0.4760 0.3710 0.3818 -0.0429 0.0129  0.0112  457 ARG   A CB  
2047 C  CG  . ARG   A 301 ? 0.6776 0.5522 0.5597 -0.0418 0.0152  0.0167  457 ARG   A CG  
2048 C  CD  . ARG   A 301 ? 0.8288 0.6839 0.7018 -0.0376 0.0133  0.0217  457 ARG   A CD  
2049 N  NE  . ARG   A 301 ? 1.0928 0.9243 0.9397 -0.0362 0.0162  0.0276  457 ARG   A NE  
2050 C  CZ  . ARG   A 301 ? 1.0348 0.8502 0.8657 -0.0455 0.0259  0.0298  457 ARG   A CZ  
2051 N  NH1 . ARG   A 301 ? 0.7894 0.6126 0.6295 -0.0575 0.0334  0.0256  457 ARG   A NH1 
2052 N  NH2 . ARG   A 301 ? 1.0692 0.8598 0.8733 -0.0429 0.0283  0.0359  457 ARG   A NH2 
2053 N  N   . LYS   A 302 ? 0.5433 0.4724 0.4608 -0.0574 0.0250  -0.0003 458 LYS   A N   
2054 C  CA  . LYS   A 302 ? 0.5065 0.4438 0.4199 -0.0655 0.0333  -0.0038 458 LYS   A CA  
2055 C  C   . LYS   A 302 ? 0.4979 0.4484 0.4139 -0.0603 0.0309  -0.0072 458 LYS   A C   
2056 O  O   . LYS   A 302 ? 0.4466 0.3998 0.3539 -0.0652 0.0375  -0.0088 458 LYS   A O   
2057 C  CB  . LYS   A 302 ? 0.5699 0.5234 0.4973 -0.0737 0.0381  -0.0100 458 LYS   A CB  
2058 C  CG  . LYS   A 302 ? 0.6147 0.5934 0.5606 -0.0690 0.0344  -0.0169 458 LYS   A CG  
2059 C  CD  . LYS   A 302 ? 0.6458 0.6412 0.6061 -0.0747 0.0369  -0.0231 458 LYS   A CD  
2060 C  CE  . LYS   A 302 ? 0.7566 0.7770 0.7321 -0.0690 0.0339  -0.0304 458 LYS   A CE  
2061 N  NZ  . LYS   A 302 ? 0.6895 0.7180 0.6784 -0.0638 0.0280  -0.0325 458 LYS   A NZ  
2062 N  N   . ASP   A 303 ? 0.3886 0.3463 0.3154 -0.0510 0.0224  -0.0086 459 ASP   A N   
2063 C  CA  . ASP   A 303 ? 0.4565 0.4256 0.3863 -0.0457 0.0198  -0.0126 459 ASP   A CA  
2064 C  C   . ASP   A 303 ? 0.3847 0.3426 0.3033 -0.0388 0.0142  -0.0092 459 ASP   A C   
2065 O  O   . ASP   A 303 ? 0.3840 0.3493 0.3069 -0.0330 0.0097  -0.0127 459 ASP   A O   
2066 C  CB  . ASP   A 303 ? 0.3942 0.3778 0.3421 -0.0404 0.0146  -0.0174 459 ASP   A CB  
2067 C  CG  . ASP   A 303 ? 0.4958 0.4940 0.4551 -0.0453 0.0189  -0.0220 459 ASP   A CG  
2068 O  OD1 . ASP   A 303 ? 0.6154 0.6218 0.5722 -0.0525 0.0264  -0.0251 459 ASP   A OD1 
2069 O  OD2 . ASP   A 303 ? 0.5245 0.5269 0.4952 -0.0423 0.0149  -0.0230 459 ASP   A OD2 
2070 N  N   . LEU   A 304 ? 0.3458 0.2857 0.2496 -0.0389 0.0141  -0.0030 460 LEU   A N   
2071 C  CA  . LEU   A 304 ? 0.3789 0.3096 0.2714 -0.0314 0.0079  -0.0003 460 LEU   A CA  
2072 C  C   . LEU   A 304 ? 0.3418 0.2804 0.2296 -0.0295 0.0082  -0.0042 460 LEU   A C   
2073 O  O   . LEU   A 304 ? 0.4524 0.3957 0.3446 -0.0229 0.0012  -0.0069 460 LEU   A O   
2074 C  CB  . LEU   A 304 ? 0.3793 0.2891 0.2513 -0.0319 0.0099  0.0067  460 LEU   A CB  
2075 C  CG  . LEU   A 304 ? 0.5027 0.4024 0.3596 -0.0232 0.0034  0.0098  460 LEU   A CG  
2076 C  CD1 . LEU   A 304 ? 0.4515 0.3562 0.3215 -0.0152 -0.0070 0.0086  460 LEU   A CD1 
2077 C  CD2 . LEU   A 304 ? 0.5192 0.3960 0.3519 -0.0234 0.0069  0.0171  460 LEU   A CD2 
2078 N  N   . GLY   A 305 ? 0.3061 0.2473 0.1856 -0.0360 0.0171  -0.0054 461 GLY   A N   
2079 C  CA  . GLY   A 305 ? 0.3568 0.3059 0.2308 -0.0344 0.0185  -0.0095 461 GLY   A CA  
2080 C  C   . GLY   A 305 ? 0.3778 0.3422 0.2683 -0.0287 0.0129  -0.0162 461 GLY   A C   
2081 O  O   . GLY   A 305 ? 0.4273 0.3915 0.3139 -0.0225 0.0075  -0.0182 461 GLY   A O   
2082 N  N   . LEU   A 306 ? 0.3522 0.3291 0.2602 -0.0303 0.0139  -0.0199 462 LEU   A N   
2083 C  CA  . LEU   A 306 ? 0.4636 0.4512 0.3849 -0.0240 0.0087  -0.0257 462 LEU   A CA  
2084 C  C   . LEU   A 306 ? 0.4187 0.3978 0.3431 -0.0181 -0.0005 -0.0239 462 LEU   A C   
2085 O  O   . LEU   A 306 ? 0.4211 0.4009 0.3451 -0.0129 -0.0052 -0.0274 462 LEU   A O   
2086 C  CB  . LEU   A 306 ? 0.3743 0.3754 0.3117 -0.0254 0.0109  -0.0295 462 LEU   A CB  
2087 C  CG  . LEU   A 306 ? 0.6368 0.6512 0.5755 -0.0322 0.0200  -0.0330 462 LEU   A CG  
2088 C  CD1 . LEU   A 306 ? 0.5035 0.5261 0.4557 -0.0354 0.0211  -0.0341 462 LEU   A CD1 
2089 C  CD2 . LEU   A 306 ? 0.5396 0.5688 0.4807 -0.0281 0.0217  -0.0403 462 LEU   A CD2 
2090 N  N   . CYS   A 307 ? 0.2790 0.2502 0.2062 -0.0192 -0.0027 -0.0190 463 CYS   A N   
2091 C  CA  . CYS   A 307 ? 0.4063 0.3728 0.3395 -0.0145 -0.0107 -0.0183 463 CYS   A CA  
2092 C  C   . CYS   A 307 ? 0.3442 0.3057 0.2670 -0.0104 -0.0157 -0.0187 463 CYS   A C   
2093 O  O   . CYS   A 307 ? 0.3433 0.3075 0.2712 -0.0067 -0.0208 -0.0230 463 CYS   A O   
2094 C  CB  . CYS   A 307 ? 0.3846 0.3439 0.3205 -0.0163 -0.0114 -0.0131 463 CYS   A CB  
2095 S  SG  . CYS   A 307 ? 0.3829 0.3488 0.3325 -0.0204 -0.0074 -0.0137 463 CYS   A SG  
2096 N  N   . PHE   A 308 ? 0.3324 0.2857 0.2392 -0.0109 -0.0140 -0.0146 464 PHE   A N   
2097 C  CA  . PHE   A 308 ? 0.4007 0.3502 0.2953 -0.0061 -0.0190 -0.0153 464 PHE   A CA  
2098 C  C   . PHE   A 308 ? 0.3711 0.3285 0.2655 -0.0046 -0.0190 -0.0219 464 PHE   A C   
2099 O  O   . PHE   A 308 ? 0.3919 0.3511 0.2882 -0.0006 -0.0256 -0.0260 464 PHE   A O   
2100 C  CB  . PHE   A 308 ? 0.3375 0.2753 0.2109 -0.0065 -0.0158 -0.0095 464 PHE   A CB  
2101 C  CG  . PHE   A 308 ? 0.3901 0.3241 0.2486 -0.0005 -0.0214 -0.0102 464 PHE   A CG  
2102 C  CD1 . PHE   A 308 ? 0.3512 0.2865 0.2141 0.0056  -0.0312 -0.0118 464 PHE   A CD1 
2103 C  CD2 . PHE   A 308 ? 0.3732 0.3036 0.2132 -0.0011 -0.0168 -0.0099 464 PHE   A CD2 
2104 C  CE1 . PHE   A 308 ? 0.3455 0.2796 0.1952 0.0116  -0.0372 -0.0135 464 PHE   A CE1 
2105 C  CE2 . PHE   A 308 ? 0.3941 0.3211 0.2189 0.0052  -0.0225 -0.0107 464 PHE   A CE2 
2106 C  CZ  . PHE   A 308 ? 0.3778 0.3070 0.2077 0.0118  -0.0332 -0.0127 464 PHE   A CZ  
2107 N  N   . ASP   A 309 ? 0.3832 0.3464 0.2762 -0.0081 -0.0115 -0.0238 465 ASP   A N   
2108 C  CA  . ASP   A 309 ? 0.3800 0.3511 0.2730 -0.0057 -0.0111 -0.0306 465 ASP   A CA  
2109 C  C   . ASP   A 309 ? 0.4300 0.4045 0.3375 -0.0021 -0.0170 -0.0356 465 ASP   A C   
2110 O  O   . ASP   A 309 ? 0.4832 0.4571 0.3880 0.0015  -0.0217 -0.0404 465 ASP   A O   
2111 C  CB  . ASP   A 309 ? 0.3248 0.3054 0.2191 -0.0096 -0.0020 -0.0330 465 ASP   A CB  
2112 C  CG  . ASP   A 309 ? 0.4951 0.4836 0.3868 -0.0061 -0.0009 -0.0402 465 ASP   A CG  
2113 O  OD1 . ASP   A 309 ? 0.5168 0.5005 0.3954 -0.0034 -0.0035 -0.0412 465 ASP   A OD1 
2114 O  OD2 . ASP   A 309 ? 0.4814 0.4810 0.3834 -0.0053 0.0022  -0.0452 465 ASP   A OD2 
2115 N  N   . ASN   A 310 ? 0.4160 0.3923 0.3374 -0.0034 -0.0168 -0.0346 466 ASN   A N   
2116 C  CA  . ASN   A 310 ? 0.4001 0.3764 0.3331 -0.0006 -0.0214 -0.0385 466 ASN   A CA  
2117 C  C   . ASN   A 310 ? 0.3346 0.3052 0.2663 0.0009  -0.0286 -0.0394 466 ASN   A C   
2118 O  O   . ASN   A 310 ? 0.3623 0.3320 0.2948 0.0031  -0.0319 -0.0451 466 ASN   A O   
2119 C  CB  . ASN   A 310 ? 0.3569 0.3341 0.3023 -0.0023 -0.0202 -0.0358 466 ASN   A CB  
2120 C  CG  . ASN   A 310 ? 0.4796 0.4660 0.4292 -0.0029 -0.0142 -0.0374 466 ASN   A CG  
2121 O  OD1 . ASN   A 310 ? 0.5541 0.5470 0.5001 -0.0009 -0.0114 -0.0419 466 ASN   A OD1 
2122 N  ND2 . ASN   A 310 ? 0.5671 0.5553 0.5245 -0.0053 -0.0125 -0.0344 466 ASN   A ND2 
2123 N  N   . CYS   A 311 ? 0.3452 0.3121 0.2744 0.0000  -0.0311 -0.0344 467 CYS   A N   
2124 C  CA  . CYS   A 311 ? 0.3278 0.2930 0.2566 0.0020  -0.0385 -0.0361 467 CYS   A CA  
2125 C  C   . CYS   A 311 ? 0.3385 0.3047 0.2567 0.0046  -0.0411 -0.0415 467 CYS   A C   
2126 O  O   . CYS   A 311 ? 0.4126 0.3799 0.3355 0.0051  -0.0453 -0.0478 467 CYS   A O   
2127 C  CB  . CYS   A 311 ? 0.3426 0.3045 0.2666 0.0027  -0.0406 -0.0301 467 CYS   A CB  
2128 S  SG  . CYS   A 311 ? 0.4305 0.3908 0.3675 0.0002  -0.0389 -0.0250 467 CYS   A SG  
2129 N  N   . VAL   A 312 ? 0.2955 0.2607 0.1987 0.0055  -0.0379 -0.0394 468 VAL   A N   
2130 C  CA  . VAL   A 312 ? 0.3347 0.3008 0.2257 0.0083  -0.0400 -0.0443 468 VAL   A CA  
2131 C  C   . VAL   A 312 ? 0.3238 0.2927 0.2218 0.0086  -0.0398 -0.0521 468 VAL   A C   
2132 O  O   . VAL   A 312 ? 0.3063 0.2751 0.2043 0.0100  -0.0454 -0.0584 468 VAL   A O   
2133 C  CB  . VAL   A 312 ? 0.3899 0.3540 0.2636 0.0082  -0.0337 -0.0408 468 VAL   A CB  
2134 C  CG1 . VAL   A 312 ? 0.3867 0.3525 0.2481 0.0111  -0.0349 -0.0467 468 VAL   A CG1 
2135 C  CG2 . VAL   A 312 ? 0.3626 0.3192 0.2245 0.0089  -0.0346 -0.0330 468 VAL   A CG2 
2136 N  N   . THR   A 313 ? 0.2904 0.2615 0.1949 0.0075  -0.0337 -0.0522 469 THR   A N   
2137 C  CA  . THR   A 313 ? 0.3310 0.3029 0.2396 0.0096  -0.0329 -0.0594 469 THR   A CA  
2138 C  C   . THR   A 313 ? 0.3026 0.2692 0.2196 0.0092  -0.0388 -0.0635 469 THR   A C   
2139 O  O   . THR   A 313 ? 0.3615 0.3255 0.2745 0.0106  -0.0418 -0.0705 469 THR   A O   
2140 C  CB  . THR   A 313 ? 0.4866 0.4627 0.4031 0.0097  -0.0268 -0.0584 469 THR   A CB  
2141 O  OG1 . THR   A 313 ? 0.5188 0.5018 0.4276 0.0091  -0.0203 -0.0572 469 THR   A OG1 
2142 C  CG2 . THR   A 313 ? 0.2833 0.2571 0.2041 0.0136  -0.0271 -0.0653 469 THR   A CG2 
2143 N  N   . TYR   A 314 ? 0.2772 0.2420 0.2052 0.0066  -0.0402 -0.0596 470 TYR   A N   
2144 C  CA  . TYR   A 314 ? 0.2841 0.2439 0.2204 0.0047  -0.0442 -0.0638 470 TYR   A CA  
2145 C  C   . TYR   A 314 ? 0.3269 0.2880 0.2587 0.0041  -0.0506 -0.0689 470 TYR   A C   
2146 O  O   . TYR   A 314 ? 0.2961 0.2532 0.2278 0.0032  -0.0528 -0.0764 470 TYR   A O   
2147 C  CB  . TYR   A 314 ? 0.2694 0.2283 0.2174 0.0016  -0.0442 -0.0586 470 TYR   A CB  
2148 C  CG  . TYR   A 314 ? 0.3162 0.2695 0.2725 -0.0017 -0.0468 -0.0630 470 TYR   A CG  
2149 C  CD1 . TYR   A 314 ? 0.3506 0.2947 0.3087 -0.0016 -0.0441 -0.0660 470 TYR   A CD1 
2150 C  CD2 . TYR   A 314 ? 0.2634 0.2206 0.2250 -0.0050 -0.0517 -0.0645 470 TYR   A CD2 
2151 C  CE1 . TYR   A 314 ? 0.3773 0.3135 0.3410 -0.0061 -0.0452 -0.0698 470 TYR   A CE1 
2152 C  CE2 . TYR   A 314 ? 0.2802 0.2333 0.2501 -0.0099 -0.0530 -0.0693 470 TYR   A CE2 
2153 C  CZ  . TYR   A 314 ? 0.3327 0.2741 0.3029 -0.0111 -0.0492 -0.0717 470 TYR   A CZ  
2154 O  OH  . TYR   A 314 ? 0.4872 0.4216 0.4634 -0.0172 -0.0491 -0.0763 470 TYR   A OH  
2155 N  N   . PHE   A 315 ? 0.2871 0.2534 0.2136 0.0050  -0.0536 -0.0653 471 PHE   A N   
2156 C  CA  . PHE   A 315 ? 0.2970 0.2671 0.2186 0.0058  -0.0607 -0.0706 471 PHE   A CA  
2157 C  C   . PHE   A 315 ? 0.3442 0.3127 0.2553 0.0077  -0.0610 -0.0779 471 PHE   A C   
2158 O  O   . PHE   A 315 ? 0.3264 0.2945 0.2394 0.0059  -0.0653 -0.0862 471 PHE   A O   
2159 C  CB  . PHE   A 315 ? 0.3009 0.2748 0.2139 0.0091  -0.0636 -0.0648 471 PHE   A CB  
2160 C  CG  . PHE   A 315 ? 0.3706 0.3509 0.2808 0.0111  -0.0725 -0.0699 471 PHE   A CG  
2161 C  CD1 . PHE   A 315 ? 0.3723 0.3588 0.2965 0.0089  -0.0775 -0.0726 471 PHE   A CD1 
2162 C  CD2 . PHE   A 315 ? 0.3257 0.3074 0.2194 0.0155  -0.0757 -0.0725 471 PHE   A CD2 
2163 C  CE1 . PHE   A 315 ? 0.3113 0.3072 0.2346 0.0111  -0.0862 -0.0785 471 PHE   A CE1 
2164 C  CE2 . PHE   A 315 ? 0.3467 0.3361 0.2377 0.0183  -0.0849 -0.0779 471 PHE   A CE2 
2165 C  CZ  . PHE   A 315 ? 0.3272 0.3248 0.2338 0.0162  -0.0904 -0.0813 471 PHE   A CZ  
2166 N  N   . LEU   A 316 ? 0.3322 0.2998 0.2328 0.0105  -0.0556 -0.0756 472 LEU   A N   
2167 C  CA  . LEU   A 316 ? 0.3281 0.2947 0.2180 0.0130  -0.0551 -0.0827 472 LEU   A CA  
2168 C  C   . LEU   A 316 ? 0.3290 0.2892 0.2261 0.0117  -0.0547 -0.0902 472 LEU   A C   
2169 O  O   . LEU   A 316 ? 0.3409 0.2988 0.2331 0.0118  -0.0582 -0.0987 472 LEU   A O   
2170 C  CB  . LEU   A 316 ? 0.3398 0.3081 0.2196 0.0156  -0.0479 -0.0791 472 LEU   A CB  
2171 C  CG  . LEU   A 316 ? 0.3641 0.3347 0.2291 0.0170  -0.0476 -0.0736 472 LEU   A CG  
2172 C  CD1 . LEU   A 316 ? 0.3428 0.3153 0.2004 0.0170  -0.0384 -0.0698 472 LEU   A CD1 
2173 C  CD2 . LEU   A 316 ? 0.3571 0.3282 0.2087 0.0199  -0.0538 -0.0795 472 LEU   A CD2 
2174 N  N   . GLN   A 317 ? 0.3186 0.2745 0.2259 0.0107  -0.0505 -0.0872 473 GLN   A N   
2175 C  CA  . GLN   A 317 ? 0.3228 0.2687 0.2344 0.0101  -0.0498 -0.0933 473 GLN   A CA  
2176 C  C   . GLN   A 317 ? 0.3279 0.2702 0.2440 0.0048  -0.0554 -0.0993 473 GLN   A C   
2177 O  O   . GLN   A 317 ? 0.3759 0.3111 0.2876 0.0040  -0.0569 -0.1081 473 GLN   A O   
2178 C  CB  . GLN   A 317 ? 0.3117 0.2535 0.2326 0.0103  -0.0452 -0.0880 473 GLN   A CB  
2179 C  CG  . GLN   A 317 ? 0.3198 0.2482 0.2409 0.0121  -0.0432 -0.0930 473 GLN   A CG  
2180 C  CD  . GLN   A 317 ? 0.4038 0.3287 0.3318 0.0140  -0.0393 -0.0873 473 GLN   A CD  
2181 O  OE1 . GLN   A 317 ? 0.4107 0.3343 0.3472 0.0098  -0.0397 -0.0826 473 GLN   A OE1 
2182 N  NE2 . GLN   A 317 ? 0.3140 0.2386 0.2383 0.0211  -0.0356 -0.0883 473 GLN   A NE2 
2183 N  N   . CYS   A 318 ? 0.3186 0.2670 0.2433 0.0009  -0.0587 -0.0956 474 CYS   A N   
2184 C  CA  . CYS   A 318 ? 0.3226 0.2720 0.2539 -0.0049 -0.0640 -0.1021 474 CYS   A CA  
2185 C  C   . CYS   A 318 ? 0.3371 0.2908 0.2590 -0.0041 -0.0694 -0.1108 474 CYS   A C   
2186 O  O   . CYS   A 318 ? 0.3470 0.2970 0.2709 -0.0089 -0.0720 -0.1202 474 CYS   A O   
2187 C  CB  . CYS   A 318 ? 0.3105 0.2697 0.2519 -0.0072 -0.0669 -0.0968 474 CYS   A CB  
2188 S  SG  . CYS   A 318 ? 0.3427 0.2964 0.2967 -0.0100 -0.0613 -0.0887 474 CYS   A SG  
2189 N  N   . LEU   A 319 ? 0.3404 0.3012 0.2508 0.0016  -0.0708 -0.1081 475 LEU   A N   
2190 C  CA  . LEU   A 319 ? 0.3558 0.3208 0.2549 0.0034  -0.0761 -0.1161 475 LEU   A CA  
2191 C  C   . LEU   A 319 ? 0.4267 0.3814 0.3187 0.0037  -0.0734 -0.1244 475 LEU   A C   
2192 O  O   . LEU   A 319 ? 0.3816 0.3352 0.2713 0.0009  -0.0777 -0.1348 475 LEU   A O   
2193 C  CB  . LEU   A 319 ? 0.3849 0.3566 0.2699 0.0098  -0.0769 -0.1102 475 LEU   A CB  
2194 C  CG  . LEU   A 319 ? 0.3586 0.3391 0.2453 0.0114  -0.0816 -0.1038 475 LEU   A CG  
2195 C  CD1 . LEU   A 319 ? 0.3598 0.3405 0.2299 0.0173  -0.0792 -0.0957 475 LEU   A CD1 
2196 C  CD2 . LEU   A 319 ? 0.3619 0.3520 0.2504 0.0106  -0.0914 -0.1122 475 LEU   A CD2 
2197 N  N   . ARG   A 320 ? 0.3669 0.3144 0.2556 0.0074  -0.0662 -0.1206 476 ARG   A N   
2198 C  CA  . ARG   A 320 ? 0.3813 0.3197 0.2610 0.0102  -0.0636 -0.1283 476 ARG   A CA  
2199 C  C   . ARG   A 320 ? 0.4022 0.3265 0.2877 0.0051  -0.0636 -0.1357 476 ARG   A C   
2200 O  O   . ARG   A 320 ? 0.4057 0.3229 0.2838 0.0045  -0.0653 -0.1459 476 ARG   A O   
2201 C  CB  . ARG   A 320 ? 0.3774 0.3146 0.2535 0.0164  -0.0561 -0.1231 476 ARG   A CB  
2202 C  CG  . ARG   A 320 ? 0.4591 0.4075 0.3252 0.0204  -0.0543 -0.1181 476 ARG   A CG  
2203 C  CD  . ARG   A 320 ? 0.4619 0.4108 0.3227 0.0262  -0.0469 -0.1182 476 ARG   A CD  
2204 N  NE  . ARG   A 320 ? 0.3731 0.3324 0.2304 0.0273  -0.0424 -0.1101 476 ARG   A NE  
2205 C  CZ  . ARG   A 320 ? 0.5411 0.5039 0.4078 0.0256  -0.0392 -0.1017 476 ARG   A CZ  
2206 N  NH1 . ARG   A 320 ? 0.3970 0.3545 0.2770 0.0235  -0.0400 -0.0996 476 ARG   A NH1 
2207 N  NH2 . ARG   A 320 ? 0.4630 0.4339 0.3248 0.0254  -0.0344 -0.0954 476 ARG   A NH2 
2208 N  N   . THR   A 321 ? 0.3783 0.2971 0.2758 0.0012  -0.0614 -0.1309 477 THR   A N   
2209 C  CA  . THR   A 321 ? 0.3874 0.2900 0.2890 -0.0045 -0.0601 -0.1366 477 THR   A CA  
2210 C  C   . THR   A 321 ? 0.3896 0.2966 0.2995 -0.0144 -0.0653 -0.1427 477 THR   A C   
2211 O  O   . THR   A 321 ? 0.4917 0.3850 0.4047 -0.0215 -0.0637 -0.1484 477 THR   A O   
2212 C  CB  . THR   A 321 ? 0.3780 0.2713 0.2864 -0.0039 -0.0546 -0.1286 477 THR   A CB  
2213 O  OG1 . THR   A 321 ? 0.3597 0.2648 0.2799 -0.0074 -0.0558 -0.1208 477 THR   A OG1 
2214 C  CG2 . THR   A 321 ? 0.3757 0.2681 0.2778 0.0062  -0.0499 -0.1240 477 THR   A CG2 
2215 N  N   . GLU   A 322 ? 0.3822 0.3079 0.2951 -0.0148 -0.0712 -0.1419 478 GLU   A N   
2216 C  CA  . GLU   A 322 ? 0.4017 0.3373 0.3235 -0.0228 -0.0773 -0.1489 478 GLU   A CA  
2217 C  C   . GLU   A 322 ? 0.4712 0.4028 0.4080 -0.0312 -0.0744 -0.1468 478 GLU   A C   
2218 O  O   . GLU   A 322 ? 0.4048 0.3325 0.3477 -0.0408 -0.0749 -0.1556 478 GLU   A O   
2219 C  CB  . GLU   A 322 ? 0.4048 0.3357 0.3198 -0.0269 -0.0805 -0.1630 478 GLU   A CB  
2220 C  CG  . GLU   A 322 ? 0.4933 0.4245 0.3915 -0.0186 -0.0819 -0.1658 478 GLU   A CG  
2221 C  CD  . GLU   A 322 ? 0.7602 0.6853 0.6510 -0.0228 -0.0849 -0.1804 478 GLU   A CD  
2222 O  OE1 . GLU   A 322 ? 0.7240 0.6593 0.6219 -0.0303 -0.0910 -0.1891 478 GLU   A OE1 
2223 O  OE2 . GLU   A 322 ? 0.7797 0.6906 0.6581 -0.0186 -0.0813 -0.1840 478 GLU   A OE2 
2224 N  N   . LYS   A 323 ? 0.3988 0.3314 0.3411 -0.0281 -0.0708 -0.1353 479 LYS   A N   
2225 C  CA  . LYS   A 323 ? 0.4202 0.3482 0.3750 -0.0348 -0.0671 -0.1319 479 LYS   A CA  
2226 C  C   . LYS   A 323 ? 0.3419 0.2837 0.3046 -0.0314 -0.0680 -0.1216 479 LYS   A C   
2227 O  O   . LYS   A 323 ? 0.3242 0.2651 0.2818 -0.0240 -0.0654 -0.1128 479 LYS   A O   
2228 C  CB  . LYS   A 323 ? 0.3821 0.2870 0.3319 -0.0343 -0.0594 -0.1290 479 LYS   A CB  
2229 N  N   . LEU   A 324 ? 0.3919 0.3472 0.3673 -0.0368 -0.0715 -0.1235 480 LEU   A N   
2230 C  CA  . LEU   A 324 ? 0.3399 0.3063 0.3237 -0.0342 -0.0719 -0.1144 480 LEU   A CA  
2231 C  C   . LEU   A 324 ? 0.3424 0.3142 0.3420 -0.0436 -0.0713 -0.1182 480 LEU   A C   
2232 O  O   . LEU   A 324 ? 0.3178 0.3065 0.3256 -0.0469 -0.0771 -0.1255 480 LEU   A O   
2233 C  CB  . LEU   A 324 ? 0.3120 0.2948 0.2916 -0.0267 -0.0788 -0.1124 480 LEU   A CB  
2234 C  CG  . LEU   A 324 ? 0.2916 0.2835 0.2777 -0.0230 -0.0793 -0.1032 480 LEU   A CG  
2235 C  CD1 . LEU   A 324 ? 0.3458 0.3259 0.3291 -0.0203 -0.0721 -0.0926 480 LEU   A CD1 
2236 C  CD2 . LEU   A 324 ? 0.3499 0.3545 0.3285 -0.0150 -0.0864 -0.1016 480 LEU   A CD2 
2237 N  N   . GLU   A 325 ? 0.3665 0.3249 0.3698 -0.0477 -0.0640 -0.1137 481 GLU   A N   
2238 C  CA  . GLU   A 325 ? 0.3725 0.3342 0.3897 -0.0576 -0.0615 -0.1167 481 GLU   A CA  
2239 C  C   . GLU   A 325 ? 0.3043 0.2872 0.3331 -0.0549 -0.0654 -0.1130 481 GLU   A C   
2240 O  O   . GLU   A 325 ? 0.2754 0.2599 0.3011 -0.0467 -0.0655 -0.1032 481 GLU   A O   
2241 C  CB  . GLU   A 325 ? 0.3691 0.3099 0.3844 -0.0608 -0.0527 -0.1109 481 GLU   A CB  
2242 C  CG  . GLU   A 325 ? 0.5219 0.4384 0.5247 -0.0626 -0.0482 -0.1143 481 GLU   A CG  
2243 C  CD  . GLU   A 325 ? 0.7199 0.6152 0.7188 -0.0640 -0.0401 -0.1078 481 GLU   A CD  
2244 O  OE1 . GLU   A 325 ? 0.5539 0.4545 0.5606 -0.0646 -0.0377 -0.1012 481 GLU   A OE1 
2245 O  OE2 . GLU   A 325 ? 0.9157 0.7881 0.9024 -0.0638 -0.0361 -0.1095 481 GLU   A OE2 
2246 N  N   . ASN   A 326 ? 0.3369 0.3363 0.3791 -0.0620 -0.0685 -0.1215 482 ASN   A N   
2247 C  CA  . ASN   A 326 ? 0.3464 0.3649 0.4013 -0.0600 -0.0710 -0.1187 482 ASN   A CA  
2248 C  C   . ASN   A 326 ? 0.2844 0.2917 0.3420 -0.0610 -0.0631 -0.1091 482 ASN   A C   
2249 O  O   . ASN   A 326 ? 0.3381 0.3302 0.3963 -0.0695 -0.0557 -0.1099 482 ASN   A O   
2250 C  CB  . ASN   A 326 ? 0.3189 0.3574 0.3899 -0.0691 -0.0741 -0.1311 482 ASN   A CB  
2251 C  CG  . ASN   A 326 ? 0.4017 0.4628 0.4866 -0.0655 -0.0775 -0.1297 482 ASN   A CG  
2252 O  OD1 . ASN   A 326 ? 0.2700 0.3281 0.3615 -0.0676 -0.0715 -0.1237 482 ASN   A OD1 
2253 N  ND2 . ASN   A 326 ? 0.3064 0.3901 0.3949 -0.0591 -0.0873 -0.1353 482 ASN   A ND2 
2254 N  N   . TYR   A 327 ? 0.2825 0.2956 0.3399 -0.0522 -0.0646 -0.1000 483 TYR   A N   
2255 C  CA  . TYR   A 327 ? 0.3611 0.3631 0.4187 -0.0517 -0.0577 -0.0905 483 TYR   A CA  
2256 C  C   . TYR   A 327 ? 0.2709 0.2756 0.3418 -0.0616 -0.0524 -0.0936 483 TYR   A C   
2257 O  O   . TYR   A 327 ? 0.2548 0.2442 0.3233 -0.0646 -0.0450 -0.0881 483 TYR   A O   
2258 C  CB  . TYR   A 327 ? 0.2806 0.2895 0.3361 -0.0414 -0.0606 -0.0817 483 TYR   A CB  
2259 C  CG  . TYR   A 327 ? 0.2952 0.2905 0.3466 -0.0394 -0.0542 -0.0717 483 TYR   A CG  
2260 C  CD1 . TYR   A 327 ? 0.2291 0.2085 0.2682 -0.0365 -0.0511 -0.0670 483 TYR   A CD1 
2261 C  CD2 . TYR   A 327 ? 0.3092 0.3092 0.3693 -0.0399 -0.0515 -0.0677 483 TYR   A CD2 
2262 C  CE1 . TYR   A 327 ? 0.2901 0.2597 0.3261 -0.0343 -0.0460 -0.0589 483 TYR   A CE1 
2263 C  CE2 . TYR   A 327 ? 0.2125 0.2009 0.2685 -0.0380 -0.0461 -0.0593 483 TYR   A CE2 
2264 C  CZ  . TYR   A 327 ? 0.3360 0.3097 0.3802 -0.0353 -0.0436 -0.0551 483 TYR   A CZ  
2265 O  OH  . TYR   A 327 ? 0.3093 0.2740 0.3500 -0.0331 -0.0390 -0.0478 483 TYR   A OH  
2266 N  N   . PHE   A 328 ? 0.2882 0.3133 0.3728 -0.0666 -0.0559 -0.1026 484 PHE   A N   
2267 C  CA  . PHE   A 328 ? 0.3283 0.3595 0.4270 -0.0772 -0.0503 -0.1071 484 PHE   A CA  
2268 C  C   . PHE   A 328 ? 0.4243 0.4489 0.5253 -0.0911 -0.0463 -0.1174 484 PHE   A C   
2269 O  O   . PHE   A 328 ? 0.3973 0.4151 0.5037 -0.1017 -0.0380 -0.1189 484 PHE   A O   
2270 C  CB  . PHE   A 328 ? 0.3257 0.3865 0.4403 -0.0745 -0.0561 -0.1119 484 PHE   A CB  
2271 C  CG  . PHE   A 328 ? 0.2816 0.3466 0.3938 -0.0618 -0.0590 -0.1020 484 PHE   A CG  
2272 C  CD1 . PHE   A 328 ? 0.3036 0.3718 0.4061 -0.0498 -0.0670 -0.0986 484 PHE   A CD1 
2273 C  CD2 . PHE   A 328 ? 0.3573 0.4216 0.4754 -0.0623 -0.0533 -0.0963 484 PHE   A CD2 
2274 C  CE1 . PHE   A 328 ? 0.3985 0.4673 0.4968 -0.0390 -0.0688 -0.0896 484 PHE   A CE1 
2275 C  CE2 . PHE   A 328 ? 0.3749 0.4412 0.4898 -0.0511 -0.0558 -0.0878 484 PHE   A CE2 
2276 C  CZ  . PHE   A 328 ? 0.3472 0.4150 0.4520 -0.0397 -0.0634 -0.0845 484 PHE   A CZ  
2277 N  N   . ILE   A 329 ? 0.3907 0.4157 0.4865 -0.0915 -0.0514 -0.1247 485 ILE   A N   
2278 C  CA  . ILE   A 329 ? 0.3383 0.3569 0.4354 -0.1050 -0.0482 -0.1361 485 ILE   A CA  
2279 C  C   . ILE   A 329 ? 0.3393 0.3316 0.4173 -0.1022 -0.0470 -0.1338 485 ILE   A C   
2280 O  O   . ILE   A 329 ? 0.3661 0.3631 0.4388 -0.0987 -0.0537 -0.1395 485 ILE   A O   
2281 C  CB  . ILE   A 329 ? 0.3032 0.3495 0.4112 -0.1069 -0.0557 -0.1470 485 ILE   A CB  
2282 C  CG1 . ILE   A 329 ? 0.2846 0.3599 0.4097 -0.1035 -0.0591 -0.1474 485 ILE   A CG1 
2283 C  CG2 . ILE   A 329 ? 0.3594 0.3988 0.4673 -0.1198 -0.0498 -0.1535 485 ILE   A CG2 
2284 C  CD1 . ILE   A 329 ? 0.3582 0.4625 0.4920 -0.1002 -0.0680 -0.1562 485 ILE   A CD1 
2285 N  N   . PRO   A 330 ? 0.3657 0.3303 0.4322 -0.1028 -0.0388 -0.1260 486 PRO   A N   
2286 C  CA  . PRO   A 330 ? 0.4361 0.3782 0.4842 -0.0957 -0.0386 -0.1222 486 PRO   A CA  
2287 C  C   . PRO   A 330 ? 0.5228 0.4554 0.5643 -0.1021 -0.0394 -0.1331 486 PRO   A C   
2288 O  O   . PRO   A 330 ? 0.4638 0.3862 0.4920 -0.0942 -0.0421 -0.1322 486 PRO   A O   
2289 C  CB  . PRO   A 330 ? 0.4484 0.3649 0.4876 -0.0957 -0.0295 -0.1130 486 PRO   A CB  
2290 C  CG  . PRO   A 330 ? 0.4783 0.3978 0.5289 -0.1080 -0.0232 -0.1155 486 PRO   A CG  
2291 C  CD  . PRO   A 330 ? 0.4040 0.3573 0.4733 -0.1093 -0.0295 -0.1209 486 PRO   A CD  
2292 N  N   . GLU   A 331 ? 0.4553 0.3915 0.5039 -0.1146 -0.0370 -0.1414 487 GLU   A N   
2293 C  CA  . GLU   A 331 ? 0.4563 0.3841 0.4968 -0.1189 -0.0380 -0.1491 487 GLU   A CA  
2294 C  C   . GLU   A 331 ? 0.4936 0.4481 0.5404 -0.1159 -0.0483 -0.1574 487 GLU   A C   
2295 O  O   . GLU   A 331 ? 0.4384 0.3885 0.4789 -0.1192 -0.0501 -0.1646 487 GLU   A O   
2296 C  CB  . GLU   A 331 ? 0.5539 0.4720 0.5965 -0.1319 -0.0304 -0.1514 487 GLU   A CB  
2297 C  CG  . GLU   A 331 ? 0.7164 0.5974 0.7427 -0.1333 -0.0213 -0.1453 487 GLU   A CG  
2298 C  CD  . GLU   A 331 ? 0.8818 0.7532 0.9097 -0.1460 -0.0133 -0.1472 487 GLU   A CD  
2299 O  OE1 . GLU   A 331 ? 0.7558 0.6512 0.7994 -0.1544 -0.0140 -0.1534 487 GLU   A OE1 
2300 O  OE2 . GLU   A 331 ? 0.8796 0.7199 0.8928 -0.1471 -0.0061 -0.1429 487 GLU   A OE2 
2301 N  N   . PHE   A 332 ? 0.3553 0.3361 0.4129 -0.1090 -0.0553 -0.1564 488 PHE   A N   
2302 C  CA  . PHE   A 332 ? 0.3901 0.3945 0.4500 -0.1027 -0.0659 -0.1626 488 PHE   A CA  
2303 C  C   . PHE   A 332 ? 0.3332 0.3308 0.3795 -0.0901 -0.0709 -0.1590 488 PHE   A C   
2304 O  O   . PHE   A 332 ? 0.3528 0.3479 0.3960 -0.0807 -0.0697 -0.1465 488 PHE   A O   
2305 C  CB  . PHE   A 332 ? 0.3460 0.3818 0.4229 -0.1001 -0.0712 -0.1630 488 PHE   A CB  
2306 C  CG  . PHE   A 332 ? 0.3270 0.3877 0.4068 -0.0952 -0.0814 -0.1703 488 PHE   A CG  
2307 C  CD1 . PHE   A 332 ? 0.4146 0.4823 0.4853 -0.0820 -0.0904 -0.1686 488 PHE   A CD1 
2308 C  CD2 . PHE   A 332 ? 0.3377 0.4146 0.4284 -0.1034 -0.0818 -0.1789 488 PHE   A CD2 
2309 C  CE1 . PHE   A 332 ? 0.3265 0.4155 0.3974 -0.0763 -0.0997 -0.1745 488 PHE   A CE1 
2310 C  CE2 . PHE   A 332 ? 0.3807 0.4808 0.4737 -0.0980 -0.0914 -0.1858 488 PHE   A CE2 
2311 C  CZ  . PHE   A 332 ? 0.3366 0.4421 0.4190 -0.0840 -0.1004 -0.1832 488 PHE   A CZ  
2312 N  N   . ASN   A 333 ? 0.3462 0.3395 0.3813 -0.0881 -0.0748 -0.1651 489 ASN   A N   
2313 C  CA  . ASN   A 333 ? 0.3567 0.3422 0.3755 -0.0754 -0.0776 -0.1593 489 ASN   A CA  
2314 C  C   . ASN   A 333 ? 0.3409 0.3511 0.3596 -0.0670 -0.0883 -0.1620 489 ASN   A C   
2315 O  O   . ASN   A 333 ? 0.3525 0.3728 0.3707 -0.0698 -0.0939 -0.1728 489 ASN   A O   
2316 C  CB  . ASN   A 333 ? 0.3645 0.3270 0.3690 -0.0779 -0.0744 -0.1649 489 ASN   A CB  
2317 C  CG  . ASN   A 333 ? 0.4060 0.3603 0.3938 -0.0648 -0.0755 -0.1582 489 ASN   A CG  
2318 O  OD1 . ASN   A 333 ? 0.3549 0.3205 0.3411 -0.0549 -0.0786 -0.1495 489 ASN   A OD1 
2319 N  ND2 . ASN   A 333 ? 0.3808 0.3148 0.3556 -0.0650 -0.0724 -0.1624 489 ASN   A ND2 
2320 N  N   . LEU   A 334 ? 0.3266 0.3447 0.3439 -0.0563 -0.0905 -0.1510 490 LEU   A N   
2321 C  CA  . LEU   A 334 ? 0.3752 0.4133 0.3891 -0.0468 -0.1003 -0.1519 490 LEU   A CA  
2322 C  C   . LEU   A 334 ? 0.3379 0.3698 0.3336 -0.0406 -0.1037 -0.1543 490 LEU   A C   
2323 O  O   . LEU   A 334 ? 0.3444 0.3918 0.3355 -0.0351 -0.1125 -0.1596 490 LEU   A O   
2324 C  CB  . LEU   A 334 ? 0.3109 0.3533 0.3244 -0.0370 -0.1005 -0.1387 490 LEU   A CB  
2325 C  CG  . LEU   A 334 ? 0.2980 0.3480 0.3286 -0.0411 -0.0975 -0.1355 490 LEU   A CG  
2326 C  CD1 . LEU   A 334 ? 0.2860 0.3308 0.3118 -0.0322 -0.0950 -0.1212 490 LEU   A CD1 
2327 C  CD2 . LEU   A 334 ? 0.2984 0.3754 0.3432 -0.0425 -0.1055 -0.1451 490 LEU   A CD2 
2328 N  N   . PHE   A 335 ? 0.3427 0.3526 0.3271 -0.0404 -0.0969 -0.1508 491 PHE   A N   
2329 C  CA  . PHE   A 335 ? 0.3550 0.3582 0.3218 -0.0345 -0.0987 -0.1532 491 PHE   A CA  
2330 C  C   . PHE   A 335 ? 0.4736 0.4668 0.4377 -0.0426 -0.0978 -0.1660 491 PHE   A C   
2331 O  O   . PHE   A 335 ? 0.4996 0.4799 0.4490 -0.0388 -0.0958 -0.1673 491 PHE   A O   
2332 C  CB  . PHE   A 335 ? 0.3635 0.3515 0.3188 -0.0270 -0.0920 -0.1414 491 PHE   A CB  
2333 C  CG  . PHE   A 335 ? 0.3705 0.3672 0.3206 -0.0176 -0.0941 -0.1307 491 PHE   A CG  
2334 C  CD1 . PHE   A 335 ? 0.3392 0.3538 0.2920 -0.0141 -0.1021 -0.1316 491 PHE   A CD1 
2335 C  CD2 . PHE   A 335 ? 0.3916 0.3781 0.3332 -0.0120 -0.0879 -0.1203 491 PHE   A CD2 
2336 C  CE1 . PHE   A 335 ? 0.3345 0.3529 0.2796 -0.0051 -0.1035 -0.1214 491 PHE   A CE1 
2337 C  CE2 . PHE   A 335 ? 0.3290 0.3210 0.2644 -0.0048 -0.0888 -0.1108 491 PHE   A CE2 
2338 C  CZ  . PHE   A 335 ? 0.3299 0.3359 0.2659 -0.0013 -0.0963 -0.1110 491 PHE   A CZ  
2339 N  N   . SER   A 336 ? 0.4330 0.4317 0.4105 -0.0541 -0.0986 -0.1760 492 SER   A N   
2340 C  CA  . SER   A 336 ? 0.4333 0.4207 0.4069 -0.0627 -0.0960 -0.1856 492 SER   A CA  
2341 C  C   . SER   A 336 ? 0.5165 0.5137 0.4790 -0.0575 -0.1030 -0.1915 492 SER   A C   
2342 O  O   . SER   A 336 ? 0.4878 0.5059 0.4506 -0.0505 -0.1108 -0.1905 492 SER   A O   
2343 C  CB  . SER   A 336 ? 0.4414 0.4343 0.4309 -0.0759 -0.0934 -0.1899 492 SER   A CB  
2344 O  OG  . SER   A 336 ? 0.5383 0.5172 0.5222 -0.0846 -0.0903 -0.1978 492 SER   A OG  
2345 N  N   . SER   A 337 ? 0.5160 0.4964 0.4670 -0.0604 -0.1000 -0.1975 493 SER   A N   
2346 C  CA  . SER   A 337 ? 0.6339 0.6222 0.5741 -0.0569 -0.1060 -0.2041 493 SER   A CA  
2347 C  C   . SER   A 337 ? 0.5415 0.5512 0.4933 -0.0633 -0.1120 -0.2111 493 SER   A C   
2348 O  O   . SER   A 337 ? 0.5151 0.5382 0.4602 -0.0583 -0.1190 -0.2154 493 SER   A O   
2349 C  CB  . SER   A 337 ? 0.5480 0.5125 0.4740 -0.0593 -0.1010 -0.2097 493 SER   A CB  
2350 O  OG  . SER   A 337 ? 0.7297 0.6801 0.6620 -0.0723 -0.0957 -0.2147 493 SER   A OG  
2351 N  N   . ASN   A 338 ? 0.5829 0.5966 0.5518 -0.0738 -0.1091 -0.2124 494 ASN   A N   
2352 C  CA  . ASN   A 338 ? 0.7038 0.7414 0.6868 -0.0793 -0.1144 -0.2191 494 ASN   A CA  
2353 C  C   . ASN   A 338 ? 0.6202 0.6851 0.6102 -0.0692 -0.1224 -0.2148 494 ASN   A C   
2354 O  O   . ASN   A 338 ? 0.7027 0.7905 0.7019 -0.0698 -0.1286 -0.2208 494 ASN   A O   
2355 C  CB  . ASN   A 338 ? 0.6731 0.7063 0.6717 -0.0936 -0.1076 -0.2214 494 ASN   A CB  
2356 C  CG  . ASN   A 338 ? 0.8843 0.8869 0.8738 -0.1031 -0.0996 -0.2249 494 ASN   A CG  
2357 O  OD1 . ASN   A 338 ? 0.9006 0.8896 0.8743 -0.1006 -0.1004 -0.2288 494 ASN   A OD1 
2358 N  ND2 . ASN   A 338 ? 0.8003 0.7906 0.7984 -0.1134 -0.0916 -0.2230 494 ASN   A ND2 
2359 N  N   . LEU   A 339 ? 0.4969 0.5591 0.4821 -0.0594 -0.1223 -0.2048 495 LEU   A N   
2360 C  CA  . LEU   A 339 ? 0.6089 0.6922 0.5976 -0.0486 -0.1295 -0.1994 495 LEU   A CA  
2361 C  C   . LEU   A 339 ? 0.5127 0.5948 0.4811 -0.0343 -0.1348 -0.1944 495 LEU   A C   
2362 O  O   . LEU   A 339 ? 0.4334 0.5331 0.3987 -0.0254 -0.1429 -0.1940 495 LEU   A O   
2363 C  CB  . LEU   A 339 ? 0.4414 0.5232 0.4412 -0.0489 -0.1253 -0.1911 495 LEU   A CB  
2364 C  CG  . LEU   A 339 ? 0.4066 0.4908 0.4263 -0.0624 -0.1193 -0.1944 495 LEU   A CG  
2365 C  CD1 . LEU   A 339 ? 0.3804 0.4605 0.4085 -0.0620 -0.1145 -0.1856 495 LEU   A CD1 
2366 C  CD2 . LEU   A 339 ? 0.4361 0.5476 0.4701 -0.0647 -0.1250 -0.2019 495 LEU   A CD2 
2367 N  N   . ILE   A 340 ? 0.4676 0.5289 0.4213 -0.0315 -0.1300 -0.1903 496 ILE   A N   
2368 C  CA  . ILE   A 340 ? 0.4224 0.4801 0.3549 -0.0191 -0.1331 -0.1853 496 ILE   A CA  
2369 C  C   . ILE   A 340 ? 0.5547 0.5942 0.4734 -0.0212 -0.1285 -0.1899 496 ILE   A C   
2370 O  O   . ILE   A 340 ? 0.4970 0.5190 0.4185 -0.0277 -0.1209 -0.1907 496 ILE   A O   
2371 C  CB  . ILE   A 340 ? 0.4867 0.5385 0.4144 -0.0112 -0.1313 -0.1738 496 ILE   A CB  
2372 C  CG1 . ILE   A 340 ? 0.4252 0.4931 0.3674 -0.0093 -0.1352 -0.1694 496 ILE   A CG1 
2373 C  CG2 . ILE   A 340 ? 0.4497 0.4975 0.3536 0.0009  -0.1335 -0.1682 496 ILE   A CG2 
2374 C  CD1 . ILE   A 340 ? 0.3810 0.4395 0.3218 -0.0043 -0.1298 -0.1551 496 ILE   A CD1 
2375 N  N   . ASP   A 341 ? 0.4828 0.5257 0.3857 -0.0151 -0.1327 -0.1928 497 ASP   A N   
2376 C  CA  . ASP   A 341 ? 0.4590 0.4859 0.3490 -0.0169 -0.1284 -0.1981 497 ASP   A CA  
2377 C  C   . ASP   A 341 ? 0.5439 0.5552 0.4198 -0.0097 -0.1225 -0.1908 497 ASP   A C   
2378 O  O   . ASP   A 341 ? 0.4884 0.5023 0.3611 -0.0026 -0.1228 -0.1815 497 ASP   A O   
2379 C  CB  . ASP   A 341 ? 0.6050 0.6411 0.4833 -0.0135 -0.1346 -0.2045 497 ASP   A CB  
2380 C  CG  . ASP   A 341 ? 0.5924 0.6372 0.4545 -0.0002 -0.1397 -0.1973 497 ASP   A CG  
2381 O  OD1 . ASP   A 341 ? 0.6602 0.6989 0.5145 0.0066  -0.1368 -0.1874 497 ASP   A OD1 
2382 O  OD2 . ASP   A 341 ? 0.7954 0.8522 0.6511 0.0033  -0.1466 -0.2014 497 ASP   A OD2 
2383 N  N   . LYS   A 342 ? 0.5240 0.5189 0.3911 -0.0114 -0.1169 -0.1954 498 LYS   A N   
2384 C  CA  . LYS   A 342 ? 0.5596 0.5404 0.4149 -0.0047 -0.1104 -0.1900 498 LYS   A CA  
2385 C  C   . LYS   A 342 ? 0.5517 0.5396 0.3893 0.0063  -0.1125 -0.1834 498 LYS   A C   
2386 O  O   . LYS   A 342 ? 0.5383 0.5224 0.3724 0.0113  -0.1072 -0.1726 498 LYS   A O   
2387 C  CB  . LYS   A 342 ? 0.6982 0.6616 0.5462 -0.0072 -0.1047 -0.1972 498 LYS   A CB  
2388 C  CG  . LYS   A 342 ? 0.8326 0.7829 0.6700 0.0003  -0.0974 -0.1928 498 LYS   A CG  
2389 C  CD  . LYS   A 342 ? 0.6063 0.5454 0.4565 -0.0025 -0.0908 -0.1859 498 LYS   A CD  
2390 C  CE  . LYS   A 342 ? 0.6385 0.5678 0.4808 0.0052  -0.0822 -0.1790 498 LYS   A CE  
2391 N  NZ  . LYS   A 342 ? 0.6742 0.6088 0.5243 0.0078  -0.0782 -0.1648 498 LYS   A NZ  
2392 N  N   . ARG   A 343 ? 0.5090 0.5062 0.3363 0.0092  -0.1179 -0.1868 499 ARG   A N   
2393 C  CA  . ARG   A 343 ? 0.5252 0.5256 0.3319 0.0193  -0.1186 -0.1804 499 ARG   A CA  
2394 C  C   . ARG   A 343 ? 0.5648 0.5725 0.3711 0.0247  -0.1213 -0.1697 499 ARG   A C   
2395 O  O   . ARG   A 343 ? 0.5600 0.5628 0.3515 0.0313  -0.1171 -0.1609 499 ARG   A O   
2396 C  CB  . ARG   A 343 ? 0.6724 0.6809 0.4685 0.0212  -0.1245 -0.1865 499 ARG   A CB  
2397 C  CG  . ARG   A 343 ? 0.9151 0.9269 0.6889 0.0314  -0.1259 -0.1792 499 ARG   A CG  
2398 C  CD  . ARG   A 343 ? 1.0268 1.0269 0.7830 0.0353  -0.1172 -0.1772 499 ARG   A CD  
2399 N  NE  . ARG   A 343 ? 0.9294 0.9250 0.6781 0.0401  -0.1114 -0.1661 499 ARG   A NE  
2400 C  CZ  . ARG   A 343 ? 0.9849 0.9817 0.7152 0.0470  -0.1112 -0.1572 499 ARG   A CZ  
2401 N  NH1 . ARG   A 343 ? 0.7917 0.7943 0.5092 0.0513  -0.1173 -0.1575 499 ARG   A NH1 
2402 N  NH2 . ARG   A 343 ? 0.9070 0.8977 0.6303 0.0496  -0.1044 -0.1477 499 ARG   A NH2 
2403 N  N   . SER   A 344 ? 0.4890 0.5080 0.3112 0.0218  -0.1275 -0.1697 500 SER   A N   
2404 C  CA  . SER   A 344 ? 0.4576 0.4821 0.2794 0.0276  -0.1303 -0.1596 500 SER   A CA  
2405 C  C   . SER   A 344 ? 0.4406 0.4534 0.2686 0.0258  -0.1197 -0.1479 500 SER   A C   
2406 O  O   . SER   A 344 ? 0.4391 0.4482 0.2568 0.0315  -0.1160 -0.1360 500 SER   A O   
2407 C  CB  . SER   A 344 ? 0.4519 0.4918 0.2936 0.0241  -0.1374 -0.1624 500 SER   A CB  
2408 O  OG  . SER   A 344 ? 0.5750 0.6272 0.4145 0.0255  -0.1444 -0.1690 500 SER   A OG  
2409 N  N   . LYS   A 345 ? 0.4469 0.4527 0.2911 0.0178  -0.1142 -0.1508 501 LYS   A N   
2410 C  CA  . LYS   A 345 ? 0.4139 0.4097 0.2652 0.0163  -0.1044 -0.1402 501 LYS   A CA  
2411 C  C   . LYS   A 345 ? 0.4200 0.4067 0.2554 0.0209  -0.0964 -0.1355 501 LYS   A C   
2412 O  O   . LYS   A 345 ? 0.4149 0.3983 0.2490 0.0228  -0.0899 -0.1246 501 LYS   A O   
2413 C  CB  . LYS   A 345 ? 0.4758 0.4649 0.3453 0.0077  -0.1008 -0.1449 501 LYS   A CB  
2414 C  CG  . LYS   A 345 ? 0.5336 0.5325 0.4211 0.0018  -0.1064 -0.1481 501 LYS   A CG  
2415 C  CD  . LYS   A 345 ? 0.5715 0.5605 0.4748 -0.0070 -0.1006 -0.1498 501 LYS   A CD  
2416 C  CE  . LYS   A 345 ? 0.6437 0.6253 0.5464 -0.0135 -0.1011 -0.1633 501 LYS   A CE  
2417 N  NZ  . LYS   A 345 ? 0.5432 0.5392 0.4535 -0.0192 -0.1097 -0.1750 501 LYS   A NZ  
2418 N  N   . GLU   A 346 ? 0.4360 0.4196 0.2593 0.0222  -0.0965 -0.1444 502 GLU   A N   
2419 C  CA  . GLU   A 346 ? 0.4719 0.4497 0.2797 0.0270  -0.0888 -0.1410 502 GLU   A CA  
2420 C  C   . GLU   A 346 ? 0.5074 0.4892 0.2980 0.0329  -0.0889 -0.1321 502 GLU   A C   
2421 O  O   . GLU   A 346 ? 0.5172 0.4954 0.3012 0.0347  -0.0803 -0.1238 502 GLU   A O   
2422 C  CB  . GLU   A 346 ? 0.5394 0.5134 0.3369 0.0278  -0.0894 -0.1532 502 GLU   A CB  
2423 C  CG  . GLU   A 346 ? 0.5567 0.5203 0.3658 0.0233  -0.0858 -0.1603 502 GLU   A CG  
2424 C  CD  . GLU   A 346 ? 0.6561 0.6143 0.4538 0.0243  -0.0870 -0.1734 502 GLU   A CD  
2425 O  OE1 . GLU   A 346 ? 0.7466 0.7115 0.5305 0.0269  -0.0929 -0.1789 502 GLU   A OE1 
2426 O  OE2 . GLU   A 346 ? 0.9215 0.8677 0.7228 0.0231  -0.0821 -0.1784 502 GLU   A OE2 
2427 N  N   . PHE   A 347 ? 0.4606 0.4497 0.2431 0.0361  -0.0983 -0.1341 503 PHE   A N   
2428 C  CA  . PHE   A 347 ? 0.4950 0.4845 0.2579 0.0427  -0.0988 -0.1251 503 PHE   A CA  
2429 C  C   . PHE   A 347 ? 0.4753 0.4618 0.2453 0.0420  -0.0942 -0.1119 503 PHE   A C   
2430 O  O   . PHE   A 347 ? 0.5583 0.5385 0.3147 0.0440  -0.0868 -0.1025 503 PHE   A O   
2431 C  CB  . PHE   A 347 ? 0.5769 0.5752 0.3305 0.0477  -0.1114 -0.1305 503 PHE   A CB  
2432 C  CG  . PHE   A 347 ? 0.5355 0.5311 0.2646 0.0560  -0.1126 -0.1213 503 PHE   A CG  
2433 C  CD1 . PHE   A 347 ? 0.5326 0.5232 0.2356 0.0607  -0.1097 -0.1216 503 PHE   A CD1 
2434 C  CD2 . PHE   A 347 ? 0.4993 0.4958 0.2299 0.0596  -0.1163 -0.1124 503 PHE   A CD2 
2435 C  CE1 . PHE   A 347 ? 0.6597 0.6445 0.3371 0.0682  -0.1101 -0.1126 503 PHE   A CE1 
2436 C  CE2 . PHE   A 347 ? 0.7376 0.7277 0.4427 0.0679  -0.1172 -0.1035 503 PHE   A CE2 
2437 C  CZ  . PHE   A 347 ? 0.6460 0.6294 0.3238 0.0720  -0.1139 -0.1033 503 PHE   A CZ  
2438 N  N   . LEU   A 348 ? 0.4403 0.4309 0.2311 0.0385  -0.0980 -0.1115 504 LEU   A N   
2439 C  CA  . LEU   A 348 ? 0.4265 0.4140 0.2246 0.0378  -0.0938 -0.0998 504 LEU   A CA  
2440 C  C   . LEU   A 348 ? 0.4268 0.4070 0.2298 0.0337  -0.0818 -0.0945 504 LEU   A C   
2441 O  O   . LEU   A 348 ? 0.5356 0.5110 0.3327 0.0342  -0.0755 -0.0843 504 LEU   A O   
2442 C  CB  . LEU   A 348 ? 0.4109 0.4056 0.2313 0.0345  -0.0998 -0.1017 504 LEU   A CB  
2443 C  CG  . LEU   A 348 ? 0.5162 0.5078 0.3439 0.0344  -0.0963 -0.0902 504 LEU   A CG  
2444 C  CD1 . LEU   A 348 ? 0.4127 0.3999 0.2191 0.0420  -0.0974 -0.0813 504 LEU   A CD1 
2445 C  CD2 . LEU   A 348 ? 0.3834 0.3836 0.2331 0.0313  -0.1019 -0.0931 504 LEU   A CD2 
2446 N  N   . THR   A 349 ? 0.4100 0.3893 0.2230 0.0299  -0.0787 -0.1018 505 THR   A N   
2447 C  CA  . THR   A 349 ? 0.4134 0.3882 0.2306 0.0278  -0.0683 -0.0986 505 THR   A CA  
2448 C  C   . THR   A 349 ? 0.4541 0.4273 0.2520 0.0307  -0.0612 -0.0941 505 THR   A C   
2449 O  O   . THR   A 349 ? 0.4287 0.4004 0.2271 0.0291  -0.0533 -0.0860 505 THR   A O   
2450 C  CB  . THR   A 349 ? 0.4695 0.4418 0.2950 0.0258  -0.0674 -0.1086 505 THR   A CB  
2451 O  OG1 . THR   A 349 ? 0.4959 0.4674 0.3396 0.0213  -0.0716 -0.1115 505 THR   A OG1 
2452 C  CG2 . THR   A 349 ? 0.4042 0.3737 0.2316 0.0262  -0.0574 -0.1065 505 THR   A CG2 
2453 N  N   . LYS   A 350 ? 0.5167 0.4904 0.2969 0.0343  -0.0634 -0.0999 506 LYS   A N   
2454 C  CA  . LYS   A 350 ? 0.5342 0.5062 0.2943 0.0366  -0.0558 -0.0965 506 LYS   A CA  
2455 C  C   . LYS   A 350 ? 0.4996 0.4673 0.2473 0.0373  -0.0538 -0.0848 506 LYS   A C   
2456 O  O   . LYS   A 350 ? 0.5496 0.5149 0.2914 0.0349  -0.0437 -0.0782 506 LYS   A O   
2457 C  CB  . LYS   A 350 ? 0.5142 0.4871 0.2565 0.0407  -0.0596 -0.1055 506 LYS   A CB  
2458 C  CG  . LYS   A 350 ? 0.7263 0.6968 0.4408 0.0442  -0.0542 -0.1023 506 LYS   A CG  
2459 C  CD  . LYS   A 350 ? 0.9572 0.9259 0.6662 0.0412  -0.0408 -0.0940 506 LYS   A CD  
2460 C  CE  . LYS   A 350 ? 0.8693 0.8434 0.5967 0.0379  -0.0327 -0.0974 506 LYS   A CE  
2461 N  NZ  . LYS   A 350 ? 0.7904 0.7654 0.5184 0.0335  -0.0214 -0.0886 506 LYS   A NZ  
2462 N  N   . GLN   A 351 ? 0.4605 0.4273 0.2041 0.0405  -0.0632 -0.0825 507 GLN   A N   
2463 C  CA  . GLN   A 351 ? 0.4888 0.4482 0.2175 0.0426  -0.0617 -0.0712 507 GLN   A CA  
2464 C  C   . GLN   A 351 ? 0.4508 0.4071 0.1935 0.0373  -0.0543 -0.0628 507 GLN   A C   
2465 O  O   . GLN   A 351 ? 0.4774 0.4259 0.2072 0.0355  -0.0458 -0.0543 507 GLN   A O   
2466 C  CB  . GLN   A 351 ? 0.4811 0.4417 0.2048 0.0489  -0.0744 -0.0714 507 GLN   A CB  
2467 C  CG  . GLN   A 351 ? 0.5819 0.5449 0.2858 0.0552  -0.0816 -0.0785 507 GLN   A CG  
2468 C  CD  . GLN   A 351 ? 0.5979 0.5525 0.2742 0.0568  -0.0730 -0.0749 507 GLN   A CD  
