data_9LIO
# 
_entry.id   9LIO 
# 
_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   9LIO         pdb_00009lio 10.2210/pdb9lio/pdb 
WWPDB D_1300055742 ?            ?                   
# 
_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                        9LIO 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-14 
_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-[bis[1-[4,6-bis(fluoranyl)-1,3-benzothiazol-2-yl]-3-methyl-5-oxidanyl-pyrazol-4-yl]methyl]benzoic acid' 
666.625   2   ?        ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                                                 
65.409    2   ?        ? ? ? 
4 water       nat water                                                                                                      
18.015    169 ?        ? ? ? 
# 
_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-[bis[1-[4,6-bis(fluoranyl)-1,3-benzothiazol-2-yl]-3-methyl-5-oxidanyl-pyrazol-4-yl]methyl]benzoic acid' A1EKD 
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 
A1EKD non-polymer         . 
'2-[bis[1-[4,6-bis(fluoranyl)-1,3-benzothiazol-2-yl]-3-methyl-5-oxidanyl-pyrazol-4-yl]methyl]benzoic acid' ? 'C30 H18 F4 N6 O4 S2' 
666.625 
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  176 176 ARG ARG A . n 
A 1 21  ASP 21  177 177 ASP ASP A . n 
A 1 22  ASP 22  178 178 ASP ASP 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  210 210 ASN ASN 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  255 255 ARG ARG 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 ?   ?   ?   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 129 285 285 LYS LYS A . n 
A 1 130 GLU 130 286 286 GLU GLU A . n 
A 1 131 GLU 131 287 287 GLU GLU A . n 
A 1 132 ILE 132 288 288 ILE ILE A . n 
A 1 133 ASN 133 289 289 ASN ASN A . n 
A 1 134 ASP 134 290 290 ASP ASP A . n 
A 1 135 ILE 135 291 291 ILE ILE 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 139 295 295 ASP ASP A . n 
A 1 140 VAL 140 296 296 VAL VAL A . n 
A 1 141 ILE 141 297 297 ILE ILE 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 145 301 301 LYS LYS 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 150 306 306 PRO PRO 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 157 313 313 SER SER 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 209 365 365 LYS LYS 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 213 369 369 GLY GLY A . n 
A 1 214 PHE 214 370 370 PHE PHE 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  175 175 SER SER B . n 
B 1 20  ARG 20  176 176 ARG ARG B . n 
B 1 21  ASP 21  177 177 ASP ASP 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 ?   ?   ?   B . n 
B 1 55  THR 55  211 ?   ?   ?   B . n 
B 1 56  GLY 56  212 ?   ?   ?   B . n 
B 1 57  SER 57  213 ?   ?   ?   B . n 
B 1 58  TYR 58  214 ?   ?   ?   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 135 291 291 ILE ILE 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 139 295 295 ASP ASP 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 145 301 301 LYS LYS 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 ?   ?   ?   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 159 315 315 LYS LYS 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 214 370 370 PHE PHE 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        A1EKD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EKD 
_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 A1EKD 1  601 601 A1EKD LIG A . 
D 3 ZN    1  602 2   ZN    ZN  A . 
E 2 A1EKD 1  601 601 A1EKD LIG B . 
F 3 ZN    1  602 1   ZN    ZN  B . 
G 4 HOH   1  701 166 HOH   HOH A . 
G 4 HOH   2  702 137 HOH   HOH A . 
G 4 HOH   3  703 11  HOH   HOH A . 
G 4 HOH   4  704 85  HOH   HOH A . 
G 4 HOH   5  705 129 HOH   HOH A . 
G 4 HOH   6  706 78  HOH   HOH A . 
G 4 HOH   7  707 95  HOH   HOH A . 
G 4 HOH   8  708 164 HOH   HOH A . 
G 4 HOH   9  709 122 HOH   HOH A . 
G 4 HOH   10 710 23  HOH   HOH A . 
G 4 HOH   11 711 110 HOH   HOH A . 
G 4 HOH   12 712 100 HOH   HOH A . 
G 4 HOH   13 713 87  HOH   HOH A . 
G 4 HOH   14 714 111 HOH   HOH A . 
G 4 HOH   15 715 83  HOH   HOH A . 
G 4 HOH   16 716 61  HOH   HOH A . 
G 4 HOH   17 717 21  HOH   HOH A . 
G 4 HOH   18 718 13  HOH   HOH A . 
G 4 HOH   19 719 67  HOH   HOH A . 
G 4 HOH   20 720 42  HOH   HOH A . 
G 4 HOH   21 721 43  HOH   HOH A . 
G 4 HOH   22 722 49  HOH   HOH A . 
G 4 HOH   23 723 155 HOH   HOH A . 
G 4 HOH   24 724 3   HOH   HOH A . 
G 4 HOH   25 725 27  HOH   HOH A . 
G 4 HOH   26 726 45  HOH   HOH A . 
G 4 HOH   27 727 70  HOH   HOH A . 
G 4 HOH   28 728 59  HOH   HOH A . 
G 4 HOH   29 729 101 HOH   HOH A . 
G 4 HOH   30 730 16  HOH   HOH A . 
G 4 HOH   31 731 29  HOH   HOH A . 
G 4 HOH   32 732 93  HOH   HOH A . 
G 4 HOH   33 733 14  HOH   HOH A . 
G 4 HOH   34 734 98  HOH   HOH A . 
G 4 HOH   35 735 163 HOH   HOH A . 
G 4 HOH   36 736 22  HOH   HOH A . 
G 4 HOH   37 737 50  HOH   HOH A . 
G 4 HOH   38 738 84  HOH   HOH A . 
G 4 HOH   39 739 44  HOH   HOH A . 
G 4 HOH   40 740 91  HOH   HOH A . 
G 4 HOH   41 741 134 HOH   HOH A . 
G 4 HOH   42 742 82  HOH   HOH A . 
G 4 HOH   43 743 99  HOH   HOH A . 
G 4 HOH   44 744 159 HOH   HOH A . 
G 4 HOH   45 745 139 HOH   HOH A . 
G 4 HOH   46 746 7   HOH   HOH A . 
G 4 HOH   47 747 149 HOH   HOH A . 
G 4 HOH   48 748 105 HOH   HOH A . 
G 4 HOH   49 749 51  HOH   HOH A . 
G 4 HOH   50 750 75  HOH   HOH A . 
G 4 HOH   51 751 1   HOH   HOH A . 
G 4 HOH   52 752 33  HOH   HOH A . 
G 4 HOH   53 753 113 HOH   HOH A . 
G 4 HOH   54 754 77  HOH   HOH A . 
G 4 HOH   55 755 52  HOH   HOH A . 
G 4 HOH   56 756 108 HOH   HOH A . 
G 4 HOH   57 757 151 HOH   HOH A . 
G 4 HOH   58 758 31  HOH   HOH A . 
G 4 HOH   59 759 136 HOH   HOH A . 
G 4 HOH   60 760 64  HOH   HOH A . 
G 4 HOH   61 761 2   HOH   HOH A . 
G 4 HOH   62 762 69  HOH   HOH A . 
G 4 HOH   63 763 62  HOH   HOH A . 
G 4 HOH   64 764 55  HOH   HOH A . 
G 4 HOH   65 765 117 HOH   HOH A . 
G 4 HOH   66 766 143 HOH   HOH A . 
G 4 HOH   67 767 15  HOH   HOH A . 
G 4 HOH   68 768 71  HOH   HOH A . 
G 4 HOH   69 769 76  HOH   HOH A . 
G 4 HOH   70 770 20  HOH   HOH A . 
G 4 HOH   71 771 73  HOH   HOH A . 
G 4 HOH   72 772 161 HOH   HOH A . 
G 4 HOH   73 773 102 HOH   HOH A . 
G 4 HOH   74 774 34  HOH   HOH A . 
G 4 HOH   75 775 135 HOH   HOH A . 
G 4 HOH   76 776 25  HOH   HOH A . 
G 4 HOH   77 777 88  HOH   HOH A . 
G 4 HOH   78 778 132 HOH   HOH A . 
G 4 HOH   79 779 165 HOH   HOH A . 
G 4 HOH   80 780 37  HOH   HOH A . 
G 4 HOH   81 781 119 HOH   HOH A . 
G 4 HOH   82 782 144 HOH   HOH A . 
G 4 HOH   83 783 90  HOH   HOH A . 
G 4 HOH   84 784 138 HOH   HOH A . 
G 4 HOH   85 785 140 HOH   HOH A . 
G 4 HOH   86 786 63  HOH   HOH A . 
G 4 HOH   87 787 120 HOH   HOH A . 
G 4 HOH   88 788 79  HOH   HOH A . 
G 4 HOH   89 789 141 HOH   HOH A . 
H 4 HOH   1  701 158 HOH   HOH B . 
H 4 HOH   2  702 89  HOH   HOH B . 
H 4 HOH   3  703 168 HOH   HOH B . 
H 4 HOH   4  704 124 HOH   HOH B . 
H 4 HOH   5  705 80  HOH   HOH B . 
H 4 HOH   6  706 57  HOH   HOH B . 
H 4 HOH   7  707 103 HOH   HOH B . 
H 4 HOH   8  708 32  HOH   HOH B . 
H 4 HOH   9  709 38  HOH   HOH B . 
H 4 HOH   10 710 92  HOH   HOH B . 
H 4 HOH   11 711 142 HOH   HOH B . 
H 4 HOH   12 712 157 HOH   HOH B . 
H 4 HOH   13 713 94  HOH   HOH B . 
H 4 HOH   14 714 26  HOH   HOH B . 
H 4 HOH   15 715 19  HOH   HOH B . 
H 4 HOH   16 716 6   HOH   HOH B . 
H 4 HOH   17 717 130 HOH   HOH B . 
H 4 HOH   18 718 145 HOH   HOH B . 
H 4 HOH   19 719 66  HOH   HOH B . 
H 4 HOH   20 720 54  HOH   HOH B . 
H 4 HOH   21 721 147 HOH   HOH B . 
H 4 HOH   22 722 152 HOH   HOH B . 
H 4 HOH   23 723 118 HOH   HOH B . 
H 4 HOH   24 724 28  HOH   HOH B . 
H 4 HOH   25 725 97  HOH   HOH B . 
H 4 HOH   26 726 17  HOH   HOH B . 
H 4 HOH   27 727 56  HOH   HOH B . 
H 4 HOH   28 728 115 HOH   HOH B . 
H 4 HOH   29 729 5   HOH   HOH B . 
H 4 HOH   30 730 104 HOH   HOH B . 
H 4 HOH   31 731 35  HOH   HOH B . 
H 4 HOH   32 732 167 HOH   HOH B . 
H 4 HOH   33 733 148 HOH   HOH B . 
H 4 HOH   34 734 146 HOH   HOH B . 
H 4 HOH   35 735 123 HOH   HOH B . 
H 4 HOH   36 736 121 HOH   HOH B . 
H 4 HOH   37 737 65  HOH   HOH B . 
H 4 HOH   38 738 8   HOH   HOH B . 
H 4 HOH   39 739 9   HOH   HOH B . 
H 4 HOH   40 740 126 HOH   HOH B . 
H 4 HOH   41 741 107 HOH   HOH B . 
H 4 HOH   42 742 41  HOH   HOH B . 
H 4 HOH   43 743 150 HOH   HOH B . 
H 4 HOH   44 744 18  HOH   HOH B . 
H 4 HOH   45 745 30  HOH   HOH B . 
H 4 HOH   46 746 4   HOH   HOH B . 
H 4 HOH   47 747 112 HOH   HOH B . 
H 4 HOH   48 748 12  HOH   HOH B . 
H 4 HOH   49 749 24  HOH   HOH B . 
H 4 HOH   50 750 96  HOH   HOH B . 
H 4 HOH   51 751 109 HOH   HOH B . 
H 4 HOH   52 752 72  HOH   HOH B . 
H 4 HOH   53 753 154 HOH   HOH B . 
H 4 HOH   54 754 153 HOH   HOH B . 
H 4 HOH   55 755 60  HOH   HOH B . 
H 4 HOH   56 756 10  HOH   HOH B . 
H 4 HOH   57 757 36  HOH   HOH B . 
H 4 HOH   58 758 125 HOH   HOH B . 
H 4 HOH   59 759 131 HOH   HOH B . 
H 4 HOH   60 760 46  HOH   HOH B . 
H 4 HOH   61 761 128 HOH   HOH B . 
H 4 HOH   62 762 58  HOH   HOH B . 
H 4 HOH   63 763 68  HOH   HOH B . 
H 4 HOH   64 764 86  HOH   HOH B . 
H 4 HOH   65 765 133 HOH   HOH B . 
H 4 HOH   66 766 40  HOH   HOH B . 
H 4 HOH   67 767 162 HOH   HOH B . 
H 4 HOH   68 768 39  HOH   HOH B . 
H 4 HOH   69 769 114 HOH   HOH B . 
H 4 HOH   70 770 156 HOH   HOH B . 
H 4 HOH   71 771 48  HOH   HOH B . 
H 4 HOH   72 772 81  HOH   HOH B . 
H 4 HOH   73 773 116 HOH   HOH B . 
H 4 HOH   74 774 53  HOH   HOH B . 
H 4 HOH   75 775 169 HOH   HOH B . 
H 4 HOH   76 776 74  HOH   HOH B . 
H 4 HOH   77 777 106 HOH   HOH B . 
H 4 HOH   78 778 127 HOH   HOH B . 
H 4 HOH   79 779 47  HOH   HOH B . 
H 4 HOH   80 780 160 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 LYS 173 ? CG  ? A LYS 17  CG  
2   1 Y 1 A LYS 173 ? CD  ? A LYS 17  CD  
3   1 Y 1 A LYS 173 ? CE  ? A LYS 17  CE  
4   1 Y 1 A LYS 173 ? NZ  ? A LYS 17  NZ  
5   1 Y 1 A ARG 176 ? CG  ? A ARG 20  CG  
6   1 Y 1 A ARG 176 ? CD  ? A ARG 20  CD  
7   1 Y 1 A ARG 176 ? NE  ? A ARG 20  NE  
8   1 Y 1 A ARG 176 ? CZ  ? A ARG 20  CZ  
9   1 Y 1 A ARG 176 ? NH1 ? A ARG 20  NH1 
10  1 Y 1 A ARG 176 ? NH2 ? A ARG 20  NH2 
11  1 Y 1 A ASP 178 ? CG  ? A ASP 22  CG  
12  1 Y 1 A ASP 178 ? OD1 ? A ASP 22  OD1 
13  1 Y 1 A ASP 178 ? OD2 ? A ASP 22  OD2 
14  1 Y 1 A ILE 179 ? CG1 ? A ILE 23  CG1 
15  1 Y 1 A ILE 179 ? CG2 ? A ILE 23  CG2 
16  1 Y 1 A ILE 179 ? CD1 ? A ILE 23  CD1 
17  1 Y 1 A SER 180 ? OG  ? A SER 24  OG  
18  1 Y 1 A ARG 196 ? CG  ? A ARG 40  CG  
19  1 Y 1 A ARG 196 ? CD  ? A ARG 40  CD  
20  1 Y 1 A ARG 196 ? NE  ? A ARG 40  NE  
21  1 Y 1 A ARG 196 ? CZ  ? A ARG 40  CZ  
22  1 Y 1 A ARG 196 ? NH1 ? A ARG 40  NH1 
23  1 Y 1 A ARG 196 ? NH2 ? A ARG 40  NH2 
24  1 Y 1 A ARG 204 ? CG  ? A ARG 48  CG  
25  1 Y 1 A ARG 204 ? CD  ? A ARG 48  CD  
26  1 Y 1 A ARG 204 ? NE  ? A ARG 48  NE  
27  1 Y 1 A ARG 204 ? CZ  ? A ARG 48  CZ  
28  1 Y 1 A ARG 204 ? NH1 ? A ARG 48  NH1 
29  1 Y 1 A ARG 204 ? NH2 ? A ARG 48  NH2 
30  1 Y 1 A ARG 236 ? CG  ? A ARG 80  CG  
31  1 Y 1 A ARG 236 ? CD  ? A ARG 80  CD  
32  1 Y 1 A ARG 236 ? NE  ? A ARG 80  NE  
33  1 Y 1 A ARG 236 ? CZ  ? A ARG 80  CZ  
34  1 Y 1 A ARG 236 ? NH1 ? A ARG 80  NH1 
35  1 Y 1 A ARG 236 ? NH2 ? A ARG 80  NH2 
36  1 Y 1 A LYS 254 ? CG  ? A LYS 98  CG  
37  1 Y 1 A LYS 254 ? CD  ? A LYS 98  CD  
38  1 Y 1 A LYS 254 ? CE  ? A LYS 98  CE  
39  1 Y 1 A LYS 254 ? NZ  ? A LYS 98  NZ  
40  1 Y 1 A ARG 255 ? CG  ? A ARG 99  CG  
41  1 Y 1 A ARG 255 ? CD  ? A ARG 99  CD  
42  1 Y 1 A ARG 255 ? NE  ? A ARG 99  NE  
43  1 Y 1 A ARG 255 ? CZ  ? A ARG 99  CZ  
44  1 Y 1 A ARG 255 ? NH1 ? A ARG 99  NH1 
45  1 Y 1 A ARG 255 ? NH2 ? A ARG 99  NH2 
46  1 Y 1 A GLU 287 ? CG  ? A GLU 131 CG  
47  1 Y 1 A GLU 287 ? CD  ? A GLU 131 CD  
48  1 Y 1 A GLU 287 ? OE1 ? A GLU 131 OE1 
49  1 Y 1 A GLU 287 ? OE2 ? A GLU 131 OE2 
50  1 Y 1 A ASP 295 ? CG  ? A ASP 139 CG  
51  1 Y 1 A ASP 295 ? OD1 ? A ASP 139 OD1 
52  1 Y 1 A ASP 295 ? OD2 ? A ASP 139 OD2 
53  1 Y 1 A VAL 296 ? CG1 ? A VAL 140 CG1 
54  1 Y 1 A VAL 296 ? CG2 ? A VAL 140 CG2 
55  1 Y 1 A ILE 297 ? CG1 ? A ILE 141 CG1 
56  1 Y 1 A ILE 297 ? CG2 ? A ILE 141 CG2 
57  1 Y 1 A ILE 297 ? CD1 ? A ILE 141 CD1 
58  1 Y 1 A LYS 299 ? CG  ? A LYS 143 CG  
59  1 Y 1 A LYS 299 ? CD  ? A LYS 143 CD  
60  1 Y 1 A LYS 299 ? CE  ? A LYS 143 CE  
61  1 Y 1 A LYS 299 ? NZ  ? A LYS 143 NZ  
62  1 Y 1 A ARG 300 ? CG  ? A ARG 144 CG  
63  1 Y 1 A ARG 300 ? CD  ? A ARG 144 CD  
64  1 Y 1 A ARG 300 ? NE  ? A ARG 144 NE  
65  1 Y 1 A ARG 300 ? CZ  ? A ARG 144 CZ  
66  1 Y 1 A ARG 300 ? NH1 ? A ARG 144 NH1 
67  1 Y 1 A ARG 300 ? NH2 ? A ARG 144 NH2 
68  1 Y 1 A LYS 315 ? CG  ? A LYS 159 CG  
69  1 Y 1 A LYS 315 ? CD  ? A LYS 159 CD  
70  1 Y 1 A LYS 315 ? CE  ? A LYS 159 CE  
71  1 Y 1 A LYS 315 ? NZ  ? A LYS 159 NZ  
72  1 Y 1 A LYS 365 ? CG  ? A LYS 209 CG  
73  1 Y 1 A LYS 365 ? CD  ? A LYS 209 CD  
74  1 Y 1 A LYS 365 ? CE  ? A LYS 209 CE  
75  1 Y 1 A LYS 365 ? NZ  ? A LYS 209 NZ  
76  1 Y 1 A PHE 370 ? CG  ? A PHE 214 CG  
77  1 Y 1 A PHE 370 ? CD1 ? A PHE 214 CD1 
78  1 Y 1 A PHE 370 ? CD2 ? A PHE 214 CD2 
79  1 Y 1 A PHE 370 ? CE1 ? A PHE 214 CE1 
80  1 Y 1 A PHE 370 ? CE2 ? A PHE 214 CE2 
81  1 Y 1 A PHE 370 ? CZ  ? A PHE 214 CZ  
82  1 Y 1 B ARG 166 ? CG  ? B ARG 10  CG  
83  1 Y 1 B ARG 166 ? CD  ? B ARG 10  CD  
84  1 Y 1 B ARG 166 ? NE  ? B ARG 10  NE  
85  1 Y 1 B ARG 166 ? CZ  ? B ARG 10  CZ  
86  1 Y 1 B ARG 166 ? NH1 ? B ARG 10  NH1 
87  1 Y 1 B ARG 166 ? NH2 ? B ARG 10  NH2 
88  1 Y 1 B LYS 171 ? CG  ? B LYS 15  CG  
89  1 Y 1 B LYS 171 ? CD  ? B LYS 15  CD  
90  1 Y 1 B LYS 171 ? CE  ? B LYS 15  CE  
91  1 Y 1 B LYS 171 ? NZ  ? B LYS 15  NZ  
92  1 Y 1 B LYS 173 ? CG  ? B LYS 17  CG  
93  1 Y 1 B LYS 173 ? CD  ? B LYS 17  CD  
94  1 Y 1 B LYS 173 ? CE  ? B LYS 17  CE  
95  1 Y 1 B LYS 173 ? NZ  ? B LYS 17  NZ  
96  1 Y 1 B ARG 176 ? CG  ? B ARG 20  CG  
97  1 Y 1 B ARG 176 ? CD  ? B ARG 20  CD  
98  1 Y 1 B ARG 176 ? NE  ? B ARG 20  NE  
99  1 Y 1 B ARG 176 ? CZ  ? B ARG 20  CZ  
100 1 Y 1 B ARG 176 ? NH1 ? B ARG 20  NH1 
101 1 Y 1 B ARG 176 ? NH2 ? B ARG 20  NH2 
102 1 Y 1 B ASP 178 ? CG  ? B ASP 22  CG  
103 1 Y 1 B ASP 178 ? OD1 ? B ASP 22  OD1 
104 1 Y 1 B ASP 178 ? OD2 ? B ASP 22  OD2 
105 1 Y 1 B ILE 291 ? CG1 ? B ILE 135 CG1 
106 1 Y 1 B ILE 291 ? CG2 ? B ILE 135 CG2 
107 1 Y 1 B ILE 291 ? CD1 ? B ILE 135 CD1 
108 1 Y 1 B ARG 300 ? CG  ? B ARG 144 CG  
109 1 Y 1 B ARG 300 ? CD  ? B ARG 144 CD  
110 1 Y 1 B ARG 300 ? NE  ? B ARG 144 NE  
111 1 Y 1 B ARG 300 ? CZ  ? B ARG 144 CZ  
112 1 Y 1 B ARG 300 ? NH1 ? B ARG 144 NH1 
113 1 Y 1 B ARG 300 ? NH2 ? B ARG 144 NH2 
114 1 Y 1 B LYS 301 ? CG  ? B LYS 145 CG  
115 1 Y 1 B LYS 301 ? CD  ? B LYS 145 CD  
116 1 Y 1 B LYS 301 ? CE  ? B LYS 145 CE  
117 1 Y 1 B LYS 301 ? NZ  ? B LYS 145 NZ  
118 1 Y 1 B LYS 365 ? CG  ? B LYS 209 CG  
119 1 Y 1 B LYS 365 ? CD  ? B LYS 209 CD  
120 1 Y 1 B LYS 365 ? CE  ? B LYS 209 CE  
121 1 Y 1 B LYS 365 ? NZ  ? B LYS 209 NZ  
122 1 Y 1 B PHE 370 ? CG  ? B PHE 214 CG  
123 1 Y 1 B PHE 370 ? CD1 ? B PHE 214 CD1 
124 1 Y 1 B PHE 370 ? CD2 ? B PHE 214 CD2 
125 1 Y 1 B PHE 370 ? CE1 ? B PHE 214 CE1 
126 1 Y 1 B PHE 370 ? CE2 ? B PHE 214 CE2 
127 1 Y 1 B PHE 370 ? CZ  ? B PHE 214 CZ  
128 1 Y 1 B GLU 401 ? CG  ? B GLU 245 CG  
129 1 Y 1 B GLU 401 ? CD  ? B GLU 245 CD  
130 1 Y 1 B GLU 401 ? OE1 ? B GLU 245 OE1 
131 1 Y 1 B GLU 401 ? OE2 ? B GLU 245 OE2 
# 
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'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   112.68 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9LIO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     210.478 
_cell.length_a_esd                 ? 
_cell.length_b                     45.949 
_cell.length_b_esd                 ? 
_cell.length_c                     86.381 
_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                         9LIO 
_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                   9LIO 
_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             2.25 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.41 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-12-23 
_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   0.97918 
_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 BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9LIO 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.92 
_reflns.d_resolution_low                               97.10 
_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                                     58969 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.81 
_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                                0.123 
_reflns.pdbx_Rpim_I_all                                0.048 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       389171 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.114 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.92 
_reflns_shell.d_res_low                                     2.02 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           49744 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             8508 
_reflns_shell.percent_possible_obs                          100.0 
_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                               5.8 
_reflns_shell.pdbx_chi_squared                              0.95 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.9 
_reflns_shell.pdbx_Rrim_I_all                               2.020 
_reflns_shell.pdbx_Rpim_I_all                               0.833 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.429 
_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                                  1.835 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9LIO 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.92 
_refine.ls_d_res_low                             78.12 
_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                     58742 
_refine.ls_number_reflns_R_free                  2932 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.62 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2261 
_refine.ls_R_factor_R_free                       0.2682 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2238 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 31.58 
_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                            0.32 
_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.details                          ? 
_refine_hist.d_res_high                       1.92 
_refine_hist.d_res_low                        78.12 
_refine_hist.number_atoms_solvent             169 
_refine_hist.number_atoms_total               5771 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5508 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         94 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009 ? 5712 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.127 ? 7684 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.797 ? 735  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.058 ? 838  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011 ? 960  ? 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' 1.92 1.95  . . 109 2524 96.00  . . . . 0.4137 . . . . . . . . . . . 0.4123 
'X-RAY DIFFRACTION' 1.95 1.98  . . 160 2562 98.00  . . . . 0.3754 . . . . . . . . . . . 0.4585 
'X-RAY DIFFRACTION' 1.98 2.02  . . 137 2649 100.00 . . . . 0.3411 . . . . . . . . . . . 0.3548 
'X-RAY DIFFRACTION' 2.02 2.06  . . 143 2639 100.00 . . . . 0.3206 . . . . . . . . . . . 0.3535 
'X-RAY DIFFRACTION' 2.06 2.10  . . 129 2675 100.00 . . . . 0.2915 . . . . . . . . . . . 0.3499 
'X-RAY DIFFRACTION' 2.10 2.15  . . 137 2618 100.00 . . . . 0.2839 . . . . . . . . . . . 0.3379 
'X-RAY DIFFRACTION' 2.15 2.20  . . 134 2698 100.00 . . . . 0.2657 . . . . . . . . . . . 0.3394 
'X-RAY DIFFRACTION' 2.20 2.25  . . 116 2643 100.00 . . . . 0.2423 . . . . . . . . . . . 0.3180 
'X-RAY DIFFRACTION' 2.25 2.31  . . 143 2650 100.00 . . . . 0.2425 . . . . . . . . . . . 0.3085 
'X-RAY DIFFRACTION' 2.31 2.38  . . 129 2646 100.00 . . . . 0.2355 . . . . . . . . . . . 0.2477 
'X-RAY DIFFRACTION' 2.38 2.46  . . 137 2660 100.00 . . . . 0.2385 . . . . . . . . . . . 0.3034 
'X-RAY DIFFRACTION' 2.46 2.54  . . 165 2643 100.00 . . . . 0.2279 . . . . . . . . . . . 0.3030 
'X-RAY DIFFRACTION' 2.54 2.65  . . 132 2658 100.00 . . . . 0.2328 . . . . . . . . . . . 0.3351 
'X-RAY DIFFRACTION' 2.65 2.77  . . 134 2680 100.00 . . . . 0.2256 . . . . . . . . . . . 0.2756 
'X-RAY DIFFRACTION' 2.77 2.91  . . 156 2655 100.00 . . . . 0.2314 . . . . . . . . . . . 0.2714 
'X-RAY DIFFRACTION' 2.91 3.09  . . 138 2657 100.00 . . . . 0.2376 . . . . . . . . . . . 0.2861 
'X-RAY DIFFRACTION' 3.09 3.33  . . 149 2681 100.00 . . . . 0.2257 . . . . . . . . . . . 0.2838 
'X-RAY DIFFRACTION' 3.33 3.67  . . 132 2680 100.00 . . . . 0.2065 . . . . . . . . . . . 0.2599 
'X-RAY DIFFRACTION' 3.67 4.20  . . 155 2701 100.00 . . . . 0.1925 . . . . . . . . . . . 0.2616 
'X-RAY DIFFRACTION' 4.20 5.29  . . 152 2700 100.00 . . . . 0.1813 . . . . . . . . . . . 0.2205 
'X-RAY DIFFRACTION' 5.29 78.12 . . 145 2791 99.00  . . . . 0.2035 . . . . . . . . . . . 0.2003 
# 
_struct.entry_id                     9LIO 
_struct.title                        'Human cGAS catalytic domain bound with XL-3123' 
_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        9LIO 
_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 9LIO A 1 ? 366 ? Q8N884 157 ? 522 ? 157 522 
2 1 9LIO B 1 ? 366 ? Q8N884 157 ? 522 ? 157 522 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,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   ? ASP A 22  ? GLY A 161 ASP A 178 1 ? 18 
HELX_P HELX_P2  AA2 ILE A 23  ? LYS A 42  ? ILE A 179 LYS A 198 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 135 ? SER A 272 ILE A 291 1 ? 20 
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 ? LYS A 199 ? SER A 345 LYS A 355 1 ? 11 
HELX_P HELX_P7  AA7 PHE A 223 ? ASN A 233 ? PHE A 379 ASN A 389 1 ? 11 
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   ? ASP B 22  ? ALA B 162 ASP B 178 1 ? 17 
HELX_P HELX_P16 AB7 ALA B 26  ? LYS B 42  ? ALA B 182 LYS B 198 1 ? 17 
HELX_P HELX_P17 AB8 CYS B 43  ? ARG B 48  ? CYS B 199 ARG B 204 5 ? 6  
HELX_P HELX_P18 AB9 LEU B 106 ? GLN B 108 ? LEU B 262 GLN B 264 5 ? 3  
HELX_P HELX_P19 AC1 SER B 116 ? ASN B 133 ? SER B 272 ASN B 289 1 ? 18 
HELX_P HELX_P20 AC2 PRO B 175 ? GLN B 179 ? PRO B 331 GLN B 335 5 ? 5  
HELX_P HELX_P21 AC3 SER B 189 ? LEU B 198 ? SER B 345 LEU B 354 1 ? 10 
HELX_P HELX_P22 AC4 PHE B 223 ? ASN B 233 ? PHE B 379 ASN B 389 1 ? 11 
HELX_P HELX_P23 AC5 ASN B 243 ? LYS B 247 ? ASN B 399 LYS B 403 5 ? 5  
HELX_P HELX_P24 AC6 CYS B 249 ? PHE B 268 ? CYS B 405 PHE B 424 1 ? 20 
HELX_P HELX_P25 AC7 SER B 278 ? ASN B 293 ? SER B 434 ASN B 449 1 ? 16 
HELX_P HELX_P26 AC8 GLN B 295 ? LYS B 302 ? GLN B 451 LYS B 458 5 ? 8  
HELX_P HELX_P27 AC9 ASP B 303 ? GLU B 322 ? ASP B 459 GLU B 478 1 ? 20 
HELX_P HELX_P28 AD1 ASP B 341 ? ASN B 358 ? ASP B 497 ASN B 514 1 ? 18 
HELX_P HELX_P29 AD2 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 ? ? ? ? ? ? ? 2.130 ? ? 
metalc2 metalc ? ? A CYS 240 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 396 A ZN 602 1_555 ? ? ? ? ? ? ? 2.281 ? ? 
metalc3 metalc ? ? A CYS 241 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 397 A ZN 602 1_555 ? ? ? ? ? ? ? 2.290 ? ? 
metalc4 metalc ? ? A CYS 248 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 404 A ZN 602 1_555 ? ? ? ? ? ? ? 2.350 ? ? 
metalc5 metalc ? ? B HIS 234 NE2 ? ? ? 1_555 F ZN . ZN ? ? B HIS 390 B ZN 602 1_555 ? ? ? ? ? ? ? 2.117 ? ? 
metalc6 metalc ? ? B CYS 240 SG  ? ? ? 1_555 F ZN . ZN ? ? B CYS 396 B ZN 602 1_555 ? ? ? ? ? ? ? 2.328 ? ? 
metalc7 metalc ? ? B CYS 241 SG  ? ? ? 1_555 F ZN . ZN ? ? B CYS 397 B ZN 602 1_555 ? ? ? ? ? ? ? 2.255 ? ? 
metalc8 metalc ? ? B CYS 248 SG  ? ? ? 1_555 F ZN . ZN ? ? B CYS 404 B ZN 602 1_555 ? ? ? ? ? ? ? 2.287 ? ? 
# 
_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_555 108.6 ? 
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_555 108.8 ? 
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_555 128.3 ? 
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 95.8  ? 
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_555 106.3 ? 
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_555 104.0 ? 
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_555 108.0 ? 
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_555 110.4 ? 
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_555 128.3 ? 
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 93.4  ? 
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_555 104.3 ? 
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_555 106.5 ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          SER 
_struct_mon_prot_cis.label_seq_id           149 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           SER 
_struct_mon_prot_cis.auth_seq_id            305 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    150 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     306 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       2.31 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
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 
AA2 4 5 ? 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 VAL A 50  ? LEU A 52  ? VAL A 206 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 VAL A 50  ? LEU A 52  ? VAL A 206 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 
AA2 5 ILE A 141 ? ARG A 144 ? ILE A 297 ARG A 300 
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 VAL B 50  ? LEU B 53  ? VAL B 206 LEU B 209 
AA4 2 GLU B 69  ? GLU B 77  ? GLU B 225 GLU B 233 
AA4 3 ILE B 160 ? SER B 170 ? ILE B 316 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 GLU B 60  ? GLU B 60  ? GLU B 216 GLU B 216 
AA5 2 GLU B 69  ? GLU B 77  ? GLU B 225 GLU B 233 
AA5 3 ILE B 160 ? SER B 170 ? ILE B 316 SER B 326 
AA5 4 VAL B 152 ? ILE B 156 ? VAL B 308 ILE B 312 
AA5 5 VAL B 140 ? ARG B 144 ? VAL B 296 ARG B 300 
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 74  ? N PHE A 230 O THR A 165 ? O THR A 321 
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 74  ? N PHE A 230 O THR A 165 ? O THR A 321 
AA2 3 4 O ILE A 160 ? O ILE A 316 N ILE A 156 ? N ILE A 312 
AA2 4 5 O LEU A 155 ? O LEU A 311 N ILE A 141 ? N ILE A 297 
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 LYS B 96  ? O LYS B 252 N GLN B 82  ? N GLN B 238 
AA5 1 2 N GLU B 60  ? N GLU B 216 O ASP B 71  ? O ASP B 227 
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                   9LIO 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O4 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   A1EKD 
_pdbx_validate_close_contact.auth_seq_id_1    601 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    701 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 246 ? ? 69.64   -23.46  
2 1 SER A 313 ? ? 58.33   -152.45 
3 1 TRP A 343 ? ? -110.50 -71.07  
4 1 SER A 345 ? ? 110.32  156.42  
5 1 LYS A 362 ? ? -163.91 112.98  
6 1 ARG B 246 ? ? 70.21   -27.67  
7 1 SER B 313 ? ? 57.83   -125.42 
8 1 SER B 345 ? ? 109.71  155.99  
# 
_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         -36.0571 
_pdbx_refine_tls.origin_y         6.5425 
_pdbx_refine_tls.origin_z         16.4843 
_pdbx_refine_tls.T[1][1]          0.3118 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0008 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0645 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.1919 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0041 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.2651 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.2628 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.3938 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.4982 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.6238 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.3480 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.0927 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0350 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.2430 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0429 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.1813 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0866 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.1704 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0248 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.1771 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0545 
_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 THR 211 ? A THR 55  
6  1 Y 1 A GLY 212 ? A GLY 56  
7  1 Y 1 A SER 213 ? A SER 57  
8  1 Y 1 A TYR 214 ? A TYR 58  
9  1 Y 1 A ASN 256 ? A ASN 100 
10 1 Y 1 A PRO 257 ? A PRO 101 
11 1 Y 1 A LYS 258 ? A LYS 102 
12 1 Y 1 A GLU 259 ? A GLU 103 
13 1 Y 1 A LYS 292 ? A LYS 136 
14 1 Y 1 A ASP 293 ? A ASP 137 
15 1 Y 1 A THR 294 ? A THR 138 
16 1 Y 1 A ARG 302 ? A ARG 146 
17 1 Y 1 A GLY 303 ? A GLY 147 
18 1 Y 1 A GLU 366 ? A GLU 210 
19 1 Y 1 A GLY 367 ? A GLY 211 
20 1 Y 1 A ASN 368 ? A ASN 212 
21 1 Y 1 A GLU 521 ? A GLU 365 
22 1 Y 1 A PHE 522 ? A PHE 366 
23 1 Y 1 B ASP 157 ? B ASP 1   
24 1 Y 1 B ALA 158 ? B ALA 2   
25 1 Y 1 B ALA 159 ? B ALA 3   
26 1 Y 1 B PRO 160 ? B PRO 4   
27 1 Y 1 B SER 180 ? B SER 24  
28 1 Y 1 B ASN 210 ? B ASN 54  
29 1 Y 1 B THR 211 ? B THR 55  
30 1 Y 1 B GLY 212 ? B GLY 56  
31 1 Y 1 B SER 213 ? B SER 57  
32 1 Y 1 B TYR 214 ? B TYR 58  
33 1 Y 1 B ARG 255 ? B ARG 99  
34 1 Y 1 B ASN 256 ? B ASN 100 
35 1 Y 1 B PRO 257 ? B PRO 101 
36 1 Y 1 B LYS 258 ? B LYS 102 
37 1 Y 1 B GLU 259 ? B GLU 103 
38 1 Y 1 B LYS 292 ? B LYS 136 
39 1 Y 1 B ASP 293 ? B ASP 137 
40 1 Y 1 B THR 294 ? B THR 138 
41 1 Y 1 B ARG 302 ? B ARG 146 
42 1 Y 1 B GLY 303 ? B GLY 147 
43 1 Y 1 B SER 305 ? B SER 149 
44 1 Y 1 B GLU 366 ? B GLU 210 
45 1 Y 1 B GLY 367 ? B GLY 211 
46 1 Y 1 B ASN 368 ? B ASN 212 
47 1 Y 1 B GLY 369 ? B GLY 213 
48 1 Y 1 B GLU 521 ? B GLU 365 
49 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 
A1EKD N1   N  Y N 1   
A1EKD N3   N  Y N 2   
A1EKD C4   C  Y N 3   
A1EKD C5   C  Y N 4   
A1EKD C6   C  N N 5   
A1EKD C7   C  Y N 6   
A1EKD C8   C  N N 7   
A1EKD C10  C  Y N 8   
A1EKD C13  C  Y N 9   
A1EKD C15  C  Y N 10  
A1EKD C17  C  Y N 11  
A1EKD C20  C  Y N 12  
A1EKD C21  C  Y N 13  
A1EKD C22  C  Y N 14  
A1EKD C24  C  Y N 15  
A1EKD C26  C  N N 16  
A1EKD C28  C  Y N 17  
A1EKD C1   C  Y N 18  
A1EKD C11  C  N N 19  
A1EKD C12  C  Y N 20  
A1EKD C14  C  Y N 21  
A1EKD C16  C  Y N 22  
A1EKD C18  C  Y N 23  
A1EKD C19  C  Y N 24  
A1EKD C2   C  Y N 25  
A1EKD C23  C  Y N 26  
A1EKD C25  C  Y N 27  
A1EKD C27  C  Y N 28  
A1EKD C29  C  Y N 29  
A1EKD C3   C  Y N 30  
A1EKD C30  C  Y N 31  
A1EKD C9   C  Y N 32  
A1EKD F1   F  N N 33  
A1EKD F2   F  N N 34  
A1EKD F3   F  N N 35  
A1EKD F4   F  N N 36  
A1EKD N2   N  Y N 37  
A1EKD N4   N  Y N 38  
A1EKD N5   N  Y N 39  
A1EKD N6   N  Y N 40  
A1EKD O1   O  N N 41  
A1EKD O2   O  N N 42  
A1EKD O3   O  N N 43  
A1EKD O4   O  N N 44  
A1EKD S1   S  Y N 45  
A1EKD S2   S  Y N 46  
A1EKD H1   H  N N 47  
A1EKD H2   H  N N 48  
A1EKD H3   H  N N 49  
A1EKD H5   H  N N 50  
A1EKD H6   H  N N 51  
A1EKD H7   H  N N 52  
A1EKD H8   H  N N 53  
A1EKD H9   H  N N 54  
A1EKD H10  H  N N 55  
A1EKD H11  H  N N 56  
A1EKD H12  H  N N 57  
A1EKD H13  H  N N 58  
A1EKD H14  H  N N 59  
A1EKD H16  H  N N 60  
A1EKD H17  H  N N 61  
A1EKD H18  H  N N 62  
A1EKD H4   H  N N 63  
A1EKD H15  H  N N 64  
ALA   N    N  N N 65  
ALA   CA   C  N S 66  
ALA   C    C  N N 67  
ALA   O    O  N N 68  
ALA   CB   C  N N 69  
ALA   OXT  O  N N 70  
ALA   H    H  N N 71  
ALA   H2   H  N N 72  
ALA   HA   H  N N 73  
ALA   HB1  H  N N 74  
ALA   HB2  H  N N 75  
ALA   HB3  H  N N 76  
ALA   HXT  H  N N 77  
ARG   N    N  N N 78  
ARG   CA   C  N S 79  
ARG   C    C  N N 80  
ARG   O    O  N N 81  
ARG   CB   C  N N 82  
ARG   CG   C  N N 83  
ARG   CD   C  N N 84  
ARG   NE   N  N N 85  
ARG   CZ   C  N N 86  
ARG   NH1  N  N N 87  
ARG   NH2  N  N N 88  
ARG   OXT  O  N N 89  
ARG   H    H  N N 90  
ARG   H2   H  N N 91  
ARG   HA   H  N N 92  
ARG   HB2  H  N N 93  
ARG   HB3  H  N N 94  
ARG   HG2  H  N N 95  
ARG   HG3  H  N N 96  
ARG   HD2  H  N N 97  
ARG   HD3  H  N N 98  
ARG   HE   H  N N 99  
ARG   HH11 H  N N 100 
ARG   HH12 H  N N 101 
ARG   HH21 H  N N 102 
ARG   HH22 H  N N 103 
ARG   HXT  H  N N 104 
ASN   N    N  N N 105 
ASN   CA   C  N S 106 
ASN   C    C  N N 107 
ASN   O    O  N N 108 
ASN   CB   C  N N 109 
ASN   CG   C  N N 110 
ASN   OD1  O  N N 111 
ASN   ND2  N  N N 112 
ASN   OXT  O  N N 113 
ASN   H    H  N N 114 
ASN   H2   H  N N 115 
ASN   HA   H  N N 116 
ASN   HB2  H  N N 117 
ASN   HB3  H  N N 118 
ASN   HD21 H  N N 119 
ASN   HD22 H  N N 120 
ASN   HXT  H  N N 121 
ASP   N    N  N N 122 
ASP   CA   C  N S 123 
ASP   C    C  N N 124 
ASP   O    O  N N 125 
ASP   CB   C  N N 126 
ASP   CG   C  N N 127 
ASP   OD1  O  N N 128 
ASP   OD2  O  N N 129 
ASP   OXT  O  N N 130 
ASP   H    H  N N 131 
ASP   H2   H  N N 132 
ASP   HA   H  N N 133 
ASP   HB2  H  N N 134 
ASP   HB3  H  N N 135 
ASP   HD2  H  N N 136 
ASP   HXT  H  N N 137 
CYS   N    N  N N 138 
CYS   CA   C  N R 139 
CYS   C    C  N N 140 
CYS   O    O  N N 141 
CYS   CB   C  N N 142 
CYS   SG   S  N N 143 
CYS   OXT  O  N N 144 
CYS   H    H  N N 145 
CYS   H2   H  N N 146 
CYS   HA   H  N N 147 
CYS   HB2  H  N N 148 
CYS   HB3  H  N N 149 
CYS   HG   H  N N 150 
CYS   HXT  H  N N 151 
GLN   N    N  N N 152 
GLN   CA   C  N S 153 
GLN   C    C  N N 154 
GLN   O    O  N N 155 
GLN   CB   C  N N 156 
GLN   CG   C  N N 157 
GLN   CD   C  N N 158 
GLN   OE1  O  N N 159 
GLN   NE2  N  N N 160 
GLN   OXT  O  N N 161 
GLN   H    H  N N 162 
GLN   H2   H  N N 163 
GLN   HA   H  N N 164 
GLN   HB2  H  N N 165 
GLN   HB3  H  N N 166 
GLN   HG2  H  N N 167 
GLN   HG3  H  N N 168 
GLN   HE21 H  N N 169 
GLN   HE22 H  N N 170 
GLN   HXT  H  N N 171 
GLU   N    N  N N 172 
GLU   CA   C  N S 173 
GLU   C    C  N N 174 
GLU   O    O  N N 175 
GLU   CB   C  N N 176 
GLU   CG   C  N N 177 
GLU   CD   C  N N 178 
GLU   OE1  O  N N 179 
GLU   OE2  O  N N 180 
GLU   OXT  O  N N 181 
GLU   H    H  N N 182 
GLU   H2   H  N N 183 
GLU   HA   H  N N 184 
GLU   HB2  H  N N 185 
GLU   HB3  H  N N 186 
GLU   HG2  H  N N 187 
GLU   HG3  H  N N 188 
GLU   HE2  H  N N 189 
GLU   HXT  H  N N 190 
GLY   N    N  N N 191 
GLY   CA   C  N N 192 
GLY   C    C  N N 193 
GLY   O    O  N N 194 
GLY   OXT  O  N N 195 
GLY   H    H  N N 196 
GLY   H2   H  N N 197 
GLY   HA2  H  N N 198 
GLY   HA3  H  N N 199 
GLY   HXT  H  N N 200 
HIS   N    N  N N 201 
HIS   CA   C  N S 202 
HIS   C    C  N N 203 
HIS   O    O  N N 204 
HIS   CB   C  N N 205 
HIS   CG   C  Y N 206 
HIS   ND1  N  Y N 207 
HIS   CD2  C  Y N 208 
HIS   CE1  C  Y N 209 
HIS   NE2  N  Y N 210 
HIS   OXT  O  N N 211 
HIS   H    H  N N 212 
HIS   H2   H  N N 213 
HIS   HA   H  N N 214 
HIS   HB2  H  N N 215 
HIS   HB3  H  N N 216 
HIS   HD1  H  N N 217 
HIS   HD2  H  N N 218 
HIS   HE1  H  N N 219 
HIS   HE2  H  N N 220 
HIS   HXT  H  N N 221 
HOH   O    O  N N 222 
HOH   H1   H  N N 223 
HOH   H2   H  N N 224 
ILE   N    N  N N 225 
ILE   CA   C  N S 226 
ILE   C    C  N N 227 
ILE   O    O  N N 228 
ILE   CB   C  N S 229 
ILE   CG1  C  N N 230 
ILE   CG2  C  N N 231 
ILE   CD1  C  N N 232 
ILE   OXT  O  N N 233 
ILE   H    H  N N 234 
ILE   H2   H  N N 235 
ILE   HA   H  N N 236 
ILE   HB   H  N N 237 
ILE   HG12 H  N N 238 
ILE   HG13 H  N N 239 
ILE   HG21 H  N N 240 
ILE   HG22 H  N N 241 
ILE   HG23 H  N N 242 
ILE   HD11 H  N N 243 
ILE   HD12 H  N N 244 
ILE   HD13 H  N N 245 
ILE   HXT  H  N N 246 
LEU   N    N  N N 247 
LEU   CA   C  N S 248 
LEU   C    C  N N 249 
LEU   O    O  N N 250 
LEU   CB   C  N N 251 
LEU   CG   C  N N 252 
LEU   CD1  C  N N 253 
LEU   CD2  C  N N 254 
LEU   OXT  O  N N 255 
LEU   H    H  N N 256 
LEU   H2   H  N N 257 
LEU   HA   H  N N 258 
LEU   HB2  H  N N 259 
LEU   HB3  H  N N 260 
LEU   HG   H  N N 261 
LEU   HD11 H  N N 262 
LEU   HD12 H  N N 263 
LEU   HD13 H  N N 264 
LEU   HD21 H  N N 265 
LEU   HD22 H  N N 266 
LEU   HD23 H  N N 267 
LEU   HXT  H  N N 268 
LYS   N    N  N N 269 
LYS   CA   C  N S 270 
LYS   C    C  N N 271 
LYS   O    O  N N 272 
LYS   CB   C  N N 273 
LYS   CG   C  N N 274 
LYS   CD   C  N N 275 
LYS   CE   C  N N 276 
LYS   NZ   N  N N 277 
LYS   OXT  O  N N 278 
LYS   H    H  N N 279 
LYS   H2   H  N N 280 
LYS   HA   H  N N 281 
LYS   HB2  H  N N 282 
LYS   HB3  H  N N 283 
LYS   HG2  H  N N 284 
LYS   HG3  H  N N 285 
LYS   HD2  H  N N 286 
LYS   HD3  H  N N 287 
LYS   HE2  H  N N 288 
LYS   HE3  H  N N 289 
LYS   HZ1  H  N N 290 
LYS   HZ2  H  N N 291 
LYS   HZ3  H  N N 292 
LYS   HXT  H  N N 293 
MET   N    N  N N 294 
MET   CA   C  N S 295 
MET   C    C  N N 296 
MET   O    O  N N 297 
MET   CB   C  N N 298 
MET   CG   C  N N 299 
MET   SD   S  N N 300 
MET   CE   C  N N 301 
MET   OXT  O  N N 302 
MET   H    H  N N 303 
MET   H2   H  N N 304 
MET   HA   H  N N 305 
MET   HB2  H  N N 306 
MET   HB3  H  N N 307 
MET   HG2  H  N N 308 
MET   HG3  H  N N 309 
MET   HE1  H  N N 310 
MET   HE2  H  N N 311 
MET   HE3  H  N N 312 
MET   HXT  H  N N 313 
PHE   N    N  N N 314 
PHE   CA   C  N S 315 
PHE   C    C  N N 316 
PHE   O    O  N N 317 
PHE   CB   C  N N 318 
PHE   CG   C  Y N 319 
PHE   CD1  C  Y N 320 
PHE   CD2  C  Y N 321 
PHE   CE1  C  Y N 322 
PHE   CE2  C  Y N 323 
PHE   CZ   C  Y N 324 
PHE   OXT  O  N N 325 
PHE   H    H  N N 326 
PHE   H2   H  N N 327 
PHE   HA   H  N N 328 
PHE   HB2  H  N N 329 
PHE   HB3  H  N N 330 
PHE   HD1  H  N N 331 
PHE   HD2  H  N N 332 
PHE   HE1  H  N N 333 
PHE   HE2  H  N N 334 
PHE   HZ   H  N N 335 
PHE   HXT  H  N N 336 
PRO   N    N  N N 337 
PRO   CA   C  N S 338 
PRO   C    C  N N 339 
PRO   O    O  N N 340 
PRO   CB   C  N N 341 
PRO   CG   C  N N 342 
PRO   CD   C  N N 343 
PRO   OXT  O  N N 344 
PRO   H    H  N N 345 
PRO   HA   H  N N 346 
PRO   HB2  H  N N 347 
PRO   HB3  H  N N 348 
PRO   HG2  H  N N 349 
PRO   HG3  H  N N 350 
PRO   HD2  H  N N 351 
PRO   HD3  H  N N 352 
PRO   HXT  H  N N 353 
SER   N    N  N N 354 
SER   CA   C  N S 355 
SER   C    C  N N 356 
SER   O    O  N N 357 
SER   CB   C  N N 358 
SER   OG   O  N N 359 
SER   OXT  O  N N 360 
SER   H    H  N N 361 
SER   H2   H  N N 362 
SER   HA   H  N N 363 
SER   HB2  H  N N 364 
SER   HB3  H  N N 365 
SER   HG   H  N N 366 
SER   HXT  H  N N 367 
THR   N    N  N N 368 
THR   CA   C  N S 369 
THR   C    C  N N 370 
THR   O    O  N N 371 
THR   CB   C  N R 372 
THR   OG1  O  N N 373 
THR   CG2  C  N N 374 
THR   OXT  O  N N 375 
THR   H    H  N N 376 
THR   H2   H  N N 377 
THR   HA   H  N N 378 
THR   HB   H  N N 379 
THR   HG1  H  N N 380 
THR   HG21 H  N N 381 
THR   HG22 H  N N 382 
THR   HG23 H  N N 383 
THR   HXT  H  N N 384 
TRP   N    N  N N 385 
TRP   CA   C  N S 386 
TRP   C    C  N N 387 
TRP   O    O  N N 388 
TRP   CB   C  N N 389 
TRP   CG   C  Y N 390 
TRP   CD1  C  Y N 391 
TRP   CD2  C  Y N 392 
TRP   NE1  N  Y N 393 
TRP   CE2  C  Y N 394 
TRP   CE3  C  Y N 395 
TRP   CZ2  C  Y N 396 
TRP   CZ3  C  Y N 397 
TRP   CH2  C  Y N 398 
TRP   OXT  O  N N 399 
TRP   H    H  N N 400 
TRP   H2   H  N N 401 
TRP   HA   H  N N 402 
TRP   HB2  H  N N 403 
TRP   HB3  H  N N 404 
TRP   HD1  H  N N 405 
TRP   HE1  H  N N 406 
TRP   HE3  H  N N 407 
TRP   HZ2  H  N N 408 
TRP   HZ3  H  N N 409 
TRP   HH2  H  N N 410 
TRP   HXT  H  N N 411 
TYR   N    N  N N 412 
TYR   CA   C  N S 413 
TYR   C    C  N N 414 
TYR   O    O  N N 415 
TYR   CB   C  N N 416 
TYR   CG   C  Y N 417 
TYR   CD1  C  Y N 418 
TYR   CD2  C  Y N 419 
TYR   CE1  C  Y N 420 
TYR   CE2  C  Y N 421 
TYR   CZ   C  Y N 422 
TYR   OH   O  N N 423 
TYR   OXT  O  N N 424 
TYR   H    H  N N 425 
TYR   H2   H  N N 426 
TYR   HA   H  N N 427 
TYR   HB2  H  N N 428 
TYR   HB3  H  N N 429 
TYR   HD1  H  N N 430 
TYR   HD2  H  N N 431 
TYR   HE1  H  N N 432 
TYR   HE2  H  N N 433 
TYR   HH   H  N N 434 
TYR   HXT  H  N N 435 
VAL   N    N  N N 436 
VAL   CA   C  N S 437 
VAL   C    C  N N 438 
VAL   O    O  N N 439 
VAL   CB   C  N N 440 
VAL   CG1  C  N N 441 
VAL   CG2  C  N N 442 
VAL   OXT  O  N N 443 
VAL   H    H  N N 444 
VAL   H2   H  N N 445 
VAL   HA   H  N N 446 
VAL   HB   H  N N 447 
VAL   HG11 H  N N 448 
VAL   HG12 H  N N 449 
VAL   HG13 H  N N 450 
VAL   HG21 H  N N 451 
VAL   HG22 H  N N 452 
VAL   HG23 H  N N 453 
VAL   HXT  H  N N 454 
ZN    ZN   ZN N N 455 
# 
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 
A1EKD F3  C22  sing N N 1   
A1EKD C21 C22  doub Y N 2   
A1EKD C21 C20  sing Y N 3   
A1EKD C22 C23  sing Y N 4   
A1EKD F2  C20  sing N N 5   
A1EKD C20 C19  doub Y N 6   
A1EKD C23 C24  doub Y N 7   
A1EKD C19 C24  sing Y N 8   
A1EKD C19 N4   sing Y N 9   
A1EKD C24 S2   sing Y N 10  
A1EKD N4  C18  doub Y N 11  
A1EKD S2  C18  sing Y N 12  
A1EKD C18 N3   sing N N 13  
A1EKD N3  N5   sing Y N 14  
A1EKD N3  C17  sing Y N 15  
A1EKD N5  C25  doub Y N 16  
A1EKD O3  C17  sing N N 17  
A1EKD C17 C16  doub Y N 18  
A1EKD C25 C16  sing Y N 19  
A1EKD C25 C26  sing N N 20  
A1EKD C16 C8   sing N N 21  
A1EKD O4  C27  sing N N 22  
A1EKD C8  C7   sing N N 23  
A1EKD C8  C9   sing N N 24  
A1EKD C27 C7   doub Y N 25  
A1EKD C27 N1   sing Y N 26  
A1EKD C7  C5   sing Y N 27  
A1EKD C15 C9   doub Y N 28  
A1EKD C15 C14  sing Y N 29  
A1EKD C9  C10  sing Y N 30  
A1EKD S1  C4   sing Y N 31  
A1EKD S1  C3   sing Y N 32  
A1EKD O2  C11  doub N N 33  
A1EKD N1  C4   sing N N 34  
A1EKD N1  N2   sing Y N 35  
A1EKD C14 C13  doub Y N 36  
A1EKD C5  N2   doub Y N 37  
A1EKD C5  C6   sing N N 38  
A1EKD C4  N6   doub Y N 39  
A1EKD C10 C11  sing N N 40  
A1EKD C10 C12  doub Y N 41  
A1EKD C3  C28  doub Y N 42  
A1EKD C3  C2   sing Y N 43  
A1EKD C28 C29  sing Y N 44  
A1EKD C11 O1   sing N N 45  
A1EKD C13 C12  sing Y N 46  
A1EKD N6  C2   sing Y N 47  
A1EKD C2  C1   doub Y N 48  
A1EKD C29 F4   sing N N 49  
A1EKD C29 C30  doub Y N 50  
A1EKD C1  C30  sing Y N 51  
A1EKD C1  F1   sing N N 52  
A1EKD C6  H1   sing N N 53  
A1EKD C6  H2   sing N N 54  
A1EKD C6  H3   sing N N 55  
A1EKD C8  H5   sing N N 56  
A1EKD C13 H6   sing N N 57  
A1EKD C15 H7   sing N N 58  
A1EKD C21 H8   sing N N 59  
A1EKD C26 H9   sing N N 60  
A1EKD C26 H10  sing N N 61  
A1EKD C26 H11  sing N N 62  
A1EKD C28 H12  sing N N 63  
A1EKD C12 H13  sing N N 64  
A1EKD C14 H14  sing N N 65  
A1EKD C23 H16  sing N N 66  
A1EKD C30 H17  sing N N 67  
A1EKD O1  H18  sing N N 68  
A1EKD O3  H4   sing N N 69  
A1EKD O4  H15  sing N N 70  
ALA   N   CA   sing N N 71  
ALA   N   H    sing N N 72  
ALA   N   H2   sing N N 73  
ALA   CA  C    sing N N 74  
ALA   CA  CB   sing N N 75  
ALA   CA  HA   sing N N 76  
ALA   C   O    doub N N 77  
ALA   C   OXT  sing N N 78  
ALA   CB  HB1  sing N N 79  
ALA   CB  HB2  sing N N 80  
ALA   CB  HB3  sing N N 81  
ALA   OXT HXT  sing N N 82  
ARG   N   CA   sing N N 83  
ARG   N   H    sing N N 84  
ARG   N   H2   sing N N 85  
ARG   CA  C    sing N N 86  
ARG   CA  CB   sing N N 87  
ARG   CA  HA   sing N N 88  
ARG   C   O    doub N N 89  
ARG   C   OXT  sing N N 90  
ARG   CB  CG   sing N N 91  
ARG   CB  HB2  sing N N 92  
ARG   CB  HB3  sing N N 93  
ARG   CG  CD   sing N N 94  
ARG   CG  HG2  sing N N 95  
ARG   CG  HG3  sing N N 96  
ARG   CD  NE   sing N N 97  
ARG   CD  HD2  sing N N 98  
ARG   CD  HD3  sing N N 99  
ARG   NE  CZ   sing N N 100 
ARG   NE  HE   sing N N 101 
ARG   CZ  NH1  sing N N 102 
ARG   CZ  NH2  doub N N 103 
ARG   NH1 HH11 sing N N 104 
ARG   NH1 HH12 sing N N 105 
ARG   NH2 HH21 sing N N 106 
ARG   NH2 HH22 sing N N 107 
ARG   OXT HXT  sing N N 108 
ASN   N   CA   sing N N 109 
ASN   N   H    sing N N 110 
ASN   N   H2   sing N N 111 
ASN   CA  C    sing N N 112 
ASN   CA  CB   sing N N 113 
ASN   CA  HA   sing N N 114 
ASN   C   O    doub N N 115 
ASN   C   OXT  sing N N 116 
ASN   CB  CG   sing N N 117 
ASN   CB  HB2  sing N N 118 
ASN   CB  HB3  sing N N 119 
ASN   CG  OD1  doub N N 120 
ASN   CG  ND2  sing N N 121 
ASN   ND2 HD21 sing N N 122 
ASN   ND2 HD22 sing N N 123 
ASN   OXT HXT  sing N N 124 
ASP   N   CA   sing N N 125 
ASP   N   H    sing N N 126 
ASP   N   H2   sing N N 127 
ASP   CA  C    sing N N 128 
ASP   CA  CB   sing N N 129 
ASP   CA  HA   sing N N 130 
ASP   C   O    doub N N 131 
ASP   C   OXT  sing N N 132 
ASP   CB  CG   sing N N 133 
ASP   CB  HB2  sing N N 134 
ASP   CB  HB3  sing N N 135 
ASP   CG  OD1  doub N N 136 
ASP   CG  OD2  sing N N 137 
ASP   OD2 HD2  sing N N 138 
ASP   OXT HXT  sing N N 139 
CYS   N   CA   sing N N 140 
CYS   N   H    sing N N 141 
CYS   N   H2   sing N N 142 
CYS   CA  C    sing N N 143 
CYS   CA  CB   sing N N 144 
CYS   CA  HA   sing N N 145 
CYS   C   O    doub N N 146 
CYS   C   OXT  sing N N 147 
CYS   CB  SG   sing N N 148 
CYS   CB  HB2  sing N N 149 
CYS   CB  HB3  sing N N 150 
CYS   SG  HG   sing N N 151 
CYS   OXT HXT  sing N N 152 
GLN   N   CA   sing N N 153 
GLN   N   H    sing N N 154 
GLN   N   H2   sing N N 155 
GLN   CA  C    sing N N 156 
GLN   CA  CB   sing N N 157 
GLN   CA  HA   sing N N 158 
GLN   C   O    doub N N 159 
GLN   C   OXT  sing N N 160 
GLN   CB  CG   sing N N 161 
GLN   CB  HB2  sing N N 162 
GLN   CB  HB3  sing N N 163 
GLN   CG  CD   sing N N 164 
GLN   CG  HG2  sing N N 165 
GLN   CG  HG3  sing N N 166 
GLN   CD  OE1  doub N N 167 
GLN   CD  NE2  sing N N 168 
GLN   NE2 HE21 sing N N 169 
GLN   NE2 HE22 sing N N 170 
GLN   OXT HXT  sing N N 171 
GLU   N   CA   sing N N 172 
GLU   N   H    sing N N 173 
GLU   N   H2   sing N N 174 
GLU   CA  C    sing N N 175 
GLU   CA  CB   sing N N 176 
GLU   CA  HA   sing N N 177 
GLU   C   O    doub N N 178 
GLU   C   OXT  sing N N 179 
GLU   CB  CG   sing N N 180 
GLU   CB  HB2  sing N N 181 
GLU   CB  HB3  sing N N 182 
GLU   CG  CD   sing N N 183 
GLU   CG  HG2  sing N N 184 
GLU   CG  HG3  sing N N 185 
GLU   CD  OE1  doub N N 186 
GLU   CD  OE2  sing N N 187 
GLU   OE2 HE2  sing N N 188 
GLU   OXT HXT  sing N N 189 
GLY   N   CA   sing N N 190 
GLY   N   H    sing N N 191 
GLY   N   H2   sing N N 192 
GLY   CA  C    sing N N 193 
GLY   CA  HA2  sing N N 194 
GLY   CA  HA3  sing N N 195 
GLY   C   O    doub N N 196 
GLY   C   OXT  sing N N 197 
GLY   OXT HXT  sing N N 198 
HIS   N   CA   sing N N 199 
HIS   N   H    sing N N 200 
HIS   N   H2   sing N N 201 
HIS   CA  C    sing N N 202 
HIS   CA  CB   sing N N 203 
HIS   CA  HA   sing N N 204 
HIS   C   O    doub N N 205 
HIS   C   OXT  sing N N 206 
HIS   CB  CG   sing N N 207 
HIS   CB  HB2  sing N N 208 
HIS   CB  HB3  sing N N 209 
HIS   CG  ND1  sing Y N 210 
HIS   CG  CD2  doub Y N 211 
HIS   ND1 CE1  doub Y N 212 
HIS   ND1 HD1  sing N N 213 
HIS   CD2 NE2  sing Y N 214 
HIS   CD2 HD2  sing N N 215 
HIS   CE1 NE2  sing Y N 216 
HIS   CE1 HE1  sing N N 217 
HIS   NE2 HE2  sing N N 218 
HIS   OXT HXT  sing N N 219 
HOH   O   H1   sing N N 220 
HOH   O   H2   sing N N 221 
ILE   N   CA   sing N N 222 
ILE   N   H    sing N N 223 
ILE   N   H2   sing N N 224 
ILE   CA  C    sing N N 225 
ILE   CA  CB   sing N N 226 
ILE   CA  HA   sing N N 227 
ILE   C   O    doub N N 228 
ILE   C   OXT  sing N N 229 
ILE   CB  CG1  sing N N 230 
ILE   CB  CG2  sing N N 231 
ILE   CB  HB   sing N N 232 
ILE   CG1 CD1  sing N N 233 
ILE   CG1 HG12 sing N N 234 
ILE   CG1 HG13 sing N N 235 
ILE   CG2 HG21 sing N N 236 
ILE   CG2 HG22 sing N N 237 
ILE   CG2 HG23 sing N N 238 
ILE   CD1 HD11 sing N N 239 
ILE   CD1 HD12 sing N N 240 
ILE   CD1 HD13 sing N N 241 
ILE   OXT HXT  sing N N 242 
LEU   N   CA   sing N N 243 
LEU   N   H    sing N N 244 
LEU   N   H2   sing N N 245 
LEU   CA  C    sing N N 246 
LEU   CA  CB   sing N N 247 
LEU   CA  HA   sing N N 248 
LEU   C   O    doub N N 249 
LEU   C   OXT  sing N N 250 
LEU   CB  CG   sing N N 251 
LEU   CB  HB2  sing N N 252 
LEU   CB  HB3  sing N N 253 
LEU   CG  CD1  sing N N 254 
LEU   CG  CD2  sing N N 255 
LEU   CG  HG   sing N N 256 
LEU   CD1 HD11 sing N N 257 
LEU   CD1 HD12 sing N N 258 
LEU   CD1 HD13 sing N N 259 
LEU   CD2 HD21 sing N N 260 
LEU   CD2 HD22 sing N N 261 
LEU   CD2 HD23 sing N N 262 
LEU   OXT HXT  sing N N 263 
LYS   N   CA   sing N N 264 
LYS   N   H    sing N N 265 
LYS   N   H2   sing N N 266 
LYS   CA  C    sing N N 267 
LYS   CA  CB   sing N N 268 
LYS   CA  HA   sing N N 269 
LYS   C   O    doub N N 270 
LYS   C   OXT  sing N N 271 
LYS   CB  CG   sing N N 272 
LYS   CB  HB2  sing N N 273 
LYS   CB  HB3  sing N N 274 
LYS   CG  CD   sing N N 275 
LYS   CG  HG2  sing N N 276 
LYS   CG  HG3  sing N N 277 
LYS   CD  CE   sing N N 278 
LYS   CD  HD2  sing N N 279 
LYS   CD  HD3  sing N N 280 
LYS   CE  NZ   sing N N 281 
LYS   CE  HE2  sing N N 282 
LYS   CE  HE3  sing N N 283 
LYS   NZ  HZ1  sing N N 284 
LYS   NZ  HZ2  sing N N 285 
LYS   NZ  HZ3  sing N N 286 
LYS   OXT HXT  sing N N 287 
MET   N   CA   sing N N 288 
MET   N   H    sing N N 289 
MET   N   H2   sing N N 290 
MET   CA  C    sing N N 291 
MET   CA  CB   sing N N 292 
MET   CA  HA   sing N N 293 
MET   C   O    doub N N 294 
MET   C   OXT  sing N N 295 
MET   CB  CG   sing N N 296 
MET   CB  HB2  sing N N 297 
MET   CB  HB3  sing N N 298 
MET   CG  SD   sing N N 299 
MET   CG  HG2  sing N N 300 
MET   CG  HG3  sing N N 301 
MET   SD  CE   sing N N 302 
MET   CE  HE1  sing N N 303 
MET   CE  HE2  sing N N 304 
MET   CE  HE3  sing N N 305 
MET   OXT HXT  sing N N 306 
PHE   N   CA   sing N N 307 
PHE   N   H    sing N N 308 
PHE   N   H2   sing N N 309 
PHE   CA  C    sing N N 310 
PHE   CA  CB   sing N N 311 
PHE   CA  HA   sing N N 312 
PHE   C   O    doub N N 313 
PHE   C   OXT  sing N N 314 
PHE   CB  CG   sing N N 315 
PHE   CB  HB2  sing N N 316 
PHE   CB  HB3  sing N N 317 
PHE   CG  CD1  doub Y N 318 
PHE   CG  CD2  sing Y N 319 
PHE   CD1 CE1  sing Y N 320 
PHE   CD1 HD1  sing N N 321 
PHE   CD2 CE2  doub Y N 322 
PHE   CD2 HD2  sing N N 323 
PHE   CE1 CZ   doub Y N 324 
PHE   CE1 HE1  sing N N 325 
PHE   CE2 CZ   sing Y N 326 
PHE   CE2 HE2  sing N N 327 
PHE   CZ  HZ   sing N N 328 
PHE   OXT HXT  sing N N 329 
PRO   N   CA   sing N N 330 
PRO   N   CD   sing N N 331 
PRO   N   H    sing N N 332 
PRO   CA  C    sing N N 333 
PRO   CA  CB   sing N N 334 
PRO   CA  HA   sing N N 335 
PRO   C   O    doub N N 336 
PRO   C   OXT  sing N N 337 
PRO   CB  CG   sing N N 338 
PRO   CB  HB2  sing N N 339 
PRO   CB  HB3  sing N N 340 
PRO   CG  CD   sing N N 341 
PRO   CG  HG2  sing N N 342 
PRO   CG  HG3  sing N N 343 
PRO   CD  HD2  sing N N 344 
PRO   CD  HD3  sing N N 345 
PRO   OXT HXT  sing N N 346 
SER   N   CA   sing N N 347 
SER   N   H    sing N N 348 
SER   N   H2   sing N N 349 
SER   CA  C    sing N N 350 
SER   CA  CB   sing N N 351 
SER   CA  HA   sing N N 352 
SER   C   O    doub N N 353 
SER   C   OXT  sing N N 354 
SER   CB  OG   sing N N 355 
SER   CB  HB2  sing N N 356 
SER   CB  HB3  sing N N 357 
SER   OG  HG   sing N N 358 
SER   OXT HXT  sing N N 359 
THR   N   CA   sing N N 360 
THR   N   H    sing N N 361 
THR   N   H2   sing N N 362 
THR   CA  C    sing N N 363 
THR   CA  CB   sing N N 364 
THR   CA  HA   sing N N 365 
THR   C   O    doub N N 366 
THR   C   OXT  sing N N 367 
THR   CB  OG1  sing N N 368 
THR   CB  CG2  sing N N 369 
THR   CB  HB   sing N N 370 
THR   OG1 HG1  sing N N 371 
THR   CG2 HG21 sing N N 372 
THR   CG2 HG22 sing N N 373 
THR   CG2 HG23 sing N N 374 
THR   OXT HXT  sing N N 375 
TRP   N   CA   sing N N 376 
TRP   N   H    sing N N 377 
TRP   N   H2   sing N N 378 
TRP   CA  C    sing N N 379 
TRP   CA  CB   sing N N 380 
TRP   CA  HA   sing N N 381 
TRP   C   O    doub N N 382 
TRP   C   OXT  sing N N 383 
TRP   CB  CG   sing N N 384 
TRP   CB  HB2  sing N N 385 
TRP   CB  HB3  sing N N 386 
TRP   CG  CD1  doub Y N 387 
TRP   CG  CD2  sing Y N 388 
TRP   CD1 NE1  sing Y N 389 
TRP   CD1 HD1  sing N N 390 
TRP   CD2 CE2  doub Y N 391 
TRP   CD2 CE3  sing Y N 392 
TRP   NE1 CE2  sing Y N 393 
TRP   NE1 HE1  sing N N 394 
TRP   CE2 CZ2  sing Y N 395 
TRP   CE3 CZ3  doub Y N 396 
TRP   CE3 HE3  sing N N 397 
TRP   CZ2 CH2  doub Y N 398 
TRP   CZ2 HZ2  sing N N 399 
TRP   CZ3 CH2  sing Y N 400 
TRP   CZ3 HZ3  sing N N 401 
TRP   CH2 HH2  sing N N 402 
TRP   OXT HXT  sing N N 403 
TYR   N   CA   sing N N 404 
TYR   N   H    sing N N 405 
TYR   N   H2   sing N N 406 
TYR   CA  C    sing N N 407 
TYR   CA  CB   sing N N 408 
TYR   CA  HA   sing N N 409 
TYR   C   O    doub N N 410 
TYR   C   OXT  sing N N 411 
TYR   CB  CG   sing N N 412 
TYR   CB  HB2  sing N N 413 
TYR   CB  HB3  sing N N 414 
TYR   CG  CD1  doub Y N 415 
TYR   CG  CD2  sing Y N 416 
TYR   CD1 CE1  sing Y N 417 
TYR   CD1 HD1  sing N N 418 
TYR   CD2 CE2  doub Y N 419 
TYR   CD2 HD2  sing N N 420 
TYR   CE1 CZ   doub Y N 421 
TYR   CE1 HE1  sing N N 422 
TYR   CE2 CZ   sing Y N 423 
TYR   CE2 HE2  sing N N 424 
TYR   CZ  OH   sing N N 425 
TYR   OH  HH   sing N N 426 
TYR   OXT HXT  sing N N 427 
VAL   N   CA   sing N N 428 
VAL   N   H    sing N N 429 
VAL   N   H2   sing N N 430 
VAL   CA  C    sing N N 431 
VAL   CA  CB   sing N N 432 
VAL   CA  HA   sing N N 433 
VAL   C   O    doub N N 434 
VAL   C   OXT  sing N N 435 
VAL   CB  CG1  sing N N 436 
VAL   CB  CG2  sing N N 437 
VAL   CB  HB   sing N N 438 
VAL   CG1 HG11 sing N N 439 
VAL   CG1 HG12 sing N N 440 
VAL   CG1 HG13 sing N N 441 
VAL   CG2 HG21 sing N N 442 
VAL   CG2 HG22 sing N N 443 
VAL   CG2 HG23 sing N N 444 
VAL   OXT HXT  sing N N 445 
# 
_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                    9LIO 
_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]   0.004751 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001985 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021763 
_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]   0.012547 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
F  
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   ? -34.899 2.706   -22.474 1.00 53.44  ?  161 GLY   A N   1 
ATOM   2    C  CA  . GLY   A 1 5   ? -33.802 1.931   -21.920 1.00 52.30  ?  161 GLY   A CA  1 
ATOM   3    C  C   . GLY   A 1 5   ? -33.933 1.571   -20.450 1.00 47.64  ?  161 GLY   A C   1 
ATOM   4    O  O   . GLY   A 1 5   ? -32.932 1.299   -19.785 1.00 54.25  ?  161 GLY   A O   1 
ATOM   5    N  N   . ALA   A 1 6   ? -35.165 1.574   -19.931 1.00 49.36  ?  162 ALA   A N   1 
ATOM   6    C  CA  . ALA   A 1 6   ? -35.367 1.270   -18.519 1.00 47.26  ?  162 ALA   A CA  1 
ATOM   7    C  C   . ALA   A 1 6   ? -34.849 -0.122  -18.173 1.00 52.04  ?  162 ALA   A C   1 
ATOM   8    O  O   . ALA   A 1 6   ? -34.284 -0.337  -17.088 1.00 45.33  ?  162 ALA   A O   1 
ATOM   9    C  CB  . ALA   A 1 6   ? -36.847 1.405   -18.164 1.00 50.67  ?  162 ALA   A CB  1 
ATOM   10   N  N   . SER   A 1 7   ? -35.024 -1.076  -19.092 1.00 46.51  ?  163 SER   A N   1 
ATOM   11   C  CA  . SER   A 1 7   ? -34.486 -2.420  -18.896 1.00 47.75  ?  163 SER   A CA  1 
ATOM   12   C  C   . SER   A 1 7   ? -32.980 -2.385  -18.677 1.00 48.28  ?  163 SER   A C   1 
ATOM   13   O  O   . SER   A 1 7   ? -32.444 -3.131  -17.843 1.00 39.24  ?  163 SER   A O   1 
ATOM   14   C  CB  . SER   A 1 7   ? -34.821 -3.296  -20.104 1.00 49.06  ?  163 SER   A CB  1 
ATOM   15   O  OG  . SER   A 1 7   ? -36.223 -3.483  -20.216 1.00 53.15  ?  163 SER   A OG  1 
ATOM   16   N  N   . LYS   A 1 8   ? -32.278 -1.536  -19.431 1.00 39.53  ?  164 LYS   A N   1 
ATOM   17   C  CA  . LYS   A 1 8   ? -30.836 -1.409  -19.257 1.00 46.29  ?  164 LYS   A CA  1 
ATOM   18   C  C   . LYS   A 1 8   ? -30.483 -0.890  -17.856 1.00 46.83  ?  164 LYS   A C   1 
ATOM   19   O  O   . LYS   A 1 8   ? -29.466 -1.291  -17.273 1.00 41.15  ?  164 LYS   A O   1 
ATOM   20   C  CB  . LYS   A 1 8   ? -30.280 -0.504  -20.353 1.00 41.18  ?  164 LYS   A CB  1 
ATOM   21   C  CG  . LYS   A 1 8   ? -28.773 -0.364  -20.396 1.00 47.97  ?  164 LYS   A CG  1 
ATOM   22   C  CD  . LYS   A 1 8   ? -28.378 0.339   -21.701 1.00 49.04  ?  164 LYS   A CD  1 
ATOM   23   C  CE  . LYS   A 1 8   ? -26.868 0.511   -21.841 1.00 56.79  ?  164 LYS   A CE  1 
ATOM   24   N  NZ  . LYS   A 1 8   ? -26.520 1.142   -23.162 1.00 57.15  ?  164 LYS   A NZ  1 
ATOM   25   N  N   . LEU   A 1 9   ? -31.326 -0.021  -17.289 1.00 42.93  ?  165 LEU   A N   1 
ATOM   26   C  CA  . LEU   A 1 9   ? -31.108 0.432   -15.917 1.00 40.05  ?  165 LEU   A CA  1 
ATOM   27   C  C   . LEU   A 1 9   ? -31.223 -0.734  -14.936 1.00 40.40  ?  165 LEU   A C   1 
ATOM   28   O  O   . LEU   A 1 9   ? -30.425 -0.859  -13.996 1.00 35.34  ?  165 LEU   A O   1 
ATOM   29   C  CB  . LEU   A 1 9   ? -32.120 1.525   -15.566 1.00 35.99  ?  165 LEU   A CB  1 
ATOM   30   C  CG  . LEU   A 1 9   ? -32.166 2.800   -16.426 1.00 37.63  ?  165 LEU   A CG  1 
ATOM   31   C  CD1 . LEU   A 1 9   ? -33.237 3.736   -15.898 1.00 34.49  ?  165 LEU   A CD1 1 
ATOM   32   C  CD2 . LEU   A 1 9   ? -30.826 3.501   -16.480 1.00 34.90  ?  165 LEU   A CD2 1 
ATOM   33   N  N   . ARG   A 1 10  ? -32.219 -1.594  -15.141 1.00 34.36  ?  166 ARG   A N   1 
ATOM   34   C  CA  . ARG   A 1 10  ? -32.368 -2.795  -14.326 1.00 43.84  ?  166 ARG   A CA  1 
ATOM   35   C  C   . ARG   A 1 10  ? -31.192 -3.752  -14.499 1.00 43.29  ?  166 ARG   A C   1 
ATOM   36   O  O   . ARG   A 1 10  ? -30.759 -4.404  -13.535 1.00 40.97  ?  166 ARG   A O   1 
ATOM   37   C  CB  . ARG   A 1 10  ? -33.685 -3.483  -14.676 1.00 46.70  ?  166 ARG   A CB  1 
ATOM   38   C  CG  . ARG   A 1 10  ? -34.866 -2.579  -14.360 1.00 48.34  ?  166 ARG   A CG  1 
ATOM   39   C  CD  . ARG   A 1 10  ? -36.237 -3.214  -14.565 1.00 52.90  ?  166 ARG   A CD  1 
ATOM   40   N  NE  . ARG   A 1 10  ? -37.199 -2.541  -13.702 1.00 57.83  ?  166 ARG   A NE  1 
ATOM   41   C  CZ  . ARG   A 1 10  ? -37.910 -1.479  -14.062 1.00 57.63  ?  166 ARG   A CZ  1 
ATOM   42   N  NH1 . ARG   A 1 10  ? -37.830 -0.974  -15.285 1.00 53.38  ?  166 ARG   A NH1 1 
ATOM   43   N  NH2 . ARG   A 1 10  ? -38.701 -0.893  -13.164 1.00 50.67  ?  166 ARG   A NH2 1 
ATOM   44   N  N   . ALA   A 1 11  ? -30.665 -3.856  -15.720 1.00 39.69  ?  167 ALA   A N   1 
ATOM   45   C  CA  . ALA   A 1 11  ? -29.457 -4.647  -15.941 1.00 43.61  ?  167 ALA   A CA  1 
ATOM   46   C  C   . ALA   A 1 11  ? -28.306 -4.148  -15.071 1.00 46.12  ?  167 ALA   A C   1 
ATOM   47   O  O   . ALA   A 1 11  ? -27.604 -4.939  -14.428 1.00 38.35  ?  167 ALA   A O   1 
ATOM   48   C  CB  . ALA   A 1 11  ? -29.064 -4.597  -17.416 1.00 36.44  ?  167 ALA   A CB  1 
ATOM   49   N  N   . VAL   A 1 12  ? -28.085 -2.829  -15.060 1.00 39.26  ?  168 VAL   A N   1 
ATOM   50   C  CA  . VAL   A 1 12  ? -27.047 -2.250  -14.209 1.00 42.76  ?  168 VAL   A CA  1 
ATOM   51   C  C   . VAL   A 1 12  ? -27.271 -2.657  -12.766 1.00 37.00  ?  168 VAL   A C   1 
ATOM   52   O  O   . VAL   A 1 12  ? -26.376 -3.186  -12.103 1.00 43.09  ?  168 VAL   A O   1 
ATOM   53   C  CB  . VAL   A 1 12  ? -27.024 -0.719  -14.350 1.00 44.87  ?  168 VAL   A CB  1 
ATOM   54   C  CG1 . VAL   A 1 12  ? -26.104 -0.116  -13.292 1.00 37.01  ?  168 VAL   A CG1 1 
ATOM   55   C  CG2 . VAL   A 1 12  ? -26.597 -0.348  -15.756 1.00 44.20  ?  168 VAL   A CG2 1 
ATOM   56   N  N   . LEU   A 1 13  ? -28.487 -2.436  -12.274 1.00 38.01  ?  169 LEU   A N   1 
ATOM   57   C  CA  . LEU   A 1 13  ? -28.795 -2.737  -10.885 1.00 35.59  ?  169 LEU   A CA  1 
ATOM   58   C  C   . LEU   A 1 13  ? -28.568 -4.214  -10.570 1.00 42.54  ?  169 LEU   A C   1 
ATOM   59   O  O   . LEU   A 1 13  ? -28.069 -4.547  -9.487  1.00 43.25  ?  169 LEU   A O   1 
ATOM   60   C  CB  . LEU   A 1 13  ? -30.230 -2.315  -10.584 1.00 39.87  ?  169 LEU   A CB  1 
ATOM   61   C  CG  . LEU   A 1 13  ? -30.501 -0.801  -10.573 1.00 33.79  ?  169 LEU   A CG  1 
ATOM   62   C  CD1 . LEU   A 1 13  ? -31.992 -0.549  -10.592 1.00 33.56  ?  169 LEU   A CD1 1 
ATOM   63   C  CD2 . LEU   A 1 13  ? -29.876 -0.162  -9.326  1.00 36.62  ?  169 LEU   A CD2 1 
ATOM   64   N  N   . GLU   A 1 14  ? -28.905 -5.111  -11.508 1.00 37.89  ?  170 GLU   A N   1 
ATOM   65   C  CA  . GLU   A 1 14  ? -28.598 -6.538  -11.340 1.00 42.48  ?  170 GLU   A CA  1 
ATOM   66   C  C   . GLU   A 1 14  ? -27.110 -6.750  -11.080 1.00 45.81  ?  170 GLU   A C   1 
ATOM   67   O  O   . GLU   A 1 14  ? -26.721 -7.423  -10.118 1.00 50.95  ?  170 GLU   A O   1 
ATOM   68   C  CB  . GLU   A 1 14  ? -29.020 -7.354  -12.579 1.00 47.37  ?  170 GLU   A CB  1 
ATOM   69   C  CG  . GLU   A 1 14  ? -30.518 -7.656  -12.772 1.00 49.62  ?  170 GLU   A CG  1 
ATOM   70   C  CD  . GLU   A 1 14  ? -30.883 -8.156  -14.209 1.00 63.33  ?  170 GLU   A CD  1 
ATOM   71   O  OE1 . GLU   A 1 14  ? -29.987 -8.578  -14.990 1.00 66.13  ?  170 GLU   A OE1 1 
ATOM   72   O  OE2 . GLU   A 1 14  ? -32.092 -8.151  -14.558 1.00 67.35  -1 170 GLU   A OE2 1 
ATOM   73   N  N   . LYS   A 1 15  ? -26.262 -6.185  -11.947 1.00 44.02  ?  171 LYS   A N   1 
ATOM   74   C  CA  . LYS   A 1 15  ? -24.813 -6.303  -11.792 1.00 49.12  ?  171 LYS   A CA  1 
ATOM   75   C  C   . LYS   A 1 15  ? -24.345 -5.770  -10.441 1.00 50.89  ?  171 LYS   A C   1 
ATOM   76   O  O   . LYS   A 1 15  ? -23.540 -6.412  -9.751  1.00 53.37  ?  171 LYS   A O   1 
ATOM   77   C  CB  . LYS   A 1 15  ? -24.117 -5.550  -12.931 1.00 52.43  ?  171 LYS   A CB  1 
ATOM   78   C  CG  . LYS   A 1 15  ? -22.618 -5.355  -12.770 1.00 54.28  ?  171 LYS   A CG  1 
ATOM   79   C  CD  . LYS   A 1 15  ? -22.004 -4.714  -14.019 1.00 55.82  ?  171 LYS   A CD  1 
ATOM   80   C  CE  . LYS   A 1 15  ? -22.186 -3.189  -14.012 1.00 51.81  ?  171 LYS   A CE  1 
ATOM   81   N  NZ  . LYS   A 1 15  ? -22.595 -2.631  -15.359 1.00 63.66  ?  171 LYS   A NZ  1 
ATOM   82   N  N   . LEU   A 1 16  ? -24.847 -4.603  -10.040 1.00 43.25  ?  172 LEU   A N   1 
ATOM   83   C  CA  . LEU   A 1 16  ? -24.396 -4.007  -8.790  1.00 53.59  ?  172 LEU   A CA  1 
ATOM   84   C  C   . LEU   A 1 16  ? -24.752 -4.887  -7.602  1.00 51.23  ?  172 LEU   A C   1 
ATOM   85   O  O   . LEU   A 1 16  ? -23.985 -4.978  -6.638  1.00 57.31  ?  172 LEU   A O   1 
ATOM   86   C  CB  . LEU   A 1 16  ? -24.992 -2.609  -8.622  1.00 48.71  ?  172 LEU   A CB  1 
ATOM   87   C  CG  . LEU   A 1 16  ? -24.472 -1.630  -9.678  1.00 54.01  ?  172 LEU   A CG  1 
ATOM   88   C  CD1 . LEU   A 1 16  ? -25.209 -0.283  -9.607  1.00 45.34  ?  172 LEU   A CD1 1 
ATOM   89   C  CD2 . LEU   A 1 16  ? -22.966 -1.461  -9.539  1.00 51.55  ?  172 LEU   A CD2 1 
ATOM   90   N  N   . LYS   A 1 17  ? -25.913 -5.550  -7.662  1.00 57.24  ?  173 LYS   A N   1 
ATOM   91   C  CA  . LYS   A 1 17  ? -26.328 -6.438  -6.579  1.00 53.72  ?  173 LYS   A CA  1 
ATOM   92   C  C   . LYS   A 1 17  ? -25.438 -7.678  -6.513  1.00 57.12  ?  173 LYS   A C   1 
ATOM   93   O  O   . LYS   A 1 17  ? -25.066 -8.127  -5.424  1.00 59.62  ?  173 LYS   A O   1 
ATOM   94   C  CB  . LYS   A 1 17  ? -27.795 -6.837  -6.758  1.00 48.95  ?  173 LYS   A CB  1 
ATOM   95   N  N   . LEU   A 1 18  ? -25.078 -8.235  -7.669  1.00 53.37  ?  174 LEU   A N   1 
ATOM   96   C  CA  . LEU   A 1 18  ? -24.140 -9.353  -7.689  1.00 54.17  ?  174 LEU   A CA  1 
ATOM   97   C  C   . LEU   A 1 18  ? -22.831 -8.992  -7.008  1.00 59.82  ?  174 LEU   A C   1 
ATOM   98   O  O   . LEU   A 1 18  ? -22.323 -9.752  -6.168  1.00 61.60  ?  174 LEU   A O   1 
ATOM   99   C  CB  . LEU   A 1 18  ? -23.880 -9.785  -9.125  1.00 53.39  ?  174 LEU   A CB  1 
ATOM   100  C  CG  . LEU   A 1 18  ? -24.632 -11.020 -9.600  1.00 63.70  ?  174 LEU   A CG  1 
ATOM   101  C  CD1 . LEU   A 1 18  ? -26.095 -11.003 -9.150  1.00 57.19  ?  174 LEU   A CD1 1 
ATOM   102  C  CD2 . LEU   A 1 18  ? -24.500 -11.134 -11.110 1.00 46.65  ?  174 LEU   A CD2 1 
ATOM   103  N  N   . SER   A 1 19  ? -22.245 -7.844  -7.390  1.00 59.57  ?  175 SER   A N   1 
ATOM   104  C  CA  . SER   A 1 19  ? -20.992 -7.393  -6.796  1.00 61.38  ?  175 SER   A CA  1 
ATOM   105  C  C   . SER   A 1 19  ? -21.082 -7.294  -5.282  1.00 59.66  ?  175 SER   A C   1 
ATOM   106  O  O   . SER   A 1 19  ? -20.101 -7.573  -4.585  1.00 64.64  ?  175 SER   A O   1 
ATOM   107  C  CB  . SER   A 1 19  ? -20.573 -6.035  -7.381  1.00 58.21  ?  175 SER   A CB  1 
ATOM   108  O  OG  . SER   A 1 19  ? -19.753 -6.189  -8.529  1.00 63.97  ?  175 SER   A OG  1 
ATOM   109  N  N   . ARG   A 1 20  ? -22.253 -6.910  -4.751  1.00 59.12  ?  176 ARG   A N   1 
ATOM   110  C  CA  . ARG   A 1 20  ? -22.429 -6.797  -3.312  1.00 58.87  ?  176 ARG   A CA  1 
ATOM   111  C  C   . ARG   A 1 20  ? -22.560 -8.165  -2.641  1.00 62.22  ?  176 ARG   A C   1 
ATOM   112  O  O   . ARG   A 1 20  ? -22.092 -8.344  -1.509  1.00 70.23  ?  176 ARG   A O   1 
ATOM   113  C  CB  . ARG   A 1 20  ? -23.651 -5.925  -3.006  1.00 52.71  ?  176 ARG   A CB  1 
ATOM   114  N  N   . ASP   A 1 21  ? -23.176 -9.138  -3.321  1.00 60.97  ?  177 ASP   A N   1 
ATOM   115  C  CA  . ASP   A 1 21  ? -23.238 -10.493 -2.766  1.00 58.57  ?  177 ASP   A CA  1 
ATOM   116  C  C   . ASP   A 1 21  ? -21.855 -11.080 -2.572  1.00 59.90  ?  177 ASP   A C   1 
ATOM   117  O  O   . ASP   A 1 21  ? -21.630 -11.822 -1.605  1.00 71.26  ?  177 ASP   A O   1 
ATOM   118  C  CB  . ASP   A 1 21  ? -24.038 -11.417 -3.684  1.00 59.88  ?  177 ASP   A CB  1 
ATOM   119  C  CG  . ASP   A 1 21  ? -25.493 -11.028 -3.779  1.00 67.82  ?  177 ASP   A CG  1 
ATOM   120  O  OD1 . ASP   A 1 21  ? -26.094 -10.736 -2.722  1.00 72.71  ?  177 ASP   A OD1 1 
ATOM   121  O  OD2 . ASP   A 1 21  ? -26.018 -11.005 -4.919  1.00 71.79  -1 177 ASP   A OD2 1 
ATOM   122  N  N   . ASP   A 1 22  ? -20.931 -10.794 -3.496  1.00 62.48  ?  178 ASP   A N   1 
ATOM   123  C  CA  . ASP   A 1 22  ? -19.610 -11.398 -3.523  1.00 64.56  ?  178 ASP   A CA  1 
ATOM   124  C  C   . ASP   A 1 22  ? -18.558 -10.578 -2.769  1.00 63.66  ?  178 ASP   A C   1 
ATOM   125  O  O   . ASP   A 1 22  ? -17.360 -10.730 -3.036  1.00 64.30  ?  178 ASP   A O   1 
ATOM   126  C  CB  . ASP   A 1 22  ? -19.183 -11.623 -4.979  1.00 63.35  ?  178 ASP   A CB  1 
ATOM   127  N  N   . ILE   A 1 23  ? -18.981 -9.724  -1.833  1.00 62.62  ?  179 ILE   A N   1 
ATOM   128  C  CA  . ILE   A 1 23  ? -18.046 -8.885  -1.088  1.00 60.64  ?  179 ILE   A CA  1 
ATOM   129  C  C   . ILE   A 1 23  ? -18.250 -9.051  0.410   1.00 64.93  ?  179 ILE   A C   1 
ATOM   130  O  O   . ILE   A 1 23  ? -17.432 -8.570  1.202   1.00 67.79  ?  179 ILE   A O   1 
ATOM   131  C  CB  . ILE   A 1 23  ? -18.175 -7.406  -1.485  1.00 55.80  ?  179 ILE   A CB  1 
ATOM   132  N  N   . SER   A 1 24  ? -19.351 -9.714  0.808   1.00 57.95  ?  180 SER   A N   1 
ATOM   133  C  CA  . SER   A 1 24  ? -19.589 -10.044 2.217   1.00 59.56  ?  180 SER   A CA  1 
ATOM   134  C  C   . SER   A 1 24  ? -18.322 -10.515 2.915   1.00 59.41  ?  180 SER   A C   1 
ATOM   135  O  O   . SER   A 1 24  ? -18.006 -10.088 4.038   1.00 59.36  ?  180 SER   A O   1 
ATOM   136  C  CB  . SER   A 1 24  ? -20.664 -11.145 2.313   1.00 59.66  ?  180 SER   A CB  1 
ATOM   137  N  N   . THR   A 1 25  ? -17.574 -11.404 2.244   1.00 56.41  ?  181 THR   A N   1 
ATOM   138  C  CA  . THR   A 1 25  ? -16.320 -11.908 2.784   1.00 55.36  ?  181 THR   A CA  1 
ATOM   139  C  C   . THR   A 1 25  ? -15.341 -10.786 3.082   1.00 59.23  ?  181 THR   A C   1 
ATOM   140  O  O   . THR   A 1 25  ? -14.737 -10.751 4.163   1.00 56.80  ?  181 THR   A O   1 
ATOM   141  C  CB  . THR   A 1 25  ? -15.704 -12.903 1.815   1.00 53.34  ?  181 THR   A CB  1 
ATOM   142  O  OG1 . THR   A 1 25  ? -16.581 -14.027 1.722   1.00 67.22  ?  181 THR   A OG1 1 
ATOM   143  C  CG2 . THR   A 1 25  ? -14.365 -13.344 2.308   1.00 57.17  ?  181 THR   A CG2 1 
ATOM   144  N  N   . ALA   A 1 26  ? -15.159 -9.864  2.131   1.00 55.49  ?  182 ALA   A N   1 
ATOM   145  C  CA  . ALA   A 1 26  ? -14.255 -8.743  2.359   1.00 54.63  ?  182 ALA   A CA  1 
ATOM   146  C  C   . ALA   A 1 26  ? -14.692 -7.934  3.568   1.00 48.36  ?  182 ALA   A C   1 
ATOM   147  O  O   . ALA   A 1 26  ? -13.870 -7.566  4.410   1.00 48.75  ?  182 ALA   A O   1 
ATOM   148  C  CB  . ALA   A 1 26  ? -14.187 -7.868  1.110   1.00 52.86  ?  182 ALA   A CB  1 
ATOM   149  N  N   . ALA   A 1 27  ? -15.998 -7.643  3.669   1.00 43.41  ?  183 ALA   A N   1 
ATOM   150  C  CA  . ALA   A 1 27  ? -16.492 -6.884  4.811   1.00 50.09  ?  183 ALA   A CA  1 
ATOM   151  C  C   . ALA   A 1 27  ? -16.173 -7.592  6.119   1.00 50.53  ?  183 ALA   A C   1 
ATOM   152  O  O   . ALA   A 1 27  ? -15.960 -6.933  7.142   1.00 51.65  ?  183 ALA   A O   1 
ATOM   153  C  CB  . ALA   A 1 27  ? -17.995 -6.650  4.687   1.00 47.93  ?  183 ALA   A CB  1 
ATOM   154  N  N   . GLY   A 1 28  ? -16.126 -8.927  6.099   1.00 46.89  ?  184 GLY   A N   1 
ATOM   155  C  CA  . GLY   A 1 28  ? -15.698 -9.660  7.279   1.00 47.00  ?  184 GLY   A CA  1 
ATOM   156  C  C   . GLY   A 1 28  ? -14.256 -9.372  7.647   1.00 45.39  ?  184 GLY   A C   1 
ATOM   157  O  O   . GLY   A 1 28  ? -13.934 -9.166  8.821   1.00 58.42  ?  184 GLY   A O   1 
ATOM   158  N  N   . MET   A 1 29  ? -13.362 -9.384  6.654   1.00 42.49  ?  185 MET   A N   1 
ATOM   159  C  CA  . MET   A 1 29  ? -11.967 -9.018  6.904   1.00 49.21  ?  185 MET   A CA  1 
ATOM   160  C  C   . MET   A 1 29  ? -11.869 -7.620  7.508   1.00 51.11  ?  185 MET   A C   1 
ATOM   161  O  O   . MET   A 1 29  ? -11.129 -7.391  8.476   1.00 43.64  ?  185 MET   A O   1 
ATOM   162  C  CB  . MET   A 1 29  ? -11.153 -9.092  5.608   1.00 44.23  ?  185 MET   A CB  1 
ATOM   163  C  CG  . MET   A 1 29  ? -10.981 -10.471 4.976   1.00 46.12  ?  185 MET   A CG  1 
ATOM   164  S  SD  . MET   A 1 29  ? -10.410 -11.920 5.908   1.00 83.15  ?  185 MET   A SD  1 
ATOM   165  C  CE  . MET   A 1 29  ? -9.628  -11.299 7.409   1.00 62.49  ?  185 MET   A CE  1 
ATOM   166  N  N   . VAL   A 1 30  ? -12.615 -6.673  6.942   1.00 45.42  ?  186 VAL   A N   1 
ATOM   167  C  CA  . VAL   A 1 30  ? -12.580 -5.297  7.428   1.00 45.77  ?  186 VAL   A CA  1 
ATOM   168  C  C   . VAL   A 1 30  ? -13.042 -5.229  8.877   1.00 44.82  ?  186 VAL   A C   1 
ATOM   169  O  O   . VAL   A 1 30  ? -12.401 -4.591  9.720   1.00 50.08  ?  186 VAL   A O   1 
ATOM   170  C  CB  . VAL   A 1 30  ? -13.427 -4.385  6.520   1.00 41.37  ?  186 VAL   A CB  1 
ATOM   171  C  CG1 . VAL   A 1 30  ? -13.548 -2.995  7.129   1.00 43.77  ?  186 VAL   A CG1 1 
ATOM   172  C  CG2 . VAL   A 1 30  ? -12.795 -4.316  5.160   1.00 45.18  ?  186 VAL   A CG2 1 
ATOM   173  N  N   . LYS   A 1 31  ? -14.157 -5.895  9.191   1.00 48.53  ?  187 LYS   A N   1 
ATOM   174  C  CA  . LYS   A 1 31  ? -14.680 -5.837  10.552  1.00 47.77  ?  187 LYS   A CA  1 
ATOM   175  C  C   . LYS   A 1 31  ? -13.668 -6.368  11.553  1.00 48.69  ?  187 LYS   A C   1 
ATOM   176  O  O   . LYS   A 1 31  ? -13.597 -5.885  12.687  1.00 55.25  ?  187 LYS   A O   1 
ATOM   177  C  CB  . LYS   A 1 31  ? -15.980 -6.625  10.679  1.00 46.52  ?  187 LYS   A CB  1 
ATOM   178  C  CG  . LYS   A 1 31  ? -16.970 -5.933  11.592  1.00 56.35  ?  187 LYS   A CG  1 
ATOM   179  C  CD  . LYS   A 1 31  ? -17.656 -6.893  12.551  1.00 53.96  ?  187 LYS   A CD  1 
ATOM   180  C  CE  . LYS   A 1 31  ? -18.659 -6.134  13.420  1.00 62.10  ?  187 LYS   A CE  1 
ATOM   181  N  NZ  . LYS   A 1 31  ? -18.092 -4.864  13.988  1.00 60.74  ?  187 LYS   A NZ  1 
ATOM   182  N  N   . GLY   A 1 32  ? -12.876 -7.361  11.153  1.00 44.26  ?  188 GLY   A N   1 
ATOM   183  C  CA  . GLY   A 1 32  ? -11.921 -7.943  12.084  1.00 52.21  ?  188 GLY   A CA  1 
ATOM   184  C  C   . GLY   A 1 32  ? -10.760 -7.010  12.366  1.00 58.79  ?  188 GLY   A C   1 
ATOM   185  O  O   . GLY   A 1 32  ? -10.318 -6.866  13.514  1.00 54.17  ?  188 GLY   A O   1 
ATOM   186  N  N   . VAL   A 1 33  ? -10.234 -6.376  11.315  1.00 49.57  ?  189 VAL   A N   1 
ATOM   187  C  CA  . VAL   A 1 33  ? -9.189  -5.371  11.504  1.00 51.34  ?  189 VAL   A CA  1 
ATOM   188  C  C   . VAL   A 1 33  ? -9.719  -4.207  12.326  1.00 49.04  ?  189 VAL   A C   1 
ATOM   189  O  O   . VAL   A 1 33  ? -9.114  -3.802  13.328  1.00 54.35  ?  189 VAL   A O   1 
ATOM   190  C  CB  . VAL   A 1 33  ? -8.641  -4.910  10.144  1.00 48.94  ?  189 VAL   A CB  1 
ATOM   191  C  CG1 . VAL   A 1 33  ? -7.771  -3.684  10.301  1.00 51.30  ?  189 VAL   A CG1 1 
ATOM   192  C  CG2 . VAL   A 1 33  ? -7.843  -6.034  9.536   1.00 47.87  ?  189 VAL   A CG2 1 
ATOM   193  N  N   . VAL   A 1 34  ? -10.882 -3.688  11.938  1.00 42.64  ?  190 VAL   A N   1 
ATOM   194  C  CA  . VAL   A 1 34  ? -11.444 -2.506  12.580  1.00 53.15  ?  190 VAL   A CA  1 
ATOM   195  C  C   . VAL   A 1 34  ? -11.755 -2.776  14.046  1.00 53.48  ?  190 VAL   A C   1 
ATOM   196  O  O   . VAL   A 1 34  ? -11.514 -1.924  14.909  1.00 51.87  ?  190 VAL   A O   1 
ATOM   197  C  CB  . VAL   A 1 34  ? -12.689 -2.040  11.808  1.00 47.19  ?  190 VAL   A CB  1 
ATOM   198  C  CG1 . VAL   A 1 34  ? -13.470 -1.015  12.613  1.00 43.50  ?  190 VAL   A CG1 1 
ATOM   199  C  CG2 . VAL   A 1 34  ? -12.267 -1.473  10.471  1.00 48.49  ?  190 VAL   A CG2 1 
ATOM   200  N  N   . ASP   A 1 35  ? -12.301 -3.952  14.354  1.00 52.28  ?  191 ASP   A N   1 
ATOM   201  C  CA  . ASP   A 1 35  ? -12.550 -4.285  15.753  1.00 51.93  ?  191 ASP   A CA  1 
ATOM   202  C  C   . ASP   A 1 35  ? -11.242 -4.311  16.543  1.00 48.97  ?  191 ASP   A C   1 
ATOM   203  O  O   . ASP   A 1 35  ? -11.179 -3.772  17.649  1.00 59.79  ?  191 ASP   A O   1 
ATOM   204  C  CB  . ASP   A 1 35  ? -13.284 -5.621  15.863  1.00 50.87  ?  191 ASP   A CB  1 
ATOM   205  C  CG  . ASP   A 1 35  ? -14.745 -5.537  15.420  1.00 53.84  ?  191 ASP   A CG  1 
ATOM   206  O  OD1 . ASP   A 1 35  ? -15.292 -4.424  15.243  1.00 57.87  ?  191 ASP   A OD1 1 
ATOM   207  O  OD2 . ASP   A 1 35  ? -15.351 -6.613  15.234  1.00 64.15  -1 191 ASP   A OD2 1 
ATOM   208  N  N   . HIS   A 1 36  ? -10.186 -4.927  15.987  1.00 54.76  ?  192 HIS   A N   1 
ATOM   209  C  CA  . HIS   A 1 36  ? -8.857  -4.886  16.612  1.00 56.65  ?  192 HIS   A CA  1 
ATOM   210  C  C   . HIS   A 1 36  ? -8.392  -3.462  16.883  1.00 61.09  ?  192 HIS   A C   1 
ATOM   211  O  O   . HIS   A 1 36  ? -7.921  -3.143  17.986  1.00 55.83  ?  192 HIS   A O   1 
ATOM   212  C  CB  . HIS   A 1 36  ? -7.801  -5.579  15.740  1.00 61.92  ?  192 HIS   A CB  1 
ATOM   213  C  CG  . HIS   A 1 36  ? -7.652  -7.053  15.963  1.00 66.10  ?  192 HIS   A CG  1 
ATOM   214  N  ND1 . HIS   A 1 36  ? -7.450  -7.944  14.928  1.00 66.88  ?  192 HIS   A ND1 1 
ATOM   215  C  CD2 . HIS   A 1 36  ? -7.542  -7.776  17.105  1.00 68.55  ?  192 HIS   A CD2 1 
ATOM   216  C  CE1 . HIS   A 1 36  ? -7.284  -9.161  15.420  1.00 68.00  ?  192 HIS   A CE1 1 
ATOM   217  N  NE2 . HIS   A 1 36  ? -7.336  -9.087  16.740  1.00 66.87  ?  192 HIS   A NE2 1 
ATOM   218  N  N   . LEU   A 1 37  ? -8.423  -2.619  15.846  1.00 49.83  ?  193 LEU   A N   1 
ATOM   219  C  CA  . LEU   A 1 37  ? -7.995  -1.232  15.986  1.00 54.29  ?  193 LEU   A CA  1 
ATOM   220  C  C   . LEU   A 1 37  ? -8.727  -0.546  17.127  1.00 48.85  ?  193 LEU   A C   1 
ATOM   221  O  O   . LEU   A 1 37  ? -8.104  0.073   17.993  1.00 51.64  ?  193 LEU   A O   1 
ATOM   222  C  CB  . LEU   A 1 37  ? -8.225  -0.475  14.675  1.00 47.87  ?  193 LEU   A CB  1 
ATOM   223  C  CG  . LEU   A 1 37  ? -7.066  -0.492  13.687  1.00 50.25  ?  193 LEU   A CG  1 
ATOM   224  C  CD1 . LEU   A 1 37  ? -7.347  0.409   12.493  1.00 52.86  ?  193 LEU   A CD1 1 
ATOM   225  C  CD2 . LEU   A 1 37  ? -5.811  -0.043  14.410  1.00 57.12  ?  193 LEU   A CD2 1 
ATOM   226  N  N   . LEU   A 1 38  ? -10.055 -0.665  17.150  1.00 44.61  ?  194 LEU   A N   1 
ATOM   227  C  CA  . LEU   A 1 38  ? -10.850 0.021   18.163  1.00 45.66  ?  194 LEU   A CA  1 
ATOM   228  C  C   . LEU   A 1 38  ? -10.511 -0.449  19.575  1.00 50.37  ?  194 LEU   A C   1 
ATOM   229  O  O   . LEU   A 1 38  ? -10.568 0.345   20.522  1.00 47.84  ?  194 LEU   A O   1 
ATOM   230  C  CB  . LEU   A 1 38  ? -12.336 -0.169  17.882  1.00 42.76  ?  194 LEU   A CB  1 
ATOM   231  C  CG  . LEU   A 1 38  ? -12.857 0.578   16.636  1.00 51.89  ?  194 LEU   A CG  1 
ATOM   232  C  CD1 . LEU   A 1 38  ? -14.284 0.150   16.297  1.00 39.38  ?  194 LEU   A CD1 1 
ATOM   233  C  CD2 . LEU   A 1 38  ? -12.774 2.091   16.821  1.00 41.30  ?  194 LEU   A CD2 1 
ATOM   234  N  N   . LEU   A 1 39  ? -10.170 -1.731  19.753  1.00 51.15  ?  195 LEU   A N   1 
ATOM   235  C  CA  . LEU   A 1 39  ? -9.784  -2.167  21.098  1.00 51.58  ?  195 LEU   A CA  1 
ATOM   236  C  C   . LEU   A 1 39  ? -8.484  -1.510  21.541  1.00 52.59  ?  195 LEU   A C   1 
ATOM   237  O  O   . LEU   A 1 39  ? -8.381  -1.020  22.670  1.00 57.79  ?  195 LEU   A O   1 
ATOM   238  C  CB  . LEU   A 1 39  ? -9.669  -3.693  21.197  1.00 56.80  ?  195 LEU   A CB  1 
ATOM   239  C  CG  . LEU   A 1 39  ? -10.813 -4.635  20.811  1.00 62.60  ?  195 LEU   A CG  1 
ATOM   240  C  CD1 . LEU   A 1 39  ? -10.303 -5.704  19.852  1.00 63.76  ?  195 LEU   A CD1 1 
ATOM   241  C  CD2 . LEU   A 1 39  ? -11.406 -5.300  22.064  1.00 67.69  ?  195 LEU   A CD2 1 
ATOM   242  N  N   . ARG   A 1 40  ? -7.469  -1.498  20.675  1.00 52.84  ?  196 ARG   A N   1 
ATOM   243  C  CA  . ARG   A 1 40  ? -6.218  -0.834  21.030  1.00 53.45  ?  196 ARG   A CA  1 
ATOM   244  C  C   . ARG   A 1 40  ? -6.438  0.655   21.318  1.00 53.78  ?  196 ARG   A C   1 
ATOM   245  O  O   . ARG   A 1 40  ? -5.996  1.166   22.355  1.00 56.19  ?  196 ARG   A O   1 
ATOM   246  C  CB  . ARG   A 1 40  ? -5.180  -1.027  19.924  1.00 51.98  ?  196 ARG   A CB  1 
ATOM   247  N  N   . LEU   A 1 41  ? -7.135  1.362   20.414  1.00 49.52  ?  197 LEU   A N   1 
ATOM   248  C  CA  . LEU   A 1 41  ? -7.387  2.797   20.585  1.00 50.62  ?  197 LEU   A CA  1 
ATOM   249  C  C   . LEU   A 1 41  ? -8.120  3.118   21.884  1.00 49.27  ?  197 LEU   A C   1 
ATOM   250  O  O   . LEU   A 1 41  ? -7.850  4.151   22.507  1.00 52.46  ?  197 LEU   A O   1 
ATOM   251  C  CB  . LEU   A 1 41  ? -8.189  3.362   19.406  1.00 46.81  ?  197 LEU   A CB  1 
ATOM   252  C  CG  . LEU   A 1 41  ? -7.510  3.773   18.093  1.00 59.05  ?  197 LEU   A CG  1 
ATOM   253  C  CD1 . LEU   A 1 41  ? -6.682  5.032   18.322  1.00 53.98  ?  197 LEU   A CD1 1 
ATOM   254  C  CD2 . LEU   A 1 41  ? -6.626  2.681   17.552  1.00 59.66  ?  197 LEU   A CD2 1 
ATOM   255  N  N   . LYS   A 1 42  ? -9.081  2.283   22.285  1.00 44.99  ?  198 LYS   A N   1 
ATOM   256  C  CA  . LYS   A 1 42  ? -9.816  2.588   23.509  1.00 47.45  ?  198 LYS   A CA  1 
ATOM   257  C  C   . LYS   A 1 42  ? -8.943  2.544   24.766  1.00 51.63  ?  198 LYS   A C   1 
ATOM   258  O  O   . LYS   A 1 42  ? -9.416  2.986   25.818  1.00 49.73  ?  198 LYS   A O   1 
ATOM   259  C  CB  . LYS   A 1 42  ? -11.018 1.651   23.702  1.00 43.01  ?  198 LYS   A CB  1 
ATOM   260  C  CG  . LYS   A 1 42  ? -10.648 0.210   23.947  1.00 56.96  ?  198 LYS   A CG  1 
ATOM   261  C  CD  . LYS   A 1 42  ? -11.620 -0.533  24.865  1.00 64.37  ?  198 LYS   A CD  1 
ATOM   262  C  CE  . LYS   A 1 42  ? -11.299 -0.214  26.347  1.00 56.18  ?  198 LYS   A CE  1 
ATOM   263  N  NZ  . LYS   A 1 42  ? -10.109 -0.923  26.898  1.00 63.74  ?  198 LYS   A NZ  1 
ATOM   264  N  N   . CYS   A 1 43  ? -7.703  2.035   24.687  1.00 47.48  ?  199 CYS   A N   1 
ATOM   265  C  CA  . CYS   A 1 43  ? -6.803  2.024   25.845  1.00 51.39  ?  199 CYS   A CA  1 
ATOM   266  C  C   . CYS   A 1 43  ? -6.020  3.316   25.994  1.00 55.86  ?  199 CYS   A C   1 
ATOM   267  O  O   . CYS   A 1 43  ? -5.455  3.568   27.071  1.00 58.57  ?  199 CYS   A O   1 
ATOM   268  C  CB  . CYS   A 1 43  ? -5.795  0.871   25.763  1.00 51.15  ?  199 CYS   A CB  1 
ATOM   269  S  SG  . CYS   A 1 43  ? -6.526  -0.766  25.860  1.00 62.20  ?  199 CYS   A SG  1 
ATOM   270  N  N   . ASP   A 1 44  ? -5.928  4.105   24.927  1.00 49.63  ?  200 ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 44  ? -5.323  5.427   24.990  1.00 56.88  ?  200 ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 44  ? -6.278  6.381   25.694  1.00 55.05  ?  200 ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 44  ? -7.481  6.381   25.419  1.00 48.42  ?  200 ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 44  ? -4.968  5.908   23.583  1.00 51.47  ?  200 ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 44  ? -4.113  7.165   23.579  1.00 60.89  ?  200 ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 44  ? -4.586  8.210   24.078  1.00 61.63  ?  200 ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 44  ? -2.949  7.097   23.125  1.00 62.21  -1 200 ASP   A OD2 1 
ATOM   278  N  N   . SER   A 1 45  ? -5.745  7.164   26.644  1.00 50.45  ?  201 SER   A N   1 
ATOM   279  C  CA  . SER   A 1 45  ? -6.618  8.059   27.400  1.00 54.46  ?  201 SER   A CA  1 
ATOM   280  C  C   . SER   A 1 45  ? -7.294  9.089   26.492  1.00 51.61  ?  201 SER   A C   1 
ATOM   281  O  O   . SER   A 1 45  ? -8.432  9.487   26.754  1.00 50.82  ?  201 SER   A O   1 
ATOM   282  C  CB  . SER   A 1 45  ? -5.835  8.740   28.530  1.00 52.03  ?  201 SER   A CB  1 
ATOM   283  O  OG  . SER   A 1 45  ? -4.865  9.628   28.014  1.00 52.68  ?  201 SER   A OG  1 
ATOM   284  N  N   . ALA   A 1 46  ? -6.628  9.520   25.420  1.00 48.35  ?  202 ALA   A N   1 
ATOM   285  C  CA  . ALA   A 1 46  ? -7.258  10.493  24.528  1.00 56.12  ?  202 ALA   A CA  1 
ATOM   286  C  C   . ALA   A 1 46  ? -8.458  9.895   23.802  1.00 55.42  ?  202 ALA   A C   1 
ATOM   287  O  O   . ALA   A 1 46  ? -9.454  10.591  23.556  1.00 50.33  ?  202 ALA   A O   1 
ATOM   288  C  CB  . ALA   A 1 46  ? -6.240  11.034  23.522  1.00 56.35  ?  202 ALA   A CB  1 
ATOM   289  N  N   . PHE   A 1 47  ? -8.389  8.609   23.452  1.00 52.31  ?  203 PHE   A N   1 
ATOM   290  C  CA  . PHE   A 1 47  ? -9.373  8.002   22.559  1.00 50.24  ?  203 PHE   A CA  1 
ATOM   291  C  C   . PHE   A 1 47  ? -10.272 7.014   23.294  1.00 53.07  ?  203 PHE   A C   1 
ATOM   292  O  O   . PHE   A 1 47  ? -10.808 6.082   22.686  1.00 50.52  ?  203 PHE   A O   1 
ATOM   293  C  CB  . PHE   A 1 47  ? -8.665  7.327   21.385  1.00 49.48  ?  203 PHE   A CB  1 
ATOM   294  C  CG  . PHE   A 1 47  ? -7.994  8.304   20.447  1.00 50.90  ?  203 PHE   A CG  1 
ATOM   295  C  CD1 . PHE   A 1 47  ? -8.744  9.074   19.577  1.00 49.79  ?  203 PHE   A CD1 1 
ATOM   296  C  CD2 . PHE   A 1 47  ? -6.615  8.469   20.466  1.00 60.83  ?  203 PHE   A CD2 1 
ATOM   297  C  CE1 . PHE   A 1 47  ? -8.133  9.981   18.726  1.00 54.67  ?  203 PHE   A CE1 1 
ATOM   298  C  CE2 . PHE   A 1 47  ? -5.994  9.376   19.612  1.00 63.26  ?  203 PHE   A CE2 1 
ATOM   299  C  CZ  . PHE   A 1 47  ? -6.754  10.126  18.740  1.00 46.65  ?  203 PHE   A CZ  1 
ATOM   300  N  N   . ARG   A 1 48  ? -10.453 7.227   24.604  1.00 53.66  ?  204 ARG   A N   1 
ATOM   301  C  CA  . ARG   A 1 48  ? -11.132 6.244   25.446  1.00 52.87  ?  204 ARG   A CA  1 
ATOM   302  C  C   . ARG   A 1 48  ? -12.532 5.937   24.945  1.00 47.42  ?  204 ARG   A C   1 
ATOM   303  O  O   . ARG   A 1 48  ? -12.994 4.796   25.048  1.00 46.88  ?  204 ARG   A O   1 
ATOM   304  C  CB  . ARG   A 1 48  ? -11.195 6.738   26.894  1.00 53.10  ?  204 ARG   A CB  1 
ATOM   305  N  N   . GLY   A 1 49  ? -13.232 6.942   24.430  1.00 44.29  ?  205 GLY   A N   1 
ATOM   306  C  CA  . GLY   A 1 49  ? -14.600 6.750   23.998  1.00 51.43  ?  205 GLY   A CA  1 
ATOM   307  C  C   . GLY   A 1 49  ? -14.731 6.607   22.499  1.00 47.43  ?  205 GLY   A C   1 
ATOM   308  O  O   . GLY   A 1 49  ? -15.759 6.966   21.922  1.00 44.10  ?  205 GLY   A O   1 
ATOM   309  N  N   . VAL   A 1 50  ? -13.690 6.082   21.856  1.00 44.65  ?  206 VAL   A N   1 
ATOM   310  C  CA  . VAL   A 1 50  ? -13.737 5.890   20.419  1.00 42.63  ?  206 VAL   A CA  1 
ATOM   311  C  C   . VAL   A 1 50  ? -14.670 4.728   20.108  1.00 46.63  ?  206 VAL   A C   1 
ATOM   312  O  O   . VAL   A 1 50  ? -14.755 3.749   20.868  1.00 43.18  ?  206 VAL   A O   1 
ATOM   313  C  CB  . VAL   A 1 50  ? -12.332 5.642   19.849  1.00 38.48  ?  206 VAL   A CB  1 
ATOM   314  C  CG1 . VAL   A 1 50  ? -11.860 4.266   20.218  1.00 43.65  ?  206 VAL   A CG1 1 
ATOM   315  C  CG2 . VAL   A 1 50  ? -12.336 5.836   18.336  1.00 46.83  ?  206 VAL   A CG2 1 
ATOM   316  N  N   . GLY   A 1 51  ? -15.371 4.832   18.984  1.00 40.87  ?  207 GLY   A N   1 
ATOM   317  C  CA  . GLY   A 1 51  ? -16.297 3.793   18.576  1.00 37.47  ?  207 GLY   A CA  1 
ATOM   318  C  C   . GLY   A 1 51  ? -16.641 3.952   17.114  1.00 43.39  ?  207 GLY   A C   1 
ATOM   319  O  O   . GLY   A 1 51  ? -16.253 4.922   16.456  1.00 38.67  ?  207 GLY   A O   1 
ATOM   320  N  N   . LEU   A 1 52  ? -17.375 2.970   16.608  1.00 40.86  ?  208 LEU   A N   1 
ATOM   321  C  CA  . LEU   A 1 52  ? -17.945 3.078   15.273  1.00 44.40  ?  208 LEU   A CA  1 
ATOM   322  C  C   . LEU   A 1 52  ? -19.157 3.975   15.327  1.00 47.67  ?  208 LEU   A C   1 
ATOM   323  O  O   . LEU   A 1 52  ? -19.914 3.961   16.303  1.00 56.80  ?  208 LEU   A O   1 
ATOM   324  C  CB  . LEU   A 1 52  ? -18.347 1.713   14.728  1.00 40.78  ?  208 LEU   A CB  1 
ATOM   325  C  CG  . LEU   A 1 52  ? -17.179 0.957   14.121  1.00 51.16  ?  208 LEU   A CG  1 
ATOM   326  C  CD1 . LEU   A 1 52  ? -17.676 -0.252  13.331  1.00 60.52  ?  208 LEU   A CD1 1 
ATOM   327  C  CD2 . LEU   A 1 52  ? -16.373 1.892   13.240  1.00 48.76  ?  208 LEU   A CD2 1 
ATOM   328  N  N   . LEU   A 1 53  ? -19.336 4.775   14.282  1.00 50.80  ?  209 LEU   A N   1 
ATOM   329  C  CA  . LEU   A 1 53  ? -20.527 5.609   14.233  1.00 43.79  ?  209 LEU   A CA  1 
ATOM   330  C  C   . LEU   A 1 53  ? -21.761 4.757   13.951  1.00 62.77  ?  209 LEU   A C   1 
ATOM   331  O  O   . LEU   A 1 53  ? -22.670 4.667   14.792  1.00 64.41  ?  209 LEU   A O   1 
ATOM   332  C  CB  . LEU   A 1 53  ? -20.336 6.733   13.212  1.00 43.38  ?  209 LEU   A CB  1 
ATOM   333  C  CG  . LEU   A 1 53  ? -21.586 7.590   13.040  1.00 48.88  ?  209 LEU   A CG  1 
ATOM   334  C  CD1 . LEU   A 1 53  ? -22.074 7.945   14.396  1.00 54.71  ?  209 LEU   A CD1 1 
ATOM   335  C  CD2 . LEU   A 1 53  ? -21.284 8.864   12.276  1.00 41.94  ?  209 LEU   A CD2 1 
ATOM   336  N  N   . ASN   A 1 54  ? -21.791 4.083   12.799  1.00 61.30  ?  210 ASN   A N   1 
ATOM   337  C  CA  . ASN   A 1 54  ? -22.944 3.253   12.446  1.00 64.21  ?  210 ASN   A CA  1 
ATOM   338  C  C   . ASN   A 1 54  ? -22.843 1.870   13.083  1.00 64.46  ?  210 ASN   A C   1 
ATOM   339  O  O   . ASN   A 1 54  ? -23.379 0.895   12.549  1.00 75.25  ?  210 ASN   A O   1 
ATOM   340  C  CB  . ASN   A 1 54  ? -23.080 3.104   10.924  1.00 63.21  ?  210 ASN   A CB  1 