2469 O  OE1 . GLN   A 351 ? 0.7283 0.6719 0.3885 0.0572  -0.0664 -0.0641 507 GLN   A OE1 
2470 N  NE2 . GLN   A 351 ? 0.5867 0.5455 0.2569 0.0570  -0.0723 -0.0841 507 GLN   A NE2 
2471 N  N   . ILE   A 352 ? 0.4708 0.4324 0.2391 0.0340  -0.0567 -0.0653 508 ILE   A N   
2472 C  CA  . ILE   A 352 ? 0.4111 0.3705 0.1930 0.0292  -0.0506 -0.0581 508 ILE   A CA  
2473 C  C   . ILE   A 352 ? 0.4354 0.3957 0.2180 0.0247  -0.0386 -0.0573 508 ILE   A C   
2474 O  O   . ILE   A 352 ? 0.4069 0.3634 0.1872 0.0210  -0.0308 -0.0498 508 ILE   A O   
2475 C  CB  . ILE   A 352 ? 0.4089 0.3735 0.2164 0.0270  -0.0559 -0.0615 508 ILE   A CB  
2476 C  CG1 . ILE   A 352 ? 0.4793 0.4456 0.2883 0.0308  -0.0666 -0.0614 508 ILE   A CG1 
2477 C  CG2 . ILE   A 352 ? 0.3719 0.3354 0.1937 0.0221  -0.0487 -0.0555 508 ILE   A CG2 
2478 C  CD1 . ILE   A 352 ? 0.3731 0.3461 0.2062 0.0277  -0.0718 -0.0669 508 ILE   A CD1 
2479 N  N   . GLU   A 353 ? 0.4072 0.3733 0.1935 0.0249  -0.0369 -0.0659 509 GLU   A N   
2480 C  CA  . GLU   A 353 ? 0.4093 0.3797 0.1968 0.0220  -0.0259 -0.0667 509 GLU   A CA  
2481 C  C   . GLU   A 353 ? 0.4250 0.3918 0.1899 0.0208  -0.0179 -0.0616 509 GLU   A C   
2482 O  O   . GLU   A 353 ? 0.4228 0.3916 0.1889 0.0158  -0.0078 -0.0578 509 GLU   A O   
2483 C  CB  . GLU   A 353 ? 0.4053 0.3812 0.1978 0.0244  -0.0263 -0.0774 509 GLU   A CB  
2484 C  CG  . GLU   A 353 ? 0.3869 0.3644 0.2016 0.0240  -0.0296 -0.0816 509 GLU   A CG  
2485 C  CD  . GLU   A 353 ? 0.4964 0.4747 0.3121 0.0274  -0.0313 -0.0924 509 GLU   A CD  
2486 O  OE1 . GLU   A 353 ? 0.4759 0.4539 0.2761 0.0302  -0.0329 -0.0974 509 GLU   A OE1 
2487 O  OE2 . GLU   A 353 ? 0.4595 0.4373 0.2899 0.0277  -0.0310 -0.0959 509 GLU   A OE2 
2488 N  N   . TYR   A 354 ? 0.4761 0.4375 0.2194 0.0251  -0.0220 -0.0620 510 TYR   A N   
2489 C  CA  . TYR   A 354 ? 0.4691 0.4234 0.1871 0.0240  -0.0143 -0.0560 510 TYR   A CA  
2490 C  C   . TYR   A 354 ? 0.5229 0.4677 0.2380 0.0199  -0.0101 -0.0449 510 TYR   A C   
2491 O  O   . TYR   A 354 ? 0.5244 0.4668 0.2322 0.0138  0.0017  -0.0405 510 TYR   A O   
2492 C  CB  . TYR   A 354 ? 0.4932 0.4414 0.1871 0.0308  -0.0214 -0.0573 510 TYR   A CB  
2493 C  CG  . TYR   A 354 ? 0.6145 0.5506 0.2781 0.0305  -0.0142 -0.0492 510 TYR   A CG  
2494 C  CD1 . TYR   A 354 ? 0.5840 0.5213 0.2312 0.0285  -0.0042 -0.0515 510 TYR   A CD1 
2495 C  CD2 . TYR   A 354 ? 0.5325 0.4545 0.1826 0.0322  -0.0166 -0.0391 510 TYR   A CD2 
2496 C  CE1 . TYR   A 354 ? 0.7255 0.6497 0.3431 0.0272  0.0037  -0.0438 510 TYR   A CE1 
2497 C  CE2 . TYR   A 354 ? 0.7522 0.6590 0.3716 0.0319  -0.0091 -0.0310 510 TYR   A CE2 
2498 C  CZ  . TYR   A 354 ? 0.8518 0.7594 0.4546 0.0288  0.0013  -0.0332 510 TYR   A CZ  
2499 O  OH  . TYR   A 354 ? 0.9936 0.8844 0.5640 0.0274  0.0099  -0.0251 510 TYR   A OH  
2500 N  N   . GLU   A 355 ? 0.4697 0.4093 0.1905 0.0229  -0.0192 -0.0410 511 GLU   A N   
2501 C  CA  . GLU   A 355 ? 0.4645 0.3930 0.1816 0.0201  -0.0160 -0.0308 511 GLU   A CA  
2502 C  C   . GLU   A 355 ? 0.4842 0.4180 0.2188 0.0114  -0.0060 -0.0294 511 GLU   A C   
2503 O  O   . GLU   A 355 ? 0.5211 0.4469 0.2451 0.0055  0.0039  -0.0230 511 GLU   A O   
2504 C  CB  . GLU   A 355 ? 0.4561 0.3823 0.1820 0.0253  -0.0280 -0.0289 511 GLU   A CB  
2505 C  CG  . GLU   A 355 ? 0.4969 0.4189 0.2045 0.0346  -0.0385 -0.0298 511 GLU   A CG  
2506 C  CD  . GLU   A 355 ? 0.6157 0.5207 0.2900 0.0374  -0.0340 -0.0214 511 GLU   A CD  
2507 O  OE1 . GLU   A 355 ? 0.6475 0.5397 0.3154 0.0345  -0.0282 -0.0123 511 GLU   A OE1 
2508 O  OE2 . GLU   A 355 ? 0.7617 0.6647 0.4148 0.0423  -0.0361 -0.0238 511 GLU   A OE2 
2509 N  N   . ARG   A 356 ? 0.4601 0.4066 0.2206 0.0104  -0.0083 -0.0357 512 ARG   A N   
2510 C  CA  . ARG   A 356 ? 0.4053 0.3584 0.1834 0.0036  -0.0005 -0.0350 512 ARG   A CA  
2511 C  C   . ARG   A 356 ? 0.4404 0.4000 0.2119 -0.0018 0.0120  -0.0370 512 ARG   A C   
2512 O  O   . ARG   A 356 ? 0.5247 0.4848 0.2986 -0.0092 0.0211  -0.0334 512 ARG   A O   
2513 C  CB  . ARG   A 356 ? 0.4151 0.3789 0.2191 0.0051  -0.0059 -0.0413 512 ARG   A CB  
2514 C  CG  . ARG   A 356 ? 0.4463 0.4195 0.2669 -0.0002 0.0019  -0.0422 512 ARG   A CG  
2515 C  CD  . ARG   A 356 ? 0.4707 0.4506 0.3138 0.0021  -0.0035 -0.0469 512 ARG   A CD  
2516 N  NE  . ARG   A 356 ? 0.4124 0.3960 0.2570 0.0075  -0.0080 -0.0552 512 ARG   A NE  
2517 C  CZ  . ARG   A 356 ? 0.3818 0.3672 0.2416 0.0102  -0.0131 -0.0598 512 ARG   A CZ  
2518 N  NH1 . ARG   A 356 ? 0.3401 0.3252 0.2151 0.0085  -0.0144 -0.0568 512 ARG   A NH1 
2519 N  NH2 . ARG   A 356 ? 0.3385 0.3244 0.1968 0.0146  -0.0164 -0.0676 512 ARG   A NH2 
2520 N  N   . ASN   A 357 ? 0.4364 0.4017 0.1997 0.0014  0.0128  -0.0436 513 ASN   A N   
2521 C  CA  . ASN   A 357 ? 0.5252 0.4991 0.2826 -0.0034 0.0251  -0.0466 513 ASN   A CA  
2522 C  C   . ASN   A 357 ? 0.6334 0.5953 0.3667 -0.0096 0.0346  -0.0388 513 ASN   A C   
2523 O  O   . ASN   A 357 ? 0.5728 0.5421 0.3049 -0.0171 0.0471  -0.0399 513 ASN   A O   
2524 C  CB  . ASN   A 357 ? 0.4449 0.4262 0.1968 0.0024  0.0235  -0.0556 513 ASN   A CB  
2525 C  CG  . ASN   A 357 ? 0.4320 0.4262 0.2074 0.0064  0.0193  -0.0644 513 ASN   A CG  
2526 O  OD1 . ASN   A 357 ? 0.4310 0.4346 0.2252 0.0035  0.0229  -0.0654 513 ASN   A OD1 
2527 N  ND2 . ASN   A 357 ? 0.4231 0.4166 0.1961 0.0132  0.0117  -0.0711 513 ASN   A ND2 
2528 N  N   . ASN   A 358 ? 0.6370 0.5805 0.3507 -0.0065 0.0294  -0.0313 514 ASN   A N   
2529 C  CA  . ASN   A 358 ? 0.6433 0.5700 0.3288 -0.0109 0.0379  -0.0231 514 ASN   A CA  
2530 C  C   . ASN   A 358 ? 0.6145 0.5252 0.2977 -0.0140 0.0377  -0.0135 514 ASN   A C   
2531 O  O   . ASN   A 358 ? 0.6555 0.5455 0.3116 -0.0141 0.0405  -0.0053 514 ASN   A O   
2532 C  CB  . ASN   A 358 ? 0.5284 0.4439 0.1859 -0.0029 0.0326  -0.0220 514 ASN   A CB  
2533 C  CG  . ASN   A 358 ? 0.5348 0.4628 0.1877 -0.0015 0.0364  -0.0307 514 ASN   A CG  
2534 O  OD1 . ASN   A 358 ? 0.6190 0.5467 0.2568 -0.0076 0.0491  -0.0304 514 ASN   A OD1 
2535 N  ND2 . ASN   A 358 ? 0.6437 0.5822 0.3089 0.0060  0.0259  -0.0390 514 ASN   A ND2 
2536 N  N   . GLU   A 359 ? 0.6277 0.5464 0.3375 -0.0158 0.0344  -0.0145 515 GLU   A N   
2537 C  CA  . GLU   A 359 ? 0.6710 0.5763 0.3818 -0.0189 0.0343  -0.0066 515 GLU   A CA  
2538 C  C   . GLU   A 359 ? 0.5849 0.4718 0.2786 -0.0096 0.0239  -0.0001 515 GLU   A C   
2539 O  O   . GLU   A 359 ? 0.7002 0.5668 0.3758 -0.0109 0.0270  0.0085  515 GLU   A O   
2540 C  CB  . GLU   A 359 ? 0.9321 0.8286 0.6308 -0.0309 0.0494  -0.0019 515 GLU   A CB  
2541 C  CG  . GLU   A 359 ? 0.9400 0.8578 0.6628 -0.0404 0.0582  -0.0086 515 GLU   A CG  
2542 C  CD  . GLU   A 359 ? 1.1043 1.0179 0.8138 -0.0536 0.0747  -0.0067 515 GLU   A CD  
2543 O  OE1 . GLU   A 359 ? 1.1539 1.0450 0.8332 -0.0556 0.0801  0.0005  515 GLU   A OE1 
2544 O  OE2 . GLU   A 359 ? 1.1862 1.1191 0.9151 -0.0620 0.0824  -0.0128 515 GLU   A OE2 
2545 N  N   . PHE   A 360 ? 0.5730 0.4672 0.2722 0.0001  0.0115  -0.0049 516 PHE   A N   
2546 C  CA  . PHE   A 360 ? 0.5715 0.4563 0.2632 0.0102  -0.0010 -0.0016 516 PHE   A CA  
2547 C  C   . PHE   A 360 ? 0.6395 0.5015 0.2953 0.0144  0.0005  0.0069  516 PHE   A C   
2548 O  O   . PHE   A 360 ? 0.6969 0.5424 0.3436 0.0162  -0.0002 0.0147  516 PHE   A O   
2549 C  CB  . PHE   A 360 ? 0.5132 0.3983 0.2256 0.0097  -0.0054 0.0009  516 PHE   A CB  
2550 C  CG  . PHE   A 360 ? 0.5209 0.4256 0.2657 0.0062  -0.0068 -0.0065 516 PHE   A CG  
2551 C  CD1 . PHE   A 360 ? 0.4228 0.3397 0.1825 0.0119  -0.0173 -0.0137 516 PHE   A CD1 
2552 C  CD2 . PHE   A 360 ? 0.5128 0.4232 0.2717 -0.0030 0.0025  -0.0067 516 PHE   A CD2 
2553 C  CE1 . PHE   A 360 ? 0.4167 0.3478 0.2028 0.0090  -0.0180 -0.0198 516 PHE   A CE1 
2554 C  CE2 . PHE   A 360 ? 0.4983 0.4252 0.2843 -0.0046 0.0008  -0.0132 516 PHE   A CE2 
2555 C  CZ  . PHE   A 360 ? 0.4210 0.3566 0.2195 0.0016  -0.0092 -0.0192 516 PHE   A CZ  
2556 N  N   . PRO   A 361 ? 0.6908 0.5498 0.3239 0.0170  0.0026  0.0056  517 PRO   A N   
2557 C  CA  . PRO   A 361 ? 0.7644 0.5994 0.3598 0.0226  0.0033  0.0141  517 PRO   A CA  
2558 C  C   . PRO   A 361 ? 0.7111 0.5400 0.2993 0.0365  -0.0121 0.0162  517 PRO   A C   
2559 O  O   . PRO   A 361 ? 0.7572 0.5633 0.3157 0.0427  -0.0125 0.0248  517 PRO   A O   
2560 C  CB  . PRO   A 361 ? 0.7161 0.5543 0.2929 0.0225  0.0082  0.0101  517 PRO   A CB  
2561 C  CG  . PRO   A 361 ? 0.6617 0.5262 0.2672 0.0224  0.0029  -0.0018 517 PRO   A CG  
2562 C  CD  . PRO   A 361 ? 0.6433 0.5190 0.2820 0.0153  0.0050  -0.0035 517 PRO   A CD  
2563 N  N   . VAL   A 362 ? 0.7089 0.5573 0.3227 0.0418  -0.0246 0.0083  518 VAL   A N   
2564 C  CA  . VAL   A 362 ? 0.8645 0.7118 0.4745 0.0548  -0.0394 0.0086  518 VAL   A CA  
2565 C  C   . VAL   A 362 ? 0.7334 0.5688 0.3469 0.0566  -0.0407 0.0161  518 VAL   A C   
2566 O  O   . VAL   A 362 ? 0.8441 0.6737 0.4477 0.0685  -0.0513 0.0185  518 VAL   A O   
2567 C  CB  . VAL   A 362 ? 0.7282 0.6005 0.3657 0.0577  -0.0511 -0.0031 518 VAL   A CB  
2568 C  CG1 . VAL   A 362 ? 0.7323 0.6158 0.4042 0.0526  -0.0525 -0.0053 518 VAL   A CG1 
2569 C  CG2 . VAL   A 362 ? 0.8142 0.6889 0.4396 0.0714  -0.0660 -0.0057 518 VAL   A CG2 
2570 N  N   . PHE   A 363 ? 0.6937 0.5262 0.3211 0.0457  -0.0304 0.0191  519 PHE   A N   
2571 C  CA  . PHE   A 363 ? 0.6847 0.5042 0.3139 0.0470  -0.0307 0.0260  519 PHE   A CA  
2572 C  C   . PHE   A 363 ? 1.0109 0.7996 0.6012 0.0522  -0.0268 0.0368  519 PHE   A C   
2573 O  O   . PHE   A 363 ? 1.1027 0.8789 0.6851 0.0616  -0.0334 0.0419  519 PHE   A O   
2574 C  CB  . PHE   A 363 ? 0.6332 0.4571 0.2851 0.0335  -0.0203 0.0260  519 PHE   A CB  
2575 C  CG  . PHE   A 363 ? 0.6222 0.4701 0.3115 0.0317  -0.0265 0.0181  519 PHE   A CG  
2576 C  CD1 . PHE   A 363 ? 0.5837 0.4442 0.2850 0.0412  -0.0403 0.0129  519 PHE   A CD1 
2577 C  CD2 . PHE   A 363 ? 0.5735 0.4311 0.2852 0.0204  -0.0184 0.0156  519 PHE   A CD2 
2578 C  CE1 . PHE   A 363 ? 0.4869 0.3669 0.2206 0.0384  -0.0447 0.0060  519 PHE   A CE1 
2579 C  CE2 . PHE   A 363 ? 0.5068 0.3833 0.2496 0.0194  -0.0238 0.0091  519 PHE   A CE2 
2580 C  CZ  . PHE   A 363 ? 0.4769 0.3633 0.2301 0.0278  -0.0364 0.0046  519 PHE   A CZ  
2581 N  N   . ASP   A 364 ? 0.8985 0.6738 0.4632 0.0466  -0.0158 0.0403  520 ASP   A N   
2582 C  CA  . ASP   A 364 ? 0.9551 0.6973 0.4780 0.0505  -0.0103 0.0509  520 ASP   A CA  
2583 C  C   . ASP   A 364 ? 0.9565 0.6900 0.4582 0.0696  -0.0249 0.0534  520 ASP   A C   
2584 O  O   . ASP   A 364 ? 1.1806 0.9063 0.6602 0.0751  -0.0249 0.0553  520 ASP   A O   
2585 C  CB  . ASP   A 364 ? 0.7806 0.5150 0.2802 0.0421  0.0027  0.0521  520 ASP   A CB  
2586 C  CG  . ASP   A 364 ? 0.9955 0.7412 0.5158 0.0238  0.0173  0.0487  520 ASP   A CG  
2587 O  OD1 . ASP   A 364 ? 1.0587 0.8104 0.6043 0.0174  0.0189  0.0479  520 ASP   A OD1 
2588 O  OD2 . ASP   A 364 ? 1.0473 0.7972 0.5589 0.0164  0.0270  0.0461  520 ASP   A OD2 
2589 N  N   . GLY   B 5   ? 1.1743 1.1175 0.9418 0.1332  -0.0583 -0.0181 161 GLY   B N   
2590 C  CA  . GLY   B 5   ? 0.9372 0.8487 0.6832 0.1318  -0.0489 -0.0077 161 GLY   B CA  
2591 C  C   . GLY   B 5   ? 1.0681 0.9614 0.8240 0.1189  -0.0380 -0.0002 161 GLY   B C   
2592 O  O   . GLY   B 5   ? 0.9487 0.8192 0.6924 0.1138  -0.0285 0.0072  161 GLY   B O   
2593 N  N   . ALA   B 6   ? 0.8867 0.7912 0.6649 0.1135  -0.0393 -0.0026 162 ALA   B N   
2594 C  CA  . ALA   B 6   ? 0.7954 0.6848 0.5837 0.1020  -0.0301 0.0036  162 ALA   B CA  
2595 C  C   . ALA   B 6   ? 0.8736 0.7307 0.6380 0.1080  -0.0247 0.0138  162 ALA   B C   
2596 O  O   . ALA   B 6   ? 0.8163 0.6563 0.5829 0.0977  -0.0149 0.0196  162 ALA   B O   
2597 C  CB  . ALA   B 6   ? 0.7139 0.6209 0.5269 0.0975  -0.0336 -0.0011 162 ALA   B CB  
2598 N  N   . SER   B 7   ? 0.7472 0.5954 0.4882 0.1247  -0.0307 0.0156  163 SER   B N   
2599 C  CA  . SER   B 7   ? 0.8250 0.6382 0.5389 0.1310  -0.0251 0.0256  163 SER   B CA  
2600 C  C   . SER   B 7   ? 0.8046 0.5953 0.5014 0.1242  -0.0144 0.0322  163 SER   B C   
2601 O  O   . SER   B 7   ? 0.7768 0.5404 0.4631 0.1183  -0.0045 0.0399  163 SER   B O   
2602 C  CB  . SER   B 7   ? 0.9402 0.7479 0.6295 0.1524  -0.0345 0.0259  163 SER   B CB  
2603 O  OG  . SER   B 7   ? 1.0150 0.8337 0.6920 0.1611  -0.0405 0.0222  163 SER   B OG  
2604 N  N   . LYS   B 8   ? 0.8012 0.6037 0.4958 0.1239  -0.0157 0.0285  164 LYS   B N   
2605 C  CA  . LYS   B 8   ? 0.6874 0.4716 0.3679 0.1165  -0.0048 0.0338  164 LYS   B CA  
2606 C  C   . LYS   B 8   ? 0.6798 0.4663 0.3846 0.0975  0.0053  0.0341  164 LYS   B C   
2607 O  O   . LYS   B 8   ? 0.7137 0.4786 0.4085 0.0898  0.0168  0.0405  164 LYS   B O   
2608 C  CB  . LYS   B 8   ? 0.7836 0.5814 0.4567 0.1209  -0.0090 0.0288  164 LYS   B CB  
2609 C  CG  . LYS   B 8   ? 0.9156 0.7033 0.5840 0.1099  0.0026  0.0316  164 LYS   B CG  
2610 C  CD  . LYS   B 8   ? 0.8295 0.6263 0.4851 0.1158  -0.0012 0.0272  164 LYS   B CD  
2611 C  CE  . LYS   B 8   ? 0.8321 0.6035 0.4617 0.1136  0.0104  0.0344  164 LYS   B CE  
2612 N  NZ  . LYS   B 8   ? 1.0013 0.7790 0.6504 0.0972  0.0206  0.0325  164 LYS   B NZ  
2613 N  N   . LEU   B 9   ? 0.6925 0.5050 0.4285 0.0898  0.0013  0.0270  165 LEU   B N   
2614 C  CA  . LEU   B 9   ? 0.6746 0.4901 0.4336 0.0738  0.0094  0.0270  165 LEU   B CA  
2615 C  C   . LEU   B 9   ? 0.6699 0.4647 0.4259 0.0698  0.0161  0.0335  165 LEU   B C   
2616 O  O   . LEU   B 9   ? 0.5223 0.3057 0.2802 0.0589  0.0267  0.0370  165 LEU   B O   
2617 C  CB  . LEU   B 9   ? 0.5272 0.3709 0.3163 0.0685  0.0030  0.0189  165 LEU   B CB  
2618 C  CG  . LEU   B 9   ? 0.5428 0.4080 0.3400 0.0682  -0.0022 0.0109  165 LEU   B CG  
2619 C  CD1 . LEU   B 9   ? 0.4539 0.3411 0.2796 0.0606  -0.0060 0.0043  165 LEU   B CD1 
2620 C  CD2 . LEU   B 9   ? 0.4434 0.3026 0.2356 0.0619  0.0059  0.0118  165 LEU   B CD2 
2621 N  N   . ARG   B 10  ? 0.6856 0.4762 0.4372 0.0784  0.0099  0.0344  166 ARG   B N   
2622 C  CA  . ARG   B 10  ? 0.6780 0.4479 0.4260 0.0748  0.0156  0.0398  166 ARG   B CA  
2623 C  C   . ARG   B 10  ? 0.6635 0.3997 0.3806 0.0762  0.0249  0.0481  166 ARG   B C   
2624 O  O   . ARG   B 10  ? 0.7812 0.4996 0.4974 0.0664  0.0345  0.0522  166 ARG   B O   
2625 C  CB  . ARG   B 10  ? 0.7184 0.4914 0.4675 0.0849  0.0067  0.0382  166 ARG   B CB  
2626 C  CG  . ARG   B 10  ? 0.8034 0.6043 0.5840 0.0794  0.0011  0.0312  166 ARG   B CG  
2627 C  CD  . ARG   B 10  ? 0.9609 0.7583 0.7590 0.0648  0.0086  0.0324  166 ARG   B CD  
2628 N  NE  . ARG   B 10  ? 0.9899 0.7578 0.7712 0.0605  0.0185  0.0393  166 ARG   B NE  
2629 C  CZ  . ARG   B 10  ? 1.0562 0.8201 0.8496 0.0466  0.0270  0.0403  166 ARG   B CZ  
2630 N  NH1 . ARG   B 10  ? 0.9103 0.6962 0.7313 0.0371  0.0264  0.0355  166 ARG   B NH1 
2631 N  NH2 . ARG   B 10  ? 0.9301 0.6670 0.7069 0.0420  0.0365  0.0458  166 ARG   B NH2 
2632 N  N   . ALA   B 11  ? 0.6169 0.3438 0.3078 0.0879  0.0225  0.0504  167 ALA   B N   
2633 C  CA  . ALA   B 11  ? 0.7644 0.4580 0.4232 0.0887  0.0325  0.0587  167 ALA   B CA  
2634 C  C   . ALA   B 11  ? 0.7437 0.4365 0.4107 0.0722  0.0451  0.0594  167 ALA   B C   
2635 O  O   . ALA   B 11  ? 0.7600 0.4285 0.4153 0.0636  0.0571  0.0650  167 ALA   B O   
2636 C  CB  . ALA   B 11  ? 0.6618 0.3489 0.2911 0.1054  0.0263  0.0603  167 ALA   B CB  
2637 N  N   . VAL   B 12  ? 0.7520 0.4715 0.4387 0.0678  0.0427  0.0532  168 VAL   B N   
2638 C  CA  . VAL   B 12  ? 0.7133 0.4369 0.4113 0.0535  0.0537  0.0524  168 VAL   B CA  
2639 C  C   . VAL   B 12  ? 0.6151 0.3393 0.3349 0.0394  0.0605  0.0522  168 VAL   B C   
2640 O  O   . VAL   B 12  ? 0.6162 0.3281 0.3331 0.0284  0.0730  0.0550  168 VAL   B O   
2641 C  CB  . VAL   B 12  ? 0.5648 0.3174 0.2816 0.0527  0.0483  0.0448  168 VAL   B CB  
2642 C  CG1 . VAL   B 12  ? 0.5362 0.2968 0.2706 0.0384  0.0584  0.0427  168 VAL   B CG1 
2643 C  CG2 . VAL   B 12  ? 0.6215 0.3719 0.3142 0.0646  0.0436  0.0446  168 VAL   B CG2 
2644 N  N   . LEU   B 13  ? 0.5055 0.2450 0.2474 0.0394  0.0526  0.0484  169 LEU   B N   
2645 C  CA  . LEU   B 13  ? 0.6453 0.3871 0.4081 0.0270  0.0578  0.0474  169 LEU   B CA  
2646 C  C   . LEU   B 13  ? 0.7069 0.4184 0.4507 0.0240  0.0661  0.0537  169 LEU   B C   
2647 O  O   . LEU   B 13  ? 0.8078 0.5145 0.5599 0.0106  0.0762  0.0540  169 LEU   B O   
2648 C  CB  . LEU   B 13  ? 0.5511 0.3136 0.3377 0.0289  0.0474  0.0424  169 LEU   B CB  
2649 C  CG  . LEU   B 13  ? 0.6043 0.3954 0.4125 0.0281  0.0414  0.0358  169 LEU   B CG  
2650 C  CD1 . LEU   B 13  ? 0.5934 0.4014 0.4169 0.0328  0.0305  0.0315  169 LEU   B CD1 
2651 C  CD2 . LEU   B 13  ? 0.5861 0.3880 0.4150 0.0152  0.0486  0.0332  169 LEU   B CD2 
2652 N  N   . GLU   B 14  ? 0.6436 0.3345 0.3617 0.0364  0.0619  0.0582  170 GLU   B N   
2653 C  CA  . GLU   B 14  ? 0.7029 0.3594 0.3976 0.0347  0.0700  0.0646  170 GLU   B CA  
2654 C  C   . GLU   B 14  ? 0.8029 0.4400 0.4806 0.0249  0.0847  0.0690  170 GLU   B C   
2655 O  O   . GLU   B 14  ? 0.8828 0.5099 0.5647 0.0117  0.0949  0.0690  170 GLU   B O   
2656 C  CB  . GLU   B 14  ? 0.8779 0.5148 0.5439 0.0529  0.0623  0.0688  170 GLU   B CB  
2657 N  N   . LYS   B 15  ? 0.7585 0.3959 0.4208 0.0308  0.0853  0.0705  171 LYS   B N   
2658 C  CA  . LYS   B 15  ? 0.8424 0.4650 0.4900 0.0217  0.0992  0.0734  171 LYS   B CA  
2659 C  C   . LYS   B 15  ? 0.8365 0.4765 0.5116 0.0036  0.1089  0.0693  171 LYS   B C   
2660 O  O   . LYS   B 15  ? 0.9000 0.5312 0.5741 -0.0088 0.1211  0.0692  171 LYS   B O   
2661 C  CB  . LYS   B 15  ? 0.7337 0.3554 0.3599 0.0323  0.0971  0.0753  171 LYS   B CB  
2662 N  N   . LEU   B 16  ? 0.8361 0.5106 0.5440 0.0025  0.1009  0.0619  172 LEU   B N   
2663 C  CA  . LEU   B 16  ? 0.7120 0.4075 0.4492 -0.0123 0.1077  0.0564  172 LEU   B CA  
2664 C  C   . LEU   B 16  ? 0.8979 0.5879 0.6474 -0.0240 0.1132  0.0557  172 LEU   B C   
2665 O  O   . LEU   B 16  ? 0.9456 0.6419 0.7084 -0.0381 0.1237  0.0529  172 LEU   B O   
2666 C  CB  . LEU   B 16  ? 0.6910 0.4205 0.4570 -0.0091 0.0971  0.0493  172 LEU   B CB  
2667 C  CG  . LEU   B 16  ? 0.6553 0.3947 0.4148 -0.0018 0.0942  0.0477  172 LEU   B CG  
2668 C  CD1 . LEU   B 16  ? 0.5176 0.2872 0.3050 -0.0001 0.0844  0.0404  172 LEU   B CD1 
2669 C  CD2 . LEU   B 16  ? 0.6811 0.4152 0.4321 -0.0099 0.1078  0.0485  172 LEU   B CD2 
2670 N  N   . LYS   B 17  ? 0.8930 0.5731 0.6393 -0.0184 0.1059  0.0573  173 LYS   B N   
2671 C  CA  . LYS   B 17  ? 0.8399 0.5122 0.5951 -0.0294 0.1111  0.0563  173 LYS   B CA  
2672 C  C   . LYS   B 17  ? 0.9358 0.5869 0.6738 -0.0373 0.1227  0.0580  173 LYS   B C   
2673 O  O   . LYS   B 17  ? 0.8147 0.4736 0.5681 -0.0520 0.1316  0.0538  173 LYS   B O   
2674 C  CB  . LYS   B 17  ? 0.7789 0.4458 0.5333 -0.0201 0.1001  0.0568  173 LYS   B CB  
2675 C  CG  . LYS   B 17  ? 0.9035 0.5799 0.6820 -0.0308 0.1004  0.0520  173 LYS   B CG  
2676 C  CD  . LYS   B 17  ? 0.9569 0.6298 0.7352 -0.0212 0.0896  0.0520  173 LYS   B CD  
2677 C  CE  . LYS   B 17  ? 0.8771 0.5713 0.6631 -0.0072 0.0760  0.0502  173 LYS   B CE  
2678 N  NZ  . LYS   B 17  ? 0.8983 0.5970 0.6918 -0.0003 0.0661  0.0481  173 LYS   B NZ  
2679 N  N   . LEU   B 18  ? 0.9507 0.5782 0.6585 -0.0270 0.1218  0.0630  174 LEU   B N   
2680 C  CA  . LEU   B 18  ? 1.0899 0.6945 0.7784 -0.0322 0.1313  0.0644  174 LEU   B CA  
2681 C  C   . LEU   B 18  ? 1.1363 0.7461 0.8312 -0.0477 0.1451  0.0618  174 LEU   B C   
2682 O  O   . LEU   B 18  ? 1.1559 0.7637 0.8588 -0.0608 0.1529  0.0583  174 LEU   B O   
2683 C  CB  . LEU   B 18  ? 1.0554 0.6360 0.7091 -0.0169 0.1282  0.0701  174 LEU   B CB  
2684 C  CG  . LEU   B 18  ? 1.1244 0.6866 0.7610 -0.0038 0.1199  0.0725  174 LEU   B CG  
2685 C  CD1 . LEU   B 18  ? 1.1192 0.6977 0.7773 -0.0003 0.1092  0.0697  174 LEU   B CD1 
2686 C  CD2 . LEU   B 18  ? 1.2342 0.7837 0.8424 0.0143  0.1138  0.0769  174 LEU   B CD2 
2687 N  N   . ASP   B 22  ? 1.1141 0.7639 0.8870 -0.1299 0.1909  0.0316  178 ASP   B N   
2688 C  CA  . ASP   B 22  ? 1.1699 0.8330 0.9512 -0.1420 0.2028  0.0270  178 ASP   B CA  
2689 C  C   . ASP   B 22  ? 1.1155 0.8186 0.9351 -0.1499 0.2017  0.0182  178 ASP   B C   
2690 O  O   . ASP   B 22  ? 1.0143 0.7332 0.8477 -0.1626 0.2110  0.0115  178 ASP   B O   
2691 C  CB  . ASP   B 22  ? 1.0694 0.7241 0.8313 -0.1346 0.2062  0.0326  178 ASP   B CB  
2692 N  N   . ILE   B 23  ? 1.1134 0.8328 0.9496 -0.1418 0.1903  0.0181  179 ILE   B N   
2693 C  CA  . ILE   B 23  ? 0.9696 0.7262 0.8410 -0.1466 0.1876  0.0102  179 ILE   B CA  
2694 C  C   . ILE   B 23  ? 1.0370 0.8039 0.9274 -0.1531 0.1831  0.0041  179 ILE   B C   
2695 O  O   . ILE   B 23  ? 1.2281 1.0172 1.1401 -0.1646 0.1877  -0.0047 179 ILE   B O   
2696 C  CB  . ILE   B 23  ? 0.9786 0.7473 0.8571 -0.1346 0.1785  0.0132  179 ILE   B CB  
2697 N  N   . THR   B 25  ? 0.9827 0.7320 0.8616 -0.1859 0.2099  -0.0065 181 THR   B N   
2698 C  CA  . THR   B 25  ? 0.8900 0.6365 0.7645 -0.1999 0.2239  -0.0110 181 THR   B CA  
2699 C  C   . THR   B 25  ? 1.1953 0.9705 1.0872 -0.2034 0.2295  -0.0158 181 THR   B C   
2700 O  O   . THR   B 25  ? 1.2674 1.0672 1.1806 -0.2155 0.2356  -0.0256 181 THR   B O   
2701 C  CB  . THR   B 25  ? 1.2914 0.9958 1.1270 -0.1984 0.2315  -0.0028 181 THR   B CB  
2702 O  OG1 . THR   B 25  ? 1.2826 0.9612 1.1027 -0.1963 0.2277  0.0001  181 THR   B OG1 
2703 C  CG2 . THR   B 25  ? 1.1762 0.8777 1.0064 -0.2132 0.2470  -0.0073 181 THR   B CG2 
2704 N  N   . ALA   B 26  ? 1.2046 0.9769 1.0870 -0.1924 0.2274  -0.0093 182 ALA   B N   
2705 C  CA  . ALA   B 26  ? 1.1424 0.9414 1.0401 -0.1937 0.2321  -0.0134 182 ALA   B CA  
2706 C  C   . ALA   B 26  ? 0.8541 0.6956 0.7910 -0.1974 0.2274  -0.0240 182 ALA   B C   
2707 O  O   . ALA   B 26  ? 0.9134 0.7801 0.8684 -0.2065 0.2347  -0.0326 182 ALA   B O   
2708 C  CB  . ALA   B 26  ? 0.9677 0.7590 0.8516 -0.1793 0.2274  -0.0051 182 ALA   B CB  
2709 N  N   . ALA   B 27  ? 0.7670 0.6170 0.7167 -0.1899 0.2150  -0.0238 183 ALA   B N   
2710 C  CA  . ALA   B 27  ? 0.9018 0.7909 0.8873 -0.1915 0.2091  -0.0335 183 ALA   B CA  
2711 C  C   . ALA   B 27  ? 0.7727 0.6790 0.7747 -0.2059 0.2153  -0.0442 183 ALA   B C   
2712 O  O   . ALA   B 27  ? 0.8747 0.8171 0.9043 -0.2092 0.2157  -0.0539 183 ALA   B O   
2713 C  CB  . ALA   B 27  ? 0.7558 0.6447 0.7480 -0.1830 0.1955  -0.0312 183 ALA   B CB  
2714 N  N   . GLY   B 28  ? 0.9553 0.8363 0.9402 -0.2142 0.2202  -0.0429 184 GLY   B N   
2715 C  CA  . GLY   B 28  ? 0.8183 0.7111 0.8148 -0.2293 0.2276  -0.0529 184 GLY   B CA  
2716 C  C   . GLY   B 28  ? 0.9011 0.8183 0.9105 -0.2366 0.2375  -0.0602 184 GLY   B C   
2717 O  O   . GLY   B 28  ? 0.9242 0.8787 0.9634 -0.2408 0.2361  -0.0712 184 GLY   B O   
2718 N  N   . MET   B 29  ? 0.9530 0.8494 0.9394 -0.2367 0.2468  -0.0538 185 MET   B N   
2719 C  CA  . MET   B 29  ? 0.9587 0.8755 0.9541 -0.2423 0.2567  -0.0594 185 MET   B CA  
2720 C  C   . MET   B 29  ? 0.8620 0.8208 0.8887 -0.2346 0.2496  -0.0658 185 MET   B C   
2721 O  O   . MET   B 29  ? 0.7335 0.7266 0.7857 -0.2412 0.2525  -0.0773 185 MET   B O   
2722 C  CB  . MET   B 29  ? 1.1162 1.0016 1.0793 -0.2387 0.2645  -0.0492 185 MET   B CB  
2723 C  CG  . MET   B 29  ? 1.1456 0.9850 1.0746 -0.2397 0.2666  -0.0402 185 MET   B CG  
2724 S  SD  . MET   B 29  ? 1.3696 1.1720 1.2592 -0.2381 0.2778  -0.0301 185 MET   B SD  
2725 C  CE  . MET   B 29  ? 1.0282 0.8624 0.9360 -0.2483 0.2899  -0.0394 185 MET   B CE  
2726 N  N   . VAL   B 30  ? 0.8715 0.8283 0.8966 -0.2200 0.2396  -0.0591 186 VAL   B N   
2727 C  CA  . VAL   B 30  ? 0.7092 0.7027 0.7621 -0.2111 0.2320  -0.0646 186 VAL   B CA  
2728 C  C   . VAL   B 30  ? 0.6964 0.7235 0.7807 -0.2156 0.2263  -0.0765 186 VAL   B C   
2729 O  O   . VAL   B 30  ? 0.6067 0.6693 0.7152 -0.2173 0.2281  -0.0867 186 VAL   B O   
2730 C  CB  . VAL   B 30  ? 0.7400 0.7218 0.7853 -0.1962 0.2213  -0.0556 186 VAL   B CB  
2731 C  CG1 . VAL   B 30  ? 0.6987 0.7172 0.7728 -0.1870 0.2133  -0.0619 186 VAL   B CG1 
2732 C  CG2 . VAL   B 30  ? 0.7813 0.7334 0.7961 -0.1906 0.2265  -0.0449 186 VAL   B CG2 
2733 N  N   . LYS   B 31  ? 0.5986 0.6150 0.6819 -0.2171 0.2193  -0.0757 187 LYS   B N   
2734 C  CA  . LYS   B 31  ? 0.7359 0.7825 0.8470 -0.2205 0.2127  -0.0867 187 LYS   B CA  
2735 C  C   . LYS   B 31  ? 0.7423 0.8111 0.8671 -0.2336 0.2223  -0.0982 187 LYS   B C   
2736 O  O   . LYS   B 31  ? 0.7241 0.8322 0.8774 -0.2323 0.2186  -0.1091 187 LYS   B O   
2737 C  CB  . LYS   B 31  ? 0.6278 0.6531 0.7298 -0.2228 0.2066  -0.0837 187 LYS   B CB  
2738 N  N   . GLY   B 32  ? 0.7081 0.7521 0.8122 -0.2456 0.2349  -0.0961 188 GLY   B N   
2739 C  CA  . GLY   B 32  ? 0.5386 0.6015 0.6544 -0.2599 0.2453  -0.1073 188 GLY   B CA  
2740 C  C   . GLY   B 32  ? 0.7047 0.8047 0.8421 -0.2567 0.2475  -0.1150 188 GLY   B C   
2741 O  O   . GLY   B 32  ? 0.6979 0.8335 0.8611 -0.2618 0.2475  -0.1279 188 GLY   B O   
2742 N  N   . VAL   B 33  ? 0.7378 0.8310 0.8651 -0.2472 0.2490  -0.1075 189 VAL   B N   
2743 C  CA  . VAL   B 33  ? 0.7022 0.8303 0.8495 -0.2419 0.2504  -0.1144 189 VAL   B CA  
2744 C  C   . VAL   B 33  ? 0.5384 0.7019 0.7149 -0.2299 0.2362  -0.1211 189 VAL   B C   
2745 O  O   . VAL   B 33  ? 0.6700 0.8720 0.8729 -0.2306 0.2350  -0.1334 189 VAL   B O   
2746 C  CB  . VAL   B 33  ? 0.6708 0.7811 0.7983 -0.2339 0.2551  -0.1045 189 VAL   B CB  
2747 C  CG1 . VAL   B 33  ? 0.7479 0.8950 0.8966 -0.2264 0.2556  -0.1118 189 VAL   B CG1 
2748 C  CG2 . VAL   B 33  ? 0.8268 0.9030 0.9247 -0.2452 0.2692  -0.0984 189 VAL   B CG2 
2749 N  N   . VAL   B 34  ? 0.5942 0.7449 0.7656 -0.2186 0.2250  -0.1133 190 VAL   B N   
2750 C  CA  . VAL   B 34  ? 0.6017 0.7822 0.7972 -0.2049 0.2115  -0.1180 190 VAL   B CA  
2751 C  C   . VAL   B 34  ? 0.6071 0.8207 0.8290 -0.2092 0.2063  -0.1313 190 VAL   B C   
2752 O  O   . VAL   B 34  ? 0.6113 0.8622 0.8569 -0.2036 0.2033  -0.1412 190 VAL   B O   
2753 C  CB  . VAL   B 34  ? 0.6696 0.8273 0.8538 -0.1952 0.2012  -0.1078 190 VAL   B CB  
2754 C  CG1 . VAL   B 34  ? 0.6215 0.8093 0.8306 -0.1824 0.1872  -0.1135 190 VAL   B CG1 
2755 C  CG2 . VAL   B 34  ? 0.7100 0.8418 0.8716 -0.1884 0.2051  -0.0964 190 VAL   B CG2 
2756 N  N   . ASP   B 35  ? 0.5182 0.7183 0.7354 -0.2185 0.2048  -0.1318 191 ASP   B N   
2757 C  CA  . ASP   B 35  ? 0.6226 0.8509 0.8616 -0.2246 0.2010  -0.1446 191 ASP   B CA  
2758 C  C   . ASP   B 35  ? 0.7032 0.9643 0.9600 -0.2303 0.2085  -0.1568 191 ASP   B C   
2759 O  O   . ASP   B 35  ? 0.8481 1.1480 1.1306 -0.2233 0.2009  -0.1674 191 ASP   B O   
2760 C  CB  . ASP   B 35  ? 0.7191 0.9218 0.9440 -0.2389 0.2052  -0.1437 191 ASP   B CB  
2761 N  N   . HIS   B 36  ? 0.6162 0.8622 0.8587 -0.2425 0.2235  -0.1554 192 HIS   B N   
2762 C  CA  . HIS   B 36  ? 0.6699 0.9467 0.9290 -0.2501 0.2319  -0.1677 192 HIS   B CA  
2763 C  C   . HIS   B 36  ? 0.6940 1.0050 0.9729 -0.2347 0.2259  -0.1722 192 HIS   B C   
2764 O  O   . HIS   B 36  ? 0.5869 0.9374 0.8915 -0.2319 0.2212  -0.1851 192 HIS   B O   
2765 C  CB  . HIS   B 36  ? 0.7493 1.0011 0.9870 -0.2642 0.2490  -0.1638 192 HIS   B CB  
2766 C  CG  . HIS   B 36  ? 0.7867 1.0134 1.0099 -0.2814 0.2566  -0.1641 192 HIS   B CG  
2767 N  ND1 . HIS   B 36  ? 0.7284 0.9224 0.9340 -0.2813 0.2515  -0.1554 192 HIS   B ND1 
2768 C  CD2 . HIS   B 36  ? 0.7026 0.9325 0.9263 -0.2993 0.2691  -0.1728 192 HIS   B CD2 
2769 C  CE1 . HIS   B 36  ? 0.7766 0.9534 0.9716 -0.2977 0.2605  -0.1583 192 HIS   B CE1 
2770 N  NE2 . HIS   B 36  ? 0.7219 0.9197 0.9275 -0.3093 0.2715  -0.1689 192 HIS   B NE2 
2771 N  N   . LEU   B 37  ? 0.6088 0.9048 0.8753 -0.2231 0.2251  -0.1618 193 LEU   B N   
2772 C  CA  . LEU   B 37  ? 0.5045 0.8297 0.7878 -0.2067 0.2189  -0.1655 193 LEU   B CA  
2773 C  C   . LEU   B 37  ? 0.3944 0.7494 0.7014 -0.1949 0.2031  -0.1731 193 LEU   B C   
2774 O  O   . LEU   B 37  ? 0.5093 0.9022 0.8391 -0.1889 0.1996  -0.1847 193 LEU   B O   
2775 C  CB  . LEU   B 37  ? 0.4934 0.7940 0.7581 -0.1953 0.2184  -0.1526 193 LEU   B CB  
2776 C  CG  . LEU   B 37  ? 0.4173 0.6882 0.6563 -0.2044 0.2332  -0.1445 193 LEU   B CG  
2777 C  CD1 . LEU   B 37  ? 0.4580 0.7054 0.6784 -0.1922 0.2314  -0.1324 193 LEU   B CD1 
2778 C  CD2 . LEU   B 37  ? 0.4338 0.7294 0.6834 -0.2101 0.2439  -0.1538 193 LEU   B CD2 
2779 N  N   . LEU   B 38  ? 0.3881 0.7262 0.6893 -0.1916 0.1934  -0.1672 194 LEU   B N   
2780 C  CA  . LEU   B 38  ? 0.4262 0.7899 0.7472 -0.1797 0.1779  -0.1736 194 LEU   B CA  
2781 C  C   . LEU   B 38  ? 0.5227 0.9189 0.8644 -0.1873 0.1772  -0.1885 194 LEU   B C   
2782 O  O   . LEU   B 38  ? 0.4730 0.9036 0.8357 -0.1753 0.1674  -0.1977 194 LEU   B O   
2783 C  CB  . LEU   B 38  ? 0.3324 0.6704 0.6421 -0.1773 0.1691  -0.1648 194 LEU   B CB  
2784 C  CG  . LEU   B 38  ? 0.4610 0.7753 0.7557 -0.1653 0.1657  -0.1521 194 LEU   B CG  
2785 C  CD1 . LEU   B 38  ? 0.3577 0.6432 0.6387 -0.1664 0.1595  -0.1432 194 LEU   B CD1 
2786 C  CD2 . LEU   B 38  ? 0.4139 0.7548 0.7248 -0.1455 0.1554  -0.1556 194 LEU   B CD2 
2787 N  N   . LEU   B 39  ? 0.6076 0.9933 0.9429 -0.2066 0.1877  -0.1915 195 LEU   B N   
2788 C  CA  . LEU   B 39  ? 0.5469 0.9650 0.9023 -0.2152 0.1887  -0.2070 195 LEU   B CA  
2789 C  C   . LEU   B 39  ? 0.4531 0.9080 0.8270 -0.2093 0.1912  -0.2171 195 LEU   B C   
2790 O  O   . LEU   B 39  ? 0.4841 0.9757 0.8801 -0.1995 0.1814  -0.2282 195 LEU   B O   
2791 C  CB  . LEU   B 39  ? 0.6126 1.0102 0.9555 -0.2379 0.2022  -0.2083 195 LEU   B CB  
2792 C  CG  . LEU   B 39  ? 0.5370 0.9200 0.8753 -0.2447 0.1967  -0.2081 195 LEU   B CG  
2793 C  CD1 . LEU   B 39  ? 0.6095 0.9481 0.9224 -0.2422 0.1948  -0.1920 195 LEU   B CD1 
2794 C  CD2 . LEU   B 39  ? 0.6456 1.0292 0.9840 -0.2659 0.2084  -0.2175 195 LEU   B CD2 
2795 N  N   . ARG   B 40  ? 0.5260 0.9707 0.8898 -0.2134 0.2037  -0.2129 196 ARG   B N   
2796 C  CA  . ARG   B 40  ? 0.4091 0.8876 0.7894 -0.2093 0.2077  -0.2227 196 ARG   B CA  
2797 C  C   . ARG   B 40  ? 0.3842 0.8874 0.7791 -0.1853 0.1935  -0.2245 196 ARG   B C   
2798 O  O   . ARG   B 40  ? 0.5297 1.0719 0.9469 -0.1783 0.1879  -0.2374 196 ARG   B O   
2799 C  CB  . ARG   B 40  ? 0.4737 0.9322 0.8371 -0.2166 0.2232  -0.2159 196 ARG   B CB  
2800 C  CG  . ARG   B 40  ? 0.5882 1.0788 0.9665 -0.2101 0.2274  -0.2243 196 ARG   B CG  
2801 C  CD  . ARG   B 40  ? 0.6375 1.1605 1.0346 -0.2234 0.2341  -0.2405 196 ARG   B CD  
2802 N  NE  . ARG   B 40  ? 0.7270 1.2474 1.1174 -0.2358 0.2513  -0.2418 196 ARG   B NE  
2803 C  CZ  . ARG   B 40  ? 0.6290 1.1735 1.0294 -0.2278 0.2548  -0.2468 196 ARG   B CZ  
2804 N  NH1 . ARG   B 40  ? 0.6323 1.2048 1.0496 -0.2069 0.2424  -0.2511 196 ARG   B NH1 
2805 N  NH2 . ARG   B 40  ? 0.7586 1.2978 1.1508 -0.2407 0.2713  -0.2474 196 ARG   B NH2 
2806 N  N   . LEU   B 41  ? 0.3657 0.8459 0.7475 -0.1722 0.1873  -0.2120 197 LEU   B N   
2807 C  CA  . LEU   B 41  ? 0.4340 0.9325 0.8264 -0.1488 0.1740  -0.2126 197 LEU   B CA  
2808 C  C   . LEU   B 41  ? 0.4906 1.0152 0.9009 -0.1403 0.1591  -0.2217 197 LEU   B C   
2809 O  O   . LEU   B 41  ? 0.4400 0.9933 0.8654 -0.1232 0.1497  -0.2287 197 LEU   B O   
2810 C  CB  . LEU   B 41  ? 0.3280 0.7941 0.7017 -0.1384 0.1700  -0.1978 197 LEU   B CB  
2811 C  CG  . LEU   B 41  ? 0.3619 0.8062 0.7182 -0.1393 0.1816  -0.1890 197 LEU   B CG  
2812 C  CD1 . LEU   B 41  ? 0.3238 0.7289 0.6578 -0.1373 0.1799  -0.1743 197 LEU   B CD1 
2813 C  CD2 . LEU   B 41  ? 0.3285 0.7960 0.6950 -0.1216 0.1789  -0.1933 197 LEU   B CD2 
2814 N  N   . LYS   B 42  ? 0.3554 0.8698 0.7631 -0.1513 0.1566  -0.2218 198 LYS   B N   
2815 C  CA  . LYS   B 42  ? 0.4556 0.9934 0.8784 -0.1428 0.1421  -0.2301 198 LYS   B CA  
2816 C  C   . LYS   B 42  ? 0.4211 1.0006 0.8660 -0.1453 0.1425  -0.2471 198 LYS   B C   
2817 O  O   . LYS   B 42  ? 0.4880 1.0928 0.9468 -0.1339 0.1294  -0.2553 198 LYS   B O   
2818 C  CB  . LYS   B 42  ? 0.4084 0.9241 0.8221 -0.1538 0.1395  -0.2261 198 LYS   B CB  
2819 C  CG  . LYS   B 42  ? 0.4320 0.9143 0.8284 -0.1458 0.1330  -0.2113 198 LYS   B CG  
2820 C  CD  . LYS   B 42  ? 0.5451 0.9951 0.9257 -0.1624 0.1380  -0.2048 198 LYS   B CD  
2821 C  CE  . LYS   B 42  ? 0.6651 1.1014 1.0404 -0.1534 0.1247  -0.1983 198 LYS   B CE  
2822 N  NZ  . LYS   B 42  ? 0.6967 1.0977 1.0539 -0.1683 0.1301  -0.1906 198 LYS   B NZ  
2823 N  N   . CYS   B 43  ? 0.3662 0.9537 0.8140 -0.1596 0.1570  -0.2529 199 CYS   B N   
2824 C  CA  . CYS   B 43  ? 0.3800 1.0095 0.8498 -0.1618 0.1581  -0.2700 199 CYS   B CA  
2825 C  C   . CYS   B 43  ? 0.5171 1.1753 0.9998 -0.1403 0.1509  -0.2749 199 CYS   B C   
2826 O  O   . CYS   B 43  ? 0.6280 1.3249 1.1304 -0.1363 0.1471  -0.2896 199 CYS   B O   
2827 C  CB  . CYS   B 43  ? 0.5250 1.1530 0.9931 -0.1847 0.1768  -0.2748 199 CYS   B CB  
2828 S  SG  . CYS   B 43  ? 0.5281 1.1189 0.9781 -0.2103 0.1870  -0.2692 199 CYS   B SG  
2829 N  N   . ASP   B 44  ? 0.5334 1.1733 1.0047 -0.1261 0.1490  -0.2634 200 ASP   B N   
2830 C  CA  . ASP   B 44  ? 0.3729 1.0348 0.8531 -0.1045 0.1425  -0.2668 200 ASP   B CA  
2831 C  C   . ASP   B 44  ? 0.3885 1.0574 0.8722 -0.0823 0.1232  -0.2663 200 ASP   B C   
2832 O  O   . ASP   B 44  ? 0.4702 1.1147 0.9427 -0.0807 0.1162  -0.2571 200 ASP   B O   
2833 C  CB  . ASP   B 44  ? 0.4322 1.0698 0.8970 -0.0998 0.1504  -0.2552 200 ASP   B CB  
2834 C  CG  . ASP   B 44  ? 0.4660 1.1279 0.9404 -0.0825 0.1489  -0.2610 200 ASP   B CG  
2835 O  OD1 . ASP   B 44  ? 0.5108 1.1776 0.9866 -0.0598 0.1353  -0.2596 200 ASP   B OD1 
2836 O  OD2 . ASP   B 44  ? 0.3837 1.0590 0.8633 -0.0915 0.1614  -0.2669 200 ASP   B OD2 
2837 N  N   . SER   B 45  ? 0.4191 1.1206 0.9173 -0.0648 0.1147  -0.2763 201 SER   B N   
2838 C  CA  . SER   B 45  ? 0.5288 1.2362 1.0281 -0.0419 0.0963  -0.2760 201 SER   B CA  
2839 C  C   . SER   B 45  ? 0.3779 1.0541 0.8596 -0.0259 0.0914  -0.2612 201 SER   B C   
2840 O  O   . SER   B 45  ? 0.6287 1.2902 1.1025 -0.0153 0.0793  -0.2547 201 SER   B O   
2841 C  CB  . SER   B 45  ? 0.4408 1.1889 0.9575 -0.0262 0.0890  -0.2902 201 SER   B CB  
2842 O  OG  . SER   B 45  ? 0.4479 1.2034 0.9667 -0.0216 0.0975  -0.2915 201 SER   B OG  
2843 N  N   . ALA   B 46  ? 0.4340 1.0998 0.9091 -0.0240 0.1009  -0.2561 202 ALA   B N   
2844 C  CA  . ALA   B 46  ? 0.3913 1.0285 0.8498 -0.0087 0.0970  -0.2432 202 ALA   B CA  
2845 C  C   . ALA   B 46  ? 0.3787 0.9793 0.8208 -0.0187 0.0984  -0.2302 202 ALA   B C   
2846 O  O   . ALA   B 46  ? 0.4923 1.0723 0.9229 -0.0046 0.0893  -0.2212 202 ALA   B O   
2847 C  CB  . ALA   B 46  ? 0.4295 1.0639 0.8841 -0.0067 0.1083  -0.2416 202 ALA   B CB  
2848 N  N   . PHE   B 47  ? 0.3209 0.9120 0.7608 -0.0426 0.1096  -0.2292 203 PHE   B N   
2849 C  CA  . PHE   B 47  ? 0.3824 0.9379 0.8058 -0.0536 0.1124  -0.2171 203 PHE   B CA  
2850 C  C   . PHE   B 47  ? 0.4336 0.9901 0.8607 -0.0655 0.1079  -0.2200 203 PHE   B C   
2851 O  O   . PHE   B 47  ? 0.2882 0.8199 0.7043 -0.0823 0.1149  -0.2134 203 PHE   B O   
2852 C  CB  . PHE   B 47  ? 0.3187 0.8535 0.7301 -0.0709 0.1299  -0.2111 203 PHE   B CB  
2853 C  CG  . PHE   B 47  ? 0.2937 0.8238 0.6986 -0.0600 0.1352  -0.2074 203 PHE   B CG  
2854 C  CD1 . PHE   B 47  ? 0.4209 0.9252 0.8108 -0.0478 0.1314  -0.1965 203 PHE   B CD1 
2855 C  CD2 . PHE   B 47  ? 0.3083 0.8599 0.7219 -0.0622 0.1442  -0.2155 203 PHE   B CD2 
2856 C  CE1 . PHE   B 47  ? 0.3457 0.8448 0.7285 -0.0378 0.1365  -0.1938 203 PHE   B CE1 
2857 C  CE2 . PHE   B 47  ? 0.3103 0.8571 0.7172 -0.0520 0.1492  -0.2124 203 PHE   B CE2 
2858 C  CZ  . PHE   B 47  ? 0.2982 0.8182 0.6892 -0.0396 0.1453  -0.2016 203 PHE   B CZ  
2859 N  N   . ARG   B 48  ? 0.5573 1.1412 0.9986 -0.0563 0.0960  -0.2299 204 ARG   B N   
2860 C  CA  . ARG   B 48  ? 0.3346 0.9245 0.7813 -0.0681 0.0925  -0.2352 204 ARG   B CA  
2861 C  C   . ARG   B 48  ? 0.3697 0.9271 0.8014 -0.0710 0.0879  -0.2237 204 ARG   B C   
2862 O  O   . ARG   B 48  ? 0.3961 0.9423 0.8244 -0.0887 0.0926  -0.2235 204 ARG   B O   
2863 C  CB  . ARG   B 48  ? 0.4609 1.0852 0.9233 -0.0538 0.0788  -0.2473 204 ARG   B CB  
2864 C  CG  . ARG   B 48  ? 0.5576 1.1918 1.0266 -0.0644 0.0743  -0.2547 204 ARG   B CG  
2865 C  CD  . ARG   B 48  ? 0.7123 1.3574 1.1893 -0.0886 0.0883  -0.2638 204 ARG   B CD  
2866 N  NE  . ARG   B 48  ? 0.8801 1.5396 1.3654 -0.0968 0.0833  -0.2733 204 ARG   B NE  
2867 C  CZ  . ARG   B 48  ? 0.8870 1.5510 1.3769 -0.1189 0.0939  -0.2808 204 ARG   B CZ  
2868 N  NH1 . ARG   B 48  ? 0.8054 1.4597 1.2917 -0.1358 0.1104  -0.2796 204 ARG   B NH1 
2869 N  NH2 . ARG   B 48  ? 0.7229 1.4006 1.2202 -0.1242 0.0881  -0.2898 204 ARG   B NH2 
2870 N  N   . GLY   B 49  ? 0.3398 0.8811 0.7620 -0.0538 0.0790  -0.2143 205 GLY   B N   
2871 C  CA  . GLY   B 49  ? 0.3748 0.8882 0.7840 -0.0547 0.0733  -0.2042 205 GLY   B CA  
2872 C  C   . GLY   B 49  ? 0.3510 0.8295 0.7431 -0.0621 0.0828  -0.1913 205 GLY   B C   
2873 O  O   . GLY   B 49  ? 0.3007 0.7564 0.6816 -0.0566 0.0769  -0.1819 205 GLY   B O   
2874 N  N   . VAL   B 50  ? 0.2499 0.7237 0.6390 -0.0747 0.0976  -0.1910 206 VAL   B N   
2875 C  CA  . VAL   B 50  ? 0.3104 0.7510 0.6814 -0.0809 0.1071  -0.1790 206 VAL   B CA  
2876 C  C   . VAL   B 50  ? 0.2475 0.6608 0.6062 -0.0965 0.1096  -0.1723 206 VAL   B C   
2877 O  O   . VAL   B 50  ? 0.4739 0.8932 0.8374 -0.1091 0.1105  -0.1780 206 VAL   B O   
2878 C  CB  . VAL   B 50  ? 0.2613 0.7033 0.6301 -0.0900 0.1223  -0.1804 206 VAL   B CB  
2879 C  CG1 . VAL   B 50  ? 0.4131 0.8594 0.7847 -0.1117 0.1327  -0.1865 206 VAL   B CG1 
2880 C  CG2 . VAL   B 50  ? 0.2978 0.7071 0.6466 -0.0913 0.1303  -0.1681 206 VAL   B CG2 
2881 N  N   . GLY   B 51  ? 0.2386 0.6215 0.5810 -0.0950 0.1104  -0.1604 207 GLY   B N   
2882 C  CA  . GLY   B 51  ? 0.2877 0.6413 0.6158 -0.1082 0.1129  -0.1530 207 GLY   B CA  
2883 C  C   . GLY   B 51  ? 0.3975 0.7187 0.7067 -0.1065 0.1168  -0.1404 207 GLY   B C   
2884 O  O   . GLY   B 51  ? 0.4205 0.7417 0.7275 -0.0960 0.1185  -0.1377 207 GLY   B O   
2885 N  N   . LEU   B 52  ? 0.2927 0.5856 0.5873 -0.1167 0.1183  -0.1329 208 LEU   B N   
2886 C  CA  . LEU   B 52  ? 0.3604 0.6201 0.6354 -0.1162 0.1212  -0.1208 208 LEU   B CA  
2887 C  C   . LEU   B 52  ? 0.5050 0.7634 0.7833 -0.1026 0.1079  -0.1176 208 LEU   B C   
2888 O  O   . LEU   B 52  ? 0.5403 0.8075 0.8267 -0.1012 0.0980  -0.1212 208 LEU   B O   
2889 C  CB  . LEU   B 52  ? 0.5359 0.7634 0.7911 -0.1326 0.1290  -0.1141 208 LEU   B CB  
2890 C  CG  . LEU   B 52  ? 0.6478 0.8641 0.8910 -0.1455 0.1441  -0.1132 208 LEU   B CG  
2891 C  CD1 . LEU   B 52  ? 0.6787 0.8774 0.9116 -0.1611 0.1488  -0.1130 208 LEU   B CD1 