ATOM   341  C  CG  . ASN   A 1 54  ? -23.406 4.416   10.231  1.00 63.40  ?  210 ASN   A CG  1 
ATOM   342  O  OD1 . ASN   A 1 54  ? -24.239 5.205   10.701  1.00 65.56  ?  210 ASN   A OD1 1 
ATOM   343  N  ND2 . ASN   A 1 54  ? -22.735 4.663   9.106   1.00 61.85  ?  210 ASN   A ND2 1 
ATOM   344  N  N   . TYR   A 1 59  ? -19.427 -0.081  8.019   1.00 50.57  ?  215 TYR   A N   1 
ATOM   345  C  CA  . TYR   A 1 59  ? -18.707 0.273   6.792   1.00 53.18  ?  215 TYR   A CA  1 
ATOM   346  C  C   . TYR   A 1 59  ? -19.636 0.892   5.739   1.00 59.50  ?  215 TYR   A C   1 
ATOM   347  O  O   . TYR   A 1 59  ? -20.858 0.798   5.842   1.00 62.24  ?  215 TYR   A O   1 
ATOM   348  C  CB  . TYR   A 1 59  ? -18.005 -0.957  6.204   1.00 61.16  ?  215 TYR   A CB  1 
ATOM   349  C  CG  . TYR   A 1 59  ? -18.959 -1.963  5.586   1.00 62.59  ?  215 TYR   A CG  1 
ATOM   350  C  CD1 . TYR   A 1 59  ? -19.314 -3.115  6.277   1.00 58.37  ?  215 TYR   A CD1 1 
ATOM   351  C  CD2 . TYR   A 1 59  ? -19.454 -1.793  4.295   1.00 60.25  ?  215 TYR   A CD2 1 
ATOM   352  C  CE1 . TYR   A 1 59  ? -20.185 -4.044  5.724   1.00 63.35  ?  215 TYR   A CE1 1 
ATOM   353  C  CE2 . TYR   A 1 59  ? -20.318 -2.718  3.727   1.00 56.22  ?  215 TYR   A CE2 1 
ATOM   354  C  CZ  . TYR   A 1 59  ? -20.681 -3.845  4.446   1.00 62.82  ?  215 TYR   A CZ  1 
ATOM   355  O  OH  . TYR   A 1 59  ? -21.536 -4.771  3.889   1.00 70.93  ?  215 TYR   A OH  1 
ATOM   356  N  N   . GLU   A 1 60  ? -19.037 1.500   4.719   1.00 58.92  ?  216 GLU   A N   1 
ATOM   357  C  CA  . GLU   A 1 60  ? -19.775 2.093   3.613   1.00 57.85  ?  216 GLU   A CA  1 
ATOM   358  C  C   . GLU   A 1 60  ? -18.851 2.127   2.399   1.00 50.90  ?  216 GLU   A C   1 
ATOM   359  O  O   . GLU   A 1 60  ? -17.633 1.932   2.509   1.00 50.20  ?  216 GLU   A O   1 
ATOM   360  C  CB  . GLU   A 1 60  ? -20.288 3.498   3.978   1.00 56.49  ?  216 GLU   A CB  1 
ATOM   361  C  CG  . GLU   A 1 60  ? -21.812 3.641   3.949   1.00 62.11  ?  216 GLU   A CG  1 
ATOM   362  C  CD  . GLU   A 1 60  ? -22.385 3.744   2.534   1.00 72.16  ?  216 GLU   A CD  1 
ATOM   363  O  OE1 . GLU   A 1 60  ? -21.668 3.393   1.557   1.00 71.84  ?  216 GLU   A OE1 1 
ATOM   364  O  OE2 . GLU   A 1 60  ? -23.560 4.169   2.401   1.00 79.23  -1 216 GLU   A OE2 1 
ATOM   365  N  N   . HIS   A 1 61  ? -19.444 2.361   1.222   1.00 53.12  ?  217 HIS   A N   1 
ATOM   366  C  CA  . HIS   A 1 61  ? -18.712 2.404   -0.047  1.00 49.66  ?  217 HIS   A CA  1 
ATOM   367  C  C   . HIS   A 1 61  ? -18.992 3.744   -0.718  1.00 50.94  ?  217 HIS   A C   1 
ATOM   368  O  O   . HIS   A 1 61  ? -20.105 3.968   -1.195  1.00 56.92  ?  217 HIS   A O   1 
ATOM   369  C  CB  . HIS   A 1 61  ? -19.129 1.259   -0.969  1.00 44.05  ?  217 HIS   A CB  1 
ATOM   370  C  CG  . HIS   A 1 61  ? -18.672 -0.084  -0.507  1.00 44.70  ?  217 HIS   A CG  1 
ATOM   371  N  ND1 . HIS   A 1 61  ? -19.418 -0.867  0.354   1.00 53.58  ?  217 HIS   A ND1 1 
ATOM   372  C  CD2 . HIS   A 1 61  ? -17.543 -0.780  -0.772  1.00 49.08  ?  217 HIS   A CD2 1 
ATOM   373  C  CE1 . HIS   A 1 61  ? -18.766 -1.995  0.583   1.00 50.02  ?  217 HIS   A CE1 1 
ATOM   374  N  NE2 . HIS   A 1 61  ? -17.625 -1.968  -0.087  1.00 51.37  ?  217 HIS   A NE2 1 
ATOM   375  N  N   . VAL   A 1 62  ? -17.984 4.632   -0.757  1.00 46.16  ?  218 VAL   A N   1 
ATOM   376  C  CA  . VAL   A 1 62  ? -18.171 5.913   -1.445  1.00 52.46  ?  218 VAL   A CA  1 
ATOM   377  C  C   . VAL   A 1 62  ? -18.326 5.698   -2.949  1.00 51.20  ?  218 VAL   A C   1 
ATOM   378  O  O   . VAL   A 1 62  ? -19.020 6.465   -3.629  1.00 46.09  ?  218 VAL   A O   1 
ATOM   379  C  CB  . VAL   A 1 62  ? -17.009 6.883   -1.125  1.00 51.18  ?  218 VAL   A CB  1 
ATOM   380  C  CG1 . VAL   A 1 62  ? -16.654 6.844   0.361   1.00 45.29  ?  218 VAL   A CG1 1 
ATOM   381  C  CG2 . VAL   A 1 62  ? -15.785 6.582   -1.981  1.00 52.10  ?  218 VAL   A CG2 1 
ATOM   382  N  N   . LYS   A 1 63  ? -17.710 4.641   -3.483  1.00 44.37  ?  219 LYS   A N   1 
ATOM   383  C  CA  . LYS   A 1 63  ? -17.764 4.291   -4.899  1.00 42.97  ?  219 LYS   A CA  1 
ATOM   384  C  C   . LYS   A 1 63  ? -18.548 2.989   -5.057  1.00 48.34  ?  219 LYS   A C   1 
ATOM   385  O  O   . LYS   A 1 63  ? -18.039 1.907   -4.731  1.00 42.40  ?  219 LYS   A O   1 
ATOM   386  C  CB  . LYS   A 1 63  ? -16.358 4.134   -5.471  1.00 44.19  ?  219 LYS   A CB  1 
ATOM   387  C  CG  . LYS   A 1 63  ? -15.650 5.430   -5.792  1.00 55.90  ?  219 LYS   A CG  1 
ATOM   388  C  CD  . LYS   A 1 63  ? -14.765 5.279   -7.028  1.00 53.62  ?  219 LYS   A CD  1 
ATOM   389  C  CE  . LYS   A 1 63  ? -13.310 5.026   -6.671  1.00 54.66  ?  219 LYS   A CE  1 
ATOM   390  N  NZ  . LYS   A 1 63  ? -12.515 4.720   -7.905  1.00 54.82  ?  219 LYS   A NZ  1 
ATOM   391  N  N   . ILE   A 1 64  ? -19.775 3.091   -5.578  1.00 46.61  ?  220 ILE   A N   1 
ATOM   392  C  CA  . ILE   A 1 64  ? -20.615 1.908   -5.765  1.00 43.95  ?  220 ILE   A CA  1 
ATOM   393  C  C   . ILE   A 1 64  ? -19.930 0.891   -6.668  1.00 46.19  ?  220 ILE   A C   1 
ATOM   394  O  O   . ILE   A 1 64  ? -20.174 -0.315  -6.555  1.00 50.86  ?  220 ILE   A O   1 
ATOM   395  C  CB  . ILE   A 1 64  ? -22.001 2.325   -6.306  1.00 50.96  ?  220 ILE   A CB  1 
ATOM   396  C  CG1 . ILE   A 1 64  ? -23.084 1.383   -5.807  1.00 53.10  ?  220 ILE   A CG1 1 
ATOM   397  C  CG2 . ILE   A 1 64  ? -22.026 2.393   -7.830  1.00 48.49  ?  220 ILE   A CG2 1 
ATOM   398  C  CD1 . ILE   A 1 64  ? -24.443 1.857   -6.159  1.00 45.47  ?  220 ILE   A CD1 1 
ATOM   399  N  N   . SER   A 1 65  ? -19.038 1.347   -7.543  1.00 47.67  ?  221 SER   A N   1 
ATOM   400  C  CA  . SER   A 1 65  ? -18.362 0.486   -8.500  1.00 50.23  ?  221 SER   A CA  1 
ATOM   401  C  C   . SER   A 1 65  ? -17.025 -0.041  -7.989  1.00 50.66  ?  221 SER   A C   1 
ATOM   402  O  O   . SER   A 1 65  ? -16.299 -0.699  -8.744  1.00 52.85  ?  221 SER   A O   1 
ATOM   403  C  CB  . SER   A 1 65  ? -18.198 1.241   -9.828  1.00 56.56  ?  221 SER   A CB  1 
ATOM   404  O  OG  . SER   A 1 65  ? -17.425 2.422   -9.682  1.00 44.60  ?  221 SER   A OG  1 
ATOM   405  N  N   . ALA   A 1 66  ? -16.695 0.214   -6.719  1.00 49.01  ?  222 ALA   A N   1 
ATOM   406  C  CA  . ALA   A 1 66  ? -15.439 -0.223  -6.108  1.00 51.29  ?  222 ALA   A CA  1 
ATOM   407  C  C   . ALA   A 1 66  ? -15.775 -1.023  -4.853  1.00 56.60  ?  222 ALA   A C   1 
ATOM   408  O  O   . ALA   A 1 66  ? -15.629 -0.525  -3.724  1.00 49.20  ?  222 ALA   A O   1 
ATOM   409  C  CB  . ALA   A 1 66  ? -14.535 0.963   -5.784  1.00 49.57  ?  222 ALA   A CB  1 
ATOM   410  N  N   . PRO   A 1 67  ? -16.220 -2.274  -5.012  1.00 53.95  ?  223 PRO   A N   1 
ATOM   411  C  CA  . PRO   A 1 67  ? -16.714 -3.036  -3.852  1.00 54.89  ?  223 PRO   A CA  1 
ATOM   412  C  C   . PRO   A 1 67  ? -15.653 -3.336  -2.807  1.00 52.34  ?  223 PRO   A C   1 
ATOM   413  O  O   . PRO   A 1 67  ? -16.012 -3.557  -1.646  1.00 55.47  ?  223 PRO   A O   1 
ATOM   414  C  CB  . PRO   A 1 67  ? -17.250 -4.332  -4.483  1.00 58.64  ?  223 PRO   A CB  1 
ATOM   415  C  CG  . PRO   A 1 67  ? -16.516 -4.460  -5.777  1.00 56.27  ?  223 PRO   A CG  1 
ATOM   416  C  CD  . PRO   A 1 67  ? -16.303 -3.047  -6.264  1.00 57.93  ?  223 PRO   A CD  1 
ATOM   417  N  N   . ASN   A 1 68  ? -14.371 -3.357  -3.175  1.00 50.91  ?  224 ASN   A N   1 
ATOM   418  C  CA  . ASN   A 1 68  ? -13.286 -3.675  -2.256  1.00 54.37  ?  224 ASN   A CA  1 
ATOM   419  C  C   . ASN   A 1 68  ? -12.704 -2.446  -1.563  1.00 53.58  ?  224 ASN   A C   1 
ATOM   420  O  O   . ASN   A 1 68  ? -11.791 -2.587  -0.742  1.00 51.71  ?  224 ASN   A O   1 
ATOM   421  C  CB  . ASN   A 1 68  ? -12.170 -4.409  -3.003  1.00 54.62  ?  224 ASN   A CB  1 
ATOM   422  C  CG  . ASN   A 1 68  ? -12.641 -5.715  -3.605  1.00 61.23  ?  224 ASN   A CG  1 
ATOM   423  O  OD1 . ASN   A 1 68  ? -12.369 -5.998  -4.770  1.00 68.20  ?  224 ASN   A OD1 1 
ATOM   424  N  ND2 . ASN   A 1 68  ? -13.362 -6.516  -2.818  1.00 63.93  ?  224 ASN   A ND2 1 
ATOM   425  N  N   . GLU   A 1 69  ? -13.201 -1.257  -1.881  1.00 50.86  ?  225 GLU   A N   1 
ATOM   426  C  CA  . GLU   A 1 69  ? -12.748 -0.013  -1.273  1.00 46.15  ?  225 GLU   A CA  1 
ATOM   427  C  C   . GLU   A 1 69  ? -13.761 0.395   -0.213  1.00 43.09  ?  225 GLU   A C   1 
ATOM   428  O  O   . GLU   A 1 69  ? -14.874 0.811   -0.536  1.00 42.23  ?  225 GLU   A O   1 
ATOM   429  C  CB  . GLU   A 1 69  ? -12.578 1.057   -2.348  1.00 44.73  ?  225 GLU   A CB  1 
ATOM   430  C  CG  . GLU   A 1 69  ? -11.464 0.692   -3.331  1.00 48.29  ?  225 GLU   A CG  1 
ATOM   431  C  CD  . GLU   A 1 69  ? -11.234 1.733   -4.415  1.00 56.98  ?  225 GLU   A CD  1 
ATOM   432  O  OE1 . GLU   A 1 69  ? -11.737 2.871   -4.285  1.00 54.00  ?  225 GLU   A OE1 1 
ATOM   433  O  OE2 . GLU   A 1 69  ? -10.522 1.406   -5.394  1.00 64.44  -1 225 GLU   A OE2 1 
ATOM   434  N  N   . PHE   A 1 70  ? -13.382 0.261   1.050   1.00 42.71  ?  226 PHE   A N   1 
ATOM   435  C  CA  . PHE   A 1 70  ? -14.295 0.502   2.154   1.00 39.62  ?  226 PHE   A CA  1 
ATOM   436  C  C   . PHE   A 1 70  ? -13.973 1.822   2.828   1.00 39.03  ?  226 PHE   A C   1 
ATOM   437  O  O   . PHE   A 1 70  ? -12.898 2.397   2.644   1.00 37.87  ?  226 PHE   A O   1 
ATOM   438  C  CB  . PHE   A 1 70  ? -14.229 -0.639  3.168   1.00 46.25  ?  226 PHE   A CB  1 
ATOM   439  C  CG  . PHE   A 1 70  ? -14.784 -1.928  2.650   1.00 40.44  ?  226 PHE   A CG  1 
ATOM   440  C  CD1 . PHE   A 1 70  ? -14.021 -2.728  1.811   1.00 46.85  ?  226 PHE   A CD1 1 
ATOM   441  C  CD2 . PHE   A 1 70  ? -16.044 -2.360  3.030   1.00 43.76  ?  226 PHE   A CD2 1 
ATOM   442  C  CE1 . PHE   A 1 70  ? -14.516 -3.923  1.331   1.00 47.65  ?  226 PHE   A CE1 1 
ATOM   443  C  CE2 . PHE   A 1 70  ? -16.546 -3.565  2.562   1.00 45.65  ?  226 PHE   A CE2 1 
ATOM   444  C  CZ  . PHE   A 1 70  ? -15.784 -4.345  1.709   1.00 41.32  ?  226 PHE   A CZ  1 
ATOM   445  N  N   . ASP   A 1 71  ? -14.932 2.277   3.627   1.00 40.26  ?  227 ASP   A N   1 
ATOM   446  C  CA  . ASP   A 1 71  ? -14.904 3.585   4.253   1.00 39.64  ?  227 ASP   A CA  1 
ATOM   447  C  C   . ASP   A 1 71  ? -15.543 3.490   5.631   1.00 44.75  ?  227 ASP   A C   1 
ATOM   448  O  O   . ASP   A 1 71  ? -16.680 3.027   5.765   1.00 35.61  ?  227 ASP   A O   1 
ATOM   449  C  CB  . ASP   A 1 71  ? -15.634 4.602   3.378   1.00 47.24  ?  227 ASP   A CB  1 
ATOM   450  C  CG  . ASP   A 1 71  ? -15.432 5.995   3.841   1.00 40.99  ?  227 ASP   A CG  1 
ATOM   451  O  OD1 . ASP   A 1 71  ? -16.180 6.430   4.739   1.00 46.46  ?  227 ASP   A OD1 1 
ATOM   452  O  OD2 . ASP   A 1 71  ? -14.486 6.635   3.339   1.00 47.67  -1 227 ASP   A OD2 1 
ATOM   453  N  N   . VAL   A 1 72  ? -14.807 3.927   6.654   1.00 39.48  ?  228 VAL   A N   1 
ATOM   454  C  CA  . VAL   A 1 72  ? -15.191 3.709   8.043   1.00 34.33  ?  228 VAL   A CA  1 
ATOM   455  C  C   . VAL   A 1 72  ? -14.958 4.989   8.840   1.00 42.59  ?  228 VAL   A C   1 
ATOM   456  O  O   . VAL   A 1 72  ? -13.925 5.657   8.691   1.00 34.84  ?  228 VAL   A O   1 
ATOM   457  C  CB  . VAL   A 1 72  ? -14.408 2.524   8.646   1.00 43.61  ?  228 VAL   A CB  1 
ATOM   458  C  CG1 . VAL   A 1 72  ? -14.678 2.405   10.128  1.00 41.64  ?  228 VAL   A CG1 1 
ATOM   459  C  CG2 . VAL   A 1 72  ? -14.824 1.232   7.958   1.00 42.27  ?  228 VAL   A CG2 1 
ATOM   460  N  N   . MET   A 1 73  ? -15.912 5.323   9.701   1.00 33.44  ?  229 MET   A N   1 
ATOM   461  C  CA  . MET   A 1 73  ? -15.808 6.504   10.545  1.00 36.14  ?  229 MET   A CA  1 
ATOM   462  C  C   . MET   A 1 73  ? -15.616 6.056   11.997  1.00 39.57  ?  229 MET   A C   1 
ATOM   463  O  O   . MET   A 1 73  ? -16.436 5.294   12.524  1.00 37.44  ?  229 MET   A O   1 
ATOM   464  C  CB  . MET   A 1 73  ? -17.054 7.376   10.398  1.00 45.88  ?  229 MET   A CB  1 
ATOM   465  C  CG  . MET   A 1 73  ? -16.939 8.683   11.149  1.00 49.28  ?  229 MET   A CG  1 
ATOM   466  S  SD  . MET   A 1 73  ? -17.944 10.030  10.485  1.00 57.62  ?  229 MET   A SD  1 
ATOM   467  C  CE  . MET   A 1 73  ? -18.342 9.473   8.815   1.00 36.30  ?  229 MET   A CE  1 
ATOM   468  N  N   . PHE   A 1 74  ? -14.519 6.510   12.633  1.00 33.52  ?  230 PHE   A N   1 
ATOM   469  C  CA  . PHE   A 1 74  ? -14.299 6.341   14.076  1.00 35.59  ?  230 PHE   A CA  1 
ATOM   470  C  C   . PHE   A 1 74  ? -14.775 7.610   14.788  1.00 40.95  ?  230 PHE   A C   1 
ATOM   471  O  O   . PHE   A 1 74  ? -14.124 8.657   14.679  1.00 39.57  ?  230 PHE   A O   1 
ATOM   472  C  CB  . PHE   A 1 74  ? -12.819 6.108   14.406  1.00 35.26  ?  230 PHE   A CB  1 
ATOM   473  C  CG  . PHE   A 1 74  ? -12.274 4.762   13.993  1.00 38.70  ?  230 PHE   A CG  1 
ATOM   474  C  CD1 . PHE   A 1 74  ? -13.039 3.864   13.257  1.00 39.96  ?  230 PHE   A CD1 1 
ATOM   475  C  CD2 . PHE   A 1 74  ? -10.995 4.375   14.391  1.00 44.73  ?  230 PHE   A CD2 1 
ATOM   476  C  CE1 . PHE   A 1 74  ? -12.523 2.640   12.888  1.00 45.42  ?  230 PHE   A CE1 1 
ATOM   477  C  CE2 . PHE   A 1 74  ? -10.475 3.148   14.036  1.00 36.91  ?  230 PHE   A CE2 1 
ATOM   478  C  CZ  . PHE   A 1 74  ? -11.245 2.274   13.285  1.00 50.29  ?  230 PHE   A CZ  1 
ATOM   479  N  N   . LYS   A 1 75  ? -15.871 7.520   15.548  1.00 36.19  ?  231 LYS   A N   1 
ATOM   480  C  CA  . LYS   A 1 75  ? -16.362 8.669   16.313  1.00 36.21  ?  231 LYS   A CA  1 
ATOM   481  C  C   . LYS   A 1 75  ? -15.738 8.712   17.707  1.00 43.71  ?  231 LYS   A C   1 
ATOM   482  O  O   . LYS   A 1 75  ? -15.388 7.674   18.284  1.00 37.44  ?  231 LYS   A O   1 
ATOM   483  C  CB  . LYS   A 1 75  ? -17.876 8.632   16.498  1.00 34.95  ?  231 LYS   A CB  1 
ATOM   484  C  CG  . LYS   A 1 75  ? -18.305 7.514   17.403  1.00 41.10  ?  231 LYS   A CG  1 
ATOM   485  C  CD  . LYS   A 1 75  ? -19.530 7.884   18.202  1.00 49.25  ?  231 LYS   A CD  1 
ATOM   486  C  CE  . LYS   A 1 75  ? -19.761 6.874   19.328  1.00 48.08  ?  231 LYS   A CE  1 
ATOM   487  N  NZ  . LYS   A 1 75  ? -20.027 7.578   20.627  1.00 50.82  ?  231 LYS   A NZ  1 
ATOM   488  N  N   . LEU   A 1 76  ? -15.690 9.924   18.275  1.00 36.13  ?  232 LEU   A N   1 
ATOM   489  C  CA  . LEU   A 1 76  ? -15.106 10.184  19.595  1.00 44.58  ?  232 LEU   A CA  1 
ATOM   490  C  C   . LEU   A 1 76  ? -15.891 11.308  20.263  1.00 42.14  ?  232 LEU   A C   1 
ATOM   491  O  O   . LEU   A 1 76  ? -15.855 12.451  19.798  1.00 34.59  ?  232 LEU   A O   1 
ATOM   492  C  CB  . LEU   A 1 76  ? -13.639 10.556  19.454  1.00 40.92  ?  232 LEU   A CB  1 
ATOM   493  C  CG  . LEU   A 1 76  ? -12.807 10.828  20.698  1.00 46.48  ?  232 LEU   A CG  1 
ATOM   494  C  CD1 . LEU   A 1 76  ? -12.502 9.579   21.515  1.00 48.31  ?  232 LEU   A CD1 1 
ATOM   495  C  CD2 . LEU   A 1 76  ? -11.547 11.466  20.246  1.00 43.96  ?  232 LEU   A CD2 1 
ATOM   496  N  N   . GLU   A 1 77  ? -16.607 11.009  21.343  1.00 43.08  ?  233 GLU   A N   1 
ATOM   497  C  CA  . GLU   A 1 77  ? -17.441 12.051  21.929  1.00 44.07  ?  233 GLU   A CA  1 
ATOM   498  C  C   . GLU   A 1 77  ? -16.592 13.110  22.620  1.00 46.00  ?  233 GLU   A C   1 
ATOM   499  O  O   . GLU   A 1 77  ? -15.663 12.797  23.363  1.00 46.22  ?  233 GLU   A O   1 
ATOM   500  C  CB  . GLU   A 1 77  ? -18.465 11.489  22.909  1.00 50.84  ?  233 GLU   A CB  1 
ATOM   501  C  CG  . GLU   A 1 77  ? -19.501 12.573  23.236  1.00 54.72  ?  233 GLU   A CG  1 
ATOM   502  C  CD  . GLU   A 1 77  ? -20.381 12.261  24.435  1.00 62.37  ?  233 GLU   A CD  1 
ATOM   503  O  OE1 . GLU   A 1 77  ? -20.361 11.106  24.929  1.00 64.25  ?  233 GLU   A OE1 1 
ATOM   504  O  OE2 . GLU   A 1 77  ? -21.037 13.213  24.924  1.00 67.12  -1 233 GLU   A OE2 1 
ATOM   505  N  N   . VAL   A 1 78  ? -16.913 14.366  22.344  1.00 53.46  ?  234 VAL   A N   1 
ATOM   506  C  CA  . VAL   A 1 78  ? -16.264 15.518  22.951  1.00 54.09  ?  234 VAL   A CA  1 
ATOM   507  C  C   . VAL   A 1 78  ? -17.319 16.278  23.744  1.00 58.40  ?  234 VAL   A C   1 
ATOM   508  O  O   . VAL   A 1 78  ? -18.143 16.997  23.173  1.00 62.01  ?  234 VAL   A O   1 
ATOM   509  C  CB  . VAL   A 1 78  ? -15.615 16.423  21.891  1.00 48.96  ?  234 VAL   A CB  1 
ATOM   510  C  CG1 . VAL   A 1 78  ? -15.083 17.674  22.551  1.00 58.32  ?  234 VAL   A CG1 1 
ATOM   511  C  CG2 . VAL   A 1 78  ? -14.515 15.682  21.169  1.00 56.06  ?  234 VAL   A CG2 1 
ATOM   512  N  N   . PRO   A 1 79  ? -17.366 16.095  25.057  1.00 58.63  ?  235 PRO   A N   1 
ATOM   513  C  CA  . PRO   A 1 79  ? -18.403 16.769  25.845  1.00 52.90  ?  235 PRO   A CA  1 
ATOM   514  C  C   . PRO   A 1 79  ? -18.119 18.265  25.937  1.00 55.83  ?  235 PRO   A C   1 
ATOM   515  O  O   . PRO   A 1 79  ? -16.979 18.716  25.793  1.00 58.05  ?  235 PRO   A O   1 
ATOM   516  C  CB  . PRO   A 1 79  ? -18.317 16.096  27.221  1.00 61.14  ?  235 PRO   A CB  1 
ATOM   517  C  CG  . PRO   A 1 79  ? -17.351 14.966  27.102  1.00 58.77  ?  235 PRO   A CG  1 
ATOM   518  C  CD  . PRO   A 1 79  ? -16.714 14.977  25.760  1.00 53.61  ?  235 PRO   A CD  1 
ATOM   519  N  N   . ARG   A 1 80  ? -19.184 19.040  26.150  1.00 56.52  ?  236 ARG   A N   1 
ATOM   520  C  CA  . ARG   A 1 80  ? -19.066 20.466  26.471  1.00 52.92  ?  236 ARG   A CA  1 
ATOM   521  C  C   . ARG   A 1 80  ? -18.275 21.229  25.409  1.00 51.88  ?  236 ARG   A C   1 
ATOM   522  O  O   . ARG   A 1 80  ? -17.561 22.186  25.706  1.00 60.64  ?  236 ARG   A O   1 
ATOM   523  C  CB  . ARG   A 1 80  ? -18.439 20.665  27.857  1.00 63.37  ?  236 ARG   A CB  1 
ATOM   524  N  N   . ILE   A 1 81  ? -18.402 20.799  24.155  1.00 55.44  ?  237 ILE   A N   1 
ATOM   525  C  CA  . ILE   A 1 81  ? -17.729 21.485  23.060  1.00 55.18  ?  237 ILE   A CA  1 
ATOM   526  C  C   . ILE   A 1 81  ? -18.245 22.927  22.925  1.00 59.77  ?  237 ILE   A C   1 
ATOM   527  O  O   . ILE   A 1 81  ? -19.350 23.268  23.360  1.00 63.34  ?  237 ILE   A O   1 
ATOM   528  C  CB  . ILE   A 1 81  ? -17.945 20.684  21.765  1.00 62.57  ?  237 ILE   A CB  1 
ATOM   529  C  CG1 . ILE   A 1 81  ? -16.679 20.657  20.920  1.00 59.66  ?  237 ILE   A CG1 1 
ATOM   530  C  CG2 . ILE   A 1 81  ? -19.107 21.219  20.962  1.00 49.73  ?  237 ILE   A CG2 1 
ATOM   531  C  CD1 . ILE   A 1 81  ? -16.740 19.617  19.845  1.00 53.49  ?  237 ILE   A CD1 1 
ATOM   532  N  N   . GLN   A 1 82  ? -17.427 23.781  22.316  1.00 54.58  ?  238 GLN   A N   1 
ATOM   533  C  CA  . GLN   A 1 82  ? -17.847 25.135  21.961  1.00 53.65  ?  238 GLN   A CA  1 
ATOM   534  C  C   . GLN   A 1 82  ? -17.351 25.427  20.552  1.00 47.85  ?  238 GLN   A C   1 
ATOM   535  O  O   . GLN   A 1 82  ? -16.151 25.315  20.288  1.00 46.38  ?  238 GLN   A O   1 
ATOM   536  C  CB  . GLN   A 1 82  ? -17.285 26.158  22.950  1.00 63.38  ?  238 GLN   A CB  1 
ATOM   537  C  CG  . GLN   A 1 82  ? -18.006 27.511  23.037  1.00 72.80  ?  238 GLN   A CG  1 
ATOM   538  C  CD  . GLN   A 1 82  ? -19.336 27.454  23.792  1.00 78.30  ?  238 GLN   A CD  1 
ATOM   539  O  OE1 . GLN   A 1 82  ? -19.934 28.493  24.090  1.00 80.44  ?  238 GLN   A OE1 1 
ATOM   540  N  NE2 . GLN   A 1 82  ? -19.802 26.245  24.105  1.00 64.87  ?  238 GLN   A NE2 1 
ATOM   541  N  N   . LEU   A 1 83  ? -18.254 25.789  19.638  1.00 47.77  ?  239 LEU   A N   1 
ATOM   542  C  CA  . LEU   A 1 83  ? -17.855 25.989  18.248  1.00 44.90  ?  239 LEU   A CA  1 
ATOM   543  C  C   . LEU   A 1 83  ? -17.719 27.466  17.886  1.00 49.74  ?  239 LEU   A C   1 
ATOM   544  O  O   . LEU   A 1 83  ? -18.491 28.311  18.344  1.00 53.74  ?  239 LEU   A O   1 
ATOM   545  C  CB  . LEU   A 1 83  ? -18.829 25.322  17.280  1.00 36.33  ?  239 LEU   A CB  1 
ATOM   546  C  CG  . LEU   A 1 83  ? -18.922 23.794  17.386  1.00 43.03  ?  239 LEU   A CG  1 
ATOM   547  C  CD1 . LEU   A 1 83  ? -19.900 23.238  16.358  1.00 40.38  ?  239 LEU   A CD1 1 
ATOM   548  C  CD2 . LEU   A 1 83  ? -17.551 23.163  17.241  1.00 46.12  ?  239 LEU   A CD2 1 
ATOM   549  N  N   . GLU   A 1 84  ? -16.739 27.755  17.031  1.00 42.97  ?  240 GLU   A N   1 
ATOM   550  C  CA  . GLU   A 1 84  ? -16.487 29.089  16.496  1.00 45.81  ?  240 GLU   A CA  1 
ATOM   551  C  C   . GLU   A 1 84  ? -16.407 28.960  14.976  1.00 46.86  ?  240 GLU   A C   1 
ATOM   552  O  O   . GLU   A 1 84  ? -15.461 28.364  14.447  1.00 39.31  ?  240 GLU   A O   1 
ATOM   553  C  CB  . GLU   A 1 84  ? -15.208 29.678  17.102  1.00 45.94  ?  240 GLU   A CB  1 
ATOM   554  C  CG  . GLU   A 1 84  ? -15.007 31.176  16.872  1.00 47.50  ?  240 GLU   A CG  1 
ATOM   555  C  CD  . GLU   A 1 84  ? -13.594 31.666  17.208  1.00 63.44  ?  240 GLU   A CD  1 
ATOM   556  O  OE1 . GLU   A 1 84  ? -12.996 31.178  18.196  1.00 68.86  ?  240 GLU   A OE1 1 
ATOM   557  O  OE2 . GLU   A 1 84  ? -13.074 32.553  16.489  1.00 59.62  -1 240 GLU   A OE2 1 
ATOM   558  N  N   . GLU   A 1 85  ? -17.419 29.479  14.277  1.00 40.97  ?  241 GLU   A N   1 
ATOM   559  C  CA  . GLU   A 1 85  ? -17.465 29.357  12.822  1.00 41.21  ?  241 GLU   A CA  1 
ATOM   560  C  C   . GLU   A 1 85  ? -16.229 29.999  12.210  1.00 39.27  ?  241 GLU   A C   1 
ATOM   561  O  O   . GLU   A 1 85  ? -15.867 31.119  12.561  1.00 38.16  ?  241 GLU   A O   1 
ATOM   562  C  CB  . GLU   A 1 85  ? -18.726 30.022  12.263  1.00 36.01  ?  241 GLU   A CB  1 
ATOM   563  C  CG  . GLU   A 1 85  ? -18.942 29.794  10.743  1.00 43.13  ?  241 GLU   A CG  1 
ATOM   564  C  CD  . GLU   A 1 85  ? -20.219 30.443  10.224  1.00 45.76  ?  241 GLU   A CD  1 
ATOM   565  O  OE1 . GLU   A 1 85  ? -20.945 31.041  11.048  1.00 39.72  ?  241 GLU   A OE1 1 
ATOM   566  O  OE2 . GLU   A 1 85  ? -20.521 30.321  9.005   1.00 43.71  -1 241 GLU   A OE2 1 
ATOM   567  N  N   . TYR   A 1 86  ? -15.577 29.292  11.295  1.00 40.73  ?  242 TYR   A N   1 
ATOM   568  C  CA  . TYR   A 1 86  ? -14.467 29.885  10.557  1.00 38.05  ?  242 TYR   A CA  1 
ATOM   569  C  C   . TYR   A 1 86  ? -14.994 30.680  9.362   1.00 43.37  ?  242 TYR   A C   1 
ATOM   570  O  O   . TYR   A 1 86  ? -15.676 30.125  8.487   1.00 44.67  ?  242 TYR   A O   1 
ATOM   571  C  CB  . TYR   A 1 86  ? -13.495 28.809  10.087  1.00 39.30  ?  242 TYR   A CB  1 
ATOM   572  C  CG  . TYR   A 1 86  ? -12.447 29.312  9.116   1.00 43.80  ?  242 TYR   A CG  1 
ATOM   573  C  CD1 . TYR   A 1 86  ? -11.391 30.131  9.537   1.00 49.08  ?  242 TYR   A CD1 1 
ATOM   574  C  CD2 . TYR   A 1 86  ? -12.531 28.984  7.763   1.00 45.07  ?  242 TYR   A CD2 1 
ATOM   575  C  CE1 . TYR   A 1 86  ? -10.427 30.591  8.628   1.00 50.87  ?  242 TYR   A CE1 1 
ATOM   576  C  CE2 . TYR   A 1 86  ? -11.593 29.435  6.852   1.00 43.26  ?  242 TYR   A CE2 1 
ATOM   577  C  CZ  . TYR   A 1 86  ? -10.544 30.233  7.278   1.00 55.80  ?  242 TYR   A CZ  1 
ATOM   578  O  OH  . TYR   A 1 86  ? -9.621  30.664  6.342   1.00 62.33  ?  242 TYR   A OH  1 
ATOM   579  N  N   . SER   A 1 87  ? -14.710 31.984  9.361   1.00 49.89  ?  243 SER   A N   1 
ATOM   580  C  CA  . SER   A 1 87  ? -14.764 32.834  8.168   1.00 46.55  ?  243 SER   A CA  1 
ATOM   581  C  C   . SER   A 1 87  ? -16.102 32.744  7.431   1.00 40.32  ?  243 SER   A C   1 
ATOM   582  O  O   . SER   A 1 87  ? -16.144 32.745  6.203   1.00 43.46  ?  243 SER   A O   1 
ATOM   583  C  CB  . SER   A 1 87  ? -13.606 32.499  7.225   1.00 50.27  ?  243 SER   A CB  1 
ATOM   584  O  OG  . SER   A 1 87  ? -13.519 33.436  6.162   1.00 55.85  ?  243 SER   A OG  1 
ATOM   585  N  N   . ASN   A 1 88  ? -17.204 32.680  8.191   1.00 38.63  ?  244 ASN   A N   1 
ATOM   586  C  CA  . ASN   A 1 88  ? -18.569 32.631  7.640   1.00 41.77  ?  244 ASN   A CA  1 
ATOM   587  C  C   . ASN   A 1 88  ? -18.775 31.468  6.671   1.00 45.15  ?  244 ASN   A C   1 
ATOM   588  O  O   . ASN   A 1 88  ? -19.637 31.537  5.793   1.00 39.30  ?  244 ASN   A O   1 
ATOM   589  C  CB  . ASN   A 1 88  ? -18.969 33.948  6.943   1.00 49.36  ?  244 ASN   A CB  1 
ATOM   590  C  CG  . ASN   A 1 88  ? -19.138 35.108  7.907   1.00 53.61  ?  244 ASN   A CG  1 
ATOM   591  O  OD1 . ASN   A 1 88  ? -19.044 34.935  9.122   1.00 64.82  ?  244 ASN   A OD1 1 
ATOM   592  N  ND2 . ASN   A 1 88  ? -19.369 36.311  7.365   1.00 50.04  ?  244 ASN   A ND2 1 
ATOM   593  N  N   . THR   A 1 89  ? -18.012 30.379  6.814   1.00 40.96  ?  245 THR   A N   1 
ATOM   594  C  CA  . THR   A 1 89  ? -18.167 29.281  5.858   1.00 36.21  ?  245 THR   A CA  1 
ATOM   595  C  C   . THR   A 1 89  ? -19.380 28.400  6.136   1.00 39.20  ?  245 THR   A C   1 
ATOM   596  O  O   . THR   A 1 89  ? -19.694 27.545  5.302   1.00 36.71  ?  245 THR   A O   1 
ATOM   597  C  CB  . THR   A 1 89  ? -16.921 28.386  5.832   1.00 42.06  ?  245 THR   A CB  1 
ATOM   598  O  OG1 . THR   A 1 89  ? -16.671 27.848  7.141   1.00 39.62  ?  245 THR   A OG1 1 
ATOM   599  C  CG2 . THR   A 1 89  ? -15.713 29.172  5.374   1.00 38.67  ?  245 THR   A CG2 1 
ATOM   600  N  N   . ARG   A 1 90  ? -20.034 28.548  7.294   1.00 38.91  ?  246 ARG   A N   1 
ATOM   601  C  CA  . ARG   A 1 90  ? -21.242 27.804  7.634   1.00 34.60  ?  246 ARG   A CA  1 
ATOM   602  C  C   . ARG   A 1 90  ? -20.982 26.318  7.880   1.00 35.28  ?  246 ARG   A C   1 
ATOM   603  O  O   . ARG   A 1 90  ? -21.783 25.668  8.562   1.00 34.33  ?  246 ARG   A O   1 
ATOM   604  C  CB  . ARG   A 1 90  ? -22.318 27.962  6.544   1.00 38.70  ?  246 ARG   A CB  1 
ATOM   605  C  CG  . ARG   A 1 90  ? -22.585 29.408  6.071   1.00 43.92  ?  246 ARG   A CG  1 
ATOM   606  C  CD  . ARG   A 1 90  ? -23.758 30.049  6.810   1.00 45.29  ?  246 ARG   A CD  1 
ATOM   607  N  NE  . ARG   A 1 90  ? -23.410 30.406  8.183   1.00 57.90  ?  246 ARG   A NE  1 
ATOM   608  C  CZ  . ARG   A 1 90  ? -24.290 30.606  9.158   1.00 57.99  ?  246 ARG   A CZ  1 
ATOM   609  N  NH1 . ARG   A 1 90  ? -25.595 30.613  8.924   1.00 54.94  ?  246 ARG   A NH1 1 
ATOM   610  N  NH2 . ARG   A 1 90  ? -23.851 30.785  10.404  1.00 53.60  ?  246 ARG   A NH2 1 
ATOM   611  N  N   . ALA   A 1 91  ? -19.894 25.754  7.329   1.00 30.38  ?  247 ALA   A N   1 
ATOM   612  C  CA  . ALA   A 1 91  ? -19.592 24.339  7.518   1.00 32.60  ?  247 ALA   A CA  1 
ATOM   613  C  C   . ALA   A 1 91  ? -18.300 24.035  8.270   1.00 34.19  ?  247 ALA   A C   1 
ATOM   614  O  O   . ALA   A 1 91  ? -18.154 22.902  8.753   1.00 31.39  ?  247 ALA   A O   1 
ATOM   615  C  CB  . ALA   A 1 91  ? -19.527 23.609  6.167   1.00 37.49  ?  247 ALA   A CB  1 
ATOM   616  N  N   . TYR   A 1 92  ? -17.367 24.987  8.373   1.00 31.23  ?  248 TYR   A N   1 
ATOM   617  C  CA  . TYR   A 1 92  ? -16.068 24.771  8.992   1.00 34.29  ?  248 TYR   A CA  1 
ATOM   618  C  C   . TYR   A 1 92  ? -15.987 25.549  10.302  1.00 39.59  ?  248 TYR   A C   1 
ATOM   619  O  O   . TYR   A 1 92  ? -16.401 26.714  10.367  1.00 39.21  ?  248 TYR   A O   1 
ATOM   620  C  CB  . TYR   A 1 92  ? -14.927 25.203  8.060   1.00 37.87  ?  248 TYR   A CB  1 
ATOM   621  C  CG  . TYR   A 1 92  ? -14.822 24.369  6.804   1.00 39.11  ?  248 TYR   A CG  1 
ATOM   622  C  CD1 . TYR   A 1 92  ? -15.597 24.675  5.695   1.00 38.31  ?  248 TYR   A CD1 1 
ATOM   623  C  CD2 . TYR   A 1 92  ? -13.915 23.304  6.715   1.00 39.10  ?  248 TYR   A CD2 1 
ATOM   624  C  CE1 . TYR   A 1 92  ? -15.522 23.912  4.525   1.00 41.44  ?  248 TYR   A CE1 1 
ATOM   625  C  CE2 . TYR   A 1 92  ? -13.822 22.533  5.566   1.00 37.94  ?  248 TYR   A CE2 1 
ATOM   626  C  CZ  . TYR   A 1 92  ? -14.629 22.848  4.463   1.00 49.86  ?  248 TYR   A CZ  1 
ATOM   627  O  OH  . TYR   A 1 92  ? -14.559 22.107  3.300   1.00 38.96  ?  248 TYR   A OH  1 
ATOM   628  N  N   . TYR   A 1 93  ? -15.439 24.905  11.339  1.00 38.87  ?  249 TYR   A N   1 
ATOM   629  C  CA  . TYR   A 1 93  ? -15.435 25.473  12.684  1.00 39.34  ?  249 TYR   A CA  1 
ATOM   630  C  C   . TYR   A 1 93  ? -14.113 25.232  13.386  1.00 43.54  ?  249 TYR   A C   1 
ATOM   631  O  O   . TYR   A 1 93  ? -13.370 24.294  13.080  1.00 38.29  ?  249 TYR   A O   1 
ATOM   632  C  CB  . TYR   A 1 93  ? -16.559 24.891  13.570  1.00 37.16  ?  249 TYR   A CB  1 
ATOM   633  C  CG  . TYR   A 1 93  ? -17.925 25.212  13.041  1.00 41.34  ?  249 TYR   A CG  1 
ATOM   634  C  CD1 . TYR   A 1 93  ? -18.483 24.457  12.008  1.00 36.43  ?  249 TYR   A CD1 1 
ATOM   635  C  CD2 . TYR   A 1 93  ? -18.666 26.263  13.570  1.00 37.31  ?  249 TYR   A CD2 1 
ATOM   636  C  CE1 . TYR   A 1 93  ? -19.717 24.742  11.508  1.00 39.86  ?  249 TYR   A CE1 1 
ATOM   637  C  CE2 . TYR   A 1 93  ? -19.931 26.560  13.061  1.00 39.81  ?  249 TYR   A CE2 1 
ATOM   638  C  CZ  . TYR   A 1 93  ? -20.438 25.794  12.027  1.00 40.36  ?  249 TYR   A CZ  1 
ATOM   639  O  OH  . TYR   A 1 93  ? -21.679 26.058  11.502  1.00 37.49  ?  249 TYR   A OH  1 
ATOM   640  N  N   . PHE   A 1 94  ? -13.832 26.108  14.342  1.00 46.82  ?  250 PHE   A N   1 
ATOM   641  C  CA  . PHE   A 1 94  ? -12.827 25.853  15.350  1.00 38.96  ?  250 PHE   A CA  1 
ATOM   642  C  C   . PHE   A 1 94  ? -13.506 25.198  16.542  1.00 44.28  ?  250 PHE   A C   1 
ATOM   643  O  O   . PHE   A 1 94  ? -14.653 25.516  16.867  1.00 40.34  ?  250 PHE   A O   1 
ATOM   644  C  CB  . PHE   A 1 94  ? -12.142 27.154  15.747  1.00 43.41  ?  250 PHE   A CB  1 
ATOM   645  C  CG  . PHE   A 1 94  ? -11.324 27.767  14.649  1.00 47.01  ?  250 PHE   A CG  1 
ATOM   646  C  CD1 . PHE   A 1 94  ? -10.221 27.100  14.140  1.00 48.51  ?  250 PHE   A CD1 1 
ATOM   647  C  CD2 . PHE   A 1 94  ? -11.623 29.025  14.156  1.00 49.96  ?  250 PHE   A CD2 1 
ATOM   648  C  CE1 . PHE   A 1 94  ? -9.442  27.665  13.143  1.00 50.37  ?  250 PHE   A CE1 1 
ATOM   649  C  CE2 . PHE   A 1 94  ? -10.846 29.597  13.150  1.00 49.21  ?  250 PHE   A CE2 1 
ATOM   650  C  CZ  . PHE   A 1 94  ? -9.753  28.921  12.650  1.00 51.11  ?  250 PHE   A CZ  1 
ATOM   651  N  N   . VAL   A 1 95  ? -12.808 24.262  17.177  1.00 54.62  ?  251 VAL   A N   1 
ATOM   652  C  CA  . VAL   A 1 95  ? -13.335 23.542  18.329  1.00 44.78  ?  251 VAL   A CA  1 
ATOM   653  C  C   . VAL   A 1 95  ? -12.712 24.131  19.585  1.00 48.64  ?  251 VAL   A C   1 
ATOM   654  O  O   . VAL   A 1 95  ? -11.486 24.127  19.731  1.00 49.82  ?  251 VAL   A O   1 
ATOM   655  C  CB  . VAL   A 1 95  ? -13.055 22.036  18.224  1.00 46.91  ?  251 VAL   A CB  1 
ATOM   656  C  CG1 . VAL   A 1 95  ? -13.474 21.335  19.483  1.00 40.36  ?  251 VAL   A CG1 1 
ATOM   657  C  CG2 . VAL   A 1 95  ? -13.815 21.438  17.024  1.00 38.70  ?  251 VAL   A CG2 1 
ATOM   658  N  N   . LYS   A 1 96  ? -13.550 24.652  20.479  1.00 46.23  ?  252 LYS   A N   1 
ATOM   659  C  CA  . LYS   A 1 96  ? -13.135 25.083  21.809  1.00 56.19  ?  252 LYS   A CA  1 
ATOM   660  C  C   . LYS   A 1 96  ? -13.874 24.255  22.849  1.00 59.79  ?  252 LYS   A C   1 
ATOM   661  O  O   . LYS   A 1 96  ? -14.766 23.466  22.523  1.00 55.45  ?  252 LYS   A O   1 
ATOM   662  C  CB  . LYS   A 1 96  ? -13.400 26.576  22.034  1.00 51.45  ?  252 LYS   A CB  1 
ATOM   663  C  CG  . LYS   A 1 96  ? -12.594 27.466  21.117  1.00 51.19  ?  252 LYS   A CG  1 
ATOM   664  C  CD  . LYS   A 1 96  ? -12.700 28.938  21.464  1.00 61.97  ?  252 LYS   A CD  1 
ATOM   665  C  CE  . LYS   A 1 96  ? -11.819 29.748  20.524  1.00 61.79  ?  252 LYS   A CE  1 
ATOM   666  N  NZ  . LYS   A 1 96  ? -11.803 31.213  20.814  1.00 65.83  ?  252 LYS   A NZ  1 
ATOM   667  N  N   . PHE   A 1 97  ? -13.494 24.441  24.119  1.00 57.38  ?  253 PHE   A N   1 
ATOM   668  C  CA  . PHE   A 1 97  ? -14.094 23.684  25.212  1.00 64.58  ?  253 PHE   A CA  1 
ATOM   669  C  C   . PHE   A 1 97  ? -14.669 24.616  26.267  1.00 56.67  ?  253 PHE   A C   1 
ATOM   670  O  O   . PHE   A 1 97  ? -14.042 25.609  26.643  1.00 60.50  ?  253 PHE   A O   1 
ATOM   671  C  CB  . PHE   A 1 97  ? -13.089 22.735  25.866  1.00 62.13  ?  253 PHE   A CB  1 
ATOM   672  C  CG  . PHE   A 1 97  ? -12.550 21.708  24.929  1.00 59.16  ?  253 PHE   A CG  1 
ATOM   673  C  CD1 . PHE   A 1 97  ? -11.445 21.981  24.141  1.00 58.43  ?  253 PHE   A CD1 1 
ATOM   674  C  CD2 . PHE   A 1 97  ? -13.194 20.504  24.774  1.00 61.41  ?  253 PHE   A CD2 1 
ATOM   675  C  CE1 . PHE   A 1 97  ? -10.962 21.038  23.259  1.00 59.62  ?  253 PHE   A CE1 1 
ATOM   676  C  CE2 . PHE   A 1 97  ? -12.724 19.565  23.887  1.00 61.63  ?  253 PHE   A CE2 1 
ATOM   677  C  CZ  . PHE   A 1 97  ? -11.613 19.828  23.126  1.00 56.93  ?  253 PHE   A CZ  1 
ATOM   678  N  N   . LYS   A 1 98  ? -15.874 24.284  26.735  1.00 66.95  ?  254 LYS   A N   1 
ATOM   679  C  CA  . LYS   A 1 98  ? -16.518 25.083  27.768  1.00 65.00  ?  254 LYS   A CA  1 
ATOM   680  C  C   . LYS   A 1 98  ? -15.806 24.948  29.108  1.00 61.94  ?  254 LYS   A C   1 
ATOM   681  O  O   . LYS   A 1 98  ? -15.720 25.925  29.857  1.00 73.53  ?  254 LYS   A O   1 
ATOM   682  C  CB  . LYS   A 1 98  ? -17.985 24.680  27.900  1.00 64.58  ?  254 LYS   A CB  1 
ATOM   683  N  N   . ARG   A 1 99  ? -15.306 23.756  29.425  1.00 70.21  ?  255 ARG   A N   1 
ATOM   684  C  CA  . ARG   A 1 99  ? -14.486 23.523  30.625  1.00 71.60  ?  255 ARG   A CA  1 
ATOM   685  C  C   . ARG   A 1 99  ? -13.799 22.160  30.528  1.00 71.96  ?  255 ARG   A C   1 
ATOM   686  O  O   . ARG   A 1 99  ? -14.420 21.165  30.131  1.00 78.58  ?  255 ARG   A O   1 
ATOM   687  C  CB  . ARG   A 1 99  ? -15.327 23.598  31.909  1.00 71.71  ?  255 ARG   A CB  1 
ATOM   688  N  N   . ASN   A 1 104 ? -9.647  17.466  30.944  1.00 60.97  ?  260 ASN   A N   1 
ATOM   689  C  CA  . ASN   A 1 104 ? -10.014 17.349  29.525  1.00 62.68  ?  260 ASN   A CA  1 
ATOM   690  C  C   . ASN   A 1 104 ? -9.018  16.379  28.903  1.00 61.41  ?  260 ASN   A C   1 
ATOM   691  O  O   . ASN   A 1 104 ? -7.819  16.680  28.814  1.00 60.51  ?  260 ASN   A O   1 
ATOM   692  C  CB  . ASN   A 1 104 ? -9.967  18.720  28.840  1.00 59.59  ?  260 ASN   A CB  1 
ATOM   693  C  CG  . ASN   A 1 104 ? -10.416 18.694  27.382  1.00 61.32  ?  260 ASN   A CG  1 
ATOM   694  O  OD1 . ASN   A 1 104 ? -10.590 17.640  26.753  1.00 58.47  ?  260 ASN   A OD1 1 
ATOM   695  N  ND2 . ASN   A 1 104 ? -10.584 19.889  26.826  1.00 65.56  ?  260 ASN   A ND2 1 
ATOM   696  N  N   . PRO   A 1 105 ? -9.496  15.200  28.493  1.00 59.84  ?  261 PRO   A N   1 
ATOM   697  C  CA  . PRO   A 1 105 ? -8.567  14.179  27.985  1.00 60.14  ?  261 PRO   A CA  1 
ATOM   698  C  C   . PRO   A 1 105 ? -7.947  14.545  26.643  1.00 68.45  ?  261 PRO   A C   1 
ATOM   699  O  O   . PRO   A 1 105 ? -6.989  13.881  26.217  1.00 63.09  ?  261 PRO   A O   1 
ATOM   700  C  CB  . PRO   A 1 105 ? -9.441  12.925  27.887  1.00 60.22  ?  261 PRO   A CB  1 
ATOM   701  C  CG  . PRO   A 1 105 ? -10.882 13.433  27.803  1.00 59.05  ?  261 PRO   A CG  1 
ATOM   702  C  CD  . PRO   A 1 105 ? -10.898 14.902  28.157  1.00 56.71  ?  261 PRO   A CD  1 
ATOM   703  N  N   . LEU   A 1 106 ? -8.440  15.595  25.988  1.00 63.18  ?  262 LEU   A N   1 
ATOM   704  C  CA  . LEU   A 1 106 ? -7.855  16.106  24.761  1.00 57.20  ?  262 LEU   A CA  1 
ATOM   705  C  C   . LEU   A 1 106 ? -6.944  17.306  24.975  1.00 61.41  ?  262 LEU   A C   1 
ATOM   706  O  O   . LEU   A 1 106 ? -6.359  17.793  24.001  1.00 64.08  ?  262 LEU   A O   1 
ATOM   707  C  CB  . LEU   A 1 106 ? -8.962  16.486  23.785  1.00 49.94  ?  262 LEU   A CB  1 
ATOM   708  C  CG  . LEU   A 1 106 ? -9.856  15.314  23.433  1.00 52.04  ?  262 LEU   A CG  1 
ATOM   709  C  CD1 . LEU   A 1 106 ? -10.930 15.769  22.462  1.00 49.15  ?  262 LEU   A CD1 1 
ATOM   710  C  CD2 . LEU   A 1 106 ? -9.021  14.194  22.844  1.00 50.96  ?  262 LEU   A CD2 1 
ATOM   711  N  N   . SER   A 1 107 ? -6.793  17.784  26.220  1.00 62.50  ?  263 SER   A N   1 
ATOM   712  C  CA  . SER   A 1 107 ? -6.028  19.002  26.469  1.00 51.65  ?  263 SER   A CA  1 
ATOM   713  C  C   . SER   A 1 107 ? -4.644  18.933  25.844  1.00 63.67  ?  263 SER   A C   1 
ATOM   714  O  O   . SER   A 1 107 ? -4.066  19.965  25.478  1.00 64.73  ?  263 SER   A O   1 
ATOM   715  C  CB  . SER   A 1 107 ? -5.907  19.249  27.980  1.00 64.72  ?  263 SER   A CB  1 
ATOM   716  O  OG  . SER   A 1 107 ? -5.182  18.205  28.610  1.00 59.20  ?  263 SER   A OG  1 
ATOM   717  N  N   . GLN   A 1 108 ? -4.092  17.725  25.723  1.00 67.55  ?  264 GLN   A N   1 
ATOM   718  C  CA  . GLN   A 1 108 ? -2.778  17.556  25.115  1.00 68.30  ?  264 GLN   A CA  1 
ATOM   719  C  C   . GLN   A 1 108 ? -2.748  17.997  23.649  1.00 59.47  ?  264 GLN   A C   1 
ATOM   720  O  O   . GLN   A 1 108 ? -1.662  18.273  23.126  1.00 60.60  ?  264 GLN   A O   1 
ATOM   721  C  CB  . GLN   A 1 108 ? -2.336  16.091  25.270  1.00 73.43  ?  264 GLN   A CB  1 
ATOM   722  C  CG  . GLN   A 1 108 ? -3.226  15.102  24.504  1.00 63.23  ?  264 GLN   A CG  1 
ATOM   723  C  CD  . GLN   A 1 108 ? -2.917  13.622  24.770  1.00 74.68  ?  264 GLN   A CD  1 
ATOM   724  O  OE1 . GLN   A 1 108 ? -1.948  13.071  24.238  1.00 76.48  ?  264 GLN   A OE1 1 
ATOM   725  N  NE2 . GLN   A 1 108 ? -3.740  12.978  25.599  1.00 69.48  ?  264 GLN   A NE2 1 
ATOM   726  N  N   . PHE   A 1 109 ? -3.907  18.097  22.982  1.00 55.99  ?  265 PHE   A N   1 
ATOM   727  C  CA  . PHE   A 1 109 ? -3.973  18.531  21.590  1.00 56.36  ?  265 PHE   A CA  1 
ATOM   728  C  C   . PHE   A 1 109 ? -4.394  19.986  21.433  1.00 57.41  ?  265 PHE   A C   1 
ATOM   729  O  O   . PHE   A 1 109 ? -4.796  20.391  20.330  1.00 58.96  ?  265 PHE   A O   1 
ATOM   730  C  CB  . PHE   A 1 109 ? -4.949  17.650  20.800  1.00 56.98  ?  265 PHE   A CB  1 
ATOM   731  C  CG  . PHE   A 1 109 ? -4.651  16.195  20.905  1.00 61.36  ?  265 PHE   A CG  1 
ATOM   732  C  CD1 . PHE   A 1 109 ? -5.380  15.397  21.763  1.00 68.46  ?  265 PHE   A CD1 1 
ATOM   733  C  CD2 . PHE   A 1 109 ? -3.593  15.638  20.210  1.00 58.41  ?  265 PHE   A CD2 1 
ATOM   734  C  CE1 . PHE   A 1 109 ? -5.096  14.044  21.887  1.00 79.31  ?  265 PHE   A CE1 1 
ATOM   735  C  CE2 . PHE   A 1 109 ? -3.301  14.294  20.325  1.00 66.46  ?  265 PHE   A CE2 1 
ATOM   736  C  CZ  . PHE   A 1 109 ? -4.047  13.494  21.174  1.00 74.79  ?  265 PHE   A CZ  1 
ATOM   737  N  N   . LEU   A 1 110 ? -4.365  20.769  22.501  1.00 57.17  ?  266 LEU   A N   1 
ATOM   738  C  CA  . LEU   A 1 110 ? -4.764  22.160  22.389  1.00 60.64  ?  266 LEU   A CA  1 
ATOM   739  C  C   . LEU   A 1 110 ? -3.651  22.984  21.757  1.00 55.26  ?  266 LEU   A C   1 
ATOM   740  O  O   . LEU   A 1 110 ? -2.470  22.773  22.036  1.00 60.51  ?  266 LEU   A O   1 
ATOM   741  C  CB  . LEU   A 1 110 ? -5.125  22.727  23.755  1.00 60.38  ?  266 LEU   A CB  1 
ATOM   742  C  CG  . LEU   A 1 110 ? -6.384  22.148  24.390  1.00 56.27  ?  266 LEU   A CG  1 
ATOM   743  C  CD1 . LEU   A 1 110 ? -6.512  22.611  25.831  1.00 62.99  ?  266 LEU   A CD1 1 
ATOM   744  C  CD2 . LEU   A 1 110 ? -7.605  22.560  23.579  1.00 58.67  ?  266 LEU   A CD2 1 
ATOM   745  N  N   . GLU   A 1 111 ? -4.035  23.894  20.864  1.00 55.75  ?  267 GLU   A N   1 
ATOM   746  C  CA  . GLU   A 1 111 ? -3.193  25.017  20.452  1.00 60.44  ?  267 GLU   A CA  1 
ATOM   747  C  C   . GLU   A 1 111 ? -3.917  26.253  20.960  1.00 61.65  ?  267 GLU   A C   1 
ATOM   748  O  O   . GLU   A 1 111 ? -4.883  26.718  20.336  1.00 63.19  ?  267 GLU   A O   1 
ATOM   749  C  CB  . GLU   A 1 111 ? -2.998  25.083  18.943  1.00 61.30  ?  267 GLU   A CB  1 
ATOM   750  C  CG  . GLU   A 1 111 ? -2.056  24.073  18.351  1.00 56.53  ?  267 GLU   A CG  1 
ATOM   751  C  CD  . GLU   A 1 111 ? -0.606  24.498  18.411  1.00 71.06  ?  267 GLU   A CD  1 
ATOM   752  O  OE1 . GLU   A 1 111 ? -0.226  25.331  19.279  1.00 66.10  ?  267 GLU   A OE1 1 
ATOM   753  O  OE2 . GLU   A 1 111 ? 0.154   24.026  17.535  1.00 78.91  -1 267 GLU   A OE2 1 
ATOM   754  N  N   . GLY   A 1 112 ? -3.458  26.762  22.099  1.00 53.25  ?  268 GLY   A N   1 
ATOM   755  C  CA  . GLY   A 1 112 ? -4.140  27.833  22.792  1.00 57.74  ?  268 GLY   A CA  1 
ATOM   756  C  C   . GLY   A 1 112 ? -5.491  27.393  23.312  1.00 62.97  ?  268 GLY   A C   1 
ATOM   757  O  O   . GLY   A 1 112 ? -5.580  26.485  24.141  1.00 68.56  ?  268 GLY   A O   1 
ATOM   758  N  N   . GLU   A 1 113 ? -6.550  28.031  22.826  1.00 60.96  ?  269 GLU   A N   1 
ATOM   759  C  CA  . GLU   A 1 113 ? -7.918  27.671  23.162  1.00 56.47  ?  269 GLU   A CA  1 
ATOM   760  C  C   . GLU   A 1 113 ? -8.541  26.690  22.179  1.00 57.49  ?  269 GLU   A C   1 
ATOM   761  O  O   . GLU   A 1 113 ? -9.686  26.276  22.391  1.00 57.44  ?  269 GLU   A O   1 
ATOM   762  C  CB  . GLU   A 1 113 ? -8.778  28.934  23.239  1.00 64.71  ?  269 GLU   A CB  1 
ATOM   763  C  CG  . GLU   A 1 113 ? -8.777  29.629  24.578  1.00 70.11  ?  269 GLU   A CG  1 
ATOM   764  C  CD  . GLU   A 1 113 ? -10.189 30.056  24.955  1.00 77.45  ?  269 GLU   A CD  1 
ATOM   765  O  OE1 . GLU   A 1 113 ? -11.044 29.166  25.200  1.00 74.15  ?  269 GLU   A OE1 1 
ATOM   766  O  OE2 . GLU   A 1 113 ? -10.435 31.281  25.033  1.00 82.55  -1 269 GLU   A OE2 1 
ATOM   767  N  N   . ILE   A 1 114 ? -7.806  26.299  21.137  1.00 55.92  ?  270 ILE   A N   1 
ATOM   768  C  CA  . ILE   A 1 114 ? -8.327  25.538  20.001  1.00 59.61  ?  270 ILE   A CA  1 
ATOM   769  C  C   . ILE   A 1 114 ? -7.810  24.106  20.030  1.00 52.29  ?  270 ILE   A C   1 
ATOM   770  O  O   . ILE   A 1 114 ? -6.603  23.874  20.169  1.00 55.46  ?  270 ILE   A O   1 
ATOM   771  C  CB  . ILE   A 1 114 ? -7.953  26.224  18.672  1.00 55.81  ?  270 ILE   A CB  1 
ATOM   772  C  CG1 . ILE   A 1 114 ? -8.900  27.382  18.400  1.00 47.63  ?  270 ILE   A CG1 1 
ATOM   773  C  CG2 . ILE   A 1 114 ? -7.882  25.245  17.535  1.00 63.17  ?  270 ILE   A CG2 1 
ATOM   774  C  CD1 . ILE   A 1 114 ? -10.311 26.981  18.620  1.00 54.59  ?  270 ILE   A CD1 1 
ATOM   775  N  N   . LEU   A 1 115 ? -8.723  23.152  19.869  1.00 56.42  ?  271 LEU   A N   1 
ATOM   776  C  CA  . LEU   A 1 115 ? -8.348  21.777  19.559  1.00 53.82  ?  271 LEU   A CA  1 
ATOM   777  C  C   . LEU   A 1 115 ? -7.685  21.702  18.186  1.00 54.60  ?  271 LEU   A C   1 
ATOM   778  O  O   . LEU   A 1 115 ? -8.323  21.983  17.162  1.00 53.18  ?  271 LEU   A O   1 
ATOM   779  C  CB  . LEU   A 1 115 ? -9.590  20.882  19.597  1.00 47.38  ?  271 LEU   A CB  1 
ATOM   780  C  CG  . LEU   A 1 115 ? -9.280  19.387  19.677  1.00 54.02  ?  271 LEU   A CG  1 
ATOM   781  C  CD1 . LEU   A 1 115 ? -8.864  18.994  21.094  1.00 51.01  ?  271 LEU   A CD1 1 
ATOM   782  C  CD2 . LEU   A 1 115 ? -10.450 18.532  19.189  1.00 42.22  ?  271 LEU   A CD2 1 
ATOM   783  N  N   . SER   A 1 116 ? -6.419  21.285  18.154  1.00 48.43  ?  272 SER   A N   1 
ATOM   784  C  CA  . SER   A 1 116 ? -5.654  21.253  16.907  1.00 48.48  ?  272 SER   A CA  1 
ATOM   785  C  C   . SER   A 1 116 ? -5.966  19.984  16.112  1.00 51.41  ?  272 SER   A C   1 
ATOM   786  O  O   . SER   A 1 116 ? -5.631  18.870  16.533  1.00 49.29  ?  272 SER   A O   1 
ATOM   787  C  CB  . SER   A 1 116 ? -4.159  21.355  17.187  1.00 49.63  ?  272 SER   A CB  1 
ATOM   788  O  OG  . SER   A 1 116 ? -3.424  21.102  16.001  1.00 54.19  ?  272 SER   A OG  1 
ATOM   789  N  N   . ALA   A 1 117 ? -6.582  20.155  14.938  1.00 43.50  ?  273 ALA   A N   1 
ATOM   790  C  CA  . ALA   A 1 117 ? -6.781  19.018  14.045  1.00 46.54  ?  273 ALA   A CA  1 
ATOM   791  C  C   . ALA   A 1 117 ? -5.452  18.390  13.641  1.00 48.45  ?  273 ALA   A C   1 
ATOM   792  O  O   . ALA   A 1 117 ? -5.331  17.160  13.583  1.00 53.75  ?  273 ALA   A O   1 
ATOM   793  C  CB  . ALA   A 1 117 ? -7.578  19.452  12.810  1.00 51.14  ?  273 ALA   A CB  1 
ATOM   794  N  N   . SER   A 1 118 ? -4.438  19.219  13.378  1.00 51.83  ?  274 SER   A N   1 
ATOM   795  C  CA  . SER   A 1 118 ? -3.113  18.711  13.031  1.00 53.25  ?  274 SER   A CA  1 
ATOM   796  C  C   . SER   A 1 118 ? -2.587  17.749  14.092  1.00 51.03  ?  274 SER   A C   1 
ATOM   797  O  O   . SER   A 1 118 ? -2.140  16.639  13.781  1.00 54.45  ?  274 SER   A O   1 
ATOM   798  C  CB  . SER   A 1 118 ? -2.135  19.876  12.861  1.00 54.54  ?  274 SER   A CB  1 
ATOM   799  O  OG  . SER   A 1 118 ? -2.495  20.706  11.772  1.00 59.29  ?  274 SER   A OG  1 
ATOM   800  N  N   . LYS   A 1 119 ? -2.604  18.168  15.353  1.00 55.80  ?  275 LYS   A N   1 
ATOM   801  C  CA  . LYS   A 1 119 ? -1.996  17.338  16.387  1.00 54.69  ?  275 LYS   A CA  1 
ATOM   802  C  C   . LYS   A 1 119 ? -2.823  16.086  16.640  1.00 52.21  ?  275 LYS   A C   1 
ATOM   803  O  O   . LYS   A 1 119 ? -2.277  14.988  16.807  1.00 61.18  ?  275 LYS   A O   1 
ATOM   804  C  CB  . LYS   A 1 119 ? -1.813  18.152  17.665  1.00 58.32  ?  275 LYS   A CB  1 
ATOM   805  C  CG  . LYS   A 1 119 ? -0.836  19.294  17.465  1.00 52.33  ?  275 LYS   A CG  1 
ATOM   806  C  CD  . LYS   A 1 119 ? -0.025  19.570  18.698  1.00 65.52  ?  275 LYS   A CD  1 
ATOM   807  C  CE  . LYS   A 1 119 ? -0.741  20.575  19.566  1.00 65.14  ?  275 LYS   A CE  1 
ATOM   808  N  NZ  . LYS   A 1 119 ? 0.172   21.104  20.613  1.00 60.94  ?  275 LYS   A NZ  1 
ATOM   809  N  N   . MET   A 1 120 ? -4.141  16.226  16.643  1.00 50.94  ?  276 MET   A N   1 
ATOM   810  C  CA  . MET   A 1 120 ? -4.984  15.076  16.925  1.00 58.21  ?  276 MET   A CA  1 
ATOM   811  C  C   . MET   A 1 120 ? -4.953  14.078  15.777  1.00 52.35  ?  276 MET   A C   1 
ATOM   812  O  O   . MET   A 1 120 ? -5.072  12.868  15.993  1.00 56.15  ?  276 MET   A O   1 
ATOM   813  C  CB  . MET   A 1 120 ? -6.402  15.544  17.211  1.00 52.89  ?  276 MET   A CB  1 
ATOM   814  C  CG  . MET   A 1 120 ? -7.019  14.798  18.370  1.00 60.19  ?  276 MET   A CG  1 
ATOM   815  S  SD  . MET   A 1 120 ? -8.732  15.260  18.549  1.00 73.86  ?  276 MET   A SD  1 
ATOM   816  C  CE  . MET   A 1 120 ? -9.441  13.753  19.121  1.00 47.14  ?  276 MET   A CE  1 
ATOM   817  N  N   . LEU   A 1 121 ? -4.772  14.566  14.551  1.00 52.86  ?  277 LEU   A N   1 
ATOM   818  C  CA  . LEU   A 1 121 ? -4.508  13.661  13.442  1.00 53.20  ?  277 LEU   A CA  1 
ATOM   819  C  C   . LEU   A 1 121 ? -3.180  12.935  13.608  1.00 55.88  ?  277 LEU   A C   1 
ATOM   820  O  O   . LEU   A 1 121 ? -3.096  11.729  13.340  1.00 57.08  ?  277 LEU   A O   1 
ATOM   821  C  CB  . LEU   A 1 121 ? -4.543  14.426  12.129  1.00 49.47  ?  277 LEU   A CB  1 
ATOM   822  C  CG  . LEU   A 1 121 ? -5.919  14.464  11.476  1.00 48.02  ?  277 LEU   A CG  1 
ATOM   823  C  CD1 . LEU   A 1 121 ? -5.744  15.011  10.101  1.00 48.04  ?  277 LEU   A CD1 1 
ATOM   824  C  CD2 . LEU   A 1 121 ? -6.469  13.057  11.406  1.00 45.18  ?  277 LEU   A CD2 1 
ATOM   825  N  N   . SER   A 1 122 ? -2.128  13.651  14.038  1.00 52.09  ?  278 SER   A N   1 
ATOM   826  C  CA  . SER   A 1 122 ? -0.823  13.025  14.259  1.00 56.94  ?  278 SER   A CA  1 
ATOM   827  C  C   . SER   A 1 122 ? -0.940  11.802  15.151  1.00 55.38  ?  278 SER   A C   1 
ATOM   828  O  O   . SER   A 1 122 ? -0.422  10.726  14.828  1.00 54.46  ?  278 SER   A O   1 
ATOM   829  C  CB  . SER   A 1 122 ? 0.166   14.010  14.899  1.00 55.35  ?  278 SER   A CB  1 
ATOM   830  O  OG  . SER   A 1 122 ? 0.796   14.843  13.946  1.00 64.65  ?  278 SER   A OG  1 
ATOM   831  N  N   . LYS   A 1 123 ? -1.611  11.959  16.292  1.00 54.30  ?  279 LYS   A N   1 
ATOM   832  C  CA  . LYS   A 1 123 ? -1.657  10.868  17.251  1.00 59.76  ?  279 LYS   A CA  1 
ATOM   833  C  C   . LYS   A 1 123 ? -2.528  9.742   16.720  1.00 52.04  ?  279 LYS   A C   1 
ATOM   834  O  O   . LYS   A 1 123 ? -2.155  8.564   16.794  1.00 56.66  ?  279 LYS   A O   1 
ATOM   835  C  CB  . LYS   A 1 123 ? -2.182  11.371  18.593  1.00 53.10  ?  279 LYS   A CB  1 
ATOM   836  C  CG  . LYS   A 1 123 ? -2.484  10.256  19.567  1.00 61.25  ?  279 LYS   A CG  1 
ATOM   837  C  CD  . LYS   A 1 123 ? -1.349  10.176  20.577  1.00 56.12  ?  279 LYS   A CD  1 
ATOM   838  C  CE  . LYS   A 1 123 ? -1.716  9.378   21.828  1.00 75.31  ?  279 LYS   A CE  1 
ATOM   839  N  NZ  . LYS   A 1 123 ? -2.371  10.174  22.896  1.00 72.23  ?  279 LYS   A NZ  1 
ATOM   840  N  N   . PHE   A 1 124 ? -3.685  10.101  16.161  1.00 57.36  ?  280 PHE   A N   1 
ATOM   841  C  CA  . PHE   A 1 124 ? -4.561  9.120   15.536  1.00 50.85  ?  280 PHE   A CA  1 
ATOM   842  C  C   . PHE   A 1 124 ? -3.778  8.266   14.542  1.00 52.07  ?  280 PHE   A C   1 
ATOM   843  O  O   . PHE   A 1 124 ? -3.882  7.032   14.555  1.00 49.43  ?  280 PHE   A O   1 
ATOM   844  C  CB  . PHE   A 1 124 ? -5.731  9.866   14.885  1.00 53.68  ?  280 PHE   A CB  1 
ATOM   845  C  CG  . PHE   A 1 124 ? -6.811  8.981   14.310  1.00 46.91  ?  280 PHE   A CG  1 
ATOM   846  C  CD1 . PHE   A 1 124 ? -7.689  8.317   15.154  1.00 43.96  ?  280 PHE   A CD1 1 
ATOM   847  C  CD2 . PHE   A 1 124 ? -7.020  8.909   12.942  1.00 41.98  ?  280 PHE   A CD2 1 
ATOM   848  C  CE1 . PHE   A 1 124 ? -8.715  7.530   14.649  1.00 52.17  ?  280 PHE   A CE1 1 
ATOM   849  C  CE2 . PHE   A 1 124 ? -8.044  8.127   12.425  1.00 47.32  ?  280 PHE   A CE2 1 
ATOM   850  C  CZ  . PHE   A 1 124 ? -8.902  7.443   13.278  1.00 43.88  ?  280 PHE   A CZ  1 
ATOM   851  N  N   . ARG   A 1 125 ? -2.910  8.903   13.743  1.00 50.06  ?  281 ARG   A N   1 
ATOM   852  C  CA  . ARG   A 1 125 ? -2.128  8.174   12.745  1.00 51.28  ?  281 ARG   A CA  1 
ATOM   853  C  C   . ARG   A 1 125 ? -1.040  7.323   13.389  1.00 57.31  ?  281 ARG   A C   1 
ATOM   854  O  O   . ARG   A 1 125 ? -0.825  6.174   12.977  1.00 61.88  ?  281 ARG   A O   1 
ATOM   855  C  CB  . ARG   A 1 125 ? -1.502  9.141   11.736  1.00 50.05  ?  281 ARG   A CB  1 
ATOM   856  C  CG  . ARG   A 1 125 ? -2.424  9.562   10.618  1.00 54.91  ?  281 ARG   A CG  1 
ATOM   857  C  CD  . ARG   A 1 125 ? -2.052  10.915  10.030  1.00 50.64  ?  281 ARG   A CD  1 
ATOM   858  N  NE  . ARG   A 1 125 ? -2.863  11.194  8.851   1.00 54.79  ?  281 ARG   A NE  1 
ATOM   859  C  CZ  . ARG   A 1 125 ? -2.890  12.355  8.211   1.00 54.04  ?  281 ARG   A CZ  1 
ATOM   860  N  NH1 . ARG   A 1 125 ? -2.161  13.381  8.615   1.00 48.31  ?  281 ARG   A NH1 1 
ATOM   861  N  NH2 . ARG   A 1 125 ? -3.647  12.481  7.119   1.00 52.50  ?  281 ARG   A NH2 1 
ATOM   862  N  N   . LYS   A 1 126 ? -0.313  7.883   14.369  1.00 60.36  ?  282 LYS   A N   1 
ATOM   863  C  CA  . LYS   A 1 126 ? 0.703   7.113   15.087  1.00 56.64  ?  282 LYS   A CA  1 
ATOM   864  C  C   . LYS   A 1 126 ? 0.140   5.812   15.635  1.00 61.58  ?  282 LYS   A C   1 
ATOM   865  O  O   . LYS   A 1 126 ? 0.727   4.737   15.444  1.00 64.84  ?  282 LYS   A O   1 
ATOM   866  C  CB  . LYS   A 1 126 ? 1.288   7.923   16.239  1.00 59.11  ?  282 LYS   A CB  1 
ATOM   867  C  CG  . LYS   A 1 126 ? 2.397   7.164   16.962  1.00 70.64  ?  282 LYS   A CG  1 
ATOM   868  C  CD  . LYS   A 1 126 ? 2.397   7.464   18.468  1.00 71.95  ?  282 LYS   A CD  1 
ATOM   869  C  CE  . LYS   A 1 126 ? 3.236   8.645   18.856  1.00 57.53  ?  282 LYS   A CE  1 
ATOM   870  N  NZ  . LYS   A 1 126 ? 4.451   8.110   19.537  1.00 75.52  ?  282 LYS   A NZ  1 
ATOM   871  N  N   . ILE   A 1 127 ? -0.978  5.896   16.356  1.00 56.97  ?  283 ILE   A N   1 
ATOM   872  C  CA  . ILE   A 1 127 ? -1.511  4.715   17.026  1.00 61.28  ?  283 ILE   A CA  1 
ATOM   873  C  C   . ILE   A 1 127 ? -1.899  3.659   16.004  1.00 62.14  ?  283 ILE   A C   1 
ATOM   874  O  O   . ILE   A 1 127 ? -1.612  2.467   16.177  1.00 67.93  ?  283 ILE   A O   1 
ATOM   875  C  CB  . ILE   A 1 127 ? -2.707  5.099   17.910  1.00 63.91  ?  283 ILE   A CB  1 
ATOM   876  C  CG1 . ILE   A 1 127 ? -2.237  5.891   19.122  1.00 57.83  ?  283 ILE   A CG1 1 
ATOM   877  C  CG2 . ILE   A 1 127 ? -3.405  3.850   18.383  1.00 58.06  ?  283 ILE   A CG2 1 
ATOM   878  C  CD1 . ILE   A 1 127 ? -3.378  6.437   19.936  1.00 63.98  ?  283 ILE   A CD1 1 
ATOM   879  N  N   . ILE   A 1 128 ? -2.564  4.076   14.926  1.00 62.30  ?  284 ILE   A N   1 
ATOM   880  C  CA  . ILE   A 1 128 ? -2.970  3.122   13.900  1.00 62.19  ?  284 ILE   A CA  1 
ATOM   881  C  C   . ILE   A 1 128 ? -1.739  2.460   13.283  1.00 63.97  ?  284 ILE   A C   1 
ATOM   882  O  O   . ILE   A 1 128 ? -1.711  1.243   13.074  1.00 64.30  ?  284 ILE   A O   1 
ATOM   883  C  CB  . ILE   A 1 128 ? -3.851  3.814   12.838  1.00 59.56  ?  284 ILE   A CB  1 
ATOM   884  C  CG1 . ILE   A 1 128 ? -5.192  4.216   13.440  1.00 55.14  ?  284 ILE   A CG1 1 
ATOM   885  C  CG2 . ILE   A 1 128 ? -4.144  2.875   11.685  1.00 55.92  ?  284 ILE   A CG2 1 
ATOM   886  C  CD1 . ILE   A 1 128 ? -6.002  5.128   12.538  1.00 57.94  ?  284 ILE   A CD1 1 
ATOM   887  N  N   . LYS   A 1 129 ? -0.693  3.244   13.004  1.00 63.67  ?  285 LYS   A N   1 
ATOM   888  C  CA  . LYS   A 1 129 ? 0.540   2.666   12.477  1.00 59.81  ?  285 LYS   A CA  1 
ATOM   889  C  C   . LYS   A 1 129 ? 1.120   1.615   13.422  1.00 74.85  ?  285 LYS   A C   1 
ATOM   890  O  O   . LYS   A 1 129 ? 1.628   0.580   12.974  1.00 76.77  ?  285 LYS   A O   1 
ATOM   891  C  CB  . LYS   A 1 129 ? 1.572   3.761   12.219  1.00 69.88  ?  285 LYS   A CB  1 
ATOM   892  C  CG  . LYS   A 1 129 ? 2.288   3.643   10.886  1.00 69.39  ?  285 LYS   A CG  1 
ATOM   893  C  CD  . LYS   A 1 129 ? 3.337   4.735   10.748  1.00 70.31  ?  285 LYS   A CD  1 
ATOM   894  C  CE  . LYS   A 1 129 ? 2.702   6.051   10.341  1.00 69.34  ?  285 LYS   A CE  1 
ATOM   895  N  NZ  . LYS   A 1 129 ? 3.720   7.052   9.902   1.00 75.75  ?  285 LYS   A NZ  1 
ATOM   896  N  N   . GLU   A 1 130 ? 1.058   1.865   14.732  1.00 64.57  ?  286 GLU   A N   1 
ATOM   897  C  CA  . GLU   A 1 130 ? 1.527   0.889   15.710  1.00 78.95  ?  286 GLU   A CA  1 
ATOM   898  C  C   . GLU   A 1 130 ? 0.817   -0.453  15.557  1.00 77.54  ?  286 GLU   A C   1 
ATOM   899  O  O   . GLU   A 1 130 ? 1.460   -1.501  15.394  1.00 73.99  ?  286 GLU   A O   1 
ATOM   900  C  CB  . GLU   A 1 130 ? 1.327   1.438   17.123  1.00 74.30  ?  286 GLU   A CB  1 
ATOM   901  C  CG  . GLU   A 1 130 ? 2.197   2.628   17.487  1.00 71.74  ?  286 GLU   A CG  1 
ATOM   902  C  CD  . GLU   A 1 130 ? 1.757   3.244   18.800  1.00 80.26  ?  286 GLU   A CD  1 
ATOM   903  O  OE1 . GLU   A 1 130 ? 0.793   2.712   19.401  1.00 81.54  ?  286 GLU   A OE1 1 
ATOM   904  O  OE2 . GLU   A 1 130 ? 2.413   4.204   19.267  1.00 86.67  -1 286 GLU   A OE2 1 
ATOM   905  N  N   . GLU   A 1 131 ? -0.517  -0.436  15.624  1.00 70.14  ?  287 GLU   A N   1 
ATOM   906  C  CA  . GLU   A 1 131 ? -1.280  -1.681  15.608  1.00 73.54  ?  287 GLU   A CA  1 
ATOM   907  C  C   . GLU   A 1 131 ? -1.090  -2.432  14.291  1.00 77.72  ?  287 GLU   A C   1 
ATOM   908  O  O   . GLU   A 1 131 ? -0.882  -3.652  14.285  1.00 77.25  ?  287 GLU   A O   1 
ATOM   909  C  CB  . GLU   A 1 131 ? -2.756  -1.388  15.860  1.00 70.46  ?  287 GLU   A CB  1 
ATOM   910  N  N   . ILE   A 1 132 ? -1.162  -1.717  13.162  1.00 74.71  ?  288 ILE   A N   1 
ATOM   911  C  CA  . ILE   A 1 132 ? -0.917  -2.339  11.860  1.00 74.58  ?  288 ILE   A CA  1 
ATOM   912  C  C   . ILE   A 1 132 ? 0.450   -3.014  11.836  1.00 74.34  ?  288 ILE   A C   1 
ATOM   913  O  O   . ILE   A 1 132 ? 0.599   -4.133  11.326  1.00 76.33  ?  288 ILE   A O   1 
ATOM   914  C  CB  . ILE   A 1 132 ? -1.062  -1.298  10.730  1.00 68.81  ?  288 ILE   A CB  1 
ATOM   915  C  CG1 . ILE   A 1 132 ? -2.410  -0.588  10.829  1.00 64.15  ?  288 ILE   A CG1 1 
ATOM   916  C  CG2 . ILE   A 1 132 ? -0.881  -1.935  9.356   1.00 66.60  ?  288 ILE   A CG2 1 
ATOM   917  C  CD1 . ILE   A 1 132 ? -3.576  -1.536  10.825  1.00 65.26  ?  288 ILE   A CD1 1 
ATOM   918  N  N   . ASN   A 1 133 ? 1.468   -2.345  12.387  1.00 78.29  ?  289 ASN   A N   1 
ATOM   919  C  CA  . ASN   A 1 133 ? 2.802   -2.938  12.447  1.00 75.89  ?  289 ASN   A CA  1 
ATOM   920  C  C   . ASN   A 1 133 ? 2.776   -4.282  13.161  1.00 76.05  ?  289 ASN   A C   1 
ATOM   921  O  O   . ASN   A 1 133 ? 3.466   -5.224  12.752  1.00 82.65  ?  289 ASN   A O   1 
ATOM   922  C  CB  . ASN   A 1 133 ? 3.787   -1.978  13.127  1.00 78.25  ?  289 ASN   A CB  1 
ATOM   923  C  CG  . ASN   A 1 133 ? 4.198   -0.813  12.223  1.00 88.35  ?  289 ASN   A CG  1 
ATOM   924  O  OD1 . ASN   A 1 133 ? 4.119   -0.903  10.995  1.00 86.76  ?  289 ASN   A OD1 1 
ATOM   925  N  ND2 . ASN   A 1 133 ? 4.641   0.286   12.832  1.00 90.39  ?  289 ASN   A ND2 1 
ATOM   926  N  N   . ASP   A 1 134 ? 1.958   -4.406  14.208  1.00 76.48  ?  290 ASP   A N   1 
ATOM   927  C  CA  . ASP   A 1 134 ? 1.919   -5.657  14.960  1.00 82.54  ?  290 ASP   A CA  1 
ATOM   928  C  C   . ASP   A 1 134 ? 1.138   -6.742  14.216  1.00 80.87  ?  290 ASP   A C   1 
ATOM   929  O  O   . ASP   A 1 134 ? 1.486   -7.926  14.296  1.00 86.42  ?  290 ASP   A O   1 
ATOM   930  C  CB  . ASP   A 1 134 ? 1.331   -5.414  16.349  1.00 80.15  ?  290 ASP   A CB  1 
ATOM   931  C  CG  . ASP   A 1 134 ? 2.303   -4.704  17.278  1.00 83.64  ?  290 ASP   A CG  1 
ATOM   932  O  OD1 . ASP   A 1 134 ? 3.507   -4.624  16.941  1.00 85.32  ?  290 ASP   A OD1 1 
ATOM   933  O  OD2 . ASP   A 1 134 ? 1.857   -4.223  18.343  1.00 89.30  -1 290 ASP   A OD2 1 
ATOM   934  N  N   . ILE   A 1 135 ? 0.088   -6.372  13.488  1.00 81.64  ?  291 ILE   A N   1 
ATOM   935  C  CA  . ILE   A 1 135 ? -0.654  -7.382  12.739  1.00 80.78  ?  291 ILE   A CA  1 
ATOM   936  C  C   . ILE   A 1 135 ? 0.173   -7.783  11.511  1.00 82.96  ?  291 ILE   A C   1 
ATOM   937  O  O   . ILE   A 1 135 ? -0.179  -7.513  10.362  1.00 85.44  ?  291 ILE   A O   1 
ATOM   938  C  CB  . ILE   A 1 135 ? -2.061  -6.891  12.365  1.00 80.77  ?  291 ILE   A CB  1 
ATOM   939  C  CG1 . ILE   A 1 135 ? -2.851  -6.565  13.633  1.00 80.66  ?  291 ILE   A CG1 1 
ATOM   940  C  CG2 . ILE   A 1 135 ? -2.824  -7.965  11.603  1.00 84.18  ?  291 ILE   A CG2 1 
ATOM   941  C  CD1 . ILE   A 1 135 ? -4.167  -5.860  13.377  1.00 71.94  ?  291 ILE   A CD1 1 
ATOM   942  N  N   . ASP   A 1 139 ? -1.307  -9.383  8.421   1.00 79.43  ?  295 ASP   A N   1 
ATOM   943  C  CA  . ASP   A 1 139 ? -0.731  -9.022  7.124   1.00 78.63  ?  295 ASP   A CA  1 
ATOM   944  C  C   . ASP   A 1 139 ? -1.310  -7.707  6.613   1.00 79.58  ?  295 ASP   A C   1 
ATOM   945  O  O   . ASP   A 1 139 ? -1.419  -7.495  5.405   1.00 88.84  ?  295 ASP   A O   1 
ATOM   946  C  CB  . ASP   A 1 139 ? -0.969  -10.129 6.092   1.00 77.79  ?  295 ASP   A CB  1 
ATOM   947  N  N   . VAL   A 1 140 ? -1.677  -6.819  7.551   1.00 75.99  ?  296 VAL   A N   1 
ATOM   948  C  CA  . VAL   A 1 140 ? -2.244  -5.517  7.193   1.00 73.88  ?  296 VAL   A CA  1 
ATOM   949  C  C   . VAL   A 1 140 ? -1.125  -4.525  6.929   1.00 74.33  ?  296 VAL   A C   1 
ATOM   950  O  O   . VAL   A 1 140 ? -0.073  -4.555  7.592   1.00 79.57  ?  296 VAL   A O   1 
ATOM   951  C  CB  . VAL   A 1 140 ? -3.185  -5.017  8.301   1.00 73.02  ?  296 VAL   A CB  1 
ATOM   952  N  N   . ILE   A 1 141 ? -1.348  -3.625  5.966   1.00 69.06  ?  297 ILE   A N   1 
ATOM   953  C  CA  . ILE   A 1 141 ? -0.403  -2.559  5.644   1.00 67.76  ?  297 ILE   A CA  1 
ATOM   954  C  C   . ILE   A 1 141 ? -1.157  -1.240  5.648   1.00 66.10  ?  297 ILE   A C   1 
ATOM   955  O  O   . ILE   A 1 141 ? -2.362  -1.190  5.364   1.00 67.55  ?  297 ILE   A O   1 
ATOM   956  C  CB  . ILE   A 1 141 ? 0.296   -2.790  4.292   1.00 67.28  ?  297 ILE   A CB  1 
ATOM   957  N  N   . MET   A 1 142 ? -0.440  -0.171  5.954   1.00 65.41  ?  298 MET   A N   1 
ATOM   958  C  CA  . MET   A 1 142 ? -1.045  1.144   6.106   1.00 64.56  ?  298 MET   A CA  1 
ATOM   959  C  C   . MET   A 1 142 ? -0.419  2.146   5.150   1.00 63.00  ?  298 MET   A C   1 
ATOM   960  O  O   . MET   A 1 142 ? 0.692   1.946   4.648   1.00 71.25  ?  298 MET   A O   1 
ATOM   961  C  CB  . MET   A 1 142 ? -0.908  1.659   7.538   1.00 66.86  ?  298 MET   A CB  1 
ATOM   962  C  CG  . MET   A 1 142 ? -1.797  2.840   7.812   1.00 61.42  ?  298 MET   A CG  1 
ATOM   963  S  SD  . MET   A 1 142 ? -1.530  3.468   9.457   1.00 96.25  ?  298 MET   A SD  1 
ATOM   964  C  CE  . MET   A 1 142 ? -0.813  5.079   9.097   1.00 65.58  ?  298 MET   A CE  1 
ATOM   965  N  N   . LYS   A 1 143 ? -1.160  3.226   4.909   1.00 62.64  ?  299 LYS   A N   1 
ATOM   966  C  CA  . LYS   A 1 143 ? -0.689  4.361   4.134   1.00 58.53  ?  299 LYS   A CA  1 
ATOM   967  C  C   . LYS   A 1 143 ? -1.453  5.600   4.591   1.00 63.49  ?  299 LYS   A C   1 
ATOM   968  O  O   . LYS   A 1 143 ? -2.675  5.557   4.772   1.00 56.25  ?  299 LYS   A O   1 
ATOM   969  C  CB  . LYS   A 1 143 ? -0.878  4.118   2.635   1.00 63.83  ?  299 LYS   A CB  1 
ATOM   970  N  N   . ARG   A 1 144 ? -0.720  6.690   4.783   1.00 65.45  ?  300 ARG   A N   1 
ATOM   971  C  CA  . ARG   A 1 144 ? -1.311  7.956   5.200   1.00 56.86  ?  300 ARG   A CA  1 
ATOM   972  C  C   . ARG   A 1 144 ? -1.988  8.638   4.013   1.00 54.76  ?  300 ARG   A C   1 
ATOM   973  O  O   . ARG   A 1 144 ? -1.449  8.664   2.905   1.00 62.86  ?  300 ARG   A O   1 
ATOM   974  C  CB  . ARG   A 1 144 ? -0.227  8.862   5.798   1.00 58.67  ?  300 ARG   A CB  1 
ATOM   975  N  N   . LYS   A 1 145 ? -3.182  9.175   4.240   1.00 53.24  ?  301 LYS   A N   1 
ATOM   976  C  CA  . LYS   A 1 145 ? -3.925  9.822   3.162   1.00 59.84  ?  301 LYS   A CA  1 
ATOM   977  C  C   . LYS   A 1 145 ? -3.612  11.311  3.075   1.00 58.76  ?  301 LYS   A C   1 
ATOM   978  O  O   . LYS   A 1 145 ? -3.649  12.016  4.079   1.00 61.58  ?  301 LYS   A O   1 
ATOM   979  C  CB  . LYS   A 1 145 ? -5.427  9.605   3.347   1.00 57.01  ?  301 LYS   A CB  1 
ATOM   980  C  CG  . LYS   A 1 145 ? -6.297  10.319  2.320   1.00 58.94  ?  301 LYS   A CG  1 
ATOM   981  C  CD  . LYS   A 1 145 ? -6.489  9.486   1.050   1.00 52.91  ?  301 LYS   A CD  1 
ATOM   982  C  CE  . LYS   A 1 145 ? -7.415  8.322   1.299   1.00 49.72  ?  301 LYS   A CE  1 
ATOM   983  N  NZ  . LYS   A 1 145 ? -8.465  8.185   0.237   1.00 53.87  ?  301 LYS   A NZ  1 
ATOM   984  N  N   . GLY   A 1 148 ? -6.913  15.863  5.634   1.00 44.10  ?  304 GLY   A N   1 
ATOM   985  C  CA  . GLY   A 1 148 ? -7.102  15.276  6.937   1.00 38.28  ?  304 GLY   A CA  1 
ATOM   986  C  C   . GLY   A 1 148 ? -8.150  14.185  7.029   1.00 44.25  ?  304 GLY   A C   1 
ATOM   987  O  O   . GLY   A 1 148 ? -7.994  13.259  7.819   1.00 50.54  ?  304 GLY   A O   1 
ATOM   988  N  N   . SER   A 1 149 ? -9.214  14.287  6.238   1.00 45.13  ?  305 SER   A N   1 
ATOM   989  C  CA  . SER   A 1 149 ? -10.288 13.290  6.217   1.00 41.99  ?  305 SER   A CA  1 
ATOM   990  C  C   . SER   A 1 149 ? -10.481 12.760  4.798   1.00 52.73  ?  305 SER   A C   1 
ATOM   991  O  O   . SER   A 1 149 ? -10.933 13.518  3.929   1.00 48.17  ?  305 SER   A O   1 
ATOM   992  C  CB  . SER   A 1 149 ? -11.594 13.885  6.724   1.00 37.47  ?  305 SER   A CB  1 
ATOM   993  O  OG  . SER   A 1 149 ? -11.544 14.242  8.093   1.00 36.26  ?  305 SER   A OG  1 
ATOM   994  N  N   . PRO   A 1 150 ? -10.236 11.460  4.529   1.00 44.79  ?  306 PRO   A N   1 
ATOM   995  C  CA  . PRO   A 1 150 ? -9.824  10.386  5.463   1.00 45.51  ?  306 PRO   A CA  1 
ATOM   996  C  C   . PRO   A 1 150 ? -8.428  10.596  6.002   1.00 46.97  ?  306 PRO   A C   1 
ATOM   997  O  O   . PRO   A 1 150 ? -7.636  11.283  5.349   1.00 47.48  ?  306 PRO   A O   1 
ATOM   998  C  CB  . PRO   A 1 150 ? -9.924  9.112   4.598   1.00 45.34  ?  306 PRO   A CB  1 
ATOM   999  C  CG  . PRO   A 1 150 ? -10.730 9.537   3.347   1.00 44.25  ?  306 PRO   A CG  1 
ATOM   1000 C  CD  . PRO   A 1 150 ? -10.320 10.963  3.148   1.00 44.42  ?  306 PRO   A CD  1 
ATOM   1001 N  N   . ALA   A 1 151 ? -8.094  10.028  7.162   1.00 47.99  ?  307 ALA   A N   1 
ATOM   1002 C  CA  . ALA   A 1 151 ? -6.791  10.222  7.791   1.00 43.28  ?  307 ALA   A CA  1 
ATOM   1003 C  C   . ALA   A 1 151 ? -5.778  9.167   7.376   1.00 48.31  ?  307 ALA   A C   1 
ATOM   1004 O  O   . ALA   A 1 151 ? -4.588  9.482   7.231   1.00 48.18  ?  307 ALA   A O   1 
ATOM   1005 C  CB  . ALA   A 1 151 ? -6.941  10.209  9.315   1.00 43.62  ?  307 ALA   A CB  1 
ATOM   1006 N  N   . VAL   A 1 152 ? -6.222  7.915   7.204   1.00 51.68  ?  308 VAL   A N   1 
ATOM   1007 C  CA  . VAL   A 1 152 ? -5.345  6.831   6.781   1.00 47.46  ?  308 VAL   A CA  1 
ATOM   1008 C  C   . VAL   A 1 152 ? -6.108  5.908   5.841   1.00 43.42  ?  308 VAL   A C   1 
ATOM   1009 O  O   . VAL   A 1 152 ? -7.339  5.916   5.786   1.00 45.09  ?  308 VAL   A O   1 
ATOM   1010 C  CB  . VAL   A 1 152 ? -4.800  6.018   7.979   1.00 45.91  ?  308 VAL   A CB  1 
ATOM   1011 C  CG1 . VAL   A 1 152 ? -3.912  6.877   8.881   1.00 49.40  ?  308 VAL   A CG1 1 
ATOM   1012 C  CG2 . VAL   A 1 152 ? -5.947  5.387   8.747   1.00 43.64  ?  308 VAL   A CG2 1 
ATOM   1013 N  N   . THR   A 1 153 ? -5.350  5.090   5.111   1.00 49.26  ?  309 THR   A N   1 
ATOM   1014 C  CA  . THR   A 1 153 ? -5.903  4.021   4.286   1.00 49.84  ?  309 THR   A CA  1 
ATOM   1015 C  C   . THR   A 1 153 ? -5.189  2.734   4.659   1.00 53.46  ?  309 THR   A C   1 
ATOM   1016 O  O   . THR   A 1 153 ? -3.961  2.663   4.569   1.00 56.34  ?  309 THR   A O   1 
ATOM   1017 C  CB  . THR   A 1 153 ? -5.718  4.313   2.793   1.00 52.85  ?  309 THR   A CB  1 
ATOM   1018 O  OG1 . THR   A 1 153 ? -6.389  5.533   2.449   1.00 50.14  ?  309 THR   A OG1 1 
ATOM   1019 C  CG2 . THR   A 1 153 ? -6.258  3.177   1.946   1.00 45.32  ?  309 THR   A CG2 1 
ATOM   1020 N  N   . LEU   A 1 154 ? -5.948  1.726   5.077   1.00 55.97  ?  310 LEU   A N   1 
ATOM   1021 C  CA  . LEU   A 1 154 ? -5.384  0.423   5.390   1.00 54.01  ?  310 LEU   A CA  1 
ATOM   1022 C  C   . LEU   A 1 154 ? -5.503  -0.480  4.173   1.00 52.03  ?  310 LEU   A C   1 
ATOM   1023 O  O   . LEU   A 1 154 ? -6.563  -0.540  3.544   1.00 55.75  ?  310 LEU   A O   1 
ATOM   1024 C  CB  . LEU   A 1 154 ? -6.105  -0.242  6.561   1.00 51.75  ?  310 LEU   A CB  1 
ATOM   1025 C  CG  . LEU   A 1 154 ? -6.379  0.549   7.830   1.00 49.27  ?  310 LEU   A CG  1 
ATOM   1026 C  CD1 . LEU   A 1 154 ? -7.324  -0.267  8.701   1.00 48.04  ?  310 LEU   A CD1 1 
ATOM   1027 C  CD2 . LEU   A 1 154 ? -5.098  0.958   8.567   1.00 57.64  ?  310 LEU   A CD2 1 
ATOM   1028 N  N   . LEU   A 1 155 ? -4.420  -1.182  3.846   1.00 58.17  ?  311 LEU   A N   1 
ATOM   1029 C  CA  . LEU   A 1 155 ? -4.460  -2.273  2.878   1.00 58.96  ?  311 LEU   A CA  1 
ATOM   1030 C  C   . LEU   A 1 155 ? -4.563  -3.591  3.635   1.00 62.84  ?  311 LEU   A C   1 
ATOM   1031 O  O   . LEU   A 1 155 ? -3.668  -3.948  4.409   1.00 67.65  ?  311 LEU   A O   1 
ATOM   1032 C  CB  . LEU   A 1 155 ? -3.240  -2.275  1.957   1.00 58.74  ?  311 LEU   A CB  1 
ATOM   1033 C  CG  . LEU   A 1 155 ? -3.148  -1.170  0.901   1.00 60.88  ?  311 LEU   A CG  1 
ATOM   1034 C  CD1 . LEU   A 1 155 ? -4.526  -0.843  0.334   1.00 59.98  ?  311 LEU   A CD1 1 
ATOM   1035 C  CD2 . LEU   A 1 155 ? -2.477  0.070   1.459   1.00 64.63  ?  311 LEU   A CD2 1 
ATOM   1036 N  N   . ILE   A 1 156 ? -5.664  -4.294  3.424   1.00 67.95  ?  312 ILE   A N   1 
ATOM   1037 C  CA  . ILE   A 1 156 ? -5.926  -5.574  4.055   1.00 58.52  ?  312 ILE   A CA  1 
ATOM   1038 C  C   . ILE   A 1 156 ? -5.885  -6.622  2.957   1.00 62.07  ?  312 ILE   A C   1 
ATOM   1039 O  O   . ILE   A 1 156 ? -6.553  -6.472  1.926   1.00 73.40  ?  312 ILE   A O   1 
ATOM   1040 C  CB  . ILE   A 1 156 ? -7.286  -5.574  4.773   1.00 58.76  ?  312 ILE   A CB  1 
ATOM   1041 C  CG1 . ILE   A 1 156 ? -7.205  -4.777  6.072   1.00 57.03  ?  312 ILE   A CG1 1 
ATOM   1042 C  CG2 . ILE   A 1 156 ? -7.727  -6.992  5.082   1.00 67.45  ?  312 ILE   A CG2 1 
ATOM   1043 C  CD1 . ILE   A 1 156 ? -8.549  -4.266  6.548   1.00 56.20  ?  312 ILE   A CD1 1 
ATOM   1044 N  N   . SER   A 1 157 ? -5.090  -7.665  3.163   1.00 70.54  ?  313 SER   A N   1 
ATOM   1045 C  CA  . SER   A 1 157 ? -5.009  -8.755  2.183   1.00 73.14  ?  313 SER   A CA  1 
ATOM   1046 C  C   . SER   A 1 157 ? -4.568  -8.169  0.839   1.00 76.97  ?  313 SER   A C   1 
ATOM   1047 O  O   . SER   A 1 157 ? -3.908  -7.122  0.789   1.00 79.11  ?  313 SER   A O   1 
ATOM   1048 C  CB  . SER   A 1 157 ? -6.327  -9.516  2.135   1.00 72.71  ?  313 SER   A CB  1 
ATOM   1049 O  OG  . SER   A 1 157 ? -6.236  -10.755 2.821   1.00 68.91  ?  313 SER   A OG  1 
ATOM   1050 N  N   . GLU   A 1 158 ? -4.962  -8.817  -0.260  1.00 82.44  ?  314 GLU   A N   1 
ATOM   1051 C  CA  . GLU   A 1 158 ? -4.390  -8.478  -1.557  1.00 74.91  ?  314 GLU   A CA  1 
ATOM   1052 C  C   . GLU   A 1 158 ? -4.963  -7.173  -2.089  1.00 73.08  ?  314 GLU   A C   1 
ATOM   1053 O  O   . GLU   A 1 158 ? -4.211  -6.290  -2.514  1.00 81.70  ?  314 GLU   A O   1 
ATOM   1054 C  CB  . GLU   A 1 158 ? -4.621  -9.621  -2.545  1.00 73.35  ?  314 GLU   A CB  1 
ATOM   1055 C  CG  . GLU   A 1 158 ? -6.037  -10.169 -2.543  1.00 81.59  ?  314 GLU   A CG  1 
ATOM   1056 C  CD  . GLU   A 1 158 ? -6.208  -11.325 -3.505  1.00 81.98  ?  314 GLU   A CD  1 
ATOM   1057 O  OE1 . GLU   A 1 158 ? -5.217  -11.676 -4.184  1.00 80.06  ?  314 GLU   A OE1 1 
ATOM   1058 O  OE2 . GLU   A 1 158 ? -7.329  -11.877 -3.585  1.00 85.68  -1 314 GLU   A OE2 1 
ATOM   1059 N  N   . LYS   A 1 159 ? -6.292  -7.016  -2.058  1.00 67.01  ?  315 LYS   A N   1 
ATOM   1060 C  CA  . LYS   A 1 159 ? -6.890  -5.883  -2.751  1.00 71.17  ?  315 LYS   A CA  1 
ATOM   1061 C  C   . LYS   A 1 159 ? -8.027  -5.232  -1.965  1.00 67.40  ?  315 LYS   A C   1 
ATOM   1062 O  O   . LYS   A 1 159 ? -8.982  -4.734  -2.568  1.00 68.80  ?  315 LYS   A O   1 
ATOM   1063 C  CB  . LYS   A 1 159 ? -7.400  -6.304  -4.133  1.00 68.61  ?  315 LYS   A CB  1 
ATOM   1064 N  N   . ILE   A 1 160 ? -7.956  -5.193  -0.633  1.00 68.03  ?  316 ILE   A N   1 
ATOM   1065 C  CA  . ILE   A 1 160 ? -8.957  -4.489  0.175   1.00 61.80  ?  316 ILE   A CA  1 
ATOM   1066 C  C   . ILE   A 1 160 ? -8.307  -3.244  0.766   1.00 54.61  ?  316 ILE   A C   1 
ATOM   1067 O  O   . ILE   A 1 160 ? -7.223  -3.328  1.359   1.00 59.60  ?  316 ILE   A O   1 
ATOM   1068 C  CB  . ILE   A 1 160 ? -9.556  -5.369  1.291   1.00 62.57  ?  316 ILE   A CB  1 
ATOM   1069 C  CG1 . ILE   A 1 160 ? -10.628 -6.330  0.758   1.00 63.54  ?  316 ILE   A CG1 1 
ATOM   1070 C  CG2 . ILE   A 1 160 ? -10.210 -4.501  2.361   1.00 55.66  ?  316 ILE   A CG2 1 
ATOM   1071 C  CD1 . ILE   A 1 160 ? -10.249 -7.120  -0.469  1.00 63.28  ?  316 ILE   A CD1 1 
ATOM   1072 N  N   . SER   A 1 161 ? -8.961  -2.094  0.599   1.00 54.93  ?  317 SER   A N   1 
ATOM   1073 C  CA  . SER   A 1 161 ? -8.549  -0.843  1.226   1.00 51.17  ?  317 SER   A CA  1 
ATOM   1074 C  C   . SER   A 1 161 ? -9.629  -0.392  2.204   1.00 47.41  ?  317 SER   A C   1 
ATOM   1075 O  O   . SER   A 1 161 ? -10.812 -0.693  2.026   1.00 43.16  ?  317 SER   A O   1 
ATOM   1076 C  CB  . SER   A 1 161 ? -8.321  0.269   0.196   1.00 46.40  ?  317 SER   A CB  1 
ATOM   1077 O  OG  . SER   A 1 161 ? -9.235  0.159   -0.880  1.00 58.45  ?  317 SER   A OG  1 
ATOM   1078 N  N   . VAL   A 1 162 ? -9.222  0.331   3.250   1.00 48.08  ?  318 VAL   A N   1 
ATOM   1079 C  CA  . VAL   A 1 162 ? -10.160 0.888   4.232   1.00 47.99  ?  318 VAL   A CA  1 
ATOM   1080 C  C   . VAL   A 1 162 ? -9.703  2.297   4.598   1.00 43.41  ?  318 VAL   A C   1 
ATOM   1081 O  O   . VAL   A 1 162 ? -8.723  2.460   5.341   1.00 46.07  ?  318 VAL   A O   1 
ATOM   1082 C  CB  . VAL   A 1 162 ? -10.275 0.027   5.506   1.00 46.71  ?  318 VAL   A CB  1 
ATOM   1083 C  CG1 . VAL   A 1 162 ? -11.471 0.466   6.337   1.00 44.06  ?  318 VAL   A CG1 1 
ATOM   1084 C  CG2 . VAL   A 1 162 ? -10.390 -1.447  5.168   1.00 46.89  ?  318 VAL   A CG2 1 
ATOM   1085 N  N   . ASP   A 1 163 ? -10.417 3.311   4.103   1.00 43.37  ?  319 ASP   A N   1 
ATOM   1086 C  CA  . ASP   A 1 163 ? -10.212 4.688   4.547   1.00 44.89  ?  319 ASP   A CA  1 
ATOM   1087 C  C   . ASP   A 1 163 ? -10.872 4.913   5.904   1.00 38.97  ?  319 ASP   A C   1 
ATOM   1088 O  O   . ASP   A 1 163 ? -12.044 4.576   6.106   1.00 40.45  ?  319 ASP   A O   1 
ATOM   1089 C  CB  . ASP   A 1 163 ? -10.754 5.693   3.520   1.00 38.74  ?  319 ASP   A CB  1 
ATOM   1090 C  CG  . ASP   A 1 163 ? -9.876  5.804   2.266   1.00 48.75  ?  319 ASP   A CG  1 
ATOM   1091 O  OD1 . ASP   A 1 163 ? -8.746  5.259   2.245   1.00 44.41  ?  319 ASP   A OD1 1 
ATOM   1092 O  OD2 . ASP   A 1 163 ? -10.311 6.470   1.295   1.00 54.26  -1 319 ASP   A OD2 1 
ATOM   1093 N  N   . ILE   A 1 164 ? -10.120 5.473   6.841   1.00 41.06  ?  320 ILE   A N   1 
ATOM   1094 C  CA  . ILE   A 1 164 ? -10.624 5.703   8.186   1.00 42.39  ?  320 ILE   A CA  1 
ATOM   1095 C  C   . ILE   A 1 164 ? -10.640 7.198   8.445   1.00 42.38  ?  320 ILE   A C   1 
ATOM   1096 O  O   . ILE   A 1 164 ? -9.618  7.877   8.274   1.00 40.71  ?  320 ILE   A O   1 
ATOM   1097 C  CB  . ILE   A 1 164 ? -9.795  4.954   9.241   1.00 39.32  ?  320 ILE   A CB  1 
ATOM   1098 C  CG1 . ILE   A 1 164 ? -9.893  3.446   8.998   1.00 40.82  ?  320 ILE   A CG1 1 
ATOM   1099 C  CG2 . ILE   A 1 164 ? -10.280 5.302   10.636  1.00 38.31  ?  320 ILE   A CG2 1 
ATOM   1100 C  CD1 . ILE   A 1 164 ? -8.921  2.649   9.850   1.00 40.72  ?  320 ILE   A CD1 1 
ATOM   1101 N  N   . THR   A 1 165 ? -11.811 7.708   8.810   1.00 42.14  ?  321 THR   A N   1 
ATOM   1102 C  CA  . THR   A 1 165 ? -12.000 9.104   9.174   1.00 39.84  ?  321 THR   A CA  1 
ATOM   1103 C  C   . THR   A 1 165 ? -12.171 9.196   10.690  1.00 42.88  ?  321 THR   A C   1 
ATOM   1104 O  O   . THR   A 1 165 ? -12.926 8.414   11.288  1.00 37.06  ?  321 THR   A O   1 
ATOM   1105 C  CB  . THR   A 1 165 ? -13.215 9.693   8.445   1.00 42.22  ?  321 THR   A CB  1 
ATOM   1106 O  OG1 . THR   A 1 165 ? -12.994 9.650   7.028   1.00 35.78  ?  321 THR   A OG1 1 
ATOM   1107 C  CG2 . THR   A 1 165 ? -13.451 11.142  8.857   1.00 35.13  ?  321 THR   A CG2 1 
ATOM   1108 N  N   . LEU   A 1 166 ? -11.446 10.128  11.303  1.00 33.99  ?  322 LEU   A N   1 
ATOM   1109 C  CA  . LEU   A 1 166 ? -11.693 10.521  12.681  1.00 38.85  ?  322 LEU   A CA  1 
ATOM   1110 C  C   . LEU   A 1 166 ? -12.820 11.546  12.728  1.00 36.36  ?  322 LEU   A C   1 
ATOM   1111 O  O   . LEU   A 1 166 ? -12.838 12.493  11.941  1.00 38.89  ?  322 LEU   A O   1 
ATOM   1112 C  CB  . LEU   A 1 166 ? -10.413 11.097  13.302  1.00 45.08  ?  322 LEU   A CB  1 
ATOM   1113 C  CG  . LEU   A 1 166 ? -10.562 11.765  14.672  1.00 41.18  ?  322 LEU   A CG  1 
ATOM   1114 C  CD1 . LEU   A 1 166 ? -11.035 10.726  15.661  1.00 35.94  ?  322 LEU   A CD1 1 
ATOM   1115 C  CD2 . LEU   A 1 166 ? -9.238  12.380  15.139  1.00 46.29  ?  322 LEU   A CD2 1 
ATOM   1116 N  N   . ALA   A 1 167 ? -13.763 11.363  13.645  1.00 34.15  ?  323 ALA   A N   1 
ATOM   1117 C  CA  . ALA   A 1 167 ? -14.910 12.262  13.746  1.00 33.89  ?  323 ALA   A CA  1 
ATOM   1118 C  C   . ALA   A 1 167 ? -15.189 12.575  15.210  1.00 42.62  ?  323 ALA   A C   1 
ATOM   1119 O  O   . ALA   A 1 167 ? -15.442 11.662  16.006  1.00 39.69  ?  323 ALA   A O   1 
ATOM   1120 C  CB  . ALA   A 1 167 ? -16.149 11.640  13.092  1.00 34.16  ?  323 ALA   A CB  1 
ATOM   1121 N  N   . LEU   A 1 168 ? -15.129 13.856  15.570  1.00 39.11  ?  324 LEU   A N   1 
ATOM   1122 C  CA  . LEU   A 1 168 ? -15.588 14.282  16.888  1.00 34.09  ?  324 LEU   A CA  1 
ATOM   1123 C  C   . LEU   A 1 168 ? -17.109 14.162  16.955  1.00 37.00  ?  324 LEU   A C   1 
ATOM   1124 O  O   . LEU   A 1 168 ? -17.810 14.465  15.983  1.00 36.55  ?  324 LEU   A O   1 
ATOM   1125 C  CB  . LEU   A 1 168 ? -15.182 15.732  17.155  1.00 34.02  ?  324 LEU   A CB  1 
ATOM   1126 C  CG  . LEU   A 1 168 ? -13.734 16.173  16.987  1.00 40.20  ?  324 LEU   A CG  1 
ATOM   1127 C  CD1 . LEU   A 1 168 ? -13.613 17.650  17.353  1.00 42.66  ?  324 LEU   A CD1 1 
ATOM   1128 C  CD2 . LEU   A 1 168 ? -12.741 15.311  17.801  1.00 39.35  ?  324 LEU   A CD2 1 
ATOM   1129 N  N   . GLU   A 1 169 ? -17.625 13.704  18.091  1.00 33.47  ?  325 GLU   A N   1 
ATOM   1130 C  CA  . GLU   A 1 169 ? -19.064 13.628  18.326  1.00 32.59  ?  325 GLU   A CA  1 
ATOM   1131 C  C   . GLU   A 1 169 ? -19.487 14.679  19.343  1.00 40.42  ?  325 GLU   A C   1 
ATOM   1132 O  O   . GLU   A 1 169 ? -18.849 14.828  20.396  1.00 40.39  ?  325 GLU   A O   1 
ATOM   1133 C  CB  . GLU   A 1 169 ? -19.483 12.245  18.825  1.00 36.04  ?  325 GLU   A CB  1 
ATOM   1134 C  CG  . GLU   A 1 169 ? -20.984 12.107  19.165  1.00 43.36  ?  325 GLU   A CG  1 
ATOM   1135 C  CD  . GLU   A 1 169 ? -21.340 10.707  19.679  1.00 42.28  ?  325 GLU   A CD  1 
ATOM   1136 O  OE1 . GLU   A 1 169 ? -21.060 10.406  20.863  1.00 41.33  ?  325 GLU   A OE1 1 
ATOM   1137 O  OE2 . GLU   A 1 169 ? -21.880 9.906   18.899  1.00 39.40  -1 325 GLU   A OE2 1 
ATOM   1138 N  N   . SER   A 1 170 ? -20.563 15.405  19.031  1.00 32.76  ?  326 SER   A N   1 
ATOM   1139 C  CA  . SER   A 1 170 ? -21.152 16.361  19.965  1.00 43.27  ?  326 SER   A CA  1 
ATOM   1140 C  C   . SER   A 1 170 ? -22.620 16.027  20.133  1.00 46.80  ?  326 SER   A C   1 
ATOM   1141 O  O   . SER   A 1 170 ? -23.360 15.985  19.145  1.00 38.04  ?  326 SER   A O   1 
ATOM   1142 C  CB  . SER   A 1 170 ? -20.988 17.805  19.484  1.00 35.57  ?  326 SER   A CB  1 
ATOM   1143 O  OG  . SER   A 1 170 ? -21.677 18.718  20.333  1.00 40.56  ?  326 SER   A OG  1 
ATOM   1144 N  N   . LYS   A 1 171 ? -23.042 15.797  21.380  1.00 39.59  ?  327 LYS   A N   1 
ATOM   1145 C  CA  . LYS   A 1 171 ? -24.455 15.577  21.669  1.00 44.24  ?  327 LYS   A CA  1 
ATOM   1146 C  C   . LYS   A 1 171 ? -25.216 16.871  21.909  1.00 41.22  ?  327 LYS   A C   1 
ATOM   1147 O  O   . LYS   A 1 171 ? -26.360 16.829  22.363  1.00 44.65  ?  327 LYS   A O   1 
ATOM   1148 C  CB  . LYS   A 1 171 ? -24.611 14.643  22.866  1.00 42.90  ?  327 LYS   A CB  1 
ATOM   1149 C  CG  . LYS   A 1 171 ? -24.167 13.227  22.556  1.00 43.50  ?  327 LYS   A CG  1 
ATOM   1150 C  CD  . LYS   A 1 171 ? -24.332 12.303  23.746  1.00 50.09  ?  327 LYS   A CD  1 
ATOM   1151 C  CE  . LYS   A 1 171 ? -24.230 10.862  23.290  1.00 57.59  ?  327 LYS   A CE  1 
ATOM   1152 N  NZ  . LYS   A 1 171 ? -22.862 10.514  22.832  1.00 51.66  ?  327 LYS   A NZ  1 
ATOM   1153 N  N   . SER   A 1 172 ? -24.619 18.011  21.595  1.00 42.77  ?  328 SER   A N   1 
ATOM   1154 C  CA  . SER   A 1 172 ? -25.272 19.290  21.771  1.00 40.11  ?  328 SER   A CA  1 
ATOM   1155 C  C   . SER   A 1 172 ? -26.167 19.616  20.569  1.00 47.07  ?  328 SER   A C   1 
ATOM   1156 O  O   . SER   A 1 172 ? -26.224 18.882  19.572  1.00 43.42  ?  328 SER   A O   1 
ATOM   1157 C  CB  . SER   A 1 172 ? -24.221 20.375  21.986  1.00 46.25  ?  328 SER   A CB  1 
ATOM   1158 O  OG  . SER   A 1 172 ? -23.484 20.573  20.785  1.00 50.12  ?  328 SER   A OG  1 
ATOM   1159 N  N   . SER   A 1 173 ? -26.878 20.737  20.689  1.00 38.92  ?  329 SER   A N   1 
ATOM   1160 C  CA  . SER   A 1 173 ? -27.737 21.223  19.622  1.00 42.68  ?  329 SER   A CA  1 
ATOM   1161 C  C   . SER   A 1 173 ? -26.930 21.470  18.355  1.00 38.14  ?  329 SER   A C   1 
ATOM   1162 O  O   . SER   A 1 173 ? -25.778 21.909  18.413  1.00 34.41  ?  329 SER   A O   1 
ATOM   1163 C  CB  . SER   A 1 173 ? -28.422 22.512  20.077  1.00 49.58  ?  329 SER   A CB  1 
ATOM   1164 O  OG  . SER   A 1 173 ? -29.640 22.200  20.714  1.00 57.87  ?  329 SER   A OG  1 
ATOM   1165 N  N   . TRP   A 1 174 ? -27.530 21.156  17.206  1.00 39.35  ?  330 TRP   A N   1 
ATOM   1166 C  CA  . TRP   A 1 174 ? -26.843 21.360  15.939  1.00 37.82  ?  330 TRP   A CA  1 
ATOM   1167 C  C   . TRP   A 1 174 ? -26.534 22.845  15.757  1.00 31.07  ?  330 TRP   A C   1 
ATOM   1168 O  O   . TRP   A 1 174 ? -27.266 23.703  16.249  1.00 34.32  ?  330 TRP   A O   1 
ATOM   1169 C  CB  . TRP   A 1 174 ? -27.683 20.852  14.759  1.00 31.79  ?  330 TRP   A CB  1 
ATOM   1170 C  CG  . TRP   A 1 174 ? -27.921 19.343  14.711  1.00 32.03  ?  330 TRP   A CG  1 
ATOM   1171 C  CD1 . TRP   A 1 174 ? -27.673 18.419  15.708  1.00 32.90  ?  330 TRP   A CD1 1 
ATOM   1172 C  CD2 . TRP   A 1 174 ? -28.440 18.592  13.594  1.00 31.24  ?  330 TRP   A CD2 1 
ATOM   1173 N  NE1 . TRP   A 1 174 ? -28.011 17.153  15.273  1.00 32.76  ?  330 TRP   A NE1 1 
ATOM   1174 C  CE2 . TRP   A 1 174 ? -28.485 17.234  13.983  1.00 32.47  ?  330 TRP   A CE2 1 
ATOM   1175 C  CE3 . TRP   A 1 174 ? -28.870 18.941  12.304  1.00 32.14  ?  330 TRP   A CE3 1 
ATOM   1176 C  CZ2 . TRP   A 1 174 ? -28.959 16.226  13.129  1.00 30.45  ?  330 TRP   A CZ2 1 
ATOM   1177 C  CZ3 . TRP   A 1 174 ? -29.327 17.931  11.452  1.00 35.33  ?  330 TRP   A CZ3 1 
ATOM   1178 C  CH2 . TRP   A 1 174 ? -29.365 16.595  11.871  1.00 36.34  ?  330 TRP   A CH2 1 
ATOM   1179 N  N   . PRO   A 1 175 ? -25.452 23.177  15.065  1.00 33.39  ?  331 PRO   A N   1 
ATOM   1180 C  CA  . PRO   A 1 175 ? -25.067 24.585  14.932  1.00 34.96  ?  331 PRO   A CA  1 
ATOM   1181 C  C   . PRO   A 1 175 ? -26.107 25.380  14.153  1.00 38.49  ?  331 PRO   A C   1 
ATOM   1182 O  O   . PRO   A 1 175 ? -26.901 24.836  13.376  1.00 37.48  ?  331 PRO   A O   1 
ATOM   1183 C  CB  . PRO   A 1 175 ? -23.745 24.518  14.163  1.00 38.97  ?  331 PRO   A CB  1 
ATOM   1184 C  CG  . PRO   A 1 175 ? -23.200 23.133  14.476  1.00 39.42  ?  331 PRO   A CG  1 
ATOM   1185 C  CD  . PRO   A 1 175 ? -24.422 22.261  14.549  1.00 38.96  ?  331 PRO   A CD  1 
ATOM   1186 N  N   . ALA   A 1 176 ? -26.032 26.705  14.319  1.00 34.88  ?  332 ALA   A N   1 
ATOM   1187 C  CA  . ALA   A 1 176 ? -27.051 27.610  13.801  1.00 35.06  ?  332 ALA   A CA  1 
ATOM   1188 C  C   . ALA   A 1 176 ? -27.199 27.516  12.281  1.00 31.78  ?  332 ALA   A C   1 
ATOM   1189 O  O   . ALA   A 1 176 ? -28.305 27.666  11.766  1.00 36.73  ?  332 ALA   A O   1 
ATOM   1190 C  CB  . ALA   A 1 176 ? -26.715 29.045  14.235  1.00 38.98  ?  332 ALA   A CB  1 
ATOM   1191 N  N   . SER   A 1 177 ? -26.109 27.251  11.554  1.00 35.56  ?  333 SER   A N   1 
ATOM   1192 C  CA  . SER   A 1 177 ? -26.145 27.122  10.095  1.00 39.95  ?  333 SER   A CA  1 
ATOM   1193 C  C   . SER   A 1 177 ? -27.075 26.009  9.610   1.00 40.26  ?  333 SER   A C   1 
ATOM   1194 O  O   . SER   A 1 177 ? -27.406 25.961  8.406   1.00 33.36  ?  333 SER   A O   1 
ATOM   1195 C  CB  . SER   A 1 177 ? -24.726 26.874  9.569   1.00 42.84  ?  333 SER   A CB  1 
ATOM   1196 O  OG  . SER   A 1 177 ? -24.223 25.595  9.984   1.00 37.27  ?  333 SER   A OG  1 
ATOM   1197 N  N   . THR   A 1 178 ? -27.495 25.105  10.498  1.00 37.45  ?  334 THR   A N   1 
ATOM   1198 C  CA  . THR   A 1 178 ? -28.373 24.002  10.110  1.00 41.43  ?  334 THR   A CA  1 
ATOM   1199 C  C   . THR   A 1 178 ? -29.841 24.305  10.368  1.00 33.71  ?  334 THR   A C   1 
ATOM   1200 O  O   . THR   A 1 178 ? -30.693 23.483  10.028  1.00 30.30  ?  334 THR   A O   1 
ATOM   1201 C  CB  . THR   A 1 178 ? -27.984 22.723  10.864  1.00 38.50  ?  334 THR   A CB  1 
ATOM   1202 O  OG1 . THR   A 1 178 ? -28.270 22.916  12.252  1.00 37.73  ?  334 THR   A OG1 1 
ATOM   1203 C  CG2 . THR   A 1 178 ? -26.487 22.455  10.712  1.00 30.02  ?  334 THR   A CG2 1 
ATOM   1204 N  N   . GLN   A 1 179 ? -30.144 25.484  10.938  1.00 39.13  ?  335 GLN   A N   1 
ATOM   1205 C  CA  . GLN   A 1 179 ? -31.496 25.773  11.422  1.00 40.13  ?  335 GLN   A CA  1 
ATOM   1206 C  C   . GLN   A 1 179 ? -32.547 25.633  10.329  1.00 41.49  ?  335 GLN   A C   1 
ATOM   1207 O  O   . GLN   A 1 179 ? -33.679 25.214  10.608  1.00 35.45  ?  335 GLN   A O   1 
ATOM   1208 C  CB  . GLN   A 1 179 ? -31.578 27.184  12.025  1.00 37.70  ?  335 GLN   A CB  1 
ATOM   1209 C  CG  . GLN   A 1 179 ? -32.851 27.369  12.876  1.00 43.70  ?  335 GLN   A CG  1 
ATOM   1210 C  CD  . GLN   A 1 179 ? -33.093 28.806  13.327  1.00 60.70  ?  335 GLN   A CD  1 
ATOM   1211 O  OE1 . GLN   A 1 179 ? -32.180 29.642  13.323  1.00 60.53  ?  335 GLN   A OE1 1 
ATOM   1212 N  NE2 . GLN   A 1 179 ? -34.345 29.109  13.683  1.00 67.06  ?  335 GLN   A NE2 1 
ATOM   1213 N  N   . GLU   A 1 180 ? -32.213 26.007  9.092   1.00 37.54  ?  336 GLU   A N   1 
ATOM   1214 C  CA  . GLU   A 1 180 ? -33.178 25.961  8.003   1.00 35.88  ?  336 GLU   A CA  1 
ATOM   1215 C  C   . GLU   A 1 180 ? -32.981 24.758  7.090   1.00 36.96  ?  336 GLU   A C   1 
ATOM   1216 O  O   . GLU   A 1 180 ? -33.650 24.660  6.054   1.00 37.23  ?  336 GLU   A O   1 
ATOM   1217 C  CB  . GLU   A 1 180 ? -33.121 27.264  7.197   1.00 39.62  ?  336 GLU   A CB  1 
ATOM   1218 C  CG  . GLU   A 1 180 ? -33.329 28.473  8.068   1.00 40.75  ?  336 GLU   A CG  1 
ATOM   1219 C  CD  . GLU   A 1 180 ? -34.718 28.512  8.693   1.00 52.86  ?  336 GLU   A CD  1 
ATOM   1220 O  OE1 . GLU   A 1 180 ? -35.617 27.780  8.205   1.00 53.60  ?  336 GLU   A OE1 1 
ATOM   1221 O  OE2 . GLU   A 1 180 ? -34.890 29.240  9.707   1.00 56.44  -1 336 GLU   A OE2 1 
ATOM   1222 N  N   . GLY   A 1 181 ? -32.100 23.829  7.461   1.00 31.75  ?  337 GLY   A N   1 
ATOM   1223 C  CA  . GLY   A 1 181 ? -31.802 22.676  6.640   1.00 31.91  ?  337 GLY   A CA  1 
ATOM   1224 C  C   . GLY   A 1 181 ? -32.722 21.504  6.933   1.00 32.05  ?  337 GLY   A C   1 
ATOM   1225 O  O   . GLY   A 1 181 ? -33.718 21.616  7.647   1.00 30.96  ?  337 GLY   A O   1 
ATOM   1226 N  N   . LEU   A 1 182 ? -32.367 20.359  6.356   1.00 29.40  ?  338 LEU   A N   1 
ATOM   1227 C  CA  . LEU   A 1 182 ? -33.084 19.097  6.541   1.00 30.93  ?  338 LEU   A CA  1 
ATOM   1228 C  C   . LEU   A 1 182 ? -34.598 19.282  6.377   1.00 30.50  ?  338 LEU   A C   1 
ATOM   1229 O  O   . LEU   A 1 182 ? -35.397 18.887  7.232   1.00 27.11  ?  338 LEU   A O   1 
ATOM   1230 C  CB  . LEU   A 1 182 ? -32.719 18.486  7.905   1.00 29.85  ?  338 LEU   A CB  1 
ATOM   1231 C  CG  . LEU   A 1 182 ? -33.106 17.032  8.225   1.00 28.45  ?  338 LEU   A CG  1 
ATOM   1232 C  CD1 . LEU   A 1 182 ? -32.380 16.027  7.285   1.00 25.56  ?  338 LEU   A CD1 1 
ATOM   1233 C  CD2 . LEU   A 1 182 ? -32.791 16.699  9.703   1.00 26.99  ?  338 LEU   A CD2 1 
ATOM   1234 N  N   . ARG   A 1 183 ? -35.000 19.878  5.242   1.00 30.15  ?  339 ARG   A N   1 
ATOM   1235 C  CA  . ARG   A 1 183 ? -36.399 20.255  5.010   1.00 32.63  ?  339 ARG   A CA  1 
ATOM   1236 C  C   . ARG   A 1 183 ? -37.236 19.043  4.581   1.00 30.81  ?  339 ARG   A C   1 
ATOM   1237 O  O   . ARG   A 1 183 ? -37.795 18.974  3.484   1.00 33.35  ?  339 ARG   A O   1 
ATOM   1238 C  CB  . ARG   A 1 183 ? -36.472 21.384  3.980   1.00 38.02  ?  339 ARG   A CB  1 
ATOM   1239 C  CG  . ARG   A 1 183 ? -36.040 22.742  4.549   1.00 42.60  ?  339 ARG   A CG  1 
ATOM   1240 C  CD  . ARG   A 1 183 ? -37.229 23.691  4.690   1.00 54.78  ?  339 ARG   A CD  1 
ATOM   1241 N  NE  . ARG   A 1 183 ? -38.361 23.060  5.368   1.00 57.96  ?  339 ARG   A NE  1 
ATOM   1242 C  CZ  . ARG   A 1 183 ? -39.605 23.527  5.342   1.00 58.54  ?  339 ARG   A CZ  1 
ATOM   1243 N  NH1 . ARG   A 1 183 ? -39.910 24.653  4.711   1.00 58.80  ?  339 ARG   A NH1 1 
ATOM   1244 N  NH2 . ARG   A 1 183 ? -40.569 22.848  5.961   1.00 61.20  ?  339 ARG   A NH2 1 
ATOM   1245 N  N   . ILE   A 1 184 ? -37.331 18.082  5.502   1.00 28.38  ?  340 ILE   A N   1 
ATOM   1246 C  CA  . ILE   A 1 184 ? -38.010 16.812  5.302   1.00 26.18  ?  340 ILE   A CA  1 
ATOM   1247 C  C   . ILE   A 1 184 ? -39.435 16.813  5.847   1.00 28.88  ?  340 ILE   A C   1 