2892 C  CD2 . LEU   B 52  ? 0.6434 0.8326 0.8654 -0.1436 0.1516  -0.1027 208 LEU   B CD2 
2893 N  N   . LEU   B 53  ? 0.5152 0.7538 0.7775 -0.0896 0.1045  -0.1084 209 LEU   B N   
2894 C  CA  . LEU   B 53  ? 0.5969 0.8199 0.8488 -0.0744 0.0896  -0.1011 209 LEU   B CA  
2895 C  C   . LEU   B 53  ? 0.8395 1.0447 1.0835 -0.0814 0.0845  -0.0967 209 LEU   B C   
2896 O  O   . LEU   B 53  ? 0.9438 1.1560 1.1935 -0.0736 0.0724  -0.0982 209 LEU   B O   
2897 C  CB  . LEU   B 53  ? 0.7276 0.9223 0.9571 -0.0656 0.0898  -0.0902 209 LEU   B CB  
2898 C  CG  . LEU   B 53  ? 0.6456 0.8384 0.8721 -0.0462 0.0768  -0.0874 209 LEU   B CG  
2899 C  CD1 . LEU   B 53  ? 0.6106 0.8293 0.8512 -0.0366 0.0786  -0.0956 209 LEU   B CD1 
2900 C  CD2 . LEU   B 53  ? 0.5852 0.7433 0.7867 -0.0417 0.0749  -0.0755 209 LEU   B CD2 
2901 N  N   . ASN   B 54  ? 0.8030 0.9838 1.0323 -0.0953 0.0936  -0.0910 210 ASN   B N   
2902 C  CA  . ASN   B 54  ? 0.8491 1.0110 1.0695 -0.1032 0.0908  -0.0873 210 ASN   B CA  
2903 C  C   . ASN   B 54  ? 0.8828 1.0336 1.0956 -0.0895 0.0758  -0.0813 210 ASN   B C   
2904 O  O   . ASN   B 54  ? 0.8193 0.9417 1.0116 -0.0847 0.0736  -0.0708 210 ASN   B O   
2905 C  CB  . ASN   B 54  ? 0.6186 0.8042 0.8589 -0.1166 0.0938  -0.0990 210 ASN   B CB  
2906 N  N   . SER   B 57  ? 0.9487 1.0266 1.1167 -0.1415 0.1172  -0.0714 213 SER   B N   
2907 C  CA  . SER   B 57  ? 0.9006 0.9566 1.0479 -0.1395 0.1251  -0.0628 213 SER   B CA  
2908 C  C   . SER   B 57  ? 0.8630 0.9421 1.0229 -0.1432 0.1352  -0.0693 213 SER   B C   
2909 O  O   . SER   B 57  ? 0.8147 0.9183 0.9896 -0.1318 0.1288  -0.0735 213 SER   B O   
2910 C  CB  . SER   B 57  ? 0.7094 0.7515 0.8433 -0.1224 0.1143  -0.0536 213 SER   B CB  
2911 O  OG  . SER   B 57  ? 0.9174 0.9472 1.0459 -0.1177 0.1036  -0.0500 213 SER   B OG  
2912 N  N   . TYR   B 58  ? 0.8298 0.8974 0.9774 -0.1537 0.1465  -0.0689 214 TYR   B N   
2913 C  CA  . TYR   B 58  ? 0.6937 0.7802 0.8490 -0.1563 0.1556  -0.0744 214 TYR   B CA  
2914 C  C   . TYR   B 58  ? 0.9421 1.0136 1.0815 -0.1502 0.1610  -0.0667 214 TYR   B C   
2915 O  O   . TYR   B 58  ? 0.9812 1.0749 1.1330 -0.1443 0.1630  -0.0711 214 TYR   B O   
2916 C  CB  . TYR   B 58  ? 0.6194 0.6932 0.7623 -0.1700 0.1669  -0.0754 214 TYR   B CB  
2917 C  CG  . TYR   B 58  ? 0.6306 0.7250 0.7903 -0.1797 0.1671  -0.0862 214 TYR   B CG  
2918 C  CD1 . TYR   B 58  ? 0.7323 0.8281 0.8986 -0.1809 0.1584  -0.0888 214 TYR   B CD1 
2919 C  CD2 . TYR   B 58  ? 0.6740 0.7858 0.8419 -0.1881 0.1766  -0.0941 214 TYR   B CD2 
2920 C  CE1 . TYR   B 58  ? 0.6333 0.7480 0.8141 -0.1899 0.1588  -0.0992 214 TYR   B CE1 
2921 C  CE2 . TYR   B 58  ? 0.6480 0.7792 0.8311 -0.1976 0.1773  -0.1046 214 TYR   B CE2 
2922 C  CZ  . TYR   B 58  ? 0.6413 0.7739 0.8307 -0.1984 0.1684  -0.1073 214 TYR   B CZ  
2923 O  OH  . TYR   B 58  ? 0.8124 0.9646 1.0163 -0.2078 0.1693  -0.1183 214 TYR   B OH  
2924 N  N   . TYR   B 59  ? 0.9978 1.0329 1.1101 -0.1498 0.1623  -0.0556 215 TYR   B N   
2925 C  CA  . TYR   B 59  ? 0.5379 0.5563 0.6308 -0.1449 0.1686  -0.0482 215 TYR   B CA  
2926 C  C   . TYR   B 59  ? 0.8597 0.8567 0.9348 -0.1295 0.1563  -0.0385 215 TYR   B C   
2927 O  O   . TYR   B 59  ? 0.8680 0.8474 0.9344 -0.1280 0.1489  -0.0337 215 TYR   B O   
2928 C  CB  . TYR   B 59  ? 0.7666 0.7563 0.8336 -0.1540 0.1780  -0.0431 215 TYR   B CB  
2929 N  N   . GLU   B 60  ? 0.8775 0.8764 0.9470 -0.1188 0.1547  -0.0362 216 GLU   B N   
2930 C  CA  . GLU   B 60  ? 0.6529 0.6331 0.7046 -0.1050 0.1447  -0.0279 216 GLU   B CA  
2931 C  C   . GLU   B 60  ? 0.6483 0.6104 0.6763 -0.1043 0.1535  -0.0224 216 GLU   B C   
2932 O  O   . GLU   B 60  ? 0.5409 0.5064 0.5674 -0.1135 0.1672  -0.0251 216 GLU   B O   
2933 C  CB  . GLU   B 60  ? 0.5990 0.5992 0.6666 -0.0914 0.1325  -0.0313 216 GLU   B CB  
2934 N  N   . HIS   B 61  ? 0.5927 0.5366 0.6022 -0.0932 0.1456  -0.0152 217 HIS   B N   
2935 C  CA  . HIS   B 61  ? 0.5723 0.4982 0.5569 -0.0900 0.1514  -0.0097 217 HIS   B CA  
2936 C  C   . HIS   B 61  ? 0.5314 0.4621 0.5151 -0.0758 0.1410  -0.0092 217 HIS   B C   
2937 O  O   . HIS   B 61  ? 0.6824 0.6062 0.6630 -0.0679 0.1291  -0.0060 217 HIS   B O   
2938 C  CB  . HIS   B 61  ? 0.5739 0.4667 0.5302 -0.0917 0.1530  -0.0007 217 HIS   B CB  
2939 C  CG  . HIS   B 61  ? 0.6176 0.4990 0.5686 -0.1066 0.1656  -0.0005 217 HIS   B CG  
2940 N  ND1 . HIS   B 61  ? 0.6759 0.5624 0.6417 -0.1146 0.1643  -0.0038 217 HIS   B ND1 
2941 C  CD2 . HIS   B 61  ? 0.7125 0.5767 0.6440 -0.1157 0.1804  0.0024  217 HIS   B CD2 
2942 C  CE1 . HIS   B 61  ? 0.6610 0.5334 0.6171 -0.1286 0.1779  -0.0034 217 HIS   B CE1 
2943 N  NE2 . HIS   B 61  ? 0.7984 0.6575 0.7336 -0.1285 0.1866  0.0004  217 HIS   B NE2 
2944 N  N   . VAL   B 62  ? 0.5688 0.5107 0.5545 -0.0731 0.1461  -0.0129 218 VAL   B N   
2945 C  CA  . VAL   B 62  ? 0.6146 0.5585 0.5972 -0.0606 0.1374  -0.0131 218 VAL   B CA  
2946 C  C   . VAL   B 62  ? 0.6870 0.6066 0.6409 -0.0554 0.1357  -0.0058 218 VAL   B C   
2947 O  O   . VAL   B 62  ? 0.7156 0.6334 0.6651 -0.0457 0.1261  -0.0053 218 VAL   B O   
2948 C  CB  . VAL   B 62  ? 0.5474 0.5108 0.5410 -0.0584 0.1432  -0.0201 218 VAL   B CB  
2949 C  CG1 . VAL   B 62  ? 0.5938 0.5839 0.6161 -0.0626 0.1451  -0.0281 218 VAL   B CG1 
2950 C  CG2 . VAL   B 62  ? 0.6451 0.5992 0.6203 -0.0635 0.1569  -0.0185 218 VAL   B CG2 
2951 N  N   . LYS   B 63  ? 0.6428 0.5431 0.5758 -0.0616 0.1447  -0.0005 219 LYS   B N   
2952 C  CA  . LYS   B 63  ? 0.5951 0.4718 0.4983 -0.0556 0.1433  0.0064  219 LYS   B CA  
2953 C  C   . LYS   B 63  ? 0.7163 0.5709 0.6045 -0.0583 0.1422  0.0132  219 LYS   B C   
2954 O  O   . LYS   B 63  ? 0.6636 0.5100 0.5488 -0.0688 0.1524  0.0145  219 LYS   B O   
2955 C  CB  . LYS   B 63  ? 0.6284 0.4985 0.5139 -0.0583 0.1560  0.0071  219 LYS   B CB  
2956 C  CG  . LYS   B 63  ? 0.6251 0.5128 0.5190 -0.0530 0.1565  0.0008  219 LYS   B CG  
2957 C  CD  . LYS   B 63  ? 0.6009 0.4788 0.4727 -0.0551 0.1691  0.0024  219 LYS   B CD  
2958 C  CE  . LYS   B 63  ? 0.7437 0.5931 0.5814 -0.0502 0.1672  0.0109  219 LYS   B CE  
2959 N  NZ  . LYS   B 63  ? 0.7705 0.6070 0.5830 -0.0528 0.1804  0.0134  219 LYS   B NZ  
2960 N  N   . ILE   B 64  ? 0.6248 0.4696 0.5032 -0.0488 0.1302  0.0170  220 ILE   B N   
2961 C  CA  . ILE   B 64  ? 0.6512 0.4757 0.5160 -0.0489 0.1275  0.0229  220 ILE   B CA  
2962 C  C   . ILE   B 64  ? 0.5452 0.3425 0.3787 -0.0511 0.1376  0.0295  220 ILE   B C   
2963 O  O   . ILE   B 64  ? 0.8983 0.6759 0.7200 -0.0549 0.1404  0.0341  220 ILE   B O   
2964 C  CB  . ILE   B 64  ? 0.6067 0.4315 0.4708 -0.0375 0.1120  0.0241  220 ILE   B CB  
2965 C  CG1 . ILE   B 64  ? 0.5871 0.4108 0.4365 -0.0267 0.1061  0.0245  220 ILE   B CG1 
2966 C  CG2 . ILE   B 64  ? 0.7853 0.6318 0.6782 -0.0379 0.1042  0.0186  220 ILE   B CG2 
2967 C  CD1 . ILE   B 64  ? 0.7541 0.5554 0.5713 -0.0227 0.1108  0.0303  220 ILE   B CD1 
2968 N  N   . SER   B 65  ? 0.6639 0.4583 0.4827 -0.0493 0.1441  0.0301  221 SER   B N   
2969 C  CA  . SER   B 65  ? 0.7994 0.5659 0.5839 -0.0495 0.1532  0.0370  221 SER   B CA  
2970 C  C   . SER   B 65  ? 0.6881 0.4524 0.4704 -0.0629 0.1712  0.0360  221 SER   B C   
2971 O  O   . SER   B 65  ? 0.7934 0.5366 0.5466 -0.0634 0.1807  0.0411  221 SER   B O   
2972 C  CB  . SER   B 65  ? 0.8866 0.6486 0.6508 -0.0366 0.1471  0.0388  221 SER   B CB  
2973 O  OG  . SER   B 65  ? 0.6882 0.4730 0.4679 -0.0363 0.1478  0.0321  221 SER   B OG  
2974 N  N   . ALA   B 66  ? 0.7906 0.5772 0.6026 -0.0735 0.1760  0.0292  222 ALA   B N   
2975 C  CA  . ALA   B 66  ? 0.7847 0.5747 0.6001 -0.0880 0.1934  0.0263  222 ALA   B CA  
2976 C  C   . ALA   B 66  ? 0.7273 0.5223 0.5621 -0.1005 0.1967  0.0233  222 ALA   B C   
2977 O  O   . ALA   B 66  ? 0.8041 0.6282 0.6705 -0.1064 0.1972  0.0149  222 ALA   B O   
2978 C  CB  . ALA   B 66  ? 0.5927 0.4119 0.4279 -0.0879 0.1965  0.0183  222 ALA   B CB  
2979 N  N   . PRO   B 67  ? 0.7985 0.5689 0.6176 -0.1016 0.1945  0.0283  223 PRO   B N   
2980 C  CA  . PRO   B 67  ? 0.8437 0.6203 0.6822 -0.1112 0.1937  0.0240  223 PRO   B CA  
2981 C  C   . PRO   B 67  ? 0.7081 0.5013 0.5634 -0.1254 0.2046  0.0162  223 PRO   B C   
2982 O  O   . PRO   B 67  ? 0.9694 0.7778 0.8476 -0.1336 0.2036  0.0100  223 PRO   B O   
2983 C  CB  . PRO   B 67  ? 0.9606 0.7037 0.7722 -0.1075 0.1902  0.0310  223 PRO   B CB  
2984 C  CG  . PRO   B 67  ? 0.8226 0.5437 0.6021 -0.1011 0.1946  0.0372  223 PRO   B CG  
2985 C  CD  . PRO   B 67  ? 0.8086 0.5454 0.5914 -0.0935 0.1926  0.0369  223 PRO   B CD  
2986 N  N   . ASN   B 68  ? 0.6383 0.4301 0.4828 -0.1284 0.2146  0.0158  224 ASN   B N   
2987 C  CA  . ASN   B 68  ? 0.7891 0.5979 0.6490 -0.1417 0.2255  0.0081  224 ASN   B CA  
2988 C  C   . ASN   B 68  ? 0.7890 0.6347 0.6767 -0.1422 0.2277  -0.0002 224 ASN   B C   
2989 O  O   . ASN   B 68  ? 0.7188 0.5814 0.6186 -0.1514 0.2369  -0.0070 224 ASN   B O   
2990 C  CB  . ASN   B 68  ? 0.7435 0.5282 0.5750 -0.1454 0.2360  0.0121  224 ASN   B CB  
2991 C  CG  . ASN   B 68  ? 0.9241 0.6737 0.7303 -0.1465 0.2357  0.0184  224 ASN   B CG  
2992 O  OD1 . ASN   B 68  ? 0.8579 0.6073 0.6746 -0.1530 0.2336  0.0155  224 ASN   B OD1 
2993 N  ND2 . ASN   B 68  ? 0.9814 0.7010 0.7532 -0.1393 0.2373  0.0266  224 ASN   B ND2 
2994 N  N   . GLU   B 69  ? 0.7583 0.6169 0.6563 -0.1322 0.2196  -0.0003 225 GLU   B N   
2995 C  CA  . GLU   B 69  ? 0.6042 0.4972 0.5280 -0.1301 0.2207  -0.0085 225 GLU   B CA  
2996 C  C   . GLU   B 69  ? 0.5245 0.4398 0.4781 -0.1293 0.2118  -0.0138 225 GLU   B C   
2997 O  O   . GLU   B 69  ? 0.5942 0.5043 0.5465 -0.1177 0.1978  -0.0102 225 GLU   B O   
2998 C  CB  . GLU   B 69  ? 0.4833 0.3714 0.3914 -0.1183 0.2200  -0.0048 225 GLU   B CB  
2999 C  CG  . GLU   B 69  ? 0.6422 0.5132 0.5234 -0.1190 0.2290  -0.0011 225 GLU   B CG  
3000 C  CD  . GLU   B 69  ? 0.8638 0.7313 0.7289 -0.1069 0.2277  0.0014  225 GLU   B CD  
3001 O  OE1 . GLU   B 69  ? 0.7409 0.6284 0.6244 -0.0969 0.2168  -0.0033 225 GLU   B OE1 
3002 O  OE2 . GLU   B 69  ? 0.8283 0.6744 0.6643 -0.1044 0.2318  0.0070  225 GLU   B OE2 
3003 N  N   . PHE   B 70  ? 0.5017 0.4433 0.4825 -0.1378 0.2139  -0.0232 226 PHE   B N   
3004 C  CA  . PHE   B 70  ? 0.4740 0.4371 0.4830 -0.1380 0.2053  -0.0291 226 PHE   B CA  
3005 C  C   . PHE   B 70  ? 0.4978 0.4971 0.5345 -0.1302 0.2012  -0.0380 226 PHE   B C   
3006 O  O   . PHE   B 70  ? 0.5693 0.5809 0.6075 -0.1287 0.2087  -0.0417 226 PHE   B O   
3007 C  CB  . PHE   B 70  ? 0.5870 0.5557 0.6068 -0.1505 0.2075  -0.0344 226 PHE   B CB  
3008 C  CG  . PHE   B 70  ? 0.6762 0.6098 0.6714 -0.1551 0.2072  -0.0267 226 PHE   B CG  
3009 C  CD1 . PHE   B 70  ? 0.7480 0.6543 0.7148 -0.1590 0.2161  -0.0209 226 PHE   B CD1 
3010 C  CD2 . PHE   B 70  ? 0.7214 0.6490 0.7212 -0.1545 0.1979  -0.0255 226 PHE   B CD2 
3011 C  CE1 . PHE   B 70  ? 0.8453 0.7189 0.7888 -0.1614 0.2156  -0.0143 226 PHE   B CE1 
3012 C  CE2 . PHE   B 70  ? 0.7479 0.6436 0.7248 -0.1572 0.1975  -0.0191 226 PHE   B CE2 
3013 C  CZ  . PHE   B 70  ? 0.7635 0.6321 0.7123 -0.1602 0.2063  -0.0136 226 PHE   B CZ  
3014 N  N   . ASP   B 71  ? 0.4697 0.4847 0.5267 -0.1233 0.1873  -0.0415 227 ASP   B N   
3015 C  CA  . ASP   B 71  ? 0.4970 0.5423 0.5775 -0.1121 0.1792  -0.0490 227 ASP   B CA  
3016 C  C   . ASP   B 71  ? 0.4688 0.5384 0.5769 -0.1147 0.1726  -0.0567 227 ASP   B C   
3017 O  O   . ASP   B 71  ? 0.4791 0.5377 0.5855 -0.1137 0.1632  -0.0531 227 ASP   B O   
3018 C  CB  . ASP   B 71  ? 0.6202 0.6535 0.6898 -0.0952 0.1656  -0.0432 227 ASP   B CB  
3019 C  CG  . ASP   B 71  ? 0.7567 0.8155 0.8452 -0.0831 0.1590  -0.0503 227 ASP   B CG  
3020 O  OD1 . ASP   B 71  ? 0.5803 0.6439 0.6648 -0.0790 0.1649  -0.0524 227 ASP   B OD1 
3021 O  OD2 . ASP   B 71  ? 0.8485 0.9212 0.9543 -0.0770 0.1480  -0.0537 227 ASP   B OD2 
3022 N  N   . VAL   B 72  ? 0.5603 0.6640 0.6935 -0.1173 0.1773  -0.0679 228 VAL   B N   
3023 C  CA  . VAL   B 72  ? 0.6107 0.7421 0.7714 -0.1210 0.1727  -0.0772 228 VAL   B CA  
3024 C  C   . VAL   B 72  ? 0.4949 0.6581 0.6778 -0.1065 0.1643  -0.0854 228 VAL   B C   
3025 O  O   . VAL   B 72  ? 0.3318 0.5059 0.5163 -0.1011 0.1698  -0.0887 228 VAL   B O   
3026 C  CB  . VAL   B 72  ? 0.5973 0.7376 0.7635 -0.1372 0.1828  -0.0832 228 VAL   B CB  
3027 C  CG1 . VAL   B 72  ? 0.6115 0.7771 0.8019 -0.1393 0.1747  -0.0922 228 VAL   B CG1 
3028 C  CG2 . VAL   B 72  ? 0.5792 0.6817 0.7171 -0.1484 0.1896  -0.0739 228 VAL   B CG2 
3029 N  N   . MET   B 73  ? 0.4317 0.6087 0.6303 -0.0995 0.1511  -0.0889 229 MET   B N   
3030 C  CA  . MET   B 73  ? 0.4448 0.6514 0.6641 -0.0848 0.1423  -0.0970 229 MET   B CA  
3031 C  C   . MET   B 73  ? 0.3318 0.5737 0.5794 -0.0910 0.1417  -0.1092 229 MET   B C   
3032 O  O   . MET   B 73  ? 0.4042 0.6432 0.6552 -0.0965 0.1358  -0.1088 229 MET   B O   
3033 C  CB  . MET   B 73  ? 0.3070 0.4987 0.5178 -0.0681 0.1259  -0.0903 229 MET   B CB  
3034 C  CG  . MET   B 73  ? 0.5368 0.7545 0.7652 -0.0517 0.1165  -0.0979 229 MET   B CG  
3035 S  SD  . MET   B 73  ? 0.5724 0.7673 0.7855 -0.0321 0.1007  -0.0895 229 MET   B SD  
3036 C  CE  . MET   B 73  ? 0.5116 0.6689 0.6948 -0.0359 0.1069  -0.0779 229 MET   B CE  
3037 N  N   . PHE   B 74  ? 0.3553 0.6282 0.6203 -0.0889 0.1457  -0.1195 230 PHE   B N   
3038 C  CA  . PHE   B 74  ? 0.3233 0.6271 0.6096 -0.0887 0.1392  -0.1299 230 PHE   B CA  
3039 C  C   . PHE   B 74  ? 0.3984 0.7227 0.6990 -0.0678 0.1255  -0.1346 230 PHE   B C   
3040 O  O   . PHE   B 74  ? 0.4560 0.7878 0.7578 -0.0545 0.1256  -0.1363 230 PHE   B O   
3041 C  CB  . PHE   B 74  ? 0.3680 0.6908 0.6612 -0.0963 0.1489  -0.1376 230 PHE   B CB  
3042 C  CG  . PHE   B 74  ? 0.3129 0.6170 0.5927 -0.1169 0.1617  -0.1345 230 PHE   B CG  
3043 C  CD1 . PHE   B 74  ? 0.3171 0.5875 0.5778 -0.1264 0.1638  -0.1248 230 PHE   B CD1 
3044 C  CD2 . PHE   B 74  ? 0.2949 0.6142 0.5801 -0.1261 0.1717  -0.1414 230 PHE   B CD2 
3045 C  CE1 . PHE   B 74  ? 0.3959 0.6461 0.6414 -0.1436 0.1751  -0.1217 230 PHE   B CE1 
3046 C  CE2 . PHE   B 74  ? 0.3779 0.6780 0.6490 -0.1445 0.1836  -0.1387 230 PHE   B CE2 
3047 C  CZ  . PHE   B 74  ? 0.3274 0.5919 0.5778 -0.1527 0.1852  -0.1287 230 PHE   B CZ  
3048 N  N   . LYS   B 75  ? 0.4031 0.7343 0.7123 -0.0640 0.1135  -0.1364 231 LYS   B N   
3049 C  CA  . LYS   B 75  ? 0.2669 0.6138 0.5861 -0.0432 0.0993  -0.1399 231 LYS   B CA  
3050 C  C   . LYS   B 75  ? 0.2896 0.6703 0.6269 -0.0389 0.0933  -0.1512 231 LYS   B C   
3051 O  O   . LYS   B 75  ? 0.3094 0.7011 0.6534 -0.0534 0.0976  -0.1566 231 LYS   B O   
3052 C  CB  . LYS   B 75  ? 0.2571 0.5846 0.5678 -0.0387 0.0874  -0.1327 231 LYS   B CB  
3053 C  CG  . LYS   B 75  ? 0.4500 0.7809 0.7673 -0.0542 0.0871  -0.1351 231 LYS   B CG  
3054 C  CD  . LYS   B 75  ? 0.4232 0.7548 0.7419 -0.0431 0.0708  -0.1344 231 LYS   B CD  
3055 C  CE  . LYS   B 75  ? 0.4732 0.8400 0.8105 -0.0347 0.0624  -0.1460 231 LYS   B CE  
3056 N  NZ  . LYS   B 75  ? 0.4735 0.8434 0.8135 -0.0343 0.0510  -0.1475 231 LYS   B NZ  
3057 N  N   . LEU   B 76  ? 0.2049 0.6004 0.5484 -0.0181 0.0832  -0.1548 232 LEU   B N   
3058 C  CA  . LEU   B 76  ? 0.2289 0.6561 0.5881 -0.0105 0.0757  -0.1654 232 LEU   B CA  
3059 C  C   . LEU   B 76  ? 0.2543 0.6835 0.6125 0.0131  0.0598  -0.1648 232 LEU   B C   
3060 O  O   . LEU   B 76  ? 0.3172 0.7361 0.6673 0.0285  0.0580  -0.1612 232 LEU   B O   
3061 C  CB  . LEU   B 76  ? 0.2249 0.6714 0.5915 -0.0104 0.0844  -0.1725 232 LEU   B CB  
3062 C  CG  . LEU   B 76  ? 0.3117 0.7929 0.6951 -0.0012 0.0769  -0.1843 232 LEU   B CG  
3063 C  CD1 . LEU   B 76  ? 0.3582 0.8547 0.7523 -0.0171 0.0768  -0.1912 232 LEU   B CD1 
3064 C  CD2 . LEU   B 76  ? 0.2752 0.7735 0.6647 0.0017  0.0851  -0.1905 232 LEU   B CD2 
3065 N  N   . GLU   B 77  ? 0.3969 0.8370 0.7610 0.0161  0.0485  -0.1683 233 GLU   B N   
3066 C  CA  . GLU   B 77  ? 0.3802 0.8175 0.7392 0.0382  0.0332  -0.1664 233 GLU   B CA  
3067 C  C   . GLU   B 77  ? 0.3119 0.7678 0.6753 0.0567  0.0285  -0.1728 233 GLU   B C   
3068 O  O   . GLU   B 77  ? 0.2982 0.7818 0.6754 0.0527  0.0312  -0.1827 233 GLU   B O   
3069 C  CB  . GLU   B 77  ? 0.3736 0.8180 0.7361 0.0366  0.0226  -0.1688 233 GLU   B CB  
3070 C  CG  . GLU   B 77  ? 0.4905 0.9280 0.8437 0.0594  0.0068  -0.1655 233 GLU   B CG  
3071 C  CD  . GLU   B 77  ? 0.5732 1.0171 0.9280 0.0583  -0.0037 -0.1678 233 GLU   B CD  
3072 O  OE1 . GLU   B 77  ? 0.7400 1.1941 1.1040 0.0399  0.0010  -0.1725 233 GLU   B OE1 
3073 O  OE2 . GLU   B 77  ? 0.4934 0.9298 0.8381 0.0762  -0.0165 -0.1647 233 GLU   B OE2 
3074 N  N   . VAL   B 78  ? 0.3057 0.7451 0.6564 0.0768  0.0214  -0.1672 234 VAL   B N   
3075 C  CA  . VAL   B 78  ? 0.3129 0.7642 0.6635 0.0974  0.0144  -0.1720 234 VAL   B CA  
3076 C  C   . VAL   B 78  ? 0.5219 0.9631 0.8613 0.1156  -0.0016 -0.1685 234 VAL   B C   
3077 O  O   . VAL   B 78  ? 0.5645 0.9764 0.8861 0.1268  -0.0060 -0.1594 234 VAL   B O   
3078 C  CB  . VAL   B 78  ? 0.4425 0.8782 0.7832 0.1064  0.0209  -0.1683 234 VAL   B CB  
3079 C  CG1 . VAL   B 78  ? 0.4140 0.8576 0.7518 0.1291  0.0129  -0.1723 234 VAL   B CG1 
3080 C  CG2 . VAL   B 78  ? 0.4745 0.9209 0.8247 0.0888  0.0370  -0.1719 234 VAL   B CG2 
3081 N  N   . PRO   B 79  ? 0.5571 1.0209 0.9051 0.1184  -0.0104 -0.1758 235 PRO   B N   
3082 C  CA  . PRO   B 79  ? 0.5301 0.9828 0.8647 0.1359  -0.0253 -0.1722 235 PRO   B CA  
3083 C  C   . PRO   B 79  ? 0.3675 0.8132 0.6902 0.1597  -0.0315 -0.1715 235 PRO   B C   
3084 O  O   . PRO   B 79  ? 0.3349 0.7971 0.6658 0.1635  -0.0266 -0.1781 235 PRO   B O   
3085 C  CB  . PRO   B 79  ? 0.5044 0.9867 0.8529 0.1305  -0.0310 -0.1821 235 PRO   B CB  
3086 C  CG  . PRO   B 79  ? 0.5479 1.0585 0.9173 0.1130  -0.0197 -0.1921 235 PRO   B CG  
3087 C  CD  . PRO   B 79  ? 0.2787 0.7780 0.6472 0.1063  -0.0066 -0.1880 235 PRO   B CD  
3088 N  N   . ARG   B 80  ? 0.4501 0.8688 0.7517 0.1754  -0.0417 -0.1632 236 ARG   B N   
3089 C  CA  . ARG   B 80  ? 0.3158 0.7212 0.6010 0.1985  -0.0487 -0.1612 236 ARG   B CA  
3090 C  C   . ARG   B 80  ? 0.4142 0.8089 0.6962 0.2016  -0.0394 -0.1597 236 ARG   B C   
3091 O  O   . ARG   B 80  ? 0.5453 0.9516 0.8291 0.2137  -0.0399 -0.1655 236 ARG   B O   
3092 C  CB  . ARG   B 80  ? 0.4062 0.8416 0.6994 0.2102  -0.0572 -0.1719 236 ARG   B CB  
3093 N  N   . ILE   B 81  ? 0.4152 0.7883 0.6925 0.1905  -0.0307 -0.1526 237 ILE   B N   
3094 C  CA  . ILE   B 81  ? 0.4943 0.8549 0.7673 0.1914  -0.0209 -0.1509 237 ILE   B CA  
3095 C  C   . ILE   B 81  ? 0.5043 0.8301 0.7510 0.2115  -0.0271 -0.1435 237 ILE   B C   
3096 O  O   . ILE   B 81  ? 0.5384 0.8409 0.7674 0.2197  -0.0363 -0.1365 237 ILE   B O   
3097 C  CB  . ILE   B 81  ? 0.5232 0.8720 0.7985 0.1724  -0.0099 -0.1462 237 ILE   B CB  
3098 C  CG1 . ILE   B 81  ? 0.5860 0.9212 0.8553 0.1729  0.0005  -0.1448 237 ILE   B CG1 
3099 C  CG2 . ILE   B 81  ? 0.7342 1.0522 0.9932 0.1720  -0.0156 -0.1361 237 ILE   B CG2 
3100 C  CD1 . ILE   B 81  ? 0.5167 0.8566 0.7961 0.1515  0.0142  -0.1452 237 ILE   B CD1 
3101 N  N   . GLN   B 82  ? 0.5138 0.8341 0.7562 0.2191  -0.0217 -0.1451 238 GLN   B N   
3102 C  CA  . GLN   B 82  ? 0.5138 0.7969 0.7296 0.2358  -0.0253 -0.1382 238 GLN   B CA  
3103 C  C   . GLN   B 82  ? 0.4997 0.7647 0.7100 0.2301  -0.0138 -0.1357 238 GLN   B C   
3104 O  O   . GLN   B 82  ? 0.5214 0.8057 0.7438 0.2284  -0.0060 -0.1427 238 GLN   B O   
3105 C  CB  . GLN   B 82  ? 0.6705 0.9636 0.8831 0.2551  -0.0324 -0.1437 238 GLN   B CB  
3106 C  CG  . GLN   B 82  ? 0.8083 1.0636 0.9944 0.2706  -0.0335 -0.1377 238 GLN   B CG  
3107 C  CD  . GLN   B 82  ? 0.9010 1.1138 1.0593 0.2754  -0.0402 -0.1261 238 GLN   B CD  
3108 O  OE1 . GLN   B 82  ? 0.8544 1.0305 0.9937 0.2739  -0.0358 -0.1185 238 GLN   B OE1 
3109 N  NE2 . GLN   B 82  ? 0.7208 0.9382 0.8757 0.2806  -0.0505 -0.1250 238 GLN   B NE2 
3110 N  N   . LEU   B 83  ? 0.5775 0.8056 0.7689 0.2269  -0.0125 -0.1264 239 LEU   B N   
3111 C  CA  . LEU   B 83  ? 0.4637 0.6721 0.6473 0.2215  -0.0022 -0.1242 239 LEU   B CA  
3112 C  C   . LEU   B 83  ? 0.5134 0.6893 0.6729 0.2371  -0.0041 -0.1209 239 LEU   B C   
3113 O  O   . LEU   B 83  ? 0.6025 0.7558 0.7434 0.2491  -0.0133 -0.1156 239 LEU   B O   
3114 C  CB  . LEU   B 83  ? 0.5087 0.6951 0.6850 0.2084  0.0008  -0.1171 239 LEU   B CB  
3115 C  CG  . LEU   B 83  ? 0.4368 0.6514 0.6353 0.1917  0.0031  -0.1200 239 LEU   B CG  
3116 C  CD1 . LEU   B 83  ? 0.3097 0.4976 0.4967 0.1740  0.0079  -0.1107 239 LEU   B CD1 
3117 C  CD2 . LEU   B 83  ? 0.5349 0.7869 0.7571 0.1827  0.0124  -0.1295 239 LEU   B CD2 
3118 N  N   . GLU   B 84  ? 0.3712 0.5442 0.5299 0.2362  0.0051  -0.1240 240 GLU   B N   
3119 C  CA  . GLU   B 84  ? 0.5902 0.7266 0.7240 0.2471  0.0052  -0.1203 240 GLU   B CA  
3120 C  C   . GLU   B 84  ? 0.6185 0.7359 0.7449 0.2360  0.0157  -0.1186 240 GLU   B C   
3121 O  O   . GLU   B 84  ? 0.4906 0.6311 0.6325 0.2276  0.0251  -0.1247 240 GLU   B O   
3122 C  CB  . GLU   B 84  ? 0.4810 0.6311 0.6178 0.2617  0.0044  -0.1272 240 GLU   B CB  
3123 C  CG  . GLU   B 84  ? 0.4940 0.6083 0.6076 0.2694  0.0077  -0.1249 240 GLU   B CG  
3124 C  CD  . GLU   B 84  ? 0.8109 0.9341 0.9241 0.2860  0.0055  -0.1310 240 GLU   B CD  
3125 O  OE1 . GLU   B 84  ? 0.8360 0.9973 0.9715 0.2860  0.0094  -0.1400 240 GLU   B OE1 
3126 O  OE2 . GLU   B 84  ? 0.8639 0.9553 0.9538 0.2987  0.0001  -0.1269 240 GLU   B OE2 
3127 N  N   . GLU   B 85  ? 0.5317 0.6069 0.6333 0.2353  0.0143  -0.1106 241 GLU   B N   
3128 C  CA  . GLU   B 85  ? 0.5003 0.5558 0.5927 0.2242  0.0229  -0.1089 241 GLU   B CA  
3129 C  C   . GLU   B 85  ? 0.4723 0.5234 0.5596 0.2286  0.0302  -0.1140 241 GLU   B C   
3130 O  O   . GLU   B 85  ? 0.6302 0.6690 0.7067 0.2417  0.0269  -0.1147 241 GLU   B O   
3131 C  CB  . GLU   B 85  ? 0.6228 0.6339 0.6892 0.2217  0.0190  -0.0995 241 GLU   B CB  
3132 C  CG  . GLU   B 85  ? 0.7493 0.7364 0.8026 0.2087  0.0266  -0.0969 241 GLU   B CG  
3133 C  CD  . GLU   B 85  ? 0.7225 0.6664 0.7500 0.2039  0.0230  -0.0876 241 GLU   B CD  
3134 O  OE1 . GLU   B 85  ? 0.7439 0.6745 0.7623 0.2130  0.0151  -0.0834 241 GLU   B OE1 
3135 O  OE2 . GLU   B 85  ? 0.6248 0.5486 0.6407 0.1900  0.0282  -0.0843 241 GLU   B OE2 
3136 N  N   . TYR   B 86  ? 0.4656 0.5288 0.5612 0.2174  0.0403  -0.1180 242 TYR   B N   
3137 C  CA  . TYR   B 86  ? 0.4447 0.5044 0.5350 0.2197  0.0485  -0.1231 242 TYR   B CA  
3138 C  C   . TYR   B 86  ? 0.5610 0.5749 0.6227 0.2195  0.0486  -0.1182 242 TYR   B C   
3139 O  O   . TYR   B 86  ? 0.5184 0.5133 0.5702 0.2085  0.0491  -0.1130 242 TYR   B O   
3140 C  CB  . TYR   B 86  ? 0.4356 0.5210 0.5410 0.2064  0.0598  -0.1283 242 TYR   B CB  
3141 C  CG  . TYR   B 86  ? 0.6173 0.6952 0.7137 0.2068  0.0689  -0.1328 242 TYR   B CG  
3142 C  CD1 . TYR   B 86  ? 0.5628 0.6492 0.6615 0.2187  0.0698  -0.1382 242 TYR   B CD1 
3143 C  CD2 . TYR   B 86  ? 0.6348 0.6960 0.7189 0.1933  0.0758  -0.1302 242 TYR   B CD2 
3144 C  CE1 . TYR   B 86  ? 0.6331 0.7125 0.7233 0.2192  0.0781  -0.1425 242 TYR   B CE1 
3145 C  CE2 . TYR   B 86  ? 0.6099 0.6648 0.6848 0.1949  0.0839  -0.1353 242 TYR   B CE2 
3146 C  CZ  . TYR   B 86  ? 0.6888 0.7526 0.7669 0.2076  0.0853  -0.1414 242 TYR   B CZ  
3147 O  OH  . TYR   B 86  ? 0.7616 0.8184 0.8301 0.2079  0.0932  -0.1458 242 TYR   B OH  
3148 N  N   . SER   B 87  ? 0.5995 0.5965 0.6484 0.2302  0.0484  -0.1200 243 SER   B N   
3149 C  CA  . SER   B 87  ? 0.6935 0.6450 0.7143 0.2291  0.0480  -0.1157 243 SER   B CA  
3150 C  C   . SER   B 87  ? 0.7321 0.6598 0.7413 0.2232  0.0414  -0.1067 243 SER   B C   
3151 O  O   . SER   B 87  ? 0.7390 0.6721 0.7521 0.2301  0.0335  -0.1034 243 SER   B O   
3152 C  CB  . SER   B 87  ? 0.8072 0.7508 0.8211 0.2193  0.0573  -0.1189 243 SER   B CB  
3153 O  OG  . SER   B 87  ? 0.6487 0.6095 0.6697 0.2257  0.0634  -0.1268 243 SER   B OG  
3154 N  N   . ASN   B 88  ? 0.6420 0.5447 0.6367 0.2110  0.0444  -0.1031 244 ASN   B N   
3155 C  CA  . ASN   B 88  ? 0.7456 0.6284 0.7308 0.2037  0.0389  -0.0946 244 ASN   B CA  
3156 C  C   . ASN   B 88  ? 0.5612 0.4566 0.5553 0.1826  0.0433  -0.0915 244 ASN   B C   
3157 O  O   . ASN   B 88  ? 0.6149 0.4862 0.5951 0.1696  0.0432  -0.0857 244 ASN   B O   
3158 C  CB  . ASN   B 88  ? 0.8835 0.7227 0.8420 0.2029  0.0362  -0.0894 244 ASN   B CB  
3159 C  CG  . ASN   B 88  ? 0.9765 0.8090 0.9290 0.2182  0.0309  -0.0892 244 ASN   B CG  
3160 O  OD1 . ASN   B 88  ? 1.0199 0.8577 0.9752 0.2249  0.0240  -0.0853 244 ASN   B OD1 
3161 N  ND2 . ASN   B 88  ? 0.8370 0.6578 0.7803 0.2243  0.0340  -0.0936 244 ASN   B ND2 
3162 N  N   . THR   B 89  ? 0.6048 0.5377 0.6217 0.1784  0.0471  -0.0951 245 THR   B N   
3163 C  CA  . THR   B 89  ? 0.6974 0.6413 0.7210 0.1579  0.0522  -0.0918 245 THR   B CA  
3164 C  C   . THR   B 89  ? 0.5300 0.4729 0.5567 0.1471  0.0468  -0.0836 245 THR   B C   
3165 O  O   . THR   B 89  ? 0.4802 0.4210 0.5053 0.1309  0.0494  -0.0793 245 THR   B O   
3166 C  CB  . THR   B 89  ? 0.5452 0.5266 0.5900 0.1563  0.0592  -0.0982 245 THR   B CB  
3167 O  OG1 . THR   B 89  ? 0.5484 0.5559 0.6115 0.1662  0.0549  -0.1013 245 THR   B OG1 
3168 C  CG2 . THR   B 89  ? 0.5449 0.5259 0.5846 0.1640  0.0662  -0.1060 245 THR   B CG2 
3169 N  N   . ARG   B 90  ? 0.4904 0.4353 0.5205 0.1567  0.0393  -0.0820 246 ARG   B N   
3170 C  CA  . ARG   B 90  ? 0.5491 0.4939 0.5821 0.1487  0.0335  -0.0749 246 ARG   B CA  
3171 C  C   . ARG   B 90  ? 0.4474 0.4236 0.5014 0.1359  0.0362  -0.0747 246 ARG   B C   
3172 O  O   . ARG   B 90  ? 0.4716 0.4549 0.5323 0.1317  0.0312  -0.0707 246 ARG   B O   
3173 C  CB  . ARG   B 90  ? 0.5135 0.4248 0.5262 0.1378  0.0325  -0.0677 246 ARG   B CB  
3174 C  CG  . ARG   B 90  ? 0.5630 0.4391 0.5526 0.1469  0.0317  -0.0681 246 ARG   B CG  
3175 C  CD  . ARG   B 90  ? 0.7122 0.5677 0.6898 0.1552  0.0244  -0.0632 246 ARG   B CD  
3176 N  NE  . ARG   B 90  ? 0.9590 0.7742 0.9107 0.1578  0.0249  -0.0618 246 ARG   B NE  
3177 C  CZ  . ARG   B 90  ? 0.9342 0.7298 0.8720 0.1752  0.0231  -0.0643 246 ARG   B CZ  
3178 N  NH1 . ARG   B 90  ? 0.7234 0.5401 0.6726 0.1908  0.0197  -0.0679 246 ARG   B NH1 
3179 N  NH2 . ARG   B 90  ? 0.8355 0.5963 0.7511 0.1711  0.0243  -0.0618 246 ARG   B NH2 
3180 N  N   . ALA   B 91  ? 0.4872 0.4808 0.5502 0.1296  0.0444  -0.0790 247 ALA   B N   
3181 C  CA  . ALA   B 91  ? 0.4051 0.4256 0.4858 0.1169  0.0484  -0.0791 247 ALA   B CA  
3182 C  C   . ALA   B 91  ? 0.3411 0.3964 0.4426 0.1225  0.0530  -0.0879 247 ALA   B C   
3183 O  O   . ALA   B 91  ? 0.2968 0.3768 0.4156 0.1143  0.0546  -0.0890 247 ALA   B O   
3184 C  CB  . ALA   B 91  ? 0.3550 0.3664 0.4275 0.1013  0.0553  -0.0755 247 ALA   B CB  
3185 N  N   . TYR   B 92  ? 0.3176 0.3760 0.4182 0.1358  0.0555  -0.0949 248 TYR   B N   
3186 C  CA  . TYR   B 92  ? 0.3160 0.4093 0.4367 0.1413  0.0610  -0.1046 248 TYR   B CA  
3187 C  C   . TYR   B 92  ? 0.4690 0.5750 0.5980 0.1614  0.0532  -0.1105 248 TYR   B C   
3188 O  O   . TYR   B 92  ? 0.4616 0.5424 0.5743 0.1753  0.0468  -0.1087 248 TYR   B O   
3189 C  CB  . TYR   B 92  ? 0.4290 0.5200 0.5434 0.1424  0.0704  -0.1095 248 TYR   B CB  
3190 C  CG  . TYR   B 92  ? 0.3615 0.4449 0.4685 0.1239  0.0786  -0.1049 248 TYR   B CG  
3191 C  CD1 . TYR   B 92  ? 0.4159 0.4661 0.5011 0.1175  0.0768  -0.0976 248 TYR   B CD1 
3192 C  CD2 . TYR   B 92  ? 0.4062 0.5156 0.5273 0.1129  0.0882  -0.1082 248 TYR   B CD2 
3193 C  CE1 . TYR   B 92  ? 0.4430 0.4871 0.5206 0.1025  0.0832  -0.0937 248 TYR   B CE1 
3194 C  CE2 . TYR   B 92  ? 0.3578 0.4577 0.4691 0.0973  0.0955  -0.1034 248 TYR   B CE2 
3195 C  CZ  . TYR   B 92  ? 0.3774 0.4451 0.4670 0.0931  0.0924  -0.0962 248 TYR   B CZ  
3196 O  OH  . TYR   B 92  ? 0.5264 0.5855 0.6053 0.0795  0.0986  -0.0917 248 TYR   B OH  
3197 N  N   . TYR   B 93  ? 0.3340 0.4788 0.4877 0.1631  0.0539  -0.1178 249 TYR   B N   
3198 C  CA  . TYR   B 93  ? 0.3361 0.4987 0.5003 0.1822  0.0453  -0.1240 249 TYR   B CA  
3199 C  C   . TYR   B 93  ? 0.4738 0.6787 0.6620 0.1846  0.0507  -0.1348 249 TYR   B C   
3200 O  O   . TYR   B 93  ? 0.4160 0.6437 0.6190 0.1701  0.0608  -0.1388 249 TYR   B O   
3201 C  CB  . TYR   B 93  ? 0.3914 0.5576 0.5607 0.1794  0.0359  -0.1194 249 TYR   B CB  
3202 C  CG  . TYR   B 93  ? 0.4515 0.5765 0.5967 0.1755  0.0299  -0.1075 249 TYR   B CG  
3203 C  CD1 . TYR   B 93  ? 0.3128 0.4209 0.4500 0.1555  0.0344  -0.0995 249 TYR   B CD1 
3204 C  CD2 . TYR   B 93  ? 0.3878 0.4910 0.5177 0.1920  0.0200  -0.1045 249 TYR   B CD2 
3205 C  CE1 . TYR   B 93  ? 0.3234 0.3972 0.4403 0.1516  0.0294  -0.0897 249 TYR   B CE1 
3206 C  CE2 . TYR   B 93  ? 0.4811 0.5474 0.5892 0.1872  0.0158  -0.0941 249 TYR   B CE2 
3207 C  CZ  . TYR   B 93  ? 0.4312 0.4845 0.5340 0.1666  0.0206  -0.0872 249 TYR   B CZ  
3208 O  OH  . TYR   B 93  ? 0.3984 0.4182 0.4812 0.1615  0.0167  -0.0780 249 TYR   B OH  
3209 N  N   . PHE   B 94  ? 0.4452 0.6561 0.6334 0.2003  0.0438  -0.1374 250 PHE   B N   
3210 C  CA  . PHE   B 94  ? 0.4060 0.6571 0.6164 0.2017  0.0447  -0.1459 250 PHE   B CA  
3211 C  C   . PHE   B 94  ? 0.4373 0.7079 0.6608 0.2007  0.0354  -0.1462 250 PHE   B C   
3212 O  O   . PHE   B 94  ? 0.4837 0.7341 0.6945 0.2093  0.0247  -0.1403 250 PHE   B O   
3213 C  CB  . PHE   B 94  ? 0.4973 0.7467 0.7016 0.2202  0.0414  -0.1497 250 PHE   B CB  
3214 C  CG  . PHE   B 94  ? 0.3785 0.6083 0.5690 0.2226  0.0499  -0.1502 250 PHE   B CG  
3215 C  CD1 . PHE   B 94  ? 0.4234 0.6730 0.6251 0.2120  0.0626  -0.1557 250 PHE   B CD1 
3216 C  CD2 . PHE   B 94  ? 0.4835 0.6741 0.6488 0.2350  0.0454  -0.1453 250 PHE   B CD2 
3217 C  CE1 . PHE   B 94  ? 0.4502 0.6818 0.6382 0.2146  0.0702  -0.1565 250 PHE   B CE1 
3218 C  CE2 . PHE   B 94  ? 0.5835 0.7557 0.7357 0.2367  0.0529  -0.1465 250 PHE   B CE2 
3219 C  CZ  . PHE   B 94  ? 0.6022 0.7954 0.7658 0.2271  0.0651  -0.1523 250 PHE   B CZ  
3220 N  N   . VAL   B 95  ? 0.3488 0.6577 0.5963 0.1894  0.0397  -0.1531 251 VAL   B N   
3221 C  CA  . VAL   B 95  ? 0.3638 0.6956 0.6257 0.1864  0.0317  -0.1554 251 VAL   B CA  
3222 C  C   . VAL   B 95  ? 0.5579 0.9155 0.8296 0.2001  0.0253  -0.1635 251 VAL   B C   
3223 O  O   . VAL   B 95  ? 0.4066 0.7894 0.6918 0.1979  0.0325  -0.1715 251 VAL   B O   
3224 C  CB  . VAL   B 95  ? 0.4456 0.8010 0.7265 0.1632  0.0405  -0.1583 251 VAL   B CB  
3225 C  CG1 . VAL   B 95  ? 0.3216 0.7019 0.6176 0.1599  0.0322  -0.1621 251 VAL   B CG1 
3226 C  CG2 . VAL   B 95  ? 0.3217 0.6513 0.5923 0.1506  0.0460  -0.1504 251 VAL   B CG2 
3227 N  N   . LYS   B 96  ? 0.4883 0.8392 0.7520 0.2145  0.0119  -0.1616 252 LYS   B N   
3228 C  CA  . LYS   B 96  ? 0.5004 0.8762 0.7724 0.2280  0.0034  -0.1693 252 LYS   B CA  
3229 C  C   . LYS   B 96  ? 0.5684 0.9608 0.8496 0.2234  -0.0054 -0.1705 252 LYS   B C   
3230 O  O   . LYS   B 96  ? 0.4699 0.8523 0.7501 0.2107  -0.0048 -0.1649 252 LYS   B O   
3231 C  CB  . LYS   B 96  ? 0.4315 0.7801 0.6807 0.2511  -0.0050 -0.1656 252 LYS   B CB  
3232 C  CG  . LYS   B 96  ? 0.6246 0.9531 0.8621 0.2566  0.0030  -0.1645 252 LYS   B CG  
3233 C  CD  . LYS   B 96  ? 0.7364 1.0364 0.9503 0.2787  -0.0057 -0.1611 252 LYS   B CD  
3234 C  CE  . LYS   B 96  ? 0.6026 0.8838 0.8052 0.2844  0.0020  -0.1613 252 LYS   B CE  
3235 N  NZ  . LYS   B 96  ? 0.4702 0.7174 0.6465 0.3042  -0.0058 -0.1569 252 LYS   B NZ  
3236 N  N   . PHE   B 97  ? 0.5001 0.9173 0.7891 0.2346  -0.0141 -0.1782 253 PHE   B N   
3237 C  CA  . PHE   B 97  ? 0.5953 1.0334 0.8950 0.2296  -0.0220 -0.1818 253 PHE   B CA  
3238 C  C   . PHE   B 97  ? 0.6049 1.0360 0.8903 0.2510  -0.0369 -0.1812 253 PHE   B C   
3239 O  O   . PHE   B 97  ? 0.7027 1.1301 0.9791 0.2692  -0.0407 -0.1833 253 PHE   B O   
3240 C  CB  . PHE   B 97  ? 0.4680 0.9522 0.7961 0.2170  -0.0164 -0.1947 253 PHE   B CB  
3241 C  CG  . PHE   B 97  ? 0.4752 0.9653 0.8154 0.1945  -0.0011 -0.1951 253 PHE   B CG  
3242 C  CD1 . PHE   B 97  ? 0.3626 0.8538 0.7045 0.1940  0.0096  -0.1971 253 PHE   B CD1 
3243 C  CD2 . PHE   B 97  ? 0.3259 0.8185 0.6739 0.1739  0.0029  -0.1931 253 PHE   B CD2 
3244 C  CE1 . PHE   B 97  ? 0.3577 0.8522 0.7079 0.1734  0.0241  -0.1969 253 PHE   B CE1 
3245 C  CE2 . PHE   B 97  ? 0.4576 0.9526 0.8138 0.1532  0.0174  -0.1929 253 PHE   B CE2 
3246 C  CZ  . PHE   B 97  ? 0.3496 0.8455 0.7064 0.1530  0.0281  -0.1946 253 PHE   B CZ  
3247 N  N   . LYS   B 98  ? 0.6332 1.0613 0.9152 0.2485  -0.0450 -0.1782 254 LYS   B N   
3248 C  CA  . LYS   B 98  ? 0.7052 1.1265 0.9722 0.2673  -0.0591 -0.1774 254 LYS   B CA  
3249 C  C   . LYS   B 98  ? 0.5661 1.0317 0.8525 0.2710  -0.0646 -0.1913 254 LYS   B C   
3250 O  O   . LYS   B 98  ? 0.7959 1.2640 1.0729 0.2867  -0.0765 -0.1934 254 LYS   B O   
3251 C  CB  . LYS   B 98  ? 0.5237 0.9215 0.7769 0.2632  -0.0652 -0.1681 254 LYS   B CB  
3252 N  N   . ASN   B 104 ? 0.3688 1.0745 0.8226 0.1511  -0.0107 -0.2663 260 ASN   B N   
3253 C  CA  . ASN   B 104 ? 0.5328 1.2053 0.9752 0.1425  -0.0003 -0.2535 260 ASN   B CA  
3254 C  C   . ASN   B 104 ? 0.5039 1.1914 0.9613 0.1191  0.0167  -0.2586 260 ASN   B C   
3255 O  O   . ASN   B 104 ? 0.5196 1.2266 0.9862 0.1218  0.0229  -0.2661 260 ASN   B O   
3256 C  CB  . ASN   B 104 ? 0.4308 1.0815 0.8569 0.1644  -0.0032 -0.2464 260 ASN   B CB  
3257 C  CG  . ASN   B 104 ? 0.5937 1.2065 1.0047 0.1580  0.0056  -0.2327 260 ASN   B CG  
3258 O  OD1 . ASN   B 104 ? 0.7627 1.3498 1.1565 0.1746  0.0023  -0.2250 260 ASN   B OD1 
3259 N  ND2 . ASN   B 104 ? 0.5530 1.1612 0.9691 0.1342  0.0166  -0.2298 260 ASN   B ND2 
3260 N  N   . PRO   B 105 ? 0.3215 0.9984 0.7799 0.0962  0.0245  -0.2545 261 PRO   B N   
3261 C  CA  . PRO   B 105 ? 0.3879 1.0744 0.8569 0.0727  0.0415  -0.2584 261 PRO   B CA  
3262 C  C   . PRO   B 105 ? 0.4606 1.1274 0.9204 0.0723  0.0528  -0.2507 261 PRO   B C   
3263 O  O   . PRO   B 105 ? 0.5802 1.2576 1.0480 0.0569  0.0668  -0.2550 261 PRO   B O   
3264 C  CB  . PRO   B 105 ? 0.5013 1.1738 0.9683 0.0513  0.0449  -0.2540 261 PRO   B CB  
3265 C  CG  . PRO   B 105 ? 0.6288 1.2724 1.0791 0.0640  0.0332  -0.2425 261 PRO   B CG  
3266 C  CD  . PRO   B 105 ? 0.3232 0.9774 0.7715 0.0910  0.0185  -0.2460 261 PRO   B CD  
3267 N  N   . LEU   B 106 ? 0.5010 1.1387 0.9433 0.0885  0.0477  -0.2398 262 LEU   B N   
3268 C  CA  . LEU   B 106 ? 0.3558 0.9736 0.7876 0.0904  0.0574  -0.2329 262 LEU   B CA  
3269 C  C   . LEU   B 106 ? 0.3964 1.0273 0.8298 0.1104  0.0551  -0.2386 262 LEU   B C   
3270 O  O   . LEU   B 106 ? 0.5253 1.1388 0.9484 0.1153  0.0619  -0.2334 262 LEU   B O   
3271 C  CB  . LEU   B 106 ? 0.3189 0.8959 0.7296 0.0959  0.0540  -0.2185 262 LEU   B CB  
3272 C  CG  . LEU   B 106 ? 0.3572 0.9173 0.7642 0.0762  0.0577  -0.2117 262 LEU   B CG  
3273 C  CD1 . LEU   B 106 ? 0.4017 0.9234 0.7886 0.0827  0.0547  -0.1984 262 LEU   B CD1 
3274 C  CD2 . LEU   B 106 ? 0.4872 1.0529 0.9007 0.0516  0.0745  -0.2138 262 LEU   B CD2 
3275 N  N   . SER   B 107 ? 0.4666 1.1274 0.9119 0.1222  0.0457  -0.2496 263 SER   B N   
3276 C  CA  . SER   B 107 ? 0.3496 1.0229 0.7959 0.1431  0.0422  -0.2554 263 SER   B CA  
3277 C  C   . SER   B 107 ? 0.4026 1.0926 0.8589 0.1340  0.0571  -0.2616 263 SER   B C   
3278 O  O   . SER   B 107 ? 0.5174 1.2095 0.9707 0.1502  0.0571  -0.2638 263 SER   B O   
3279 C  CB  . SER   B 107 ? 0.4966 1.2009 0.9540 0.1566  0.0289  -0.2668 263 SER   B CB  
3280 O  OG  . SER   B 107 ? 0.6267 1.3687 1.1064 0.1401  0.0346  -0.2799 263 SER   B OG  
3281 N  N   . GLN   B 108 ? 0.4757 1.1759 0.9424 0.1086  0.0701  -0.2643 264 GLN   B N   
3282 C  CA  . GLN   B 108 ? 0.3957 1.1087 0.8696 0.0980  0.0857  -0.2691 264 GLN   B CA  
3283 C  C   . GLN   B 108 ? 0.4484 1.1277 0.9039 0.0987  0.0948  -0.2577 264 GLN   B C   
3284 O  O   . GLN   B 108 ? 0.4372 1.1242 0.8949 0.0970  0.1058  -0.2611 264 GLN   B O   
3285 C  CB  . GLN   B 108 ? 0.3574 1.0866 0.8443 0.0697  0.0972  -0.2746 264 GLN   B CB  
3286 C  CG  . GLN   B 108 ? 0.3755 1.0730 0.8500 0.0513  0.1028  -0.2629 264 GLN   B CG  
3287 C  CD  . GLN   B 108 ? 0.4273 1.1367 0.9117 0.0236  0.1146  -0.2680 264 GLN   B CD  
3288 O  OE1 . GLN   B 108 ? 0.5009 1.2125 0.9862 0.0095  0.1297  -0.2695 264 GLN   B OE1 
3289 N  NE2 . GLN   B 108 ? 0.3407 1.0561 0.8311 0.0155  0.1080  -0.2709 264 GLN   B NE2 
3290 N  N   . PHE   B 109 ? 0.4042 1.0473 0.8416 0.1009  0.0909  -0.2449 265 PHE   B N   
3291 C  CA  . PHE   B 109 ? 0.3442 0.9540 0.7625 0.1030  0.0981  -0.2344 265 PHE   B CA  
3292 C  C   . PHE   B 109 ? 0.4814 1.0724 0.8855 0.1296  0.0876  -0.2303 265 PHE   B C   
3293 O  O   . PHE   B 109 ? 0.5171 1.0774 0.9033 0.1334  0.0918  -0.2217 265 PHE   B O   
3294 C  CB  . PHE   B 109 ? 0.3617 0.9416 0.7677 0.0872  0.1019  -0.2230 265 PHE   B CB  
3295 C  CG  . PHE   B 109 ? 0.3716 0.9641 0.7884 0.0616  0.1103  -0.2259 265 PHE   B CG  
3296 C  CD1 . PHE   B 109 ? 0.3402 0.9459 0.7634 0.0454  0.1255  -0.2307 265 PHE   B CD1 
3297 C  CD2 . PHE   B 109 ? 0.4248 1.0137 0.8436 0.0535  0.1034  -0.2237 265 PHE   B CD2 
3298 C  CE1 . PHE   B 109 ? 0.3332 0.9467 0.7637 0.0217  0.1337  -0.2332 265 PHE   B CE1 
3299 C  CE2 . PHE   B 109 ? 0.3461 0.9434 0.7728 0.0299  0.1114  -0.2265 265 PHE   B CE2 
3300 C  CZ  . PHE   B 109 ? 0.3804 0.9891 0.8124 0.0138  0.1266  -0.2312 265 PHE   B CZ  
3301 N  N   . LEU   B 110 ? 0.5407 1.1473 0.9504 0.1480  0.0742  -0.2363 266 LEU   B N   
3302 C  CA  . LEU   B 110 ? 0.5484 1.1325 0.9413 0.1732  0.0633  -0.2316 266 LEU   B CA  
3303 C  C   . LEU   B 110 ? 0.4992 1.0848 0.8888 0.1852  0.0692  -0.2353 266 LEU   B C   
3304 O  O   . LEU   B 110 ? 0.6777 1.2968 1.0835 0.1872  0.0717  -0.2466 266 LEU   B O   
3305 C  CB  . LEU   B 110 ? 0.4674 1.0665 0.8650 0.1889  0.0468  -0.2365 266 LEU   B CB  
3306 C  CG  . LEU   B 110 ? 0.6353 1.2098 1.0197 0.1932  0.0349  -0.2275 266 LEU   B CG  
3307 C  CD1 . LEU   B 110 ? 0.5390 1.1359 0.9308 0.2053  0.0204  -0.2348 266 LEU   B CD1 
3308 C  CD2 . LEU   B 110 ? 0.6526 1.1836 1.0110 0.2083  0.0310  -0.2161 266 LEU   B CD2 
3309 N  N   . GLU   B 111 ? 0.5783 1.1276 0.9467 0.1933  0.0712  -0.2263 267 GLU   B N   
3310 C  CA  . GLU   B 111 ? 0.6320 1.1753 0.9925 0.2084  0.0745  -0.2288 267 GLU   B CA  
3311 C  C   . GLU   B 111 ? 0.7243 1.2459 1.0687 0.2334  0.0598  -0.2255 267 GLU   B C   
3312 O  O   . GLU   B 111 ? 0.6837 1.1659 1.0063 0.2388  0.0565  -0.2152 267 GLU   B O   
3313 C  CB  . GLU   B 111 ? 0.5252 1.0416 0.8713 0.1991  0.0877  -0.2219 267 GLU   B CB  
3314 N  N   . GLY   B 112 ? 0.6181 1.1650 0.9721 0.2487  0.0508  -0.2344 268 GLY   B N   