ATOM   1248 O  O   . ILE   A 1 184 ? -40.086 15.756  5.828   1.00 28.48  ?  340 ILE   A O   1 
ATOM   1249 C  CB  . ILE   A 1 184 ? -37.219 15.656  5.968   1.00 27.99  ?  340 ILE   A CB  1 
ATOM   1250 C  CG1 . ILE   A 1 184 ? -37.133 15.861  7.504   1.00 28.41  ?  340 ILE   A CG1 1 
ATOM   1251 C  CG2 . ILE   A 1 184 ? -35.835 15.532  5.376   1.00 27.64  ?  340 ILE   A CG2 1 
ATOM   1252 C  CD1 . ILE   A 1 184 ? -36.367 14.745  8.252   1.00 22.48  ?  340 ILE   A CD1 1 
ATOM   1253 N  N   . GLN   A 1 185 ? -39.933 17.956  6.342   1.00 24.50  ?  341 GLN   A N   1 
ATOM   1254 C  CA  . GLN   A 1 185 ? -41.199 17.965  7.080   1.00 28.84  ?  341 GLN   A CA  1 
ATOM   1255 C  C   . GLN   A 1 185 ? -42.371 17.474  6.226   1.00 34.42  ?  341 GLN   A C   1 
ATOM   1256 O  O   . GLN   A 1 185 ? -43.276 16.801  6.737   1.00 28.53  ?  341 GLN   A O   1 
ATOM   1257 C  CB  . GLN   A 1 185 ? -41.520 19.374  7.587   1.00 30.41  ?  341 GLN   A CB  1 
ATOM   1258 C  CG  . GLN   A 1 185 ? -40.571 19.942  8.602   1.00 39.73  ?  341 GLN   A CG  1 
ATOM   1259 C  CD  . GLN   A 1 185 ? -39.488 20.791  7.955   1.00 40.62  ?  341 GLN   A CD  1 
ATOM   1260 O  OE1 . GLN   A 1 185 ? -39.199 20.654  6.767   1.00 39.04  ?  341 GLN   A OE1 1 
ATOM   1261 N  NE2 . GLN   A 1 185 ? -38.875 21.666  8.739   1.00 45.91  ?  341 GLN   A NE2 1 
ATOM   1262 N  N   . ASN   A 1 186 ? -42.414 17.852  4.932   1.00 24.43  ?  342 ASN   A N   1 
ATOM   1263 C  CA  . ASN   A 1 186 ? -43.539 17.412  4.112   1.00 29.09  ?  342 ASN   A CA  1 
ATOM   1264 C  C   . ASN   A 1 186 ? -43.354 16.002  3.580   1.00 29.04  ?  342 ASN   A C   1 
ATOM   1265 O  O   . ASN   A 1 186 ? -44.289 15.451  2.986   1.00 28.41  ?  342 ASN   A O   1 
ATOM   1266 C  CB  . ASN   A 1 186 ? -43.770 18.371  2.940   1.00 32.94  ?  342 ASN   A CB  1 
ATOM   1267 C  CG  . ASN   A 1 186 ? -44.157 19.756  3.399   1.00 44.39  ?  342 ASN   A CG  1 
ATOM   1268 O  OD1 . ASN   A 1 186 ? -44.842 19.915  4.409   1.00 50.23  ?  342 ASN   A OD1 1 
ATOM   1269 N  ND2 . ASN   A 1 186 ? -43.764 20.772  2.632   1.00 54.39  ?  342 ASN   A ND2 1 
ATOM   1270 N  N   . TRP   A 1 187 ? -42.176 15.415  3.794   1.00 26.65  ?  343 TRP   A N   1 
ATOM   1271 C  CA  . TRP   A 1 187 ? -41.839 14.097  3.282   1.00 28.65  ?  343 TRP   A CA  1 
ATOM   1272 C  C   . TRP   A 1 187 ? -41.745 13.083  4.450   1.00 28.89  ?  343 TRP   A C   1 
ATOM   1273 O  O   . TRP   A 1 187 ? -42.605 12.219  4.568   1.00 27.38  ?  343 TRP   A O   1 
ATOM   1274 C  CB  . TRP   A 1 187 ? -40.520 14.201  2.522   1.00 25.76  ?  343 TRP   A CB  1 
ATOM   1275 C  CG  . TRP   A 1 187 ? -39.800 12.923  2.192   1.00 23.80  ?  343 TRP   A CG  1 
ATOM   1276 C  CD1 . TRP   A 1 187 ? -40.329 11.680  1.982   1.00 26.17  ?  343 TRP   A CD1 1 
ATOM   1277 C  CD2 . TRP   A 1 187 ? -38.382 12.775  2.108   1.00 22.52  ?  343 TRP   A CD2 1 
ATOM   1278 N  NE1 . TRP   A 1 187 ? -39.313 10.766  1.735   1.00 25.32  ?  343 TRP   A NE1 1 
ATOM   1279 C  CE2 . TRP   A 1 187 ? -38.108 11.423  1.830   1.00 26.55  ?  343 TRP   A CE2 1 
ATOM   1280 C  CE3 . TRP   A 1 187 ? -37.311 13.667  2.233   1.00 25.95  ?  343 TRP   A CE3 1 
ATOM   1281 C  CZ2 . TRP   A 1 187 ? -36.796 10.936  1.704   1.00 28.60  ?  343 TRP   A CZ2 1 
ATOM   1282 C  CZ3 . TRP   A 1 187 ? -36.020 13.191  2.096   1.00 25.76  ?  343 TRP   A CZ3 1 
ATOM   1283 C  CH2 . TRP   A 1 187 ? -35.772 11.842  1.824   1.00 24.19  ?  343 TRP   A CH2 1 
ATOM   1284 N  N   . LEU   A 1 188 ? -40.715 13.184  5.279   1.00 24.38  ?  344 LEU   A N   1 
ATOM   1285 C  CA  . LEU   A 1 188 ? -40.570 12.238  6.386   1.00 29.59  ?  344 LEU   A CA  1 
ATOM   1286 C  C   . LEU   A 1 188 ? -41.274 12.691  7.667   1.00 26.62  ?  344 LEU   A C   1 
ATOM   1287 O  O   . LEU   A 1 188 ? -41.434 11.868  8.582   1.00 25.71  ?  344 LEU   A O   1 
ATOM   1288 C  CB  . LEU   A 1 188 ? -39.084 12.009  6.662   1.00 28.60  ?  344 LEU   A CB  1 
ATOM   1289 C  CG  . LEU   A 1 188 ? -38.348 11.452  5.437   1.00 27.81  ?  344 LEU   A CG  1 
ATOM   1290 C  CD1 . LEU   A 1 188 ? -36.849 11.329  5.706   1.00 27.93  ?  344 LEU   A CD1 1 
ATOM   1291 C  CD2 . LEU   A 1 188 ? -38.882 10.047  5.147   1.00 26.68  ?  344 LEU   A CD2 1 
ATOM   1292 N  N   . SER   A 1 189 ? -41.644 13.976  7.755   1.00 24.20  ?  345 SER   A N   1 
ATOM   1293 C  CA  . SER   A 1 189 ? -42.508 14.584  8.778   1.00 27.27  ?  345 SER   A CA  1 
ATOM   1294 C  C   . SER   A 1 189 ? -41.744 15.512  9.708   1.00 28.35  ?  345 SER   A C   1 
ATOM   1295 O  O   . SER   A 1 189 ? -40.531 15.391  9.891   1.00 26.67  ?  345 SER   A O   1 
ATOM   1296 C  CB  . SER   A 1 189 ? -43.242 13.573  9.670   1.00 31.88  ?  345 SER   A CB  1 
ATOM   1297 O  OG  . SER   A 1 189 ? -42.346 13.025  10.642  1.00 28.64  ?  345 SER   A OG  1 
ATOM   1298 N  N   . ALA   A 1 190 ? -42.486 16.436  10.304  1.00 27.92  ?  346 ALA   A N   1 
ATOM   1299 C  CA  . ALA   A 1 190 ? -41.917 17.348  11.281  1.00 27.54  ?  346 ALA   A CA  1 
ATOM   1300 C  C   . ALA   A 1 190 ? -41.500 16.611  12.547  1.00 28.83  ?  346 ALA   A C   1 
ATOM   1301 O  O   . ALA   A 1 190 ? -40.559 17.031  13.214  1.00 30.14  ?  346 ALA   A O   1 
ATOM   1302 C  CB  . ALA   A 1 190 ? -42.930 18.431  11.620  1.00 26.63  ?  346 ALA   A CB  1 
ATOM   1303 N  N   . LYS   A 1 191 ? -42.208 15.533  12.884  1.00 27.38  ?  347 LYS   A N   1 
ATOM   1304 C  CA  . LYS   A 1 191 ? -41.825 14.687  14.002  1.00 30.33  ?  347 LYS   A CA  1 
ATOM   1305 C  C   . LYS   A 1 191 ? -40.445 14.089  13.774  1.00 33.61  ?  347 LYS   A C   1 
ATOM   1306 O  O   . LYS   A 1 191 ? -39.577 14.133  14.657  1.00 29.86  ?  347 LYS   A O   1 
ATOM   1307 C  CB  . LYS   A 1 191 ? -42.854 13.570  14.197  1.00 33.81  ?  347 LYS   A CB  1 
ATOM   1308 C  CG  . LYS   A 1 191 ? -43.336 13.413  15.637  1.00 46.52  ?  347 LYS   A CG  1 
ATOM   1309 C  CD  . LYS   A 1 191 ? -44.091 12.089  15.822  1.00 42.93  ?  347 LYS   A CD  1 
ATOM   1310 C  CE  . LYS   A 1 191 ? -45.209 11.929  14.820  1.00 37.81  ?  347 LYS   A CE  1 
ATOM   1311 N  NZ  . LYS   A 1 191 ? -46.317 12.922  15.055  1.00 53.47  ?  347 LYS   A NZ  1 
ATOM   1312 N  N   . VAL   A 1 192 ? -40.231 13.500  12.597  1.00 31.46  ?  348 VAL   A N   1 
ATOM   1313 C  CA  . VAL   A 1 192 ? -38.952 12.867  12.316  1.00 26.68  ?  348 VAL   A CA  1 
ATOM   1314 C  C   . VAL   A 1 192 ? -37.845 13.898  12.290  1.00 27.51  ?  348 VAL   A C   1 
ATOM   1315 O  O   . VAL   A 1 192 ? -36.761 13.676  12.850  1.00 29.55  ?  348 VAL   A O   1 
ATOM   1316 C  CB  . VAL   A 1 192 ? -39.029 12.057  11.012  1.00 31.63  ?  348 VAL   A CB  1 
ATOM   1317 C  CG1 . VAL   A 1 192 ? -37.647 11.598  10.581  1.00 28.30  ?  348 VAL   A CG1 1 
ATOM   1318 C  CG2 . VAL   A 1 192 ? -39.911 10.835  11.244  1.00 32.13  ?  348 VAL   A CG2 1 
ATOM   1319 N  N   . ARG   A 1 193 ? -38.098 15.056  11.679  1.00 27.03  ?  349 ARG   A N   1 
ATOM   1320 C  CA  . ARG   A 1 193 ? -37.071 16.083  11.668  1.00 29.49  ?  349 ARG   A CA  1 
ATOM   1321 C  C   . ARG   A 1 193 ? -36.632 16.435  13.091  1.00 28.87  ?  349 ARG   A C   1 
ATOM   1322 O  O   . ARG   A 1 193 ? -35.433 16.589  13.353  1.00 25.46  ?  349 ARG   A O   1 
ATOM   1323 C  CB  . ARG   A 1 193 ? -37.561 17.336  10.952  1.00 30.63  ?  349 ARG   A CB  1 
ATOM   1324 C  CG  . ARG   A 1 193 ? -36.448 18.359  10.796  1.00 28.93  ?  349 ARG   A CG  1 
ATOM   1325 C  CD  . ARG   A 1 193 ? -36.910 19.616  10.080  1.00 32.03  ?  349 ARG   A CD  1 
ATOM   1326 N  NE  . ARG   A 1 193 ? -35.808 20.516  9.760   1.00 34.33  ?  349 ARG   A NE  1 
ATOM   1327 C  CZ  . ARG   A 1 193 ? -35.357 21.497  10.538  1.00 40.72  ?  349 ARG   A CZ  1 
ATOM   1328 N  NH1 . ARG   A 1 193 ? -35.835 21.701  11.766  1.00 37.65  ?  349 ARG   A NH1 1 
ATOM   1329 N  NH2 . ARG   A 1 193 ? -34.407 22.307  10.071  1.00 37.72  ?  349 ARG   A NH2 1 
ATOM   1330 N  N   . LYS   A 1 194 ? -37.584 16.551  14.020  1.00 26.41  ?  350 LYS   A N   1 
ATOM   1331 C  CA  . LYS   A 1 194 ? -37.220 16.894  15.401  1.00 28.00  ?  350 LYS   A CA  1 
ATOM   1332 C  C   . LYS   A 1 194 ? -36.409 15.779  16.056  1.00 29.55  ?  350 LYS   A C   1 
ATOM   1333 O  O   . LYS   A 1 194 ? -35.383 16.037  16.703  1.00 31.39  ?  350 LYS   A O   1 
ATOM   1334 C  CB  . LYS   A 1 194 ? -38.471 17.188  16.224  1.00 33.94  ?  350 LYS   A CB  1 
ATOM   1335 C  CG  . LYS   A 1 194 ? -38.192 17.588  17.677  1.00 32.92  ?  350 LYS   A CG  1 
ATOM   1336 C  CD  . LYS   A 1 194 ? -39.469 17.906  18.431  1.00 37.00  ?  350 LYS   A CD  1 
ATOM   1337 C  CE  . LYS   A 1 194 ? -39.164 18.349  19.866  1.00 54.36  ?  350 LYS   A CE  1 
ATOM   1338 N  NZ  . LYS   A 1 194 ? -40.395 18.705  20.640  1.00 64.26  ?  350 LYS   A NZ  1 
ATOM   1339 N  N   . GLN   A 1 195 ? -36.862 14.530  15.910  1.00 26.78  ?  351 GLN   A N   1 
ATOM   1340 C  CA  . GLN   A 1 195 ? -36.071 13.393  16.366  1.00 30.69  ?  351 GLN   A CA  1 
ATOM   1341 C  C   . GLN   A 1 195 ? -34.656 13.378  15.788  1.00 35.38  ?  351 GLN   A C   1 
ATOM   1342 O  O   . GLN   A 1 195 ? -33.679 13.132  16.516  1.00 28.83  ?  351 GLN   A O   1 
ATOM   1343 C  CB  . GLN   A 1 195 ? -36.791 12.072  16.078  1.00 30.23  ?  351 GLN   A CB  1 
ATOM   1344 C  CG  . GLN   A 1 195 ? -37.976 11.854  17.029  1.00 46.46  ?  351 GLN   A CG  1 
ATOM   1345 C  CD  . GLN   A 1 195 ? -39.027 10.870  16.544  1.00 45.81  ?  351 GLN   A CD  1 
ATOM   1346 O  OE1 . GLN   A 1 195 ? -38.768 10.032  15.662  1.00 53.20  ?  351 GLN   A OE1 1 
ATOM   1347 N  NE2 . GLN   A 1 195 ? -40.193 10.885  17.211  1.00 35.45  ?  351 GLN   A NE2 1 
ATOM   1348 N  N   . LEU   A 1 196 ? -34.514 13.620  14.493  1.00 29.17  ?  352 LEU   A N   1 
ATOM   1349 C  CA  . LEU   A 1 196 ? -33.179 13.535  13.915  1.00 31.28  ?  352 LEU   A CA  1 
ATOM   1350 C  C   . LEU   A 1 196 ? -32.276 14.645  14.462  1.00 30.66  ?  352 LEU   A C   1 
ATOM   1351 O  O   . LEU   A 1 196 ? -31.086 14.420  14.696  1.00 30.34  ?  352 LEU   A O   1 
ATOM   1352 C  CB  . LEU   A 1 196 ? -33.279 13.564  12.387  1.00 27.80  ?  352 LEU   A CB  1 
ATOM   1353 C  CG  . LEU   A 1 196 ? -33.975 12.374  11.683  1.00 30.90  ?  352 LEU   A CG  1 
ATOM   1354 C  CD1 . LEU   A 1 196 ? -34.144 12.635  10.180  1.00 30.23  ?  352 LEU   A CD1 1 
ATOM   1355 C  CD2 . LEU   A 1 196 ? -33.288 11.019  11.911  1.00 31.34  ?  352 LEU   A CD2 1 
ATOM   1356 N  N   . ARG   A 1 197 ? -32.823 15.842  14.688  1.00 24.69  ?  353 ARG   A N   1 
ATOM   1357 C  CA  . ARG   A 1 197 ? -32.013 16.948  15.175  1.00 30.27  ?  353 ARG   A CA  1 
ATOM   1358 C  C   . ARG   A 1 197 ? -31.685 16.815  16.670  1.00 30.03  ?  353 ARG   A C   1 
ATOM   1359 O  O   . ARG   A 1 197 ? -30.836 17.567  17.171  1.00 28.52  ?  353 ARG   A O   1 
ATOM   1360 C  CB  . ARG   A 1 197 ? -32.727 18.280  14.880  1.00 33.86  ?  353 ARG   A CB  1 
ATOM   1361 C  CG  . ARG   A 1 197 ? -32.661 18.722  13.389  1.00 34.58  ?  353 ARG   A CG  1 
ATOM   1362 C  CD  . ARG   A 1 197 ? -33.431 20.029  13.129  1.00 37.87  ?  353 ARG   A CD  1 
ATOM   1363 N  NE  . ARG   A 1 197 ? -33.001 21.107  14.015  1.00 48.20  ?  353 ARG   A NE  1 
ATOM   1364 C  CZ  . ARG   A 1 197 ? -31.951 21.887  13.803  1.00 45.35  ?  353 ARG   A CZ  1 
ATOM   1365 N  NH1 . ARG   A 1 197 ? -31.215 21.773  12.710  1.00 44.00  ?  353 ARG   A NH1 1 
ATOM   1366 N  NH2 . ARG   A 1 197 ? -31.612 22.780  14.729  1.00 52.12  ?  353 ARG   A NH2 1 
ATOM   1367 N  N   . LEU   A 1 198 ? -32.319 15.869  17.373  1.00 32.45  ?  354 LEU   A N   1 
ATOM   1368 C  CA  . LEU   A 1 198 ? -31.888 15.518  18.723  1.00 40.68  ?  354 LEU   A CA  1 
ATOM   1369 C  C   . LEU   A 1 198 ? -30.744 14.507  18.713  1.00 40.77  ?  354 LEU   A C   1 
ATOM   1370 O  O   . LEU   A 1 198 ? -30.094 14.302  19.750  1.00 32.31  ?  354 LEU   A O   1 
ATOM   1371 C  CB  . LEU   A 1 198 ? -33.079 14.967  19.525  1.00 35.79  ?  354 LEU   A CB  1 
ATOM   1372 C  CG  . LEU   A 1 198 ? -34.229 15.921  19.871  1.00 34.43  ?  354 LEU   A CG  1 
ATOM   1373 C  CD1 . LEU   A 1 198 ? -35.402 15.131  20.435  1.00 39.70  ?  354 LEU   A CD1 1 
ATOM   1374 C  CD2 . LEU   A 1 198 ? -33.752 16.961  20.918  1.00 41.16  ?  354 LEU   A CD2 1 
ATOM   1375 N  N   . LYS   A 1 199 ? -30.471 13.882  17.569  1.00 32.53  ?  355 LYS   A N   1 
ATOM   1376 C  CA  . LYS   A 1 199 ? -29.300 13.033  17.460  1.00 35.46  ?  355 LYS   A CA  1 
ATOM   1377 C  C   . LYS   A 1 199 ? -28.043 13.901  17.471  1.00 37.58  ?  355 LYS   A C   1 
ATOM   1378 O  O   . LYS   A 1 199 ? -28.111 15.111  17.241  1.00 34.59  ?  355 LYS   A O   1 
ATOM   1379 C  CB  . LYS   A 1 199 ? -29.390 12.192  16.191  1.00 35.15  ?  355 LYS   A CB  1 
ATOM   1380 C  CG  . LYS   A 1 199 ? -30.550 11.241  16.260  1.00 37.72  ?  355 LYS   A CG  1 
ATOM   1381 C  CD  . LYS   A 1 199 ? -30.577 10.244  15.110  1.00 38.16  ?  355 LYS   A CD  1 
ATOM   1382 C  CE  . LYS   A 1 199 ? -31.726 9.268   15.347  1.00 43.19  ?  355 LYS   A CE  1 
ATOM   1383 N  NZ  . LYS   A 1 199 ? -31.545 7.985   14.605  1.00 52.88  ?  355 LYS   A NZ  1 
ATOM   1384 N  N   . PRO   A 1 200 ? -26.890 13.320  17.794  1.00 36.99  ?  356 PRO   A N   1 
ATOM   1385 C  CA  . PRO   A 1 200 ? -25.641 14.097  17.770  1.00 37.24  ?  356 PRO   A CA  1 
ATOM   1386 C  C   . PRO   A 1 200 ? -25.231 14.479  16.350  1.00 38.54  ?  356 PRO   A C   1 
ATOM   1387 O  O   . PRO   A 1 200 ? -25.780 14.007  15.351  1.00 36.20  ?  356 PRO   A O   1 
ATOM   1388 C  CB  . PRO   A 1 200 ? -24.617 13.163  18.427  1.00 34.69  ?  356 PRO   A CB  1 
ATOM   1389 C  CG  . PRO   A 1 200 ? -25.202 11.800  18.351  1.00 39.98  ?  356 PRO   A CG  1 
ATOM   1390 C  CD  . PRO   A 1 200 ? -26.708 11.991  18.401  1.00 40.15  ?  356 PRO   A CD  1 
ATOM   1391 N  N   . PHE   A 1 201 ? -24.237 15.364  16.271  1.00 36.69  ?  357 PHE   A N   1 
ATOM   1392 C  CA  . PHE   A 1 201 ? -23.618 15.694  14.994  1.00 37.89  ?  357 PHE   A CA  1 
ATOM   1393 C  C   . PHE   A 1 201 ? -22.120 15.482  15.147  1.00 41.08  ?  357 PHE   A C   1 
ATOM   1394 O  O   . PHE   A 1 201 ? -21.605 15.278  16.262  1.00 34.37  ?  357 PHE   A O   1 
ATOM   1395 C  CB  . PHE   A 1 201 ? -23.926 17.137  14.543  1.00 35.69  ?  357 PHE   A CB  1 
ATOM   1396 C  CG  . PHE   A 1 201 ? -23.279 18.201  15.396  1.00 32.97  ?  357 PHE   A CG  1 
ATOM   1397 C  CD1 . PHE   A 1 201 ? -23.924 18.704  16.511  1.00 39.57  ?  357 PHE   A CD1 1 
ATOM   1398 C  CD2 . PHE   A 1 201 ? -22.041 18.718  15.057  1.00 31.96  ?  357 PHE   A CD2 1 
ATOM   1399 C  CE1 . PHE   A 1 201 ? -23.319 19.668  17.317  1.00 44.34  ?  357 PHE   A CE1 1 
ATOM   1400 C  CE2 . PHE   A 1 201 ? -21.423 19.688  15.840  1.00 38.77  ?  357 PHE   A CE2 1 
ATOM   1401 C  CZ  . PHE   A 1 201 ? -22.067 20.174  16.981  1.00 44.33  ?  357 PHE   A CZ  1 
ATOM   1402 N  N   . TYR   A 1 202 ? -21.422 15.535  14.010  1.00 33.57  ?  358 TYR   A N   1 
ATOM   1403 C  CA  . TYR   A 1 202 ? -20.034 15.113  13.952  1.00 31.89  ?  358 TYR   A CA  1 
ATOM   1404 C  C   . TYR   A 1 202 ? -19.189 16.187  13.295  1.00 32.18  ?  358 TYR   A C   1 
ATOM   1405 O  O   . TYR   A 1 202 ? -19.689 17.008  12.518  1.00 34.78  ?  358 TYR   A O   1 
ATOM   1406 C  CB  . TYR   A 1 202 ? -19.928 13.742  13.235  1.00 31.97  ?  358 TYR   A CB  1 
ATOM   1407 C  CG  . TYR   A 1 202 ? -20.681 12.702  14.042  1.00 33.09  ?  358 TYR   A CG  1 
ATOM   1408 C  CD1 . TYR   A 1 202 ? -22.056 12.545  13.911  1.00 33.06  ?  358 TYR   A CD1 1 
ATOM   1409 C  CD2 . TYR   A 1 202 ? -20.028 11.966  15.021  1.00 36.80  ?  358 TYR   A CD2 1 
ATOM   1410 C  CE1 . TYR   A 1 202 ? -22.750 11.633  14.695  1.00 40.07  ?  358 TYR   A CE1 1 
ATOM   1411 C  CE2 . TYR   A 1 202 ? -20.702 11.058  15.805  1.00 37.83  ?  358 TYR   A CE2 1 
ATOM   1412 C  CZ  . TYR   A 1 202 ? -22.061 10.901  15.658  1.00 40.34  ?  358 TYR   A CZ  1 
ATOM   1413 O  OH  . TYR   A 1 202 ? -22.707 9.990   16.466  1.00 39.57  ?  358 TYR   A OH  1 
ATOM   1414 N  N   . LEU   A 1 203 ? -17.895 16.177  13.638  1.00 32.39  ?  359 LEU   A N   1 
ATOM   1415 C  CA  . LEU   A 1 203 ? -16.919 17.117  13.108  1.00 31.54  ?  359 LEU   A CA  1 
ATOM   1416 C  C   . LEU   A 1 203 ? -15.698 16.327  12.667  1.00 34.37  ?  359 LEU   A C   1 
ATOM   1417 O  O   . LEU   A 1 203 ? -15.102 15.601  13.472  1.00 36.18  ?  359 LEU   A O   1 
ATOM   1418 C  CB  . LEU   A 1 203 ? -16.534 18.160  14.167  1.00 43.34  ?  359 LEU   A CB  1 
ATOM   1419 C  CG  . LEU   A 1 203 ? -17.630 19.144  14.579  1.00 40.46  ?  359 LEU   A CG  1 
ATOM   1420 C  CD1 . LEU   A 1 203 ? -17.247 19.812  15.882  1.00 40.49  ?  359 LEU   A CD1 1 
ATOM   1421 C  CD2 . LEU   A 1 203 ? -17.703 20.180  13.535  1.00 35.74  ?  359 LEU   A CD2 1 
ATOM   1422 N  N   . VAL   A 1 204 ? -15.306 16.487  11.407  1.00 31.66  ?  360 VAL   A N   1 
ATOM   1423 C  CA  . VAL   A 1 204 ? -14.162 15.754  10.877  1.00 33.21  ?  360 VAL   A CA  1 
ATOM   1424 C  C   . VAL   A 1 204 ? -13.052 16.761  10.631  1.00 34.84  ?  360 VAL   A C   1 
ATOM   1425 O  O   . VAL   A 1 204 ? -13.336 17.902  10.234  1.00 36.03  ?  360 VAL   A O   1 
ATOM   1426 C  CB  . VAL   A 1 204 ? -14.525 14.976  9.597   1.00 34.87  ?  360 VAL   A CB  1 
ATOM   1427 C  CG1 . VAL   A 1 204 ? -15.615 13.948  9.882   1.00 32.62  ?  360 VAL   A CG1 1 
ATOM   1428 C  CG2 . VAL   A 1 204 ? -14.959 15.925  8.452   1.00 33.81  ?  360 VAL   A CG2 1 
ATOM   1429 N  N   . PRO   A 1 205 ? -11.790 16.385  10.820  1.00 33.11  ?  361 PRO   A N   1 
ATOM   1430 C  CA  . PRO   A 1 205 ? -10.700 17.327  10.557  1.00 39.33  ?  361 PRO   A CA  1 
ATOM   1431 C  C   . PRO   A 1 205 ? -10.592 17.592  9.065   1.00 43.57  ?  361 PRO   A C   1 
ATOM   1432 O  O   . PRO   A 1 205 ? -10.540 16.661  8.255   1.00 40.67  ?  361 PRO   A O   1 
ATOM   1433 C  CB  . PRO   A 1 205 ? -9.464  16.609  11.103  1.00 37.73  ?  361 PRO   A CB  1 
ATOM   1434 C  CG  . PRO   A 1 205 ? -9.827  15.138  11.035  1.00 36.00  ?  361 PRO   A CG  1 
ATOM   1435 C  CD  . PRO   A 1 205 ? -11.304 15.048  11.220  1.00 38.54  ?  361 PRO   A CD  1 
ATOM   1436 N  N   . LYS   A 1 206 ? -10.573 18.872  8.704   1.00 40.04  ?  362 LYS   A N   1 
ATOM   1437 C  CA  . LYS   A 1 206 ? -10.693 19.241  7.295   1.00 40.12  ?  362 LYS   A CA  1 
ATOM   1438 C  C   . LYS   A 1 206 ? -10.243 20.688  7.148   1.00 46.69  ?  362 LYS   A C   1 
ATOM   1439 O  O   . LYS   A 1 206 ? -10.909 21.597  7.658   1.00 40.01  ?  362 LYS   A O   1 
ATOM   1440 C  CB  . LYS   A 1 206 ? -12.127 19.066  6.823   1.00 37.62  ?  362 LYS   A CB  1 
ATOM   1441 C  CG  . LYS   A 1 206 ? -12.284 18.907  5.330   1.00 42.74  ?  362 LYS   A CG  1 
ATOM   1442 C  CD  . LYS   A 1 206 ? -11.960 17.479  4.925   1.00 40.09  ?  362 LYS   A CD  1 
ATOM   1443 C  CE  . LYS   A 1 206 ? -12.175 17.249  3.438   1.00 49.11  ?  362 LYS   A CE  1 
ATOM   1444 N  NZ  . LYS   A 1 206 ? -11.856 15.831  3.063   1.00 50.60  ?  362 LYS   A NZ  1 
ATOM   1445 N  N   . HIS   A 1 207 ? -9.126  20.902  6.460   1.00 50.73  ?  363 HIS   A N   1 
ATOM   1446 C  CA  . HIS   A 1 207 ? -8.673  22.265  6.248   1.00 51.77  ?  363 HIS   A CA  1 
ATOM   1447 C  C   . HIS   A 1 207 ? -9.567  22.978  5.239   1.00 50.29  ?  363 HIS   A C   1 
ATOM   1448 O  O   . HIS   A 1 207 ? -10.199 22.360  4.377   1.00 43.73  ?  363 HIS   A O   1 
ATOM   1449 C  CB  . HIS   A 1 207 ? -7.189  22.310  5.838   1.00 53.82  ?  363 HIS   A CB  1 
ATOM   1450 C  CG  . HIS   A 1 207 ? -6.859  21.690  4.510   1.00 55.03  ?  363 HIS   A CG  1 
ATOM   1451 N  ND1 . HIS   A 1 207 ? -5.590  21.758  3.965   1.00 55.54  ?  363 HIS   A ND1 1 
ATOM   1452 C  CD2 . HIS   A 1 207 ? -7.602  20.967  3.638   1.00 56.79  ?  363 HIS   A CD2 1 
ATOM   1453 C  CE1 . HIS   A 1 207 ? -5.574  21.126  2.804   1.00 61.19  ?  363 HIS   A CE1 1 
ATOM   1454 N  NE2 . HIS   A 1 207 ? -6.782  20.635  2.582   1.00 64.28  ?  363 HIS   A NE2 1 
ATOM   1455 N  N   . ALA   A 1 208 ? -9.663  24.291  5.409   1.00 55.78  ?  364 ALA   A N   1 
ATOM   1456 C  CA  . ALA   A 1 208 ? -10.438 25.168  4.548   1.00 56.93  ?  364 ALA   A CA  1 
ATOM   1457 C  C   . ALA   A 1 208 ? -9.505  26.124  3.811   1.00 56.08  ?  364 ALA   A C   1 
ATOM   1458 O  O   . ALA   A 1 208 ? -8.411  26.445  4.281   1.00 65.14  ?  364 ALA   A O   1 
ATOM   1459 C  CB  . ALA   A 1 208 ? -11.469 25.957  5.366   1.00 56.15  ?  364 ALA   A CB  1 
ATOM   1460 N  N   . LYS   A 1 209 ? -9.956  26.591  2.648   1.00 69.67  ?  365 LYS   A N   1 
ATOM   1461 C  CA  . LYS   A 1 209 ? -9.165  27.524  1.834   1.00 61.40  ?  365 LYS   A CA  1 
ATOM   1462 C  C   . LYS   A 1 209 ? -8.941  28.903  2.481   1.00 65.99  ?  365 LYS   A C   1 
ATOM   1463 O  O   . LYS   A 1 209 ? -9.293  29.145  3.640   1.00 71.21  ?  365 LYS   A O   1 
ATOM   1464 C  CB  . LYS   A 1 209 ? -9.831  27.709  0.467   1.00 61.86  ?  365 LYS   A CB  1 
ATOM   1465 N  N   . GLY   A 1 213 ? -2.731  29.786  1.431   1.00 73.87  ?  369 GLY   A N   1 
ATOM   1466 C  CA  . GLY   A 1 213 ? -2.956  28.353  1.371   1.00 57.91  ?  369 GLY   A CA  1 
ATOM   1467 C  C   . GLY   A 1 213 ? -4.278  27.905  1.970   1.00 67.35  ?  369 GLY   A C   1 
ATOM   1468 O  O   . GLY   A 1 213 ? -5.347  28.067  1.368   1.00 69.21  ?  369 GLY   A O   1 
ATOM   1469 N  N   . PHE   A 1 214 ? -4.211  27.335  3.171   1.00 69.58  ?  370 PHE   A N   1 
ATOM   1470 C  CA  . PHE   A 1 214 ? -5.392  26.762  3.797   1.00 67.10  ?  370 PHE   A CA  1 
ATOM   1471 C  C   . PHE   A 1 214 ? -5.325  26.941  5.308   1.00 62.48  ?  370 PHE   A C   1 
ATOM   1472 O  O   . PHE   A 1 214 ? -4.242  26.901  5.902   1.00 67.53  ?  370 PHE   A O   1 
ATOM   1473 C  CB  . PHE   A 1 214 ? -5.533  25.275  3.442   1.00 65.00  ?  370 PHE   A CB  1 
ATOM   1474 N  N   . GLN   A 1 215 ? -6.494  27.156  5.912   1.00 61.05  ?  371 GLN   A N   1 
ATOM   1475 C  CA  . GLN   A 1 215 ? -6.628  27.173  7.362   1.00 62.01  ?  371 GLN   A CA  1 
ATOM   1476 C  C   . GLN   A 1 215 ? -6.605  25.741  7.892   1.00 58.07  ?  371 GLN   A C   1 
ATOM   1477 O  O   . GLN   A 1 215 ? -7.506  24.947  7.598   1.00 56.02  ?  371 GLN   A O   1 
ATOM   1478 C  CB  . GLN   A 1 215 ? -7.922  27.889  7.752   1.00 61.72  ?  371 GLN   A CB  1 
ATOM   1479 C  CG  . GLN   A 1 215 ? -8.171  27.932  9.240   1.00 55.72  ?  371 GLN   A CG  1 
ATOM   1480 C  CD  . GLN   A 1 215 ? -6.919  28.231  10.034  1.00 61.44  ?  371 GLN   A CD  1 
ATOM   1481 O  OE1 . GLN   A 1 215 ? -6.554  27.466  10.929  1.00 62.67  ?  371 GLN   A OE1 1 
ATOM   1482 N  NE2 . GLN   A 1 215 ? -6.261  29.344  9.725   1.00 62.03  ?  371 GLN   A NE2 1 
ATOM   1483 N  N   . GLU   A 1 216 ? -5.579  25.411  8.676   1.00 60.27  ?  372 GLU   A N   1 
ATOM   1484 C  CA  . GLU   A 1 216 ? -5.239  24.024  8.960   1.00 57.01  ?  372 GLU   A CA  1 
ATOM   1485 C  C   . GLU   A 1 216 ? -5.755  23.524  10.305  1.00 55.56  ?  372 GLU   A C   1 
ATOM   1486 O  O   . GLU   A 1 216 ? -5.385  22.420  10.722  1.00 57.88  ?  372 GLU   A O   1 
ATOM   1487 C  CB  . GLU   A 1 216 ? -3.723  23.830  8.881   1.00 55.60  ?  372 GLU   A CB  1 
ATOM   1488 C  CG  . GLU   A 1 216 ? -3.156  23.831  7.463   1.00 57.28  ?  372 GLU   A CG  1 
ATOM   1489 C  CD  . GLU   A 1 216 ? -3.615  22.658  6.585   1.00 65.57  ?  372 GLU   A CD  1 
ATOM   1490 O  OE1 . GLU   A 1 216 ? -4.535  21.888  6.955   1.00 66.37  ?  372 GLU   A OE1 1 
ATOM   1491 O  OE2 . GLU   A 1 216 ? -3.041  22.519  5.486   1.00 73.22  -1 372 GLU   A OE2 1 
ATOM   1492 N  N   . GLU   A 1 217 ? -6.601  24.289  10.993  1.00 51.73  ?  373 GLU   A N   1 
ATOM   1493 C  CA  . GLU   A 1 217 ? -7.143  23.809  12.257  1.00 44.17  ?  373 GLU   A CA  1 
ATOM   1494 C  C   . GLU   A 1 217 ? -8.662  23.854  12.269  1.00 46.48  ?  373 GLU   A C   1 
ATOM   1495 O  O   . GLU   A 1 217 ? -9.273  24.025  13.326  1.00 42.18  ?  373 GLU   A O   1 
ATOM   1496 C  CB  . GLU   A 1 217 ? -6.578  24.593  13.447  1.00 43.37  ?  373 GLU   A CB  1 
ATOM   1497 C  CG  . GLU   A 1 217 ? -5.080  24.541  13.591  1.00 54.70  ?  373 GLU   A CG  1 
ATOM   1498 C  CD  . GLU   A 1 217 ? -4.516  23.135  13.484  1.00 54.75  ?  373 GLU   A CD  1 
ATOM   1499 O  OE1 . GLU   A 1 217 ? -5.207  22.176  13.897  1.00 50.41  ?  373 GLU   A OE1 1 
ATOM   1500 O  OE2 . GLU   A 1 217 ? -3.350  22.996  13.044  1.00 49.25  -1 373 GLU   A OE2 1 
ATOM   1501 N  N   . THR   A 1 218 ? -9.289  23.693  11.106  1.00 41.15  ?  374 THR   A N   1 
ATOM   1502 C  CA  . THR   A 1 218 ? -10.737 23.716  11.012  1.00 41.37  ?  374 THR   A CA  1 
ATOM   1503 C  C   . THR   A 1 218 ? -11.289 22.295  11.030  1.00 37.57  ?  374 THR   A C   1 
ATOM   1504 O  O   . THR   A 1 218 ? -10.631 21.349  10.587  1.00 41.87  ?  374 THR   A O   1 
ATOM   1505 C  CB  . THR   A 1 218 ? -11.175 24.436  9.735   1.00 44.23  ?  374 THR   A CB  1 
ATOM   1506 O  OG1 . THR   A 1 218 ? -10.248 24.129  8.682   1.00 47.31  ?  374 THR   A OG1 1 
ATOM   1507 C  CG2 . THR   A 1 218 ? -11.185 25.954  9.965   1.00 47.26  ?  374 THR   A CG2 1 
ATOM   1508 N  N   . TRP   A 1 219 ? -12.507 22.162  11.544  1.00 34.49  ?  375 TRP   A N   1 
ATOM   1509 C  CA  . TRP   A 1 219 ? -13.261 20.915  11.547  1.00 36.54  ?  375 TRP   A CA  1 
ATOM   1510 C  C   . TRP   A 1 219 ? -14.561 21.116  10.768  1.00 33.85  ?  375 TRP   A C   1 
ATOM   1511 O  O   . TRP   A 1 219 ? -15.233 22.139  10.922  1.00 35.62  ?  375 TRP   A O   1 
ATOM   1512 C  CB  . TRP   A 1 219 ? -13.582 20.479  12.978  1.00 34.39  ?  375 TRP   A CB  1 
ATOM   1513 C  CG  . TRP   A 1 219 ? -12.367 20.291  13.870  1.00 42.49  ?  375 TRP   A CG  1 
ATOM   1514 C  CD1 . TRP   A 1 219 ? -11.643 21.274  14.492  1.00 40.06  ?  375 TRP   A CD1 1 
ATOM   1515 C  CD2 . TRP   A 1 219 ? -11.811 19.048  14.303  1.00 37.59  ?  375 TRP   A CD2 1 
ATOM   1516 N  NE1 . TRP   A 1 219 ? -10.633 20.714  15.240  1.00 45.60  ?  375 TRP   A NE1 1 
ATOM   1517 C  CE2 . TRP   A 1 219 ? -10.727 19.348  15.157  1.00 48.16  ?  375 TRP   A CE2 1 
ATOM   1518 C  CE3 . TRP   A 1 219 ? -12.115 17.705  14.041  1.00 47.09  ?  375 TRP   A CE3 1 
ATOM   1519 C  CZ2 . TRP   A 1 219 ? -9.940  18.355  15.746  1.00 41.76  ?  375 TRP   A CZ2 1 
ATOM   1520 C  CZ3 . TRP   A 1 219 ? -11.333 16.713  14.636  1.00 40.39  ?  375 TRP   A CZ3 1 
ATOM   1521 C  CH2 . TRP   A 1 219 ? -10.264 17.047  15.478  1.00 46.75  ?  375 TRP   A CH2 1 
ATOM   1522 N  N   . ARG   A 1 220 ? -14.937 20.141  9.949   1.00 32.22  ?  376 ARG   A N   1 
ATOM   1523 C  CA  . ARG   A 1 220 ? -16.108 20.283  9.083   1.00 31.24  ?  376 ARG   A CA  1 
ATOM   1524 C  C   . ARG   A 1 220 ? -17.263 19.430  9.596   1.00 31.08  ?  376 ARG   A C   1 
ATOM   1525 O  O   . ARG   A 1 220 ? -17.053 18.319  10.095  1.00 31.16  ?  376 ARG   A O   1 
ATOM   1526 C  CB  . ARG   A 1 220 ? -15.774 19.905  7.639   1.00 31.77  ?  376 ARG   A CB  1 
ATOM   1527 C  CG  . ARG   A 1 220 ? -16.757 20.482  6.606   1.00 34.37  ?  376 ARG   A CG  1 
ATOM   1528 C  CD  . ARG   A 1 220 ? -16.665 19.698  5.319   1.00 33.24  ?  376 ARG   A CD  1 
ATOM   1529 N  NE  . ARG   A 1 220 ? -17.268 18.396  5.565   1.00 40.69  ?  376 ARG   A NE  1 
ATOM   1530 C  CZ  . ARG   A 1 220 ? -16.775 17.227  5.178   1.00 41.53  ?  376 ARG   A CZ  1 
ATOM   1531 N  NH1 . ARG   A 1 220 ? -15.727 17.147  4.373   1.00 34.19  ?  376 ARG   A NH1 1 
ATOM   1532 N  NH2 . ARG   A 1 220 ? -17.377 16.107  5.580   1.00 42.36  ?  376 ARG   A NH2 1 
ATOM   1533 N  N   . LEU   A 1 221 ? -18.479 19.971  9.515   1.00 29.15  ?  377 LEU   A N   1 
ATOM   1534 C  CA  . LEU   A 1 221 ? -19.649 19.224  9.956   1.00 29.03  ?  377 LEU   A CA  1 
ATOM   1535 C  C   . LEU   A 1 221 ? -19.851 17.985  9.090   1.00 33.69  ?  377 LEU   A C   1 
ATOM   1536 O  O   . LEU   A 1 221 ? -19.507 17.957  7.905   1.00 34.43  ?  377 LEU   A O   1 
ATOM   1537 C  CB  . LEU   A 1 221 ? -20.913 20.082  9.896   1.00 28.73  ?  377 LEU   A CB  1 
ATOM   1538 C  CG  . LEU   A 1 221 ? -21.034 21.267  10.858  1.00 33.86  ?  377 LEU   A CG  1 
ATOM   1539 C  CD1 . LEU   A 1 221 ? -22.220 22.120  10.512  1.00 28.94  ?  377 LEU   A CD1 1 
ATOM   1540 C  CD2 . LEU   A 1 221 ? -21.128 20.800  12.319  1.00 39.87  ?  377 LEU   A CD2 1 
ATOM   1541 N  N   . SER   A 1 222 ? -20.443 16.961  9.692   1.00 30.16  ?  378 SER   A N   1 
ATOM   1542 C  CA  . SER   A 1 222 ? -20.717 15.705  9.004   1.00 30.18  ?  378 SER   A CA  1 
ATOM   1543 C  C   . SER   A 1 222 ? -22.049 15.199  9.513   1.00 33.52  ?  378 SER   A C   1 
ATOM   1544 O  O   . SER   A 1 222 ? -22.272 15.143  10.726  1.00 28.87  ?  378 SER   A O   1 
ATOM   1545 C  CB  . SER   A 1 222 ? -19.621 14.659  9.247   1.00 31.50  ?  378 SER   A CB  1 
ATOM   1546 O  OG  . SER   A 1 222 ? -19.947 13.395  8.676   1.00 34.36  ?  378 SER   A OG  1 
ATOM   1547 N  N   . PHE   A 1 223 ? -22.933 14.861  8.570   1.00 32.04  ?  379 PHE   A N   1 
ATOM   1548 C  CA  . PHE   A 1 223 ? -24.259 14.342  8.863   1.00 36.78  ?  379 PHE   A CA  1 
ATOM   1549 C  C   . PHE   A 1 223 ? -24.476 13.003  8.172   1.00 34.06  ?  379 PHE   A C   1 
ATOM   1550 O  O   . PHE   A 1 223 ? -25.618 12.598  7.966   1.00 32.87  ?  379 PHE   A O   1 
ATOM   1551 C  CB  . PHE   A 1 223 ? -25.314 15.375  8.438   1.00 38.65  ?  379 PHE   A CB  1 
ATOM   1552 C  CG  . PHE   A 1 223 ? -25.214 16.663  9.218   1.00 32.63  ?  379 PHE   A CG  1 
ATOM   1553 C  CD1 . PHE   A 1 223 ? -25.709 16.748  10.501  1.00 34.86  ?  379 PHE   A CD1 1 
ATOM   1554 C  CD2 . PHE   A 1 223 ? -24.539 17.748  8.697   1.00 33.53  ?  379 PHE   A CD2 1 
ATOM   1555 C  CE1 . PHE   A 1 223 ? -25.573 17.927  11.252  1.00 34.56  ?  379 PHE   A CE1 1 
ATOM   1556 C  CE2 . PHE   A 1 223 ? -24.412 18.933  9.426   1.00 35.67  ?  379 PHE   A CE2 1 
ATOM   1557 C  CZ  . PHE   A 1 223 ? -24.925 19.016  10.702  1.00 38.54  ?  379 PHE   A CZ  1 
ATOM   1558 N  N   . SER   A 1 224 ? -23.388 12.309  7.833   1.00 33.33  ?  380 SER   A N   1 
ATOM   1559 C  CA  . SER   A 1 224 ? -23.470 11.030  7.138   1.00 34.81  ?  380 SER   A CA  1 
ATOM   1560 C  C   . SER   A 1 224 ? -24.368 10.020  7.850   1.00 35.25  ?  380 SER   A C   1 
ATOM   1561 O  O   . SER   A 1 224 ? -25.050 9.223   7.189   1.00 39.42  ?  380 SER   A O   1 
ATOM   1562 C  CB  . SER   A 1 224 ? -22.057 10.482  6.946   1.00 45.25  ?  380 SER   A CB  1 
ATOM   1563 O  OG  . SER   A 1 224 ? -21.480 11.088  5.783   1.00 55.19  ?  380 SER   A OG  1 
ATOM   1564 N  N   . HIS   A 1 225 ? -24.414 10.041  9.178   1.00 32.70  ?  381 HIS   A N   1 
ATOM   1565 C  CA  . HIS   A 1 225 ? -25.314 9.117   9.875   1.00 31.15  ?  381 HIS   A CA  1 
ATOM   1566 C  C   . HIS   A 1 225 ? -26.776 9.452   9.585   1.00 30.53  ?  381 HIS   A C   1 
ATOM   1567 O  O   . HIS   A 1 225 ? -27.630 8.557   9.491   1.00 28.89  ?  381 HIS   A O   1 
ATOM   1568 C  CB  . HIS   A 1 225 ? -25.019 9.156   11.383  1.00 32.74  ?  381 HIS   A CB  1 
ATOM   1569 C  CG  . HIS   A 1 225 ? -25.265 10.495  12.010  1.00 31.32  ?  381 HIS   A CG  1 
ATOM   1570 N  ND1 . HIS   A 1 225 ? -24.631 11.646  11.581  1.00 31.09  ?  381 HIS   A ND1 1 
ATOM   1571 C  CD2 . HIS   A 1 225 ? -26.046 10.863  13.052  1.00 32.83  ?  381 HIS   A CD2 1 
ATOM   1572 C  CE1 . HIS   A 1 225 ? -25.040 12.669  12.309  1.00 28.62  ?  381 HIS   A CE1 1 
ATOM   1573 N  NE2 . HIS   A 1 225 ? -25.895 12.222  13.213  1.00 32.73  ?  381 HIS   A NE2 1 
ATOM   1574 N  N   . ILE   A 1 226 ? -27.085 10.740  9.462   1.00 28.93  ?  382 ILE   A N   1 
ATOM   1575 C  CA  . ILE   A 1 226 ? -28.453 11.151  9.193   1.00 28.87  ?  382 ILE   A CA  1 
ATOM   1576 C  C   . ILE   A 1 226 ? -28.811 10.821  7.748   1.00 34.12  ?  382 ILE   A C   1 
ATOM   1577 O  O   . ILE   A 1 226 ? -29.917 10.356  7.461   1.00 28.39  ?  382 ILE   A O   1 
ATOM   1578 C  CB  . ILE   A 1 226 ? -28.624 12.651  9.503   1.00 30.41  ?  382 ILE   A CB  1 
ATOM   1579 C  CG1 . ILE   A 1 226 ? -28.226 12.971  10.963  1.00 30.83  ?  382 ILE   A CG1 1 
ATOM   1580 C  CG2 . ILE   A 1 226 ? -30.042 13.102  9.265   1.00 32.46  ?  382 ILE   A CG2 1 
ATOM   1581 C  CD1 . ILE   A 1 226 ? -29.019 12.226  12.029  1.00 27.69  ?  382 ILE   A CD1 1 
ATOM   1582 N  N   . GLU   A 1 227 ? -27.854 11.024  6.830   1.00 31.59  ?  383 GLU   A N   1 
ATOM   1583 C  CA  . GLU   A 1 227 ? -28.022 10.634  5.427   1.00 31.52  ?  383 GLU   A CA  1 
ATOM   1584 C  C   . GLU   A 1 227 ? -28.348 9.150   5.320   1.00 32.19  ?  383 GLU   A C   1 
ATOM   1585 O  O   . GLU   A 1 227 ? -29.306 8.747   4.646   1.00 27.83  ?  383 GLU   A O   1 
ATOM   1586 C  CB  . GLU   A 1 227 ? -26.729 10.970  4.671   1.00 37.71  ?  383 GLU   A CB  1 
ATOM   1587 C  CG  . GLU   A 1 227 ? -26.454 12.493  4.643   1.00 39.58  ?  383 GLU   A CG  1 
ATOM   1588 C  CD  . GLU   A 1 227 ? -24.998 12.878  4.345   1.00 42.01  ?  383 GLU   A CD  1 
ATOM   1589 O  OE1 . GLU   A 1 227 ? -24.146 11.989  4.195   1.00 45.62  ?  383 GLU   A OE1 1 
ATOM   1590 O  OE2 . GLU   A 1 227 ? -24.679 14.093  4.389   1.00 50.33  -1 383 GLU   A OE2 1 
ATOM   1591 N  N   . LYS   A 1 228 ? -27.562 8.321   6.008   1.00 29.09  ?  384 LYS   A N   1 
ATOM   1592 C  CA  . LYS   A 1 228 ? -27.831 6.888   6.076   1.00 34.89  ?  384 LYS   A CA  1 
ATOM   1593 C  C   . LYS   A 1 228 ? -29.251 6.620   6.563   1.00 33.42  ?  384 LYS   A C   1 
ATOM   1594 O  O   . LYS   A 1 228 ? -29.991 5.832   5.959   1.00 33.69  ?  384 LYS   A O   1 
ATOM   1595 C  CB  . LYS   A 1 228 ? -26.767 6.226   6.979   1.00 31.33  ?  384 LYS   A CB  1 
ATOM   1596 C  CG  . LYS   A 1 228 ? -26.871 4.719   7.289   1.00 38.64  ?  384 LYS   A CG  1 
ATOM   1597 C  CD  . LYS   A 1 228 ? -27.991 4.386   8.286   1.00 49.17  ?  384 LYS   A CD  1 
ATOM   1598 C  CE  . LYS   A 1 228 ? -27.614 3.262   9.265   1.00 58.58  ?  384 LYS   A CE  1 
ATOM   1599 N  NZ  . LYS   A 1 228 ? -28.549 3.279   10.432  1.00 58.40  ?  384 LYS   A NZ  1 
ATOM   1600 N  N   . GLU   A 1 229 ? -29.665 7.288   7.643   1.00 31.93  ?  385 GLU   A N   1 
ATOM   1601 C  CA  . GLU   A 1 229 ? -30.980 6.981   8.195   1.00 33.82  ?  385 GLU   A CA  1 
ATOM   1602 C  C   . GLU   A 1 229 ? -32.091 7.314   7.216   1.00 36.66  ?  385 GLU   A C   1 
ATOM   1603 O  O   . GLU   A 1 229 ? -33.078 6.572   7.107   1.00 31.91  ?  385 GLU   A O   1 
ATOM   1604 C  CB  . GLU   A 1 229 ? -31.197 7.714   9.501   1.00 33.93  ?  385 GLU   A CB  1 
ATOM   1605 C  CG  . GLU   A 1 229 ? -32.094 6.895   10.397  1.00 52.50  ?  385 GLU   A CG  1 
ATOM   1606 C  CD  . GLU   A 1 229 ? -31.844 7.199   11.839  1.00 46.39  ?  385 GLU   A CD  1 
ATOM   1607 O  OE1 . GLU   A 1 229 ? -30.959 6.531   12.422  1.00 59.48  ?  385 GLU   A OE1 1 
ATOM   1608 O  OE2 . GLU   A 1 229 ? -32.483 8.121   12.388  1.00 63.30  -1 385 GLU   A OE2 1 
ATOM   1609 N  N   . ILE   A 1 230 ? -31.962 8.434   6.513   1.00 28.29  ?  386 ILE   A N   1 
ATOM   1610 C  CA  . ILE   A 1 230 ? -33.010 8.827   5.588   1.00 31.01  ?  386 ILE   A CA  1 
ATOM   1611 C  C   . ILE   A 1 230 ? -33.076 7.849   4.411   1.00 37.65  ?  386 ILE   A C   1 
ATOM   1612 O  O   . ILE   A 1 230 ? -34.159 7.414   4.009   1.00 40.38  ?  386 ILE   A O   1 
ATOM   1613 C  CB  . ILE   A 1 230 ? -32.783 10.274  5.133   1.00 32.27  ?  386 ILE   A CB  1 
ATOM   1614 C  CG1 . ILE   A 1 230 ? -33.117 11.243  6.269   1.00 31.35  ?  386 ILE   A CG1 1 
ATOM   1615 C  CG2 . ILE   A 1 230 ? -33.603 10.570  3.915   1.00 40.75  ?  386 ILE   A CG2 1 
ATOM   1616 C  CD1 . ILE   A 1 230 ? -32.576 12.617  6.004   1.00 35.71  ?  386 ILE   A CD1 1 
ATOM   1617 N  N   . LEU   A 1 231 ? -31.924 7.456   3.866   1.00 35.17  ?  387 LEU   A N   1 
ATOM   1618 C  CA  . LEU   A 1 231 ? -31.930 6.573   2.697   1.00 30.96  ?  387 LEU   A CA  1 
ATOM   1619 C  C   . LEU   A 1 231 ? -32.595 5.235   2.988   1.00 37.13  ?  387 LEU   A C   1 
ATOM   1620 O  O   . LEU   A 1 231 ? -33.292 4.680   2.124   1.00 32.36  ?  387 LEU   A O   1 
ATOM   1621 C  CB  . LEU   A 1 231 ? -30.507 6.339   2.220   1.00 28.67  ?  387 LEU   A CB  1 
ATOM   1622 C  CG  . LEU   A 1 231 ? -30.018 7.411   1.279   1.00 40.13  ?  387 LEU   A CG  1 
ATOM   1623 C  CD1 . LEU   A 1 231 ? -28.530 7.226   1.054   1.00 37.86  ?  387 LEU   A CD1 1 
ATOM   1624 C  CD2 . LEU   A 1 231 ? -30.813 7.186   0.008   1.00 41.08  ?  387 LEU   A CD2 1 
ATOM   1625 N  N   . ASN   A 1 232 ? -32.349 4.675   4.184   1.00 32.00  ?  388 ASN   A N   1 
ATOM   1626 C  CA  . ASN   A 1 232 ? -32.865 3.372   4.600   1.00 33.06  ?  388 ASN   A CA  1 
ATOM   1627 C  C   . ASN   A 1 232 ? -34.234 3.426   5.256   1.00 32.43  ?  388 ASN   A C   1 
ATOM   1628 O  O   . ASN   A 1 232 ? -34.775 2.374   5.615   1.00 35.86  ?  388 ASN   A O   1 
ATOM   1629 C  CB  . ASN   A 1 232 ? -31.905 2.717   5.600   1.00 35.32  ?  388 ASN   A CB  1 
ATOM   1630 C  CG  . ASN   A 1 232 ? -30.653 2.233   4.941   1.00 49.27  ?  388 ASN   A CG  1 
ATOM   1631 O  OD1 . ASN   A 1 232 ? -30.647 1.987   3.740   1.00 41.92  ?  388 ASN   A OD1 1 
ATOM   1632 N  ND2 . ASN   A 1 232 ? -29.587 2.061   5.720   1.00 45.39  ?  388 ASN   A ND2 1 
ATOM   1633 N  N   . ASN   A 1 233 ? -34.756 4.597   5.518   1.00 27.13  ?  389 ASN   A N   1 
ATOM   1634 C  CA  . ASN   A 1 233 ? -36.077 4.739   6.085   1.00 28.67  ?  389 ASN   A CA  1 
ATOM   1635 C  C   . ASN   A 1 233 ? -36.638 5.950   5.351   1.00 29.35  ?  389 ASN   A C   1 
ATOM   1636 O  O   . ASN   A 1 233 ? -36.699 7.055   5.870   1.00 26.01  ?  389 ASN   A O   1 
ATOM   1637 C  CB  . ASN   A 1 233 ? -36.031 4.901   7.616   1.00 28.08  ?  389 ASN   A CB  1 
ATOM   1638 C  CG  . ASN   A 1 233 ? -37.415 4.844   8.265   1.00 30.48  ?  389 ASN   A CG  1 
ATOM   1639 O  OD1 . ASN   A 1 233 ? -38.425 4.584   7.609   1.00 27.34  ?  389 ASN   A OD1 1 
ATOM   1640 N  ND2 . ASN   A 1 233 ? -37.455 5.050   9.580   1.00 34.61  ?  389 ASN   A ND2 1 
ATOM   1641 N  N   . HIS   A 1 234 ? -37.008 5.735   4.077   1.00 33.09  ?  390 HIS   A N   1 
ATOM   1642 C  CA  . HIS   A 1 234 ? -37.078 6.814   3.095   1.00 29.77  ?  390 HIS   A CA  1 
ATOM   1643 C  C   . HIS   A 1 234 ? -38.488 7.152   2.622   1.00 32.26  ?  390 HIS   A C   1 
ATOM   1644 O  O   . HIS   A 1 234 ? -38.637 8.055   1.779   1.00 26.35  ?  390 HIS   A O   1 
ATOM   1645 C  CB  . HIS   A 1 234 ? -36.265 6.425   1.854   1.00 27.95  ?  390 HIS   A CB  1 
ATOM   1646 C  CG  . HIS   A 1 234 ? -36.689 5.101   1.288   1.00 26.84  ?  390 HIS   A CG  1 
ATOM   1647 N  ND1 . HIS   A 1 234 ? -35.894 3.980   1.306   1.00 32.38  ?  390 HIS   A ND1 1 
ATOM   1648 C  CD2 . HIS   A 1 234 ? -37.878 4.706   0.776   1.00 26.15  ?  390 HIS   A CD2 1 
ATOM   1649 C  CE1 . HIS   A 1 234 ? -36.558 2.957   0.790   1.00 25.99  ?  390 HIS   A CE1 1 
ATOM   1650 N  NE2 . HIS   A 1 234 ? -37.761 3.375   0.461   1.00 29.29  ?  390 HIS   A NE2 1 
ATOM   1651 N  N   . GLY   A 1 235 ? -39.509 6.410   3.037   1.00 27.07  ?  391 GLY   A N   1 
ATOM   1652 C  CA  . GLY   A 1 235 ? -40.832 6.597   2.483   1.00 27.95  ?  391 GLY   A CA  1 
ATOM   1653 C  C   . GLY   A 1 235 ? -41.649 7.550   3.349   1.00 33.87  ?  391 GLY   A C   1 
ATOM   1654 O  O   . GLY   A 1 235 ? -41.327 7.784   4.514   1.00 25.56  ?  391 GLY   A O   1 
ATOM   1655 N  N   . LYS   A 1 236 ? -42.711 8.118   2.763   1.00 25.12  ?  392 LYS   A N   1 
ATOM   1656 C  CA  . LYS   A 1 236 ? -43.722 8.749   3.605   1.00 25.03  ?  392 LYS   A CA  1 
ATOM   1657 C  C   . LYS   A 1 236 ? -44.490 7.697   4.394   1.00 28.11  ?  392 LYS   A C   1 
ATOM   1658 O  O   . LYS   A 1 236 ? -44.774 7.891   5.589   1.00 27.05  ?  392 LYS   A O   1 
ATOM   1659 C  CB  . LYS   A 1 236 ? -44.651 9.630   2.784   1.00 24.98  ?  392 LYS   A CB  1 
ATOM   1660 C  CG  . LYS   A 1 236 ? -45.820 10.129  3.589   1.00 31.35  ?  392 LYS   A CG  1 
ATOM   1661 C  CD  . LYS   A 1 236 ? -46.486 11.348  3.005   1.00 30.14  ?  392 LYS   A CD  1 
ATOM   1662 C  CE  . LYS   A 1 236 ? -45.704 12.591  3.432   1.00 38.39  ?  392 LYS   A CE  1 
ATOM   1663 N  NZ  . LYS   A 1 236 ? -46.540 13.735  3.044   1.00 50.72  ?  392 LYS   A NZ  1 
ATOM   1664 N  N   . SER   A 1 237 ? -44.778 6.560   3.769   1.00 25.34  ?  393 SER   A N   1 
ATOM   1665 C  CA  . SER   A 1 237 ? -45.288 5.411   4.511   1.00 27.62  ?  393 SER   A CA  1 
ATOM   1666 C  C   . SER   A 1 237 ? -44.162 4.745   5.291   1.00 27.58  ?  393 SER   A C   1 
ATOM   1667 O  O   . SER   A 1 237 ? -43.071 4.495   4.762   1.00 24.54  ?  393 SER   A O   1 
ATOM   1668 C  CB  . SER   A 1 237 ? -45.923 4.382   3.584   1.00 24.24  ?  393 SER   A CB  1 
ATOM   1669 O  OG  . SER   A 1 237 ? -46.320 3.204   4.285   1.00 26.48  ?  393 SER   A OG  1 
ATOM   1670 N  N   . LYS   A 1 238 ? -44.462 4.392   6.539   1.00 23.91  ?  394 LYS   A N   1 
ATOM   1671 C  CA  . LYS   A 1 238 ? -43.488 3.642   7.324   1.00 27.08  ?  394 LYS   A CA  1 
ATOM   1672 C  C   . LYS   A 1 238 ? -43.208 2.272   6.724   1.00 30.88  ?  394 LYS   A C   1 
ATOM   1673 O  O   . LYS   A 1 238 ? -42.127 1.708   6.947   1.00 26.12  ?  394 LYS   A O   1 
ATOM   1674 C  CB  . LYS   A 1 238 ? -43.989 3.498   8.762   1.00 23.03  ?  394 LYS   A CB  1 
ATOM   1675 C  CG  . LYS   A 1 238 ? -43.976 4.842   9.505   1.00 21.19  ?  394 LYS   A CG  1 
ATOM   1676 C  CD  . LYS   A 1 238 ? -44.684 4.708   10.865  1.00 24.28  ?  394 LYS   A CD  1 
ATOM   1677 C  CE  . LYS   A 1 238 ? -44.849 6.088   11.514  1.00 23.76  ?  394 LYS   A CE  1 
ATOM   1678 N  NZ  . LYS   A 1 238 ? -45.796 5.994   12.655  1.00 25.71  ?  394 LYS   A NZ  1 
ATOM   1679 N  N   . THR   A 1 239 ? -44.169 1.697   5.995   1.00 27.76  ?  395 THR   A N   1 
ATOM   1680 C  CA  . THR   A 1 239 ? -43.979 0.372   5.408   1.00 32.93  ?  395 THR   A CA  1 
ATOM   1681 C  C   . THR   A 1 239 ? -43.552 0.446   3.947   1.00 32.40  ?  395 THR   A C   1 
ATOM   1682 O  O   . THR   A 1 239 ? -43.643 -0.554  3.233   1.00 28.04  ?  395 THR   A O   1 
ATOM   1683 C  CB  . THR   A 1 239 ? -45.247 -0.483  5.499   1.00 34.89  ?  395 THR   A CB  1 
ATOM   1684 O  OG1 . THR   A 1 239 ? -46.385 0.285   5.060   1.00 28.58  ?  395 THR   A OG1 1 
ATOM   1685 C  CG2 . THR   A 1 239 ? -45.446 -0.972  6.936   1.00 30.72  ?  395 THR   A CG2 1 
ATOM   1686 N  N   . CYS   A 1 240 ? -43.071 1.597   3.501   1.00 31.77  ?  396 CYS   A N   1 
ATOM   1687 C  CA  . CYS   A 1 240 ? -42.618 1.699   2.129   1.00 27.96  ?  396 CYS   A CA  1 
ATOM   1688 C  C   . CYS   A 1 240 ? -41.476 0.703   1.902   1.00 31.02  ?  396 CYS   A C   1 
ATOM   1689 O  O   . CYS   A 1 240 ? -40.559 0.573   2.728   1.00 29.05  ?  396 CYS   A O   1 
ATOM   1690 C  CB  . CYS   A 1 240 ? -42.213 3.150   1.827   1.00 28.46  ?  396 CYS   A CB  1 
ATOM   1691 S  SG  . CYS   A 1 240 ? -41.337 3.437   0.235   1.00 25.60  ?  396 CYS   A SG  1 
ATOM   1692 N  N   . CYS   A 1 241 ? -41.570 -0.047  0.810   1.00 26.61  ?  397 CYS   A N   1 
ATOM   1693 C  CA  . CYS   A 1 241 ? -40.698 -1.150  0.397   1.00 26.14  ?  397 CYS   A CA  1 
ATOM   1694 C  C   . CYS   A 1 241 ? -40.735 -2.382  1.299   1.00 26.47  ?  397 CYS   A C   1 
ATOM   1695 O  O   . CYS   A 1 241 ? -39.938 -3.307  1.080   1.00 27.74  ?  397 CYS   A O   1 
ATOM   1696 C  CB  . CYS   A 1 241 ? -39.241 -0.726  0.201   1.00 25.83  ?  397 CYS   A CB  1 
ATOM   1697 S  SG  . CYS   A 1 241 ? -38.943 0.422   -1.213  1.00 27.42  ?  397 CYS   A SG  1 
ATOM   1698 N  N   . GLU   A 1 242 ? -41.682 -2.496  2.232   1.00 24.32  ?  398 GLU   A N   1 
ATOM   1699 C  CA  . GLU   A 1 242 ? -41.768 -3.715  3.036   1.00 29.58  ?  398 GLU   A CA  1 
ATOM   1700 C  C   . GLU   A 1 242 ? -42.786 -4.728  2.497   1.00 32.99  ?  398 GLU   A C   1 
ATOM   1701 O  O   . GLU   A 1 242 ? -42.964 -5.793  3.094   1.00 27.07  ?  398 GLU   A O   1 
ATOM   1702 C  CB  . GLU   A 1 242 ? -42.105 -3.373  4.507   1.00 27.10  ?  398 GLU   A CB  1 
ATOM   1703 C  CG  . GLU   A 1 242 ? -40.982 -2.571  5.235   1.00 23.73  ?  398 GLU   A CG  1 
ATOM   1704 C  CD  . GLU   A 1 242 ? -41.150 -2.537  6.775   1.00 35.70  ?  398 GLU   A CD  1 
ATOM   1705 O  OE1 . GLU   A 1 242 ? -42.219 -2.943  7.291   1.00 31.36  ?  398 GLU   A OE1 1 
ATOM   1706 O  OE2 . GLU   A 1 242 ? -40.191 -2.137  7.469   1.00 31.76  -1 398 GLU   A OE2 1 
ATOM   1707 N  N   . ASN   A 1 243 ? -43.462 -4.425  1.395   1.00 34.80  ?  399 ASN   A N   1 
ATOM   1708 C  CA  . ASN   A 1 243 ? -44.437 -5.331  0.796   1.00 33.76  ?  399 ASN   A CA  1 
ATOM   1709 C  C   . ASN   A 1 243 ? -44.515 -5.021  -0.698  1.00 33.64  ?  399 ASN   A C   1 
ATOM   1710 O  O   . ASN   A 1 243 ? -44.021 -3.988  -1.161  1.00 30.60  ?  399 ASN   A O   1 
ATOM   1711 C  CB  . ASN   A 1 243 ? -45.807 -5.182  1.467   1.00 31.11  ?  399 ASN   A CB  1 
ATOM   1712 C  CG  . ASN   A 1 243 ? -46.351 -3.757  1.363   1.00 34.96  ?  399 ASN   A CG  1 
ATOM   1713 O  OD1 . ASN   A 1 243 ? -46.556 -3.231  0.261   1.00 31.27  ?  399 ASN   A OD1 1 
ATOM   1714 N  ND2 . ASN   A 1 243 ? -46.588 -3.122  2.517   1.00 32.07  ?  399 ASN   A ND2 1 
ATOM   1715 N  N   . LYS   A 1 244 ? -45.146 -5.925  -1.453  1.00 33.97  ?  400 LYS   A N   1 
ATOM   1716 C  CA  . LYS   A 1 244 ? -45.288 -5.717  -2.902  1.00 38.72  ?  400 LYS   A CA  1 
ATOM   1717 C  C   . LYS   A 1 244 ? -45.980 -4.406  -3.243  1.00 32.66  ?  400 LYS   A C   1 
ATOM   1718 O  O   . LYS   A 1 244 ? -45.522 -3.678  -4.124  1.00 36.25  ?  400 LYS   A O   1 
ATOM   1719 C  CB  . LYS   A 1 244 ? -46.060 -6.854  -3.556  1.00 38.45  ?  400 LYS   A CB  1 
ATOM   1720 C  CG  . LYS   A 1 244 ? -45.261 -8.057  -3.830  1.00 48.43  ?  400 LYS   A CG  1 
ATOM   1721 C  CD  . LYS   A 1 244 ? -46.171 -9.131  -4.393  1.00 43.29  ?  400 LYS   A CD  1 
ATOM   1722 C  CE  . LYS   A 1 244 ? -45.758 -9.419  -5.806  1.00 52.60  ?  400 LYS   A CE  1 
ATOM   1723 N  NZ  . LYS   A 1 244 ? -46.848 -9.561  -6.897  1.00 46.08  ?  400 LYS   A NZ  1 
ATOM   1724 N  N   . GLU   A 1 245 ? -47.116 -4.105  -2.591  1.00 35.91  ?  401 GLU   A N   1 
ATOM   1725 C  CA  . GLU   A 1 245 ? -47.879 -2.893  -2.905  1.00 32.89  ?  401 GLU   A CA  1 
ATOM   1726 C  C   . GLU   A 1 245 ? -47.047 -1.616  -2.805  1.00 33.91  ?  401 GLU   A C   1 
ATOM   1727 O  O   . GLU   A 1 245 ? -47.381 -0.612  -3.440  1.00 33.26  ?  401 GLU   A O   1 
ATOM   1728 C  CB  . GLU   A 1 245 ? -49.099 -2.777  -1.972  1.00 40.17  ?  401 GLU   A CB  1 
ATOM   1729 C  CG  . GLU   A 1 245 ? -50.152 -1.772  -2.467  1.00 41.88  ?  401 GLU   A CG  1 
ATOM   1730 C  CD  . GLU   A 1 245 ? -51.028 -2.296  -3.628  1.00 52.59  ?  401 GLU   A CD  1 
ATOM   1731 O  OE1 . GLU   A 1 245 ? -51.308 -3.515  -3.705  1.00 54.52  ?  401 GLU   A OE1 1 
ATOM   1732 O  OE2 . GLU   A 1 245 ? -51.387 -1.481  -4.509  1.00 51.74  -1 401 GLU   A OE2 1 
ATOM   1733 N  N   . GLU   A 1 246 ? -45.977 -1.618  -2.016  1.00 36.46  ?  402 GLU   A N   1 
ATOM   1734 C  CA  . GLU   A 1 246 ? -45.304 -0.372  -1.677  1.00 35.12  ?  402 GLU   A CA  1 
ATOM   1735 C  C   . GLU   A 1 246 ? -43.846 -0.360  -2.105  1.00 33.78  ?  402 GLU   A C   1 
ATOM   1736 O  O   . GLU   A 1 246 ? -43.065 0.418   -1.549  1.00 29.61  ?  402 GLU   A O   1 
ATOM   1737 C  CB  . GLU   A 1 246 ? -45.422 -0.107  -0.172  1.00 33.94  ?  402 GLU   A CB  1 
ATOM   1738 C  CG  . GLU   A 1 246 ? -46.874 0.014   0.344   1.00 32.45  ?  402 GLU   A CG  1 
ATOM   1739 C  CD  . GLU   A 1 246 ? -46.915 0.462   1.835   1.00 31.60  ?  402 GLU   A CD  1 
ATOM   1740 O  OE1 . GLU   A 1 246 ? -46.628 1.640   2.083   1.00 27.66  ?  402 GLU   A OE1 1 
ATOM   1741 O  OE2 . GLU   A 1 246 ? -47.243 -0.347  2.735   1.00 32.06  -1 402 GLU   A OE2 1 
ATOM   1742 N  N   . LYS   A 1 247 ? -43.444 -1.194  -3.077  1.00 28.70  ?  403 LYS   A N   1 
ATOM   1743 C  CA  . LYS   A 1 247 ? -42.065 -1.099  -3.544  1.00 30.81  ?  403 LYS   A CA  1 
ATOM   1744 C  C   . LYS   A 1 247 ? -41.861 0.245   -4.239  1.00 33.56  ?  403 LYS   A C   1 
ATOM   1745 O  O   . LYS   A 1 247 ? -42.668 0.637   -5.086  1.00 32.10  ?  403 LYS   A O   1 
ATOM   1746 C  CB  . LYS   A 1 247 ? -41.705 -2.251  -4.482  1.00 27.70  ?  403 LYS   A CB  1 
ATOM   1747 C  CG  . LYS   A 1 247 ? -41.752 -3.613  -3.812  1.00 36.14  ?  403 LYS   A CG  1 
ATOM   1748 C  CD  . LYS   A 1 247 ? -40.591 -3.772  -2.817  1.00 39.69  ?  403 LYS   A CD  1 
ATOM   1749 C  CE  . LYS   A 1 247 ? -40.603 -5.133  -2.170  1.00 42.84  ?  403 LYS   A CE  1 
ATOM   1750 N  NZ  . LYS   A 1 247 ? -39.473 -5.312  -1.188  1.00 36.61  ?  403 LYS   A NZ  1 
ATOM   1751 N  N   . CYS   A 1 248 ? -40.795 0.964   -3.864  1.00 33.40  ?  404 CYS   A N   1 
ATOM   1752 C  CA  . CYS   A 1 248 ? -40.469 2.239   -4.503  1.00 28.84  ?  404 CYS   A CA  1 
ATOM   1753 C  C   . CYS   A 1 248 ? -39.099 2.117   -5.159  1.00 27.86  ?  404 CYS   A C   1 
ATOM   1754 O  O   . CYS   A 1 248 ? -38.403 1.120   -4.976  1.00 28.89  ?  404 CYS   A O   1 
ATOM   1755 C  CB  . CYS   A 1 248 ? -40.516 3.403   -3.497  1.00 27.80  ?  404 CYS   A CB  1 
ATOM   1756 S  SG  . CYS   A 1 248 ? -38.984 3.804   -2.604  1.00 26.65  ?  404 CYS   A SG  1 
ATOM   1757 N  N   . CYS   A 1 249 ? -38.693 3.129   -5.936  1.00 24.06  ?  405 CYS   A N   1 
ATOM   1758 C  CA  . CYS   A 1 249 ? -37.393 3.079   -6.612  1.00 25.81  ?  405 CYS   A CA  1 
ATOM   1759 C  C   . CYS   A 1 249 ? -36.451 4.196   -6.142  1.00 24.40  ?  405 CYS   A C   1 
ATOM   1760 O  O   . CYS   A 1 249 ? -35.490 4.549   -6.841  1.00 26.51  ?  405 CYS   A O   1 
ATOM   1761 C  CB  . CYS   A 1 249 ? -37.560 3.133   -8.138  1.00 32.86  ?  405 CYS   A CB  1 
ATOM   1762 S  SG  . CYS   A 1 249 ? -38.258 4.699   -8.758  1.00 29.38  ?  405 CYS   A SG  1 
ATOM   1763 N  N   . ARG   A 1 250 ? -36.669 4.734   -4.947  1.00 26.98  ?  406 ARG   A N   1 
ATOM   1764 C  CA  . ARG   A 1 250 ? -35.786 5.792   -4.441  1.00 27.12  ?  406 ARG   A CA  1 
ATOM   1765 C  C   . ARG   A 1 250 ? -34.332 5.326   -4.341  1.00 26.90  ?  406 ARG   A C   1 
ATOM   1766 O  O   . ARG   A 1 250 ? -33.424 5.968   -4.896  1.00 24.66  ?  406 ARG   A O   1 
ATOM   1767 C  CB  . ARG   A 1 250 ? -36.289 6.295   -3.085  1.00 22.85  ?  406 ARG   A CB  1 
ATOM   1768 C  CG  . ARG   A 1 250 ? -37.523 7.230   -3.145  1.00 28.59  ?  406 ARG   A CG  1 
ATOM   1769 C  CD  . ARG   A 1 250 ? -37.877 7.618   -1.682  1.00 30.90  ?  406 ARG   A CD  1 
ATOM   1770 N  NE  . ARG   A 1 250 ? -39.020 8.503   -1.512  1.00 25.61  ?  406 ARG   A NE  1 
ATOM   1771 C  CZ  . ARG   A 1 250 ? -40.244 8.080   -1.212  1.00 26.35  ?  406 ARG   A CZ  1 
ATOM   1772 N  NH1 . ARG   A 1 250 ? -40.527 6.791   -1.110  1.00 22.00  ?  406 ARG   A NH1 1 
ATOM   1773 N  NH2 . ARG   A 1 250 ? -41.207 8.974   -1.002  1.00 27.87  ?  406 ARG   A NH2 1 
ATOM   1774 N  N   . LYS   A 1 251 ? -34.082 4.202   -3.641  1.00 25.46  ?  407 LYS   A N   1 
ATOM   1775 C  CA  . LYS   A 1 251 ? -32.699 3.760   -3.474  1.00 26.74  ?  407 LYS   A CA  1 
ATOM   1776 C  C   . LYS   A 1 251 ? -32.062 3.396   -4.812  1.00 27.05  ?  407 LYS   A C   1 
ATOM   1777 O  O   . LYS   A 1 251 ? -30.895 3.719   -5.048  1.00 25.05  ?  407 LYS   A O   1 
ATOM   1778 C  CB  . LYS   A 1 251 ? -32.610 2.571   -2.503  1.00 30.37  ?  407 LYS   A CB  1 
ATOM   1779 C  CG  . LYS   A 1 251 ? -32.975 2.931   -1.031  1.00 28.09  ?  407 LYS   A CG  1 
ATOM   1780 C  CD  . LYS   A 1 251 ? -32.886 1.723   -0.072  1.00 35.47  ?  407 LYS   A CD  1 
ATOM   1781 C  CE  . LYS   A 1 251 ? -31.467 1.442   0.410   1.00 47.85  ?  407 LYS   A CE  1 
ATOM   1782 N  NZ  . LYS   A 1 251 ? -31.426 0.219   1.260   1.00 51.51  ?  407 LYS   A NZ  1 
ATOM   1783 N  N   . ASP   A 1 252 ? -32.811 2.717   -5.702  1.00 25.73  ?  408 ASP   A N   1 
ATOM   1784 C  CA  . ASP   A 1 252 ? -32.280 2.397   -7.032  1.00 24.18  ?  408 ASP   A CA  1 
ATOM   1785 C  C   . ASP   A 1 252 ? -31.910 3.655   -7.818  1.00 25.18  ?  408 ASP   A C   1 
ATOM   1786 O  O   . ASP   A 1 252 ? -30.907 3.673   -8.538  1.00 25.93  ?  408 ASP   A O   1 
ATOM   1787 C  CB  . ASP   A 1 252 ? -33.299 1.575   -7.825  1.00 25.47  ?  408 ASP   A CB  1 
ATOM   1788 C  CG  . ASP   A 1 252 ? -33.327 0.128   -7.408  1.00 36.51  ?  408 ASP   A CG  1 
ATOM   1789 O  OD1 . ASP   A 1 252 ? -32.329 -0.335  -6.808  1.00 34.42  ?  408 ASP   A OD1 1 
ATOM   1790 O  OD2 . ASP   A 1 252 ? -34.337 -0.547  -7.694  1.00 43.51  -1 408 ASP   A OD2 1 
ATOM   1791 N  N   . CYS   A 1 253 ? -32.728 4.706   -7.723  1.00 24.76  ?  409 CYS   A N   1 
ATOM   1792 C  CA  . CYS   A 1 253 ? -32.390 5.970   -8.379  1.00 24.96  ?  409 CYS   A CA  1 
ATOM   1793 C  C   . CYS   A 1 253 ? -31.063 6.531   -7.898  1.00 28.62  ?  409 CYS   A C   1 
ATOM   1794 O  O   . CYS   A 1 253 ? -30.237 6.977   -8.710  1.00 26.23  ?  409 CYS   A O   1 
ATOM   1795 C  CB  . CYS   A 1 253 ? -33.501 6.989   -8.183  1.00 24.58  ?  409 CYS   A CB  1 
ATOM   1796 S  SG  . CYS   A 1 253 ? -34.906 6.666   -9.335  1.00 26.58  ?  409 CYS   A SG  1 
ATOM   1797 N  N   . LEU   A 1 254 ? -30.839 6.550   -6.572  1.00 26.17  ?  410 LEU   A N   1 
ATOM   1798 C  CA  . LEU   A 1 254 ? -29.558 7.067   -6.085  1.00 27.71  ?  410 LEU   A CA  1 
ATOM   1799 C  C   . LEU   A 1 254 ? -28.394 6.206   -6.560  1.00 26.24  ?  410 LEU   A C   1 
ATOM   1800 O  O   . LEU   A 1 254 ? -27.345 6.738   -6.937  1.00 27.59  ?  410 LEU   A O   1 
ATOM   1801 C  CB  . LEU   A 1 254 ? -29.552 7.174   -4.550  1.00 24.48  ?  410 LEU   A CB  1 
ATOM   1802 C  CG  . LEU   A 1 254 ? -28.200 7.645   -3.970  1.00 28.71  ?  410 LEU   A CG  1 
ATOM   1803 C  CD1 . LEU   A 1 254 ? -27.747 9.033   -4.522  1.00 25.98  ?  410 LEU   A CD1 1 
ATOM   1804 C  CD2 . LEU   A 1 254 ? -28.260 7.681   -2.439  1.00 31.43  ?  410 LEU   A CD2 1 
ATOM   1805 N  N   . LYS   A 1 255 ? -28.545 4.874   -6.518  1.00 26.47  ?  411 LYS   A N   1 
ATOM   1806 C  CA  . LYS   A 1 255 ? -27.475 3.990   -6.988  1.00 27.28  ?  411 LYS   A CA  1 
ATOM   1807 C  C   . LYS   A 1 255 ? -27.107 4.300   -8.437  1.00 28.81  ?  411 LYS   A C   1 
ATOM   1808 O  O   . LYS   A 1 255 ? -25.924 4.401   -8.785  1.00 29.23  ?  411 LYS   A O   1 
ATOM   1809 C  CB  . LYS   A 1 255 ? -27.893 2.518   -6.851  1.00 27.07  ?  411 LYS   A CB  1 
ATOM   1810 C  CG  . LYS   A 1 255 ? -27.981 2.052   -5.392  1.00 34.24  ?  411 LYS   A CG  1 
ATOM   1811 C  CD  . LYS   A 1 255 ? -28.448 0.596   -5.243  1.00 36.94  ?  411 LYS   A CD  1 
ATOM   1812 C  CE  . LYS   A 1 255 ? -28.549 0.242   -3.742  1.00 43.36  ?  411 LYS   A CE  1 
ATOM   1813 N  NZ  . LYS   A 1 255 ? -29.061 -1.133  -3.543  1.00 50.12  ?  411 LYS   A NZ  1 
ATOM   1814 N  N   . LEU   A 1 256 ? -28.127 4.426   -9.300  1.00 25.98  ?  412 LEU   A N   1 
ATOM   1815 C  CA  . LEU   A 1 256 ? -27.898 4.757   -10.704 1.00 27.78  ?  412 LEU   A CA  1 
ATOM   1816 C  C   . LEU   A 1 256 ? -27.200 6.105   -10.854 1.00 27.72  ?  412 LEU   A C   1 
ATOM   1817 O  O   . LEU   A 1 256 ? -26.251 6.228   -11.636 1.00 28.49  ?  412 LEU   A O   1 
ATOM   1818 C  CB  . LEU   A 1 256 ? -29.236 4.726   -11.462 1.00 26.89  ?  412 LEU   A CB  1 
ATOM   1819 C  CG  . LEU   A 1 256 ? -29.841 3.308   -11.570 1.00 26.48  ?  412 LEU   A CG  1 
ATOM   1820 C  CD1 . LEU   A 1 256 ? -31.305 3.344   -12.101 1.00 27.12  ?  412 LEU   A CD1 1 
ATOM   1821 C  CD2 . LEU   A 1 256 ? -28.998 2.352   -12.414 1.00 28.50  ?  412 LEU   A CD2 1 
ATOM   1822 N  N   . MET   A 1 257 ? -27.639 7.126   -10.104 1.00 29.60  ?  413 MET   A N   1 
ATOM   1823 C  CA  . MET   A 1 257 ? -26.944 8.422   -10.139 1.00 29.70  ?  413 MET   A CA  1 
ATOM   1824 C  C   . MET   A 1 257 ? -25.472 8.302   -9.740  1.00 31.51  ?  413 MET   A C   1 
ATOM   1825 O  O   . MET   A 1 257 ? -24.595 8.891   -10.383 1.00 31.06  ?  413 MET   A O   1 
ATOM   1826 C  CB  . MET   A 1 257 ? -27.638 9.451   -9.239  1.00 28.44  ?  413 MET   A CB  1 
ATOM   1827 C  CG  . MET   A 1 257 ? -29.051 9.856   -9.635  1.00 32.21  ?  413 MET   A CG  1 
ATOM   1828 S  SD  . MET   A 1 257 ? -29.825 10.964  -8.413  1.00 40.09  ?  413 MET   A SD  1 
ATOM   1829 C  CE  . MET   A 1 257 ? -29.050 12.559  -8.731  1.00 31.21  ?  413 MET   A CE  1 
ATOM   1830 N  N   . LYS   A 1 258 ? -25.177 7.565   -8.663  1.00 30.17  ?  414 LYS   A N   1 
ATOM   1831 C  CA  . LYS   A 1 258 ? -23.781 7.384   -8.258  1.00 32.23  ?  414 LYS   A CA  1 
ATOM   1832 C  C   . LYS   A 1 258 ? -22.980 6.648   -9.324  1.00 30.89  ?  414 LYS   A C   1 
ATOM   1833 O  O   . LYS   A 1 258 ? -21.847 7.029   -9.648  1.00 30.90  ?  414 LYS   A O   1 
ATOM   1834 C  CB  . LYS   A 1 258 ? -23.705 6.612   -6.933  1.00 29.41  ?  414 LYS   A CB  1 
ATOM   1835 C  CG  . LYS   A 1 258 ? -24.090 7.418   -5.689  1.00 32.20  ?  414 LYS   A CG  1 
ATOM   1836 C  CD  . LYS   A 1 258 ? -23.870 6.563   -4.429  1.00 41.26  ?  414 LYS   A CD  1 
ATOM   1837 C  CE  . LYS   A 1 258 ? -24.153 7.323   -3.148  1.00 42.44  ?  414 LYS   A CE  1 
ATOM   1838 N  NZ  . LYS   A 1 258 ? -23.844 6.447   -1.974  1.00 57.94  ?  414 LYS   A NZ  1 
ATOM   1839 N  N   . TYR   A 1 259 ? -23.544 5.560   -9.853  1.00 29.94  ?  415 TYR   A N   1 
ATOM   1840 C  CA  . TYR   A 1 259 ? -22.830 4.770   -10.853 1.00 30.45  ?  415 TYR   A CA  1 
ATOM   1841 C  C   . TYR   A 1 259 ? -22.578 5.592   -12.118 1.00 31.66  ?  415 TYR   A C   1 
ATOM   1842 O  O   . TYR   A 1 259 ? -21.527 5.454   -12.763 1.00 30.99  ?  415 TYR   A O   1 
ATOM   1843 C  CB  . TYR   A 1 259 ? -23.622 3.492   -11.147 1.00 30.61  ?  415 TYR   A CB  1 
ATOM   1844 C  CG  . TYR   A 1 259 ? -22.929 2.519   -12.067 1.00 37.08  ?  415 TYR   A CG  1 
ATOM   1845 C  CD1 . TYR   A 1 259 ? -21.809 1.832   -11.645 1.00 34.81  ?  415 TYR   A CD1 1 
ATOM   1846 C  CD2 . TYR   A 1 259 ? -23.434 2.240   -13.337 1.00 40.39  ?  415 TYR   A CD2 1 
ATOM   1847 C  CE1 . TYR   A 1 259 ? -21.172 0.932   -12.458 1.00 40.52  ?  415 TYR   A CE1 1 
ATOM   1848 C  CE2 . TYR   A 1 259 ? -22.805 1.330   -14.168 1.00 41.99  ?  415 TYR   A CE2 1 
ATOM   1849 C  CZ  . TYR   A 1 259 ? -21.670 0.680   -13.718 1.00 46.77  ?  415 TYR   A CZ  1 
ATOM   1850 O  OH  . TYR   A 1 259 ? -21.016 -0.224  -14.514 1.00 49.24  ?  415 TYR   A OH  1 
ATOM   1851 N  N   . LEU   A 1 260 ? -23.514 6.487   -12.460 1.00 32.43  ?  416 LEU   A N   1 
ATOM   1852 C  CA  . LEU   A 1 260 ? -23.323 7.361   -13.625 1.00 36.87  ?  416 LEU   A CA  1 
ATOM   1853 C  C   . LEU   A 1 260 ? -22.106 8.256   -13.436 1.00 34.80  ?  416 LEU   A C   1 
ATOM   1854 O  O   . LEU   A 1 260 ? -21.207 8.306   -14.295 1.00 34.59  ?  416 LEU   A O   1 
ATOM   1855 C  CB  . LEU   A 1 260 ? -24.580 8.206   -13.872 1.00 31.50  ?  416 LEU   A CB  1 
ATOM   1856 C  CG  . LEU   A 1 260 ? -24.543 9.252   -15.011 1.00 39.00  ?  416 LEU   A CG  1 
ATOM   1857 C  CD1 . LEU   A 1 260 ? -24.254 8.630   -16.390 1.00 31.81  ?  416 LEU   A CD1 1 
ATOM   1858 C  CD2 . LEU   A 1 260 ? -25.848 10.033  -15.086 1.00 33.00  ?  416 LEU   A CD2 1 
ATOM   1859 N  N   . LEU   A 1 261 ? -22.052 8.960   -12.300 1.00 32.20  ?  417 LEU   A N   1 
ATOM   1860 C  CA  . LEU   A 1 261 ? -20.931 9.857   -12.037 1.00 31.74  ?  417 LEU   A CA  1 
ATOM   1861 C  C   . LEU   A 1 261 ? -19.626 9.084   -11.992 1.00 37.04  ?  417 LEU   A C   1 
ATOM   1862 O  O   . LEU   A 1 261 ? -18.610 9.525   -12.549 1.00 34.61  ?  417 LEU   A O   1 
ATOM   1863 C  CB  . LEU   A 1 261 ? -21.140 10.602  -10.714 1.00 32.64  ?  417 LEU   A CB  1 
ATOM   1864 C  CG  . LEU   A 1 261 ? -20.021 11.594  -10.391 1.00 31.77  ?  417 LEU   A CG  1 
ATOM   1865 C  CD1 . LEU   A 1 261 ? -20.009 12.716  -11.397 1.00 32.33  ?  417 LEU   A CD1 1 
ATOM   1866 C  CD2 . LEU   A 1 261 ? -20.172 12.179  -8.993  1.00 40.60  ?  417 LEU   A CD2 1 
ATOM   1867 N  N   . GLU   A 1 262 ? -19.640 7.909   -11.348 1.00 33.98  ?  418 GLU   A N   1 
ATOM   1868 C  CA  . GLU   A 1 262 ? -18.407 7.150   -11.189 1.00 39.32  ?  418 GLU   A CA  1 
ATOM   1869 C  C   . GLU   A 1 262 ? -17.877 6.698   -12.543 1.00 34.95  ?  418 GLU   A C   1 
ATOM   1870 O  O   . GLU   A 1 262 ? -16.676 6.777   -12.809 1.00 35.91  ?  418 GLU   A O   1 
ATOM   1871 C  CB  . GLU   A 1 262 ? -18.651 5.946   -10.276 1.00 36.14  ?  418 GLU   A CB  1 
ATOM   1872 C  CG  . GLU   A 1 262 ? -18.825 6.329   -8.791  1.00 41.85  ?  418 GLU   A CG  1 
ATOM   1873 C  CD  . GLU   A 1 262 ? -19.310 5.157   -7.941  1.00 43.60  ?  418 GLU   A CD  1 
ATOM   1874 O  OE1 . GLU   A 1 262 ? -18.988 3.992   -8.294  1.00 45.29  ?  418 GLU   A OE1 1 
ATOM   1875 O  OE2 . GLU   A 1 262 ? -20.106 5.395   -6.997  1.00 37.13  -1 418 GLU   A OE2 1 
ATOM   1876 N  N   . GLN   A 1 263 ? -18.761 6.216   -13.410 1.00 35.78  ?  419 GLN   A N   1 
ATOM   1877 C  CA  . GLN   A 1 263 ? -18.324 5.796   -14.739 1.00 41.58  ?  419 GLN   A CA  1 
ATOM   1878 C  C   . GLN   A 1 263 ? -17.761 6.976   -15.532 1.00 36.93  ?  419 GLN   A C   1 
ATOM   1879 O  O   . GLN   A 1 263 ? -16.729 6.852   -16.200 1.00 37.66  ?  419 GLN   A O   1 
ATOM   1880 C  CB  . GLN   A 1 263 ? -19.495 5.138   -15.460 1.00 39.75  ?  419 GLN   A CB  1 
ATOM   1881 C  CG  . GLN   A 1 263 ? -19.873 3.808   -14.850 1.00 38.86  ?  419 GLN   A CG  1 
ATOM   1882 C  CD  . GLN   A 1 263 ? -18.869 2.741   -15.201 1.00 45.11  ?  419 GLN   A CD  1 
ATOM   1883 O  OE1 . GLN   A 1 263 ? -17.945 2.463   -14.444 1.00 45.36  ?  419 GLN   A OE1 1 
ATOM   1884 N  NE2 . GLN   A 1 263 ? -19.056 2.122   -16.365 1.00 51.68  ?  419 GLN   A NE2 1 
ATOM   1885 N  N   . LEU   A 1 264 ? -18.399 8.143   -15.428 1.00 36.97  ?  420 LEU   A N   1 
ATOM   1886 C  CA  . LEU   A 1 264 ? -17.898 9.319   -16.131 1.00 38.17  ?  420 LEU   A CA  1 
ATOM   1887 C  C   . LEU   A 1 264 ? -16.572 9.801   -15.556 1.00 41.53  ?  420 LEU   A C   1 
ATOM   1888 O  O   . LEU   A 1 264 ? -15.667 10.182  -16.311 1.00 39.44  ?  420 LEU   A O   1 
ATOM   1889 C  CB  . LEU   A 1 264 ? -18.940 10.435  -16.105 1.00 35.24  ?  420 LEU   A CB  1 
ATOM   1890 C  CG  . LEU   A 1 264 ? -20.183 10.173  -16.969 1.00 37.60  ?  420 LEU   A CG  1 
ATOM   1891 C  CD1 . LEU   A 1 264 ? -21.238 11.271  -16.724 1.00 40.94  ?  420 LEU   A CD1 1 
ATOM   1892 C  CD2 . LEU   A 1 264 ? -19.821 10.065  -18.457 1.00 35.32  ?  420 LEU   A CD2 1 
ATOM   1893 N  N   . LYS   A 1 265 ? -16.421 9.795   -14.228 1.00 39.92  ?  421 LYS   A N   1 
ATOM   1894 C  CA  . LYS   A 1 265 ? -15.132 10.209  -13.684 1.00 40.80  ?  421 LYS   A CA  1 
ATOM   1895 C  C   . LYS   A 1 265 ? -14.031 9.274   -14.149 1.00 41.89  ?  421 LYS   A C   1 
ATOM   1896 O  O   . LYS   A 1 265 ? -12.948 9.727   -14.538 1.00 40.09  ?  421 LYS   A O   1 
ATOM   1897 C  CB  . LYS   A 1 265 ? -15.160 10.286  -12.160 1.00 40.14  ?  421 LYS   A CB  1 
ATOM   1898 C  CG  . LYS   A 1 265 ? -15.927 11.487  -11.675 1.00 43.37  ?  421 LYS   A CG  1 
ATOM   1899 C  CD  . LYS   A 1 265 ? -15.881 11.623  -10.184 1.00 44.43  ?  421 LYS   A CD  1 
ATOM   1900 C  CE  . LYS   A 1 265 ? -14.473 12.038  -9.814  1.00 40.18  ?  421 LYS   A CE  1 
ATOM   1901 N  NZ  . LYS   A 1 265 ? -14.405 12.472  -8.430  1.00 50.69  ?  421 LYS   A NZ  1 
ATOM   1902 N  N   . GLU   A 1 266 ? -14.304 7.968   -14.151 1.00 40.77  ?  422 GLU   A N   1 
ATOM   1903 C  CA  . GLU   A 1 266 ? -13.332 7.022   -14.684 1.00 47.59  ?  422 GLU   A CA  1 
ATOM   1904 C  C   . GLU   A 1 266 ? -13.044 7.318   -16.153 1.00 49.31  ?  422 GLU   A C   1 
ATOM   1905 O  O   . GLU   A 1 266 ? -11.883 7.467   -16.549 1.00 48.92  ?  422 GLU   A O   1 
ATOM   1906 C  CB  . GLU   A 1 266 ? -13.843 5.591   -14.507 1.00 46.48  ?  422 GLU   A CB  1 
ATOM   1907 C  CG  . GLU   A 1 266 ? -12.785 4.488   -14.693 1.00 52.09  ?  422 GLU   A CG  1 
ATOM   1908 C  CD  . GLU   A 1 266 ? -11.514 4.710   -13.866 1.00 54.59  ?  422 GLU   A CD  1 
ATOM   1909 O  OE1 . GLU   A 1 266 ? -11.608 5.289   -12.762 1.00 57.07  ?  422 GLU   A OE1 1 
ATOM   1910 O  OE2 . GLU   A 1 266 ? -10.419 4.303   -14.320 1.00 62.59  -1 422 GLU   A OE2 1 
ATOM   1911 N  N   . ARG   A 1 267 ? -14.101 7.444   -16.970 1.00 49.56  ?  423 ARG   A N   1 
ATOM   1912 C  CA  . ARG   A 1 267 ? -13.924 7.668   -18.409 1.00 48.54  ?  423 ARG   A CA  1 
ATOM   1913 C  C   . ARG   A 1 267 ? -13.049 8.880   -18.703 1.00 47.85  ?  423 ARG   A C   1 
ATOM   1914 O  O   . ARG   A 1 267 ? -12.230 8.851   -19.627 1.00 48.03  ?  423 ARG   A O   1 
ATOM   1915 C  CB  . ARG   A 1 267 ? -15.280 7.820   -19.092 1.00 46.28  ?  423 ARG   A CB  1 
ATOM   1916 C  CG  . ARG   A 1 267 ? -15.167 8.106   -20.579 1.00 53.69  ?  423 ARG   A CG  1 
ATOM   1917 C  CD  . ARG   A 1 267 ? -16.277 7.439   -21.384 1.00 54.71  ?  423 ARG   A CD  1 
ATOM   1918 N  NE  . ARG   A 1 267 ? -15.912 6.088   -21.803 1.00 59.57  ?  423 ARG   A NE  1 
ATOM   1919 C  CZ  . ARG   A 1 267 ? -14.979 5.806   -22.707 1.00 62.00  ?  423 ARG   A CZ  1 
ATOM   1920 N  NH1 . ARG   A 1 267 ? -14.277 6.760   -23.305 1.00 66.98  ?  423 ARG   A NH1 1 
ATOM   1921 N  NH2 . ARG   A 1 267 ? -14.748 4.535   -23.030 1.00 63.65  ?  423 ARG   A NH2 1 
ATOM   1922 N  N   . PHE   A 1 268 ? -13.191 9.950   -17.928 1.00 50.19  ?  424 PHE   A N   1 
ATOM   1923 C  CA  . PHE   A 1 268 ? -12.432 11.172  -18.166 1.00 50.70  ?  424 PHE   A CA  1 
ATOM   1924 C  C   . PHE   A 1 268 ? -11.382 11.433  -17.092 1.00 54.14  ?  424 PHE   A C   1 
ATOM   1925 O  O   . PHE   A 1 268 ? -11.077 12.590  -16.792 1.00 60.75  ?  424 PHE   A O   1 
ATOM   1926 C  CB  . PHE   A 1 268 ? -13.384 12.357  -18.292 1.00 53.56  ?  424 PHE   A CB  1 
ATOM   1927 C  CG  . PHE   A 1 268 ? -14.314 12.254  -19.463 1.00 48.39  ?  424 PHE   A CG  1 
ATOM   1928 C  CD1 . PHE   A 1 268 ? -13.837 12.424  -20.754 1.00 50.24  ?  424 PHE   A CD1 1 
ATOM   1929 C  CD2 . PHE   A 1 268 ? -15.651 11.950  -19.281 1.00 51.80  ?  424 PHE   A CD2 1 
ATOM   1930 C  CE1 . PHE   A 1 268 ? -14.686 12.322  -21.839 1.00 49.68  ?  424 PHE   A CE1 1 
ATOM   1931 C  CE2 . PHE   A 1 268 ? -16.506 11.847  -20.363 1.00 46.72  ?  424 PHE   A CE2 1 
ATOM   1932 C  CZ  . PHE   A 1 268 ? -16.022 12.031  -21.640 1.00 48.72  ?  424 PHE   A CZ  1 
ATOM   1933 N  N   . LYS   A 1 269 ? -10.811 10.368  -16.517 1.00 51.31  ?  425 LYS   A N   1 
ATOM   1934 C  CA  . LYS   A 1 269 ? -9.793  10.524  -15.482 1.00 57.08  ?  425 LYS   A CA  1 
ATOM   1935 C  C   . LYS   A 1 269 ? -8.626  11.399  -15.929 1.00 60.48  ?  425 LYS   A C   1 
ATOM   1936 O  O   . LYS   A 1 269 ? -7.959  12.002  -15.081 1.00 60.36  ?  425 LYS   A O   1 
ATOM   1937 C  CB  . LYS   A 1 269 ? -9.278  9.149   -15.047 1.00 56.40  ?  425 LYS   A CB  1 
ATOM   1938 C  CG  . LYS   A 1 269 ? -8.057  8.670   -15.816 1.00 60.13  ?  425 LYS   A CG  1 
ATOM   1939 C  CD  . LYS   A 1 269 ? -7.636  7.280   -15.367 1.00 56.55  ?  425 LYS   A CD  1 
ATOM   1940 C  CE  . LYS   A 1 269 ? -8.710  6.242   -15.676 1.00 56.14  ?  425 LYS   A CE  1 
ATOM   1941 N  NZ  . LYS   A 1 269 ? -8.124  4.932   -16.094 1.00 59.43  ?  425 LYS   A NZ  1 
ATOM   1942 N  N   . ASP   A 1 270 ? -8.385  11.505  -17.235 1.00 62.30  ?  426 ASP   A N   1 
ATOM   1943 C  CA  . ASP   A 1 270 ? -7.246  12.245  -17.762 1.00 64.35  ?  426 ASP   A CA  1 
ATOM   1944 C  C   . ASP   A 1 270 ? -7.519  13.735  -17.913 1.00 63.65  ?  426 ASP   A C   1 
ATOM   1945 O  O   . ASP   A 1 270 ? -6.597  14.490  -18.239 1.00 65.74  ?  426 ASP   A O   1 
ATOM   1946 C  CB  . ASP   A 1 270 ? -6.840  11.668  -19.117 1.00 68.22  ?  426 ASP   A CB  1 
ATOM   1947 C  CG  . ASP   A 1 270 ? -6.350  10.241  -19.003 1.00 72.64  ?  426 ASP   A CG  1 
ATOM   1948 O  OD1 . ASP   A 1 270 ? -5.912  9.870   -17.888 1.00 75.12  ?  426 ASP   A OD1 1 
ATOM   1949 O  OD2 . ASP   A 1 270 ? -6.402  9.492   -20.013 1.00 74.18  -1 426 ASP   A OD2 1 
ATOM   1950 N  N   . LYS   A 1 271 ? -8.758  14.164  -17.723 1.00 62.77  ?  427 LYS   A N   1 
ATOM   1951 C  CA  . LYS   A 1 271 ? -9.114  15.571  -17.720 1.00 60.69  ?  427 LYS   A CA  1 
ATOM   1952 C  C   . LYS   A 1 271 ? -9.243  16.039  -16.277 1.00 63.67  ?  427 LYS   A C   1 
ATOM   1953 O  O   . LYS   A 1 271 ? -9.534  15.246  -15.378 1.00 66.34  ?  427 LYS   A O   1 
ATOM   1954 C  CB  . LYS   A 1 271 ? -10.429 15.793  -18.465 1.00 64.88  ?  427 LYS   A CB  1 
ATOM   1955 C  CG  . LYS   A 1 271 ? -10.339 15.522  -19.962 1.00 69.83  ?  427 LYS   A CG  1 
ATOM   1956 C  CD  . LYS   A 1 271 ? -11.672 15.757  -20.630 1.00 59.17  ?  427 LYS   A CD  1 
ATOM   1957 C  CE  . LYS   A 1 271 ? -11.561 15.605  -22.118 1.00 65.14  ?  427 LYS   A CE  1 
ATOM   1958 N  NZ  . LYS   A 1 271 ? -10.865 16.787  -22.682 1.00 69.52  ?  427 LYS   A NZ  1 
ATOM   1959 N  N   . LYS   A 1 272 ? -8.997  17.329  -16.055 1.00 65.65  ?  428 LYS   A N   1 
ATOM   1960 C  CA  . LYS   A 1 272 ? -9.259  17.917  -14.748 1.00 60.06  ?  428 LYS   A CA  1 
ATOM   1961 C  C   . LYS   A 1 272 ? -10.730 18.259  -14.540 1.00 57.22  ?  428 LYS   A C   1 
ATOM   1962 O  O   . LYS   A 1 272 ? -11.106 18.641  -13.424 1.00 59.94  ?  428 LYS   A O   1 
ATOM   1963 C  CB  . LYS   A 1 272 ? -8.396  19.168  -14.547 1.00 57.44  ?  428 LYS   A CB  1 
ATOM   1964 C  CG  . LYS   A 1 272 ? -6.892  18.900  -14.478 1.00 64.05  ?  428 LYS   A CG  1 
ATOM   1965 C  CD  . LYS   A 1 272 ? -6.531  18.049  -13.250 1.00 65.49  ?  428 LYS   A CD  1 
ATOM   1966 C  CE  . LYS   A 1 272 ? -6.779  18.814  -11.947 1.00 63.95  ?  428 LYS   A CE  1 
ATOM   1967 N  NZ  . LYS   A 1 272 ? -6.549  17.984  -10.716 1.00 66.45  ?  428 LYS   A NZ  1 
ATOM   1968 N  N   . HIS   A 1 273 ? -11.570 18.086  -15.568 1.00 51.02  ?  429 HIS   A N   1 
ATOM   1969 C  CA  . HIS   A 1 273 ? -12.912 18.660  -15.555 1.00 49.31  ?  429 HIS   A CA  1 
ATOM   1970 C  C   . HIS   A 1 273 ? -13.834 18.008  -14.531 1.00 48.40  ?  429 HIS   A C   1 
ATOM   1971 O  O   . HIS   A 1 273 ? -14.750 18.667  -14.024 1.00 45.83  ?  429 HIS   A O   1 
ATOM   1972 C  CB  . HIS   A 1 273 ? -13.546 18.549  -16.943 1.00 51.03  ?  429 HIS   A CB  1 
ATOM   1973 C  CG  . HIS   A 1 273 ? -12.982 19.508  -17.944 1.00 50.28  ?  429 HIS   A CG  1 
ATOM   1974 N  ND1 . HIS   A 1 273 ? -11.646 19.534  -18.279 1.00 60.08  ?  429 HIS   A ND1 1 
ATOM   1975 C  CD2 . HIS   A 1 273 ? -13.573 20.480  -18.676 1.00 49.58  ?  429 HIS   A CD2 1 
ATOM   1976 C  CE1 . HIS   A 1 273 ? -11.436 20.484  -19.173 1.00 53.63  ?  429 HIS   A CE1 1 
ATOM   1977 N  NE2 . HIS   A 1 273 ? -12.590 21.071  -19.432 1.00 60.15  ?  429 HIS   A NE2 1 
ATOM   1978 N  N   . LEU   A 1 274 ? -13.658 16.719  -14.249 1.00 43.43  ?  430 LEU   A N   1 
ATOM   1979 C  CA  . LEU   A 1 274 ? -14.582 16.024  -13.361 1.00 45.47  ?  430 LEU   A CA  1 
ATOM   1980 C  C   . LEU   A 1 274 ? -13.976 15.714  -11.995 1.00 44.02  ?  430 LEU   A C   1 
ATOM   1981 O  O   . LEU   A 1 274 ? -14.611 15.019  -11.194 1.00 42.56  ?  430 LEU   A O   1 
ATOM   1982 C  CB  . LEU   A 1 274 ? -15.080 14.734  -14.012 1.00 43.76  ?  430 LEU   A CB  1 
ATOM   1983 C  CG  . LEU   A 1 274 ? -15.775 14.856  -15.371 1.00 40.42  ?  430 LEU   A CG  1 
ATOM   1984 C  CD1 . LEU   A 1 274 ? -16.304 13.489  -15.764 1.00 41.43  ?  430 LEU   A CD1 1 
ATOM   1985 C  CD2 . LEU   A 1 274 ? -16.892 15.882  -15.324 1.00 36.30  ?  430 LEU   A CD2 1 
ATOM   1986 N  N   . ASP   A 1 275 ? -12.786 16.243  -11.697 1.00 45.08  ?  431 ASP   A N   1 
ATOM   1987 C  CA  . ASP   A 1 275 ? -12.086 15.847  -10.477 1.00 48.26  ?  431 ASP   A CA  1 
ATOM   1988 C  C   . ASP   A 1 275 ? -12.793 16.317  -9.216  1.00 48.69  ?  431 ASP   A C   1 
ATOM   1989 O  O   . ASP   A 1 275 ? -12.700 15.651  -8.177  1.00 48.42  ?  431 ASP   A O   1 
ATOM   1990 C  CB  . ASP   A 1 275 ? -10.665 16.390  -10.479 1.00 45.97  ?  431 ASP   A CB  1 
ATOM   1991 C  CG  . ASP   A 1 275 ? -9.814  15.767  -11.544 1.00 55.24  ?  431 ASP   A CG  1 
ATOM   1992 O  OD1 . ASP   A 1 275 ? -10.257 14.769  -12.154 1.00 59.67  ?  431 ASP   A OD1 1 
ATOM   1993 O  OD2 . ASP   A 1 275 ? -8.690  16.259  -11.756 1.00 59.72  -1 431 ASP   A OD2 1 
ATOM   1994 N  N   . LYS   A 1 276 ? -13.462 17.465  -9.265  1.00 37.64  ?  432 LYS   A N   1 
ATOM   1995 C  CA  . LYS   A 1 276 ? -14.073 18.042  -8.075  1.00 39.37  ?  432 LYS   A CA  1 
ATOM   1996 C  C   . LYS   A 1 276 ? -15.490 17.542  -7.827  1.00 44.34  ?  432 LYS   A C   1 
ATOM   1997 O  O   . LYS   A 1 276 ? -16.097 17.930  -6.825  1.00 42.99  ?  432 LYS   A O   1 
ATOM   1998 C  CB  . LYS   A 1 276 ? -14.065 19.569  -8.173  1.00 43.90  ?  432 LYS   A CB  1 
ATOM   1999 C  CG  . LYS   A 1 276 ? -12.644 20.155  -8.158  1.00 50.52  ?  432 LYS   A CG  1 
ATOM   2000 C  CD  . LYS   A 1 276 ? -12.653 21.674  -8.200  1.00 50.55  ?  432 LYS   A CD  1 
ATOM   2001 C  CE  . LYS   A 1 276 ? -11.270 22.259  -7.956  1.00 48.88  ?  432 LYS   A CE  1 
ATOM   2002 N  NZ  . LYS   A 1 276 ? -11.328 23.741  -8.015  1.00 56.40  ?  432 LYS   A NZ  1 
ATOM   2003 N  N   . PHE   A 1 277 ? -16.044 16.700  -8.707  1.00 41.09  ?  433 PHE   A N   1 
ATOM   2004 C  CA  . PHE   A 1 277 ? -17.368 16.134  -8.480  1.00 36.88  ?  433 PHE   A CA  1 
ATOM   2005 C  C   . PHE   A 1 277 ? -17.227 14.845  -7.672  1.00 40.18  ?  433 PHE   A C   1 
ATOM   2006 O  O   . PHE   A 1 277 ? -16.276 14.081  -7.864  1.00 37.04  ?  433 PHE   A O   1 
ATOM   2007 C  CB  . PHE   A 1 277 ? -18.079 15.876  -9.818  1.00 33.50  ?  433 PHE   A CB  1 
ATOM   2008 C  CG  . PHE   A 1 277 ? -18.336 17.141  -10.610 1.00 33.37  ?  433 PHE   A CG  1 
ATOM   2009 C  CD1 . PHE   A 1 277 ? -19.362 18.007  -10.259 1.00 32.76  ?  433 PHE   A CD1 1 
ATOM   2010 C  CD2 . PHE   A 1 277 ? -17.527 17.468  -11.699 1.00 34.76  ?  433 PHE   A CD2 1 
ATOM   2011 C  CE1 . PHE   A 1 277 ? -19.579 19.181  -10.971 1.00 37.69  ?  433 PHE   A CE1 1 
ATOM   2012 C  CE2 . PHE   A 1 277 ? -17.732 18.634  -12.420 1.00 34.04  ?  433 PHE   A CE2 1 
ATOM   2013 C  CZ  . PHE   A 1 277 ? -18.757 19.498  -12.061 1.00 34.42  ?  433 PHE   A CZ  1 
ATOM   2014 N  N   . SER   A 1 278 ? -18.159 14.617  -6.740  1.00 38.34  ?  434 SER   A N   1 
ATOM   2015 C  CA  . SER   A 1 278 ? -18.120 13.416  -5.915  1.00 37.46  ?  434 SER   A CA  1 
ATOM   2016 C  C   . SER   A 1 278 ? -19.526 12.887  -5.683  1.00 32.14  ?  434 SER   A C   1 
ATOM   2017 O  O   . SER   A 1 278 ? -20.529 13.535  -6.007  1.00 31.18  ?  434 SER   A O   1 
ATOM   2018 C  CB  . SER   A 1 278 ? -17.447 13.676  -4.546  1.00 39.41  ?  434 SER   A CB  1 
ATOM   2019 O  OG  . SER   A 1 278 ? -18.331 14.381  -3.684  1.00 36.48  ?  434 SER   A OG  1 
ATOM   2020 N  N   . SER   A 1 279 ? -19.592 11.699  -5.066  1.00 33.27  ?  435 SER   A N   1 
ATOM   2021 C  CA  . SER   A 1 279 ? -20.883 11.113  -4.715  1.00 34.43  ?  435 SER   A CA  1 
ATOM   2022 C  C   . SER   A 1 279 ? -21.689 12.005  -3.780  1.00 30.51  ?  435 SER   A C   1 
ATOM   2023 O  O   . SER   A 1 279 ? -22.912 11.844  -3.689  1.00 30.35  ?  435 SER   A O   1 
ATOM   2024 C  CB  . SER   A 1 279 ? -20.702 9.770   -4.020  1.00 35.48  ?  435 SER   A CB  1 
ATOM   2025 O  OG  . SER   A 1 279 ? -20.183 10.017  -2.727  1.00 35.55  ?  435 SER   A OG  1 
ATOM   2026 N  N   . TYR   A 1 280 ? -21.038 12.923  -3.063  1.00 32.19  ?  436 TYR   A N   1 
ATOM   2027 C  CA  . TYR   A 1 280 ? -21.790 13.806  -2.174  1.00 33.16  ?  436 TYR   A CA  1 
ATOM   2028 C  C   . TYR   A 1 280 ? -22.669 14.779  -2.970  1.00 30.13  ?  436 TYR   A C   1 
ATOM   2029 O  O   . TYR   A 1 280 ? -23.803 15.075  -2.566  1.00 27.69  ?  436 TYR   A O   1 
ATOM   2030 C  CB  . TYR   A 1 280 ? -20.831 14.554  -1.248  1.00 31.69  ?  436 TYR   A CB  1 
ATOM   2031 C  CG  . TYR   A 1 280 ? -21.534 15.263  -0.118  1.00 32.49  ?  436 TYR   A CG  1 
ATOM   2032 C  CD1 . TYR   A 1 280 ? -22.060 14.548  0.959   1.00 38.39  ?  436 TYR   A CD1 1 
ATOM   2033 C  CD2 . TYR   A 1 280 ? -21.673 16.645  -0.126  1.00 30.23  ?  436 TYR   A CD2 1 
ATOM   2034 C  CE1 . TYR   A 1 280 ? -22.714 15.196  2.002   1.00 31.24  ?  436 TYR   A CE1 1 
ATOM   2035 C  CE2 . TYR   A 1 280 ? -22.329 17.301  0.900   1.00 34.82  ?  436 TYR   A CE2 1 
ATOM   2036 C  CZ  . TYR   A 1 280 ? -22.844 16.569  1.966   1.00 31.83  ?  436 TYR   A CZ  1 
ATOM   2037 O  OH  . TYR   A 1 280 ? -23.494 17.227  2.995   1.00 34.25  ?  436 TYR   A OH  1 
ATOM   2038 N  N   . HIS   A 1 281 ? -22.171 15.275  -4.108  1.00 29.14  ?  437 HIS   A N   1 
ATOM   2039 C  CA  . HIS   A 1 281 ? -23.004 16.108  -4.991  1.00 30.49  ?  437 HIS   A CA  1 
ATOM   2040 C  C   . HIS   A 1 281 ? -24.235 15.345  -5.465  1.00 27.24  ?  437 HIS   A C   1 
ATOM   2041 O  O   . HIS   A 1 281 ? -25.367 15.839  -5.373  1.00 28.37  ?  437 HIS   A O   1 
ATOM   2042 C  CB  . HIS   A 1 281 ? -22.164 16.571  -6.183  1.00 28.69  ?  437 HIS   A CB  1 
ATOM   2043 C  CG  . HIS   A 1 281 ? -21.005 17.418  -5.774  1.00 29.17  ?  437 HIS   A CG  1 
ATOM   2044 N  ND1 . HIS   A 1 281 ? -19.707 17.115  -6.129  1.00 31.18  ?  437 HIS   A ND1 1 
ATOM   2045 C  CD2 . HIS   A 1 281 ? -20.943 18.555  -5.044  1.00 27.81  ?  437 HIS   A CD2 1 
ATOM   2046 C  CE1 . HIS   A 1 281 ? -18.893 18.012  -5.602  1.00 33.77  ?  437 HIS   A CE1 1 
ATOM   2047 N  NE2 . HIS   A 1 281 ? -19.618 18.897  -4.943  1.00 36.72  ?  437 HIS   A NE2 1 
ATOM   2048 N  N   . VAL   A 1 282 ? -24.029 14.126  -5.977  1.00 28.19  ?  438 VAL   A N   1 
ATOM   2049 C  CA  . VAL   A 1 282 ? -25.140 13.309  -6.450  1.00 27.82  ?  438 VAL   A CA  1 
ATOM   2050 C  C   . VAL   A 1 282 ? -26.132 13.035  -5.318  1.00 32.93  ?  438 VAL   A C   1 
ATOM   2051 O  O   . VAL   A 1 282 ? -27.353 13.191  -5.478  1.00 26.01  ?  438 VAL   A O   1 
ATOM   2052 C  CB  . VAL   A 1 282 ? -24.579 12.009  -7.066  1.00 34.37  ?  438 VAL   A CB  1 
ATOM   2053 C  CG1 . VAL   A 1 282 ? -25.617 10.972  -7.107  1.00 38.33  ?  438 VAL   A CG1 1 
ATOM   2054 C  CG2 . VAL   A 1 282 ? -24.085 12.287  -8.481  1.00 35.85  ?  438 VAL   A CG2 1 
ATOM   2055 N  N   . LYS   A 1 283 ? -25.618 12.664  -4.140  1.00 28.89  ?  439 LYS   A N   1 
ATOM   2056 C  CA  . LYS   A 1 283 ? -26.499 12.335  -3.029  1.00 28.67  ?  439 LYS   A CA  1 
ATOM   2057 C  C   . LYS   A 1 283 ? -27.251 13.574  -2.556  1.00 25.40  ?  439 LYS   A C   1 
ATOM   2058 O  O   . LYS   A 1 283 ? -28.463 13.520  -2.319  1.00 29.21  ?  439 LYS   A O   1 
ATOM   2059 C  CB  . LYS   A 1 283 ? -25.657 11.706  -1.896  1.00 27.66  ?  439 LYS   A CB  1 
ATOM   2060 C  CG  . LYS   A 1 283 ? -26.435 11.077  -0.770  1.00 38.36  ?  439 LYS   A CG  1 
ATOM   2061 C  CD  . LYS   A 1 283 ? -25.551 10.030  0.015   1.00 40.01  ?  439 LYS   A CD  1 
ATOM   2062 C  CE  . LYS   A 1 283 ? -24.238 10.645  0.528   1.00 48.12  ?  439 LYS   A CE  1 
ATOM   2063 N  NZ  . LYS   A 1 283 ? -24.132 10.752  2.059   1.00 49.81  ?  439 LYS   A NZ  1 
ATOM   2064 N  N   . THR   A 1 284 ? -26.560 14.713  -2.455  1.00 26.06  ?  440 THR   A N   1 
ATOM   2065 C  CA  . THR   A 1 284 ? -27.255 15.950  -2.114  1.00 26.80  ?  440 THR   A CA  1 
ATOM   2066 C  C   . THR   A 1 284 ? -28.365 16.249  -3.127  1.00 27.44  ?  440 THR   A C   1 
ATOM   2067 O  O   . THR   A 1 284 ? -29.512 16.515  -2.744  1.00 27.15  ?  440 THR   A O   1 
ATOM   2068 C  CB  . THR   A 1 284 ? -26.267 17.116  -2.006  1.00 31.90  ?  440 THR   A CB  1 
ATOM   2069 O  OG1 . THR   A 1 284 ? -25.259 16.805  -1.027  1.00 31.43  ?  440 THR   A OG1 1 
ATOM   2070 C  CG2 . THR   A 1 284 ? -26.991 18.379  -1.550  1.00 28.70  ?  440 THR   A CG2 1 
ATOM   2071 N  N   . ALA   A 1 285 ? -28.045 16.188  -4.432  1.00 27.14  ?  441 ALA   A N   1 
ATOM   2072 C  CA  . ALA   A 1 285 ? -29.070 16.403  -5.462  1.00 30.27  ?  441 ALA   A CA  1 
ATOM   2073 C  C   . ALA   A 1 285 ? -30.267 15.484  -5.234  1.00 25.72  ?  441 ALA   A C   1 
ATOM   2074 O  O   . ALA   A 1 285 ? -31.428 15.910  -5.308  1.00 28.08  ?  441 ALA   A O   1 
ATOM   2075 C  CB  . ALA   A 1 285 ? -28.475 16.158  -6.859  1.00 24.20  ?  441 ALA   A CB  1 
ATOM   2076 N  N   . PHE   A 1 286 ? -29.987 14.214  -4.947  1.00 24.11  ?  442 PHE   A N   1 
ATOM   2077 C  CA  . PHE   A 1 286 ? -31.041 13.232  -4.746  1.00 24.52  ?  442 PHE   A CA  1 
ATOM   2078 C  C   . PHE   A 1 286 ? -31.955 13.621  -3.594  1.00 26.80  ?  442 PHE   A C   1 
ATOM   2079 O  O   . PHE   A 1 286 ? -33.183 13.551  -3.724  1.00 22.24  ?  442 PHE   A O   1 
ATOM   2080 C  CB  . PHE   A 1 286 ? -30.427 11.854  -4.493  1.00 24.28  ?  442 PHE   A CB  1 
ATOM   2081 C  CG  . PHE   A 1 286 ? -31.434 10.801  -4.082  1.00 27.11  ?  442 PHE   A CG  1 
ATOM   2082 C  CD1 . PHE   A 1 286 ? -32.220 10.160  -5.024  1.00 34.90  ?  442 PHE   A CD1 1 
ATOM   2083 C  CD2 . PHE   A 1 286 ? -31.594 10.463  -2.738  1.00 33.97  ?  442 PHE   A CD2 1 
ATOM   2084 C  CE1 . PHE   A 1 286 ? -33.153 9.183   -4.644  1.00 33.23  ?  442 PHE   A CE1 1 
ATOM   2085 C  CE2 . PHE   A 1 286 ? -32.510 9.495   -2.352  1.00 36.41  ?  442 PHE   A CE2 1 
ATOM   2086 C  CZ  . PHE   A 1 286 ? -33.300 8.860   -3.320  1.00 36.19  ?  442 PHE   A CZ  1 
ATOM   2087 N  N   . PHE   A 1 287 ? -31.379 13.979  -2.419  1.00 25.45  ?  443 PHE   A N   1 
ATOM   2088 C  CA  . PHE   A 1 287 ? -32.249 14.328  -1.295  1.00 24.37  ?  443 PHE   A CA  1 
ATOM   2089 C  C   . PHE   A 1 287 ? -33.143 15.513  -1.635  1.00 26.06  ?  443 PHE   A C   1 
ATOM   2090 O  O   . PHE   A 1 287 ? -34.302 15.569  -1.200  1.00 21.29  ?  443 PHE   A O   1 
ATOM   2091 C  CB  . PHE   A 1 287 ? -31.433 14.618  -0.026  1.00 23.52  ?  443 PHE   A CB  1 
ATOM   2092 C  CG  . PHE   A 1 287 ? -30.781 13.389  0.539   1.00 31.42  ?  443 PHE   A CG  1 
ATOM   2093 C  CD1 . PHE   A 1 287 ? -31.481 12.198  0.601   1.00 27.52  ?  443 PHE   A CD1 1 
ATOM   2094 C  CD2 . PHE   A 1 287 ? -29.470 13.413  0.981   1.00 34.14  ?  443 PHE   A CD2 1 
ATOM   2095 C  CE1 . PHE   A 1 287 ? -30.884 11.042  1.124   1.00 32.26  ?  443 PHE   A CE1 1 
ATOM   2096 C  CE2 . PHE   A 1 287 ? -28.873 12.270  1.500   1.00 35.49  ?  443 PHE   A CE2 1 
ATOM   2097 C  CZ  . PHE   A 1 287 ? -29.581 11.089  1.578   1.00 35.22  ?  443 PHE   A CZ  1 
ATOM   2098 N  N   . HIS   A 1 288 ? -32.615 16.486  -2.383  1.00 24.60  ?  444 HIS   A N   1 
ATOM   2099 C  CA  . HIS   A 1 288 ? -33.468 17.583  -2.848  1.00 27.06  ?  444 HIS   A CA  1 
ATOM   2100 C  C   . HIS   A 1 288 ? -34.626 17.067  -3.698  1.00 27.44  ?  444 HIS   A C   1 
ATOM   2101 O  O   . HIS   A 1 288 ? -35.762 17.557  -3.594  1.00 28.47  ?  444 HIS   A O   1 
ATOM   2102 C  CB  . HIS   A 1 288 ? -32.644 18.628  -3.612  1.00 27.71  ?  444 HIS   A CB  1 
ATOM   2103 C  CG  . HIS   A 1 288 ? -31.788 19.497  -2.731  1.00 33.45  ?  444 HIS   A CG  1 
ATOM   2104 N  ND1 . HIS   A 1 288 ? -32.318 20.293  -1.733  1.00 29.80  ?  444 HIS   A ND1 1 
ATOM   2105 C  CD2 . HIS   A 1 288 ? -30.448 19.700  -2.699  1.00 27.56  ?  444 HIS   A CD2 1 
ATOM   2106 C  CE1 . HIS   A 1 288 ? -31.341 20.960  -1.138  1.00 28.21  ?  444 HIS   A CE1 1 
ATOM   2107 N  NE2 . HIS   A 1 288 ? -30.197 20.620  -1.704  1.00 30.26  ?  444 HIS   A NE2 1 
ATOM   2108 N  N   . VAL   A 1 289 ? -34.375 16.049  -4.520  1.00 26.30  ?  445 VAL   A N   1 
ATOM   2109 C  CA  . VAL   A 1 289 ? -35.470 15.494  -5.318  1.00 26.45  ?  445 VAL   A CA  1 
ATOM   2110 C  C   . VAL   A 1 289 ? -36.480 14.784  -4.423  1.00 26.08  ?  445 VAL   A C   1 
ATOM   2111 O  O   . VAL   A 1 289 ? -37.691 14.864  -4.655  1.00 28.05  ?  445 VAL   A O   1 
ATOM   2112 C  CB  . VAL   A 1 289 ? -34.917 14.560  -6.407  1.00 25.62  ?  445 VAL   A CB  1 
ATOM   2113 C  CG1 . VAL   A 1 289 ? -36.080 13.894  -7.171  1.00 25.72  ?  445 VAL   A CG1 1 
ATOM   2114 C  CG2 . VAL   A 1 289 ? -34.002 15.363  -7.345  1.00 25.91  ?  445 VAL   A CG2 1 
ATOM   2115 N  N   . CYS   A 1 290 ? -36.007 14.091  -3.379  1.00 25.01  ?  446 CYS   A N   1 
ATOM   2116 C  CA  . CYS   A 1 290 ? -36.942 13.503  -2.416  1.00 25.35  ?  446 CYS   A CA  1 
ATOM   2117 C  C   . CYS   A 1 290 ? -37.831 14.563  -1.788  1.00 24.68  ?  446 CYS   A C   1 
ATOM   2118 O  O   . CYS   A 1 290 ? -39.028 14.333  -1.559  1.00 26.52  ?  446 CYS   A O   1 
ATOM   2119 C  CB  . CYS   A 1 290 ? -36.183 12.756  -1.316  1.00 22.73  ?  446 CYS   A CB  1 
ATOM   2120 S  SG  . CYS   A 1 290 ? -35.456 11.198  -1.861  1.00 30.01  ?  446 CYS   A SG  1 
ATOM   2121 N  N   . THR   A 1 291 ? -37.257 15.728  -1.490  1.00 23.96  ?  447 THR   A N   1 
ATOM   2122 C  CA  . THR   A 1 291 ? -38.046 16.823  -0.940  1.00 23.68  ?  447 THR   A CA  1 
ATOM   2123 C  C   . THR   A 1 291 ? -39.067 17.338  -1.949  1.00 30.48  ?  447 THR   A C   1 
ATOM   2124 O  O   . THR   A 1 291 ? -40.223 17.595  -1.598  1.00 24.18  ?  447 THR   A O   1 
ATOM   2125 C  CB  . THR   A 1 291 ? -37.130 17.952  -0.501  1.00 30.15  ?  447 THR   A CB  1 
ATOM   2126 O  OG1 . THR   A 1 291 ? -36.321 17.496  0.601   1.00 31.73  ?  447 THR   A OG1 1 
ATOM   2127 C  CG2 . THR   A 1 291 ? -37.950 19.188  -0.139  1.00 29.36  ?  447 THR   A CG2 1 
ATOM   2128 N  N   . GLN   A 1 292 ? -38.647 17.523  -3.203  1.00 33.34  ?  448 GLN   A N   1 
ATOM   2129 C  CA  . GLN   A 1 292 ? -39.574 18.002  -4.227  1.00 36.94  ?  448 GLN   A CA  1 
ATOM   2130 C  C   . GLN   A 1 292 ? -40.657 16.982  -4.543  1.00 26.48  ?  448 GLN   A C   1 
ATOM   2131 O  O   . GLN   A 1 292 ? -41.739 17.371  -4.989  1.00 31.54  ?  448 GLN   A O   1 
ATOM   2132 C  CB  . GLN   A 1 292 ? -38.825 18.360  -5.508  1.00 37.45  ?  448 GLN   A CB  1 
ATOM   2133 C  CG  . GLN   A 1 292 ? -37.886 19.527  -5.372  1.00 39.37  ?  448 GLN   A CG  1 
ATOM   2134 C  CD  . GLN   A 1 292 ? -37.569 20.167  -6.714  1.00 58.75  ?  448 GLN   A CD  1 
ATOM   2135 O  OE1 . GLN   A 1 292 ? -37.510 19.484  -7.755  1.00 60.25  ?  448 GLN   A OE1 1 
ATOM   2136 N  NE2 . GLN   A 1 292 ? -37.382 21.490  -6.709  1.00 56.53  ?  448 GLN   A NE2 1 
ATOM   2137 N  N   . ASN   A 1 293 ? -40.408 15.695  -4.297  1.00 28.23  ?  449 ASN   A N   1 
ATOM   2138 C  CA  . ASN   A 1 293 ? -41.347 14.631  -4.642  1.00 28.49  ?  449 ASN   A CA  1 
ATOM   2139 C  C   . ASN   A 1 293 ? -41.584 13.773  -3.403  1.00 27.60  ?  449 ASN   A C   1 
ATOM   2140 O  O   . ASN   A 1 293 ? -41.085 12.637  -3.313  1.00 24.47  ?  449 ASN   A O   1 
ATOM   2141 C  CB  . ASN   A 1 293 ? -40.825 13.800  -5.822  1.00 26.36  ?  449 ASN   A CB  1 
ATOM   2142 C  CG  . ASN   A 1 293 ? -40.572 14.663  -7.060  1.00 32.54  ?  449 ASN   A CG  1 
ATOM   2143 O  OD1 . ASN   A 1 293 ? -41.495 15.015  -7.765  1.00 28.26  ?  449 ASN   A OD1 1 
ATOM   2144 N  ND2 . ASN   A 1 293 ? -39.314 15.008  -7.306  1.00 33.37  ?  449 ASN   A ND2 1 
ATOM   2145 N  N   . PRO   A 1 294 ? -42.378 14.273  -2.443  1.00 23.94  ?  450 PRO   A N   1 
ATOM   2146 C  CA  . PRO   A 1 294 ? -42.509 13.576  -1.140  1.00 29.33  ?  450 PRO   A CA  1 
ATOM   2147 C  C   . PRO   A 1 294 ? -43.425 12.360  -1.114  1.00 30.68  ?  450 PRO   A C   1 
ATOM   2148 O  O   . PRO   A 1 294 ? -43.299 11.564  -0.175  1.00 29.88  ?  450 PRO   A O   1 
ATOM   2149 C  CB  . PRO   A 1 294 ? -43.053 14.669  -0.204  1.00 29.53  ?  450 PRO   A CB  1 
ATOM   2150 C  CG  . PRO   A 1 294 ? -43.827 15.611  -1.174  1.00 31.31  ?  450 PRO   A CG  1 
ATOM   2151 C  CD  . PRO   A 1 294 ? -42.984 15.615  -2.428  1.00 25.35  ?  450 PRO   A CD  1 
ATOM   2152 N  N   . GLN   A 1 295 ? -44.353 12.192  -2.060  1.00 29.69  ?  451 GLN   A N   1 
ATOM   2153 C  CA  . GLN   A 1 295 ? -45.285 11.076  -1.986  1.00 25.34  ?  451 GLN   A CA  1 
ATOM   2154 C  C   . GLN   A 1 295 ? -44.662 9.797   -2.537  1.00 25.79  ?  451 GLN   A C   1 
ATOM   2155 O  O   . GLN   A 1 295 ? -43.967 9.804   -3.560  1.00 25.95  ?  451 GLN   A O   1 