3315 C  CA  . GLY   B 112 ? 0.5703 1.0989 0.9087 0.2719  0.0357  -0.2316 268 GLY   B CA  
3316 C  C   . GLY   B 112 ? 0.6194 1.1383 0.9535 0.2694  0.0250  -0.2255 268 GLY   B C   
3317 O  O   . GLY   B 112 ? 0.6011 1.1507 0.9530 0.2619  0.0212  -0.2317 268 GLY   B O   
3318 N  N   . GLU   B 113 ? 0.6682 1.1439 0.9783 0.2747  0.0205  -0.2136 269 GLU   B N   
3319 C  CA  . GLU   B 113 ? 0.7073 1.1694 1.0104 0.2730  0.0105  -0.2067 269 GLU   B CA  
3320 C  C   . GLU   B 113 ? 0.6604 1.1012 0.9589 0.2537  0.0177  -0.1976 269 GLU   B C   
3321 O  O   . GLU   B 113 ? 0.6239 1.0482 0.9141 0.2517  0.0105  -0.1906 269 GLU   B O   
3322 C  CB  . GLU   B 113 ? 0.6618 1.0903 0.9391 0.2954  -0.0018 -0.2002 269 GLU   B CB  
3323 C  CG  . GLU   B 113 ? 0.7822 1.2324 1.0627 0.3155  -0.0125 -0.2088 269 GLU   B CG  
3324 C  CD  . GLU   B 113 ? 0.9561 1.4089 1.2328 0.3220  -0.0264 -0.2076 269 GLU   B CD  
3325 O  OE1 . GLU   B 113 ? 0.8219 1.2396 1.0786 0.3228  -0.0314 -0.1966 269 GLU   B OE1 
3326 O  OE2 . GLU   B 113 ? 0.8075 1.2982 1.1010 0.3263  -0.0321 -0.2182 269 GLU   B OE2 
3327 N  N   . ILE   B 114 ? 0.5610 1.0021 0.8638 0.2399  0.0318  -0.1978 270 ILE   B N   
3328 C  CA  . ILE   B 114 ? 0.6513 1.0693 0.9466 0.2232  0.0396  -0.1893 270 ILE   B CA  
3329 C  C   . ILE   B 114 ? 0.6122 1.0596 0.9286 0.2000  0.0509  -0.1942 270 ILE   B C   
3330 O  O   . ILE   B 114 ? 0.5543 1.0297 0.8854 0.1960  0.0586  -0.2029 270 ILE   B O   
3331 C  CB  . ILE   B 114 ? 0.5543 0.9388 0.8296 0.2276  0.0467  -0.1841 270 ILE   B CB  
3332 C  CG1 . ILE   B 114 ? 0.5753 0.9182 0.8245 0.2436  0.0364  -0.1754 270 ILE   B CG1 
3333 C  CG2 . ILE   B 114 ? 0.5351 0.9118 0.8101 0.2071  0.0598  -0.1803 270 ILE   B CG2 
3334 C  CD1 . ILE   B 114 ? 0.5981 0.9174 0.8298 0.2577  0.0386  -0.1752 270 ILE   B CD1 
3335 N  N   . LEU   B 115 ? 0.5278 0.9677 0.8448 0.1842  0.0521  -0.1886 271 LEU   B N   
3336 C  CA  . LEU   B 115 ? 0.4586 0.9199 0.7918 0.1605  0.0633  -0.1919 271 LEU   B CA  
3337 C  C   . LEU   B 115 ? 0.4790 0.9283 0.8054 0.1503  0.0784  -0.1895 271 LEU   B C   
3338 O  O   . LEU   B 115 ? 0.5808 0.9970 0.8884 0.1516  0.0802  -0.1813 271 LEU   B O   
3339 C  CB  . LEU   B 115 ? 0.3033 0.7567 0.6369 0.1476  0.0597  -0.1862 271 LEU   B CB  
3340 C  CG  . LEU   B 115 ? 0.5144 0.9834 0.8613 0.1216  0.0707  -0.1881 271 LEU   B CG  
3341 C  CD1 . LEU   B 115 ? 0.4907 0.9999 0.8600 0.1155  0.0712  -0.1997 271 LEU   B CD1 
3342 C  CD2 . LEU   B 115 ? 0.3090 0.7606 0.6507 0.1112  0.0672  -0.1806 271 LEU   B CD2 
3343 N  N   . SER   B 116 ? 0.3944 0.8700 0.7347 0.1399  0.0893  -0.1970 272 SER   B N   
3344 C  CA  . SER   B 116 ? 0.4257 0.8916 0.7584 0.1304  0.1042  -0.1953 272 SER   B CA  
3345 C  C   . SER   B 116 ? 0.4327 0.8888 0.7630 0.1069  0.1135  -0.1896 272 SER   B C   
3346 O  O   . SER   B 116 ? 0.3960 0.8732 0.7409 0.0903  0.1175  -0.1932 272 SER   B O   
3347 C  CB  . SER   B 116 ? 0.5176 1.0142 0.8645 0.1290  0.1126  -0.2054 272 SER   B CB  
3348 O  OG  . SER   B 116 ? 0.4480 0.9367 0.7876 0.1163  0.1281  -0.2035 272 SER   B OG  
3349 N  N   . ALA   B 117 ? 0.4161 0.8391 0.7267 0.1053  0.1169  -0.1809 273 ALA   B N   
3350 C  CA  . ALA   B 117 ? 0.3764 0.7876 0.6816 0.0836  0.1271  -0.1753 273 ALA   B CA  
3351 C  C   . ALA   B 117 ? 0.4946 0.9212 0.8049 0.0679  0.1426  -0.1792 273 ALA   B C   
3352 O  O   . ALA   B 117 ? 0.3774 0.8078 0.6915 0.0475  0.1502  -0.1778 273 ALA   B O   
3353 C  CB  . ALA   B 117 ? 0.4261 0.7997 0.7081 0.0866  0.1279  -0.1666 273 ALA   B CB  
3354 N  N   . SER   B 118 ? 0.3887 0.8230 0.6981 0.0773  0.1474  -0.1841 274 SER   B N   
3355 C  CA  . SER   B 118 ? 0.4972 0.9443 0.8091 0.0634  0.1626  -0.1875 274 SER   B CA  
3356 C  C   . SER   B 118 ? 0.5033 0.9841 0.8377 0.0507  0.1650  -0.1953 274 SER   B C   
3357 O  O   . SER   B 118 ? 0.5215 1.0040 0.8562 0.0298  0.1764  -0.1943 274 SER   B O   
3358 C  CB  . SER   B 118 ? 0.3973 0.8468 0.7043 0.0782  0.1661  -0.1919 274 SER   B CB  
3359 O  OG  . SER   B 118 ? 0.5499 0.9660 0.8335 0.0859  0.1667  -0.1851 274 SER   B OG  
3360 N  N   . LYS   B 119 ? 0.3895 0.8959 0.7413 0.0631  0.1543  -0.2033 275 LYS   B N   
3361 C  CA  . LYS   B 119 ? 0.4290 0.9698 0.8027 0.0518  0.1561  -0.2126 275 LYS   B CA  
3362 C  C   . LYS   B 119 ? 0.4204 0.9573 0.7975 0.0340  0.1546  -0.2093 275 LYS   B C   
3363 O  O   . LYS   B 119 ? 0.4639 1.0128 0.8485 0.0138  0.1642  -0.2126 275 LYS   B O   
3364 C  CB  . LYS   B 119 ? 0.3661 0.9340 0.7555 0.0711  0.1436  -0.2221 275 LYS   B CB  
3365 C  CG  . LYS   B 119 ? 0.4137 0.9851 0.7998 0.0898  0.1445  -0.2260 275 LYS   B CG  
3366 C  CD  . LYS   B 119 ? 0.4933 1.1039 0.9004 0.0991  0.1399  -0.2392 275 LYS   B CD  
3367 C  CE  . LYS   B 119 ? 0.4142 1.0311 0.8193 0.1117  0.1457  -0.2440 275 LYS   B CE  
3368 N  NZ  . LYS   B 119 ? 0.5618 1.2005 0.9773 0.1341  0.1338  -0.2530 275 LYS   B NZ  
3369 N  N   . MET   B 120 ? 0.4460 0.9649 0.8164 0.0413  0.1429  -0.2029 276 MET   B N   
3370 C  CA  . MET   B 120 ? 0.4599 0.9724 0.8319 0.0255  0.1411  -0.1992 276 MET   B CA  
3371 C  C   . MET   B 120 ? 0.3120 0.8027 0.6706 0.0039  0.1555  -0.1920 276 MET   B C   
3372 O  O   . MET   B 120 ? 0.3235 0.8194 0.6875 -0.0157 0.1613  -0.1933 276 MET   B O   
3373 C  CB  . MET   B 120 ? 0.2891 0.7827 0.6535 0.0385  0.1268  -0.1926 276 MET   B CB  
3374 C  CG  . MET   B 120 ? 0.3297 0.8332 0.7047 0.0317  0.1180  -0.1945 276 MET   B CG  
3375 S  SD  . MET   B 120 ? 0.3791 0.8603 0.7441 0.0478  0.1013  -0.1867 276 MET   B SD  
3376 C  CE  . MET   B 120 ? 0.2577 0.7454 0.6317 0.0297  0.0981  -0.1874 276 MET   B CE  
3377 N  N   . LEU   B 121 ? 0.3487 0.8136 0.6883 0.0072  0.1615  -0.1844 277 LEU   B N   
3378 C  CA  . LEU   B 121 ? 0.5636 1.0055 0.8870 -0.0118 0.1751  -0.1770 277 LEU   B CA  
3379 C  C   . LEU   B 121 ? 0.5080 0.9664 0.8370 -0.0269 0.1890  -0.1827 277 LEU   B C   
3380 O  O   . LEU   B 121 ? 0.4764 0.9250 0.7996 -0.0473 0.1982  -0.1795 277 LEU   B O   
3381 C  CB  . LEU   B 121 ? 0.4647 0.8773 0.7658 -0.0035 0.1780  -0.1692 277 LEU   B CB  
3382 C  CG  . LEU   B 121 ? 0.4624 0.8489 0.7520 0.0040  0.1684  -0.1612 277 LEU   B CG  
3383 C  CD1 . LEU   B 121 ? 0.2998 0.6621 0.5694 0.0154  0.1703  -0.1567 277 LEU   B CD1 
3384 C  CD2 . LEU   B 121 ? 0.3707 0.7395 0.6531 -0.0149 0.1719  -0.1541 277 LEU   B CD2 
3385 N  N   . SER   B 122 ? 0.3380 0.8195 0.6768 -0.0170 0.1911  -0.1909 278 SER   B N   
3386 C  CA  . SER   B 122 ? 0.4460 0.9452 0.7911 -0.0309 0.2046  -0.1971 278 SER   B CA  
3387 C  C   . SER   B 122 ? 0.4789 0.9967 0.8399 -0.0478 0.2053  -0.2032 278 SER   B C   
3388 O  O   . SER   B 122 ? 0.4589 0.9704 0.8144 -0.0684 0.2178  -0.2021 278 SER   B O   
3389 C  CB  . SER   B 122 ? 0.4487 0.9739 0.8052 -0.0152 0.2043  -0.2065 278 SER   B CB  
3390 O  OG  . SER   B 122 ? 0.7118 1.2201 1.0507 -0.0103 0.2129  -0.2021 278 SER   B OG  
3391 N  N   . LYS   B 123 ? 0.4134 0.9517 0.7920 -0.0392 0.1919  -0.2095 279 LYS   B N   
3392 C  CA  . LYS   B 123 ? 0.4579 1.0139 0.8511 -0.0548 0.1917  -0.2163 279 LYS   B CA  
3393 C  C   . LYS   B 123 ? 0.3483 0.8744 0.7274 -0.0722 0.1946  -0.2069 279 LYS   B C   
3394 O  O   . LYS   B 123 ? 0.4151 0.9416 0.7951 -0.0927 0.2038  -0.2092 279 LYS   B O   
3395 C  CB  . LYS   B 123 ? 0.4230 1.0061 0.8357 -0.0402 0.1756  -0.2249 279 LYS   B CB  
3396 C  CG  . LYS   B 123 ? 0.3466 0.9460 0.7729 -0.0552 0.1737  -0.2319 279 LYS   B CG  
3397 C  CD  . LYS   B 123 ? 0.3545 0.9970 0.8048 -0.0475 0.1678  -0.2472 279 LYS   B CD  
3398 C  CE  . LYS   B 123 ? 0.5374 1.1960 1.0007 -0.0607 0.1641  -0.2550 279 LYS   B CE  
3399 N  NZ  . LYS   B 123 ? 0.3589 1.0557 0.8430 -0.0467 0.1519  -0.2682 279 LYS   B NZ  
3400 N  N   . PHE   B 124 ? 0.3401 0.8393 0.7055 -0.0640 0.1870  -0.1966 280 PHE   B N   
3401 C  CA  . PHE   B 124 ? 0.3879 0.8566 0.7383 -0.0785 0.1891  -0.1870 280 PHE   B CA  
3402 C  C   . PHE   B 124 ? 0.4119 0.8599 0.7452 -0.0978 0.2061  -0.1818 280 PHE   B C   
3403 O  O   . PHE   B 124 ? 0.3786 0.8198 0.7096 -0.1166 0.2122  -0.1818 280 PHE   B O   
3404 C  CB  . PHE   B 124 ? 0.3829 0.8264 0.7198 -0.0646 0.1800  -0.1770 280 PHE   B CB  
3405 C  CG  . PHE   B 124 ? 0.3566 0.7700 0.6792 -0.0762 0.1796  -0.1673 280 PHE   B CG  
3406 C  CD1 . PHE   B 124 ? 0.2973 0.7162 0.6295 -0.0804 0.1708  -0.1694 280 PHE   B CD1 
3407 C  CD2 . PHE   B 124 ? 0.3080 0.6871 0.6066 -0.0811 0.1871  -0.1562 280 PHE   B CD2 
3408 C  CE1 . PHE   B 124 ? 0.3040 0.6947 0.6228 -0.0900 0.1701  -0.1606 280 PHE   B CE1 
3409 C  CE2 . PHE   B 124 ? 0.3036 0.6545 0.5885 -0.0903 0.1862  -0.1473 280 PHE   B CE2 
3410 C  CZ  . PHE   B 124 ? 0.4608 0.8176 0.7562 -0.0948 0.1778  -0.1494 280 PHE   B CZ  
3411 N  N   . ARG   B 125 ? 0.4676 0.9045 0.7874 -0.0928 0.2140  -0.1776 281 ARG   B N   
3412 C  CA  . ARG   B 125 ? 0.4153 0.8303 0.7156 -0.1094 0.2298  -0.1719 281 ARG   B CA  
3413 C  C   . ARG   B 125 ? 0.4219 0.8594 0.7338 -0.1239 0.2405  -0.1814 281 ARG   B C   
3414 O  O   . ARG   B 125 ? 0.4494 0.8685 0.7477 -0.1424 0.2521  -0.1777 281 ARG   B O   
3415 C  CB  . ARG   B 125 ? 0.5945 0.9929 0.8763 -0.1001 0.2354  -0.1657 281 ARG   B CB  
3416 C  CG  . ARG   B 125 ? 0.6599 1.0496 0.9375 -0.0798 0.2242  -0.1616 281 ARG   B CG  
3417 C  CD  . ARG   B 125 ? 0.5726 0.9520 0.8346 -0.0707 0.2307  -0.1589 281 ARG   B CD  
3418 N  NE  . ARG   B 125 ? 0.7559 1.1056 0.9920 -0.0849 0.2434  -0.1500 281 ARG   B NE  
3419 C  CZ  . ARG   B 125 ? 0.6896 1.0421 0.9195 -0.0943 0.2568  -0.1516 281 ARG   B CZ  
3420 N  NH1 . ARG   B 125 ? 0.7204 1.1055 0.9695 -0.0923 0.2601  -0.1624 281 ARG   B NH1 
3421 N  NH2 . ARG   B 125 ? 0.7511 1.0725 0.9541 -0.1058 0.2669  -0.1423 281 ARG   B NH2 
3422 N  N   . LYS   B 126 ? 0.3951 0.8710 0.7309 -0.1158 0.2373  -0.1938 282 LYS   B N   
3423 C  CA  . LYS   B 126 ? 0.4159 0.9157 0.7644 -0.1303 0.2475  -0.2042 282 LYS   B CA  
3424 C  C   . LYS   B 126 ? 0.4418 0.9396 0.7948 -0.1485 0.2479  -0.2067 282 LYS   B C   
3425 O  O   . LYS   B 126 ? 0.4854 0.9737 0.8305 -0.1683 0.2610  -0.2070 282 LYS   B O   
3426 C  CB  . LYS   B 126 ? 0.4421 0.9850 0.8166 -0.1161 0.2415  -0.2176 282 LYS   B CB  
3427 C  CG  . LYS   B 126 ? 0.5154 1.0815 0.8985 -0.1246 0.2547  -0.2270 282 LYS   B CG  
3428 C  CD  . LYS   B 126 ? 0.4416 1.0536 0.8545 -0.1171 0.2475  -0.2428 282 LYS   B CD  
3429 C  CE  . LYS   B 126 ? 0.6615 1.2956 1.0810 -0.1147 0.2577  -0.2503 282 LYS   B CE  
3430 N  NZ  . LYS   B 126 ? 0.6832 1.2964 1.0854 -0.1362 0.2759  -0.2453 282 LYS   B NZ  
3431 N  N   . ILE   B 127 ? 0.4853 0.9908 0.8498 -0.1416 0.2335  -0.2087 283 ILE   B N   
3432 C  CA  . ILE   B 127 ? 0.4072 0.9096 0.7751 -0.1575 0.2326  -0.2112 283 ILE   B CA  
3433 C  C   . ILE   B 127 ? 0.4995 0.9576 0.8400 -0.1726 0.2412  -0.1985 283 ILE   B C   
3434 O  O   . ILE   B 127 ? 0.5474 0.9970 0.8829 -0.1922 0.2509  -0.2004 283 ILE   B O   
3435 C  CB  . ILE   B 127 ? 0.4568 0.9714 0.8383 -0.1449 0.2147  -0.2138 283 ILE   B CB  
3436 C  CG1 . ILE   B 127 ? 0.4708 1.0249 0.8751 -0.1259 0.2050  -0.2248 283 ILE   B CG1 
3437 C  CG2 . ILE   B 127 ? 0.3914 0.9077 0.7786 -0.1609 0.2139  -0.2187 283 ILE   B CG2 
3438 C  CD1 . ILE   B 127 ? 0.6276 1.2024 1.0487 -0.1175 0.1891  -0.2317 283 ILE   B CD1 
3439 N  N   . ILE   B 128 ? 0.5242 0.9525 0.8456 -0.1634 0.2378  -0.1857 284 ILE   B N   
3440 C  CA  . ILE   B 128 ? 0.4152 0.8002 0.7089 -0.1757 0.2447  -0.1732 284 ILE   B CA  
3441 C  C   . ILE   B 128 ? 0.5282 0.8999 0.8062 -0.1904 0.2622  -0.1716 284 ILE   B C   
3442 O  O   . ILE   B 128 ? 0.4662 0.8137 0.7290 -0.2072 0.2703  -0.1679 284 ILE   B O   
3443 C  CB  . ILE   B 128 ? 0.4944 0.8524 0.7709 -0.1621 0.2378  -0.1608 284 ILE   B CB  
3444 C  CG1 . ILE   B 128 ? 0.4681 0.8247 0.7519 -0.1557 0.2231  -0.1594 284 ILE   B CG1 
3445 C  CG2 . ILE   B 128 ? 0.4147 0.7295 0.6590 -0.1722 0.2481  -0.1480 284 ILE   B CG2 
3446 C  CD1 . ILE   B 128 ? 0.3572 0.7129 0.6413 -0.1355 0.2121  -0.1551 284 ILE   B CD1 
3447 N  N   . LYS   B 129 ? 0.4507 0.8369 0.7311 -0.1839 0.2683  -0.1745 285 LYS   B N   
3448 C  CA  . LYS   B 129 ? 0.5532 0.9268 0.8177 -0.1971 0.2851  -0.1727 285 LYS   B CA  
3449 C  C   . LYS   B 129 ? 0.6574 1.0462 0.9330 -0.2162 0.2940  -0.1829 285 LYS   B C   
3450 O  O   . LYS   B 129 ? 0.7343 1.0973 0.9905 -0.2330 0.3063  -0.1786 285 LYS   B O   
3451 C  CB  . LYS   B 129 ? 0.4810 0.8719 0.7489 -0.1852 0.2891  -0.1755 285 LYS   B CB  
3452 C  CG  . LYS   B 129 ? 0.7173 1.0991 0.9702 -0.1981 0.3067  -0.1747 285 LYS   B CG  
3453 C  CD  . LYS   B 129 ? 0.8395 1.2045 1.0723 -0.1867 0.3104  -0.1663 285 LYS   B CD  
3454 C  CE  . LYS   B 129 ? 0.8298 1.2295 1.0828 -0.1688 0.3056  -0.1748 285 LYS   B CE  
3455 N  NZ  . LYS   B 129 ? 0.8538 1.2356 1.0888 -0.1527 0.3031  -0.1665 285 LYS   B NZ  
3456 N  N   . GLU   B 130 ? 0.6067 1.0367 0.9125 -0.2137 0.2879  -0.1969 286 GLU   B N   
3457 C  CA  . GLU   B 130 ? 0.6520 1.0988 0.9697 -0.2324 0.2962  -0.2081 286 GLU   B CA  
3458 C  C   . GLU   B 130 ? 0.5865 1.0067 0.8929 -0.2468 0.2959  -0.2042 286 GLU   B C   
3459 O  O   . GLU   B 130 ? 0.6048 1.0155 0.9040 -0.2664 0.3082  -0.2072 286 GLU   B O   
3460 C  CB  . GLU   B 130 ? 0.5241 1.0218 0.8763 -0.2251 0.2883  -0.2244 286 GLU   B CB  
3461 C  CG  . GLU   B 130 ? 0.6450 1.1710 1.0088 -0.2138 0.2915  -0.2306 286 GLU   B CG  
3462 C  CD  . GLU   B 130 ? 0.8473 1.4237 1.2441 -0.2082 0.2850  -0.2478 286 GLU   B CD  
3463 O  OE1 . GLU   B 130 ? 0.8499 1.4396 1.2603 -0.2139 0.2783  -0.2553 286 GLU   B OE1 
3464 O  OE2 . GLU   B 130 ? 0.7899 1.3926 1.1983 -0.1975 0.2865  -0.2542 286 GLU   B OE2 
3465 N  N   . GLU   B 131 ? 0.5376 0.9441 0.8411 -0.2374 0.2825  -0.1975 287 GLU   B N   
3466 C  CA  . GLU   B 131 ? 0.5890 0.9681 0.8801 -0.2499 0.2819  -0.1932 287 GLU   B CA  
3467 C  C   . GLU   B 131 ? 0.6846 1.0146 0.9404 -0.2591 0.2927  -0.1792 287 GLU   B C   
3468 O  O   . GLU   B 131 ? 0.8783 1.1866 1.1210 -0.2759 0.3009  -0.1785 287 GLU   B O   
3469 C  CB  . GLU   B 131 ? 0.5459 0.9252 0.8440 -0.2366 0.2645  -0.1902 287 GLU   B CB  
3470 C  CG  . GLU   B 131 ? 0.6423 0.9949 0.9287 -0.2476 0.2626  -0.1862 287 GLU   B CG  
3471 C  CD  . GLU   B 131 ? 0.7488 1.1247 1.0531 -0.2614 0.2645  -0.2002 287 GLU   B CD  
3472 O  OE1 . GLU   B 131 ? 0.8003 1.2184 1.1305 -0.2585 0.2625  -0.2136 287 GLU   B OE1 
3473 O  OE2 . GLU   B 131 ? 0.6297 0.9817 0.9215 -0.2748 0.2679  -0.1981 287 GLU   B OE2 
3474 N  N   . ILE   B 132 ? 0.7073 1.0187 0.9462 -0.2476 0.2927  -0.1682 288 ILE   B N   
3475 C  CA  . ILE   B 132 ? 0.8046 1.0694 1.0081 -0.2531 0.3016  -0.1544 288 ILE   B CA  
3476 C  C   . ILE   B 132 ? 0.8393 1.0959 1.0313 -0.2709 0.3193  -0.1571 288 ILE   B C   
3477 O  O   . ILE   B 132 ? 0.9252 1.1425 1.0892 -0.2815 0.3273  -0.1486 288 ILE   B O   
3478 C  CB  . ILE   B 132 ? 0.7498 1.0046 0.9413 -0.2360 0.2979  -0.1448 288 ILE   B CB  
3479 C  CG1 . ILE   B 132 ? 0.5791 0.8281 0.7732 -0.2216 0.2819  -0.1391 288 ILE   B CG1 
3480 C  CG2 . ILE   B 132 ? 0.7984 1.0130 0.9547 -0.2411 0.3095  -0.1330 288 ILE   B CG2 
3481 C  CD1 . ILE   B 132 ? 0.8055 1.0243 0.9856 -0.2291 0.2784  -0.1326 288 ILE   B CD1 
3482 N  N   . ASN   B 133 ? 0.9234 1.2163 1.1362 -0.2741 0.3256  -0.1692 289 ASN   B N   
3483 C  CA  . ASN   B 133 ? 0.8350 1.1227 1.0378 -0.2908 0.3433  -0.1723 289 ASN   B CA  
3484 C  C   . ASN   B 133 ? 0.9139 1.1913 1.1140 -0.3112 0.3503  -0.1775 289 ASN   B C   
3485 O  O   . ASN   B 133 ? 0.9292 1.1881 1.1119 -0.3267 0.3658  -0.1768 289 ASN   B O   
3486 C  CB  . ASN   B 133 ? 0.8212 1.1539 1.0492 -0.2879 0.3474  -0.1850 289 ASN   B CB  
3487 C  CG  . ASN   B 133 ? 0.9273 1.2616 1.1491 -0.2711 0.3464  -0.1788 289 ASN   B CG  
3488 O  OD1 . ASN   B 133 ? 0.8872 1.1850 1.0805 -0.2665 0.3479  -0.1651 289 ASN   B OD1 
3489 N  ND2 . ASN   B 133 ? 0.8158 1.1924 1.0637 -0.2613 0.3437  -0.1894 289 ASN   B ND2 
3490 N  N   . ASP   B 134 ? 0.9450 1.2329 1.1607 -0.3117 0.3398  -0.1828 290 ASP   B N   
3491 C  CA  . ASP   B 134 ? 0.9687 1.2452 1.1808 -0.3304 0.3457  -0.1879 290 ASP   B CA  
3492 C  C   . ASP   B 134 ? 1.0611 1.2871 1.2425 -0.3315 0.3435  -0.1737 290 ASP   B C   
3493 O  O   . ASP   B 134 ? 1.3038 1.4985 1.4632 -0.3468 0.3548  -0.1709 290 ASP   B O   
3494 C  CB  . ASP   B 134 ? 0.9096 1.2264 1.1552 -0.3307 0.3358  -0.2025 290 ASP   B CB  
3495 C  CG  . ASP   B 134 ? 1.0240 1.3246 1.2641 -0.3468 0.3383  -0.2060 290 ASP   B CG  
3496 O  OD1 . ASP   B 134 ? 1.0427 1.3171 1.2626 -0.3641 0.3533  -0.2046 290 ASP   B OD1 
3497 O  OD2 . ASP   B 134 ? 1.0690 1.3823 1.3239 -0.3421 0.3256  -0.2101 290 ASP   B OD2 
3498 N  N   . VAL   B 140 ? 0.8265 0.8695 0.8568 -0.2782 0.3378  -0.0958 296 VAL   B N   
3499 C  CA  . VAL   B 140 ? 0.8036 0.8622 0.8448 -0.2599 0.3254  -0.0932 296 VAL   B CA  
3500 C  C   . VAL   B 140 ? 0.8053 0.8889 0.8553 -0.2546 0.3310  -0.0973 296 VAL   B C   
3501 O  O   . VAL   B 140 ? 0.9748 1.0787 1.0359 -0.2649 0.3416  -0.1062 296 VAL   B O   
3502 C  CB  . VAL   B 140 ? 0.7481 0.8368 0.8212 -0.2550 0.3119  -0.1009 296 VAL   B CB  
3503 C  CG1 . VAL   B 140 ? 0.9480 1.0078 1.0081 -0.2544 0.3036  -0.0936 296 VAL   B CG1 
3504 C  CG2 . VAL   B 140 ? 0.7536 0.8761 0.8541 -0.2678 0.3165  -0.1157 296 VAL   B CG2 
3505 N  N   . ILE   B 141 ? 0.7768 0.8586 0.8212 -0.2384 0.3240  -0.0911 297 ILE   B N   
3506 C  CA  . ILE   B 141 ? 0.7621 0.8653 0.8124 -0.2309 0.3283  -0.0943 297 ILE   B CA  
3507 C  C   . ILE   B 141 ? 0.6676 0.7884 0.7320 -0.2123 0.3152  -0.0944 297 ILE   B C   
3508 O  O   . ILE   B 141 ? 0.8163 0.9195 0.8729 -0.2044 0.3049  -0.0872 297 ILE   B O   
3509 C  CB  . ILE   B 141 ? 0.8827 0.9535 0.8975 -0.2318 0.3390  -0.0847 297 ILE   B CB  
3510 N  N   . MET   B 142 ? 0.6994 0.8541 0.7837 -0.2050 0.3159  -0.1026 298 MET   B N   
3511 C  CA  . MET   B 142 ? 0.6869 0.8625 0.7878 -0.1872 0.3041  -0.1051 298 MET   B CA  
3512 C  C   . MET   B 142 ? 0.7314 0.8973 0.8141 -0.1755 0.3067  -0.0999 298 MET   B C   
3513 O  O   . MET   B 142 ? 0.7829 0.9503 0.8569 -0.1793 0.3180  -0.1011 298 MET   B O   
3514 C  CB  . MET   B 142 ? 0.6484 0.8716 0.7869 -0.1847 0.3009  -0.1196 298 MET   B CB  
3515 N  N   . LYS   B 143 ? 0.6154 0.7708 0.6916 -0.1614 0.2964  -0.0944 299 LYS   B N   
3516 C  CA  . LYS   B 143 ? 0.8992 1.0486 0.9609 -0.1482 0.2968  -0.0912 299 LYS   B CA  
3517 C  C   . LYS   B 143 ? 0.8730 1.0560 0.9615 -0.1329 0.2883  -0.1004 299 LYS   B C   
3518 O  O   . LYS   B 143 ? 0.9806 1.1807 1.0918 -0.1292 0.2783  -0.1051 299 LYS   B O   
3519 C  CB  . LYS   B 143 ? 0.6437 0.7547 0.6755 -0.1426 0.2918  -0.0788 299 LYS   B CB  
3520 N  N   . ARG   B 144 ? 0.9241 1.1154 1.0085 -0.1234 0.2921  -0.1032 300 ARG   B N   
3521 C  CA  . ARG   B 144 ? 0.8769 1.0951 0.9817 -0.1065 0.2843  -0.1115 300 ARG   B CA  
3522 C  C   . ARG   B 144 ? 0.8427 1.0395 0.9315 -0.0928 0.2757  -0.1054 300 ARG   B C   
3523 O  O   . ARG   B 144 ? 1.0168 1.1806 1.0762 -0.0955 0.2781  -0.0955 300 ARG   B O   
3524 C  CB  . ARG   B 144 ? 0.7618 1.0003 0.8708 -0.1028 0.2930  -0.1186 300 ARG   B CB  
3525 N  N   . GLY   B 148 ? 0.5890 0.8370 0.7646 -0.0060 0.1983  -0.1275 304 GLY   B N   
3526 C  CA  . GLY   B 148 ? 0.6106 0.8782 0.8092 0.0034  0.1857  -0.1325 304 GLY   B CA  
3527 C  C   . GLY   B 148 ? 0.5205 0.7749 0.7186 -0.0051 0.1772  -0.1248 304 GLY   B C   
3528 O  O   . GLY   B 148 ? 0.4070 0.6854 0.6261 -0.0132 0.1786  -0.1301 304 GLY   B O   
3529 N  N   . SER   B 149 ? 0.5374 0.7564 0.7129 -0.0033 0.1688  -0.1134 305 SER   B N   
3530 C  CA  . SER   B 149 ? 0.5006 0.7068 0.6754 -0.0089 0.1593  -0.1062 305 SER   B CA  
3531 C  C   . SER   B 149 ? 0.7858 0.9908 0.9594 -0.0291 0.1701  -0.1035 305 SER   B C   
3532 O  O   . SER   B 149 ? 0.9573 1.1826 1.1507 -0.0360 0.1695  -0.1083 305 SER   B O   
3533 C  CB  . SER   B 149 ? 0.6114 0.7836 0.7643 -0.0023 0.1484  -0.0961 305 SER   B CB  
3534 O  OG  . SER   B 149 ? 0.9036 1.0655 1.0565 -0.0080 0.1405  -0.0899 305 SER   B OG  
3535 N  N   . PRO   B 150 ? 0.8195 1.0021 0.9707 -0.0391 0.1800  -0.0967 306 PRO   B N   
3536 C  CA  . PRO   B 150 ? 0.7355 0.9163 0.8849 -0.0581 0.1916  -0.0948 306 PRO   B CA  
3537 C  C   . PRO   B 150 ? 0.6028 0.8174 0.7715 -0.0628 0.2049  -0.1067 306 PRO   B C   
3538 O  O   . PRO   B 150 ? 0.8765 1.0843 1.0310 -0.0679 0.2161  -0.1055 306 PRO   B O   
3539 C  CB  . PRO   B 150 ? 0.6916 0.8367 0.8085 -0.0633 0.1968  -0.0839 306 PRO   B CB  
3540 C  CG  . PRO   B 150 ? 0.8896 1.0198 0.9930 -0.0469 0.1866  -0.0807 306 PRO   B CG  
3541 C  CD  . PRO   B 150 ? 0.7074 0.8645 0.8329 -0.0332 0.1807  -0.0906 306 PRO   B CD  
3542 N  N   . ALA   B 151 ? 0.5206 0.7666 0.7167 -0.0595 0.1989  -0.1158 307 ALA   B N   
3543 C  CA  . ALA   B 151 ? 0.5390 0.8146 0.7512 -0.0607 0.2035  -0.1250 307 ALA   B CA  
3544 C  C   . ALA   B 151 ? 0.6858 0.9531 0.8859 -0.0786 0.2176  -0.1224 307 ALA   B C   
3545 O  O   . ALA   B 151 ? 0.6544 0.9322 0.8536 -0.0777 0.2256  -0.1264 307 ALA   B O   
3546 C  CB  . ALA   B 151 ? 0.5269 0.8305 0.7655 -0.0597 0.1943  -0.1326 307 ALA   B CB  
3547 N  N   . VAL   B 152 ? 0.5502 0.7985 0.7405 -0.0937 0.2204  -0.1160 308 VAL   B N   
3548 C  CA  . VAL   B 152 ? 0.5876 0.8266 0.7657 -0.1106 0.2336  -0.1141 308 VAL   B CA  
3549 C  C   . VAL   B 152 ? 0.5627 0.7609 0.7118 -0.1203 0.2374  -0.1017 308 VAL   B C   
3550 O  O   . VAL   B 152 ? 0.5570 0.7420 0.7043 -0.1196 0.2294  -0.0969 308 VAL   B O   
3551 C  CB  . VAL   B 152 ? 0.5105 0.7761 0.7113 -0.1212 0.2346  -0.1232 308 VAL   B CB  
3552 C  CG1 . VAL   B 152 ? 0.5510 0.7949 0.7389 -0.1404 0.2414  -0.1184 308 VAL   B CG1 
3553 C  CG2 . VAL   B 152 ? 0.4383 0.7334 0.6531 -0.1199 0.2413  -0.1330 308 VAL   B CG2 
3554 N  N   . THR   B 153 ? 0.6230 0.8018 0.7492 -0.1276 0.2489  -0.0966 309 THR   B N   
3555 C  CA  . THR   B 153 ? 0.6754 0.8144 0.7716 -0.1361 0.2526  -0.0848 309 THR   B CA  
3556 C  C   . THR   B 153 ? 0.5882 0.7214 0.6785 -0.1532 0.2634  -0.0854 309 THR   B C   
3557 O  O   . THR   B 153 ? 0.6875 0.8316 0.7781 -0.1573 0.2732  -0.0897 309 THR   B O   
3558 C  CB  . THR   B 153 ? 0.8152 0.9291 0.8828 -0.1282 0.2557  -0.0767 309 THR   B CB  
3559 O  OG1 . THR   B 153 ? 0.6942 0.8126 0.7672 -0.1127 0.2460  -0.0772 309 THR   B OG1 
3560 C  CG2 . THR   B 153 ? 0.6050 0.6774 0.6402 -0.1351 0.2582  -0.0644 309 THR   B CG2 
3561 N  N   . LEU   B 154 ? 0.5815 0.6977 0.6668 -0.1630 0.2616  -0.0817 310 LEU   B N   
3562 C  CA  . LEU   B 154 ? 0.6064 0.7123 0.6840 -0.1797 0.2714  -0.0821 310 LEU   B CA  
3563 C  C   . LEU   B 154 ? 0.7381 0.7976 0.7788 -0.1837 0.2751  -0.0693 310 LEU   B C   
3564 O  O   . LEU   B 154 ? 0.8113 0.8498 0.8402 -0.1771 0.2666  -0.0615 310 LEU   B O   
3565 C  CB  . LEU   B 154 ? 0.6131 0.7361 0.7136 -0.1880 0.2667  -0.0896 310 LEU   B CB  
3566 C  CG  . LEU   B 154 ? 0.7062 0.8757 0.8435 -0.1832 0.2612  -0.1029 310 LEU   B CG  
3567 C  CD1 . LEU   B 154 ? 0.5365 0.7180 0.6914 -0.1920 0.2563  -0.1094 310 LEU   B CD1 
3568 C  CD2 . LEU   B 154 ? 0.4666 0.6593 0.6125 -0.1862 0.2715  -0.1108 310 LEU   B CD2 
3569 N  N   . LEU   B 155 ? 0.8507 0.8948 0.8726 -0.1932 0.2876  -0.0672 311 LEU   B N   
3570 C  CA  . LEU   B 155 ? 0.8384 0.8370 0.8228 -0.1966 0.2917  -0.0553 311 LEU   B CA  
3571 C  C   . LEU   B 155 ? 0.8376 0.8245 0.8190 -0.2129 0.2983  -0.0572 311 LEU   B C   
3572 O  O   . LEU   B 155 ? 0.7115 0.7075 0.6959 -0.2241 0.3100  -0.0630 311 LEU   B O   
3573 C  CB  . LEU   B 155 ? 0.8721 0.8559 0.8317 -0.1934 0.3005  -0.0500 311 LEU   B CB  
3574 C  CG  . LEU   B 155 ? 0.8734 0.8803 0.8431 -0.1804 0.2978  -0.0532 311 LEU   B CG  
3575 C  CD1 . LEU   B 155 ? 0.7810 0.7804 0.7312 -0.1819 0.3096  -0.0515 311 LEU   B CD1 
3576 C  CD2 . LEU   B 155 ? 0.6975 0.6893 0.6558 -0.1659 0.2864  -0.0457 311 LEU   B CD2 
3577 N  N   . ILE   B 156 ? 0.8328 0.8007 0.8086 -0.2140 0.2913  -0.0531 312 ILE   B N   
3578 C  CA  . ILE   B 156 ? 0.7535 0.7082 0.7255 -0.2288 0.2966  -0.0554 312 ILE   B CA  
3579 C  C   . ILE   B 156 ? 1.0607 0.9709 0.9927 -0.2324 0.3055  -0.0452 312 ILE   B C   
3580 O  O   . ILE   B 156 ? 1.0850 0.9690 0.9924 -0.2209 0.3006  -0.0346 312 ILE   B O   
3581 C  CB  . ILE   B 156 ? 0.8589 0.8116 0.8406 -0.2266 0.2847  -0.0552 312 ILE   B CB  
3582 C  CG1 . ILE   B 156 ? 0.8534 0.8503 0.8749 -0.2273 0.2782  -0.0674 312 ILE   B CG1 
3583 C  CG2 . ILE   B 156 ? 1.0169 0.9376 0.9790 -0.2372 0.2889  -0.0520 312 ILE   B CG2 
3584 C  CD1 . ILE   B 156 ? 0.6291 0.6511 0.6686 -0.2123 0.2684  -0.0686 312 ILE   B CD1 
3585 N  N   . SER   B 157 ? 0.9753 0.8783 0.9007 -0.2474 0.3182  -0.0489 313 SER   B N   
3586 C  CA  . SER   B 157 ? 1.1291 0.9889 1.0152 -0.2512 0.3277  -0.0398 313 SER   B CA  
3587 C  C   . SER   B 157 ? 1.1480 0.9981 1.0145 -0.2391 0.3284  -0.0319 313 SER   B C   
3588 O  O   . SER   B 157 ? 1.1097 0.9883 0.9917 -0.2383 0.3325  -0.0375 313 SER   B O   
3589 C  CB  . SER   B 157 ? 0.9766 0.8000 0.8410 -0.2493 0.3221  -0.0321 313 SER   B CB  
3590 N  N   . GLU   B 158 ? 1.0893 0.9014 0.9226 -0.2295 0.3243  -0.0200 314 GLU   B N   
3591 C  CA  . GLU   B 158 ? 1.1799 0.9804 0.9914 -0.2171 0.3240  -0.0123 314 GLU   B CA  
3592 C  C   . GLU   B 158 ? 0.9740 0.7893 0.7976 -0.2013 0.3096  -0.0104 314 GLU   B C   
3593 O  O   . GLU   B 158 ? 1.1556 0.9517 0.9551 -0.1889 0.3056  -0.0019 314 GLU   B O   
3594 C  CB  . GLU   B 158 ? 1.1271 0.8791 0.8952 -0.2141 0.3269  -0.0009 314 GLU   B CB  
3595 N  N   . ILE   B 160 ? 0.8973 0.7356 0.7671 -0.1887 0.2767  -0.0130 316 ILE   B N   
3596 C  CA  . ILE   B 160 ? 0.8764 0.7386 0.7744 -0.1839 0.2648  -0.0173 316 ILE   B CA  
3597 C  C   . ILE   B 160 ? 0.9034 0.8073 0.8319 -0.1819 0.2650  -0.0265 316 ILE   B C   
3598 O  O   . ILE   B 160 ? 0.7185 0.6430 0.6616 -0.1916 0.2738  -0.0347 316 ILE   B O   
3599 C  CB  . ILE   B 160 ? 0.9210 0.7841 0.8316 -0.1939 0.2630  -0.0218 316 ILE   B CB  
3600 C  CG1 . ILE   B 160 ? 1.0457 0.8674 0.9262 -0.1927 0.2610  -0.0127 316 ILE   B CG1 
3601 C  CG2 . ILE   B 160 ? 0.7911 0.6848 0.7344 -0.1902 0.2520  -0.0282 316 ILE   B CG2 
3602 C  CD1 . ILE   B 160 ? 1.1461 0.9681 1.0384 -0.2000 0.2572  -0.0168 316 ILE   B CD1 
3603 N  N   . SER   B 161 ? 0.9150 0.8302 0.8519 -0.1693 0.2557  -0.0254 317 SER   B N   
3604 C  CA  . SER   B 161 ? 0.6625 0.6160 0.6272 -0.1647 0.2549  -0.0342 317 SER   B CA  
3605 C  C   . SER   B 161 ? 0.6673 0.6457 0.6621 -0.1611 0.2439  -0.0401 317 SER   B C   
3606 O  O   . SER   B 161 ? 0.5394 0.5011 0.5276 -0.1573 0.2353  -0.0343 317 SER   B O   
3607 C  CB  . SER   B 161 ? 0.7709 0.7186 0.7202 -0.1527 0.2547  -0.0297 317 SER   B CB  
3608 O  OG  . SER   B 161 ? 0.9035 0.8132 0.8153 -0.1511 0.2577  -0.0191 317 SER   B OG  
3609 N  N   . VAL   B 162 ? 0.5301 0.5471 0.5562 -0.1615 0.2438  -0.0512 318 VAL   B N   
3610 C  CA  . VAL   B 162 ? 0.6222 0.6653 0.6776 -0.1573 0.2333  -0.0578 318 VAL   B CA  
3611 C  C   . VAL   B 162 ? 0.4666 0.5423 0.5431 -0.1467 0.2313  -0.0654 318 VAL   B C   
3612 O  O   . VAL   B 162 ? 0.5414 0.6405 0.6309 -0.1496 0.2377  -0.0734 318 VAL   B O   
3613 C  CB  . VAL   B 162 ? 0.5871 0.6462 0.6619 -0.1691 0.2335  -0.0657 318 VAL   B CB  
3614 C  CG1 . VAL   B 162 ? 0.5606 0.6463 0.6639 -0.1631 0.2214  -0.0722 318 VAL   B CG1 
3615 C  CG2 . VAL   B 162 ? 0.7155 0.7405 0.7678 -0.1791 0.2363  -0.0589 318 VAL   B CG2 
3616 N  N   . ASP   B 163 ? 0.5222 0.5988 0.6016 -0.1340 0.2225  -0.0633 319 ASP   B N   
3617 C  CA  . ASP   B 163 ? 0.4927 0.5989 0.5929 -0.1217 0.2187  -0.0711 319 ASP   B CA  
3618 C  C   . ASP   B 163 ? 0.5362 0.6709 0.6674 -0.1191 0.2087  -0.0794 319 ASP   B C   
3619 O  O   . ASP   B 163 ? 0.6088 0.7342 0.7409 -0.1170 0.1993  -0.0756 319 ASP   B O   
3620 C  CB  . ASP   B 163 ? 0.4946 0.5828 0.5781 -0.1068 0.2109  -0.0643 319 ASP   B CB  
3621 C  CG  . ASP   B 163 ? 0.7072 0.7724 0.7614 -0.1073 0.2206  -0.0580 319 ASP   B CG  
3622 O  OD1 . ASP   B 163 ? 0.5732 0.6537 0.6307 -0.1069 0.2301  -0.0639 319 ASP   B OD1 
3623 O  OD2 . ASP   B 163 ? 0.9612 0.9936 0.9885 -0.1070 0.2180  -0.0476 319 ASP   B OD2 
3624 N  N   . ILE   B 164 ? 0.6108 0.7795 0.7658 -0.1180 0.2092  -0.0903 320 ILE   B N   
3625 C  CA  . ILE   B 164 ? 0.5344 0.7328 0.7183 -0.1144 0.1992  -0.0991 320 ILE   B CA  
3626 C  C   . ILE   B 164 ? 0.3979 0.6184 0.5969 -0.0960 0.1918  -0.1049 320 ILE   B C   
3627 O  O   . ILE   B 164 ? 0.4346 0.6648 0.6333 -0.0897 0.1969  -0.1084 320 ILE   B O   
3628 C  CB  . ILE   B 164 ? 0.3801 0.6011 0.5796 -0.1257 0.2037  -0.1079 320 ILE   B CB  
3629 C  CG1 . ILE   B 164 ? 0.3712 0.5656 0.5520 -0.1434 0.2122  -0.1022 320 ILE   B CG1 
3630 C  CG2 . ILE   B 164 ? 0.4868 0.7366 0.7134 -0.1215 0.1921  -0.1166 320 ILE   B CG2 
3631 C  CD1 . ILE   B 164 ? 0.4685 0.6764 0.6545 -0.1556 0.2228  -0.1092 320 ILE   B CD1 
3632 N  N   . THR   B 165 ? 0.3610 0.5865 0.5709 -0.0863 0.1787  -0.1054 321 THR   B N   
3633 C  CA  . THR   B 165 ? 0.4698 0.7070 0.6878 -0.0659 0.1666  -0.1085 321 THR   B CA  
3634 C  C   . THR   B 165 ? 0.5012 0.7738 0.7488 -0.0615 0.1588  -0.1193 321 THR   B C   
3635 O  O   . THR   B 165 ? 0.4896 0.7635 0.7441 -0.0686 0.1539  -0.1192 321 THR   B O   
3636 C  CB  . THR   B 165 ? 0.4576 0.6617 0.6545 -0.0549 0.1534  -0.0971 321 THR   B CB  
3637 O  OG1 . THR   B 165 ? 0.4438 0.6205 0.6149 -0.0554 0.1594  -0.0891 321 THR   B OG1 
3638 C  CG2 . THR   B 165 ? 0.3404 0.5548 0.5461 -0.0352 0.1400  -0.1004 321 THR   B CG2 
3639 N  N   . LEU   B 166 ? 0.4154 0.7153 0.6785 -0.0488 0.1567  -0.1284 322 LEU   B N   
3640 C  CA  . LEU   B 166 ? 0.4143 0.7430 0.6994 -0.0392 0.1448  -0.1368 322 LEU   B CA  
3641 C  C   . LEU   B 166 ? 0.3491 0.6691 0.6316 -0.0198 0.1304  -0.1338 322 LEU   B C   
3642 O  O   . LEU   B 166 ? 0.3131 0.6130 0.5789 -0.0083 0.1282  -0.1284 322 LEU   B O   
3643 C  CB  . LEU   B 166 ? 0.2901 0.6476 0.5883 -0.0335 0.1472  -0.1464 322 LEU   B CB  
3644 C  CG  . LEU   B 166 ? 0.3872 0.7747 0.7060 -0.0206 0.1344  -0.1554 322 LEU   B CG  
3645 C  CD1 . LEU   B 166 ? 0.3966 0.7950 0.7264 -0.0334 0.1309  -0.1584 322 LEU   B CD1 
3646 C  CD2 . LEU   B 166 ? 0.3600 0.7732 0.6892 -0.0138 0.1379  -0.1642 322 LEU   B CD2 
3647 N  N   . ALA   B 167 ? 0.2795 0.6077 0.5723 -0.0164 0.1186  -0.1353 323 ALA   B N   
3648 C  CA  . ALA   B 167 ? 0.2938 0.6066 0.5776 0.0016  0.1027  -0.1299 323 ALA   B CA  
3649 C  C   . ALA   B 167 ? 0.4770 0.8209 0.7829 0.0113  0.0919  -0.1393 323 ALA   B C   
3650 O  O   . ALA   B 167 ? 0.3152 0.6775 0.6354 -0.0003 0.0923  -0.1445 323 ALA   B O   
3651 C  CB  . ALA   B 167 ? 0.2108 0.4853 0.4725 -0.0043 0.0975  -0.1166 323 ALA   B CB  
3652 N  N   . LEU   B 168 ? 0.3241 0.6704 0.6292 0.0328  0.0815  -0.1408 324 LEU   B N   
3653 C  CA  . LEU   B 168 ? 0.2374 0.6048 0.5560 0.0457  0.0682  -0.1469 324 LEU   B CA  
3654 C  C   . LEU   B 168 ? 0.2393 0.5791 0.5428 0.0473  0.0570  -0.1369 324 LEU   B C   
3655 O  O   . LEU   B 168 ? 0.2799 0.5824 0.5596 0.0493  0.0552  -0.1253 324 LEU   B O   
3656 C  CB  . LEU   B 168 ? 0.2307 0.6031 0.5468 0.0687  0.0610  -0.1501 324 LEU   B CB  
3657 C  CG  . LEU   B 168 ? 0.3464 0.7320 0.6660 0.0695  0.0706  -0.1555 324 LEU   B CG  
3658 C  CD1 . LEU   B 168 ? 0.3476 0.7305 0.6606 0.0936  0.0627  -0.1570 324 LEU   B CD1 
3659 C  CD2 . LEU   B 168 ? 0.2662 0.6841 0.6043 0.0571  0.0754  -0.1644 324 LEU   B CD2 
3660 N  N   . GLU   B 169 ? 0.1931 0.5520 0.5103 0.0460  0.0493  -0.1418 325 GLU   B N   
3661 C  CA  . GLU   B 169 ? 0.2989 0.6354 0.6031 0.0478  0.0382  -0.1335 325 GLU   B CA  
3662 C  C   . GLU   B 169 ? 0.3482 0.6941 0.6542 0.0703  0.0238  -0.1367 325 GLU   B C   
3663 O  O   . GLU   B 169 ? 0.3272 0.7043 0.6491 0.0763  0.0197  -0.1466 325 GLU   B O   
3664 C  CB  . GLU   B 169 ? 0.2623 0.6099 0.5775 0.0297  0.0398  -0.1362 325 GLU   B CB  
3665 C  CG  . GLU   B 169 ? 0.3997 0.7277 0.7030 0.0320  0.0282  -0.1290 325 GLU   B CG  
3666 C  CD  . GLU   B 169 ? 0.3542 0.6930 0.6681 0.0145  0.0298  -0.1327 325 GLU   B CD  
3667 O  OE1 . GLU   B 169 ? 0.4454 0.8190 0.7805 0.0155  0.0254  -0.1444 325 GLU   B OE1 
3668 O  OE2 . GLU   B 169 ? 0.3613 0.6738 0.6618 0.0001  0.0352  -0.1245 325 GLU   B OE2 
3669 N  N   . SER   B 170 ? 0.3194 0.6312 0.6021 0.0812  0.0157  -0.1260 326 SER   B N   
3670 C  CA  . SER   B 170 ? 0.3250 0.6386 0.6040 0.1022  0.0018  -0.1270 326 SER   B CA  
3671 C  C   . SER   B 170 ? 0.3063 0.5957 0.5702 0.0994  -0.0064 -0.1179 326 SER   B C   
3672 O  O   . SER   B 170 ? 0.3817 0.6368 0.6262 0.0913  -0.0035 -0.1068 326 SER   B O   
3673 C  CB  . SER   B 170 ? 0.2538 0.5479 0.5168 0.1209  -0.0002 -0.1237 326 SER   B CB  
3674 O  OG  . SER   B 170 ? 0.5192 0.8074 0.7732 0.1409  -0.0134 -0.1226 326 SER   B OG  
3675 N  N   . LYS   B 171 ? 0.4039 0.7132 0.6770 0.1063  -0.0166 -0.1234 327 LYS   B N   
3676 C  CA  . LYS   B 171 ? 0.3177 0.6073 0.5768 0.1061  -0.0254 -0.1160 327 LYS   B CA  
3677 C  C   . LYS   B 171 ? 0.3629 0.6326 0.6025 0.1281  -0.0364 -0.1107 327 LYS   B C   
3678 O  O   . LYS   B 171 ? 0.4539 0.7111 0.6821 0.1313  -0.0449 -0.1059 327 LYS   B O   
3679 C  CB  . LYS   B 171 ? 0.2882 0.6092 0.5669 0.0989  -0.0298 -0.1250 327 LYS   B CB  
3680 C  CG  . LYS   B 171 ? 0.3432 0.6754 0.6362 0.0744  -0.0184 -0.1284 327 LYS   B CG  
3681 C  CD  . LYS   B 171 ? 0.5430 0.9154 0.8601 0.0682  -0.0198 -0.1418 327 LYS   B CD  
3682 C  CE  . LYS   B 171 ? 0.5289 0.9018 0.8528 0.0453  -0.0138 -0.1427 327 LYS   B CE  
3683 N  NZ  . LYS   B 171 ? 0.6649 1.0438 0.9981 0.0269  0.0016  -0.1458 327 LYS   B NZ  
3684 N  N   . SER   B 172 ? 0.2776 0.5423 0.5115 0.1433  -0.0359 -0.1114 328 SER   B N   
3685 C  CA  . SER   B 172 ? 0.3473 0.5856 0.5581 0.1636  -0.0446 -0.1053 328 SER   B CA  
3686 C  C   . SER   B 172 ? 0.3656 0.5575 0.5498 0.1561  -0.0408 -0.0915 328 SER   B C   
3687 O  O   . SER   B 172 ? 0.4098 0.5923 0.5942 0.1371  -0.0325 -0.0872 328 SER   B O   
3688 C  CB  . SER   B 172 ? 0.2970 0.5423 0.5077 0.1800  -0.0443 -0.1103 328 SER   B CB  
3689 O  OG  . SER   B 172 ? 0.5823 0.8272 0.7991 0.1738  -0.0330 -0.1120 328 SER   B OG  
3690 N  N   . SER   B 173 ? 0.5848 0.7471 0.7451 0.1714  -0.0468 -0.0849 329 SER   B N   
3691 C  CA  . SER   B 173 ? 0.4655 0.5850 0.6007 0.1645  -0.0432 -0.0730 329 SER   B CA  
3692 C  C   . SER   B 173 ? 0.2731 0.3829 0.4077 0.1561  -0.0323 -0.0722 329 SER   B C   
3693 O  O   . SER   B 173 ? 0.2759 0.4023 0.4212 0.1633  -0.0290 -0.0794 329 SER   B O   
3694 C  CB  . SER   B 173 ? 0.5926 0.6819 0.7017 0.1829  -0.0506 -0.0672 329 SER   B CB  
3695 O  OG  . SER   B 173 ? 0.7782 0.8702 0.8827 0.1888  -0.0603 -0.0658 329 SER   B OG  
3696 N  N   . TRP   B 174 ? 0.4291 0.5132 0.5513 0.1412  -0.0269 -0.0639 330 TRP   B N   
3697 C  CA  . TRP   B 174 ? 0.3741 0.4460 0.4924 0.1335  -0.0174 -0.0625 330 TRP   B CA  
3698 C  C   . TRP   B 174 ? 0.3915 0.4424 0.4935 0.1493  -0.0181 -0.0621 330 TRP   B C   
3699 O  O   . TRP   B 174 ? 0.3538 0.3835 0.4382 0.1615  -0.0247 -0.0581 330 TRP   B O   
3700 C  CB  . TRP   B 174 ? 0.3170 0.3650 0.4232 0.1167  -0.0132 -0.0540 330 TRP   B CB  
3701 C  CG  . TRP   B 174 ? 0.3358 0.4009 0.4564 0.1000  -0.0102 -0.0544 330 TRP   B CG  
3702 C  CD1 . TRP   B 174 ? 0.3151 0.4109 0.4558 0.0978  -0.0120 -0.0609 330 TRP   B CD1 
3703 C  CD2 . TRP   B 174 ? 0.2977 0.3490 0.4125 0.0837  -0.0049 -0.0486 330 TRP   B CD2 
3704 N  NE1 . TRP   B 174 ? 0.3387 0.4377 0.4851 0.0805  -0.0076 -0.0590 330 TRP   B NE1 
3705 C  CE2 . TRP   B 174 ? 0.2839 0.3559 0.4143 0.0726  -0.0034 -0.0513 330 TRP   B CE2 
3706 C  CE3 . TRP   B 174 ? 0.2792 0.3033 0.3771 0.0776  -0.0014 -0.0421 330 TRP   B CE3 
3707 C  CZ2 . TRP   B 174 ? 0.3202 0.3842 0.4482 0.0572  0.0012  -0.0469 330 TRP   B CZ2 
3708 C  CZ3 . TRP   B 174 ? 0.3470 0.3667 0.4442 0.0627  0.0027  -0.0383 330 TRP   B CZ3 
3709 C  CH2 . TRP   B 174 ? 0.3266 0.3651 0.4379 0.0533  0.0039  -0.0404 330 TRP   B CH2 
3710 N  N   . PRO   B 175 ? 0.3898 0.4444 0.4957 0.1497  -0.0109 -0.0662 331 PRO   B N   
3711 C  CA  . PRO   B 175 ? 0.4241 0.4582 0.5143 0.1650  -0.0111 -0.0668 331 PRO   B CA  
3712 C  C   . PRO   B 175 ? 0.5056 0.4963 0.5680 0.1631  -0.0117 -0.0576 331 PRO   B C   
3713 O  O   . PRO   B 175 ? 0.4317 0.4094 0.4883 0.1474  -0.0095 -0.0513 331 PRO   B O   
3714 C  CB  . PRO   B 175 ? 0.4273 0.4730 0.5270 0.1599  -0.0015 -0.0722 331 PRO   B CB  
3715 C  CG  . PRO   B 175 ? 0.4037 0.4875 0.5297 0.1493  0.0016  -0.0778 331 PRO   B CG  
3716 C  CD  . PRO   B 175 ? 0.3631 0.4428 0.4882 0.1374  -0.0022 -0.0716 331 PRO   B CD  
3717 N  N   . ALA   B 176 ? 0.5161 0.4840 0.5606 0.1795  -0.0145 -0.0573 332 ALA   B N   
3718 C  CA  . ALA   B 176 ? 0.5379 0.4629 0.5544 0.1785  -0.0149 -0.0493 332 ALA   B CA  
3719 C  C   . ALA   B 176 ? 0.4355 0.3426 0.4445 0.1624  -0.0065 -0.0467 332 ALA   B C   
3720 O  O   . ALA   B 176 ? 0.5194 0.3969 0.5099 0.1546  -0.0058 -0.0402 332 ALA   B O   
3721 C  CB  . ALA   B 176 ? 0.5741 0.4768 0.5718 0.2001  -0.0187 -0.0503 332 ALA   B CB  
3722 N  N   . SER   B 177 ? 0.4127 0.3378 0.4353 0.1572  0.0000  -0.0521 333 SER   B N   
3723 C  CA  . SER   B 177 ? 0.3523 0.2629 0.3678 0.1427  0.0073  -0.0504 333 SER   B CA  
3724 C  C   . SER   B 177 ? 0.4461 0.3595 0.4656 0.1239  0.0085  -0.0451 333 SER   B C   
3725 O  O   . SER   B 177 ? 0.4431 0.3419 0.4541 0.1122  0.0130  -0.0429 333 SER   B O   
3726 C  CB  . SER   B 177 ? 0.3936 0.3237 0.4217 0.1430  0.0139  -0.0576 333 SER   B CB  
3727 O  OG  . SER   B 177 ? 0.4655 0.4312 0.5172 0.1369  0.0154  -0.0607 333 SER   B OG  
3728 N  N   . THR   B 178 ? 0.3629 0.2948 0.3946 0.1213  0.0042  -0.0436 334 THR   B N   
3729 C  CA  . THR   B 178 ? 0.4797 0.4144 0.5151 0.1051  0.0049  -0.0389 334 THR   B CA  
3730 C  C   . THR   B 178 ? 0.3853 0.2990 0.4062 0.1036  -0.0002 -0.0323 334 THR   B C   
3731 O  O   . THR   B 178 ? 0.3926 0.3092 0.4164 0.0917  -0.0004 -0.0286 334 THR   B O   
3732 C  CB  . THR   B 178 ? 0.4873 0.4555 0.5453 0.1009  0.0045  -0.0421 334 THR   B CB  
3733 O  OG1 . THR   B 178 ? 0.4575 0.4353 0.5200 0.1111  -0.0031 -0.0429 334 THR   B OG1 
3734 C  CG2 . THR   B 178 ? 0.3775 0.3681 0.4501 0.1031  0.0101  -0.0493 334 THR   B CG2 
3735 N  N   . GLN   B 179 ? 0.4520 0.3435 0.4562 0.1156  -0.0037 -0.0307 335 GLN   B N   
3736 C  CA  . GLN   B 179 ? 0.4475 0.3217 0.4382 0.1161  -0.0086 -0.0247 335 GLN   B CA  
3737 C  C   . GLN   B 179 ? 0.5826 0.4381 0.5625 0.1001  -0.0051 -0.0195 335 GLN   B C   
3738 O  O   . GLN   B 179 ? 0.5430 0.3950 0.5193 0.0950  -0.0079 -0.0150 335 GLN   B O   
3739 C  CB  . GLN   B 179 ? 0.6052 0.4553 0.5765 0.1328  -0.0121 -0.0238 335 GLN   B CB  
3740 C  CG  . GLN   B 179 ? 0.9401 0.8012 0.9138 0.1468  -0.0204 -0.0238 335 GLN   B CG  
3741 C  CD  . GLN   B 179 ? 0.9301 0.7749 0.8888 0.1678  -0.0241 -0.0251 335 GLN   B CD  
3742 O  OE1 . GLN   B 179 ? 0.9357 0.7457 0.8713 0.1705  -0.0213 -0.0221 335 GLN   B OE1 
3743 N  NE2 . GLN   B 179 ? 0.9400 0.8101 0.9115 0.1831  -0.0302 -0.0303 335 GLN   B NE2 
3744 N  N   . GLU   B 180 ? 0.5250 0.3697 0.4998 0.0925  0.0007  -0.0207 336 GLU   B N   
3745 C  CA  . GLU   B 180 ? 0.5149 0.3451 0.4810 0.0775  0.0039  -0.0173 336 GLU   B CA  
3746 C  C   . GLU   B 180 ? 0.4638 0.3131 0.4439 0.0652  0.0075  -0.0190 336 GLU   B C   
3747 O  O   . GLU   B 180 ? 0.5582 0.3986 0.5323 0.0538  0.0104  -0.0179 336 GLU   B O   
3748 C  CB  . GLU   B 180 ? 0.6036 0.4025 0.5491 0.0775  0.0075  -0.0175 336 GLU   B CB  
3749 C  CG  . GLU   B 180 ? 0.7454 0.5213 0.6740 0.0921  0.0048  -0.0161 336 GLU   B CG  
3750 C  CD  . GLU   B 180 ? 0.9381 0.6909 0.8493 0.0885  0.0035  -0.0101 336 GLU   B CD  
3751 O  OE1 . GLU   B 180 ? 1.1631 0.8925 1.0596 0.0782  0.0080  -0.0089 336 GLU   B OE1 
3752 O  OE2 . GLU   B 180 ? 0.9483 0.7070 0.8605 0.0954  -0.0018 -0.0070 336 GLU   B OE2 
3753 N  N   . GLY   B 181 ? 0.4513 0.3267 0.4492 0.0673  0.0075  -0.0220 337 GLY   B N   
3754 C  CA  . GLY   B 181 ? 0.3777 0.2697 0.3869 0.0563  0.0108  -0.0226 337 GLY   B CA  
3755 C  C   . GLY   B 181 ? 0.3758 0.2791 0.3929 0.0495  0.0079  -0.0193 337 GLY   B C   
3756 O  O   . GLY   B 181 ? 0.3953 0.2952 0.4097 0.0530  0.0033  -0.0168 337 GLY   B O   
3757 N  N   . LEU   B 182 ? 0.3544 0.2701 0.3798 0.0403  0.0108  -0.0194 338 LEU   B N   
3758 C  CA  . LEU   B 182 ? 0.3077 0.2335 0.3403 0.0335  0.0088  -0.0169 338 LEU   B CA  
3759 C  C   . LEU   B 182 ? 0.3346 0.2459 0.3566 0.0299  0.0056  -0.0127 338 LEU   B C   
3760 O  O   . LEU   B 182 ? 0.3142 0.2283 0.3379 0.0312  0.0015  -0.0108 338 LEU   B O   
3761 C  CB  . LEU   B 182 ? 0.2582 0.2029 0.3046 0.0386  0.0061  -0.0190 338 LEU   B CB  
3762 C  CG  . LEU   B 182 ? 0.2546 0.2127 0.3109 0.0315  0.0048  -0.0180 338 LEU   B CG  
3763 C  CD1 . LEU   B 182 ? 0.2017 0.1663 0.2626 0.0225  0.0104  -0.0184 338 LEU   B CD1 
3764 C  CD2 . LEU   B 182 ? 0.3787 0.3548 0.4477 0.0376  0.0013  -0.0216 338 LEU   B CD2 
3765 N  N   . ARG   B 183 ? 0.3183 0.2146 0.3290 0.0249  0.0078  -0.0119 339 ARG   B N   
3766 C  CA  . ARG   B 183 ? 0.4024 0.2846 0.4024 0.0204  0.0062  -0.0089 339 ARG   B CA  
3767 C  C   . ARG   B 183 ? 0.3065 0.1981 0.3116 0.0116  0.0058  -0.0072 339 ARG   B C   
3768 O  O   . ARG   B 183 ? 0.4414 0.3300 0.4425 0.0044  0.0076  -0.0076 339 ARG   B O   
3769 C  CB  . ARG   B 183 ? 0.4473 0.3107 0.4339 0.0180  0.0092  -0.0101 339 ARG   B CB  
3770 C  CG  . ARG   B 183 ? 0.5669 0.4174 0.5460 0.0278  0.0096  -0.0117 339 ARG   B CG  
3771 C  CD  . ARG   B 183 ? 0.7636 0.5917 0.7274 0.0245  0.0128  -0.0131 339 ARG   B CD  
3772 N  NE  . ARG   B 183 ? 0.8853 0.7018 0.8400 0.0155  0.0131  -0.0108 339 ARG   B NE  
3773 C  CZ  . ARG   B 183 ? 0.9395 0.7329 0.8785 0.0119  0.0159  -0.0113 339 ARG   B CZ  
3774 N  NH1 . ARG   B 183 ? 0.9376 0.7144 0.8668 0.0172  0.0181  -0.0138 339 ARG   B NH1 
3775 N  NH2 . ARG   B 183 ? 0.8546 0.6410 0.7874 0.0023  0.0170  -0.0097 339 ARG   B NH2 
3776 N  N   . ILE   B 184 ? 0.3243 0.2280 0.3384 0.0128  0.0030  -0.0061 340 ILE   B N   
3777 C  CA  . ILE   B 184 ? 0.2848 0.1969 0.3036 0.0062  0.0023  -0.0047 340 ILE   B CA  
3778 C  C   . ILE   B 184 ? 0.2856 0.1924 0.2993 0.0046  -0.0007 -0.0020 340 ILE   B C   
3779 O  O   . ILE   B 184 ? 0.3148 0.2288 0.3325 0.0006  -0.0020 -0.0011 340 ILE   B O   
3780 C  CB  . ILE   B 184 ? 0.3581 0.2864 0.3897 0.0068  0.0023  -0.0058 340 ILE   B CB  
3781 C  CG1 . ILE   B 184 ? 0.3913 0.3258 0.4283 0.0133  -0.0016 -0.0064 340 ILE   B CG1 
3782 C  CG2 . ILE   B 184 ? 0.2028 0.1363 0.2385 0.0074  0.0065  -0.0084 340 ILE   B CG2 
3783 C  CD1 . ILE   B 184 ? 0.2304 0.1823 0.2812 0.0125  -0.0014 -0.0089 340 ILE   B CD1 
3784 N  N   . GLN   B 185 ? 0.3188 0.2115 0.3219 0.0079  -0.0015 -0.0008 341 GLN   B N   
3785 C  CA  . GLN   B 185 ? 0.3206 0.2076 0.3174 0.0076  -0.0041 0.0020  341 GLN   B CA  
3786 C  C   . GLN   B 185 ? 0.3794 0.2673 0.3745 -0.0016 -0.0027 0.0027  341 GLN   B C   
3787 O  O   . GLN   B 185 ? 0.3530 0.2467 0.3502 -0.0030 -0.0049 0.0040  341 GLN   B O   
3788 C  CB  . GLN   B 185 ? 0.3575 0.2246 0.3394 0.0123  -0.0039 0.0037  341 GLN   B CB  
3789 C  CG  . GLN   B 185 ? 0.4323 0.2989 0.4147 0.0242  -0.0067 0.0031  341 GLN   B CG  
3790 C  CD  . GLN   B 185 ? 0.3987 0.2588 0.3792 0.0276  -0.0038 0.0006  341 GLN   B CD  
3791 O  OE1 . GLN   B 185 ? 0.4927 0.3552 0.4763 0.0211  -0.0002 -0.0014 341 GLN   B OE1 
3792 N  NE2 . GLN   B 185 ? 0.3694 0.2210 0.3436 0.0388  -0.0057 0.0004  341 GLN   B NE2 
3793 N  N   . ASN   B 186 ? 0.3775 0.2610 0.3690 -0.0075 0.0006  0.0011  342 ASN   B N   
3794 C  CA  . ASN   B 186 ? 0.3960 0.2832 0.3870 -0.0155 0.0017  0.0005  342 ASN   B CA  
3795 C  C   . ASN   B 186 ? 0.2130 0.1159 0.2142 -0.0168 0.0007  -0.0006 342 ASN   B C   
3796 O  O   . ASN   B 186 ? 0.3255 0.2341 0.3274 -0.0215 0.0006  -0.0013 342 ASN   B O   
3797 C  CB  . ASN   B 186 ? 0.4420 0.3203 0.4255 -0.0215 0.0054  -0.0020 342 ASN   B CB  
3798 C  CG  . ASN   B 186 ? 0.7772 0.6362 0.7471 -0.0228 0.0075  -0.0007 342 ASN   B CG  
3799 O  OD1 . ASN   B 186 ? 0.6802 0.5320 0.6451 -0.0177 0.0059  0.0027  342 ASN   B OD1 
3800 N  ND2 . ASN   B 186 ? 0.9093 0.7590 0.8721 -0.0297 0.0114  -0.0035 342 ASN   B ND2 
3801 N  N   . TRP   B 187 ? 0.3011 0.2108 0.3097 -0.0127 0.0001  -0.0008 343 TRP   B N   
3802 C  CA  . TRP   B 187 ? 0.2797 0.2001 0.2950 -0.0139 0.0001  -0.0014 343 TRP   B CA  
3803 C  C   . TRP   B 187 ? 0.2939 0.2213 0.3163 -0.0117 -0.0020 -0.0003 343 TRP   B C   
3804 O  O   . TRP   B 187 ? 0.2688 0.2001 0.2924 -0.0138 -0.0034 0.0002  343 TRP   B O   
3805 C  CB  . TRP   B 187 ? 0.1982 0.1195 0.2147 -0.0128 0.0027  -0.0030 343 TRP   B CB  
3806 C  CG  . TRP   B 187 ? 0.2574 0.1863 0.2788 -0.0128 0.0037  -0.0029 343 TRP   B CG  
3807 C  CD1 . TRP   B 187 ? 0.2154 0.1486 0.2379 -0.0146 0.0027  -0.0020 343 TRP   B CD1 
3808 C  CD2 . TRP   B 187 ? 0.2745 0.2059 0.2989 -0.0110 0.0067  -0.0037 343 TRP   B CD2 
3809 N  NE1 . TRP   B 187 ? 0.2555 0.1912 0.2800 -0.0142 0.0050  -0.0017 343 TRP   B NE1 
3810 C  CE2 . TRP   B 187 ? 0.2544 0.1897 0.2803 -0.0126 0.0077  -0.0027 343 TRP   B CE2 
3811 C  CE3 . TRP   B 187 ? 0.2446 0.1745 0.2695 -0.0080 0.0089  -0.0053 343 TRP   B CE3 
3812 C  CZ2 . TRP   B 187 ? 0.1811 0.1186 0.2086 -0.0125 0.0117  -0.0031 343 TRP   B CZ2 
3813 C  CZ3 . TRP   B 187 ? 0.2419 0.1766 0.2701 -0.0075 0.0126  -0.0061 343 TRP   B CZ3 
3814 C  CH2 . TRP   B 187 ? 0.1847 0.1229 0.2139 -0.0103 0.0142  -0.0049 343 TRP   B CH2 
3815 N  N   . LEU   B 188 ? 0.2228 0.1527 0.2502 -0.0075 -0.0024 -0.0007 344 LEU   B N   
3816 C  CA  . LEU   B 188 ? 0.2487 0.1873 0.2840 -0.0063 -0.0044 -0.0011 344 LEU   B CA  
3817 C  C   . LEU   B 188 ? 0.2699 0.2075 0.3038 -0.0025 -0.0083 -0.0004 344 LEU   B C   
3818 O  O   . LEU   B 188 ? 0.3421 0.2879 0.3824 -0.0018 -0.0107 -0.0015 344 LEU   B O   
3819 C  CB  . LEU   B 188 ? 0.2247 0.1708 0.2682 -0.0045 -0.0022 -0.0032 344 LEU   B CB  
3820 C  CG  . LEU   B 188 ? 0.2026 0.1487 0.2457 -0.0078 0.0022  -0.0035 344 LEU   B CG  
3821 C  CD1 . LEU   B 188 ? 0.1843 0.1380 0.2351 -0.0068 0.0055  -0.0058 344 LEU   B CD1 
3822 C  CD2 . LEU   B 188 ? 0.2481 0.1942 0.2898 -0.0121 0.0024  -0.0023 344 LEU   B CD2 
3823 N  N   . SER   B 189 ? 0.2891 0.2159 0.3135 -0.0004 -0.0088 0.0011  345 SER   B N   
3824 C  CA  . SER   B 189 ? 0.3534 0.2743 0.3711 0.0038  -0.0121 0.0027  345 SER   B CA  
3825 C  C   . SER   B 189 ? 0.3658 0.2850 0.3830 0.0124  -0.0140 0.0020  345 SER   B C   
3826 O  O   . SER   B 189 ? 0.3429 0.2710 0.3692 0.0150  -0.0133 -0.0006 345 SER   B O   
3827 C  CB  . SER   B 189 ? 0.3272 0.2561 0.3486 0.0031  -0.0155 0.0026  345 SER   B CB  
3828 O  OG  . SER   B 189 ? 0.2828 0.2241 0.3148 0.0070  -0.0181 -0.0001 345 SER   B OG  
3829 N  N   . ALA   B 190 ? 0.3006 0.2080 0.3062 0.0174  -0.0162 0.0043  346 ALA   B N   
3830 C  CA  . ALA   B 190 ? 0.3506 0.2547 0.3531 0.0280  -0.0190 0.0038  346 ALA   B CA  
3831 C  C   . ALA   B 190 ? 0.3345 0.2564 0.3483 0.0340  -0.0242 0.0009  346 ALA   B C   
3832 O  O   . ALA   B 190 ? 0.3522 0.2818 0.3720 0.0421  -0.0261 -0.0020 346 ALA   B O   
3833 C  CB  . ALA   B 190 ? 0.3154 0.1979 0.2985 0.0319  -0.0195 0.0076  346 ALA   B CB  
3834 N  N   . LYS   B 191 ? 0.2479 0.1775 0.2648 0.0303  -0.0267 0.0009  347 LYS   B N   
3835 C  CA  . LYS   B 191 ? 0.4122 0.3604 0.4411 0.0341  -0.0315 -0.0030 347 LYS   B CA  
3836 C  C   . LYS   B 191 ? 0.3082 0.2733 0.3545 0.0310  -0.0289 -0.0077 347 LYS   B C   
3837 O  O   . LYS   B 191 ? 0.4207 0.4009 0.4773 0.0368  -0.0316 -0.0123 347 LYS   B O   
3838 C  CB  . LYS   B 191 ? 0.3593 0.3110 0.3877 0.0289  -0.0336 -0.0026 347 LYS   B CB  
3839 C  CG  . LYS   B 191 ? 0.4472 0.4194 0.4904 0.0284  -0.0371 -0.0080 347 LYS   B CG  
3840 C  CD  . LYS   B 191 ? 0.5676 0.5405 0.6087 0.0228  -0.0386 -0.0078 347 LYS   B CD  
3841 C  CE  . LYS   B 191 ? 0.6089 0.5651 0.6321 0.0242  -0.0392 -0.0026 347 LYS   B CE  
3842 N  NZ  . LYS   B 191 ? 0.6737 0.6283 0.6878 0.0341  -0.0454 -0.0022 347 LYS   B NZ  
3843 N  N   . VAL   B 192 ? 0.2851 0.2481 0.3340 0.0221  -0.0234 -0.0070 348 VAL   B N   
3844 C  CA  . VAL   B 192 ? 0.3310 0.3067 0.3932 0.0184  -0.0197 -0.0106 348 VAL   B CA  
3845 C  C   . VAL   B 192 ? 0.2817 0.2587 0.3459 0.0249  -0.0181 -0.0124 348 VAL   B C   
3846 O  O   . VAL   B 192 ? 0.3061 0.2991 0.3831 0.0263  -0.0172 -0.0172 348 VAL   B O   
3847 C  CB  . VAL   B 192 ? 0.3371 0.3071 0.3978 0.0090  -0.0146 -0.0086 348 VAL   B CB  
3848 C  CG1 . VAL   B 192 ? 0.1830 0.1601 0.2520 0.0061  -0.0094 -0.0111 348 VAL   B CG1 
3849 C  CG2 . VAL   B 192 ? 0.1975 0.1706 0.2600 0.0034  -0.0159 -0.0086 348 VAL   B CG2 
3850 N  N   . ARG   B 193 ? 0.2807 0.2411 0.3322 0.0287  -0.0172 -0.0093 349 ARG   B N   
3851 C  CA  . ARG   B 193 ? 0.3087 0.2684 0.3605 0.0359  -0.0158 -0.0113 349 ARG   B CA  
3852 C  C   . ARG   B 193 ? 0.3569 0.3274 0.4136 0.0474  -0.0212 -0.0147 349 ARG   B C   
3853 O  O   . ARG   B 193 ? 0.2808 0.2645 0.3477 0.0524  -0.0202 -0.0194 349 ARG   B O   
3854 C  CB  . ARG   B 193 ? 0.3518 0.2888 0.3872 0.0372  -0.0138 -0.0078 349 ARG   B CB  
3855 C  CG  . ARG   B 193 ? 0.3020 0.2352 0.3353 0.0461  -0.0126 -0.0100 349 ARG   B CG  
3856 C  CD  . ARG   B 193 ? 0.2848 0.1935 0.3010 0.0460  -0.0101 -0.0071 349 ARG   B CD  
3857 N  NE  . ARG   B 193 ? 0.2558 0.1613 0.2711 0.0520  -0.0073 -0.0101 349 ARG   B NE  
3858 C  CZ  . ARG   B 193 ? 0.4016 0.2961 0.4081 0.0637  -0.0094 -0.0106 349 ARG   B CZ  
3859 N  NH1 . ARG   B 193 ? 0.4672 0.3515 0.4633 0.0710  -0.0142 -0.0078 349 ARG   B NH1 
3860 N  NH2 . ARG   B 193 ? 0.3896 0.2822 0.3960 0.0691  -0.0064 -0.0140 349 ARG   B NH2 
3861 N  N   . LYS   B 194 ? 0.2985 0.2648 0.3480 0.0523  -0.0270 -0.0128 350 LYS   B N   
3862 C  CA  . LYS   B 194 ? 0.2714 0.2498 0.3250 0.0645  -0.0334 -0.0165 350 LYS   B CA  
3863 C  C   . LYS   B 194 ? 0.3169 0.3244 0.3921 0.0616  -0.0343 -0.0235 350 LYS   B C   
3864 O  O   . LYS   B 194 ? 0.3124 0.3370 0.3983 0.0699  -0.0364 -0.0292 350 LYS   B O   
3865 C  CB  . LYS   B 194 ? 0.3864 0.3540 0.4260 0.0701  -0.0396 -0.0129 350 LYS   B CB  
3866 C  CG  . LYS   B 194 ? 0.5926 0.5694 0.6323 0.0858  -0.0470 -0.0163 350 LYS   B CG  
3867 C  CD  . LYS   B 194 ? 0.5174 0.4799 0.5389 0.0930  -0.0531 -0.0119 350 LYS   B CD  
3868 C  CE  . LYS   B 194 ? 0.7787 0.7413 0.7932 0.1119  -0.0599 -0.0137 350 LYS   B CE  
3869 N  NZ  . LYS   B 194 ? 0.8977 0.8626 0.9038 0.1198  -0.0682 -0.0132 350 LYS   B NZ  
3870 N  N   . GLN   B 195 ? 0.2034 0.2168 0.2851 0.0498  -0.0324 -0.0236 351 GLN   B N   
3871 C  CA  . GLN   B 195 ? 0.3097 0.3484 0.4109 0.0447  -0.0320 -0.0305 351 GLN   B CA  
3872 C  C   . GLN   B 195 ? 0.2825 0.3317 0.3955 0.0415  -0.0253 -0.0343 351 GLN   B C   
3873 O  O   . GLN   B 195 ? 0.3150 0.3875 0.4440 0.0432  -0.0255 -0.0417 351 GLN   B O   
3874 C  CB  . GLN   B 195 ? 0.2631 0.3009 0.3658 0.0326  -0.0306 -0.0294 351 GLN   B CB  
3875 C  CG  . GLN   B 195 ? 0.4395 0.4838 0.5417 0.0352  -0.0380 -0.0312 351 GLN   B CG  
3876 C  CD  . GLN   B 195 ? 0.4920 0.5246 0.5866 0.0264  -0.0371 -0.0273 351 GLN   B CD  
3877 O  OE1 . GLN   B 195 ? 0.5848 0.6121 0.6704 0.0298  -0.0424 -0.0255 351 GLN   B OE1 
3878 N  NE2 . GLN   B 195 ? 0.6969 0.7252 0.7941 0.0158  -0.0305 -0.0262 351 GLN   B NE2 
3879 N  N   . LEU   B 196 ? 0.2611 0.2946 0.3662 0.0368  -0.0190 -0.0300 352 LEU   B N   
3880 C  CA  . LEU   B 196 ? 0.3311 0.3724 0.4445 0.0340  -0.0121 -0.0331 352 LEU   B CA  
3881 C  C   . LEU   B 196 ? 0.2934 0.3435 0.4108 0.0466  -0.0138 -0.0373 352 LEU   B C   
3882 O  O   . LEU   B 196 ? 0.3136 0.3835 0.4455 0.0464  -0.0103 -0.0437 352 LEU   B O   
3883 C  CB  . LEU   B 196 ? 0.2531 0.2747 0.3548 0.0279  -0.0063 -0.0277 352 LEU   B CB  
3884 C  CG  . LEU   B 196 ? 0.1791 0.1946 0.2784 0.0160  -0.0033 -0.0245 352 LEU   B CG  
3885 C  CD1 . LEU   B 196 ? 0.2246 0.2227 0.3119 0.0123  0.0011  -0.0199 352 LEU   B CD1 
3886 C  CD2 . LEU   B 196 ? 0.2598 0.2918 0.3730 0.0079  0.0011  -0.0292 352 LEU   B CD2 
3887 N  N   . ARG   B 197 ? 0.2258 0.2607 0.3295 0.0577  -0.0187 -0.0341 353 ARG   B N   
3888 C  CA  . ARG   B 197 ? 0.3357 0.3760 0.4407 0.0717  -0.0208 -0.0379 353 ARG   B CA  
3889 C  C   . ARG   B 197 ? 0.3283 0.3953 0.4478 0.0802  -0.0271 -0.0452 353 ARG   B C   
3890 O  O   . ARG   B 197 ? 0.2612 0.3407 0.3871 0.0917  -0.0284 -0.0506 353 ARG   B O   
3891 C  CB  . ARG   B 197 ? 0.3732 0.3857 0.4565 0.0812  -0.0239 -0.0321 353 ARG   B CB  
3892 C  CG  . ARG   B 197 ? 0.4179 0.4076 0.4887 0.0743  -0.0174 -0.0274 353 ARG   B CG  
3893 C  CD  . ARG   B 197 ? 0.4041 0.3651 0.4531 0.0818  -0.0195 -0.0225 353 ARG   B CD  
3894 N  NE  . ARG   B 197 ? 0.5955 0.5560 0.6411 0.0983  -0.0229 -0.0255 353 ARG   B NE  
3895 C  CZ  . ARG   B 197 ? 0.4756 0.4355 0.5221 0.1040  -0.0193 -0.0289 353 ARG   B CZ  
3896 N  NH1 . ARG   B 197 ? 0.5374 0.4976 0.5878 0.0943  -0.0120 -0.0297 353 ARG   B NH1 
3897 N  NH2 . ARG   B 197 ? 0.5203 0.4791 0.5627 0.1208  -0.0232 -0.0317 353 ARG   B NH2 
3898 N  N   . LEU   B 198 ? 0.2674 0.3446 0.3927 0.0752  -0.0312 -0.0463 354 LEU   B N   
3899 C  CA  . LEU   B 198 ? 0.3742 0.4809 0.5160 0.0813  -0.0371 -0.0548 354 LEU   B CA  
3900 C  C   . LEU   B 198 ? 0.2986 0.4334 0.4634 0.0715  -0.0309 -0.0632 354 LEU   B C   
3901 O  O   . LEU   B 198 ? 0.2825 0.4464 0.4642 0.0759  -0.0346 -0.0723 354 LEU   B O   
3902 C  CB  . LEU   B 198 ? 0.2841 0.3911 0.4225 0.0795  -0.0441 -0.0536 354 LEU   B CB  
3903 C  CG  . LEU   B 198 ? 0.3588 0.4429 0.4751 0.0912  -0.0513 -0.0469 354 LEU   B CG  
3904 C  CD1 . LEU   B 198 ? 0.5330 0.6197 0.6467 0.0885  -0.0575 -0.0464 354 LEU   B CD1 
3905 C  CD2 . LEU   B 198 ? 0.3105 0.3996 0.4239 0.1107  -0.0573 -0.0500 354 LEU   B CD2 
3906 N  N   . LYS   B 199 ? 0.3034 0.4304 0.4686 0.0583  -0.0213 -0.0607 355 LYS   B N   
3907 C  CA  . LYS   B 199 ? 0.2942 0.4435 0.4780 0.0480  -0.0135 -0.0677 355 LYS   B CA  
3908 C  C   . LYS   B 199 ? 0.2750 0.4376 0.4665 0.0570  -0.0103 -0.0731 355 LYS   B C   
3909 O  O   . LYS   B 199 ? 0.3283 0.4762 0.5075 0.0696  -0.0128 -0.0698 355 LYS   B O   
3910 C  CB  . LYS   B 199 ? 0.3030 0.4354 0.4803 0.0322  -0.0046 -0.0622 355 LYS   B CB  
3911 C  CG  . LYS   B 199 ? 0.3203 0.4370 0.4880 0.0247  -0.0076 -0.0565 355 LYS   B CG  
3912 C  CD  . LYS   B 199 ? 0.3807 0.5015 0.5555 0.0083  -0.0005 -0.0581 355 LYS   B CD  
3913 C  CE  . LYS   B 199 ? 0.5208 0.6239 0.6844 0.0022  -0.0033 -0.0524 355 LYS   B CE  
3914 N  NZ  . LYS   B 199 ? 0.6613 0.7779 0.8322 0.0032  -0.0107 -0.0571 355 LYS   B NZ  
3915 N  N   . PRO   B 200 ? 0.2349 0.4253 0.4464 0.0508  -0.0045 -0.0821 356 PRO   B N   
3916 C  CA  . PRO   B 200 ? 0.1877 0.3932 0.4077 0.0592  -0.0005 -0.0881 356 PRO   B CA  
3917 C  C   . PRO   B 200 ? 0.3088 0.4910 0.5152 0.0558  0.0079  -0.0817 356 PRO   B C   
3918 O  O   . PRO   B 200 ? 0.3007 0.4596 0.4942 0.0450  0.0119  -0.0739 356 PRO   B O   
3919 C  CB  . PRO   B 200 ? 0.2564 0.4974 0.5014 0.0489  0.0054  -0.0992 356 PRO   B CB  
3920 C  CG  . PRO   B 200 ? 0.2684 0.5031 0.5132 0.0314  0.0080  -0.0967 356 PRO   B CG  
3921 C  CD  . PRO   B 200 ? 0.3054 0.5166 0.5334 0.0365  -0.0015 -0.0884 356 PRO   B CD  
3922 N  N   . PHE   B 201 ? 0.2418 0.4312 0.4508 0.0662  0.0103  -0.0858 357 PHE   B N   
3923 C  CA  . PHE   B 201 ? 0.2684 0.4411 0.4669 0.0635  0.0189  -0.0822 357 PHE   B CA  
3924 C  C   . PHE   B 201 ? 0.2173 0.4177 0.4335 0.0606  0.0280  -0.0915 357 PHE   B C   
3925 O  O   . PHE   B 201 ? 0.2141 0.4469 0.4504 0.0645  0.0262  -0.1014 357 PHE   B O   
3926 C  CB  . PHE   B 201 ? 0.2278 0.3767 0.4081 0.0788  0.0141  -0.0777 357 PHE   B CB  
3927 C  CG  . PHE   B 201 ? 0.2236 0.3892 0.4112 0.0975  0.0094  -0.0851 357 PHE   B CG  
3928 C  CD1 . PHE   B 201 ? 0.3374 0.5091 0.5260 0.1104  -0.0016 -0.0867 357 PHE   B CD1 
3929 C  CD2 . PHE   B 201 ? 0.2299 0.4041 0.4217 0.1033  0.0157  -0.0906 357 PHE   B CD2 
3930 C  CE1 . PHE   B 201 ? 0.2612 0.4475 0.4549 0.1297  -0.0067 -0.0936 357 PHE   B CE1 
3931 C  CE2 . PHE   B 201 ? 0.3103 0.5000 0.5084 0.1221  0.0110  -0.0979 357 PHE   B CE2 
3932 C  CZ  . PHE   B 201 ? 0.2846 0.4801 0.4835 0.1358  -0.0005 -0.0994 357 PHE   B CZ  
3933 N  N   . TYR   B 202 ? 0.3610 0.5501 0.5697 0.0535  0.0379  -0.0890 358 TYR   B N   
3934 C  CA  . TYR   B 202 ? 0.2671 0.4815 0.4915 0.0479  0.0484  -0.0975 358 TYR   B CA  
3935 C  C   . TYR   B 202 ? 0.2210 0.4301 0.4385 0.0579  0.0527  -0.0988 358 TYR   B C   
3936 O  O   . TYR   B 202 ? 0.2292 0.4095 0.4269 0.0642  0.0500  -0.0919 358 TYR   B O   
3937 C  CB  . TYR   B 202 ? 0.2470 0.4574 0.4709 0.0271  0.0586  -0.0947 358 TYR   B CB  
3938 C  CG  . TYR   B 202 ? 0.2534 0.4726 0.4865 0.0180  0.0546  -0.0956 358 TYR   B CG  
3939 C  CD1 . TYR   B 202 ? 0.3293 0.5832 0.5860 0.0132  0.0567  -0.1065 358 TYR   B CD1 
3940 C  CD2 . TYR   B 202 ? 0.2171 0.4115 0.4360 0.0147  0.0484  -0.0867 358 TYR   B CD2 
3941 C  CE1 . TYR   B 202 ? 0.3430 0.6049 0.6079 0.0048  0.0527  -0.1083 358 TYR   B CE1 
3942 C  CE2 . TYR   B 202 ? 0.3109 0.5129 0.5376 0.0071  0.0446  -0.0880 358 TYR   B CE2 
3943 C  CZ  . TYR   B 202 ? 0.3538 0.5889 0.6032 0.0021  0.0466  -0.0989 358 TYR   B CZ  
3944 O  OH  . TYR   B 202 ? 0.2924 0.5354 0.5495 -0.0061 0.0429  -0.1013 358 TYR   B OH  
3945 N  N   . LEU   B 203 ? 0.2157 0.4541 0.4503 0.0592  0.0596  -0.1089 359 LEU   B N   
3946 C  CA  . LEU   B 203 ? 0.2350 0.4729 0.4654 0.0691  0.0646  -0.1122 359 LEU   B CA  
3947 C  C   . LEU   B 203 ? 0.3362 0.5905 0.5754 0.0556  0.0793  -0.1171 359 LEU   B C   
3948 O  O   . LEU   B 203 ? 0.3220 0.6089 0.5830 0.0488  0.0840  -0.1259 359 LEU   B O   
3949 C  CB  . LEU   B 203 ? 0.2315 0.4908 0.4734 0.0897  0.0573  -0.1210 359 LEU   B CB  
3950 C  CG  . LEU   B 203 ? 0.3232 0.5555 0.5468 0.1075  0.0458  -0.1153 359 LEU   B CG  
3951 C  CD1 . LEU   B 203 ? 0.5116 0.7667 0.7468 0.1286  0.0383  -0.1245 359 LEU   B CD1 
3952 C  CD2 . LEU   B 203 ? 0.3022 0.5023 0.5035 0.1092  0.0502  -0.1093 359 LEU   B CD2 
3953 N  N   . VAL   B 204 ? 0.2609 0.4928 0.4826 0.0514  0.0868  -0.1117 360 VAL   B N   
3954 C  CA  . VAL   B 204 ? 0.3051 0.5456 0.5292 0.0377  0.1015  -0.1143 360 VAL   B CA  
3955 C  C   . VAL   B 204 ? 0.2922 0.5409 0.5163 0.0489  0.1070  -0.1206 360 VAL   B C   
3956 O  O   . VAL   B 204 ? 0.3244 0.5515 0.5328 0.0617  0.1015  -0.1172 360 VAL   B O   
3957 C  CB  . VAL   B 204 ? 0.2408 0.4490 0.4430 0.0240  0.1060  -0.1031 360 VAL   B CB  
3958 C  CG1 . VAL   B 204 ? 0.6713 0.8842 0.8714 0.0115  0.1214  -0.1048 360 VAL   B CG1 
3959 C  CG2 . VAL   B 204 ? 0.3589 0.5599 0.5616 0.0139  0.1008  -0.0976 360 VAL   B CG2 
3960 N  N   . PRO   B 205 ? 0.2831 0.5619 0.5236 0.0446  0.1180  -0.1304 361 PRO   B N   
3961 C  CA  . PRO   B 205 ? 0.3044 0.5914 0.5445 0.0563  0.1234  -0.1369 361 PRO   B CA  
3962 C  C   . PRO   B 205 ? 0.4501 0.7046 0.6640 0.0524  0.1296  -0.1291 361 PRO   B C   
3963 O  O   . PRO   B 205 ? 0.4359 0.6794 0.6403 0.0359  0.1385  -0.1237 361 PRO   B O   
3964 C  CB  . PRO   B 205 ? 0.2628 0.5888 0.5257 0.0477  0.1348  -0.1479 361 PRO   B CB  
3965 C  CG  . PRO   B 205 ? 0.3213 0.6478 0.5877 0.0261  0.1408  -0.1445 361 PRO   B CG  
3966 C  CD  . PRO   B 205 ? 0.3308 0.6354 0.5892 0.0271  0.1277  -0.1357 361 PRO   B CD  
3967 N  N   . LYS   B 206 ? 0.4176 0.6557 0.6184 0.0680  0.1247  -0.1287 362 LYS   B N   
3968 C  CA  . LYS   B 206 ? 0.3685 0.5748 0.5435 0.0658  0.1283  -0.1219 362 LYS   B CA  
3969 C  C   . LYS   B 206 ? 0.4082 0.6097 0.5765 0.0836  0.1267  -0.1271 362 LYS   B C   
3970 O  O   . LYS   B 206 ? 0.5417 0.7431 0.7136 0.0994  0.1165  -0.1296 362 LYS   B O   
3971 C  CB  . LYS   B 206 ? 0.4053 0.5780 0.5621 0.0615  0.1191  -0.1100 362 LYS   B CB  
3972 C  CG  . LYS   B 206 ? 0.5283 0.6705 0.6595 0.0575  0.1222  -0.1033 362 LYS   B CG  
3973 C  CD  . LYS   B 206 ? 0.6107 0.7527 0.7363 0.0405  0.1337  -0.1000 362 LYS   B CD  
3974 C  CE  . LYS   B 206 ? 0.8007 0.9164 0.9008 0.0389  0.1370  -0.0951 362 LYS   B CE  
3975 N  NZ  . LYS   B 206 ? 0.9247 1.0390 1.0165 0.0242  0.1489  -0.0919 362 LYS   B NZ  
3976 N  N   . HIS   B 207 ? 0.4481 0.6437 0.6049 0.0817  0.1366  -0.1287 363 HIS   B N   
3977 C  CA  . HIS   B 207 ? 0.6210 0.8105 0.7701 0.0983  0.1357  -0.1343 363 HIS   B CA  
3978 C  C   . HIS   B 207 ? 0.4832 0.6324 0.6066 0.1027  0.1275  -0.1265 363 HIS   B C   
3979 O  O   . HIS   B 207 ? 0.6388 0.7659 0.7474 0.0908  0.1266  -0.1175 363 HIS   B O   
3980 C  CB  . HIS   B 207 ? 0.4274 0.6297 0.5753 0.0955  0.1501  -0.1409 363 HIS   B CB  
3981 C  CG  . HIS   B 207 ? 0.7694 0.9546 0.8995 0.0787  0.1590  -0.1337 363 HIS   B CG  
3982 N  ND1 . HIS   B 207 ? 0.6877 0.8775 0.8104 0.0752  0.1720  -0.1377 363 HIS   B ND1 
3983 C  CD2 . HIS   B 207 ? 0.8359 0.9998 0.9533 0.0655  0.1566  -0.1230 363 HIS   B CD2 
3984 C  CE1 . HIS   B 207 ? 0.7473 0.9180 0.8522 0.0608  0.1769  -0.1292 363 HIS   B CE1 
3985 N  NE2 . HIS   B 207 ? 0.9139 1.0691 1.0157 0.0551  0.1676  -0.1204 363 HIS   B NE2 
3986 N  N   . ALA   B 208 ? 0.6151 0.7552 0.7334 0.1204  0.1216  -0.1308 364 ALA   B N   
3987 C  CA  . ALA   B 208 ? 0.6638 0.7666 0.7592 0.1259  0.1138  -0.1254 364 ALA   B CA  
3988 C  C   . ALA   B 208 ? 0.7164 0.8084 0.7980 0.1348  0.1190  -0.1313 364 ALA   B C   
3989 O  O   . ALA   B 208 ? 0.8277 0.9417 0.9199 0.1443  0.1250  -0.1408 364 ALA   B O   
3990 C  CB  . ALA   B 208 ? 0.5062 0.6008 0.6037 0.1390  0.1013  -0.1243 364 ALA   B CB  
3991 N  N   . LYS   B 209 ? 0.9602 1.0194 1.0186 0.1317  0.1168  -0.1265 365 LYS   B N   
3992 C  CA  . LYS   B 209 ? 0.9522 0.9973 0.9946 0.1389  0.1212  -0.1320 365 LYS   B CA  
3993 C  C   . LYS   B 209 ? 0.7401 0.7664 0.7746 0.1568  0.1136  -0.1357 365 LYS   B C   
3994 O  O   . LYS   B 209 ? 1.0834 1.1082 1.1244 0.1639  0.1050  -0.1335 365 LYS   B O   
3995 C  CB  . LYS   B 209 ? 0.8052 0.8254 0.8258 0.1263  0.1228  -0.1264 365 LYS   B CB  
3996 N  N   . GLN   B 215 ? 0.7527 0.9191 0.8745 0.1704  0.1311  -0.1598 371 GLN   B N   
3997 C  CA  . GLN   B 215 ? 0.7354 0.9263 0.8785 0.1757  0.1240  -0.1609 371 GLN   B CA  
3998 C  C   . GLN   B 215 ? 0.7330 0.9506 0.8945 0.1583  0.1290  -0.1599 371 GLN   B C   
3999 O  O   . GLN   B 215 ? 0.7459 0.9514 0.9021 0.1468  0.1292  -0.1549 371 GLN   B O   
4000 C  CB  . GLN   B 215 ? 0.5896 0.7572 0.7245 0.1872  0.1098  -0.1562 371 GLN   B CB  
4001 C  CG  . GLN   B 215 ? 0.5596 0.7512 0.7142 0.1929  0.1013  -0.1569 371 GLN   B CG  
4002 C  CD  . GLN   B 215 ? 0.6988 0.9068 0.8614 0.2075  0.0994  -0.1633 371 GLN   B CD  
4003 O  OE1 . GLN   B 215 ? 0.7337 0.9189 0.8810 0.2213  0.0957  -0.1636 371 GLN   B OE1 
4004 N  NE2 . GLN   B 215 ? 0.6777 0.9254 0.8642 0.2040  0.1021  -0.1689 371 GLN   B NE2 
4005 N  N   . GLU   B 216 ? 0.6183 0.8710 0.8010 0.1558  0.1329  -0.1650 372 GLU   B N   
4006 C  CA  . GLU   B 216 ? 0.7299 1.0070 0.9277 0.1364  0.1413  -0.1650 372 GLU   B CA  
4007 C  C   . GLU   B 216 ? 0.7135 1.0175 0.9342 0.1352  0.1341  -0.1669 372 GLU   B C   
4008 O  O   . GLU   B 216 ? 0.6967 1.0250 0.9326 0.1198  0.1410  -0.1687 372 GLU   B O   
4009 C  CB  . GLU   B 216 ? 0.4340 0.7289 0.6351 0.1293  0.1551  -0.1698 372 GLU   B CB  
4010 C  CG  . GLU   B 216 ? 0.6419 0.9169 0.8235 0.1171  0.1663  -0.1659 372 GLU   B CG  
4011 C  CD  . GLU   B 216 ? 0.7936 1.0760 0.9798 0.0947  0.1744  -0.1617 372 GLU   B CD  
4012 O  OE1 . GLU   B 216 ? 0.7494 1.0322 0.9435 0.0894  0.1679  -0.1584 372 GLU   B OE1 
4013 O  OE2 . GLU   B 216 ? 0.9823 1.2676 1.1624 0.0824  0.1872  -0.1613 372 GLU   B OE2 
4014 N  N   . GLU   B 217 ? 0.5142 0.8128 0.7361 0.1502  0.1203  -0.1662 373 GLU   B N   
4015 C  CA  . GLU   B 217 ? 0.4138 0.7366 0.6553 0.1494  0.1123  -0.1680 373 GLU   B CA  
4016 C  C   . GLU   B 217 ? 0.5993 0.9008 0.8332 0.1537  0.1003  -0.1614 373 GLU   B C   
4017 O  O   . GLU   B 217 ? 0.4878 0.7980 0.7293 0.1631  0.0890  -0.1621 373 GLU   B O   
4018 C  CB  . GLU   B 217 ? 0.6692 1.0154 0.9231 0.1645  0.1069  -0.1756 373 GLU   B CB  
4019 C  CG  . GLU   B 217 ? 0.6556 1.0428 0.9349 0.1539  0.1101  -0.1825 373 GLU   B CG  
4020 C  CD  . GLU   B 217 ? 0.7160 1.1163 1.0001 0.1357  0.1265  -0.1849 373 GLU   B CD  
4021 O  OE1 . GLU   B 217 ? 0.6069 1.0068 0.8853 0.1406  0.1340  -0.1881 373 GLU   B OE1 
4022 O  OE2 . GLU   B 217 ? 0.7259 1.1351 1.0177 0.1164  0.1320  -0.1834 373 GLU   B OE2 
4023 N  N   . THR   B 218 ? 0.4460 0.7192 0.6638 0.1468  0.1026  -0.1550 374 THR   B N   
4024 C  CA  . THR   B 218 ? 0.5187 0.7696 0.7278 0.1496  0.0922  -0.1486 374 THR   B CA  
4025 C  C   . THR   B 218 ? 0.3888 0.6447 0.6053 0.1292  0.0946  -0.1437 374 THR   B C   
4026 O  O   . THR   B 218 ? 0.4271 0.6958 0.6501 0.1125  0.1061  -0.1448 374 THR   B O   
4027 C  CB  . THR   B 218 ? 0.4309 0.6384 0.6117 0.1540  0.0904  -0.1416 374 THR   B CB  
4028 O  OG1 . THR   B 218 ? 0.4696 0.6707 0.6414 0.1438  0.1024  -0.1416 374 THR   B OG1 
4029 C  CG2 . THR   B 218 ? 0.6174 0.8107 0.7879 0.1765  0.0825  -0.1439 374 THR   B CG2 
4030 N  N   . TRP   B 219 ? 0.3615 0.6034 0.5737 0.1301  0.0834  -0.1369 375 TRP   B N   
4031 C  CA  . TRP   B 219 ? 0.2941 0.5325 0.5080 0.1117  0.0830  -0.1299 375 TRP   B CA  
4032 C  C   . TRP   B 219 ? 0.3218 0.5181 0.5109 0.1101  0.0758  -0.1176 375 TRP   B C   
4033 O  O   . TRP   B 219 ? 0.4205 0.5973 0.5973 0.1250  0.0672  -0.1156 375 TRP   B O   
4034 C  CB  . TRP   B 219 ? 0.3018 0.5703 0.5381 0.1133  0.0763  -0.1352 375 TRP   B CB  
4035 C  CG  . TRP   B 219 ? 0.3379 0.6505 0.6000 0.1146  0.0821  -0.1481 375 TRP   B CG  
4036 C  CD1 . TRP   B 219 ? 0.3236 0.6473 0.5877 0.1298  0.0792  -0.1533 375 TRP   B CD1 
4037 C  CD2 . TRP   B 219 ? 0.2543 0.5939 0.5342 0.0961  0.0895  -0.1519 375 TRP   B CD2 
4038 N  NE1 . TRP   B 219 ? 0.2786 0.6368 0.5622 0.1221  0.0842  -0.1608 375 TRP   B NE1 
4039 C  CE2 . TRP   B 219 ? 0.3452 0.7127 0.6381 0.1011  0.0906  -0.1600 375 TRP   B CE2 
4040 C  CE3 . TRP   B 219 ? 0.2900 0.6306 0.5747 0.0755  0.0955  -0.1492 375 TRP   B CE3 
4041 C  CZ2 . TRP   B 219 ? 0.2648 0.6614 0.5754 0.0856  0.0974  -0.1660 375 TRP   B CZ2 
4042 C  CZ3 . TRP   B 219 ? 0.2687 0.6353 0.5691 0.0601  0.1023  -0.1543 375 TRP   B CZ3 
4043 C  CH2 . TRP   B 219 ? 0.2985 0.6930 0.6118 0.0650  0.1032  -0.1628 375 TRP   B CH2 
4044 N  N   . ARG   B 220 ? 0.2754 0.4573 0.4565 0.0923  0.0797  -0.1098 376 ARG   B N   
4045 C  CA  . ARG   B 220 ? 0.2875 0.4327 0.4463 0.0886  0.0744  -0.0989 376 ARG   B CA  
4046 C  C   . ARG   B 220 ? 0.2689 0.4125 0.4313 0.0800  0.0680  -0.0933 376 ARG   B C   
4047 O  O   . ARG   B 220 ? 0.2816 0.4457 0.4588 0.0688  0.0720  -0.0955 376 ARG   B O   
4048 C  CB  . ARG   B 220 ? 0.2705 0.3979 0.4138 0.0767  0.0833  -0.0943 376 ARG   B CB  
4049 C  CG  . ARG   B 220 ? 0.3456 0.4371 0.4660 0.0755  0.0778  -0.0853 376 ARG   B CG  
4050 C  CD  . ARG   B 220 ? 0.3475 0.4241 0.4525 0.0659  0.0857  -0.0821 376 ARG   B CD  
4051 N  NE  . ARG   B 220 ? 0.3464 0.4301 0.4549 0.0503  0.0920  -0.0789 376 ARG   B NE  
4052 C  CZ  . ARG   B 220 ? 0.4964 0.5732 0.5939 0.0415  0.1006  -0.0768 376 ARG   B CZ  
4053 N  NH1 . ARG   B 220 ? 0.5784 0.6427 0.6616 0.0460  0.1036  -0.0780 376 ARG   B NH1 
4054 N  NH2 . ARG   B 220 ? 0.5138 0.5949 0.6132 0.0280  0.1064  -0.0736 376 ARG   B NH2 
4055 N  N   . LEU   B 221 ? 0.2541 0.3723 0.4021 0.0848  0.0588  -0.0864 377 LEU   B N   
4056 C  CA  . LEU   B 221 ? 0.2774 0.3921 0.4269 0.0784  0.0520  -0.0810 377 LEU   B CA  
4057 C  C   . LEU   B 221 ? 0.3669 0.4742 0.5123 0.0601  0.0577  -0.0752 377 LEU   B C   
4058 O  O   . LEU   B 221 ? 0.3312 0.4205 0.4621 0.0544  0.0627  -0.0712 377 LEU   B O   
4059 C  CB  . LEU   B 221 ? 0.2745 0.3611 0.4068 0.0869  0.0424  -0.0748 377 LEU   B CB  
4060 C  CG  . LEU   B 221 ? 0.3475 0.4374 0.4813 0.1058  0.0344  -0.0787 377 LEU   B CG  
4061 C  CD1 . LEU   B 221 ? 0.4057 0.4625 0.5185 0.1115  0.0269  -0.0714 377 LEU   B CD1 
4062 C  CD2 . LEU   B 221 ? 0.3038 0.4241 0.4581 0.1086  0.0298  -0.0840 377 LEU   B CD2 
4063 N  N   . SER   B 222 ? 0.2784 0.3989 0.4353 0.0515  0.0564  -0.0751 378 SER   B N   
4064 C  CA  . SER   B 222 ? 0.3045 0.4170 0.4570 0.0352  0.0611  -0.0697 378 SER   B CA  
4065 C  C   . SER   B 222 ? 0.3661 0.4730 0.5188 0.0324  0.0526  -0.0653 378 SER   B C   
4066 O  O   . SER   B 222 ? 0.2711 0.3956 0.4374 0.0373  0.0468  -0.0697 378 SER   B O   
4067 C  CB  . SER   B 222 ? 0.2436 0.3787 0.4103 0.0240  0.0717  -0.0752 378 SER   B CB  
4068 O  OG  . SER   B 222 ? 0.2819 0.4031 0.4394 0.0094  0.0770  -0.0690 378 SER   B OG  
4069 N  N   . PHE   B 223 ? 0.2849 0.3680 0.4220 0.0253  0.0517  -0.0571 379 PHE   B N   
4070 C  CA  . PHE   B 223 ? 0.2557 0.3297 0.3896 0.0217  0.0447  -0.0520 379 PHE   B CA  
4071 C  C   . PHE   B 223 ? 0.2608 0.3255 0.3886 0.0077  0.0497  -0.0472 379 PHE   B C   
4072 O  O   . PHE   B 223 ? 0.3826 0.4324 0.5016 0.0049  0.0449  -0.0415 379 PHE   B O   
4073 C  CB  . PHE   B 223 ? 0.3072 0.3587 0.4257 0.0296  0.0371  -0.0467 379 PHE   B CB  
4074 C  CG  . PHE   B 223 ? 0.2487 0.3036 0.3693 0.0442  0.0312  -0.0501 379 PHE   B CG  
4075 C  CD1 . PHE   B 223 ? 0.3263 0.3934 0.4561 0.0502  0.0240  -0.0524 379 PHE   B CD1 
4076 C  CD2 . PHE   B 223 ? 0.2675 0.3127 0.3794 0.0528  0.0327  -0.0513 379 PHE   B CD2 
4077 C  CE1 . PHE   B 223 ? 0.3960 0.4645 0.5253 0.0655  0.0181  -0.0553 379 PHE   B CE1 
4078 C  CE2 . PHE   B 223 ? 0.3482 0.3935 0.4596 0.0675  0.0273  -0.0543 379 PHE   B CE2 
4079 C  CZ  . PHE   B 223 ? 0.3581 0.4147 0.4777 0.0743  0.0199  -0.0560 379 PHE   B CZ  
4080 N  N   . SER   B 224 ? 0.2938 0.3661 0.4250 -0.0006 0.0597  -0.0495 380 SER   B N   
4081 C  CA  . SER   B 224 ? 0.2907 0.3497 0.4119 -0.0125 0.0650  -0.0443 380 SER   B CA  
4082 C  C   . SER   B 224 ? 0.3469 0.4073 0.4734 -0.0194 0.0615  -0.0431 380 SER   B C   
4083 O  O   . SER   B 224 ? 0.2820 0.3254 0.3966 -0.0257 0.0619  -0.0373 380 SER   B O   
4084 C  CB  . SER   B 224 ? 0.4795 0.5462 0.6026 -0.0201 0.0772  -0.0474 380 SER   B CB  
4085 O  OG  . SER   B 224 ? 0.6467 0.7397 0.7902 -0.0230 0.0808  -0.0555 380 SER   B OG  
4086 N  N   . HIS   B 225 ? 0.2752 0.3557 0.4187 -0.0175 0.0576  -0.0491 381 HIS   B N   
4087 C  CA  . HIS   B 225 ? 0.2861 0.3676 0.4340 -0.0231 0.0531  -0.0485 381 HIS   B CA  
4088 C  C   . HIS   B 225 ? 0.2393 0.3016 0.3744 -0.0178 0.0439  -0.0417 381 HIS   B C   
4089 O  O   . HIS   B 225 ? 0.2798 0.3301 0.4079 -0.0242 0.0429  -0.0375 381 HIS   B O   
4090 C  CB  . HIS   B 225 ? 0.2274 0.3366 0.3962 -0.0209 0.0497  -0.0573 381 HIS   B CB  
4091 C  CG  . HIS   B 225 ? 0.2131 0.3307 0.3862 -0.0055 0.0412  -0.0598 381 HIS   B CG  
4092 N  ND1 . HIS   B 225 ? 0.2208 0.3369 0.3901 0.0038  0.0426  -0.0603 381 HIS   B ND1 
4093 C  CD2 . HIS   B 225 ? 0.2871 0.4134 0.4662 0.0027  0.0312  -0.0620 381 HIS   B CD2 
4094 C  CE1 . HIS   B 225 ? 0.2334 0.3549 0.4054 0.0174  0.0340  -0.0624 381 HIS   B CE1 
4095 N  NE2 . HIS   B 225 ? 0.2855 0.4135 0.4632 0.0172  0.0269  -0.0632 381 HIS   B NE2 
4096 N  N   . ILE   B 226 ? 0.2910 0.3493 0.4219 -0.0064 0.0378  -0.0407 382 ILE   B N   
4097 C  CA  . ILE   B 226 ? 0.1939 0.2338 0.3120 -0.0024 0.0305  -0.0345 382 ILE   B CA  
4098 C  C   . ILE   B 226 ? 0.3188 0.3388 0.4212 -0.0079 0.0339  -0.0284 382 ILE   B C   
4099 O  O   . ILE   B 226 ? 0.3444 0.3525 0.4389 -0.0103 0.0302  -0.0239 382 ILE   B O   
4100 C  CB  . ILE   B 226 ? 0.3057 0.3426 0.4204 0.0101  0.0249  -0.0349 382 ILE   B CB  
4101 C  CG1 . ILE   B 226 ? 0.2864 0.3443 0.4159 0.0178  0.0209  -0.0415 382 ILE   B CG1 
4102 C  CG2 . ILE   B 226 ? 0.2196 0.2379 0.3212 0.0124  0.0183  -0.0290 382 ILE   B CG2 
4103 C  CD1 . ILE   B 226 ? 0.2914 0.3574 0.4276 0.0162  0.0148  -0.0424 382 ILE   B CD1 
4104 N  N   . GLU   B 227 ? 0.2913 0.3084 0.3889 -0.0093 0.0409  -0.0285 383 GLU   B N   
4105 C  CA  . GLU   B 227 ? 0.3073 0.3071 0.3893 -0.0134 0.0438  -0.0233 383 GLU   B CA  
4106 C  C   . GLU   B 227 ? 0.3322 0.3270 0.4116 -0.0222 0.0461  -0.0206 383 GLU   B C   
4107 O  O   . GLU   B 227 ? 0.2759 0.2569 0.3441 -0.0232 0.0431  -0.0159 383 GLU   B O   
4108 C  CB  . GLU   B 227 ? 0.3206 0.3200 0.3979 -0.0134 0.0514  -0.0246 383 GLU   B CB  
4109 C  CG  . GLU   B 227 ? 0.5111 0.5126 0.5887 -0.0045 0.0500  -0.0276 383 GLU   B CG  
4110 C  CD  . GLU   B 227 ? 0.5500 0.5549 0.6253 -0.0049 0.0585  -0.0303 383 GLU   B CD  
4111 O  OE1 . GLU   B 227 ? 0.4965 0.4955 0.5637 -0.0118 0.0649  -0.0279 383 GLU   B OE1 
4112 O  OE2 . GLU   B 227 ? 0.5513 0.5638 0.6315 0.0022  0.0591  -0.0348 383 GLU   B OE2 
4113 N  N   . LYS   B 228 ? 0.2320 0.2380 0.3212 -0.0289 0.0519  -0.0242 384 LYS   B N   
4114 C  CA  . LYS   B 228 ? 0.3016 0.3008 0.3876 -0.0379 0.0549  -0.0222 384 LYS   B CA  
4115 C  C   . LYS   B 228 ? 0.3695 0.3653 0.4563 -0.0368 0.0466  -0.0205 384 LYS   B C   
4116 O  O   . LYS   B 228 ? 0.3506 0.3314 0.4260 -0.0393 0.0456  -0.0160 384 LYS   B O   
4117 C  CB  . LYS   B 228 ? 0.3658 0.3799 0.4647 -0.0463 0.0627  -0.0279 384 LYS   B CB  
4118 C  CG  . LYS   B 228 ? 0.3619 0.3690 0.4589 -0.0564 0.0656  -0.0272 384 LYS   B CG  
4119 C  CD  . LYS   B 228 ? 0.5614 0.5856 0.6734 -0.0662 0.0734  -0.0344 384 LYS   B CD  
4120 C  CE  . LYS   B 228 ? 0.6613 0.6760 0.7703 -0.0770 0.0762  -0.0341 384 LYS   B CE  
4121 N  NZ  . LYS   B 228 ? 0.9988 1.0292 1.1236 -0.0774 0.0689  -0.0398 384 LYS   B NZ  
4122 N  N   . GLU   B 229 ? 0.3268 0.3359 0.4256 -0.0320 0.0403  -0.0241 385 GLU   B N   
4123 C  CA  . GLU   B 229 ? 0.2668 0.2737 0.3661 -0.0308 0.0325  -0.0230 385 GLU   B CA  
4124 C  C   . GLU   B 229 ? 0.3230 0.3128 0.4076 -0.0266 0.0279  -0.0169 385 GLU   B C   
4125 O  O   . GLU   B 229 ? 0.3863 0.3676 0.4652 -0.0292 0.0257  -0.0143 385 GLU   B O   
4126 C  CB  . GLU   B 229 ? 0.2631 0.2867 0.3754 -0.0246 0.0263  -0.0278 385 GLU   B CB  
4127 C  CG  . GLU   B 229 ? 0.5123 0.5567 0.6414 -0.0296 0.0293  -0.0352 385 GLU   B CG  
4128 C  CD  . GLU   B 229 ? 0.5976 0.6569 0.7377 -0.0248 0.0212  -0.0397 385 GLU   B CD  
4129 O  OE1 . GLU   B 229 ? 0.5394 0.5892 0.6718 -0.0202 0.0140  -0.0360 385 GLU   B OE1 
4130 O  OE2 . GLU   B 229 ? 0.7874 0.8686 0.9433 -0.0257 0.0220  -0.0473 385 GLU   B OE2 
4131 N  N   . ILE   B 230 ? 0.2399 0.2255 0.3188 -0.0207 0.0271  -0.0155 386 ILE   B N   
4132 C  CA  . ILE   B 230 ? 0.2763 0.2483 0.3430 -0.0178 0.0228  -0.0111 386 ILE   B CA  
4133 C  C   . ILE   B 230 ? 0.4095 0.3699 0.4647 -0.0219 0.0263  -0.0076 386 ILE   B C   
4134 O  O   . ILE   B 230 ? 0.4312 0.3838 0.4790 -0.0212 0.0225  -0.0049 386 ILE   B O   
4135 C  CB  . ILE   B 230 ? 0.4557 0.4249 0.5186 -0.0113 0.0207  -0.0112 386 ILE   B CB  
4136 C  CG1 . ILE   B 230 ? 0.4770 0.4464 0.5377 -0.0105 0.0265  -0.0126 386 ILE   B CG1 
4137 C  CG2 . ILE   B 230 ? 0.4536 0.4304 0.5242 -0.0055 0.0159  -0.0137 386 ILE   B CG2 
4138 C  CD1 . ILE   B 230 ? 0.4643 0.4321 0.5233 -0.0036 0.0248  -0.0143 386 ILE   B CD1 
4139 N  N   . LEU   B 231 ? 0.3893 0.3491 0.4426 -0.0256 0.0334  -0.0080 387 LEU   B N   
4140 C  CA  . LEU   B 231 ? 0.3790 0.3254 0.4181 -0.0278 0.0366  -0.0042 387 LEU   B CA  
4141 C  C   . LEU   B 231 ? 0.3133 0.2539 0.3507 -0.0323 0.0365  -0.0027 387 LEU   B C   
4142 O  O   . LEU   B 231 ? 0.3860 0.3149 0.4114 -0.0309 0.0348  0.0007  387 LEU   B O   
4143 C  CB  . LEU   B 231 ? 0.3134 0.2582 0.3478 -0.0301 0.0448  -0.0045 387 LEU   B CB  
4144 C  CG  . LEU   B 231 ? 0.5285 0.4706 0.5552 -0.0250 0.0447  -0.0042 387 LEU   B CG  
4145 C  CD1 . LEU   B 231 ? 0.5309 0.4761 0.5570 -0.0270 0.0531  -0.0060 387 LEU   B CD1 
4146 C  CD2 . LEU   B 231 ? 0.4788 0.4084 0.4899 -0.0227 0.0418  -0.0004 387 LEU   B CD2 
4147 N  N   . ASN   B 232 ? 0.2674 0.2164 0.3163 -0.0371 0.0382  -0.0060 388 ASN   B N   
4148 C  CA  . ASN   B 232 ? 0.3702 0.3123 0.4169 -0.0422 0.0387  -0.0054 388 ASN   B CA  
4149 C  C   . ASN   B 232 ? 0.3843 0.3301 0.4362 -0.0397 0.0307  -0.0062 388 ASN   B C   
4150 O  O   . ASN   B 232 ? 0.4878 0.4287 0.5387 -0.0435 0.0304  -0.0066 388 ASN   B O   
4151 C  CB  . ASN   B 232 ? 0.3152 0.2636 0.3705 -0.0510 0.0460  -0.0094 388 ASN   B CB  
4152 C  CG  . ASN   B 232 ? 0.4817 0.4221 0.5278 -0.0550 0.0556  -0.0078 388 ASN   B CG  
4153 O  OD1 . ASN   B 232 ? 0.4753 0.3976 0.5040 -0.0541 0.0578  -0.0028 388 ASN   B OD1 
4154 N  ND2 . ASN   B 232 ? 0.4251 0.3795 0.4823 -0.0586 0.0613  -0.0122 388 ASN   B ND2 
4155 N  N   . ASN   B 233 ? 0.2384 0.1909 0.2940 -0.0336 0.0246  -0.0064 389 ASN   B N   
4156 C  CA  . ASN   B 233 ? 0.2967 0.2510 0.3541 -0.0305 0.0174  -0.0064 389 ASN   B CA  
4157 C  C   . ASN   B 233 ? 0.2053 0.1570 0.2570 -0.0247 0.0139  -0.0042 389 ASN   B C   
4158 O  O   . ASN   B 233 ? 0.2740 0.2316 0.3303 -0.0210 0.0112  -0.0054 389 ASN   B O   
4159 C  CB  . ASN   B 233 ? 0.2144 0.1825 0.2851 -0.0308 0.0145  -0.0107 389 ASN   B CB  
4160 C  CG  . ASN   B 233 ? 0.3071 0.2750 0.3776 -0.0293 0.0081  -0.0107 389 ASN   B CG  