ATOM   2156 C  CB  . GLN   A 1 295 ? -46.585 11.374  -2.749  1.00 29.78  ?  451 GLN   A CB  1 
ATOM   2157 C  CG  . GLN   A 1 295 ? -47.374 12.606  -2.301  1.00 34.41  ?  451 GLN   A CG  1 
ATOM   2158 C  CD  . GLN   A 1 295 ? -47.766 12.591  -0.809  1.00 37.50  ?  451 GLN   A CD  1 
ATOM   2159 O  OE1 . GLN   A 1 295 ? -48.125 11.544  -0.251  1.00 41.03  ?  451 GLN   A OE1 1 
ATOM   2160 N  NE2 . GLN   A 1 295 ? -47.819 13.778  -0.205  1.00 36.27  ?  451 GLN   A NE2 1 
ATOM   2161 N  N   . ASP   A 1 296 ? -44.935 8.684   -1.856  1.00 24.92  ?  452 ASP   A N   1 
ATOM   2162 C  CA  . ASP   A 1 296 ? -44.369 7.416   -2.297  1.00 25.85  ?  452 ASP   A CA  1 
ATOM   2163 C  C   . ASP   A 1 296 ? -44.874 7.038   -3.695  1.00 29.04  ?  452 ASP   A C   1 
ATOM   2164 O  O   . ASP   A 1 296 ? -44.162 6.370   -4.457  1.00 25.90  ?  452 ASP   A O   1 
ATOM   2165 C  CB  . ASP   A 1 296 ? -44.739 6.324   -1.306  1.00 25.13  ?  452 ASP   A CB  1 
ATOM   2166 C  CG  . ASP   A 1 296 ? -44.043 6.496   0.067   1.00 27.23  ?  452 ASP   A CG  1 
ATOM   2167 O  OD1 . ASP   A 1 296 ? -43.105 7.314   0.206   1.00 26.65  ?  452 ASP   A OD1 1 
ATOM   2168 O  OD2 . ASP   A 1 296 ? -44.518 5.851   1.013   1.00 27.40  -1 452 ASP   A OD2 1 
ATOM   2169 N  N   . SER   A 1 297 ? -46.097 7.447   -4.039  1.00 26.40  ?  453 SER   A N   1 
ATOM   2170 C  CA  . SER   A 1 297 ? -46.625 7.137   -5.370  1.00 28.90  ?  453 SER   A CA  1 
ATOM   2171 C  C   . SER   A 1 297 ? -45.839 7.828   -6.477  1.00 33.77  ?  453 SER   A C   1 
ATOM   2172 O  O   . SER   A 1 297 ? -45.990 7.460   -7.644  1.00 33.10  ?  453 SER   A O   1 
ATOM   2173 C  CB  . SER   A 1 297 ? -48.091 7.542   -5.470  1.00 28.34  ?  453 SER   A CB  1 
ATOM   2174 O  OG  . SER   A 1 297 ? -48.209 8.958   -5.311  1.00 29.44  ?  453 SER   A OG  1 
ATOM   2175 N  N   . GLN   A 1 298 ? -45.014 8.826   -6.151  1.00 27.69  ?  454 GLN   A N   1 
ATOM   2176 C  CA  . GLN   A 1 298 ? -44.183 9.449   -7.172  1.00 27.96  ?  454 GLN   A CA  1 
ATOM   2177 C  C   . GLN   A 1 298 ? -42.922 8.658   -7.429  1.00 27.75  ?  454 GLN   A C   1 
ATOM   2178 O  O   . GLN   A 1 298 ? -42.100 9.078   -8.251  1.00 32.16  ?  454 GLN   A O   1 
ATOM   2179 C  CB  . GLN   A 1 298 ? -43.826 10.892  -6.782  1.00 27.86  ?  454 GLN   A CB  1 
ATOM   2180 C  CG  . GLN   A 1 298 ? -45.048 11.804  -6.719  1.00 32.80  ?  454 GLN   A CG  1 
ATOM   2181 C  CD  . GLN   A 1 298 ? -44.750 13.162  -6.102  1.00 38.42  ?  454 GLN   A CD  1 
ATOM   2182 O  OE1 . GLN   A 1 298 ? -44.456 13.263  -4.904  1.00 33.66  ?  454 GLN   A OE1 1 
ATOM   2183 N  NE2 . GLN   A 1 298 ? -44.850 14.220  -6.914  1.00 32.24  ?  454 GLN   A NE2 1 
ATOM   2184 N  N   . TRP   A 1 299 ? -42.748 7.530   -6.743  1.00 27.02  ?  455 TRP   A N   1 
ATOM   2185 C  CA  . TRP   A 1 299 ? -41.540 6.732   -6.858  1.00 26.56  ?  455 TRP   A CA  1 
ATOM   2186 C  C   . TRP   A 1 299 ? -41.868 5.274   -7.124  1.00 32.32  ?  455 TRP   A C   1 
ATOM   2187 O  O   . TRP   A 1 299 ? -41.078 4.393   -6.770  1.00 30.00  ?  455 TRP   A O   1 
ATOM   2188 C  CB  . TRP   A 1 299 ? -40.692 6.840   -5.593  1.00 28.81  ?  455 TRP   A CB  1 
ATOM   2189 C  CG  . TRP   A 1 299 ? -40.196 8.188   -5.318  1.00 24.56  ?  455 TRP   A CG  1 
ATOM   2190 C  CD1 . TRP   A 1 299 ? -40.819 9.166   -4.599  1.00 27.04  ?  455 TRP   A CD1 1 
ATOM   2191 C  CD2 . TRP   A 1 299 ? -38.965 8.740   -5.765  1.00 25.19  ?  455 TRP   A CD2 1 
ATOM   2192 N  NE1 . TRP   A 1 299 ? -40.030 10.300  -4.546  1.00 26.06  ?  455 TRP   A NE1 1 
ATOM   2193 C  CE2 . TRP   A 1 299 ? -38.875 10.052  -5.240  1.00 24.90  ?  455 TRP   A CE2 1 
ATOM   2194 C  CE3 . TRP   A 1 299 ? -37.912 8.247   -6.532  1.00 25.01  ?  455 TRP   A CE3 1 
ATOM   2195 C  CZ2 . TRP   A 1 299 ? -37.790 10.879  -5.488  1.00 27.19  ?  455 TRP   A CZ2 1 
ATOM   2196 C  CZ3 . TRP   A 1 299 ? -36.824 9.063   -6.754  1.00 27.58  ?  455 TRP   A CZ3 1 
ATOM   2197 C  CH2 . TRP   A 1 299 ? -36.779 10.370  -6.252  1.00 25.35  ?  455 TRP   A CH2 1 
ATOM   2198 N  N   . ASP   A 1 300 ? -43.032 5.008   -7.723  1.00 32.02  ?  456 ASP   A N   1 
ATOM   2199 C  CA  . ASP   A 1 300 ? -43.437 3.641   -8.056  1.00 27.86  ?  456 ASP   A CA  1 
ATOM   2200 C  C   . ASP   A 1 300 ? -42.322 2.916   -8.802  1.00 34.03  ?  456 ASP   A C   1 
ATOM   2201 O  O   . ASP   A 1 300 ? -41.713 3.465   -9.720  1.00 33.00  ?  456 ASP   A O   1 
ATOM   2202 C  CB  . ASP   A 1 300 ? -44.732 3.667   -8.885  1.00 35.74  ?  456 ASP   A CB  1 
ATOM   2203 C  CG  . ASP   A 1 300 ? -45.438 2.293   -8.953  1.00 49.19  ?  456 ASP   A CG  1 
ATOM   2204 O  OD1 . ASP   A 1 300 ? -44.774 1.262   -9.219  1.00 46.30  ?  456 ASP   A OD1 1 
ATOM   2205 O  OD2 . ASP   A 1 300 ? -46.669 2.240   -8.725  1.00 55.94  -1 456 ASP   A OD2 1 
ATOM   2206 N  N   . ARG   A 1 301 ? -42.032 1.687   -8.362  1.00 35.22  ?  457 ARG   A N   1 
ATOM   2207 C  CA  . ARG   A 1 301 ? -40.922 0.914   -8.921  1.00 41.26  ?  457 ARG   A CA  1 
ATOM   2208 C  C   . ARG   A 1 301 ? -41.108 0.686   -10.410 1.00 37.35  ?  457 ARG   A C   1 
ATOM   2209 O  O   . ARG   A 1 301 ? -40.130 0.630   -11.168 1.00 43.45  ?  457 ARG   A O   1 
ATOM   2210 C  CB  . ARG   A 1 301 ? -40.796 -0.423  -8.166  1.00 49.45  ?  457 ARG   A CB  1 
ATOM   2211 C  CG  . ARG   A 1 301 ? -39.522 -1.280  -8.391  1.00 43.46  ?  457 ARG   A CG  1 
ATOM   2212 C  CD  . ARG   A 1 301 ? -38.203 -0.507  -8.268  1.00 58.87  ?  457 ARG   A CD  1 
ATOM   2213 N  NE  . ARG   A 1 301 ? -37.035 -1.390  -8.280  1.00 61.78  ?  457 ARG   A NE  1 
ATOM   2214 C  CZ  . ARG   A 1 301 ? -36.365 -1.788  -9.361  1.00 45.38  ?  457 ARG   A CZ  1 
ATOM   2215 N  NH1 . ARG   A 1 301 ? -36.745 -1.452  -10.582 1.00 59.99  ?  457 ARG   A NH1 1 
ATOM   2216 N  NH2 . ARG   A 1 301 ? -35.292 -2.564  -9.212  1.00 51.75  ?  457 ARG   A NH2 1 
ATOM   2217 N  N   . LYS   A 1 302 ? -42.362 0.585   -10.852 1.00 37.08  ?  458 LYS   A N   1 
ATOM   2218 C  CA  . LYS   A 1 302 ? -42.673 0.441   -12.267 1.00 43.15  ?  458 LYS   A CA  1 
ATOM   2219 C  C   . LYS   A 1 302 ? -42.280 1.671   -13.086 1.00 46.73  ?  458 LYS   A C   1 
ATOM   2220 O  O   . LYS   A 1 302 ? -42.202 1.580   -14.321 1.00 41.47  ?  458 LYS   A O   1 
ATOM   2221 C  CB  . LYS   A 1 302 ? -44.169 0.133   -12.401 1.00 38.75  ?  458 LYS   A CB  1 
ATOM   2222 C  CG  . LYS   A 1 302 ? -45.050 1.369   -12.580 1.00 44.82  ?  458 LYS   A CG  1 
ATOM   2223 C  CD  . LYS   A 1 302 ? -46.543 0.996   -12.640 1.00 50.03  ?  458 LYS   A CD  1 
ATOM   2224 C  CE  . LYS   A 1 302 ? -47.379 2.118   -13.275 1.00 54.83  ?  458 LYS   A CE  1 
ATOM   2225 N  NZ  . LYS   A 1 302 ? -48.215 2.860   -12.275 1.00 53.28  ?  458 LYS   A NZ  1 
ATOM   2226 N  N   . ASP   A 1 303 ? -42.012 2.805   -12.423 1.00 32.97  ?  459 ASP   A N   1 
ATOM   2227 C  CA  . ASP   A 1 303 ? -41.657 4.074   -13.052 1.00 35.91  ?  459 ASP   A CA  1 
ATOM   2228 C  C   . ASP   A 1 303 ? -40.171 4.409   -12.932 1.00 34.16  ?  459 ASP   A C   1 
ATOM   2229 O  O   . ASP   A 1 303 ? -39.801 5.590   -12.991 1.00 30.99  ?  459 ASP   A O   1 
ATOM   2230 C  CB  . ASP   A 1 303 ? -42.501 5.194   -12.444 1.00 31.60  ?  459 ASP   A CB  1 
ATOM   2231 C  CG  . ASP   A 1 303 ? -43.974 5.063   -12.805 1.00 44.37  ?  459 ASP   A CG  1 
ATOM   2232 O  OD1 . ASP   A 1 303 ? -44.827 5.719   -12.147 1.00 43.69  ?  459 ASP   A OD1 1 
ATOM   2233 O  OD2 . ASP   A 1 303 ? -44.265 4.333   -13.787 1.00 43.27  -1 459 ASP   A OD2 1 
ATOM   2234 N  N   . LEU   A 1 304 ? -39.325 3.392   -12.728 1.00 33.31  ?  460 LEU   A N   1 
ATOM   2235 C  CA  . LEU   A 1 304 ? -37.886 3.582   -12.566 1.00 34.07  ?  460 LEU   A CA  1 
ATOM   2236 C  C   . LEU   A 1 304 ? -37.288 4.448   -13.670 1.00 30.53  ?  460 LEU   A C   1 
ATOM   2237 O  O   . LEU   A 1 304 ? -36.430 5.312   -13.421 1.00 28.25  ?  460 LEU   A O   1 
ATOM   2238 C  CB  . LEU   A 1 304 ? -37.192 2.215   -12.568 1.00 37.51  ?  460 LEU   A CB  1 
ATOM   2239 C  CG  . LEU   A 1 304 ? -35.668 2.290   -12.531 1.00 30.77  ?  460 LEU   A CG  1 
ATOM   2240 C  CD1 . LEU   A 1 304 ? -35.201 2.912   -11.184 1.00 31.35  ?  460 LEU   A CD1 1 
ATOM   2241 C  CD2 . LEU   A 1 304 ? -35.035 0.920   -12.792 1.00 39.56  ?  460 LEU   A CD2 1 
ATOM   2242 N  N   . GLY   A 1 305 ? -37.723 4.193   -14.911 1.00 30.05  ?  461 GLY   A N   1 
ATOM   2243 C  CA  . GLY   A 1 305 ? -37.159 4.909   -16.041 1.00 28.97  ?  461 GLY   A CA  1 
ATOM   2244 C  C   . GLY   A 1 305 ? -37.366 6.401   -15.919 1.00 28.74  ?  461 GLY   A C   1 
ATOM   2245 O  O   . GLY   A 1 305 ? -36.414 7.176   -15.990 1.00 28.57  ?  461 GLY   A O   1 
ATOM   2246 N  N   . LEU   A 1 306 ? -38.612 6.819   -15.675 1.00 30.44  ?  462 LEU   A N   1 
ATOM   2247 C  CA  . LEU   A 1 306 ? -38.879 8.251   -15.574 1.00 31.44  ?  462 LEU   A CA  1 
ATOM   2248 C  C   . LEU   A 1 306 ? -38.371 8.834   -14.263 1.00 29.15  ?  462 LEU   A C   1 
ATOM   2249 O  O   . LEU   A 1 306 ? -37.963 10.000  -14.230 1.00 29.38  ?  462 LEU   A O   1 
ATOM   2250 C  CB  . LEU   A 1 306 ? -40.368 8.546   -15.726 1.00 33.57  ?  462 LEU   A CB  1 
ATOM   2251 C  CG  . LEU   A 1 306 ? -40.860 8.630   -17.173 1.00 49.01  ?  462 LEU   A CG  1 
ATOM   2252 C  CD1 . LEU   A 1 306 ? -42.093 9.531   -17.224 1.00 56.44  ?  462 LEU   A CD1 1 
ATOM   2253 C  CD2 . LEU   A 1 306 ? -39.771 9.111   -18.174 1.00 39.98  ?  462 LEU   A CD2 1 
ATOM   2254 N  N   . CYS   A 1 307 ? -38.373 8.037   -13.184 1.00 28.91  ?  463 CYS   A N   1 
ATOM   2255 C  CA  . CYS   A 1 307 ? -37.849 8.516   -11.906 1.00 29.93  ?  463 CYS   A CA  1 
ATOM   2256 C  C   . CYS   A 1 307 ? -36.363 8.850   -12.008 1.00 28.69  ?  463 CYS   A C   1 
ATOM   2257 O  O   . CYS   A 1 307 ? -35.938 9.961   -11.668 1.00 28.87  ?  463 CYS   A O   1 
ATOM   2258 C  CB  . CYS   A 1 307 ? -38.105 7.475   -10.816 1.00 27.00  ?  463 CYS   A CB  1 
ATOM   2259 S  SG  . CYS   A 1 307 ? -39.868 7.327   -10.362 1.00 28.84  ?  463 CYS   A SG  1 
ATOM   2260 N  N   . PHE   A 1 308 ? -35.558 7.915   -12.519 1.00 26.42  ?  464 PHE   A N   1 
ATOM   2261 C  CA  . PHE   A 1 308 ? -34.140 8.211   -12.741 1.00 26.42  ?  464 PHE   A CA  1 
ATOM   2262 C  C   . PHE   A 1 308 ? -33.937 9.378   -13.707 1.00 27.52  ?  464 PHE   A C   1 
ATOM   2263 O  O   . PHE   A 1 308 ? -33.025 10.201  -13.516 1.00 26.90  ?  464 PHE   A O   1 
ATOM   2264 C  CB  . PHE   A 1 308 ? -33.410 6.974   -13.262 1.00 27.00  ?  464 PHE   A CB  1 
ATOM   2265 C  CG  . PHE   A 1 308 ? -31.961 7.205   -13.519 1.00 27.87  ?  464 PHE   A CG  1 
ATOM   2266 C  CD1 . PHE   A 1 308 ? -31.109 7.627   -12.491 1.00 27.54  ?  464 PHE   A CD1 1 
ATOM   2267 C  CD2 . PHE   A 1 308 ? -31.432 6.998   -14.799 1.00 28.04  ?  464 PHE   A CD2 1 
ATOM   2268 C  CE1 . PHE   A 1 308 ? -29.771 7.838   -12.726 1.00 27.47  ?  464 PHE   A CE1 1 
ATOM   2269 C  CE2 . PHE   A 1 308 ? -30.081 7.209   -15.045 1.00 28.87  ?  464 PHE   A CE2 1 
ATOM   2270 C  CZ  . PHE   A 1 308 ? -29.245 7.625   -13.986 1.00 28.11  ?  464 PHE   A CZ  1 
ATOM   2271 N  N   . ASP   A 1 309 ? -34.730 9.429   -14.789 1.00 27.52  ?  465 ASP   A N   1 
ATOM   2272 C  CA  . ASP   A 1 309 ? -34.609 10.547  -15.724 1.00 28.42  ?  465 ASP   A CA  1 
ATOM   2273 C  C   . ASP   A 1 309 ? -34.823 11.870  -15.005 1.00 26.89  ?  465 ASP   A C   1 
ATOM   2274 O  O   . ASP   A 1 309 ? -34.144 12.854  -15.293 1.00 27.71  ?  465 ASP   A O   1 
ATOM   2275 C  CB  . ASP   A 1 309 ? -35.609 10.393  -16.890 1.00 27.47  ?  465 ASP   A CB  1 
ATOM   2276 C  CG  . ASP   A 1 309 ? -35.424 11.447  -18.004 1.00 28.13  ?  465 ASP   A CG  1 
ATOM   2277 O  OD1 . ASP   A 1 309 ? -34.324 11.518  -18.603 1.00 30.26  ?  465 ASP   A OD1 1 
ATOM   2278 O  OD2 . ASP   A 1 309 ? -36.417 12.158  -18.349 1.00 28.34  -1 465 ASP   A OD2 1 
ATOM   2279 N  N   . ASN   A 1 310 ? -35.773 11.903  -14.068 1.00 28.66  ?  466 ASN   A N   1 
ATOM   2280 C  CA  . ASN   A 1 310 ? -36.076 13.145  -13.364 1.00 27.98  ?  466 ASN   A CA  1 
ATOM   2281 C  C   . ASN   A 1 310 ? -35.006 13.466  -12.321 1.00 29.14  ?  466 ASN   A C   1 
ATOM   2282 O  O   . ASN   A 1 310 ? -34.767 14.646  -12.042 1.00 28.14  ?  466 ASN   A O   1 
ATOM   2283 C  CB  . ASN   A 1 310 ? -37.493 13.085  -12.752 1.00 27.36  ?  466 ASN   A CB  1 
ATOM   2284 C  CG  . ASN   A 1 310 ? -38.616 13.039  -13.830 1.00 35.21  ?  466 ASN   A CG  1 
ATOM   2285 O  OD1 . ASN   A 1 310 ? -38.413 13.434  -14.980 1.00 28.93  ?  466 ASN   A OD1 1 
ATOM   2286 N  ND2 . ASN   A 1 310 ? -39.797 12.556  -13.441 1.00 30.84  ?  466 ASN   A ND2 1 
ATOM   2287 N  N   . CYS   A 1 311 ? -34.317 12.443  -11.785 1.00 27.44  ?  467 CYS   A N   1 
ATOM   2288 C  CA  . CYS   A 1 311 ? -33.151 12.707  -10.938 1.00 27.94  ?  467 CYS   A CA  1 
ATOM   2289 C  C   . CYS   A 1 311 ? -32.013 13.273  -11.767 1.00 28.59  ?  467 CYS   A C   1 
ATOM   2290 O  O   . CYS   A 1 311 ? -31.393 14.273  -11.386 1.00 27.57  ?  467 CYS   A O   1 
ATOM   2291 C  CB  . CYS   A 1 311 ? -32.688 11.427  -10.230 1.00 26.86  ?  467 CYS   A CB  1 
ATOM   2292 S  SG  . CYS   A 1 311 ? -33.882 10.808  -9.044  1.00 27.26  ?  467 CYS   A SG  1 
ATOM   2293 N  N   . VAL   A 1 312 ? -31.772 12.679  -12.944 1.00 26.53  ?  468 VAL   A N   1 
ATOM   2294 C  CA  . VAL   A 1 312 ? -30.727 13.174  -13.833 1.00 26.62  ?  468 VAL   A CA  1 
ATOM   2295 C  C   . VAL   A 1 312 ? -30.996 14.625  -14.193 1.00 26.07  ?  468 VAL   A C   1 
ATOM   2296 O  O   . VAL   A 1 312 ? -30.097 15.479  -14.155 1.00 25.75  ?  468 VAL   A O   1 
ATOM   2297 C  CB  . VAL   A 1 312 ? -30.638 12.296  -15.093 1.00 26.96  ?  468 VAL   A CB  1 
ATOM   2298 C  CG1 . VAL   A 1 312 ? -29.702 12.933  -16.109 1.00 27.78  ?  468 VAL   A CG1 1 
ATOM   2299 C  CG2 . VAL   A 1 312 ? -30.135 10.911  -14.719 1.00 27.35  ?  468 VAL   A CG2 1 
ATOM   2300 N  N   . THR   A 1 313 ? -32.251 14.914  -14.529 1.00 28.69  ?  469 THR   A N   1 
ATOM   2301 C  CA  . THR   A 1 313 ? -32.641 16.255  -14.934 1.00 28.11  ?  469 THR   A CA  1 
ATOM   2302 C  C   . THR   A 1 313 ? -32.421 17.252  -13.805 1.00 26.95  ?  469 THR   A C   1 
ATOM   2303 O  O   . THR   A 1 313 ? -31.931 18.360  -14.045 1.00 26.91  ?  469 THR   A O   1 
ATOM   2304 C  CB  . THR   A 1 313 ? -34.101 16.234  -15.402 1.00 28.20  ?  469 THR   A CB  1 
ATOM   2305 O  OG1 . THR   A 1 313 ? -34.193 15.523  -16.654 1.00 36.07  ?  469 THR   A OG1 1 
ATOM   2306 C  CG2 . THR   A 1 313 ? -34.685 17.636  -15.525 1.00 27.16  ?  469 THR   A CG2 1 
ATOM   2307 N  N   . TYR   A 1 314 ? -32.753 16.861  -12.568 1.00 28.88  ?  470 TYR   A N   1 
ATOM   2308 C  CA  . TYR   A 1 314 ? -32.567 17.779  -11.441 1.00 27.50  ?  470 TYR   A CA  1 
ATOM   2309 C  C   . TYR   A 1 314 ? -31.097 18.089  -11.234 1.00 27.70  ?  470 TYR   A C   1 
ATOM   2310 O  O   . TYR   A 1 314 ? -30.717 19.261  -11.094 1.00 27.42  ?  470 TYR   A O   1 
ATOM   2311 C  CB  . TYR   A 1 314 ? -33.192 17.221  -10.161 1.00 27.36  ?  470 TYR   A CB  1 
ATOM   2312 C  CG  . TYR   A 1 314 ? -33.102 18.236  -9.032  1.00 32.22  ?  470 TYR   A CG  1 
ATOM   2313 C  CD1 . TYR   A 1 314 ? -34.021 19.281  -8.939  1.00 37.24  ?  470 TYR   A CD1 1 
ATOM   2314 C  CD2 . TYR   A 1 314 ? -32.073 18.176  -8.094  1.00 26.02  ?  470 TYR   A CD2 1 
ATOM   2315 C  CE1 . TYR   A 1 314 ? -33.923 20.242  -7.923  1.00 40.71  ?  470 TYR   A CE1 1 
ATOM   2316 C  CE2 . TYR   A 1 314 ? -31.973 19.124  -7.067  1.00 35.46  ?  470 TYR   A CE2 1 
ATOM   2317 C  CZ  . TYR   A 1 314 ? -32.906 20.151  -6.992  1.00 40.34  ?  470 TYR   A CZ  1 
ATOM   2318 O  OH  . TYR   A 1 314 ? -32.816 21.098  -6.000  1.00 43.59  ?  470 TYR   A OH  1 
ATOM   2319 N  N   . PHE   A 1 315 ? -30.244 17.056  -11.253 1.00 28.07  ?  471 PHE   A N   1 
ATOM   2320 C  CA  . PHE   A 1 315 ? -28.806 17.283  -11.097 1.00 29.46  ?  471 PHE   A CA  1 
ATOM   2321 C  C   . PHE   A 1 315 ? -28.276 18.219  -12.181 1.00 29.22  ?  471 PHE   A C   1 
ATOM   2322 O  O   . PHE   A 1 315 ? -27.504 19.151  -11.894 1.00 28.43  ?  471 PHE   A O   1 
ATOM   2323 C  CB  . PHE   A 1 315 ? -28.068 15.939  -11.102 1.00 28.42  ?  471 PHE   A CB  1 
ATOM   2324 C  CG  . PHE   A 1 315 ? -26.595 16.037  -10.853 1.00 31.21  ?  471 PHE   A CG  1 
ATOM   2325 C  CD1 . PHE   A 1 315 ? -26.102 16.305  -9.571  1.00 30.34  ?  471 PHE   A CD1 1 
ATOM   2326 C  CD2 . PHE   A 1 315 ? -25.688 15.765  -11.873 1.00 29.65  ?  471 PHE   A CD2 1 
ATOM   2327 C  CE1 . PHE   A 1 315 ? -24.735 16.371  -9.332  1.00 32.66  ?  471 PHE   A CE1 1 
ATOM   2328 C  CE2 . PHE   A 1 315 ? -24.326 15.818  -11.653 1.00 29.95  ?  471 PHE   A CE2 1 
ATOM   2329 C  CZ  . PHE   A 1 315 ? -23.838 16.129  -10.378 1.00 28.79  ?  471 PHE   A CZ  1 
ATOM   2330 N  N   . LEU   A 1 316 ? -28.718 18.011  -13.431 1.00 25.79  ?  472 LEU   A N   1 
ATOM   2331 C  CA  . LEU   A 1 316 ? -28.308 18.881  -14.528 1.00 25.61  ?  472 LEU   A CA  1 
ATOM   2332 C  C   . LEU   A 1 316 ? -28.744 20.323  -14.281 1.00 25.07  ?  472 LEU   A C   1 
ATOM   2333 O  O   . LEU   A 1 316 ? -28.001 21.254  -14.575 1.00 25.19  ?  472 LEU   A O   1 
ATOM   2334 C  CB  . LEU   A 1 316 ? -28.911 18.365  -15.855 1.00 26.25  ?  472 LEU   A CB  1 
ATOM   2335 C  CG  . LEU   A 1 316 ? -28.300 17.095  -16.459 1.00 26.81  ?  472 LEU   A CG  1 
ATOM   2336 C  CD1 . LEU   A 1 316 ? -29.186 16.573  -17.619 1.00 27.36  ?  472 LEU   A CD1 1 
ATOM   2337 C  CD2 . LEU   A 1 316 ? -26.921 17.470  -16.961 1.00 26.85  ?  472 LEU   A CD2 1 
ATOM   2338 N  N   . GLN   A 1 317 ? -29.978 20.522  -13.800 1.00 26.35  ?  473 GLN   A N   1 
ATOM   2339 C  CA  . GLN   A 1 317 ? -30.439 21.871  -13.519 1.00 26.09  ?  473 GLN   A CA  1 
ATOM   2340 C  C   . GLN   A 1 317 ? -29.574 22.531  -12.447 1.00 28.69  ?  473 GLN   A C   1 
ATOM   2341 O  O   . GLN   A 1 317 ? -29.287 23.737  -12.525 1.00 30.71  ?  473 GLN   A O   1 
ATOM   2342 C  CB  . GLN   A 1 317 ? -31.903 21.853  -13.098 1.00 26.40  ?  473 GLN   A CB  1 
ATOM   2343 C  CG  . GLN   A 1 317 ? -32.455 23.275  -12.884 1.00 26.36  ?  473 GLN   A CG  1 
ATOM   2344 C  CD  . GLN   A 1 317 ? -33.923 23.280  -12.495 1.00 34.51  ?  473 GLN   A CD  1 
ATOM   2345 O  OE1 . GLN   A 1 317 ? -34.833 23.499  -13.326 1.00 30.85  ?  473 GLN   A OE1 1 
ATOM   2346 N  NE2 . GLN   A 1 317 ? -34.173 22.935  -11.244 1.00 28.34  ?  473 GLN   A NE2 1 
ATOM   2347 N  N   . CYS   A 1 318 ? -29.126 21.748  -11.447 1.00 25.12  ?  474 CYS   A N   1 
ATOM   2348 C  CA  . CYS   A 1 318 ? -28.186 22.291  -10.464 1.00 25.96  ?  474 CYS   A CA  1 
ATOM   2349 C  C   . CYS   A 1 318 ? -26.883 22.707  -11.134 1.00 26.86  ?  474 CYS   A C   1 
ATOM   2350 O  O   . CYS   A 1 318 ? -26.351 23.784  -10.850 1.00 25.60  ?  474 CYS   A O   1 
ATOM   2351 C  CB  . CYS   A 1 318 ? -27.921 21.262  -9.369  1.00 24.30  ?  474 CYS   A CB  1 
ATOM   2352 S  SG  . CYS   A 1 318 ? -29.422 20.924  -8.419  1.00 29.58  ?  474 CYS   A SG  1 
ATOM   2353 N  N   . LEU   A 1 319 ? -26.373 21.874  -12.056 1.00 25.84  ?  475 LEU   A N   1 
ATOM   2354 C  CA  . LEU   A 1 319 ? -25.138 22.196  -12.779 1.00 26.71  ?  475 LEU   A CA  1 
ATOM   2355 C  C   . LEU   A 1 319 ? -25.268 23.491  -13.587 1.00 32.16  ?  475 LEU   A C   1 
ATOM   2356 O  O   . LEU   A 1 319 ? -24.388 24.366  -13.522 1.00 30.90  ?  475 LEU   A O   1 
ATOM   2357 C  CB  . LEU   A 1 319 ? -24.758 21.034  -13.716 1.00 27.15  ?  475 LEU   A CB  1 
ATOM   2358 C  CG  . LEU   A 1 319 ? -24.202 19.762  -13.066 1.00 32.18  ?  475 LEU   A CG  1 
ATOM   2359 C  CD1 . LEU   A 1 319 ? -24.142 18.554  -14.041 1.00 27.53  ?  475 LEU   A CD1 1 
ATOM   2360 C  CD2 . LEU   A 1 319 ? -22.830 20.032  -12.439 1.00 27.13  ?  475 LEU   A CD2 1 
ATOM   2361 N  N   . ARG   A 1 320 ? -26.365 23.638  -14.354 1.00 28.06  ?  476 ARG   A N   1 
ATOM   2362 C  CA  . ARG   A 1 320 ? -26.468 24.800  -15.233 1.00 27.84  ?  476 ARG   A CA  1 
ATOM   2363 C  C   . ARG   A 1 320 ? -26.630 26.089  -14.439 1.00 27.77  ?  476 ARG   A C   1 
ATOM   2364 O  O   . ARG   A 1 320 ? -26.063 27.114  -14.816 1.00 27.95  ?  476 ARG   A O   1 
ATOM   2365 C  CB  . ARG   A 1 320 ? -27.636 24.657  -16.229 1.00 34.54  ?  476 ARG   A CB  1 
ATOM   2366 C  CG  . ARG   A 1 320 ? -27.506 23.543  -17.279 1.00 28.45  ?  476 ARG   A CG  1 
ATOM   2367 C  CD  . ARG   A 1 320 ? -28.623 23.662  -18.325 1.00 28.90  ?  476 ARG   A CD  1 
ATOM   2368 N  NE  . ARG   A 1 320 ? -28.838 22.367  -18.962 1.00 29.33  ?  476 ARG   A NE  1 
ATOM   2369 C  CZ  . ARG   A 1 320 ? -29.644 21.439  -18.471 1.00 29.45  ?  476 ARG   A CZ  1 
ATOM   2370 N  NH1 . ARG   A 1 320 ? -30.356 21.656  -17.370 1.00 28.51  ?  476 ARG   A NH1 1 
ATOM   2371 N  NH2 . ARG   A 1 320 ? -29.745 20.266  -19.097 1.00 29.36  ?  476 ARG   A NH2 1 
ATOM   2372 N  N   . THR   A 1 321 ? -27.436 26.071  -13.365 1.00 28.62  ?  477 THR   A N   1 
ATOM   2373 C  CA  . THR   A 1 321 ? -27.632 27.249  -12.512 1.00 29.71  ?  477 THR   A CA  1 
ATOM   2374 C  C   . THR   A 1 321 ? -26.520 27.426  -11.468 1.00 36.86  ?  477 THR   A C   1 
ATOM   2375 O  O   . THR   A 1 321 ? -26.504 28.450  -10.773 1.00 32.44  ?  477 THR   A O   1 
ATOM   2376 C  CB  . THR   A 1 321 ? -28.994 27.166  -11.801 1.00 26.86  ?  477 THR   A CB  1 
ATOM   2377 O  OG1 . THR   A 1 321 ? -29.022 26.001  -10.976 1.00 27.40  ?  477 THR   A OG1 1 
ATOM   2378 C  CG2 . THR   A 1 321 ? -30.146 27.061  -12.790 1.00 30.61  ?  477 THR   A CG2 1 
ATOM   2379 N  N   . GLU   A 1 322 ? -25.599 26.459  -11.351 1.00 31.49  ?  478 GLU   A N   1 
ATOM   2380 C  CA  . GLU   A 1 322 ? -24.488 26.499  -10.385 1.00 35.69  ?  478 GLU   A CA  1 
ATOM   2381 C  C   . GLU   A 1 322 ? -25.000 26.627  -8.947  1.00 36.79  ?  478 GLU   A C   1 
ATOM   2382 O  O   . GLU   A 1 322 ? -24.404 27.314  -8.104  1.00 34.03  ?  478 GLU   A O   1 
ATOM   2383 C  CB  . GLU   A 1 322 ? -23.492 27.615  -10.717 1.00 38.20  ?  478 GLU   A CB  1 
ATOM   2384 C  CG  . GLU   A 1 322 ? -22.883 27.496  -12.101 1.00 34.49  ?  478 GLU   A CG  1 
ATOM   2385 C  CD  . GLU   A 1 322 ? -21.775 28.500  -12.355 1.00 38.48  ?  478 GLU   A CD  1 
ATOM   2386 O  OE1 . GLU   A 1 322 ? -20.646 28.289  -11.862 1.00 43.21  ?  478 GLU   A OE1 1 
ATOM   2387 O  OE2 . GLU   A 1 322 ? -22.035 29.515  -13.046 1.00 51.60  -1 478 GLU   A OE2 1 
ATOM   2388 N  N   . LYS   A 1 323 ? -26.103 25.939  -8.662  1.00 30.75  ?  479 LYS   A N   1 
ATOM   2389 C  CA  . LYS   A 1 323 ? -26.759 26.005  -7.364  1.00 32.92  ?  479 LYS   A CA  1 
ATOM   2390 C  C   . LYS   A 1 323 ? -27.006 24.577  -6.906  1.00 31.23  ?  479 LYS   A C   1 
ATOM   2391 O  O   . LYS   A 1 323 ? -27.739 23.830  -7.563  1.00 30.24  ?  479 LYS   A O   1 
ATOM   2392 C  CB  . LYS   A 1 323 ? -28.082 26.774  -7.438  1.00 37.50  ?  479 LYS   A CB  1 
ATOM   2393 C  CG  . LYS   A 1 323 ? -28.514 27.374  -6.129  1.00 47.92  ?  479 LYS   A CG  1 
ATOM   2394 C  CD  . LYS   A 1 323 ? -30.005 27.210  -5.849  1.00 50.10  ?  479 LYS   A CD  1 
ATOM   2395 C  CE  . LYS   A 1 323 ? -30.235 27.234  -4.324  1.00 42.31  ?  479 LYS   A CE  1 
ATOM   2396 N  NZ  . LYS   A 1 323 ? -31.369 26.363  -3.898  1.00 52.29  ?  479 LYS   A NZ  1 
ATOM   2397 N  N   . LEU   A 1 324 ? -26.369 24.190  -5.803  1.00 29.12  ?  480 LEU   A N   1 
ATOM   2398 C  CA  . LEU   A 1 324 ? -26.599 22.895  -5.160  1.00 28.02  ?  480 LEU   A CA  1 
ATOM   2399 C  C   . LEU   A 1 324 ? -26.426 23.147  -3.665  1.00 32.62  ?  480 LEU   A C   1 
ATOM   2400 O  O   . LEU   A 1 324 ? -25.310 23.060  -3.145  1.00 29.69  ?  480 LEU   A O   1 
ATOM   2401 C  CB  . LEU   A 1 324 ? -25.640 21.814  -5.648  1.00 27.26  ?  480 LEU   A CB  1 
ATOM   2402 C  CG  . LEU   A 1 324 ? -25.910 20.456  -4.977  1.00 27.47  ?  480 LEU   A CG  1 
ATOM   2403 C  CD1 . LEU   A 1 324 ? -27.288 19.949  -5.342  1.00 28.39  ?  480 LEU   A CD1 1 
ATOM   2404 C  CD2 . LEU   A 1 324 ? -24.853 19.409  -5.335  1.00 28.48  ?  480 LEU   A CD2 1 
ATOM   2405 N  N   . GLU   A 1 325 ? -27.516 23.522  -2.999  1.00 31.40  ?  481 GLU   A N   1 
ATOM   2406 C  CA  . GLU   A 1 325 ? -27.417 23.787  -1.566  1.00 38.50  ?  481 GLU   A CA  1 
ATOM   2407 C  C   . GLU   A 1 325 ? -27.080 22.519  -0.804  1.00 27.25  ?  481 GLU   A C   1 
ATOM   2408 O  O   . GLU   A 1 325 ? -27.631 21.445  -1.066  1.00 28.71  ?  481 GLU   A O   1 
ATOM   2409 C  CB  . GLU   A 1 325 ? -28.717 24.351  -1.010  1.00 37.53  ?  481 GLU   A CB  1 
ATOM   2410 C  CG  . GLU   A 1 325 ? -29.103 25.676  -1.532  1.00 36.77  ?  481 GLU   A CG  1 
ATOM   2411 C  CD  . GLU   A 1 325 ? -30.394 26.120  -0.918  1.00 44.31  ?  481 GLU   A CD  1 
ATOM   2412 O  OE1 . GLU   A 1 325 ? -31.101 25.262  -0.332  1.00 43.84  ?  481 GLU   A OE1 1 
ATOM   2413 O  OE2 . GLU   A 1 325 ? -30.663 27.331  -0.957  1.00 63.71  -1 481 GLU   A OE2 1 
ATOM   2414 N  N   . ASN   A 1 326 ? -26.173 22.646  0.158   1.00 31.80  ?  482 ASN   A N   1 
ATOM   2415 C  CA  . ASN   A 1 326 ? -26.002 21.562  1.110   1.00 27.27  ?  482 ASN   A CA  1 
ATOM   2416 C  C   . ASN   A 1 326 ? -27.339 21.250  1.768   1.00 26.08  ?  482 ASN   A C   1 
ATOM   2417 O  O   . ASN   A 1 326 ? -28.059 22.160  2.183   1.00 26.23  ?  482 ASN   A O   1 
ATOM   2418 C  CB  . ASN   A 1 326 ? -24.965 21.938  2.174   1.00 29.55  ?  482 ASN   A CB  1 
ATOM   2419 C  CG  . ASN   A 1 326 ? -24.690 20.792  3.113   1.00 32.03  ?  482 ASN   A CG  1 
ATOM   2420 O  OD1 . ASN   A 1 326 ? -25.579 20.353  3.857   1.00 29.03  ?  482 ASN   A OD1 1 
ATOM   2421 N  ND2 . ASN   A 1 326 ? -23.476 20.267  3.051   1.00 31.19  ?  482 ASN   A ND2 1 
ATOM   2422 N  N   . TYR   A 1 327 ? -27.675 19.959  1.859   1.00 26.78  ?  483 TYR   A N   1 
ATOM   2423 C  CA  . TYR   A 1 327 ? -29.008 19.566  2.316   1.00 28.38  ?  483 TYR   A CA  1 
ATOM   2424 C  C   . TYR   A 1 327 ? -29.234 19.932  3.778   1.00 28.18  ?  483 TYR   A C   1 
ATOM   2425 O  O   . TYR   A 1 327 ? -30.378 20.119  4.217   1.00 27.82  ?  483 TYR   A O   1 
ATOM   2426 C  CB  . TYR   A 1 327 ? -29.206 18.061  2.129   1.00 27.84  ?  483 TYR   A CB  1 
ATOM   2427 C  CG  . TYR   A 1 327 ? -30.659 17.634  2.157   1.00 25.86  ?  483 TYR   A CG  1 
ATOM   2428 C  CD1 . TYR   A 1 327 ? -31.551 18.027  1.147   1.00 26.41  ?  483 TYR   A CD1 1 
ATOM   2429 C  CD2 . TYR   A 1 327 ? -31.135 16.833  3.179   1.00 28.85  ?  483 TYR   A CD2 1 
ATOM   2430 C  CE1 . TYR   A 1 327 ? -32.869 17.648  1.188   1.00 24.16  ?  483 TYR   A CE1 1 
ATOM   2431 C  CE2 . TYR   A 1 327 ? -32.443 16.446  3.229   1.00 29.79  ?  483 TYR   A CE2 1 
ATOM   2432 C  CZ  . TYR   A 1 327 ? -33.305 16.839  2.213   1.00 29.52  ?  483 TYR   A CZ  1 
ATOM   2433 O  OH  . TYR   A 1 327 ? -34.601 16.452  2.288   1.00 27.06  ?  483 TYR   A OH  1 
ATOM   2434 N  N   . PHE   A 1 328 ? -28.155 20.024  4.541   1.00 28.17  ?  484 PHE   A N   1 
ATOM   2435 C  CA  . PHE   A 1 328 ? -28.232 20.304  5.964   1.00 29.31  ?  484 PHE   A CA  1 
ATOM   2436 C  C   . PHE   A 1 328 ? -27.874 21.732  6.288   1.00 29.98  ?  484 PHE   A C   1 
ATOM   2437 O  O   . PHE   A 1 328 ? -28.314 22.246  7.320   1.00 32.88  ?  484 PHE   A O   1 
ATOM   2438 C  CB  . PHE   A 1 328 ? -27.294 19.356  6.713   1.00 29.42  ?  484 PHE   A CB  1 
ATOM   2439 C  CG  . PHE   A 1 328 ? -27.669 17.918  6.547   1.00 28.81  ?  484 PHE   A CG  1 
ATOM   2440 C  CD1 . PHE   A 1 328 ? -28.562 17.318  7.420   1.00 30.69  ?  484 PHE   A CD1 1 
ATOM   2441 C  CD2 . PHE   A 1 328 ? -27.178 17.181  5.483   1.00 30.70  ?  484 PHE   A CD2 1 
ATOM   2442 C  CE1 . PHE   A 1 328 ? -28.922 15.987  7.259   1.00 32.99  ?  484 PHE   A CE1 1 
ATOM   2443 C  CE2 . PHE   A 1 328 ? -27.541 15.838  5.310   1.00 36.06  ?  484 PHE   A CE2 1 
ATOM   2444 C  CZ  . PHE   A 1 328 ? -28.411 15.245  6.202   1.00 28.80  ?  484 PHE   A CZ  1 
ATOM   2445 N  N   . ILE   A 1 329 ? -27.095 22.374  5.425   1.00 30.66  ?  485 ILE   A N   1 
ATOM   2446 C  CA  . ILE   A 1 329 ? -26.606 23.737  5.622   1.00 30.64  ?  485 ILE   A CA  1 
ATOM   2447 C  C   . ILE   A 1 329 ? -26.969 24.521  4.364   1.00 34.41  ?  485 ILE   A C   1 
ATOM   2448 O  O   . ILE   A 1 329 ? -26.148 24.623  3.435   1.00 29.96  ?  485 ILE   A O   1 
ATOM   2449 C  CB  . ILE   A 1 329 ? -25.089 23.748  5.859   1.00 32.18  ?  485 ILE   A CB  1 
ATOM   2450 C  CG1 . ILE   A 1 329 ? -24.704 22.738  6.957   1.00 36.07  ?  485 ILE   A CG1 1 
ATOM   2451 C  CG2 . ILE   A 1 329 ? -24.615 25.147  6.192   1.00 30.56  ?  485 ILE   A CG2 1 
ATOM   2452 C  CD1 . ILE   A 1 329 ? -23.224 22.498  7.041   1.00 33.74  ?  485 ILE   A CD1 1 
ATOM   2453 N  N   . PRO   A 1 330 ? -28.183 25.060  4.268   1.00 34.88  ?  486 PRO   A N   1 
ATOM   2454 C  CA  . PRO   A 1 330 ? -28.646 25.566  2.960   1.00 35.28  ?  486 PRO   A CA  1 
ATOM   2455 C  C   . PRO   A 1 330 ? -27.887 26.788  2.465   1.00 35.11  ?  486 PRO   A C   1 
ATOM   2456 O  O   . PRO   A 1 330 ? -27.947 27.073  1.266   1.00 34.94  ?  486 PRO   A O   1 
ATOM   2457 C  CB  . PRO   A 1 330 ? -30.132 25.868  3.199   1.00 43.23  ?  486 PRO   A CB  1 
ATOM   2458 C  CG  . PRO   A 1 330 ? -30.223 26.102  4.706   1.00 45.90  ?  486 PRO   A CG  1 
ATOM   2459 C  CD  . PRO   A 1 330 ? -29.190 25.199  5.332   1.00 31.36  ?  486 PRO   A CD  1 
ATOM   2460 N  N   . GLU   A 1 331 ? -27.156 27.500  3.320   1.00 34.38  ?  487 GLU   A N   1 
ATOM   2461 C  CA  . GLU   A 1 331 ? -26.368 28.625  2.829   1.00 32.53  ?  487 GLU   A CA  1 
ATOM   2462 C  C   . GLU   A 1 331 ? -25.040 28.184  2.232   1.00 30.58  ?  487 GLU   A C   1 
ATOM   2463 O  O   . GLU   A 1 331 ? -24.320 29.019  1.684   1.00 33.46  ?  487 GLU   A O   1 
ATOM   2464 C  CB  . GLU   A 1 331 ? -26.128 29.634  3.957   1.00 36.01  ?  487 GLU   A CB  1 
ATOM   2465 C  CG  . GLU   A 1 331 ? -27.399 30.297  4.463   1.00 35.92  ?  487 GLU   A CG  1 
ATOM   2466 C  CD  . GLU   A 1 331 ? -27.173 31.048  5.757   1.00 46.45  ?  487 GLU   A CD  1 
ATOM   2467 O  OE1 . GLU   A 1 331 ? -27.130 30.402  6.831   1.00 52.96  ?  487 GLU   A OE1 1 
ATOM   2468 O  OE2 . GLU   A 1 331 ? -27.018 32.281  5.703   1.00 48.76  -1 487 GLU   A OE2 1 
ATOM   2469 N  N   . PHE   A 1 332 ? -24.703 26.895  2.315   1.00 31.05  ?  488 PHE   A N   1 
ATOM   2470 C  CA  . PHE   A 1 332 ? -23.475 26.360  1.739   1.00 33.34  ?  488 PHE   A CA  1 
ATOM   2471 C  C   . PHE   A 1 332 ? -23.790 25.832  0.331   1.00 31.33  ?  488 PHE   A C   1 
ATOM   2472 O  O   . PHE   A 1 332 ? -24.438 24.790  0.182   1.00 25.79  ?  488 PHE   A O   1 
ATOM   2473 C  CB  . PHE   A 1 332 ? -22.916 25.257  2.638   1.00 29.74  ?  488 PHE   A CB  1 
ATOM   2474 C  CG  . PHE   A 1 332 ? -21.507 24.866  2.315   1.00 33.66  ?  488 PHE   A CG  1 
ATOM   2475 C  CD1 . PHE   A 1 332 ? -21.218 23.978  1.294   1.00 40.12  ?  488 PHE   A CD1 1 
ATOM   2476 C  CD2 . PHE   A 1 332 ? -20.455 25.442  3.014   1.00 32.81  ?  488 PHE   A CD2 1 
ATOM   2477 C  CE1 . PHE   A 1 332 ? -19.894 23.645  0.996   1.00 35.86  ?  488 PHE   A CE1 1 
ATOM   2478 C  CE2 . PHE   A 1 332 ? -19.136 25.119  2.726   1.00 39.65  ?  488 PHE   A CE2 1 
ATOM   2479 C  CZ  . PHE   A 1 332 ? -18.856 24.214  1.716   1.00 43.33  ?  488 PHE   A CZ  1 
ATOM   2480 N  N   . ASN   A 1 333 ? -23.288 26.532  -0.689  1.00 32.22  ?  489 ASN   A N   1 
ATOM   2481 C  CA  . ASN   A 1 333 ? -23.503 26.163  -2.084  1.00 38.26  ?  489 ASN   A CA  1 
ATOM   2482 C  C   . ASN   A 1 333 ? -22.370 25.261  -2.563  1.00 30.51  ?  489 ASN   A C   1 
ATOM   2483 O  O   . ASN   A 1 333 ? -21.277 25.746  -2.874  1.00 33.94  ?  489 ASN   A O   1 
ATOM   2484 C  CB  . ASN   A 1 333 ? -23.602 27.408  -2.971  1.00 33.42  ?  489 ASN   A CB  1 
ATOM   2485 C  CG  . ASN   A 1 333 ? -23.974 27.062  -4.422  1.00 32.45  ?  489 ASN   A CG  1 
ATOM   2486 O  OD1 . ASN   A 1 333 ? -24.228 25.896  -4.754  1.00 31.43  ?  489 ASN   A OD1 1 
ATOM   2487 N  ND2 . ASN   A 1 333 ? -23.999 28.079  -5.285  1.00 29.54  ?  489 ASN   A ND2 1 
ATOM   2488 N  N   . LEU   A 1 334 ? -22.668 23.964  -2.706  1.00 29.97  ?  490 LEU   A N   1 
ATOM   2489 C  CA  . LEU   A 1 334 ? -21.678 23.007  -3.192  1.00 31.07  ?  490 LEU   A CA  1 
ATOM   2490 C  C   . LEU   A 1 334 ? -21.237 23.319  -4.617  1.00 30.55  ?  490 LEU   A C   1 
ATOM   2491 O  O   . LEU   A 1 334 ? -20.101 23.019  -4.995  1.00 33.24  ?  490 LEU   A O   1 
ATOM   2492 C  CB  . LEU   A 1 334 ? -22.242 21.583  -3.111  1.00 29.05  ?  490 LEU   A CB  1 
ATOM   2493 C  CG  . LEU   A 1 334 ? -22.596 21.060  -1.712  1.00 29.87  ?  490 LEU   A CG  1 
ATOM   2494 C  CD1 . LEU   A 1 334 ? -23.321 19.734  -1.754  1.00 29.16  ?  490 LEU   A CD1 1 
ATOM   2495 C  CD2 . LEU   A 1 334 ? -21.339 20.927  -0.853  1.00 32.62  ?  490 LEU   A CD2 1 
ATOM   2496 N  N   . PHE   A 1 335 ? -22.110 23.914  -5.429  1.00 32.45  ?  491 PHE   A N   1 
ATOM   2497 C  CA  . PHE   A 1 335 ? -21.759 24.265  -6.801  1.00 33.37  ?  491 PHE   A CA  1 
ATOM   2498 C  C   . PHE   A 1 335 ? -21.318 25.717  -6.962  1.00 38.04  ?  491 PHE   A C   1 
ATOM   2499 O  O   . PHE   A 1 335 ? -21.411 26.270  -8.063  1.00 38.54  ?  491 PHE   A O   1 
ATOM   2500 C  CB  . PHE   A 1 335 ? -22.914 23.940  -7.751  1.00 31.30  ?  491 PHE   A CB  1 
ATOM   2501 C  CG  . PHE   A 1 335 ? -22.992 22.495  -8.125  1.00 31.46  ?  491 PHE   A CG  1 
ATOM   2502 C  CD1 . PHE   A 1 335 ? -21.987 21.611  -7.738  1.00 29.00  ?  491 PHE   A CD1 1 
ATOM   2503 C  CD2 . PHE   A 1 335 ? -24.023 22.025  -8.925  1.00 29.10  ?  491 PHE   A CD2 1 
ATOM   2504 C  CE1 . PHE   A 1 335 ? -22.040 20.271  -8.108  1.00 28.69  ?  491 PHE   A CE1 1 
ATOM   2505 C  CE2 . PHE   A 1 335 ? -24.078 20.689  -9.299  1.00 27.53  ?  491 PHE   A CE2 1 
ATOM   2506 C  CZ  . PHE   A 1 335 ? -23.087 19.813  -8.896  1.00 31.74  ?  491 PHE   A CZ  1 
ATOM   2507 N  N   . SER   A 1 336 ? -20.799 26.342  -5.903  1.00 40.25  ?  492 SER   A N   1 
ATOM   2508 C  CA  . SER   A 1 336 ? -20.265 27.696  -6.039  1.00 41.07  ?  492 SER   A CA  1 
ATOM   2509 C  C   . SER   A 1 336 ? -19.131 27.725  -7.058  1.00 39.79  ?  492 SER   A C   1 
ATOM   2510 O  O   . SER   A 1 336 ? -18.382 26.760  -7.221  1.00 42.06  ?  492 SER   A O   1 
ATOM   2511 C  CB  . SER   A 1 336 ? -19.759 28.215  -4.690  1.00 36.62  ?  492 SER   A CB  1 
ATOM   2512 O  OG  . SER   A 1 336 ? -19.039 29.438  -4.821  1.00 48.12  ?  492 SER   A OG  1 
ATOM   2513 N  N   . SER   A 1 337 ? -18.998 28.851  -7.750  1.00 42.09  ?  493 SER   A N   1 
ATOM   2514 C  CA  . SER   A 1 337 ? -17.857 28.951  -8.643  1.00 43.35  ?  493 SER   A CA  1 
ATOM   2515 C  C   . SER   A 1 337 ? -16.545 29.133  -7.884  1.00 45.44  ?  493 SER   A C   1 
ATOM   2516 O  O   . SER   A 1 337 ? -15.482 28.965  -8.487  1.00 46.30  ?  493 SER   A O   1 
ATOM   2517 C  CB  . SER   A 1 337 ? -18.082 30.076  -9.658  1.00 43.53  ?  493 SER   A CB  1 
ATOM   2518 O  OG  . SER   A 1 337 ? -18.207 31.336  -9.033  1.00 51.11  ?  493 SER   A OG  1 
ATOM   2519 N  N   . ASN   A 1 338 ? -16.591 29.450  -6.581  1.00 49.88  ?  494 ASN   A N   1 
ATOM   2520 C  CA  . ASN   A 1 338 ? -15.387 29.427  -5.746  1.00 46.46  ?  494 ASN   A CA  1 
ATOM   2521 C  C   . ASN   A 1 338 ? -14.893 28.011  -5.494  1.00 45.57  ?  494 ASN   A C   1 
ATOM   2522 O  O   . ASN   A 1 338 ? -13.719 27.828  -5.149  1.00 51.74  ?  494 ASN   A O   1 
ATOM   2523 C  CB  . ASN   A 1 338 ? -15.646 30.133  -4.403  1.00 46.28  ?  494 ASN   A CB  1 
ATOM   2524 C  CG  . ASN   A 1 338 ? -15.978 31.611  -4.574  1.00 55.66  ?  494 ASN   A CG  1 
ATOM   2525 O  OD1 . ASN   A 1 338 ? -15.515 32.257  -5.523  1.00 64.13  ?  494 ASN   A OD1 1 
ATOM   2526 N  ND2 . ASN   A 1 338 ? -16.819 32.142  -3.689  1.00 56.10  ?  494 ASN   A ND2 1 
ATOM   2527 N  N   . LEU   A 1 339 ? -15.760 27.015  -5.654  1.00 41.43  ?  495 LEU   A N   1 
ATOM   2528 C  CA  . LEU   A 1 339 ? -15.402 25.620  -5.448  1.00 42.42  ?  495 LEU   A CA  1 
ATOM   2529 C  C   . LEU   A 1 339 ? -15.196 24.862  -6.757  1.00 46.22  ?  495 LEU   A C   1 
ATOM   2530 O  O   . LEU   A 1 339 ? -14.217 24.125  -6.892  1.00 47.73  ?  495 LEU   A O   1 
ATOM   2531 C  CB  . LEU   A 1 339 ? -16.482 24.933  -4.604  1.00 44.95  ?  495 LEU   A CB  1 
ATOM   2532 C  CG  . LEU   A 1 339 ? -16.680 25.512  -3.203  1.00 44.73  ?  495 LEU   A CG  1 
ATOM   2533 C  CD1 . LEU   A 1 339 ? -17.835 24.797  -2.501  1.00 40.48  ?  495 LEU   A CD1 1 
ATOM   2534 C  CD2 . LEU   A 1 339 ? -15.375 25.427  -2.387  1.00 42.55  ?  495 LEU   A CD2 1 
ATOM   2535 N  N   . ILE   A 1 340 ? -16.108 25.005  -7.722  1.00 40.92  ?  496 ILE   A N   1 
ATOM   2536 C  CA  . ILE   A 1 340 ? -16.001 24.309  -8.999  1.00 39.89  ?  496 ILE   A CA  1 
ATOM   2537 C  C   . ILE   A 1 340 ? -16.265 25.336  -10.097 1.00 45.78  ?  496 ILE   A C   1 
ATOM   2538 O  O   . ILE   A 1 340 ? -17.275 26.048  -10.050 1.00 43.23  ?  496 ILE   A O   1 
ATOM   2539 C  CB  . ILE   A 1 340 ? -17.001 23.138  -9.084  1.00 45.03  ?  496 ILE   A CB  1 
ATOM   2540 C  CG1 . ILE   A 1 340 ? -16.770 22.132  -7.956  1.00 43.76  ?  496 ILE   A CG1 1 
ATOM   2541 C  CG2 . ILE   A 1 340 ? -16.870 22.407  -10.407 1.00 41.57  ?  496 ILE   A CG2 1 
ATOM   2542 C  CD1 . ILE   A 1 340 ? -17.836 21.054  -7.862  1.00 38.10  ?  496 ILE   A CD1 1 
ATOM   2543 N  N   . ASP   A 1 341 ? -15.368 25.434  -11.072 1.00 43.27  ?  497 ASP   A N   1 
ATOM   2544 C  CA  . ASP   A 1 341 ? -15.582 26.509  -12.031 1.00 38.54  ?  497 ASP   A CA  1 
ATOM   2545 C  C   . ASP   A 1 341 ? -16.612 26.121  -13.107 1.00 46.29  ?  497 ASP   A C   1 
ATOM   2546 O  O   . ASP   A 1 341 ? -16.921 24.943  -13.328 1.00 39.15  ?  497 ASP   A O   1 
ATOM   2547 C  CB  . ASP   A 1 341 ? -14.263 26.943  -12.656 1.00 50.37  ?  497 ASP   A CB  1 
ATOM   2548 C  CG  . ASP   A 1 341 ? -13.592 25.849  -13.447 1.00 49.55  ?  497 ASP   A CG  1 
ATOM   2549 O  OD1 . ASP   A 1 341 ? -14.262 24.876  -13.850 1.00 56.23  ?  497 ASP   A OD1 1 
ATOM   2550 O  OD2 . ASP   A 1 341 ? -12.370 25.983  -13.684 1.00 64.69  -1 497 ASP   A OD2 1 
ATOM   2551 N  N   . LYS   A 1 342 ? -17.151 27.154  -13.769 1.00 45.78  ?  498 LYS   A N   1 
ATOM   2552 C  CA  . LYS   A 1 342 ? -18.265 26.961  -14.697 1.00 48.73  ?  498 LYS   A CA  1 
ATOM   2553 C  C   . LYS   A 1 342 ? -17.926 25.934  -15.772 1.00 42.15  ?  498 LYS   A C   1 
ATOM   2554 O  O   . LYS   A 1 342 ? -18.745 25.063  -16.084 1.00 40.88  ?  498 LYS   A O   1 
ATOM   2555 C  CB  . LYS   A 1 342 ? -18.658 28.303  -15.329 1.00 50.23  ?  498 LYS   A CB  1 
ATOM   2556 C  CG  . LYS   A 1 342 ? -19.625 28.187  -16.494 1.00 43.18  ?  498 LYS   A CG  1 
ATOM   2557 C  CD  . LYS   A 1 342 ? -21.052 28.118  -15.973 1.00 49.98  ?  498 LYS   A CD  1 
ATOM   2558 C  CE  . LYS   A 1 342 ? -22.050 28.628  -16.993 1.00 50.27  ?  498 LYS   A CE  1 
ATOM   2559 N  NZ  . LYS   A 1 342 ? -21.577 29.927  -17.557 1.00 56.08  ?  498 LYS   A NZ  1 
ATOM   2560 N  N   . ARG   A 1 343 ? -16.705 26.000  -16.316 1.00 41.26  ?  499 ARG   A N   1 
ATOM   2561 C  CA  . ARG   A 1 343 ? -16.305 25.091  -17.390 1.00 46.49  ?  499 ARG   A CA  1 
ATOM   2562 C  C   . ARG   A 1 343 ? -16.465 23.630  -16.984 1.00 44.46  ?  499 ARG   A C   1 
ATOM   2563 O  O   . ARG   A 1 343 ? -16.914 22.798  -17.780 1.00 43.16  ?  499 ARG   A O   1 
ATOM   2564 C  CB  . ARG   A 1 343 ? -14.858 25.378  -17.797 1.00 50.89  ?  499 ARG   A CB  1 
ATOM   2565 C  CG  . ARG   A 1 343 ? -14.286 24.358  -18.768 1.00 53.38  ?  499 ARG   A CG  1 
ATOM   2566 C  CD  . ARG   A 1 343 ? -14.864 24.502  -20.182 1.00 58.88  ?  499 ARG   A CD  1 
ATOM   2567 N  NE  . ARG   A 1 343 ? -15.648 23.340  -20.608 1.00 50.62  ?  499 ARG   A NE  1 
ATOM   2568 C  CZ  . ARG   A 1 343 ? -16.775 23.403  -21.311 1.00 64.35  ?  499 ARG   A CZ  1 
ATOM   2569 N  NH1 . ARG   A 1 343 ? -17.304 24.568  -21.673 1.00 56.08  ?  499 ARG   A NH1 1 
ATOM   2570 N  NH2 . ARG   A 1 343 ? -17.378 22.268  -21.682 1.00 54.66  ?  499 ARG   A NH2 1 
ATOM   2571 N  N   . SER   A 1 344 ? -16.103 23.293  -15.745 1.00 43.70  ?  500 SER   A N   1 
ATOM   2572 C  CA  . SER   A 1 344 ? -16.208 21.902  -15.320 1.00 36.98  ?  500 SER   A CA  1 
ATOM   2573 C  C   . SER   A 1 344 ? -17.660 21.449  -15.275 1.00 35.10  ?  500 SER   A C   1 
ATOM   2574 O  O   . SER   A 1 344 ? -17.981 20.321  -15.664 1.00 35.33  ?  500 SER   A O   1 
ATOM   2575 C  CB  . SER   A 1 344 ? -15.538 21.739  -13.957 1.00 39.66  ?  500 SER   A CB  1 
ATOM   2576 O  OG  . SER   A 1 344 ? -14.159 22.044  -14.079 1.00 44.16  ?  500 SER   A OG  1 
ATOM   2577 N  N   . LYS   A 1 345 ? -18.544 22.313  -14.785 1.00 34.19  ?  501 LYS   A N   1 
ATOM   2578 C  CA  . LYS   A 1 345 ? -19.955 21.976  -14.715 1.00 34.07  ?  501 LYS   A CA  1 
ATOM   2579 C  C   . LYS   A 1 345 ? -20.539 21.846  -16.118 1.00 36.72  ?  501 LYS   A C   1 
ATOM   2580 O  O   . LYS   A 1 345 ? -21.366 20.965  -16.373 1.00 33.65  ?  501 LYS   A O   1 
ATOM   2581 C  CB  . LYS   A 1 345 ? -20.677 23.057  -13.915 1.00 36.26  ?  501 LYS   A CB  1 
ATOM   2582 C  CG  . LYS   A 1 345 ? -20.223 23.173  -12.451 1.00 41.70  ?  501 LYS   A CG  1 
ATOM   2583 C  CD  . LYS   A 1 345 ? -20.771 24.470  -11.880 1.00 41.18  ?  501 LYS   A CD  1 
ATOM   2584 C  CE  . LYS   A 1 345 ? -19.962 24.923  -10.719 1.00 47.94  ?  501 LYS   A CE  1 
ATOM   2585 N  NZ  . LYS   A 1 345 ? -20.261 26.306  -10.220 1.00 45.07  ?  501 LYS   A NZ  1 
ATOM   2586 N  N   . GLU   A 1 346 ? -20.093 22.700  -17.050 1.00 34.62  ?  502 GLU   A N   1 
ATOM   2587 C  CA  . GLU   A 1 346 ? -20.579 22.616  -18.428 1.00 41.47  ?  502 GLU   A CA  1 
ATOM   2588 C  C   . GLU   A 1 346 ? -20.127 21.324  -19.097 1.00 35.06  ?  502 GLU   A C   1 
ATOM   2589 O  O   . GLU   A 1 346 ? -20.876 20.734  -19.892 1.00 36.91  ?  502 GLU   A O   1 
ATOM   2590 C  CB  . GLU   A 1 346 ? -20.111 23.842  -19.238 1.00 40.11  ?  502 GLU   A CB  1 
ATOM   2591 C  CG  . GLU   A 1 346 ? -20.846 25.127  -18.843 1.00 43.09  ?  502 GLU   A CG  1 
ATOM   2592 C  CD  . GLU   A 1 346 ? -20.302 26.397  -19.503 1.00 51.18  ?  502 GLU   A CD  1 
ATOM   2593 O  OE1 . GLU   A 1 346 ? -19.143 26.410  -19.974 1.00 47.15  ?  502 GLU   A OE1 1 
ATOM   2594 O  OE2 . GLU   A 1 346 ? -21.057 27.393  -19.543 1.00 59.07  -1 502 GLU   A OE2 1 
ATOM   2595 N  N   . PHE   A 1 347 ? -18.904 20.873  -18.795 1.00 35.44  ?  503 PHE   A N   1 
ATOM   2596 C  CA  . PHE   A 1 347 ? -18.426 19.617  -19.360 1.00 36.68  ?  503 PHE   A CA  1 
ATOM   2597 C  C   . PHE   A 1 347 ? -19.271 18.463  -18.848 1.00 35.54  ?  503 PHE   A C   1 
ATOM   2598 O  O   . PHE   A 1 347 ? -19.780 17.644  -19.626 1.00 38.03  ?  503 PHE   A O   1 
ATOM   2599 C  CB  . PHE   A 1 347 ? -16.950 19.396  -19.012 1.00 37.94  ?  503 PHE   A CB  1 
ATOM   2600 C  CG  . PHE   A 1 347 ? -16.374 18.105  -19.568 1.00 45.25  ?  503 PHE   A CG  1 
ATOM   2601 C  CD1 . PHE   A 1 347 ? -15.945 18.018  -20.887 1.00 44.96  ?  503 PHE   A CD1 1 
ATOM   2602 C  CD2 . PHE   A 1 347 ? -16.328 16.961  -18.790 1.00 46.31  ?  503 PHE   A CD2 1 
ATOM   2603 C  CE1 . PHE   A 1 347 ? -15.428 16.833  -21.390 1.00 47.31  ?  503 PHE   A CE1 1 
ATOM   2604 C  CE2 . PHE   A 1 347 ? -15.827 15.777  -19.296 1.00 47.96  ?  503 PHE   A CE2 1 
ATOM   2605 C  CZ  . PHE   A 1 347 ? -15.378 15.712  -20.596 1.00 44.32  ?  503 PHE   A CZ  1 
ATOM   2606 N  N   . LEU   A 1 348 ? -19.456 18.395  -17.528 1.00 35.23  ?  504 LEU   A N   1 
ATOM   2607 C  CA  . LEU   A 1 348 ? -20.264 17.315  -16.974 1.00 34.04  ?  504 LEU   A CA  1 
ATOM   2608 C  C   . LEU   A 1 348 ? -21.693 17.386  -17.514 1.00 32.07  ?  504 LEU   A C   1 
ATOM   2609 O  O   . LEU   A 1 348 ? -22.310 16.356  -17.826 1.00 31.54  ?  504 LEU   A O   1 
ATOM   2610 C  CB  . LEU   A 1 348 ? -20.238 17.386  -15.453 1.00 31.79  ?  504 LEU   A CB  1 
ATOM   2611 C  CG  . LEU   A 1 348 ? -20.977 16.320  -14.654 1.00 33.89  ?  504 LEU   A CG  1 
ATOM   2612 C  CD1 . LEU   A 1 348 ? -20.454 14.927  -15.010 1.00 36.44  ?  504 LEU   A CD1 1 
ATOM   2613 C  CD2 . LEU   A 1 348 ? -20.819 16.613  -13.172 1.00 29.17  ?  504 LEU   A CD2 1 
ATOM   2614 N  N   . THR   A 1 349 ? -22.222 18.602  -17.662 1.00 30.41  ?  505 THR   A N   1 
ATOM   2615 C  CA  . THR   A 1 349 ? -23.555 18.763  -18.225 1.00 31.91  ?  505 THR   A CA  1 
ATOM   2616 C  C   . THR   A 1 349 ? -23.631 18.147  -19.620 1.00 31.07  ?  505 THR   A C   1 
ATOM   2617 O  O   . THR   A 1 349 ? -24.546 17.370  -19.915 1.00 30.51  ?  505 THR   A O   1 
ATOM   2618 C  CB  . THR   A 1 349 ? -23.933 20.249  -18.245 1.00 36.77  ?  505 THR   A CB  1 
ATOM   2619 O  OG1 . THR   A 1 349 ? -24.124 20.716  -16.887 1.00 30.08  ?  505 THR   A OG1 1 
ATOM   2620 C  CG2 . THR   A 1 349 ? -25.201 20.498  -19.120 1.00 29.93  ?  505 THR   A CG2 1 
ATOM   2621 N  N   . LYS   A 1 350 ? -22.642 18.450  -20.469 1.00 33.06  ?  506 LYS   A N   1 
ATOM   2622 C  CA  . LYS   A 1 350 ? -22.616 17.941  -21.844 1.00 40.74  ?  506 LYS   A CA  1 
ATOM   2623 C  C   . LYS   A 1 350 ? -22.540 16.420  -21.875 1.00 35.03  ?  506 LYS   A C   1 
ATOM   2624 O  O   . LYS   A 1 350 ? -23.237 15.764  -22.664 1.00 33.74  ?  506 LYS   A O   1 
ATOM   2625 C  CB  . LYS   A 1 350 ? -21.414 18.552  -22.574 1.00 42.81  ?  506 LYS   A CB  1 
ATOM   2626 C  CG  . LYS   A 1 350 ? -21.273 18.199  -24.032 1.00 50.11  ?  506 LYS   A CG  1 
ATOM   2627 C  CD  . LYS   A 1 350 ? -19.978 18.833  -24.606 1.00 54.86  ?  506 LYS   A CD  1 
ATOM   2628 C  CE  . LYS   A 1 350 ? -18.763 18.625  -23.703 1.00 49.07  ?  506 LYS   A CE  1 
ATOM   2629 N  NZ  . LYS   A 1 350 ? -17.469 19.084  -24.319 1.00 57.00  ?  506 LYS   A NZ  1 
ATOM   2630 N  N   . GLN   A 1 351 ? -21.707 15.840  -21.004 1.00 35.79  ?  507 GLN   A N   1 
ATOM   2631 C  CA  . GLN   A 1 351 ? -21.493 14.399  -21.026 1.00 34.37  ?  507 GLN   A CA  1 
ATOM   2632 C  C   . GLN   A 1 351 ? -22.742 13.651  -20.582 1.00 36.25  ?  507 GLN   A C   1 
ATOM   2633 O  O   . GLN   A 1 351 ? -23.160 12.677  -21.225 1.00 33.42  ?  507 GLN   A O   1 
ATOM   2634 C  CB  . GLN   A 1 351 ? -20.306 14.029  -20.142 1.00 37.85  ?  507 GLN   A CB  1 
ATOM   2635 C  CG  . GLN   A 1 351 ? -18.995 14.534  -20.681 1.00 42.02  ?  507 GLN   A CG  1 
ATOM   2636 C  CD  . GLN   A 1 351 ? -18.766 14.064  -22.093 1.00 50.89  ?  507 GLN   A CD  1 
ATOM   2637 O  OE1 . GLN   A 1 351 ? -18.954 12.886  -22.410 1.00 58.10  ?  507 GLN   A OE1 1 
ATOM   2638 N  NE2 . GLN   A 1 351 ? -18.377 14.988  -22.965 1.00 51.40  ?  507 GLN   A NE2 1 
ATOM   2639 N  N   . ILE   A 1 352 ? -23.347 14.090  -19.474 1.00 30.07  ?  508 ILE   A N   1 
ATOM   2640 C  CA  . ILE   A 1 352 ? -24.577 13.462  -18.995 1.00 29.64  ?  508 ILE   A CA  1 
ATOM   2641 C  C   . ILE   A 1 352 ? -25.687 13.577  -20.051 1.00 29.79  ?  508 ILE   A C   1 
ATOM   2642 O  O   . ILE   A 1 352 ? -26.411 12.608  -20.324 1.00 30.05  ?  508 ILE   A O   1 
ATOM   2643 C  CB  . ILE   A 1 352 ? -24.984 14.087  -17.643 1.00 29.50  ?  508 ILE   A CB  1 
ATOM   2644 C  CG1 . ILE   A 1 352 ? -23.979 13.698  -16.528 1.00 29.21  ?  508 ILE   A CG1 1 
ATOM   2645 C  CG2 . ILE   A 1 352 ? -26.369 13.671  -17.231 1.00 28.72  ?  508 ILE   A CG2 1 
ATOM   2646 C  CD1 . ILE   A 1 352 ? -24.180 14.531  -15.219 1.00 28.34  ?  508 ILE   A CD1 1 
ATOM   2647 N  N   . GLU   A 1 353 ? -25.838 14.758  -20.664 1.00 30.21  ?  509 GLU   A N   1 
ATOM   2648 C  CA  . GLU   A 1 353 ? -26.863 14.925  -21.694 1.00 30.43  ?  509 GLU   A CA  1 
ATOM   2649 C  C   . GLU   A 1 353 ? -26.634 13.974  -22.862 1.00 30.37  ?  509 GLU   A C   1 
ATOM   2650 O  O   . GLU   A 1 353 ? -27.580 13.380  -23.383 1.00 29.92  ?  509 GLU   A O   1 
ATOM   2651 C  CB  . GLU   A 1 353 ? -26.912 16.380  -22.188 1.00 29.61  ?  509 GLU   A CB  1 
ATOM   2652 C  CG  . GLU   A 1 353 ? -27.600 17.324  -21.190 1.00 29.21  ?  509 GLU   A CG  1 
ATOM   2653 C  CD  . GLU   A 1 353 ? -27.615 18.764  -21.641 1.00 31.61  ?  509 GLU   A CD  1 
ATOM   2654 O  OE1 . GLU   A 1 353 ? -26.626 19.204  -22.275 1.00 29.27  ?  509 GLU   A OE1 1 
ATOM   2655 O  OE2 . GLU   A 1 353 ? -28.638 19.440  -21.362 1.00 29.20  -1 509 GLU   A OE2 1 
ATOM   2656 N  N   . TYR   A 1 354 ? -25.378 13.815  -23.273 1.00 32.24  ?  510 TYR   A N   1 
ATOM   2657 C  CA  . TYR   A 1 354 ? -25.052 12.825  -24.287 1.00 35.47  ?  510 TYR   A CA  1 
ATOM   2658 C  C   . TYR   A 1 354 ? -25.462 11.431  -23.825 1.00 37.80  ?  510 TYR   A C   1 
ATOM   2659 O  O   . TYR   A 1 354 ? -26.135 10.696  -24.557 1.00 38.22  ?  510 TYR   A O   1 
ATOM   2660 C  CB  . TYR   A 1 354 ? -23.559 12.875  -24.601 1.00 32.88  ?  510 TYR   A CB  1 
ATOM   2661 C  CG  . TYR   A 1 354 ? -23.105 11.771  -25.526 1.00 44.77  ?  510 TYR   A CG  1 
ATOM   2662 C  CD1 . TYR   A 1 354 ? -23.179 11.915  -26.910 1.00 40.28  ?  510 TYR   A CD1 1 
ATOM   2663 C  CD2 . TYR   A 1 354 ? -22.645 10.557  -25.012 1.00 48.82  ?  510 TYR   A CD2 1 
ATOM   2664 C  CE1 . TYR   A 1 354 ? -22.770 10.904  -27.749 1.00 47.53  ?  510 TYR   A CE1 1 
ATOM   2665 C  CE2 . TYR   A 1 354 ? -22.246 9.530   -25.857 1.00 53.34  ?  510 TYR   A CE2 1 
ATOM   2666 C  CZ  . TYR   A 1 354 ? -22.314 9.710   -27.216 1.00 46.35  ?  510 TYR   A CZ  1 
ATOM   2667 O  OH  . TYR   A 1 354 ? -21.912 8.691   -28.048 1.00 62.26  ?  510 TYR   A OH  1 
ATOM   2668 N  N   . GLU   A 1 355 ? -25.038 11.034  -22.615 1.00 35.56  ?  511 GLU   A N   1 
ATOM   2669 C  CA  . GLU   A 1 355 ? -25.405 9.710   -22.123 1.00 34.67  ?  511 GLU   A CA  1 
ATOM   2670 C  C   . GLU   A 1 355 ? -26.909 9.509   -22.166 1.00 35.47  ?  511 GLU   A C   1 
ATOM   2671 O  O   . GLU   A 1 355 ? -27.398 8.499   -22.692 1.00 35.64  ?  511 GLU   A O   1 
ATOM   2672 C  CB  . GLU   A 1 355 ? -24.881 9.499   -20.700 1.00 37.04  ?  511 GLU   A CB  1 
ATOM   2673 C  CG  . GLU   A 1 355 ? -23.378 9.357   -20.621 1.00 34.79  ?  511 GLU   A CG  1 
ATOM   2674 C  CD  . GLU   A 1 355 ? -22.886 8.154   -21.388 1.00 36.64  ?  511 GLU   A CD  1 
ATOM   2675 O  OE1 . GLU   A 1 355 ? -23.474 7.061   -21.245 1.00 40.07  ?  511 GLU   A OE1 1 
ATOM   2676 O  OE2 . GLU   A 1 355 ? -21.897 8.286   -22.115 1.00 42.45  -1 511 GLU   A OE2 1 
ATOM   2677 N  N   . ARG   A 1 356 ? -27.663 10.486  -21.657 1.00 30.45  ?  512 ARG   A N   1 
ATOM   2678 C  CA  . ARG   A 1 356 ? -29.108 10.327  -21.541 1.00 30.16  ?  512 ARG   A CA  1 
ATOM   2679 C  C   . ARG   A 1 356 ? -29.780 10.269  -22.909 1.00 35.55  ?  512 ARG   A C   1 
ATOM   2680 O  O   . ARG   A 1 356 ? -30.765 9.549   -23.087 1.00 41.33  ?  512 ARG   A O   1 
ATOM   2681 C  CB  . ARG   A 1 356 ? -29.679 11.464  -20.692 1.00 30.09  ?  512 ARG   A CB  1 
ATOM   2682 C  CG  . ARG   A 1 356 ? -31.131 11.340  -20.234 1.00 29.34  ?  512 ARG   A CG  1 
ATOM   2683 C  CD  . ARG   A 1 356 ? -32.063 12.251  -21.033 1.00 33.12  ?  512 ARG   A CD  1 
ATOM   2684 N  NE  . ARG   A 1 356 ? -31.708 13.649  -20.819 1.00 31.21  ?  512 ARG   A NE  1 
ATOM   2685 C  CZ  . ARG   A 1 356 ? -32.091 14.380  -19.780 1.00 28.92  ?  512 ARG   A CZ  1 
ATOM   2686 N  NH1 . ARG   A 1 356 ? -32.932 13.908  -18.870 1.00 28.99  ?  512 ARG   A NH1 1 
ATOM   2687 N  NH2 . ARG   A 1 356 ? -31.606 15.612  -19.641 1.00 28.35  ?  512 ARG   A NH2 1 
ATOM   2688 N  N   . ASN   A 1 357 ? -29.260 11.011  -23.894 1.00 34.38  ?  513 ASN   A N   1 
ATOM   2689 C  CA  . ASN   A 1 357 ? -29.810 10.930  -25.248 1.00 33.41  ?  513 ASN   A CA  1 
ATOM   2690 C  C   . ASN   A 1 357 ? -29.504 9.603   -25.927 1.00 39.58  ?  513 ASN   A C   1 
ATOM   2691 O  O   . ASN   A 1 357 ? -30.210 9.233   -26.881 1.00 37.45  ?  513 ASN   A O   1 
ATOM   2692 C  CB  . ASN   A 1 357 ? -29.276 12.084  -26.101 1.00 33.78  ?  513 ASN   A CB  1 
ATOM   2693 C  CG  . ASN   A 1 357 ? -29.997 13.374  -25.823 1.00 32.67  ?  513 ASN   A CG  1 
ATOM   2694 O  OD1 . ASN   A 1 357 ? -31.180 13.346  -25.522 1.00 34.72  ?  513 ASN   A OD1 1 
ATOM   2695 N  ND2 . ASN   A 1 357 ? -29.284 14.499  -25.850 1.00 32.31  ?  513 ASN   A ND2 1 
ATOM   2696 N  N   . ASN   A 1 358 ? -28.479 8.877   -25.455 1.00 35.71  ?  514 ASN   A N   1 
ATOM   2697 C  CA  . ASN   A 1 358 ? -28.013 7.671   -26.122 1.00 36.53  ?  514 ASN   A CA  1 
ATOM   2698 C  C   . ASN   A 1 358 ? -28.237 6.418   -25.280 1.00 39.36  ?  514 ASN   A C   1 
ATOM   2699 O  O   . ASN   A 1 358 ? -27.584 5.396   -25.498 1.00 37.67  ?  514 ASN   A O   1 
ATOM   2700 C  CB  . ASN   A 1 358 ? -26.551 7.823   -26.529 1.00 36.06  ?  514 ASN   A CB  1 
ATOM   2701 C  CG  . ASN   A 1 358 ? -26.365 8.837   -27.672 1.00 39.16  ?  514 ASN   A CG  1 
ATOM   2702 O  OD1 . ASN   A 1 358 ? -26.604 8.524   -28.842 1.00 41.41  ?  514 ASN   A OD1 1 
ATOM   2703 N  ND2 . ASN   A 1 358 ? -25.927 10.044  -27.335 1.00 36.74  ?  514 ASN   A ND2 1 
ATOM   2704 N  N   . GLU   A 1 359 ? -29.196 6.484   -24.352 1.00 34.75  ?  515 GLU   A N   1 
ATOM   2705 C  CA  . GLU   A 1 359 ? -29.545 5.380   -23.455 1.00 43.87  ?  515 GLU   A CA  1 
ATOM   2706 C  C   . GLU   A 1 359 ? -28.348 4.894   -22.645 1.00 44.82  ?  515 GLU   A C   1 
ATOM   2707 O  O   . GLU   A 1 359 ? -28.162 3.690   -22.425 1.00 46.03  ?  515 GLU   A O   1 
ATOM   2708 C  CB  . GLU   A 1 359 ? -30.204 4.235   -24.213 1.00 47.68  ?  515 GLU   A CB  1 
ATOM   2709 C  CG  . GLU   A 1 359 ? -31.332 4.701   -25.104 1.00 48.26  ?  515 GLU   A CG  1 
ATOM   2710 C  CD  . GLU   A 1 359 ? -32.110 3.541   -25.671 1.00 58.69  ?  515 GLU   A CD  1 
ATOM   2711 O  OE1 . GLU   A 1 359 ? -31.538 2.434   -25.707 1.00 61.49  ?  515 GLU   A OE1 1 
ATOM   2712 O  OE2 . GLU   A 1 359 ? -33.303 3.719   -26.014 1.00 58.50  -1 515 GLU   A OE2 1 
ATOM   2713 N  N   . PHE   A 1 360 ? -27.546 5.850   -22.192 1.00 36.03  ?  516 PHE   A N   1 
ATOM   2714 C  CA  . PHE   A 1 360 ? -26.463 5.618   -21.254 1.00 39.73  ?  516 PHE   A CA  1 
ATOM   2715 C  C   . PHE   A 1 360 ? -25.523 4.507   -21.680 1.00 44.34  ?  516 PHE   A C   1 
ATOM   2716 O  O   . PHE   A 1 360 ? -25.415 3.467   -21.032 1.00 47.38  ?  516 PHE   A O   1 
ATOM   2717 C  CB  . PHE   A 1 360 ? -27.047 5.322   -19.854 1.00 38.98  ?  516 PHE   A CB  1 
ATOM   2718 C  CG  . PHE   A 1 360 ? -27.927 6.421   -19.355 1.00 35.17  ?  516 PHE   A CG  1 
ATOM   2719 C  CD1 . PHE   A 1 360 ? -27.379 7.553   -18.776 1.00 37.17  ?  516 PHE   A CD1 1 
ATOM   2720 C  CD2 . PHE   A 1 360 ? -29.299 6.331   -19.465 1.00 36.66  ?  516 PHE   A CD2 1 
ATOM   2721 C  CE1 . PHE   A 1 360 ? -28.186 8.571   -18.313 1.00 33.16  ?  516 PHE   A CE1 1 
ATOM   2722 C  CE2 . PHE   A 1 360 ? -30.116 7.354   -18.993 1.00 37.40  ?  516 PHE   A CE2 1 
ATOM   2723 C  CZ  . PHE   A 1 360 ? -29.553 8.475   -18.421 1.00 32.12  ?  516 PHE   A CZ  1 
ATOM   2724 N  N   . PRO   A 1 361 ? -24.808 4.699   -22.808 1.00 39.42  ?  517 PRO   A N   1 
ATOM   2725 C  CA  . PRO   A 1 361 ? -23.761 3.737   -23.180 1.00 39.85  ?  517 PRO   A CA  1 
ATOM   2726 C  C   . PRO   A 1 361 ? -22.711 3.546   -22.100 1.00 44.30  ?  517 PRO   A C   1 
ATOM   2727 O  O   . PRO   A 1 361 ? -22.166 2.443   -21.968 1.00 42.56  ?  517 PRO   A O   1 
ATOM   2728 C  CB  . PRO   A 1 361 ? -23.159 4.348   -24.459 1.00 44.13  ?  517 PRO   A CB  1 
ATOM   2729 C  CG  . PRO   A 1 361 ? -23.543 5.810   -24.423 1.00 42.96  ?  517 PRO   A CG  1 
ATOM   2730 C  CD  . PRO   A 1 361 ? -24.891 5.830   -23.749 1.00 41.53  ?  517 PRO   A CD  1 
ATOM   2731 N  N   . VAL   A 1 362 ? -22.429 4.579   -21.300 1.00 42.04  ?  518 VAL   A N   1 
ATOM   2732 C  CA  . VAL   A 1 362 ? -21.374 4.471   -20.295 1.00 40.99  ?  518 VAL   A CA  1 
ATOM   2733 C  C   . VAL   A 1 362 ? -21.670 3.362   -19.300 1.00 40.96  ?  518 VAL   A C   1 
ATOM   2734 O  O   . VAL   A 1 362 ? -20.745 2.817   -18.695 1.00 51.72  ?  518 VAL   A O   1 
ATOM   2735 C  CB  . VAL   A 1 362 ? -21.176 5.810   -19.562 1.00 40.46  ?  518 VAL   A CB  1 
ATOM   2736 C  CG1 . VAL   A 1 362 ? -22.193 5.937   -18.448 1.00 39.45  ?  518 VAL   A CG1 1 
ATOM   2737 C  CG2 . VAL   A 1 362 ? -19.752 5.925   -19.023 1.00 42.26  ?  518 VAL   A CG2 1 
ATOM   2738 N  N   . PHE   A 1 363 ? -22.938 2.981   -19.141 1.00 39.64  ?  519 PHE   A N   1 
ATOM   2739 C  CA  . PHE   A 1 363 ? -23.253 1.921   -18.192 1.00 48.36  ?  519 PHE   A CA  1 
ATOM   2740 C  C   . PHE   A 1 363 ? -22.586 0.607   -18.584 1.00 59.06  ?  519 PHE   A C   1 
ATOM   2741 O  O   . PHE   A 1 363 ? -22.055 -0.112  -17.723 1.00 59.03  ?  519 PHE   A O   1 
ATOM   2742 C  CB  . PHE   A 1 363 ? -24.766 1.761   -18.064 1.00 40.80  ?  519 PHE   A CB  1 
ATOM   2743 C  CG  . PHE   A 1 363 ? -25.393 2.803   -17.187 1.00 40.10  ?  519 PHE   A CG  1 
ATOM   2744 C  CD1 . PHE   A 1 363 ? -24.594 3.631   -16.418 1.00 42.02  ?  519 PHE   A CD1 1 
ATOM   2745 C  CD2 . PHE   A 1 363 ? -26.768 2.925   -17.099 1.00 37.23  ?  519 PHE   A CD2 1 
ATOM   2746 C  CE1 . PHE   A 1 363 ? -25.158 4.600   -15.594 1.00 42.72  ?  519 PHE   A CE1 1 
ATOM   2747 C  CE2 . PHE   A 1 363 ? -27.343 3.876   -16.280 1.00 35.71  ?  519 PHE   A CE2 1 
ATOM   2748 C  CZ  . PHE   A 1 363 ? -26.538 4.716   -15.521 1.00 35.15  ?  519 PHE   A CZ  1 
ATOM   2749 N  N   . ASP   A 1 364 ? -22.573 0.290   -19.875 1.00 58.61  ?  520 ASP   A N   1 
ATOM   2750 C  CA  . ASP   A 1 364 ? -21.859 -0.899  -20.324 1.00 63.35  ?  520 ASP   A CA  1 
ATOM   2751 C  C   . ASP   A 1 364 ? -20.410 -0.585  -20.683 1.00 57.25  ?  520 ASP   A C   1 
ATOM   2752 O  O   . ASP   A 1 364 ? -19.988 -0.781  -21.818 1.00 64.65  ?  520 ASP   A O   1 
ATOM   2753 C  CB  . ASP   A 1 364 ? -22.572 -1.534  -21.508 1.00 58.18  ?  520 ASP   A CB  1 
ATOM   2754 C  CG  . ASP   A 1 364 ? -22.793 -3.017  -21.306 1.00 72.32  ?  520 ASP   A CG  1 
ATOM   2755 O  OD1 . ASP   A 1 364 ? -21.857 -3.700  -20.828 1.00 71.06  ?  520 ASP   A OD1 1 
ATOM   2756 O  OD2 . ASP   A 1 364 ? -23.896 -3.503  -21.627 1.00 76.89  -1 520 ASP   A OD2 1 
ATOM   2757 N  N   . GLY   B 1 5   ? -75.124 10.502  17.383  1.00 60.24  ?  161 GLY   B N   1 
ATOM   2758 C  CA  . GLY   B 1 5   ? -74.657 11.465  18.367  1.00 54.75  ?  161 GLY   B CA  1 
ATOM   2759 C  C   . GLY   B 1 5   ? -73.151 11.654  18.309  1.00 52.32  ?  161 GLY   B C   1 
ATOM   2760 O  O   . GLY   B 1 5   ? -72.475 11.730  19.341  1.00 53.56  ?  161 GLY   B O   1 
ATOM   2761 N  N   . ALA   B 1 6   ? -72.615 11.709  17.090  1.00 50.66  ?  162 ALA   B N   1 
ATOM   2762 C  CA  . ALA   B 1 6   ? -71.181 11.923  16.934  1.00 56.61  ?  162 ALA   B CA  1 
ATOM   2763 C  C   . ALA   B 1 6   ? -70.778 13.297  17.455  1.00 54.99  ?  162 ALA   B C   1 
ATOM   2764 O  O   . ALA   B 1 6   ? -69.738 13.441  18.114  1.00 45.91  ?  162 ALA   B O   1 
ATOM   2765 C  CB  . ALA   B 1 6   ? -70.778 11.759  15.467  1.00 39.91  ?  162 ALA   B CB  1 
ATOM   2766 N  N   . SER   B 1 7   ? -71.606 14.314  17.191  1.00 45.07  ?  163 SER   B N   1 
ATOM   2767 C  CA  . SER   B 1 7   ? -71.305 15.647  17.699  1.00 51.04  ?  163 SER   B CA  1 
ATOM   2768 C  C   . SER   B 1 7   ? -71.228 15.656  19.224  1.00 43.49  ?  163 SER   B C   1 
ATOM   2769 O  O   . SER   B 1 7   ? -70.534 16.498  19.795  1.00 42.05  ?  163 SER   B O   1 
ATOM   2770 C  CB  . SER   B 1 7   ? -72.354 16.655  17.223  1.00 42.15  ?  163 SER   B CB  1 
ATOM   2771 O  OG  . SER   B 1 7   ? -73.619 16.350  17.781  1.00 47.89  ?  163 SER   B OG  1 
ATOM   2772 N  N   . LYS   B 1 8   ? -71.945 14.748  19.892  1.00 41.00  ?  164 LYS   B N   1 
ATOM   2773 C  CA  . LYS   B 1 8   ? -71.800 14.609  21.340  1.00 49.50  ?  164 LYS   B CA  1 
ATOM   2774 C  C   . LYS   B 1 8   ? -70.385 14.175  21.706  1.00 45.80  ?  164 LYS   B C   1 
ATOM   2775 O  O   . LYS   B 1 8   ? -69.776 14.718  22.636  1.00 43.87  ?  164 LYS   B O   1 
ATOM   2776 C  CB  . LYS   B 1 8   ? -72.828 13.614  21.889  1.00 47.34  ?  164 LYS   B CB  1 
ATOM   2777 C  CG  . LYS   B 1 8   ? -74.230 14.205  22.050  1.00 52.58  ?  164 LYS   B CG  1 
ATOM   2778 C  CD  . LYS   B 1 8   ? -75.185 13.283  22.832  1.00 51.94  ?  164 LYS   B CD  1 
ATOM   2779 C  CE  . LYS   B 1 8   ? -76.465 13.009  22.014  1.00 60.12  ?  164 LYS   B CE  1 
ATOM   2780 N  NZ  . LYS   B 1 8   ? -77.716 12.836  22.845  1.00 45.33  ?  164 LYS   B NZ  1 
ATOM   2781 N  N   . LEU   B 1 9   ? -69.847 13.196  20.978  1.00 38.15  ?  165 LEU   B N   1 
ATOM   2782 C  CA  . LEU   B 1 9   ? -68.466 12.779  21.182  1.00 39.75  ?  165 LEU   B CA  1 
ATOM   2783 C  C   . LEU   B 1 9   ? -67.524 13.974  21.123  1.00 42.73  ?  165 LEU   B C   1 
ATOM   2784 O  O   . LEU   B 1 9   ? -66.655 14.147  21.986  1.00 34.86  ?  165 LEU   B O   1 
ATOM   2785 C  CB  . LEU   B 1 9   ? -68.076 11.752  20.123  1.00 36.57  ?  165 LEU   B CB  1 
ATOM   2786 C  CG  . LEU   B 1 9   ? -68.938 10.495  20.151  1.00 40.64  ?  165 LEU   B CG  1 
ATOM   2787 C  CD1 . LEU   B 1 9   ? -68.490 9.547   19.037  1.00 34.14  ?  165 LEU   B CD1 1 
ATOM   2788 C  CD2 . LEU   B 1 9   ? -68.928 9.821   21.517  1.00 35.24  ?  165 LEU   B CD2 1 
ATOM   2789 N  N   . ARG   B 1 10  ? -67.702 14.826  20.113  1.00 41.33  ?  166 ARG   B N   1 
ATOM   2790 C  CA  . ARG   B 1 10  ? -66.832 15.989  19.971  1.00 39.09  ?  166 ARG   B CA  1 
ATOM   2791 C  C   . ARG   B 1 10  ? -66.967 16.932  21.162  1.00 39.52  ?  166 ARG   B C   1 
ATOM   2792 O  O   . ARG   B 1 10  ? -65.962 17.466  21.651  1.00 38.30  ?  166 ARG   B O   1 
ATOM   2793 C  CB  . ARG   B 1 10  ? -67.136 16.723  18.664  1.00 43.37  ?  166 ARG   B CB  1 
ATOM   2794 N  N   . ALA   B 1 11  ? -68.196 17.150  21.644  1.00 38.24  ?  167 ALA   B N   1 
ATOM   2795 C  CA  . ALA   B 1 11  ? -68.389 17.976  22.840  1.00 43.92  ?  167 ALA   B CA  1 
ATOM   2796 C  C   . ALA   B 1 11  ? -67.577 17.446  24.018  1.00 42.00  ?  167 ALA   B C   1 
ATOM   2797 O  O   . ALA   B 1 11  ? -66.974 18.219  24.781  1.00 39.60  ?  167 ALA   B O   1 
ATOM   2798 C  CB  . ALA   B 1 11  ? -69.872 18.030  23.204  1.00 39.86  ?  167 ALA   B CB  1 
ATOM   2799 N  N   . VAL   B 1 12  ? -67.568 16.122  24.182  1.00 39.10  ?  168 VAL   B N   1 
ATOM   2800 C  CA  . VAL   B 1 12  ? -66.768 15.478  25.220  1.00 36.78  ?  168 VAL   B CA  1 
ATOM   2801 C  C   . VAL   B 1 12  ? -65.294 15.820  25.041  1.00 36.52  ?  168 VAL   B C   1 
ATOM   2802 O  O   . VAL   B 1 12  ? -64.622 16.287  25.971  1.00 42.65  ?  168 VAL   B O   1 
ATOM   2803 C  CB  . VAL   B 1 12  ? -66.997 13.955  25.182  1.00 35.80  ?  168 VAL   B CB  1 
ATOM   2804 C  CG1 . VAL   B 1 12  ? -66.002 13.234  26.094  1.00 40.94  ?  168 VAL   B CG1 1 
ATOM   2805 C  CG2 . VAL   B 1 12  ? -68.442 13.643  25.529  1.00 36.59  ?  168 VAL   B CG2 1 
ATOM   2806 N  N   . LEU   B 1 13  ? -64.771 15.569  23.840  1.00 34.25  ?  169 LEU   B N   1 
ATOM   2807 C  CA  . LEU   B 1 13  ? -63.363 15.806  23.552  1.00 34.47  ?  169 LEU   B CA  1 
ATOM   2808 C  C   . LEU   B 1 13  ? -63.003 17.269  23.775  1.00 41.17  ?  169 LEU   B C   1 
ATOM   2809 O  O   . LEU   B 1 13  ? -61.902 17.591  24.242  1.00 42.69  ?  169 LEU   B O   1 
ATOM   2810 C  CB  . LEU   B 1 13  ? -63.076 15.412  22.108  1.00 36.05  ?  169 LEU   B CB  1 
ATOM   2811 C  CG  . LEU   B 1 13  ? -63.198 13.912  21.818  1.00 34.03  ?  169 LEU   B CG  1 
ATOM   2812 C  CD1 . LEU   B 1 13  ? -63.208 13.691  20.336  1.00 36.69  ?  169 LEU   B CD1 1 
ATOM   2813 C  CD2 . LEU   B 1 13  ? -62.075 13.149  22.458  1.00 32.90  ?  169 LEU   B CD2 1 
ATOM   2814 N  N   . GLU   B 1 14  ? -63.917 18.167  23.422  1.00 38.77  ?  170 GLU   B N   1 
ATOM   2815 C  CA  . GLU   B 1 14  ? -63.704 19.584  23.669  1.00 47.60  ?  170 GLU   B CA  1 
ATOM   2816 C  C   . GLU   B 1 14  ? -63.510 19.844  25.158  1.00 45.88  ?  170 GLU   B C   1 
ATOM   2817 O  O   . GLU   B 1 14  ? -62.538 20.493  25.563  1.00 51.74  ?  170 GLU   B O   1 
ATOM   2818 C  CB  . GLU   B 1 14  ? -64.887 20.386  23.117  1.00 43.38  ?  170 GLU   B CB  1 
ATOM   2819 C  CG  . GLU   B 1 14  ? -64.638 21.058  21.764  1.00 55.31  ?  170 GLU   B CG  1 
ATOM   2820 C  CD  . GLU   B 1 14  ? -63.267 21.733  21.672  1.00 67.35  ?  170 GLU   B CD  1 
ATOM   2821 O  OE1 . GLU   B 1 14  ? -62.547 21.501  20.669  1.00 67.69  ?  170 GLU   B OE1 1 
ATOM   2822 O  OE2 . GLU   B 1 14  ? -62.905 22.479  22.620  1.00 66.42  -1 170 GLU   B OE2 1 
ATOM   2823 N  N   . LYS   B 1 15  ? -64.404 19.297  25.990  1.00 42.30  ?  171 LYS   B N   1 
ATOM   2824 C  CA  . LYS   B 1 15  ? -64.339 19.544  27.429  1.00 47.71  ?  171 LYS   B CA  1 
ATOM   2825 C  C   . LYS   B 1 15  ? -63.087 18.928  28.047  1.00 55.23  ?  171 LYS   B C   1 
ATOM   2826 O  O   . LYS   B 1 15  ? -62.485 19.508  28.962  1.00 57.92  ?  171 LYS   B O   1 
ATOM   2827 C  CB  . LYS   B 1 15  ? -65.589 19.000  28.118  1.00 49.50  ?  171 LYS   B CB  1 
ATOM   2828 N  N   . LEU   B 1 16  ? -62.684 17.749  27.567  1.00 51.44  ?  172 LEU   B N   1 
ATOM   2829 C  CA  . LEU   B 1 16  ? -61.486 17.109  28.102  1.00 56.15  ?  172 LEU   B CA  1 
ATOM   2830 C  C   . LEU   B 1 16  ? -60.255 17.963  27.830  1.00 57.89  ?  172 LEU   B C   1 
ATOM   2831 O  O   . LEU   B 1 16  ? -59.378 18.098  28.693  1.00 51.99  ?  172 LEU   B O   1 
ATOM   2832 C  CB  . LEU   B 1 16  ? -61.309 15.707  27.503  1.00 44.32  ?  172 LEU   B CB  1 
ATOM   2833 C  CG  . LEU   B 1 16  ? -62.345 14.648  27.908  1.00 46.71  ?  172 LEU   B CG  1 
ATOM   2834 C  CD1 . LEU   B 1 16  ? -62.169 13.353  27.132  1.00 41.08  ?  172 LEU   B CD1 1 
ATOM   2835 C  CD2 . LEU   B 1 16  ? -62.321 14.392  29.395  1.00 50.05  ?  172 LEU   B CD2 1 
ATOM   2836 N  N   . LYS   B 1 17  ? -60.184 18.552  26.633  1.00 58.04  ?  173 LYS   B N   1 
ATOM   2837 C  CA  . LYS   B 1 17  ? -59.055 19.402  26.268  1.00 56.70  ?  173 LYS   B CA  1 
ATOM   2838 C  C   . LYS   B 1 17  ? -58.986 20.636  27.162  1.00 60.87  ?  173 LYS   B C   1 
ATOM   2839 O  O   . LYS   B 1 17  ? -57.908 21.022  27.630  1.00 61.79  ?  173 LYS   B O   1 
ATOM   2840 C  CB  . LYS   B 1 17  ? -59.158 19.807  24.795  1.00 55.58  ?  173 LYS   B CB  1 
ATOM   2841 N  N   . LEU   B 1 18  ? -60.131 21.268  27.417  1.00 55.45  ?  174 LEU   B N   1 
ATOM   2842 C  CA  . LEU   B 1 18  ? -60.123 22.433  28.290  1.00 59.90  ?  174 LEU   B CA  1 
ATOM   2843 C  C   . LEU   B 1 18  ? -59.706 22.048  29.702  1.00 65.52  ?  174 LEU   B C   1 
ATOM   2844 O  O   . LEU   B 1 18  ? -58.978 22.796  30.366  1.00 66.83  ?  174 LEU   B O   1 
ATOM   2845 C  CB  . LEU   B 1 18  ? -61.495 23.098  28.301  1.00 61.58  ?  174 LEU   B CB  1 
ATOM   2846 C  CG  . LEU   B 1 18  ? -61.699 24.113  27.181  1.00 67.64  ?  174 LEU   B CG  1 
ATOM   2847 C  CD1 . LEU   B 1 18  ? -63.186 24.389  26.996  1.00 65.10  ?  174 LEU   B CD1 1 
ATOM   2848 C  CD2 . LEU   B 1 18  ? -60.917 25.399  27.458  1.00 63.99  ?  174 LEU   B CD2 1 
ATOM   2849 N  N   . SER   B 1 19  ? -60.149 20.877  30.173  1.00 64.27  ?  175 SER   B N   1 
ATOM   2850 C  CA  . SER   B 1 19  ? -59.789 20.436  31.520  1.00 71.09  ?  175 SER   B CA  1 
ATOM   2851 C  C   . SER   B 1 19  ? -58.283 20.247  31.646  1.00 67.40  ?  175 SER   B C   1 
ATOM   2852 O  O   . SER   B 1 19  ? -57.686 20.590  32.673  1.00 74.64  ?  175 SER   B O   1 
ATOM   2853 C  CB  . SER   B 1 19  ? -60.527 19.139  31.868  1.00 71.89  ?  175 SER   B CB  1 
ATOM   2854 O  OG  . SER   B 1 19  ? -61.934 19.328  31.851  1.00 77.37  ?  175 SER   B OG  1 
ATOM   2855 N  N   . ARG   B 1 20  ? -57.649 19.726  30.595  1.00 70.67  ?  176 ARG   B N   1 
ATOM   2856 C  CA  . ARG   B 1 20  ? -56.201 19.548  30.623  1.00 71.12  ?  176 ARG   B CA  1 
ATOM   2857 C  C   . ARG   B 1 20  ? -55.471 20.884  30.557  1.00 70.87  ?  176 ARG   B C   1 
ATOM   2858 O  O   . ARG   B 1 20  ? -54.517 21.111  31.310  1.00 76.78  ?  176 ARG   B O   1 
ATOM   2859 C  CB  . ARG   B 1 20  ? -55.762 18.645  29.471  1.00 63.73  ?  176 ARG   B CB  1 
ATOM   2860 N  N   . ASP   B 1 21  ? -55.915 21.785  29.675  1.00 71.45  ?  177 ASP   B N   1 
ATOM   2861 C  CA  . ASP   B 1 21  ? -55.165 23.012  29.419  1.00 73.99  ?  177 ASP   B CA  1 
ATOM   2862 C  C   . ASP   B 1 21  ? -55.131 23.923  30.639  1.00 70.42  ?  177 ASP   B C   1 
ATOM   2863 O  O   . ASP   B 1 21  ? -54.118 24.585  30.894  1.00 82.95  ?  177 ASP   B O   1 
ATOM   2864 C  CB  . ASP   B 1 21  ? -55.762 23.754  28.225  1.00 73.84  ?  177 ASP   B CB  1 
ATOM   2865 C  CG  . ASP   B 1 21  ? -55.504 23.040  26.919  1.00 80.93  ?  177 ASP   B CG  1 
ATOM   2866 O  OD1 . ASP   B 1 21  ? -54.682 22.095  26.920  1.00 81.62  ?  177 ASP   B OD1 1 
ATOM   2867 O  OD2 . ASP   B 1 21  ? -56.118 23.422  25.895  1.00 91.29  -1 177 ASP   B OD2 1 
ATOM   2868 N  N   . ASP   B 1 22  ? -56.225 23.990  31.393  1.00 75.89  ?  178 ASP   B N   1 
ATOM   2869 C  CA  . ASP   B 1 22  ? -56.262 24.839  32.572  1.00 72.17  ?  178 ASP   B CA  1 
ATOM   2870 C  C   . ASP   B 1 22  ? -55.646 24.160  33.791  1.00 75.31  ?  178 ASP   B C   1 
ATOM   2871 O  O   . ASP   B 1 22  ? -55.709 24.711  34.896  1.00 68.69  ?  178 ASP   B O   1 
ATOM   2872 C  CB  . ASP   B 1 22  ? -57.705 25.270  32.865  1.00 79.64  ?  178 ASP   B CB  1 
ATOM   2873 N  N   . ILE   B 1 23  ? -55.057 22.982  33.606  1.00 78.37  ?  179 ILE   B N   1 
ATOM   2874 C  CA  . ILE   B 1 23  ? -54.436 22.228  34.687  1.00 74.35  ?  179 ILE   B CA  1 
ATOM   2875 C  C   . ILE   B 1 23  ? -53.169 21.541  34.187  1.00 79.12  ?  179 ILE   B C   1 
ATOM   2876 O  O   . ILE   B 1 23  ? -52.129 21.590  34.851  1.00 79.46  ?  179 ILE   B O   1 
ATOM   2877 C  CB  . ILE   B 1 23  ? -55.416 21.196  35.293  1.00 74.80  ?  179 ILE   B CB  1 
ATOM   2878 C  CG1 . ILE   B 1 23  ? -56.644 21.897  35.891  1.00 77.99  ?  179 ILE   B CG1 1 
ATOM   2879 C  CG2 . ILE   B 1 23  ? -54.715 20.323  36.333  1.00 77.93  ?  179 ILE   B CG2 1 
ATOM   2880 C  CD1 . ILE   B 1 23  ? -57.744 20.960  36.349  1.00 78.65  ?  179 ILE   B CD1 1 
ATOM   2881 N  N   . THR   B 1 25  ? -50.278 23.607  34.596  1.00 70.00  ?  181 THR   B N   1 
ATOM   2882 C  CA  . THR   B 1 25  ? -49.877 24.332  35.796  1.00 67.23  ?  181 THR   B CA  1 
ATOM   2883 C  C   . THR   B 1 25  ? -49.534 23.365  36.919  1.00 76.22  ?  181 THR   B C   1 
ATOM   2884 O  O   . THR   B 1 25  ? -48.468 23.454  37.542  1.00 73.18  ?  181 THR   B O   1 
ATOM   2885 C  CB  . THR   B 1 25  ? -50.985 25.270  36.300  1.00 70.87  ?  181 THR   B CB  1 
ATOM   2886 O  OG1 . THR   B 1 25  ? -51.338 26.196  35.265  1.00 73.35  ?  181 THR   B OG1 1 
ATOM   2887 C  CG2 . THR   B 1 25  ? -50.495 26.048  37.524  1.00 55.95  ?  181 THR   B CG2 1 
ATOM   2888 N  N   . ALA   B 1 26  ? -50.480 22.463  37.188  1.00 75.76  ?  182 ALA   B N   1 
ATOM   2889 C  CA  . ALA   B 1 26  ? -50.266 21.429  38.192  1.00 73.65  ?  182 ALA   B CA  1 
ATOM   2890 C  C   . ALA   B 1 26  ? -49.018 20.618  37.872  1.00 67.40  ?  182 ALA   B C   1 
ATOM   2891 O  O   . ALA   B 1 26  ? -48.194 20.355  38.756  1.00 77.35  ?  182 ALA   B O   1 
ATOM   2892 C  CB  . ALA   B 1 26  ? -51.493 20.521  38.270  1.00 68.71  ?  182 ALA   B CB  1 
ATOM   2893 N  N   . ALA   B 1 27  ? -48.848 20.253  36.598  1.00 67.44  ?  183 ALA   B N   1 
ATOM   2894 C  CA  . ALA   B 1 27  ? -47.706 19.441  36.186  1.00 66.69  ?  183 ALA   B CA  1 
ATOM   2895 C  C   . ALA   B 1 27  ? -46.383 20.115  36.515  1.00 64.41  ?  183 ALA   B C   1 
ATOM   2896 O  O   . ALA   B 1 27  ? -45.360 19.433  36.662  1.00 66.73  ?  183 ALA   B O   1 
ATOM   2897 C  CB  . ALA   B 1 27  ? -47.783 19.151  34.692  1.00 60.66  ?  183 ALA   B CB  1 
ATOM   2898 N  N   . GLY   B 1 28  ? -46.374 21.448  36.602  1.00 62.40  ?  184 GLY   B N   1 
ATOM   2899 C  CA  . GLY   B 1 28  ? -45.175 22.142  37.037  1.00 62.03  ?  184 GLY   B CA  1 
ATOM   2900 C  C   . GLY   B 1 28  ? -44.902 21.935  38.514  1.00 59.81  ?  184 GLY   B C   1 
ATOM   2901 O  O   . GLY   B 1 28  ? -43.744 21.804  38.925  1.00 74.54  ?  184 GLY   B O   1 
ATOM   2902 N  N   . MET   B 1 29  ? -45.961 21.922  39.335  1.00 58.08  ?  185 MET   B N   1 
ATOM   2903 C  CA  . MET   B 1 29  ? -45.805 21.576  40.751  1.00 68.47  ?  185 MET   B CA  1 
ATOM   2904 C  C   . MET   B 1 29  ? -45.212 20.182  40.912  1.00 62.49  ?  185 MET   B C   1 
ATOM   2905 O  O   . MET   B 1 29  ? -44.273 19.973  41.690  1.00 66.85  ?  185 MET   B O   1 
ATOM   2906 C  CB  . MET   B 1 29  ? -47.149 21.657  41.478  1.00 63.94  ?  185 MET   B CB  1 
ATOM   2907 C  CG  . MET   B 1 29  ? -47.151 22.516  42.729  1.00 72.21  ?  185 MET   B CG  1 
ATOM   2908 S  SD  . MET   B 1 29  ? -46.475 24.165  42.490  1.00 106.47 ?  185 MET   B SD  1 
ATOM   2909 C  CE  . MET   B 1 29  ? -48.003 25.084  42.296  1.00 75.81  ?  185 MET   B CE  1 
ATOM   2910 N  N   . VAL   B 1 30  ? -45.764 19.213  40.178  1.00 61.37  ?  186 VAL   B N   1 
ATOM   2911 C  CA  . VAL   B 1 30  ? -45.251 17.843  40.207  1.00 63.32  ?  186 VAL   B CA  1 
ATOM   2912 C  C   . VAL   B 1 30  ? -43.771 17.820  39.842  1.00 65.38  ?  186 VAL   B C   1 
ATOM   2913 O  O   . VAL   B 1 30  ? -42.938 17.280  40.581  1.00 63.98  ?  186 VAL   B O   1 
ATOM   2914 C  CB  . VAL   B 1 30  ? -46.085 16.946  39.275  1.00 58.18  ?  186 VAL   B CB  1 
ATOM   2915 C  CG1 . VAL   B 1 30  ? -45.492 15.545  39.185  1.00 58.08  ?  186 VAL   B CG1 1 
ATOM   2916 C  CG2 . VAL   B 1 30  ? -47.514 16.909  39.765  1.00 63.39  ?  186 VAL   B CG2 1 
ATOM   2917 N  N   . LYS   B 1 31  ? -43.426 18.423  38.701  1.00 62.35  ?  187 LYS   B N   1 
ATOM   2918 C  CA  . LYS   B 1 31  ? -42.033 18.498  38.268  1.00 59.48  ?  187 LYS   B CA  1 
ATOM   2919 C  C   . LYS   B 1 31  ? -41.121 18.921  39.407  1.00 69.34  ?  187 LYS   B C   1 
ATOM   2920 O  O   . LYS   B 1 31  ? -40.075 18.305  39.644  1.00 77.94  ?  187 LYS   B O   1 
ATOM   2921 C  CB  . LYS   B 1 31  ? -41.896 19.479  37.105  1.00 70.50  ?  187 LYS   B CB  1 
ATOM   2922 C  CG  . LYS   B 1 31  ? -40.541 20.201  37.094  1.00 72.69  ?  187 LYS   B CG  1 
ATOM   2923 C  CD  . LYS   B 1 31  ? -40.361 21.079  35.867  1.00 77.50  ?  187 LYS   B CD  1 
ATOM   2924 C  CE  . LYS   B 1 31  ? -40.656 22.536  36.244  1.00 65.04  ?  187 LYS   B CE  1 
ATOM   2925 N  NZ  . LYS   B 1 31  ? -40.052 22.910  37.569  1.00 69.16  ?  187 LYS   B NZ  1 
ATOM   2926 N  N   . GLY   B 1 32  ? -41.515 19.967  40.136  1.00 69.31  ?  188 GLY   B N   1 
ATOM   2927 C  CA  . GLY   B 1 32  ? -40.690 20.436  41.238  1.00 56.02  ?  188 GLY   B CA  1 
ATOM   2928 C  C   . GLY   B 1 32  ? -40.386 19.340  42.235  1.00 66.50  ?  188 GLY   B C   1 
ATOM   2929 O  O   . GLY   B 1 32  ? -39.225 19.087  42.575  1.00 76.76  ?  188 GLY   B O   1 
ATOM   2930 N  N   . VAL   B 1 33  ? -41.431 18.662  42.712  1.00 69.27  ?  189 VAL   B N   1 
ATOM   2931 C  CA  . VAL   B 1 33  ? -41.240 17.632  43.732  1.00 65.14  ?  189 VAL   B CA  1 
ATOM   2932 C  C   . VAL   B 1 33  ? -40.411 16.482  43.169  1.00 60.86  ?  189 VAL   B C   1 
ATOM   2933 O  O   . VAL   B 1 33  ? -39.497 15.974  43.830  1.00 67.58  ?  189 VAL   B O   1 
ATOM   2934 C  CB  . VAL   B 1 33  ? -42.606 17.147  44.261  1.00 61.26  ?  189 VAL   B CB  1 
ATOM   2935 C  CG1 . VAL   B 1 33  ? -42.490 15.770  44.898  1.00 60.72  ?  189 VAL   B CG1 1 
ATOM   2936 C  CG2 . VAL   B 1 33  ? -43.223 18.156  45.198  1.00 65.78  ?  189 VAL   B CG2 1 
ATOM   2937 N  N   . VAL   B 1 34  ? -40.706 16.061  41.933  1.00 63.32  ?  190 VAL   B N   1 
ATOM   2938 C  CA  . VAL   B 1 34  ? -39.958 14.963  41.319  1.00 54.76  ?  190 VAL   B CA  1 
ATOM   2939 C  C   . VAL   B 1 34  ? -38.474 15.312  41.212  1.00 65.84  ?  190 VAL   B C   1 
ATOM   2940 O  O   . VAL   B 1 34  ? -37.604 14.452  41.402  1.00 63.58  ?  190 VAL   B O   1 
ATOM   2941 C  CB  . VAL   B 1 34  ? -40.558 14.602  39.947  1.00 63.71  ?  190 VAL   B CB  1 
ATOM   2942 C  CG1 . VAL   B 1 34  ? -39.638 13.649  39.196  1.00 56.25  ?  190 VAL   B CG1 1 
ATOM   2943 C  CG2 . VAL   B 1 34  ? -41.949 13.990  40.101  1.00 65.58  ?  190 VAL   B CG2 1 
ATOM   2944 N  N   . ASP   B 1 35  ? -38.159 16.582  40.930  1.00 73.65  ?  191 ASP   B N   1 
ATOM   2945 C  CA  . ASP   B 1 35  ? -36.761 17.004  40.818  1.00 70.15  ?  191 ASP   B CA  1 
ATOM   2946 C  C   . ASP   B 1 35  ? -36.033 16.888  42.152  1.00 63.92  ?  191 ASP   B C   1 
ATOM   2947 O  O   . ASP   B 1 35  ? -34.901 16.395  42.211  1.00 76.75  ?  191 ASP   B O   1 
ATOM   2948 C  CB  . ASP   B 1 35  ? -36.682 18.442  40.300  1.00 66.35  ?  191 ASP   B CB  1 
ATOM   2949 C  CG  . ASP   B 1 35  ? -36.961 18.553  38.806  1.00 71.43  ?  191 ASP   B CG  1 
ATOM   2950 O  OD1 . ASP   B 1 35  ? -36.939 17.526  38.081  1.00 78.72  ?  191 ASP   B OD1 1 
ATOM   2951 O  OD2 . ASP   B 1 35  ? -37.214 19.688  38.350  1.00 80.16  -1 191 ASP   B OD2 1 
ATOM   2952 N  N   . HIS   B 1 36  ? -36.652 17.382  43.230  1.00 71.19  ?  192 HIS   B N   1 
ATOM   2953 C  CA  . HIS   B 1 36  ? -36.092 17.220  44.572  1.00 66.20  ?  192 HIS   B CA  1 
ATOM   2954 C  C   . HIS   B 1 36  ? -35.874 15.752  44.932  1.00 70.34  ?  192 HIS   B C   1 
ATOM   2955 O  O   . HIS   B 1 36  ? -34.846 15.392  45.530  1.00 60.82  ?  192 HIS   B O   1 
ATOM   2956 C  CB  . HIS   B 1 36  ? -37.008 17.875  45.613  1.00 72.03  ?  192 HIS   B CB  1 
ATOM   2957 C  CG  . HIS   B 1 36  ? -36.957 19.373  45.645  1.00 73.71  ?  192 HIS   B CG  1 
ATOM   2958 N  ND1 . HIS   B 1 36  ? -35.877 20.067  46.152  1.00 78.44  ?  192 HIS   B ND1 1 
ATOM   2959 C  CD2 . HIS   B 1 36  ? -37.829 20.309  45.197  1.00 71.26  ?  192 HIS   B CD2 1 
ATOM   2960 C  CE1 . HIS   B 1 36  ? -36.106 21.366  46.058  1.00 67.25  ?  192 HIS   B CE1 1 
ATOM   2961 N  NE2 . HIS   B 1 36  ? -37.279 21.540  45.473  1.00 83.70  ?  192 HIS   B NE2 1 
ATOM   2962 N  N   . LEU   B 1 37  ? -36.863 14.901  44.650  1.00 54.52  ?  193 LEU   B N   1 
ATOM   2963 C  CA  . LEU   B 1 37  ? -36.742 13.498  45.032  1.00 61.74  ?  193 LEU   B CA  1 
ATOM   2964 C  C   . LEU   B 1 37  ? -35.585 12.842  44.295  1.00 57.33  ?  193 LEU   B C   1 
ATOM   2965 O  O   . LEU   B 1 37  ? -34.721 12.199  44.910  1.00 50.39  ?  193 LEU   B O   1 
ATOM   2966 C  CB  . LEU   B 1 37  ? -38.053 12.751  44.776  1.00 50.64  ?  193 LEU   B CB  1 
ATOM   2967 C  CG  . LEU   B 1 37  ? -39.224 13.066  45.714  1.00 55.79  ?  193 LEU   B CG  1 
ATOM   2968 C  CD1 . LEU   B 1 37  ? -40.516 12.373  45.292  1.00 57.97  ?  193 LEU   B CD1 1 
ATOM   2969 C  CD2 . LEU   B 1 37  ? -38.886 12.721  47.159  1.00 64.14  ?  193 LEU   B CD2 1 
ATOM   2970 N  N   . LEU   B 1 38  ? -35.531 13.030  42.975  1.00 52.73  ?  194 LEU   B N   1 
ATOM   2971 C  CA  . LEU   B 1 38  ? -34.471 12.412  42.189  1.00 55.35  ?  194 LEU   B CA  1 
ATOM   2972 C  C   . LEU   B 1 38  ? -33.099 12.862  42.658  1.00 57.51  ?  194 LEU   B C   1 
ATOM   2973 O  O   . LEU   B 1 38  ? -32.157 12.067  42.661  1.00 63.59  ?  194 LEU   B O   1 
ATOM   2974 C  CB  . LEU   B 1 38  ? -34.663 12.710  40.703  1.00 56.21  ?  194 LEU   B CB  1 
ATOM   2975 C  CG  . LEU   B 1 38  ? -35.869 11.974  40.126  1.00 54.56  ?  194 LEU   B CG  1 
ATOM   2976 C  CD1 . LEU   B 1 38  ? -36.160 12.410  38.703  1.00 56.56  ?  194 LEU   B CD1 1 
ATOM   2977 C  CD2 . LEU   B 1 38  ? -35.647 10.459  40.229  1.00 53.23  ?  194 LEU   B CD2 1 
ATOM   2978 N  N   . LEU   B 1 39  ? -32.973 14.117  43.104  1.00 65.89  ?  195 LEU   B N   1 
ATOM   2979 C  CA  . LEU   B 1 39  ? -31.690 14.592  43.630  1.00 58.82  ?  195 LEU   B CA  1 
ATOM   2980 C  C   . LEU   B 1 39  ? -31.274 13.826  44.884  1.00 60.90  ?  195 LEU   B C   1 
ATOM   2981 O  O   . LEU   B 1 39  ? -30.127 13.379  44.992  1.00 64.70  ?  195 LEU   B O   1 
ATOM   2982 C  CB  . LEU   B 1 39  ? -31.740 16.099  43.904  1.00 66.76  ?  195 LEU   B CB  1 
ATOM   2983 C  CG  . LEU   B 1 39  ? -31.002 16.976  42.870  1.00 65.80  ?  195 LEU   B CG  1 
ATOM   2984 C  CD1 . LEU   B 1 39  ? -31.445 16.672  41.440  1.00 60.58  ?  195 LEU   B CD1 1 
ATOM   2985 C  CD2 . LEU   B 1 39  ? -31.137 18.476  43.170  1.00 68.19  ?  195 LEU   B CD2 1 
ATOM   2986 N  N   . ARG   B 1 40  ? -32.187 13.664  45.847  1.00 60.33  ?  196 ARG   B N   1 
ATOM   2987 C  CA  . ARG   B 1 40  ? -31.864 12.894  47.047  1.00 57.90  ?  196 ARG   B CA  1 
ATOM   2988 C  C   . ARG   B 1 40  ? -31.616 11.416  46.759  1.00 62.34  ?  196 ARG   B C   1 
ATOM   2989 O  O   . ARG   B 1 40  ? -30.698 10.811  47.336  1.00 65.96  ?  196 ARG   B O   1 
ATOM   2990 C  CB  . ARG   B 1 40  ? -32.966 12.993  48.083  1.00 56.55  ?  196 ARG   B CB  1 
ATOM   2991 C  CG  . ARG   B 1 40  ? -32.483 12.442  49.418  1.00 61.26  ?  196 ARG   B CG  1 
ATOM   2992 C  CD  . ARG   B 1 40  ? -31.492 13.354  50.173  1.00 76.79  ?  196 ARG   B CD  1 
ATOM   2993 N  NE  . ARG   B 1 40  ? -31.736 14.752  49.836  1.00 81.82  ?  196 ARG   B NE  1 
ATOM   2994 C  CZ  . ARG   B 1 40  ? -30.825 15.640  49.455  1.00 87.09  ?  196 ARG   B CZ  1 
ATOM   2995 N  NH1 . ARG   B 1 40  ? -29.523 15.401  49.568  1.00 80.60  ?  196 ARG   B NH1 1 
ATOM   2996 N  NH2 . ARG   B 1 40  ? -31.228 16.830  49.018  1.00 87.82  ?  196 ARG   B NH2 1 
ATOM   2997 N  N   . LEU   B 1 41  ? -32.499 10.788  45.981  1.00 54.03  ?  197 LEU   B N   1 
ATOM   2998 C  CA  . LEU   B 1 41  ? -32.339 9.375   45.637  1.00 58.69  ?  197 LEU   B CA  1 
ATOM   2999 C  C   . LEU   B 1 41  ? -30.966 9.089   45.057  1.00 59.28  ?  197 LEU   B C   1 
ATOM   3000 O  O   . LEU   B 1 41  ? -30.353 8.065   45.386  1.00 55.51  ?  197 LEU   B O   1 
ATOM   3001 C  CB  . LEU   B 1 41  ? -33.412 8.931   44.632  1.00 51.04  ?  197 LEU   B CB  1 
ATOM   3002 C  CG  . LEU   B 1 41  ? -34.787 8.732   45.251  1.00 57.15  ?  197 LEU   B CG  1 
ATOM   3003 C  CD1 . LEU   B 1 41  ? -35.870 8.603   44.183  1.00 49.64  ?  197 LEU   B CD1 1 
ATOM   3004 C  CD2 . LEU   B 1 41  ? -34.731 7.525   46.175  1.00 48.67  ?  197 LEU   B CD2 1 
ATOM   3005 N  N   . LYS   B 1 42  ? -30.477 9.968   44.176  1.00 52.35  ?  198 LYS   B N   1 
ATOM   3006 C  CA  . LYS   B 1 42  ? -29.162 9.775   43.580  1.00 62.28  ?  198 LYS   B CA  1 
ATOM   3007 C  C   . LYS   B 1 42  ? -28.034 9.864   44.601  1.00 61.66  ?  198 LYS   B C   1 
ATOM   3008 O  O   . LYS   B 1 42  ? -26.887 9.586   44.240  1.00 77.23  ?  198 LYS   B O   1 
ATOM   3009 C  CB  . LYS   B 1 42  ? -28.922 10.781  42.438  1.00 57.21  ?  198 LYS   B CB  1 
ATOM   3010 C  CG  . LYS   B 1 42  ? -29.928 10.715  41.305  1.00 69.58  ?  198 LYS   B CG  1 
ATOM   3011 C  CD  . LYS   B 1 42  ? -29.751 11.835  40.251  1.00 61.62  ?  198 LYS   B CD  1 
ATOM   3012 C  CE  . LYS   B 1 42  ? -29.024 11.351  38.995  1.00 60.26  ?  198 LYS   B CE  1 
ATOM   3013 N  NZ  . LYS   B 1 42  ? -28.000 12.329  38.505  1.00 70.22  ?  198 LYS   B NZ  1 
ATOM   3014 N  N   . CYS   B 1 43  ? -28.325 10.225  45.860  1.00 54.24  ?  199 CYS   B N   1 
ATOM   3015 C  CA  . CYS   B 1 43  ? -27.314 10.230  46.907  1.00 61.18  ?  199 CYS   B CA  1 
ATOM   3016 C  C   . CYS   B 1 43  ? -27.182 8.877   47.599  1.00 57.19  ?  199 CYS   B C   1 
ATOM   3017 O  O   . CYS   B 1 43  ? -26.183 8.638   48.288  1.00 70.24  ?  199 CYS   B O   1 
ATOM   3018 C  CB  . CYS   B 1 43  ? -27.632 11.316  47.941  1.00 66.57  ?  199 CYS   B CB  1 
ATOM   3019 S  SG  . CYS   B 1 43  ? -27.529 12.995  47.270  1.00 81.53  ?  199 CYS   B SG  1 
ATOM   3020 N  N   . ASP   B 1 44  ? -28.167 7.998   47.449  1.00 59.13  ?  200 ASP   B N   1 
ATOM   3021 C  CA  . ASP   B 1 44  ? -28.015 6.622   47.897  1.00 59.99  ?  200 ASP   B CA  1 
ATOM   3022 C  C   . ASP   B 1 44  ? -27.214 5.829   46.872  1.00 54.52  ?  200 ASP   B C   1 
ATOM   3023 O  O   . ASP   B 1 44  ? -27.541 5.836   45.685  1.00 53.47  ?  200 ASP   B O   1 
ATOM   3024 C  CB  . ASP   B 1 44  ? -29.375 5.973   48.118  1.00 58.78  ?  200 ASP   B CB  1 
ATOM   3025 C  CG  . ASP   B 1 44  ? -29.285 4.734   48.966  1.00 57.99  ?  200 ASP   B CG  1 
ATOM   3026 O  OD1 . ASP   B 1 44  ? -29.080 3.653   48.380  1.00 63.04  ?  200 ASP   B OD1 1 
ATOM   3027 O  OD2 . ASP   B 1 44  ? -29.426 4.832   50.198  1.00 60.96  -1 200 ASP   B OD2 1 
ATOM   3028 N  N   . SER   B 1 45  ? -26.153 5.153   47.335  1.00 63.64  ?  201 SER   B N   1 
ATOM   3029 C  CA  . SER   B 1 45  ? -25.317 4.381   46.419  1.00 57.05  ?  201 SER   B CA  1 
ATOM   3030 C  C   . SER   B 1 45  ? -26.130 3.332   45.674  1.00 57.38  ?  201 SER   B C   1 
ATOM   3031 O  O   . SER   B 1 45  ? -25.813 3.013   44.522  1.00 58.99  ?  201 SER   B O   1 
ATOM   3032 C  CB  . SER   B 1 45  ? -24.150 3.723   47.166  1.00 57.68  ?  201 SER   B CB  1 
ATOM   3033 O  OG  . SER   B 1 45  ? -24.586 2.680   48.028  1.00 59.79  ?  201 SER   B OG  1 
ATOM   3034 N  N   . ALA   B 1 46  ? -27.196 2.813   46.295  1.00 58.34  ?  202 ALA   B N   1 
ATOM   3035 C  CA  . ALA   B 1 46  ? -28.027 1.807   45.638  1.00 55.17  ?  202 ALA   B CA  1 
ATOM   3036 C  C   . ALA   B 1 46  ? -28.944 2.396   44.572  1.00 53.30  ?  202 ALA   B C   1 
ATOM   3037 O  O   . ALA   B 1 46  ? -29.371 1.661   43.670  1.00 51.92  ?  202 ALA   B O   1 
ATOM   3038 C  CB  . ALA   B 1 46  ? -28.865 1.056   46.675  1.00 56.79  ?  202 ALA   B CB  1 
ATOM   3039 N  N   . PHE   B 1 47  ? -29.274 3.686   44.650  1.00 51.74  ?  203 PHE   B N   1 
ATOM   3040 C  CA  . PHE   B 1 47  ? -30.148 4.314   43.660  1.00 53.06  ?  203 PHE   B CA  1 
ATOM   3041 C  C   . PHE   B 1 47  ? -29.398 5.312   42.777  1.00 55.10  ?  203 PHE   B C   1 
ATOM   3042 O  O   . PHE   B 1 47  ? -30.025 6.157   42.125  1.00 51.99  ?  203 PHE   B O   1 
ATOM   3043 C  CB  . PHE   B 1 47  ? -31.343 4.986   44.349  1.00 52.43  ?  203 PHE   B CB  1 
ATOM   3044 C  CG  . PHE   B 1 47  ? -32.301 4.016   45.014  1.00 51.57  ?  203 PHE   B CG  1 
ATOM   3045 C  CD1 . PHE   B 1 47  ? -33.207 3.296   44.257  1.00 54.38  ?  203 PHE   B CD1 1 
ATOM   3046 C  CD2 . PHE   B 1 47  ? -32.307 3.842   46.389  1.00 54.65  ?  203 PHE   B CD2 1 
ATOM   3047 C  CE1 . PHE   B 1 47  ? -34.087 2.415   44.855  1.00 55.28  ?  203 PHE   B CE1 1 
ATOM   3048 C  CE2 . PHE   B 1 47  ? -33.196 2.954   46.997  1.00 54.48  ?  203 PHE   B CE2 1 
ATOM   3049 C  CZ  . PHE   B 1 47  ? -34.087 2.242   46.219  1.00 52.04  ?  203 PHE   B CZ  1 
ATOM   3050 N  N   . ARG   B 1 48  ? -28.066 5.202   42.726  1.00 58.96  ?  204 ARG   B N   1 
ATOM   3051 C  CA  . ARG   B 1 48  ? -27.226 6.223   42.103  1.00 55.84  ?  204 ARG   B CA  1 
ATOM   3052 C  C   . ARG   B 1 48  ? -27.708 6.575   40.707  1.00 59.39  ?  204 ARG   B C   1 
ATOM   3053 O  O   . ARG   B 1 48  ? -27.821 7.755   40.359  1.00 65.78  ?  204 ARG   B O   1 
ATOM   3054 C  CB  . ARG   B 1 48  ? -25.774 5.739   42.046  1.00 57.73  ?  204 ARG   B CB  1 
ATOM   3055 C  CG  . ARG   B 1 48  ? -24.765 6.775   41.547  1.00 63.38  ?  204 ARG   B CG  1 
ATOM   3056 C  CD  . ARG   B 1 48  ? -24.668 7.950   42.524  1.00 63.40  ?  204 ARG   B CD  1 
ATOM   3057 N  NE  . ARG   B 1 48  ? -23.499 7.866   43.396  1.00 65.88  ?  204 ARG   B NE  1 
ATOM   3058 C  CZ  . ARG   B 1 48  ? -23.507 8.166   44.689  1.00 67.43  ?  204 ARG   B CZ  1 
ATOM   3059 N  NH1 . ARG   B 1 48  ? -24.618 8.540   45.304  1.00 75.34  ?  204 ARG   B NH1 1 
ATOM   3060 N  NH2 . ARG   B 1 48  ? -22.375 8.078   45.388  1.00 72.22  ?  204 ARG   B NH2 1 
ATOM   3061 N  N   . GLY   B 1 49  ? -28.008 5.569   39.900  1.00 56.29  ?  205 GLY   B N   1 
ATOM   3062 C  CA  . GLY   B 1 49  ? -28.405 5.823   38.534  1.00 56.14  ?  205 GLY   B CA  1 