4161 O  OD1 . ASN   B 233 ? 0.2872 0.2457 0.3485 -0.0280 0.0061  -0.0076 389 ASN   B OD1 
4162 N  ND2 . ASN   B 233 ? 0.1685 0.1483 0.2491 -0.0291 0.0049  -0.0148 389 ASN   B ND2 
4163 N  N   . HIS   B 234 ? 0.2879 0.2300 0.3285 -0.0237 0.0141  -0.0012 390 HIS   B N   
4164 C  CA  . HIS   B 234 ? 0.2293 0.1690 0.2638 -0.0203 0.0135  -0.0002 390 HIS   B CA  
4165 C  C   . HIS   B 234 ? 0.2573 0.1948 0.2868 -0.0179 0.0086  0.0007  390 HIS   B C   
4166 O  O   . HIS   B 234 ? 0.2306 0.1670 0.2557 -0.0162 0.0081  0.0005  390 HIS   B O   
4167 C  CB  . HIS   B 234 ? 0.2335 0.1663 0.2588 -0.0207 0.0182  0.0013  390 HIS   B CB  
4168 C  CG  . HIS   B 234 ? 0.3249 0.2487 0.3409 -0.0211 0.0184  0.0036  390 HIS   B CG  
4169 N  ND1 . HIS   B 234 ? 0.3377 0.2544 0.3497 -0.0245 0.0237  0.0047  390 HIS   B ND1 
4170 C  CD2 . HIS   B 234 ? 0.2640 0.1841 0.2733 -0.0180 0.0143  0.0047  390 HIS   B CD2 
4171 C  CE1 . HIS   B 234 ? 0.4295 0.3360 0.4310 -0.0227 0.0225  0.0069  390 HIS   B CE1 
4172 N  NE2 . HIS   B 234 ? 0.3903 0.3003 0.3908 -0.0182 0.0165  0.0067  390 HIS   B NE2 
4173 N  N   . GLY   B 235 ? 0.2774 0.2149 0.3075 -0.0183 0.0055  0.0009  391 GLY   B N   
4174 C  CA  . GLY   B 235 ? 0.2903 0.2275 0.3161 -0.0168 0.0019  0.0012  391 GLY   B CA  
4175 C  C   . GLY   B 235 ? 0.2255 0.1662 0.2554 -0.0167 -0.0012 0.0005  391 GLY   B C   
4176 O  O   . GLY   B 235 ? 0.2208 0.1644 0.2566 -0.0167 -0.0017 -0.0001 391 GLY   B O   
4177 N  N   . LYS   B 236 ? 0.3460 0.2867 0.3719 -0.0165 -0.0030 0.0002  392 LYS   B N   
4178 C  CA  . LYS   B 236 ? 0.2093 0.1507 0.2358 -0.0169 -0.0053 0.0002  392 LYS   B CA  
4179 C  C   . LYS   B 236 ? 0.2910 0.2345 0.3195 -0.0169 -0.0073 0.0001  392 LYS   B C   
4180 O  O   . LYS   B 236 ? 0.2563 0.2008 0.2869 -0.0164 -0.0092 0.0001  392 LYS   B O   
4181 C  CB  . LYS   B 236 ? 0.2726 0.2140 0.2943 -0.0185 -0.0054 -0.0007 392 LYS   B CB  
4182 C  CG  . LYS   B 236 ? 0.1816 0.1219 0.2012 -0.0199 -0.0066 -0.0004 392 LYS   B CG  
4183 C  CD  . LYS   B 236 ? 0.2137 0.1536 0.2287 -0.0235 -0.0052 -0.0020 392 LYS   B CD  
4184 C  CE  . LYS   B 236 ? 0.2776 0.2100 0.2892 -0.0246 -0.0031 -0.0020 392 LYS   B CE  
4185 N  NZ  . LYS   B 236 ? 0.3073 0.2322 0.3174 -0.0216 -0.0037 0.0003  392 LYS   B NZ  
4186 N  N   . SER   B 237 ? 0.2271 0.1706 0.2537 -0.0166 -0.0073 -0.0001 393 SER   B N   
4187 C  CA  . SER   B 237 ? 0.3175 0.2610 0.3450 -0.0165 -0.0088 -0.0007 393 SER   B CA  
4188 C  C   . SER   B 237 ? 0.2850 0.2268 0.3168 -0.0179 -0.0073 -0.0009 393 SER   B C   
4189 O  O   . SER   B 237 ? 0.2475 0.1864 0.2787 -0.0186 -0.0042 -0.0003 393 SER   B O   
4190 C  CB  . SER   B 237 ? 0.2471 0.1895 0.2695 -0.0146 -0.0092 -0.0012 393 SER   B CB  
4191 O  OG  . SER   B 237 ? 0.3069 0.2462 0.3288 -0.0142 -0.0099 -0.0019 393 SER   B OG  
4192 N  N   . LYS   B 238 ? 0.2205 0.1647 0.2562 -0.0189 -0.0092 -0.0024 394 LYS   B N   
4193 C  CA  . LYS   B 238 ? 0.2304 0.1753 0.2716 -0.0217 -0.0076 -0.0041 394 LYS   B CA  
4194 C  C   . LYS   B 238 ? 0.2878 0.2242 0.3243 -0.0236 -0.0046 -0.0040 394 LYS   B C   
4195 O  O   . LYS   B 238 ? 0.2705 0.2049 0.3096 -0.0273 -0.0010 -0.0049 394 LYS   B O   
4196 C  CB  . LYS   B 238 ? 0.2999 0.2508 0.3463 -0.0223 -0.0110 -0.0068 394 LYS   B CB  
4197 C  CG  . LYS   B 238 ? 0.2197 0.1774 0.2699 -0.0195 -0.0137 -0.0069 394 LYS   B CG  
4198 C  CD  . LYS   B 238 ? 0.2059 0.1675 0.2561 -0.0180 -0.0184 -0.0086 394 LYS   B CD  
4199 C  CE  . LYS   B 238 ? 0.2138 0.1778 0.2626 -0.0134 -0.0212 -0.0075 394 LYS   B CE  
4200 N  NZ  . LYS   B 238 ? 0.2858 0.2529 0.3323 -0.0111 -0.0260 -0.0088 394 LYS   B NZ  
4201 N  N   . THR   B 239 ? 0.2460 0.1770 0.2749 -0.0209 -0.0058 -0.0031 395 THR   B N   
4202 C  CA  . THR   B 239 ? 0.3590 0.2787 0.3800 -0.0206 -0.0033 -0.0025 395 THR   B CA  
4203 C  C   . THR   B 239 ? 0.3208 0.2356 0.3341 -0.0172 -0.0015 0.0002  395 THR   B C   
4204 O  O   . THR   B 239 ? 0.3017 0.2070 0.3052 -0.0137 -0.0010 0.0012  395 THR   B O   
4205 C  CB  . THR   B 239 ? 0.3135 0.2300 0.3297 -0.0178 -0.0061 -0.0038 395 THR   B CB  
4206 O  OG1 . THR   B 239 ? 0.3766 0.3015 0.3932 -0.0142 -0.0094 -0.0039 395 THR   B OG1 
4207 C  CG2 . THR   B 239 ? 0.2979 0.2153 0.3191 -0.0218 -0.0070 -0.0070 395 THR   B CG2 
4208 N  N   . CYS   B 240 ? 0.2131 0.1336 0.2294 -0.0173 -0.0008 0.0011  396 CYS   B N   
4209 C  CA  . CYS   B 240 ? 0.2737 0.1900 0.2823 -0.0144 0.0009  0.0030  396 CYS   B CA  
4210 C  C   . CYS   B 240 ? 0.2710 0.1747 0.2721 -0.0158 0.0057  0.0047  396 CYS   B C   
4211 O  O   . CYS   B 240 ? 0.3869 0.2894 0.3929 -0.0213 0.0095  0.0041  396 CYS   B O   
4212 C  CB  . CYS   B 240 ? 0.3374 0.2607 0.3506 -0.0153 0.0016  0.0030  396 CYS   B CB  
4213 S  SG  . CYS   B 240 ? 0.3188 0.2394 0.3223 -0.0113 0.0025  0.0042  396 CYS   B SG  
4214 N  N   . CYS   B 241 ? 0.2570 0.1510 0.2455 -0.0106 0.0056  0.0065  397 CYS   B N   
4215 C  CA  . CYS   B 241 ? 0.2900 0.1676 0.2660 -0.0106 0.0104  0.0091  397 CYS   B CA  
4216 C  C   . CYS   B 241 ? 0.4128 0.2784 0.3863 -0.0147 0.0132  0.0087  397 CYS   B C   
4217 O  O   . CYS   B 241 ? 0.3583 0.2083 0.3219 -0.0175 0.0190  0.0107  397 CYS   B O   
4218 C  CB  . CYS   B 241 ? 0.3446 0.2219 0.3212 -0.0147 0.0157  0.0104  397 CYS   B CB  
4219 S  SG  . CYS   B 241 ? 0.3348 0.2185 0.3067 -0.0089 0.0136  0.0112  397 CYS   B SG  
4220 N  N   . GLU   B 242 ? 0.3406 0.2119 0.3217 -0.0157 0.0097  0.0059  398 GLU   B N   
4221 C  CA  . GLU   B 242 ? 0.3101 0.1698 0.2882 -0.0195 0.0118  0.0044  398 GLU   B CA  
4222 C  C   . GLU   B 242 ? 0.3372 0.1860 0.3034 -0.0119 0.0088  0.0047  398 GLU   B C   
4223 O  O   . GLU   B 242 ? 0.4220 0.2585 0.3835 -0.0142 0.0103  0.0033  398 GLU   B O   
4224 C  CB  . GLU   B 242 ? 0.3044 0.1770 0.2978 -0.0257 0.0100  0.0003  398 GLU   B CB  
4225 C  CG  . GLU   B 242 ? 0.3395 0.2225 0.3448 -0.0328 0.0132  -0.0011 398 GLU   B CG  
4226 C  CD  . GLU   B 242 ? 0.4032 0.2967 0.4214 -0.0384 0.0115  -0.0059 398 GLU   B CD  
4227 O  OE1 . GLU   B 242 ? 0.5034 0.3966 0.5211 -0.0368 0.0075  -0.0078 398 GLU   B OE1 
4228 O  OE2 . GLU   B 242 ? 0.4760 0.3792 0.5047 -0.0440 0.0139  -0.0082 398 GLU   B OE2 
4229 N  N   . ASN   B 243 ? 0.3917 0.2452 0.3530 -0.0028 0.0046  0.0058  399 ASN   B N   
4230 C  CA  . ASN   B 243 ? 0.4577 0.3029 0.4076 0.0064  0.0015  0.0056  399 ASN   B CA  
4231 C  C   . ASN   B 243 ? 0.3730 0.2220 0.3154 0.0158  -0.0013 0.0072  399 ASN   B C   
4232 O  O   . ASN   B 243 ? 0.4430 0.3023 0.3904 0.0142  -0.0012 0.0080  399 ASN   B O   
4233 C  CB  . ASN   B 243 ? 0.3002 0.1572 0.2590 0.0075  -0.0030 0.0016  399 ASN   B CB  
4234 C  CG  . ASN   B 243 ? 0.3833 0.2630 0.3548 0.0074  -0.0067 0.0000  399 ASN   B CG  
4235 O  OD1 . ASN   B 243 ? 0.4363 0.3242 0.4062 0.0131  -0.0091 0.0001  399 ASN   B OD1 
4236 N  ND2 . ASN   B 243 ? 0.3111 0.2008 0.2946 0.0007  -0.0071 -0.0019 399 ASN   B ND2 
4237 N  N   . LYS   B 244 ? 0.4067 0.2476 0.3366 0.0263  -0.0042 0.0071  400 LYS   B N   
4238 C  CA  . LYS   B 244 ? 0.3840 0.2285 0.3051 0.0368  -0.0075 0.0080  400 LYS   B CA  
4239 C  C   . LYS   B 244 ? 0.4612 0.3330 0.3966 0.0376  -0.0123 0.0042  400 LYS   B C   
4240 O  O   . LYS   B 244 ? 0.5248 0.4046 0.4587 0.0408  -0.0139 0.0043  400 LYS   B O   
4241 C  CB  . LYS   B 244 ? 0.4781 0.3088 0.3826 0.0495  -0.0102 0.0080  400 LYS   B CB  
4242 C  CG  . LYS   B 244 ? 0.5222 0.3211 0.4055 0.0511  -0.0051 0.0127  400 LYS   B CG  
4243 C  CD  . LYS   B 244 ? 0.7363 0.5207 0.6017 0.0660  -0.0086 0.0126  400 LYS   B CD  
4244 C  CE  . LYS   B 244 ? 0.5748 0.3232 0.4146 0.0687  -0.0032 0.0181  400 LYS   B CE  
4245 N  NZ  . LYS   B 244 ? 0.7401 0.4711 0.5617 0.0835  -0.0064 0.0177  400 LYS   B NZ  
4246 N  N   . GLU   B 245 ? 0.3546 0.2399 0.3026 0.0345  -0.0143 0.0006  401 GLU   B N   
4247 C  CA  . GLU   B 245 ? 0.3612 0.2704 0.3214 0.0339  -0.0176 -0.0032 401 GLU   B CA  
4248 C  C   . GLU   B 245 ? 0.3829 0.2997 0.3521 0.0251  -0.0155 -0.0021 401 GLU   B C   
4249 O  O   . GLU   B 245 ? 0.4315 0.3645 0.4074 0.0245  -0.0175 -0.0048 401 GLU   B O   
4250 C  CB  . GLU   B 245 ? 0.2990 0.2183 0.2682 0.0320  -0.0191 -0.0068 401 GLU   B CB  
4251 C  CG  . GLU   B 245 ? 0.5972 0.5397 0.5754 0.0333  -0.0221 -0.0115 401 GLU   B CG  
4252 C  CD  . GLU   B 245 ? 0.7169 0.6663 0.6892 0.0453  -0.0261 -0.0150 401 GLU   B CD  
4253 O  OE1 . GLU   B 245 ? 0.6467 0.5837 0.6093 0.0531  -0.0270 -0.0146 401 GLU   B OE1 
4254 O  OE2 . GLU   B 245 ? 0.7004 0.6680 0.6775 0.0472  -0.0284 -0.0186 401 GLU   B OE2 
4255 N  N   . GLU   B 246 ? 0.3824 0.2881 0.3519 0.0182  -0.0113 0.0010  402 GLU   B N   
4256 C  CA  . GLU   B 246 ? 0.4279 0.3407 0.4068 0.0106  -0.0093 0.0015  402 GLU   B CA  
4257 C  C   . GLU   B 246 ? 0.3877 0.2902 0.3600 0.0092  -0.0054 0.0047  402 GLU   B C   
4258 O  O   . GLU   B 246 ? 0.4511 0.3537 0.4299 0.0024  -0.0021 0.0056  402 GLU   B O   
4259 C  CB  . GLU   B 246 ? 0.3764 0.2912 0.3654 0.0033  -0.0081 0.0010  402 GLU   B CB  
4260 C  CG  . GLU   B 246 ? 0.4662 0.3912 0.4610 0.0036  -0.0112 -0.0020 402 GLU   B CG  
4261 C  CD  . GLU   B 246 ? 0.4699 0.3958 0.4724 -0.0025 -0.0106 -0.0024 402 GLU   B CD  
4262 O  OE1 . GLU   B 246 ? 0.3227 0.2557 0.3320 -0.0065 -0.0105 -0.0023 402 GLU   B OE1 
4263 O  OE2 . GLU   B 246 ? 0.4313 0.3503 0.4321 -0.0028 -0.0105 -0.0030 402 GLU   B OE2 
4264 N  N   . LYS   B 247 ? 0.3845 0.2787 0.3434 0.0162  -0.0056 0.0063  403 LYS   B N   
4265 C  CA  . LYS   B 247 ? 0.4422 0.3268 0.3931 0.0151  -0.0015 0.0094  403 LYS   B CA  
4266 C  C   . LYS   B 247 ? 0.4083 0.3063 0.3633 0.0152  -0.0032 0.0076  403 LYS   B C   
4267 O  O   . LYS   B 247 ? 0.3459 0.2539 0.2993 0.0211  -0.0079 0.0049  403 LYS   B O   
4268 C  CB  . LYS   B 247 ? 0.3321 0.1986 0.2633 0.0230  -0.0007 0.0125  403 LYS   B CB  
4269 C  CG  . LYS   B 247 ? 0.5565 0.4041 0.4807 0.0213  0.0027  0.0145  403 LYS   B CG  
4270 C  CD  . LYS   B 247 ? 0.6300 0.4642 0.5515 0.0124  0.0107  0.0174  403 LYS   B CD  
4271 C  CE  . LYS   B 247 ? 0.4995 0.3196 0.4199 0.0067  0.0145  0.0174  403 LYS   B CE  
4272 N  NZ  . LYS   B 247 ? 0.7627 0.5550 0.6610 0.0092  0.0195  0.0214  403 LYS   B NZ  
4273 N  N   . CYS   B 248 ? 0.3641 0.2630 0.3247 0.0086  0.0007  0.0083  404 CYS   B N   
4274 C  CA  . CYS   B 248 ? 0.3290 0.2373 0.2922 0.0079  0.0001  0.0065  404 CYS   B CA  
4275 C  C   . CYS   B 248 ? 0.3356 0.2337 0.2879 0.0086  0.0046  0.0093  404 CYS   B C   
4276 O  O   . CYS   B 248 ? 0.3496 0.2334 0.2938 0.0077  0.0092  0.0127  404 CYS   B O   
4277 C  CB  . CYS   B 248 ? 0.2643 0.1821 0.2421 0.0009  0.0008  0.0046  404 CYS   B CB  
4278 S  SG  . CYS   B 248 ? 0.2921 0.2045 0.2745 -0.0054 0.0073  0.0064  404 CYS   B SG  
4279 N  N   . CYS   B 249 ? 0.3232 0.2281 0.2745 0.0094  0.0038  0.0074  405 CYS   B N   
4280 C  CA  . CYS   B 249 ? 0.3893 0.2855 0.3282 0.0111  0.0076  0.0095  405 CYS   B CA  
4281 C  C   . CYS   B 249 ? 0.3807 0.2807 0.3272 0.0050  0.0120  0.0084  405 CYS   B C   
4282 O  O   . CYS   B 249 ? 0.4451 0.3435 0.3836 0.0066  0.0138  0.0082  405 CYS   B O   
4283 C  CB  . CYS   B 249 ? 0.3231 0.2230 0.2507 0.0193  0.0027  0.0077  405 CYS   B CB  
4284 S  SG  . CYS   B 249 ? 0.3798 0.2999 0.3184 0.0176  -0.0022 0.0009  405 CYS   B SG  
4285 N  N   . ARG   B 250 ? 0.3554 0.2603 0.3163 -0.0010 0.0135  0.0075  406 ARG   B N   
4286 C  CA  . ARG   B 250 ? 0.3437 0.2529 0.3122 -0.0052 0.0170  0.0060  406 ARG   B CA  
4287 C  C   . ARG   B 250 ? 0.2943 0.1951 0.2560 -0.0069 0.0243  0.0082  406 ARG   B C   
4288 O  O   . ARG   B 250 ? 0.4357 0.3367 0.3924 -0.0061 0.0269  0.0073  406 ARG   B O   
4289 C  CB  . ARG   B 250 ? 0.3122 0.2279 0.2961 -0.0095 0.0164  0.0047  406 ARG   B CB  
4290 C  CG  . ARG   B 250 ? 0.2491 0.1728 0.2394 -0.0092 0.0110  0.0020  406 ARG   B CG  
4291 C  CD  . ARG   B 250 ? 0.3348 0.2623 0.3370 -0.0123 0.0106  0.0016  406 ARG   B CD  
4292 N  NE  . ARG   B 250 ? 0.2179 0.1503 0.2240 -0.0127 0.0066  -0.0004 406 ARG   B NE  
4293 C  CZ  . ARG   B 250 ? 0.2093 0.1441 0.2171 -0.0129 0.0033  -0.0004 406 ARG   B CZ  
4294 N  NH1 . ARG   B 250 ? 0.2402 0.1729 0.2463 -0.0117 0.0027  0.0011  406 ARG   B NH1 
4295 N  NH2 . ARG   B 250 ? 0.2332 0.1716 0.2436 -0.0144 0.0011  -0.0022 406 ARG   B NH2 
4296 N  N   . LYS   B 251 ? 0.3265 0.2197 0.2874 -0.0100 0.0284  0.0108  407 LYS   B N   
4297 C  CA  . LYS   B 251 ? 0.3440 0.2295 0.2993 -0.0138 0.0368  0.0126  407 LYS   B CA  
4298 C  C   . LYS   B 251 ? 0.4111 0.2853 0.3463 -0.0092 0.0390  0.0153  407 LYS   B C   
4299 O  O   . LYS   B 251 ? 0.4212 0.2929 0.3513 -0.0112 0.0454  0.0155  407 LYS   B O   
4300 C  CB  . LYS   B 251 ? 0.3294 0.2076 0.2865 -0.0191 0.0408  0.0141  407 LYS   B CB  
4301 C  CG  . LYS   B 251 ? 0.4010 0.2913 0.3776 -0.0238 0.0390  0.0109  407 LYS   B CG  
4302 C  CD  . LYS   B 251 ? 0.4127 0.2960 0.3906 -0.0300 0.0431  0.0114  407 LYS   B CD  
4303 C  CE  . LYS   B 251 ? 0.8627 0.7457 0.8428 -0.0375 0.0528  0.0104  407 LYS   B CE  
4304 N  NZ  . LYS   B 251 ? 0.6820 0.5620 0.6675 -0.0456 0.0568  0.0089  407 LYS   B NZ  
4305 N  N   . ASP   B 252 ? 0.3910 0.2591 0.3140 -0.0024 0.0336  0.0170  408 ASP   B N   
4306 C  CA  . ASP   B 252 ? 0.3470 0.2046 0.2490 0.0039  0.0343  0.0194  408 ASP   B CA  
4307 C  C   . ASP   B 252 ? 0.3451 0.2130 0.2473 0.0063  0.0323  0.0160  408 ASP   B C   
4308 O  O   . ASP   B 252 ? 0.4368 0.2978 0.3252 0.0079  0.0365  0.0173  408 ASP   B O   
4309 C  CB  . ASP   B 252 ? 0.4449 0.2961 0.3349 0.0124  0.0278  0.0210  408 ASP   B CB  
4310 C  CG  . ASP   B 252 ? 0.5750 0.4080 0.4555 0.0116  0.0316  0.0254  408 ASP   B CG  
4311 O  OD1 . ASP   B 252 ? 0.5682 0.3937 0.4509 0.0032  0.0399  0.0270  408 ASP   B OD1 
4312 O  OD2 . ASP   B 252 ? 0.8243 0.6509 0.6953 0.0192  0.0265  0.0267  408 ASP   B OD2 
4313 N  N   . CYS   B 253 ? 0.3245 0.2075 0.2410 0.0061  0.0263  0.0114  409 CYS   B N   
4314 C  CA  . CYS   B 253 ? 0.3871 0.2785 0.3043 0.0070  0.0249  0.0073  409 CYS   B CA  
4315 C  C   . CYS   B 253 ? 0.3931 0.2839 0.3140 0.0022  0.0325  0.0069  409 CYS   B C   
4316 O  O   . CYS   B 253 ? 0.3765 0.2661 0.2881 0.0040  0.0348  0.0056  409 CYS   B O   
4317 C  CB  . CYS   B 253 ? 0.3776 0.2825 0.3089 0.0059  0.0184  0.0025  409 CYS   B CB  
4318 S  SG  . CYS   B 253 ? 0.4254 0.3374 0.3521 0.0123  0.0092  0.0001  409 CYS   B SG  
4319 N  N   . LEU   B 254 ? 0.3504 0.2434 0.2849 -0.0036 0.0364  0.0073  410 LEU   B N   
4320 C  CA  . LEU   B 254 ? 0.3395 0.2347 0.2792 -0.0076 0.0439  0.0060  410 LEU   B CA  
4321 C  C   . LEU   B 254 ? 0.3153 0.1991 0.2390 -0.0082 0.0519  0.0094  410 LEU   B C   
4322 O  O   . LEU   B 254 ? 0.4302 0.3146 0.3491 -0.0082 0.0569  0.0079  410 LEU   B O   
4323 C  CB  . LEU   B 254 ? 0.3233 0.2252 0.2809 -0.0129 0.0458  0.0052  410 LEU   B CB  
4324 C  CG  . LEU   B 254 ? 0.4422 0.3491 0.4063 -0.0164 0.0537  0.0030  410 LEU   B CG  
4325 C  CD1 . LEU   B 254 ? 0.3651 0.2783 0.3314 -0.0131 0.0526  -0.0010 410 LEU   B CD1 
4326 C  CD2 . LEU   B 254 ? 0.4278 0.3432 0.4093 -0.0212 0.0555  0.0015  410 LEU   B CD2 
4327 N  N   . LYS   B 255 ? 0.3353 0.2070 0.2493 -0.0089 0.0539  0.0139  411 LYS   B N   
4328 C  CA  . LYS   B 255 ? 0.3227 0.1793 0.2178 -0.0099 0.0623  0.0179  411 LYS   B CA  
4329 C  C   . LYS   B 255 ? 0.3573 0.2088 0.2332 -0.0026 0.0605  0.0184  411 LYS   B C   
4330 O  O   . LYS   B 255 ? 0.4321 0.2777 0.2965 -0.0037 0.0681  0.0194  411 LYS   B O   
4331 C  CB  . LYS   B 255 ? 0.4061 0.2466 0.2906 -0.0105 0.0636  0.0228  411 LYS   B CB  
4332 C  CG  . LYS   B 255 ? 0.5651 0.4055 0.4622 -0.0203 0.0701  0.0226  411 LYS   B CG  
4333 C  CD  . LYS   B 255 ? 0.7235 0.5420 0.6036 -0.0218 0.0743  0.0278  411 LYS   B CD  
4334 C  CE  . LYS   B 255 ? 0.7414 0.5593 0.6277 -0.0196 0.0666  0.0279  411 LYS   B CE  
4335 N  NZ  . LYS   B 255 ? 0.9074 0.7307 0.8113 -0.0294 0.0701  0.0254  411 LYS   B NZ  
4336 N  N   . LEU   B 256 ? 0.3328 0.1875 0.2048 0.0048  0.0507  0.0173  412 LEU   B N   
4337 C  CA  . LEU   B 256 ? 0.3555 0.2075 0.2093 0.0124  0.0477  0.0168  412 LEU   B CA  
4338 C  C   . LEU   B 256 ? 0.3936 0.2561 0.2532 0.0109  0.0493  0.0116  412 LEU   B C   
4339 O  O   . LEU   B 256 ? 0.3577 0.2146 0.2011 0.0136  0.0529  0.0119  412 LEU   B O   
4340 C  CB  . LEU   B 256 ? 0.3657 0.2231 0.2174 0.0201  0.0364  0.0151  412 LEU   B CB  
4341 C  CG  . LEU   B 256 ? 0.4205 0.2656 0.2611 0.0249  0.0340  0.0199  412 LEU   B CG  
4342 C  CD1 . LEU   B 256 ? 0.3423 0.1994 0.1892 0.0311  0.0228  0.0164  412 LEU   B CD1 
4343 C  CD2 . LEU   B 256 ? 0.4229 0.2487 0.2346 0.0314  0.0376  0.0251  412 LEU   B CD2 
4344 N  N   . MET   B 257 ? 0.3371 0.2134 0.2181 0.0070  0.0469  0.0069  413 MET   B N   
4345 C  CA  . MET   B 257 ? 0.3586 0.2426 0.2448 0.0058  0.0490  0.0019  413 MET   B CA  
4346 C  C   . MET   B 257 ? 0.4131 0.2929 0.2961 0.0021  0.0601  0.0031  413 MET   B C   
4347 O  O   . MET   B 257 ? 0.4297 0.3086 0.3027 0.0040  0.0636  0.0010  413 MET   B O   
4348 C  CB  . MET   B 257 ? 0.2989 0.1945 0.2067 0.0027  0.0451  -0.0024 413 MET   B CB  
4349 C  CG  . MET   B 257 ? 0.3770 0.2788 0.2878 0.0052  0.0354  -0.0057 413 MET   B CG  
4350 S  SD  . MET   B 257 ? 0.6539 0.5574 0.5500 0.0099  0.0317  -0.0108 413 MET   B SD  
4351 C  CE  . MET   B 257 ? 0.5098 0.4181 0.4173 0.0063  0.0343  -0.0169 413 MET   B CE  
4352 N  N   . LYS   B 258 ? 0.3646 0.2427 0.2561 -0.0037 0.0661  0.0059  414 LYS   B N   
4353 C  CA  . LYS   B 258 ? 0.3465 0.2234 0.2372 -0.0086 0.0776  0.0062  414 LYS   B CA  
4354 C  C   . LYS   B 258 ? 0.4044 0.2657 0.2691 -0.0070 0.0838  0.0106  414 LYS   B C   
4355 O  O   . LYS   B 258 ? 0.4289 0.2901 0.2869 -0.0082 0.0918  0.0092  414 LYS   B O   
4356 C  CB  . LYS   B 258 ? 0.3573 0.2375 0.2635 -0.0160 0.0822  0.0071  414 LYS   B CB  
4357 C  CG  . LYS   B 258 ? 0.4846 0.3814 0.4157 -0.0172 0.0782  0.0021  414 LYS   B CG  
4358 C  CD  . LYS   B 258 ? 0.4642 0.3661 0.4106 -0.0240 0.0814  0.0023  414 LYS   B CD  
4359 C  CE  . LYS   B 258 ? 0.5633 0.4627 0.5062 -0.0311 0.0939  0.0029  414 LYS   B CE  
4360 N  NZ  . LYS   B 258 ? 0.8689 0.7868 0.8337 -0.0353 0.0984  -0.0029 414 LYS   B NZ  
4361 N  N   . TYR   B 259 ? 0.4648 0.3123 0.3133 -0.0036 0.0805  0.0158  415 TYR   B N   
4362 C  CA  . TYR   B 259 ? 0.4672 0.2967 0.2870 -0.0002 0.0856  0.0207  415 TYR   B CA  
4363 C  C   . TYR   B 259 ? 0.4501 0.2824 0.2569 0.0072  0.0817  0.0177  415 TYR   B C   
4364 O  O   . TYR   B 259 ? 0.4467 0.2702 0.2348 0.0079  0.0891  0.0193  415 TYR   B O   
4365 C  CB  . TYR   B 259 ? 0.4423 0.2558 0.2466 0.0043  0.0812  0.0266  415 TYR   B CB  
4366 C  CG  . TYR   B 259 ? 0.5403 0.3303 0.3117 0.0081  0.0872  0.0330  415 TYR   B CG  
4367 C  CD1 . TYR   B 259 ? 0.5533 0.3329 0.3142 0.0011  0.1011  0.0355  415 TYR   B CD1 
4368 C  CD2 . TYR   B 259 ? 0.5291 0.3073 0.2791 0.0192  0.0793  0.0365  415 TYR   B CD2 
4369 C  CE1 . TYR   B 259 ? 0.8644 0.6196 0.5926 0.0043  0.1073  0.0420  415 TYR   B CE1 
4370 C  CE2 . TYR   B 259 ? 0.5410 0.2954 0.2582 0.0242  0.0843  0.0429  415 TYR   B CE2 
4371 C  CZ  . TYR   B 259 ? 0.6389 0.3804 0.3443 0.0165  0.0986  0.0460  415 TYR   B CZ  
4372 O  OH  . TYR   B 259 ? 0.7573 0.4722 0.4271 0.0212  0.1046  0.0531  415 TYR   B OH  
4373 N  N   . LEU   B 260 ? 0.3930 0.2374 0.2088 0.0122  0.0705  0.0130  416 LEU   B N   
4374 C  CA  . LEU   B 260 ? 0.4232 0.2724 0.2291 0.0181  0.0662  0.0084  416 LEU   B CA  
4375 C  C   . LEU   B 260 ? 0.5050 0.3594 0.3152 0.0141  0.0746  0.0045  416 LEU   B C   
4376 O  O   . LEU   B 260 ? 0.4192 0.2679 0.2105 0.0172  0.0786  0.0042  416 LEU   B O   
4377 C  CB  . LEU   B 260 ? 0.3899 0.2530 0.2095 0.0209  0.0542  0.0027  416 LEU   B CB  
4378 C  CG  . LEU   B 260 ? 0.4300 0.3007 0.2433 0.0255  0.0485  -0.0041 416 LEU   B CG  
4379 C  CD1 . LEU   B 260 ? 0.4518 0.3135 0.2373 0.0340  0.0461  -0.0019 416 LEU   B CD1 
4380 C  CD2 . LEU   B 260 ? 0.3633 0.2475 0.1930 0.0252  0.0383  -0.0098 416 LEU   B CD2 
4381 N  N   . LEU   B 261 ? 0.4216 0.2869 0.2557 0.0080  0.0773  0.0013  417 LEU   B N   
4382 C  CA  . LEU   B 261 ? 0.4351 0.3070 0.2748 0.0055  0.0850  -0.0032 417 LEU   B CA  
4383 C  C   . LEU   B 261 ? 0.5002 0.3633 0.3268 0.0019  0.0981  0.0006  417 LEU   B C   
4384 O  O   . LEU   B 261 ? 0.4864 0.3491 0.3024 0.0031  0.1041  -0.0019 417 LEU   B O   
4385 C  CB  . LEU   B 261 ? 0.3739 0.2591 0.2411 0.0014  0.0847  -0.0073 417 LEU   B CB  
4386 C  CG  . LEU   B 261 ? 0.3942 0.2872 0.2671 0.0011  0.0915  -0.0130 417 LEU   B CG  
4387 C  CD1 . LEU   B 261 ? 0.3892 0.2810 0.2499 0.0067  0.0875  -0.0179 417 LEU   B CD1 
4388 C  CD2 . LEU   B 261 ? 0.3432 0.2487 0.2415 -0.0010 0.0909  -0.0169 417 LEU   B CD2 
4389 N  N   . GLU   B 262 ? 0.4774 0.3329 0.3040 -0.0034 0.1033  0.0062  418 GLU   B N   
4390 C  CA  . GLU   B 262 ? 0.5107 0.3567 0.3247 -0.0090 0.1171  0.0096  418 GLU   B CA  
4391 C  C   . GLU   B 262 ? 0.5098 0.3391 0.2909 -0.0034 0.1194  0.0135  418 GLU   B C   
4392 O  O   . GLU   B 262 ? 0.4737 0.3003 0.2433 -0.0053 0.1296  0.0129  418 GLU   B O   
4393 C  CB  . GLU   B 262 ? 0.4894 0.3275 0.3073 -0.0163 0.1216  0.0147  418 GLU   B CB  
4394 C  CG  . GLU   B 262 ? 0.5072 0.3628 0.3565 -0.0229 0.1217  0.0104  418 GLU   B CG  
4395 C  CD  . GLU   B 262 ? 0.6450 0.4927 0.4978 -0.0297 0.1240  0.0146  418 GLU   B CD  
4396 O  OE1 . GLU   B 262 ? 0.6922 0.5202 0.5237 -0.0328 0.1314  0.0205  418 GLU   B OE1 
4397 O  OE2 . GLU   B 262 ? 0.5621 0.4218 0.4375 -0.0319 0.1185  0.0120  418 GLU   B OE2 
4398 N  N   . GLN   B 263 ? 0.4741 0.2931 0.2394 0.0044  0.1096  0.0171  419 GLN   B N   
4399 C  CA  . GLN   B 263 ? 0.5324 0.3354 0.2647 0.0117  0.1101  0.0208  419 GLN   B CA  
4400 C  C   . GLN   B 263 ? 0.5434 0.3558 0.2709 0.0167  0.1078  0.0144  419 GLN   B C   
4401 O  O   . GLN   B 263 ? 0.5919 0.3944 0.2957 0.0189  0.1148  0.0160  419 GLN   B O   
4402 C  CB  . GLN   B 263 ? 0.5329 0.3264 0.2518 0.0206  0.0985  0.0248  419 GLN   B CB  
4403 C  CG  . GLN   B 263 ? 0.6799 0.4578 0.3951 0.0171  0.1017  0.0320  419 GLN   B CG  
4404 C  CD  . GLN   B 263 ? 0.6919 0.4472 0.3828 0.0125  0.1162  0.0388  419 GLN   B CD  
4405 O  OE1 . GLN   B 263 ? 0.7647 0.5016 0.4233 0.0200  0.1172  0.0435  419 GLN   B OE1 
4406 N  NE2 . GLN   B 263 ? 0.7731 0.5297 0.4785 -0.0001 0.1279  0.0389  419 GLN   B NE2 
4407 N  N   . LEU   B 264 ? 0.5200 0.3500 0.2682 0.0184  0.0986  0.0070  420 LEU   B N   
4408 C  CA  . LEU   B 264 ? 0.5165 0.3544 0.2605 0.0224  0.0967  -0.0001 420 LEU   B CA  
4409 C  C   . LEU   B 264 ? 0.5652 0.4069 0.3131 0.0171  0.1096  -0.0028 420 LEU   B C   
4410 O  O   . LEU   B 264 ? 0.5101 0.3489 0.2406 0.0203  0.1136  -0.0052 420 LEU   B O   
4411 C  CB  . LEU   B 264 ? 0.5818 0.4351 0.3464 0.0239  0.0850  -0.0075 420 LEU   B CB  
4412 C  CG  . LEU   B 264 ? 0.5186 0.3722 0.2774 0.0302  0.0717  -0.0074 420 LEU   B CG  
4413 C  CD1 . LEU   B 264 ? 0.5061 0.3746 0.2877 0.0287  0.0626  -0.0147 420 LEU   B CD1 
4414 C  CD2 . LEU   B 264 ? 0.4707 0.3182 0.2011 0.0387  0.0682  -0.0082 420 LEU   B CD2 
4415 N  N   . LYS   B 265 ? 0.4766 0.3260 0.2472 0.0093  0.1162  -0.0032 421 LYS   B N   
4416 C  CA  . LYS   B 265 ? 0.6188 0.4747 0.3950 0.0045  0.1290  -0.0065 421 LYS   B CA  
4417 C  C   . LYS   B 265 ? 0.6642 0.5052 0.4153 0.0016  0.1418  -0.0008 421 LYS   B C   
4418 O  O   . LYS   B 265 ? 0.6328 0.4758 0.3760 0.0009  0.1514  -0.0038 421 LYS   B O   
4419 C  CB  . LYS   B 265 ? 0.4876 0.3572 0.2942 -0.0025 0.1323  -0.0087 421 LYS   B CB  
4420 C  CG  . LYS   B 265 ? 0.4689 0.3526 0.2989 0.0005  0.1222  -0.0151 421 LYS   B CG  
4421 C  CD  . LYS   B 265 ? 0.4534 0.3504 0.3110 -0.0051 0.1254  -0.0170 421 LYS   B CD  
4422 C  CE  . LYS   B 265 ? 0.4830 0.3910 0.3480 -0.0078 0.1376  -0.0219 421 LYS   B CE  
4423 N  NZ  . LYS   B 265 ? 0.6061 0.5307 0.4994 -0.0116 0.1393  -0.0253 421 LYS   B NZ  
4424 N  N   . GLU   B 266 ? 0.6105 0.4351 0.3473 0.0001  0.1427  0.0076  422 GLU   B N   
4425 C  CA  . GLU   B 266 ? 0.6510 0.4565 0.3594 -0.0027 0.1552  0.0140  422 GLU   B CA  
4426 C  C   . GLU   B 266 ? 0.7157 0.5104 0.3925 0.0069  0.1527  0.0147  422 GLU   B C   
4427 O  O   . GLU   B 266 ? 0.6835 0.4720 0.3424 0.0053  0.1643  0.0151  422 GLU   B O   
4428 C  CB  . GLU   B 266 ? 0.7138 0.5010 0.4125 -0.0057 0.1560  0.0228  422 GLU   B CB  
4429 C  CG  . GLU   B 266 ? 0.9429 0.7157 0.6290 -0.0162 0.1736  0.0279  422 GLU   B CG  
4430 C  CD  . GLU   B 266 ? 1.1486 0.9391 0.8666 -0.0287 0.1821  0.0233  422 GLU   B CD  
4431 O  OE1 . GLU   B 266 ? 0.9862 0.7936 0.7168 -0.0323 0.1899  0.0168  422 GLU   B OE1 
4432 O  OE2 . GLU   B 266 ? 1.2429 1.0314 0.9734 -0.0344 0.1809  0.0257  422 GLU   B OE2 
4433 N  N   . ARG   B 267 ? 0.7161 0.5096 0.3857 0.0168  0.1376  0.0143  423 ARG   B N   
4434 C  CA  . ARG   B 267 ? 0.6807 0.4649 0.3195 0.0268  0.1337  0.0145  423 ARG   B CA  
4435 C  C   . ARG   B 267 ? 0.7273 0.5234 0.3675 0.0275  0.1374  0.0062  423 ARG   B C   
4436 O  O   . ARG   B 267 ? 0.8729 0.6591 0.4849 0.0320  0.1420  0.0070  423 ARG   B O   
4437 C  CB  . ARG   B 267 ? 0.7501 0.5367 0.3863 0.0368  0.1160  0.0134  423 ARG   B CB  
4438 C  CG  . ARG   B 267 ? 0.9239 0.7095 0.5358 0.0475  0.1090  0.0097  423 ARG   B CG  
4439 C  CD  . ARG   B 267 ? 0.7666 0.5607 0.3811 0.0563  0.0912  0.0061  423 ARG   B CD  
4440 N  NE  . ARG   B 267 ? 0.9232 0.7063 0.5313 0.0601  0.0860  0.0137  423 ARG   B NE  
4441 C  CZ  . ARG   B 267 ? 0.9672 0.7354 0.5445 0.0711  0.0810  0.0189  423 ARG   B CZ  
4442 N  NH1 . ARG   B 267 ? 0.9258 0.6879 0.4745 0.0790  0.0808  0.0179  423 ARG   B NH1 
4443 N  NH2 . ARG   B 267 ? 0.9528 0.7117 0.5268 0.0750  0.0760  0.0250  423 ARG   B NH2 
4444 N  N   . PHE   B 268 ? 0.7825 0.5985 0.4537 0.0237  0.1358  -0.0019 424 PHE   B N   
4445 C  CA  . PHE   B 268 ? 0.6858 0.5129 0.3602 0.0253  0.1382  -0.0107 424 PHE   B CA  
4446 C  C   . PHE   B 268 ? 0.6499 0.4866 0.3416 0.0171  0.1525  -0.0135 424 PHE   B C   
4447 O  O   . PHE   B 268 ? 0.6801 0.5305 0.3868 0.0179  0.1529  -0.0221 424 PHE   B O   
4448 C  CB  . PHE   B 268 ? 0.6266 0.4675 0.3195 0.0292  0.1243  -0.0190 424 PHE   B CB  
4449 C  CG  . PHE   B 268 ? 0.7542 0.5909 0.4321 0.0371  0.1103  -0.0189 424 PHE   B CG  
4450 C  CD1 . PHE   B 268 ? 0.6614 0.4933 0.3128 0.0443  0.1078  -0.0217 424 PHE   B CD1 
4451 C  CD2 . PHE   B 268 ? 0.6507 0.4899 0.3410 0.0375  0.0996  -0.0167 424 PHE   B CD2 
4452 C  CE1 . PHE   B 268 ? 0.7226 0.5539 0.3612 0.0521  0.0942  -0.0228 424 PHE   B CE1 
4453 C  CE2 . PHE   B 268 ? 0.7186 0.5573 0.3968 0.0450  0.0867  -0.0177 424 PHE   B CE2 
4454 C  CZ  . PHE   B 268 ? 0.6851 0.5206 0.3378 0.0524  0.0838  -0.0210 424 PHE   B CZ  
4455 N  N   . LYS   B 269 ? 0.8184 0.6479 0.5077 0.0094  0.1645  -0.0070 425 LYS   B N   
4456 C  CA  . LYS   B 269 ? 0.7997 0.6424 0.5095 0.0009  0.1777  -0.0107 425 LYS   B CA  
4457 C  C   . LYS   B 269 ? 0.8883 0.7340 0.5855 0.0015  0.1892  -0.0155 425 LYS   B C   
4458 O  O   . LYS   B 269 ? 0.8075 0.6698 0.5250 -0.0028 0.1979  -0.0218 425 LYS   B O   
4459 C  CB  . LYS   B 269 ? 0.7715 0.6065 0.4825 -0.0093 0.1879  -0.0035 425 LYS   B CB  
4460 C  CG  . LYS   B 269 ? 0.8747 0.6868 0.5503 -0.0119 0.1998  0.0045  425 LYS   B CG  
4461 C  CD  . LYS   B 269 ? 1.0125 0.8146 0.6904 -0.0229 0.2087  0.0113  425 LYS   B CD  
4462 C  CE  . LYS   B 269 ? 0.9143 0.6936 0.5619 -0.0262 0.2183  0.0191  425 LYS   B CE  
4463 N  NZ  . LYS   B 269 ? 1.1539 0.9252 0.8092 -0.0381 0.2251  0.0240  425 LYS   B NZ  
4464 N  N   . ASP   B 270 ? 0.9096 0.7406 0.5737 0.0075  0.1893  -0.0133 426 ASP   B N   
4465 C  CA  . ASP   B 270 ? 0.9501 0.7833 0.6000 0.0088  0.2000  -0.0181 426 ASP   B CA  
4466 C  C   . ASP   B 270 ? 0.8481 0.6949 0.5082 0.0164  0.1914  -0.0289 426 ASP   B C   
4467 O  O   . ASP   B 270 ? 1.1145 0.9663 0.7679 0.0178  0.1999  -0.0349 426 ASP   B O   
4468 C  CB  . ASP   B 270 ? 1.0639 0.8762 0.6753 0.0122  0.2022  -0.0109 426 ASP   B CB  
4469 C  CG  . ASP   B 270 ? 1.2647 1.0602 0.8669 0.0060  0.2062  0.0004  426 ASP   B CG  
4470 O  OD1 . ASP   B 270 ? 1.1516 0.9524 0.7703 -0.0051 0.2176  0.0017  426 ASP   B OD1 
4471 O  OD2 . ASP   B 270 ? 1.0794 0.8571 0.6588 0.0123  0.1974  0.0074  426 ASP   B OD2 
4472 N  N   . LYS   B 271 ? 0.9834 0.8351 0.6582 0.0208  0.1756  -0.0317 427 LYS   B N   
4473 C  CA  . LYS   B 271 ? 0.7911 0.6558 0.4827 0.0254  0.1683  -0.0422 427 LYS   B CA  
4474 C  C   . LYS   B 271 ? 0.8224 0.7020 0.5501 0.0211  0.1678  -0.0449 427 LYS   B C   
4475 O  O   . LYS   B 271 ? 0.9052 0.7855 0.6448 0.0150  0.1700  -0.0389 427 LYS   B O   
4476 C  CB  . LYS   B 271 ? 0.8856 0.7454 0.5684 0.0323  0.1517  -0.0443 427 LYS   B CB  
4477 C  CG  . LYS   B 271 ? 1.0373 0.8830 0.6836 0.0377  0.1501  -0.0408 427 LYS   B CG  
4478 C  CD  . LYS   B 271 ? 1.0418 0.8862 0.6817 0.0441  0.1330  -0.0434 427 LYS   B CD  
4479 C  CE  . LYS   B 271 ? 1.0825 0.9147 0.6851 0.0512  0.1310  -0.0409 427 LYS   B CE  
4480 N  NZ  . LYS   B 271 ? 1.2209 1.0560 0.8177 0.0579  0.1142  -0.0456 427 LYS   B NZ  
4481 N  N   . LYS   B 272 ? 0.8375 0.7280 0.5812 0.0247  0.1649  -0.0543 428 LYS   B N   
4482 C  CA  . LYS   B 272 ? 0.8965 0.8009 0.6724 0.0228  0.1639  -0.0575 428 LYS   B CA  
4483 C  C   . LYS   B 272 ? 0.6876 0.5910 0.4763 0.0254  0.1485  -0.0588 428 LYS   B C   
4484 O  O   . LYS   B 272 ? 0.6075 0.5202 0.4205 0.0254  0.1460  -0.0617 428 LYS   B O   
4485 C  CB  . LYS   B 272 ? 0.7674 0.6839 0.5535 0.0261  0.1717  -0.0670 428 LYS   B CB  
4486 C  CG  . LYS   B 272 ? 1.0720 0.9827 0.8394 0.0329  0.1702  -0.0742 428 LYS   B CG  
4487 C  CD  . LYS   B 272 ? 1.0118 0.9314 0.7771 0.0344  0.1843  -0.0804 428 LYS   B CD  
4488 C  CE  . LYS   B 272 ? 1.1243 1.0386 0.8674 0.0295  0.1968  -0.0746 428 LYS   B CE  
4489 N  NZ  . LYS   B 272 ? 0.9339 0.8616 0.6824 0.0282  0.2129  -0.0799 428 LYS   B NZ  
4490 N  N   . HIS   B 273 ? 0.6081 0.5009 0.3806 0.0277  0.1383  -0.0568 429 HIS   B N   
4491 C  CA  . HIS   B 273 ? 0.5501 0.4428 0.3332 0.0295  0.1247  -0.0597 429 HIS   B CA  
4492 C  C   . HIS   B 273 ? 0.6285 0.5253 0.4333 0.0254  0.1204  -0.0546 429 HIS   B C   
4493 O  O   . HIS   B 273 ? 0.6316 0.5315 0.4527 0.0262  0.1130  -0.0582 429 HIS   B O   
4494 C  CB  . HIS   B 273 ? 0.6268 0.5108 0.3886 0.0323  0.1152  -0.0592 429 HIS   B CB  
4495 C  CG  . HIS   B 273 ? 0.7869 0.6670 0.5266 0.0368  0.1175  -0.0653 429 HIS   B CG  
4496 N  ND1 . HIS   B 273 ? 0.8283 0.7110 0.5717 0.0395  0.1179  -0.0753 429 HIS   B ND1 
4497 C  CD2 . HIS   B 273 ? 0.8606 0.7334 0.5728 0.0396  0.1195  -0.0629 429 HIS   B CD2 
4498 C  CE1 . HIS   B 273 ? 0.9474 0.8257 0.6675 0.0432  0.1201  -0.0793 429 HIS   B CE1 
4499 N  NE2 . HIS   B 273 ? 0.9960 0.8687 0.6966 0.0435  0.1209  -0.0718 429 HIS   B NE2 
4500 N  N   . LEU   B 274 ? 0.5124 0.4077 0.3162 0.0210  0.1251  -0.0464 430 LEU   B N   
4501 C  CA  . LEU   B 274 ? 0.5876 0.4855 0.4089 0.0171  0.1204  -0.0414 430 LEU   B CA  
4502 C  C   . LEU   B 274 ? 0.6050 0.5132 0.4458 0.0123  0.1296  -0.0405 430 LEU   B C   
4503 O  O   . LEU   B 274 ? 0.5945 0.5048 0.4482 0.0082  0.1273  -0.0360 430 LEU   B O   
4504 C  CB  . LEU   B 274 ? 0.5098 0.3970 0.3154 0.0159  0.1168  -0.0331 430 LEU   B CB  
4505 C  CG  . LEU   B 274 ? 0.5729 0.4536 0.3619 0.0211  0.1056  -0.0343 430 LEU   B CG  
4506 C  CD1 . LEU   B 274 ? 0.4900 0.3615 0.2660 0.0216  0.1015  -0.0261 430 LEU   B CD1 
4507 C  CD2 . LEU   B 274 ? 0.4568 0.3438 0.2621 0.0222  0.0951  -0.0405 430 LEU   B CD2 
4508 N  N   . ASP   B 275 ? 0.6862 0.6025 0.5301 0.0128  0.1398  -0.0455 431 ASP   B N   
4509 C  CA  . ASP   B 275 ? 0.5048 0.4342 0.3672 0.0078  0.1494  -0.0458 431 ASP   B CA  
4510 C  C   . ASP   B 275 ? 0.5716 0.5127 0.4615 0.0089  0.1430  -0.0487 431 ASP   B C   
4511 O  O   . ASP   B 275 ? 0.4945 0.4461 0.4009 0.0039  0.1475  -0.0476 431 ASP   B O   
4512 C  CB  . ASP   B 275 ? 0.6381 0.5760 0.4980 0.0089  0.1617  -0.0519 431 ASP   B CB  
4513 C  CG  . ASP   B 275 ? 0.8286 0.7567 0.6634 0.0049  0.1724  -0.0476 431 ASP   B CG  
4514 O  OD1 . ASP   B 275 ? 0.8665 0.7809 0.6867 0.0014  0.1706  -0.0393 431 ASP   B OD1 
4515 O  OD2 . ASP   B 275 ? 1.0407 0.9740 0.8692 0.0059  0.1828  -0.0523 431 ASP   B OD2 
4516 N  N   . LYS   B 276 ? 0.4871 0.4257 0.3810 0.0151  0.1328  -0.0527 432 LYS   B N   
4517 C  CA  . LYS   B 276 ? 0.4022 0.3498 0.3190 0.0177  0.1272  -0.0556 432 LYS   B CA  
4518 C  C   . LYS   B 276 ? 0.4416 0.3844 0.3649 0.0150  0.1171  -0.0501 432 LYS   B C   
4519 O  O   . LYS   B 276 ? 0.4206 0.3702 0.3619 0.0166  0.1127  -0.0514 432 LYS   B O   
4520 C  CB  . LYS   B 276 ? 0.5253 0.4703 0.4420 0.0259  0.1229  -0.0632 432 LYS   B CB  
4521 C  CG  . LYS   B 276 ? 0.4847 0.4396 0.4039 0.0305  0.1325  -0.0705 432 LYS   B CG  
4522 C  CD  . LYS   B 276 ? 0.5456 0.4952 0.4643 0.0393  0.1278  -0.0779 432 LYS   B CD  
4523 C  CE  . LYS   B 276 ? 0.8264 0.7886 0.7523 0.0456  0.1367  -0.0857 432 LYS   B CE  
4524 N  NZ  . LYS   B 276 ? 0.7850 0.7388 0.7081 0.0552  0.1324  -0.0932 432 LYS   B NZ  
4525 N  N   . PHE   B 277 ? 0.4238 0.3555 0.3324 0.0118  0.1134  -0.0442 433 PHE   B N   
4526 C  CA  . PHE   B 277 ? 0.3969 0.3248 0.3110 0.0094  0.1045  -0.0392 433 PHE   B CA  
4527 C  C   . PHE   B 277 ? 0.4627 0.3951 0.3848 0.0030  0.1094  -0.0339 433 PHE   B C   
4528 O  O   . PHE   B 277 ? 0.3969 0.3281 0.3101 -0.0010 0.1189  -0.0315 433 PHE   B O   
4529 C  CB  . PHE   B 277 ? 0.4331 0.3487 0.3284 0.0101  0.0975  -0.0364 433 PHE   B CB  
4530 C  CG  . PHE   B 277 ? 0.4586 0.3702 0.3468 0.0148  0.0921  -0.0426 433 PHE   B CG  
4531 C  CD1 . PHE   B 277 ? 0.4905 0.4016 0.3891 0.0160  0.0840  -0.0457 433 PHE   B CD1 
4532 C  CD2 . PHE   B 277 ? 0.4359 0.3431 0.3059 0.0173  0.0955  -0.0457 433 PHE   B CD2 
4533 C  CE1 . PHE   B 277 ? 0.4766 0.3822 0.3679 0.0188  0.0798  -0.0520 433 PHE   B CE1 
4534 C  CE2 . PHE   B 277 ? 0.4579 0.3612 0.3213 0.0208  0.0906  -0.0525 433 PHE   B CE2 
4535 C  CZ  . PHE   B 277 ? 0.4262 0.3283 0.3005 0.0210  0.0829  -0.0558 433 PHE   B CZ  
4536 N  N   . SER   B 278 ? 0.4223 0.3588 0.3600 0.0015  0.1034  -0.0322 434 SER   B N   
4537 C  CA  . SER   B 278 ? 0.4183 0.3605 0.3665 -0.0049 0.1075  -0.0287 434 SER   B CA  
4538 C  C   . SER   B 278 ? 0.3997 0.3362 0.3507 -0.0064 0.0983  -0.0239 434 SER   B C   
4539 O  O   . SER   B 278 ? 0.3300 0.2616 0.2792 -0.0026 0.0890  -0.0242 434 SER   B O   
4540 C  CB  . SER   B 278 ? 0.4043 0.3644 0.3747 -0.0048 0.1116  -0.0340 434 SER   B CB  
4541 O  OG  . SER   B 278 ? 0.4518 0.4160 0.4357 0.0002  0.1022  -0.0363 434 SER   B OG  
4542 N  N   . SER   B 279 ? 0.4208 0.3578 0.3759 -0.0127 0.1018  -0.0200 435 SER   B N   
4543 C  CA  . SER   B 279 ? 0.3729 0.3062 0.3328 -0.0143 0.0940  -0.0161 435 SER   B CA  
4544 C  C   . SER   B 279 ? 0.3575 0.3009 0.3364 -0.0113 0.0866  -0.0195 435 SER   B C   
4545 O  O   . SER   B 279 ? 0.4231 0.3631 0.4046 -0.0111 0.0787  -0.0170 435 SER   B O   
4546 C  CB  . SER   B 279 ? 0.3918 0.3233 0.3527 -0.0222 0.1003  -0.0123 435 SER   B CB  
4547 O  OG  . SER   B 279 ? 0.4428 0.3905 0.4239 -0.0262 0.1051  -0.0166 435 SER   B OG  
4548 N  N   . TYR   B 280 ? 0.3475 0.3030 0.3387 -0.0083 0.0892  -0.0252 436 TYR   B N   
4549 C  CA  . TYR   B 280 ? 0.3169 0.2789 0.3222 -0.0035 0.0818  -0.0281 436 TYR   B CA  
4550 C  C   . TYR   B 280 ? 0.3100 0.2607 0.3061 0.0013  0.0737  -0.0280 436 TYR   B C   
4551 O  O   . TYR   B 280 ? 0.3423 0.2909 0.3436 0.0025  0.0662  -0.0270 436 TYR   B O   
4552 C  CB  . TYR   B 280 ? 0.3584 0.3349 0.3767 0.0008  0.0861  -0.0346 436 TYR   B CB  
4553 C  CG  . TYR   B 280 ? 0.3664 0.3503 0.3995 0.0061  0.0791  -0.0371 436 TYR   B CG  
4554 C  CD1 . TYR   B 280 ? 0.3620 0.3558 0.4090 0.0028  0.0770  -0.0363 436 TYR   B CD1 
4555 C  CD2 . TYR   B 280 ? 0.3265 0.3057 0.3580 0.0146  0.0743  -0.0402 436 TYR   B CD2 
4556 C  CE1 . TYR   B 280 ? 0.2940 0.2940 0.3524 0.0087  0.0701  -0.0383 436 TYR   B CE1 
4557 C  CE2 . TYR   B 280 ? 0.3678 0.3507 0.4095 0.0204  0.0679  -0.0417 436 TYR   B CE2 
4558 C  CZ  . TYR   B 280 ? 0.3669 0.3607 0.4219 0.0179  0.0656  -0.0406 436 TYR   B CZ  
4559 O  OH  . TYR   B 280 ? 0.3993 0.3965 0.4626 0.0247  0.0587  -0.0420 436 TYR   B OH  
4560 N  N   . HIS   B 281 ? 0.3364 0.2797 0.3182 0.0033  0.0756  -0.0294 437 HIS   B N   
4561 C  CA  . HIS   B 281 ? 0.3839 0.3172 0.3566 0.0060  0.0684  -0.0303 437 HIS   B CA  
4562 C  C   . HIS   B 281 ? 0.3292 0.2565 0.2967 0.0027  0.0623  -0.0256 437 HIS   B C   
4563 O  O   . HIS   B 281 ? 0.3122 0.2362 0.2819 0.0032  0.0552  -0.0258 437 HIS   B O   
4564 C  CB  . HIS   B 281 ? 0.2967 0.2247 0.2544 0.0082  0.0719  -0.0335 437 HIS   B CB  
4565 C  CG  . HIS   B 281 ? 0.3518 0.2852 0.3137 0.0125  0.0778  -0.0391 437 HIS   B CG  
4566 N  ND1 . HIS   B 281 ? 0.3799 0.3162 0.3346 0.0125  0.0864  -0.0408 437 HIS   B ND1 
4567 C  CD2 . HIS   B 281 ? 0.3014 0.2374 0.2729 0.0178  0.0764  -0.0436 437 HIS   B CD2 
4568 C  CE1 . HIS   B 281 ? 0.3516 0.2939 0.3128 0.0175  0.0901  -0.0466 437 HIS   B CE1 
4569 N  NE2 . HIS   B 281 ? 0.3627 0.3046 0.3339 0.0214  0.0839  -0.0483 437 HIS   B NE2 
4570 N  N   . VAL   B 282 ? 0.2969 0.2219 0.2563 -0.0004 0.0653  -0.0213 438 VAL   B N   
4571 C  CA  . VAL   B 282 ? 0.3049 0.2247 0.2589 -0.0022 0.0598  -0.0169 438 VAL   B CA  
4572 C  C   . VAL   B 282 ? 0.2843 0.2082 0.2529 -0.0040 0.0552  -0.0153 438 VAL   B C   
4573 O  O   . VAL   B 282 ? 0.2840 0.2057 0.2527 -0.0037 0.0481  -0.0147 438 VAL   B O   
4574 C  CB  . VAL   B 282 ? 0.4257 0.3400 0.3675 -0.0044 0.0651  -0.0123 438 VAL   B CB  
4575 C  CG1 . VAL   B 282 ? 0.4124 0.3212 0.3499 -0.0050 0.0594  -0.0078 438 VAL   B CG1 
4576 C  CG2 . VAL   B 282 ? 0.3816 0.2902 0.3054 -0.0016 0.0682  -0.0134 438 VAL   B CG2 
4577 N  N   . LYS   B 283 ? 0.3372 0.2684 0.3183 -0.0059 0.0593  -0.0154 439 LYS   B N   
4578 C  CA  . LYS   B 283 ? 0.2802 0.2161 0.2745 -0.0074 0.0551  -0.0142 439 LYS   B CA  
4579 C  C   . LYS   B 283 ? 0.2479 0.1844 0.2483 -0.0036 0.0488  -0.0168 439 LYS   B C   
4580 O  O   . LYS   B 283 ? 0.3166 0.2515 0.3200 -0.0043 0.0428  -0.0151 439 LYS   B O   
4581 C  CB  . LYS   B 283 ? 0.3459 0.2921 0.3528 -0.0103 0.0611  -0.0154 439 LYS   B CB  
4582 C  CG  . LYS   B 283 ? 0.5741 0.5173 0.5772 -0.0165 0.0660  -0.0117 439 LYS   B CG  
4583 C  CD  . LYS   B 283 ? 0.5548 0.5107 0.5729 -0.0209 0.0717  -0.0144 439 LYS   B CD  
4584 C  CE  . LYS   B 283 ? 0.5423 0.5015 0.5572 -0.0238 0.0824  -0.0164 439 LYS   B CE  
4585 N  NZ  . LYS   B 283 ? 0.7197 0.6980 0.7534 -0.0239 0.0862  -0.0226 439 LYS   B NZ  
4586 N  N   . THR   B 284 ? 0.2492 0.1867 0.2503 0.0004  0.0505  -0.0210 440 THR   B N   
4587 C  CA  . THR   B 284 ? 0.2681 0.2017 0.2714 0.0042  0.0454  -0.0233 440 THR   B CA  
4588 C  C   . THR   B 284 ? 0.3444 0.2685 0.3378 0.0024  0.0401  -0.0225 440 THR   B C   
4589 O  O   . THR   B 284 ? 0.2623 0.1834 0.2584 0.0017  0.0351  -0.0216 440 THR   B O   
4590 C  CB  . THR   B 284 ? 0.2770 0.2106 0.2795 0.0095  0.0489  -0.0283 440 THR   B CB  
4591 O  OG1 . THR   B 284 ? 0.3426 0.2886 0.3554 0.0109  0.0544  -0.0299 440 THR   B OG1 
4592 C  CG2 . THR   B 284 ? 0.2684 0.1951 0.2719 0.0142  0.0443  -0.0303 440 THR   B CG2 
4593 N  N   . ALA   B 285 ? 0.2601 0.1805 0.2419 0.0014  0.0414  -0.0235 441 ALA   B N   
4594 C  CA  . ALA   B 285 ? 0.3356 0.2507 0.3094 -0.0007 0.0363  -0.0241 441 ALA   B CA  
4595 C  C   . ALA   B 285 ? 0.2391 0.1566 0.2159 -0.0035 0.0321  -0.0201 441 ALA   B C   
4596 O  O   . ALA   B 285 ? 0.3320 0.2478 0.3092 -0.0054 0.0273  -0.0208 441 ALA   B O   
4597 C  CB  . ALA   B 285 ? 0.2588 0.1721 0.2196 -0.0003 0.0378  -0.0262 441 ALA   B CB  
4598 N  N   . PHE   B 286 ? 0.2734 0.1942 0.2519 -0.0042 0.0343  -0.0162 442 PHE   B N   
4599 C  CA  . PHE   B 286 ? 0.2991 0.2210 0.2795 -0.0061 0.0306  -0.0126 442 PHE   B CA  
4600 C  C   . PHE   B 286 ? 0.3211 0.2450 0.3125 -0.0070 0.0274  -0.0122 442 PHE   B C   
4601 O  O   . PHE   B 286 ? 0.3759 0.2997 0.3677 -0.0085 0.0227  -0.0114 442 PHE   B O   
4602 C  CB  . PHE   B 286 ? 0.2847 0.2067 0.2635 -0.0071 0.0348  -0.0088 442 PHE   B CB  
4603 C  CG  . PHE   B 286 ? 0.2653 0.1869 0.2463 -0.0086 0.0315  -0.0054 442 PHE   B CG  
4604 C  CD1 . PHE   B 286 ? 0.3196 0.2387 0.2920 -0.0071 0.0272  -0.0044 442 PHE   B CD1 
4605 C  CD2 . PHE   B 286 ? 0.2929 0.2178 0.2849 -0.0108 0.0325  -0.0041 442 PHE   B CD2 
4606 C  CE1 . PHE   B 286 ? 0.4278 0.3463 0.4019 -0.0076 0.0242  -0.0017 442 PHE   B CE1 
4607 C  CE2 . PHE   B 286 ? 0.3245 0.2483 0.3178 -0.0121 0.0296  -0.0016 442 PHE   B CE2 
4608 C  CZ  . PHE   B 286 ? 0.3137 0.2336 0.2978 -0.0103 0.0256  -0.0002 442 PHE   B CZ  
4609 N  N   . PHE   B 287 ? 0.2324 0.1591 0.2325 -0.0056 0.0297  -0.0130 443 PHE   B N   
4610 C  CA  . PHE   B 287 ? 0.2810 0.2088 0.2895 -0.0051 0.0261  -0.0125 443 PHE   B CA  
4611 C  C   . PHE   B 287 ? 0.3203 0.2409 0.3242 -0.0050 0.0226  -0.0143 443 PHE   B C   
4612 O  O   . PHE   B 287 ? 0.3020 0.2212 0.3076 -0.0065 0.0189  -0.0130 443 PHE   B O   
4613 C  CB  . PHE   B 287 ? 0.2108 0.1444 0.2288 -0.0020 0.0287  -0.0140 443 PHE   B CB  
4614 C  CG  . PHE   B 287 ? 0.3152 0.2577 0.3410 -0.0042 0.0319  -0.0129 443 PHE   B CG  
4615 C  CD1 . PHE   B 287 ? 0.3278 0.2705 0.3544 -0.0080 0.0302  -0.0099 443 PHE   B CD1 
4616 C  CD2 . PHE   B 287 ? 0.3356 0.2859 0.3676 -0.0030 0.0373  -0.0155 443 PHE   B CD2 
4617 C  CE1 . PHE   B 287 ? 0.3294 0.2780 0.3620 -0.0114 0.0338  -0.0094 443 PHE   B CE1 
4618 C  CE2 . PHE   B 287 ? 0.3357 0.2944 0.3751 -0.0069 0.0412  -0.0153 443 PHE   B CE2 
4619 C  CZ  . PHE   B 287 ? 0.3709 0.3276 0.4100 -0.0116 0.0396  -0.0122 443 PHE   B CZ  
4620 N  N   . HIS   B 288 ? 0.2480 0.1635 0.2452 -0.0039 0.0243  -0.0176 444 HIS   B N   
4621 C  CA  . HIS   B 288 ? 0.2900 0.1968 0.2812 -0.0056 0.0219  -0.0200 444 HIS   B CA  
4622 C  C   . HIS   B 288 ? 0.2890 0.1980 0.2772 -0.0105 0.0187  -0.0198 444 HIS   B C   
4623 O  O   . HIS   B 288 ? 0.2875 0.1928 0.2752 -0.0136 0.0163  -0.0202 444 HIS   B O   
4624 C  CB  . HIS   B 288 ? 0.3390 0.2395 0.3228 -0.0042 0.0246  -0.0245 444 HIS   B CB  
4625 C  CG  . HIS   B 288 ? 0.3479 0.2440 0.3337 0.0015  0.0270  -0.0259 444 HIS   B CG  
4626 N  ND1 . HIS   B 288 ? 0.3025 0.1909 0.2894 0.0041  0.0252  -0.0252 444 HIS   B ND1 
4627 C  CD2 . HIS   B 288 ? 0.2800 0.1784 0.2663 0.0061  0.0311  -0.0282 444 HIS   B CD2 
4628 C  CE1 . HIS   B 288 ? 0.3091 0.1956 0.2972 0.0110  0.0274  -0.0271 444 HIS   B CE1 
4629 N  NE2 . HIS   B 288 ? 0.2796 0.1731 0.2683 0.0120  0.0311  -0.0293 444 HIS   B NE2 
4630 N  N   . VAL   B 289 ? 0.2785 0.1935 0.2639 -0.0109 0.0186  -0.0193 445 VAL   B N   
4631 C  CA  . VAL   B 289 ? 0.3112 0.2307 0.2944 -0.0137 0.0149  -0.0196 445 VAL   B CA  
4632 C  C   . VAL   B 289 ? 0.2708 0.1932 0.2608 -0.0146 0.0126  -0.0160 445 VAL   B C   
4633 O  O   . VAL   B 289 ? 0.2967 0.2215 0.2870 -0.0177 0.0097  -0.0172 445 VAL   B O   
4634 C  CB  . VAL   B 289 ? 0.3446 0.2683 0.3210 -0.0115 0.0149  -0.0194 445 VAL   B CB  
4635 C  CG1 . VAL   B 289 ? 0.2901 0.2203 0.2648 -0.0123 0.0103  -0.0201 445 VAL   B CG1 
4636 C  CG2 . VAL   B 289 ? 0.2974 0.2186 0.2658 -0.0106 0.0169  -0.0235 445 VAL   B CG2 
4637 N  N   . CYS   B 290 ? 0.2577 0.1810 0.2533 -0.0126 0.0140  -0.0125 446 CYS   B N   
4638 C  CA  . CYS   B 290 ? 0.3164 0.2420 0.3181 -0.0134 0.0117  -0.0097 446 CYS   B CA  
4639 C  C   . CYS   B 290 ? 0.3142 0.2357 0.3175 -0.0149 0.0101  -0.0104 446 CYS   B C   
4640 O  O   . CYS   B 290 ? 0.3489 0.2720 0.3535 -0.0171 0.0077  -0.0096 446 CYS   B O   
4641 C  CB  . CYS   B 290 ? 0.2137 0.1416 0.2216 -0.0118 0.0139  -0.0071 446 CYS   B CB  
4642 S  SG  . CYS   B 290 ? 0.3160 0.2451 0.3201 -0.0116 0.0164  -0.0048 446 CYS   B SG  
4643 N  N   . THR   B 291 ? 0.2291 0.1440 0.2310 -0.0134 0.0119  -0.0119 447 THR   B N   
4644 C  CA  . THR   B 291 ? 0.2800 0.1866 0.2794 -0.0145 0.0110  -0.0122 447 THR   B CA  
4645 C  C   . THR   B 291 ? 0.3623 0.2663 0.3558 -0.0204 0.0105  -0.0150 447 THR   B C   
4646 O  O   . THR   B 291 ? 0.2656 0.1664 0.2579 -0.0238 0.0096  -0.0144 447 THR   B O   
4647 C  CB  . THR   B 291 ? 0.4031 0.3010 0.4000 -0.0101 0.0130  -0.0134 447 THR   B CB  
4648 O  OG1 . THR   B 291 ? 0.3493 0.2532 0.3538 -0.0047 0.0131  -0.0117 447 THR   B OG1 
4649 C  CG2 . THR   B 291 ? 0.2749 0.1593 0.2651 -0.0109 0.0125  -0.0134 447 THR   B CG2 
4650 N  N   . GLN   B 292 ? 0.3192 0.2257 0.3092 -0.0222 0.0112  -0.0187 448 GLN   B N   
4651 C  CA  . GLN   B 292 ? 0.4156 0.3231 0.4016 -0.0285 0.0106  -0.0230 448 GLN   B CA  
4652 C  C   . GLN   B 292 ? 0.3027 0.2214 0.2929 -0.0309 0.0078  -0.0225 448 GLN   B C   
4653 O  O   . GLN   B 292 ? 0.4733 0.3935 0.4627 -0.0369 0.0077  -0.0254 448 GLN   B O   
4654 C  CB  . GLN   B 292 ? 0.4931 0.4032 0.4745 -0.0290 0.0111  -0.0278 448 GLN   B CB  
4655 C  CG  . GLN   B 292 ? 0.4270 0.3251 0.4026 -0.0282 0.0142  -0.0304 448 GLN   B CG  
4656 C  CD  . GLN   B 292 ? 0.7243 0.6260 0.6946 -0.0291 0.0143  -0.0359 448 GLN   B CD  
4657 O  OE1 . GLN   B 292 ? 0.6885 0.6020 0.6593 -0.0279 0.0120  -0.0364 448 GLN   B OE1 
4658 N  NE2 . GLN   B 292 ? 0.6623 0.5530 0.6262 -0.0304 0.0168  -0.0401 448 GLN   B NE2 
4659 N  N   . ASN   B 293 ? 0.2738 0.2002 0.2678 -0.0266 0.0061  -0.0193 449 ASN   B N   
4660 C  CA  . ASN   B 293 ? 0.2781 0.2148 0.2750 -0.0269 0.0033  -0.0191 449 ASN   B CA  
4661 C  C   . ASN   B 293 ? 0.3628 0.2987 0.3644 -0.0245 0.0027  -0.0141 449 ASN   B C   
4662 O  O   . ASN   B 293 ? 0.3098 0.2483 0.3126 -0.0206 0.0020  -0.0115 449 ASN   B O   
4663 C  CB  . ASN   B 293 ? 0.3174 0.2618 0.3115 -0.0232 0.0015  -0.0204 449 ASN   B CB  
4664 C  CG  . ASN   B 293 ? 0.3662 0.3139 0.3556 -0.0254 0.0012  -0.0264 449 ASN   B CG  
4665 O  OD1 . ASN   B 293 ? 0.5150 0.4724 0.5054 -0.0285 -0.0011 -0.0312 449 ASN   B OD1 
4666 N  ND2 . ASN   B 293 ? 0.4619 0.4029 0.4468 -0.0240 0.0034  -0.0269 449 ASN   B ND2 
4667 N  N   . PRO   B 294 ? 0.2892 0.2204 0.2921 -0.0269 0.0031  -0.0129 450 PRO   B N   
4668 C  CA  . PRO   B 294 ? 0.2686 0.1984 0.2754 -0.0241 0.0023  -0.0088 450 PRO   B CA  
4669 C  C   . PRO   B 294 ? 0.3873 0.3249 0.3971 -0.0237 0.0000  -0.0079 450 PRO   B C   
4670 O  O   . PRO   B 294 ? 0.3233 0.2606 0.3364 -0.0213 -0.0008 -0.0051 450 PRO   B O   
4671 C  CB  . PRO   B 294 ? 0.3935 0.3144 0.3976 -0.0262 0.0031  -0.0081 450 PRO   B CB  
4672 C  CG  . PRO   B 294 ? 0.3128 0.2332 0.3125 -0.0324 0.0044  -0.0119 450 PRO   B CG  
4673 C  CD  . PRO   B 294 ? 0.3480 0.2738 0.3472 -0.0326 0.0045  -0.0155 450 PRO   B CD  
4674 N  N   . GLN   B 295 ? 0.3022 0.2474 0.3112 -0.0255 -0.0012 -0.0108 451 GLN   B N   
4675 C  CA  . GLN   B 295 ? 0.2656 0.2180 0.2769 -0.0242 -0.0034 -0.0105 451 GLN   B CA  
4676 C  C   . GLN   B 295 ? 0.3665 0.3211 0.3766 -0.0188 -0.0048 -0.0094 451 GLN   B C   
4677 O  O   . GLN   B 295 ? 0.3152 0.2707 0.3217 -0.0170 -0.0048 -0.0107 451 GLN   B O   
4678 C  CB  . GLN   B 295 ? 0.2828 0.2444 0.2944 -0.0281 -0.0039 -0.0150 451 GLN   B CB  
4679 C  CG  . GLN   B 295 ? 0.3289 0.2858 0.3391 -0.0348 -0.0013 -0.0160 451 GLN   B CG  
4680 C  CD  . GLN   B 295 ? 0.4424 0.3931 0.4524 -0.0346 -0.0010 -0.0121 451 GLN   B CD  
4681 O  OE1 . GLN   B 295 ? 0.3989 0.3531 0.4115 -0.0309 -0.0030 -0.0103 451 GLN   B OE1 
4682 N  NE2 . GLN   B 295 ? 0.3195 0.2595 0.3248 -0.0382 0.0015  -0.0110 451 GLN   B NE2 
4683 N  N   . ASP   B 296 ? 0.2054 0.1593 0.2169 -0.0163 -0.0058 -0.0070 452 ASP   B N   
4684 C  CA  . ASP   B 296 ? 0.2215 0.1736 0.2293 -0.0114 -0.0065 -0.0056 452 ASP   B CA  
4685 C  C   . ASP   B 296 ? 0.3647 0.3244 0.3683 -0.0078 -0.0090 -0.0087 452 ASP   B C   
4686 O  O   . ASP   B 296 ? 0.2446 0.2013 0.2416 -0.0030 -0.0095 -0.0078 452 ASP   B O   
4687 C  CB  . ASP   B 296 ? 0.2673 0.2163 0.2766 -0.0102 -0.0071 -0.0036 452 ASP   B CB  
4688 C  CG  . ASP   B 296 ? 0.3868 0.3308 0.4008 -0.0130 -0.0053 -0.0015 452 ASP   B CG  
4689 O  OD1 . ASP   B 296 ? 0.3482 0.2899 0.3634 -0.0143 -0.0033 -0.0009 452 ASP   B OD1 
4690 O  OD2 . ASP   B 296 ? 0.3015 0.2450 0.3181 -0.0133 -0.0063 -0.0009 452 ASP   B OD2 
4691 N  N   . SER   B 297 ? 0.2876 0.2579 0.2946 -0.0100 -0.0106 -0.0127 453 SER   B N   
4692 C  CA  . SER   B 297 ? 0.2240 0.2060 0.2292 -0.0063 -0.0136 -0.0172 453 SER   B CA  
4693 C  C   . SER   B 297 ? 0.2936 0.2787 0.2957 -0.0066 -0.0139 -0.0201 453 SER   B C   
4694 O  O   . SER   B 297 ? 0.3090 0.3047 0.3087 -0.0022 -0.0171 -0.0242 453 SER   B O   
4695 C  CB  . SER   B 297 ? 0.1720 0.1669 0.1834 -0.0101 -0.0142 -0.0218 453 SER   B CB  
4696 O  OG  . SER   B 297 ? 0.3886 0.3832 0.4030 -0.0187 -0.0113 -0.0234 453 SER   B OG  
4697 N  N   . GLN   B 298 ? 0.2924 0.2693 0.2941 -0.0110 -0.0109 -0.0187 454 GLN   B N   
4698 C  CA  . GLN   B 298 ? 0.3208 0.2983 0.3181 -0.0109 -0.0108 -0.0211 454 GLN   B CA  
4699 C  C   . GLN   B 298 ? 0.3282 0.2964 0.3175 -0.0049 -0.0101 -0.0170 454 GLN   B C   
4700 O  O   . GLN   B 298 ? 0.3616 0.3288 0.3455 -0.0040 -0.0097 -0.0186 454 GLN   B O   
4701 C  CB  . GLN   B 298 ? 0.3119 0.2839 0.3115 -0.0181 -0.0074 -0.0222 454 GLN   B CB  
4702 C  CG  . GLN   B 298 ? 0.2575 0.2356 0.2621 -0.0254 -0.0068 -0.0263 454 GLN   B CG  
4703 C  CD  . GLN   B 298 ? 0.4440 0.4110 0.4479 -0.0315 -0.0031 -0.0259 454 GLN   B CD  
4704 O  OE1 . GLN   B 298 ? 0.3733 0.3299 0.3776 -0.0311 -0.0014 -0.0211 454 GLN   B OE1 
4705 N  NE2 . GLN   B 298 ? 0.3424 0.3111 0.3446 -0.0369 -0.0020 -0.0314 454 GLN   B NE2 
4706 N  N   . TRP   B 299 ? 0.3159 0.2765 0.3033 -0.0014 -0.0095 -0.0122 455 TRP   B N   
4707 C  CA  . TRP   B 299 ? 0.3841 0.3336 0.3626 0.0029  -0.0075 -0.0080 455 TRP   B CA  
4708 C  C   . TRP   B 299 ? 0.2904 0.2363 0.2616 0.0099  -0.0096 -0.0058 455 TRP   B C   
4709 O  O   . TRP   B 299 ? 0.3513 0.2842 0.3153 0.0118  -0.0067 -0.0013 455 TRP   B O   
4710 C  CB  . TRP   B 299 ? 0.2935 0.2336 0.2760 -0.0014 -0.0027 -0.0042 455 TRP   B CB  
4711 C  CG  . TRP   B 299 ? 0.2327 0.1738 0.2197 -0.0059 -0.0005 -0.0060 455 TRP   B CG  
4712 C  CD1 . TRP   B 299 ? 0.2925 0.2363 0.2874 -0.0105 -0.0006 -0.0075 455 TRP   B CD1 
4713 C  CD2 . TRP   B 299 ? 0.2252 0.1628 0.2072 -0.0057 0.0023  -0.0064 455 TRP   B CD2 
4714 N  NE1 . TRP   B 299 ? 0.2926 0.2336 0.2875 -0.0126 0.0018  -0.0089 455 TRP   B NE1 
4715 C  CE2 . TRP   B 299 ? 0.1982 0.1364 0.1861 -0.0098 0.0036  -0.0085 455 TRP   B CE2 
4716 C  CE3 . TRP   B 299 ? 0.2232 0.1558 0.1948 -0.0019 0.0040  -0.0050 455 TRP   B CE3 
4717 C  CZ2 . TRP   B 299 ? 0.3148 0.2499 0.2996 -0.0101 0.0064  -0.0100 455 TRP   B CZ2 
4718 C  CZ3 . TRP   B 299 ? 0.2251 0.1556 0.1938 -0.0028 0.0071  -0.0064 455 TRP   B CZ3 
4719 C  CH2 . TRP   B 299 ? 0.2669 0.1991 0.2428 -0.0068 0.0081  -0.0091 455 TRP   B CH2 
4720 N  N   . ASP   B 300 ? 0.3388 0.2955 0.3114 0.0136  -0.0142 -0.0094 456 ASP   B N   
4721 C  CA  . ASP   B 300 ? 0.3621 0.3151 0.3269 0.0220  -0.0168 -0.0079 456 ASP   B CA  
4722 C  C   . ASP   B 300 ? 0.4062 0.3470 0.3549 0.0292  -0.0164 -0.0047 456 ASP   B C   
4723 O  O   . ASP   B 300 ? 0.3212 0.2660 0.2648 0.0310  -0.0174 -0.0066 456 ASP   B O   
4724 C  CB  . ASP   B 300 ? 0.4003 0.3713 0.3692 0.0261  -0.0222 -0.0140 456 ASP   B CB  
4725 C  CG  . ASP   B 300 ? 0.5540 0.5224 0.5178 0.0348  -0.0250 -0.0133 456 ASP   B CG  
4726 O  OD1 . ASP   B 300 ? 0.6557 0.6103 0.6053 0.0430  -0.0254 -0.0096 456 ASP   B OD1 
4727 O  OD2 . ASP   B 300 ? 0.7098 0.6887 0.6824 0.0335  -0.0264 -0.0164 456 ASP   B OD2 
4728 N  N   . ARG   B 301 ? 0.4042 0.3284 0.3433 0.0329  -0.0143 0.0002  457 ARG   B N   
4729 C  CA  . ARG   B 301 ? 0.5387 0.4468 0.4593 0.0393  -0.0126 0.0044  457 ARG   B CA  
4730 C  C   . ARG   B 301 ? 0.4905 0.4070 0.4010 0.0502  -0.0188 0.0012  457 ARG   B C   
4731 O  O   . ARG   B 301 ? 0.5374 0.4488 0.4358 0.0535  -0.0183 0.0024  457 ARG   B O   
4732 C  CB  . ARG   B 301 ? 0.6421 0.5303 0.5527 0.0418  -0.0098 0.0093  457 ARG   B CB  
4733 C  CG  . ARG   B 301 ? 0.6983 0.5656 0.5857 0.0492  -0.0075 0.0142  457 ARG   B CG  
4734 C  CD  . ARG   B 301 ? 0.8750 0.7204 0.7571 0.0435  -0.0004 0.0192  457 ARG   B CD  
4735 N  NE  . ARG   B 301 ? 0.7399 0.5844 0.6299 0.0319  0.0066  0.0204  457 ARG   B NE  
4736 C  CZ  . ARG   B 301 ? 0.9565 0.7996 0.8405 0.0306  0.0099  0.0216  457 ARG   B CZ  
4737 N  NH1 . ARG   B 301 ? 0.9613 0.7983 0.8271 0.0399  0.0079  0.0230  457 ARG   B NH1 
4738 N  NH2 . ARG   B 301 ? 0.6848 0.5328 0.5806 0.0207  0.0152  0.0210  457 ARG   B NH2 
4739 N  N   . LYS   B 302 ? 0.4917 0.4232 0.4077 0.0558  -0.0249 -0.0036 458 LYS   B N   
4740 C  CA  . LYS   B 302 ? 0.5678 0.5122 0.4767 0.0667  -0.0319 -0.0083 458 LYS   B CA  
4741 C  C   . LYS   B 302 ? 0.5411 0.4974 0.4523 0.0632  -0.0328 -0.0123 458 LYS   B C   
4742 O  O   . LYS   B 302 ? 0.5185 0.4778 0.4172 0.0725  -0.0371 -0.0141 458 LYS   B O   
4743 C  CB  . LYS   B 302 ? 0.5385 0.5041 0.4595 0.0699  -0.0374 -0.0149 458 LYS   B CB  
4744 C  CG  . LYS   B 302 ? 0.7136 0.6941 0.6273 0.0837  -0.0454 -0.0205 458 LYS   B CG  
4745 C  CD  . LYS   B 302 ? 0.7895 0.8002 0.7191 0.0785  -0.0490 -0.0302 458 LYS   B CD  
4746 C  CE  . LYS   B 302 ? 0.5382 0.5646 0.4594 0.0916  -0.0570 -0.0363 458 LYS   B CE  
4747 N  NZ  . LYS   B 302 ? 0.8134 0.8508 0.7368 0.0859  -0.0577 -0.0409 458 LYS   B NZ  
4748 N  N   . ASP   B 303 ? 0.4534 0.4153 0.3787 0.0506  -0.0289 -0.0138 459 ASP   B N   
4749 C  CA  . ASP   B 303 ? 0.4097 0.3824 0.3384 0.0460  -0.0294 -0.0185 459 ASP   B CA  
4750 C  C   . ASP   B 303 ? 0.3956 0.3522 0.3155 0.0427  -0.0237 -0.0137 459 ASP   B C   
4751 O  O   . ASP   B 303 ? 0.4214 0.3838 0.3462 0.0363  -0.0223 -0.0171 459 ASP   B O   
4752 C  CB  . ASP   B 303 ? 0.4378 0.4251 0.3854 0.0347  -0.0284 -0.0238 459 ASP   B CB  
4753 C  CG  . ASP   B 303 ? 0.4622 0.4696 0.4191 0.0366  -0.0334 -0.0303 459 ASP   B CG  
4754 O  OD1 . ASP   B 303 ? 0.7648 0.7846 0.7165 0.0459  -0.0394 -0.0349 459 ASP   B OD1 
4755 O  OD2 . ASP   B 303 ? 0.4351 0.4470 0.4045 0.0291  -0.0314 -0.0311 459 ASP   B OD2 
4756 N  N   . LEU   B 304 ? 0.3828 0.3188 0.2894 0.0464  -0.0198 -0.0064 460 LEU   B N   
4757 C  CA  . LEU   B 304 ? 0.4216 0.3432 0.3195 0.0430  -0.0134 -0.0021 460 LEU   B CA  
4758 C  C   . LEU   B 304 ? 0.3250 0.2549 0.2173 0.0448  -0.0156 -0.0066 460 LEU   B C   
4759 O  O   . LEU   B 304 ? 0.4130 0.3448 0.3117 0.0373  -0.0119 -0.0083 460 LEU   B O   
4760 C  CB  . LEU   B 304 ? 0.3427 0.2416 0.2213 0.0490  -0.0098 0.0053  460 LEU   B CB  
4761 C  CG  . LEU   B 304 ? 0.4863 0.3703 0.3528 0.0463  -0.0025 0.0096  460 LEU   B CG  
4762 C  CD1 . LEU   B 304 ? 0.3863 0.2710 0.2686 0.0340  0.0044  0.0099  460 LEU   B CD1 
4763 C  CD2 . LEU   B 304 ? 0.5106 0.3704 0.3551 0.0521  0.0014  0.0167  460 LEU   B CD2 
4764 N  N   . GLY   B 305 ? 0.3057 0.2420 0.1864 0.0555  -0.0223 -0.0094 461 GLY   B N   
4765 C  CA  . GLY   B 305 ? 0.3222 0.2667 0.1955 0.0583  -0.0252 -0.0143 461 GLY   B CA  
4766 C  C   . GLY   B 305 ? 0.3443 0.3047 0.2344 0.0480  -0.0252 -0.0216 461 GLY   B C   
4767 O  O   . GLY   B 305 ? 0.4229 0.3803 0.3098 0.0441  -0.0220 -0.0228 461 GLY   B O   
4768 N  N   . LEU   B 306 ? 0.4036 0.3796 0.3109 0.0432  -0.0282 -0.0267 462 LEU   B N   
4769 C  CA  . LEU   B 306 ? 0.3524 0.3401 0.2735 0.0327  -0.0273 -0.0335 462 LEU   B CA  
4770 C  C   . LEU   B 306 ? 0.3723 0.3467 0.3000 0.0233  -0.0196 -0.0291 462 LEU   B C   
4771 O  O   . LEU   B 306 ? 0.3265 0.2998 0.2553 0.0178  -0.0169 -0.0320 462 LEU   B O   
4772 C  CB  . LEU   B 306 ? 0.3481 0.3552 0.2842 0.0292  -0.0315 -0.0402 462 LEU   B CB  
4773 C  CG  . LEU   B 306 ? 0.5878 0.6166 0.5251 0.0305  -0.0378 -0.0509 462 LEU   B CG  
4774 C  CD1 . LEU   B 306 ? 0.7995 0.8351 0.7240 0.0454  -0.0450 -0.0517 462 LEU   B CD1 
4775 C  CD2 . LEU   B 306 ? 0.8851 0.9327 0.8401 0.0214  -0.0389 -0.0588 462 LEU   B CD2 
4776 N  N   . CYS   B 307 ? 0.3097 0.2738 0.2411 0.0222  -0.0161 -0.0225 463 CYS   B N   
4777 C  CA  . CYS   B 307 ? 0.3957 0.3501 0.3346 0.0144  -0.0096 -0.0190 463 CYS   B CA  
4778 C  C   . CYS   B 307 ? 0.3659 0.3102 0.2956 0.0145  -0.0048 -0.0171 463 CYS   B C   
4779 O  O   . CYS   B 307 ? 0.3563 0.3007 0.2910 0.0090  -0.0020 -0.0198 463 CYS   B O   
4780 C  CB  . CYS   B 307 ? 0.3870 0.3329 0.3295 0.0143  -0.0073 -0.0128 463 CYS   B CB  
4781 S  SG  . CYS   B 307 ? 0.3404 0.2976 0.2951 0.0130  -0.0116 -0.0151 463 CYS   B SG  
4782 N  N   . PHE   B 308 ? 0.3098 0.2445 0.2244 0.0212  -0.0036 -0.0127 464 PHE   B N   
4783 C  CA  . PHE   B 308 ? 0.3296 0.2552 0.2334 0.0216  0.0015  -0.0111 464 PHE   B CA  
4784 C  C   . PHE   B 308 ? 0.3412 0.2758 0.2437 0.0208  -0.0009 -0.0183 464 PHE   B C   
4785 O  O   . PHE   B 308 ? 0.3229 0.2542 0.2271 0.0165  0.0038  -0.0196 464 PHE   B O   
4786 C  CB  . PHE   B 308 ? 0.3621 0.2754 0.2460 0.0296  0.0026  -0.0057 464 PHE   B CB  
4787 C  CG  . PHE   B 308 ? 0.3577 0.2615 0.2285 0.0299  0.0086  -0.0040 464 PHE   B CG  
4788 C  CD1 . PHE   B 308 ? 0.3525 0.2510 0.2302 0.0228  0.0167  -0.0023 464 PHE   B CD1 
4789 C  CD2 . PHE   B 308 ? 0.3306 0.2318 0.1818 0.0378  0.0060  -0.0047 464 PHE   B CD2 
4790 C  CE1 . PHE   B 308 ? 0.3512 0.2424 0.2175 0.0228  0.0230  -0.0013 464 PHE   B CE1 
4791 C  CE2 . PHE   B 308 ? 0.4065 0.2987 0.2444 0.0379  0.0122  -0.0032 464 PHE   B CE2 
4792 C  CZ  . PHE   B 308 ? 0.3398 0.2272 0.1857 0.0301  0.0211  -0.0015 464 PHE   B CZ  
4793 N  N   . ASP   B 309 ? 0.3333 0.2801 0.2331 0.0249  -0.0083 -0.0238 465 ASP   B N   
4794 C  CA  . ASP   B 309 ? 0.3795 0.3359 0.2784 0.0231  -0.0109 -0.0320 465 ASP   B CA  
4795 C  C   . ASP   B 309 ? 0.3736 0.3313 0.2868 0.0130  -0.0076 -0.0357 465 ASP   B C   
4796 O  O   . ASP   B 309 ? 0.4293 0.3829 0.3397 0.0102  -0.0044 -0.0385 465 ASP   B O   
4797 C  CB  . ASP   B 309 ? 0.3563 0.3301 0.2548 0.0276  -0.0198 -0.0390 465 ASP   B CB  
4798 C  CG  . ASP   B 309 ? 0.4460 0.4303 0.3409 0.0263  -0.0230 -0.0483 465 ASP   B CG  
4799 O  OD1 . ASP   B 309 ? 0.4164 0.3939 0.2960 0.0312  -0.0219 -0.0476 465 ASP   B OD1 
4800 O  OD2 . ASP   B 309 ? 0.4652 0.4641 0.3719 0.0199  -0.0261 -0.0567 465 ASP   B OD2 
4801 N  N   . ASN   B 310 ? 0.3003 0.2614 0.2274 0.0079  -0.0080 -0.0353 466 ASN   B N   
4802 C  CA  . ASN   B 310 ? 0.3044 0.2644 0.2427 -0.0009 -0.0052 -0.0383 466 ASN   B CA  
4803 C  C   . ASN   B 310 ? 0.3575 0.3040 0.2961 -0.0022 0.0017  -0.0336 466 ASN   B C   
4804 O  O   . ASN   B 310 ? 0.3562 0.2988 0.2980 -0.0069 0.0044  -0.0368 466 ASN   B O   
4805 C  CB  . ASN   B 310 ? 0.3326 0.2982 0.2833 -0.0052 -0.0068 -0.0382 466 ASN   B CB  
4806 C  CG  . ASN   B 310 ? 0.4009 0.3835 0.3541 -0.0051 -0.0130 -0.0449 466 ASN   B CG  
4807 O  OD1 . ASN   B 310 ? 0.4252 0.4165 0.3742 -0.0053 -0.0159 -0.0521 466 ASN   B OD1 
4808 N  ND2 . ASN   B 310 ? 0.3889 0.3776 0.3493 -0.0049 -0.0150 -0.0433 466 ASN   B ND2 
4809 N  N   . CYS   B 311 ? 0.3310 0.2702 0.2657 0.0017  0.0048  -0.0265 467 CYS   B N   
4810 C  CA  . CYS   B 311 ? 0.2966 0.2266 0.2318 0.0007  0.0115  -0.0235 467 CYS   B CA  
4811 C  C   . CYS   B 311 ? 0.4330 0.3606 0.3575 0.0024  0.0137  -0.0270 467 CYS   B C   
4812 O  O   . CYS   B 311 ? 0.3969 0.3214 0.3245 -0.0002 0.0170  -0.0300 467 CYS   B O   
4813 C  CB  . CYS   B 311 ? 0.4006 0.3244 0.3338 0.0030  0.0151  -0.0162 467 CYS   B CB  
4814 S  SG  . CYS   B 311 ? 0.3790 0.3039 0.3259 0.0002  0.0139  -0.0124 467 CYS   B SG  
4815 N  N   . VAL   B 312 ? 0.3226 0.2512 0.2333 0.0077  0.0115  -0.0272 468 VAL   B N   
4816 C  CA  . VAL   B 312 ? 0.3733 0.2997 0.2717 0.0099  0.0134  -0.0307 468 VAL   B CA  
4817 C  C   . VAL   B 312 ? 0.3133 0.2442 0.2166 0.0054  0.0115  -0.0391 468 VAL   B C   
4818 O  O   . VAL   B 312 ? 0.2966 0.2220 0.1995 0.0037  0.0162  -0.0413 468 VAL   B O   
4819 C  CB  . VAL   B 312 ? 0.3807 0.3087 0.2622 0.0173  0.0092  -0.0303 468 VAL   B CB  
4820 C  CG1 . VAL   B 312 ? 0.3289 0.2565 0.1972 0.0196  0.0099  -0.0353 468 VAL   B CG1 
4821 C  CG2 . VAL   B 312 ? 0.3506 0.2683 0.2231 0.0215  0.0130  -0.0214 468 VAL   B CG2 
4822 N  N   . THR   B 313 ? 0.3073 0.2480 0.2155 0.0031  0.0051  -0.0442 469 THR   B N   
4823 C  CA  . THR   B 313 ? 0.3049 0.2487 0.2174 -0.0031 0.0039  -0.0528 469 THR   B CA  
4824 C  C   . THR   B 313 ? 0.2875 0.2206 0.2077 -0.0077 0.0095  -0.0519 469 THR   B C   
4825 O  O   . THR   B 313 ? 0.3656 0.2927 0.2817 -0.0092 0.0123  -0.0566 469 THR   B O   
4826 C  CB  . THR   B 313 ? 0.3700 0.3262 0.2907 -0.0072 -0.0021 -0.0575 469 THR   B CB  
4827 O  OG1 . THR   B 313 ? 0.4445 0.4130 0.3573 -0.0017 -0.0083 -0.0608 469 THR   B OG1 
4828 C  CG2 . THR   B 313 ? 0.3725 0.3285 0.2982 -0.0161 -0.0016 -0.0658 469 THR   B CG2 
4829 N  N   . TYR   B 314 ? 0.3150 0.2450 0.2452 -0.0089 0.0112  -0.0459 470 TYR   B N   
4830 C  CA  . TYR   B 314 ? 0.3142 0.2348 0.2510 -0.0117 0.0155  -0.0453 470 TYR   B CA  
4831 C  C   . TYR   B 314 ? 0.2996 0.2134 0.2311 -0.0077 0.0210  -0.0445 470 TYR   B C   
4832 O  O   . TYR   B 314 ? 0.3560 0.2627 0.2861 -0.0087 0.0236  -0.0488 470 TYR   B O   
4833 C  CB  . TYR   B 314 ? 0.3010 0.2207 0.2484 -0.0123 0.0159  -0.0390 470 TYR   B CB  
4834 C  CG  . TYR   B 314 ? 0.3684 0.2786 0.3210 -0.0133 0.0194  -0.0386 470 TYR   B CG  
4835 C  CD1 . TYR   B 314 ? 0.3503 0.2539 0.3031 -0.0181 0.0189  -0.0430 470 TYR   B CD1 
4836 C  CD2 . TYR   B 314 ? 0.3230 0.2306 0.2794 -0.0093 0.0234  -0.0343 470 TYR   B CD2 
4837 C  CE1 . TYR   B 314 ? 0.3945 0.2869 0.3492 -0.0172 0.0218  -0.0423 470 TYR   B CE1 
4838 C  CE2 . TYR   B 314 ? 0.3840 0.2844 0.3448 -0.0082 0.0258  -0.0345 470 TYR   B CE2 
4839 C  CZ  . TYR   B 314 ? 0.3551 0.2466 0.3140 -0.0114 0.0247  -0.0381 470 TYR   B CZ  
4840 O  OH  . TYR   B 314 ? 0.5420 0.4237 0.5025 -0.0086 0.0266  -0.0379 470 TYR   B OH  
4841 N  N   . PHE   B 315 ? 0.2801 0.1954 0.2076 -0.0034 0.0234  -0.0394 471 PHE   B N   
4842 C  CA  . PHE   B 315 ? 0.3294 0.2402 0.2517 -0.0002 0.0297  -0.0392 471 PHE   B CA  
4843 C  C   . PHE   B 315 ? 0.3528 0.2616 0.2644 0.0003  0.0295  -0.0465 471 PHE   B C   
4844 O  O   . PHE   B 315 ? 0.3109 0.2141 0.2222 0.0008  0.0335  -0.0499 471 PHE   B O   
4845 C  CB  . PHE   B 315 ? 0.3189 0.2305 0.2354 0.0029  0.0327  -0.0331 471 PHE   B CB  
4846 C  CG  . PHE   B 315 ? 0.3390 0.2476 0.2532 0.0048  0.0408  -0.0321 471 PHE   B CG  
4847 C  CD1 . PHE   B 315 ? 0.3233 0.2328 0.2501 0.0039  0.0451  -0.0301 471 PHE   B CD1 
4848 C  CD2 . PHE   B 315 ? 0.3129 0.2193 0.2123 0.0076  0.0441  -0.0335 471 PHE   B CD2 
4849 C  CE1 . PHE   B 315 ? 0.3163 0.2263 0.2430 0.0054  0.0529  -0.0303 471 PHE   B CE1 
4850 C  CE2 . PHE   B 315 ? 0.3471 0.2520 0.2447 0.0087  0.0525  -0.0329 471 PHE   B CE2 
4851 C  CZ  . PHE   B 315 ? 0.3135 0.2211 0.2256 0.0074  0.0571  -0.0316 471 PHE   B CZ  
4852 N  N   . LEU   B 316 ? 0.3246 0.2387 0.2277 0.0004  0.0244  -0.0497 472 LEU   B N   
4853 C  CA  . LEU   B 316 ? 0.3206 0.2344 0.2135 0.0002  0.0233  -0.0579 472 LEU   B CA  
4854 C  C   . LEU   B 316 ? 0.3223 0.2299 0.2207 -0.0049 0.0238  -0.0642 472 LEU   B C   
4855 O  O   . LEU   B 316 ? 0.3336 0.2345 0.2261 -0.0041 0.0273  -0.0690 472 LEU   B O   
4856 C  CB  . LEU   B 316 ? 0.3536 0.2773 0.2393 0.0009  0.0160  -0.0614 472 LEU   B CB  
4857 C  CG  . LEU   B 316 ? 0.3696 0.2951 0.2414 0.0082  0.0157  -0.0571 472 LEU   B CG  
4858 C  CD1 . LEU   B 316 ? 0.3362 0.2732 0.2023 0.0107  0.0072  -0.0606 472 LEU   B CD1 
4859 C  CD2 . LEU   B 316 ? 0.3488 0.2682 0.2072 0.0113  0.0207  -0.0595 472 LEU   B CD2 
4860 N  N   . GLN   B 317 ? 0.3130 0.2213 0.2215 -0.0101 0.0210  -0.0642 473 GLN   B N   
4861 C  CA  . GLN   B 317 ? 0.3181 0.2166 0.2293 -0.0154 0.0222  -0.0694 473 GLN   B CA  
4862 C  C   . GLN   B 317 ? 0.3519 0.2387 0.2635 -0.0113 0.0282  -0.0675 473 GLN   B C   
4863 O  O   . GLN   B 317 ? 0.3361 0.2132 0.2414 -0.0115 0.0307  -0.0735 473 GLN   B O   
4864 C  CB  . GLN   B 317 ? 0.3080 0.2076 0.2292 -0.0211 0.0196  -0.0676 473 GLN   B CB  
4865 C  CG  . GLN   B 317 ? 0.3172 0.2040 0.2382 -0.0277 0.0212  -0.0728 473 GLN   B CG  
4866 C  CD  . GLN   B 317 ? 0.4097 0.2985 0.3382 -0.0346 0.0190  -0.0719 473 GLN   B CD  
4867 O  OE1 . GLN   B 317 ? 0.3725 0.2582 0.3076 -0.0330 0.0198  -0.0650 473 GLN   B OE1 
4868 N  NE2 . GLN   B 317 ? 0.3965 0.2915 0.3240 -0.0427 0.0164  -0.0795 473 GLN   B NE2 
4869 N  N   . CYS   B 318 ? 0.3125 0.2011 0.2313 -0.0071 0.0307  -0.0598 474 CYS   B N   
4870 C  CA  . CYS   B 318 ? 0.3157 0.1974 0.2371 -0.0023 0.0360  -0.0586 474 CYS   B CA  
4871 C  C   . CYS   B 318 ? 0.4180 0.2978 0.3294 0.0016  0.0401  -0.0631 474 CYS   B C   
4872 O  O   . CYS   B 318 ? 0.3390 0.2100 0.2487 0.0045  0.0436  -0.0668 474 CYS   B O   
4873 C  CB  . CYS   B 318 ? 0.3028 0.1911 0.2341 0.0008  0.0378  -0.0508 474 CYS   B CB  
4874 S  SG  . CYS   B 318 ? 0.3763 0.2653 0.3193 -0.0025 0.0337  -0.0458 474 CYS   B SG  
4875 N  N   . LEU   B 319 ? 0.3318 0.2190 0.2352 0.0024  0.0398  -0.0629 475 LEU   B N   
4876 C  CA  . LEU   B 319 ? 0.3460 0.2316 0.2382 0.0061  0.0439  -0.0672 475 LEU   B CA  
4877 C  C   . LEU   B 319 ? 0.3679 0.2456 0.2518 0.0037  0.0423  -0.0766 475 LEU   B C   
4878 O  O   . LEU   B 319 ? 0.4354 0.3061 0.3138 0.0070  0.0467  -0.0812 475 LEU   B O   
4879 C  CB  . LEU   B 319 ? 0.3877 0.2808 0.2699 0.0079  0.0435  -0.0644 475 LEU   B CB  
4880 C  CG  . LEU   B 319 ? 0.3856 0.2829 0.2711 0.0101  0.0477  -0.0558 475 LEU   B CG  
4881 C  CD1 . LEU   B 319 ? 0.3466 0.2475 0.2201 0.0114  0.0451  -0.0526 475 LEU   B CD1 
4882 C  CD2 . LEU   B 319 ? 0.3489 0.2451 0.2338 0.0136  0.0564  -0.0560 475 LEU   B CD2 
4883 N  N   . ARG   B 320 ? 0.3595 0.2387 0.2427 -0.0023 0.0363  -0.0804 476 ARG   B N   
4884 C  CA  . ARG   B 320 ? 0.3749 0.2476 0.2495 -0.0062 0.0349  -0.0906 476 ARG   B CA  
4885 C  C   . ARG   B 320 ? 0.3826 0.2388 0.2594 -0.0077 0.0380  -0.0936 476 ARG   B C   
4886 O  O   . ARG   B 320 ? 0.5055 0.3513 0.3735 -0.0067 0.0408  -0.1007 476 ARG   B O   
4887 C  CB  . ARG   B 320 ? 0.3726 0.2541 0.2474 -0.0132 0.0280  -0.0948 476 ARG   B CB  
4888 C  CG  . ARG   B 320 ? 0.3694 0.2661 0.2390 -0.0099 0.0239  -0.0930 476 ARG   B CG  
4889 C  CD  . ARG   B 320 ? 0.5169 0.4240 0.3839 -0.0154 0.0169  -0.1015 476 ARG   B CD  
4890 N  NE  . ARG   B 320 ? 0.4382 0.3605 0.3039 -0.0114 0.0115  -0.0978 476 ARG   B NE  
4891 C  CZ  . ARG   B 320 ? 0.6107 0.5397 0.4865 -0.0120 0.0088  -0.0918 476 ARG   B CZ  
4892 N  NH1 . ARG   B 320 ? 0.4187 0.3417 0.3066 -0.0170 0.0109  -0.0886 476 ARG   B NH1 
4893 N  NH2 . ARG   B 320 ? 0.4394 0.3805 0.3115 -0.0068 0.0037  -0.0890 476 ARG   B NH2 
4894 N  N   . THR   B 321 ? 0.3726 0.2249 0.2596 -0.0095 0.0375  -0.0884 477 THR   B N   
4895 C  CA  . THR   B 321 ? 0.4122 0.2464 0.2994 -0.0097 0.0401  -0.0899 477 THR   B CA  
4896 C  C   . THR   B 321 ? 0.4190 0.2487 0.3087 0.0002  0.0450  -0.0864 477 THR   B C   
4897 O  O   . THR   B 321 ? 0.5087 0.3229 0.3975 0.0029  0.0469  -0.0872 477 THR   B O   
4898 C  CB  . THR   B 321 ? 0.3732 0.2047 0.2682 -0.0154 0.0375  -0.0858 477 THR   B CB  
4899 O  OG1 . THR   B 321 ? 0.4803 0.3229 0.3862 -0.0112 0.0367  -0.0766 477 THR   B OG1 
4900 C  CG2 . THR   B 321 ? 0.3721 0.2111 0.2663 -0.0255 0.0331  -0.0905 477 THR   B CG2 
4901 N  N   . GLU   B 322 ? 0.3856 0.2284 0.2779 0.0058  0.0473  -0.0828 478 GLU   B N   
4902 C  CA  . GLU   B 322 ? 0.4205 0.2639 0.3171 0.0146  0.0525  -0.0807 478 GLU   B CA  
4903 C  C   . GLU   B 322 ? 0.3980 0.2379 0.3055 0.0176  0.0519  -0.0755 478 GLU   B C   
4904 O  O   . GLU   B 322 ? 0.4279 0.2602 0.3363 0.0248  0.0547  -0.0770 478 GLU   B O   
4905 C  CB  . GLU   B 322 ? 0.4187 0.2508 0.3050 0.0194  0.0566  -0.0885 478 GLU   B CB  
4906 C  CG  . GLU   B 322 ? 0.4958 0.3322 0.3703 0.0181  0.0577  -0.0940 478 GLU   B CG  
4907 C  CD  . GLU   B 322 ? 0.6004 0.4271 0.4658 0.0242  0.0627  -0.1014 478 GLU   B CD  
4908 O  OE1 . GLU   B 322 ? 0.6389 0.4728 0.5072 0.0316  0.0682  -0.1002 478 GLU   B OE1 
4909 O  OE2 . GLU   B 322 ? 0.7141 0.5261 0.5695 0.0214  0.0617  -0.1090 478 GLU   B OE2 
4910 N  N   . LYS   B 323 ? 0.4468 0.2925 0.3620 0.0128  0.0479  -0.0697 479 LYS   B N   
4911 C  CA  . LYS   B 323 ? 0.4784 0.3206 0.4025 0.0152  0.0465  -0.0649 479 LYS   B CA  
4912 C  C   . LYS   B 323 ? 0.4038 0.2617 0.3393 0.0134  0.0446  -0.0577 479 LYS   B C   
4913 O  O   . LYS   B 323 ? 0.3191 0.1817 0.2544 0.0068  0.0412  -0.0559 479 LYS   B O   
4914 C  CB  . LYS   B 323 ? 0.4567 0.2822 0.3752 0.0098  0.0436  -0.0665 479 LYS   B CB  
4915 C  CG  . LYS   B 323 ? 0.7006 0.5229 0.6264 0.0116  0.0415  -0.0606 479 LYS   B CG  
4916 C  CD  . LYS   B 323 ? 0.9386 0.7459 0.8581 0.0038  0.0393  -0.0612 479 LYS   B CD  
4917 C  CE  . LYS   B 323 ? 0.7101 0.5137 0.6349 0.0063  0.0373  -0.0548 479 LYS   B CE  
4918 N  NZ  . LYS   B 323 ? 0.8442 0.6410 0.7692 0.0184  0.0388  -0.0540 479 LYS   B NZ  
4919 N  N   . LEU   B 324 ? 0.4322 0.2983 0.3775 0.0194  0.0468  -0.0544 480 LEU   B N   
4920 C  CA  . LEU   B 324 ? 0.3522 0.2313 0.3087 0.0177  0.0453  -0.0481 480 LEU   B CA  
4921 C  C   . LEU   B 324 ? 0.4336 0.3150 0.4003 0.0245  0.0456  -0.0466 480 LEU   B C   
4922 O  O   . LEU   B 324 ? 0.3991 0.2900 0.3719 0.0300  0.0496  -0.0480 480 LEU   B O   
4923 C  CB  . LEU   B 324 ? 0.2971 0.1891 0.2545 0.0164  0.0488  -0.0464 480 LEU   B CB  
4924 C  CG  . LEU   B 324 ? 0.2971 0.2004 0.2647 0.0140  0.0483  -0.0404 480 LEU   B CG  
4925 C  CD1 . LEU   B 324 ? 0.3266 0.2275 0.2938 0.0086  0.0423  -0.0371 480 LEU   B CD1 
4926 C  CD2 . LEU   B 324 ? 0.3687 0.2804 0.3338 0.0127  0.0533  -0.0389 480 LEU   B CD2 
4927 N  N   . GLU   B 325 ? 0.3632 0.2364 0.3310 0.0243  0.0413  -0.0443 481 GLU   B N   
4928 C  CA  . GLU   B 325 ? 0.4162 0.2911 0.3920 0.0319  0.0402  -0.0430 481 GLU   B CA  
4929 C  C   . GLU   B 325 ? 0.3478 0.2426 0.3379 0.0317  0.0406  -0.0397 481 GLU   B C   
4930 O  O   . GLU   B 325 ? 0.2815 0.1822 0.2743 0.0247  0.0392  -0.0360 481 GLU   B O   
4931 C  CB  . GLU   B 325 ? 0.3934 0.2540 0.3647 0.0310  0.0356  -0.0404 481 GLU   B CB  
4932 C  CG  . GLU   B 325 ? 0.5288 0.3667 0.4850 0.0299  0.0359  -0.0437 481 GLU   B CG  
4933 C  CD  . GLU   B 325 ? 0.7619 0.5847 0.7124 0.0274  0.0326  -0.0405 481 GLU   B CD  
4934 O  OE1 . GLU   B 325 ? 0.4608 0.2919 0.4191 0.0271  0.0296  -0.0357 481 GLU   B OE1 
4935 O  OE2 . GLU   B 325 ? 0.8479 0.6496 0.7851 0.0252  0.0335  -0.0430 481 GLU   B OE2 
4936 N  N   . ASN   B 326 ? 0.3010 0.2064 0.3003 0.0394  0.0427  -0.0419 482 ASN   B N   
4937 C  CA  . ASN   B 326 ? 0.2806 0.2047 0.2948 0.0389  0.0426  -0.0398 482 ASN   B CA  
4938 C  C   . ASN   B 326 ? 0.2975 0.2182 0.3138 0.0366  0.0365  -0.0352 482 ASN   B C   
4939 O  O   . ASN   B 326 ? 0.3126 0.2202 0.3230 0.0412  0.0326  -0.0347 482 ASN   B O   
4940 C  CB  . ASN   B 326 ? 0.3202 0.2569 0.3446 0.0488  0.0446  -0.0443 482 ASN   B CB  
4941 C  CG  . ASN   B 326 ? 0.3792 0.3376 0.4205 0.0473  0.0449  -0.0438 482 ASN   B CG  
4942 O  OD1 . ASN   B 326 ? 0.2533 0.2137 0.2997 0.0476  0.0395  -0.0411 482 ASN   B OD1 
4943 N  ND2 . ASN   B 326 ? 0.3181 0.2929 0.3675 0.0450  0.0516  -0.0468 482 ASN   B ND2 
4944 N  N   . TYR   B 327 ? 0.3269 0.2575 0.3498 0.0296  0.0361  -0.0318 483 TYR   B N   
4945 C  CA  . TYR   B 327 ? 0.2987 0.2259 0.3223 0.0265  0.0307  -0.0276 483 TYR   B CA  
4946 C  C   . TYR   B 327 ? 0.3582 0.2893 0.3888 0.0342  0.0267  -0.0279 483 TYR   B C   
4947 O  O   . TYR   B 327 ? 0.3349 0.2572 0.3614 0.0343  0.0219  -0.0249 483 TYR   B O   
4948 C  CB  . TYR   B 327 ? 0.2295 0.1662 0.2584 0.0185  0.0314  -0.0245 483 TYR   B CB  
4949 C  CG  . TYR   B 327 ? 0.3750 0.3065 0.4020 0.0144  0.0263  -0.0205 483 TYR   B CG  
4950 C  CD1 . TYR   B 327 ? 0.2510 0.1704 0.2673 0.0104  0.0245  -0.0192 483 TYR   B CD1 
4951 C  CD2 . TYR   B 327 ? 0.3129 0.2528 0.3490 0.0144  0.0233  -0.0189 483 TYR   B CD2 
4952 C  CE1 . TYR   B 327 ? 0.2779 0.1943 0.2930 0.0065  0.0206  -0.0162 483 TYR   B CE1 
4953 C  CE2 . TYR   B 327 ? 0.2440 0.1792 0.2777 0.0109  0.0190  -0.0155 483 TYR   B CE2 
4954 C  CZ  . TYR   B 327 ? 0.3508 0.2744 0.3740 0.0071  0.0180  -0.0141 483 TYR   B CZ  
4955 O  OH  . TYR   B 327 ? 0.2911 0.2117 0.3124 0.0035  0.0144  -0.0114 483 TYR   B OH  
4956 N  N   . PHE   B 328 ? 0.3414 0.2865 0.3821 0.0409  0.0285  -0.0318 484 PHE   B N   
4957 C  CA  . PHE   B 328 ? 0.3667 0.3187 0.4147 0.0500  0.0240  -0.0331 484 PHE   B CA  
4958 C  C   . PHE   B 328 ? 0.3631 0.3052 0.4042 0.0623  0.0230  -0.0363 484 PHE   B C   
4959 O  O   . PHE   B 328 ? 0.3279 0.2676 0.3684 0.0714  0.0178  -0.0361 484 PHE   B O   
4960 C  CB  . PHE   B 328 ? 0.3012 0.2794 0.3674 0.0497  0.0260  -0.0367 484 PHE   B CB  
4961 C  CG  . PHE   B 328 ? 0.3478 0.3337 0.4200 0.0383  0.0269  -0.0338 484 PHE   B CG  
4962 C  CD1 . PHE   B 328 ? 0.3761 0.3624 0.4464 0.0293  0.0331  -0.0329 484 PHE   B CD1 
4963 C  CD2 . PHE   B 328 ? 0.3315 0.3227 0.4093 0.0374  0.0215  -0.0320 484 PHE   B CD2 
4964 C  CE1 . PHE   B 328 ? 0.3686 0.3588 0.4419 0.0198  0.0340  -0.0300 484 PHE   B CE1 
4965 C  CE2 . PHE   B 328 ? 0.3659 0.3622 0.4481 0.0273  0.0226  -0.0298 484 PHE   B CE2 
4966 C  CZ  . PHE   B 328 ? 0.2987 0.2937 0.3783 0.0187  0.0289  -0.0287 484 PHE   B CZ  
4967 N  N   . ILE   B 329 ? 0.3399 0.2751 0.3744 0.0636  0.0277  -0.0392 485 ILE   B N   
4968 C  CA  . ILE   B 329 ? 0.3809 0.3046 0.4075 0.0757  0.0276  -0.0428 485 ILE   B CA  
4969 C  C   . ILE   B 329 ? 0.3828 0.2812 0.3913 0.0713  0.0295  -0.0419 485 ILE   B C   
4970 O  O   . ILE   B 329 ? 0.3847 0.2832 0.3905 0.0688  0.0346  -0.0451 485 ILE   B O   
4971 C  CB  . ILE   B 329 ? 0.3580 0.3012 0.3958 0.0826  0.0322  -0.0494 485 ILE   B CB  
4972 C  CG1 . ILE   B 329 ? 0.3950 0.3674 0.4532 0.0823  0.0315  -0.0512 485 ILE   B CG1 
4973 C  CG2 . ILE   B 329 ? 0.3611 0.2940 0.3917 0.0980  0.0308  -0.0535 485 ILE   B CG2 
4974 C  CD1 . ILE   B 329 ? 0.3776 0.3735 0.4493 0.0830  0.0384  -0.0576 485 ILE   B CD1 
4975 N  N   . PRO   B 330 ? 0.4130 0.2895 0.4084 0.0698  0.0258  -0.0382 486 PRO   B N   
4976 C  CA  . PRO   B 330 ? 0.4296 0.2856 0.4101 0.0614  0.0279  -0.0378 486 PRO   B CA  
4977 C  C   . PRO   B 330 ? 0.3856 0.2286 0.3559 0.0664  0.0318  -0.0431 486 PRO   B C   
4978 O  O   . PRO   B 330 ? 0.4281 0.2636 0.3909 0.0582  0.0346  -0.0448 486 PRO   B O   
4979 C  CB  . PRO   B 330 ? 0.3866 0.2223 0.3557 0.0604  0.0240  -0.0335 486 PRO   B CB  
4980 C  CG  . PRO   B 330 ? 0.4011 0.2516 0.3813 0.0640  0.0195  -0.0302 486 PRO   B CG  
4981 C  CD  . PRO   B 330 ? 0.3588 0.2302 0.3528 0.0740  0.0200  -0.0342 486 PRO   B CD  
4982 N  N   . GLU   B 331 ? 0.4293 0.2700 0.3989 0.0801  0.0317  -0.0463 487 GLU   B N   
4983 C  CA  . GLU   B 331 ? 0.4662 0.2922 0.4246 0.0858  0.0354  -0.0517 487 GLU   B CA  
4984 C  C   . GLU   B 331 ? 0.4284 0.2743 0.3962 0.0864  0.0406  -0.0569 487 GLU   B C   
4985 O  O   . GLU   B 331 ? 0.4849 0.3202 0.4436 0.0904  0.0441  -0.0620 487 GLU   B O   
4986 C  CB  . GLU   B 331 ? 0.6392 0.4502 0.5895 0.1020  0.0329  -0.0532 487 GLU   B CB  
4987 C  CG  . GLU   B 331 ? 0.5635 0.3476 0.4983 0.1017  0.0291  -0.0480 487 GLU   B CG  
4988 C  CD  . GLU   B 331 ? 0.8721 0.6377 0.7952 0.1192  0.0265  -0.0489 487 GLU   B CD  
4989 O  OE1 . GLU   B 331 ? 0.9662 0.7501 0.9006 0.1318  0.0229  -0.0494 487 GLU   B OE1 
4990 O  OE2 . GLU   B 331 ? 1.1052 0.8377 1.0072 0.1205  0.0281  -0.0493 487 GLU   B OE2 
4991 N  N   . PHE   B 332 ? 0.4874 0.3601 0.4719 0.0821  0.0417  -0.0558 488 PHE   B N   
4992 C  CA  . PHE   B 332 ? 0.3817 0.2718 0.3732 0.0799  0.0479  -0.0597 488 PHE   B CA  
4993 C  C   . PHE   B 332 ? 0.3783 0.2637 0.3625 0.0663  0.0498  -0.0577 488 PHE   B C   
4994 O  O   . PHE   B 332 ? 0.3275 0.2200 0.3167 0.0574  0.0480  -0.0528 488 PHE   B O   
4995 C  CB  . PHE   B 332 ? 0.3882 0.3078 0.3995 0.0808  0.0492  -0.0600 488 PHE   B CB  
4996 C  CG  . PHE   B 332 ? 0.4313 0.3682 0.4492 0.0809  0.0568  -0.0651 488 PHE   B CG  
4997 C  CD1 . PHE   B 332 ? 0.3863 0.3322 0.4092 0.0932  0.0595  -0.0717 488 PHE   B CD1 
4998 C  CD2 . PHE   B 332 ? 0.4278 0.3715 0.4455 0.0693  0.0616  -0.0632 488 PHE   B CD2 
4999 C  CE1 . PHE   B 332 ? 0.3976 0.3603 0.4264 0.0927  0.0675  -0.0767 488 PHE   B CE1 
5000 C  CE2 . PHE   B 332 ? 0.3843 0.3421 0.4057 0.0688  0.0695  -0.0674 488 PHE   B CE2 
5001 C  CZ  . PHE   B 332 ? 0.3208 0.2888 0.3483 0.0799  0.0729  -0.0744 488 PHE   B CZ  
5002 N  N   . ASN   B 333 ? 0.3999 0.2734 0.3719 0.0656  0.0531  -0.0618 489 ASN   B N   
5003 C  CA  . ASN   B 333 ? 0.4395 0.3092 0.4033 0.0545  0.0543  -0.0612 489 ASN   B CA  
5004 C  C   . ASN   B 333 ? 0.3627 0.2511 0.3321 0.0523  0.0600  -0.0624 489 ASN   B C   
5005 O  O   . ASN   B 333 ? 0.4672 0.3586 0.4346 0.0580  0.0651  -0.0677 489 ASN   B O   