ATOM   3063 C  C   . GLY   B 1 49  ? -29.896 5.996   38.323  1.00 54.08  ?  205 GLY   B C   1 
ATOM   3064 O  O   . GLY   B 1 49  ? -30.397 5.677   37.245  1.00 49.40  ?  205 GLY   B O   1 
ATOM   3065 N  N   . VAL   B 1 50  ? -30.622 6.498   39.324  1.00 51.12  ?  206 VAL   B N   1 
ATOM   3066 C  CA  . VAL   B 1 50  ? -32.062 6.676   39.175  1.00 46.08  ?  206 VAL   B CA  1 
ATOM   3067 C  C   . VAL   B 1 50  ? -32.342 7.886   38.287  1.00 51.93  ?  206 VAL   B C   1 
ATOM   3068 O  O   . VAL   B 1 50  ? -31.629 8.901   38.329  1.00 53.76  ?  206 VAL   B O   1 
ATOM   3069 C  CB  . VAL   B 1 50  ? -32.751 6.787   40.550  1.00 43.51  ?  206 VAL   B CB  1 
ATOM   3070 C  CG1 . VAL   B 1 50  ? -32.438 8.109   41.233  1.00 50.14  ?  206 VAL   B CG1 1 
ATOM   3071 C  CG2 . VAL   B 1 50  ? -34.262 6.638   40.372  1.00 50.10  ?  206 VAL   B CG2 1 
ATOM   3072 N  N   . GLY   B 1 51  ? -33.369 7.765   37.449  1.00 43.35  ?  207 GLY   B N   1 
ATOM   3073 C  CA  . GLY   B 1 51  ? -33.775 8.872   36.607  1.00 49.35  ?  207 GLY   B CA  1 
ATOM   3074 C  C   . GLY   B 1 51  ? -35.210 8.711   36.170  1.00 48.41  ?  207 GLY   B C   1 
ATOM   3075 O  O   . GLY   B 1 51  ? -35.865 7.702   36.441  1.00 52.60  ?  207 GLY   B O   1 
ATOM   3076 N  N   . LEU   B 1 52  ? -35.689 9.723   35.463  1.00 51.66  ?  208 LEU   B N   1 
ATOM   3077 C  CA  . LEU   B 1 52  ? -37.077 9.731   35.056  1.00 51.10  ?  208 LEU   B CA  1 
ATOM   3078 C  C   . LEU   B 1 52  ? -37.279 8.834   33.839  1.00 50.02  ?  208 LEU   B C   1 
ATOM   3079 O  O   . LEU   B 1 52  ? -36.350 8.575   33.068  1.00 54.36  ?  208 LEU   B O   1 
ATOM   3080 C  CB  . LEU   B 1 52  ? -37.529 11.148  34.726  1.00 56.40  ?  208 LEU   B CB  1 
ATOM   3081 C  CG  . LEU   B 1 52  ? -38.590 11.768  35.632  1.00 58.73  ?  208 LEU   B CG  1 
ATOM   3082 C  CD1 . LEU   B 1 52  ? -39.237 12.924  34.869  1.00 64.32  ?  208 LEU   B CD1 1 
ATOM   3083 C  CD2 . LEU   B 1 52  ? -39.626 10.767  36.150  1.00 55.10  ?  208 LEU   B CD2 1 
ATOM   3084 N  N   . LEU   B 1 53  ? -38.503 8.340   33.687  1.00 47.25  ?  209 LEU   B N   1 
ATOM   3085 C  CA  . LEU   B 1 53  ? -38.901 7.645   32.462  1.00 53.24  ?  209 LEU   B CA  1 
ATOM   3086 C  C   . LEU   B 1 53  ? -40.128 8.323   31.873  1.00 55.88  ?  209 LEU   B C   1 
ATOM   3087 O  O   . LEU   B 1 53  ? -40.917 8.920   32.606  1.00 57.04  ?  209 LEU   B O   1 
ATOM   3088 C  CB  . LEU   B 1 53  ? -39.177 6.158   32.720  1.00 44.31  ?  209 LEU   B CB  1 
ATOM   3089 C  CG  . LEU   B 1 53  ? -39.414 5.335   31.445  1.00 57.42  ?  209 LEU   B CG  1 
ATOM   3090 C  CD1 . LEU   B 1 53  ? -38.335 5.585   30.414  1.00 51.34  ?  209 LEU   B CD1 1 
ATOM   3091 C  CD2 . LEU   B 1 53  ? -39.474 3.857   31.786  1.00 50.35  ?  209 LEU   B CD2 1 
ATOM   3092 N  N   . TYR   B 1 59  ? -44.268 13.032  33.741  1.00 75.24  ?  215 TYR   B N   1 
ATOM   3093 C  CA  . TYR   B 1 59  ? -45.645 12.915  34.209  1.00 61.99  ?  215 TYR   B CA  1 
ATOM   3094 C  C   . TYR   B 1 59  ? -46.538 12.348  33.106  1.00 65.31  ?  215 TYR   B C   1 
ATOM   3095 O  O   . TYR   B 1 59  ? -46.372 12.658  31.923  1.00 68.43  ?  215 TYR   B O   1 
ATOM   3096 C  CB  . TYR   B 1 59  ? -46.181 14.275  34.676  1.00 63.82  ?  215 TYR   B CB  1 
ATOM   3097 C  CG  . TYR   B 1 59  ? -46.760 15.118  33.554  1.00 68.65  ?  215 TYR   B CG  1 
ATOM   3098 C  CD1 . TYR   B 1 59  ? -45.959 15.996  32.832  1.00 65.36  ?  215 TYR   B CD1 1 
ATOM   3099 C  CD2 . TYR   B 1 59  ? -48.109 15.041  33.223  1.00 70.46  ?  215 TYR   B CD2 1 
ATOM   3100 C  CE1 . TYR   B 1 59  ? -46.478 16.761  31.800  1.00 65.69  ?  215 TYR   B CE1 1 
ATOM   3101 C  CE2 . TYR   B 1 59  ? -48.641 15.801  32.191  1.00 64.29  ?  215 TYR   B CE2 1 
ATOM   3102 C  CZ  . TYR   B 1 59  ? -47.822 16.664  31.483  1.00 74.62  ?  215 TYR   B CZ  1 
ATOM   3103 O  OH  . TYR   B 1 59  ? -48.355 17.424  30.458  1.00 74.52  ?  215 TYR   B OH  1 
ATOM   3104 N  N   . GLU   B 1 60  ? -47.485 11.515  33.517  1.00 64.48  ?  216 GLU   B N   1 
ATOM   3105 C  CA  . GLU   B 1 60  ? -48.502 10.948  32.649  1.00 54.76  ?  216 GLU   B CA  1 
ATOM   3106 C  C   . GLU   B 1 60  ? -49.798 10.919  33.450  1.00 54.28  ?  216 GLU   B C   1 
ATOM   3107 O  O   . GLU   B 1 60  ? -49.795 11.129  34.672  1.00 52.72  ?  216 GLU   B O   1 
ATOM   3108 C  CB  . GLU   B 1 60  ? -48.090 9.545   32.160  1.00 67.06  ?  216 GLU   B CB  1 
ATOM   3109 C  CG  . GLU   B 1 60  ? -46.722 9.493   31.440  1.00 59.42  ?  216 GLU   B CG  1 
ATOM   3110 C  CD  . GLU   B 1 60  ? -46.780 9.732   29.926  1.00 70.76  ?  216 GLU   B CD  1 
ATOM   3111 O  OE1 . GLU   B 1 60  ? -47.612 9.089   29.243  1.00 69.64  ?  216 GLU   B OE1 1 
ATOM   3112 O  OE2 . GLU   B 1 60  ? -45.983 10.561  29.421  1.00 68.68  -1 216 GLU   B OE2 1 
ATOM   3113 N  N   . HIS   B 1 61  ? -50.922 10.679  32.766  1.00 50.82  ?  217 HIS   B N   1 
ATOM   3114 C  CA  . HIS   B 1 61  ? -52.225 10.565  33.420  1.00 52.94  ?  217 HIS   B CA  1 
ATOM   3115 C  C   . HIS   B 1 61  ? -52.843 9.214   33.111  1.00 55.85  ?  217 HIS   B C   1 
ATOM   3116 O  O   . HIS   B 1 61  ? -52.998 8.852   31.943  1.00 63.37  ?  217 HIS   B O   1 
ATOM   3117 C  CB  . HIS   B 1 61  ? -53.170 11.686  32.998  1.00 58.13  ?  217 HIS   B CB  1 
ATOM   3118 C  CG  . HIS   B 1 61  ? -52.790 13.012  33.556  1.00 50.72  ?  217 HIS   B CG  1 
ATOM   3119 N  ND1 . HIS   B 1 61  ? -51.697 13.722  33.107  1.00 56.88  ?  217 HIS   B ND1 1 
ATOM   3120 C  CD2 . HIS   B 1 61  ? -53.353 13.756  34.539  1.00 56.34  ?  217 HIS   B CD2 1 
ATOM   3121 C  CE1 . HIS   B 1 61  ? -51.604 14.848  33.794  1.00 55.63  ?  217 HIS   B CE1 1 
ATOM   3122 N  NE2 . HIS   B 1 61  ? -52.595 14.892  34.669  1.00 52.28  ?  217 HIS   B NE2 1 
ATOM   3123 N  N   . VAL   B 1 62  ? -53.187 8.472   34.166  1.00 56.32  ?  218 VAL   B N   1 
ATOM   3124 C  CA  . VAL   B 1 62  ? -53.917 7.226   34.003  1.00 56.80  ?  218 VAL   B CA  1 
ATOM   3125 C  C   . VAL   B 1 62  ? -55.390 7.511   33.748  1.00 53.30  ?  218 VAL   B C   1 
ATOM   3126 O  O   . VAL   B 1 62  ? -56.018 6.881   32.892  1.00 50.23  ?  218 VAL   B O   1 
ATOM   3127 C  CB  . VAL   B 1 62  ? -53.737 6.341   35.249  1.00 49.21  ?  218 VAL   B CB  1 
ATOM   3128 C  CG1 . VAL   B 1 62  ? -54.589 5.113   35.095  1.00 58.59  ?  218 VAL   B CG1 1 
ATOM   3129 C  CG2 . VAL   B 1 62  ? -52.275 5.968   35.449  1.00 52.68  ?  218 VAL   B CG2 1 
ATOM   3130 N  N   . LYS   B 1 63  ? -55.970 8.441   34.518  1.00 44.56  ?  219 LYS   B N   1 
ATOM   3131 C  CA  . LYS   B 1 63  ? -57.371 8.820   34.374  1.00 43.37  ?  219 LYS   B CA  1 
ATOM   3132 C  C   . LYS   B 1 63  ? -57.450 10.134  33.592  1.00 55.19  ?  219 LYS   B C   1 
ATOM   3133 O  O   . LYS   B 1 63  ? -57.122 11.206  34.127  1.00 47.04  ?  219 LYS   B O   1 
ATOM   3134 C  CB  . LYS   B 1 63  ? -58.054 8.961   35.729  1.00 50.92  ?  219 LYS   B CB  1 
ATOM   3135 C  CG  . LYS   B 1 63  ? -58.237 7.666   36.528  1.00 49.16  ?  219 LYS   B CG  1 
ATOM   3136 C  CD  . LYS   B 1 63  ? -58.929 7.986   37.831  1.00 46.62  ?  219 LYS   B CD  1 
ATOM   3137 C  CE  . LYS   B 1 63  ? -60.399 8.302   37.617  1.00 50.83  ?  219 LYS   B CE  1 
ATOM   3138 N  NZ  . LYS   B 1 63  ? -61.111 8.572   38.904  1.00 62.99  ?  219 LYS   B NZ  1 
ATOM   3139 N  N   . ILE   B 1 64  ? -57.906 10.037  32.334  1.00 43.95  ?  220 ILE   B N   1 
ATOM   3140 C  CA  . ILE   B 1 64  ? -58.153 11.200  31.479  1.00 41.22  ?  220 ILE   B CA  1 
ATOM   3141 C  C   . ILE   B 1 64  ? -59.007 12.235  32.193  1.00 40.45  ?  220 ILE   B C   1 
ATOM   3142 O  O   . ILE   B 1 64  ? -58.817 13.438  32.014  1.00 42.75  ?  220 ILE   B O   1 
ATOM   3143 C  CB  . ILE   B 1 64  ? -58.808 10.747  30.143  1.00 42.13  ?  220 ILE   B CB  1 
ATOM   3144 C  CG1 . ILE   B 1 64  ? -58.478 11.702  28.990  1.00 43.08  ?  220 ILE   B CG1 1 
ATOM   3145 C  CG2 . ILE   B 1 64  ? -60.322 10.599  30.270  1.00 41.90  ?  220 ILE   B CG2 1 
ATOM   3146 C  CD1 . ILE   B 1 64  ? -57.066 11.542  28.427  1.00 54.97  ?  220 ILE   B CD1 1 
ATOM   3147 N  N   . SER   B 1 65  ? -59.941 11.792  33.024  1.00 43.59  ?  221 SER   B N   1 
ATOM   3148 C  CA  . SER   B 1 65  ? -60.898 12.664  33.688  1.00 48.32  ?  221 SER   B CA  1 
ATOM   3149 C  C   . SER   B 1 65  ? -60.422 13.142  35.061  1.00 47.74  ?  221 SER   B C   1 
ATOM   3150 O  O   . SER   B 1 65  ? -61.239 13.635  35.843  1.00 51.26  ?  221 SER   B O   1 
ATOM   3151 C  CB  . SER   B 1 65  ? -62.245 11.938  33.836  1.00 53.16  ?  221 SER   B CB  1 
ATOM   3152 O  OG  . SER   B 1 65  ? -62.134 10.790  34.679  1.00 52.11  ?  221 SER   B OG  1 
ATOM   3153 N  N   . ALA   B 1 66  ? -59.133 12.983  35.377  1.00 45.27  ?  222 ALA   B N   1 
ATOM   3154 C  CA  . ALA   B 1 66  ? -58.561 13.377  36.666  1.00 54.96  ?  222 ALA   B CA  1 
ATOM   3155 C  C   . ALA   B 1 66  ? -57.248 14.089  36.378  1.00 62.96  ?  222 ALA   B C   1 
ATOM   3156 O  O   . ALA   B 1 66  ? -56.161 13.516  36.552  1.00 58.58  ?  222 ALA   B O   1 
ATOM   3157 C  CB  . ALA   B 1 66  ? -58.348 12.172  37.583  1.00 50.96  ?  222 ALA   B CB  1 
ATOM   3158 N  N   . PRO   B 1 67  ? -57.311 15.343  35.917  1.00 69.23  ?  223 PRO   B N   1 
ATOM   3159 C  CA  . PRO   B 1 67  ? -56.077 16.041  35.518  1.00 61.51  ?  223 PRO   B CA  1 
ATOM   3160 C  C   . PRO   B 1 67  ? -55.131 16.314  36.680  1.00 57.44  ?  223 PRO   B C   1 
ATOM   3161 O  O   . PRO   B 1 67  ? -53.930 16.502  36.440  1.00 63.06  ?  223 PRO   B O   1 
ATOM   3162 C  CB  . PRO   B 1 67  ? -56.594 17.349  34.905  1.00 58.63  ?  223 PRO   B CB  1 
ATOM   3163 C  CG  . PRO   B 1 67  ? -57.927 17.560  35.560  1.00 58.39  ?  223 PRO   B CG  1 
ATOM   3164 C  CD  . PRO   B 1 67  ? -58.508 16.194  35.770  1.00 61.55  ?  223 PRO   B CD  1 
ATOM   3165 N  N   . ASN   B 1 68  ? -55.625 16.348  37.919  1.00 61.22  ?  224 ASN   B N   1 
ATOM   3166 C  CA  . ASN   B 1 68  ? -54.781 16.568  39.091  1.00 59.44  ?  224 ASN   B CA  1 
ATOM   3167 C  C   . ASN   B 1 68  ? -54.130 15.298  39.629  1.00 58.25  ?  224 ASN   B C   1 
ATOM   3168 O  O   . ASN   B 1 68  ? -53.421 15.376  40.640  1.00 53.70  ?  224 ASN   B O   1 
ATOM   3169 C  CB  . ASN   B 1 68  ? -55.575 17.223  40.225  1.00 67.30  ?  224 ASN   B CB  1 
ATOM   3170 C  CG  . ASN   B 1 68  ? -55.914 18.671  39.940  1.00 72.04  ?  224 ASN   B CG  1 
ATOM   3171 O  OD1 . ASN   B 1 68  ? -55.181 19.362  39.228  1.00 70.08  ?  224 ASN   B OD1 1 
ATOM   3172 N  ND2 . ASN   B 1 68  ? -57.001 19.155  40.538  1.00 70.43  ?  224 ASN   B ND2 1 
ATOM   3173 N  N   . GLU   B 1 69  ? -54.345 14.150  38.986  1.00 55.18  ?  225 GLU   B N   1 
ATOM   3174 C  CA  . GLU   B 1 69  ? -53.792 12.862  39.403  1.00 46.75  ?  225 GLU   B CA  1 
ATOM   3175 C  C   . GLU   B 1 69  ? -52.725 12.419  38.415  1.00 46.28  ?  225 GLU   B C   1 
ATOM   3176 O  O   . GLU   B 1 69  ? -53.031 11.956  37.312  1.00 54.33  ?  225 GLU   B O   1 
ATOM   3177 C  CB  . GLU   B 1 69  ? -54.916 11.852  39.559  1.00 47.68  ?  225 GLU   B CB  1 
ATOM   3178 C  CG  . GLU   B 1 69  ? -55.865 12.308  40.657  1.00 47.23  ?  225 GLU   B CG  1 
ATOM   3179 C  CD  . GLU   B 1 69  ? -56.968 11.321  40.959  1.00 55.61  ?  225 GLU   B CD  1 
ATOM   3180 O  OE1 . GLU   B 1 69  ? -57.974 11.753  41.566  1.00 61.14  ?  225 GLU   B OE1 1 
ATOM   3181 O  OE2 . GLU   B 1 69  ? -56.886 10.157  40.505  1.00 58.28  -1 225 GLU   B OE2 1 
ATOM   3182 N  N   . PHE   B 1 70  ? -51.471 12.580  38.809  1.00 40.24  ?  226 PHE   B N   1 
ATOM   3183 C  CA  . PHE   B 1 70  ? -50.344 12.337  37.928  1.00 42.33  ?  226 PHE   B CA  1 
ATOM   3184 C  C   . PHE   B 1 70  ? -49.710 10.984  38.211  1.00 48.95  ?  226 PHE   B C   1 
ATOM   3185 O  O   . PHE   B 1 70  ? -49.797 10.440  39.318  1.00 51.87  ?  226 PHE   B O   1 
ATOM   3186 C  CB  . PHE   B 1 70  ? -49.291 13.425  38.080  1.00 49.69  ?  226 PHE   B CB  1 
ATOM   3187 C  CG  . PHE   B 1 70  ? -49.741 14.778  37.622  1.00 52.38  ?  226 PHE   B CG  1 
ATOM   3188 C  CD1 . PHE   B 1 70  ? -50.486 15.586  38.461  1.00 49.06  ?  226 PHE   B CD1 1 
ATOM   3189 C  CD2 . PHE   B 1 70  ? -49.420 15.244  36.363  1.00 52.75  ?  226 PHE   B CD2 1 
ATOM   3190 C  CE1 . PHE   B 1 70  ? -50.892 16.840  38.060  1.00 60.75  ?  226 PHE   B CE1 1 
ATOM   3191 C  CE2 . PHE   B 1 70  ? -49.827 16.501  35.944  1.00 59.38  ?  226 PHE   B CE2 1 
ATOM   3192 C  CZ  . PHE   B 1 70  ? -50.565 17.302  36.796  1.00 54.30  ?  226 PHE   B CZ  1 
ATOM   3193 N  N   . ASP   B 1 71  ? -49.032 10.465  37.191  1.00 49.27  ?  227 ASP   B N   1 
ATOM   3194 C  CA  . ASP   B 1 71  ? -48.383 9.167   37.253  1.00 48.70  ?  227 ASP   B CA  1 
ATOM   3195 C  C   . ASP   B 1 71  ? -46.948 9.272   36.757  1.00 49.09  ?  227 ASP   B C   1 
ATOM   3196 O  O   . ASP   B 1 71  ? -46.701 9.723   35.635  1.00 44.34  ?  227 ASP   B O   1 
ATOM   3197 C  CB  . ASP   B 1 71  ? -49.167 8.141   36.457  1.00 50.57  ?  227 ASP   B CB  1 
ATOM   3198 C  CG  . ASP   B 1 71  ? -48.626 6.777   36.636  1.00 56.34  ?  227 ASP   B CG  1 
ATOM   3199 O  OD1 . ASP   B 1 71  ? -47.705 6.398   35.879  1.00 58.05  ?  227 ASP   B OD1 1 
ATOM   3200 O  OD2 . ASP   B 1 71  ? -49.055 6.134   37.621  1.00 62.46  -1 227 ASP   B OD2 1 
ATOM   3201 N  N   . VAL   B 1 72  ? -46.009 8.844   37.601  1.00 45.20  ?  228 VAL   B N   1 
ATOM   3202 C  CA  . VAL   B 1 72  ? -44.584 9.104   37.430  1.00 41.17  ?  228 VAL   B CA  1 
ATOM   3203 C  C   . VAL   B 1 72  ? -43.828 7.796   37.632  1.00 48.33  ?  228 VAL   B C   1 
ATOM   3204 O  O   . VAL   B 1 72  ? -44.113 7.049   38.576  1.00 44.56  ?  228 VAL   B O   1 
ATOM   3205 C  CB  . VAL   B 1 72  ? -44.128 10.192  38.430  1.00 51.48  ?  228 VAL   B CB  1 
ATOM   3206 C  CG1 . VAL   B 1 72  ? -42.667 10.036  38.808  1.00 49.84  ?  228 VAL   B CG1 1 
ATOM   3207 C  CG2 . VAL   B 1 72  ? -44.391 11.575  37.862  1.00 52.16  ?  228 VAL   B CG2 1 
ATOM   3208 N  N   . MET   B 1 73  ? -42.856 7.515   36.763  1.00 39.51  ?  229 MET   B N   1 
ATOM   3209 C  CA  . MET   B 1 73  ? -42.038 6.319   36.921  1.00 45.79  ?  229 MET   B CA  1 
ATOM   3210 C  C   . MET   B 1 73  ? -40.569 6.716   37.074  1.00 46.35  ?  229 MET   B C   1 
ATOM   3211 O  O   . MET   B 1 73  ? -40.053 7.525   36.293  1.00 45.94  ?  229 MET   B O   1 
ATOM   3212 C  CB  . MET   B 1 73  ? -42.266 5.338   35.752  1.00 40.11  ?  229 MET   B CB  1 
ATOM   3213 C  CG  . MET   B 1 73  ? -41.208 4.250   35.601  1.00 50.41  ?  229 MET   B CG  1 
ATOM   3214 S  SD  . MET   B 1 73  ? -41.677 2.891   34.468  1.00 55.29  ?  229 MET   B SD  1 
ATOM   3215 C  CE  . MET   B 1 73  ? -43.459 3.027   34.446  1.00 54.22  ?  229 MET   B CE  1 
ATOM   3216 N  N   . PHE   B 1 74  ? -39.917 6.188   38.119  1.00 38.88  ?  230 PHE   B N   1 
ATOM   3217 C  CA  . PHE   B 1 74  ? -38.478 6.335   38.350  1.00 46.99  ?  230 PHE   B CA  1 
ATOM   3218 C  C   . PHE   B 1 74  ? -37.773 5.051   37.912  1.00 52.04  ?  230 PHE   B C   1 
ATOM   3219 O  O   . PHE   B 1 74  ? -37.963 3.997   38.529  1.00 48.31  ?  230 PHE   B O   1 
ATOM   3220 C  CB  . PHE   B 1 74  ? -38.162 6.609   39.826  1.00 42.93  ?  230 PHE   B CB  1 
ATOM   3221 C  CG  . PHE   B 1 74  ? -38.561 7.979   40.332  1.00 45.20  ?  230 PHE   B CG  1 
ATOM   3222 C  CD1 . PHE   B 1 74  ? -39.262 8.875   39.542  1.00 57.44  ?  230 PHE   B CD1 1 
ATOM   3223 C  CD2 . PHE   B 1 74  ? -38.192 8.378   41.605  1.00 54.35  ?  230 PHE   B CD2 1 
ATOM   3224 C  CE1 . PHE   B 1 74  ? -39.594 10.128  40.032  1.00 51.94  ?  230 PHE   B CE1 1 
ATOM   3225 C  CE2 . PHE   B 1 74  ? -38.530 9.633   42.094  1.00 55.50  ?  230 PHE   B CE2 1 
ATOM   3226 C  CZ  . PHE   B 1 74  ? -39.236 10.501  41.297  1.00 50.95  ?  230 PHE   B CZ  1 
ATOM   3227 N  N   . LYS   B 1 75  ? -36.921 5.139   36.897  1.00 47.63  ?  231 LYS   B N   1 
ATOM   3228 C  CA  . LYS   B 1 75  ? -36.184 3.974   36.423  1.00 48.11  ?  231 LYS   B CA  1 
ATOM   3229 C  C   . LYS   B 1 75  ? -34.776 3.916   37.013  1.00 43.56  ?  231 LYS   B C   1 
ATOM   3230 O  O   . LYS   B 1 75  ? -34.171 4.939   37.355  1.00 42.04  ?  231 LYS   B O   1 
ATOM   3231 C  CB  . LYS   B 1 75  ? -36.067 3.976   34.898  1.00 41.63  ?  231 LYS   B CB  1 
ATOM   3232 C  CG  . LYS   B 1 75  ? -35.217 5.125   34.407  1.00 48.48  ?  231 LYS   B CG  1 
ATOM   3233 C  CD  . LYS   B 1 75  ? -34.295 4.720   33.280  1.00 56.40  ?  231 LYS   B CD  1 
ATOM   3234 C  CE  . LYS   B 1 75  ? -33.191 5.761   33.071  1.00 55.16  ?  231 LYS   B CE  1 
ATOM   3235 N  NZ  . LYS   B 1 75  ? -31.853 5.156   32.785  1.00 52.67  ?  231 LYS   B NZ  1 
ATOM   3236 N  N   . LEU   B 1 76  ? -34.228 2.701   37.029  1.00 43.24  ?  232 LEU   B N   1 
ATOM   3237 C  CA  . LEU   B 1 76  ? -32.891 2.436   37.559  1.00 47.59  ?  232 LEU   B CA  1 
ATOM   3238 C  C   . LEU   B 1 76  ? -32.251 1.306   36.763  1.00 47.91  ?  232 LEU   B C   1 
ATOM   3239 O  O   . LEU   B 1 76  ? -32.787 0.195   36.738  1.00 45.10  ?  232 LEU   B O   1 
ATOM   3240 C  CB  . LEU   B 1 76  ? -32.974 2.058   39.035  1.00 45.75  ?  232 LEU   B CB  1 
ATOM   3241 C  CG  . LEU   B 1 76  ? -31.669 1.688   39.732  1.00 49.57  ?  232 LEU   B CG  1 
ATOM   3242 C  CD1 . LEU   B 1 76  ? -30.749 2.895   39.812  1.00 49.72  ?  232 LEU   B CD1 1 
ATOM   3243 C  CD2 . LEU   B 1 76  ? -31.982 1.173   41.114  1.00 55.57  ?  232 LEU   B CD2 1 
ATOM   3244 N  N   . GLU   B 1 77  ? -31.105 1.553   36.133  1.00 45.71  ?  233 GLU   B N   1 
ATOM   3245 C  CA  . GLU   B 1 77  ? -30.553 0.497   35.297  1.00 50.09  ?  233 GLU   B CA  1 
ATOM   3246 C  C   . GLU   B 1 77  ? -29.945 -0.611  36.155  1.00 54.61  ?  233 GLU   B C   1 
ATOM   3247 O  O   . GLU   B 1 77  ? -29.223 -0.355  37.128  1.00 53.03  ?  233 GLU   B O   1 
ATOM   3248 C  CB  . GLU   B 1 77  ? -29.506 1.024   34.311  1.00 50.06  ?  233 GLU   B CB  1 
ATOM   3249 C  CG  . GLU   B 1 77  ? -28.973 -0.121  33.409  1.00 54.84  ?  233 GLU   B CG  1 
ATOM   3250 C  CD  . GLU   B 1 77  ? -27.997 0.315   32.307  1.00 65.59  ?  233 GLU   B CD  1 
ATOM   3251 O  OE1 . GLU   B 1 77  ? -27.565 1.493   32.283  1.00 61.98  ?  233 GLU   B OE1 1 
ATOM   3252 O  OE2 . GLU   B 1 77  ? -27.730 -0.521  31.406  1.00 65.96  -1 233 GLU   B OE2 1 
ATOM   3253 N  N   . VAL   B 1 78  ? -30.258 -1.849  35.792  1.00 55.84  ?  234 VAL   B N   1 
ATOM   3254 C  CA  . VAL   B 1 78  ? -29.685 -3.031  36.429  1.00 52.59  ?  234 VAL   B CA  1 
ATOM   3255 C  C   . VAL   B 1 78  ? -28.836 -3.751  35.392  1.00 56.30  ?  234 VAL   B C   1 
ATOM   3256 O  O   . VAL   B 1 78  ? -29.362 -4.561  34.613  1.00 58.83  ?  234 VAL   B O   1 
ATOM   3257 C  CB  . VAL   B 1 78  ? -30.784 -3.941  37.003  1.00 52.59  ?  234 VAL   B CB  1 
ATOM   3258 C  CG1 . VAL   B 1 78  ? -30.201 -5.311  37.448  1.00 58.76  ?  234 VAL   B CG1 1 
ATOM   3259 C  CG2 . VAL   B 1 78  ? -31.477 -3.257  38.162  1.00 59.64  ?  234 VAL   B CG2 1 
ATOM   3260 N  N   . PRO   B 1 79  ? -27.534 -3.488  35.329  1.00 59.95  ?  235 PRO   B N   1 
ATOM   3261 C  CA  . PRO   B 1 79  ? -26.703 -4.180  34.348  1.00 65.53  ?  235 PRO   B CA  1 
ATOM   3262 C  C   . PRO   B 1 79  ? -26.628 -5.664  34.671  1.00 61.57  ?  235 PRO   B C   1 
ATOM   3263 O  O   . PRO   B 1 79  ? -26.801 -6.080  35.817  1.00 60.65  ?  235 PRO   B O   1 
ATOM   3264 C  CB  . PRO   B 1 79  ? -25.333 -3.509  34.500  1.00 65.84  ?  235 PRO   B CB  1 
ATOM   3265 C  CG  . PRO   B 1 79  ? -25.459 -2.564  35.696  1.00 66.50  ?  235 PRO   B CG  1 
ATOM   3266 C  CD  . PRO   B 1 79  ? -26.722 -2.904  36.410  1.00 64.27  ?  235 PRO   B CD  1 
ATOM   3267 N  N   . ARG   B 1 80  ? -26.406 -6.470  33.629  1.00 68.04  ?  236 ARG   B N   1 
ATOM   3268 C  CA  . ARG   B 1 80  ? -26.116 -7.888  33.794  1.00 63.23  ?  236 ARG   B CA  1 
ATOM   3269 C  C   . ARG   B 1 80  ? -27.281 -8.608  34.462  1.00 59.48  ?  236 ARG   B C   1 
ATOM   3270 O  O   . ARG   B 1 80  ? -27.087 -9.510  35.276  1.00 68.61  ?  236 ARG   B O   1 
ATOM   3271 C  CB  . ARG   B 1 80  ? -24.829 -8.078  34.596  1.00 67.57  ?  236 ARG   B CB  1 
ATOM   3272 C  CG  . ARG   B 1 80  ? -23.605 -7.413  33.986  1.00 70.55  ?  236 ARG   B CG  1 
ATOM   3273 C  CD  . ARG   B 1 80  ? -22.374 -7.605  34.856  1.00 70.37  ?  236 ARG   B CD  1 
ATOM   3274 N  NE  . ARG   B 1 80  ? -22.499 -6.995  36.178  1.00 79.78  ?  236 ARG   B NE  1 
ATOM   3275 C  CZ  . ARG   B 1 80  ? -22.269 -5.713  36.438  1.00 70.32  ?  236 ARG   B CZ  1 
ATOM   3276 N  NH1 . ARG   B 1 80  ? -21.917 -4.866  35.483  1.00 74.49  ?  236 ARG   B NH1 1 
ATOM   3277 N  NH2 . ARG   B 1 80  ? -22.392 -5.270  37.688  1.00 77.44  ?  236 ARG   B NH2 1 
ATOM   3278 N  N   . ILE   B 1 81  ? -28.505 -8.181  34.145  1.00 54.65  ?  237 ILE   B N   1 
ATOM   3279 C  CA  . ILE   B 1 81  ? -29.668 -8.788  34.773  1.00 50.12  ?  237 ILE   B CA  1 
ATOM   3280 C  C   . ILE   B 1 81  ? -29.801 -10.238 34.316  1.00 61.33  ?  237 ILE   B C   1 
ATOM   3281 O  O   . ILE   B 1 81  ? -29.363 -10.613 33.222  1.00 62.62  ?  237 ILE   B O   1 
ATOM   3282 C  CB  . ILE   B 1 81  ? -30.946 -7.982  34.475  1.00 60.82  ?  237 ILE   B CB  1 
ATOM   3283 C  CG1 . ILE   B 1 81  ? -31.954 -8.175  35.607  1.00 59.30  ?  237 ILE   B CG1 1 
ATOM   3284 C  CG2 . ILE   B 1 81  ? -31.560 -8.380  33.127  1.00 54.74  ?  237 ILE   B CG2 1 
ATOM   3285 C  CD1 . ILE   B 1 81  ? -33.331 -7.655  35.291  1.00 46.36  ?  237 ILE   B CD1 1 
ATOM   3286 N  N   . GLN   B 1 82  ? -30.364 -11.076 35.188  1.00 65.77  ?  238 GLN   B N   1 
ATOM   3287 C  CA  . GLN   B 1 82  ? -30.723 -12.447 34.843  1.00 57.09  ?  238 GLN   B CA  1 
ATOM   3288 C  C   . GLN   B 1 82  ? -32.126 -12.714 35.363  1.00 54.03  ?  238 GLN   B C   1 
ATOM   3289 O  O   . GLN   B 1 82  ? -32.360 -12.667 36.575  1.00 56.65  ?  238 GLN   B O   1 
ATOM   3290 C  CB  . GLN   B 1 82  ? -29.713 -13.450 35.409  1.00 65.02  ?  238 GLN   B CB  1 
ATOM   3291 C  CG  . GLN   B 1 82  ? -30.269 -14.839 35.761  1.00 71.10  ?  238 GLN   B CG  1 
ATOM   3292 C  CD  . GLN   B 1 82  ? -30.010 -15.875 34.664  1.00 78.58  ?  238 GLN   B CD  1 
ATOM   3293 O  OE1 . GLN   B 1 82  ? -29.421 -15.565 33.618  1.00 74.98  ?  238 GLN   B OE1 1 
ATOM   3294 N  NE2 . GLN   B 1 82  ? -30.420 -17.118 34.915  1.00 68.25  ?  238 GLN   B NE2 1 
ATOM   3295 N  N   . LEU   B 1 83  ? -33.057 -12.962 34.444  1.00 51.38  ?  239 LEU   B N   1 
ATOM   3296 C  CA  . LEU   B 1 83  ? -34.463 -13.133 34.768  1.00 50.20  ?  239 LEU   B CA  1 
ATOM   3297 C  C   . LEU   B 1 83  ? -34.810 -14.606 34.910  1.00 53.35  ?  239 LEU   B C   1 
ATOM   3298 O  O   . LEU   B 1 83  ? -34.322 -15.448 34.151  1.00 59.23  ?  239 LEU   B O   1 
ATOM   3299 C  CB  . LEU   B 1 83  ? -35.354 -12.513 33.691  1.00 39.63  ?  239 LEU   B CB  1 
ATOM   3300 C  CG  . LEU   B 1 83  ? -35.473 -10.991 33.715  1.00 43.19  ?  239 LEU   B CG  1 
ATOM   3301 C  CD1 . LEU   B 1 83  ? -36.579 -10.523 32.763  1.00 46.70  ?  239 LEU   B CD1 1 
ATOM   3302 C  CD2 . LEU   B 1 83  ? -35.699 -10.495 35.127  1.00 48.14  ?  239 LEU   B CD2 1 
ATOM   3303 N  N   . GLU   B 1 84  ? -35.685 -14.901 35.865  1.00 44.56  ?  240 GLU   B N   1 
ATOM   3304 C  CA  . GLU   B 1 84  ? -36.218 -16.243 36.065  1.00 47.86  ?  240 GLU   B CA  1 
ATOM   3305 C  C   . GLU   B 1 84  ? -37.734 -16.102 36.106  1.00 51.74  ?  240 GLU   B C   1 
ATOM   3306 O  O   . GLU   B 1 84  ? -38.275 -15.506 37.043  1.00 47.17  ?  240 GLU   B O   1 
ATOM   3307 C  CB  . GLU   B 1 84  ? -35.666 -16.867 37.351  1.00 55.83  ?  240 GLU   B CB  1 
ATOM   3308 C  CG  . GLU   B 1 84  ? -36.133 -18.285 37.629  1.00 57.72  ?  240 GLU   B CG  1 
ATOM   3309 C  CD  . GLU   B 1 84  ? -35.525 -18.858 38.899  1.00 66.09  ?  240 GLU   B CD  1 
ATOM   3310 O  OE1 . GLU   B 1 84  ? -34.292 -19.081 38.933  1.00 74.99  ?  240 GLU   B OE1 1 
ATOM   3311 O  OE2 . GLU   B 1 84  ? -36.286 -19.115 39.858  1.00 75.88  -1 240 GLU   B OE2 1 
ATOM   3312 N  N   . GLU   B 1 85  ? -38.409 -16.599 35.064  1.00 45.78  ?  241 GLU   B N   1 
ATOM   3313 C  CA  . GLU   B 1 85  ? -39.861 -16.516 34.995  1.00 47.64  ?  241 GLU   B CA  1 
ATOM   3314 C  C   . GLU   B 1 85  ? -40.498 -17.152 36.221  1.00 45.67  ?  241 GLU   B C   1 
ATOM   3315 O  O   . GLU   B 1 85  ? -40.044 -18.192 36.711  1.00 49.78  ?  241 GLU   B O   1 
ATOM   3316 C  CB  . GLU   B 1 85  ? -40.373 -17.204 33.728  1.00 44.37  ?  241 GLU   B CB  1 
ATOM   3317 C  CG  . GLU   B 1 85  ? -41.872 -17.025 33.496  1.00 49.86  ?  241 GLU   B CG  1 
ATOM   3318 C  CD  . GLU   B 1 85  ? -42.333 -17.566 32.148  1.00 49.06  ?  241 GLU   B CD  1 
ATOM   3319 O  OE1 . GLU   B 1 85  ? -41.479 -18.046 31.375  1.00 58.96  ?  241 GLU   B OE1 1 
ATOM   3320 O  OE2 . GLU   B 1 85  ? -43.543 -17.479 31.853  1.00 48.85  -1 241 GLU   B OE2 1 
ATOM   3321 N  N   . TYR   B 1 86  ? -41.547 -16.518 36.729  1.00 43.63  ?  242 TYR   B N   1 
ATOM   3322 C  CA  . TYR   B 1 86  ? -42.251 -17.032 37.892  1.00 47.24  ?  242 TYR   B CA  1 
ATOM   3323 C  C   . TYR   B 1 86  ? -43.459 -17.836 37.436  1.00 47.24  ?  242 TYR   B C   1 
ATOM   3324 O  O   . TYR   B 1 86  ? -44.393 -17.273 36.855  1.00 50.74  ?  242 TYR   B O   1 
ATOM   3325 C  CB  . TYR   B 1 86  ? -42.689 -15.919 38.843  1.00 42.80  ?  242 TYR   B CB  1 
ATOM   3326 C  CG  . TYR   B 1 86  ? -43.727 -16.383 39.846  1.00 46.68  ?  242 TYR   B CG  1 
ATOM   3327 C  CD1 . TYR   B 1 86  ? -43.374 -17.218 40.900  1.00 54.64  ?  242 TYR   B CD1 1 
ATOM   3328 C  CD2 . TYR   B 1 86  ? -45.063 -16.008 39.729  1.00 55.26  ?  242 TYR   B CD2 1 
ATOM   3329 C  CE1 . TYR   B 1 86  ? -44.309 -17.654 41.823  1.00 59.49  ?  242 TYR   B CE1 1 
ATOM   3330 C  CE2 . TYR   B 1 86  ? -46.009 -16.446 40.650  1.00 52.57  ?  242 TYR   B CE2 1 
ATOM   3331 C  CZ  . TYR   B 1 86  ? -45.622 -17.268 41.696  1.00 60.95  ?  242 TYR   B CZ  1 
ATOM   3332 O  OH  . TYR   B 1 86  ? -46.544 -17.712 42.626  1.00 57.59  ?  242 TYR   B OH  1 
ATOM   3333 N  N   . SER   B 1 87  ? -43.423 -19.144 37.702  1.00 46.45  ?  243 SER   B N   1 
ATOM   3334 C  CA  . SER   B 1 87  ? -44.572 -20.041 37.572  1.00 50.50  ?  243 SER   B CA  1 
ATOM   3335 C  C   . SER   B 1 87  ? -45.316 -19.831 36.250  1.00 47.78  ?  243 SER   B C   1 
ATOM   3336 O  O   . SER   B 1 87  ? -46.534 -19.641 36.217  1.00 60.74  ?  243 SER   B O   1 
ATOM   3337 C  CB  . SER   B 1 87  ? -45.513 -19.877 38.768  1.00 60.26  ?  243 SER   B CB  1 
ATOM   3338 O  OG  . SER   B 1 87  ? -46.660 -20.713 38.664  1.00 63.74  ?  243 SER   B OG  1 
ATOM   3339 N  N   . ASN   B 1 88  ? -44.560 -19.851 35.148  1.00 44.11  ?  244 ASN   B N   1 
ATOM   3340 C  CA  . ASN   B 1 88  ? -45.106 -19.785 33.778  1.00 52.59  ?  244 ASN   B CA  1 
ATOM   3341 C  C   . ASN   B 1 88  ? -45.998 -18.564 33.534  1.00 48.32  ?  244 ASN   B C   1 
ATOM   3342 O  O   . ASN   B 1 88  ? -46.801 -18.565 32.602  1.00 53.79  ?  244 ASN   B O   1 
ATOM   3343 C  CB  . ASN   B 1 88  ? -45.877 -21.066 33.434  1.00 50.75  ?  244 ASN   B CB  1 
ATOM   3344 C  CG  . ASN   B 1 88  ? -44.961 -22.264 33.237  1.00 61.97  ?  244 ASN   B CG  1 
ATOM   3345 O  OD1 . ASN   B 1 88  ? -43.743 -22.112 33.101  1.00 68.29  ?  244 ASN   B OD1 1 
ATOM   3346 N  ND2 . ASN   B 1 88  ? -45.534 -23.471 33.291  1.00 57.45  ?  244 ASN   B ND2 1 
ATOM   3347 N  N   . THR   B 1 89  ? -45.870 -17.501 34.333  1.00 54.30  ?  245 THR   B N   1 
ATOM   3348 C  CA  . THR   B 1 89  ? -46.800 -16.379 34.215  1.00 41.60  ?  245 THR   B CA  1 
ATOM   3349 C  C   . THR   B 1 89  ? -46.549 -15.529 32.977  1.00 43.75  ?  245 THR   B C   1 
ATOM   3350 O  O   . THR   B 1 89  ? -47.418 -14.726 32.616  1.00 42.59  ?  245 THR   B O   1 
ATOM   3351 C  CB  . THR   B 1 89  ? -46.734 -15.485 35.465  1.00 46.60  ?  245 THR   B CB  1 
ATOM   3352 O  OG1 . THR   B 1 89  ? -45.370 -15.169 35.778  1.00 43.58  ?  245 THR   B OG1 1 
ATOM   3353 C  CG2 . THR   B 1 89  ? -47.345 -16.213 36.655  1.00 41.05  ?  245 THR   B CG2 1 
ATOM   3354 N  N   . ARG   B 1 90  ? -45.381 -15.667 32.340  1.00 42.67  ?  246 ARG   B N   1 
ATOM   3355 C  CA  . ARG   B 1 90  ? -45.007 -14.918 31.138  1.00 42.50  ?  246 ARG   B CA  1 
ATOM   3356 C  C   . ARG   B 1 90  ? -44.745 -13.432 31.392  1.00 40.03  ?  246 ARG   B C   1 
ATOM   3357 O  O   . ARG   B 1 90  ? -43.941 -12.816 30.684  1.00 39.08  ?  246 ARG   B O   1 
ATOM   3358 C  CB  . ARG   B 1 90  ? -46.074 -15.105 30.047  1.00 49.03  ?  246 ARG   B CB  1 
ATOM   3359 C  CG  . ARG   B 1 90  ? -46.282 -16.585 29.690  1.00 47.55  ?  246 ARG   B CG  1 
ATOM   3360 C  CD  . ARG   B 1 90  ? -45.464 -17.017 28.461  1.00 49.75  ?  246 ARG   B CD  1 
ATOM   3361 N  NE  . ARG   B 1 90  ? -44.226 -17.682 28.849  1.00 65.03  ?  246 ARG   B NE  1 
ATOM   3362 C  CZ  . ARG   B 1 90  ? -43.103 -17.684 28.140  1.00 51.26  ?  246 ARG   B CZ  1 
ATOM   3363 N  NH1 . ARG   B 1 90  ? -43.080 -17.309 26.874  1.00 59.27  ?  246 ARG   B NH1 1 
ATOM   3364 N  NH2 . ARG   B 1 90  ? -41.977 -18.092 28.712  1.00 64.27  ?  246 ARG   B NH2 1 
ATOM   3365 N  N   . ALA   B 1 91  ? -45.376 -12.844 32.413  1.00 45.00  ?  247 ALA   B N   1 
ATOM   3366 C  CA  . ALA   B 1 91  ? -45.172 -11.434 32.725  1.00 40.49  ?  247 ALA   B CA  1 
ATOM   3367 C  C   . ALA   B 1 91  ? -44.416 -11.161 34.023  1.00 43.71  ?  247 ALA   B C   1 
ATOM   3368 O  O   . ALA   B 1 91  ? -43.894 -10.048 34.175  1.00 36.53  ?  247 ALA   B O   1 
ATOM   3369 C  CB  . ALA   B 1 91  ? -46.520 -10.705 32.802  1.00 41.92  ?  247 ALA   B CB  1 
ATOM   3370 N  N   . TYR   B 1 92  ? -44.367 -12.127 34.956  1.00 39.89  ?  248 TYR   B N   1 
ATOM   3371 C  CA  . TYR   B 1 92  ? -43.766 -11.968 36.279  1.00 42.95  ?  248 TYR   B CA  1 
ATOM   3372 C  C   . TYR   B 1 92  ? -42.456 -12.746 36.365  1.00 42.12  ?  248 TYR   B C   1 
ATOM   3373 O  O   . TYR   B 1 92  ? -42.340 -13.850 35.819  1.00 43.45  ?  248 TYR   B O   1 
ATOM   3374 C  CB  . TYR   B 1 92  ? -44.740 -12.442 37.369  1.00 42.57  ?  248 TYR   B CB  1 
ATOM   3375 C  CG  . TYR   B 1 92  ? -45.971 -11.563 37.483  1.00 48.56  ?  248 TYR   B CG  1 
ATOM   3376 C  CD1 . TYR   B 1 92  ? -47.030 -11.712 36.583  1.00 44.15  ?  248 TYR   B CD1 1 
ATOM   3377 C  CD2 . TYR   B 1 92  ? -46.087 -10.591 38.489  1.00 47.27  ?  248 TYR   B CD2 1 
ATOM   3378 C  CE1 . TYR   B 1 92  ? -48.165 -10.910 36.657  1.00 51.70  ?  248 TYR   B CE1 1 
ATOM   3379 C  CE2 . TYR   B 1 92  ? -47.235 -9.784  38.585  1.00 46.12  ?  248 TYR   B CE2 1 
ATOM   3380 C  CZ  . TYR   B 1 92  ? -48.271 -9.951  37.662  1.00 54.70  ?  248 TYR   B CZ  1 
ATOM   3381 O  OH  . TYR   B 1 92  ? -49.413 -9.166  37.717  1.00 53.78  ?  248 TYR   B OH  1 
ATOM   3382 N  N   . TYR   B 1 93  ? -41.472 -12.173 37.066  1.00 50.70  ?  249 TYR   B N   1 
ATOM   3383 C  CA  . TYR   B 1 93  ? -40.116 -12.708 37.088  1.00 40.40  ?  249 TYR   B CA  1 
ATOM   3384 C  C   . TYR   B 1 93  ? -39.450 -12.424 38.423  1.00 48.31  ?  249 TYR   B C   1 
ATOM   3385 O  O   . TYR   B 1 93  ? -39.743 -11.428 39.093  1.00 42.67  ?  249 TYR   B O   1 
ATOM   3386 C  CB  . TYR   B 1 93  ? -39.245 -12.111 35.966  1.00 37.93  ?  249 TYR   B CB  1 
ATOM   3387 C  CG  . TYR   B 1 93  ? -39.733 -12.423 34.568  1.00 41.65  ?  249 TYR   B CG  1 
ATOM   3388 C  CD1 . TYR   B 1 93  ? -40.794 -11.714 34.011  1.00 40.97  ?  249 TYR   B CD1 1 
ATOM   3389 C  CD2 . TYR   B 1 93  ? -39.098 -13.381 33.782  1.00 43.86  ?  249 TYR   B CD2 1 
ATOM   3390 C  CE1 . TYR   B 1 93  ? -41.258 -11.994 32.751  1.00 43.74  ?  249 TYR   B CE1 1 
ATOM   3391 C  CE2 . TYR   B 1 93  ? -39.546 -13.661 32.487  1.00 41.71  ?  249 TYR   B CE2 1 
ATOM   3392 C  CZ  . TYR   B 1 93  ? -40.629 -12.959 31.981  1.00 43.37  ?  249 TYR   B CZ  1 
ATOM   3393 O  OH  . TYR   B 1 93  ? -41.101 -13.186 30.704  1.00 49.63  ?  249 TYR   B OH  1 
ATOM   3394 N  N   . PHE   B 1 94  ? -38.539 -13.314 38.792  1.00 48.23  ?  250 PHE   B N   1 
ATOM   3395 C  CA  . PHE   B 1 94  ? -37.545 -13.028 39.807  1.00 50.86  ?  250 PHE   B CA  1 
ATOM   3396 C  C   . PHE   B 1 94  ? -36.345 -12.391 39.123  1.00 52.69  ?  250 PHE   B C   1 
ATOM   3397 O  O   . PHE   B 1 94  ? -35.997 -12.751 37.999  1.00 44.96  ?  250 PHE   B O   1 
ATOM   3398 C  CB  . PHE   B 1 94  ? -37.121 -14.303 40.528  1.00 53.58  ?  250 PHE   B CB  1 
ATOM   3399 C  CG  . PHE   B 1 94  ? -38.238 -14.995 41.244  1.00 53.66  ?  250 PHE   B CG  1 
ATOM   3400 C  CD1 . PHE   B 1 94  ? -38.759 -14.472 42.416  1.00 50.29  ?  250 PHE   B CD1 1 
ATOM   3401 C  CD2 . PHE   B 1 94  ? -38.795 -16.152 40.723  1.00 53.75  ?  250 PHE   B CD2 1 
ATOM   3402 C  CE1 . PHE   B 1 94  ? -39.793 -15.129 43.101  1.00 58.77  ?  250 PHE   B CE1 1 
ATOM   3403 C  CE2 . PHE   B 1 94  ? -39.831 -16.806 41.387  1.00 61.69  ?  250 PHE   B CE2 1 
ATOM   3404 C  CZ  . PHE   B 1 94  ? -40.329 -16.296 42.581  1.00 59.46  ?  250 PHE   B CZ  1 
ATOM   3405 N  N   . VAL   B 1 95  ? -35.727 -11.430 39.797  1.00 55.22  ?  251 VAL   B N   1 
ATOM   3406 C  CA  . VAL   B 1 95  ? -34.506 -10.801 39.315  1.00 45.86  ?  251 VAL   B CA  1 
ATOM   3407 C  C   . VAL   B 1 95  ? -33.312 -11.432 40.009  1.00 48.59  ?  251 VAL   B C   1 
ATOM   3408 O  O   . VAL   B 1 95  ? -33.232 -11.430 41.238  1.00 49.71  ?  251 VAL   B O   1 
ATOM   3409 C  CB  . VAL   B 1 95  ? -34.532 -9.283  39.526  1.00 46.92  ?  251 VAL   B CB  1 
ATOM   3410 C  CG1 . VAL   B 1 95  ? -33.375 -8.651  38.806  1.00 48.36  ?  251 VAL   B CG1 1 
ATOM   3411 C  CG2 . VAL   B 1 95  ? -35.805 -8.731  38.929  1.00 53.05  ?  251 VAL   B CG2 1 
ATOM   3412 N  N   . LYS   B 1 96  ? -32.399 -11.974 39.213  1.00 50.01  ?  252 LYS   B N   1 
ATOM   3413 C  CA  . LYS   B 1 96  ? -31.110 -12.471 39.652  1.00 63.58  ?  252 LYS   B CA  1 
ATOM   3414 C  C   . LYS   B 1 96  ? -30.028 -11.733 38.874  1.00 61.26  ?  252 LYS   B C   1 
ATOM   3415 O  O   . LYS   B 1 96  ? -30.311 -10.875 38.038  1.00 61.95  ?  252 LYS   B O   1 
ATOM   3416 C  CB  . LYS   B 1 96  ? -31.015 -13.988 39.469  1.00 58.50  ?  252 LYS   B CB  1 
ATOM   3417 C  CG  . LYS   B 1 96  ? -32.055 -14.732 40.278  1.00 62.32  ?  252 LYS   B CG  1 
ATOM   3418 C  CD  . LYS   B 1 96  ? -32.024 -16.228 40.040  1.00 65.23  ?  252 LYS   B CD  1 
ATOM   3419 C  CE  . LYS   B 1 96  ? -33.153 -16.890 40.811  1.00 67.03  ?  252 LYS   B CE  1 
ATOM   3420 N  NZ  . LYS   B 1 96  ? -32.893 -18.327 41.113  1.00 67.36  ?  252 LYS   B NZ  1 
ATOM   3421 N  N   . PHE   B 1 97  ? -28.775 -12.056 39.167  1.00 68.92  ?  253 PHE   B N   1 
ATOM   3422 C  CA  . PHE   B 1 97  ? -27.658 -11.296 38.625  1.00 69.12  ?  253 PHE   B CA  1 
ATOM   3423 C  C   . PHE   B 1 97  ? -26.608 -12.223 38.037  1.00 71.98  ?  253 PHE   B C   1 
ATOM   3424 O  O   . PHE   B 1 97  ? -26.299 -13.276 38.605  1.00 76.27  ?  253 PHE   B O   1 
ATOM   3425 C  CB  . PHE   B 1 97  ? -27.015 -10.398 39.705  1.00 68.72  ?  253 PHE   B CB  1 
ATOM   3426 C  CG  . PHE   B 1 97  ? -27.970 -9.406  40.282  1.00 68.31  ?  253 PHE   B CG  1 
ATOM   3427 C  CD1 . PHE   B 1 97  ? -28.792 -9.749  41.349  1.00 69.80  ?  253 PHE   B CD1 1 
ATOM   3428 C  CD2 . PHE   B 1 97  ? -28.112 -8.155  39.698  1.00 57.11  ?  253 PHE   B CD2 1 
ATOM   3429 C  CE1 . PHE   B 1 97  ? -29.703 -8.833  41.855  1.00 71.72  ?  253 PHE   B CE1 1 
ATOM   3430 C  CE2 . PHE   B 1 97  ? -29.017 -7.243  40.191  1.00 58.49  ?  253 PHE   B CE2 1 
ATOM   3431 C  CZ  . PHE   B 1 97  ? -29.818 -7.580  41.268  1.00 64.45  ?  253 PHE   B CZ  1 
ATOM   3432 N  N   . LYS   B 1 98  ? -26.046 -11.806 36.910  1.00 72.54  ?  254 LYS   B N   1 
ATOM   3433 C  CA  . LYS   B 1 98  ? -24.954 -12.548 36.299  1.00 72.23  ?  254 LYS   B CA  1 
ATOM   3434 C  C   . LYS   B 1 98  ? -23.615 -12.242 36.979  1.00 62.79  ?  254 LYS   B C   1 
ATOM   3435 O  O   . LYS   B 1 98  ? -23.323 -12.757 38.063  1.00 75.92  ?  254 LYS   B O   1 
ATOM   3436 C  CB  . LYS   B 1 98  ? -24.891 -12.223 34.814  1.00 67.85  ?  254 LYS   B CB  1 
ATOM   3437 C  CG  . LYS   B 1 98  ? -26.196 -12.523 34.110  1.00 72.25  ?  254 LYS   B CG  1 
ATOM   3438 C  CD  . LYS   B 1 98  ? -26.301 -11.789 32.802  1.00 70.50  ?  254 LYS   B CD  1 
ATOM   3439 C  CE  . LYS   B 1 98  ? -26.446 -12.775 31.662  1.00 75.42  ?  254 LYS   B CE  1 
ATOM   3440 N  NZ  . LYS   B 1 98  ? -25.132 -13.362 31.268  1.00 72.80  ?  254 LYS   B NZ  1 
ATOM   3441 N  N   . ASN   B 1 104 ? -21.893 -4.918  43.285  1.00 70.62  ?  260 ASN   B N   1 
ATOM   3442 C  CA  . ASN   B 1 104 ? -23.300 -4.824  42.888  1.00 70.76  ?  260 ASN   B CA  1 
ATOM   3443 C  C   . ASN   B 1 104 ? -23.979 -3.842  43.839  1.00 66.58  ?  260 ASN   B C   1 
ATOM   3444 O  O   . ASN   B 1 104 ? -24.044 -4.097  45.057  1.00 63.36  ?  260 ASN   B O   1 
ATOM   3445 C  CB  . ASN   B 1 104 ? -23.969 -6.202  42.947  1.00 69.27  ?  260 ASN   B CB  1 
ATOM   3446 C  CG  . ASN   B 1 104 ? -25.393 -6.209  42.396  1.00 65.79  ?  260 ASN   B CG  1 
ATOM   3447 O  OD1 . ASN   B 1 104 ? -26.076 -5.186  42.350  1.00 61.21  ?  260 ASN   B OD1 1 
ATOM   3448 N  ND2 . ASN   B 1 104 ? -25.854 -7.390  42.004  1.00 72.71  ?  260 ASN   B ND2 1 
ATOM   3449 N  N   . PRO   B 1 105 ? -24.453 -2.711  43.303  1.00 59.27  ?  261 PRO   B N   1 
ATOM   3450 C  CA  . PRO   B 1 105 ? -25.030 -1.672  44.179  1.00 60.11  ?  261 PRO   B CA  1 
ATOM   3451 C  C   . PRO   B 1 105 ? -26.287 -2.112  44.911  1.00 61.19  ?  261 PRO   B C   1 
ATOM   3452 O  O   . PRO   B 1 105 ? -26.605 -1.545  45.966  1.00 59.12  ?  261 PRO   B O   1 
ATOM   3453 C  CB  . PRO   B 1 105 ? -25.320 -0.518  43.212  1.00 59.63  ?  261 PRO   B CB  1 
ATOM   3454 C  CG  . PRO   B 1 105 ? -24.352 -0.723  42.080  1.00 69.67  ?  261 PRO   B CG  1 
ATOM   3455 C  CD  . PRO   B 1 105 ? -24.223 -2.218  41.934  1.00 67.24  ?  261 PRO   B CD  1 
ATOM   3456 N  N   . LEU   B 1 106 ? -26.991 -3.120  44.408  1.00 56.18  ?  262 LEU   B N   1 
ATOM   3457 C  CA  . LEU   B 1 106 ? -28.225 -3.599  45.010  1.00 55.70  ?  262 LEU   B CA  1 
ATOM   3458 C  C   . LEU   B 1 106 ? -28.016 -4.761  45.966  1.00 52.02  ?  262 LEU   B C   1 
ATOM   3459 O  O   . LEU   B 1 106 ? -29.007 -5.301  46.464  1.00 52.01  ?  262 LEU   B O   1 
ATOM   3460 C  CB  . LEU   B 1 106 ? -29.215 -4.016  43.906  1.00 50.55  ?  262 LEU   B CB  1 
ATOM   3461 C  CG  . LEU   B 1 106 ? -29.502 -2.925  42.874  1.00 55.94  ?  262 LEU   B CG  1 
ATOM   3462 C  CD1 . LEU   B 1 106 ? -30.645 -3.295  41.896  1.00 46.41  ?  262 LEU   B CD1 1 
ATOM   3463 C  CD2 . LEU   B 1 106 ? -29.830 -1.647  43.619  1.00 53.55  ?  262 LEU   B CD2 1 
ATOM   3464 N  N   . SER   B 1 107 ? -26.763 -5.154  46.249  1.00 53.85  ?  263 SER   B N   1 
ATOM   3465 C  CA  . SER   B 1 107 ? -26.541 -6.383  47.003  1.00 54.77  ?  263 SER   B CA  1 
ATOM   3466 C  C   . SER   B 1 107 ? -27.171 -6.322  48.386  1.00 60.24  ?  263 SER   B C   1 
ATOM   3467 O  O   . SER   B 1 107 ? -27.455 -7.367  48.979  1.00 56.99  ?  263 SER   B O   1 
ATOM   3468 C  CB  . SER   B 1 107 ? -25.048 -6.686  47.161  1.00 73.01  ?  263 SER   B CB  1 
ATOM   3469 O  OG  . SER   B 1 107 ? -24.286 -5.527  47.451  1.00 79.54  ?  263 SER   B OG  1 
ATOM   3470 N  N   . GLN   B 1 108 ? -27.414 -5.119  48.903  1.00 59.41  ?  264 GLN   B N   1 
ATOM   3471 C  CA  . GLN   B 1 108 ? -28.066 -5.001  50.199  1.00 57.27  ?  264 GLN   B CA  1 
ATOM   3472 C  C   . GLN   B 1 108 ? -29.539 -5.381  50.138  1.00 56.04  ?  264 GLN   B C   1 
ATOM   3473 O  O   . GLN   B 1 108 ? -30.193 -5.416  51.183  1.00 64.37  ?  264 GLN   B O   1 
ATOM   3474 C  CB  . GLN   B 1 108 ? -27.931 -3.569  50.730  1.00 60.24  ?  264 GLN   B CB  1 
ATOM   3475 C  CG  . GLN   B 1 108 ? -28.710 -2.515  49.885  1.00 57.03  ?  264 GLN   B CG  1 
ATOM   3476 C  CD  . GLN   B 1 108 ? -28.449 -1.099  50.368  1.00 66.57  ?  264 GLN   B CD  1 
ATOM   3477 O  OE1 . GLN   B 1 108 ? -29.259 -0.511  51.091  1.00 61.75  ?  264 GLN   B OE1 1 
ATOM   3478 N  NE2 . GLN   B 1 108 ? -27.333 -0.527  49.931  1.00 67.61  ?  264 GLN   B NE2 1 
ATOM   3479 N  N   . PHE   B 1 109 ? -30.080 -5.650  48.952  1.00 63.54  ?  265 PHE   B N   1 
ATOM   3480 C  CA  . PHE   B 1 109 ? -31.474 -6.039  48.821  1.00 61.31  ?  265 PHE   B CA  1 
ATOM   3481 C  C   . PHE   B 1 109 ? -31.642 -7.516  48.502  1.00 59.70  ?  265 PHE   B C   1 
ATOM   3482 O  O   . PHE   B 1 109 ? -32.766 -7.960  48.270  1.00 57.07  ?  265 PHE   B O   1 
ATOM   3483 C  CB  . PHE   B 1 109 ? -32.174 -5.203  47.747  1.00 57.01  ?  265 PHE   B CB  1 
ATOM   3484 C  CG  . PHE   B 1 109 ? -32.129 -3.721  48.000  1.00 58.06  ?  265 PHE   B CG  1 
ATOM   3485 C  CD1 . PHE   B 1 109 ? -32.578 -3.188  49.202  1.00 63.78  ?  265 PHE   B CD1 1 
ATOM   3486 C  CD2 . PHE   B 1 109 ? -31.677 -2.854  47.014  1.00 56.02  ?  265 PHE   B CD2 1 
ATOM   3487 C  CE1 . PHE   B 1 109 ? -32.537 -1.819  49.425  1.00 65.68  ?  265 PHE   B CE1 1 
ATOM   3488 C  CE2 . PHE   B 1 109 ? -31.643 -1.489  47.233  1.00 59.59  ?  265 PHE   B CE2 1 
ATOM   3489 C  CZ  . PHE   B 1 109 ? -32.082 -0.970  48.427  1.00 55.04  ?  265 PHE   B CZ  1 
ATOM   3490 N  N   . LEU   B 1 110 ? -30.567 -8.296  48.513  1.00 66.56  ?  266 LEU   B N   1 
ATOM   3491 C  CA  . LEU   B 1 110 ? -30.679 -9.681  48.085  1.00 63.33  ?  266 LEU   B CA  1 
ATOM   3492 C  C   . LEU   B 1 110 ? -31.364 -10.537 49.147  1.00 60.02  ?  266 LEU   B C   1 
ATOM   3493 O  O   . LEU   B 1 110 ? -31.207 -10.327 50.355  1.00 60.61  ?  266 LEU   B O   1 
ATOM   3494 C  CB  . LEU   B 1 110 ? -29.304 -10.273 47.787  1.00 55.69  ?  266 LEU   B CB  1 
ATOM   3495 C  CG  . LEU   B 1 110 ? -28.817 -10.164 46.340  1.00 69.74  ?  266 LEU   B CG  1 
ATOM   3496 C  CD1 . LEU   B 1 110 ? -27.333 -10.520 46.289  1.00 68.47  ?  266 LEU   B CD1 1 
ATOM   3497 C  CD2 . LEU   B 1 110 ? -29.672 -10.901 45.271  1.00 64.13  ?  266 LEU   B CD2 1 
ATOM   3498 N  N   . GLU   B 1 111 ? -32.139 -11.511 48.679  1.00 59.66  ?  267 GLU   B N   1 
ATOM   3499 C  CA  . GLU   B 1 111 ? -32.506 -12.684 49.467  1.00 68.61  ?  267 GLU   B CA  1 
ATOM   3500 C  C   . GLU   B 1 111 ? -31.934 -13.888 48.737  1.00 66.18  ?  267 GLU   B C   1 
ATOM   3501 O  O   . GLU   B 1 111 ? -32.446 -14.279 47.680  1.00 61.51  ?  267 GLU   B O   1 
ATOM   3502 C  CB  . GLU   B 1 111 ? -34.015 -12.819 49.646  1.00 71.20  ?  267 GLU   B CB  1 
ATOM   3503 C  CG  . GLU   B 1 111 ? -34.716 -11.539 49.994  1.00 71.39  ?  267 GLU   B CG  1 
ATOM   3504 C  CD  . GLU   B 1 111 ? -35.593 -11.668 51.224  1.00 75.61  ?  267 GLU   B CD  1 
ATOM   3505 O  OE1 . GLU   B 1 111 ? -35.097 -12.069 52.313  1.00 70.90  ?  267 GLU   B OE1 1 
ATOM   3506 O  OE2 . GLU   B 1 111 ? -36.805 -11.381 51.072  1.00 86.34  -1 267 GLU   B OE2 1 
ATOM   3507 N  N   . GLY   B 1 112 ? -30.876 -14.465 49.303  1.00 67.30  ?  268 GLY   B N   1 
ATOM   3508 C  CA  . GLY   B 1 112 ? -30.130 -15.492 48.613  1.00 64.09  ?  268 GLY   B CA  1 
ATOM   3509 C  C   . GLY   B 1 112 ? -29.696 -15.024 47.243  1.00 65.67  ?  268 GLY   B C   1 
ATOM   3510 O  O   . GLY   B 1 112 ? -28.809 -14.174 47.120  1.00 66.62  ?  268 GLY   B O   1 
ATOM   3511 N  N   . GLU   B 1 113 ? -30.336 -15.554 46.202  1.00 63.16  ?  269 GLU   B N   1 
ATOM   3512 C  CA  . GLU   B 1 113 ? -29.993 -15.195 44.835  1.00 64.58  ?  269 GLU   B CA  1 
ATOM   3513 C  C   . GLU   B 1 113 ? -30.868 -14.102 44.241  1.00 62.68  ?  269 GLU   B C   1 
ATOM   3514 O  O   . GLU   B 1 113 ? -30.457 -13.481 43.251  1.00 66.33  ?  269 GLU   B O   1 
ATOM   3515 C  CB  . GLU   B 1 113 ? -30.063 -16.429 43.924  1.00 72.32  ?  269 GLU   B CB  1 
ATOM   3516 C  CG  . GLU   B 1 113 ? -28.713 -17.032 43.543  1.00 74.49  ?  269 GLU   B CG  1 
ATOM   3517 C  CD  . GLU   B 1 113 ? -28.732 -17.599 42.125  1.00 83.90  ?  269 GLU   B CD  1 
ATOM   3518 O  OE1 . GLU   B 1 113 ? -28.077 -17.021 41.223  1.00 77.85  ?  269 GLU   B OE1 1 
ATOM   3519 O  OE2 . GLU   B 1 113 ? -29.394 -18.642 41.924  1.00 91.06  -1 269 GLU   B OE2 1 
ATOM   3520 N  N   . ILE   B 1 114 ? -32.053 -13.848 44.802  1.00 64.73  ?  270 ILE   B N   1 
ATOM   3521 C  CA  . ILE   B 1 114 ? -33.047 -12.985 44.159  1.00 55.80  ?  270 ILE   B CA  1 
ATOM   3522 C  C   . ILE   B 1 114 ? -33.018 -11.591 44.772  1.00 57.80  ?  270 ILE   B C   1 
ATOM   3523 O  O   . ILE   B 1 114 ? -32.743 -11.415 45.972  1.00 58.44  ?  270 ILE   B O   1 
ATOM   3524 C  CB  . ILE   B 1 114 ? -34.464 -13.588 44.244  1.00 57.88  ?  270 ILE   B CB  1 
ATOM   3525 C  CG1 . ILE   B 1 114 ? -35.013 -13.471 45.670  1.00 60.83  ?  270 ILE   B CG1 1 
ATOM   3526 C  CG2 . ILE   B 1 114 ? -34.485 -15.026 43.709  1.00 57.20  ?  270 ILE   B CG2 1 
ATOM   3527 C  CD1 . ILE   B 1 114 ? -36.507 -13.367 45.754  1.00 63.32  ?  270 ILE   B CD1 1 
ATOM   3528 N  N   . LEU   B 1 115 ? -33.273 -10.597 43.925  1.00 55.53  ?  271 LEU   B N   1 
ATOM   3529 C  CA  . LEU   B 1 115 ? -33.490 -9.226  44.369  1.00 53.38  ?  271 LEU   B CA  1 
ATOM   3530 C  C   . LEU   B 1 115 ? -34.817 -9.146  45.102  1.00 55.19  ?  271 LEU   B C   1 
ATOM   3531 O  O   . LEU   B 1 115 ? -35.863 -9.457  44.522  1.00 55.71  ?  271 LEU   B O   1 
ATOM   3532 C  CB  . LEU   B 1 115 ? -33.520 -8.288  43.164  1.00 48.65  ?  271 LEU   B CB  1 
ATOM   3533 C  CG  . LEU   B 1 115 ? -33.185 -6.797  43.283  1.00 49.65  ?  271 LEU   B CG  1 
ATOM   3534 C  CD1 . LEU   B 1 115 ? -32.163 -6.470  44.382  1.00 60.54  ?  271 LEU   B CD1 1 
ATOM   3535 C  CD2 . LEU   B 1 115 ? -32.868 -6.116  41.909  1.00 47.29  ?  271 LEU   B CD2 1 
ATOM   3536 N  N   . SER   B 1 116 ? -34.800 -8.704  46.357  1.00 51.22  ?  272 SER   B N   1 
ATOM   3537 C  CA  . SER   B 1 116 ? -36.050 -8.557  47.098  1.00 52.60  ?  272 SER   B CA  1 
ATOM   3538 C  C   . SER   B 1 116 ? -36.743 -7.269  46.660  1.00 58.14  ?  272 SER   B C   1 
ATOM   3539 O  O   . SER   B 1 116 ? -36.233 -6.165  46.899  1.00 56.27  ?  272 SER   B O   1 
ATOM   3540 C  CB  . SER   B 1 116 ? -35.813 -8.543  48.600  1.00 57.03  ?  272 SER   B CB  1 
ATOM   3541 O  OG  . SER   B 1 116 ? -37.003 -8.183  49.280  1.00 55.80  ?  272 SER   B OG  1 
ATOM   3542 N  N   . ALA   B 1 117 ? -37.908 -7.408  46.027  1.00 50.85  ?  273 ALA   B N   1 
ATOM   3543 C  CA  . ALA   B 1 117 ? -38.747 -6.245  45.777  1.00 50.98  ?  273 ALA   B CA  1 
ATOM   3544 C  C   . ALA   B 1 117 ? -39.231 -5.639  47.087  1.00 54.50  ?  273 ALA   B C   1 
ATOM   3545 O  O   . ALA   B 1 117 ? -39.303 -4.413  47.216  1.00 49.62  ?  273 ALA   B O   1 
ATOM   3546 C  CB  . ALA   B 1 117 ? -39.922 -6.626  44.868  1.00 48.89  ?  273 ALA   B CB  1 
ATOM   3547 N  N   . SER   B 1 118 ? -39.528 -6.488  48.085  1.00 50.31  ?  274 SER   B N   1 
ATOM   3548 C  CA  . SER   B 1 118 ? -39.951 -6.007  49.399  1.00 56.93  ?  274 SER   B CA  1 
ATOM   3549 C  C   . SER   B 1 118 ? -38.899 -5.106  50.022  1.00 56.51  ?  274 SER   B C   1 
ATOM   3550 O  O   . SER   B 1 118 ? -39.219 -4.049  50.578  1.00 59.97  ?  274 SER   B O   1 
ATOM   3551 C  CB  . SER   B 1 118 ? -40.233 -7.184  50.346  1.00 54.37  ?  274 SER   B CB  1 
ATOM   3552 O  OG  . SER   B 1 118 ? -41.352 -7.944  49.919  1.00 66.44  ?  274 SER   B OG  1 
ATOM   3553 N  N   . LYS   B 1 119 ? -37.639 -5.540  49.980  1.00 56.83  ?  275 LYS   B N   1 
ATOM   3554 C  CA  . LYS   B 1 119 ? -36.551 -4.751  50.544  1.00 54.48  ?  275 LYS   B CA  1 
ATOM   3555 C  C   . LYS   B 1 119 ? -36.299 -3.499  49.710  1.00 53.70  ?  275 LYS   B C   1 
ATOM   3556 O  O   . LYS   B 1 119 ? -36.176 -2.395  50.254  1.00 56.83  ?  275 LYS   B O   1 
ATOM   3557 C  CB  . LYS   B 1 119 ? -35.279 -5.599  50.632  1.00 52.48  ?  275 LYS   B CB  1 
ATOM   3558 C  CG  . LYS   B 1 119 ? -35.304 -6.735  51.668  1.00 56.85  ?  275 LYS   B CG  1 
ATOM   3559 C  CD  . LYS   B 1 119 ? -33.952 -7.452  51.652  1.00 62.72  ?  275 LYS   B CD  1 
ATOM   3560 C  CE  . LYS   B 1 119 ? -33.856 -8.562  52.671  1.00 66.62  ?  275 LYS   B CE  1 
ATOM   3561 N  NZ  . LYS   B 1 119 ? -32.481 -9.124  52.639  1.00 77.95  ?  275 LYS   B NZ  1 
ATOM   3562 N  N   . MET   B 1 120 ? -36.197 -3.656  48.388  1.00 49.27  ?  276 MET   B N   1 
ATOM   3563 C  CA  . MET   B 1 120 ? -35.968 -2.501  47.522  1.00 57.61  ?  276 MET   B CA  1 
ATOM   3564 C  C   . MET   B 1 120 ? -37.034 -1.433  47.732  1.00 57.53  ?  276 MET   B C   1 
ATOM   3565 O  O   . MET   B 1 120 ? -36.723 -0.245  47.887  1.00 59.85  ?  276 MET   B O   1 
ATOM   3566 C  CB  . MET   B 1 120 ? -35.941 -2.925  46.061  1.00 58.14  ?  276 MET   B CB  1 
ATOM   3567 C  CG  . MET   B 1 120 ? -35.259 -1.931  45.141  1.00 66.62  ?  276 MET   B CG  1 
ATOM   3568 S  SD  . MET   B 1 120 ? -34.345 -2.680  43.786  1.00 57.66  ?  276 MET   B SD  1 
ATOM   3569 C  CE  . MET   B 1 120 ? -33.962 -1.234  42.822  1.00 53.42  ?  276 MET   B CE  1 
ATOM   3570 N  N   . LEU   B 1 121 ? -38.298 -1.850  47.771  1.00 55.48  ?  277 LEU   B N   1 
ATOM   3571 C  CA  . LEU   B 1 121 ? -39.399 -0.910  47.934  1.00 54.07  ?  277 LEU   B CA  1 
ATOM   3572 C  C   . LEU   B 1 121 ? -39.387 -0.260  49.305  1.00 55.59  ?  277 LEU   B C   1 
ATOM   3573 O  O   . LEU   B 1 121 ? -39.623 0.948   49.420  1.00 54.32  ?  277 LEU   B O   1 
ATOM   3574 C  CB  . LEU   B 1 121 ? -40.731 -1.616  47.721  1.00 53.53  ?  277 LEU   B CB  1 
ATOM   3575 C  CG  . LEU   B 1 121 ? -41.144 -1.842  46.293  1.00 45.99  ?  277 LEU   B CG  1 
ATOM   3576 C  CD1 . LEU   B 1 121 ? -42.530 -2.430  46.312  1.00 54.42  ?  277 LEU   B CD1 1 
ATOM   3577 C  CD2 . LEU   B 1 121 ? -41.151 -0.487  45.654  1.00 48.11  ?  277 LEU   B CD2 1 
ATOM   3578 N  N   . SER   B 1 122 ? -39.148 -1.045  50.359  1.00 54.24  ?  278 SER   B N   1 
ATOM   3579 C  CA  . SER   B 1 122 ? -39.110 -0.470  51.698  1.00 55.74  ?  278 SER   B CA  1 
ATOM   3580 C  C   . SER   B 1 122 ? -38.142 0.702   51.751  1.00 54.84  ?  278 SER   B C   1 
ATOM   3581 O  O   . SER   B 1 122 ? -38.444 1.740   52.356  1.00 52.08  ?  278 SER   B O   1 
ATOM   3582 C  CB  . SER   B 1 122 ? -38.718 -1.534  52.736  1.00 61.12  ?  278 SER   B CB  1 
ATOM   3583 O  OG  . SER   B 1 122 ? -39.690 -2.562  52.832  1.00 72.12  ?  278 SER   B OG  1 
ATOM   3584 N  N   . LYS   B 1 123 ? -36.972 0.559   51.118  1.00 50.93  ?  279 LYS   B N   1 
ATOM   3585 C  CA  . LYS   B 1 123 ? -35.974 1.624   51.190  1.00 59.44  ?  279 LYS   B CA  1 
ATOM   3586 C  C   . LYS   B 1 123 ? -36.381 2.804   50.327  1.00 54.73  ?  279 LYS   B C   1 
ATOM   3587 O  O   . LYS   B 1 123 ? -36.216 3.966   50.728  1.00 54.26  ?  279 LYS   B O   1 
ATOM   3588 C  CB  . LYS   B 1 123 ? -34.593 1.120   50.762  1.00 60.71  ?  279 LYS   B CB  1 
ATOM   3589 C  CG  . LYS   B 1 123 ? -33.490 2.146   51.039  1.00 64.84  ?  279 LYS   B CG  1 
ATOM   3590 C  CD  . LYS   B 1 123 ? -32.088 1.672   50.699  1.00 63.63  ?  279 LYS   B CD  1 
ATOM   3591 C  CE  . LYS   B 1 123 ? -31.066 2.553   51.424  1.00 60.33  ?  279 LYS   B CE  1 
ATOM   3592 N  NZ  . LYS   B 1 123 ? -29.673 2.267   51.014  1.00 64.77  ?  279 LYS   B NZ  1 
ATOM   3593 N  N   . PHE   B 1 124 ? -36.890 2.509   49.127  1.00 61.48  ?  280 PHE   B N   1 
ATOM   3594 C  CA  . PHE   B 1 124 ? -37.414 3.524   48.220  1.00 51.82  ?  280 PHE   B CA  1 
ATOM   3595 C  C   . PHE   B 1 124 ? -38.458 4.388   48.925  1.00 52.76  ?  280 PHE   B C   1 
ATOM   3596 O  O   . PHE   B 1 124 ? -38.354 5.619   48.943  1.00 55.15  ?  280 PHE   B O   1 
ATOM   3597 C  CB  . PHE   B 1 124 ? -37.992 2.820   46.996  1.00 47.55  ?  280 PHE   B CB  1 
ATOM   3598 C  CG  . PHE   B 1 124 ? -38.434 3.745   45.882  1.00 46.62  ?  280 PHE   B CG  1 
ATOM   3599 C  CD1 . PHE   B 1 124 ? -37.501 4.331   45.052  1.00 42.71  ?  280 PHE   B CD1 1 
ATOM   3600 C  CD2 . PHE   B 1 124 ? -39.776 3.975   45.634  1.00 48.47  ?  280 PHE   B CD2 1 
ATOM   3601 C  CE1 . PHE   B 1 124 ? -37.889 5.163   44.007  1.00 45.10  ?  280 PHE   B CE1 1 
ATOM   3602 C  CE2 . PHE   B 1 124 ? -40.175 4.807   44.590  1.00 40.90  ?  280 PHE   B CE2 1 
ATOM   3603 C  CZ  . PHE   B 1 124 ? -39.229 5.396   43.771  1.00 46.28  ?  280 PHE   B CZ  1 
ATOM   3604 N  N   . ARG   B 1 125 ? -39.445 3.747   49.556  1.00 47.47  ?  281 ARG   B N   1 
ATOM   3605 C  CA  . ARG   B 1 125 ? -40.450 4.466   50.331  1.00 51.26  ?  281 ARG   B CA  1 
ATOM   3606 C  C   . ARG   B 1 125 ? -39.822 5.256   51.471  1.00 56.45  ?  281 ARG   B C   1 
ATOM   3607 O  O   . ARG   B 1 125 ? -40.208 6.401   51.732  1.00 56.40  ?  281 ARG   B O   1 
ATOM   3608 C  CB  . ARG   B 1 125 ? -41.482 3.481   50.879  1.00 56.08  ?  281 ARG   B CB  1 
ATOM   3609 C  CG  . ARG   B 1 125 ? -42.159 2.637   49.801  1.00 52.96  ?  281 ARG   B CG  1 
ATOM   3610 C  CD  . ARG   B 1 125 ? -43.606 2.365   50.150  1.00 70.97  ?  281 ARG   B CD  1 
ATOM   3611 N  NE  . ARG   B 1 125 ? -43.780 0.979   50.577  1.00 82.66  ?  281 ARG   B NE  1 
ATOM   3612 C  CZ  . ARG   B 1 125 ? -44.564 0.099   49.965  1.00 62.71  ?  281 ARG   B CZ  1 
ATOM   3613 N  NH1 . ARG   B 1 125 ? -45.334 0.450   48.955  1.00 55.78  ?  281 ARG   B NH1 1 
ATOM   3614 N  NH2 . ARG   B 1 125 ? -44.597 -1.159  50.400  1.00 71.13  ?  281 ARG   B NH2 1 
ATOM   3615 N  N   . LYS   B 1 126 ? -38.873 4.647   52.190  1.00 53.91  ?  282 LYS   B N   1 
ATOM   3616 C  CA  . LYS   B 1 126 ? -38.283 5.333   53.329  1.00 57.42  ?  282 LYS   B CA  1 
ATOM   3617 C  C   . LYS   B 1 126 ? -37.592 6.611   52.886  1.00 55.18  ?  282 LYS   B C   1 
ATOM   3618 O  O   . LYS   B 1 126 ? -37.805 7.680   53.470  1.00 57.21  ?  282 LYS   B O   1 
ATOM   3619 C  CB  . LYS   B 1 126 ? -37.306 4.409   54.065  1.00 63.52  ?  282 LYS   B CB  1 
ATOM   3620 C  CG  . LYS   B 1 126 ? -36.246 5.168   54.816  1.00 63.81  ?  282 LYS   B CG  1 
ATOM   3621 C  CD  . LYS   B 1 126 ? -34.902 4.441   54.815  1.00 78.31  ?  282 LYS   B CD  1 
ATOM   3622 C  CE  . LYS   B 1 126 ? -34.956 3.087   55.513  1.00 75.26  ?  282 LYS   B CE  1 
ATOM   3623 N  NZ  . LYS   B 1 126 ? -35.413 3.196   56.929  1.00 73.12  ?  282 LYS   B NZ  1 
ATOM   3624 N  N   . ILE   B 1 127 ? -36.761 6.520   51.847  1.00 52.51  ?  283 ILE   B N   1 
ATOM   3625 C  CA  . ILE   B 1 127 ? -36.040 7.700   51.374  1.00 60.81  ?  283 ILE   B CA  1 
ATOM   3626 C  C   . ILE   B 1 127 ? -37.017 8.791   50.948  1.00 60.03  ?  283 ILE   B C   1 
ATOM   3627 O  O   . ILE   B 1 127 ? -36.878 9.955   51.342  1.00 63.04  ?  283 ILE   B O   1 
ATOM   3628 C  CB  . ILE   B 1 127 ? -35.062 7.335   50.240  1.00 54.68  ?  283 ILE   B CB  1 
ATOM   3629 C  CG1 . ILE   B 1 127 ? -33.900 6.496   50.780  1.00 64.55  ?  283 ILE   B CG1 1 
ATOM   3630 C  CG2 . ILE   B 1 127 ? -34.497 8.594   49.616  1.00 59.67  ?  283 ILE   B CG2 1 
ATOM   3631 C  CD1 . ILE   B 1 127 ? -33.031 5.883   49.702  1.00 59.00  ?  283 ILE   B CD1 1 
ATOM   3632 N  N   . ILE   B 1 128 ? -38.034 8.427   50.160  1.00 56.42  ?  284 ILE   B N   1 
ATOM   3633 C  CA  . ILE   B 1 128 ? -39.007 9.418   49.694  1.00 53.04  ?  284 ILE   B CA  1 
ATOM   3634 C  C   . ILE   B 1 128 ? -39.739 10.059  50.868  1.00 62.86  ?  284 ILE   B C   1 
ATOM   3635 O  O   . ILE   B 1 128 ? -39.893 11.287  50.919  1.00 57.08  ?  284 ILE   B O   1 
ATOM   3636 C  CB  . ILE   B 1 128 ? -39.986 8.790   48.679  1.00 53.93  ?  284 ILE   B CB  1 
ATOM   3637 C  CG1 . ILE   B 1 128 ? -39.275 8.525   47.347  1.00 52.75  ?  284 ILE   B CG1 1 
ATOM   3638 C  CG2 . ILE   B 1 128 ? -41.196 9.693   48.456  1.00 56.44  ?  284 ILE   B CG2 1 
ATOM   3639 C  CD1 . ILE   B 1 128 ? -40.080 7.710   46.351  1.00 47.54  ?  284 ILE   B CD1 1 
ATOM   3640 N  N   . LYS   B 1 129 ? -40.190 9.244   51.834  1.00 55.49  ?  285 LYS   B N   1 
ATOM   3641 C  CA  . LYS   B 1 129 ? -40.882 9.784   53.002  1.00 65.10  ?  285 LYS   B CA  1 
ATOM   3642 C  C   . LYS   B 1 129 ? -40.012 10.785  53.750  1.00 66.65  ?  285 LYS   B C   1 
ATOM   3643 O  O   . LYS   B 1 129 ? -40.507 11.814  54.226  1.00 63.82  ?  285 LYS   B O   1 
ATOM   3644 C  CB  . LYS   B 1 129 ? -41.314 8.653   53.938  1.00 65.91  ?  285 LYS   B CB  1 
ATOM   3645 C  CG  . LYS   B 1 129 ? -42.497 9.021   54.823  1.00 69.15  ?  285 LYS   B CG  1 
ATOM   3646 C  CD  . LYS   B 1 129 ? -42.857 7.894   55.767  1.00 66.92  ?  285 LYS   B CD  1 
ATOM   3647 C  CE  . LYS   B 1 129 ? -43.357 8.390   57.115  1.00 70.75  ?  285 LYS   B CE  1 
ATOM   3648 N  NZ  . LYS   B 1 129 ? -44.622 9.175   57.035  1.00 71.77  ?  285 LYS   B NZ  1 
ATOM   3649 N  N   . GLU   B 1 130 ? -38.708 10.504  53.847  1.00 70.94  ?  286 GLU   B N   1 
ATOM   3650 C  CA  . GLU   B 1 130 ? -37.791 11.417  54.525  1.00 70.31  ?  286 GLU   B CA  1 
ATOM   3651 C  C   . GLU   B 1 130 ? -37.548 12.683  53.711  1.00 65.59  ?  286 GLU   B C   1 
ATOM   3652 O  O   . GLU   B 1 130 ? -37.412 13.772  54.279  1.00 75.88  ?  286 GLU   B O   1 
ATOM   3653 C  CB  . GLU   B 1 130 ? -36.483 10.686  54.841  1.00 67.54  ?  286 GLU   B CB  1 
ATOM   3654 C  CG  . GLU   B 1 130 ? -36.662 9.603   55.913  1.00 69.32  ?  286 GLU   B CG  1 
ATOM   3655 C  CD  . GLU   B 1 130 ? -35.356 8.982   56.361  1.00 74.00  ?  286 GLU   B CD  1 
ATOM   3656 O  OE1 . GLU   B 1 130 ? -34.305 9.312   55.766  1.00 81.70  ?  286 GLU   B OE1 1 
ATOM   3657 O  OE2 . GLU   B 1 130 ? -35.378 8.211   57.346  1.00 74.52  -1 286 GLU   B OE2 1 
ATOM   3658 N  N   . GLU   B 1 131 ? -37.538 12.578  52.397  1.00 69.69  ?  287 GLU   B N   1 
ATOM   3659 C  CA  . GLU   B 1 131 ? -37.345 13.762  51.578  1.00 67.88  ?  287 GLU   B CA  1 
ATOM   3660 C  C   . GLU   B 1 131 ? -38.636 14.532  51.366  1.00 71.30  ?  287 GLU   B C   1 
ATOM   3661 O  O   . GLU   B 1 131 ? -38.595 15.706  50.980  1.00 74.15  ?  287 GLU   B O   1 
ATOM   3662 C  CB  . GLU   B 1 131 ? -36.699 13.340  50.271  1.00 69.26  ?  287 GLU   B CB  1 
ATOM   3663 C  CG  . GLU   B 1 131 ? -35.715 14.344  49.819  1.00 68.95  ?  287 GLU   B CG  1 
ATOM   3664 C  CD  . GLU   B 1 131 ? -34.720 14.606  50.913  1.00 78.63  ?  287 GLU   B CD  1 
ATOM   3665 O  OE1 . GLU   B 1 131 ? -34.134 13.636  51.457  1.00 82.85  ?  287 GLU   B OE1 1 
ATOM   3666 O  OE2 . GLU   B 1 131 ? -34.482 15.797  51.197  1.00 89.46  -1 287 GLU   B OE2 1 
ATOM   3667 N  N   . ILE   B 1 132 ? -39.775 13.917  51.667  1.00 71.83  ?  288 ILE   B N   1 
ATOM   3668 C  CA  . ILE   B 1 132 ? -41.025 14.654  51.649  1.00 69.24  ?  288 ILE   B CA  1 
ATOM   3669 C  C   . ILE   B 1 132 ? -41.186 15.501  52.920  1.00 69.60  ?  288 ILE   B C   1 
ATOM   3670 O  O   . ILE   B 1 132 ? -41.762 16.597  52.866  1.00 69.85  ?  288 ILE   B O   1 
ATOM   3671 C  CB  . ILE   B 1 132 ? -42.187 13.667  51.433  1.00 66.69  ?  288 ILE   B CB  1 
ATOM   3672 C  CG1 . ILE   B 1 132 ? -42.238 13.205  49.966  1.00 67.40  ?  288 ILE   B CG1 1 
ATOM   3673 C  CG2 . ILE   B 1 132 ? -43.504 14.260  51.876  1.00 68.12  ?  288 ILE   B CG2 1 
ATOM   3674 C  CD1 . ILE   B 1 132 ? -41.811 14.262  48.968  1.00 61.04  ?  288 ILE   B CD1 1 
ATOM   3675 N  N   . ASN   B 1 133 ? -40.653 15.050  54.066  1.00 69.85  ?  289 ASN   B N   1 
ATOM   3676 C  CA  . ASN   B 1 133 ? -40.840 15.830  55.287  1.00 72.21  ?  289 ASN   B CA  1 
ATOM   3677 C  C   . ASN   B 1 133 ? -40.165 17.193  55.217  1.00 70.19  ?  289 ASN   B C   1 
ATOM   3678 O  O   . ASN   B 1 133 ? -40.559 18.100  55.953  1.00 78.15  ?  289 ASN   B O   1 
ATOM   3679 C  CB  . ASN   B 1 133 ? -40.351 15.085  56.539  1.00 69.97  ?  289 ASN   B CB  1 
ATOM   3680 C  CG  . ASN   B 1 133 ? -40.735 13.617  56.538  1.00 80.01  ?  289 ASN   B CG  1 
ATOM   3681 O  OD1 . ASN   B 1 133 ? -41.854 13.260  56.147  1.00 88.05  ?  289 ASN   B OD1 1 
ATOM   3682 N  ND2 . ASN   B 1 133 ? -39.844 12.766  57.046  1.00 69.56  ?  289 ASN   B ND2 1 
ATOM   3683 N  N   . ASP   B 1 134 ? -39.183 17.377  54.337  1.00 78.56  ?  290 ASP   B N   1 
ATOM   3684 C  CA  . ASP   B 1 134 ? -38.647 18.720  54.132  1.00 79.41  ?  290 ASP   B CA  1 
ATOM   3685 C  C   . ASP   B 1 134 ? -39.603 19.530  53.259  1.00 78.84  ?  290 ASP   B C   1 
ATOM   3686 O  O   . ASP   B 1 134 ? -40.190 20.519  53.712  1.00 97.09  ?  290 ASP   B O   1 
ATOM   3687 C  CB  . ASP   B 1 134 ? -37.255 18.660  53.497  1.00 71.37  ?  290 ASP   B CB  1 
ATOM   3688 C  CG  . ASP   B 1 134 ? -36.867 19.968  52.839  1.00 72.38  ?  290 ASP   B CG  1 
ATOM   3689 O  OD1 . ASP   B 1 134 ? -37.150 20.168  51.637  1.00 86.84  ?  290 ASP   B OD1 1 
ATOM   3690 O  OD2 . ASP   B 1 134 ? -36.284 20.812  53.550  1.00 88.65  -1 290 ASP   B OD2 1 
ATOM   3691 N  N   . ILE   B 1 135 ? -39.776 19.100  52.010  1.00 80.29  ?  291 ILE   B N   1 
ATOM   3692 C  CA  . ILE   B 1 135 ? -40.561 19.800  50.987  1.00 74.60  ?  291 ILE   B CA  1 
ATOM   3693 C  C   . ILE   B 1 135 ? -41.885 20.371  51.501  1.00 84.00  ?  291 ILE   B C   1 
ATOM   3694 O  O   . ILE   B 1 135 ? -42.749 19.644  51.993  1.00 89.61  ?  291 ILE   B O   1 
ATOM   3695 C  CB  . ILE   B 1 135 ? -40.825 18.865  49.801  1.00 68.62  ?  291 ILE   B CB  1 
ATOM   3696 N  N   . ASP   B 1 139 ? -47.130 22.256  51.459  1.00 78.00  ?  295 ASP   B N   1 
ATOM   3697 C  CA  . ASP   B 1 139 ? -46.370 21.048  51.768  1.00 74.81  ?  295 ASP   B CA  1 
ATOM   3698 C  C   . ASP   B 1 139 ? -46.772 19.867  50.876  1.00 76.87  ?  295 ASP   B C   1 
ATOM   3699 O  O   . ASP   B 1 139 ? -47.374 20.061  49.819  1.00 79.02  ?  295 ASP   B O   1 
ATOM   3700 C  CB  . ASP   B 1 139 ? -46.516 20.699  53.262  1.00 82.63  ?  295 ASP   B CB  1 
ATOM   3701 C  CG  . ASP   B 1 139 ? -47.951 20.326  53.669  1.00 77.40  ?  295 ASP   B CG  1 
ATOM   3702 O  OD1 . ASP   B 1 139 ? -48.824 20.167  52.786  1.00 85.73  ?  295 ASP   B OD1 1 
ATOM   3703 O  OD2 . ASP   B 1 139 ? -48.202 20.200  54.896  1.00 79.62  -1 295 ASP   B OD2 1 
ATOM   3704 N  N   . VAL   B 1 140 ? -46.414 18.655  51.298  1.00 79.03  ?  296 VAL   B N   1 
ATOM   3705 C  CA  . VAL   B 1 140 ? -46.719 17.427  50.565  1.00 63.11  ?  296 VAL   B CA  1 
ATOM   3706 C  C   . VAL   B 1 140 ? -46.697 16.271  51.553  1.00 66.55  ?  296 VAL   B C   1 
ATOM   3707 O  O   . VAL   B 1 140 ? -45.823 16.196  52.419  1.00 74.92  ?  296 VAL   B O   1 
ATOM   3708 C  CB  . VAL   B 1 140 ? -45.743 17.199  49.386  1.00 64.55  ?  296 VAL   B CB  1 
ATOM   3709 C  CG1 . VAL   B 1 140 ? -44.312 17.338  49.832  1.00 73.56  ?  296 VAL   B CG1 1 
ATOM   3710 C  CG2 . VAL   B 1 140 ? -45.953 15.812  48.769  1.00 63.39  ?  296 VAL   B CG2 1 
ATOM   3711 N  N   . ILE   B 1 141 ? -47.696 15.399  51.453  1.00 62.63  ?  297 ILE   B N   1 
ATOM   3712 C  CA  . ILE   B 1 141 ? -47.857 14.251  52.338  1.00 58.37  ?  297 ILE   B CA  1 
ATOM   3713 C  C   . ILE   B 1 141 ? -47.675 12.987  51.511  1.00 59.89  ?  297 ILE   B C   1 
ATOM   3714 O  O   . ILE   B 1 141 ? -48.162 12.907  50.380  1.00 66.05  ?  297 ILE   B O   1 
ATOM   3715 C  CB  . ILE   B 1 141 ? -49.242 14.257  53.018  1.00 67.18  ?  297 ILE   B CB  1 
ATOM   3716 C  CG1 . ILE   B 1 141 ? -49.483 15.584  53.748  1.00 64.37  ?  297 ILE   B CG1 1 
ATOM   3717 C  CG2 . ILE   B 1 141 ? -49.379 13.080  54.004  1.00 64.52  ?  297 ILE   B CG2 1 
ATOM   3718 C  CD1 . ILE   B 1 141 ? -48.493 15.850  54.859  1.00 62.07  ?  297 ILE   B CD1 1 
ATOM   3719 N  N   . MET   B 1 142 ? -46.968 12.008  52.061  1.00 60.38  ?  298 MET   B N   1 
ATOM   3720 C  CA  . MET   B 1 142 ? -46.907 10.688  51.449  1.00 60.80  ?  298 MET   B CA  1 
ATOM   3721 C  C   . MET   B 1 142 ? -47.964 9.764   52.033  1.00 64.88  ?  298 MET   B C   1 
ATOM   3722 O  O   . MET   B 1 142 ? -48.234 9.784   53.236  1.00 76.37  ?  298 MET   B O   1 
ATOM   3723 C  CB  . MET   B 1 142 ? -45.534 10.040  51.631  1.00 71.42  ?  298 MET   B CB  1 
ATOM   3724 C  CG  . MET   B 1 142 ? -45.613 8.495   51.730  1.00 75.22  ?  298 MET   B CG  1 
ATOM   3725 S  SD  . MET   B 1 142 ? -44.136 7.508   51.380  1.00 99.81  ?  298 MET   B SD  1 
ATOM   3726 C  CE  . MET   B 1 142 ? -44.680 5.848   51.823  1.00 72.66  ?  298 MET   B CE  1 
ATOM   3727 N  N   . LYS   B 1 143 ? -48.544 8.945   51.165  1.00 67.01  ?  299 LYS   B N   1 
ATOM   3728 C  CA  . LYS   B 1 143 ? -49.396 7.829   51.539  1.00 69.34  ?  299 LYS   B CA  1 
ATOM   3729 C  C   . LYS   B 1 143 ? -48.739 6.565   50.998  1.00 64.37  ?  299 LYS   B C   1 
ATOM   3730 O  O   . LYS   B 1 143 ? -48.366 6.513   49.822  1.00 66.38  ?  299 LYS   B O   1 
ATOM   3731 C  CB  . LYS   B 1 143 ? -50.799 8.018   50.953  1.00 72.01  ?  299 LYS   B CB  1 
ATOM   3732 C  CG  . LYS   B 1 143 ? -51.735 6.827   51.051  1.00 70.92  ?  299 LYS   B CG  1 
ATOM   3733 C  CD  . LYS   B 1 143 ? -51.587 6.086   52.378  1.00 64.24  ?  299 LYS   B CD  1 
ATOM   3734 C  CE  . LYS   B 1 143 ? -52.914 5.531   52.876  1.00 81.58  ?  299 LYS   B CE  1 
ATOM   3735 N  NZ  . LYS   B 1 143 ? -53.969 6.578   53.043  1.00 78.18  ?  299 LYS   B NZ  1 
ATOM   3736 N  N   . ARG   B 1 144 ? -48.554 5.570   51.857  1.00 74.03  ?  300 ARG   B N   1 
ATOM   3737 C  CA  . ARG   B 1 144 ? -47.991 4.292   51.438  1.00 72.06  ?  300 ARG   B CA  1 
ATOM   3738 C  C   . ARG   B 1 144 ? -49.121 3.381   50.972  1.00 70.65  ?  300 ARG   B C   1 
ATOM   3739 O  O   . ARG   B 1 144 ? -50.042 3.086   51.740  1.00 83.46  ?  300 ARG   B O   1 
ATOM   3740 C  CB  . ARG   B 1 144 ? -47.204 3.644   52.579  1.00 63.94  ?  300 ARG   B CB  1 
ATOM   3741 N  N   . LYS   B 1 145 ? -49.052 2.934   49.720  1.00 77.35  ?  301 LYS   B N   1 
ATOM   3742 C  CA  . LYS   B 1 145 ? -50.108 2.095   49.156  1.00 74.80  ?  301 LYS   B CA  1 
ATOM   3743 C  C   . LYS   B 1 145 ? -50.097 0.674   49.716  1.00 80.54  ?  301 LYS   B C   1 
ATOM   3744 O  O   . LYS   B 1 145 ? -50.876 -0.176  49.269  1.00 82.46  ?  301 LYS   B O   1 
ATOM   3745 C  CB  . LYS   B 1 145 ? -49.993 2.045   47.634  1.00 72.51  ?  301 LYS   B CB  1 
ATOM   3746 N  N   . GLY   B 1 148 ? -47.108 -3.546  45.167  1.00 44.71  ?  304 GLY   B N   1 
ATOM   3747 C  CA  . GLY   B 1 148 ? -46.343 -2.318  45.307  1.00 42.78  ?  304 GLY   B CA  1 
ATOM   3748 C  C   . GLY   B 1 148 ? -46.008 -1.580  44.013  1.00 51.44  ?  304 GLY   B C   1 
ATOM   3749 O  O   . GLY   B 1 148 ? -44.910 -1.032  43.876  1.00 56.88  ?  304 GLY   B O   1 
ATOM   3750 N  N   . PRO   B 1 150 ? -48.241 1.155   42.029  1.00 54.57  ?  306 PRO   B N   1 
ATOM   3751 C  CA  . PRO   B 1 150 ? -47.496 2.322   42.540  1.00 49.52  ?  306 PRO   B CA  1 
ATOM   3752 C  C   . PRO   B 1 150 ? -46.915 2.097   43.924  1.00 51.64  ?  306 PRO   B C   1 
ATOM   3753 O  O   . PRO   B 1 150 ? -47.571 1.563   44.814  1.00 52.67  ?  306 PRO   B O   1 
ATOM   3754 C  CB  . PRO   B 1 150 ? -48.547 3.449   42.618  1.00 52.37  ?  306 PRO   B CB  1 
ATOM   3755 C  CG  . PRO   B 1 150 ? -49.865 2.832   42.340  1.00 59.55  ?  306 PRO   B CG  1 
ATOM   3756 C  CD  . PRO   B 1 150 ? -49.687 1.447   41.810  1.00 56.99  ?  306 PRO   B CD  1 
ATOM   3757 N  N   . ALA   B 1 151 ? -45.667 2.523   44.120  1.00 51.39  ?  307 ALA   B N   1 
ATOM   3758 C  CA  . ALA   B 1 151 ? -45.003 2.315   45.402  1.00 53.49  ?  307 ALA   B CA  1 
ATOM   3759 C  C   . ALA   B 1 151 ? -45.408 3.373   46.407  1.00 54.78  ?  307 ALA   B C   1 
ATOM   3760 O  O   . ALA   B 1 151 ? -45.665 3.062   47.576  1.00 54.39  ?  307 ALA   B O   1 
ATOM   3761 C  CB  . ALA   B 1 151 ? -43.490 2.317   45.208  1.00 45.62  ?  307 ALA   B CB  1 
ATOM   3762 N  N   . VAL   B 1 152 ? -45.465 4.625   45.956  1.00 53.90  ?  308 VAL   B N   1 
ATOM   3763 C  CA  . VAL   B 1 152 ? -45.775 5.744   46.824  1.00 55.80  ?  308 VAL   B CA  1 
ATOM   3764 C  C   . VAL   B 1 152 ? -46.753 6.638   46.081  1.00 54.46  ?  308 VAL   B C   1 
ATOM   3765 O  O   . VAL   B 1 152 ? -46.658 6.803   44.858  1.00 49.80  ?  308 VAL   B O   1 
ATOM   3766 C  CB  . VAL   B 1 152 ? -44.490 6.504   47.232  1.00 52.45  ?  308 VAL   B CB  1 
ATOM   3767 C  CG1 . VAL   B 1 152 ? -44.808 7.857   47.827  1.00 60.26  ?  308 VAL   B CG1 1 
ATOM   3768 C  CG2 . VAL   B 1 152 ? -43.653 5.663   48.175  1.00 47.68  ?  308 VAL   B CG2 1 
ATOM   3769 N  N   . THR   B 1 153 ? -47.708 7.192   46.825  1.00 56.13  ?  309 THR   B N   1 
ATOM   3770 C  CA  . THR   B 1 153 ? -48.592 8.230   46.331  1.00 60.36  ?  309 THR   B CA  1 
ATOM   3771 C  C   . THR   B 1 153 ? -48.357 9.462   47.193  1.00 56.81  ?  309 THR   B C   1 
ATOM   3772 O  O   . THR   B 1 153 ? -48.393 9.372   48.419  1.00 55.16  ?  309 THR   B O   1 
ATOM   3773 C  CB  . THR   B 1 153 ? -50.045 7.786   46.410  1.00 54.20  ?  309 THR   B CB  1 
ATOM   3774 O  OG1 . THR   B 1 153 ? -50.230 6.639   45.580  1.00 51.82  ?  309 THR   B OG1 1 
ATOM   3775 C  CG2 . THR   B 1 153 ? -50.951 8.897   45.934  1.00 52.34  ?  309 THR   B CG2 1 
ATOM   3776 N  N   . LEU   B 1 154 ? -48.063 10.581  46.552  1.00 61.09  ?  310 LEU   B N   1 
ATOM   3777 C  CA  . LEU   B 1 154 ? -47.884 11.864  47.211  1.00 53.01  ?  310 LEU   B CA  1 
ATOM   3778 C  C   . LEU   B 1 154 ? -49.132 12.713  47.031  1.00 56.88  ?  310 LEU   B C   1 
ATOM   3779 O  O   . LEU   B 1 154 ? -49.723 12.743  45.952  1.00 49.73  ?  310 LEU   B O   1 
ATOM   3780 C  CB  . LEU   B 1 154 ? -46.686 12.604  46.622  1.00 48.57  ?  310 LEU   B CB  1 
ATOM   3781 C  CG  . LEU   B 1 154 ? -45.358 11.865  46.619  1.00 59.19  ?  310 LEU   B CG  1 
ATOM   3782 C  CD1 . LEU   B 1 154 ? -44.273 12.775  46.081  1.00 57.57  ?  310 LEU   B CD1 1 
ATOM   3783 C  CD2 . LEU   B 1 154 ? -45.044 11.449  48.057  1.00 59.33  ?  310 LEU   B CD2 1 
ATOM   3784 N  N   . LEU   B 1 155 ? -49.520 13.404  48.079  1.00 56.83  ?  311 LEU   B N   1 
ATOM   3785 C  CA  . LEU   B 1 155 ? -50.594 14.383  48.014  1.00 61.53  ?  311 LEU   B CA  1 
ATOM   3786 C  C   . LEU   B 1 155 ? -49.953 15.761  48.135  1.00 56.47  ?  311 LEU   B C   1 
ATOM   3787 O  O   . LEU   B 1 155 ? -49.557 16.174  49.225  1.00 70.12  ?  311 LEU   B O   1 
ATOM   3788 C  CB  . LEU   B 1 155 ? -51.625 14.129  49.105  1.00 55.24  ?  311 LEU   B CB  1 
ATOM   3789 C  CG  . LEU   B 1 155 ? -52.737 15.176  49.155  1.00 66.19  ?  311 LEU   B CG  1 
ATOM   3790 C  CD1 . LEU   B 1 155 ? -53.506 15.199  47.831  1.00 61.25  ?  311 LEU   B CD1 1 
ATOM   3791 C  CD2 . LEU   B 1 155 ? -53.677 14.910  50.323  1.00 66.68  ?  311 LEU   B CD2 1 
ATOM   3792 N  N   . ILE   B 1 156 ? -49.828 16.457  47.011  1.00 63.60  ?  312 ILE   B N   1 
ATOM   3793 C  CA  . ILE   B 1 156 ? -49.249 17.798  46.999  1.00 62.57  ?  312 ILE   B CA  1 
ATOM   3794 C  C   . ILE   B 1 156 ? -50.351 18.814  47.278  1.00 69.42  ?  312 ILE   B C   1 
ATOM   3795 O  O   . ILE   B 1 156 ? -51.384 18.836  46.589  1.00 75.36  ?  312 ILE   B O   1 
ATOM   3796 C  CB  . ILE   B 1 156 ? -48.555 18.085  45.655  1.00 66.49  ?  312 ILE   B CB  1 
ATOM   3797 C  CG1 . ILE   B 1 156 ? -47.401 17.110  45.412  1.00 60.34  ?  312 ILE   B CG1 1 
ATOM   3798 C  CG2 . ILE   B 1 156 ? -48.069 19.534  45.599  1.00 68.65  ?  312 ILE   B CG2 1 
ATOM   3799 C  CD1 . ILE   B 1 156 ? -46.804 17.210  44.028  1.00 63.36  ?  312 ILE   B CD1 1 
ATOM   3800 N  N   . SER   B 1 157 ? -50.131 19.664  48.285  1.00 76.47  ?  313 SER   B N   1 
ATOM   3801 C  CA  . SER   B 1 157 ? -51.132 20.637  48.767  1.00 68.79  ?  313 SER   B CA  1 
ATOM   3802 C  C   . SER   B 1 157 ? -52.358 19.827  49.174  1.00 78.04  ?  313 SER   B C   1 
ATOM   3803 O  O   . SER   B 1 157 ? -52.229 18.898  49.992  1.00 83.47  ?  313 SER   B O   1 
ATOM   3804 C  CB  . SER   B 1 157 ? -51.381 21.720  47.721  1.00 66.43  ?  313 SER   B CB  1 
ATOM   3805 O  OG  . SER   B 1 157 ? -52.265 21.257  46.711  1.00 85.44  ?  313 SER   B OG  1 
ATOM   3806 N  N   . GLU   B 1 158 ? -53.550 20.120  48.652  1.00 77.59  ?  314 GLU   B N   1 
ATOM   3807 C  CA  . GLU   B 1 158 ? -54.721 19.313  48.951  1.00 69.18  ?  314 GLU   B CA  1 
ATOM   3808 C  C   . GLU   B 1 158 ? -55.306 18.629  47.731  1.00 68.87  ?  314 GLU   B C   1 
ATOM   3809 O  O   . GLU   B 1 158 ? -56.000 17.621  47.889  1.00 74.19  ?  314 GLU   B O   1 
ATOM   3810 C  CB  . GLU   B 1 158 ? -55.815 20.163  49.614  1.00 78.34  ?  314 GLU   B CB  1 
ATOM   3811 C  CG  . GLU   B 1 158 ? -56.063 19.798  51.062  1.00 62.93  ?  314 GLU   B CG  1 
ATOM   3812 C  CD  . GLU   B 1 158 ? -55.014 20.377  51.988  1.00 81.81  ?  314 GLU   B CD  1 
ATOM   3813 O  OE1 . GLU   B 1 158 ? -54.969 21.618  52.148  1.00 85.56  ?  314 GLU   B OE1 1 
ATOM   3814 O  OE2 . GLU   B 1 158 ? -54.239 19.588  52.570  1.00 86.26  -1 314 GLU   B OE2 1 
ATOM   3815 N  N   . LYS   B 1 159 ? -55.027 19.126  46.529  1.00 73.21  ?  315 LYS   B N   1 
ATOM   3816 C  CA  . LYS   B 1 159 ? -55.687 18.618  45.332  1.00 68.16  ?  315 LYS   B CA  1 
ATOM   3817 C  C   . LYS   B 1 159 ? -54.795 17.759  44.445  1.00 72.68  ?  315 LYS   B C   1 
ATOM   3818 O  O   . LYS   B 1 159 ? -55.274 16.768  43.884  1.00 76.19  ?  315 LYS   B O   1 
ATOM   3819 C  CB  . LYS   B 1 159 ? -56.267 19.785  44.522  1.00 67.94  ?  315 LYS   B CB  1 
ATOM   3820 C  CG  . LYS   B 1 159 ? -56.495 21.048  45.350  1.00 72.13  ?  315 LYS   B CG  1 
ATOM   3821 C  CD  . LYS   B 1 159 ? -57.184 22.143  44.541  1.00 76.87  ?  315 LYS   B CD  1 
ATOM   3822 C  CE  . LYS   B 1 159 ? -56.255 22.779  43.513  1.00 76.92  ?  315 LYS   B CE  1 
ATOM   3823 N  NZ  . LYS   B 1 159 ? -57.020 23.321  42.348  1.00 79.11  ?  315 LYS   B NZ  1 
ATOM   3824 N  N   . ILE   B 1 160 ? -53.507 18.083  44.307  1.00 65.69  ?  316 ILE   B N   1 
ATOM   3825 C  CA  . ILE   B 1 160 ? -52.633 17.345  43.396  1.00 58.55  ?  316 ILE   B CA  1 
ATOM   3826 C  C   . ILE   B 1 160 ? -52.146 16.061  44.049  1.00 65.99  ?  316 ILE   B C   1 
ATOM   3827 O  O   . ILE   B 1 160 ? -51.717 16.052  45.211  1.00 61.36  ?  316 ILE   B O   1 
ATOM   3828 C  CB  . ILE   B 1 160 ? -51.435 18.204  42.976  1.00 65.26  ?  316 ILE   B CB  1 
ATOM   3829 C  CG1 . ILE   B 1 160 ? -51.894 19.585  42.538  1.00 76.70  ?  316 ILE   B CG1 1 
ATOM   3830 C  CG2 . ILE   B 1 160 ? -50.663 17.522  41.861  1.00 52.20  ?  316 ILE   B CG2 1 
ATOM   3831 C  CD1 . ILE   B 1 160 ? -50.905 20.258  41.621  1.00 71.67  ?  316 ILE   B CD1 1 
ATOM   3832 N  N   . SER   B 1 161 ? -52.151 14.979  43.275  1.00 60.84  ?  317 SER   B N   1 
ATOM   3833 C  CA  . SER   B 1 161 ? -51.670 13.686  43.738  1.00 56.19  ?  317 SER   B CA  1 
ATOM   3834 C  C   . SER   B 1 161 ? -50.753 13.084  42.684  1.00 55.33  ?  317 SER   B C   1 
ATOM   3835 O  O   . SER   B 1 161 ? -51.035 13.151  41.479  1.00 52.03  ?  317 SER   B O   1 
ATOM   3836 C  CB  . SER   B 1 161 ? -52.838 12.746  44.058  1.00 49.92  ?  317 SER   B CB  1 
ATOM   3837 O  OG  . SER   B 1 161 ? -53.088 11.859  42.970  1.00 54.03  ?  317 SER   B OG  1 
ATOM   3838 N  N   . VAL   B 1 162 ? -49.644 12.505  43.139  1.00 49.20  ?  318 VAL   B N   1 
ATOM   3839 C  CA  . VAL   B 1 162 ? -48.631 11.963  42.242  1.00 52.52  ?  318 VAL   B CA  1 
ATOM   3840 C  C   . VAL   B 1 162 ? -48.331 10.538  42.668  1.00 52.47  ?  318 VAL   B C   1 
ATOM   3841 O  O   . VAL   B 1 162 ? -47.822 10.313  43.776  1.00 50.33  ?  318 VAL   B O   1 
ATOM   3842 C  CB  . VAL   B 1 162 ? -47.340 12.796  42.250  1.00 54.39  ?  318 VAL   B CB  1 
ATOM   3843 C  CG1 . VAL   B 1 162 ? -46.381 12.273  41.175  1.00 55.13  ?  318 VAL   B CG1 1 
ATOM   3844 C  CG2 . VAL   B 1 162 ? -47.650 14.260  42.054  1.00 52.54  ?  318 VAL   B CG2 1 
ATOM   3845 N  N   . ASP   B 1 163 ? -48.620 9.584   41.785  1.00 47.62  ?  319 ASP   B N   1 
ATOM   3846 C  CA  . ASP   B 1 163 ? -48.234 8.196   41.995  1.00 49.72  ?  319 ASP   B CA  1 
ATOM   3847 C  C   . ASP   B 1 163 ? -46.840 7.971   41.429  1.00 47.31  ?  319 ASP   B C   1 
ATOM   3848 O  O   . ASP   B 1 163 ? -46.547 8.378   40.304  1.00 51.82  ?  319 ASP   B O   1 
ATOM   3849 C  CB  . ASP   B 1 163 ? -49.240 7.245   41.346  1.00 44.86  ?  319 ASP   B CB  1 
ATOM   3850 C  CG  . ASP   B 1 163 ? -50.444 6.981   42.234  1.00 52.17  ?  319 ASP   B CG  1 
ATOM   3851 O  OD1 . ASP   B 1 163 ? -51.168 6.013   41.957  1.00 78.54  ?  319 ASP   B OD1 1 
ATOM   3852 O  OD2 . ASP   B 1 163 ? -50.656 7.704   43.229  1.00 53.29  -1 319 ASP   B OD2 1 
ATOM   3853 N  N   . ILE   B 1 164 ? -45.982 7.331   42.211  1.00 46.70  ?  320 ILE   B N   1 
ATOM   3854 C  CA  . ILE   B 1 164 ? -44.592 7.132   41.833  1.00 39.76  ?  320 ILE   B CA  1 
ATOM   3855 C  C   . ILE   B 1 164 ? -44.330 5.638   41.821  1.00 42.62  ?  320 ILE   B C   1 
ATOM   3856 O  O   . ILE   B 1 164 ? -44.530 4.956   42.837  1.00 37.26  ?  320 ILE   B O   1 
ATOM   3857 C  CB  . ILE   B 1 164 ? -43.622 7.838   42.789  1.00 48.63  ?  320 ILE   B CB  1 
ATOM   3858 C  CG1 . ILE   B 1 164 ? -43.951 9.322   42.866  1.00 43.80  ?  320 ILE   B CG1 1 
ATOM   3859 C  CG2 . ILE   B 1 164 ? -42.215 7.690   42.243  1.00 49.57  ?  320 ILE   B CG2 1 
ATOM   3860 C  CD1 . ILE   B 1 164 ? -43.201 10.048  43.958  1.00 45.83  ?  320 ILE   B CD1 1 
ATOM   3861 N  N   . THR   B 1 165 ? -43.888 5.139   40.675  1.00 39.16  ?  321 THR   B N   1 
ATOM   3862 C  CA  . THR   B 1 165 ? -43.561 3.740   40.448  1.00 40.07  ?  321 THR   B CA  1 
ATOM   3863 C  C   . THR   B 1 165 ? -42.055 3.574   40.269  1.00 41.73  ?  321 THR   B C   1 
ATOM   3864 O  O   . THR   B 1 165 ? -41.431 4.319   39.506  1.00 37.37  ?  321 THR   B O   1 
ATOM   3865 C  CB  . THR   B 1 165 ? -44.329 3.225   39.215  1.00 37.05  ?  321 THR   B CB  1 
ATOM   3866 O  OG1 . THR   B 1 165 ? -45.731 3.187   39.519  1.00 39.90  ?  321 THR   B OG1 1 
ATOM   3867 C  CG2 . THR   B 1 165 ? -43.834 1.879   38.743  1.00 39.75  ?  321 THR   B CG2 1 
ATOM   3868 N  N   . LEU   B 1 166 ? -41.471 2.621   41.006  1.00 40.07  ?  322 LEU   B N   1 
ATOM   3869 C  CA  . LEU   B 1 166 ? -40.085 2.204   40.798  1.00 36.81  ?  322 LEU   B CA  1 
ATOM   3870 C  C   . LEU   B 1 166 ? -40.004 1.163   39.679  1.00 39.49  ?  322 LEU   B C   1 
ATOM   3871 O  O   . LEU   B 1 166 ? -40.853 0.274   39.583  1.00 38.51  ?  322 LEU   B O   1 
ATOM   3872 C  CB  . LEU   B 1 166 ? -39.504 1.625   42.103  1.00 41.38  ?  322 LEU   B CB  1 
ATOM   3873 C  CG  . LEU   B 1 166 ? -38.145 0.923   41.993  1.00 46.52  ?  322 LEU   B CG  1 
ATOM   3874 C  CD1 . LEU   B 1 166 ? -37.098 1.913   41.517  1.00 50.27  ?  322 LEU   B CD1 1 
ATOM   3875 C  CD2 . LEU   B 1 166 ? -37.699 0.308   43.328  1.00 49.87  ?  322 LEU   B CD2 1 
ATOM   3876 N  N   . ALA   B 1 167 ? -38.981 1.272   38.825  1.00 40.18  ?  323 ALA   B N   1 
ATOM   3877 C  CA  . ALA   B 1 167 ? -38.841 0.373   37.680  1.00 41.80  ?  323 ALA   B CA  1 
ATOM   3878 C  C   . ALA   B 1 167 ? -37.376 0.059   37.410  1.00 49.34  ?  323 ALA   B C   1 
ATOM   3879 O  O   . ALA   B 1 167 ? -36.589 0.965   37.116  1.00 48.91  ?  323 ALA   B O   1 
ATOM   3880 C  CB  . ALA   B 1 167 ? -39.467 0.975   36.418  1.00 36.63  ?  323 ALA   B CB  1 
ATOM   3881 N  N   . LEU   B 1 168 ? -37.025 -1.224  37.433  1.00 44.08  ?  324 LEU   B N   1 
ATOM   3882 C  CA  . LEU   B 1 168 ? -35.699 -1.623  36.990  1.00 41.06  ?  324 LEU   B CA  1 
ATOM   3883 C  C   . LEU   B 1 168 ? -35.614 -1.503  35.475  1.00 45.75  ?  324 LEU   B C   1 
ATOM   3884 O  O   . LEU   B 1 168 ? -36.550 -1.858  34.757  1.00 43.84  ?  324 LEU   B O   1 
ATOM   3885 C  CB  . LEU   B 1 168 ? -35.400 -3.060  37.422  1.00 45.05  ?  324 LEU   B CB  1 
ATOM   3886 C  CG  . LEU   B 1 168 ? -35.567 -3.413  38.897  1.00 44.09  ?  324 LEU   B CG  1 
ATOM   3887 C  CD1 . LEU   B 1 168 ? -35.293 -4.898  39.160  1.00 46.59  ?  324 LEU   B CD1 1 
ATOM   3888 C  CD2 . LEU   B 1 168 ? -34.701 -2.531  39.768  1.00 44.16  ?  324 LEU   B CD2 1 
ATOM   3889 N  N   . GLU   B 1 169 ? -34.491 -0.997  34.982  1.00 47.18  ?  325 GLU   B N   1 
ATOM   3890 C  CA  . GLU   B 1 169 ? -34.264 -0.876  33.549  1.00 40.15  ?  325 GLU   B CA  1 
ATOM   3891 C  C   . GLU   B 1 169 ? -33.262 -1.931  33.115  1.00 48.70  ?  325 GLU   B C   1 
ATOM   3892 O  O   . GLU   B 1 169 ? -32.231 -2.119  33.771  1.00 44.41  ?  325 GLU   B O   1 
ATOM   3893 C  CB  . GLU   B 1 169 ? -33.741 0.511   33.174  1.00 42.01  ?  325 GLU   B CB  1 
ATOM   3894 C  CG  . GLU   B 1 169 ? -33.483 0.697   31.656  1.00 43.78  ?  325 GLU   B CG  1 
ATOM   3895 C  CD  . GLU   B 1 169 ? -32.940 2.074   31.336  1.00 40.23  ?  325 GLU   B CD  1 
ATOM   3896 O  OE1 . GLU   B 1 169 ? -31.787 2.372   31.706  1.00 49.64  ?  325 GLU   B OE1 1 
ATOM   3897 O  OE2 . GLU   B 1 169 ? -33.683 2.873   30.747  1.00 43.43  -1 325 GLU   B OE2 1 
ATOM   3898 N  N   . SER   B 1 170 ? -33.546 -2.600  31.998  1.00 45.99  ?  326 SER   B N   1 
ATOM   3899 C  CA  . SER   B 1 170 ? -32.632 -3.587  31.439  1.00 45.88  ?  326 SER   B CA  1 
ATOM   3900 C  C   . SER   B 1 170 ? -32.403 -3.288  29.974  1.00 43.91  ?  326 SER   B C   1 
ATOM   3901 O  O   . SER   B 1 170 ? -33.362 -3.221  29.197  1.00 41.53  ?  326 SER   B O   1 
ATOM   3902 C  CB  . SER   B 1 170 ? -33.164 -5.015  31.574  1.00 43.36  ?  326 SER   B CB  1 
ATOM   3903 O  OG  . SER   B 1 170 ? -32.272 -5.915  30.937  1.00 49.61  ?  326 SER   B OG  1 
ATOM   3904 N  N   . LYS   B 1 171 ? -31.141 -3.123  29.588  1.00 44.54  ?  327 LYS   B N   1 
ATOM   3905 C  CA  . LYS   B 1 171 ? -30.848 -2.886  28.181  1.00 45.39  ?  327 LYS   B CA  1 
ATOM   3906 C  C   . LYS   B 1 171 ? -30.540 -4.170  27.415  1.00 41.14  ?  327 LYS   B C   1 
ATOM   3907 O  O   . LYS   B 1 171 ? -29.953 -4.111  26.328  1.00 57.07  ?  327 LYS   B O   1 
ATOM   3908 C  CB  . LYS   B 1 171 ? -29.716 -1.867  28.032  1.00 49.02  ?  327 LYS   B CB  1 
ATOM   3909 C  CG  . LYS   B 1 171 ? -30.098 -0.479  28.557  1.00 52.99  ?  327 LYS   B CG  1 
ATOM   3910 C  CD  . LYS   B 1 171 ? -28.980 0.553   28.429  1.00 55.04  ?  327 LYS   B CD  1 
ATOM   3911 C  CE  . LYS   B 1 171 ? -29.450 1.923   28.902  1.00 50.24  ?  327 LYS   B CE  1 
ATOM   3912 N  NZ  . LYS   B 1 171 ? -28.432 2.996   28.725  1.00 59.55  ?  327 LYS   B NZ  1 
ATOM   3913 N  N   . SER   B 1 172 ? -30.958 -5.316  27.934  1.00 43.17  ?  328 SER   B N   1 
ATOM   3914 C  CA  . SER   B 1 172 ? -30.798 -6.587  27.249  1.00 40.16  ?  328 SER   B CA  1 
ATOM   3915 C  C   . SER   B 1 172 ? -32.022 -6.879  26.372  1.00 47.91  ?  328 SER   B C   1 
ATOM   3916 O  O   . SER   B 1 172 ? -33.014 -6.143  26.380  1.00 39.89  ?  328 SER   B O   1 
ATOM   3917 C  CB  . SER   B 1 172 ? -30.559 -7.700  28.267  1.00 47.79  ?  328 SER   B CB  1 
ATOM   3918 O  OG  . SER   B 1 172 ? -31.694 -7.873  29.094  1.00 52.31  ?  328 SER   B OG  1 
ATOM   3919 N  N   . SER   B 1 173 ? -31.934 -7.959  25.591  1.00 40.62  ?  329 SER   B N   1 
ATOM   3920 C  CA  . SER   B 1 173 ? -33.030 -8.327  24.704  1.00 48.37  ?  329 SER   B CA  1 
ATOM   3921 C  C   . SER   B 1 173 ? -34.282 -8.613  25.513  1.00 42.17  ?  329 SER   B C   1 
ATOM   3922 O  O   . SER   B 1 173 ? -34.217 -9.182  26.606  1.00 45.27  ?  329 SER   B O   1 
ATOM   3923 C  CB  . SER   B 1 173 ? -32.675 -9.561  23.866  1.00 48.22  ?  329 SER   B CB  1 
ATOM   3924 O  OG  . SER   B 1 173 ? -31.561 -9.304  23.039  1.00 54.86  ?  329 SER   B OG  1 
ATOM   3925 N  N   . TRP   B 1 174 ? -35.424 -8.223  24.962  1.00 39.75  ?  330 TRP   B N   1 
ATOM   3926 C  CA  . TRP   B 1 174 ? -36.690 -8.448  25.635  1.00 39.55  ?  330 TRP   B CA  1 
ATOM   3927 C  C   . TRP   B 1 174 ? -36.876 -9.938  25.941  1.00 38.26  ?  330 TRP   B C   1 
ATOM   3928 O  O   . TRP   B 1 174 ? -36.335 -10.791 25.236  1.00 44.33  ?  330 TRP   B O   1 
ATOM   3929 C  CB  . TRP   B 1 174 ? -37.837 -7.941  24.773  1.00 31.64  ?  330 TRP   B CB  1 
ATOM   3930 C  CG  . TRP   B 1 174 ? -37.828 -6.467  24.566  1.00 33.86  ?  330 TRP   B CG  1 
ATOM   3931 C  CD1 . TRP   B 1 174 ? -36.810 -5.581  24.854  1.00 33.36  ?  330 TRP   B CD1 1 
ATOM   3932 C  CD2 . TRP   B 1 174 ? -38.912 -5.687  24.083  1.00 33.68  ?  330 TRP   B CD2 1 
ATOM   3933 N  NE1 . TRP   B 1 174 ? -37.202 -4.302  24.554  1.00 36.15  ?  330 TRP   B NE1 1 
ATOM   3934 C  CE2 . TRP   B 1 174 ? -38.489 -4.339  24.071  1.00 32.66  ?  330 TRP   B CE2 1 
ATOM   3935 C  CE3 . TRP   B 1 174 ? -40.204 -5.996  23.646  1.00 34.68  ?  330 TRP   B CE3 1 
ATOM   3936 C  CZ2 . TRP   B 1 174 ? -39.312 -3.308  23.637  1.00 33.31  ?  330 TRP   B CZ2 1 
ATOM   3937 C  CZ3 . TRP   B 1 174 ? -41.026 -4.952  23.201  1.00 33.65  ?  330 TRP   B CZ3 1 
ATOM   3938 C  CH2 . TRP   B 1 174 ? -40.575 -3.636  23.205  1.00 31.61  ?  330 TRP   B CH2 1 
ATOM   3939 N  N   . PRO   B 1 175 ? -37.613 -10.281 26.998  1.00 42.96  ?  331 PRO   B N   1 
ATOM   3940 C  CA  . PRO   B 1 175 ? -37.768 -11.701 27.345  1.00 44.41  ?  331 PRO   B CA  1 
ATOM   3941 C  C   . PRO   B 1 175 ? -38.495 -12.467 26.249  1.00 41.27  ?  331 PRO   B C   1 
ATOM   3942 O  O   . PRO   B 1 175 ? -39.289 -11.910 25.482  1.00 45.79  ?  331 PRO   B O   1 
ATOM   3943 C  CB  . PRO   B 1 175 ? -38.583 -11.668 28.643  1.00 38.27  ?  331 PRO   B CB  1 
ATOM   3944 C  CG  . PRO   B 1 175 ? -38.255 -10.331 29.245  1.00 43.47  ?  331 PRO   B CG  1 
ATOM   3945 C  CD  . PRO   B 1 175 ? -38.101 -9.392  28.071  1.00 39.42  ?  331 PRO   B CD  1 
ATOM   3946 N  N   . ALA   B 1 176 ? -38.217 -13.772 26.207  1.00 46.40  ?  332 ALA   B N   1 
ATOM   3947 C  CA  . ALA   B 1 176 ? -38.751 -14.651 25.170  1.00 40.69  ?  332 ALA   B CA  1 
ATOM   3948 C  C   . ALA   B 1 176 ? -40.271 -14.599 25.090  1.00 40.79  ?  332 ALA   B C   1 
ATOM   3949 O  O   . ALA   B 1 176 ? -40.831 -14.733 24.005  1.00 42.58  ?  332 ALA   B O   1 
ATOM   3950 C  CB  . ALA   B 1 176 ? -38.285 -16.091 25.421  1.00 33.31  ?  332 ALA   B CB  1 
ATOM   3951 N  N   . SER   B 1 177 ? -40.959 -14.399 26.214  1.00 44.77  ?  333 SER   B N   1 
ATOM   3952 C  CA  . SER   B 1 177 ? -42.415 -14.290 26.171  1.00 37.77  ?  333 SER   B CA  1 
ATOM   3953 C  C   . SER   B 1 177 ? -42.910 -13.066 25.409  1.00 34.45  ?  333 SER   B C   1 
ATOM   3954 O  O   . SER   B 1 177 ? -44.128 -12.892 25.307  1.00 35.58  ?  333 SER   B O   1 
ATOM   3955 C  CB  . SER   B 1 177 ? -42.992 -14.238 27.584  1.00 44.45  ?  333 SER   B CB  1 
ATOM   3956 O  OG  . SER   B 1 177 ? -42.644 -13.005 28.201  1.00 47.71  ?  333 SER   B OG  1 
ATOM   3957 N  N   . THR   B 1 178 ? -42.033 -12.201 24.903  1.00 35.81  ?  334 THR   B N   1 
ATOM   3958 C  CA  . THR   B 1 178 ? -42.477 -11.096 24.062  1.00 45.61  ?  334 THR   B CA  1 
ATOM   3959 C  C   . THR   B 1 178 ? -42.267 -11.348 22.571  1.00 37.04  ?  334 THR   B C   1 
ATOM   3960 O  O   . THR   B 1 178 ? -42.662 -10.507 21.758  1.00 29.40  ?  334 THR   B O   1 
ATOM   3961 C  CB  . THR   B 1 178 ? -41.762 -9.798  24.453  1.00 37.49  ?  334 THR   B CB  1 
ATOM   3962 O  OG1 . THR   B 1 178 ? -40.375 -9.899  24.111  1.00 38.99  ?  334 THR   B OG1 1 
ATOM   3963 C  CG2 . THR   B 1 178 ? -41.917 -9.534  25.965  1.00 35.76  ?  334 THR   B CG2 1 
ATOM   3964 N  N   . GLN   B 1 179 ? -41.668 -12.483 22.196  1.00 37.98  ?  335 GLN   B N   1 
ATOM   3965 C  CA  . GLN   B 1 179 ? -41.203 -12.655 20.816  1.00 42.69  ?  335 GLN   B CA  1 
ATOM   3966 C  C   . GLN   B 1 179 ? -42.328 -12.553 19.799  1.00 43.80  ?  335 GLN   B C   1 
ATOM   3967 O  O   . GLN   B 1 179 ? -42.095 -12.104 18.668  1.00 40.71  ?  335 GLN   B O   1 
ATOM   3968 C  CB  . GLN   B 1 179 ? -40.494 -13.997 20.626  1.00 47.26  ?  335 GLN   B CB  1 
ATOM   3969 C  CG  . GLN   B 1 179 ? -39.035 -13.834 20.232  1.00 56.06  ?  335 GLN   B CG  1 