5006 C  CB  . ASN   B 333 ? 0.3604 0.2076 0.3072 0.0543  0.0547  -0.0659 489 ASN   B CB  
5007 C  CG  . ASN   B 333 ? 0.4085 0.2540 0.3471 0.0434  0.0549  -0.0666 489 ASN   B CG  
5008 O  OD1 . ASN   B 333 ? 0.4388 0.2980 0.3828 0.0371  0.0545  -0.0628 489 ASN   B OD1 
5009 N  ND2 . ASN   B 333 ? 0.4277 0.2558 0.3522 0.0418  0.0554  -0.0719 489 ASN   B ND2 
5010 N  N   . LEU   B 334 ? 0.3973 0.2971 0.3723 0.0442  0.0597  -0.0575 490 LEU   B N   
5011 C  CA  . LEU   B 334 ? 0.4192 0.3338 0.3971 0.0412  0.0659  -0.0576 490 LEU   B CA  
5012 C  C   . LEU   B 334 ? 0.4006 0.3076 0.3634 0.0389  0.0690  -0.0608 490 LEU   B C   
5013 O  O   . LEU   B 334 ? 0.3740 0.2897 0.3355 0.0396  0.0757  -0.0629 490 LEU   B O   
5014 C  CB  . LEU   B 334 ? 0.3446 0.2682 0.3288 0.0333  0.0647  -0.0513 490 LEU   B CB  
5015 C  CG  . LEU   B 334 ? 0.3774 0.3120 0.3774 0.0345  0.0623  -0.0486 490 LEU   B CG  
5016 C  CD1 . LEU   B 334 ? 0.2748 0.2113 0.2768 0.0262  0.0594  -0.0425 490 LEU   B CD1 
5017 C  CD2 . LEU   B 334 ? 0.3098 0.2630 0.3223 0.0379  0.0687  -0.0519 490 LEU   B CD2 
5018 N  N   . PHE   B 335 ? 0.3765 0.2683 0.3276 0.0356  0.0646  -0.0617 491 PHE   B N   
5019 C  CA  . PHE   B 335 ? 0.3815 0.2667 0.3179 0.0332  0.0662  -0.0657 491 PHE   B CA  
5020 C  C   . PHE   B 335 ? 0.4422 0.3144 0.3701 0.0390  0.0676  -0.0730 491 PHE   B C   
5021 O  O   . PHE   B 335 ? 0.4811 0.3430 0.3959 0.0361  0.0666  -0.0773 491 PHE   B O   
5022 C  CB  . PHE   B 335 ? 0.4101 0.2897 0.3395 0.0253  0.0604  -0.0636 491 PHE   B CB  
5023 C  CG  . PHE   B 335 ? 0.4252 0.3156 0.3560 0.0206  0.0602  -0.0579 491 PHE   B CG  
5024 C  CD1 . PHE   B 335 ? 0.3420 0.2436 0.2775 0.0219  0.0661  -0.0551 491 PHE   B CD1 
5025 C  CD2 . PHE   B 335 ? 0.3725 0.2614 0.2991 0.0149  0.0546  -0.0558 491 PHE   B CD2 
5026 C  CE1 . PHE   B 335 ? 0.3644 0.2718 0.2984 0.0177  0.0665  -0.0496 491 PHE   B CE1 
5027 C  CE2 . PHE   B 335 ? 0.3251 0.2217 0.2510 0.0122  0.0542  -0.0505 491 PHE   B CE2 
5028 C  CZ  . PHE   B 335 ? 0.3420 0.2459 0.2704 0.0136  0.0603  -0.0471 491 PHE   B CZ  
5029 N  N   . SER   B 336 ? 0.3712 0.2436 0.3059 0.0477  0.0696  -0.0751 492 SER   B N   
5030 C  CA  . SER   B 336 ? 0.4530 0.3105 0.3785 0.0547  0.0710  -0.0821 492 SER   B CA  
5031 C  C   . SER   B 336 ? 0.4935 0.3536 0.4094 0.0559  0.0768  -0.0879 492 SER   B C   
5032 O  O   . SER   B 336 ? 0.4987 0.3751 0.4186 0.0549  0.0817  -0.0866 492 SER   B O   
5033 C  CB  . SER   B 336 ? 0.4363 0.2964 0.3714 0.0661  0.0718  -0.0832 492 SER   B CB  
5034 O  OG  . SER   B 336 ? 0.6362 0.4822 0.5614 0.0747  0.0741  -0.0904 492 SER   B OG  
5035 N  N   . SER   B 337 ? 0.4965 0.3389 0.3984 0.0575  0.0767  -0.0945 493 SER   B N   
5036 C  CA  . SER   B 337 ? 0.6294 0.4725 0.5206 0.0594  0.0820  -0.1011 493 SER   B CA  
5037 C  C   . SER   B 337 ? 0.5987 0.4546 0.4973 0.0694  0.0890  -0.1038 493 SER   B C   
5038 O  O   . SER   B 337 ? 0.5232 0.3866 0.4159 0.0702  0.0950  -0.1074 493 SER   B O   
5039 C  CB  . SER   B 337 ? 0.4528 0.2730 0.3281 0.0595  0.0805  -0.1087 493 SER   B CB  
5040 O  OG  . SER   B 337 ? 0.9060 0.7152 0.7768 0.0499  0.0742  -0.1070 493 SER   B OG  
5041 N  N   . ASN   B 338 ? 0.6200 0.4798 0.5312 0.0773  0.0885  -0.1027 494 ASN   B N   
5042 C  CA  . ASN   B 338 ? 0.5469 0.4232 0.4683 0.0872  0.0948  -0.1062 494 ASN   B CA  
5043 C  C   . ASN   B 338 ? 0.5634 0.4656 0.4988 0.0823  0.0992  -0.1016 494 ASN   B C   
5044 O  O   . ASN   B 338 ? 0.5202 0.4396 0.4637 0.0877  0.1063  -0.1054 494 ASN   B O   
5045 C  CB  . ASN   B 338 ? 0.6788 0.5506 0.6080 0.0987  0.0915  -0.1073 494 ASN   B CB  
5046 C  CG  . ASN   B 338 ? 0.8717 0.7144 0.7847 0.1047  0.0887  -0.1123 494 ASN   B CG  
5047 O  OD1 . ASN   B 338 ? 0.8514 0.6799 0.7488 0.1005  0.0901  -0.1166 494 ASN   B OD1 
5048 N  ND2 . ASN   B 338 ? 0.9705 0.8032 0.8858 0.1146  0.0848  -0.1120 494 ASN   B ND2 
5049 N  N   . LEU   B 339 ? 0.5838 0.4888 0.5219 0.0721  0.0957  -0.0941 495 LEU   B N   
5050 C  CA  . LEU   B 339 ? 0.5079 0.4330 0.4563 0.0660  0.1000  -0.0893 495 LEU   B CA  
5051 C  C   . LEU   B 339 ? 0.5075 0.4310 0.4425 0.0573  0.1031  -0.0869 495 LEU   B C   
5052 O  O   . LEU   B 339 ? 0.5352 0.4718 0.4714 0.0549  0.1111  -0.0864 495 LEU   B O   
5053 C  CB  . LEU   B 339 ? 0.5296 0.4589 0.4906 0.0617  0.0940  -0.0823 495 LEU   B CB  
5054 C  CG  . LEU   B 339 ? 0.4908 0.4245 0.4658 0.0705  0.0904  -0.0836 495 LEU   B CG  
5055 C  CD1 . LEU   B 339 ? 0.3448 0.2810 0.3292 0.0652  0.0840  -0.0765 495 LEU   B CD1 
5056 C  CD2 . LEU   B 339 ? 0.4613 0.4173 0.4503 0.0774  0.0974  -0.0887 495 LEU   B CD2 
5057 N  N   . ILE   B 340 ? 0.4987 0.4067 0.4204 0.0526  0.0971  -0.0855 496 ILE   B N   
5058 C  CA  . ILE   B 340 ? 0.4888 0.3945 0.3958 0.0462  0.0981  -0.0836 496 ILE   B CA  
5059 C  C   . ILE   B 340 ? 0.5842 0.4740 0.4749 0.0470  0.0944  -0.0897 496 ILE   B C   
5060 O  O   . ILE   B 340 ? 0.5194 0.3973 0.4100 0.0464  0.0877  -0.0910 496 ILE   B O   
5061 C  CB  . ILE   B 340 ? 0.4578 0.3649 0.3670 0.0383  0.0930  -0.0754 496 ILE   B CB  
5062 C  CG1 . ILE   B 340 ? 0.3781 0.2992 0.3043 0.0368  0.0960  -0.0701 496 ILE   B CG1 
5063 C  CG2 . ILE   B 340 ? 0.5351 0.4400 0.4275 0.0339  0.0940  -0.0734 496 ILE   B CG2 
5064 C  CD1 . ILE   B 340 ? 0.3820 0.3026 0.3121 0.0303  0.0901  -0.0626 496 ILE   B CD1 
5065 N  N   . ASP   B 341 ? 0.5628 0.4521 0.4393 0.0479  0.0993  -0.0939 497 ASP   B N   
5066 C  CA  . ASP   B 341 ? 0.4964 0.3717 0.3574 0.0484  0.0961  -0.1011 497 ASP   B CA  
5067 C  C   . ASP   B 341 ? 0.5978 0.4690 0.4494 0.0409  0.0887  -0.0986 497 ASP   B C   
5068 O  O   . ASP   B 341 ? 0.5078 0.3866 0.3612 0.0368  0.0874  -0.0914 497 ASP   B O   
5069 C  CB  . ASP   B 341 ? 0.6285 0.5052 0.4770 0.0530  0.1039  -0.1074 497 ASP   B CB  
5070 C  CG  . ASP   B 341 ? 0.7268 0.6075 0.5604 0.0489  0.1056  -0.1050 497 ASP   B CG  
5071 O  OD1 . ASP   B 341 ? 0.9066 0.7981 0.7427 0.0474  0.1116  -0.0990 497 ASP   B OD1 
5072 O  OD2 . ASP   B 341 ? 0.9559 0.8282 0.7742 0.0471  0.1010  -0.1093 497 ASP   B OD2 
5073 N  N   . LYS   B 342 ? 0.5864 0.4454 0.4277 0.0393  0.0838  -0.1055 498 LYS   B N   
5074 C  CA  . LYS   B 342 ? 0.6701 0.5274 0.5055 0.0322  0.0758  -0.1050 498 LYS   B CA  
5075 C  C   . LYS   B 342 ? 0.5426 0.4079 0.3648 0.0312  0.0759  -0.1033 498 LYS   B C   
5076 O  O   . LYS   B 342 ? 0.5875 0.4570 0.4083 0.0270  0.0697  -0.0996 498 LYS   B O   
5077 C  CB  . LYS   B 342 ? 0.7188 0.5621 0.5465 0.0295  0.0715  -0.1143 498 LYS   B CB  
5078 C  CG  . LYS   B 342 ? 0.8275 0.6714 0.6527 0.0212  0.0630  -0.1153 498 LYS   B CG  
5079 C  CD  . LYS   B 342 ? 0.7108 0.5492 0.5489 0.0167  0.0592  -0.1121 498 LYS   B CD  
5080 C  CE  . LYS   B 342 ? 0.8074 0.6414 0.6417 0.0077  0.0526  -0.1181 498 LYS   B CE  
5081 N  NZ  . LYS   B 342 ? 0.8872 0.7361 0.7171 0.0045  0.0473  -0.1178 498 LYS   B NZ  
5082 N  N   . ARG   B 343 ? 0.5222 0.3891 0.3332 0.0357  0.0829  -0.1060 499 ARG   B N   
5083 C  CA  . ARG   B 343 ? 0.6074 0.4794 0.4024 0.0358  0.0836  -0.1037 499 ARG   B CA  
5084 C  C   . ARG   B 343 ? 0.5418 0.4212 0.3424 0.0339  0.0840  -0.0926 499 ARG   B C   
5085 O  O   . ARG   B 343 ? 0.5413 0.4225 0.3322 0.0324  0.0788  -0.0893 499 ARG   B O   
5086 C  CB  . ARG   B 343 ? 0.6749 0.5471 0.4580 0.0410  0.0930  -0.1077 499 ARG   B CB  
5087 C  CG  . ARG   B 343 ? 0.7622 0.6357 0.5230 0.0422  0.0940  -0.1074 499 ARG   B CG  
5088 C  CD  . ARG   B 343 ? 0.7727 0.6467 0.5237 0.0469  0.1051  -0.1107 499 ARG   B CD  
5089 N  NE  . ARG   B 343 ? 0.8182 0.6886 0.5452 0.0494  0.1044  -0.1170 499 ARG   B NE  
5090 C  CZ  . ARG   B 343 ? 1.0099 0.8799 0.7237 0.0536  0.1135  -0.1209 499 ARG   B CZ  
5091 N  NH1 . ARG   B 343 ? 0.9215 0.7960 0.6448 0.0557  0.1244  -0.1198 499 ARG   B NH1 
5092 N  NH2 . ARG   B 343 ? 0.9715 0.8380 0.6623 0.0558  0.1114  -0.1268 499 ARG   B NH2 
5093 N  N   . SER   B 344 ? 0.5133 0.3972 0.3293 0.0342  0.0898  -0.0873 500 SER   B N   
5094 C  CA  . SER   B 344 ? 0.5791 0.4685 0.4008 0.0314  0.0908  -0.0773 500 SER   B CA  
5095 C  C   . SER   B 344 ? 0.4627 0.3516 0.2913 0.0276  0.0807  -0.0737 500 SER   B C   
5096 O  O   . SER   B 344 ? 0.4786 0.3688 0.3010 0.0262  0.0781  -0.0676 500 SER   B O   
5097 C  CB  . SER   B 344 ? 0.4586 0.3549 0.2977 0.0318  0.0986  -0.0745 500 SER   B CB  
5098 O  OG  . SER   B 344 ? 0.4989 0.3984 0.3329 0.0352  0.1087  -0.0783 500 SER   B OG  
5099 N  N   . LYS   B 345 ? 0.4118 0.2979 0.2522 0.0263  0.0755  -0.0775 501 LYS   B N   
5100 C  CA  . LYS   B 345 ? 0.4556 0.3420 0.3032 0.0220  0.0667  -0.0748 501 LYS   B CA  
5101 C  C   . LYS   B 345 ? 0.4568 0.3436 0.2902 0.0207  0.0597  -0.0779 501 LYS   B C   
5102 O  O   . LYS   B 345 ? 0.5455 0.4366 0.3799 0.0189  0.0541  -0.0733 501 LYS   B O   
5103 C  CB  . LYS   B 345 ? 0.4048 0.2857 0.2646 0.0206  0.0638  -0.0787 501 LYS   B CB  
5104 C  CG  . LYS   B 345 ? 0.5898 0.4720 0.4645 0.0233  0.0688  -0.0757 501 LYS   B CG  
5105 C  CD  . LYS   B 345 ? 0.5960 0.4685 0.4766 0.0243  0.0668  -0.0805 501 LYS   B CD  
5106 C  CE  . LYS   B 345 ? 0.5738 0.4483 0.4650 0.0305  0.0725  -0.0802 501 LYS   B CE  
5107 N  NZ  . LYS   B 345 ? 0.4497 0.3110 0.3410 0.0342  0.0714  -0.0858 501 LYS   B NZ  
5108 N  N   . GLU   B 346 ? 0.4484 0.3319 0.2686 0.0222  0.0596  -0.0862 502 GLU   B N   
5109 C  CA  . GLU   B 346 ? 0.5116 0.3981 0.3181 0.0216  0.0524  -0.0905 502 GLU   B CA  
5110 C  C   . GLU   B 346 ? 0.5350 0.4254 0.3276 0.0256  0.0532  -0.0839 502 GLU   B C   
5111 O  O   . GLU   B 346 ? 0.5231 0.4186 0.3102 0.0260  0.0456  -0.0828 502 GLU   B O   
5112 C  CB  . GLU   B 346 ? 0.4985 0.3803 0.2933 0.0222  0.0526  -0.1017 502 GLU   B CB  
5113 C  CG  . GLU   B 346 ? 0.5563 0.4304 0.3603 0.0177  0.0511  -0.1091 502 GLU   B CG  
5114 C  CD  . GLU   B 346 ? 0.7682 0.6347 0.5599 0.0189  0.0534  -0.1200 502 GLU   B CD  
5115 O  OE1 . GLU   B 346 ? 0.7553 0.6233 0.5328 0.0239  0.0573  -0.1212 502 GLU   B OE1 
5116 O  OE2 . GLU   B 346 ? 0.7334 0.5909 0.5284 0.0147  0.0518  -0.1274 502 GLU   B OE2 
5117 N  N   . PHE   B 347 ? 0.4769 0.3646 0.2629 0.0289  0.0625  -0.0797 503 PHE   B N   
5118 C  CA  . PHE   B 347 ? 0.4958 0.3831 0.2662 0.0323  0.0648  -0.0723 503 PHE   B CA  
5119 C  C   . PHE   B 347 ? 0.4913 0.3804 0.2707 0.0306  0.0616  -0.0633 503 PHE   B C   
5120 O  O   . PHE   B 347 ? 0.5417 0.4310 0.3091 0.0334  0.0561  -0.0597 503 PHE   B O   
5121 C  CB  . PHE   B 347 ? 0.5035 0.3873 0.2674 0.0341  0.0773  -0.0696 503 PHE   B CB  
5122 C  CG  . PHE   B 347 ? 0.5473 0.4266 0.2907 0.0369  0.0814  -0.0621 503 PHE   B CG  
5123 C  CD1 . PHE   B 347 ? 0.6034 0.4794 0.3216 0.0419  0.0798  -0.0649 503 PHE   B CD1 
5124 C  CD2 . PHE   B 347 ? 0.5411 0.4182 0.2890 0.0347  0.0870  -0.0523 503 PHE   B CD2 
5125 C  CE1 . PHE   B 347 ? 0.6856 0.5543 0.3817 0.0453  0.0839  -0.0573 503 PHE   B CE1 
5126 C  CE2 . PHE   B 347 ? 0.6206 0.4896 0.3471 0.0369  0.0916  -0.0450 503 PHE   B CE2 
5127 C  CZ  . PHE   B 347 ? 0.5898 0.4538 0.2895 0.0426  0.0902  -0.0470 503 PHE   B CZ  
5128 N  N   . LEU   B 348 ? 0.4238 0.3141 0.2236 0.0268  0.0644  -0.0598 504 LEU   B N   
5129 C  CA  . LEU   B 348 ? 0.4101 0.3018 0.2189 0.0249  0.0618  -0.0518 504 LEU   B CA  
5130 C  C   . LEU   B 348 ? 0.4312 0.3273 0.2431 0.0242  0.0503  -0.0541 504 LEU   B C   
5131 O  O   . LEU   B 348 ? 0.4538 0.3506 0.2621 0.0257  0.0461  -0.0486 504 LEU   B O   
5132 C  CB  . LEU   B 348 ? 0.3935 0.2870 0.2237 0.0212  0.0666  -0.0491 504 LEU   B CB  
5133 C  CG  . LEU   B 348 ? 0.4171 0.3118 0.2573 0.0187  0.0647  -0.0412 504 LEU   B CG  
5134 C  CD1 . LEU   B 348 ? 0.3927 0.2819 0.2160 0.0206  0.0678  -0.0340 504 LEU   B CD1 
5135 C  CD2 . LEU   B 348 ? 0.4143 0.3124 0.2742 0.0157  0.0702  -0.0393 504 LEU   B CD2 
5136 N  N   . THR   B 349 ? 0.3990 0.2977 0.2170 0.0219  0.0454  -0.0627 505 THR   B N   
5137 C  CA  . THR   B 349 ? 0.5154 0.4206 0.3371 0.0198  0.0353  -0.0665 505 THR   B CA  
5138 C  C   . THR   B 349 ? 0.4163 0.3259 0.2195 0.0249  0.0294  -0.0680 505 THR   B C   
5139 O  O   . THR   B 349 ? 0.4019 0.3176 0.2056 0.0265  0.0225  -0.0657 505 THR   B O   
5140 C  CB  . THR   B 349 ? 0.4488 0.3537 0.2780 0.0150  0.0331  -0.0762 505 THR   B CB  
5141 O  OG1 . THR   B 349 ? 0.4398 0.3396 0.2849 0.0118  0.0373  -0.0740 505 THR   B OG1 
5142 C  CG2 . THR   B 349 ? 0.5168 0.4303 0.3492 0.0114  0.0235  -0.0818 505 THR   B CG2 
5143 N  N   . LYS   B 350 ? 0.4460 0.3529 0.2320 0.0286  0.0317  -0.0723 506 LYS   B N   
5144 C  CA  . LYS   B 350 ? 0.4701 0.3808 0.2359 0.0350  0.0258  -0.0738 506 LYS   B CA  
5145 C  C   . LYS   B 350 ? 0.4461 0.3524 0.2020 0.0406  0.0267  -0.0627 506 LYS   B C   
5146 O  O   . LYS   B 350 ? 0.4733 0.3853 0.2223 0.0455  0.0183  -0.0621 506 LYS   B O   
5147 C  CB  . LYS   B 350 ? 0.5012 0.4079 0.2487 0.0383  0.0296  -0.0794 506 LYS   B CB  
5148 C  CG  . LYS   B 350 ? 0.7131 0.6229 0.4366 0.0463  0.0234  -0.0810 506 LYS   B CG  
5149 C  CD  . LYS   B 350 ? 0.8750 0.7803 0.5797 0.0492  0.0277  -0.0868 506 LYS   B CD  
5150 C  CE  . LYS   B 350 ? 1.0524 0.9494 0.7302 0.0578  0.0314  -0.0792 506 LYS   B CE  
5151 N  NZ  . LYS   B 350 ? 1.1677 1.0528 0.8436 0.0562  0.0455  -0.0715 506 LYS   B NZ  
5152 N  N   . GLN   B 351 ? 0.4599 0.3561 0.2151 0.0399  0.0370  -0.0544 507 GLN   B N   
5153 C  CA  . GLN   B 351 ? 0.4543 0.3426 0.1984 0.0440  0.0394  -0.0438 507 GLN   B CA  
5154 C  C   . GLN   B 351 ? 0.4374 0.3302 0.1952 0.0431  0.0327  -0.0401 507 GLN   B C   
5155 O  O   . GLN   B 351 ? 0.4461 0.3375 0.1915 0.0495  0.0271  -0.0362 507 GLN   B O   
5156 C  CB  . GLN   B 351 ? 0.5010 0.3794 0.2452 0.0408  0.0527  -0.0371 507 GLN   B CB  
5157 C  CG  . GLN   B 351 ? 0.5347 0.4082 0.2625 0.0425  0.0607  -0.0399 507 GLN   B CG  
5158 C  CD  . GLN   B 351 ? 0.5803 0.4498 0.2790 0.0508  0.0562  -0.0407 507 GLN   B CD  
5159 O  OE1 . GLN   B 351 ? 0.6860 0.5586 0.3750 0.0531  0.0548  -0.0485 507 GLN   B OE1 
5160 N  NE2 . GLN   B 351 ? 0.6717 0.5337 0.3553 0.0561  0.0536  -0.0328 507 GLN   B NE2 
5161 N  N   . ILE   B 352 ? 0.4149 0.3126 0.1971 0.0360  0.0331  -0.0413 508 ILE   B N   
5162 C  CA  . ILE   B 352 ? 0.3985 0.3004 0.1945 0.0345  0.0278  -0.0378 508 ILE   B CA  
5163 C  C   . ILE   B 352 ? 0.3980 0.3115 0.1924 0.0378  0.0160  -0.0439 508 ILE   B C   
5164 O  O   . ILE   B 352 ? 0.3967 0.3123 0.1894 0.0420  0.0106  -0.0401 508 ILE   B O   
5165 C  CB  . ILE   B 352 ? 0.4389 0.3433 0.2595 0.0266  0.0307  -0.0385 508 ILE   B CB  
5166 C  CG1 . ILE   B 352 ? 0.3952 0.2915 0.2196 0.0241  0.0413  -0.0317 508 ILE   B CG1 
5167 C  CG2 . ILE   B 352 ? 0.3603 0.2714 0.1950 0.0246  0.0238  -0.0375 508 ILE   B CG2 
5168 C  CD1 . ILE   B 352 ? 0.3755 0.2749 0.2222 0.0182  0.0440  -0.0332 508 ILE   B CD1 
5169 N  N   . GLU   B 353 ? 0.3998 0.3218 0.1954 0.0359  0.0119  -0.0541 509 GLU   B N   
5170 C  CA  . GLU   B 353 ? 0.4415 0.3780 0.2375 0.0379  0.0009  -0.0617 509 GLU   B CA  
5171 C  C   . GLU   B 353 ? 0.4333 0.3709 0.2067 0.0491  -0.0046 -0.0600 509 GLU   B C   
5172 O  O   . GLU   B 353 ? 0.4635 0.4115 0.2375 0.0538  -0.0133 -0.0612 509 GLU   B O   
5173 C  CB  . GLU   B 353 ? 0.4005 0.3444 0.2013 0.0321  -0.0013 -0.0738 509 GLU   B CB  
5174 C  CG  . GLU   B 353 ? 0.4176 0.3625 0.2404 0.0219  0.0005  -0.0770 509 GLU   B CG  
5175 C  CD  . GLU   B 353 ? 0.4396 0.3888 0.2649 0.0156  -0.0014 -0.0892 509 GLU   B CD  
5176 O  OE1 . GLU   B 353 ? 0.5217 0.4682 0.3329 0.0182  -0.0002 -0.0941 509 GLU   B OE1 
5177 O  OE2 . GLU   B 353 ? 0.4801 0.4341 0.3204 0.0075  -0.0035 -0.0941 509 GLU   B OE2 
5178 N  N   . TYR   B 354 ? 0.4396 0.3664 0.1918 0.0542  0.0004  -0.0574 510 TYR   B N   
5179 C  CA  . TYR   B 354 ? 0.4621 0.3856 0.1890 0.0661  -0.0040 -0.0539 510 TYR   B CA  
5180 C  C   . TYR   B 354 ? 0.4612 0.3763 0.1857 0.0707  -0.0039 -0.0432 510 TYR   B C   
5181 O  O   . TYR   B 354 ? 0.5240 0.4452 0.2407 0.0797  -0.0130 -0.0433 510 TYR   B O   
5182 C  CB  . TYR   B 354 ? 0.5227 0.4322 0.2262 0.0696  0.0039  -0.0511 510 TYR   B CB  
5183 C  CG  . TYR   B 354 ? 0.7784 0.6792 0.4517 0.0824  0.0009  -0.0454 510 TYR   B CG  
5184 C  CD1 . TYR   B 354 ? 0.6903 0.6014 0.3474 0.0914  -0.0092 -0.0530 510 TYR   B CD1 
5185 C  CD2 . TYR   B 354 ? 0.6212 0.5027 0.2810 0.0857  0.0080  -0.0328 510 TYR   B CD2 
5186 C  CE1 . TYR   B 354 ? 0.6804 0.5823 0.3075 0.1049  -0.0126 -0.0476 510 TYR   B CE1 
5187 C  CE2 . TYR   B 354 ? 0.8001 0.6698 0.4291 0.0982  0.0056  -0.0270 510 TYR   B CE2 
5188 C  CZ  . TYR   B 354 ? 0.6644 0.5440 0.2764 0.1086  -0.0050 -0.0341 510 TYR   B CZ  
5189 O  OH  . TYR   B 354 ? 0.8035 0.6700 0.3824 0.1226  -0.0079 -0.0279 510 TYR   B OH  
5190 N  N   . GLU   B 355 ? 0.4538 0.3555 0.1853 0.0650  0.0062  -0.0346 511 GLU   B N   
5191 C  CA  . GLU   B 355 ? 0.4803 0.3718 0.2097 0.0679  0.0075  -0.0248 511 GLU   B CA  
5192 C  C   . GLU   B 355 ? 0.5392 0.4449 0.2845 0.0690  -0.0025 -0.0279 511 GLU   B C   
5193 O  O   . GLU   B 355 ? 0.4808 0.3843 0.2150 0.0783  -0.0081 -0.0242 511 GLU   B O   
5194 C  CB  . GLU   B 355 ? 0.4779 0.3579 0.2188 0.0587  0.0194  -0.0180 511 GLU   B CB  
5195 C  CG  . GLU   B 355 ? 0.5680 0.4340 0.2927 0.0577  0.0307  -0.0142 511 GLU   B CG  
5196 C  CD  . GLU   B 355 ? 0.6432 0.4920 0.3366 0.0668  0.0324  -0.0065 511 GLU   B CD  
5197 O  OE1 . GLU   B 355 ? 0.6056 0.4461 0.2942 0.0707  0.0303  0.0000  511 GLU   B OE1 
5198 O  OE2 . GLU   B 355 ? 0.6705 0.5127 0.3424 0.0707  0.0361  -0.0069 511 GLU   B OE2 
5199 N  N   . ARG   B 356 ? 0.4136 0.3335 0.1841 0.0600  -0.0044 -0.0347 512 ARG   B N   
5200 C  CA  . ARG   B 356 ? 0.4022 0.3364 0.1892 0.0593  -0.0124 -0.0381 512 ARG   B CA  
5201 C  C   . ARG   B 356 ? 0.4068 0.3571 0.1854 0.0682  -0.0241 -0.0457 512 ARG   B C   
5202 O  O   . ARG   B 356 ? 0.5090 0.4680 0.2914 0.0735  -0.0309 -0.0457 512 ARG   B O   
5203 C  CB  . ARG   B 356 ? 0.3741 0.3174 0.1866 0.0471  -0.0108 -0.0438 512 ARG   B CB  
5204 C  CG  . ARG   B 356 ? 0.3554 0.3089 0.1867 0.0439  -0.0152 -0.0445 512 ARG   B CG  
5205 C  CD  . ARG   B 356 ? 0.3603 0.3345 0.2020 0.0407  -0.0232 -0.0562 512 ARG   B CD  
5206 N  NE  . ARG   B 356 ? 0.3618 0.3366 0.2117 0.0310  -0.0195 -0.0629 512 ARG   B NE  
5207 C  CZ  . ARG   B 356 ? 0.4386 0.4114 0.3058 0.0210  -0.0155 -0.0635 512 ARG   B CZ  
5208 N  NH1 . ARG   B 356 ? 0.4027 0.3746 0.2819 0.0188  -0.0146 -0.0580 512 ARG   B NH1 
5209 N  NH2 . ARG   B 356 ? 0.3341 0.3045 0.2050 0.0137  -0.0124 -0.0697 512 ARG   B NH2 
5210 N  N   . ASN   B 357 ? 0.4829 0.4388 0.2502 0.0705  -0.0266 -0.0528 513 ASN   B N   
5211 C  CA  . ASN   B 357 ? 0.4453 0.4191 0.2045 0.0795  -0.0384 -0.0613 513 ASN   B CA  
5212 C  C   . ASN   B 357 ? 0.5353 0.4996 0.2677 0.0955  -0.0422 -0.0543 513 ASN   B C   
5213 O  O   . ASN   B 357 ? 0.4860 0.4661 0.2128 0.1057  -0.0532 -0.0600 513 ASN   B O   
5214 C  CB  . ASN   B 357 ? 0.4380 0.4212 0.1933 0.0764  -0.0403 -0.0723 513 ASN   B CB  
5215 C  CG  . ASN   B 357 ? 0.5016 0.4987 0.2820 0.0625  -0.0404 -0.0824 513 ASN   B CG  
5216 O  OD1 . ASN   B 357 ? 0.4427 0.4538 0.2415 0.0583  -0.0447 -0.0859 513 ASN   B OD1 
5217 N  ND2 . ASN   B 357 ? 0.4206 0.4127 0.2008 0.0552  -0.0353 -0.0872 513 ASN   B ND2 
5218 N  N   . ASN   B 358 ? 0.5694 0.5082 0.2844 0.0982  -0.0333 -0.0425 514 ASN   B N   
5219 C  CA  . ASN   B 358 ? 0.6511 0.5753 0.3363 0.1134  -0.0356 -0.0349 514 ASN   B CA  
5220 C  C   . ASN   B 358 ? 0.6841 0.5889 0.3669 0.1148  -0.0303 -0.0229 514 ASN   B C   
5221 O  O   . ASN   B 358 ? 0.7469 0.6286 0.4027 0.1233  -0.0263 -0.0135 514 ASN   B O   
5222 C  CB  . ASN   B 358 ? 0.5235 0.4318 0.1818 0.1168  -0.0297 -0.0320 514 ASN   B CB  
5223 C  CG  . ASN   B 358 ? 0.5987 0.5255 0.2539 0.1185  -0.0368 -0.0443 514 ASN   B CG  
5224 O  OD1 . ASN   B 358 ? 0.5960 0.5317 0.2342 0.1315  -0.0471 -0.0486 514 ASN   B OD1 
5225 N  ND2 . ASN   B 358 ? 0.6857 0.6183 0.3569 0.1057  -0.0315 -0.0506 514 ASN   B ND2 
5226 N  N   . GLU   B 359 ? 0.5697 0.4822 0.2790 0.1065  -0.0298 -0.0233 515 GLU   B N   
5227 C  CA  . GLU   B 359 ? 0.6835 0.5803 0.3934 0.1072  -0.0258 -0.0137 515 GLU   B CA  
5228 C  C   . GLU   B 359 ? 0.5815 0.4508 0.2795 0.1016  -0.0122 -0.0031 515 GLU   B C   
5229 O  O   . GLU   B 359 ? 0.6876 0.5353 0.3683 0.1071  -0.0085 0.0062  515 GLU   B O   
5230 C  CB  . GLU   B 359 ? 0.7737 0.6681 0.4654 0.1239  -0.0349 -0.0114 515 GLU   B CB  
5231 C  CG  . GLU   B 359 ? 0.8617 0.7866 0.5641 0.1307  -0.0488 -0.0230 515 GLU   B CG  
5232 C  CD  . GLU   B 359 ? 1.0583 0.9821 0.7448 0.1486  -0.0579 -0.0210 515 GLU   B CD  
5233 O  OE1 . GLU   B 359 ? 1.1712 1.0791 0.8260 0.1625  -0.0598 -0.0161 515 GLU   B OE1 
5234 O  OE2 . GLU   B 359 ? 1.1429 1.0811 0.8474 0.1493  -0.0631 -0.0241 515 GLU   B OE2 
5235 N  N   . PHE   B 360 ? 0.5843 0.4545 0.2917 0.0906  -0.0043 -0.0051 516 PHE   B N   
5236 C  CA  . PHE   B 360 ? 0.5928 0.4436 0.2974 0.0822  0.0095  0.0026  516 PHE   B CA  
5237 C  C   . PHE   B 360 ? 0.6958 0.5200 0.3667 0.0895  0.0158  0.0121  516 PHE   B C   
5238 O  O   . PHE   B 360 ? 0.7539 0.5598 0.4195 0.0878  0.0221  0.0204  516 PHE   B O   
5239 C  CB  . PHE   B 360 ? 0.5126 0.3629 0.2403 0.0731  0.0132  0.0057  516 PHE   B CB  
5240 C  CG  . PHE   B 360 ? 0.5001 0.3728 0.2584 0.0654  0.0084  -0.0025 516 PHE   B CG  
5241 C  CD1 . PHE   B 360 ? 0.4761 0.3546 0.2501 0.0553  0.0142  -0.0062 516 PHE   B CD1 
5242 C  CD2 . PHE   B 360 ? 0.4695 0.3566 0.2393 0.0688  -0.0015 -0.0065 516 PHE   B CD2 
5243 C  CE1 . PHE   B 360 ? 0.4862 0.3813 0.2848 0.0486  0.0102  -0.0131 516 PHE   B CE1 
5244 C  CE2 . PHE   B 360 ? 0.4674 0.3729 0.2630 0.0609  -0.0048 -0.0137 516 PHE   B CE2 
5245 C  CZ  . PHE   B 360 ? 0.4575 0.3655 0.2665 0.0507  0.0011  -0.0167 516 PHE   B CZ  
5246 N  N   . PRO   B 361 ? 0.5982 0.4185 0.2447 0.0972  0.0147  0.0110  517 PRO   B N   
5247 C  CA  . PRO   B 361 ? 0.7242 0.5161 0.3359 0.1034  0.0224  0.0207  517 PRO   B CA  
5248 C  C   . PRO   B 361 ? 0.6720 0.4482 0.2840 0.0908  0.0389  0.0264  517 PRO   B C   
5249 O  O   . PRO   B 361 ? 0.8218 0.5715 0.4085 0.0924  0.0476  0.0357  517 PRO   B O   
5250 C  CB  . PRO   B 361 ? 0.6557 0.4516 0.2439 0.1141  0.0164  0.0162  517 PRO   B CB  
5251 C  CG  . PRO   B 361 ? 0.6182 0.4419 0.2321 0.1076  0.0113  0.0043  517 PRO   B CG  
5252 C  CD  . PRO   B 361 ? 0.6020 0.4421 0.2491 0.1010  0.0063  0.0007  517 PRO   B CD  
5253 N  N   . VAL   B 362 ? 0.7287 0.5200 0.3679 0.0785  0.0438  0.0209  518 VAL   B N   
5254 C  CA  . VAL   B 362 ? 0.7190 0.5000 0.3619 0.0667  0.0591  0.0249  518 VAL   B CA  
5255 C  C   . VAL   B 362 ? 0.6886 0.4563 0.3380 0.0605  0.0653  0.0321  518 VAL   B C   
5256 O  O   . VAL   B 362 ? 0.8172 0.5716 0.4625 0.0519  0.0788  0.0369  518 VAL   B O   
5257 C  CB  . VAL   B 362 ? 0.6854 0.4872 0.3572 0.0571  0.0613  0.0165  518 VAL   B CB  
5258 C  CG1 . VAL   B 362 ? 0.5938 0.4090 0.2986 0.0500  0.0577  0.0141  518 VAL   B CG1 
5259 C  CG2 . VAL   B 362 ? 0.8032 0.5974 0.4712 0.0489  0.0765  0.0184  518 VAL   B CG2 
5260 N  N   . PHE   B 363 ? 0.6562 0.4282 0.3158 0.0642  0.0560  0.0323  519 PHE   B N   
5261 C  CA  . PHE   B 363 ? 0.6711 0.4299 0.3360 0.0587  0.0611  0.0384  519 PHE   B CA  
5262 C  C   . PHE   B 363 ? 0.9356 0.6623 0.5654 0.0631  0.0687  0.0482  519 PHE   B C   
5263 O  O   . PHE   B 363 ? 0.9489 0.6598 0.5787 0.0541  0.0791  0.0536  519 PHE   B O   
5264 C  CB  . PHE   B 363 ? 0.6448 0.4151 0.3260 0.0632  0.0491  0.0360  519 PHE   B CB  
5265 C  CG  . PHE   B 363 ? 0.7568 0.5516 0.4744 0.0544  0.0460  0.0289  519 PHE   B CG  
5266 C  CD1 . PHE   B 363 ? 0.6129 0.4144 0.3477 0.0427  0.0548  0.0267  519 PHE   B CD1 
5267 C  CD2 . PHE   B 363 ? 0.5859 0.3968 0.3195 0.0582  0.0344  0.0244  519 PHE   B CD2 
5268 C  CE1 . PHE   B 363 ? 0.5551 0.3765 0.3206 0.0360  0.0517  0.0207  519 PHE   B CE1 
5269 C  CE2 . PHE   B 363 ? 0.5134 0.3438 0.2775 0.0500  0.0322  0.0185  519 PHE   B CE2 
5270 C  CZ  . PHE   B 363 ? 0.5174 0.3519 0.2965 0.0394  0.0406  0.0170  519 PHE   B CZ  
5271 N  N   . ASP   B 364 ? 0.9622 0.6782 0.5612 0.0765  0.0638  0.0504  520 ASP   B N   
5272 C  CA  . ASP   B 364 ? 0.9701 0.6520 0.5306 0.0826  0.0704  0.0603  520 ASP   B CA  
5273 C  C   . ASP   B 364 ? 0.9773 0.6419 0.5281 0.0698  0.0887  0.0651  520 ASP   B C   
5274 O  O   . ASP   B 364 ? 1.3481 0.9952 0.8728 0.0734  0.0941  0.0689  520 ASP   B O   
5275 C  CB  . ASP   B 364 ? 0.9131 0.5899 0.4421 0.1001  0.0615  0.0606  520 ASP   B CB  
5276 C  CG  . ASP   B 364 ? 1.0852 0.7809 0.6230 0.1132  0.0435  0.0551  520 ASP   B CG  
5277 O  OD1 . ASP   B 364 ? 1.1092 0.8148 0.6714 0.1098  0.0392  0.0532  520 ASP   B OD1 
5278 O  OD2 . ASP   B 364 ? 1.0174 0.7200 0.5394 0.1265  0.0338  0.0517  520 ASP   B OD2 
5279 C  C4  . A1EAH C .   ? 0.4000 0.5626 0.5189 -0.0466 -0.1107 -0.1554 601 A1EAH A C4  
5280 C  C14 . A1EAH C .   ? 0.4974 0.6250 0.4862 0.0574  -0.1527 -0.1032 601 A1EAH A C14 
5281 C  C5  . A1EAH C .   ? 0.4432 0.6091 0.5477 -0.0339 -0.1205 -0.1548 601 A1EAH A C5  
5282 C  C6  . A1EAH C .   ? 0.3686 0.5253 0.4602 -0.0359 -0.1222 -0.1588 601 A1EAH A C6  
5283 C  C11 . A1EAH C .   ? 0.6149 0.7951 0.6379 0.0524  -0.1653 -0.1298 601 A1EAH A C11 
5284 C  C7  . A1EAH C .   ? 0.4159 0.5872 0.4953 -0.0104 -0.1358 -0.1506 601 A1EAH A C7  
5285 C  C8  . A1EAH C .   ? 0.5153 0.6879 0.5469 0.0267  -0.1569 -0.1419 601 A1EAH A C8  
5286 C  C9  . A1EAH C .   ? 0.5022 0.6819 0.5421 0.0335  -0.1577 -0.1369 601 A1EAH A C9  
5287 C  C10 . A1EAH C .   ? 0.5806 0.7636 0.6421 0.0201  -0.1502 -0.1401 601 A1EAH A C10 
5288 C  C12 . A1EAH C .   ? 0.5961 0.7493 0.5917 0.0608  -0.1639 -0.1165 601 A1EAH A C12 
5289 C  C13 . A1EAH C .   ? 0.6545 0.8544 0.6917 0.0602  -0.1684 -0.1314 601 A1EAH A C13 
5290 N  N1  . A1EAH C .   ? 0.3775 0.5528 0.4745 -0.0176 -0.1294 -0.1500 601 A1EAH A N1  
5291 N  N2  . A1EAH C .   ? 0.5028 0.6641 0.5794 -0.0214 -0.1318 -0.1565 601 A1EAH A N2  
5292 C  C3  . A1EAH C .   ? 0.4321 0.5800 0.5509 -0.0608 -0.1027 -0.1595 601 A1EAH A C3  
5293 N  N3  . A1EAH C .   ? 0.4646 0.6399 0.5286 0.0062  -0.1449 -0.1461 601 A1EAH A N3  
5294 C  C1  . A1EAH C .   ? 0.3632 0.5063 0.4563 -0.0502 -0.1144 -0.1636 601 A1EAH A C1  
5295 C  C15 . A1EAH C .   ? 0.4962 0.6423 0.4667 0.0718  -0.1701 -0.1139 601 A1EAH A C15 
5296 C  C16 . A1EAH C .   ? 0.4459 0.5464 0.3655 0.0838  -0.1642 -0.0923 601 A1EAH A C16 
5297 C  C17 . A1EAH C .   ? 0.4410 0.5246 0.3131 0.1023  -0.1719 -0.0855 601 A1EAH A C17 
5298 C  C18 . A1EAH C .   ? 0.3970 0.4604 0.2701 0.0916  -0.1584 -0.0766 601 A1EAH A C18 
5299 C  C19 . A1EAH C .   ? 0.4366 0.5129 0.2833 0.1132  -0.1755 -0.0821 601 A1EAH A C19 
5300 C  C2  . A1EAH C .   ? 0.3035 0.4415 0.4096 -0.0624 -0.1048 -0.1636 601 A1EAH A C2  
5301 C  C20 . A1EAH C .   ? 0.5177 0.5677 0.3348 0.1154  -0.1701 -0.0719 601 A1EAH A C20 
5302 C  C21 . A1EAH C .   ? 0.5171 0.5490 0.3357 0.1044  -0.1573 -0.0641 601 A1EAH A C21 
5303 C  C22 . A1EAH C .   ? 0.4806 0.5191 0.3277 0.0927  -0.1512 -0.0662 601 A1EAH A C22 
5304 C  C23 . A1EAH C .   ? 0.7607 1.0037 0.8329 0.0594  -0.1707 -0.1459 601 A1EAH A C23 
5305 C  C24 . A1EAH C .   ? 0.6844 0.9228 0.7482 0.0743  -0.1734 -0.1373 601 A1EAH A C24 
5306 C  C25 . A1EAH C .   ? 0.7178 0.9297 0.7581 0.0819  -0.1734 -0.1248 601 A1EAH A C25 
5307 C  C26 . A1EAH C .   ? 0.7490 0.9421 0.7759 0.0745  -0.1708 -0.1219 601 A1EAH A C26 
5308 C  C27 . A1EAH C .   ? 0.5721 0.7389 0.5809 0.0352  -0.1624 -0.1412 601 A1EAH A C27 
5309 C  C28 . A1EAH C .   ? 0.4489 0.5711 0.4551 0.0469  -0.1425 -0.0996 601 A1EAH A C28 
5310 N  N4  . A1EAH C .   ? 0.4812 0.6509 0.5272 0.0108  -0.1495 -0.1474 601 A1EAH A N4  
5311 N  N5  . A1EAH C .   ? 0.4619 0.5695 0.4242 0.0652  -0.1521 -0.0937 601 A1EAH A N5  
5312 N  N6  . A1EAH C .   ? 0.5852 0.7031 0.5350 0.0744  -0.1628 -0.0998 601 A1EAH A N6  
5313 N  N7  . A1EAH C .   ? 0.4310 0.5383 0.3340 0.0964  -0.1744 -0.0952 601 A1EAH A N7  
5314 N  N8  . A1EAH C .   ? 0.3727 0.4462 0.2749 0.0807  -0.1540 -0.0807 601 A1EAH A N8  
5315 N  N9  . A1EAH C .   ? 0.6896 0.9130 0.7485 0.0526  -0.1682 -0.1430 601 A1EAH A N9  
5316 O  O1  . A1EAH C .   ? 0.4456 0.6354 0.5219 0.0197  -0.1471 -0.1378 601 A1EAH A O1  
5317 O  O2  . A1EAH C .   ? 0.5077 0.6658 0.4739 0.0772  -0.1759 -0.1198 601 A1EAH A O2  
5318 ZN ZN  . ZN    D .   ? 0.3505 0.2752 0.3240 -0.0071 -0.0240 0.0067  602 ZN    A ZN  
5319 C  C4  . A1EAH E .   ? 0.3979 0.3059 0.3001 -0.0240 0.1291  -0.0097 601 A1EAH B C4  
5320 C  C14 . A1EAH E .   ? 0.4497 0.4726 0.4911 0.0029  0.1151  -0.0528 601 A1EAH B C14 
5321 C  C5  . A1EAH E .   ? 0.4696 0.3968 0.3956 -0.0270 0.1333  -0.0157 601 A1EAH B C5  
5322 C  C6  . A1EAH E .   ? 0.4582 0.3948 0.3869 -0.0314 0.1462  -0.0195 601 A1EAH B C6  
5323 C  C11 . A1EAH E .   ? 0.5392 0.5690 0.5919 -0.0162 0.1202  -0.0470 601 A1EAH B C11 
5324 C  C7  . A1EAH E .   ? 0.3900 0.3496 0.3566 -0.0284 0.1343  -0.0255 601 A1EAH B C7  
5325 C  C8  . A1EAH E .   ? 0.3894 0.3803 0.4085 -0.0223 0.1149  -0.0329 601 A1EAH B C8  
5326 C  C9  . A1EAH E .   ? 0.5164 0.5238 0.5451 -0.0213 0.1231  -0.0397 601 A1EAH B C9  
5327 C  C10 . A1EAH E .   ? 0.5312 0.5294 0.5420 -0.0244 0.1325  -0.0380 601 A1EAH B C10 
5328 C  C12 . A1EAH E .   ? 0.4558 0.4858 0.5094 -0.0037 0.1133  -0.0506 601 A1EAH B C12 
5329 C  C13 . A1EAH E .   ? 0.4349 0.4880 0.5047 -0.0225 0.1305  -0.0534 601 A1EAH B C13 
5330 N  N1  . A1EAH E .   ? 0.4462 0.3877 0.3962 -0.0259 0.1266  -0.0194 601 A1EAH B N1  
5331 N  N2  . A1EAH E .   ? 0.4676 0.4263 0.4232 -0.0323 0.1470  -0.0262 601 A1EAH B N2  
5332 C  C3  . A1EAH E .   ? 0.4815 0.3775 0.3604 -0.0250 0.1379  -0.0069 601 A1EAH B C3  
5333 N  N3  . A1EAH E .   ? 0.5580 0.5348 0.5492 -0.0264 0.1290  -0.0303 601 A1EAH B N3  
5334 C  C1  . A1EAH E .   ? 0.5325 0.4566 0.4377 -0.0335 0.1559  -0.0166 601 A1EAH B C1  
5335 C  C15 . A1EAH E .   ? 0.4784 0.5134 0.5437 0.0037  0.1034  -0.0524 601 A1EAH B C15 
5336 C  C16 . A1EAH E .   ? 0.4293 0.4578 0.4945 0.0242  0.0911  -0.0574 601 A1EAH B C16 
5337 C  C17 . A1EAH E .   ? 0.3896 0.4066 0.4521 0.0422  0.0799  -0.0610 601 A1EAH B C17 
5338 C  C18 . A1EAH E .   ? 0.4165 0.4455 0.4925 0.0381  0.0769  -0.0592 601 A1EAH B C18 
5339 C  C19 . A1EAH E .   ? 0.4692 0.4741 0.5248 0.0529  0.0750  -0.0633 601 A1EAH B C19 
5340 C  C2  . A1EAH E .   ? 0.5020 0.4048 0.3815 -0.0300 0.1513  -0.0100 601 A1EAH B C2  
5341 C  C20 . A1EAH E .   ? 0.4924 0.4965 0.5540 0.0601  0.0669  -0.0630 601 A1EAH B C20 
5342 C  C21 . A1EAH E .   ? 0.4074 0.4246 0.4823 0.0569  0.0634  -0.0610 601 A1EAH B C21 
5343 C  C22 . A1EAH E .   ? 0.2780 0.3082 0.3609 0.0456  0.0683  -0.0595 601 A1EAH B C22 
5344 C  C23 . A1EAH E .   ? 0.6863 0.7816 0.7847 -0.0208 0.1424  -0.0683 601 A1EAH B C23 
5345 C  C24 . A1EAH E .   ? 0.8106 0.9120 0.9153 -0.0345 0.1492  -0.0678 601 A1EAH B C24 
5346 C  C25 . A1EAH E .   ? 0.7642 0.8439 0.8557 -0.0416 0.1462  -0.0592 601 A1EAH B C25 
5347 C  C26 . A1EAH E .   ? 0.5753 0.6315 0.6496 -0.0348 0.1364  -0.0520 601 A1EAH B C26 
5348 C  C27 . A1EAH E .   ? 0.3746 0.3663 0.4041 -0.0203 0.1040  -0.0315 601 A1EAH B C27 
5349 C  C28 . A1EAH E .   ? 0.5669 0.5821 0.5912 0.0000  0.1243  -0.0522 601 A1EAH B C28 
5350 N  N4  . A1EAH E .   ? 0.4634 0.4370 0.4610 -0.0250 0.1182  -0.0276 601 A1EAH B N4  
5351 N  N5  . A1EAH E .   ? 0.5971 0.6197 0.6430 0.0132  0.1072  -0.0559 601 A1EAH B N5  
5352 N  N6  . A1EAH E .   ? 0.4308 0.4603 0.4908 0.0139  0.1000  -0.0553 601 A1EAH B N6  
5353 N  N7  . A1EAH E .   ? 0.5905 0.6087 0.6469 0.0336  0.0885  -0.0600 601 A1EAH B N7  
5354 N  N8  . A1EAH E .   ? 0.3340 0.3703 0.4123 0.0265  0.0839  -0.0574 601 A1EAH B N8  
5355 N  N9  . A1EAH E .   ? 0.7203 0.7913 0.8014 -0.0154 0.1333  -0.0613 601 A1EAH B N9  
5356 O  O1  . A1EAH E .   ? 0.5015 0.5086 0.5117 -0.0251 0.1429  -0.0426 601 A1EAH B O1  
5357 O  O2  . A1EAH E .   ? 0.4646 0.5070 0.5428 0.0019  0.0979  -0.0518 601 A1EAH B O2  
5358 ZN ZN  . ZN    F .   ? 0.3415 0.2487 0.3325 -0.0111 0.0096  0.0074  602 ZN    B ZN  
5359 O  O   . HOH   G .   ? 0.3485 0.5953 0.5205 0.0144  -0.1211 -0.1337 701 HOH   A O   
5360 O  O   . HOH   G .   ? 0.6611 0.7139 0.6050 0.0722  -0.1306 -0.0568 702 HOH   A O   
5361 O  O   . HOH   G .   ? 0.3833 0.6106 0.5294 -0.0289 -0.1238 -0.1646 703 HOH   A O   
5362 O  O   . HOH   G .   ? 0.3752 0.3096 0.3832 0.0021  -0.0264 0.0041  704 HOH   A O   
5363 O  O   . HOH   G .   ? 0.3431 0.3332 0.3207 -0.0290 0.0016  -0.0191 705 HOH   A O   
5364 O  O   . HOH   G .   ? 0.3842 0.3639 0.2225 0.0352  -0.0243 -0.1092 706 HOH   A O   
5365 O  O   . HOH   G .   ? 0.3433 0.4353 0.3461 -0.0238 -0.1295 -0.1631 707 HOH   A O   
5366 O  O   . HOH   G .   ? 0.2656 0.2222 0.2755 -0.0123 -0.0298 -0.0172 708 HOH   A O   
5367 O  O   . HOH   G .   ? 0.3524 0.3050 0.4253 -0.1354 -0.0246 -0.1416 709 HOH   A O   
5368 O  O   . HOH   G .   ? 0.3351 0.3857 0.3955 -0.0367 -0.0815 -0.1030 710 HOH   A O   
5369 O  O   . HOH   G .   ? 0.5792 0.6053 0.3715 -0.0095 0.0482  -0.0674 711 HOH   A O   
5370 O  O   . HOH   G .   ? 0.4792 0.3841 0.4952 -0.0310 -0.0174 -0.0316 712 HOH   A O   
5371 O  O   . HOH   G .   ? 0.5679 0.5524 0.2995 0.1267  -0.1561 -0.0447 713 HOH   A O   
5372 O  O   . HOH   G .   ? 0.4687 0.3706 0.4386 0.0145  -0.0292 0.0123  714 HOH   A O   
5373 O  O   . HOH   G .   ? 0.3682 0.3206 0.4126 -0.0541 -0.0369 -0.0710 715 HOH   A O   
5374 O  O   . HOH   G .   ? 0.2606 0.2123 0.2863 -0.0048 -0.0265 -0.0014 716 HOH   A O   
5375 O  O   . HOH   G .   ? 0.4433 0.4588 0.4449 -0.0368 0.0063  -0.0261 717 HOH   A O   
5376 O  O   . HOH   G .   ? 0.4341 0.3690 0.4180 -0.0311 -0.0548 -0.0942 718 HOH   A O   
5377 O  O   . HOH   G .   ? 0.4348 0.3954 0.4045 0.0041  -0.0283 -0.0442 719 HOH   A O   
5378 O  O   . HOH   G .   ? 0.4613 0.5867 0.4688 0.0087  -0.1428 -0.1397 720 HOH   A O   
5379 O  O   . HOH   G .   ? 0.4189 0.3102 0.3195 0.0033  -0.0263 0.0159  721 HOH   A O   
5380 O  O   . HOH   G .   ? 0.2795 0.2502 0.3463 -0.0124 -0.0020 -0.0084 722 HOH   A O   
5381 O  O   . HOH   G .   ? 0.4409 0.4025 0.4567 -0.0143 -0.0151 -0.0082 723 HOH   A O   
5382 O  O   . HOH   G .   ? 0.5776 0.5075 0.6482 -0.1892 -0.0087 -0.1807 724 HOH   A O   
5383 O  O   . HOH   G .   ? 0.5285 0.4367 0.5299 -0.0070 -0.0122 -0.0090 725 HOH   A O   
5384 O  O   . HOH   G .   ? 0.3037 0.3117 0.3794 -0.0108 -0.0383 -0.0275 726 HOH   A O   
5385 O  O   . HOH   G .   ? 0.4278 0.3728 0.2700 -0.0195 0.0095  -0.0136 727 HOH   A O   
5386 O  O   . HOH   G .   ? 0.5093 0.4598 0.4968 0.0146  -0.0229 -0.0349 728 HOH   A O   
5387 O  O   . HOH   G .   ? 0.4922 0.4966 0.3562 0.0670  -0.1205 -0.0491 729 HOH   A O   
5388 O  O   . HOH   G .   ? 0.5155 0.4774 0.3567 -0.0117 0.0058  -0.0261 730 HOH   A O   
5389 O  O   . HOH   G .   ? 0.3740 0.3173 0.3770 0.0085  -0.0360 0.0015  731 HOH   A O   
5390 O  O   . HOH   G .   ? 0.4346 0.3662 0.4273 0.0127  -0.0203 -0.0202 732 HOH   A O   
5391 O  O   . HOH   G .   ? 0.4202 0.3337 0.3612 0.0025  -0.0305 0.0097  733 HOH   A O   
5392 O  O   . HOH   G .   ? 0.5774 0.5382 0.4876 0.0583  -0.0884 -0.0115 734 HOH   A O   
5393 O  O   . HOH   H .   ? 0.4389 0.3217 0.4463 -0.0310 0.0021  -0.0100 701 HOH   B O   
5394 O  O   . HOH   H .   ? 0.5743 0.5211 0.3494 0.0299  -0.0021 -0.1000 702 HOH   B O   
5395 O  O   . HOH   H .   ? 0.2947 0.7432 0.6690 -0.0187 0.0515  -0.1744 703 HOH   B O   
5396 O  O   . HOH   H .   ? 0.2818 0.2388 0.3175 0.0224  0.0466  -0.0331 704 HOH   B O   
5397 O  O   . HOH   H .   ? 0.5604 0.4786 0.4240 0.0256  0.1198  -0.0614 705 HOH   B O   
5398 O  O   . HOH   H .   ? 0.3919 0.7401 0.6609 0.1732  0.0632  -0.1652 706 HOH   B O   
5399 O  O   . HOH   H .   ? 0.5123 0.4057 0.4619 -0.0394 0.0166  -0.0575 707 HOH   B O   
5400 O  O   . HOH   H .   ? 0.4933 0.3595 0.3447 0.0099  0.0494  -0.0956 708 HOH   B O   
5401 O  O   . HOH   H .   ? 0.3885 0.3802 0.3694 0.0104  -0.0207 -0.0242 709 HOH   B O   
5402 O  O   . HOH   H .   ? 0.7152 0.5993 0.4893 0.0134  0.1480  -0.0343 710 HOH   B O   
5403 O  O   . HOH   H .   ? 0.4757 0.3586 0.4689 -0.0076 0.0056  -0.0043 711 HOH   B O   
5404 O  O   . HOH   H .   ? 0.3238 0.4245 0.4540 0.0345  0.0852  -0.0736 712 HOH   B O   
5405 O  O   . HOH   H .   ? 0.5094 0.3495 0.4820 0.1071  0.0082  -0.0316 713 HOH   B O   
5406 O  O   . HOH   H .   ? 0.3987 0.4107 0.4664 0.1026  -0.0453 -0.0299 714 HOH   B O   
5407 O  O   . HOH   H .   ? 0.3970 0.3406 0.4052 -0.0058 -0.0096 -0.0023 715 HOH   B O   
5408 O  O   . HOH   H .   ? 0.4517 0.3294 0.4445 0.0323  0.0249  -0.0279 716 HOH   B O   
5409 O  O   . HOH   H .   ? 0.4292 0.2844 0.4108 0.1087  0.0224  -0.0462 717 HOH   B O   
5410 O  O   . HOH   H .   ? 0.3747 0.4189 0.4702 0.1256  -0.0329 -0.0478 718 HOH   B O   
5411 O  O   . HOH   H .   ? 0.5482 0.5191 0.5957 0.1897  0.0001  -0.0704 719 HOH   B O   
5412 O  O   . HOH   H .   ? 0.3748 0.3610 0.4424 -0.0165 -0.0272 -0.0189 720 HOH   B O   
5413 O  O   . HOH   H .   ? 0.4877 0.3321 0.2873 -0.0258 0.1563  0.0082  721 HOH   B O   
5414 O  O   . HOH   H .   ? 0.4910 0.4307 0.4843 -0.0502 0.0065  -0.0339 722 HOH   B O   
5415 O  O   . HOH   H .   ? 0.2868 0.2684 0.3646 -0.0154 0.0080  -0.0126 723 HOH   B O   
5416 O  O   . HOH   H .   ? 0.2948 0.2344 0.3342 -0.0234 0.0037  -0.0013 724 HOH   B O   
5417 O  O   . HOH   H .   ? 0.2159 0.1491 0.2258 -0.0155 0.0054  -0.0048 725 HOH   B O   
5418 O  O   . HOH   H .   ? 0.4997 0.3642 0.4587 0.0071  0.0341  -0.0415 726 HOH   B O   
5419 O  O   . HOH   H .   ? 0.3966 0.2605 0.3255 -0.0001 0.0253  0.0179  727 HOH   B O   
5420 O  O   . HOH   H .   ? 0.3997 0.2917 0.4048 0.0228  0.0170  -0.0186 728 HOH   B O   
5421 O  O   . HOH   H .   ? 0.3795 0.2673 0.3440 -0.0086 0.0204  0.0122  729 HOH   B O   
5422 O  O   . HOH   H .   ? 0.4488 0.3285 0.4396 -0.0124 -0.0045 -0.0066 730 HOH   B O   
5423 O  O   . HOH   H .   ? 0.4827 0.3671 0.3247 0.0073  0.0399  -0.0931 731 HOH   B O   
5424 O  O   . HOH   H .   ? 0.3599 0.8800 0.7629 0.0111  0.0414  -0.1985 732 HOH   B O   
5425 O  O   . HOH   H .   ? 0.4924 0.4343 0.5160 0.1019  -0.0353 -0.0164 733 HOH   B O   
5426 O  O   . HOH   H .   ? 0.4436 0.3624 0.4572 0.0734  -0.0259 -0.0080 734 HOH   B O   
5427 O  O   . HOH   H .   ? 0.3723 0.2954 0.4003 -0.0296 0.0171  0.0011  735 HOH   B O   
5428 O  O   . HOH   H .   ? 0.4492 0.3921 0.4484 -0.0494 0.0057  -0.0268 736 HOH   B O   
# 