ATOM   3970 C  CD  . GLN   B 1 179 ? -38.255 -15.126 20.321  1.00 65.93  ?  335 GLN   B CD  1 
ATOM   3971 O  OE1 . GLN   B 1 179 ? -38.796 -16.212 20.078  1.00 70.36  ?  335 GLN   B OE1 1 
ATOM   3972 N  NE2 . GLN   B 1 179 ? -36.977 -15.023 20.708  1.00 67.65  ?  335 GLN   B NE2 1 
ATOM   3973 N  N   . GLU   B 1 180 ? -43.538 -12.972 20.159  1.00 40.03  ?  336 GLU   B N   1 
ATOM   3974 C  CA  . GLU   B 1 180 ? -44.656 -12.889 19.229  1.00 38.14  ?  336 GLU   B CA  1 
ATOM   3975 C  C   . GLU   B 1 180 ? -45.555 -11.689 19.468  1.00 42.04  ?  336 GLU   B C   1 
ATOM   3976 O  O   . GLU   B 1 180 ? -46.572 -11.551 18.781  1.00 35.61  ?  336 GLU   B O   1 
ATOM   3977 C  CB  . GLU   B 1 180 ? -45.484 -14.171 19.278  1.00 44.44  ?  336 GLU   B CB  1 
ATOM   3978 C  CG  . GLU   B 1 180 ? -44.676 -15.351 18.833  1.00 49.08  ?  336 GLU   B CG  1 
ATOM   3979 C  CD  . GLU   B 1 180 ? -44.205 -15.161 17.403  1.00 52.22  ?  336 GLU   B CD  1 
ATOM   3980 O  OE1 . GLU   B 1 180 ? -45.024 -14.740 16.553  1.00 60.59  ?  336 GLU   B OE1 1 
ATOM   3981 O  OE2 . GLU   B 1 180 ? -43.011 -15.403 17.135  1.00 62.88  -1 336 GLU   B OE2 1 
ATOM   3982 N  N   . GLY   B 1 181 ? -45.215 -10.814 20.413  1.00 32.52  ?  337 GLY   B N   1 
ATOM   3983 C  CA  . GLY   B 1 181 ? -46.029 -9.655  20.705  1.00 30.94  ?  337 GLY   B CA  1 
ATOM   3984 C  C   . GLY   B 1 181 ? -45.713 -8.488  19.786  1.00 30.29  ?  337 GLY   B C   1 
ATOM   3985 O  O   . GLY   B 1 181 ? -44.930 -8.588  18.840  1.00 30.20  ?  337 GLY   B O   1 
ATOM   3986 N  N   . LEU   B 1 182 ? -46.292 -7.343  20.128  1.00 26.32  ?  338 LEU   B N   1 
ATOM   3987 C  CA  . LEU   B 1 182 ? -46.025 -6.095  19.421  1.00 33.39  ?  338 LEU   B CA  1 
ATOM   3988 C  C   . LEU   B 1 182 ? -46.186 -6.286  17.907  1.00 34.25  ?  338 LEU   B C   1 
ATOM   3989 O  O   . LEU   B 1 182 ? -45.303 -5.964  17.108  1.00 31.70  ?  338 LEU   B O   1 
ATOM   3990 C  CB  . LEU   B 1 182 ? -44.635 -5.552  19.775  1.00 25.67  ?  338 LEU   B CB  1 
ATOM   3991 C  CG  . LEU   B 1 182 ? -44.378 -4.108  19.301  1.00 28.44  ?  338 LEU   B CG  1 
ATOM   3992 C  CD1 . LEU   B 1 182 ? -45.356 -3.128  19.972  1.00 30.11  ?  338 LEU   B CD1 1 
ATOM   3993 C  CD2 . LEU   B 1 182 ? -42.927 -3.701  19.583  1.00 33.32  ?  338 LEU   B CD2 1 
ATOM   3994 N  N   . ARG   B 1 183 ? -47.336 -6.842  17.515  1.00 35.63  ?  339 ARG   B N   1 
ATOM   3995 C  CA  . ARG   B 1 183 ? -47.568 -7.265  16.127  1.00 33.03  ?  339 ARG   B CA  1 
ATOM   3996 C  C   . ARG   B 1 183 ? -47.949 -6.048  15.280  1.00 27.93  ?  339 ARG   B C   1 
ATOM   3997 O  O   . ARG   B 1 183 ? -49.064 -5.922  14.772  1.00 30.51  ?  339 ARG   B O   1 
ATOM   3998 C  CB  . ARG   B 1 183 ? -48.654 -8.334  16.067  1.00 34.92  ?  339 ARG   B CB  1 
ATOM   3999 C  CG  . ARG   B 1 183 ? -48.193 -9.727  16.527  1.00 39.61  ?  339 ARG   B CG  1 
ATOM   4000 C  CD  . ARG   B 1 183 ? -49.290 -10.789 16.327  1.00 54.61  ?  339 ARG   B CD  1 
ATOM   4001 N  NE  . ARG   B 1 183 ? -50.502 -10.504 17.094  1.00 59.78  ?  339 ARG   B NE  1 
ATOM   4002 C  CZ  . ARG   B 1 183 ? -51.666 -10.142 16.560  1.00 63.55  ?  339 ARG   B CZ  1 
ATOM   4003 N  NH1 . ARG   B 1 183 ? -51.836 -10.076 15.243  1.00 64.51  ?  339 ARG   B NH1 1 
ATOM   4004 N  NH2 . ARG   B 1 183 ? -52.685 -9.832  17.367  1.00 52.89  ?  339 ARG   B NH2 1 
ATOM   4005 N  N   . ILE   B 1 184 ? -46.988 -5.137  15.133  1.00 23.78  ?  340 ILE   B N   1 
ATOM   4006 C  CA  . ILE   B 1 184 ? -47.234 -3.846  14.484  1.00 26.74  ?  340 ILE   B CA  1 
ATOM   4007 C  C   . ILE   B 1 184 ? -46.765 -3.823  13.031  1.00 26.27  ?  340 ILE   B C   1 
ATOM   4008 O  O   . ILE   B 1 184 ? -46.717 -2.748  12.429  1.00 27.77  ?  340 ILE   B O   1 
ATOM   4009 C  CB  . ILE   B 1 184 ? -46.548 -2.701  15.244  1.00 32.37  ?  340 ILE   B CB  1 
ATOM   4010 C  CG1 . ILE   B 1 184 ? -45.016 -2.892  15.212  1.00 26.04  ?  340 ILE   B CG1 1 
ATOM   4011 C  CG2 . ILE   B 1 184 ? -47.108 -2.545  16.660  1.00 30.06  ?  340 ILE   B CG2 1 
ATOM   4012 C  CD1 . ILE   B 1 184 ? -44.252 -1.728  15.920  1.00 30.42  ?  340 ILE   B CD1 1 
ATOM   4013 N  N   . GLN   B 1 185 ? -46.366 -4.969  12.473  1.00 25.46  ?  341 GLN   B N   1 
ATOM   4014 C  CA  . GLN   B 1 185 ? -45.592 -4.950  11.237  1.00 30.25  ?  341 GLN   B CA  1 
ATOM   4015 C  C   . GLN   B 1 185 ? -46.400 -4.418  10.054  1.00 30.84  ?  341 GLN   B C   1 
ATOM   4016 O  O   . GLN   B 1 185 ? -45.840 -3.732  9.196   1.00 31.01  ?  341 GLN   B O   1 
ATOM   4017 C  CB  . GLN   B 1 185 ? -45.052 -6.340  10.916  1.00 29.64  ?  341 GLN   B CB  1 
ATOM   4018 C  CG  . GLN   B 1 185 ? -44.058 -6.898  11.938  1.00 36.47  ?  341 GLN   B CG  1 
ATOM   4019 C  CD  . GLN   B 1 185 ? -44.736 -7.805  12.937  1.00 32.09  ?  341 GLN   B CD  1 
ATOM   4020 O  OE1 . GLN   B 1 185 ? -45.886 -7.571  13.314  1.00 39.83  ?  341 GLN   B OE1 1 
ATOM   4021 N  NE2 . GLN   B 1 185 ? -44.063 -8.880  13.315  1.00 34.70  ?  341 GLN   B NE2 1 
ATOM   4022 N  N   . ASN   B 1 186 ? -47.700 -4.719  9.966   1.00 27.60  ?  342 ASN   B N   1 
ATOM   4023 C  CA  . ASN   B 1 186 ? -48.494 -4.238  8.831   1.00 32.77  ?  342 ASN   B CA  1 
ATOM   4024 C  C   . ASN   B 1 186 ? -49.066 -2.847  9.053   1.00 34.08  ?  342 ASN   B C   1 
ATOM   4025 O  O   . ASN   B 1 186 ? -49.728 -2.303  8.154   1.00 27.02  ?  342 ASN   B O   1 
ATOM   4026 C  CB  . ASN   B 1 186 ? -49.626 -5.219  8.504   1.00 32.61  ?  342 ASN   B CB  1 
ATOM   4027 C  CG  . ASN   B 1 186 ? -49.105 -6.616  8.200   1.00 46.40  ?  342 ASN   B CG  1 
ATOM   4028 O  OD1 . ASN   B 1 186 ? -49.673 -7.631  8.623   1.00 50.83  ?  342 ASN   B OD1 1 
ATOM   4029 N  ND2 . ASN   B 1 186 ? -48.001 -6.672  7.455   1.00 55.82  ?  342 ASN   B ND2 1 
ATOM   4030 N  N   . TRP   B 1 187 ? -48.805 -2.258  10.215  1.00 29.29  ?  343 TRP   B N   1 
ATOM   4031 C  CA  . TRP   B 1 187 ? -49.335 -0.947  10.586  1.00 28.28  ?  343 TRP   B CA  1 
ATOM   4032 C  C   . TRP   B 1 187 ? -48.223 0.060   10.627  1.00 32.53  ?  343 TRP   B C   1 
ATOM   4033 O  O   . TRP   B 1 187 ? -48.129 0.932   9.740   1.00 30.38  ?  343 TRP   B O   1 
ATOM   4034 C  CB  . TRP   B 1 187 ? -50.076 -1.079  11.930  1.00 25.29  ?  343 TRP   B CB  1 
ATOM   4035 C  CG  . TRP   B 1 187 ? -50.392 0.222   12.641  1.00 26.07  ?  343 TRP   B CG  1 
ATOM   4036 C  CD1 . TRP   B 1 187 ? -50.559 1.461   12.075  1.00 26.88  ?  343 TRP   B CD1 1 
ATOM   4037 C  CD2 . TRP   B 1 187 ? -50.458 0.424   14.062  1.00 26.75  ?  343 TRP   B CD2 1 
ATOM   4038 N  NE1 . TRP   B 1 187 ? -50.793 2.406   13.062  1.00 26.36  ?  343 TRP   B NE1 1 
ATOM   4039 C  CE2 . TRP   B 1 187 ? -50.733 1.793   14.283  1.00 28.92  ?  343 TRP   B CE2 1 
ATOM   4040 C  CE3 . TRP   B 1 187 ? -50.351 -0.434  15.177  1.00 25.12  ?  343 TRP   B CE3 1 
ATOM   4041 C  CZ2 . TRP   B 1 187 ? -50.861 2.335   15.573  1.00 27.38  ?  343 TRP   B CZ2 1 
ATOM   4042 C  CZ3 . TRP   B 1 187 ? -50.478 0.107   16.445  1.00 28.48  ?  343 TRP   B CZ3 1 
ATOM   4043 C  CH2 . TRP   B 1 187 ? -50.735 1.474   16.634  1.00 24.27  ?  343 TRP   B CH2 1 
ATOM   4044 N  N   . LEU   B 1 188 ? -47.314 -0.038  11.615  1.00 24.63  ?  344 LEU   B N   1 
ATOM   4045 C  CA  . LEU   B 1 188 ? -46.199 0.879   11.829  1.00 28.76  ?  344 LEU   B CA  1 
ATOM   4046 C  C   . LEU   B 1 188 ? -44.886 0.421   11.197  1.00 26.11  ?  344 LEU   B C   1 
ATOM   4047 O  O   . LEU   B 1 188 ? -43.960 1.230   11.129  1.00 24.05  ?  344 LEU   B O   1 
ATOM   4048 C  CB  . LEU   B 1 188 ? -45.960 1.081   13.340  1.00 29.01  ?  344 LEU   B CB  1 
ATOM   4049 C  CG  . LEU   B 1 188 ? -47.122 1.688   14.147  1.00 28.89  ?  344 LEU   B CG  1 
ATOM   4050 C  CD1 . LEU   B 1 188 ? -46.796 1.754   15.684  1.00 28.70  ?  344 LEU   B CD1 1 
ATOM   4051 C  CD2 . LEU   B 1 188 ? -47.523 3.079   13.559  1.00 28.33  ?  344 LEU   B CD2 1 
ATOM   4052 N  N   . SER   B 1 189 ? -44.766 -0.861  10.820  1.00 26.44  ?  345 SER   B N   1 
ATOM   4053 C  CA  . SER   B 1 189 ? -43.692 -1.471  10.013  1.00 30.23  ?  345 SER   B CA  1 
ATOM   4054 C  C   . SER   B 1 189 ? -42.774 -2.406  10.798  1.00 34.17  ?  345 SER   B C   1 
ATOM   4055 O  O   . SER   B 1 189 ? -42.634 -2.301  12.019  1.00 26.79  ?  345 SER   B O   1 
ATOM   4056 C  CB  . SER   B 1 189 ? -42.789 -0.443  9.314   1.00 29.22  ?  345 SER   B CB  1 
ATOM   4057 O  OG  . SER   B 1 189 ? -41.908 0.179   10.264  1.00 27.77  ?  345 SER   B OG  1 
ATOM   4058 N  N   . ALA   B 1 190 ? -42.139 -3.334  10.077  1.00 30.73  ?  346 ALA   B N   1 
ATOM   4059 C  CA  . ALA   B 1 190 ? -41.189 -4.235  10.705  1.00 30.81  ?  346 ALA   B CA  1 
ATOM   4060 C  C   . ALA   B 1 190 ? -39.942 -3.487  11.161  1.00 35.72  ?  346 ALA   B C   1 
ATOM   4061 O  O   . ALA   B 1 190 ? -39.323 -3.867  12.173  1.00 27.35  ?  346 ALA   B O   1 
ATOM   4062 C  CB  . ALA   B 1 190 ? -40.829 -5.367  9.734   1.00 27.89  ?  346 ALA   B CB  1 
ATOM   4063 N  N   . LYS   B 1 191 ? -39.552 -2.439  10.419  1.00 34.11  ?  347 LYS   B N   1 
ATOM   4064 C  CA  . LYS   B 1 191 ? -38.407 -1.628  10.822  1.00 33.42  ?  347 LYS   B CA  1 
ATOM   4065 C  C   . LYS   B 1 191 ? -38.657 -0.997  12.169  1.00 31.68  ?  347 LYS   B C   1 
ATOM   4066 O  O   . LYS   B 1 191 ? -37.771 -0.968  13.034  1.00 34.30  ?  347 LYS   B O   1 
ATOM   4067 C  CB  . LYS   B 1 191 ? -38.123 -0.517  9.811   1.00 33.46  ?  347 LYS   B CB  1 
ATOM   4068 C  CG  . LYS   B 1 191 ? -37.010 -0.823  8.861   1.00 43.49  ?  347 LYS   B CG  1 
ATOM   4069 C  CD  . LYS   B 1 191 ? -36.668 0.459   8.109   1.00 46.74  ?  347 LYS   B CD  1 
ATOM   4070 C  CE  . LYS   B 1 191 ? -37.482 0.624   6.880   1.00 35.59  ?  347 LYS   B CE  1 
ATOM   4071 N  NZ  . LYS   B 1 191 ? -37.789 2.087   6.756   1.00 48.66  ?  347 LYS   B NZ  1 
ATOM   4072 N  N   . VAL   B 1 192 ? -39.853 -0.446  12.349  1.00 29.26  ?  348 VAL   B N   1 
ATOM   4073 C  CA  . VAL   B 1 192 ? -40.185 0.176   13.619  1.00 34.91  ?  348 VAL   B CA  1 
ATOM   4074 C  C   . VAL   B 1 192 ? -40.258 -0.880  14.723  1.00 32.56  ?  348 VAL   B C   1 
ATOM   4075 O  O   . VAL   B 1 192 ? -39.761 -0.659  15.828  1.00 31.79  ?  348 VAL   B O   1 
ATOM   4076 C  CB  . VAL   B 1 192 ? -41.476 1.007   13.478  1.00 28.29  ?  348 VAL   B CB  1 
ATOM   4077 C  CG1 . VAL   B 1 192 ? -41.995 1.494   14.849  1.00 26.12  ?  348 VAL   B CG1 1 
ATOM   4078 C  CG2 . VAL   B 1 192 ? -41.200 2.225   12.581  1.00 28.40  ?  348 VAL   B CG2 1 
ATOM   4079 N  N   . ARG   B 1 193 ? -40.807 -2.065  14.434  1.00 31.07  ?  349 ARG   B N   1 
ATOM   4080 C  CA  . ARG   B 1 193 ? -40.813 -3.107  15.465  1.00 32.73  ?  349 ARG   B CA  1 
ATOM   4081 C  C   . ARG   B 1 193 ? -39.394 -3.447  15.905  1.00 32.68  ?  349 ARG   B C   1 
ATOM   4082 O  O   . ARG   B 1 193 ? -39.105 -3.530  17.108  1.00 36.52  ?  349 ARG   B O   1 
ATOM   4083 C  CB  . ARG   B 1 193 ? -41.527 -4.361  14.970  1.00 28.09  ?  349 ARG   B CB  1 
ATOM   4084 C  CG  . ARG   B 1 193 ? -41.661 -5.424  16.042  1.00 30.20  ?  349 ARG   B CG  1 
ATOM   4085 C  CD  . ARG   B 1 193 ? -42.481 -6.638  15.588  1.00 31.21  ?  349 ARG   B CD  1 
ATOM   4086 N  NE  . ARG   B 1 193 ? -42.771 -7.558  16.691  1.00 27.95  ?  349 ARG   B NE  1 
ATOM   4087 C  CZ  . ARG   B 1 193 ? -42.019 -8.596  17.039  1.00 35.29  ?  349 ARG   B CZ  1 
ATOM   4088 N  NH1 . ARG   B 1 193 ? -40.866 -8.860  16.434  1.00 33.49  ?  349 ARG   B NH1 1 
ATOM   4089 N  NH2 . ARG   B 1 193 ? -42.438 -9.402  18.017  1.00 37.63  ?  349 ARG   B NH2 1 
ATOM   4090 N  N   . LYS   B 1 194 ? -38.481 -3.624  14.943  1.00 32.81  ?  350 LYS   B N   1 
ATOM   4091 C  CA  . LYS   B 1 194 ? -37.094 -3.941  15.287  1.00 36.36  ?  350 LYS   B CA  1 
ATOM   4092 C  C   . LYS   B 1 194 ? -36.454 -2.838  16.128  1.00 39.75  ?  350 LYS   B C   1 
ATOM   4093 O  O   . LYS   B 1 194 ? -35.731 -3.115  17.100  1.00 35.76  ?  350 LYS   B O   1 
ATOM   4094 C  CB  . LYS   B 1 194 ? -36.289 -4.176  14.009  1.00 36.34  ?  350 LYS   B CB  1 
ATOM   4095 C  CG  . LYS   B 1 194 ? -34.930 -4.817  14.266  1.00 35.65  ?  350 LYS   B CG  1 
ATOM   4096 C  CD  . LYS   B 1 194 ? -34.000 -4.676  13.072  1.00 47.89  ?  350 LYS   B CD  1 
ATOM   4097 C  CE  . LYS   B 1 194 ? -33.001 -5.824  13.017  1.00 38.59  ?  350 LYS   B CE  1 
ATOM   4098 N  NZ  . LYS   B 1 194 ? -32.502 -6.175  14.396  1.00 60.38  ?  350 LYS   B NZ  1 
ATOM   4099 N  N   . GLN   B 1 195 ? -36.724 -1.580  15.785  1.00 34.98  ?  351 GLN   B N   1 
ATOM   4100 C  CA  . GLN   B 1 195 ? -36.133 -0.467  16.520  1.00 35.08  ?  351 GLN   B CA  1 
ATOM   4101 C  C   . GLN   B 1 195 ? -36.696 -0.387  17.940  1.00 32.78  ?  351 GLN   B C   1 
ATOM   4102 O  O   . GLN   B 1 195 ? -35.957 -0.114  18.901  1.00 34.55  ?  351 GLN   B O   1 
ATOM   4103 C  CB  . GLN   B 1 195 ? -36.425 0.831   15.783  1.00 36.36  ?  351 GLN   B CB  1 
ATOM   4104 C  CG  . GLN   B 1 195 ? -35.681 1.035   14.476  1.00 40.74  ?  351 GLN   B CG  1 
ATOM   4105 C  CD  . GLN   B 1 195 ? -36.020 2.398   13.891  1.00 54.61  ?  351 GLN   B CD  1 
ATOM   4106 O  OE1 . GLN   B 1 195 ? -35.454 2.827   12.871  1.00 62.86  ?  351 GLN   B OE1 1 
ATOM   4107 N  NE2 . GLN   B 1 195 ? -36.897 3.131   14.596  1.00 48.29  ?  351 GLN   B NE2 1 
ATOM   4108 N  N   . LEU   B 1 196 ? -38.012 -0.570  18.085  1.00 29.03  ?  352 LEU   B N   1 
ATOM   4109 C  CA  . LEU   B 1 196 ? -38.615 -0.520  19.412  1.00 33.57  ?  352 LEU   B CA  1 
ATOM   4110 C  C   . LEU   B 1 196 ? -38.054 -1.631  20.289  1.00 36.87  ?  352 LEU   B C   1 
ATOM   4111 O  O   . LEU   B 1 196 ? -37.636 -1.383  21.424  1.00 37.37  ?  352 LEU   B O   1 
ATOM   4112 C  CB  . LEU   B 1 196 ? -40.144 -0.589  19.318  1.00 26.74  ?  352 LEU   B CB  1 
ATOM   4113 C  CG  . LEU   B 1 196 ? -40.833 0.618   18.646  1.00 30.04  ?  352 LEU   B CG  1 
ATOM   4114 C  CD1 . LEU   B 1 196 ? -42.350 0.414   18.469  1.00 25.73  ?  352 LEU   B CD1 1 
ATOM   4115 C  CD2 . LEU   B 1 196 ? -40.562 1.924   19.406  1.00 34.57  ?  352 LEU   B CD2 1 
ATOM   4116 N  N   . ARG   B 1 197 ? -37.948 -2.847  19.741  1.00 33.88  ?  353 ARG   B N   1 
ATOM   4117 C  CA  . ARG   B 1 197 ? -37.479 -3.997  20.513  1.00 32.97  ?  353 ARG   B CA  1 
ATOM   4118 C  C   . ARG   B 1 197 ? -35.997 -3.912  20.887  1.00 30.56  ?  353 ARG   B C   1 
ATOM   4119 O  O   . ARG   B 1 197 ? -35.537 -4.706  21.725  1.00 31.46  ?  353 ARG   B O   1 
ATOM   4120 C  CB  . ARG   B 1 197 ? -37.750 -5.296  19.744  1.00 34.18  ?  353 ARG   B CB  1 
ATOM   4121 C  CG  . ARG   B 1 197 ? -39.232 -5.727  19.729  1.00 38.46  ?  353 ARG   B CG  1 
ATOM   4122 C  CD  . ARG   B 1 197 ? -39.474 -7.035  18.922  1.00 39.12  ?  353 ARG   B CD  1 
ATOM   4123 N  NE  . ARG   B 1 197 ? -38.628 -8.132  19.408  1.00 41.28  ?  353 ARG   B NE  1 
ATOM   4124 C  CZ  . ARG   B 1 197 ? -38.847 -8.828  20.517  1.00 40.74  ?  353 ARG   B CZ  1 
ATOM   4125 N  NH1 . ARG   B 1 197 ? -39.863 -8.557  21.323  1.00 41.08  ?  353 ARG   B NH1 1 
ATOM   4126 N  NH2 . ARG   B 1 197 ? -38.005 -9.800  20.849  1.00 48.09  ?  353 ARG   B NH2 1 
ATOM   4127 N  N   . LEU   B 1 198 ? -35.241 -2.993  20.291  1.00 30.11  ?  354 LEU   B N   1 
ATOM   4128 C  CA  . LEU   B 1 198 ? -33.877 -2.728  20.733  1.00 39.54  ?  354 LEU   B CA  1 
ATOM   4129 C  C   . LEU   B 1 198 ? -33.820 -1.734  21.891  1.00 35.33  ?  354 LEU   B C   1 
ATOM   4130 O  O   . LEU   B 1 198 ? -32.760 -1.587  22.514  1.00 38.40  ?  354 LEU   B O   1 
ATOM   4131 C  CB  . LEU   B 1 198 ? -33.033 -2.204  19.562  1.00 36.21  ?  354 LEU   B CB  1 
ATOM   4132 C  CG  . LEU   B 1 198 ? -32.716 -3.232  18.471  1.00 34.99  ?  354 LEU   B CG  1 
ATOM   4133 C  CD1 . LEU   B 1 198 ? -32.091 -2.532  17.270  1.00 46.01  ?  354 LEU   B CD1 1 
ATOM   4134 C  CD2 . LEU   B 1 198 ? -31.754 -4.269  19.031  1.00 50.04  ?  354 LEU   B CD2 1 
ATOM   4135 N  N   . LYS   B 1 199 ? -34.925 -1.055  22.187  1.00 31.14  ?  355 LYS   B N   1 
ATOM   4136 C  CA  . LYS   B 1 199 ? -34.980 -0.179  23.335  1.00 34.55  ?  355 LYS   B CA  1 
ATOM   4137 C  C   . LYS   B 1 199 ? -34.990 -1.027  24.605  1.00 32.66  ?  355 LYS   B C   1 
ATOM   4138 O  O   . LYS   B 1 199 ? -35.268 -2.232  24.561  1.00 33.47  ?  355 LYS   B O   1 
ATOM   4139 C  CB  . LYS   B 1 199 ? -36.218 0.711   23.275  1.00 29.61  ?  355 LYS   B CB  1 
ATOM   4140 C  CG  . LYS   B 1 199 ? -36.234 1.642   22.068  1.00 31.69  ?  355 LYS   B CG  1 
ATOM   4141 C  CD  . LYS   B 1 199 ? -37.511 2.454   21.970  1.00 41.26  ?  355 LYS   B CD  1 
ATOM   4142 C  CE  . LYS   B 1 199 ? -37.288 3.740   21.134  1.00 36.35  ?  355 LYS   B CE  1 
ATOM   4143 N  NZ  . LYS   B 1 199 ? -37.007 4.947   21.945  1.00 53.66  ?  355 LYS   B NZ  1 
ATOM   4144 N  N   . PRO   B 1 200 ? -34.695 -0.431  25.754  1.00 30.72  ?  356 PRO   B N   1 
ATOM   4145 C  CA  . PRO   B 1 200 ? -34.712 -1.219  26.989  1.00 32.33  ?  356 PRO   B CA  1 
ATOM   4146 C  C   . PRO   B 1 200 ? -36.134 -1.573  27.386  1.00 35.21  ?  356 PRO   B C   1 
ATOM   4147 O  O   . PRO   B 1 200 ? -37.104 -0.966  26.930  1.00 40.00  ?  356 PRO   B O   1 
ATOM   4148 C  CB  . PRO   B 1 200 ? -34.044 -0.304  28.030  1.00 35.63  ?  356 PRO   B CB  1 
ATOM   4149 C  CG  . PRO   B 1 200 ? -34.148 1.054   27.499  1.00 31.89  ?  356 PRO   B CG  1 
ATOM   4150 C  CD  . PRO   B 1 200 ? -34.144 0.921   25.966  1.00 33.14  ?  356 PRO   B CD  1 
ATOM   4151 N  N   . PHE   B 1 201 ? -36.246 -2.605  28.214  1.00 36.90  ?  357 PHE   B N   1 
ATOM   4152 C  CA  . PHE   B 1 201 ? -37.508 -2.945  28.849  1.00 36.47  ?  357 PHE   B CA  1 
ATOM   4153 C  C   . PHE   B 1 201 ? -37.377 -2.700  30.343  1.00 36.78  ?  357 PHE   B C   1 
ATOM   4154 O  O   . PHE   B 1 201 ? -36.275 -2.530  30.875  1.00 39.92  ?  357 PHE   B O   1 
ATOM   4155 C  CB  . PHE   B 1 201 ? -37.921 -4.402  28.570  1.00 40.58  ?  357 PHE   B CB  1 
ATOM   4156 C  CG  . PHE   B 1 201 ? -37.019 -5.434  29.183  1.00 37.78  ?  357 PHE   B CG  1 
ATOM   4157 C  CD1 . PHE   B 1 201 ? -35.922 -5.923  28.494  1.00 41.70  ?  357 PHE   B CD1 1 
ATOM   4158 C  CD2 . PHE   B 1 201 ? -37.309 -5.968  30.441  1.00 42.07  ?  357 PHE   B CD2 1 
ATOM   4159 C  CE1 . PHE   B 1 201 ? -35.089 -6.898  29.074  1.00 46.67  ?  357 PHE   B CE1 1 
ATOM   4160 C  CE2 . PHE   B 1 201 ? -36.484 -6.935  31.030  1.00 38.50  ?  357 PHE   B CE2 1 
ATOM   4161 C  CZ  . PHE   B 1 201 ? -35.381 -7.405  30.348  1.00 46.94  ?  357 PHE   B CZ  1 
ATOM   4162 N  N   . TYR   B 1 202 ? -38.518 -2.711  31.022  1.00 35.22  ?  358 TYR   B N   1 
ATOM   4163 C  CA  . TYR   B 1 202 ? -38.598 -2.324  32.419  1.00 36.72  ?  358 TYR   B CA  1 
ATOM   4164 C  C   . TYR   B 1 202 ? -39.291 -3.404  33.233  1.00 39.89  ?  358 TYR   B C   1 
ATOM   4165 O  O   . TYR   B 1 202 ? -40.062 -4.211  32.704  1.00 37.47  ?  358 TYR   B O   1 
ATOM   4166 C  CB  . TYR   B 1 202 ? -39.310 -0.968  32.561  1.00 35.10  ?  358 TYR   B CB  1 
ATOM   4167 C  CG  . TYR   B 1 202 ? -38.505 0.099   31.861  1.00 33.26  ?  358 TYR   B CG  1 
ATOM   4168 C  CD1 . TYR   B 1 202 ? -38.642 0.320   30.494  1.00 35.74  ?  358 TYR   B CD1 1 
ATOM   4169 C  CD2 . TYR   B 1 202 ? -37.513 0.795   32.548  1.00 40.00  ?  358 TYR   B CD2 1 
ATOM   4170 C  CE1 . TYR   B 1 202 ? -37.878 1.247   29.842  1.00 38.34  ?  358 TYR   B CE1 1 
ATOM   4171 C  CE2 . TYR   B 1 202 ? -36.728 1.728   31.898  1.00 41.49  ?  358 TYR   B CE2 1 
ATOM   4172 C  CZ  . TYR   B 1 202 ? -36.923 1.946   30.536  1.00 39.83  ?  358 TYR   B CZ  1 
ATOM   4173 O  OH  . TYR   B 1 202 ? -36.156 2.852   29.858  1.00 41.90  ?  358 TYR   B OH  1 
ATOM   4174 N  N   . LEU   B 1 203 ? -39.003 -3.395  34.531  1.00 33.95  ?  359 LEU   B N   1 
ATOM   4175 C  CA  . LEU   B 1 203 ? -39.576 -4.329  35.483  1.00 33.84  ?  359 LEU   B CA  1 
ATOM   4176 C  C   . LEU   B 1 203 ? -40.036 -3.556  36.707  1.00 38.67  ?  359 LEU   B C   1 
ATOM   4177 O  O   . LEU   B 1 203 ? -39.269 -2.772  37.284  1.00 41.03  ?  359 LEU   B O   1 
ATOM   4178 C  CB  . LEU   B 1 203 ? -38.560 -5.399  35.889  1.00 46.20  ?  359 LEU   B CB  1 
ATOM   4179 C  CG  . LEU   B 1 203 ? -38.277 -6.437  34.806  1.00 40.95  ?  359 LEU   B CG  1 
ATOM   4180 C  CD1 . LEU   B 1 203 ? -36.958 -7.117  35.124  1.00 46.64  ?  359 LEU   B CD1 1 
ATOM   4181 C  CD2 . LEU   B 1 203 ? -39.383 -7.449  34.783  1.00 39.34  ?  359 LEU   B CD2 1 
ATOM   4182 N  N   . VAL   B 1 204 ? -41.261 -3.817  37.122  1.00 38.42  ?  360 VAL   B N   1 
ATOM   4183 C  CA  . VAL   B 1 204 ? -41.940 -3.057  38.167  1.00 39.93  ?  360 VAL   B CA  1 
ATOM   4184 C  C   . VAL   B 1 204 ? -42.316 -4.012  39.261  1.00 41.50  ?  360 VAL   B C   1 
ATOM   4185 O  O   . VAL   B 1 204 ? -42.822 -5.108  38.982  1.00 35.99  ?  360 VAL   B O   1 
ATOM   4186 C  CB  . VAL   B 1 204 ? -43.178 -2.329  37.581  1.00 45.49  ?  360 VAL   B CB  1 
ATOM   4187 C  CG1 . VAL   B 1 204 ? -44.203 -2.043  38.614  1.00 56.76  ?  360 VAL   B CG1 1 
ATOM   4188 C  CG2 . VAL   B 1 204 ? -42.717 -1.011  36.903  1.00 34.26  ?  360 VAL   B CG2 1 
ATOM   4189 N  N   . PRO   B 1 205 ? -42.034 -3.711  40.541  1.00 44.93  ?  361 PRO   B N   1 
ATOM   4190 C  CA  . PRO   B 1 205 ? -42.359 -4.653  41.626  1.00 49.94  ?  361 PRO   B CA  1 
ATOM   4191 C  C   . PRO   B 1 205 ? -43.862 -4.845  41.760  1.00 55.65  ?  361 PRO   B C   1 
ATOM   4192 O  O   . PRO   B 1 205 ? -44.619 -3.894  41.974  1.00 48.85  ?  361 PRO   B O   1 
ATOM   4193 C  CB  . PRO   B 1 205 ? -41.749 -3.998  42.866  1.00 48.11  ?  361 PRO   B CB  1 
ATOM   4194 C  CG  . PRO   B 1 205 ? -41.622 -2.548  42.510  1.00 46.86  ?  361 PRO   B CG  1 
ATOM   4195 C  CD  . PRO   B 1 205 ? -41.417 -2.471  41.040  1.00 46.63  ?  361 PRO   B CD  1 
ATOM   4196 N  N   . LYS   B 1 206 ? -44.296 -6.094  41.620  1.00 56.80  ?  362 LYS   B N   1 
ATOM   4197 C  CA  . LYS   B 1 206 ? -45.721 -6.396  41.541  1.00 52.62  ?  362 LYS   B CA  1 
ATOM   4198 C  C   . LYS   B 1 206 ? -45.964 -7.825  41.971  1.00 56.39  ?  362 LYS   B C   1 
ATOM   4199 O  O   . LYS   B 1 206 ? -45.336 -8.759  41.457  1.00 49.28  ?  362 LYS   B O   1 
ATOM   4200 C  CB  . LYS   B 1 206 ? -46.269 -6.211  40.144  1.00 48.39  ?  362 LYS   B CB  1 
ATOM   4201 C  CG  . LYS   B 1 206 ? -47.784 -6.239  40.053  1.00 48.21  ?  362 LYS   B CG  1 
ATOM   4202 C  CD  . LYS   B 1 206 ? -48.304 -4.817  39.936  1.00 55.80  ?  362 LYS   B CD  1 
ATOM   4203 C  CE  . LYS   B 1 206 ? -49.825 -4.757  39.839  1.00 63.91  ?  362 LYS   B CE  1 
ATOM   4204 N  NZ  . LYS   B 1 206 ? -50.361 -3.498  40.430  1.00 64.66  ?  362 LYS   B NZ  1 
ATOM   4205 N  N   . HIS   B 1 207 ? -46.944 -7.978  42.844  1.00 58.30  ?  363 HIS   B N   1 
ATOM   4206 C  CA  . HIS   B 1 207 ? -47.163 -9.254  43.481  1.00 63.57  ?  363 HIS   B CA  1 
ATOM   4207 C  C   . HIS   B 1 207 ? -47.747 -10.210 42.463  1.00 53.90  ?  363 HIS   B C   1 
ATOM   4208 O  O   . HIS   B 1 207 ? -48.399 -9.794  41.518  1.00 59.49  ?  363 HIS   B O   1 
ATOM   4209 C  CB  . HIS   B 1 207 ? -48.135 -9.092  44.622  1.00 65.53  ?  363 HIS   B CB  1 
ATOM   4210 C  CG  . HIS   B 1 207 ? -47.468 -8.759  45.917  1.00 54.75  ?  363 HIS   B CG  1 
ATOM   4211 N  ND1 . HIS   B 1 207 ? -48.174 -8.398  47.040  1.00 76.60  ?  363 HIS   B ND1 1 
ATOM   4212 C  CD2 . HIS   B 1 207 ? -46.164 -8.483  46.203  1.00 63.93  ?  363 HIS   B CD2 1 
ATOM   4213 C  CE1 . HIS   B 1 207 ? -47.337 -8.100  48.027  1.00 74.09  ?  363 HIS   B CE1 1 
ATOM   4214 N  NE2 . HIS   B 1 207 ? -46.114 -8.091  47.531  1.00 79.15  ?  363 HIS   B NE2 1 
ATOM   4215 N  N   . ALA   B 1 208 ? -47.520 -11.505 42.654  1.00 62.75  ?  364 ALA   B N   1 
ATOM   4216 C  CA  . ALA   B 1 208 ? -48.203 -12.491 41.829  1.00 58.45  ?  364 ALA   B CA  1 
ATOM   4217 C  C   . ALA   B 1 208 ? -48.973 -13.457 42.722  1.00 52.47  ?  364 ALA   B C   1 
ATOM   4218 O  O   . ALA   B 1 208 ? -48.510 -13.813 43.812  1.00 76.05  ?  364 ALA   B O   1 
ATOM   4219 C  CB  . ALA   B 1 208 ? -47.224 -13.235 40.915  1.00 49.94  ?  364 ALA   B CB  1 
ATOM   4220 N  N   . LYS   B 1 209 ? -50.161 -13.854 42.258  1.00 74.48  ?  365 LYS   B N   1 
ATOM   4221 C  CA  . LYS   B 1 209 ? -51.105 -14.701 43.003  1.00 66.30  ?  365 LYS   B CA  1 
ATOM   4222 C  C   . LYS   B 1 209 ? -50.503 -16.022 43.494  1.00 72.70  ?  365 LYS   B C   1 
ATOM   4223 O  O   . LYS   B 1 209 ? -50.077 -16.862 42.701  1.00 78.06  ?  365 LYS   B O   1 
ATOM   4224 C  CB  . LYS   B 1 209 ? -52.332 -14.990 42.126  1.00 68.25  ?  365 LYS   B CB  1 
ATOM   4225 N  N   . PHE   B 1 214 ? -49.843 -13.537 48.483  1.00 65.64  ?  370 PHE   B N   1 
ATOM   4226 C  CA  . PHE   B 1 214 ? -49.168 -14.679 47.870  1.00 70.97  ?  370 PHE   B CA  1 
ATOM   4227 C  C   . PHE   B 1 214 ? -47.666 -14.401 47.651  1.00 71.95  ?  370 PHE   B C   1 
ATOM   4228 O  O   . PHE   B 1 214 ? -46.956 -14.047 48.603  1.00 74.60  ?  370 PHE   B O   1 
ATOM   4229 C  CB  . PHE   B 1 214 ? -49.857 -15.054 46.558  1.00 67.33  ?  370 PHE   B CB  1 
ATOM   4230 N  N   . GLN   B 1 215 ? -47.182 -14.570 46.417  1.00 71.97  ?  371 GLN   B N   1 
ATOM   4231 C  CA  . GLN   B 1 215 ? -45.757 -14.429 46.113  1.00 63.24  ?  371 GLN   B CA  1 
ATOM   4232 C  C   . GLN   B 1 215 ? -45.328 -12.966 46.153  1.00 68.94  ?  371 GLN   B C   1 
ATOM   4233 O  O   . GLN   B 1 215 ? -45.839 -12.135 45.400  1.00 57.08  ?  371 GLN   B O   1 
ATOM   4234 C  CB  . GLN   B 1 215 ? -45.436 -15.085 44.768  1.00 61.80  ?  371 GLN   B CB  1 
ATOM   4235 C  CG  . GLN   B 1 215 ? -44.021 -14.809 44.308  1.00 60.00  ?  371 GLN   B CG  1 
ATOM   4236 C  CD  . GLN   B 1 215 ? -42.978 -15.198 45.339  1.00 65.59  ?  371 GLN   B CD  1 
ATOM   4237 O  OE1 . GLN   B 1 215 ? -42.200 -14.339 45.777  1.00 68.04  ?  371 GLN   B OE1 1 
ATOM   4238 N  NE2 . GLN   B 1 215 ? -42.987 -16.459 45.784  1.00 65.19  ?  371 GLN   B NE2 1 
ATOM   4239 N  N   . GLU   B 1 216 ? -44.381 -12.627 47.012  1.00 67.35  ?  372 GLU   B N   1 
ATOM   4240 C  CA  . GLU   B 1 216 ? -44.131 -11.218 47.294  1.00 59.28  ?  372 GLU   B CA  1 
ATOM   4241 C  C   . GLU   B 1 216 ? -42.890 -10.619 46.622  1.00 67.95  ?  372 GLU   B C   1 
ATOM   4242 O  O   . GLU   B 1 216 ? -42.672 -9.402  46.728  1.00 65.87  ?  372 GLU   B O   1 
ATOM   4243 C  CB  . GLU   B 1 216 ? -44.092 -11.061 48.806  1.00 63.84  ?  372 GLU   B CB  1 
ATOM   4244 C  CG  . GLU   B 1 216 ? -45.492 -10.805 49.319  1.00 70.07  ?  372 GLU   B CG  1 
ATOM   4245 C  CD  . GLU   B 1 216 ? -45.604 -9.583  50.245  1.00 81.43  ?  372 GLU   B CD  1 
ATOM   4246 O  OE1 . GLU   B 1 216 ? -44.692 -8.708  50.221  1.00 92.06  ?  372 GLU   B OE1 1 
ATOM   4247 O  OE2 . GLU   B 1 216 ? -46.523 -9.619  51.126  1.00 84.26  -1 372 GLU   B OE2 1 
ATOM   4248 N  N   . GLU   B 1 217 ? -42.128 -11.399 45.841  1.00 62.90  ?  373 GLU   B N   1 
ATOM   4249 C  CA  . GLU   B 1 217 ? -40.816 -10.959 45.363  1.00 55.74  ?  373 GLU   B CA  1 
ATOM   4250 C  C   . GLU   B 1 217 ? -40.710 -10.958 43.838  1.00 52.37  ?  373 GLU   B C   1 
ATOM   4251 O  O   . GLU   B 1 217 ? -39.597 -10.976 43.290  1.00 46.29  ?  373 GLU   B O   1 
ATOM   4252 C  CB  . GLU   B 1 217 ? -39.704 -11.839 45.946  1.00 47.55  ?  373 GLU   B CB  1 
ATOM   4253 C  CG  . GLU   B 1 217 ? -39.353 -11.656 47.435  1.00 65.83  ?  373 GLU   B CG  1 
ATOM   4254 C  CD  . GLU   B 1 217 ? -39.750 -10.311 48.034  1.00 64.35  ?  373 GLU   B CD  1 
ATOM   4255 O  OE1 . GLU   B 1 217 ? -39.342 -9.263  47.479  1.00 63.91  ?  373 GLU   B OE1 1 
ATOM   4256 O  OE2 . GLU   B 1 217 ? -40.423 -10.307 49.094  1.00 65.98  -1 373 GLU   B OE2 1 
ATOM   4257 N  N   . THR   B 1 218 ? -41.832 -10.941 43.140  1.00 45.06  ?  374 THR   B N   1 
ATOM   4258 C  CA  . THR   B 1 218 ? -41.791 -10.936 41.694  1.00 45.39  ?  374 THR   B CA  1 
ATOM   4259 C  C   . THR   B 1 218 ? -41.843 -9.508  41.156  1.00 51.80  ?  374 THR   B C   1 
ATOM   4260 O  O   . THR   B 1 218 ? -42.295 -8.573  41.823  1.00 55.65  ?  374 THR   B O   1 
ATOM   4261 C  CB  . THR   B 1 218 ? -42.932 -11.780 41.132  1.00 50.72  ?  374 THR   B CB  1 
ATOM   4262 O  OG1 . THR   B 1 218 ? -44.165 -11.385 41.751  1.00 51.82  ?  374 THR   B OG1 1 
ATOM   4263 C  CG2 . THR   B 1 218 ? -42.665 -13.263 41.376  1.00 55.17  ?  374 THR   B CG2 1 
ATOM   4264 N  N   . TRP   B 1 219 ? -41.342 -9.362  39.937  1.00 46.66  ?  375 TRP   B N   1 
ATOM   4265 C  CA  . TRP   B 1 219 ? -41.316 -8.112  39.203  1.00 45.67  ?  375 TRP   B CA  1 
ATOM   4266 C  C   . TRP   B 1 219 ? -42.086 -8.340  37.911  1.00 48.70  ?  375 TRP   B C   1 
ATOM   4267 O  O   . TRP   B 1 219 ? -42.017 -9.426  37.325  1.00 47.51  ?  375 TRP   B O   1 
ATOM   4268 C  CB  . TRP   B 1 219 ? -39.878 -7.696  38.905  1.00 40.37  ?  375 TRP   B CB  1 
ATOM   4269 C  CG  . TRP   B 1 219 ? -39.013 -7.534  40.135  1.00 44.37  ?  375 TRP   B CG  1 
ATOM   4270 C  CD1 . TRP   B 1 219 ? -38.430 -8.541  40.866  1.00 47.43  ?  375 TRP   B CD1 1 
ATOM   4271 C  CD2 . TRP   B 1 219 ? -38.554 -6.305  40.719  1.00 46.46  ?  375 TRP   B CD2 1 
ATOM   4272 N  NE1 . TRP   B 1 219 ? -37.675 -8.011  41.887  1.00 41.96  ?  375 TRP   B NE1 1 
ATOM   4273 C  CE2 . TRP   B 1 219 ? -37.731 -6.644  41.817  1.00 47.89  ?  375 TRP   B CE2 1 
ATOM   4274 C  CE3 . TRP   B 1 219 ? -38.775 -4.954  40.433  1.00 48.74  ?  375 TRP   B CE3 1 
ATOM   4275 C  CZ2 . TRP   B 1 219 ? -37.132 -5.678  42.630  1.00 52.32  ?  375 TRP   B CZ2 1 
ATOM   4276 C  CZ3 . TRP   B 1 219 ? -38.180 -4.000  41.235  1.00 44.54  ?  375 TRP   B CZ3 1 
ATOM   4277 C  CH2 . TRP   B 1 219 ? -37.368 -4.363  42.320  1.00 52.62  ?  375 TRP   B CH2 1 
ATOM   4278 N  N   . ARG   B 1 220 ? -42.816 -7.328  37.459  1.00 42.49  ?  376 ARG   B N   1 
ATOM   4279 C  CA  . ARG   B 1 220 ? -43.687 -7.476  36.302  1.00 36.64  ?  376 ARG   B CA  1 
ATOM   4280 C  C   . ARG   B 1 220 ? -43.180 -6.609  35.157  1.00 37.91  ?  376 ARG   B C   1 
ATOM   4281 O  O   . ARG   B 1 220 ? -42.771 -5.467  35.375  1.00 35.85  ?  376 ARG   B O   1 
ATOM   4282 C  CB  . ARG   B 1 220 ? -45.120 -7.089  36.645  1.00 42.04  ?  376 ARG   B CB  1 
ATOM   4283 C  CG  . ARG   B 1 220 ? -46.150 -7.672  35.709  1.00 44.88  ?  376 ARG   B CG  1 
ATOM   4284 C  CD  . ARG   B 1 220 ? -47.355 -6.774  35.686  1.00 42.66  ?  376 ARG   B CD  1 
ATOM   4285 N  NE  . ARG   B 1 220 ? -46.985 -5.526  35.035  1.00 51.83  ?  376 ARG   B NE  1 
ATOM   4286 C  CZ  . ARG   B 1 220 ? -47.326 -4.315  35.454  1.00 49.56  ?  376 ARG   B CZ  1 
ATOM   4287 N  NH1 . ARG   B 1 220 ? -48.123 -4.141  36.495  1.00 52.10  ?  376 ARG   B NH1 1 
ATOM   4288 N  NH2 . ARG   B 1 220 ? -46.846 -3.251  34.812  1.00 46.40  ?  376 ARG   B NH2 1 
ATOM   4289 N  N   . LEU   B 1 221 ? -43.211 -7.159  33.944  1.00 33.66  ?  377 LEU   B N   1 
ATOM   4290 C  CA  . LEU   B 1 221 ? -42.725 -6.427  32.781  1.00 43.94  ?  377 LEU   B CA  1 
ATOM   4291 C  C   . LEU   B 1 221 ? -43.530 -5.150  32.574  1.00 39.32  ?  377 LEU   B C   1 
ATOM   4292 O  O   . LEU   B 1 221 ? -44.727 -5.087  32.867  1.00 41.07  ?  377 LEU   B O   1 
ATOM   4293 C  CB  . LEU   B 1 221 ? -42.807 -7.281  31.515  1.00 36.51  ?  377 LEU   B CB  1 
ATOM   4294 C  CG  . LEU   B 1 221 ? -41.830 -8.461  31.402  1.00 46.30  ?  377 LEU   B CG  1 
ATOM   4295 C  CD1 . LEU   B 1 221 ? -42.147 -9.357  30.186  1.00 38.45  ?  377 LEU   B CD1 1 
ATOM   4296 C  CD2 . LEU   B 1 221 ? -40.366 -8.017  31.407  1.00 40.16  ?  377 LEU   B CD2 1 
ATOM   4297 N  N   . SER   B 1 222 ? -42.855 -4.118  32.081  1.00 34.65  ?  378 SER   B N   1 
ATOM   4298 C  CA  . SER   B 1 222 ? -43.511 -2.857  31.790  1.00 32.75  ?  378 SER   B CA  1 
ATOM   4299 C  C   . SER   B 1 222 ? -43.004 -2.325  30.454  1.00 31.14  ?  378 SER   B C   1 
ATOM   4300 O  O   . SER   B 1 222 ? -41.793 -2.192  30.240  1.00 33.47  ?  378 SER   B O   1 
ATOM   4301 C  CB  . SER   B 1 222 ? -43.292 -1.821  32.899  1.00 32.66  ?  378 SER   B CB  1 
ATOM   4302 O  OG  . SER   B 1 222 ? -43.878 -0.567  32.530  1.00 33.19  ?  378 SER   B OG  1 
ATOM   4303 N  N   . PHE   B 1 223 ? -43.943 -1.992  29.576  1.00 30.61  ?  379 PHE   B N   1 
ATOM   4304 C  CA  . PHE   B 1 223 ? -43.628 -1.435  28.261  1.00 35.55  ?  379 PHE   B CA  1 
ATOM   4305 C  C   . PHE   B 1 223 ? -44.275 -0.078  28.043  1.00 34.13  ?  379 PHE   B C   1 
ATOM   4306 O  O   . PHE   B 1 223 ? -44.429 0.348   26.895  1.00 31.41  ?  379 PHE   B O   1 
ATOM   4307 C  CB  . PHE   B 1 223 ? -44.057 -2.410  27.165  1.00 30.50  ?  379 PHE   B CB  1 
ATOM   4308 C  CG  . PHE   B 1 223 ? -43.346 -3.721  27.230  1.00 28.94  ?  379 PHE   B CG  1 
ATOM   4309 C  CD1 . PHE   B 1 223 ? -42.032 -3.835  26.790  1.00 31.11  ?  379 PHE   B CD1 1 
ATOM   4310 C  CD2 . PHE   B 1 223 ? -43.969 -4.820  27.778  1.00 29.70  ?  379 PHE   B CD2 1 
ATOM   4311 C  CE1 . PHE   B 1 223 ? -41.350 -5.051  26.867  1.00 34.95  ?  379 PHE   B CE1 1 
ATOM   4312 C  CE2 . PHE   B 1 223 ? -43.300 -6.041  27.876  1.00 35.38  ?  379 PHE   B CE2 1 
ATOM   4313 C  CZ  . PHE   B 1 223 ? -41.983 -6.156  27.421  1.00 35.80  ?  379 PHE   B CZ  1 
ATOM   4314 N  N   . SER   B 1 224 ? -44.633 0.622   29.123  1.00 34.43  ?  380 SER   B N   1 
ATOM   4315 C  CA  . SER   B 1 224 ? -45.397 1.857   28.977  1.00 35.72  ?  380 SER   B CA  1 
ATOM   4316 C  C   . SER   B 1 224 ? -44.668 2.885   28.114  1.00 32.68  ?  380 SER   B C   1 
ATOM   4317 O  O   . SER   B 1 224 ? -45.318 3.722   27.480  1.00 36.43  ?  380 SER   B O   1 
ATOM   4318 C  CB  . SER   B 1 224 ? -45.717 2.445   30.351  1.00 42.81  ?  380 SER   B CB  1 
ATOM   4319 O  OG  . SER   B 1 224 ? -44.523 2.857   30.971  1.00 55.23  ?  380 SER   B OG  1 
ATOM   4320 N  N   . HIS   B 1 225 ? -43.335 2.848   28.070  1.00 30.70  ?  381 HIS   B N   1 
ATOM   4321 C  CA  . HIS   B 1 225 ? -42.616 3.772   27.194  1.00 34.09  ?  381 HIS   B CA  1 
ATOM   4322 C  C   . HIS   B 1 225 ? -42.841 3.439   25.725  1.00 31.69  ?  381 HIS   B C   1 
ATOM   4323 O  O   . HIS   B 1 225 ? -42.826 4.335   24.877  1.00 33.53  ?  381 HIS   B O   1 
ATOM   4324 C  CB  . HIS   B 1 225 ? -41.126 3.737   27.498  1.00 35.80  ?  381 HIS   B CB  1 
ATOM   4325 C  CG  . HIS   B 1 225 ? -40.514 2.389   27.295  1.00 31.50  ?  381 HIS   B CG  1 
ATOM   4326 N  ND1 . HIS   B 1 225 ? -41.003 1.255   27.908  1.00 32.47  ?  381 HIS   B ND1 1 
ATOM   4327 C  CD2 . HIS   B 1 225 ? -39.460 1.989   26.548  1.00 31.94  ?  381 HIS   B CD2 1 
ATOM   4328 C  CE1 . HIS   B 1 225 ? -40.278 0.214   27.542  1.00 33.15  ?  381 HIS   B CE1 1 
ATOM   4329 N  NE2 . HIS   B 1 225 ? -39.326 0.633   26.729  1.00 33.58  ?  381 HIS   B NE2 1 
ATOM   4330 N  N   . ILE   B 1 226 ? -42.995 2.151   25.404  1.00 31.02  ?  382 ILE   B N   1 
ATOM   4331 C  CA  . ILE   B 1 226 ? -43.315 1.749   24.033  1.00 28.59  ?  382 ILE   B CA  1 
ATOM   4332 C  C   . ILE   B 1 226 ? -44.734 2.167   23.681  1.00 31.34  ?  382 ILE   B C   1 
ATOM   4333 O  O   . ILE   B 1 226 ? -44.999 2.658   22.571  1.00 28.41  ?  382 ILE   B O   1 
ATOM   4334 C  CB  . ILE   B 1 226 ? -43.140 0.228   23.845  1.00 28.34  ?  382 ILE   B CB  1 
ATOM   4335 C  CG1 . ILE   B 1 226 ? -41.744 -0.262  24.252  1.00 28.39  ?  382 ILE   B CG1 1 
ATOM   4336 C  CG2 . ILE   B 1 226 ? -43.448 -0.189  22.375  1.00 28.15  ?  382 ILE   B CG2 1 
ATOM   4337 C  CD1 . ILE   B 1 226 ? -40.596 0.375   23.542  1.00 28.84  ?  382 ILE   B CD1 1 
ATOM   4338 N  N   . GLU   B 1 227 ? -45.674 1.957   24.606  1.00 28.03  ?  383 GLU   B N   1 
ATOM   4339 C  CA  . GLU   B 1 227 ? -47.052 2.388   24.383  1.00 33.45  ?  383 GLU   B CA  1 
ATOM   4340 C  C   . GLU   B 1 227 ? -47.119 3.875   24.046  1.00 32.91  ?  383 GLU   B C   1 
ATOM   4341 O  O   . GLU   B 1 227 ? -47.847 4.288   23.134  1.00 30.08  ?  383 GLU   B O   1 
ATOM   4342 C  CB  . GLU   B 1 227 ? -47.874 2.055   25.625  1.00 30.80  ?  383 GLU   B CB  1 
ATOM   4343 C  CG  . GLU   B 1 227 ? -47.436 0.713   26.211  1.00 47.20  ?  383 GLU   B CG  1 
ATOM   4344 C  CD  . GLU   B 1 227 ? -48.172 0.312   27.498  1.00 43.39  ?  383 GLU   B CD  1 
ATOM   4345 O  OE1 . GLU   B 1 227 ? -48.208 -0.893  27.808  1.00 52.67  ?  383 GLU   B OE1 1 
ATOM   4346 O  OE2 . GLU   B 1 227 ? -48.666 1.195   28.218  1.00 45.88  -1 383 GLU   B OE2 1 
ATOM   4347 N  N   . LYS   B 1 228 ? -46.342 4.685   24.763  1.00 32.82  ?  384 LYS   B N   1 
ATOM   4348 C  CA  . LYS   B 1 228 ? -46.341 6.127   24.534  1.00 38.37  ?  384 LYS   B CA  1 
ATOM   4349 C  C   . LYS   B 1 228 ? -45.840 6.452   23.130  1.00 33.70  ?  384 LYS   B C   1 
ATOM   4350 O  O   . LYS   B 1 228 ? -46.412 7.292   22.424  1.00 33.20  ?  384 LYS   B O   1 
ATOM   4351 C  CB  . LYS   B 1 228 ? -45.488 6.805   25.623  1.00 31.85  ?  384 LYS   B CB  1 
ATOM   4352 C  CG  . LYS   B 1 228 ? -45.289 8.325   25.500  1.00 37.57  ?  384 LYS   B CG  1 
ATOM   4353 C  CD  . LYS   B 1 228 ? -44.153 8.670   24.504  1.00 43.46  ?  384 LYS   B CD  1 
ATOM   4354 C  CE  . LYS   B 1 228 ? -42.773 8.738   25.189  1.00 53.12  ?  384 LYS   B CE  1 
ATOM   4355 N  NZ  . LYS   B 1 228 ? -41.634 8.902   24.218  1.00 51.28  ?  384 LYS   B NZ  1 
ATOM   4356 N  N   . GLU   B 1 229 ? -44.767 5.791   22.705  1.00 33.87  ?  385 GLU   B N   1 
ATOM   4357 C  CA  . GLU   B 1 229 ? -44.243 6.062   21.373  1.00 40.29  ?  385 GLU   B CA  1 
ATOM   4358 C  C   . GLU   B 1 229 ? -45.253 5.695   20.295  1.00 38.46  ?  385 GLU   B C   1 
ATOM   4359 O  O   . GLU   B 1 229 ? -45.487 6.474   19.365  1.00 31.98  ?  385 GLU   B O   1 
ATOM   4360 C  CB  . GLU   B 1 229 ? -42.912 5.341   21.154  1.00 36.19  ?  385 GLU   B CB  1 
ATOM   4361 C  CG  . GLU   B 1 229 ? -41.821 5.876   22.079  1.00 42.95  ?  385 GLU   B CG  1 
ATOM   4362 C  CD  . GLU   B 1 229 ? -40.426 5.743   21.483  1.00 49.08  ?  385 GLU   B CD  1 
ATOM   4363 O  OE1 . GLU   B 1 229 ? -40.313 5.705   20.233  1.00 48.61  ?  385 GLU   B OE1 1 
ATOM   4364 O  OE2 . GLU   B 1 229 ? -39.444 5.720   22.263  1.00 61.08  -1 385 GLU   B OE2 1 
ATOM   4365 N  N   . ILE   B 1 230 ? -45.879 4.519   20.412  1.00 36.59  ?  386 ILE   B N   1 
ATOM   4366 C  CA  . ILE   B 1 230 ? -46.919 4.136   19.456  1.00 31.38  ?  386 ILE   B CA  1 
ATOM   4367 C  C   . ILE   B 1 230 ? -48.023 5.186   19.397  1.00 37.05  ?  386 ILE   B C   1 
ATOM   4368 O  O   . ILE   B 1 230 ? -48.374 5.676   18.317  1.00 40.67  ?  386 ILE   B O   1 
ATOM   4369 C  CB  . ILE   B 1 230 ? -47.480 2.750   19.807  1.00 31.80  ?  386 ILE   B CB  1 
ATOM   4370 C  CG1 . ILE   B 1 230 ? -46.453 1.679   19.458  1.00 30.18  ?  386 ILE   B CG1 1 
ATOM   4371 C  CG2 . ILE   B 1 230 ? -48.763 2.516   19.062  1.00 43.67  ?  386 ILE   B CG2 1 
ATOM   4372 C  CD1 . ILE   B 1 230 ? -46.826 0.323   20.055  1.00 37.50  ?  386 ILE   B CD1 1 
ATOM   4373 N  N   . LEU   B 1 231 ? -48.568 5.572   20.556  1.00 34.98  ?  387 LEU   B N   1 
ATOM   4374 C  CA  . LEU   B 1 231 ? -49.713 6.486   20.585  1.00 30.64  ?  387 LEU   B CA  1 
ATOM   4375 C  C   . LEU   B 1 231 ? -49.406 7.842   19.958  1.00 33.96  ?  387 LEU   B C   1 
ATOM   4376 O  O   . LEU   B 1 231 ? -50.278 8.446   19.316  1.00 32.14  ?  387 LEU   B O   1 
ATOM   4377 C  CB  . LEU   B 1 231 ? -50.171 6.688   22.030  1.00 28.33  ?  387 LEU   B CB  1 
ATOM   4378 C  CG  . LEU   B 1 231 ? -51.242 5.701   22.466  1.00 36.70  ?  387 LEU   B CG  1 
ATOM   4379 C  CD1 . LEU   B 1 231 ? -51.739 6.148   23.844  1.00 40.84  ?  387 LEU   B CD1 1 
ATOM   4380 C  CD2 . LEU   B 1 231 ? -52.376 5.673   21.448  1.00 41.28  ?  387 LEU   B CD2 1 
ATOM   4381 N  N   . ASN   B 1 232 ? -48.208 8.378   20.203  1.00 32.94  ?  388 ASN   B N   1 
ATOM   4382 C  CA  . ASN   B 1 232 ? -47.833 9.702   19.704  1.00 36.58  ?  388 ASN   B CA  1 
ATOM   4383 C  C   . ASN   B 1 232 ? -47.219 9.673   18.305  1.00 36.10  ?  388 ASN   B C   1 
ATOM   4384 O  O   . ASN   B 1 232 ? -46.860 10.732  17.774  1.00 33.15  ?  388 ASN   B O   1 
ATOM   4385 C  CB  . ASN   B 1 232 ? -46.816 10.345  20.636  1.00 31.13  ?  388 ASN   B CB  1 
ATOM   4386 C  CG  . ASN   B 1 232 ? -47.419 10.817  21.953  1.00 41.29  ?  388 ASN   B CG  1 
ATOM   4387 O  OD1 . ASN   B 1 232 ? -48.629 11.009  22.099  1.00 33.44  ?  388 ASN   B OD1 1 
ATOM   4388 N  ND2 . ASN   B 1 232 ? -46.545 10.987  22.942  1.00 44.23  ?  388 ASN   B ND2 1 
ATOM   4389 N  N   . ASN   B 1 233 ? -46.997 8.502   17.752  1.00 29.69  ?  389 ASN   B N   1 
ATOM   4390 C  CA  . ASN   B 1 233 ? -46.411 8.342   16.438  1.00 32.44  ?  389 ASN   B CA  1 
ATOM   4391 C  C   . ASN   B 1 233 ? -47.155 7.156   15.829  1.00 28.55  ?  389 ASN   B C   1 
ATOM   4392 O  O   . ASN   B 1 233 ? -46.660 6.037   15.738  1.00 26.91  ?  389 ASN   B O   1 
ATOM   4393 C  CB  . ASN   B 1 233 ? -44.900 8.135   16.515  1.00 31.60  ?  389 ASN   B CB  1 
ATOM   4394 C  CG  . ASN   B 1 233 ? -44.228 8.277   15.177  1.00 35.74  ?  389 ASN   B CG  1 
ATOM   4395 O  OD1 . ASN   B 1 233 ? -44.867 8.624   14.174  1.00 32.63  ?  389 ASN   B OD1 1 
ATOM   4396 N  ND2 . ASN   B 1 233 ? -42.926 8.038   15.149  1.00 31.56  ?  389 ASN   B ND2 1 
ATOM   4397 N  N   . HIS   B 1 234 ? -48.414 7.407   15.463  1.00 25.81  ?  390 HIS   B N   1 
ATOM   4398 C  CA  . HIS   B 1 234 ? -49.420 6.353   15.408  1.00 28.55  ?  390 HIS   B CA  1 
ATOM   4399 C  C   . HIS   B 1 234 ? -49.936 6.030   13.999  1.00 28.39  ?  390 HIS   B C   1 
ATOM   4400 O  O   . HIS   B 1 234 ? -50.743 5.103   13.856  1.00 27.63  ?  390 HIS   B O   1 
ATOM   4401 C  CB  . HIS   B 1 234 ? -50.621 6.748   16.285  1.00 27.18  ?  390 HIS   B CB  1 
ATOM   4402 C  CG  . HIS   B 1 234 ? -51.261 8.031   15.851  1.00 30.35  ?  390 HIS   B CG  1 
ATOM   4403 N  ND1 . HIS   B 1 234 ? -51.191 9.196   16.580  1.00 34.43  ?  390 HIS   B ND1 1 
ATOM   4404 C  CD2 . HIS   B 1 234 ? -51.922 8.343   14.704  1.00 26.75  ?  390 HIS   B CD2 1 
ATOM   4405 C  CE1 . HIS   B 1 234 ? -51.807 10.167  15.918  1.00 32.50  ?  390 HIS   B CE1 1 
ATOM   4406 N  NE2 . HIS   B 1 234 ? -52.270 9.667   14.789  1.00 32.33  ?  390 HIS   B NE2 1 
ATOM   4407 N  N   . GLY   B 1 235 ? -49.525 6.768   12.961  1.00 31.36  ?  391 GLY   B N   1 
ATOM   4408 C  CA  . GLY   B 1 235 ? -50.041 6.496   11.630  1.00 28.01  ?  391 GLY   B CA  1 
ATOM   4409 C  C   . GLY   B 1 235 ? -49.130 5.590   10.828  1.00 27.84  ?  391 GLY   B C   1 
ATOM   4410 O  O   . GLY   B 1 235 ? -47.961 5.423   11.132  1.00 22.59  ?  391 GLY   B O   1 
ATOM   4411 N  N   . LYS   B 1 236 ? -49.685 4.993   9.766   1.00 28.22  ?  392 LYS   B N   1 
ATOM   4412 C  CA  . LYS   B 1 236 ? -48.831 4.391   8.739   1.00 24.17  ?  392 LYS   B CA  1 
ATOM   4413 C  C   . LYS   B 1 236 ? -48.026 5.468   8.018   1.00 24.78  ?  392 LYS   B C   1 
ATOM   4414 O  O   . LYS   B 1 236 ? -46.847 5.274   7.692   1.00 23.34  ?  392 LYS   B O   1 
ATOM   4415 C  CB  . LYS   B 1 236 ? -49.682 3.597   7.733   1.00 25.88  ?  392 LYS   B CB  1 
ATOM   4416 C  CG  . LYS   B 1 236 ? -48.842 2.947   6.610   1.00 30.17  ?  392 LYS   B CG  1 
ATOM   4417 C  CD  . LYS   B 1 236 ? -49.676 2.041   5.679   1.00 35.94  ?  392 LYS   B CD  1 
ATOM   4418 C  CE  . LYS   B 1 236 ? -50.008 0.682   6.339   1.00 37.01  ?  392 LYS   B CE  1 
ATOM   4419 N  NZ  . LYS   B 1 236 ? -48.823 -0.023  6.946   1.00 33.16  ?  392 LYS   B NZ  1 
ATOM   4420 N  N   . SER   B 1 237 ? -48.665 6.589   7.724   1.00 26.35  ?  393 SER   B N   1 
ATOM   4421 C  CA  . SER   B 1 237 ? -47.965 7.761   7.211   1.00 28.82  ?  393 SER   B CA  1 
ATOM   4422 C  C   . SER   B 1 237 ? -47.192 8.434   8.333   1.00 29.10  ?  393 SER   B C   1 
ATOM   4423 O  O   . SER   B 1 237 ? -47.765 8.748   9.377   1.00 25.52  ?  393 SER   B O   1 
ATOM   4424 C  CB  . SER   B 1 237 ? -48.962 8.754   6.632   1.00 26.65  ?  393 SER   B CB  1 
ATOM   4425 O  OG  . SER   B 1 237 ? -48.355 10.004  6.349   1.00 27.98  ?  393 SER   B OG  1 
ATOM   4426 N  N   . LYS   B 1 238 ? -45.915 8.713   8.086   1.00 25.56  ?  394 LYS   B N   1 
ATOM   4427 C  CA  . LYS   B 1 238 ? -45.117 9.474   9.041   1.00 29.62  ?  394 LYS   B CA  1 
ATOM   4428 C  C   . LYS   B 1 238 ? -45.701 10.857  9.302   1.00 32.88  ?  394 LYS   B C   1 
ATOM   4429 O  O   . LYS   B 1 238 ? -45.504 11.405  10.388  1.00 27.62  ?  394 LYS   B O   1 
ATOM   4430 C  CB  . LYS   B 1 238 ? -43.677 9.599   8.546   1.00 29.67  ?  394 LYS   B CB  1 
ATOM   4431 C  CG  . LYS   B 1 238 ? -42.948 8.279   8.524   1.00 26.09  ?  394 LYS   B CG  1 
ATOM   4432 C  CD  . LYS   B 1 238 ? -41.614 8.367   7.818   1.00 23.73  ?  394 LYS   B CD  1 
ATOM   4433 C  CE  . LYS   B 1 238 ? -41.015 6.986   7.673   1.00 22.40  ?  394 LYS   B CE  1 
ATOM   4434 N  NZ  . LYS   B 1 238 ? -39.794 7.020   6.836   1.00 25.56  ?  394 LYS   B NZ  1 
ATOM   4435 N  N   . THR   B 1 239 ? -46.435 11.437  8.340   1.00 30.96  ?  395 THR   B N   1 
ATOM   4436 C  CA  . THR   B 1 239 ? -47.069 12.740  8.537   1.00 31.67  ?  395 THR   B CA  1 
ATOM   4437 C  C   . THR   B 1 239 ? -48.535 12.633  8.962   1.00 29.37  ?  395 THR   B C   1 
ATOM   4438 O  O   . THR   B 1 239 ? -49.273 13.621  8.872   1.00 27.51  ?  395 THR   B O   1 
ATOM   4439 C  CB  . THR   B 1 239 ? -46.972 13.618  7.274   1.00 32.84  ?  395 THR   B CB  1 
ATOM   4440 O  OG1 . THR   B 1 239 ? -47.392 12.870  6.126   1.00 30.89  ?  395 THR   B OG1 1 
ATOM   4441 C  CG2 . THR   B 1 239 ? -45.553 14.162  7.065   1.00 30.51  ?  395 THR   B CG2 1 
ATOM   4442 N  N   . CYS   B 1 240 ? -48.973 11.479  9.456   1.00 28.04  ?  396 CYS   B N   1 
ATOM   4443 C  CA  . CYS   B 1 240 ? -50.373 11.405  9.860   1.00 30.28  ?  396 CYS   B CA  1 
ATOM   4444 C  C   . CYS   B 1 240 ? -50.597 12.419  10.989  1.00 30.30  ?  396 CYS   B C   1 
ATOM   4445 O  O   . CYS   B 1 240 ? -49.717 12.645  11.826  1.00 29.26  ?  396 CYS   B O   1 
ATOM   4446 C  CB  . CYS   B 1 240 ? -50.740 9.957   10.256  1.00 32.49  ?  396 CYS   B CB  1 
ATOM   4447 S  SG  . CYS   B 1 240 ? -52.257 9.681   11.190  1.00 29.77  ?  396 CYS   B SG  1 
ATOM   4448 N  N   . CYS   B 1 241 ? -51.730 13.121  10.922  1.00 27.24  ?  397 CYS   B N   1 
ATOM   4449 C  CA  . CYS   B 1 241 ? -52.168 14.191  11.815  1.00 25.82  ?  397 CYS   B CA  1 
ATOM   4450 C  C   . CYS   B 1 241 ? -51.284 15.437  11.774  1.00 28.16  ?  397 CYS   B C   1 
ATOM   4451 O  O   . CYS   B 1 241 ? -51.498 16.345  12.576  1.00 26.39  ?  397 CYS   B O   1 
ATOM   4452 C  CB  . CYS   B 1 241 ? -52.281 13.701  13.265  1.00 36.27  ?  397 CYS   B CB  1 
ATOM   4453 S  SG  . CYS   B 1 241 ? -53.756 12.700  13.568  1.00 27.55  ?  397 CYS   B SG  1 
ATOM   4454 N  N   . GLU   B 1 242 ? -50.321 15.535  10.850  1.00 25.76  ?  398 GLU   B N   1 
ATOM   4455 C  CA  . GLU   B 1 242 ? -49.504 16.743  10.753  1.00 28.07  ?  398 GLU   B CA  1 
ATOM   4456 C  C   . GLU   B 1 242 ? -50.052 17.761  9.756   1.00 32.44  ?  398 GLU   B C   1 
ATOM   4457 O  O   . GLU   B 1 242 ? -49.447 18.825  9.588   1.00 30.97  ?  398 GLU   B O   1 
ATOM   4458 C  CB  . GLU   B 1 242 ? -48.037 16.394  10.406  1.00 28.84  ?  398 GLU   B CB  1 
ATOM   4459 C  CG  . GLU   B 1 242 ? -47.242 15.715  11.575  1.00 30.56  ?  398 GLU   B CG  1 
ATOM   4460 C  CD  . GLU   B 1 242 ? -45.723 15.711  11.326  1.00 36.84  ?  398 GLU   B CD  1 
ATOM   4461 O  OE1 . GLU   B 1 242 ? -45.326 16.113  10.200  1.00 31.39  ?  398 GLU   B OE1 1 
ATOM   4462 O  OE2 . GLU   B 1 242 ? -44.924 15.364  12.258  1.00 29.76  -1 398 GLU   B OE2 1 
ATOM   4463 N  N   . ASN   B 1 243 ? -51.194 17.486  9.128   1.00 35.34  ?  399 ASN   B N   1 
ATOM   4464 C  CA  . ASN   B 1 243 ? -51.792 18.406  8.167   1.00 36.30  ?  399 ASN   B CA  1 
ATOM   4465 C  C   . ASN   B 1 243 ? -53.281 18.085  8.065   1.00 39.20  ?  399 ASN   B C   1 
ATOM   4466 O  O   . ASN   B 1 243 ? -53.712 16.994  8.442   1.00 34.17  ?  399 ASN   B O   1 
ATOM   4467 C  CB  . ASN   B 1 243 ? -51.085 18.301  6.805   1.00 31.10  ?  399 ASN   B CB  1 
ATOM   4468 C  CG  . ASN   B 1 243 ? -51.153 16.909  6.222   1.00 32.41  ?  399 ASN   B CG  1 
ATOM   4469 O  OD1 . ASN   B 1 243 ? -52.234 16.388  5.973   1.00 34.65  ?  399 ASN   B OD1 1 
ATOM   4470 N  ND2 . ASN   B 1 243 ? -49.986 16.266  6.061   1.00 29.81  ?  399 ASN   B ND2 1 
ATOM   4471 N  N   . LYS   B 1 244 ? -54.069 19.046  7.552   1.00 39.13  ?  400 LYS   B N   1 
ATOM   4472 C  CA  . LYS   B 1 244 ? -55.514 18.818  7.443   1.00 40.95  ?  400 LYS   B CA  1 
ATOM   4473 C  C   . LYS   B 1 244 ? -55.853 17.567  6.639   1.00 31.33  ?  400 LYS   B C   1 
ATOM   4474 O  O   . LYS   B 1 244 ? -56.815 16.865  6.966   1.00 37.44  ?  400 LYS   B O   1 
ATOM   4475 C  CB  . LYS   B 1 244 ? -56.248 20.010  6.822   1.00 41.84  ?  400 LYS   B CB  1 
ATOM   4476 C  CG  . LYS   B 1 244 ? -56.446 21.235  7.669   1.00 38.87  ?  400 LYS   B CG  1 
ATOM   4477 C  CD  . LYS   B 1 244 ? -57.181 22.262  6.792   1.00 42.84  ?  400 LYS   B CD  1 
ATOM   4478 C  CE  . LYS   B 1 244 ? -58.629 21.781  6.512   1.00 41.86  ?  400 LYS   B CE  1 
ATOM   4479 N  NZ  . LYS   B 1 244 ? -59.512 22.714  5.686   1.00 40.28  ?  400 LYS   B NZ  1 
ATOM   4480 N  N   . GLU   B 1 245 ? -55.102 17.269  5.573   1.00 39.29  ?  401 GLU   B N   1 
ATOM   4481 C  CA  . GLU   B 1 245 ? -55.477 16.115  4.755   1.00 32.00  ?  401 GLU   B CA  1 
ATOM   4482 C  C   . GLU   B 1 245 ? -55.314 14.792  5.510   1.00 37.34  ?  401 GLU   B C   1 
ATOM   4483 O  O   . GLU   B 1 245 ? -55.944 13.797  5.140   1.00 35.05  ?  401 GLU   B O   1 
ATOM   4484 C  CB  . GLU   B 1 245 ? -54.668 16.094  3.448   1.00 34.99  ?  401 GLU   B CB  1 
ATOM   4485 N  N   . GLU   B 1 246 ? -54.503 14.756  6.576   1.00 36.30  ?  402 GLU   B N   1 
ATOM   4486 C  CA  . GLU   B 1 246 ? -54.165 13.493  7.221   1.00 33.42  ?  402 GLU   B CA  1 
ATOM   4487 C  C   . GLU   B 1 246 ? -54.610 13.450  8.677   1.00 34.21  ?  402 GLU   B C   1 
ATOM   4488 O  O   . GLU   B 1 246 ? -54.042 12.694  9.472   1.00 33.42  ?  402 GLU   B O   1 
ATOM   4489 C  CB  . GLU   B 1 246 ? -52.664 13.220  7.114   1.00 33.41  ?  402 GLU   B CB  1 
ATOM   4490 C  CG  . GLU   B 1 246 ? -52.149 13.159  5.681   1.00 35.21  ?  402 GLU   B CG  1 
ATOM   4491 C  CD  . GLU   B 1 246 ? -50.689 12.753  5.611   1.00 32.57  ?  402 GLU   B CD  1 
ATOM   4492 O  OE1 . GLU   B 1 246 ? -50.401 11.565  5.891   1.00 32.33  ?  402 GLU   B OE1 1 
ATOM   4493 O  OE2 . GLU   B 1 246 ? -49.834 13.603  5.274   1.00 31.13  -1 402 GLU   B OE2 1 
ATOM   4494 N  N   . LYS   B 1 247 ? -55.597 14.260  9.063   1.00 33.35  ?  403 LYS   B N   1 
ATOM   4495 C  CA  . LYS   B 1 247 ? -56.089 14.182  10.441  1.00 34.06  ?  403 LYS   B CA  1 
ATOM   4496 C  C   . LYS   B 1 247 ? -56.844 12.870  10.637  1.00 33.55  ?  403 LYS   B C   1 
ATOM   4497 O  O   . LYS   B 1 247 ? -57.803 12.596  9.897   1.00 31.06  ?  403 LYS   B O   1 
ATOM   4498 C  CB  . LYS   B 1 247 ? -56.997 15.364  10.788  1.00 33.58  ?  403 LYS   B CB  1 
ATOM   4499 C  CG  . LYS   B 1 247 ? -56.316 16.715  10.757  1.00 39.24  ?  403 LYS   B CG  1 
ATOM   4500 C  CD  . LYS   B 1 247 ? -55.200 16.797  11.836  1.00 43.78  ?  403 LYS   B CD  1 
ATOM   4501 C  CE  . LYS   B 1 247 ? -54.589 18.189  11.869  1.00 46.02  ?  403 LYS   B CE  1 
ATOM   4502 N  NZ  . LYS   B 1 247 ? -53.844 18.437  13.140  1.00 46.43  ?  403 LYS   B NZ  1 
ATOM   4503 N  N   . CYS   B 1 248 ? -56.422 12.066  11.630  1.00 33.81  ?  404 CYS   B N   1 
ATOM   4504 C  CA  . CYS   B 1 248 ? -57.127 10.828  11.971  1.00 31.76  ?  404 CYS   B CA  1 
ATOM   4505 C  C   . CYS   B 1 248 ? -57.749 10.966  13.358  1.00 29.44  ?  404 CYS   B C   1 
ATOM   4506 O  O   . CYS   B 1 248 ? -57.578 12.007  14.001  1.00 27.60  ?  404 CYS   B O   1 
ATOM   4507 C  CB  . CYS   B 1 248 ? -56.178 9.630   11.891  1.00 28.49  ?  404 CYS   B CB  1 
ATOM   4508 S  SG  . CYS   B 1 248 ? -55.140 9.339   13.394  1.00 27.13  ?  404 CYS   B SG  1 
ATOM   4509 N  N   . CYS   B 1 249 ? -58.485 9.940   13.831  1.00 28.25  ?  405 CYS   B N   1 
ATOM   4510 C  CA  . CYS   B 1 249 ? -59.182 10.084  15.110  1.00 27.17  ?  405 CYS   B CA  1 
ATOM   4511 C  C   . CYS   B 1 249 ? -58.735 8.993   16.076  1.00 24.45  ?  405 CYS   B C   1 
ATOM   4512 O  O   . CYS   B 1 249 ? -59.504 8.588   16.947  1.00 25.26  ?  405 CYS   B O   1 
ATOM   4513 C  CB  . CYS   B 1 249 ? -60.701 9.957   14.992  1.00 30.27  ?  405 CYS   B CB  1 
ATOM   4514 S  SG  . CYS   B 1 249 ? -61.334 8.521   14.075  1.00 34.51  ?  405 CYS   B SG  1 
ATOM   4515 N  N   . ARG   B 1 250 ? -57.565 8.408   15.815  1.00 27.84  ?  406 ARG   B N   1 
ATOM   4516 C  CA  . ARG   B 1 250 ? -57.108 7.305   16.645  1.00 26.65  ?  406 ARG   B CA  1 
ATOM   4517 C  C   . ARG   B 1 250 ? -56.958 7.738   18.102  1.00 26.37  ?  406 ARG   B C   1 
ATOM   4518 O  O   . ARG   B 1 250 ? -57.387 7.032   19.022  1.00 25.81  ?  406 ARG   B O   1 
ATOM   4519 C  CB  . ARG   B 1 250 ? -55.776 6.826   16.114  1.00 29.77  ?  406 ARG   B CB  1 
ATOM   4520 C  CG  . ARG   B 1 250 ? -55.821 6.011   14.858  1.00 26.68  ?  406 ARG   B CG  1 
ATOM   4521 C  CD  . ARG   B 1 250 ? -54.427 5.442   14.676  1.00 27.64  ?  406 ARG   B CD  1 
ATOM   4522 N  NE  . ARG   B 1 250 ? -54.258 4.612   13.495  1.00 26.48  ?  406 ARG   B NE  1 
ATOM   4523 C  CZ  . ARG   B 1 250 ? -53.845 5.053   12.309  1.00 25.91  ?  406 ARG   B CZ  1 
ATOM   4524 N  NH1 . ARG   B 1 250 ? -53.742 6.350   12.035  1.00 26.93  ?  406 ARG   B NH1 1 
ATOM   4525 N  NH2 . ARG   B 1 250 ? -53.515 4.171   11.381  1.00 26.01  ?  406 ARG   B NH2 1 
ATOM   4526 N  N   . LYS   B 1 251 ? -56.313 8.882   18.328  1.00 26.61  ?  407 LYS   B N   1 
ATOM   4527 C  CA  . LYS   B 1 251 ? -56.085 9.323   19.707  1.00 30.22  ?  407 LYS   B CA  1 
ATOM   4528 C  C   . LYS   B 1 251 ? -57.383 9.736   20.380  1.00 31.02  ?  407 LYS   B C   1 
ATOM   4529 O  O   . LYS   B 1 251 ? -57.595 9.444   21.558  1.00 27.46  ?  407 LYS   B O   1 
ATOM   4530 C  CB  . LYS   B 1 251 ? -55.079 10.473  19.758  1.00 38.89  ?  407 LYS   B CB  1 
ATOM   4531 C  CG  . LYS   B 1 251 ? -53.630 10.016  19.785  1.00 39.86  ?  407 LYS   B CG  1 
ATOM   4532 C  CD  . LYS   B 1 251 ? -52.721 11.050  19.126  1.00 47.28  ?  407 LYS   B CD  1 
ATOM   4533 C  CE  . LYS   B 1 251 ? -51.571 11.443  20.042  1.00 45.95  ?  407 LYS   B CE  1 
ATOM   4534 N  NZ  . LYS   B 1 251 ? -52.007 12.389  21.091  1.00 60.38  ?  407 LYS   B NZ  1 
ATOM   4535 N  N   . ASP   B 1 252 ? -58.278 10.404  19.644  1.00 30.50  ?  408 ASP   B N   1 
ATOM   4536 C  CA  . ASP   B 1 252 ? -59.581 10.718  20.224  1.00 26.76  ?  408 ASP   B CA  1 
ATOM   4537 C  C   . ASP   B 1 252 ? -60.405 9.476   20.545  1.00 26.73  ?  408 ASP   B C   1 
ATOM   4538 O  O   . ASP   B 1 252 ? -61.186 9.504   21.500  1.00 27.08  ?  408 ASP   B O   1 
ATOM   4539 C  CB  . ASP   B 1 252 ? -60.363 11.649  19.304  1.00 28.12  ?  408 ASP   B CB  1 
ATOM   4540 C  CG  . ASP   B 1 252 ? -59.806 13.077  19.291  1.00 37.91  ?  408 ASP   B CG  1 
ATOM   4541 O  OD1 . ASP   B 1 252 ? -58.965 13.430  20.172  1.00 36.60  ?  408 ASP   B OD1 1 
ATOM   4542 O  OD2 . ASP   B 1 252 ? -60.208 13.845  18.396  1.00 38.05  -1 408 ASP   B OD2 1 
ATOM   4543 N  N   . CYS   B 1 253 ? -60.304 8.404   19.744  1.00 24.96  ?  409 CYS   B N   1 
ATOM   4544 C  CA  . CYS   B 1 253 ? -61.016 7.182   20.110  1.00 27.85  ?  409 CYS   B CA  1 
ATOM   4545 C  C   . CYS   B 1 253 ? -60.502 6.601   21.429  1.00 24.81  ?  409 CYS   B C   1 
ATOM   4546 O  O   . CYS   B 1 253 ? -61.294 6.143   22.259  1.00 25.39  ?  409 CYS   B O   1 
ATOM   4547 C  CB  . CYS   B 1 253 ? -60.926 6.128   19.008  1.00 25.65  ?  409 CYS   B CB  1 
ATOM   4548 S  SG  . CYS   B 1 253 ? -61.960 6.466   17.520  1.00 30.32  ?  409 CYS   B SG  1 
ATOM   4549 N  N   . LEU   B 1 254 ? -59.184 6.539   21.612  1.00 27.16  ?  410 LEU   B N   1 
ATOM   4550 C  CA  . LEU   B 1 254 ? -58.678 6.074   22.918  1.00 26.13  ?  410 LEU   B CA  1 
ATOM   4551 C  C   . LEU   B 1 254 ? -59.160 6.966   24.052  1.00 26.25  ?  410 LEU   B C   1 
ATOM   4552 O  O   . LEU   B 1 254 ? -59.626 6.465   25.085  1.00 28.61  ?  410 LEU   B O   1 
ATOM   4553 C  CB  . LEU   B 1 254 ? -57.160 5.979   22.915  1.00 25.67  ?  410 LEU   B CB  1 
ATOM   4554 C  CG  . LEU   B 1 254 ? -56.474 5.563   24.225  1.00 32.23  ?  410 LEU   B CG  1 
ATOM   4555 C  CD1 . LEU   B 1 254 ? -57.021 4.258   24.714  1.00 26.82  ?  410 LEU   B CD1 1 
ATOM   4556 C  CD2 . LEU   B 1 254 ? -55.069 5.303   23.836  1.00 33.05  ?  410 LEU   B CD2 1 
ATOM   4557 N  N   . LYS   B 1 255 ? -59.098 8.287   23.877  1.00 26.58  ?  411 LYS   B N   1 
ATOM   4558 C  CA  . LYS   B 1 255 ? -59.559 9.174   24.950  1.00 26.96  ?  411 LYS   B CA  1 
ATOM   4559 C  C   . LYS   B 1 255 ? -60.999 8.873   25.325  1.00 28.32  ?  411 LYS   B C   1 
ATOM   4560 O  O   . LYS   B 1 255 ? -61.350 8.851   26.507  1.00 27.62  ?  411 LYS   B O   1 
ATOM   4561 C  CB  . LYS   B 1 255 ? -59.425 10.635  24.537  1.00 28.41  ?  411 LYS   B CB  1 
ATOM   4562 C  CG  . LYS   B 1 255 ? -57.998 11.138  24.507  1.00 35.41  ?  411 LYS   B CG  1 
ATOM   4563 C  CD  . LYS   B 1 255 ? -57.949 12.608  24.098  1.00 49.92  ?  411 LYS   B CD  1 
ATOM   4564 C  CE  . LYS   B 1 255 ? -56.537 13.024  23.682  1.00 46.80  ?  411 LYS   B CE  1 
ATOM   4565 N  NZ  . LYS   B 1 255 ? -56.558 13.910  22.488  1.00 52.80  ?  411 LYS   B NZ  1 
ATOM   4566 N  N   . LEU   B 1 256 ? -61.855 8.629   24.317  1.00 26.25  ?  412 LEU   B N   1 
ATOM   4567 C  CA  . LEU   B 1 256 ? -63.272 8.408   24.592  1.00 26.85  ?  412 LEU   B CA  1 
ATOM   4568 C  C   . LEU   B 1 256 ? -63.508 7.057   25.247  1.00 26.21  ?  412 LEU   B C   1 
ATOM   4569 O  O   . LEU   B 1 256 ? -64.388 6.934   26.102  1.00 28.95  ?  412 LEU   B O   1 
ATOM   4570 C  CB  . LEU   B 1 256 ? -64.095 8.535   23.292  1.00 26.98  ?  412 LEU   B CB  1 
ATOM   4571 C  CG  . LEU   B 1 256 ? -64.263 9.929   22.658  1.00 28.94  ?  412 LEU   B CG  1 
ATOM   4572 C  CD1 . LEU   B 1 256 ? -64.829 9.812   21.224  1.00 28.23  ?  412 LEU   B CD1 1 
ATOM   4573 C  CD2 . LEU   B 1 256 ? -65.159 10.810  23.501  1.00 28.45  ?  412 LEU   B CD2 1 
ATOM   4574 N  N   . MET   B 1 257 ? -62.774 6.020   24.834  1.00 27.78  ?  413 MET   B N   1 
ATOM   4575 C  CA  . MET   B 1 257 ? -62.831 4.746   25.559  1.00 28.08  ?  413 MET   B CA  1 
ATOM   4576 C  C   . MET   B 1 257 ? -62.341 4.876   27.006  1.00 30.22  ?  413 MET   B C   1 
ATOM   4577 O  O   . MET   B 1 257 ? -62.934 4.287   27.920  1.00 28.60  ?  413 MET   B O   1 
ATOM   4578 C  CB  . MET   B 1 257 ? -62.038 3.646   24.855  1.00 27.19  ?  413 MET   B CB  1 
ATOM   4579 C  CG  . MET   B 1 257 ? -62.476 3.247   23.478  1.00 27.16  ?  413 MET   B CG  1 
ATOM   4580 S  SD  . MET   B 1 257 ? -61.181 2.189   22.753  1.00 38.44  ?  413 MET   B SD  1 
ATOM   4581 C  CE  . MET   B 1 257 ? -61.721 0.597   23.416  1.00 28.03  ?  413 MET   B CE  1 
ATOM   4582 N  N   . LYS   B 1 258 ? -61.232 5.592   27.229  1.00 30.74  ?  414 LYS   B N   1 
ATOM   4583 C  CA  . LYS   B 1 258 ? -60.779 5.802   28.606  1.00 35.49  ?  414 LYS   B CA  1 
ATOM   4584 C  C   . LYS   B 1 258 ? -61.826 6.576   29.398  1.00 33.54  ?  414 LYS   B C   1 
ATOM   4585 O  O   . LYS   B 1 258 ? -62.112 6.248   30.554  1.00 34.26  ?  414 LYS   B O   1 
ATOM   4586 C  CB  . LYS   B 1 258 ? -59.428 6.533   28.626  1.00 29.89  ?  414 LYS   B CB  1 
ATOM   4587 C  CG  . LYS   B 1 258 ? -58.223 5.661   28.284  1.00 30.90  ?  414 LYS   B CG  1 
ATOM   4588 C  CD  . LYS   B 1 258 ? -56.924 6.481   28.275  1.00 36.56  ?  414 LYS   B CD  1 
ATOM   4589 C  CE  . LYS   B 1 258 ? -56.656 7.114   29.643  1.00 45.36  ?  414 LYS   B CE  1 
ATOM   4590 N  NZ  . LYS   B 1 258 ? -55.477 8.040   29.654  1.00 50.98  ?  414 LYS   B NZ  1 
ATOM   4591 N  N   . TYR   B 1 259 ? -62.448 7.582   28.766  1.00 35.26  ?  415 TYR   B N   1 
ATOM   4592 C  CA  . TYR   B 1 259 ? -63.409 8.400   29.499  1.00 31.04  ?  415 TYR   B CA  1 
ATOM   4593 C  C   . TYR   B 1 259 ? -64.688 7.611   29.783  1.00 34.63  ?  415 TYR   B C   1 
ATOM   4594 O  O   . TYR   B 1 259 ? -65.302 7.760   30.850  1.00 31.00  ?  415 TYR   B O   1 
ATOM   4595 C  CB  . TYR   B 1 259 ? -63.692 9.690   28.720  1.00 31.73  ?  415 TYR   B CB  1 
ATOM   4596 C  CG  . TYR   B 1 259 ? -64.608 10.650  29.453  1.00 41.95  ?  415 TYR   B CG  1 
ATOM   4597 C  CD1 . TYR   B 1 259 ? -64.188 11.265  30.635  1.00 47.35  ?  415 TYR   B CD1 1 
ATOM   4598 C  CD2 . TYR   B 1 259 ? -65.868 10.968  28.967  1.00 35.71  ?  415 TYR   B CD2 1 
ATOM   4599 C  CE1 . TYR   B 1 259 ? -65.018 12.149  31.323  1.00 50.01  ?  415 TYR   B CE1 1 
ATOM   4600 C  CE2 . TYR   B 1 259 ? -66.698 11.854  29.641  1.00 42.92  ?  415 TYR   B CE2 1 
ATOM   4601 C  CZ  . TYR   B 1 259 ? -66.269 12.447  30.809  1.00 50.04  ?  415 TYR   B CZ  1 
ATOM   4602 O  OH  . TYR   B 1 259 ? -67.094 13.326  31.488  1.00 58.22  ?  415 TYR   B OH  1 
ATOM   4603 N  N   . LEU   B 1 260 ? -65.093 6.742   28.846  1.00 33.85  ?  416 LEU   B N   1 
ATOM   4604 C  CA  . LEU   B 1 260 ? -66.258 5.892   29.086  1.00 33.83  ?  416 LEU   B CA  1 
ATOM   4605 C  C   . LEU   B 1 260 ? -66.037 4.965   30.286  1.00 31.66  ?  416 LEU   B C   1 
ATOM   4606 O  O   . LEU   B 1 260 ? -66.912 4.823   31.149  1.00 31.04  ?  416 LEU   B O   1 
ATOM   4607 C  CB  . LEU   B 1 260 ? -66.584 5.097   27.817  1.00 30.73  ?  416 LEU   B CB  1 
ATOM   4608 C  CG  . LEU   B 1 260 ? -67.738 4.118   28.042  1.00 31.28  ?  416 LEU   B CG  1 
ATOM   4609 C  CD1 . LEU   B 1 260 ? -69.019 4.830   28.471  1.00 34.72  ?  416 LEU   B CD1 1 
ATOM   4610 C  CD2 . LEU   B 1 260 ? -67.984 3.270   26.789  1.00 35.31  ?  416 LEU   B CD2 1 
ATOM   4611 N  N   . LEU   B 1 261 ? -64.875 4.305   30.346  1.00 33.21  ?  417 LEU   B N   1 
ATOM   4612 C  CA  . LEU   B 1 261 ? -64.607 3.401   31.464  1.00 31.96  ?  417 LEU   B CA  1 
ATOM   4613 C  C   . LEU   B 1 261 ? -64.514 4.159   32.779  1.00 35.04  ?  417 LEU   B C   1 
ATOM   4614 O  O   . LEU   B 1 261 ? -64.953 3.662   33.826  1.00 35.45  ?  417 LEU   B O   1 
ATOM   4615 C  CB  . LEU   B 1 261 ? -63.316 2.619   31.238  1.00 31.27  ?  417 LEU   B CB  1 
ATOM   4616 C  CG  . LEU   B 1 261 ? -63.026 1.650   32.397  1.00 39.57  ?  417 LEU   B CG  1 
ATOM   4617 C  CD1 . LEU   B 1 261 ? -64.116 0.602   32.500  1.00 35.02  ?  417 LEU   B CD1 1 
ATOM   4618 C  CD2 . LEU   B 1 261 ? -61.662 0.999   32.248  1.00 37.89  ?  417 LEU   B CD2 1 
ATOM   4619 N  N   . GLU   B 1 262 ? -63.946 5.359   32.734  1.00 34.92  ?  418 GLU   B N   1 
ATOM   4620 C  CA  . GLU   B 1 262 ? -63.707 6.105   33.954  1.00 37.30  ?  418 GLU   B CA  1 
ATOM   4621 C  C   . GLU   B 1 262 ? -65.036 6.586   34.520  1.00 39.45  ?  418 GLU   B C   1 
ATOM   4622 O  O   . GLU   B 1 262 ? -65.308 6.410   35.713  1.00 37.45  ?  418 GLU   B O   1 
ATOM   4623 C  CB  . GLU   B 1 262 ? -62.762 7.265   33.655  1.00 37.10  ?  418 GLU   B CB  1 
ATOM   4624 C  CG  . GLU   B 1 262 ? -61.302 6.805   33.618  1.00 39.03  ?  418 GLU   B CG  1 
ATOM   4625 C  CD  . GLU   B 1 262 ? -60.402 7.796   32.886  1.00 43.74  ?  418 GLU   B CD  1 
ATOM   4626 O  OE1 . GLU   B 1 262 ? -59.381 7.397   32.274  1.00 38.93  ?  418 GLU   B OE1 1 
ATOM   4627 O  OE2 . GLU   B 1 262 ? -60.647 9.014   33.079  1.00 47.45  -1 418 GLU   B OE2 1 
ATOM   4628 N  N   . GLN   B 1 263 ? -65.914 7.106   33.646  1.00 40.31  ?  419 GLN   B N   1 
ATOM   4629 C  CA  . GLN   B 1 263 ? -67.258 7.498   34.068  1.00 38.36  ?  419 GLN   B CA  1 
ATOM   4630 C  C   . GLN   B 1 263 ? -68.037 6.321   34.639  1.00 39.63  ?  419 GLN   B C   1 
ATOM   4631 O  O   . GLN   B 1 263 ? -68.740 6.465   35.645  1.00 42.77  ?  419 GLN   B O   1 
ATOM   4632 C  CB  . GLN   B 1 263 ? -68.025 8.125   32.905  1.00 41.64  ?  419 GLN   B CB  1 
ATOM   4633 C  CG  . GLN   B 1 263 ? -67.524 9.487   32.509  1.00 40.09  ?  419 GLN   B CG  1 
ATOM   4634 C  CD  . GLN   B 1 263 ? -67.855 10.519  33.571  1.00 50.73  ?  419 GLN   B CD  1 
ATOM   4635 O  OE1 . GLN   B 1 263 ? -67.040 10.811  34.439  1.00 43.58  ?  419 GLN   B OE1 1 
ATOM   4636 N  NE2 . GLN   B 1 263 ? -69.072 11.053  33.521  1.00 51.95  ?  419 GLN   B NE2 1 
ATOM   4637 N  N   . LEU   B 1 264 ? -67.921 5.142   34.025  1.00 41.40  ?  420 LEU   B N   1 
ATOM   4638 C  CA  . LEU   B 1 264 ? -68.659 3.991   34.544  1.00 42.49  ?  420 LEU   B CA  1 
ATOM   4639 C  C   . LEU   B 1 264 ? -68.094 3.521   35.877  1.00 41.61  ?  420 LEU   B C   1 
ATOM   4640 O  O   . LEU   B 1 264 ? -68.852 3.198   36.804  1.00 37.01  ?  420 LEU   B O   1 
ATOM   4641 C  CB  . LEU   B 1 264 ? -68.644 2.849   33.532  1.00 34.94  ?  420 LEU   B CB  1 
ATOM   4642 C  CG  . LEU   B 1 264 ? -69.426 3.103   32.254  1.00 35.50  ?  420 LEU   B CG  1 
ATOM   4643 C  CD1 . LEU   B 1 264 ? -69.268 1.929   31.281  1.00 40.15  ?  420 LEU   B CD1 1 
ATOM   4644 C  CD2 . LEU   B 1 264 ? -70.876 3.363   32.578  1.00 40.58  ?  420 LEU   B CD2 1 
ATOM   4645 N  N   . LYS   B 1 265 ? -66.768 3.432   35.973  1.00 39.58  ?  421 LYS   B N   1 
ATOM   4646 C  CA  . LYS   B 1 265 ? -66.157 3.046   37.234  1.00 36.59  ?  421 LYS   B CA  1 
ATOM   4647 C  C   . LYS   B 1 265 ? -66.544 4.001   38.353  1.00 43.70  ?  421 LYS   B C   1 
ATOM   4648 O  O   . LYS   B 1 265 ? -66.758 3.561   39.488  1.00 46.64  ?  421 LYS   B O   1 
ATOM   4649 C  CB  . LYS   B 1 265 ? -64.640 2.968   37.101  1.00 35.99  ?  421 LYS   B CB  1 
ATOM   4650 C  CG  . LYS   B 1 265 ? -64.173 1.735   36.376  1.00 37.32  ?  421 LYS   B CG  1 
ATOM   4651 C  CD  . LYS   B 1 265 ? -62.691 1.562   36.445  1.00 41.83  ?  421 LYS   B CD  1 
ATOM   4652 C  CE  . LYS   B 1 265 ? -62.311 1.201   37.883  1.00 40.03  ?  421 LYS   B CE  1 
ATOM   4653 N  NZ  . LYS   B 1 265 ? -60.917 0.764   37.992  1.00 49.42  ?  421 LYS   B NZ  1 
ATOM   4654 N  N   . GLU   B 1 266 ? -66.647 5.297   38.048  1.00 40.16  ?  422 GLU   B N   1 
ATOM   4655 C  CA  . GLU   B 1 266 ? -67.102 6.284   39.024  1.00 47.83  ?  422 GLU   B CA  1 
ATOM   4656 C  C   . GLU   B 1 266 ? -68.561 6.082   39.411  1.00 48.54  ?  422 GLU   B C   1 
ATOM   4657 O  O   . GLU   B 1 266 ? -68.922 6.266   40.578  1.00 52.01  ?  422 GLU   B O   1 
ATOM   4658 C  CB  . GLU   B 1 266 ? -66.884 7.693   38.476  1.00 52.16  ?  422 GLU   B CB  1 
ATOM   4659 C  CG  . GLU   B 1 266 ? -65.471 8.219   38.612  1.00 50.11  ?  422 GLU   B CG  1 
ATOM   4660 C  CD  . GLU   B 1 266 ? -65.052 8.415   40.076  1.00 53.21  ?  422 GLU   B CD  1 
ATOM   4661 O  OE1 . GLU   B 1 266 ? -65.903 8.279   40.986  1.00 52.47  ?  422 GLU   B OE1 1 
ATOM   4662 O  OE2 . GLU   B 1 266 ? -63.864 8.715   40.316  1.00 66.35  -1 422 GLU   B OE2 1 
ATOM   4663 N  N   . ARG   B 1 267 ? -69.420 5.726   38.458  1.00 51.63  ?  423 ARG   B N   1 
ATOM   4664 C  CA  . ARG   B 1 267 ? -70.831 5.567   38.794  1.00 52.25  ?  423 ARG   B CA  1 
ATOM   4665 C  C   . ARG   B 1 267 ? -71.016 4.392   39.752  1.00 57.04  ?  423 ARG   B C   1 
ATOM   4666 O  O   . ARG   B 1 267 ? -71.768 4.489   40.731  1.00 50.30  ?  423 ARG   B O   1 
ATOM   4667 C  CB  . ARG   B 1 267 ? -71.653 5.405   37.507  1.00 55.92  ?  423 ARG   B CB  1 
ATOM   4668 C  CG  . ARG   B 1 267 ? -73.026 4.749   37.653  1.00 59.33  ?  423 ARG   B CG  1 
ATOM   4669 C  CD  . ARG   B 1 267 ? -74.140 5.770   37.938  1.00 58.88  ?  423 ARG   B CD  1 
ATOM   4670 N  NE  . ARG   B 1 267 ? -74.249 6.835   36.945  1.00 55.46  ?  423 ARG   B NE  1 
ATOM   4671 C  CZ  . ARG   B 1 267 ? -74.704 6.667   35.711  1.00 60.74  ?  423 ARG   B CZ  1 
ATOM   4672 N  NH1 . ARG   B 1 267 ? -75.126 5.486   35.283  1.00 67.43  ?  423 ARG   B NH1 1 
ATOM   4673 N  NH2 . ARG   B 1 267 ? -74.744 7.711   34.886  1.00 68.48  ?  423 ARG   B NH2 1 
ATOM   4674 N  N   . PHE   B 1 268 ? -70.274 3.301   39.538  1.00 50.65  ?  424 PHE   B N   1 
ATOM   4675 C  CA  . PHE   B 1 268 ? -70.469 2.078   40.310  1.00 52.50  ?  424 PHE   B CA  1 
ATOM   4676 C  C   . PHE   B 1 268 ? -69.287 1.769   41.234  1.00 49.96  ?  424 PHE   B C   1 
ATOM   4677 O  O   . PHE   B 1 268 ? -69.051 0.608   41.576  1.00 55.18  ?  424 PHE   B O   1 
ATOM   4678 C  CB  . PHE   B 1 268 ? -70.732 0.896   39.371  1.00 51.51  ?  424 PHE   B CB  1 
ATOM   4679 C  CG  . PHE   B 1 268 ? -71.973 1.056   38.517  1.00 55.89  ?  424 PHE   B CG  1 
ATOM   4680 C  CD1 . PHE   B 1 268 ? -71.877 1.511   37.204  1.00 51.43  ?  424 PHE   B CD1 1 
ATOM   4681 C  CD2 . PHE   B 1 268 ? -73.234 0.806   39.043  1.00 43.79  ?  424 PHE   B CD2 1 
ATOM   4682 C  CE1 . PHE   B 1 268 ? -73.023 1.668   36.413  1.00 55.16  ?  424 PHE   B CE1 1 
ATOM   4683 C  CE2 . PHE   B 1 268 ? -74.379 0.974   38.270  1.00 50.36  ?  424 PHE   B CE2 1 
ATOM   4684 C  CZ  . PHE   B 1 268 ? -74.277 1.407   36.952  1.00 49.15  ?  424 PHE   B CZ  1 
ATOM   4685 N  N   . LYS   B 1 269 ? -68.542 2.796   41.654  1.00 55.37  ?  425 LYS   B N   1 
ATOM   4686 C  CA  . LYS   B 1 269 ? -67.348 2.581   42.480  1.00 55.96  ?  425 LYS   B CA  1 
ATOM   4687 C  C   . LYS   B 1 269 ? -67.663 1.878   43.803  1.00 61.16  ?  425 LYS   B C   1 
ATOM   4688 O  O   . LYS   B 1 269 ? -66.856 1.077   44.298  1.00 61.67  ?  425 LYS   B O   1 
ATOM   4689 C  CB  . LYS   B 1 269 ? -66.642 3.918   42.732  1.00 53.10  ?  425 LYS   B CB  1 
ATOM   4690 C  CG  . LYS   B 1 269 ? -67.473 4.923   43.499  1.00 47.11  ?  425 LYS   B CG  1 
ATOM   4691 C  CD  . LYS   B 1 269 ? -66.622 5.863   44.367  1.00 59.77  ?  425 LYS   B CD  1 
ATOM   4692 C  CE  . LYS   B 1 269 ? -65.543 6.620   43.613  1.00 55.34  ?  425 LYS   B CE  1 
ATOM   4693 N  NZ  . LYS   B 1 269 ? -65.424 8.003   44.194  1.00 58.57  ?  425 LYS   B NZ  1 
ATOM   4694 N  N   . ASP   B 1 270 ? -68.814 2.168   44.400  1.00 54.05  ?  426 ASP   B N   1 
ATOM   4695 C  CA  . ASP   B 1 270 ? -69.170 1.514   45.654  1.00 62.88  ?  426 ASP   B CA  1 
ATOM   4696 C  C   . ASP   B 1 270 ? -69.670 0.087   45.465  1.00 60.46  ?  426 ASP   B C   1 
ATOM   4697 O  O   . ASP   B 1 270 ? -69.826 -0.630  46.458  1.00 62.13  ?  426 ASP   B O   1 
ATOM   4698 C  CB  . ASP   B 1 270 ? -70.209 2.356   46.402  1.00 62.34  ?  426 ASP   B CB  1 
ATOM   4699 C  CG  . ASP   B 1 270 ? -71.224 3.004   45.460  1.00 64.01  ?  426 ASP   B CG  1 
ATOM   4700 O  OD1 . ASP   B 1 270 ? -70.997 2.980   44.223  1.00 64.40  ?  426 ASP   B OD1 1 
ATOM   4701 O  OD2 . ASP   B 1 270 ? -72.239 3.543   45.960  1.00 71.31  -1 426 ASP   B OD2 1 
ATOM   4702 N  N   . LYS   B 1 271 ? -69.926 -0.341  44.234  1.00 57.97  ?  427 LYS   B N   1 
ATOM   4703 C  CA  . LYS   B 1 271 ? -70.127 -1.755  43.977  1.00 55.96  ?  427 LYS   B CA  1 
ATOM   4704 C  C   . LYS   B 1 271 ? -68.789 -2.378  43.594  1.00 61.22  ?  427 LYS   B C   1 
ATOM   4705 O  O   . LYS   B 1 271 ? -67.815 -1.684  43.283  1.00 55.56  ?  427 LYS   B O   1 
ATOM   4706 C  CB  . LYS   B 1 271 ? -71.134 -2.002  42.852  1.00 57.90  ?  427 LYS   B CB  1 
ATOM   4707 C  CG  . LYS   B 1 271 ? -72.260 -0.994  42.607  1.00 59.43  ?  427 LYS   B CG  1 
ATOM   4708 C  CD  . LYS   B 1 271 ? -72.955 -0.440  43.835  1.00 57.85  ?  427 LYS   B CD  1 
ATOM   4709 C  CE  . LYS   B 1 271 ? -73.360 1.009   43.575  1.00 62.76  ?  427 LYS   B CE  1 
ATOM   4710 N  NZ  . LYS   B 1 271 ? -73.997 1.659   44.756  1.00 63.09  ?  427 LYS   B NZ  1 
ATOM   4711 N  N   . LYS   B 1 272 ? -68.754 -3.707  43.584  1.00 61.47  ?  428 LYS   B N   1 
ATOM   4712 C  CA  . LYS   B 1 272 ? -67.517 -4.423  43.298  1.00 55.82  ?  428 LYS   B CA  1 
ATOM   4713 C  C   . LYS   B 1 272 ? -67.313 -4.713  41.814  1.00 53.91  ?  428 LYS   B C   1 
ATOM   4714 O  O   . LYS   B 1 272 ? -66.212 -5.111  41.423  1.00 53.19  ?  428 LYS   B O   1 
ATOM   4715 C  CB  . LYS   B 1 272 ? -67.490 -5.734  44.086  1.00 57.11  ?  428 LYS   B CB  1 
ATOM   4716 C  CG  . LYS   B 1 272 ? -68.121 -5.617  45.488  1.00 62.26  ?  428 LYS   B CG  1 
ATOM   4717 C  CD  . LYS   B 1 272 ? -67.090 -5.605  46.619  1.00 59.78  ?  428 LYS   B CD  1 
ATOM   4718 C  CE  . LYS   B 1 272 ? -66.649 -4.176  46.977  1.00 57.86  ?  428 LYS   B CE  1 
ATOM   4719 N  NZ  . LYS   B 1 272 ? -65.980 -4.112  48.304  1.00 57.68  ?  428 LYS   B NZ  1 
ATOM   4720 N  N   . HIS   B 1 273 ? -68.331 -4.502  40.982  1.00 52.08  ?  429 HIS   B N   1 
ATOM   4721 C  CA  . HIS   B 1 273 ? -68.325 -5.064  39.632  1.00 48.26  ?  429 HIS   B CA  1 
ATOM   4722 C  C   . HIS   B 1 273 ? -67.129 -4.560  38.824  1.00 43.32  ?  429 HIS   B C   1 
ATOM   4723 O  O   . HIS   B 1 273 ? -66.386 -5.349  38.229  1.00 48.95  ?  429 HIS   B O   1 
ATOM   4724 C  CB  . HIS   B 1 273 ? -69.651 -4.720  38.944  1.00 52.39  ?  429 HIS   B CB  1 
ATOM   4725 C  CG  . HIS   B 1 273 ? -70.826 -5.409  39.560  1.00 51.41  ?  429 HIS   B CG  1 
ATOM   4726 N  ND1 . HIS   B 1 273 ? -70.813 -6.747  39.892  1.00 57.63  ?  429 HIS   B ND1 1 
ATOM   4727 C  CD2 . HIS   B 1 273 ? -71.997 -4.916  40.032  1.00 54.71  ?  429 HIS   B CD2 1 
ATOM   4728 C  CE1 . HIS   B 1 273 ? -71.952 -7.064  40.485  1.00 59.63  ?  429 HIS   B CE1 1 
ATOM   4729 N  NE2 . HIS   B 1 273 ? -72.686 -5.969  40.587  1.00 61.46  ?  429 HIS   B NE2 1 
ATOM   4730 N  N   . LEU   B 1 274 ? -66.898 -3.254  38.827  1.00 40.04  ?  430 LEU   B N   1 
ATOM   4731 C  CA  . LEU   B 1 274 ? -65.956 -2.651  37.898  1.00 41.60  ?  430 LEU   B CA  1 
ATOM   4732 C  C   . LEU   B 1 274 ? -64.593 -2.356  38.510  1.00 44.67  ?  430 LEU   B C   1 
ATOM   4733 O  O   . LEU   B 1 274 ? -63.766 -1.727  37.840  1.00 42.44  ?  430 LEU   B O   1 
ATOM   4734 C  CB  . LEU   B 1 274 ? -66.552 -1.370  37.317  1.00 37.93  ?  430 LEU   B CB  1 
ATOM   4735 C  CG  . LEU   B 1 274 ? -67.897 -1.521  36.597  1.00 39.24  ?  430 LEU   B CG  1 
ATOM   4736 C  CD1 . LEU   B 1 274 ? -68.321 -0.175  36.012  1.00 41.44  ?  430 LEU   B CD1 1 
ATOM   4737 C  CD2 . LEU   B 1 274 ? -67.876 -2.617  35.508  1.00 38.18  ?  430 LEU   B CD2 1 
ATOM   4738 N  N   . ASP   B 1 275 ? -64.330 -2.811  39.748  1.00 44.25  ?  431 ASP   B N   1 
ATOM   4739 C  CA  . ASP   B 1 275 ? -63.076 -2.481  40.429  1.00 49.80  ?  431 ASP   B CA  1 
ATOM   4740 C  C   . ASP   B 1 275 ? -61.855 -3.039  39.693  1.00 44.33  ?  431 ASP   B C   1 
ATOM   4741 O  O   . ASP   B 1 275 ? -60.790 -2.412  39.695  1.00 46.22  ?  431 ASP   B O   1 
ATOM   4742 C  CB  . ASP   B 1 275 ? -63.086 -3.004  41.878  1.00 51.03  ?  431 ASP   B CB  1 
ATOM   4743 C  CG  . ASP   B 1 275 ? -64.185 -2.375  42.754  1.00 54.51  ?  431 ASP   B CG  1 
ATOM   4744 O  OD1 . ASP   B 1 275 ? -65.206 -1.894  42.221  1.00 60.39  ?  431 ASP   B OD1 1 
ATOM   4745 O  OD2 . ASP   B 1 275 ? -64.031 -2.390  44.003  1.00 70.82  -1 431 ASP   B OD2 1 
ATOM   4746 N  N   . LYS   B 1 276 ? -61.971 -4.231  39.099  1.00 36.88  ?  432 LYS   B N   1 
ATOM   4747 C  CA  . LYS   B 1 276 ? -60.836 -4.884  38.450  1.00 41.79  ?  432 LYS   B CA  1 
ATOM   4748 C  C   . LYS   B 1 276 ? -60.542 -4.363  37.042  1.00 46.26  ?  432 LYS   B C   1 
ATOM   4749 O  O   . LYS   B 1 276 ? -59.532 -4.758  36.446  1.00 48.36  ?  432 LYS   B O   1 
ATOM   4750 C  CB  . LYS   B 1 276 ? -61.065 -6.398  38.389  1.00 46.20  ?  432 LYS   B CB  1 
ATOM   4751 C  CG  . LYS   B 1 276 ? -60.616 -7.131  39.658  1.00 44.13  ?  432 LYS   B CG  1 
ATOM   4752 C  CD  . LYS   B 1 276 ? -61.427 -8.392  39.929  1.00 51.82  ?  432 LYS   B CD  1 
ATOM   4753 C  CE  . LYS   B 1 276 ? -60.846 -9.198  41.080  1.00 44.43  ?  432 LYS   B CE  1 
ATOM   4754 N  NZ  . LYS   B 1 276 ? -61.036 -10.671 40.915  1.00 62.12  ?  432 LYS   B NZ  1 
ATOM   4755 N  N   . PHE   B 1 277 ? -61.377 -3.496  36.484  1.00 41.09  ?  433 PHE   B N   1 
ATOM   4756 C  CA  . PHE   B 1 277 ? -61.113 -2.973  35.152  1.00 40.38  ?  433 PHE   B CA  1 
ATOM   4757 C  C   . PHE   B 1 277 ? -60.242 -1.731  35.268  1.00 45.34  ?  433 PHE   B C   1 
ATOM   4758 O  O   . PHE   B 1 277 ? -60.330 -1.000  36.256  1.00 41.19  ?  433 PHE   B O   1 
ATOM   4759 C  CB  . PHE   B 1 277 ? -62.428 -2.671  34.436  1.00 38.02  ?  433 PHE   B CB  1 
ATOM   4760 C  CG  . PHE   B 1 277 ? -63.196 -3.913  34.088  1.00 37.27  ?  433 PHE   B CG  1 
ATOM   4761 C  CD1 . PHE   B 1 277 ? -62.764 -4.736  33.065  1.00 33.00  ?  433 PHE   B CD1 1 
ATOM   4762 C  CD2 . PHE   B 1 277 ? -64.314 -4.283  34.824  1.00 36.82  ?  433 PHE   B CD2 1 
ATOM   4763 C  CE1 . PHE   B 1 277 ? -63.452 -5.897  32.741  1.00 40.93  ?  433 PHE   B CE1 1 
ATOM   4764 C  CE2 . PHE   B 1 277 ? -65.015 -5.431  34.516  1.00 35.40  ?  433 PHE   B CE2 1 
ATOM   4765 C  CZ  . PHE   B 1 277 ? -64.584 -6.249  33.469  1.00 36.47  ?  433 PHE   B CZ  1 
ATOM   4766 N  N   . SER   B 1 278 ? -59.380 -1.506  34.274  1.00 40.62  ?  434 SER   B N   1 
ATOM   4767 C  CA  . SER   B 1 278 ? -58.462 -0.374  34.324  1.00 46.23  ?  434 SER   B CA  1 
ATOM   4768 C  C   . SER   B 1 278 ? -58.272 0.206   32.932  1.00 39.88  ?  434 SER   B C   1 
ATOM   4769 O  O   . SER   B 1 278 ? -58.601 -0.420  31.915  1.00 35.03  ?  434 SER   B O   1 
ATOM   4770 C  CB  . SER   B 1 278 ? -57.087 -0.761  34.860  1.00 38.52  ?  434 SER   B CB  1 
ATOM   4771 O  OG  . SER   B 1 278 ? -56.333 -1.412  33.854  1.00 39.85  ?  434 SER   B OG  1 
ATOM   4772 N  N   . SER   B 1 279 ? -57.662 1.396   32.895  1.00 37.91  ?  435 SER   B N   1 
ATOM   4773 C  CA  . SER   B 1 279 ? -57.376 2.009   31.607  1.00 42.80  ?  435 SER   B CA  1 
ATOM   4774 C  C   . SER   B 1 279 ? -56.433 1.154   30.770  1.00 40.77  ?  435 SER   B C   1 
ATOM   4775 O  O   . SER   B 1 279 ? -56.407 1.311   29.543  1.00 33.71  ?  435 SER   B O   1 
ATOM   4776 C  CB  . SER   B 1 279 ? -56.758 3.386   31.777  1.00 35.53  ?  435 SER   B CB  1 
ATOM   4777 O  OG  . SER   B 1 279 ? -55.444 3.229   32.241  1.00 39.12  ?  435 SER   B OG  1 
ATOM   4778 N  N   . TYR   B 1 280 ? -55.646 0.275   31.411  1.00 34.78  ?  436 TYR   B N   1 
ATOM   4779 C  CA  . TYR   B 1 280 ? -54.771 -0.627  30.660  1.00 43.38  ?  436 TYR   B CA  1 
ATOM   4780 C  C   . TYR   B 1 280 ? -55.559 -1.593  29.780  1.00 32.27  ?  436 TYR   B C   1 
ATOM   4781 O  O   . TYR   B 1 280 ? -55.067 -2.010  28.723  1.00 31.74  ?  436 TYR   B O   1 
ATOM   4782 C  CB  . TYR   B 1 280 ? -53.883 -1.443  31.602  1.00 33.39  ?  436 TYR   B CB  1 
ATOM   4783 C  CG  . TYR   B 1 280 ? -52.746 -2.135  30.871  1.00 38.85  ?  436 TYR   B CG  1 
ATOM   4784 C  CD1 . TYR   B 1 280 ? -51.658 -1.405  30.409  1.00 46.44  ?  436 TYR   B CD1 1 
ATOM   4785 C  CD2 . TYR   B 1 280 ? -52.779 -3.499  30.595  1.00 36.14  ?  436 TYR   B CD2 1 
ATOM   4786 C  CE1 . TYR   B 1 280 ? -50.609 -2.015  29.719  1.00 43.09  ?  436 TYR   B CE1 1 
ATOM   4787 C  CE2 . TYR   B 1 280 ? -51.731 -4.125  29.906  1.00 32.08  ?  436 TYR   B CE2 1 
ATOM   4788 C  CZ  . TYR   B 1 280 ? -50.645 -3.376  29.480  1.00 43.67  ?  436 TYR   B CZ  1 
ATOM   4789 O  OH  . TYR   B 1 280 ? -49.601 -3.966  28.785  1.00 43.42  ?  436 TYR   B OH  1 
ATOM   4790 N  N   . HIS   B 1 281 ? -56.744 -2.013  30.228  1.00 29.28  ?  437 HIS   B N   1 
ATOM   4791 C  CA  . HIS   B 1 281 ? -57.583 -2.875  29.397  1.00 30.43  ?  437 HIS   B CA  1 
ATOM   4792 C  C   . HIS   B 1 281 ? -58.069 -2.120  28.165  1.00 30.85  ?  437 HIS   B C   1 
ATOM   4793 O  O   . HIS   B 1 281 ? -57.993 -2.631  27.049  1.00 31.47  ?  437 HIS   B O   1 
ATOM   4794 C  CB  . HIS   B 1 281 ? -58.776 -3.390  30.195  1.00 29.89  ?  437 HIS   B CB  1 
ATOM   4795 C  CG  . HIS   B 1 281 ? -58.397 -4.260  31.357  1.00 34.68  ?  437 HIS   B CG  1 
ATOM   4796 N  ND1 . HIS   B 1 281 ? -58.846 -4.021  32.637  1.00 41.95  ?  437 HIS   B ND1 1 
ATOM   4797 C  CD2 . HIS   B 1 281 ? -57.631 -5.377  31.432  1.00 30.23  ?  437 HIS   B CD2 1 
ATOM   4798 C  CE1 . HIS   B 1 281 ? -58.365 -4.940  33.454  1.00 36.40  ?  437 HIS   B CE1 1 
ATOM   4799 N  NE2 . HIS   B 1 281 ? -57.622 -5.775  32.749  1.00 31.96  ?  437 HIS   B NE2 1 
ATOM   4800 N  N   . VAL   B 1 282 ? -58.608 -0.916  28.365  1.00 30.63  ?  438 VAL   B N   1 
ATOM   4801 C  CA  . VAL   B 1 282 ? -59.048 -0.071  27.248  1.00 31.51  ?  438 VAL   B CA  1 
ATOM   4802 C  C   . VAL   B 1 282 ? -57.916 0.143   26.257  1.00 31.91  ?  438 VAL   B C   1 
ATOM   4803 O  O   . VAL   B 1 282 ? -58.099 0.097   25.023  1.00 30.69  ?  438 VAL   B O   1 
ATOM   4804 C  CB  . VAL   B 1 282 ? -59.558 1.267   27.810  1.00 33.96  ?  438 VAL   B CB  1 
ATOM   4805 C  CG1 . VAL   B 1 282 ? -59.553 2.302   26.764  1.00 41.41  ?  438 VAL   B CG1 1 
ATOM   4806 C  CG2 . VAL   B 1 282 ? -60.945 1.074   28.367  1.00 43.89  ?  438 VAL   B CG2 1 
ATOM   4807 N  N   . LYS   B 1 283 ? -56.729 0.396   26.783  1.00 30.62  ?  439 LYS   B N   1 
ATOM   4808 C  CA  . LYS   B 1 283 ? -55.599 0.752   25.943  1.00 29.85  ?  439 LYS   B CA  1 
ATOM   4809 C  C   . LYS   B 1 283 ? -55.108 -0.474  25.178  1.00 29.77  ?  439 LYS   B C   1 
ATOM   4810 O  O   . LYS   B 1 283 ? -54.796 -0.395  23.981  1.00 26.64  ?  439 LYS   B O   1 
ATOM   4811 C  CB  . LYS   B 1 283 ? -54.515 1.382   26.837  1.00 30.92  ?  439 LYS   B CB  1 
ATOM   4812 C  CG  . LYS   B 1 283 ? -53.327 1.936   26.096  1.00 38.09  ?  439 LYS   B CG  1 
ATOM   4813 C  CD  . LYS   B 1 283 ? -52.470 2.827   27.003  1.00 40.50  ?  439 LYS   B CD  1 
ATOM   4814 C  CE  . LYS   B 1 283 ? -51.748 2.045   28.064  1.00 47.75  ?  439 LYS   B CE  1 
ATOM   4815 N  NZ  . LYS   B 1 283 ? -50.874 2.965   28.832  1.00 57.36  ?  439 LYS   B NZ  1 
ATOM   4816 N  N   . THR   B 1 284 ? -55.116 -1.638  25.831  1.00 26.50  ?  440 THR   B N   1 
ATOM   4817 C  CA  . THR   B 1 284 ? -54.767 -2.873  25.137  1.00 28.26  ?  440 THR   B CA  1 
ATOM   4818 C  C   . THR   B 1 284 ? -55.754 -3.180  24.008  1.00 27.72  ?  440 THR   B C   1 
ATOM   4819 O  O   . THR   B 1 284 ? -55.351 -3.541  22.892  1.00 25.24  ?  440 THR   B O   1 
ATOM   4820 C  CB  . THR   B 1 284 ? -54.713 -4.022  26.135  1.00 26.98  ?  440 THR   B CB  1 
ATOM   4821 O  OG1 . THR   B 1 284 ? -53.744 -3.698  27.145  1.00 32.25  ?  440 THR   B OG1 1 
ATOM   4822 C  CG2 . THR   B 1 284 ? -54.285 -5.291  25.434  1.00 27.92  ?  440 THR   B CG2 1 
ATOM   4823 N  N   . ALA   B 1 285 ? -57.052 -3.074  24.294  1.00 27.08  ?  441 ALA   B N   1 
ATOM   4824 C  CA  . ALA   B 1 285 ? -58.045 -3.312  23.249  1.00 31.47  ?  441 ALA   B CA  1 
ATOM   4825 C  C   . ALA   B 1 285 ? -57.852 -2.350  22.083  1.00 30.10  ?  441 ALA   B C   1 
ATOM   4826 O  O   . ALA   B 1 285 ? -57.942 -2.745  20.917  1.00 28.86  ?  441 ALA   B O   1 
ATOM   4827 C  CB  . ALA   B 1 285 ? -59.458 -3.190  23.821  1.00 32.71  ?  441 ALA   B CB  1 
ATOM   4828 N  N   . PHE   B 1 286 ? -57.535 -1.092  22.388  1.00 28.71  ?  442 PHE   B N   1 
ATOM   4829 C  CA  . PHE   B 1 286 ? -57.341 -0.096  21.348  1.00 26.99  ?  442 PHE   B CA  1 
ATOM   4830 C  C   . PHE   B 1 286 ? -56.178 -0.469  20.441  1.00 28.62  ?  442 PHE   B C   1 
ATOM   4831 O  O   . PHE   B 1 286 ? -56.305 -0.421  19.211  1.00 28.53  ?  442 PHE   B O   1 
ATOM   4832 C  CB  . PHE   B 1 286 ? -57.140 1.289   21.971  1.00 26.96  ?  442 PHE   B CB  1 
ATOM   4833 C  CG  . PHE   B 1 286 ? -56.747 2.338   20.971  1.00 26.17  ?  442 PHE   B CG  1 
ATOM   4834 C  CD1 . PHE   B 1 286 ? -57.701 2.909   20.112  1.00 27.97  ?  442 PHE   B CD1 1 
ATOM   4835 C  CD2 . PHE   B 1 286 ? -55.429 2.753   20.880  1.00 28.25  ?  442 PHE   B CD2 1 
ATOM   4836 C  CE1 . PHE   B 1 286 ? -57.335 3.869   19.197  1.00 26.23  ?  442 PHE   B CE1 1 
ATOM   4837 C  CE2 . PHE   B 1 286 ? -55.055 3.716   19.966  1.00 36.29  ?  442 PHE   B CE2 1 
ATOM   4838 C  CZ  . PHE   B 1 286 ? -56.004 4.275   19.115  1.00 30.70  ?  442 PHE   B CZ  1 
ATOM   4839 N  N   . PHE   B 1 287 ? -55.042 -0.873  21.031  1.00 24.89  ?  443 PHE   B N   1 
ATOM   4840 C  CA  . PHE   B 1 287 ? -53.886 -1.259  20.227  1.00 24.26  ?  443 PHE   B CA  1 
ATOM   4841 C  C   . PHE   B 1 287 ? -54.221 -2.431  19.297  1.00 26.89  ?  443 PHE   B C   1 
ATOM   4842 O  O   . PHE   B 1 287 ? -53.746 -2.477  18.153  1.00 23.21  ?  443 PHE   B O   1 
ATOM   4843 C  CB  . PHE   B 1 287 ? -52.696 -1.607  21.121  1.00 26.34  ?  443 PHE   B CB  1 
ATOM   4844 C  CG  . PHE   B 1 287 ? -52.028 -0.397  21.763  1.00 32.80  ?  443 PHE   B CG  1 
ATOM   4845 C  CD1 . PHE   B 1 287 ? -51.732 0.731   21.008  1.00 30.27  ?  443 PHE   B CD1 1 
ATOM   4846 C  CD2 . PHE   B 1 287 ? -51.690 -0.403  23.104  1.00 39.88  ?  443 PHE   B CD2 1 
ATOM   4847 C  CE1 . PHE   B 1 287 ? -51.128 1.828   21.579  1.00 36.56  ?  443 PHE   B CE1 1 
ATOM   4848 C  CE2 . PHE   B 1 287 ? -51.078 0.693   23.688  1.00 32.44  ?  443 PHE   B CE2 1 
ATOM   4849 C  CZ  . PHE   B 1 287 ? -50.785 1.806   22.917  1.00 35.02  ?  443 PHE   B CZ  1 
ATOM   4850 N  N   . HIS   B 1 288 ? -55.029 -3.388  19.770  1.00 23.47  ?  444 HIS   B N   1 
ATOM   4851 C  CA  . HIS   B 1 288 ? -55.476 -4.463  18.885  1.00 31.19  ?  444 HIS   B CA  1 
ATOM   4852 C  C   . HIS   B 1 288 ? -56.342 -3.921  17.736  1.00 27.67  ?  444 HIS   B C   1 
ATOM   4853 O  O   . HIS   B 1 288 ? -56.239 -4.390  16.595  1.00 25.17  ?  444 HIS   B O   1 
ATOM   4854 C  CB  . HIS   B 1 288 ? -56.234 -5.523  19.686  1.00 27.95  ?  444 HIS   B CB  1 
ATOM   4855 C  CG  . HIS   B 1 288 ? -55.357 -6.350  20.586  1.00 37.12  ?  444 HIS   B CG  1 
ATOM   4856 N  ND1 . HIS   B 1 288 ? -54.271 -7.065  20.120  1.00 34.50  ?  444 HIS   B ND1 1 
ATOM   4857 C  CD2 . HIS   B 1 288 ? -55.402 -6.564  21.927  1.00 29.04  ?  444 HIS   B CD2 1 
ATOM   4858 C  CE1 . HIS   B 1 288 ? -53.694 -7.694  21.134  1.00 36.62  ?  444 HIS   B CE1 1 
ATOM   4859 N  NE2 . HIS   B 1 288 ? -54.366 -7.415  22.240  1.00 29.05  ?  444 HIS   B NE2 1 
ATOM   4860 N  N   . VAL   B 1 289 ? -57.186 -2.923  18.018  1.00 25.45  ?  445 VAL   B N   1 
ATOM   4861 C  CA  . VAL   B 1 289 ? -57.995 -2.331  16.951  1.00 26.72  ?  445 VAL   B CA  1 
ATOM   4862 C  C   . VAL   B 1 289 ? -57.094 -1.632  15.931  1.00 27.37  ?  445 VAL   B C   1 
ATOM   4863 O  O   . VAL   B 1 289 ? -57.359 -1.664  14.717  1.00 28.36  ?  445 VAL   B O   1 
ATOM   4864 C  CB  . VAL   B 1 289 ? -59.051 -1.366  17.531  1.00 25.82  ?  445 VAL   B CB  1 
ATOM   4865 C  CG1 . VAL   B 1 289 ? -59.839 -0.694  16.407  1.00 31.14  ?  445 VAL   B CG1 1 
ATOM   4866 C  CG2 . VAL   B 1 289 ? -60.000 -2.085  18.518  1.00 27.00  ?  445 VAL   B CG2 1 
ATOM   4867 N  N   . CYS   B 1 290 ? -56.004 -1.009  16.397  1.00 23.40  ?  446 CYS   B N   1 
ATOM   4868 C  CA  . CYS   B 1 290 ? -55.056 -0.401  15.458  1.00 25.34  ?  446 CYS   B CA  1 
ATOM   4869 C  C   . CYS   B 1 290 ? -54.404 -1.461  14.575  1.00 30.00  ?  446 CYS   B C   1 
ATOM   4870 O  O   . CYS   B 1 290 ? -54.172 -1.229  13.376  1.00 29.53  ?  446 CYS   B O   1 
ATOM   4871 C  CB  . CYS   B 1 290 ? -53.967 0.377   16.188  1.00 22.35  ?  446 CYS   B CB  1 
ATOM   4872 S  SG  . CYS   B 1 290 ? -54.537 1.917   16.932  1.00 28.13  ?  446 CYS   B SG  1 
ATOM   4873 N  N   . THR   B 1 291 ? -54.073 -2.618  15.161  1.00 23.06  ?  447 THR   B N   1 
ATOM   4874 C  CA  . THR   B 1 291 ? -53.538 -3.719  14.364  1.00 29.48  ?  447 THR   B CA  1 
ATOM   4875 C  C   . THR   B 1 291 ? -54.555 -4.221  13.330  1.00 30.59  ?  447 THR   B C   1 
ATOM   4876 O  O   . THR   B 1 291 ? -54.201 -4.435  12.163  1.00 30.28  ?  447 THR   B O   1 
ATOM   4877 C  CB  . THR   B 1 291 ? -53.066 -4.856  15.271  1.00 33.65  ?  447 THR   B CB  1 
ATOM   4878 O  OG1 . THR   B 1 291 ? -51.974 -4.387  16.071  1.00 32.28  ?  447 THR   B OG1 1 
ATOM   4879 C  CG2 . THR   B 1 291 ? -52.625 -6.070  14.439  1.00 33.85  ?  447 THR   B CG2 1 
ATOM   4880 N  N   . GLN   B 1 292 ? -55.822 -4.423  13.732  1.00 31.26  ?  448 GLN   B N   1 
ATOM   4881 C  CA  . GLN   B 1 292 ? -56.819 -4.888  12.756  1.00 33.50  ?  448 GLN   B CA  1 
ATOM   4882 C  C   . GLN   B 1 292 ? -57.120 -3.859  11.676  1.00 28.26  ?  448 GLN   B C   1 
ATOM   4883 O  O   . GLN   B 1 292 ? -57.608 -4.234  10.599  1.00 28.70  ?  448 GLN   B O   1 
ATOM   4884 C  CB  . GLN   B 1 292 ? -58.156 -5.238  13.400  1.00 33.40  ?  448 GLN   B CB  1 
ATOM   4885 C  CG  . GLN   B 1 292 ? -58.179 -6.312  14.433  1.00 49.55  ?  448 GLN   B CG  1 
ATOM   4886 C  CD  . GLN   B 1 292 ? -59.553 -6.964  14.464  1.00 58.63  ?  448 GLN   B CD  1 
ATOM   4887 O  OE1 . GLN   B 1 292 ? -60.535 -6.340  14.882  1.00 57.14  ?  448 GLN   B OE1 1 
ATOM   4888 N  NE2 . GLN   B 1 292 ? -59.641 -8.207  13.972  1.00 53.99  ?  448 GLN   B NE2 1 
ATOM   4889 N  N   . ASN   B 1 293 ? -56.871 -2.581  11.939  1.00 28.67  ?  449 ASN   B N   1 
ATOM   4890 C  CA  . ASN   B 1 293 ? -57.242 -1.490  11.035  1.00 29.59  ?  449 ASN   B CA  1 
ATOM   4891 C  C   . ASN   B 1 293 ? -56.023 -0.617  10.784  1.00 26.16  ?  449 ASN   B C   1 
ATOM   4892 O  O   . ASN   B 1 293 ? -55.939 0.510   11.279  1.00 28.27  ?  449 ASN   B O   1 
ATOM   4893 C  CB  . ASN   B 1 293 ? -58.391 -0.681  11.632  1.00 27.21  ?  449 ASN   B CB  1 
ATOM   4894 C  CG  . ASN   B 1 293 ? -59.632 -1.545  11.872  1.00 41.01  ?  449 ASN   B CG  1 
ATOM   4895 O  OD1 . ASN   B 1 293 ? -60.412 -1.796  10.973  1.00 36.87  ?  449 ASN   B OD1 1 
ATOM   4896 N  ND2 . ASN   B 1 293 ? -59.765 -2.053  13.086  1.00 39.08  ?  449 ASN   B ND2 1 
ATOM   4897 N  N   . PRO   B 1 294 ? -55.047 -1.112  10.021  1.00 29.13  ?  450 PRO   B N   1 
ATOM   4898 C  CA  . PRO   B 1 294 ? -53.744 -0.430  9.965   1.00 29.70  ?  450 PRO   B CA  1 
ATOM   4899 C  C   . PRO   B 1 294 ? -53.710 0.820   9.095   1.00 32.84  ?  450 PRO   B C   1 
ATOM   4900 O  O   . PRO   B 1 294 ? -52.785 1.633   9.250   1.00 29.80  ?  450 PRO   B O   1 
ATOM   4901 C  CB  . PRO   B 1 294 ? -52.808 -1.517  9.405   1.00 31.23  ?  450 PRO   B CB  1 
ATOM   4902 C  CG  . PRO   B 1 294 ? -53.715 -2.391  8.580   1.00 32.80  ?  450 PRO   B CG  1 
ATOM   4903 C  CD  . PRO   B 1 294 ? -55.033 -2.408  9.317   1.00 29.65  ?  450 PRO   B CD  1 
ATOM   4904 N  N   . GLN   B 1 295 ? -54.661 1.008   8.190   1.00 26.47  ?  451 GLN   B N   1 
ATOM   4905 C  CA  . GLN   B 1 295 ? -54.584 2.103   7.237   1.00 24.73  ?  451 GLN   B CA  1 
ATOM   4906 C  C   . GLN   B 1 295 ? -55.126 3.390   7.836   1.00 23.47  ?  451 GLN   B C   1 
ATOM   4907 O  O   . GLN   B 1 295 ? -56.161 3.386   8.500   1.00 24.17  ?  451 GLN   B O   1 
ATOM   4908 C  CB  . GLN   B 1 295 ? -55.377 1.733   5.971   1.00 29.67  ?  451 GLN   B CB  1 
ATOM   4909 C  CG  . GLN   B 1 295 ? -54.800 0.523   5.211   1.00 24.41  ?  451 GLN   B CG  1 
ATOM   4910 C  CD  . GLN   B 1 295 ? -53.396 0.779   4.678   1.00 29.82  ?  451 GLN   B CD  1 
ATOM   4911 O  OE1 . GLN   B 1 295 ? -53.004 1.928   4.418   1.00 36.47  ?  451 GLN   B OE1 1 
ATOM   4912 N  NE2 . GLN   B 1 295 ? -52.652 -0.289  4.452   1.00 34.23  ?  451 GLN   B NE2 1 
ATOM   4913 N  N   . ASP   B 1 296 ? -54.429 4.502   7.582   1.00 23.54  ?  452 ASP   B N   1 
ATOM   4914 C  CA  . ASP   B 1 296 ? -54.878 5.785   8.119   1.00 25.00  ?  452 ASP   B CA  1 
ATOM   4915 C  C   . ASP   B 1 296 ? -56.283 6.130   7.641   1.00 32.64  ?  452 ASP   B C   1 
ATOM   4916 O  O   . ASP   B 1 296 ? -57.076 6.733   8.399   1.00 28.09  ?  452 ASP   B O   1 
ATOM   4917 C  CB  . ASP   B 1 296 ? -53.898 6.879   7.722   1.00 26.35  ?  452 ASP   B CB  1 
ATOM   4918 C  CG  . ASP   B 1 296 ? -52.517 6.667   8.344   1.00 30.56  ?  452 ASP   B CG  1 
ATOM   4919 O  OD1 . ASP   B 1 296 ? -52.446 5.893   9.320   1.00 25.21  ?  452 ASP   B OD1 1 
ATOM   4920 O  OD2 . ASP   B 1 296 ? -51.518 7.219   7.822   1.00 28.15  -1 452 ASP   B OD2 1 
ATOM   4921 N  N   . SER   B 1 297 ? -56.610 5.742   6.393   1.00 28.08  ?  453 SER   B N   1 
ATOM   4922 C  CA  . SER   B 1 297 ? -57.927 6.011   5.825   1.00 27.37  ?  453 SER   B CA  1 
ATOM   4923 C  C   . SER   B 1 297 ? -59.052 5.395   6.648   1.00 31.75  ?  453 SER   B C   1 
ATOM   4924 O  O   . SER   B 1 297 ? -60.197 5.876   6.576   1.00 31.06  ?  453 SER   B O   1 
ATOM   4925 C  CB  . SER   B 1 297 ? -57.988 5.501   4.364   1.00 34.44  ?  453 SER   B CB  1 
ATOM   4926 O  OG  . SER   B 1 297 ? -57.933 4.066   4.257   1.00 30.46  ?  453 SER   B OG  1 
ATOM   4927 N  N   . GLN   B 1 298 ? -58.761 4.356   7.439   1.00 27.35  ?  454 GLN   B N   1 
ATOM   4928 C  CA  . GLN   B 1 298 ? -59.813 3.732   8.230   1.00 28.42  ?  454 GLN   B CA  1 
ATOM   4929 C  C   . GLN   B 1 298 ? -60.079 4.504   9.511   1.00 27.31  ?  454 GLN   B C   1 
ATOM   4930 O  O   . GLN   B 1 298 ? -60.909 4.078   10.320  1.00 28.59  ?  454 GLN   B O   1 
ATOM   4931 C  CB  . GLN   B 1 298 ? -59.441 2.291   8.593   1.00 27.95  ?  454 GLN   B CB  1 
ATOM   4932 C  CG  . GLN   B 1 298 ? -59.084 1.407   7.433   1.00 28.54  ?  454 GLN   B CG  1 
ATOM   4933 C  CD  . GLN   B 1 298 ? -58.682 0.010   7.882   1.00 34.64  ?  454 GLN   B CD  1 
ATOM   4934 O  OE1 . GLN   B 1 298 ? -57.502 -0.264  8.164   1.00 34.00  ?  454 GLN   B OE1 1 
ATOM   4935 N  NE2 . GLN   B 1 298 ? -59.649 -0.909  7.869   1.00 41.58  ?  454 GLN   B NE2 1 
ATOM   4936 N  N   . TRP   B 1 299 ? -59.371 5.612   9.715   1.00 27.72  ?  455 TRP   B N   1 
ATOM   4937 C  CA  . TRP   B 1 299 ? -59.421 6.407   10.931  1.00 27.96  ?  455 TRP   B CA  1 
ATOM   4938 C  C   . TRP   B 1 299 ? -59.679 7.870   10.586  1.00 33.71  ?  455 TRP   B C   1 
ATOM   4939 O  O   . TRP   B 1 299 ? -59.311 8.759   11.357  1.00 31.55  ?  455 TRP   B O   1 
ATOM   4940 C  CB  . TRP   B 1 299 ? -58.124 6.271   11.738  1.00 27.59  ?  455 TRP   B CB  1 
ATOM   4941 C  CG  . TRP   B 1 299 ? -57.868 4.892   12.250  1.00 26.20  ?  455 TRP   B CG  1 
ATOM   4942 C  CD1 . TRP   B 1 299 ? -57.144 3.917   11.641  1.00 26.39  ?  455 TRP   B CD1 1 
ATOM   4943 C  CD2 . TRP   B 1 299 ? -58.342 4.332   13.477  1.00 25.71  ?  455 TRP   B CD2 1 
ATOM   4944 N  NE1 . TRP   B 1 299 ? -57.124 2.784   12.412  1.00 25.78  ?  455 TRP   B NE1 1 
ATOM   4945 C  CE2 . TRP   B 1 299 ? -57.859 3.011   13.546  1.00 25.91  ?  455 TRP   B CE2 1 
ATOM   4946 C  CE3 . TRP   B 1 299 ? -59.126 4.819   14.526  1.00 26.96  ?  455 TRP   B CE3 1 
ATOM   4947 C  CZ2 . TRP   B 1 299 ? -58.126 2.171   14.627  1.00 26.08  ?  455 TRP   B CZ2 1 
ATOM   4948 C  CZ3 . TRP   B 1 299 ? -59.401 3.982   15.587  1.00 26.47  ?  455 TRP   B CZ3 1 
ATOM   4949 C  CH2 . TRP   B 1 299 ? -58.902 2.669   15.631  1.00 27.94  ?  455 TRP   B CH2 1 
ATOM   4950 N  N   . ASP   B 1 300 ? -60.315 8.134   9.434   1.00 28.43  ?  456 ASP   B N   1 
ATOM   4951 C  CA  . ASP   B 1 300 ? -60.519 9.510   9.003   1.00 29.12  ?  456 ASP   B CA  1 
ATOM   4952 C  C   . ASP   B 1 300 ? -61.306 10.252  10.068  1.00 30.76  ?  456 ASP   B C   1 
ATOM   4953 O  O   . ASP   B 1 300 ? -62.264 9.721   10.631  1.00 30.82  ?  456 ASP   B O   1 
ATOM   4954 C  CB  . ASP   B 1 300 ? -61.296 9.550   7.674   1.00 35.78  ?  456 ASP   B CB  1 
ATOM   4955 C  CG  . ASP   B 1 300 ? -61.214 10.897  6.985   1.00 43.96  ?  456 ASP   B CG  1 
ATOM   4956 O  OD1 . ASP   B 1 300 ? -61.165 11.954  7.659   1.00 39.42  ?  456 ASP   B OD1 1 
ATOM   4957 O  OD2 . ASP   B 1 300 ? -61.296 10.895  5.738   1.00 52.95  -1 456 ASP   B OD2 1 
ATOM   4958 N  N   . ARG   B 1 301 ? -60.907 11.494  10.346  1.00 35.73  ?  457 ARG   B N   1 
ATOM   4959 C  CA  . ARG   B 1 301 ? -61.482 12.191  11.495  1.00 40.55  ?  457 ARG   B CA  1 
ATOM   4960 C  C   . ARG   B 1 301 ? -62.977 12.450  11.319  1.00 38.74  ?  457 ARG   B C   1 
ATOM   4961 O  O   . ARG   B 1 301 ? -63.706 12.522  12.315  1.00 38.43  ?  457 ARG   B O   1 
ATOM   4962 C  CB  . ARG   B 1 301 ? -60.739 13.503  11.759  1.00 46.80  ?  457 ARG   B CB  1 
ATOM   4963 C  CG  . ARG   B 1 301 ? -61.282 14.291  12.935  1.00 49.21  ?  457 ARG   B CG  1 
ATOM   4964 C  CD  . ARG   B 1 301 ? -60.595 15.639  13.038  1.00 59.68  ?  457 ARG   B CD  1 
ATOM   4965 N  NE  . ARG   B 1 301 ? -61.232 16.585  12.123  1.00 61.44  ?  457 ARG   B NE  1 
ATOM   4966 C  CZ  . ARG   B 1 301 ? -62.115 17.508  12.490  1.00 58.12  ?  457 ARG   B CZ  1 
ATOM   4967 N  NH1 . ARG   B 1 301 ? -62.413 17.710  13.764  1.00 63.62  ?  457 ARG   B NH1 1 
ATOM   4968 N  NH2 . ARG   B 1 301 ? -62.715 18.245  11.554  1.00 66.54  ?  457 ARG   B NH2 1 
ATOM   4969 N  N   . LYS   B 1 302 ? -63.461 12.573  10.070  1.00 36.66  ?  458 LYS   B N   1 
ATOM   4970 C  CA  . LYS   B 1 302 ? -64.904 12.705  9.845   1.00 39.43  ?  458 LYS   B CA  1 
ATOM   4971 C  C   . LYS   B 1 302 ? -65.680 11.478  10.312  1.00 43.89  ?  458 LYS   B C   1 
ATOM   4972 O  O   . LYS   B 1 302 ? -66.890 11.567  10.565  1.00 46.10  ?  458 LYS   B O   1 
ATOM   4973 C  CB  . LYS   B 1 302 ? -65.213 12.909  8.366   1.00 45.72  ?  458 LYS   B CB  1 
ATOM   4974 C  CG  . LYS   B 1 302 ? -64.463 11.911  7.480   1.00 45.82  ?  458 LYS   B CG  1 
ATOM   4975 C  CD  . LYS   B 1 302 ? -65.186 11.545  6.192   1.00 54.71  ?  458 LYS   B CD  1 
ATOM   4976 C  CE  . LYS   B 1 302 ? -64.251 10.704  5.290   1.00 59.19  ?  458 LYS   B CE  1 
ATOM   4977 N  NZ  . LYS   B 1 302 ? -64.339 9.204   5.430   1.00 41.41  ?  458 LYS   B NZ  1 
ATOM   4978 N  N   . ASP   B 1 303 ? -65.030 10.319  10.359  1.00 36.15  ?  459 ASP   B N   1 
ATOM   4979 C  CA  . ASP   B 1 303 ? -65.671 9.068   10.737  1.00 33.12  ?  459 ASP   B CA  1 
ATOM   4980 C  C   . ASP   B 1 303 ? -65.537 8.765   12.231  1.00 36.80  ?  459 ASP   B C   1 
ATOM   4981 O  O   . ASP   B 1 303 ? -65.773 7.618   12.635  1.00 31.83  ?  459 ASP   B O   1 
ATOM   4982 C  CB  . ASP   B 1 303 ? -65.098 7.916   9.895   1.00 30.96  ?  459 ASP   B CB  1 
ATOM   4983 C  CG  . ASP   B 1 303 ? -65.434 8.064   8.405   1.00 46.59  ?  459 ASP   B CG  1 
ATOM   4984 O  OD1 . ASP   B 1 303 ? -66.570 8.492   8.127   1.00 33.92  ?  459 ASP   B OD1 1 
ATOM   4985 O  OD2 . ASP   B 1 303 ? -64.589 7.732   7.530   1.00 37.62  -1 459 ASP   B OD2 1 
ATOM   4986 N  N   . LEU   B 1 304 ? -65.169 9.773   13.043  1.00 31.83  ?  460 LEU   B N   1 
ATOM   4987 C  CA  . LEU   B 1 304 ? -65.059 9.616   14.486  1.00 32.14  ?  460 LEU   B CA  1 
ATOM   4988 C  C   . LEU   B 1 304 ? -66.211 8.810   15.066  1.00 33.10  ?  460 LEU   B C   1 
ATOM   4989 O  O   . LEU   B 1 304 ? -65.984 7.870   15.827  1.00 30.69  ?  460 LEU   B O   1 
ATOM   4990 C  CB  . LEU   B 1 304 ? -64.976 10.984  15.177  1.00 33.94  ?  460 LEU   B CB  1 
ATOM   4991 C  CG  . LEU   B 1 304 ? -65.045 10.906  16.708  1.00 30.76  ?  460 LEU   B CG  1 
ATOM   4992 C  CD1 . LEU   B 1 304 ? -63.888 10.084  17.299  1.00 33.50  ?  460 LEU   B CD1 1 
ATOM   4993 C  CD2 . LEU   B 1 304 ? -65.102 12.281  17.350  1.00 32.18  ?  460 LEU   B CD2 1 
ATOM   4994 N  N   . GLY   B 1 305 ? -67.451 9.132   14.667  1.00 31.60  ?  461 GLY   B N   1 
ATOM   4995 C  CA  . GLY   B 1 305 ? -68.603 8.421   15.209  1.00 32.08  ?  461 GLY   B CA  1 
ATOM   4996 C  C   . GLY   B 1 305 ? -68.520 6.919   14.997  1.00 33.83  ?  461 GLY   B C   1 
ATOM   4997 O  O   . GLY   B 1 305 ? -68.646 6.131   15.943  1.00 32.14  ?  461 GLY   B O   1 
ATOM   4998 N  N   . LEU   B 1 306 ? -68.278 6.506   13.752  1.00 32.59  ?  462 LEU   B N   1 
ATOM   4999 C  CA  . LEU   B 1 306 ? -68.203 5.086   13.426  1.00 31.59  ?  462 LEU   B CA  1 
ATOM   5000 C  C   . LEU   B 1 306 ? -66.937 4.452   14.005  1.00 32.37  ?  462 LEU   B C   1 
ATOM   5001 O  O   . LEU   B 1 306 ? -66.969 3.306   14.477  1.00 29.12  ?  462 LEU   B O   1 
ATOM   5002 C  CB  . LEU   B 1 306 ? -68.253 4.902   11.908  1.00 29.77  ?  462 LEU   B CB  1 
ATOM   5003 C  CG  . LEU   B 1 306 ? -69.580 5.292   11.238  1.00 41.55  ?  462 LEU   B CG  1 
ATOM   5004 C  CD1 . LEU   B 1 306 ? -69.642 4.779   9.798   1.00 42.90  ?  462 LEU   B CD1 1 
ATOM   5005 C  CD2 . LEU   B 1 306 ? -70.808 4.806   12.022  1.00 41.31  ?  462 LEU   B CD2 1 
ATOM   5006 N  N   . CYS   B 1 307 ? -65.815 5.185   13.976  1.00 30.32  ?  463 CYS   B N   1 
ATOM   5007 C  CA  . CYS   B 1 307 ? -64.567 4.643   14.503  1.00 30.55  ?  463 CYS   B CA  1 
ATOM   5008 C  C   . CYS   B 1 307 ? -64.679 4.365   16.002  1.00 30.20  ?  463 CYS   B C   1 
ATOM   5009 O  O   . CYS   B 1 307 ? -64.317 3.276   16.471  1.00 30.23  ?  463 CYS   B O   1 
ATOM   5010 C  CB  . CYS   B 1 307 ? -63.413 5.593   14.199  1.00 30.26  ?  463 CYS   B CB  1 
ATOM   5011 S  SG  . CYS   B 1 307 ? -62.956 5.700   12.453  1.00 32.38  ?  463 CYS   B SG  1 
ATOM   5012 N  N   . PHE   B 1 308 ? -65.229 5.317   16.772  1.00 30.64  ?  464 PHE   B N   1 
ATOM   5013 C  CA  . PHE   B 1 308 ? -65.436 5.052   18.202  1.00 29.40  ?  464 PHE   B CA  1 
ATOM   5014 C  C   . PHE   B 1 308 ? -66.391 3.887   18.422  1.00 29.43  ?  464 PHE   B C   1 
ATOM   5015 O  O   . PHE   B 1 308 ? -66.158 3.036   19.290  1.00 28.47  ?  464 PHE   B O   1 
ATOM   5016 C  CB  . PHE   B 1 308 ? -65.971 6.289   18.925  1.00 34.76  ?  464 PHE   B CB  1 
ATOM   5017 C  CG  . PHE   B 1 308 ? -66.175 6.068   20.403  1.00 29.74  ?  464 PHE   B CG  1 
ATOM   5018 C  CD1 . PHE   B 1 308 ? -65.114 5.691   21.216  1.00 30.92  ?  464 PHE   B CD1 1 
ATOM   5019 C  CD2 . PHE   B 1 308 ? -67.425 6.214   20.970  1.00 30.02  ?  464 PHE   B CD2 1 
ATOM   5020 C  CE1 . PHE   B 1 308 ? -65.289 5.476   22.583  1.00 28.28  ?  464 PHE   B CE1 1 
ATOM   5021 C  CE2 . PHE   B 1 308 ? -67.610 6.009   22.334  1.00 34.21  ?  464 PHE   B CE2 1 
ATOM   5022 C  CZ  . PHE   B 1 308 ? -66.538 5.636   23.138  1.00 31.39  ?  464 PHE   B CZ  1 
ATOM   5023 N  N   . ASP   B 1 309 ? -67.486 3.842   17.655  1.00 27.70  ?  465 ASP   B N   1 
ATOM   5024 C  CA  . ASP   B 1 309 ? -68.428 2.739   17.804  1.00 27.88  ?  465 ASP   B CA  1 
ATOM   5025 C  C   . ASP   B 1 309 ? -67.734 1.405   17.584  1.00 26.86  ?  465 ASP   B C   1 
ATOM   5026 O  O   . ASP   B 1 309 ? -68.013 0.424   18.284  1.00 27.06  ?  465 ASP   B O   1 
ATOM   5027 C  CB  . ASP   B 1 309 ? -69.608 2.894   16.836  1.00 28.47  ?  465 ASP   B CB  1 
ATOM   5028 C  CG  . ASP   B 1 309 ? -70.690 1.842   17.082  1.00 29.21  ?  465 ASP   B CG  1 
ATOM   5029 O  OD1 . ASP   B 1 309 ? -71.316 1.849   18.175  1.00 28.11  ?  465 ASP   B OD1 1 
ATOM   5030 O  OD2 . ASP   B 1 309 ? -70.926 1.012   16.160  1.00 31.97  -1 465 ASP   B OD2 1 
ATOM   5031 N  N   . ASN   B 1 310 ? -66.808 1.368   16.628  1.00 27.97  ?  466 ASN   B N   1 
ATOM   5032 C  CA  . ASN   B 1 310 ? -66.118 0.132   16.298  1.00 27.44  ?  466 ASN   B CA  1 
ATOM   5033 C  C   . ASN   B 1 310 ? -65.123 -0.224  17.404  1.00 28.32  ?  466 ASN   B C   1 
ATOM   5034 O  O   . ASN   B 1 310 ? -64.888 -1.406  17.682  1.00 28.20  ?  466 ASN   B O   1 
ATOM   5035 C  CB  . ASN   B 1 310 ? -65.424 0.277   14.928  1.00 27.19  ?  466 ASN   B CB  1 
ATOM   5036 C  CG  . ASN   B 1 310 ? -66.428 0.386   13.734  1.00 29.28  ?  466 ASN   B CG  1 
ATOM   5037 O  OD1 . ASN   B 1 310 ? -67.594 -0.008  13.835  1.00 32.13  ?  466 ASN   B OD1 1 
ATOM   5038 N  ND2 . ASN   B 1 310 ? -65.950 0.910   12.601  1.00 27.98  ?  466 ASN   B ND2 1 
ATOM   5039 N  N   . CYS   B 1 311 ? -64.566 0.786   18.083  1.00 28.48  ?  467 CYS   B N   1 
ATOM   5040 C  CA  . CYS   B 1 311 ? -63.677 0.507   19.222  1.00 27.80  ?  467 CYS   B CA  1 
ATOM   5041 C  C   . CYS   B 1 311 ? -64.462 -0.053  20.397  1.00 28.43  ?  467 CYS   B C   1 
ATOM   5042 O  O   . CYS   B 1 311 ? -64.046 -1.031  21.041  1.00 28.27  ?  467 CYS   B O   1 
ATOM   5043 C  CB  . CYS   B 1 311 ? -62.922 1.770   19.632  1.00 27.77  ?  467 CYS   B CB  1 
ATOM   5044 S  SG  . CYS   B 1 311 ? -61.664 2.285   18.462  1.00 30.62  ?  467 CYS   B SG  1 
ATOM   5045 N  N   . VAL   B 1 312 ? -65.626 0.539   20.665  1.00 26.18  ?  468 VAL   B N   1 
ATOM   5046 C  CA  . VAL   B 1 312 ? -66.495 0.048   21.729  1.00 25.80  ?  468 VAL   B CA  1 
ATOM   5047 C  C   . VAL   B 1 312 ? -66.880 -1.397  21.458  1.00 26.12  ?  468 VAL   B C   1 
ATOM   5048 O  O   . VAL   B 1 312 ? -66.810 -2.259  22.345  1.00 26.00  ?  468 VAL   B O   1 
ATOM   5049 C  CB  . VAL   B 1 312 ? -67.733 0.950   21.860  1.00 26.59  ?  468 VAL   B CB  1 
ATOM   5050 C  CG1 . VAL   B 1 312 ? -68.755 0.281   22.770  1.00 26.88  ?  468 VAL   B CG1 1 
ATOM   5051 C  CG2 . VAL   B 1 312 ? -67.332 2.352   22.431  1.00 27.19  ?  468 VAL   B CG2 1 
ATOM   5052 N  N   . THR   B 1 313 ? -67.300 -1.673  20.215  1.00 25.34  ?  469 THR   B N   1 
ATOM   5053 C  CA  . THR   B 1 313 ? -67.655 -3.025  19.817  1.00 25.04  ?  469 THR   B CA  1 
ATOM   5054 C  C   . THR   B 1 313 ? -66.518 -4.010  20.025  1.00 24.41  ?  469 THR   B C   1 
ATOM   5055 O  O   . THR   B 1 313 ? -66.743 -5.116  20.507  1.00 24.54  ?  469 THR   B O   1 
ATOM   5056 C  CB  . THR   B 1 313 ? -68.111 -3.006  18.353  1.00 26.05  ?  469 THR   B CB  1 
ATOM   5057 O  OG1 . THR   B 1 313 ? -69.404 -2.413  18.301  1.00 25.33  ?  469 THR   B OG1 1 
ATOM   5058 C  CG2 . THR   B 1 313 ? -68.064 -4.387  17.723  1.00 24.80  ?  469 THR   B CG2 1 
ATOM   5059 N  N   . TYR   B 1 314 ? -65.305 -3.658  19.603  1.00 27.24  ?  470 TYR   B N   1 
ATOM   5060 C  CA  . TYR   B 1 314 ? -64.183 -4.575  19.809  1.00 31.17  ?  470 TYR   B CA  1 
ATOM   5061 C  C   . TYR   B 1 314 ? -63.983 -4.873  21.292  1.00 29.36  ?  470 TYR   B C   1 
ATOM   5062 O  O   . TYR   B 1 314 ? -63.821 -6.037  21.692  1.00 27.62  ?  470 TYR   B O   1 
ATOM   5063 C  CB  . TYR   B 1 314 ? -62.890 -4.009  19.220  1.00 29.76  ?  470 TYR   B CB  1 
ATOM   5064 C  CG  . TYR   B 1 314 ? -61.773 -5.016  19.310  1.00 33.52  ?  470 TYR   B CG  1 
ATOM   5065 C  CD1 . TYR   B 1 314 ? -61.678 -6.069  18.376  1.00 41.23  ?  470 TYR   B CD1 1 
ATOM   5066 C  CD2 . TYR   B 1 314 ? -60.849 -4.977  20.354  1.00 35.67  ?  470 TYR   B CD2 1 
ATOM   5067 C  CE1 . TYR   B 1 314 ? -60.664 -7.028  18.478  1.00 43.48  ?  470 TYR   B CE1 1 
ATOM   5068 C  CE2 . TYR   B 1 314 ? -59.838 -5.926  20.458  1.00 35.18  ?  470 TYR   B CE2 1 
ATOM   5069 C  CZ  . TYR   B 1 314 ? -59.753 -6.945  19.526  1.00 36.94  ?  470 TYR   B CZ  1 
ATOM   5070 O  OH  . TYR   B 1 314 ? -58.752 -7.881  19.655  1.00 44.30  ?  470 TYR   B OH  1 
ATOM   5071 N  N   . PHE   B 1 315 ? -64.015 -3.829  22.124  1.00 27.18  ?  471 PHE   B N   1 
ATOM   5072 C  CA  . PHE   B 1 315 ? -63.844 -4.036  23.563  1.00 29.39  ?  471 PHE   B CA  1 
ATOM   5073 C  C   . PHE   B 1 315 ? -64.972 -4.897  24.098  1.00 29.82  ?  471 PHE   B C   1 
ATOM   5074 O  O   . PHE   B 1 315 ? -64.739 -5.799  24.915  1.00 26.97  ?  471 PHE   B O   1 
ATOM   5075 C  CB  . PHE   B 1 315 ? -63.789 -2.692  24.293  1.00 26.48  ?  471 PHE   B CB  1 
ATOM   5076 C  CG  . PHE   B 1 315 ? -63.488 -2.806  25.758  1.00 31.92  ?  471 PHE   B CG  1 
ATOM   5077 C  CD1 . PHE   B 1 315 ? -62.188 -3.088  26.198  1.00 27.75  ?  471 PHE   B CD1 1 
ATOM   5078 C  CD2 . PHE   B 1 315 ? -64.485 -2.599  26.706  1.00 27.87  ?  471 PHE   B CD2 1 
ATOM   5079 C  CE1 . PHE   B 1 315 ? -61.888 -3.175  27.546  1.00 27.53  ?  471 PHE   B CE1 1 
ATOM   5080 C  CE2 . PHE   B 1 315 ? -64.182 -2.682  28.088  1.00 30.49  ?  471 PHE   B CE2 1 
ATOM   5081 C  CZ  . PHE   B 1 315 ? -62.888 -2.970  28.495  1.00 29.05  ?  471 PHE   B CZ  1 
ATOM   5082 N  N   . LEU   B 1 316 ? -66.189 -4.698  23.571  1.00 27.99  ?  472 LEU   B N   1 
ATOM   5083 C  CA  . LEU   B 1 316 ? -67.298 -5.544  23.995  1.00 28.25  ?  472 LEU   B CA  1 
ATOM   5084 C  C   . LEU   B 1 316 ? -67.072 -7.004  23.599  1.00 30.43  ?  472 LEU   B C   1 
ATOM   5085 O  O   . LEU   B 1 316 ? -67.436 -7.915  24.350  1.00 28.89  ?  472 LEU   B O   1 
ATOM   5086 C  CB  . LEU   B 1 316 ? -68.621 -5.029  23.412  1.00 29.15  ?  472 LEU   B CB  1 
ATOM   5087 C  CG  . LEU   B 1 316 ? -69.128 -3.728  24.054  1.00 34.08  ?  472 LEU   B CG  1 
ATOM   5088 C  CD1 . LEU   B 1 316 ? -70.285 -3.165  23.212  1.00 30.61  ?  472 LEU   B CD1 1 
ATOM   5089 C  CD2 . LEU   B 1 316 ? -69.555 -4.046  25.479  1.00 32.29  ?  472 LEU   B CD2 1 
ATOM   5090 N  N   . GLN   B 1 317 ? -66.504 -7.251  22.406  1.00 28.95  ?  473 GLN   B N   1 
ATOM   5091 C  CA  . GLN   B 1 317 ? -66.272 -8.641  21.999  1.00 28.87  ?  473 GLN   B CA  1 
ATOM   5092 C  C   . GLN   B 1 317 ? -65.264 -9.315  22.928  1.00 30.39  ?  473 GLN   B C   1 
ATOM   5093 O  O   . GLN   B 1 317 ? -65.347 -10.521 23.199  1.00 30.45  ?  473 GLN   B O   1 
ATOM   5094 C  CB  . GLN   B 1 317 ? -65.746 -8.701  20.581  1.00 28.53  ?  473 GLN   B CB  1 
ATOM   5095 C  CG  . GLN   B 1 317 ? -65.667 -10.117 20.031  1.00 28.41  ?  473 GLN   B CG  1 
ATOM   5096 C  CD  . GLN   B 1 317 ? -65.271 -10.086 18.586  1.00 34.43  ?  473 GLN   B CD  1 
ATOM   5097 O  OE1 . GLN   B 1 317 ? -64.121 -9.762  18.285  1.00 31.71  ?  473 GLN   B OE1 1 
ATOM   5098 N  NE2 . GLN   B 1 317 ? -66.213 -10.401 17.673  1.00 33.11  ?  473 GLN   B NE2 1 
ATOM   5099 N  N   . CYS   B 1 318 ? -64.266 -8.550  23.372  1.00 29.28  ?  474 CYS   B N   1 
ATOM   5100 C  CA  . CYS   B 1 318 ? -63.291 -9.061  24.330  1.00 30.94  ?  474 CYS   B CA  1 
ATOM   5101 C  C   . CYS   B 1 318 ? -63.958 -9.439  25.653  1.00 31.09  ?  474 CYS   B C   1 
ATOM   5102 O  O   . CYS   B 1 318 ? -63.690 -10.510 26.213  1.00 31.73  ?  474 CYS   B O   1 
ATOM   5103 C  CB  . CYS   B 1 318 ? -62.210 -8.012  24.548  1.00 28.75  ?  474 CYS   B CB  1 
ATOM   5104 S  SG  . CYS   B 1 318 ? -61.162 -7.743  23.096  1.00 31.42  ?  474 CYS   B SG  1 
ATOM   5105 N  N   . LEU   B 1 319 ? -64.849 -8.582  26.155  1.00 30.54  ?  475 LEU   B N   1 
ATOM   5106 C  CA  . LEU   B 1 319 ? -65.558 -8.890  27.393  1.00 28.84  ?  475 LEU   B CA  1 
ATOM   5107 C  C   . LEU   B 1 319 ? -66.370 -10.169 27.262  1.00 35.00  ?  475 LEU   B C   1 
ATOM   5108 O  O   . LEU   B 1 319 ? -66.325 -11.045 28.147  1.00 30.37  ?  475 LEU   B O   1 
ATOM   5109 C  CB  . LEU   B 1 319 ? -66.472 -7.728  27.785  1.00 30.69  ?  475 LEU   B CB  1 
ATOM   5110 C  CG  . LEU   B 1 319 ? -65.786 -6.459  28.318  1.00 34.82  ?  475 LEU   B CG  1 
ATOM   5111 C  CD1 . LEU   B 1 319 ? -66.743 -5.248  28.358  1.00 30.69  ?  475 LEU   B CD1 1 
ATOM   5112 C  CD2 . LEU   B 1 319 ? -65.154 -6.716  29.693  1.00 30.11  ?  475 LEU   B CD2 1 
ATOM   5113 N  N   . ARG   B 1 320 ? -67.137 -10.295 26.167  1.00 31.42  ?  476 ARG   B N   1 
ATOM   5114 C  CA  . ARG   B 1 320 ? -68.026 -11.447 26.062  1.00 29.37  ?  476 ARG   B CA  1 
ATOM   5115 C  C   . ARG   B 1 320 ? -67.244 -12.740 25.879  1.00 28.85  ?  476 ARG   B C   1 
ATOM   5116 O  O   . ARG   B 1 320 ? -67.653 -13.782 26.390  1.00 31.17  ?  476 ARG   B O   1 
ATOM   5117 C  CB  . ARG   B 1 320 ? -69.020 -11.270 24.900  1.00 29.33  ?  476 ARG   B CB  1 
ATOM   5118 C  CG  . ARG   B 1 320 ? -70.059 -10.184 25.119  1.00 28.70  ?  476 ARG   B CG  1 
ATOM   5119 C  CD  . ARG   B 1 320 ? -71.128 -10.246 24.000  1.00 32.34  ?  476 ARG   B CD  1 
ATOM   5120 N  NE  . ARG   B 1 320 ? -71.728 -8.933  23.814  1.00 31.51  ?  476 ARG   B NE  1 
ATOM   5121 C  CZ  . ARG   B 1 320 ? -71.274 -8.050  22.934  1.00 31.28  ?  476 ARG   B CZ  1 
ATOM   5122 N  NH1 . ARG   B 1 320 ? -70.237 -8.320  22.150  1.00 28.90  ?  476 ARG   B NH1 1 
ATOM   5123 N  NH2 . ARG   B 1 320 ? -71.864 -6.861  22.844  1.00 33.56  ?  476 ARG   B NH2 1 
ATOM   5124 N  N   . THR   B 1 321 ? -66.143 -12.709 25.135  1.00 28.36  ?  477 THR   B N   1 
ATOM   5125 C  CA  . THR   B 1 321 ? -65.371 -13.923 24.890  1.00 30.16  ?  477 THR   B CA  1 
ATOM   5126 C  C   . THR   B 1 321 ? -64.278 -14.133 25.940  1.00 34.21  ?  477 THR   B C   1 
ATOM   5127 O  O   . THR   B 1 321 ? -63.531 -15.115 25.844  1.00 33.13  ?  477 THR   B O   1 
ATOM   5128 C  CB  . THR   B 1 321 ? -64.691 -13.901 23.517  1.00 27.99  ?  477 THR   B CB  1 
ATOM   5129 O  OG1 . THR   B 1 321 ? -63.758 -12.832 23.497  1.00 30.18  ?  477 THR   B OG1 1 
ATOM   5130 C  CG2 . THR   B 1 321 ? -65.707 -13.733 22.306  1.00 28.00  ?  477 THR   B CG2 1 
ATOM   5131 N  N   . GLU   B 1 322 ? -64.123 -13.194 26.884  1.00 30.07  ?  478 GLU   B N   1 
ATOM   5132 C  CA  . GLU   B 1 322 ? -63.137 -13.294 27.968  1.00 36.49  ?  478 GLU   B CA  1 
ATOM   5133 C  C   . GLU   B 1 322 ? -61.715 -13.482 27.445  1.00 37.37  ?  478 GLU   B C   1 
ATOM   5134 O  O   . GLU   B 1 322 ? -60.942 -14.290 27.972  1.00 36.47  ?  478 GLU   B O   1 
ATOM   5135 C  CB  . GLU   B 1 322 ? -63.498 -14.422 28.943  1.00 34.03  ?  478 GLU   B CB  1 
ATOM   5136 C  CG  . GLU   B 1 322 ? -64.868 -14.298 29.550  1.00 33.31  ?  478 GLU   B CG  1 
ATOM   5137 C  CD  . GLU   B 1 322 ? -65.074 -15.286 30.681  1.00 42.58  ?  478 GLU   B CD  1 
ATOM   5138 O  OE1 . GLU   B 1 322 ? -64.559 -15.028 31.794  1.00 40.90  ?  478 GLU   B OE1 1 
ATOM   5139 O  OE2 . GLU   B 1 322 ? -65.760 -16.311 30.463  1.00 44.25  -1 478 GLU   B OE2 1 
ATOM   5140 N  N   . LYS   B 1 323 ? -61.367 -12.724 26.411  1.00 32.23  ?  479 LYS   B N   1 
ATOM   5141 C  CA  . LYS   B 1 323 ? -60.063 -12.812 25.759  1.00 32.49  ?  479 LYS   B CA  1 
ATOM   5142 C  C   . LYS   B 1 323 ? -59.594 -11.397 25.447  1.00 34.84  ?  479 LYS   B C   1 
ATOM   5143 O  O   . LYS   B 1 323 ? -60.200 -10.691 24.627  1.00 27.89  ?  479 LYS   B O   1 
ATOM   5144 C  CB  . LYS   B 1 323 ? -60.130 -13.676 24.498  1.00 32.29  ?  479 LYS   B CB  1 
ATOM   5145 C  CG  . LYS   B 1 323 ? -60.388 -15.152 24.846  1.00 42.55  ?  479 LYS   B CG  1 
ATOM   5146 C  CD  . LYS   B 1 323 ? -60.415 -16.059 23.629  1.00 59.91  ?  479 LYS   B CD  1 
ATOM   5147 C  CE  . LYS   B 1 323 ? -60.704 -17.503 24.049  1.00 55.27  ?  479 LYS   B CE  1 
ATOM   5148 N  NZ  . LYS   B 1 323 ? -60.822 -18.433 22.873  1.00 63.88  ?  479 LYS   B NZ  1 
ATOM   5149 N  N   . LEU   B 1 324 ? -58.520 -10.981 26.125  1.00 29.10  ?  480 LEU   B N   1 
ATOM   5150 C  CA  . LEU   B 1 324 ? -57.833 -9.721  25.838  1.00 29.55  ?  480 LEU   B CA  1 
ATOM   5151 C  C   . LEU   B 1 324 ? -56.350 -9.996  26.077  1.00 39.87  ?  480 LEU   B C   1 
ATOM   5152 O  O   . LEU   B 1 324 ? -55.864 -9.879  27.207  1.00 33.39  ?  480 LEU   B O   1 
ATOM   5153 C  CB  . LEU   B 1 324 ? -58.349 -8.598  26.719  1.00 31.22  ?  480 LEU   B CB  1 
ATOM   5154 C  CG  . LEU   B 1 324 ? -57.726 -7.235  26.443  1.00 30.93  ?  480 LEU   B CG  1 
ATOM   5155 C  CD1 . LEU   B 1 324 ? -58.190 -6.748  25.089  1.00 28.51  ?  480 LEU   B CD1 1 
ATOM   5156 C  CD2 . LEU   B 1 324 ? -58.100 -6.255  27.529  1.00 33.43  ?  480 LEU   B CD2 1 
ATOM   5157 N  N   . GLU   B 1 325 ? -55.652 -10.398 25.018  1.00 37.80  ?  481 GLU   B N   1 
ATOM   5158 C  CA  . GLU   B 1 325 ? -54.215 -10.642 25.102  1.00 41.97  ?  481 GLU   B CA  1 
ATOM   5159 C  C   . GLU   B 1 325 ? -53.455 -9.369  25.445  1.00 39.26  ?  481 GLU   B C   1 
ATOM   5160 O  O   . GLU   B 1 325 ? -53.760 -8.286  24.940  1.00 32.40  ?  481 GLU   B O   1 
ATOM   5161 C  CB  . GLU   B 1 325 ? -53.677 -11.161 23.769  1.00 41.62  ?  481 GLU   B CB  1 
ATOM   5162 C  CG  . GLU   B 1 325 ? -54.162 -12.535 23.343  1.00 40.96  ?  481 GLU   B CG  1 
ATOM   5163 C  CD  . GLU   B 1 325 ? -53.518 -12.947 22.040  1.00 45.70  ?  481 GLU   B CD  1 
ATOM   5164 O  OE1 . GLU   B 1 325 ? -53.057 -12.041 21.302  1.00 37.56  ?  481 GLU   B OE1 1 
ATOM   5165 O  OE2 . GLU   B 1 325 ? -53.440 -14.170 21.770  1.00 64.60  -1 481 GLU   B OE2 1 
ATOM   5166 N  N   . ASN   B 1 326 ? -52.417 -9.512  26.262  1.00 36.92  ?  482 ASN   B N   1 
ATOM   5167 C  CA  . ASN   B 1 326 ? -51.452 -8.434  26.368  1.00 33.13  ?  482 ASN   B CA  1 
ATOM   5168 C  C   . ASN   B 1 326 ? -50.791 -8.199  25.003  1.00 31.51  ?  482 ASN   B C   1 
ATOM   5169 O  O   . ASN   B 1 326 ? -50.361 -9.148  24.331  1.00 27.47  ?  482 ASN   B O   1 
ATOM   5170 C  CB  . ASN   B 1 326 ? -50.407 -8.766  27.437  1.00 30.64  ?  482 ASN   B CB  1 
ATOM   5171 C  CG  . ASN   B 1 326 ? -49.464 -7.624  27.685  1.00 34.04  ?  482 ASN   B CG  1 
ATOM   5172 O  OD1 . ASN   B 1 326 ? -48.607 -7.337  26.849  1.00 33.03  ?  482 ASN   B OD1 1 
ATOM   5173 N  ND2 . ASN   B 1 326 ? -49.595 -6.971  28.848  1.00 35.19  ?  482 ASN   B ND2 1 
ATOM   5174 N  N   . TYR   B 1 327 ? -50.695 -6.922  24.617  1.00 29.98  ?  483 TYR   B N   1 
ATOM   5175 C  CA  . TYR   B 1 327 ? -50.236 -6.544  23.273  1.00 31.32  ?  483 TYR   B CA  1 
ATOM   5176 C  C   . TYR   B 1 327 ? -48.771 -6.896  23.067  1.00 32.56  ?  483 TYR   B C   1 
ATOM   5177 O  O   . TYR   B 1 327 ? -48.335 -7.106  21.927  1.00 32.69  ?  483 TYR   B O   1 
ATOM   5178 C  CB  . TYR   B 1 327 ? -50.456 -5.048  23.061  1.00 26.24  ?  483 TYR   B CB  1 
ATOM   5179 C  CG  . TYR   B 1 327 ? -50.412 -4.589  21.616  1.00 28.97  ?  483 TYR   B CG  1 
ATOM   5180 C  CD1 . TYR   B 1 327 ? -51.423 -4.949  20.713  1.00 27.37  ?  483 TYR   B CD1 1 
ATOM   5181 C  CD2 . TYR   B 1 327 ? -49.366 -3.806  21.152  1.00 32.73  ?  483 TYR   B CD2 1 
ATOM   5182 C  CE1 . TYR   B 1 327 ? -51.396 -4.522  19.379  1.00 27.42  ?  483 TYR   B CE1 1 
ATOM   5183 C  CE2 . TYR   B 1 327 ? -49.316 -3.374  19.824  1.00 29.26  ?  483 TYR   B CE2 1 
ATOM   5184 C  CZ  . TYR   B 1 327 ? -50.335 -3.737  18.946  1.00 32.54  ?  483 TYR   B CZ  1 
ATOM   5185 O  OH  . TYR   B 1 327 ? -50.276 -3.326  17.636  1.00 31.46  ?  483 TYR   B OH  1 
ATOM   5186 N  N   . PHE   B 1 328 ? -48.009 -6.962  24.167  1.00 31.48  ?  484 PHE   B N   1 
ATOM   5187 C  CA  . PHE   B 1 328 ? -46.589 -7.283  24.179  1.00 30.52  ?  484 PHE   B CA  1 
ATOM   5188 C  C   . PHE   B 1 328 ? -46.328 -8.732  24.547  1.00 29.95  ?  484 PHE   B C   1 
ATOM   5189 O  O   . PHE   B 1 328 ? -45.302 -9.282  24.150  1.00 32.97  ?  484 PHE   B O   1 
ATOM   5190 C  CB  . PHE   B 1 328 ? -45.871 -6.358  25.180  1.00 28.90  ?  484 PHE   B CB  1 
ATOM   5191 C  CG  . PHE   B 1 328 ? -46.007 -4.914  24.814  1.00 31.03  ?  484 PHE   B CG  1 
ATOM   5192 C  CD1 . PHE   B 1 328 ? -47.124 -4.201  25.218  1.00 31.39  ?  484 PHE   B CD1 1 
ATOM   5193 C  CD2 . PHE   B 1 328 ? -45.066 -4.283  24.029  1.00 29.83  ?  484 PHE   B CD2 1 
ATOM   5194 C  CE1 . PHE   B 1 328 ? -47.299 -2.858  24.835  1.00 32.42  ?  484 PHE   B CE1 1 
ATOM   5195 C  CE2 . PHE   B 1 328 ? -45.228 -2.955  23.656  1.00 32.10  ?  484 PHE   B CE2 1 
ATOM   5196 C  CZ  . PHE   B 1 328 ? -46.346 -2.243  24.059  1.00 27.67  ?  484 PHE   B CZ  1 
ATOM   5197 N  N   . ILE   B 1 329 ? -47.249 -9.353  25.282  1.00 31.91  ?  485 ILE   B N   1 
ATOM   5198 C  CA  . ILE   B 1 329 ? -47.088 -10.696 25.847  1.00 35.02  ?  485 ILE   B CA  1 
ATOM   5199 C  C   . ILE   B 1 329 ? -48.336 -11.501 25.492  1.00 32.30  ?  485 ILE   B C   1 
ATOM   5200 O  O   . ILE   B 1 329 ? -49.260 -11.624 26.310  1.00 31.76  ?  485 ILE   B O   1 
ATOM   5201 C  CB  . ILE   B 1 329 ? -46.861 -10.635 27.371  1.00 30.81  ?  485 ILE   B CB  1 
ATOM   5202 C  CG1 . ILE   B 1 329 ? -45.738 -9.646  27.719  1.00 33.77  ?  485 ILE   B CG1 1 
ATOM   5203 C  CG2 . ILE   B 1 329 ? -46.599 -12.053 27.957  1.00 30.58  ?  485 ILE   B CG2 1 
ATOM   5204 C  CD1 . ILE   B 1 329 ? -45.572 -9.419  29.265  1.00 38.78  ?  485 ILE   B CD1 1 
ATOM   5205 N  N   . PRO   B 1 330 ? -48.417 -12.066 24.290  1.00 32.76  ?  486 PRO   B N   1 
ATOM   5206 C  CA  . PRO   B 1 330 ? -49.727 -12.516 23.789  1.00 38.28  ?  486 PRO   B CA  1 
ATOM   5207 C  C   . PRO   B 1 330 ? -50.282 -13.721 24.529  1.00 37.10  ?  486 PRO   B C   1 
ATOM   5208 O  O   . PRO   B 1 330 ? -51.505 -13.910 24.546  1.00 39.85  ?  486 PRO   B O   1 
ATOM   5209 C  CB  . PRO   B 1 330 ? -49.455 -12.826 22.309  1.00 42.37  ?  486 PRO   B CB  1 
ATOM   5210 C  CG  . PRO   B 1 330 ? -47.967 -13.117 22.254  1.00 47.21  ?  486 PRO   B CG  1 
ATOM   5211 C  CD  . PRO   B 1 330 ? -47.323 -12.277 23.329  1.00 39.88  ?  486 PRO   B CD  1 
ATOM   5212 N  N   . GLU   B 1 331 ? -49.436 -14.521 25.164  1.00 40.19  ?  487 GLU   B N   1 
ATOM   5213 C  CA  . GLU   B 1 331 ? -49.919 -15.631 25.971  1.00 45.46  ?  487 GLU   B CA  1 
ATOM   5214 C  C   . GLU   B 1 331 ? -50.561 -15.176 27.270  1.00 38.43  ?  487 GLU   B C   1 
ATOM   5215 O  O   . GLU   B 1 331 ? -51.119 -16.013 27.982  1.00 40.35  ?  487 GLU   B O   1 
ATOM   5216 C  CB  . GLU   B 1 331 ? -48.763 -16.584 26.260  1.00 38.19  ?  487 GLU   B CB  1 
ATOM   5217 C  CG  . GLU   B 1 331 ? -48.280 -17.272 25.008  1.00 44.14  ?  487 GLU   B CG  1 
ATOM   5218 C  CD  . GLU   B 1 331 ? -46.983 -18.006 25.204  1.00 54.09  ?  487 GLU   B CD  1 
ATOM   5219 O  OE1 . GLU   B 1 331 ? -45.922 -17.335 25.272  1.00 60.44  ?  487 GLU   B OE1 1 
ATOM   5220 O  OE2 . GLU   B 1 331 ? -47.024 -19.251 25.277  1.00 60.62  -1 487 GLU   B OE2 1 
ATOM   5221 N  N   . PHE   B 1 332 ? -50.506 -13.881 27.594  1.00 40.87  ?  488 PHE   B N   1 
ATOM   5222 C  CA  . PHE   B 1 332 ? -51.033 -13.366 28.856  1.00 37.95  ?  488 PHE   B CA  1 
ATOM   5223 C  C   . PHE   B 1 332 ? -52.435 -12.824 28.599  1.00 38.38  ?  488 PHE   B C   1 
ATOM   5224 O  O   . PHE   B 1 332 ? -52.599 -11.785 27.954  1.00 37.67  ?  488 PHE   B O   1 
ATOM   5225 C  CB  . PHE   B 1 332 ? -50.111 -12.292 29.436  1.00 37.47  ?  488 PHE   B CB  1 
ATOM   5226 C  CG  . PHE   B 1 332 ? -50.436 -11.901 30.859  1.00 42.16  ?  488 PHE   B CG  1 
ATOM   5227 C  CD1 . PHE   B 1 332 ? -51.461 -11.013 31.134  1.00 41.30  ?  488 PHE   B CD1 1 
ATOM   5228 C  CD2 . PHE   B 1 332 ? -49.726 -12.446 31.921  1.00 47.18  ?  488 PHE   B CD2 1 
ATOM   5229 C  CE1 . PHE   B 1 332 ? -51.757 -10.646 32.445  1.00 43.18  ?  488 PHE   B CE1 1 
ATOM   5230 C  CE2 . PHE   B 1 332 ? -50.021 -12.096 33.242  1.00 50.97  ?  488 PHE   B CE2 1 
ATOM   5231 C  CZ  . PHE   B 1 332 ? -51.042 -11.192 33.501  1.00 46.44  ?  488 PHE   B CZ  1 
ATOM   5232 N  N   . ASN   B 1 333 ? -53.450 -13.514 29.111  1.00 35.45  ?  489 ASN   B N   1 
ATOM   5233 C  CA  . ASN   B 1 333 ? -54.827 -13.097 28.860  1.00 41.12  ?  489 ASN   B CA  1 
ATOM   5234 C  C   . ASN   B 1 333 ? -55.311 -12.170 29.981  1.00 37.36  ?  489 ASN   B C   1 
ATOM   5235 O  O   . ASN   B 1 333 ? -55.736 -12.635 31.035  1.00 39.47  ?  489 ASN   B O   1 
ATOM   5236 C  CB  . ASN   B 1 333 ? -55.739 -14.311 28.705  1.00 32.19  ?  489 ASN   B CB  1 
ATOM   5237 C  CG  . ASN   B 1 333 ? -57.166 -13.909 28.403  1.00 31.92  ?  489 ASN   B CG  1 
ATOM   5238 O  OD1 . ASN   B 1 333 ? -57.449 -12.727 28.161  1.00 34.95  ?  489 ASN   B OD1 1 
ATOM   5239 N  ND2 . ASN   B 1 333 ? -58.074 -14.869 28.427  1.00 31.84  ?  489 ASN   B ND2 1 
ATOM   5240 N  N   . LEU   B 1 334 ? -55.323 -10.849 29.709  1.00 33.53  ?  490 LEU   B N   1 
ATOM   5241 C  CA  . LEU   B 1 334 ? -55.775 -9.862  30.694  1.00 30.95  ?  490 LEU   B CA  1 
ATOM   5242 C  C   . LEU   B 1 334 ? -57.187 -10.131 31.203  1.00 33.11  ?  490 LEU   B C   1 
ATOM   5243 O  O   . LEU   B 1 334 ? -57.502 -9.792  32.353  1.00 38.00  ?  490 LEU   B O   1 
ATOM   5244 C  CB  . LEU   B 1 334 ? -55.722 -8.451  30.113  1.00 29.52  ?  490 LEU   B CB  1 
ATOM   5245 C  CG  . LEU   B 1 334 ? -54.336 -7.950  29.736  1.00 33.05  ?  490 LEU   B CG  1 
ATOM   5246 C  CD1 . LEU   B 1 334 ? -54.393 -6.594  29.020  1.00 31.78  ?  490 LEU   B CD1 1 
ATOM   5247 C  CD2 . LEU   B 1 334 ? -53.464 -7.904  31.015  1.00 37.93  ?  490 LEU   B CD2 1 
ATOM   5248 N  N   . PHE   B 1 335 ? -58.054 -10.716 30.374  1.00 33.87  ?  491 PHE   B N   1 
ATOM   5249 C  CA  . PHE   B 1 335 ? -59.436 -10.990 30.743  1.00 34.85  ?  491 PHE   B CA  1 
ATOM   5250 C  C   . PHE   B 1 335 ? -59.669 -12.442 31.165  1.00 41.11  ?  491 PHE   B C   1 
ATOM   5251 O  O   . PHE   B 1 335 ? -60.806 -12.917 31.082  1.00 39.81  ?  491 PHE   B O   1 
ATOM   5252 C  CB  . PHE   B 1 335 ? -60.388 -10.619 29.595  1.00 34.63  ?  491 PHE   B CB  1 
ATOM   5253 C  CG  . PHE   B 1 335 ? -60.731 -9.147  29.527  1.00 36.20  ?  491 PHE   B CG  1 
ATOM   5254 C  CD1 . PHE   B 1 335 ? -60.299 -8.275  30.520  1.00 36.37  ?  491 PHE   B CD1 1 
ATOM   5255 C  CD2 . PHE   B 1 335 ? -61.507 -8.638  28.478  1.00 34.73  ?  491 PHE   B CD2 1 
ATOM   5256 C  CE1 . PHE   B 1 335 ? -60.628 -6.925  30.472  1.00 34.08  ?  491 PHE   B CE1 1 
ATOM   5257 C  CE2 . PHE   B 1 335 ? -61.839 -7.285  28.426  1.00 31.78  ?  491 PHE   B CE2 1 
ATOM   5258 C  CZ  . PHE   B 1 335 ? -61.396 -6.431  29.416  1.00 33.49  ?  491 PHE   B CZ  1 
ATOM   5259 N  N   . SER   B 1 336 ? -58.644 -13.159 31.644  1.00 39.87  ?  492 SER   B N   1 
ATOM   5260 C  CA  . SER   B 1 336 ? -58.895 -14.550 32.018  1.00 40.95  ?  492 SER   B CA  1 
ATOM   5261 C  C   . SER   B 1 336 ? -59.784 -14.608 33.257  1.00 44.44  ?  492 SER   B C   1 
ATOM   5262 O  O   . SER   B 1 336 ? -59.784 -13.701 34.097  1.00 45.89  ?  492 SER   B O   1 
ATOM   5263 C  CB  . SER   B 1 336 ? -57.601 -15.319 32.291  1.00 47.94  ?  492 SER   B CB  1 
ATOM   5264 O  OG  . SER   B 1 336 ? -56.942 -14.868 33.469  1.00 54.27  ?  492 SER   B OG  1 
ATOM   5265 N  N   . SER   B 1 337 ? -60.560 -15.691 33.360  1.00 42.88  ?  493 SER   B N   1 
ATOM   5266 C  CA  . SER   B 1 337 ? -61.410 -15.876 34.530  1.00 50.63  ?  493 SER   B CA  1 
ATOM   5267 C  C   . SER   B 1 337 ? -60.595 -15.977 35.825  1.00 50.10  ?  493 SER   B C   1 
ATOM   5268 O  O   . SER   B 1 337 ? -61.117 -15.660 36.898  1.00 45.48  ?  493 SER   B O   1 
ATOM   5269 C  CB  . SER   B 1 337 ? -62.296 -17.115 34.341  1.00 54.13  ?  493 SER   B CB  1 
ATOM   5270 O  OG  . SER   B 1 337 ? -61.574 -18.212 33.802  1.00 61.84  ?  493 SER   B OG  1 
ATOM   5271 N  N   . ASN   B 1 338 ? -59.327 -16.392 35.745  1.00 51.89  ?  494 ASN   B N   1 
ATOM   5272 C  CA  . ASN   B 1 338 ? -58.420 -16.303 36.894  1.00 44.06  ?  494 ASN   B CA  1 
ATOM   5273 C  C   . ASN   B 1 338 ? -58.289 -14.878 37.423  1.00 50.94  ?  494 ASN   B C   1 
ATOM   5274 O  O   . ASN   B 1 338 ? -58.057 -14.683 38.620  1.00 47.66  ?  494 ASN   B O   1 
ATOM   5275 C  CB  . ASN   B 1 338 ? -57.040 -16.816 36.493  1.00 50.57  ?  494 ASN   B CB  1 
ATOM   5276 C  CG  . ASN   B 1 338 ? -57.030 -18.297 36.220  1.00 53.59  ?  494 ASN   B CG  1 
ATOM   5277 O  OD1 . ASN   B 1 338 ? -57.929 -19.024 36.648  1.00 57.73  ?  494 ASN   B OD1 1 
ATOM   5278 N  ND2 . ASN   B 1 338 ? -56.039 -18.747 35.456  1.00 56.88  ?  494 ASN   B ND2 1 
ATOM   5279 N  N   . LEU   B 1 339 ? -58.395 -13.869 36.552  1.00 48.02  ?  495 LEU   B N   1 
ATOM   5280 C  CA  . LEU   B 1 339 ? -58.181 -12.490 36.975  1.00 42.82  ?  495 LEU   B CA  1 
ATOM   5281 C  C   . LEU   B 1 339 ? -59.471 -11.702 37.179  1.00 45.08  ?  495 LEU   B C   1 
ATOM   5282 O  O   . LEU   B 1 339 ? -59.513 -10.817 38.039  1.00 51.87  ?  495 LEU   B O   1 
ATOM   5283 C  CB  . LEU   B 1 339 ? -57.298 -11.740 35.961  1.00 40.05  ?  495 LEU   B CB  1 
ATOM   5284 C  CG  . LEU   B 1 339 ? -55.817 -12.142 35.888  1.00 49.80  ?  495 LEU   B CG  1 
ATOM   5285 C  CD1 . LEU   B 1 339 ? -55.212 -11.934 34.503  1.00 45.39  ?  495 LEU   B CD1 1 
ATOM   5286 C  CD2 . LEU   B 1 339 ? -54.944 -11.521 37.004  1.00 47.42  ?  495 LEU   B CD2 1 
ATOM   5287 N  N   . ILE   B 1 340 ? -60.516 -11.974 36.399  1.00 52.66  ?  496 ILE   B N   1 
ATOM   5288 C  CA  . ILE   B 1 340 ? -61.761 -11.212 36.451  1.00 42.07  ?  496 ILE   B CA  1 
ATOM   5289 C  C   . ILE   B 1 340 ? -62.916 -12.197 36.316  1.00 52.74  ?  496 ILE   B C   1 
ATOM   5290 O  O   . ILE   B 1 340 ? -62.914 -13.027 35.401  1.00 47.87  ?  496 ILE   B O   1 
ATOM   5291 C  CB  . ILE   B 1 340 ? -61.843 -10.150 35.332  1.00 48.34  ?  496 ILE   B CB  1 
ATOM   5292 C  CG1 . ILE   B 1 340 ? -60.693 -9.139  35.408  1.00 40.07  ?  496 ILE   B CG1 1 
ATOM   5293 C  CG2 . ILE   B 1 340 ? -63.161 -9.408  35.414  1.00 51.47  ?  496 ILE   B CG2 1 
ATOM   5294 C  CD1 . ILE   B 1 340 ? -60.641 -8.172  34.199  1.00 43.54  ?  496 ILE   B CD1 1 
ATOM   5295 N  N   . ASP   B 1 341 ? -63.908 -12.106 37.209  1.00 43.95  ?  497 ASP   B N   1 
ATOM   5296 C  CA  . ASP   B 1 341 ? -65.061 -12.995 37.114  1.00 44.57  ?  497 ASP   B CA  1 
ATOM   5297 C  C   . ASP   B 1 341 ? -65.922 -12.679 35.889  1.00 48.09  ?  497 ASP   B C   1 
ATOM   5298 O  O   . ASP   B 1 341 ? -66.025 -11.527 35.458  1.00 43.55  ?  497 ASP   B O   1 
ATOM   5299 C  CB  . ASP   B 1 341 ? -65.913 -12.906 38.370  1.00 43.14  ?  497 ASP   B CB  1 
ATOM   5300 C  CG  . ASP   B 1 341 ? -65.195 -13.454 39.581  1.00 54.71  ?  497 ASP   B CG  1 
ATOM   5301 O  OD1 . ASP   B 1 341 ? -64.429 -14.426 39.405  1.00 66.89  ?  497 ASP   B OD1 1 
ATOM   5302 O  OD2 . ASP   B 1 341 ? -65.399 -12.936 40.698  1.00 57.86  -1 497 ASP   B OD2 1 
ATOM   5303 N  N   . LYS   B 1 342 ? -66.548 -13.731 35.337  1.00 42.98  ?  498 LYS   B N   1 
ATOM   5304 C  CA  . LYS   B 1 342 ? -67.477 -13.570 34.220  1.00 47.88  ?  498 LYS   B CA  1 
ATOM   5305 C  C   . LYS   B 1 342 ? -68.540 -12.529 34.551  1.00 45.94  ?  498 LYS   B C   1 
ATOM   5306 O  O   . LYS   B 1 342 ? -68.761 -11.588 33.782  1.00 40.93  ?  498 LYS   B O   1 
ATOM   5307 C  CB  . LYS   B 1 342 ? -68.121 -14.919 33.864  1.00 44.30  ?  498 LYS   B CB  1 
ATOM   5308 C  CG  . LYS   B 1 342 ? -69.175 -14.820 32.744  1.00 43.50  ?  498 LYS   B CG  1 
ATOM   5309 C  CD  . LYS   B 1 342 ? -68.604 -15.295 31.428  1.00 39.53  ?  498 LYS   B CD  1 
ATOM   5310 C  CE  . LYS   B 1 342 ? -69.695 -15.393 30.357  1.00 44.40  ?  498 LYS   B CE  1 
ATOM   5311 N  NZ  . LYS   B 1 342 ? -69.505 -14.265 29.408  1.00 35.49  ?  498 LYS   B NZ  1 
ATOM   5312 N  N   . ARG   B 1 343 ? -69.147 -12.651 35.741  1.00 41.72  ?  499 ARG   B N   1 
ATOM   5313 C  CA  . ARG   B 1 343 ? -70.156 -11.700 36.210  1.00 43.87  ?  499 ARG   B CA  1 
ATOM   5314 C  C   . ARG   B 1 343 ? -69.715 -10.244 36.040  1.00 45.49  ?  499 ARG   B C   1 
ATOM   5315 O  O   . ARG   B 1 343 ? -70.490 -9.402  35.571  1.00 46.59  ?  499 ARG   B O   1 
ATOM   5316 C  CB  . ARG   B 1 343 ? -70.480 -11.987 37.682  1.00 50.84  ?  499 ARG   B CB  1 
ATOM   5317 C  CG  . ARG   B 1 343 ? -70.766 -10.719 38.491  1.00 54.00  ?  499 ARG   B CG  1 
ATOM   5318 C  CD  . ARG   B 1 343 ? -70.771 -10.921 39.982  1.00 54.28  ?  499 ARG   B CD  1 
ATOM   5319 N  NE  . ARG   B 1 343 ? -72.117 -11.110 40.509  1.00 54.42  ?  499 ARG   B NE  1 
ATOM   5320 C  CZ  . ARG   B 1 343 ? -72.389 -11.469 41.754  1.00 47.93  ?  499 ARG   B CZ  1 
ATOM   5321 N  NH1 . ARG   B 1 343 ? -71.440 -11.532 42.680  1.00 55.56  ?  499 ARG   B NH1 1 
ATOM   5322 N  NH2 . ARG   B 1 343 ? -73.643 -11.770 42.082  1.00 52.29  ?  499 ARG   B NH2 1 
ATOM   5323 N  N   . SER   B 1 344 ? -68.469 -9.925  36.404  1.00 40.41  ?  500 SER   B N   1 
ATOM   5324 C  CA  . SER   B 1 344 ? -67.992 -8.550  36.251  1.00 37.50  ?  500 SER   B CA  1 
ATOM   5325 C  C   . SER   B 1 344 ? -67.971 -8.114  34.777  1.00 36.62  ?  500 SER   B C   1 
ATOM   5326 O  O   . SER   B 1 344 ? -68.444 -7.021  34.440  1.00 35.39  ?  500 SER   B O   1 
ATOM   5327 C  CB  . SER   B 1 344 ? -66.610 -8.407  36.903  1.00 45.63  ?  500 SER   B CB  1 
ATOM   5328 O  OG  . SER   B 1 344 ? -66.633 -8.899  38.238  1.00 48.70  ?  500 SER   B OG  1 
ATOM   5329 N  N   . LYS   B 1 345 ? -67.438 -8.960  33.885  1.00 38.17  ?  501 LYS   B N   1 
ATOM   5330 C  CA  . LYS   B 1 345 ? -67.409 -8.644  32.456  1.00 40.13  ?  501 LYS   B CA  1 
ATOM   5331 C  C   . LYS   B 1 345 ? -68.827 -8.449  31.929  1.00 38.36  ?  501 LYS   B C   1 
ATOM   5332 O  O   . LYS   B 1 345 ? -69.109 -7.494  31.192  1.00 32.82  ?  501 LYS   B O   1 
ATOM   5333 C  CB  . LYS   B 1 345 ? -66.718 -9.791  31.718  1.00 36.55  ?  501 LYS   B CB  1 
ATOM   5334 C  CG  . LYS   B 1 345 ? -65.269 -9.992  32.159  1.00 46.48  ?  501 LYS   B CG  1 
ATOM   5335 C  CD  . LYS   B 1 345 ? -64.753 -11.357 31.704  1.00 48.82  ?  501 LYS   B CD  1 
ATOM   5336 C  CE  . LYS   B 1 345 ? -63.541 -11.751 32.529  1.00 44.60  ?  501 LYS   B CE  1 
ATOM   5337 N  NZ  . LYS   B 1 345 ? -63.028 -13.138 32.366  1.00 44.11  ?  501 LYS   B NZ  1 
ATOM   5338 N  N   . GLU   B 1 346 ? -69.736 -9.339  32.343  1.00 37.50  ?  502 GLU   B N   1 
ATOM   5339 C  CA  . GLU   B 1 346 ? -71.140 -9.257  31.972  1.00 34.36  ?  502 GLU   B CA  1 
ATOM   5340 C  C   . GLU   B 1 346 ? -71.768 -7.955  32.439  1.00 36.05  ?  502 GLU   B C   1 
ATOM   5341 O  O   . GLU   B 1 346 ? -72.578 -7.361  31.722  1.00 36.00  ?  502 GLU   B O   1 
ATOM   5342 C  CB  . GLU   B 1 346 ? -71.887 -10.445 32.572  1.00 37.44  ?  502 GLU   B CB  1 
ATOM   5343 C  CG  . GLU   B 1 346 ? -71.701 -11.715 31.781  1.00 39.64  ?  502 GLU   B CG  1 
ATOM   5344 C  CD  . GLU   B 1 346 ? -72.361 -12.924 32.443  1.00 48.28  ?  502 GLU   B CD  1 
ATOM   5345 O  OE1 . GLU   B 1 346 ? -72.544 -12.919 33.683  1.00 46.64  ?  502 GLU   B OE1 1 
ATOM   5346 O  OE2 . GLU   B 1 346 ? -72.682 -13.883 31.704  1.00 53.45  -1 502 GLU   B OE2 1 
ATOM   5347 N  N   . PHE   B 1 347 ? -71.433 -7.503  33.652  1.00 38.62  ?  503 PHE   B N   1 
ATOM   5348 C  CA  . PHE   B 1 347 ? -72.000 -6.245  34.132  1.00 33.78  ?  503 PHE   B CA  1 
ATOM   5349 C  C   . PHE   B 1 347 ? -71.481 -5.077  33.301  1.00 32.41  ?  503 PHE   B C   1 
ATOM   5350 O  O   . PHE   B 1 347 ? -72.246 -4.185  32.917  1.00 33.95  ?  503 PHE   B O   1 
ATOM   5351 C  CB  . PHE   B 1 347 ? -71.680 -6.043  35.623  1.00 38.35  ?  503 PHE   B CB  1 
ATOM   5352 C  CG  . PHE   B 1 347 ? -72.273 -4.791  36.211  1.00 36.34  ?  503 PHE   B CG  1 
ATOM   5353 C  CD1 . PHE   B 1 347 ? -73.592 -4.764  36.653  1.00 45.03  ?  503 PHE   B CD1 1 
ATOM   5354 C  CD2 . PHE   B 1 347 ? -71.523 -3.628  36.302  1.00 41.92  ?  503 PHE   B CD2 1 
ATOM   5355 C  CE1 . PHE   B 1 347 ? -74.139 -3.600  37.208  1.00 45.55  ?  503 PHE   B CE1 1 
ATOM   5356 C  CE2 . PHE   B 1 347 ? -72.066 -2.466  36.845  1.00 42.23  ?  503 PHE   B CE2 1 
ATOM   5357 C  CZ  . PHE   B 1 347 ? -73.374 -2.450  37.290  1.00 42.42  ?  503 PHE   B CZ  1 
ATOM   5358 N  N   . LEU   B 1 348 ? -70.187 -5.072  32.998  1.00 30.63  ?  504 LEU   B N   1 
ATOM   5359 C  CA  . LEU   B 1 348 ? -69.649 -3.970  32.218  1.00 31.17  ?  504 LEU   B CA  1 
ATOM   5360 C  C   . LEU   B 1 348 ? -70.196 -4.007  30.792  1.00 33.29  ?  504 LEU   B C   1 
ATOM   5361 O  O   . LEU   B 1 348 ? -70.424 -2.952  30.187  1.00 30.84  ?  504 LEU   B O   1 
ATOM   5362 C  CB  . LEU   B 1 348 ? -68.121 -4.016  32.220  1.00 30.98  ?  504 LEU   B CB  1 
ATOM   5363 C  CG  . LEU   B 1 348 ? -67.427 -2.885  31.440  1.00 34.71  ?  504 LEU   B CG  1 
ATOM   5364 C  CD1 . LEU   B 1 348 ? -67.877 -1.475  31.906  1.00 30.23  ?  504 LEU   B CD1 1 
ATOM   5365 C  CD2 . LEU   B 1 348 ? -65.905 -3.043  31.478  1.00 30.94  ?  504 LEU   B CD2 1 
ATOM   5366 N  N   . THR   B 1 349 ? -70.455 -5.206  30.260  1.00 30.93  ?  505 THR   B N   1 
ATOM   5367 C  CA  . THR   B 1 349 ? -71.042 -5.305  28.928  1.00 31.05  ?  505 THR   B CA  1 
ATOM   5368 C  C   . THR   B 1 349 ? -72.437 -4.707  28.922  1.00 30.65  ?  505 THR   B C   1 
ATOM   5369 O  O   . THR   B 1 349 ? -72.774 -3.897  28.051  1.00 33.63  ?  505 THR   B O   1 
ATOM   5370 C  CB  . THR   B 1 349 ? -71.078 -6.759  28.463  1.00 33.09  ?  505 THR   B CB  1 
ATOM   5371 O  OG1 . THR   B 1 349 ? -69.732 -7.218  28.318  1.00 33.34  ?  505 THR   B OG1 1 
ATOM   5372 C  CG2 . THR   B 1 349 ? -71.810 -6.868  27.053  1.00 30.59  ?  505 THR   B CG2 1 
ATOM   5373 N  N   . LYS   B 1 350 ? -73.248 -5.084  29.918  1.00 32.11  ?  506 LYS   B N   1 
ATOM   5374 C  CA  . LYS   B 1 350 ? -74.591 -4.542  30.066  1.00 33.40  ?  506 LYS   B CA  1 
ATOM   5375 C  C   . LYS   B 1 350 ? -74.563 -3.019  30.119  1.00 34.31  ?  506 LYS   B C   1 
ATOM   5376 O  O   . LYS   B 1 350 ? -75.314 -2.347  29.407  1.00 33.50  ?  506 LYS   B O   1 
ATOM   5377 C  CB  . LYS   B 1 350 ? -75.239 -5.132  31.320  1.00 33.42  ?  506 LYS   B CB  1 
ATOM   5378 C  CG  . LYS   B 1 350 ? -76.676 -4.737  31.568  1.00 37.21  ?  506 LYS   B CG  1 
ATOM   5379 C  CD  . LYS   B 1 350 ? -77.345 -5.638  32.634  1.00 39.13  ?  506 LYS   B CD  1 
ATOM   5380 C  CE  . LYS   B 1 350 ? -78.850 -5.727  32.357  1.00 56.09  ?  506 LYS   B CE  1 
ATOM   5381 N  NZ  . LYS   B 1 350 ? -79.192 -6.914  31.472  1.00 45.37  ?  506 LYS   B NZ  1 
ATOM   5382 N  N   . GLN   B 1 351 ? -73.649 -2.453  30.916  1.00 32.89  ?  507 GLN   B N   1 
ATOM   5383 C  CA  . GLN   B 1 351 ? -73.616 -0.999  31.078  1.00 37.01  ?  507 GLN   B CA  1 
ATOM   5384 C  C   . GLN   B 1 351 ? -73.181 -0.302  29.781  1.00 32.79  ?  507 GLN   B C   1 
ATOM   5385 O  O   . GLN   B 1 351 ? -73.795 0.689   29.352  1.00 33.26  ?  507 GLN   B O   1 
ATOM   5386 C  CB  . GLN   B 1 351 ? -72.689 -0.628  32.248  1.00 33.40  ?  507 GLN   B CB  1 
ATOM   5387 C  CG  . GLN   B 1 351 ? -73.121 -1.172  33.603  1.00 36.69  ?  507 GLN   B CG  1 
ATOM   5388 C  CD  . GLN   B 1 351 ? -74.540 -0.801  33.959  1.00 37.79  ?  507 GLN   B CD  1 
ATOM   5389 O  OE1 . GLN   B 1 351 ? -74.925 0.360   33.879  1.00 44.39  ?  507 GLN   B OE1 1 
ATOM   5390 N  NE2 . GLN   B 1 351 ? -75.311 -1.778  34.420  1.00 35.63  ?  507 GLN   B NE2 1 
ATOM   5391 N  N   . ILE   B 1 352 ? -72.129 -0.803  29.129  1.00 31.08  ?  508 ILE   B N   1 
ATOM   5392 C  CA  . ILE   B 1 352 ? -71.676 -0.129  27.921  1.00 31.30  ?  508 ILE   B CA  1 
ATOM   5393 C  C   . ILE   B 1 352 ? -72.729 -0.250  26.811  1.00 32.05  ?  508 ILE   B C   1 
ATOM   5394 O  O   . ILE   B 1 352 ? -72.992 0.719   26.077  1.00 31.78  ?  508 ILE   B O   1 
ATOM   5395 C  CB  . ILE   B 1 352 ? -70.302 -0.659  27.464  1.00 35.92  ?  508 ILE   B CB  1 
ATOM   5396 C  CG1 . ILE   B 1 352 ? -69.189 -0.217  28.416  1.00 31.28  ?  508 ILE   B CG1 1 
ATOM   5397 C  CG2 . ILE   B 1 352 ? -69.993 -0.227  26.025  1.00 29.91  ?  508 ILE   B CG2 1 
ATOM   5398 C  CD1 . ILE   B 1 352 ? -67.873 -0.865  28.088  1.00 31.04  ?  508 ILE   B CD1 1 
ATOM   5399 N  N   . GLU   B 1 353 ? -73.367 -1.420  26.685  1.00 31.33  ?  509 GLU   B N   1 
ATOM   5400 C  CA  . GLU   B 1 353 ? -74.395 -1.567  25.653  1.00 31.88  ?  509 GLU   B CA  1 
ATOM   5401 C  C   . GLU   B 1 353 ? -75.546 -0.618  25.896  1.00 33.41  ?  509 GLU   B C   1 
ATOM   5402 O  O   . GLU   B 1 353 ? -76.114 -0.069  24.942  1.00 33.12  ?  509 GLU   B O   1 
ATOM   5403 C  CB  . GLU   B 1 353 ? -74.920 -2.998  25.573  1.00 31.29  ?  509 GLU   B CB  1 
ATOM   5404 C  CG  . GLU   B 1 353 ? -73.940 -3.946  24.911  1.00 31.32  ?  509 GLU   B CG  1 
ATOM   5405 C  CD  . GLU   B 1 353 ? -74.463 -5.375  24.846  1.00 34.32  ?  509 GLU   B CD  1 
ATOM   5406 O  OE1 . GLU   B 1 353 ? -75.244 -5.770  25.733  1.00 35.12  ?  509 GLU   B OE1 1 
ATOM   5407 O  OE2 . GLU   B 1 353 ? -74.052 -6.114  23.927  1.00 30.95  -1 509 GLU   B OE2 1 
ATOM   5408 N  N   . TYR   B 1 354 ? -75.905 -0.414  27.171  1.00 33.27  ?  510 TYR   B N   1 
ATOM   5409 C  CA  . TYR   B 1 354 ? -76.900 0.600   27.482  1.00 36.60  ?  510 TYR   B CA  1 
ATOM   5410 C  C   . TYR   B 1 354 ? -76.439 1.973   26.998  1.00 36.64  ?  510 TYR   B C   1 
ATOM   5411 O  O   . TYR   B 1 354 ? -77.181 2.689   26.313  1.00 35.00  ?  510 TYR   B O   1 
ATOM   5412 C  CB  . TYR   B 1 354 ? -77.187 0.635   28.979  1.00 38.38  ?  510 TYR   B CB  1 
ATOM   5413 C  CG  . TYR   B 1 354 ? -78.137 1.743   29.314  1.00 42.22  ?  510 TYR   B CG  1 
ATOM   5414 C  CD1 . TYR   B 1 354 ? -79.498 1.595   29.080  1.00 44.54  ?  510 TYR   B CD1 1 
ATOM   5415 C  CD2 . TYR   B 1 354 ? -77.680 2.953   29.832  1.00 40.60  ?  510 TYR   B CD2 1 
ATOM   5416 C  CE1 . TYR   B 1 354 ? -80.385 2.609   29.368  1.00 51.86  ?  510 TYR   B CE1 1 
ATOM   5417 C  CE2 . TYR   B 1 354 ? -78.566 3.983   30.116  1.00 44.43  ?  510 TYR   B CE2 1 
ATOM   5418 C  CZ  . TYR   B 1 354 ? -79.915 3.801   29.881  1.00 49.41  ?  510 TYR   B CZ  1 
ATOM   5419 O  OH  . TYR   B 1 354 ? -80.808 4.810   30.145  1.00 56.95  ?  510 TYR   B OH  1 
ATOM   5420 N  N   . GLU   B 1 355 ? -75.211 2.360   27.357  1.00 37.28  ?  511 GLU   B N   1 
ATOM   5421 C  CA  . GLU   B 1 355 ? -74.709 3.672   26.954  1.00 36.36  ?  511 GLU   B CA  1 
ATOM   5422 C  C   . GLU   B 1 355 ? -74.766 3.831   25.440  1.00 36.58  ?  511 GLU   B C   1 
ATOM   5423 O  O   . GLU   B 1 355 ? -75.304 4.820   24.927  1.00 36.06  ?  511 GLU   B O   1 
ATOM   5424 C  CB  . GLU   B 1 355 ? -73.285 3.876   27.474  1.00 35.87  ?  511 GLU   B CB  1 
ATOM   5425 C  CG  . GLU   B 1 355 ? -73.214 4.050   28.998  1.00 35.18  ?  511 GLU   B CG  1 
ATOM   5426 C  CD  . GLU   B 1 355 ? -73.988 5.276   29.472  1.00 38.13  ?  511 GLU   B CD  1 
ATOM   5427 O  OE1 . GLU   B 1 355 ? -73.823 6.362   28.872  1.00 40.87  ?  511 GLU   B OE1 1 
ATOM   5428 O  OE2 . GLU   B 1 355 ? -74.784 5.150   30.421  1.00 41.41  -1 511 GLU   B OE2 1 
ATOM   5429 N  N   . ARG   B 1 356 ? -74.242 2.839   24.706  1.00 32.78  ?  512 ARG   B N   1 
ATOM   5430 C  CA  . ARG   B 1 356 ? -74.121 2.972   23.261  1.00 34.01  ?  512 ARG   B CA  1 
ATOM   5431 C  C   . ARG   B 1 356 ? -75.494 3.020   22.587  1.00 35.45  ?  512 ARG   B C   1 
ATOM   5432 O  O   . ARG   B 1 356 ? -75.664 3.753   21.610  1.00 32.76  ?  512 ARG   B O   1 
ATOM   5433 C  CB  . ARG   B 1 356 ? -73.238 1.836   22.716  1.00 31.70  ?  512 ARG   B CB  1 
ATOM   5434 C  CG  . ARG   B 1 356 ? -72.760 1.950   21.278  1.00 31.87  ?  512 ARG   B CG  1 
ATOM   5435 C  CD  . ARG   B 1 356 ? -73.605 1.042   20.340  1.00 31.01  ?  512 ARG   B CD  1 
ATOM   5436 N  NE  . ARG   B 1 356 ? -73.490 -0.369  20.712  1.00 30.05  ?  512 ARG   B NE  1 
ATOM   5437 C  CZ  . ARG   B 1 356 ? -72.479 -1.164  20.383  1.00 29.95  ?  512 ARG   B CZ  1 
ATOM   5438 N  NH1 . ARG   B 1 356 ? -71.502 -0.753  19.573  1.00 29.59  ?  512 ARG   B NH1 1 
ATOM   5439 N  NH2 . ARG   B 1 356 ? -72.464 -2.414  20.846  1.00 29.18  ?  512 ARG   B NH2 1 
ATOM   5440 N  N   . ASN   B 1 357 ? -76.497 2.319   23.143  1.00 33.00  ?  513 ASN   B N   1 
ATOM   5441 C  CA  . ASN   B 1 357 ? -77.849 2.390   22.603  1.00 33.30  ?  513 ASN   B CA  1 
ATOM   5442 C  C   . ASN   B 1 357 ? -78.522 3.730   22.857  1.00 40.97  ?  513 ASN   B C   1 
ATOM   5443 O  O   . ASN   B 1 357 ? -79.563 4.005   22.252  1.00 34.11  ?  513 ASN   B O   1 
ATOM   5444 C  CB  . ASN   B 1 357 ? -78.739 1.273   23.175  1.00 32.54  ?  513 ASN   B CB  1 
ATOM   5445 C  CG  . ASN   B 1 357 ? -78.522 -0.060  22.468  1.00 32.50  ?  513 ASN   B CG  1 
ATOM   5446 O  OD1 . ASN   B 1 357 ? -78.315 -0.080  21.260  1.00 31.71  ?  513 ASN   B OD1 1 
ATOM   5447 N  ND2 . ASN   B 1 357 ? -78.552 -1.169  23.213  1.00 31.83  ?  513 ASN   B ND2 1 
ATOM   5448 N  N   . ASN   B 1 358 ? -77.982 4.550   23.764  1.00 39.40  ?  514 ASN   B N   1 
ATOM   5449 C  CA  . ASN   B 1 358 ? -78.665 5.770   24.177  1.00 49.12  ?  514 ASN   B CA  1 
ATOM   5450 C  C   . ASN   B 1 358 ? -77.810 7.006   23.945  1.00 44.83  ?  514 ASN   B C   1 
ATOM   5451 O  O   . ASN   B 1 358 ? -78.062 8.054   24.546  1.00 48.04  ?  514 ASN   B O   1 
ATOM   5452 C  CB  . ASN   B 1 358 ? -79.061 5.680   25.644  1.00 38.45  ?  514 ASN   B CB  1 
ATOM   5453 C  CG  . ASN   B 1 358 ? -80.152 4.670   25.880  1.00 42.89  ?  514 ASN   B CG  1 
ATOM   5454 O  OD1 . ASN   B 1 358 ? -81.325 4.952   25.678  1.00 48.52  ?  514 ASN   B OD1 1 
ATOM   5455 N  ND2 . ASN   B 1 358 ? -79.766 3.471   26.305  1.00 42.00  ?  514 ASN   B ND2 1 
ATOM   5456 N  N   . GLU   B 1 359 ? -76.793 6.889   23.106  1.00 38.01  ?  515 GLU   B N   1 
ATOM   5457 C  CA  . GLU   B 1 359 ? -75.893 7.990   22.791  1.00 44.73  ?  515 GLU   B CA  1 
ATOM   5458 C  C   . GLU   B 1 359 ? -75.117 8.445   24.029  1.00 47.78  ?  515 GLU   B C   1 
ATOM   5459 O  O   . GLU   B 1 359 ? -74.893 9.636   24.245  1.00 44.81  ?  515 GLU   B O   1 
ATOM   5460 C  CB  . GLU   B 1 359 ? -76.645 9.143   22.125  1.00 46.30  ?  515 GLU   B CB  1 
ATOM   5461 C  CG  . GLU   B 1 359 ? -77.758 8.677   21.170  1.00 50.44  ?  515 GLU   B CG  1 
ATOM   5462 C  CD  . GLU   B 1 359 ? -78.044 9.694   20.084  1.00 57.85  ?  515 GLU   B CD  1 
ATOM   5463 O  OE1 . GLU   B 1 359 ? -78.174 10.888  20.421  1.00 64.55  ?  515 GLU   B OE1 1 
ATOM   5464 O  OE2 . GLU   B 1 359 ? -78.092 9.308   18.893  1.00 65.98  -1 515 GLU   B OE2 1 
ATOM   5465 N  N   . PHE   B 1 360 ? -74.695 7.471   24.838  1.00 36.93  ?  516 PHE   B N   1 
ATOM   5466 C  CA  . PHE   B 1 360 ? -73.746 7.645   25.934  1.00 41.13  ?  516 PHE   B CA  1 
ATOM   5467 C  C   . PHE   B 1 360 ? -74.137 8.727   26.941  1.00 47.75  ?  516 PHE   B C   1 
ATOM   5468 O  O   . PHE   B 1 360 ? -73.327 9.617   27.231  1.00 49.26  ?  516 PHE   B O   1 
ATOM   5469 C  CB  . PHE   B 1 360 ? -72.364 7.947   25.355  1.00 41.57  ?  516 PHE   B CB  1 
ATOM   5470 C  CG  . PHE   B 1 360 ? -71.871 6.893   24.401  1.00 42.29  ?  516 PHE   B CG  1 
ATOM   5471 C  CD1 . PHE   B 1 360 ? -71.228 5.763   24.881  1.00 35.16  ?  516 PHE   B CD1 1 
ATOM   5472 C  CD2 . PHE   B 1 360 ? -72.068 7.024   23.031  1.00 40.36  ?  516 PHE   B CD2 1 
ATOM   5473 C  CE1 . PHE   B 1 360 ? -70.789 4.782   24.020  1.00 38.72  ?  516 PHE   B CE1 1 
ATOM   5474 C  CE2 . PHE   B 1 360 ? -71.621 6.044   22.148  1.00 37.93  ?  516 PHE   B CE2 1 
ATOM   5475 C  CZ  . PHE   B 1 360 ? -70.979 4.917   22.651  1.00 37.93  ?  516 PHE   B CZ  1 
ATOM   5476 N  N   . PRO   B 1 361 ? -75.330 8.669   27.539  1.00 45.35  ?  517 PRO   B N   1 
ATOM   5477 C  CA  . PRO   B 1 361 ? -75.685 9.687   28.541  1.00 40.55  ?  517 PRO   B CA  1 
ATOM   5478 C  C   . PRO   B 1 361 ? -74.693 9.808   29.695  1.00 49.40  ?  517 PRO   B C   1 
ATOM   5479 O  O   . PRO   B 1 361 ? -74.602 10.891  30.294  1.00 54.87  ?  517 PRO   B O   1 
ATOM   5480 C  CB  . PRO   B 1 361 ? -77.066 9.231   29.034  1.00 44.31  ?  517 PRO   B CB  1 
ATOM   5481 C  CG  . PRO   B 1 361 ? -77.139 7.773   28.706  1.00 49.81  ?  517 PRO   B CG  1 
ATOM   5482 C  CD  . PRO   B 1 361 ? -76.362 7.621   27.425  1.00 44.26  ?  517 PRO   B CD  1 
ATOM   5483 N  N   . VAL   B 1 362 ? -73.947 8.749   30.032  1.00 50.82  ?  518 VAL   B N   1 
ATOM   5484 C  CA  . VAL   B 1 362 ? -73.012 8.828   31.159  1.00 45.36  ?  518 VAL   B CA  1 
ATOM   5485 C  C   . VAL   B 1 362 ? -71.921 9.853   30.890  1.00 55.23  ?  518 VAL   B C   1 
ATOM   5486 O  O   . VAL   B 1 362 ? -71.243 10.298  31.829  1.00 58.00  ?  518 VAL   B O   1 
ATOM   5487 C  CB  . VAL   B 1 362 ? -72.361 7.464   31.479  1.00 42.80  ?  518 VAL   B CB  1 
ATOM   5488 C  CG1 . VAL   B 1 362 ? -71.252 7.149   30.468  1.00 49.61  ?  518 VAL   B CG1 1 
ATOM   5489 C  CG2 . VAL   B 1 362 ? -71.820 7.435   32.910  1.00 48.95  ?  518 VAL   B CG2 1 
ATOM   5490 N  N   . PHE   B 1 363 ? -71.725 10.229  29.621  1.00 49.57  ?  519 PHE   B N   1 
ATOM   5491 C  CA  . PHE   B 1 363 ? -70.753 11.251  29.267  1.00 52.05  ?  519 PHE   B CA  1 
ATOM   5492 C  C   . PHE   B 1 363 ? -71.156 12.615  29.808  1.00 55.71  ?  519 PHE   B C   1 
ATOM   5493 O  O   . PHE   B 1 363 ? -70.299 13.496  29.945  1.00 57.26  ?  519 PHE   B O   1 
ATOM   5494 C  CB  . PHE   B 1 363 ? -70.609 11.320  27.745  1.00 49.15  ?  519 PHE   B CB  1 
ATOM   5495 C  CG  . PHE   B 1 363 ? -69.658 10.290  27.164  1.00 47.11  ?  519 PHE   B CG  1 
ATOM   5496 C  CD1 . PHE   B 1 363 ? -68.912 9.457   27.986  1.00 48.95  ?  519 PHE   B CD1 1 
ATOM   5497 C  CD2 . PHE   B 1 363 ? -69.571 10.116  25.798  1.00 42.18  ?  519 PHE   B CD2 1 
ATOM   5498 C  CE1 . PHE   B 1 363 ? -68.053 8.505   27.432  1.00 50.57  ?  519 PHE   B CE1 1 
ATOM   5499 C  CE2 . PHE   B 1 363 ? -68.729 9.163   25.234  1.00 37.69  ?  519 PHE   B CE2 1 
ATOM   5500 C  CZ  . PHE   B 1 363 ? -67.980 8.350   26.046  1.00 41.83  ?  519 PHE   B CZ  1 
ATOM   5501 N  N   . ASP   B 1 364 ? -72.438 12.808  30.107  1.00 54.46  ?  520 ASP   B N   1 
ATOM   5502 C  CA  . ASP   B 1 364 ? -72.913 14.050  30.711  1.00 61.01  ?  520 ASP   B CA  1 
ATOM   5503 C  C   . ASP   B 1 364 ? -73.694 13.818  32.000  1.00 59.26  ?  520 ASP   B C   1 
ATOM   5504 O  O   . ASP   B 1 364 ? -74.023 14.771  32.706  1.00 55.72  ?  520 ASP   B O   1 
ATOM   5505 C  CB  . ASP   B 1 364 ? -73.762 14.824  29.712  1.00 56.89  ?  520 ASP   B CB  1 
ATOM   5506 C  CG  . ASP   B 1 364 ? -72.921 15.689  28.820  1.00 66.25  ?  520 ASP   B CG  1 
ATOM   5507 O  OD1 . ASP   B 1 364 ? -72.586 16.808  29.272  1.00 65.08  ?  520 ASP   B OD1 1 
ATOM   5508 O  OD2 . ASP   B 1 364 ? -72.576 15.240  27.697  1.00 66.06  -1 520 ASP   B OD2 1 
HETATM 5509 N  N1  . A1EKD C 2 .   ? -18.749 14.917  2.719   1.00 39.90  ?  601 A1EKD A N1  1 
HETATM 5510 N  N3  . A1EKD C 2 .   ? -16.825 10.904  -2.166  1.00 39.56  ?  601 A1EKD A N3  1 
HETATM 5511 C  C4  . A1EKD C 2 .   ? -19.298 16.167  3.023   1.00 32.86  ?  601 A1EKD A C4  1 
HETATM 5512 C  C5  . A1EKD C 2 .   ? -18.375 12.787  2.933   1.00 45.30  ?  601 A1EKD A C5  1 
HETATM 5513 C  C6  . A1EKD C 2 .   ? -18.577 11.409  3.487   1.00 41.35  ?  601 A1EKD A C6  1 
HETATM 5514 C  C7  . A1EKD C 2 .   ? -17.514 13.277  1.914   1.00 36.45  ?  601 A1EKD A C7  1 
HETATM 5515 C  C8  . A1EKD C 2 .   ? -16.476 12.527  1.111   1.00 41.24  ?  601 A1EKD A C8  1 
HETATM 5516 C  C10 . A1EKD C 2 .   ? -14.891 12.206  3.090   1.00 42.41  ?  601 A1EKD A C10 1 
HETATM 5517 C  C13 . A1EKD C 2 .   ? -14.327 9.986   3.870   1.00 43.42  ?  601 A1EKD A C13 1 
HETATM 5518 C  C15 . A1EKD C 2 .   ? -15.791 10.257  1.999   1.00 40.42  ?  601 A1EKD A C15 1 
HETATM 5519 C  C17 . A1EKD C 2 .   ? -16.083 11.472  -1.168  1.00 41.79  ?  601 A1EKD A C17 1 
HETATM 5520 C  C20 . A1EKD C 2 .   ? -16.985 9.139   -6.715  1.00 51.53  ?  601 A1EKD A C20 1 
HETATM 5521 C  C21 . A1EKD C 2 .   ? -16.129 8.681   -7.697  1.00 47.44  ?  601 A1EKD A C21 1 
HETATM 5522 C  C22 . A1EKD C 2 .   ? -14.773 8.652   -7.449  1.00 49.70  ?  601 A1EKD A C22 1 
HETATM 5523 C  C24 . A1EKD C 2 .   ? -15.068 9.517   -5.280  1.00 52.19  ?  601 A1EKD A C24 1 
HETATM 5524 C  C26 . A1EKD C 2 .   ? -19.590 11.603  0.019   1.00 34.13  ?  601 A1EKD A C26 1 
HETATM 5525 C  C28 . A1EKD C 2 .   ? -19.839 19.955  3.331   1.00 34.34  ?  601 A1EKD A C28 1 
HETATM 5526 C  C1  . A1EKD C 2 .   ? -21.187 18.299  5.182   1.00 35.99  ?  601 A1EKD A C1  1 
HETATM 5527 C  C11 . A1EKD C 2 .   ? -14.674 13.683  3.323   1.00 47.50  ?  601 A1EKD A C11 1 
HETATM 5528 C  C12 . A1EKD C 2 .   ? -14.216 11.360  3.970   1.00 41.90  ?  601 A1EKD A C12 1 
HETATM 5529 C  C14 . A1EKD C 2 .   ? -15.113 9.436   2.880   1.00 44.90  ?  601 A1EKD A C14 1 
HETATM 5530 C  C16 . A1EKD C 2 .   ? -16.944 11.843  -0.158  1.00 40.99  ?  601 A1EKD A C16 1 
HETATM 5531 C  C18 . A1EKD C 2 .   ? -16.386 10.371  -3.388  1.00 43.27  ?  601 A1EKD A C18 1 
HETATM 5532 C  C19 . A1EKD C 2 .   ? -16.462 9.557   -5.504  1.00 45.78  ?  601 A1EKD A C19 1 
HETATM 5533 C  C2  . A1EKD C 2 .   ? -20.365 17.749  4.218   1.00 41.22  ?  601 A1EKD A C2  1 
HETATM 5534 C  C23 . A1EKD C 2 .   ? -14.201 9.063   -6.262  1.00 52.01  ?  601 A1EKD A C23 1 
HETATM 5535 C  C25 . A1EKD C 2 .   ? -18.240 11.475  -0.614  1.00 39.88  ?  601 A1EKD A C25 1 
HETATM 5536 C  C27 . A1EKD C 2 .   ? -17.766 14.627  1.826   1.00 40.44  ?  601 A1EKD A C27 1 
HETATM 5537 C  C29 . A1EKD C 2 .   ? -20.663 20.449  4.323   1.00 36.50  ?  601 A1EKD A C29 1 
HETATM 5538 C  C3  . A1EKD C 2 .   ? -19.695 18.577  3.288   1.00 35.14  ?  601 A1EKD A C3  1 
HETATM 5539 C  C30 . A1EKD C 2 .   ? -21.333 19.669  5.234   1.00 36.94  ?  601 A1EKD A C30 1 
HETATM 5540 C  C9  . A1EKD C 2 .   ? -15.689 11.645  2.080   1.00 38.73  ?  601 A1EKD A C9  1 
HETATM 5541 F  F1  . A1EKD C 2 .   ? -21.848 17.501  6.056   1.00 38.91  ?  601 A1EKD A F1  1 
HETATM 5542 F  F2  . A1EKD C 2 .   ? -18.324 9.166   -6.928  1.00 50.67  ?  601 A1EKD A F2  1 
HETATM 5543 F  F3  . A1EKD C 2 .   ? -13.939 8.197   -8.427  1.00 59.73  ?  601 A1EKD A F3  1 
HETATM 5544 F  F4  . A1EKD C 2 .   ? -20.857 21.792  4.375   1.00 42.83  ?  601 A1EKD A F4  1 
HETATM 5545 N  N2  . A1EKD C 2 .   ? -19.122 13.776  3.404   1.00 39.27  ?  601 A1EKD A N2  1 
HETATM 5546 N  N4  . A1EKD C 2 .   ? -17.214 10.051  -4.400  1.00 45.90  ?  601 A1EKD A N4  1 
HETATM 5547 N  N5  . A1EKD C 2 .   ? -18.156 10.902  -1.809  1.00 38.73  ?  601 A1EKD A N5  1 
HETATM 5548 N  N6  . A1EKD C 2 .   ? -20.156 16.350  4.031   1.00 42.89  ?  601 A1EKD A N6  1 
HETATM 5549 O  O1  . A1EKD C 2 .   ? -15.260 14.219  4.301   1.00 43.31  -1 601 A1EKD A O1  1 
HETATM 5550 O  O2  . A1EKD C 2 .   ? -13.900 14.300  2.540   1.00 48.43  ?  601 A1EKD A O2  1 
HETATM 5551 O  O3  . A1EKD C 2 .   ? -14.764 11.606  -1.227  1.00 41.31  ?  601 A1EKD A O3  1 
HETATM 5552 O  O4  . A1EKD C 2 .   ? -17.227 15.557  1.042   1.00 42.77  ?  601 A1EKD A O4  1 
HETATM 5553 S  S1  . A1EKD C 2 .   ? -18.757 17.592  2.210   1.00 38.72  ?  601 A1EKD A S1  1 
HETATM 5554 S  S2  . A1EKD C 2 .   ? -14.703 10.097  -3.689  1.00 50.86  ?  601 A1EKD A S2  1 
HETATM 5555 ZN ZN  . ZN    D 3 .   ? -39.408 2.589   -0.638  1.00 29.31  ?  602 ZN    A ZN  1 
HETATM 5556 N  N1  . A1EKD E 2 .   ? -49.778 -1.961  33.723  1.00 49.91  ?  601 A1EKD B N1  1 
HETATM 5557 N  N3  . A1EKD E 2 .   ? -54.724 1.808   35.701  1.00 48.98  ?  601 A1EKD B N3  1 
HETATM 5558 C  C4  . A1EKD E 2 .   ? -49.546 -3.199  33.115  1.00 46.12  ?  601 A1EKD B C4  1 
HETATM 5559 C  C5  . A1EKD E 2 .   ? -49.473 0.121   34.242  1.00 55.51  ?  601 A1EKD B C5  1 
HETATM 5560 C  C6  . A1EKD E 2 .   ? -48.848 1.482   34.169  1.00 54.76  ?  601 A1EKD B C6  1 
HETATM 5561 C  C7  . A1EKD E 2 .   ? -50.552 -0.372  35.022  1.00 43.46  ?  601 A1EKD B C7  1 
HETATM 5562 C  C8  . A1EKD E 2 .   ? -51.394 0.324   36.065  1.00 50.18  ?  601 A1EKD B C8  1 
HETATM 5563 C  C10 . A1EKD E 2 .   ? -49.462 0.733   37.682  1.00 49.35  ?  601 A1EKD B C10 1 
HETATM 5564 C  C13 . A1EKD E 2 .   ? -48.942 2.971   38.428  1.00 58.59  ?  601 A1EKD B C13 1 
HETATM 5565 C  C15 . A1EKD E 2 .   ? -50.756 2.614   36.916  1.00 51.56  ?  601 A1EKD B C15 1 
HETATM 5566 C  C17 . A1EKD E 2 .   ? -53.720 1.234   36.435  1.00 53.20  ?  601 A1EKD B C17 1 
HETATM 5567 C  C20 . A1EKD E 2 .   ? -59.218 3.811   35.627  1.00 54.90  ?  601 A1EKD B C20 1 
HETATM 5568 C  C21 . A1EKD E 2 .   ? -60.130 4.332   36.524  1.00 48.21  ?  601 A1EKD B C21 1 
HETATM 5569 C  C22 . A1EKD E 2 .   ? -59.858 4.272   37.873  1.00 55.43  ?  601 A1EKD B C22 1 
HETATM 5570 C  C24 . A1EKD E 2 .   ? -57.795 3.194   37.498  1.00 49.45  ?  601 A1EKD B C24 1 
HETATM 5571 C  C26 . A1EKD E 2 .   ? -52.400 1.397   32.976  1.00 43.80  ?  601 A1EKD B C26 1 
HETATM 5572 C  C28 . A1EKD E 2 .   ? -49.484 -6.961  32.495  1.00 37.79  ?  601 A1EKD B C28 1 
HETATM 5573 C  C1  . A1EKD E 2 .   ? -47.496 -5.415  31.205  1.00 51.70  ?  601 A1EKD B C1  1 
HETATM 5574 C  C11 . A1EKD E 2 .   ? -49.086 -0.727  37.777  1.00 55.06  ?  601 A1EKD B C11 1 
HETATM 5575 C  C12 . A1EKD E 2 .   ? -48.683 1.614   38.430  1.00 54.35  ?  601 A1EKD B C12 1 
HETATM 5576 C  C14 . A1EKD E 2 .   ? -49.974 3.469   37.664  1.00 50.65  ?  601 A1EKD B C14 1 
HETATM 5577 C  C16 . A1EKD E 2 .   ? -52.674 0.969   35.583  1.00 55.14  ?  601 A1EKD B C16 1 
HETATM 5578 C  C18 . A1EKD E 2 .   ? -55.976 2.271   36.147  1.00 49.62  ?  601 A1EKD B C18 1 
HETATM 5579 C  C19 . A1EKD E 2 .   ? -58.045 3.241   36.104  1.00 55.79  ?  601 A1EKD B C19 1 
HETATM 5580 C  C2  . A1EKD E 2 .   ? -48.445 -4.812  32.015  1.00 51.42  ?  601 A1EKD B C2  1 
HETATM 5581 C  C23 . A1EKD E 2 .   ? -58.712 3.712   38.398  1.00 59.81  ?  601 A1EKD B C23 1 
HETATM 5582 C  C25 . A1EKD E 2 .   ? -53.097 1.411   34.301  1.00 41.09  ?  601 A1EKD B C25 1 
HETATM 5583 C  C27 . A1EKD E 2 .   ? -50.699 -1.690  34.677  1.00 50.21  ?  601 A1EKD B C27 1 
HETATM 5584 C  C29 . A1EKD E 2 .   ? -48.504 -7.511  31.696  1.00 37.64  ?  601 A1EKD B C29 1 
HETATM 5585 C  C3  . A1EKD E 2 .   ? -49.444 -5.585  32.656  1.00 45.33  ?  601 A1EKD B C3  1 
HETATM 5586 C  C30 . A1EKD E 2 .   ? -47.524 -6.786  31.061  1.00 45.21  ?  601 A1EKD B C30 1 
HETATM 5587 C  C9  . A1EKD E 2 .   ? -50.525 1.242   36.918  1.00 49.11  ?  601 A1EKD B C9  1 
HETATM 5588 F  F1  . A1EKD E 2 .   ? -46.543 -4.677  30.579  1.00 41.54  ?  601 A1EKD B F1  1 
HETATM 5589 F  F2  . A1EKD E 2 .   ? -59.467 3.874   34.295  1.00 47.83  ?  601 A1EKD B F2  1 
HETATM 5590 F  F3  . A1EKD E 2 .   ? -60.766 4.786   38.753  1.00 69.76  ?  601 A1EKD B F3  1 
HETATM 5591 F  F4  . A1EKD E 2 .   ? -48.529 -8.856  31.495  1.00 59.20  ?  601 A1EKD B F4  1 
HETATM 5592 N  N2  . A1EKD E 2 .   ? -49.014 -0.844  33.455  1.00 50.63  ?  601 A1EKD B N2  1 
HETATM 5593 N  N4  . A1EKD E 2 .   ? -56.984 2.665   35.330  1.00 44.86  ?  601 A1EKD B N4  1 
HETATM 5594 N  N5  . A1EKD E 2 .   ? -54.324 1.913   34.382  1.00 45.97  ?  601 A1EKD B N5  1 
HETATM 5595 N  N6  . A1EKD E 2 .   ? -48.546 -3.414  32.260  1.00 53.29  ?  601 A1EKD B N6  1 
HETATM 5596 O  O1  . A1EKD E 2 .   ? -48.005 -1.105  37.251  1.00 54.90  -1 601 A1EKD B O1  1 
HETATM 5597 O  O2  . A1EKD E 2 .   ? -49.871 -1.496  38.384  1.00 59.44  ?  601 A1EKD B O2  1 
HETATM 5598 O  O3  . A1EKD E 2 .   ? -53.756 0.986   37.732  1.00 45.29  ?  601 A1EKD B O3  1 
HETATM 5599 O  O4  . A1EKD E 2 .   ? -51.565 -2.611  35.095  1.00 48.14  ?  601 A1EKD B O4  1 
HETATM 5600 S  S1  . A1EKD E 2 .   ? -50.502 -4.562  33.583  1.00 45.60  ?  601 A1EKD B S1  1 
HETATM 5601 S  S2  . A1EKD E 2 .   ? -56.274 2.433   37.856  1.00 60.06  ?  601 A1EKD B S2  1 
HETATM 5602 ZN ZN  . ZN    F 3 .   ? -53.222 10.555  13.120  1.00 29.69  ?  602 ZN    B ZN  1 
HETATM 5603 O  O   . HOH   G 4 .   ? -16.812 15.291  -1.092  1.00 43.40  ?  701 HOH   A O   1 
HETATM 5604 O  O   . HOH   G 4 .   ? -8.782  -1.475  -2.573  1.00 54.30  ?  702 HOH   A O   1 
HETATM 5605 O  O   . HOH   G 4 .   ? -36.239 14.923  -17.757 1.00 32.24  ?  703 HOH   A O   1 
HETATM 5606 O  O   . HOH   G 4 .   ? -37.963 15.631  -16.008 1.00 34.25  ?  704 HOH   A O   1 
HETATM 5607 O  O   . HOH   G 4 .   ? -48.098 9.854   -7.644  1.00 42.08  ?  705 HOH   A O   1 
HETATM 5608 O  O   . HOH   G 4 .   ? -8.297  21.062  9.705   1.00 40.77  ?  706 HOH   A O   1 
HETATM 5609 O  O   . HOH   G 4 .   ? -45.200 17.730  8.061   1.00 31.95  ?  707 HOH   A O   1 
HETATM 5610 O  O   . HOH   G 4 .   ? -15.326 19.040  2.753   1.00 37.90  ?  708 HOH   A O   1 
HETATM 5611 O  O   . HOH   G 4 .   ? -27.874 16.959  19.334  1.00 39.61  ?  709 HOH   A O   1 
HETATM 5612 O  O   . HOH   G 4 .   ? -40.438 18.356  3.389   1.00 33.44  ?  710 HOH   A O   1 
HETATM 5613 O  O   . HOH   G 4 .   ? -17.140 33.345  10.660  1.00 48.30  ?  711 HOH   A O   1 
HETATM 5614 O  O   . HOH   G 4 .   ? -40.003 19.542  13.251  1.00 35.71  ?  712 HOH   A O   1 
HETATM 5615 O  O   . HOH   G 4 .   ? -30.958 18.309  -21.493 1.00 32.14  ?  713 HOH   A O   1 
HETATM 5616 O  O   . HOH   G 4 .   ? -37.222 -5.712  -2.399  1.00 52.54  ?  714 HOH   A O   1 
HETATM 5617 O  O   . HOH   G 4 .   ? -44.118 2.782   -1.556  1.00 30.89  ?  715 HOH   A O   1 
HETATM 5618 O  O   . HOH   G 4 .   ? -20.622 30.858  -7.553  1.00 46.49  ?  716 HOH   A O   1 
HETATM 5619 O  O   . HOH   G 4 .   ? -39.876 1.737   4.939   1.00 31.06  ?  717 HOH   A O   1 
HETATM 5620 O  O   . HOH   G 4 .   ? -29.761 21.546  -22.410 1.00 29.65  ?  718 HOH   A O   1 
HETATM 5621 O  O   . HOH   G 4 .   ? -21.720 11.902  3.227   1.00 43.32  ?  719 HOH   A O   1 
HETATM 5622 O  O   . HOH   G 4 .   ? -9.494  10.232  -19.230 1.00 54.79  ?  720 HOH   A O   1 
HETATM 5623 O  O   . HOH   G 4 .   ? -23.974 16.370  -25.099 1.00 32.73  ?  721 HOH   A O   1 
HETATM 5624 O  O   . HOH   G 4 .   ? -23.319 27.777  12.600  1.00 39.37  ?  722 HOH   A O   1 
HETATM 5625 O  O   . HOH   G 4 .   ? -7.418  31.887  7.082   1.00 65.57  ?  723 HOH   A O   1 
HETATM 5626 O  O   . HOH   G 4 .   ? -30.167 14.768  -22.650 1.00 28.12  ?  724 HOH   A O   1 
HETATM 5627 O  O   . HOH   G 4 .   ? -10.060 23.638  16.046  1.00 46.41  ?  725 HOH   A O   1 
HETATM 5628 O  O   . HOH   G 4 .   ? -32.313 19.982  -16.113 1.00 32.22  ?  726 HOH   A O   1 
HETATM 5629 O  O   . HOH   G 4 .   ? -30.353 20.204  17.029  1.00 35.24  ?  727 HOH   A O   1 
HETATM 5630 O  O   . HOH   G 4 .   ? -43.899 6.636   -9.798  1.00 36.69  ?  728 HOH   A O   1 
HETATM 5631 O  O   . HOH   G 4 .   ? -34.953 24.318  12.800  1.00 46.77  ?  729 HOH   A O   1 
HETATM 5632 O  O   . HOH   G 4 .   ? -27.037 27.759  6.290   1.00 33.58  ?  730 HOH   A O   1 
HETATM 5633 O  O   . HOH   G 4 .   ? -34.986 1.222   -5.111  1.00 29.34  ?  731 HOH   A O   1 
HETATM 5634 O  O   . HOH   G 4 .   ? -18.602 13.310  6.325   1.00 41.92  ?  732 HOH   A O   1 
HETATM 5635 O  O   . HOH   G 4 .   ? -47.017 9.079   -0.052  1.00 32.28  ?  733 HOH   A O   1 
HETATM 5636 O  O   . HOH   G 4 .   ? -37.171 19.997  13.408  1.00 36.26  ?  734 HOH   A O   1 
HETATM 5637 O  O   . HOH   G 4 .   ? -45.833 8.037   -13.148 1.00 54.45  ?  735 HOH   A O   1 
HETATM 5638 O  O   . HOH   G 4 .   ? -25.666 17.985  1.398   1.00 27.04  ?  736 HOH   A O   1 
HETATM 5639 O  O   . HOH   G 4 .   ? -40.277 14.305  17.301  1.00 36.73  ?  737 HOH   A O   1 
HETATM 5640 O  O   . HOH   G 4 .   ? -32.631 12.290  -27.598 1.00 37.52  ?  738 HOH   A O   1 
HETATM 5641 O  O   . HOH   G 4 .   ? -13.223 7.203   5.797   1.00 40.65  ?  739 HOH   A O   1 
HETATM 5642 O  O   . HOH   G 4 .   ? -18.359 21.207  -3.879  1.00 39.28  ?  740 HOH   A O   1 
HETATM 5643 O  O   . HOH   G 4 .   ? -34.150 7.007   -17.548 1.00 37.08  ?  741 HOH   A O   1 
HETATM 5644 O  O   . HOH   G 4 .   ? -36.031 20.243  -3.034  1.00 38.91  ?  742 HOH   A O   1 
HETATM 5645 O  O   . HOH   G 4 .   ? -20.363 18.787  22.765  1.00 50.26  ?  743 HOH   A O   1 
HETATM 5646 O  O   . HOH   G 4 .   ? -24.460 27.893  16.265  1.00 46.43  ?  744 HOH   A O   1 
HETATM 5647 O  O   . HOH   G 4 .   ? -33.595 11.334  18.640  1.00 37.40  ?  745 HOH   A O   1 
HETATM 5648 O  O   . HOH   G 4 .   ? -40.539 3.194   8.788   1.00 24.92  ?  746 HOH   A O   1 
HETATM 5649 O  O   . HOH   G 4 .   ? -23.095 33.087  7.468   1.00 57.39  ?  747 HOH   A O   1 
HETATM 5650 O  O   . HOH   G 4 .   ? -36.812 16.524  -11.740 1.00 39.22  ?  748 HOH   A O   1 
HETATM 5651 O  O   . HOH   G 4 .   ? -33.475 8.891   -19.035 1.00 37.02  ?  749 HOH   A O   1 
HETATM 5652 O  O   . HOH   G 4 .   ? -39.944 4.835   10.843  1.00 32.47  ?  750 HOH   A O   1 
HETATM 5653 O  O   . HOH   G 4 .   ? -39.720 11.375  -1.216  1.00 23.73  ?  751 HOH   A O   1 
HETATM 5654 O  O   . HOH   G 4 .   ? -43.954 4.448   14.102  1.00 29.83  ?  752 HOH   A O   1 
HETATM 5655 O  O   . HOH   G 4 .   ? -22.752 25.334  -15.588 1.00 35.00  ?  753 HOH   A O   1 
HETATM 5656 O  O   . HOH   G 4 .   ? -29.908 27.453  8.400   1.00 35.96  ?  754 HOH   A O   1 
HETATM 5657 O  O   . HOH   G 4 .   ? -23.491 30.637  -4.240  1.00 37.35  ?  755 HOH   A O   1 
HETATM 5658 O  O   . HOH   G 4 .   ? -10.875 2.525   0.686   1.00 46.37  ?  756 HOH   A O   1 
HETATM 5659 O  O   . HOH   G 4 .   ? -47.880 16.354  -1.348  1.00 51.69  ?  757 HOH   A O   1 
HETATM 5660 O  O   . HOH   G 4 .   ? -34.883 18.644  17.653  1.00 36.95  ?  758 HOH   A O   1 
HETATM 5661 O  O   . HOH   G 4 .   ? -12.714 33.137  10.987  1.00 50.94  ?  759 HOH   A O   1 
HETATM 5662 O  O   . HOH   G 4 .   ? -45.879 3.543   0.101   1.00 29.76  ?  760 HOH   A O   1 
HETATM 5663 O  O   . HOH   G 4 .   ? -40.269 4.494   5.177   1.00 25.84  ?  761 HOH   A O   1 
HETATM 5664 O  O   . HOH   G 4 .   ? -53.628 -4.991  -2.990  1.00 41.48  ?  762 HOH   A O   1 
HETATM 5665 O  O   . HOH   G 4 .   ? -32.048 18.102  -18.340 1.00 31.06  ?  763 HOH   A O   1 
HETATM 5666 O  O   . HOH   G 4 .   ? -44.316 3.515   -4.308  1.00 30.48  ?  764 HOH   A O   1 
HETATM 5667 O  O   . HOH   G 4 .   ? -40.534 4.839   -16.470 1.00 38.65  ?  765 HOH   A O   1 
HETATM 5668 O  O   . HOH   G 4 .   ? -13.539 14.284  -5.793  1.00 45.41  ?  766 HOH   A O   1 
HETATM 5669 O  O   . HOH   G 4 .   ? -33.080 20.432  3.171   1.00 29.53  ?  767 HOH   A O   1 
HETATM 5670 O  O   . HOH   G 4 .   ? -48.207 7.951   -2.146  1.00 31.82  ?  768 HOH   A O   1 
HETATM 5671 O  O   . HOH   G 4 .   ? -23.820 23.553  -17.296 1.00 35.78  ?  769 HOH   A O   1 
HETATM 5672 O  O   . HOH   G 4 .   ? -37.438 2.884   3.785   1.00 29.44  ?  770 HOH   A O   1 
HETATM 5673 O  O   . HOH   G 4 .   ? -39.699 1.952   -15.735 1.00 38.84  ?  771 HOH   A O   1 
HETATM 5674 O  O   . HOH   G 4 .   ? -14.799 6.643   -10.587 1.00 46.52  ?  772 HOH   A O   1 
HETATM 5675 O  O   . HOH   G 4 .   ? -16.157 12.426  6.428   1.00 47.21  ?  773 HOH   A O   1 
HETATM 5676 O  O   . HOH   G 4 .   ? -31.288 24.210  -16.286 1.00 31.22  ?  774 HOH   A O   1 
HETATM 5677 O  O   . HOH   G 4 .   ? -40.020 21.395  11.458  1.00 41.81  ?  775 HOH   A O   1 
HETATM 5678 O  O   . HOH   G 4 .   ? -36.096 2.219   -2.731  1.00 31.60  ?  776 HOH   A O   1 
HETATM 5679 O  O   . HOH   G 4 .   ? -31.310 25.572  -9.095  1.00 37.07  ?  777 HOH   A O   1 
HETATM 5680 O  O   . HOH   G 4 .   ? -35.522 20.668  15.578  1.00 40.22  ?  778 HOH   A O   1 
HETATM 5681 O  O   . HOH   G 4 .   ? -21.949 14.621  5.712   1.00 40.79  ?  779 HOH   A O   1 
HETATM 5682 O  O   . HOH   G 4 .   ? -35.725 8.652   8.264   1.00 29.39  ?  780 HOH   A O   1 
HETATM 5683 O  O   . HOH   G 4 .   ? -46.264 -4.631  5.160   1.00 36.44  ?  781 HOH   A O   1 
HETATM 5684 O  O   . HOH   G 4 .   ? -27.189 22.308  23.362  1.00 48.56  ?  782 HOH   A O   1 
HETATM 5685 O  O   . HOH   G 4 .   ? -24.029 30.450  -8.187  1.00 45.77  ?  783 HOH   A O   1 
HETATM 5686 O  O   . HOH   G 4 .   ? -33.724 1.502   8.507   1.00 42.59  ?  784 HOH   A O   1 
HETATM 5687 O  O   . HOH   G 4 .   ? -33.830 4.469   -19.127 1.00 46.98  ?  785 HOH   A O   1 
HETATM 5688 O  O   . HOH   G 4 .   ? -39.483 7.541   10.986  1.00 31.60  ?  786 HOH   A O   1 
HETATM 5689 O  O   . HOH   G 4 .   ? -35.559 19.379  -12.007 1.00 34.66  ?  787 HOH   A O   1 
HETATM 5690 O  O   . HOH   G 4 .   ? -38.522 21.500  -2.859  1.00 40.92  ?  788 HOH   A O   1 
HETATM 5691 O  O   . HOH   G 4 .   ? -47.916 3.996   -1.720  1.00 38.84  ?  789 HOH   A O   1 
HETATM 5692 O  O   . HOH   H 4 .   ? -50.449 -9.272  40.608  1.00 57.56  ?  701 HOH   B O   1 
HETATM 5693 O  O   . HOH   H 4 .   ? -30.032 4.199   35.504  1.00 55.95  ?  702 HOH   B O   1 
HETATM 5694 O  O   . HOH   H 4 .   ? -53.823 -2.267  35.596  1.00 47.96  ?  703 HOH   B O   1 
HETATM 5695 O  O   . HOH   H 4 .   ? -59.947 2.831   4.470   1.00 42.14  ?  704 HOH   B O   1 
HETATM 5696 O  O   . HOH   H 4 .   ? -29.883 -5.563  32.494  1.00 52.45  ?  705 HOH   B O   1 
HETATM 5697 O  O   . HOH   H 4 .   ? -70.670 -1.483  16.268  1.00 28.56  ?  706 HOH   B O   1 
HETATM 5698 O  O   . HOH   H 4 .   ? -42.059 -20.230 35.165  1.00 55.25  ?  707 HOH   B O   1 
HETATM 5699 O  O   . HOH   H 4 .   ? -68.250 -12.063 29.506  1.00 34.66  ?  708 HOH   B O   1 
HETATM 5700 O  O   . HOH   H 4 .   ? -51.844 10.424  41.270  1.00 48.98  ?  709 HOH   B O   1 
HETATM 5701 O  O   . HOH   H 4 .   ? -35.555 -7.220  22.161  1.00 38.80  ?  710 HOH   B O   1 
HETATM 5702 O  O   . HOH   H 4 .   ? -52.786 9.260   36.579  1.00 47.63  ?  711 HOH   B O   1 
HETATM 5703 O  O   . HOH   H 4 .   ? -42.466 1.309   30.958  1.00 40.55  ?  712 HOH   B O   1 
HETATM 5704 O  O   . HOH   H 4 .   ? -61.318 6.738   4.423   1.00 34.38  ?  713 HOH   B O   1 
HETATM 5705 O  O   . HOH   H 4 .   ? -52.409 4.251   5.364   1.00 30.74  ?  714 HOH   B O   1 
HETATM 5706 O  O   . HOH   H 4 .   ? -62.045 6.390   8.308   1.00 40.39  ?  715 HOH   B O   1 
HETATM 5707 O  O   . HOH   H 4 .   ? -36.963 -10.814 42.604  1.00 48.25  ?  716 HOH   B O   1 
HETATM 5708 O  O   . HOH   H 4 .   ? -49.485 -5.261  11.788  1.00 38.19  ?  717 HOH   B O   1 
HETATM 5709 O  O   . HOH   H 4 .   ? -59.348 15.840  21.098  1.00 43.80  ?  718 HOH   B O   1 
HETATM 5710 O  O   . HOH   H 4 .   ? -34.887 -5.559  17.480  1.00 37.91  ?  719 HOH   B O   1 
HETATM 5711 O  O   . HOH   H 4 .   ? -52.914 21.231  6.663   1.00 39.32  ?  720 HOH   B O   1 
HETATM 5712 O  O   . HOH   H 4 .   ? -39.739 -14.706 29.044  1.00 44.51  ?  721 HOH   B O   1 
HETATM 5713 O  O   . HOH   H 4 .   ? -51.963 -4.930  10.864  1.00 35.42  ?  722 HOH   B O   1 
HETATM 5714 O  O   . HOH   H 4 .   ? -44.448 -4.523  7.081   1.00 34.47  ?  723 HOH   B O   1 
HETATM 5715 O  O   . HOH   H 4 .   ? -52.236 9.671   6.212   1.00 28.61  ?  724 HOH   B O   1 
HETATM 5716 O  O   . HOH   H 4 .   ? -77.719 -3.022  28.476  1.00 36.94  ?  725 HOH   B O   1 
HETATM 5717 O  O   . HOH   H 4 .   ? -46.387 -14.709 25.324  1.00 39.01  ?  726 HOH   B O   1 
HETATM 5718 O  O   . HOH   H 4 .   ? -56.369 -7.860  33.853  1.00 36.58  ?  727 HOH   B O   1 
HETATM 5719 O  O   . HOH   H 4 .   ? -45.911 16.324  14.563  1.00 42.80  ?  728 HOH   B O   1 
HETATM 5720 O  O   . HOH   H 4 .   ? -38.323 8.509   8.538   1.00 28.30  ?  729 HOH   B O   1 
HETATM 5721 O  O   . HOH   H 4 .   ? -68.516 11.252  12.701  1.00 42.67  ?  730 HOH   B O   1 
HETATM 5722 O  O   . HOH   H 4 .   ? -47.517 11.260  12.578  1.00 32.51  ?  731 HOH   B O   1 
HETATM 5723 O  O   . HOH   H 4 .   ? -50.091 -6.001  36.471  1.00 48.99  ?  732 HOH   B O   1 
HETATM 5724 O  O   . HOH   H 4 .   ? -27.794 -0.764  39.397  1.00 58.06  ?  733 HOH   B O   1 
HETATM 5725 O  O   . HOH   H 4 .   ? -41.059 -12.401 50.715  1.00 63.29  ?  734 HOH   B O   1 
HETATM 5726 O  O   . HOH   H 4 .   ? -25.435 -5.309  38.059  1.00 60.15  ?  735 HOH   B O   1 
HETATM 5727 O  O   . HOH   H 4 .   ? -62.157 -9.898  20.196  1.00 39.86  ?  736 HOH   B O   1 
HETATM 5728 O  O   . HOH   H 4 .   ? -80.306 1.180   19.853  1.00 36.85  ?  737 HOH   B O   1 
HETATM 5729 O  O   . HOH   H 4 .   ? -43.735 10.026  12.087  1.00 28.32  ?  738 HOH   B O   1 
HETATM 5730 O  O   . HOH   H 4 .   ? -51.168 -4.851  26.682  1.00 30.05  ?  739 HOH   B O   1 
HETATM 5731 O  O   . HOH   H 4 .   ? -55.338 18.402  15.477  1.00 53.85  ?  740 HOH   B O   1 
HETATM 5732 O  O   . HOH   H 4 .   ? -43.309 0.916   42.237  1.00 43.33  ?  741 HOH   B O   1 
HETATM 5733 O  O   . HOH   H 4 .   ? -68.890 -2.365  14.593  1.00 30.79  ?  742 HOH   B O   1 
HETATM 5734 O  O   . HOH   H 4 .   ? -28.935 -3.116  31.305  1.00 48.35  ?  743 HOH   B O   1 
HETATM 5735 O  O   . HOH   H 4 .   ? -48.637 10.174  15.130  1.00 30.83  ?  744 HOH   B O   1 
HETATM 5736 O  O   . HOH   H 4 .   ? -57.008 9.530   8.236   1.00 32.63  ?  745 HOH   B O   1 
HETATM 5737 O  O   . HOH   H 4 .   ? -53.883 1.523   12.929  1.00 25.99  ?  746 HOH   B O   1 
HETATM 5738 O  O   . HOH   H 4 .   ? -64.586 -3.547  15.892  1.00 39.32  ?  747 HOH   B O   1 
HETATM 5739 O  O   . HOH   H 4 .   ? -68.977 -6.764  20.081  1.00 27.77  ?  748 HOH   B O   1 
HETATM 5740 O  O   . HOH   H 4 .   ? -57.639 11.751  17.238  1.00 29.66  ?  749 HOH   B O   1 
HETATM 5741 O  O   . HOH   H 4 .   ? -38.859 -7.226  15.286  1.00 34.04  ?  750 HOH   B O   1 
HETATM 5742 O  O   . HOH   H 4 .   ? -46.613 -1.596  30.475  1.00 46.56  ?  751 HOH   B O   1 
HETATM 5743 O  O   . HOH   H 4 .   ? -49.018 0.861   31.022  1.00 49.53  ?  752 HOH   B O   1 
HETATM 5744 O  O   . HOH   H 4 .   ? -71.598 4.566   18.976  1.00 37.80  ?  753 HOH   B O   1 
HETATM 5745 O  O   . HOH   H 4 .   ? -44.509 -14.234 22.522  1.00 45.41  ?  754 HOH   B O   1 
HETATM 5746 O  O   . HOH   H 4 .   ? -70.235 6.350   18.304  1.00 34.81  ?  755 HOH   B O   1 
HETATM 5747 O  O   . HOH   H 4 .   ? -47.468 8.632   12.267  1.00 22.17  ?  756 HOH   B O   1 
HETATM 5748 O  O   . HOH   H 4 .   ? -49.635 -7.528  19.387  1.00 31.15  ?  757 HOH   B O   1 
HETATM 5749 O  O   . HOH   H 4 .   ? -43.471 -7.902  44.393  1.00 45.07  ?  758 HOH   B O   1 
HETATM 5750 O  O   . HOH   H 4 .   ? -47.369 17.525  6.161   1.00 35.44  ?  759 HOH   B O   1 
HETATM 5751 O  O   . HOH   H 4 .   ? -54.665 5.022   4.279   1.00 31.73  ?  760 HOH   B O   1 
HETATM 5752 O  O   . HOH   H 4 .   ? -70.854 -5.145  20.647  1.00 38.09  ?  761 HOH   B O   1 
HETATM 5753 O  O   . HOH   H 4 .   ? -55.366 10.875  16.339  1.00 31.48  ?  762 HOH   B O   1 
HETATM 5754 O  O   . HOH   H 4 .   ? -47.645 5.217   33.149  1.00 48.80  ?  763 HOH   B O   1 
HETATM 5755 O  O   . HOH   H 4 .   ? -70.232 -10.122 28.805  1.00 33.69  ?  764 HOH   B O   1 
HETATM 5756 O  O   . HOH   H 4 .   ? -36.941 -7.701  16.961  1.00 43.00  ?  765 HOH   B O   1 
HETATM 5757 O  O   . HOH   H 4 .   ? -44.358 4.431   16.825  1.00 27.66  ?  766 HOH   B O   1 
HETATM 5758 O  O   . HOH   H 4 .   ? -25.833 5.523   50.309  1.00 59.50  ?  767 HOH   B O   1 
HETATM 5759 O  O   . HOH   H 4 .   ? -43.888 9.045   19.561  1.00 37.24  ?  768 HOH   B O   1 
HETATM 5760 O  O   . HOH   H 4 .   ? -48.990 14.178  14.345  1.00 39.98  ?  769 HOH   B O   1 
HETATM 5761 O  O   . HOH   H 4 .   ? -39.290 -11.202 17.557  1.00 42.89  ?  770 HOH   B O   1 
HETATM 5762 O  O   . HOH   H 4 .   ? -41.877 5.943   17.625  1.00 44.03  ?  771 HOH   B O   1 
HETATM 5763 O  O   . HOH   H 4 .   ? -69.011 -10.998 21.309  1.00 28.25  ?  772 HOH   B O   1 
HETATM 5764 O  O   . HOH   H 4 .   ? -55.364 -7.356  16.573  1.00 43.42  ?  773 HOH   B O   1 
HETATM 5765 O  O   . HOH   H 4 .   ? -41.528 8.021   12.343  1.00 28.85  ?  774 HOH   B O   1 
HETATM 5766 O  O   . HOH   H 4 .   ? -62.636 6.024   37.324  1.00 43.01  ?  775 HOH   B O   1 
HETATM 5767 O  O   . HOH   H 4 .   ? -71.892 8.734   18.236  1.00 47.69  ?  776 HOH   B O   1 
HETATM 5768 O  O   . HOH   H 4 .   ? -41.565 5.673   12.921  1.00 36.13  ?  777 HOH   B O   1 
HETATM 5769 O  O   . HOH   H 4 .   ? -65.057 -6.029  16.658  1.00 42.46  ?  778 HOH   B O   1 
HETATM 5770 O  O   . HOH   H 4 .   ? -53.694 12.993  16.551  1.00 35.83  ?  779 HOH   B O   1 
HETATM 5771 O  O   . HOH   H 4 .   ? -57.577 17.033  14.370  1.00 44.23  ?  780 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   ? 0.6935 0.7457 0.5913 -0.1037 0.0780  -0.0763 161 GLY   A N   
2    C  CA  . GLY   A 5   ? 0.6823 0.7153 0.5896 -0.0956 0.0859  -0.0843 161 GLY   A CA  
3    C  C   . GLY   A 5   ? 0.6261 0.6400 0.5440 -0.0861 0.0818  -0.0836 161 GLY   A C   
4    O  O   . GLY   A 5   ? 0.7098 0.7110 0.6406 -0.0766 0.0852  -0.0848 161 GLY   A O   
5    N  N   . ALA   A 6   ? 0.6498 0.6631 0.5627 -0.0886 0.0745  -0.0809 162 ALA   A N   
6    C  CA  . ALA   A 6   ? 0.6259 0.6222 0.5477 -0.0801 0.0702  -0.0796 162 ALA   A CA  
7    C  C   . ALA   A 6   ? 0.6927 0.6691 0.6156 -0.0776 0.0799  -0.0914 162 ALA   A C   
8    O  O   . ALA   A 6   ? 0.6083 0.5705 0.5436 -0.0674 0.0792  -0.0896 162 ALA   A O   
9    C  CB  . ALA   A 6   ? 0.6701 0.6706 0.5847 -0.0847 0.0622  -0.0759 162 ALA   A CB  
10   N  N   . SER   A 7   ? 0.6275 0.6026 0.5372 -0.0871 0.0893  -0.1033 163 SER   A N   
11   C  CA  . SER   A 7   ? 0.6496 0.6045 0.5603 -0.0848 0.1006  -0.1151 163 SER   A CA  
12   C  C   . SER   A 7   ? 0.6531 0.6020 0.5794 -0.0737 0.1061  -0.1137 163 SER   A C   
13   O  O   . SER   A 7   ? 0.5411 0.4724 0.4774 -0.0650 0.1102  -0.1160 163 SER   A O   
14   C  CB  . SER   A 7   ? 0.6716 0.6278 0.5646 -0.0981 0.1110  -0.1287 163 SER   A CB  
15   O  OG  . SER   A 7   ? 0.7264 0.6875 0.6055 -0.1089 0.1061  -0.1306 163 SER   A OG  
16   N  N   . LYS   A 8   ? 0.5362 0.5006 0.4651 -0.0739 0.1064  -0.1094 164 LYS   A N   
17   C  CA  . LYS   A 8   ? 0.6173 0.5793 0.5621 -0.0638 0.1111  -0.1071 164 LYS   A CA  
18   C  C   . LYS   A 8   ? 0.6204 0.5766 0.5823 -0.0519 0.1019  -0.0965 164 LYS   A C   
19   O  O   . LYS   A 8   ? 0.5469 0.4939 0.5227 -0.0423 0.1061  -0.0963 164 LYS   A O   
20   C  CB  . LYS   A 8   ? 0.5466 0.5281 0.4898 -0.0678 0.1122  -0.1036 164 LYS   A CB  
21   C  CG  . LYS   A 8   ? 0.6273 0.6098 0.5858 -0.0593 0.1183  -0.1019 164 LYS   A CG  
22   C  CD  . LYS   A 8   ? 0.6362 0.6382 0.5888 -0.0662 0.1216  -0.1007 164 LYS   A CD  
23   C  CE  . LYS   A 8   ? 0.7281 0.7336 0.6960 -0.0587 0.1282  -0.0989 164 LYS   A CE  
24   N  NZ  . LYS   A 8   ? 0.7287 0.7533 0.6895 -0.0663 0.1322  -0.0982 164 LYS   A NZ  
25   N  N   . LEU   A 9   ? 0.5695 0.5313 0.5304 -0.0525 0.0896  -0.0875 165 LEU   A N   
26   C  CA  . LEU   A 9   ? 0.5305 0.4860 0.5051 -0.0426 0.0810  -0.0788 165 LEU   A CA  
27   C  C   . LEU   A 9   ? 0.5403 0.4766 0.5180 -0.0374 0.0838  -0.0835 165 LEU   A C   
28   O  O   . LEU   A 9   ? 0.4741 0.4029 0.4658 -0.0277 0.0829  -0.0797 165 LEU   A O   
29   C  CB  . LEU   A 9   ? 0.4774 0.4414 0.4485 -0.0451 0.0690  -0.0697 165 LEU   A CB  
30   C  CG  . LEU   A 9   ? 0.4928 0.4754 0.4615 -0.0497 0.0649  -0.0625 165 LEU   A CG  
31   C  CD1 . LEU   A 9   ? 0.4521 0.4393 0.4190 -0.0503 0.0540  -0.0536 165 LEU   A CD1 
32   C  CD2 . LEU   A 9   ? 0.4520 0.4399 0.4340 -0.0441 0.0657  -0.0573 165 LEU   A CD2 
33   N  N   . ARG   A 10  ? 0.4707 0.3995 0.4353 -0.0444 0.0870  -0.0913 166 ARG   A N   
34   C  CA  . ARG   A 10  ? 0.5967 0.5060 0.5630 -0.0406 0.0911  -0.0963 166 ARG   A CA  
35   C  C   . ARG   A 10  ? 0.5906 0.4889 0.5652 -0.0347 0.1035  -0.1026 166 ARG   A C   
36   O  O   . ARG   A 10  ? 0.5624 0.4469 0.5476 -0.0258 0.1051  -0.1011 166 ARG   A O   
37   C  CB  . ARG   A 10  ? 0.6400 0.5449 0.5895 -0.0513 0.0928  -0.1041 166 ARG   A CB  
38   C  CG  . ARG   A 10  ? 0.6589 0.5749 0.6028 -0.0554 0.0806  -0.0965 166 ARG   A CG  
39   C  CD  . ARG   A 10  ? 0.7224 0.6363 0.6513 -0.0659 0.0807  -0.1026 166 ARG   A CD  
40   N  NE  . ARG   A 10  ? 0.7831 0.7015 0.7128 -0.0646 0.0692  -0.0937 166 ARG   A NE  
41   C  CZ  . ARG   A 10  ? 0.7759 0.7122 0.7016 -0.0689 0.0613  -0.0868 166 ARG   A CZ  
42   N  NH1 . ARG   A 10  ? 0.7189 0.6711 0.6383 -0.0755 0.0628  -0.0871 166 ARG   A NH1 
43   N  NH2 . ARG   A 10  ? 0.6861 0.6244 0.6146 -0.0659 0.0520  -0.0788 166 ARG   A NH2 
44   N  N   . ALA   A 11  ? 0.5443 0.4491 0.5146 -0.0392 0.1127  -0.1092 167 ALA   A N   
45   C  CA  . ALA   A 11  ? 0.5936 0.4898 0.5735 -0.0326 0.1253  -0.1145 167 ALA   A CA  
46   C  C   . ALA   A 11  ? 0.6174 0.5166 0.6182 -0.0197 0.1210  -0.1039 167 ALA   A C   
47   O  O   . ALA   A 11  ? 0.5190 0.4060 0.5322 -0.0103 0.1265  -0.1038 167 ALA   A O   
48   C  CB  . ALA   A 11  ? 0.5021 0.4086 0.4738 -0.0400 0.1348  -0.1221 167 ALA   A CB  
49   N  N   . VAL   A 12  ? 0.5235 0.4395 0.5288 -0.0195 0.1113  -0.0946 168 VAL   A N   
50   C  CA  . VAL   A 12  ? 0.5600 0.4807 0.5841 -0.0091 0.1058  -0.0845 168 VAL   A CA  
51   C  C   . VAL   A 12  ? 0.4887 0.3970 0.5200 -0.0018 0.0998  -0.0797 168 VAL   A C   
52   O  O   . VAL   A 12  ? 0.5629 0.4654 0.6088 0.0078  0.1030  -0.0769 168 VAL   A O   
53   C  CB  . VAL   A 12  ? 0.5804 0.5188 0.6056 -0.0119 0.0954  -0.0756 168 VAL   A CB  
54   C  CG1 . VAL   A 12  ? 0.4737 0.4157 0.5169 -0.0027 0.0883  -0.0655 168 VAL   A CG1 
55   C  CG2 . VAL   A 12  ? 0.5691 0.5207 0.5895 -0.0180 0.1021  -0.0789 168 VAL   A CG2 
56   N  N   . LEU   A 13  ? 0.5060 0.4110 0.5270 -0.0064 0.0914  -0.0784 169 LEU   A N   
57   C  CA  . LEU   A 13  ? 0.4773 0.3718 0.5034 -0.0005 0.0850  -0.0735 169 LEU   A CA  
58   C  C   . LEU   A 13  ? 0.5699 0.4467 0.5996 0.0045  0.0948  -0.0788 169 LEU   A C   
59   O  O   . LEU   A 13  ? 0.5769 0.4475 0.6188 0.0136  0.0927  -0.0728 169 LEU   A O   
60   C  CB  . LEU   A 13  ? 0.5358 0.4303 0.5489 -0.0073 0.0762  -0.0725 169 LEU   A CB  
61   C  CG  . LEU   A 13  ? 0.4541 0.3636 0.4662 -0.0100 0.0654  -0.0649 169 LEU   A CG  
62   C  CD1 . LEU   A 13  ? 0.4556 0.3659 0.4538 -0.0174 0.0598  -0.0655 169 LEU   A CD1 
63   C  CD2 . LEU   A 13  ? 0.4850 0.3957 0.5105 -0.0019 0.0569  -0.0555 169 LEU   A CD2 
64   N  N   . GLU   A 14  ? 0.5173 0.3858 0.5366 -0.0014 0.1061  -0.0899 170 GLU   A N   
65   C  CA  . GLU   A 14  ? 0.5804 0.4300 0.6037 0.0034  0.1178  -0.0957 170 GLU   A CA  
66   C  C   . GLU   A 14  ? 0.6156 0.4663 0.6589 0.0155  0.1232  -0.0908 170 GLU   A C   
67   O  O   . GLU   A 14  ? 0.6803 0.5205 0.7352 0.0248  0.1243  -0.0860 170 GLU   A O   
68   C  CB  . GLU   A 14  ? 0.6498 0.4916 0.6585 -0.0060 0.1306  -0.1098 170 GLU   A CB  
69   C  CG  . GLU   A 14  ? 0.6867 0.5226 0.6761 -0.0180 0.1286  -0.1165 170 GLU   A CG  
70   C  CD  . GLU   A 14  ? 0.8661 0.7012 0.8390 -0.0302 0.1398  -0.1305 170 GLU   A CD  
71   O  OE1 . GLU   A 14  ? 0.9013 0.7342 0.8773 -0.0286 0.1521  -0.1371 170 GLU   A OE1 
72   O  OE2 . GLU   A 14  ? 0.9217 0.7590 0.8782 -0.0420 0.1365  -0.1352 170 GLU   A OE2 
73   N  N   . LYS   A 15  ? 0.5868 0.4512 0.6346 0.0154  0.1268  -0.0913 171 LYS   A N   
74   C  CA  . LYS   A 15  ? 0.6431 0.5121 0.7109 0.0264  0.1320  -0.0863 171 LYS   A CA  
75   C  C   . LYS   A 15  ? 0.6584 0.5338 0.7414 0.0351  0.1200  -0.0728 171 LYS   A C   
76   O  O   . LYS   A 15  ? 0.6861 0.5567 0.7850 0.0457  0.1235  -0.0676 171 LYS   A O   
77   C  CB  . LYS   A 15  ? 0.6792 0.5653 0.7478 0.0229  0.1356  -0.0880 171 LYS   A CB  
78   C  CG  . LYS   A 15  ? 0.6919 0.5887 0.7820 0.0332  0.1383  -0.0808 171 LYS   A CG  
79   C  CD  . LYS   A 15  ? 0.7064 0.6191 0.7954 0.0286  0.1436  -0.0839 171 LYS   A CD  
80   C  CE  . LYS   A 15  ? 0.6506 0.5813 0.7366 0.0228  0.1298  -0.0763 171 LYS   A CE  
81   N  NZ  . LYS   A 15  ? 0.8028 0.7430 0.8732 0.0115  0.1326  -0.0825 171 LYS   A NZ  
82   N  N   . LEU   A 16  ? 0.5596 0.4460 0.6378 0.0305  0.1062  -0.0668 172 LEU   A N   
83   C  CA  . LEU   A 16  ? 0.6840 0.5773 0.7747 0.0371  0.0947  -0.0550 172 LEU   A CA  
84   C  C   . LEU   A 16  ? 0.6581 0.5370 0.7516 0.0428  0.0929  -0.0518 172 LEU   A C   
85   O  O   . LEU   A 16  ? 0.7290 0.6110 0.8376 0.0516  0.0892  -0.0429 172 LEU   A O   
86   C  CB  . LEU   A 16  ? 0.6210 0.5258 0.7040 0.0302  0.0816  -0.0508 172 LEU   A CB  
87   C  CG  . LEU   A 16  ? 0.6826 0.6033 0.7660 0.0256  0.0824  -0.0511 172 LEU   A CG  
88   C  CD1 . LEU   A 16  ? 0.5730 0.5023 0.6475 0.0185  0.0708  -0.0473 172 LEU   A CD1 
89   C  CD2 . LEU   A 16  ? 0.6413 0.5731 0.7443 0.0332  0.0843  -0.0450 172 LEU   A CD2 
90   N  N   . LYS   A 17  ? 0.7440 0.6080 0.8229 0.0376  0.0954  -0.0586 173 LYS   A N   
91   C  CA  . LYS   A 17  ? 0.7039 0.5530 0.7841 0.0422  0.0945  -0.0558 173 LYS   A CA  
92   C  C   . LYS   A 17  ? 0.7461 0.5843 0.8401 0.0520  0.1067  -0.0557 173 LYS   A C   
93   O  O   . LYS   A 17  ? 0.7752 0.6094 0.8806 0.0607  0.1041  -0.0471 173 LYS   A O   
94   C  CB  . LYS   A 17  ? 0.6539 0.4906 0.7153 0.0330  0.0950  -0.0635 173 LYS   A CB  
95   N  N   . LEU   A 18  ? 0.7005 0.5340 0.7935 0.0509  0.1204  -0.0648 174 LEU   A N   
96   C  CA  . LEU   A 18  ? 0.7090 0.5323 0.8167 0.0612  0.1335  -0.0646 174 LEU   A CA  
97   C  C   . LEU   A 18  ? 0.7682 0.6064 0.8983 0.0727  0.1292  -0.0519 174 LEU   A C   
98   O  O   . LEU   A 18  ? 0.7881 0.6199 0.9325 0.0832  0.1315  -0.0442 174 LEU   A O   
99   C  CB  . LEU   A 18  ? 0.7022 0.5215 0.8050 0.0574  0.1488  -0.0771 174 LEU   A CB  
100  C  CG  . LEU   A 18  ? 0.8449 0.6402 0.9353 0.0527  0.1616  -0.0893 174 LEU   A CG  
101  C  CD1 . LEU   A 18  ? 0.7710 0.5582 0.8438 0.0433  0.1530  -0.0915 174 LEU   A CD1 
102  C  CD2 . LEU   A 18  ? 0.6320 0.4277 0.7129 0.0454  0.1743  -0.1027 174 LEU   A CD2 
103  N  N   . SER   A 19  ? 0.7568 0.6158 0.8909 0.0705  0.1233  -0.0490 175 SER   A N   
104  C  CA  . SER   A 19  ? 0.7669 0.6432 0.9219 0.0796  0.1184  -0.0371 175 SER   A CA  
105  C  C   . SER   A 19  ? 0.7425 0.6205 0.9037 0.0843  0.1059  -0.0254 175 SER   A C   
106  O  O   . SER   A 19  ? 0.7968 0.6821 0.9771 0.0945  0.1054  -0.0151 175 SER   A O   
107  C  CB  . SER   A 19  ? 0.7198 0.6172 0.8746 0.0737  0.1120  -0.0361 175 SER   A CB  
108  O  OG  . SER   A 19  ? 0.7888 0.6918 0.9498 0.0751  0.1243  -0.0413 175 SER   A OG  
109  N  N   . ARG   A 20  ? 0.7427 0.6154 0.8882 0.0769  0.0960  -0.0264 176 ARG   A N   
110  C  CA  . ARG   A 20  ? 0.7380 0.6121 0.8868 0.0802  0.0843  -0.0162 176 ARG   A CA  
111  C  C   . ARG   A 20  ? 0.7845 0.6413 0.9382 0.0879  0.0906  -0.0133 176 ARG   A C   
112  O  O   . ARG   A 20  ? 0.8804 0.7420 1.0459 0.0953  0.0846  -0.0017 176 ARG   A O   
113  C  CB  . ARG   A 20  ? 0.6660 0.5400 0.7966 0.0700  0.0729  -0.0186 176 ARG   A CB  
114  N  N   . ASP   A 21  ? 0.7782 0.6153 0.9229 0.0858  0.1026  -0.0232 177 ASP   A N   
115  C  CA  . ASP   A 21  ? 0.7523 0.5706 0.9026 0.0934  0.1105  -0.0206 177 ASP   A CA  
116  C  C   . ASP   A 21  ? 0.7594 0.5826 0.9337 0.1070  0.1177  -0.0117 177 ASP   A C   
117  O  O   . ASP   A 21  ? 0.9017 0.7190 1.0867 0.1159  0.1176  -0.0018 177 ASP   A O   
118  C  CB  . ASP   A 21  ? 0.7809 0.5768 0.9176 0.0877  0.1239  -0.0344 177 ASP   A CB  
119  C  CG  . ASP   A 21  ? 0.8907 0.6814 1.0048 0.0747  0.1173  -0.0419 177 ASP   A CG  
120  O  OD1 . ASP   A 21  ? 0.9535 0.7457 1.0636 0.0736  0.1058  -0.0352 177 ASP   A OD1 
121  O  OD2 . ASP   A 21  ? 0.9469 0.7334 1.0475 0.0656  0.1237  -0.0543 177 ASP   A OD2 
122  N  N   . ASP   A 22  ? 0.7855 0.6196 0.9689 0.1091  0.1244  -0.0145 178 ASP   A N   
123  C  CA  . ASP   A 22  ? 0.8024 0.6414 1.0093 0.1222  0.1338  -0.0075 178 ASP   A CA  
124  C  C   . ASP   A 22  ? 0.7760 0.6419 1.0007 0.1279  0.1221  0.0070  178 ASP   A C   
125  O  O   . ASP   A 22  ? 0.7737 0.6512 1.0181 0.1368  0.1287  0.0122  178 ASP   A O   
126  C  CB  . ASP   A 22  ? 0.7880 0.6238 0.9950 0.1212  0.1493  -0.0192 178 ASP   A CB  
127  N  N   . ILE   A 23  ? 0.7616 0.6380 0.9797 0.1227  0.1054  0.0132  179 ILE   A N   
128  C  CA  . ILE   A 23  ? 0.7230 0.6252 0.9557 0.1258  0.0934  0.0259  179 ILE   A CA  
129  C  C   . ILE   A 23  ? 0.7760 0.6799 1.0111 0.1291  0.0822  0.0379  179 ILE   A C   
130  O  O   . ILE   A 23  ? 0.8007 0.7256 1.0492 0.1327  0.0726  0.0499  179 ILE   A O   
131  C  CB  . ILE   A 23  ? 0.6599 0.5777 0.8825 0.1146  0.0835  0.0215  179 ILE   A CB  
132  N  N   . SER   A 24  ? 0.6992 0.5820 0.9207 0.1271  0.0832  0.0347  180 SER   A N   
133  C  CA  . SER   A 24  ? 0.7191 0.6014 0.9424 0.1307  0.0743  0.0462  180 SER   A CA  
134  C  C   . SER   A 24  ? 0.7040 0.6008 0.9524 0.1436  0.0744  0.0622  180 SER   A C   
135  O  O   . SER   A 24  ? 0.6960 0.6097 0.9497 0.1445  0.0615  0.0741  180 SER   A O   
136  C  CB  . SER   A 24  ? 0.7336 0.5880 0.9452 0.1305  0.0819  0.0412  180 SER   A CB  
137  N  N   . THR   A 25  ? 0.6627 0.5537 0.9269 0.1537  0.0892  0.0626  181 THR   A N   
138  C  CA  . THR   A 25  ? 0.6357 0.5417 0.9258 0.1669  0.0908  0.0782  181 THR   A CA  
139  C  C   . THR   A 25  ? 0.6698 0.6084 0.9720 0.1660  0.0790  0.0866  181 THR   A C   
140  O  O   . THR   A 25  ? 0.6287 0.5854 0.9441 0.1712  0.0696  0.1021  181 THR   A O   
141  C  CB  . THR   A 25  ? 0.6111 0.5080 0.9077 0.1724  0.1076  0.0728  181 THR   A CB  
142  O  OG1 . THR   A 25  ? 0.8011 0.6702 1.0830 0.1704  0.1159  0.0656  181 THR   A OG1 
143  C  CG2 . THR   A 25  ? 0.6458 0.5619 0.9647 0.1830  0.1077  0.0878  181 THR   A CG2 
144  N  N   . ALA   A 26  ? 0.6212 0.5686 0.9186 0.1584  0.0792  0.0769  182 ALA   A N   
145  C  CA  . ALA   A 26  ? 0.5969 0.5746 0.9041 0.1555  0.0681  0.0837  182 ALA   A CA  
146  C  C   . ALA   A 26  ? 0.5175 0.5056 0.8143 0.1475  0.0499  0.0894  182 ALA   A C   
147  O  O   . ALA   A 26  ? 0.5100 0.5219 0.8202 0.1497  0.0400  0.1022  182 ALA   A O   
148  C  CB  . ALA   A 26  ? 0.5756 0.5572 0.8758 0.1471  0.0715  0.0712  182 ALA   A CB  
149  N  N   . ALA   A 27  ? 0.4685 0.4396 0.7412 0.1378  0.0456  0.0799  183 ALA   A N   
150  C  CA  . ALA   A 27  ? 0.5543 0.5332 0.8156 0.1301  0.0296  0.0840  183 ALA   A CA  
151  C  C   . ALA   A 27  ? 0.5541 0.5394 0.8262 0.1382  0.0243  0.0995  183 ALA   A C   
152  O  O   . ALA   A 27  ? 0.5626 0.5657 0.8343 0.1341  0.0106  0.1075  183 ALA   A O   
153  C  CB  . ALA   A 27  ? 0.5427 0.5005 0.7781 0.1204  0.0280  0.0719  183 ALA   A CB  
154  N  N   . GLY   A 28  ? 0.5098 0.4807 0.7913 0.1493  0.0354  0.1040  184 GLY   A N   
155  C  CA  . GLY   A 28  ? 0.5041 0.4827 0.7988 0.1585  0.0314  0.1209  184 GLY   A CA  
156  C  C   . GLY   A 28  ? 0.4653 0.4756 0.7838 0.1645  0.0261  0.1351  184 GLY   A C   
157  O  O   . GLY   A 28  ? 0.6225 0.6517 0.9456 0.1644  0.0137  0.1481  184 GLY   A O   
158  N  N   . MET   A 29  ? 0.4207 0.4386 0.7551 0.1697  0.0355  0.1332  185 MET   A N   
159  C  CA  . MET   A 29  ? 0.4872 0.5378 0.8449 0.1744  0.0304  0.1462  185 MET   A CA  
160  C  C   . MET   A 29  ? 0.5065 0.5798 0.8555 0.1612  0.0130  0.1466  185 MET   A C   
161  O  O   . MET   A 29  ? 0.3993 0.4987 0.7602 0.1622  0.0020  0.1608  185 MET   A O   
162  C  CB  . MET   A 29  ? 0.4180 0.4720 0.7907 0.1798  0.0438  0.1410  185 MET   A CB  
163  C  CG  . MET   A 29  ? 0.4473 0.4811 0.8239 0.1892  0.0614  0.1381  185 MET   A CG  
164  S  SD  . MET   A 29  ? 0.9133 0.9467 1.2994 0.1995  0.0644  0.1528  185 MET   A SD  
165  C  CE  . MET   A 29  ? 0.6356 0.7059 1.0329 0.1985  0.0448  0.1723  185 MET   A CE  
166  N  N   . VAL   A 30  ? 0.4446 0.5083 0.7728 0.1485  0.0105  0.1312  186 VAL   A N   
167  C  CA  . VAL   A 30  ? 0.4464 0.5278 0.7650 0.1354  -0.0045 0.1298  186 VAL   A CA  
168  C  C   . VAL   A 30  ? 0.4361 0.5216 0.7452 0.1316  -0.0176 0.1374  186 VAL   A C   
169  O  O   . VAL   A 30  ? 0.4925 0.6032 0.8069 0.1270  -0.0299 0.1462  186 VAL   A O   
170  C  CB  . VAL   A 30  ? 0.4025 0.4690 0.7003 0.1237  -0.0031 0.1122  186 VAL   A CB  
171  C  CG1 . VAL   A 30  ? 0.4324 0.5122 0.7183 0.1101  -0.0179 0.1103  186 VAL   A CG1 
172  C  CG2 . VAL   A 30  ? 0.4467 0.5153 0.7548 0.1263  0.0082  0.1063  186 VAL   A CG2 
173  N  N   . LYS   A 31  ? 0.4961 0.5574 0.7904 0.1327  -0.0150 0.1341  187 LYS   A N   
174  C  CA  . LYS   A 31  ? 0.4892 0.5533 0.7726 0.1286  -0.0267 0.1406  187 LYS   A CA  
175  C  C   . LYS   A 31  ? 0.4861 0.5743 0.7895 0.1368  -0.0324 0.1602  187 LYS   A C   
176  O  O   . LYS   A 31  ? 0.5652 0.6702 0.8637 0.1306  -0.0458 0.1673  187 LYS   A O   
177  C  CB  . LYS   A 31  ? 0.4887 0.5232 0.7558 0.1298  -0.0213 0.1352  187 LYS   A CB  
178  C  CG  . LYS   A 31  ? 0.6219 0.6531 0.8662 0.1185  -0.0329 0.1312  187 LYS   A CG  
179  C  CD  . LYS   A 31  ? 0.5974 0.6169 0.8358 0.1228  -0.0335 0.1387  187 LYS   A CD  
180  C  CE  . LYS   A 31  ? 0.7093 0.7260 0.9242 0.1110  -0.0443 0.1335  187 LYS   A CE  
181  N  NZ  . LYS   A 31  ? 0.6845 0.7258 0.8975 0.1015  -0.0573 0.1347  187 LYS   A NZ  
182  N  N   . GLY   A 32  ? 0.4215 0.5123 0.7477 0.1508  -0.0221 0.1693  188 GLY   A N   
183  C  CA  . GLY   A 32  ? 0.5074 0.6218 0.8547 0.1601  -0.0269 0.1898  188 GLY   A CA  
184  C  C   . GLY   A 32  ? 0.5742 0.7252 0.9344 0.1551  -0.0377 0.1972  188 GLY   A C   
185  O  O   . GLY   A 32  ? 0.5069 0.6812 0.8700 0.1526  -0.0498 0.2097  188 GLY   A O   
186  N  N   . VAL   A 33  ? 0.4535 0.6101 0.8198 0.1524  -0.0331 0.1887  189 VAL   A N   
187  C  CA  . VAL   A 33  ? 0.4611 0.6515 0.8380 0.1453  -0.0433 0.1937  189 VAL   A CA  
188  C  C   . VAL   A 33  ? 0.4374 0.6337 0.7921 0.1285  -0.0587 0.1880  189 VAL   A C   
189  O  O   . VAL   A 33  ? 0.4938 0.7178 0.8534 0.1235  -0.0715 0.1988  189 VAL   A O   
190  C  CB  . VAL   A 33  ? 0.4273 0.6193 0.8129 0.1449  -0.0342 0.1843  189 VAL   A CB  
191  C  CG1 . VAL   A 33  ? 0.4450 0.6680 0.8361 0.1339  -0.0453 0.1862  189 VAL   A CG1 
192  C  CG2 . VAL   A 33  ? 0.4043 0.5984 0.8161 0.1621  -0.0202 0.1931  189 VAL   A CG2 
193  N  N   . VAL   A 34  ? 0.3733 0.5437 0.7033 0.1195  -0.0572 0.1712  190 VAL   A N   
194  C  CA  . VAL   A 34  ? 0.5129 0.6853 0.8212 0.1035  -0.0697 0.1636  190 VAL   A CA  
195  C  C   . VAL   A 34  ? 0.5175 0.6966 0.8179 0.1018  -0.0803 0.1733  190 VAL   A C   
196  O  O   . VAL   A 34  ? 0.4928 0.6911 0.7869 0.0906  -0.0932 0.1754  190 VAL   A O   
197  C  CB  . VAL   A 34  ? 0.4553 0.5970 0.7406 0.0968  -0.0641 0.1449  190 VAL   A CB  
198  C  CG1 . VAL   A 34  ? 0.4174 0.5563 0.6792 0.0825  -0.0754 0.1377  190 VAL   A CG1 
199  C  CG2 . VAL   A 34  ? 0.4698 0.6113 0.7612 0.0950  -0.0567 0.1360  190 VAL   A CG2 
200  N  N   . ASP   A 35  ? 0.5076 0.6710 0.8077 0.1119  -0.0749 0.1791  191 ASP   A N   
201  C  CA  . ASP   A 35  ? 0.5026 0.6739 0.7964 0.1109  -0.0846 0.1900  191 ASP   A CA  
202  C  C   . ASP   A 35  ? 0.4457 0.6551 0.7598 0.1131  -0.0940 0.2084  191 ASP   A C   
203  O  O   . ASP   A 35  ? 0.5797 0.8072 0.8850 0.1035  -0.1073 0.2131  191 ASP   A O   
204  C  CB  . ASP   A 35  ? 0.4976 0.6452 0.7901 0.1224  -0.0758 0.1943  191 ASP   A CB  
205  C  CG  . ASP   A 35  ? 0.5548 0.6680 0.8229 0.1172  -0.0700 0.1772  191 ASP   A CG  
206  O  OD1 . ASP   A 35  ? 0.6134 0.7217 0.8637 0.1046  -0.0745 0.1635  191 ASP   A OD1 
207  O  OD2 . ASP   A 35  ? 0.6931 0.7839 0.9606 0.1259  -0.0605 0.1780  191 ASP   A OD2 
208  N  N   . HIS   A 36  ? 0.5054 0.7282 0.8469 0.1254  -0.0871 0.2188  192 HIS   A N   
209  C  CA  . HIS   A 36  ? 0.5122 0.7704 0.8698 0.1252  -0.0941 0.2328  192 HIS   A CA  
210  C  C   . HIS   A 36  ? 0.5605 0.8453 0.9155 0.1099  -0.1078 0.2301  192 HIS   A C   
211  O  O   . HIS   A 36  ? 0.4872 0.7958 0.8382 0.1015  -0.1196 0.2375  192 HIS   A O   
212  C  CB  . HIS   A 36  ? 0.5697 0.8326 0.9504 0.1373  -0.0814 0.2372  192 HIS   A CB  
213  C  CG  . HIS   A 36  ? 0.6238 0.8758 1.0118 0.1508  -0.0714 0.2465  192 HIS   A CG  
214  N  ND1 . HIS   A 36  ? 0.6355 0.8699 1.0356 0.1632  -0.0548 0.2440  192 HIS   A ND1 
215  C  CD2 . HIS   A 36  ? 0.6532 0.9120 1.0396 0.1533  -0.0755 0.2589  192 HIS   A CD2 
216  C  CE1 . HIS   A 36  ? 0.6500 0.8787 1.0551 0.1727  -0.0491 0.2540  192 HIS   A CE1 
217  N  NE2 . HIS   A 36  ? 0.6332 0.8769 1.0308 0.1672  -0.0615 0.2637  192 HIS   A NE2 
218  N  N   . LEU   A 37  ? 0.4213 0.6985 0.7736 0.1037  -0.1038 0.2159  193 LEU   A N   
219  C  CA  . LEU   A 37  ? 0.4735 0.7697 0.8196 0.0872  -0.1142 0.2095  193 LEU   A CA  
220  C  C   . LEU   A 37  ? 0.4135 0.7084 0.7341 0.0728  -0.1266 0.2047  193 LEU   A C   
221  O  O   . LEU   A 37  ? 0.4393 0.7625 0.7603 0.0624  -0.1393 0.2109  193 LEU   A O   
222  C  CB  . LEU   A 37  ? 0.4000 0.6784 0.7402 0.0823  -0.1059 0.1922  193 LEU   A CB  
223  C  CG  . LEU   A 37  ? 0.4160 0.7114 0.7817 0.0885  -0.0990 0.1963  193 LEU   A CG  
224  C  CD1 . LEU   A 37  ? 0.4575 0.7368 0.8140 0.0809  -0.0927 0.1791  193 LEU   A CD1 
225  C  CD2 . LEU   A 37  ? 0.4836 0.8209 0.8658 0.0828  -0.1109 0.2096  193 LEU   A CD2 
226  N  N   . LEU   A 38  ? 0.3781 0.6407 0.6760 0.0716  -0.1228 0.1937  194 LEU   A N   
227  C  CA  . LEU   A 38  ? 0.4014 0.6596 0.6737 0.0581  -0.1329 0.1872  194 LEU   A CA  
228  C  C   . LEU   A 38  ? 0.4524 0.7345 0.7269 0.0580  -0.1438 0.2035  194 LEU   A C   
229  O  O   . LEU   A 38  ? 0.4211 0.7160 0.6807 0.0439  -0.1554 0.2014  194 LEU   A O   
230  C  CB  . LEU   A 38  ? 0.3846 0.6049 0.6351 0.0590  -0.1255 0.1740  194 LEU   A CB  
231  C  CG  . LEU   A 38  ? 0.5107 0.7083 0.7527 0.0547  -0.1174 0.1560  194 LEU   A CG  
232  C  CD1 . LEU   A 38  ? 0.3697 0.5323 0.5942 0.0581  -0.1092 0.1458  194 LEU   A CD1 
233  C  CD2 . LEU   A 38  ? 0.3782 0.5834 0.6077 0.0377  -0.1256 0.1458  194 LEU   A CD2 
234  N  N   . LEU   A 39  ? 0.4543 0.7424 0.7465 0.0734  -0.1400 0.2199  195 LEU   A N   
235  C  CA  . LEU   A 39  ? 0.4518 0.7633 0.7450 0.0728  -0.1497 0.2357  195 LEU   A CA  
236  C  C   . LEU   A 39  ? 0.4500 0.7968 0.7515 0.0634  -0.1582 0.2408  195 LEU   A C   
237  O  O   . LEU   A 39  ? 0.5148 0.8783 0.8028 0.0510  -0.1694 0.2425  195 LEU   A O   
238  C  CB  . LEU   A 39  ? 0.5173 0.8196 0.8214 0.0895  -0.1396 0.2474  195 LEU   A CB  
239  C  CG  . LEU   A 39  ? 0.6044 0.8714 0.9026 0.1004  -0.1289 0.2443  195 LEU   A CG  
240  C  CD1 . LEU   A 39  ? 0.6159 0.8720 0.9348 0.1167  -0.1135 0.2481  195 LEU   A CD1 
241  C  CD2 . LEU   A 39  ? 0.6749 0.9382 0.9589 0.1002  -0.1329 0.2518  195 LEU   A CD2 
242  N  N   . ARG   A 40  ? 0.4421 0.8005 0.7650 0.0687  -0.1525 0.2432  196 ARG   A N   
243  C  CA  . ARG   A 40  ? 0.4359 0.8278 0.7671 0.0591  -0.1602 0.2477  196 ARG   A CA  
244  C  C   . ARG   A 40  ? 0.4434 0.8427 0.7573 0.0387  -0.1716 0.2356  196 ARG   A C   
245  O  O   . ARG   A 40  ? 0.4699 0.8904 0.7747 0.0259  -0.1819 0.2380  196 ARG   A O   
246  C  CB  . ARG   A 40  ? 0.4058 0.8066 0.7625 0.0682  -0.1511 0.2509  196 ARG   A CB  
247  N  N   . LEU   A 41  ? 0.3973 0.7782 0.7060 0.0348  -0.1693 0.2221  197 LEU   A N   
248  C  CA  . LEU   A 41  ? 0.4177 0.7983 0.7073 0.0149  -0.1770 0.2074  197 LEU   A CA  
249  C  C   . LEU   A 41  ? 0.4098 0.7885 0.6736 0.0030  -0.1870 0.2043  197 LEU   A C   
250  O  O   . LEU   A 41  ? 0.4488 0.8429 0.7013 -0.0145 -0.1970 0.1990  197 LEU   A O   
251  C  CB  . LEU   A 41  ? 0.3852 0.7302 0.6631 0.0136  -0.1661 0.1879  197 LEU   A CB  
252  C  CG  . LEU   A 41  ? 0.5343 0.8808 0.8285 0.0154  -0.1586 0.1832  197 LEU   A CG  
253  C  CD1 . LEU   A 41  ? 0.4618 0.8328 0.7565 -0.0021 -0.1681 0.1802  197 LEU   A CD1 
254  C  CD2 . LEU   A 41  ? 0.5271 0.8887 0.8512 0.0327  -0.1519 0.1984  197 LEU   A CD2 
255  N  N   . LYS   A 42  ? 0.3661 0.7246 0.6189 0.0114  -0.1837 0.2062  198 LYS   A N   
256  C  CA  . LYS   A 42  ? 0.4063 0.7627 0.6338 0.0001  -0.1923 0.2027  198 LYS   A CA  
257  C  C   . LYS   A 42  ? 0.4485 0.8372 0.6759 -0.0071 -0.2021 0.2141  198 LYS   A C   
258  O  O   . LYS   A 42  ? 0.4316 0.8214 0.6364 -0.0195 -0.2095 0.2093  198 LYS   A O   
259  C  CB  . LYS   A 42  ? 0.3636 0.6915 0.5791 0.0105  -0.1858 0.2027  198 LYS   A CB  
260  C  CG  . LYS   A 42  ? 0.5305 0.8687 0.7652 0.0275  -0.1836 0.2230  198 LYS   A CG  
261  C  CD  . LYS   A 42  ? 0.6344 0.9588 0.8526 0.0306  -0.1840 0.2270  198 LYS   A CD  
262  C  CE  . LYS   A 42  ? 0.5280 0.8752 0.7316 0.0177  -0.1947 0.2310  198 LYS   A CE  
263  N  NZ  . LYS   A 42  ? 0.6096 0.9826 0.8297 0.0233  -0.1953 0.2471  198 LYS   A NZ  
264  N  N   . CYS   A 43  ? 0.3812 0.7924 0.6305 0.0001  -0.2002 0.2267  199 CYS   A N   
265  C  CA  . CYS   A 43  ? 0.4212 0.8615 0.6698 -0.0072 -0.2078 0.2363  199 CYS   A CA  
266  C  C   . CYS   A 43  ? 0.4724 0.9329 0.7171 -0.0256 -0.2153 0.2287  199 CYS   A C   
267  O  O   . CYS   A 43  ? 0.5018 0.9844 0.7392 -0.0362 -0.2230 0.2329  199 CYS   A O   
268  C  CB  . CYS   A 43  ? 0.4044 0.8608 0.6784 0.0084  -0.2025 0.2544  199 CYS   A CB  
269  S  SG  . CYS   A 43  ? 0.5500 0.9853 0.8283 0.0288  -0.1935 0.2655  199 CYS   A SG  
270  N  N   . ASP   A 44  ? 0.3938 0.8477 0.6442 -0.0294 -0.2126 0.2182  200 ASP   A N   
271  C  CA  . ASP   A 44  ? 0.4829 0.9507 0.7276 -0.0481 -0.2187 0.2085  200 ASP   A CA  
272  C  C   . ASP   A 44  ? 0.4747 0.9282 0.6888 -0.0653 -0.2246 0.1931  200 ASP   A C   
273  O  O   . ASP   A 44  ? 0.4037 0.8305 0.6054 -0.0630 -0.2219 0.1846  200 ASP   A O   
274  C  CB  . ASP   A 44  ? 0.4104 0.8739 0.6715 -0.0460 -0.2129 0.2027  200 ASP   A CB  
275  C  CG  . ASP   A 44  ? 0.5244 1.0049 0.7842 -0.0640 -0.2179 0.1952  200 ASP   A CG  
276  O  OD1 . ASP   A 44  ? 0.5440 1.0166 0.7810 -0.0816 -0.2233 0.1816  200 ASP   A OD1 
277  O  OD2 . ASP   A 44  ? 0.5272 1.0285 0.8081 -0.0609 -0.2161 0.2030  200 ASP   A OD2 
278  N  N   . SER   A 45  ? 0.4148 0.8858 0.6163 -0.0826 -0.2323 0.1897  201 SER   A N   
279  C  CA  . SER   A 45  ? 0.4804 0.9371 0.6517 -0.0991 -0.2366 0.1743  201 SER   A CA  
280  C  C   . SER   A 45  ? 0.4554 0.8872 0.6183 -0.1069 -0.2334 0.1564  201 SER   A C   
281  O  O   . SER   A 45  ? 0.4606 0.8691 0.6012 -0.1129 -0.2332 0.1442  201 SER   A O   
282  C  CB  . SER   A 45  ? 0.4456 0.9255 0.6059 -0.1165 -0.2442 0.1733  201 SER   A CB  
283  O  OG  . SER   A 45  ? 0.4464 0.9388 0.6163 -0.1263 -0.2449 0.1689  201 SER   A OG  
284  N  N   . ALA   A 46  ? 0.4069 0.8428 0.5874 -0.1066 -0.2303 0.1547  202 ALA   A N   
285  C  CA  . ALA   A 46  ? 0.5155 0.9277 0.6891 -0.1141 -0.2268 0.1385  202 ALA   A CA  
286  C  C   . ALA   A 46  ? 0.5183 0.8982 0.6893 -0.0994 -0.2181 0.1352  202 ALA   A C   
287  O  O   . ALA   A 46  ? 0.4713 0.8185 0.6226 -0.1044 -0.2122 0.1184  202 ALA   A O   
288  C  CB  . ALA   A 46  ? 0.5077 0.9316 0.7015 -0.1164 -0.2242 0.1385  202 ALA   A CB  
289  N  N   . PHE   A 47  ? 0.4720 0.8547 0.6607 -0.0798 -0.2137 0.1491  203 PHE   A N   
290  C  CA  . PHE   A 47  ? 0.4580 0.8057 0.6454 -0.0641 -0.2010 0.1442  203 PHE   A CA  
291  C  C   . PHE   A 47  ? 0.5011 0.8377 0.6775 -0.0550 -0.2008 0.1496  203 PHE   A C   
292  O  O   . PHE   A 47  ? 0.4730 0.7907 0.6557 -0.0388 -0.1916 0.1526  203 PHE   A O   
293  C  CB  . PHE   A 47  ? 0.4370 0.7904 0.6525 -0.0487 -0.1932 0.1531  203 PHE   A CB  
294  C  CG  . PHE   A 47  ? 0.4509 0.8079 0.6754 -0.0564 -0.1907 0.1457  203 PHE   A CG  
295  C  CD1 . PHE   A 47  ? 0.4513 0.7768 0.6636 -0.0597 -0.1824 0.1290  203 PHE   A CD1 
296  C  CD2 . PHE   A 47  ? 0.5575 0.9509 0.8029 -0.0607 -0.1969 0.1560  203 PHE   A CD2 
297  C  CE1 . PHE   A 47  ? 0.5094 0.8380 0.7298 -0.0670 -0.1799 0.1229  203 PHE   A CE1 
298  C  CE2 . PHE   A 47  ? 0.5844 0.9813 0.8381 -0.0684 -0.1944 0.1494  203 PHE   A CE2 
299  C  CZ  . PHE   A 47  ? 0.3892 0.7531 0.6301 -0.0715 -0.1858 0.1329  203 PHE   A CZ  
300  N  N   . ARG   A 48  ? 0.5105 0.8586 0.6698 -0.0662 -0.2105 0.1504  204 ARG   A N   
301  C  CA  . ARG   A 48  ? 0.5045 0.8490 0.6553 -0.0585 -0.2119 0.1587  204 ARG   A CA  
302  C  C   . ARG   A 48  ? 0.4535 0.7573 0.5908 -0.0496 -0.2008 0.1482  204 ARG   A C   
303  O  O   . ARG   A 48  ? 0.4482 0.7443 0.5888 -0.0360 -0.1971 0.1572  204 ARG   A O   
304  C  CB  . ARG   A 48  ? 0.5088 0.8698 0.6390 -0.0750 -0.2237 0.1578  204 ARG   A CB  
305  N  N   . GLY   A 49  ? 0.4276 0.7056 0.5497 -0.0575 -0.1955 0.1295  205 GLY   A N   
306  C  CA  . GLY   A 49  ? 0.5347 0.7763 0.6430 -0.0506 -0.1858 0.1192  205 GLY   A CA  
307  C  C   . GLY   A 49  ? 0.4863 0.7084 0.6075 -0.0398 -0.1744 0.1148  205 GLY   A C   
308  O  O   . GLY   A 49  ? 0.4580 0.6508 0.5668 -0.0393 -0.1666 0.1018  205 GLY   A O   
309  N  N   . VAL   A 50  ? 0.4370 0.6765 0.5831 -0.0312 -0.1732 0.1257  206 VAL   A N   
310  C  CA  . VAL   A 50  ? 0.4127 0.6357 0.5713 -0.0211 -0.1621 0.1219  206 VAL   A CA  
311  C  C   . VAL   A 50  ? 0.4714 0.6717 0.6286 -0.0064 -0.1534 0.1240  206 VAL   A C   
312  O  O   . VAL   A 50  ? 0.4251 0.6319 0.5839 0.0004  -0.1559 0.1354  206 VAL   A O   
313  C  CB  . VAL   A 50  ? 0.3424 0.5914 0.5283 -0.0161 -0.1625 0.1331  206 VAL   A CB  
314  C  CG1 . VAL   A 50  ? 0.3969 0.6617 0.5998 -0.0022 -0.1631 0.1512  206 VAL   A CG1 
315  C  CG2 . VAL   A 50  ? 0.4505 0.6832 0.6455 -0.0105 -0.1516 0.1254  206 VAL   A CG2 
316  N  N   . GLY   A 51  ? 0.4082 0.5823 0.5625 -0.0020 -0.1431 0.1135  207 GLY   A N   
317  C  CA  . GLY   A 51  ? 0.3734 0.5246 0.5256 0.0104  -0.1341 0.1135  207 GLY   A CA  
318  C  C   . GLY   A 51  ? 0.4540 0.5851 0.6093 0.0147  -0.1233 0.1038  207 GLY   A C   
319  O  O   . GLY   A 51  ? 0.3927 0.5261 0.5503 0.0080  -0.1227 0.0968  207 GLY   A O   
320  N  N   . LEU   A 52  ? 0.4286 0.5403 0.5838 0.0255  -0.1145 0.1037  208 LEU   A N   
321  C  CA  . LEU   A 52  ? 0.4809 0.5713 0.6347 0.0286  -0.1041 0.0934  208 LEU   A CA  
322  C  C   . LEU   A 52  ? 0.5363 0.6072 0.6677 0.0198  -0.1042 0.0800  208 LEU   A C   
323  O  O   . LEU   A 52  ? 0.6589 0.7241 0.7753 0.0163  -0.1083 0.0790  208 LEU   A O   
324  C  CB  . LEU   A 52  ? 0.4378 0.5138 0.5980 0.0419  -0.0944 0.0970  208 LEU   A CB  
325  C  CG  . LEU   A 52  ? 0.5566 0.6461 0.7412 0.0521  -0.0897 0.1067  208 LEU   A CG  
326  C  CD1 . LEU   A 52  ? 0.6803 0.7500 0.8692 0.0638  -0.0775 0.1062  208 LEU   A CD1 
327  C  CD2 . LEU   A 52  ? 0.5197 0.6197 0.7131 0.0472  -0.0889 0.1021  208 LEU   A CD2 
328  N  N   . LEU   A 53  ? 0.5797 0.6410 0.7093 0.0163  -0.0993 0.0702  209 LEU   A N   
329  C  CA  . LEU   A 53  ? 0.5038 0.5458 0.6140 0.0094  -0.0981 0.0584  209 LEU   A CA  
330  C  C   . LEU   A 53  ? 0.7542 0.7751 0.8558 0.0164  -0.0911 0.0555  209 LEU   A C   
331  O  O   . LEU   A 53  ? 0.7826 0.7949 0.8697 0.0143  -0.0934 0.0537  209 LEU   A O   
332  C  CB  . LEU   A 53  ? 0.4993 0.5382 0.6108 0.0036  -0.0952 0.0503  209 LEU   A CB  
333  C  CG  . LEU   A 53  ? 0.5817 0.6002 0.6752 -0.0020 -0.0928 0.0390  209 LEU   A CG  
334  C  CD1 . LEU   A 53  ? 0.6607 0.6786 0.7395 -0.0087 -0.0996 0.0374  209 LEU   A CD1 
335  C  CD2 . LEU   A 53  ? 0.4936 0.5115 0.5883 -0.0093 -0.0916 0.0327  209 LEU   A CD2 
336  N  N   . ASN   A 54  ? 0.7353 0.7482 0.8455 0.0243  -0.0823 0.0550  210 ASN   A N   
337  C  CA  . ASN   A 54  ? 0.7813 0.7746 0.8837 0.0299  -0.0752 0.0517  210 ASN   A CA  
338  C  C   . ASN   A 54  ? 0.7822 0.7768 0.8903 0.0383  -0.0746 0.0614  210 ASN   A C   
339  O  O   . ASN   A 54  ? 0.9231 0.9040 1.0318 0.0450  -0.0667 0.0608  210 ASN   A O   
340  C  CB  . ASN   A 54  ? 0.7703 0.7538 0.8775 0.0335  -0.0655 0.0462  210 ASN   A CB  
341  C  CG  . ASN   A 54  ? 0.7766 0.7558 0.8766 0.0258  -0.0652 0.0372  210 ASN   A CG  
342  O  OD1 . ASN   A 54  ? 0.8111 0.7829 0.8969 0.0194  -0.0685 0.0317  210 ASN   A OD1 
343  N  ND2 . ASN   A 54  ? 0.7519 0.7358 0.8622 0.0266  -0.0607 0.0359  210 ASN   A ND2 
344  N  N   . TYR   A 59  ? 0.5790 0.5861 0.7562 0.0665  -0.0383 0.0653  215 TYR   A N   
345  C  CA  . TYR   A 59  ? 0.6066 0.6200 0.7939 0.0668  -0.0321 0.0619  215 TYR   A CA  
346  C  C   . TYR   A 59  ? 0.6965 0.6950 0.8692 0.0605  -0.0274 0.0495  215 TYR   A C   
347  O  O   . TYR   A 59  ? 0.7421 0.7240 0.8988 0.0579  -0.0270 0.0437  215 TYR   A O   
348  C  CB  . TYR   A 59  ? 0.7020 0.7156 0.9064 0.0783  -0.0215 0.0667  215 TYR   A CB  
349  C  CG  . TYR   A 59  ? 0.7308 0.7206 0.9269 0.0827  -0.0108 0.0601  215 TYR   A CG  
350  C  CD1 . TYR   A 59  ? 0.6805 0.6603 0.8771 0.0895  -0.0088 0.0654  215 TYR   A CD1 
351  C  CD2 . TYR   A 59  ? 0.7075 0.6857 0.8959 0.0795  -0.0026 0.0490  215 TYR   A CD2 
352  C  CE1 . TYR   A 59  ? 0.7537 0.7109 0.9424 0.0923  0.0012  0.0589  215 TYR   A CE1 
353  C  CE2 . TYR   A 59  ? 0.6661 0.6236 0.8462 0.0820  0.0071  0.0424  215 TYR   A CE2 
354  C  CZ  . TYR   A 59  ? 0.7533 0.6998 0.9337 0.0882  0.0091  0.0470  215 TYR   A CZ  
355  O  OH  . TYR   A 59  ? 0.8660 0.7912 1.0379 0.0896  0.0189  0.0400  215 TYR   A OH  
356  N  N   . GLU   A 60  ? 0.6846 0.6904 0.8636 0.0582  -0.0238 0.0464  216 GLU   A N   
357  C  CA  . GLU   A 60  ? 0.6786 0.6736 0.8459 0.0526  -0.0191 0.0363  216 GLU   A CA  
358  C  C   . GLU   A 60  ? 0.5834 0.5872 0.7633 0.0546  -0.0113 0.0354  216 GLU   A C   
359  O  O   . GLU   A 60  ? 0.5633 0.5833 0.7608 0.0591  -0.0110 0.0426  216 GLU   A O   
360  C  CB  . GLU   A 60  ? 0.6654 0.6608 0.8203 0.0423  -0.0278 0.0328  216 GLU   A CB  
361  C  CG  . GLU   A 60  ? 0.7490 0.7261 0.8846 0.0385  -0.0275 0.0255  216 GLU   A CG  
362  C  CD  . GLU   A 60  ? 0.8814 0.8497 1.0108 0.0368  -0.0193 0.0180  216 GLU   A CD  
363  O  OE1 . GLU   A 60  ? 0.8724 0.8458 1.0116 0.0400  -0.0120 0.0177  216 GLU   A OE1 
364  O  OE2 . GLU   A 60  ? 0.9794 0.9367 1.0942 0.0323  -0.0201 0.0126  216 GLU   A OE2 
365  N  N   . HIS   A 61  ? 0.6176 0.6120 0.7885 0.0513  -0.0046 0.0271  217 HIS   A N   
366  C  CA  . HIS   A 61  ? 0.5686 0.5699 0.7484 0.0523  0.0039  0.0249  217 HIS   A CA  
367  C  C   . HIS   A 61  ? 0.5869 0.5905 0.7580 0.0428  0.0013  0.0204  217 HIS   A C   
368  O  O   . HIS   A 61  ? 0.6720 0.6629 0.8277 0.0385  0.0027  0.0139  217 HIS   A O   
369  C  CB  . HIS   A 61  ? 0.5029 0.4908 0.6798 0.0574  0.0163  0.0191  217 HIS   A CB  
370  C  CG  . HIS   A 61  ? 0.5082 0.4935 0.6967 0.0678  0.0214  0.0239  217 HIS   A CG  
371  N  ND1 . HIS   A 61  ? 0.6271 0.5994 0.8093 0.0709  0.0197  0.0252  217 HIS   A ND1 
372  C  CD2 . HIS   A 61  ? 0.5546 0.5487 0.7616 0.0761  0.0287  0.0286  217 HIS   A CD2 
373  C  CE1 . HIS   A 61  ? 0.5774 0.5497 0.7736 0.0808  0.0258  0.0308  217 HIS   A CE1 
374  N  NE2 . HIS   A 61  ? 0.5848 0.5703 0.7966 0.0845  0.0315  0.0329  217 HIS   A NE2 
375  N  N   . VAL   A 62  ? 0.5175 0.5376 0.6990 0.0393  -0.0025 0.0244  218 VAL   A N   
376  C  CA  . VAL   A 62  ? 0.5989 0.6206 0.7736 0.0305  -0.0041 0.0210  218 VAL   A CA  
377  C  C   . VAL   A 62  ? 0.5850 0.6034 0.7569 0.0307  0.0066  0.0156  218 VAL   A C   
378  O  O   . VAL   A 62  ? 0.5259 0.5390 0.6863 0.0244  0.0069  0.0115  218 VAL   A O   
379  C  CB  . VAL   A 62  ? 0.5724 0.6126 0.7595 0.0260  -0.0102 0.0267  218 VAL   A CB  
380  C  CG1 . VAL   A 62  ? 0.4939 0.5409 0.6858 0.0265  -0.0198 0.0326  218 VAL   A CG1 
381  C  CG2 . VAL   A 62  ? 0.5734 0.6287 0.7774 0.0297  -0.0028 0.0296  218 VAL   A CG2 
382  N  N   . LYS   A 63  ? 0.4941 0.5154 0.6762 0.0380  0.0158  0.0156  219 LYS   A N   
383  C  CA  . LYS   A 63  ? 0.4782 0.4969 0.6576 0.0382  0.0271  0.0098  219 LYS   A CA  
384  C  C   . LYS   A 63  ? 0.5542 0.5566 0.7259 0.0433  0.0345  0.0043  219 LYS   A C   
385  O  O   . LYS   A 63  ? 0.4758 0.4772 0.6580 0.0518  0.0394  0.0065  219 LYS   A O   
386  C  CB  . LYS   A 63  ? 0.4821 0.5172 0.6798 0.0421  0.0336  0.0132  219 LYS   A CB  
387  C  CG  . LYS   A 63  ? 0.6232 0.6739 0.8266 0.0351  0.0294  0.0166  219 LYS   A CG  
388  C  CD  . LYS   A 63  ? 0.5875 0.6493 0.8006 0.0366  0.0402  0.0156  219 LYS   A CD  
389  C  CE  . LYS   A 63  ? 0.5866 0.6672 0.8228 0.0425  0.0411  0.0232  219 LYS   A CE  
390  N  NZ  . LYS   A 63  ? 0.5825 0.6725 0.8278 0.0451  0.0535  0.0214  219 LYS   A NZ  
391  N  N   . ILE   A 64  ? 0.5424 0.5324 0.6962 0.0381  0.0357  -0.0025 220 ILE   A N   
392  C  CA  . ILE   A 64  ? 0.5171 0.4911 0.6617 0.0409  0.0426  -0.0087 220 ILE   A CA  
393  C  C   . ILE   A 64  ? 0.5428 0.5168 0.6953 0.0462  0.0561  -0.0123 220 ILE   A C   
394  O  O   . ILE   A 64  ? 0.6063 0.5679 0.7583 0.0514  0.0629  -0.0154 220 ILE   A O   
395  C  CB  . ILE   A 64  ? 0.6156 0.5804 0.7403 0.0329  0.0414  -0.0149 220 ILE   A CB  
396  C  CG1 . ILE   A 64  ? 0.6517 0.6001 0.7660 0.0343  0.0421  -0.0186 220 ILE   A CG1 
397  C  CG2 . ILE   A 64  ? 0.5851 0.5530 0.7041 0.0285  0.0503  -0.0209 220 ILE   A CG2 
398  C  CD1 . ILE   A 64  ? 0.5629 0.5051 0.6596 0.0267  0.0392  -0.0230 220 ILE   A CD1 
399  N  N   . SER   A 65  ? 0.5546 0.5418 0.7150 0.0451  0.0607  -0.0120 221 SER   A N   
400  C  CA  . SER   A 65  ? 0.5844 0.5724 0.7518 0.0496  0.0746  -0.0163 221 SER   A CA  
401  C  C   . SER   A 65  ? 0.5789 0.5768 0.7691 0.0596  0.0776  -0.0091 221 SER   A C   
402  O  O   . SER   A 65  ? 0.6028 0.6032 0.8020 0.0646  0.0898  -0.0117 221 SER   A O   
403  C  CB  . SER   A 65  ? 0.6631 0.6608 0.8253 0.0424  0.0791  -0.0202 221 SER   A CB  
404  O  OG  . SER   A 65  ? 0.5027 0.5175 0.6745 0.0397  0.0718  -0.0128 221 SER   A OG  
405  N  N   . ALA   A 66  ? 0.5529 0.5569 0.7525 0.0628  0.0671  0.0000  222 ALA   A N   
406  C  CA  . ALA   A 66  ? 0.5701 0.5866 0.7922 0.0721  0.0680  0.0089  222 ALA   A CA  
407  C  C   . ALA   A 66  ? 0.6398 0.6467 0.8639 0.0785  0.0635  0.0138  222 ALA   A C   
408  O  O   . ALA   A 66  ? 0.5421 0.5572 0.7702 0.0778  0.0514  0.0216  222 ALA   A O   
409  C  CB  . ALA   A 66  ? 0.5372 0.5757 0.7705 0.0684  0.0586  0.0168  222 ALA   A CB  
410  N  N   . PRO   A 67  ? 0.6131 0.6026 0.8341 0.0843  0.0733  0.0092  223 PRO   A N   
411  C  CA  . PRO   A 67  ? 0.6292 0.6071 0.8494 0.0894  0.0692  0.0136  223 PRO   A CA  
412  C  C   . PRO   A 67  ? 0.5850 0.5769 0.8266 0.0987  0.0650  0.0267  223 PRO   A C   
413  O  O   . PRO   A 67  ? 0.6264 0.6147 0.8665 0.1005  0.0569  0.0327  223 PRO   A O   
414  C  CB  . PRO   A 67  ? 0.6859 0.6423 0.9000 0.0933  0.0834  0.0052  223 PRO   A CB  
415  C  CG  . PRO   A 67  ? 0.6518 0.6135 0.8726 0.0947  0.0962  -0.0003 223 PRO   A CG  
416  C  CD  . PRO   A 67  ? 0.6683 0.6471 0.8856 0.0857  0.0890  -0.0006 223 PRO   A CD  
417  N  N   . ASN   A 68  ? 0.5547 0.5635 0.8161 0.1045  0.0702  0.0318  224 ASN   A N   
418  C  CA  . ASN   A 68  ? 0.5855 0.6108 0.8694 0.1138  0.0667  0.0455  224 ASN   A CA  
419  C  C   . ASN   A 68  ? 0.5657 0.6148 0.8553 0.1076  0.0519  0.0535  224 ASN   A C   
420  O  O   . ASN   A 68  ? 0.5300 0.5967 0.8379 0.1137  0.0470  0.0656  224 ASN   A O   
421  C  CB  . ASN   A 68  ? 0.5793 0.6119 0.8839 0.1241  0.0810  0.0476  224 ASN   A CB  
422  C  CG  . ASN   A 68  ? 0.6726 0.6808 0.9733 0.1308  0.0968  0.0398  224 ASN   A CG  
423  O  OD1 . ASN   A 68  ? 0.7616 0.7661 1.0637 0.1320  0.1104  0.0319  224 ASN   A OD1 
424  N  ND2 . ASN   A 68  ? 0.7144 0.7052 1.0093 0.1344  0.0956  0.0416  224 ASN   A ND2 
425  N  N   . GLU   A 69  ? 0.5359 0.5859 0.8106 0.0956  0.0451  0.0473  225 GLU   A N   
426  C  CA  . GLU   A 69  ? 0.4689 0.5381 0.7463 0.0879  0.0318  0.0529  225 GLU   A CA  
427  C  C   . GLU   A 69  ? 0.4390 0.4986 0.6997 0.0817  0.0197  0.0525  225 GLU   A C   
428  O  O   . GLU   A 69  ? 0.4398 0.4838 0.6808 0.0745  0.0188  0.0437  225 GLU   A O   
429  C  CB  . GLU   A 69  ? 0.4502 0.5259 0.7233 0.0791  0.0334  0.0468  225 GLU   A CB  
430  C  CG  . GLU   A 69  ? 0.4852 0.5735 0.7761 0.0852  0.0452  0.0480  225 GLU   A CG  
431  C  CD  . GLU   A 69  ? 0.5938 0.6901 0.8811 0.0764  0.0473  0.0430  225 GLU   A CD  
432  O  OE1 . GLU   A 69  ? 0.5605 0.6562 0.8350 0.0656  0.0380  0.0408  225 GLU   A OE1 
433  O  OE2 . GLU   A 69  ? 0.6825 0.7857 0.9803 0.0805  0.0588  0.0416  225 GLU   A OE2 
434  N  N   . PHE   A 70  ? 0.4279 0.4979 0.6968 0.0844  0.0107  0.0625  226 PHE   A N   
435  C  CA  . PHE   A 70  ? 0.3967 0.4581 0.6505 0.0795  0.0001  0.0627  226 PHE   A CA  
436  C  C   . PHE   A 70  ? 0.3846 0.4618 0.6366 0.0693  -0.0130 0.0654  226 PHE   A C   
437  O  O   . PHE   A 70  ? 0.3584 0.4561 0.6242 0.0672  -0.0149 0.0698  226 PHE   A O   
438  C  CB  . PHE   A 70  ? 0.4787 0.5386 0.7399 0.0890  -0.0008 0.0716  226 PHE   A CB  
439  C  CG  . PHE   A 70  ? 0.4128 0.4518 0.6720 0.0976  0.0117  0.0677  226 PHE   A CG  
440  C  CD1 . PHE   A 70  ? 0.4881 0.5287 0.7633 0.1069  0.0245  0.0687  226 PHE   A CD1 
441  C  CD2 . PHE   A 70  ? 0.4677 0.4853 0.7095 0.0962  0.0112  0.0629  226 PHE   A CD2 
442  C  CE1 . PHE   A 70  ? 0.5060 0.5256 0.7788 0.1140  0.0370  0.0641  226 PHE   A CE1 
443  C  CE2 . PHE   A 70  ? 0.4991 0.4967 0.7388 0.1030  0.0230  0.0589  226 PHE   A CE2 
444  C  CZ  . PHE   A 70  ? 0.4392 0.4370 0.6940 0.1117  0.0360  0.0591  226 PHE   A CZ  
445  N  N   . ASP   A 71  ? 0.4093 0.4765 0.6440 0.0628  -0.0214 0.0626  227 ASP   A N   
446  C  CA  . ASP   A 71  ? 0.4007 0.4767 0.6287 0.0516  -0.0328 0.0622  227 ASP   A CA  
447  C  C   . ASP   A 71  ? 0.4705 0.5419 0.6878 0.0497  -0.0419 0.0648  227 ASP   A C   
448  O  O   . ASP   A 71  ? 0.3659 0.4179 0.5692 0.0512  -0.0399 0.0602  227 ASP   A O   
449  C  CB  . ASP   A 71  ? 0.5059 0.5700 0.7191 0.0429  -0.0309 0.0519  227 ASP   A CB  
450  C  CG  . ASP   A 71  ? 0.4252 0.4980 0.6342 0.0316  -0.0404 0.0513  227 ASP   A CG  
451  O  OD1 . ASP   A 71  ? 0.5017 0.5666 0.6970 0.0262  -0.0477 0.0492  227 ASP   A OD1 
452  O  OD2 . ASP   A 71  ? 0.5011 0.5888 0.7211 0.0279  -0.0402 0.0531  227 ASP   A OD2 
453  N  N   . VAL   A 72  ? 0.3952 0.4857 0.6190 0.0457  -0.0521 0.0722  228 VAL   A N   
454  C  CA  . VAL   A 72  ? 0.3324 0.4233 0.5487 0.0446  -0.0608 0.0767  228 VAL   A CA  
455  C  C   . VAL   A 72  ? 0.4352 0.5379 0.6451 0.0319  -0.0722 0.0758  228 VAL   A C   
456  O  O   . VAL   A 72  ? 0.3269 0.4486 0.5482 0.0270  -0.0753 0.0787  228 VAL   A O   
457  C  CB  . VAL   A 72  ? 0.4395 0.5444 0.6731 0.0553  -0.0609 0.0896  228 VAL   A CB  
458  C  CG1 . VAL   A 72  ? 0.4154 0.5250 0.6416 0.0528  -0.0711 0.0957  228 VAL   A CG1 
459  C  CG2 . VAL   A 72  ? 0.4271 0.5150 0.6641 0.0673  -0.0488 0.0890  228 VAL   A CG2 
460  N  N   . MET   A 73  ? 0.3292 0.4206 0.5208 0.0261  -0.0780 0.0717  229 MET   A N   
461  C  CA  . MET   A 73  ? 0.3637 0.4630 0.5465 0.0135  -0.0880 0.0695  229 MET   A CA  
462  C  C   . MET   A 73  ? 0.4033 0.5151 0.5853 0.0133  -0.0970 0.0778  229 MET   A C   
463  O  O   . MET   A 73  ? 0.3831 0.4831 0.5563 0.0183  -0.0963 0.0788  229 MET   A O   
464  C  CB  . MET   A 73  ? 0.5015 0.5784 0.6634 0.0062  -0.0870 0.0575  229 MET   A CB  
465  C  CG  . MET   A 73  ? 0.5458 0.6279 0.6985 -0.0073 -0.0954 0.0536  229 MET   A CG  
466  S  SD  . MET   A 73  ? 0.6645 0.7242 0.8007 -0.0157 -0.0917 0.0405  229 MET   A SD  
467  C  CE  . MET   A 73  ? 0.3968 0.4439 0.5384 -0.0062 -0.0797 0.0381  229 MET   A CE  
468  N  N   . PHE   A 74  ? 0.3150 0.4521 0.5065 0.0070  -0.1054 0.0843  230 PHE   A N   
469  C  CA  . PHE   A 74  ? 0.3372 0.4895 0.5255 0.0034  -0.1157 0.0917  230 PHE   A CA  
470  C  C   . PHE   A 74  ? 0.4133 0.5608 0.5820 -0.0119 -0.1227 0.0823  230 PHE   A C   
471  O  O   . PHE   A 74  ? 0.3915 0.5495 0.5624 -0.0224 -0.1263 0.0791  230 PHE   A O   
472  C  CB  . PHE   A 74  ? 0.3149 0.5002 0.5247 0.0043  -0.1214 0.1048  230 PHE   A CB  
473  C  CG  . PHE   A 74  ? 0.3490 0.5418 0.5795 0.0203  -0.1151 0.1165  230 PHE   A CG  
474  C  CD1 . PHE   A 74  ? 0.3733 0.5427 0.6024 0.0318  -0.1042 0.1136  230 PHE   A CD1 
475  C  CD2 . PHE   A 74  ? 0.4081 0.6319 0.6597 0.0235  -0.1200 0.1307  230 PHE   A CD2 
476  C  CE1 . PHE   A 74  ? 0.4345 0.6089 0.6825 0.0462  -0.0974 0.1236  230 PHE   A CE1 
477  C  CE2 . PHE   A 74  ? 0.3001 0.5304 0.5720 0.0390  -0.1134 0.1420  230 PHE   A CE2 
478  C  CZ  . PHE   A 74  ? 0.4790 0.6831 0.7487 0.0504  -0.1016 0.1380  230 PHE   A CZ  
479  N  N   . LYS   A 75  ? 0.3644 0.4964 0.5142 -0.0135 -0.1244 0.0780  231 LYS   A N   
480  C  CA  . LYS   A 75  ? 0.3730 0.4993 0.5036 -0.0275 -0.1301 0.0687  231 LYS   A CA  
481  C  C   . LYS   A 75  ? 0.4608 0.6104 0.5894 -0.0352 -0.1415 0.0756  231 LYS   A C   
482  O  O   . LYS   A 75  ? 0.3739 0.5379 0.5107 -0.0279 -0.1447 0.0877  231 LYS   A O   
483  C  CB  . LYS   A 75  ? 0.3727 0.4720 0.4831 -0.0262 -0.1261 0.0601  231 LYS   A CB  
484  C  CG  . LYS   A 75  ? 0.4516 0.5521 0.5579 -0.0195 -0.1284 0.0676  231 LYS   A CG  
485  C  CD  . LYS   A 75  ? 0.5680 0.6519 0.6513 -0.0252 -0.1295 0.0594  231 LYS   A CD  
486  C  CE  . LYS   A 75  ? 0.5525 0.6430 0.6314 -0.0211 -0.1339 0.0684  231 LYS   A CE  
487  N  NZ  . LYS   A 75  ? 0.5918 0.6868 0.6525 -0.0334 -0.1416 0.0643  231 LYS   A NZ  
488  N  N   . LEU   A 76  ? 0.3683 0.5199 0.4845 -0.0504 -0.1471 0.0675  232 LEU   A N   
489  C  CA  . LEU   A 76  ? 0.4694 0.6436 0.5807 -0.0613 -0.1582 0.0717  232 LEU   A CA  
490  C  C   . LEU   A 76  ? 0.4518 0.6105 0.5389 -0.0752 -0.1600 0.0578  232 LEU   A C   
491  O  O   . LEU   A 76  ? 0.3605 0.5101 0.4436 -0.0844 -0.1578 0.0476  232 LEU   A O   
492  C  CB  . LEU   A 76  ? 0.4076 0.6106 0.5366 -0.0675 -0.1638 0.0781  232 LEU   A CB  
493  C  CG  . LEU   A 76  ? 0.4687 0.7011 0.5961 -0.0799 -0.1761 0.0839  232 LEU   A CG  
494  C  CD1 . LEU   A 76  ? 0.4824 0.7356 0.6176 -0.0712 -0.1818 0.0998  232 LEU   A CD1 
495  C  CD2 . LEU   A 76  ? 0.4242 0.6784 0.5677 -0.0874 -0.1791 0.0862  232 LEU   A CD2 
496  N  N   . GLU   A 77  ? 0.4704 0.6253 0.5411 -0.0768 -0.1634 0.0574  233 GLU   A N   
497  C  CA  . GLU   A 77  ? 0.4964 0.6340 0.5439 -0.0888 -0.1632 0.0433  233 GLU   A CA  
498  C  C   . GLU   A 77  ? 0.5168 0.6716 0.5594 -0.1068 -0.1711 0.0391  233 GLU   A C   
499  O  O   . GLU   A 77  ? 0.5079 0.6916 0.5566 -0.1115 -0.1804 0.0487  233 GLU   A O   
500  C  CB  . GLU   A 77  ? 0.5908 0.7197 0.6211 -0.0865 -0.1639 0.0430  233 GLU   A CB  
501  C  CG  . GLU   A 77  ? 0.6554 0.7606 0.6630 -0.0961 -0.1602 0.0269  233 GLU   A CG  
502  C  CD  . GLU   A 77  ? 0.7604 0.8610 0.7484 -0.0981 -0.1622 0.0253  233 GLU   A CD  
503  O  OE1 . GLU   A 77  ? 0.7790 0.8915 0.7705 -0.0903 -0.1656 0.0370  233 GLU   A OE1 
504  O  OE2 . GLU   A 77  ? 0.8316 0.9177 0.8008 -0.1081 -0.1603 0.0124  233 GLU   A OE2 
505  N  N   . VAL   A 78  ? 0.6206 0.7576 0.6529 -0.1169 -0.1672 0.0252  234 VAL   A N   
506  C  CA  . VAL   A 78  ? 0.6278 0.7748 0.6525 -0.1358 -0.1730 0.0180  234 VAL   A CA  
507  C  C   . VAL   A 78  ? 0.6984 0.8235 0.6972 -0.1450 -0.1706 0.0039  234 VAL   A C   
508  O  O   . VAL   A 78  ? 0.7560 0.8529 0.7473 -0.1445 -0.1618 -0.0072 234 VAL   A O   
509  C  CB  . VAL   A 78  ? 0.5599 0.7040 0.5964 -0.1406 -0.1693 0.0136  234 VAL   A CB  
510  C  CG1 . VAL   A 78  ? 0.6800 0.8299 0.7061 -0.1614 -0.1742 0.0043  234 VAL   A CG1 
511  C  CG2 . VAL   A 78  ? 0.6333 0.8012 0.6956 -0.1321 -0.1715 0.0275  234 VAL   A CG2 
512  N  N   . PRO   A 79  ? 0.7018 0.8392 0.6865 -0.1527 -0.1776 0.0045  235 PRO   A N   
513  C  CA  . PRO   A 79  ? 0.6447 0.7611 0.6041 -0.1610 -0.1744 -0.0093 235 PRO   A CA  
514  C  C   . PRO   A 79  ? 0.6878 0.7958 0.6376 -0.1788 -0.1732 -0.0236 235 PRO   A C   
515  O  O   . PRO   A 79  ? 0.7066 0.8327 0.6664 -0.1886 -0.1784 -0.0218 235 PRO   A O   
516  C  CB  . PRO   A 79  ? 0.7456 0.8831 0.6942 -0.1652 -0.1834 -0.0028 235 PRO   A CB  
517  C  CG  . PRO   A 79  ? 0.6987 0.8662 0.6682 -0.1564 -0.1907 0.0158  235 PRO   A CG  
518  C  CD  . PRO   A 79  ? 0.6255 0.7934 0.6180 -0.1488 -0.1870 0.0200  235 PRO   A CD  
519  N  N   . ARG   A 80  ? 0.7122 0.7916 0.6435 -0.1827 -0.1654 -0.0379 236 ARG   A N   
520  C  CA  . ARG   A 80  ? 0.6751 0.7427 0.5931 -0.2006 -0.1632 -0.0532 236 ARG   A CA  
521  C  C   . ARG   A 80  ? 0.6573 0.7232 0.5909 -0.2044 -0.1610 -0.0544 236 ARG   A C   
522  O  O   . ARG   A 80  ? 0.7679 0.8388 0.6975 -0.2216 -0.1636 -0.0617 236 ARG   A O   
523  C  CB  . ARG   A 80  ? 0.8045 0.8947 0.7083 -0.2185 -0.1731 -0.0556 236 ARG   A CB  
524  N  N   . ILE   A 81  ? 0.6988 0.7578 0.6500 -0.1890 -0.1558 -0.0473 237 ILE   A N   
525  C  CA  . ILE   A 81  ? 0.6914 0.7477 0.6575 -0.1913 -0.1527 -0.0477 237 ILE   A CA  
526  C  C   . ILE   A 81  ? 0.7635 0.7902 0.7172 -0.2015 -0.1441 -0.0634 237 ILE   A C   
527  O  O   . ILE   A 81  ? 0.8222 0.8255 0.7591 -0.2010 -0.1379 -0.0729 237 ILE   A O   
528  C  CB  . ILE   A 81  ? 0.7802 0.8327 0.7646 -0.1720 -0.1477 -0.0378 237 ILE   A CB  
529  C  CG1 . ILE   A 81  ? 0.7294 0.8020 0.7356 -0.1726 -0.1507 -0.0294 237 ILE   A CG1 
530  C  CG2 . ILE   A 81  ? 0.6304 0.6492 0.6098 -0.1646 -0.1359 -0.0456 237 ILE   A CG2 
531  C  CD1 . ILE   A 81  ? 0.6444 0.7198 0.6682 -0.1541 -0.1473 -0.0184 237 ILE   A CD1 
532  N  N   . GLN   A 82  ? 0.6943 0.7222 0.6574 -0.2107 -0.1433 -0.0656 238 GLN   A N   
533  C  CA  . GLN   A 82  ? 0.6949 0.6931 0.6504 -0.2185 -0.1340 -0.0784 238 GLN   A CA  
534  C  C   . GLN   A 82  ? 0.6156 0.6116 0.5907 -0.2136 -0.1298 -0.0730 238 GLN   A C   
535  O  O   . GLN   A 82  ? 0.5841 0.6045 0.5735 -0.2189 -0.1362 -0.0660 238 GLN   A O   
536  C  CB  . GLN   A 82  ? 0.8220 0.8225 0.7635 -0.2414 -0.1373 -0.0900 238 GLN   A CB  
537  C  CG  . GLN   A 82  ? 0.9575 0.9230 0.8854 -0.2472 -0.1253 -0.1053 238 GLN   A CG  
538  C  CD  . GLN   A 82  ? 1.0406 0.9853 0.9493 -0.2418 -0.1193 -0.1133 238 GLN   A CD  
539  O  OE1 . GLN   A 82  ? 1.0798 0.9992 0.9775 -0.2444 -0.1092 -0.1250 238 GLN   A OE1 
540  N  NE2 . GLN   A 82  ? 0.8677 0.8236 0.7736 -0.2328 -0.1249 -0.1063 238 GLN   A NE2 
541  N  N   . LEU   A 83  ? 0.6234 0.5920 0.5996 -0.2035 -0.1193 -0.0755 239 LEU   A N   
542  C  CA  . LEU   A 83  ? 0.5815 0.5486 0.5758 -0.1977 -0.1151 -0.0694 239 LEU   A CA  
543  C  C   . LEU   A 83  ? 0.6504 0.5970 0.6424 -0.2099 -0.1084 -0.0784 239 LEU   A C   
544  O  O   . LEU   A 83  ? 0.7147 0.6356 0.6916 -0.2153 -0.1019 -0.0897 239 LEU   A O   
545  C  CB  . LEU   A 83  ? 0.4753 0.4299 0.4754 -0.1779 -0.1084 -0.0634 239 LEU   A CB  
546  C  CG  . LEU   A 83  ? 0.5520 0.5253 0.5577 -0.1643 -0.1137 -0.0532 239 LEU   A CG  
547  C  CD1 . LEU   A 83  ? 0.5215 0.4807 0.5321 -0.1468 -0.1063 -0.0488 239 LEU   A CD1 
548  C  CD2 . LEU   A 83  ? 0.5749 0.5804 0.5971 -0.1660 -0.1220 -0.0430 239 LEU   A CD2 
549  N  N   . GLU   A 84  ? 0.5556 0.5132 0.5637 -0.2136 -0.1092 -0.0730 240 GLU   A N   
550  C  CA  . GLU   A 84  ? 0.5970 0.5369 0.6066 -0.2243 -0.1026 -0.0790 240 GLU   A CA  
551  C  C   . GLU   A 84  ? 0.6047 0.5435 0.6320 -0.2124 -0.0975 -0.0695 240 GLU   A C   
552  O  O   . GLU   A 84  ? 0.4953 0.4596 0.5385 -0.2101 -0.1027 -0.0597 240 GLU   A O   
553  C  CB  . GLU   A 84  ? 0.5924 0.5502 0.6027 -0.2452 -0.1097 -0.0826 240 GLU   A CB  
554  C  CG  . GLU   A 84  ? 0.6206 0.5564 0.6278 -0.2599 -0.1026 -0.0919 240 GLU   A CG  
555  C  CD  . GLU   A 84  ? 0.8124 0.7714 0.8266 -0.2737 -0.1078 -0.0918 240 GLU   A CD  
556  O  OE1 . GLU   A 84  ? 0.8737 0.8582 0.8844 -0.2792 -0.1169 -0.0911 240 GLU   A OE1 
557  O  OE2 . GLU   A 84  ? 0.7634 0.7155 0.7865 -0.2793 -0.1028 -0.0919 240 GLU   A OE2 
558  N  N   . GLU   A 85  ? 0.5406 0.4510 0.5651 -0.2043 -0.0873 -0.0717 241 GLU   A N   
559  C  CA  . GLU   A 85  ? 0.5392 0.4481 0.5785 -0.1929 -0.0821 -0.0626 241 GLU   A CA  
560  C  C   . GLU   A 85  ? 0.5066 0.4266 0.5589 -0.2040 -0.0830 -0.0595 241 GLU   A C   
561  O  O   . GLU   A 85  ? 0.4977 0.4070 0.5452 -0.2195 -0.0813 -0.0672 241 GLU   A O   
562  C  CB  . GLU   A 85  ? 0.4861 0.3627 0.5194 -0.1851 -0.0710 -0.0657 241 GLU   A CB  
563  C  CG  . GLU   A 85  ? 0.5720 0.4479 0.6188 -0.1720 -0.0658 -0.0556 241 GLU   A CG  
564  C  CD  . GLU   A 85  ? 0.6169 0.4634 0.6583 -0.1641 -0.0555 -0.0572 241 GLU   A CD  
565  O  OE1 . GLU   A 85  ? 0.5517 0.3777 0.5798 -0.1678 -0.0518 -0.0663 241 GLU   A OE1 
566  O  OE2 . GLU   A 85  ? 0.5884 0.4333 0.6389 -0.1539 -0.0509 -0.0492 241 GLU   A OE2 
567  N  N   . TYR   A 86  ? 0.5125 0.4537 0.5814 -0.1965 -0.0853 -0.0487 242 TYR   A N   
568  C  CA  . TYR   A 86  ? 0.4704 0.4222 0.5531 -0.2055 -0.0850 -0.0447 242 TYR   A CA  
569  C  C   . TYR   A 86  ? 0.5445 0.4731 0.6305 -0.2011 -0.0745 -0.0431 242 TYR   A C   
570  O  O   . TYR   A 86  ? 0.5610 0.4856 0.6507 -0.1857 -0.0702 -0.0369 242 TYR   A O   
571  C  CB  . TYR   A 86  ? 0.4694 0.4547 0.5691 -0.1994 -0.0910 -0.0338 242 TYR   A CB  
572  C  CG  . TYR   A 86  ? 0.5173 0.5141 0.6330 -0.2057 -0.0893 -0.0282 242 TYR   A CG  
573  C  CD1 . TYR   A 86  ? 0.5798 0.5864 0.6985 -0.2245 -0.0930 -0.0313 242 TYR   A CD1 
574  C  CD2 . TYR   A 86  ? 0.5292 0.5271 0.6563 -0.1936 -0.0835 -0.0199 242 TYR   A CD2 
575  C  CE1 . TYR   A 86  ? 0.5936 0.6115 0.7275 -0.2305 -0.0912 -0.0256 242 TYR   A CE1 
576  C  CE2 . TYR   A 86  ? 0.4979 0.5067 0.6393 -0.1992 -0.0814 -0.0145 242 TYR   A CE2 
577  C  CZ  . TYR   A 86  ? 0.6521 0.6709 0.7974 -0.2173 -0.0851 -0.0170 242 TYR   A CZ  
578  O  OH  . TYR   A 86  ? 0.7260 0.7563 0.8861 -0.2227 -0.0827 -0.0111 242 TYR   A OH  
579  N  N   . SER   A 87  ? 0.6329 0.5460 0.7168 -0.2152 -0.0704 -0.0486 243 SER   A N   
580  C  CA  . SER   A 87  ? 0.5931 0.4910 0.6844 -0.2147 -0.0618 -0.0446 243 SER   A CA  
581  C  C   . SER   A 87  ? 0.5225 0.3992 0.6104 -0.1983 -0.0537 -0.0415 243 SER   A C   
582  O  O   . SER   A 87  ? 0.5587 0.4361 0.6564 -0.1908 -0.0490 -0.0331 243 SER   A O   
583  C  CB  . SER   A 87  ? 0.6253 0.5499 0.7350 -0.2152 -0.0644 -0.0346 243 SER   A CB  
584  O  OG  . SER   A 87  ? 0.6982 0.6094 0.8145 -0.2179 -0.0565 -0.0309 243 SER   A OG  
585  N  N   . ASN   A 88  ? 0.5117 0.3707 0.5855 -0.1933 -0.0519 -0.0482 244 ASN   A N   
586  C  CA  . ASN   A 88  ? 0.5595 0.3985 0.6291 -0.1785 -0.0444 -0.0459 244 ASN   A CA  
587  C  C   . ASN   A 88  ? 0.5937 0.4497 0.6722 -0.1627 -0.0457 -0.0355 244 ASN   A C   
588  O  O   . ASN   A 88  ? 0.5231 0.3675 0.6028 -0.1520 -0.0393 -0.0306 244 ASN   A O   
589  C  CB  . ASN   A 88  ? 0.6642 0.4765 0.7350 -0.1809 -0.0342 -0.0454 244 ASN   A CB  
590  C  CG  . ASN   A 88  ? 0.7300 0.5174 0.7895 -0.1937 -0.0300 -0.0571 244 ASN   A CG  
591  O  OD1 . ASN   A 88  ? 0.8748 0.6645 0.9237 -0.2010 -0.0348 -0.0663 244 ASN   A OD1 
592  N  ND2 . ASN   A 88  ? 0.6922 0.4554 0.7536 -0.1971 -0.0206 -0.0567 244 ASN   A ND2 
593  N  N   . THR   A 89  ? 0.5293 0.4128 0.6140 -0.1611 -0.0536 -0.0320 245 THR   A N   
594  C  CA  . THR   A 89  ? 0.4615 0.3596 0.5546 -0.1468 -0.0536 -0.0231 245 THR   A CA  
595  C  C   . THR   A 89  ? 0.5044 0.3964 0.5885 -0.1336 -0.0533 -0.0239 245 THR   A C   
596  O  O   . THR   A 89  ? 0.4686 0.3685 0.5577 -0.1218 -0.0520 -0.0175 245 THR   A O   
597  C  CB  . THR   A 89  ? 0.5214 0.4505 0.6261 -0.1482 -0.0608 -0.0182 245 THR   A CB  
598  O  OG1 . THR   A 89  ? 0.4890 0.4286 0.5879 -0.1521 -0.0686 -0.0228 245 THR   A OG1 
599  C  CG2 . THR   A 89  ? 0.4718 0.4102 0.5875 -0.1603 -0.0607 -0.0158 245 THR   A CG2 
600  N  N   . ARG   A 90  ? 0.5095 0.3887 0.5804 -0.1358 -0.0544 -0.0319 246 ARG   A N   
601  C  CA  . ARG   A 90  ? 0.4603 0.3324 0.5221 -0.1243 -0.0537 -0.0331 246 ARG   A CA  
602  C  C   . ARG   A 90  ? 0.4605 0.3547 0.5251 -0.1171 -0.0604 -0.0294 246 ARG   A C   
603  O  O   . ARG   A 90  ? 0.4526 0.3434 0.5082 -0.1111 -0.0618 -0.0319 246 ARG   A O   
604  C  CB  . ARG   A 90  ? 0.5165 0.3747 0.5793 -0.1133 -0.0458 -0.0284 246 ARG   A CB  
605  C  CG  . ARG   A 90  ? 0.5897 0.4263 0.6526 -0.1181 -0.0380 -0.0292 246 ARG   A CG  
606  C  CD  . ARG   A 90  ? 0.6195 0.4312 0.6701 -0.1170 -0.0329 -0.0361 246 ARG   A CD  
607  N  NE  . ARG   A 90  ? 0.7840 0.5910 0.8251 -0.1283 -0.0361 -0.0463 246 ARG   A NE  
608  C  CZ  . ARG   A 90  ? 0.7946 0.5859 0.8230 -0.1279 -0.0338 -0.0541 246 ARG   A CZ  
609  N  NH1 . ARG   A 90  ? 0.7619 0.5389 0.7866 -0.1168 -0.0277 -0.0528 246 ARG   A NH1 
610  N  NH2 . ARG   A 90  ? 0.7421 0.5335 0.7612 -0.1392 -0.0378 -0.0634 246 ARG   A NH2 
611  N  N   . ALA   A 91  ? 0.3867 0.3032 0.4644 -0.1172 -0.0639 -0.0230 247 ALA   A N   
612  C  CA  . ALA   A 91  ? 0.4066 0.3432 0.4887 -0.1096 -0.0692 -0.0187 247 ALA   A CA  
613  C  C   . ALA   A 91  ? 0.4170 0.3765 0.5055 -0.1177 -0.0773 -0.0176 247 ALA   A C   
614  O  O   . ALA   A 91  ? 0.3762 0.3502 0.4663 -0.1119 -0.0822 -0.0146 247 ALA   A O   
615  C  CB  . ALA   A 91  ? 0.4620 0.4076 0.5550 -0.0991 -0.0655 -0.0110 247 ALA   A CB  
616  N  N   . TYR   A 92  ? 0.3766 0.3404 0.4694 -0.1309 -0.0789 -0.0193 248 TYR   A N   
617  C  CA  . TYR   A 92  ? 0.4046 0.3931 0.5052 -0.1397 -0.0869 -0.0173 248 TYR   A CA  
618  C  C   . TYR   A 92  ? 0.4777 0.4606 0.5660 -0.1541 -0.0913 -0.0259 248 TYR   A C   
619  O  O   . TYR   A 92  ? 0.4830 0.4441 0.5627 -0.1621 -0.0866 -0.0331 248 TYR   A O   
620  C  CB  . TYR   A 92  ? 0.4401 0.4424 0.5565 -0.1452 -0.0857 -0.0121 248 TYR   A CB  
621  C  CG  . TYR   A 92  ? 0.4484 0.4603 0.5773 -0.1322 -0.0816 -0.0037 248 TYR   A CG  
622  C  CD1 . TYR   A 92  ? 0.4445 0.4391 0.5719 -0.1256 -0.0734 -0.0030 248 TYR   A CD1 
623  C  CD2 . TYR   A 92  ? 0.4348 0.4736 0.5774 -0.1271 -0.0856 0.0035  248 TYR   A CD2 
624  C  CE1 . TYR   A 92  ? 0.4779 0.4814 0.6151 -0.1147 -0.0692 0.0037  248 TYR   A CE1 
625  C  CE2 . TYR   A 92  ? 0.4141 0.4603 0.5673 -0.1155 -0.0807 0.0099  248 TYR   A CE2 
626  C  CZ  . TYR   A 92  ? 0.5721 0.6005 0.7217 -0.1099 -0.0725 0.0095  248 TYR   A CZ  
627  O  OH  . TYR   A 92  ? 0.4288 0.4644 0.5872 -0.0997 -0.0673 0.0149  248 TYR   A OH  
628  N  N   . TYR   A 93  ? 0.4621 0.4650 0.5497 -0.1576 -0.0999 -0.0250 249 TYR   A N   
629  C  CA  . TYR   A 93  ? 0.4739 0.4735 0.5474 -0.1710 -0.1047 -0.0335 249 TYR   A CA  
630  C  C   . TYR   A 93  ? 0.5143 0.5448 0.5953 -0.1816 -0.1146 -0.0299 249 TYR   A C   
631  O  O   . TYR   A 93  ? 0.4343 0.4900 0.5303 -0.1747 -0.1188 -0.0199 249 TYR   A O   
632  C  CB  . TYR   A 93  ? 0.4550 0.4438 0.5130 -0.1641 -0.1053 -0.0374 249 TYR   A CB  
633  C  CG  . TYR   A 93  ? 0.5208 0.4798 0.5703 -0.1552 -0.0959 -0.0415 249 TYR   A CG  
634  C  CD1 . TYR   A 93  ? 0.4569 0.4136 0.5138 -0.1394 -0.0913 -0.0347 249 TYR   A CD1 
635  C  CD2 . TYR   A 93  ? 0.4830 0.4170 0.5176 -0.1626 -0.0912 -0.0520 249 TYR   A CD2 
636  C  CE1 . TYR   A 93  ? 0.5107 0.4433 0.5607 -0.1316 -0.0834 -0.0374 249 TYR   A CE1 
637  C  CE2 . TYR   A 93  ? 0.5251 0.4335 0.5538 -0.1534 -0.0823 -0.0544 249 TYR   A CE2 
638  C  CZ  . TYR   A 93  ? 0.5291 0.4383 0.5659 -0.1381 -0.0789 -0.0466 249 TYR   A CZ  
639  O  OH  . TYR   A 93  ? 0.5019 0.3890 0.5337 -0.1292 -0.0708 -0.0478 249 TYR   A OH  
640  N  N   . PHE   A 94  ? 0.5602 0.5885 0.6305 -0.1986 -0.1181 -0.0384 250 PHE   A N   
641  C  CA  . PHE   A 94  ? 0.4505 0.5075 0.5222 -0.2099 -0.1288 -0.0365 250 PHE   A CA  
642  C  C   . PHE   A 94  ? 0.5229 0.5801 0.5795 -0.2071 -0.1333 -0.0391 250 PHE   A C   
643  O  O   . PHE   A 94  ? 0.4874 0.5178 0.5275 -0.2051 -0.1280 -0.0476 250 PHE   A O   
644  C  CB  . PHE   A 94  ? 0.5090 0.5645 0.5761 -0.2316 -0.1302 -0.0449 250 PHE   A CB  
645  C  CG  . PHE   A 94  ? 0.5479 0.6074 0.6310 -0.2360 -0.1268 -0.0412 250 PHE   A CG  
646  C  CD1 . PHE   A 94  ? 0.5493 0.6407 0.6531 -0.2326 -0.1317 -0.0294 250 PHE   A CD1 
647  C  CD2 . PHE   A 94  ? 0.5960 0.6280 0.6742 -0.2438 -0.1184 -0.0491 250 PHE   A CD2 
648  C  CE1 . PHE   A 94  ? 0.5662 0.6628 0.6848 -0.2372 -0.1283 -0.0258 250 PHE   A CE1 
649  C  CE2 . PHE   A 94  ? 0.5801 0.6166 0.6731 -0.2485 -0.1152 -0.0450 250 PHE   A CE2 
650  C  CZ  . PHE   A 94  ? 0.5866 0.6558 0.6994 -0.2456 -0.1203 -0.0336 250 PHE   A CZ  
651  N  N   . VAL   A 95  ? 0.6415 0.7293 0.7044 -0.2062 -0.1429 -0.0307 251 VAL   A N   
652  C  CA  . VAL   A 95  ? 0.5197 0.6120 0.5695 -0.2037 -0.1481 -0.0310 251 VAL   A CA  
653  C  C   . VAL   A 95  ? 0.5676 0.6742 0.6063 -0.2240 -0.1565 -0.0370 251 VAL   A C   
654  O  O   . VAL   A 95  ? 0.5688 0.7048 0.6192 -0.2333 -0.1642 -0.0310 251 VAL   A O   
655  C  CB  . VAL   A 95  ? 0.5343 0.6502 0.5980 -0.1880 -0.1527 -0.0167 251 VAL   A CB  
656  C  CG1 . VAL   A 95  ? 0.4532 0.5764 0.5040 -0.1872 -0.1589 -0.0158 251 VAL   A CG1 
657  C  CG2 . VAL   A 95  ? 0.4334 0.5321 0.5047 -0.1688 -0.1436 -0.0128 251 VAL   A CG2 
658  N  N   . LYS   A 96  ? 0.5512 0.6379 0.5675 -0.2315 -0.1547 -0.0489 252 LYS   A N   
659  C  CA  . LYS   A 96  ? 0.6780 0.7774 0.6796 -0.2505 -0.1625 -0.0557 252 LYS   A CA  
660  C  C   . LYS   A 96  ? 0.7277 0.8295 0.7147 -0.2448 -0.1661 -0.0549 252 LYS   A C   
661  O  O   . LYS   A 96  ? 0.6763 0.7665 0.6641 -0.2270 -0.1617 -0.0506 252 LYS   A O   
662  C  CB  . LYS   A 96  ? 0.6322 0.7038 0.6189 -0.2631 -0.1539 -0.0717 252 LYS   A CB  
663  C  CG  . LYS   A 96  ? 0.6249 0.6948 0.6252 -0.2697 -0.1501 -0.0722 252 LYS   A CG  
664  C  CD  . LYS   A 96  ? 0.7741 0.8192 0.7612 -0.2813 -0.1417 -0.0867 252 LYS   A CD  
665  C  CE  . LYS   A 96  ? 0.7666 0.8124 0.7687 -0.2877 -0.1386 -0.0854 252 LYS   A CE  
666  N  NZ  . LYS   A 96  ? 0.8290 0.8517 0.8206 -0.2993 -0.1307 -0.0984 252 LYS   A NZ  
667  N  N   . PHE   A 97  ? 0.6965 0.8125 0.6711 -0.2557 -0.1712 -0.0584 253 PHE   A N   
668  C  CA  . PHE   A 97  ? 0.7907 0.9121 0.7508 -0.2521 -0.1752 -0.0571 253 PHE   A CA  
669  C  C   . PHE   A 97  ? 0.7053 0.8069 0.6409 -0.2620 -0.1694 -0.0726 253 PHE   A C   
670  O  O   . PHE   A 97  ? 0.7552 0.8572 0.6864 -0.2747 -0.1678 -0.0800 253 PHE   A O   
671  C  CB  . PHE   A 97  ? 0.7430 0.9051 0.7126 -0.2513 -0.1867 -0.0427 253 PHE   A CB  
672  C  CG  . PHE   A 97  ? 0.6900 0.8732 0.6848 -0.2395 -0.1919 -0.0263 253 PHE   A CG  
673  C  CD1 . PHE   A 97  ? 0.6687 0.8675 0.6837 -0.2421 -0.1931 -0.0208 253 PHE   A CD1 
674  C  CD2 . PHE   A 97  ? 0.7171 0.8998 0.7163 -0.2220 -0.1920 -0.0168 253 PHE   A CD2 
675  C  CE1 . PHE   A 97  ? 0.6698 0.8865 0.7091 -0.2287 -0.1955 -0.0059 253 PHE   A CE1 
676  C  CE2 . PHE   A 97  ? 0.7074 0.9039 0.7304 -0.2059 -0.1919 -0.0023 253 PHE   A CE2 
677  C  CZ  . PHE   A 97  ? 0.6355 0.8489 0.6786 -0.2089 -0.1934 0.0030  253 PHE   A CZ  
678  N  N   . LYS   A 98  ? 0.8465 0.9307 0.7665 -0.2558 -0.1659 -0.0772 254 LYS   A N   
679  C  CA  . LYS   A 98  ? 0.8358 0.9013 0.7328 -0.2635 -0.1596 -0.0914 254 LYS   A CA  
680  C  C   . LYS   A 98  ? 0.7911 0.8832 0.6791 -0.2735 -0.1672 -0.0894 254 LYS   A C   
681  O  O   . LYS   A 98  ? 0.9452 1.0292 0.8193 -0.2854 -0.1632 -0.1008 254 LYS   A O   
682  C  CB  . LYS   A 98  ? 0.8425 0.8848 0.7265 -0.2534 -0.1538 -0.0955 254 LYS   A CB  
683  N  N   . ARG   A 99  ? 0.8826 1.0061 0.7788 -0.2684 -0.1777 -0.0746 255 ARG   A N   
684  C  CA  . ARG   A 99  ? 0.8921 1.0455 0.7829 -0.2771 -0.1859 -0.0694 255 ARG   A CA  
685  C  C   . ARG   A 99  ? 0.8792 1.0671 0.7878 -0.2678 -0.1967 -0.0494 255 ARG   A C   
686  O  O   . ARG   A 99  ? 0.9617 1.1478 0.8759 -0.2540 -0.1978 -0.0412 255 ARG   A O   
687  C  CB  . ARG   A 99  ? 0.9048 1.0490 0.7707 -0.2810 -0.1832 -0.0778 255 ARG   A CB  
688  N  N   . ASN   A 104 ? 0.6606 1.0054 0.6507 -0.2364 -0.2356 0.0360  260 ASN   A N   
689  C  CA  . ASN   A 104 ? 0.6829 1.0106 0.6879 -0.2256 -0.2307 0.0356  260 ASN   A CA  
690  C  C   . ASN   A 104 ? 0.6475 1.0036 0.6821 -0.2130 -0.2349 0.0551  260 ASN   A C   
691  O  O   . ASN   A 104 ? 0.6244 1.0028 0.6719 -0.2189 -0.2378 0.0600  260 ASN   A O   
692  C  CB  . ASN   A 104 ? 0.6518 0.9588 0.6533 -0.2373 -0.2247 0.0195  260 ASN   A CB  
693  C  CG  . ASN   A 104 ? 0.6758 0.9633 0.6907 -0.2277 -0.2191 0.0182  260 ASN   A CG  
694  O  OD1 . ASN   A 104 ? 0.6328 0.9255 0.6633 -0.2121 -0.2202 0.0303  260 ASN   A OD1 
695  N  ND2 . ASN   A 104 ? 0.7391 1.0035 0.7483 -0.2371 -0.2126 0.0036  260 ASN   A ND2 
696  N  N   . PRO   A 105 ? 0.6242 0.9796 0.6698 -0.1954 -0.2347 0.0667  261 PRO   A N   
697  C  CA  . PRO   A 105 ? 0.6098 0.9915 0.6840 -0.1815 -0.2373 0.0861  261 PRO   A CA  
698  C  C   . PRO   A 105 ? 0.7075 1.0900 0.8031 -0.1793 -0.2338 0.0861  261 PRO   A C   
699  O  O   . PRO   A 105 ? 0.6236 1.0297 0.7437 -0.1697 -0.2351 0.1008  261 PRO   A O   
700  C  CB  . PRO   A 105 ? 0.6125 0.9858 0.6897 -0.1637 -0.2360 0.0956  261 PRO   A CB  
701  C  CG  . PRO   A 105 ? 0.6170 0.9551 0.6716 -0.1675 -0.2316 0.0794  261 PRO   A CG  
702  C  CD  . PRO   A 105 ? 0.5978 0.9239 0.6330 -0.1873 -0.2301 0.0608  261 PRO   A CD  
703  N  N   . LEU   A 106 ? 0.6521 1.0094 0.7391 -0.1880 -0.2289 0.0701  262 LEU   A N   
704  C  CA  . LEU   A 106 ? 0.5704 0.9274 0.6754 -0.1886 -0.2253 0.0687  262 LEU   A CA  
705  C  C   . LEU   A 106 ? 0.6222 0.9874 0.7237 -0.2064 -0.2261 0.0606  262 LEU   A C   
706  O  O   . LEU   A 106 ? 0.6505 1.0173 0.7669 -0.2082 -0.2231 0.0597  262 LEU   A O   
707  C  CB  . LEU   A 106 ? 0.4923 0.8135 0.5916 -0.1852 -0.2173 0.0572  262 LEU   A CB  
708  C  CG  . LEU   A 106 ? 0.5238 0.8279 0.6255 -0.1632 -0.2106 0.0633  262 LEU   A CG  
709  C  CD1 . LEU   A 106 ? 0.5037 0.7667 0.5972 -0.1570 -0.1981 0.0503  262 LEU   A CD1 
710  C  CD2 . LEU   A 106 ? 0.4928 0.8206 0.6229 -0.1474 -0.2111 0.0813  262 LEU   A CD2 
711  N  N   . SER   A 107 ? 0.6404 1.0114 0.7230 -0.2195 -0.2299 0.0551  263 SER   A N   
712  C  CA  . SER   A 107 ? 0.5036 0.8787 0.5803 -0.2376 -0.2302 0.0457  263 SER   A CA  
713  C  C   . SER   A 107 ? 0.6379 1.0411 0.7402 -0.2366 -0.2323 0.0568  263 SER   A C   
714  O  O   . SER   A 107 ? 0.6515 1.0527 0.7552 -0.2487 -0.2303 0.0491  263 SER   A O   
715  C  CB  . SER   A 107 ? 0.6726 1.0576 0.7288 -0.2498 -0.2351 0.0424  263 SER   A CB  
716  O  OG  . SER   A 107 ? 0.5879 1.0064 0.6551 -0.2429 -0.2422 0.0602  263 SER   A OG  
717  N  N   . GLN   A 108 ? 0.6716 1.1004 0.7945 -0.2219 -0.2357 0.0752  264 GLN   A N   
718  C  CA  . GLN   A 108 ? 0.6633 1.1196 0.8121 -0.2189 -0.2369 0.0869  264 GLN   A CA  
719  C  C   . GLN   A 108 ? 0.5511 0.9940 0.7144 -0.2161 -0.2301 0.0826  264 GLN   A C   
720  O  O   . GLN   A 108 ? 0.5535 1.0149 0.7341 -0.2189 -0.2300 0.0874  264 GLN   A O   
721  C  CB  . GLN   A 108 ? 0.7134 1.1954 0.8812 -0.2012 -0.2400 0.1075  264 GLN   A CB  
722  C  CG  . GLN   A 108 ? 0.5865 1.0525 0.7633 -0.1816 -0.2352 0.1127  264 GLN   A CG  
723  C  CD  . GLN   A 108 ? 0.7192 1.2058 0.9123 -0.1633 -0.2370 0.1323  264 GLN   A CD  
724  O  OE1 . GLN   A 108 ? 0.7267 1.2346 0.9446 -0.1537 -0.2358 0.1454  264 GLN   A OE1 
725  N  NE2 . GLN   A 108 ? 0.6607 1.1397 0.8396 -0.1585 -0.2391 0.1344  264 GLN   A NE2 
726  N  N   . PHE   A 109 ? 0.5197 0.9315 0.6762 -0.2113 -0.2244 0.0738  265 PHE   A N   
727  C  CA  . PHE   A 109 ? 0.5250 0.9226 0.6939 -0.2091 -0.2176 0.0696  265 PHE   A CA  
728  C  C   . PHE   A 109 ? 0.5534 0.9232 0.7046 -0.2258 -0.2132 0.0510  265 PHE   A C   
729  O  O   . PHE   A 109 ? 0.5781 0.9279 0.7342 -0.2242 -0.2066 0.0456  265 PHE   A O   
730  C  CB  . PHE   A 109 ? 0.5358 0.9173 0.7117 -0.1919 -0.2134 0.0736  265 PHE   A CB  
731  C  CG  . PHE   A 109 ? 0.5782 0.9818 0.7715 -0.1738 -0.2159 0.0913  265 PHE   A CG  
732  C  CD1 . PHE   A 109 ? 0.6732 1.0732 0.8548 -0.1668 -0.2190 0.0949  265 PHE   A CD1 
733  C  CD2 . PHE   A 109 ? 0.5234 0.9513 0.7444 -0.1639 -0.2143 0.1046  265 PHE   A CD2 
734  C  CE1 . PHE   A 109 ? 0.7992 1.2174 0.9969 -0.1496 -0.2202 0.1118  265 PHE   A CE1 
735  C  CE2 . PHE   A 109 ? 0.6141 1.0599 0.8512 -0.1462 -0.2150 0.1209  265 PHE   A CE2 
736  C  CZ  . PHE   A 109 ? 0.7253 1.1657 0.9508 -0.1390 -0.2179 0.1247  265 PHE   A CZ  
737  N  N   . LEU   A 110 ? 0.5585 0.9247 0.6888 -0.2411 -0.2157 0.0412  266 LEU   A N   
738  C  CA  . LEU   A 110 ? 0.6177 0.9553 0.7313 -0.2559 -0.2101 0.0235  266 LEU   A CA  
739  C  C   . LEU   A 110 ? 0.5415 0.8896 0.6685 -0.2654 -0.2085 0.0231  266 LEU   A C   
740  O  O   . LEU   A 110 ? 0.5932 0.9733 0.7327 -0.2678 -0.2139 0.0328  266 LEU   A O   
741  C  CB  . LEU   A 110 ? 0.6261 0.9551 0.7129 -0.2686 -0.2122 0.0125  266 LEU   A CB  
742  C  CG  . LEU   A 110 ? 0.5855 0.8977 0.6548 -0.2616 -0.2121 0.0095  266 LEU   A CG  
743  C  CD1 . LEU   A 110 ? 0.6789 0.9903 0.7241 -0.2742 -0.2148 0.0010  266 LEU   A CD1 
744  C  CD2 . LEU   A 110 ? 0.6313 0.9049 0.6929 -0.2579 -0.2035 -0.0016 266 LEU   A CD2 
745  N  N   . GLU   A 111 ? 0.5574 0.8785 0.6825 -0.2700 -0.2007 0.0128  267 GLU   A N   
746  C  CA  . GLU   A 111 ? 0.6150 0.9367 0.7449 -0.2832 -0.1978 0.0075  267 GLU   A CA  
747  C  C   . GLU   A 111 ? 0.6500 0.9380 0.7545 -0.2968 -0.1926 -0.0108 267 GLU   A C   
748  O  O   . GLU   A 111 ? 0.6830 0.9376 0.7805 -0.2946 -0.1847 -0.0196 267 GLU   A O   
749  C  CB  . GLU   A 111 ? 0.6204 0.9383 0.7705 -0.2769 -0.1918 0.0117  267 GLU   A CB  
750  C  CG  . GLU   A 111 ? 0.5393 0.8916 0.7170 -0.2651 -0.1951 0.0290  267 GLU   A CG  
751  C  CD  . GLU   A 111 ? 0.7099 1.0903 0.8998 -0.2746 -0.1982 0.0339  267 GLU   A CD  
752  O  OE1 . GLU   A 111 ? 0.6515 1.0327 0.8275 -0.2904 -0.2009 0.0261  267 GLU   A OE1 
753  O  OE2 . GLU   A 111 ? 0.7944 1.1954 1.0085 -0.2664 -0.1971 0.0453  267 GLU   A OE2 
754  N  N   . GLY   A 112 ? 0.5451 0.8418 0.6362 -0.3101 -0.1967 -0.0160 268 GLY   A N   
755  C  CA  . GLY   A 112 ? 0.6203 0.8872 0.6863 -0.3222 -0.1919 -0.0330 268 GLY   A CA  
756  C  C   . GLY   A 112 ? 0.6997 0.9450 0.7480 -0.3145 -0.1900 -0.0384 268 GLY   A C   
757  O  O   . GLY   A 112 ? 0.7660 1.0289 0.8101 -0.3095 -0.1967 -0.0317 268 GLY   A O   
758  N  N   . GLU   A 113 ? 0.6903 0.8974 0.7286 -0.3131 -0.1806 -0.0498 269 GLU   A N   
759  C  CA  . GLU   A 113 ? 0.6465 0.8300 0.6690 -0.3049 -0.1773 -0.0553 269 GLU   A CA  
760  C  C   . GLU   A 113 ? 0.6565 0.8364 0.6916 -0.2880 -0.1764 -0.0465 269 GLU   A C   
761  O  O   . GLU   A 113 ? 0.6658 0.8275 0.6890 -0.2802 -0.1742 -0.0497 269 GLU   A O   
762  C  CB  . GLU   A 113 ? 0.7706 0.9134 0.7746 -0.3120 -0.1667 -0.0726 269 GLU   A CB  
763  C  CG  . GLU   A 113 ? 0.8474 0.9862 0.8302 -0.3251 -0.1668 -0.0836 269 GLU   A CG  
764  C  CD  . GLU   A 113 ? 0.9596 1.0614 0.9216 -0.3224 -0.1580 -0.0966 269 GLU   A CD  
765  O  OE1 . GLU   A 113 ? 0.9205 1.0202 0.8769 -0.3116 -0.1593 -0.0937 269 GLU   A OE1 
766  O  OE2 . GLU   A 113 ? 1.0364 1.1118 0.9882 -0.3309 -0.1495 -0.1094 269 GLU   A OE2 
767  N  N   . ILE   A 114 ? 0.6228 0.8204 0.6815 -0.2825 -0.1780 -0.0353 270 ILE   A N   
768  C  CA  . ILE   A 114 ? 0.6669 0.8588 0.7392 -0.2679 -0.1757 -0.0276 270 ILE   A CA  
769  C  C   . ILE   A 114 ? 0.5569 0.7834 0.6466 -0.2560 -0.1842 -0.0107 270 ILE   A C   
770  O  O   . ILE   A 114 ? 0.5816 0.8402 0.6856 -0.2582 -0.1897 -0.0015 270 ILE   A O   
771  C  CB  . ILE   A 114 ? 0.6169 0.7999 0.7039 -0.2697 -0.1692 -0.0276 270 ILE   A CB  
772  C  CG1 . ILE   A 114 ? 0.5327 0.6735 0.6037 -0.2749 -0.1588 -0.0422 270 ILE   A CG1 
773  C  CG2 . ILE   A 114 ? 0.6995 0.8927 0.8078 -0.2531 -0.1682 -0.0146 270 ILE   A CG2 
774  C  CD1 . ILE   A 114 ? 0.6341 0.7502 0.6900 -0.2661 -0.1558 -0.0470 270 ILE   A CD1 
775  N  N   . LEU   A 115 ? 0.6126 0.8298 0.7011 -0.2404 -0.1830 -0.0064 271 LEU   A N   
776  C  CA  . LEU   A 115 ? 0.5654 0.8064 0.6731 -0.2226 -0.1858 0.0099  271 LEU   A CA  
777  C  C   . LEU   A 115 ? 0.5654 0.8126 0.6966 -0.2145 -0.1805 0.0172  271 LEU   A C   
778  O  O   . LEU   A 115 ? 0.5566 0.7765 0.6876 -0.2065 -0.1703 0.0125  271 LEU   A O   
779  C  CB  . LEU   A 115 ? 0.4938 0.7140 0.5924 -0.2046 -0.1810 0.0105  271 LEU   A CB  
780  C  CG  . LEU   A 115 ? 0.5648 0.8092 0.6785 -0.1882 -0.1852 0.0266  271 LEU   A CG  
781  C  CD1 . LEU   A 115 ? 0.5195 0.7915 0.6272 -0.1965 -0.1972 0.0320  271 LEU   A CD1 
782  C  CD2 . LEU   A 115 ? 0.4246 0.6444 0.5350 -0.1684 -0.1771 0.0275  271 LEU   A CD2 
783  N  N   . SER   A 116 ? 0.4679 0.7525 0.6198 -0.2159 -0.1873 0.0293  272 SER   A N   
784  C  CA  . SER   A 116 ? 0.4574 0.7519 0.6324 -0.2099 -0.1825 0.0363  272 SER   A CA  
785  C  C   . SER   A 116 ? 0.4908 0.7834 0.6791 -0.1857 -0.1764 0.0463  272 SER   A C   
786  O  O   . SER   A 116 ? 0.4529 0.7684 0.6515 -0.1757 -0.1814 0.0581  272 SER   A O   
787  C  CB  . SER   A 116 ? 0.4523 0.7886 0.6450 -0.2215 -0.1916 0.0453  272 SER   A CB  
788  O  OG  . SER   A 116 ? 0.4977 0.8465 0.7146 -0.2127 -0.1866 0.0540  272 SER   A OG  
789  N  N   . ALA   A 117 ? 0.3994 0.6653 0.5882 -0.1765 -0.1654 0.0419  273 ALA   A N   
790  C  CA  . ALA   A 117 ? 0.4339 0.6983 0.6360 -0.1553 -0.1587 0.0503  273 ALA   A CA  
791  C  C   . ALA   A 117 ? 0.4371 0.7374 0.6664 -0.1503 -0.1610 0.0640  273 ALA   A C   
792  O  O   . ALA   A 117 ? 0.4962 0.8087 0.7375 -0.1346 -0.1604 0.0745  273 ALA   A O   
793  C  CB  . ALA   A 117 ? 0.5044 0.7369 0.7020 -0.1493 -0.1469 0.0429  273 ALA   A CB  
794  N  N   . SER   A 118 ? 0.4706 0.7882 0.7104 -0.1637 -0.1632 0.0645  274 SER   A N   
795  C  CA  . SER   A 118 ? 0.4674 0.8218 0.7342 -0.1602 -0.1655 0.0778  274 SER   A CA  
796  C  C   . SER   A 118 ? 0.4261 0.8118 0.7012 -0.1562 -0.1753 0.0898  274 SER   A C   
797  O  O   . SER   A 118 ? 0.4570 0.8605 0.7515 -0.1403 -0.1734 0.1022  274 SER   A O   
798  C  CB  . SER   A 118 ? 0.4763 0.8460 0.7499 -0.1792 -0.1683 0.0755  274 SER   A CB  
799  O  OG  . SER   A 118 ? 0.5464 0.8902 0.8161 -0.1815 -0.1587 0.0671  274 SER   A OG  
800  N  N   . LYS   A 119 ? 0.4886 0.8821 0.7496 -0.1708 -0.1855 0.0865  275 LYS   A N   
801  C  CA  . LYS   A 119 ? 0.4602 0.8880 0.7298 -0.1690 -0.1959 0.0993  275 LYS   A CA  
802  C  C   . LYS   A 119 ? 0.4339 0.8501 0.6996 -0.1497 -0.1935 0.1046  275 LYS   A C   
803  O  O   . LYS   A 119 ? 0.5332 0.9743 0.8170 -0.1371 -0.1960 0.1196  275 LYS   A O   
804  C  CB  . LYS   A 119 ? 0.5128 0.9425 0.7608 -0.1869 -0.2029 0.0914  275 LYS   A CB  
805  C  CG  . LYS   A 119 ? 0.4333 0.8714 0.6837 -0.2028 -0.2025 0.0863  275 LYS   A CG  
806  C  CD  . LYS   A 119 ? 0.5959 1.0553 0.8383 -0.2145 -0.2102 0.0876  275 LYS   A CD  
807  C  CE  . LYS   A 119 ? 0.6088 1.0446 0.8216 -0.2311 -0.2119 0.0714  275 LYS   A CE  
808  N  NZ  . LYS   A 119 ? 0.5514 1.0073 0.7569 -0.2459 -0.2183 0.0708  275 LYS   A NZ  
809  N  N   . MET   A 120 ? 0.4379 0.8163 0.6812 -0.1469 -0.1881 0.0929  276 MET   A N   
810  C  CA  . MET   A 120 ? 0.5358 0.9021 0.7738 -0.1303 -0.1858 0.0972  276 MET   A CA  
811  C  C   . MET   A 120 ? 0.4568 0.8188 0.7134 -0.1094 -0.1757 0.1048  276 MET   A C   
812  O  O   . MET   A 120 ? 0.5007 0.8682 0.7647 -0.0943 -0.1751 0.1148  276 MET   A O   
813  C  CB  . MET   A 120 ? 0.4906 0.8188 0.7003 -0.1336 -0.1824 0.0825  276 MET   A CB  
814  C  CG  . MET   A 120 ? 0.5871 0.9156 0.7840 -0.1297 -0.1880 0.0858  276 MET   A CG  
815  S  SD  . MET   A 120 ? 0.7856 1.0689 0.9518 -0.1309 -0.1819 0.0692  276 MET   A SD  
816  C  CE  . MET   A 120 ? 0.4486 0.7298 0.6125 -0.1136 -0.1822 0.0785  276 MET   A CE  
817  N  N   . LEU   A 121 ? 0.4639 0.8163 0.7283 -0.1087 -0.1673 0.1002  277 LEU   A N   
818  C  CA  . LEU   A 121 ? 0.4611 0.8152 0.7453 -0.0908 -0.1578 0.1077  277 LEU   A CA  
819  C  C   . LEU   A 121 ? 0.4723 0.8669 0.7838 -0.0852 -0.1622 0.1243  277 LEU   A C   
820  O  O   . LEU   A 121 ? 0.4814 0.8806 0.8069 -0.0674 -0.1573 0.1340  277 LEU   A O   
821  C  CB  . LEU   A 121 ? 0.4186 0.7565 0.7044 -0.0932 -0.1485 0.0995  277 LEU   A CB  
822  C  CG  . LEU   A 121 ? 0.4197 0.7174 0.6876 -0.0865 -0.1391 0.0884  277 LEU   A CG  
823  C  CD1 . LEU   A 121 ? 0.4206 0.7096 0.6951 -0.0866 -0.1299 0.0843  277 LEU   A CD1 
824  C  CD2 . LEU   A 121 ? 0.3853 0.6755 0.6559 -0.0677 -0.1343 0.0940  277 LEU   A CD2 
825  N  N   . SER   A 122 ? 0.4116 0.8360 0.7315 -0.1002 -0.1709 0.1278  278 SER   A N   
826  C  CA  . SER   A 122 ? 0.4498 0.9167 0.7969 -0.0959 -0.1759 0.1447  278 SER   A CA  
827  C  C   . SER   A 122 ? 0.4249 0.9035 0.7758 -0.0835 -0.1805 0.1570  278 SER   A C   
828  O  O   . SER   A 122 ? 0.4013 0.8942 0.7737 -0.0665 -0.1759 0.1699  278 SER   A O   
829  C  CB  . SER   A 122 ? 0.4212 0.9138 0.7680 -0.1158 -0.1853 0.1444  278 SER   A CB  
830  O  OG  . SER   A 122 ? 0.5346 1.0308 0.8912 -0.1235 -0.1807 0.1404  278 SER   A OG  
831  N  N   . LYS   A 123 ? 0.4209 0.8922 0.7500 -0.0917 -0.1887 0.1529  279 LYS   A N   
832  C  CA  . LYS   A 123 ? 0.4869 0.9678 0.8158 -0.0812 -0.1925 0.1642  279 LYS   A CA  
833  C  C   . LYS   A 123 ? 0.3956 0.8538 0.7277 -0.0607 -0.1835 0.1669  279 LYS   A C   
834  O  O   . LYS   A 123 ? 0.4436 0.9157 0.7934 -0.0447 -0.1816 0.1814  279 LYS   A O   
835  C  CB  . LYS   A 123 ? 0.4132 0.8894 0.7150 -0.0957 -0.2020 0.1575  279 LYS   A CB  
836  C  CG  . LYS   A 123 ? 0.5166 0.9963 0.8142 -0.0849 -0.2049 0.1677  279 LYS   A CG  
837  C  CD  . LYS   A 123 ? 0.4405 0.9508 0.7410 -0.0905 -0.2116 0.1774  279 LYS   A CD  
838  C  CE  . LYS   A 123 ? 0.6863 1.1998 0.9754 -0.0863 -0.2166 0.1851  279 LYS   A CE  
839  N  NZ  . LYS   A 123 ? 0.6600 1.1647 0.9197 -0.1037 -0.2240 0.1736  279 LYS   A NZ  
840  N  N   . PHE   A 124 ? 0.4831 0.9012 0.7950 -0.0606 -0.1755 0.1514  280 PHE   A N   
841  C  CA  . PHE   A 124 ? 0.4105 0.8007 0.7209 -0.0424 -0.1643 0.1503  280 PHE   A CA  
842  C  C   . PHE   A 124 ? 0.4126 0.8148 0.7510 -0.0262 -0.1553 0.1607  280 PHE   A C   
843  O  O   . PHE   A 124 ? 0.3763 0.7773 0.7246 -0.0095 -0.1507 0.1702  280 PHE   A O   
844  C  CB  . PHE   A 124 ? 0.4671 0.8177 0.7549 -0.0471 -0.1571 0.1321  280 PHE   A CB  
845  C  CG  . PHE   A 124 ? 0.3939 0.7135 0.6752 -0.0315 -0.1465 0.1287  280 PHE   A CG  
846  C  CD1 . PHE   A 124 ? 0.3651 0.6724 0.6326 -0.0267 -0.1488 0.1298  280 PHE   A CD1 
847  C  CD2 . PHE   A 124 ? 0.3357 0.6374 0.6221 -0.0238 -0.1345 0.1230  280 PHE   A CD2 
848  C  CE1 . PHE   A 124 ? 0.4809 0.7596 0.7416 -0.0140 -0.1393 0.1261  280 PHE   A CE1 
849  C  CE2 . PHE   A 124 ? 0.4152 0.6888 0.6940 -0.0113 -0.1250 0.1189  280 PHE   A CE2 
850  C  CZ  . PHE   A 124 ? 0.3799 0.6416 0.6459 -0.0066 -0.1275 0.1202  280 PHE   A CZ  
851  N  N   . ARG   A 125 ? 0.3778 0.7940 0.7304 -0.0313 -0.1529 0.1599  281 ARG   A N   
852  C  CA  . ARG   A 125 ? 0.3803 0.8085 0.7596 -0.0167 -0.1433 0.1687  281 ARG   A CA  
853  C  C   . ARG   A 125 ? 0.4354 0.9020 0.8400 -0.0086 -0.1488 0.1884  281 ARG   A C   
854  O  O   . ARG   A 125 ? 0.4868 0.9552 0.9092 0.0099  -0.1404 0.1980  281 ARG   A O   
855  C  CB  . ARG   A 125 ? 0.3604 0.7940 0.7473 -0.0254 -0.1393 0.1626  281 ARG   A CB  
856  C  CG  . ARG   A 125 ? 0.4392 0.8360 0.8109 -0.0250 -0.1284 0.1474  281 ARG   A CG  
857  C  CD  . ARG   A 125 ? 0.3854 0.7841 0.7547 -0.0407 -0.1287 0.1390  281 ARG   A CD  
858  N  NE  . ARG   A 125 ? 0.4525 0.8188 0.8105 -0.0379 -0.1174 0.1271  281 ARG   A NE  
859  C  CZ  . ARG   A 125 ? 0.4483 0.8058 0.7994 -0.0499 -0.1155 0.1179  281 ARG   A CZ  
860  N  NH1 . ARG   A 125 ? 0.3687 0.7448 0.7221 -0.0664 -0.1236 0.1180  281 ARG   A NH1 
861  N  NH2 . ARG   A 125 ? 0.4411 0.7708 0.7828 -0.0457 -0.1050 0.1089  281 ARG   A NH2 
862  N  N   . LYS   A 126 ? 0.4653 0.9593 0.8689 -0.0222 -0.1610 0.1932  282 LYS   A N   
863  C  CA  . LYS   A 126 ? 0.4063 0.9246 0.8212 -0.0152 -0.1629 0.2077  282 LYS   A CA  
864  C  C   . LYS   A 126 ? 0.4729 0.9807 0.8863 0.0008  -0.1606 0.2160  282 LYS   A C   
865  O  O   . LYS   A 126 ? 0.5059 1.0209 0.9369 0.0170  -0.1533 0.2276  282 LYS   A O   
866  C  CB  . LYS   A 126 ? 0.4345 0.9736 0.8377 -0.0337 -0.1755 0.2078  282 LYS   A CB  
867  C  CG  . LYS   A 126 ? 0.5670 1.1339 0.9833 -0.0271 -0.1779 0.2238  282 LYS   A CG  
868  C  CD  . LYS   A 126 ? 0.5858 1.1642 0.9837 -0.0404 -0.1904 0.2253  282 LYS   A CD  
869  C  CE  . LYS   A 126 ? 0.3979 0.9969 0.7910 -0.0607 -0.1984 0.2212  282 LYS   A CE  
870  N  NZ  . LYS   A 126 ? 0.6104 1.2417 1.0171 -0.0578 -0.2020 0.2371  282 LYS   A NZ  
871  N  N   . ILE   A 127 ? 0.4275 0.9179 0.8192 -0.0041 -0.1665 0.2104  283 ILE   A N   
872  C  CA  . ILE   A 127 ? 0.4864 0.9675 0.8743 0.0089  -0.1653 0.2186  283 ILE   A CA  
873  C  C   . ILE   A 127 ? 0.4994 0.9606 0.9009 0.0293  -0.1513 0.2208  283 ILE   A C   
874  O  O   . ILE   A 127 ? 0.5688 1.0311 0.9809 0.0446  -0.1455 0.2321  283 ILE   A O   
875  C  CB  . ILE   A 127 ? 0.5343 0.9989 0.8951 -0.0012 -0.1736 0.2106  283 ILE   A CB  
876  C  CG1 . ILE   A 127 ? 0.4552 0.9402 0.8020 -0.0196 -0.1862 0.2101  283 ILE   A CG1 
877  C  CG2 . ILE   A 127 ? 0.4662 0.9163 0.8236 0.0135  -0.1703 0.2180  283 ILE   A CG2 
878  C  CD1 . ILE   A 127 ? 0.5480 1.0163 0.8666 -0.0318 -0.1936 0.1997  283 ILE   A CD1 
879  N  N   . ILE   A 128 ? 0.5086 0.9497 0.9089 0.0294  -0.1451 0.2096  284 ILE   A N   
880  C  CA  . ILE   A 128 ? 0.5133 0.9293 0.9206 0.0471  -0.1295 0.2078  284 ILE   A CA  
881  C  C   . ILE   A 128 ? 0.5193 0.9558 0.9556 0.0597  -0.1212 0.2192  284 ILE   A C   
882  O  O   . ILE   A 128 ? 0.5236 0.9503 0.9691 0.0767  -0.1111 0.2257  284 ILE   A O   
883  C  CB  . ILE   A 128 ? 0.4978 0.8791 0.8862 0.0416  -0.1209 0.1877  284 ILE   A CB  
884  C  CG1 . ILE   A 128 ? 0.4616 0.8150 0.8186 0.0328  -0.1253 0.1758  284 ILE   A CG1 
885  C  CG2 . ILE   A 128 ? 0.4564 0.8154 0.8529 0.0583  -0.1045 0.1853  284 ILE   A CG2 
886  C  CD1 . ILE   A 128 ? 0.5128 0.8373 0.8511 0.0246  -0.1195 0.1572  284 ILE   A CD1 
887  N  N   . LYS   A 129 ? 0.5042 0.9646 0.9506 0.0507  -0.1239 0.2196  285 LYS   A N   
888  C  CA  . LYS   A 129 ? 0.4418 0.9196 0.9114 0.0612  -0.1154 0.2288  285 LYS   A CA  
889  C  C   . LYS   A 129 ? 0.6259 1.1162 1.1020 0.0707  -0.1167 0.2437  285 LYS   A C   
890  O  O   . LYS   A 129 ? 0.6449 1.1344 1.1376 0.0868  -0.1055 0.2514  285 LYS   A O   
891  C  CB  . LYS   A 129 ? 0.5582 1.0617 1.0354 0.0476  -0.1201 0.2275  285 LYS   A CB  
892  C  CG  . LYS   A 129 ? 0.5438 1.0515 1.0412 0.0557  -0.1073 0.2271  285 LYS   A CG  
893  C  CD  . LYS   A 129 ? 0.5445 1.0787 1.0484 0.0411  -0.1129 0.2267  285 LYS   A CD  
894  C  CE  . LYS   A 129 ? 0.5400 1.0644 1.0304 0.0243  -0.1172 0.2127  285 LYS   A CE  
895  N  NZ  . LYS   A 129 ? 0.6111 1.1570 1.1100 0.0117  -0.1189 0.2112  285 LYS   A NZ  
896  N  N   . GLU   A 130 ? 0.4962 0.9979 0.9592 0.0607  -0.1298 0.2478  286 GLU   A N   
897  C  CA  . GLU   A 130 ? 0.6727 1.1865 1.1407 0.0687  -0.1318 0.2626  286 GLU   A CA  
898  C  C   . GLU   A 130 ? 0.6631 1.1508 1.1323 0.0869  -0.1211 0.2660  286 GLU   A C   
899  O  O   . GLU   A 130 ? 0.6113 1.1027 1.0974 0.1015  -0.1123 0.2767  286 GLU   A O   
900  C  CB  . GLU   A 130 ? 0.6161 1.1418 1.0652 0.0535  -0.1472 0.2639  286 GLU   A CB  
901  C  CG  . GLU   A 130 ? 0.5748 1.1285 1.0226 0.0351  -0.1578 0.2624  286 GLU   A CG  
902  C  CD  . GLU   A 130 ? 0.6888 1.2473 1.1132 0.0188  -0.1716 0.2596  286 GLU   A CD  
903  O  OE1 . GLU   A 130 ? 0.7154 1.2567 1.1260 0.0228  -0.1728 0.2596  286 GLU   A OE1 
904  O  OE2 . GLU   A 130 ? 0.7644 1.3444 1.1844 0.0022  -0.1807 0.2577  286 GLU   A OE2 
905  N  N   . GLU   A 131 ? 0.5845 1.0450 1.0354 0.0858  -0.1216 0.2569  287 GLU   A N   
906  C  CA  . GLU   A 131 ? 0.6371 1.0713 1.0860 0.1011  -0.1123 0.2594  287 GLU   A CA  
907  C  C   . GLU   A 131 ? 0.6897 1.1084 1.1550 0.1167  -0.0950 0.2575  287 GLU   A C   
908  O  O   . GLU   A 131 ? 0.6830 1.0941 1.1580 0.1312  -0.0856 0.2658  287 GLU   A O   
909  C  CB  . GLU   A 131 ? 0.6144 1.0229 1.0400 0.0954  -0.1164 0.2489  287 GLU   A CB  
910  N  N   . ILE   A 132 ? 0.6524 1.0656 1.1205 0.1133  -0.0902 0.2464  288 ILE   A N   
911  C  CA  . ILE   A 132 ? 0.6502 1.0505 1.1330 0.1265  -0.0733 0.2433  288 ILE   A CA  
912  C  C   . ILE   A 132 ? 0.6328 1.0544 1.1374 0.1358  -0.0678 0.2561  288 ILE   A C   
913  O  O   . ILE   A 132 ? 0.6592 1.0671 1.1740 0.1509  -0.0540 0.2591  288 ILE   A O   
914  C  CB  . ILE   A 132 ? 0.5779 0.9756 1.0610 0.1189  -0.0707 0.2305  288 ILE   A CB  
915  C  CG1 . ILE   A 132 ? 0.5323 0.9104 0.9945 0.1092  -0.0771 0.2190  288 ILE   A CG1 
916  C  CG2 . ILE   A 132 ? 0.5506 0.9335 1.0465 0.1319  -0.0524 0.2259  288 ILE   A CG2 
917  C  CD1 . ILE   A 132 ? 0.5611 0.9060 1.0123 0.1194  -0.0698 0.2156  288 ILE   A CD1 
918  N  N   . ASN   A 133 ? 0.6694 1.1245 1.1810 0.1264  -0.0784 0.2636  289 ASN   A N   
919  C  CA  . ASN   A 133 ? 0.6241 1.1025 1.1570 0.1345  -0.0744 0.2771  289 ASN   A CA  
920  C  C   . ASN   A 133 ? 0.6273 1.0987 1.1636 0.1476  -0.0706 0.2892  289 ASN   A C   
921  O  O   . ASN   A 133 ? 0.7048 1.1770 1.2586 0.1614  -0.0591 0.2968  289 ASN   A O   
922  C  CB  . ASN   A 133 ? 0.6405 1.1557 1.1770 0.1202  -0.0883 0.2834  289 ASN   A CB  
923  C  CG  . ASN   A 133 ? 0.7634 1.2893 1.3040 0.1098  -0.0886 0.2740  289 ASN   A CG  
924  O  OD1 . ASN   A 133 ? 0.7455 1.2577 1.2933 0.1165  -0.0762 0.2665  289 ASN   A OD1 
925  N  ND2 . ASN   A 133 ? 0.7830 1.3329 1.3183 0.0926  -0.1023 0.2740  289 ASN   A ND2 
926  N  N   . ASP   A 134 ? 0.6411 1.1043 1.1604 0.1434  -0.0793 0.2907  290 ASP   A N   
927  C  CA  . ASP   A 134 ? 0.7188 1.1763 1.2408 0.1547  -0.0763 0.3030  290 ASP   A CA  
928  C  C   . ASP   A 134 ? 0.7103 1.1309 1.2315 0.1692  -0.0603 0.2974  290 ASP   A C   
929  O  O   . ASP   A 134 ? 0.7784 1.1940 1.3111 0.1825  -0.0511 0.3071  290 ASP   A O   
930  C  CB  . ASP   A 134 ? 0.6930 1.1555 1.1967 0.1446  -0.0909 0.3067  290 ASP   A CB  
931  C  CG  . ASP   A 134 ? 0.7234 1.2245 1.2302 0.1326  -0.1051 0.3162  290 ASP   A CG  
932  O  OD1 . ASP   A 134 ? 0.7304 1.2552 1.2562 0.1345  -0.1030 0.3231  290 ASP   A OD1 
933  O  OD2 . ASP   A 134 ? 0.7986 1.3061 1.2881 0.1207  -0.1181 0.3163  290 ASP   A OD2 
934  N  N   . ILE   A 135 ? 0.7334 1.1275 1.2410 0.1664  -0.0563 0.2817  291 ILE   A N   
935  C  CA  . ILE   A 135 ? 0.7351 1.0935 1.2405 0.1788  -0.0406 0.2751  291 ILE   A CA  
936  C  C   . ILE   A 135 ? 0.7565 1.1145 1.2811 0.1889  -0.0253 0.2735  291 ILE   A C   
937  O  O   . ILE   A 135 ? 0.7941 1.1358 1.3166 0.1893  -0.0163 0.2603  291 ILE   A O   
938  C  CB  . ILE   A 135 ? 0.7513 1.0819 1.2359 0.1726  -0.0410 0.2592  291 ILE   A CB  
939  C  CG1 . ILE   A 135 ? 0.7558 1.0871 1.2217 0.1632  -0.0556 0.2615  291 ILE   A CG1 
940  C  CG2 . ILE   A 135 ? 0.8079 1.1014 1.2890 0.1842  -0.0245 0.2518  291 ILE   A CG2 
941  C  CD1 . ILE   A 135 ? 0.6595 0.9689 1.1051 0.1549  -0.0588 0.2469  291 ILE   A CD1 
942  N  N   . ASP   A 139 ? 0.7422 1.0156 1.2602 0.2098  0.0193  0.2415  295 ASP   A N   
943  C  CA  . ASP   A 139 ? 0.7274 1.0046 1.2555 0.2110  0.0295  0.2335  295 ASP   A CA  
944  C  C   . ASP   A 139 ? 0.7428 1.0209 1.2600 0.1988  0.0232  0.2210  295 ASP   A C   
945  O  O   . ASP   A 139 ? 0.8636 1.1310 1.3809 0.1991  0.0339  0.2093  295 ASP   A O   
946  C  CB  . ASP   A 139 ? 0.7268 0.9733 1.2557 0.2220  0.0498  0.2251  295 ASP   A CB  
947  N  N   . VAL   A 140 ? 0.6962 0.9875 1.2037 0.1875  0.0060  0.2237  296 VAL   A N   
948  C  CA  . VAL   A 140 ? 0.6722 0.9654 1.1695 0.1749  -0.0014 0.2130  296 VAL   A CA  
949  C  C   . VAL   A 140 ? 0.6622 0.9886 1.1735 0.1677  -0.0069 0.2162  296 VAL   A C   
950  O  O   . VAL   A 140 ? 0.7152 1.0690 1.2389 0.1677  -0.0134 0.2289  296 VAL   A O   
951  C  CB  . VAL   A 140 ? 0.6683 0.9586 1.1476 0.1653  -0.0168 0.2134  296 VAL   A CB  
952  N  N   . ILE   A 141 ? 0.5966 0.9215 1.1060 0.1608  -0.0045 0.2050  297 ILE   A N   
953  C  CA  . ILE   A 141 ? 0.5664 0.9210 1.0871 0.1518  -0.0098 0.2063  297 ILE   A CA  
954  C  C   . ILE   A 141 ? 0.5498 0.9044 1.0573 0.1364  -0.0205 0.1974  297 ILE   A C   
955  O  O   . ILE   A 141 ? 0.5878 0.9090 1.0699 0.1323  -0.0176 0.1834  297 ILE   A O   
956  C  CB  . ILE   A 141 ? 0.5554 0.9106 1.0902 0.1589  0.0064  0.2020  297 ILE   A CB  
957  N  N   . MET   A 142 ? 0.5299 0.9132 1.0423 0.1238  -0.0320 0.2009  298 MET   A N   
958  C  CA  . MET   A 142 ? 0.5298 0.9058 1.0173 0.1044  -0.0427 0.1889  298 MET   A CA  
959  C  C   . MET   A 142 ? 0.5045 0.8924 0.9969 0.0950  -0.0400 0.1827  298 MET   A C   
960  O  O   . MET   A 142 ? 0.5925 1.0044 1.1103 0.1015  -0.0340 0.1908  298 MET   A O   
961  C  CB  . MET   A 142 ? 0.5535 0.9500 1.0368 0.0939  -0.0609 0.1971  298 MET   A CB  
962  C  CG  . MET   A 142 ? 0.4999 0.8801 0.9538 0.0757  -0.0702 0.1833  298 MET   A CG  
963  S  SD  . MET   A 142 ? 0.9340 1.3401 1.3830 0.0621  -0.0906 0.1919  298 MET   A SD  
964  C  CE  . MET   A 142 ? 0.5391 0.9645 0.9882 0.0423  -0.0971 0.1856  298 MET   A CE  
965  N  N   . LYS   A 143 ? 0.5137 0.8845 0.9819 0.0800  -0.0443 0.1688  299 LYS   A N   
966  C  CA  . LYS   A 143 ? 0.4582 0.8384 0.9271 0.0681  -0.0439 0.1627  299 LYS   A CA  
967  C  C   . LYS   A 143 ? 0.5339 0.9016 0.9767 0.0498  -0.0552 0.1526  299 LYS   A C   
968  O  O   . LYS   A 143 ? 0.4598 0.7980 0.8793 0.0485  -0.0557 0.1435  299 LYS   A O   
969  C  CB  . LYS   A 143 ? 0.5316 0.8937 1.0000 0.0744  -0.0274 0.1533  299 LYS   A CB  
970  N  N   . ARG   A 144 ? 0.5496 0.9400 0.9973 0.0358  -0.0638 0.1543  300 ARG   A N   
971  C  CA  . ARG   A 144 ? 0.4519 0.8316 0.8769 0.0177  -0.0736 0.1448  300 ARG   A CA  
972  C  C   . ARG   A 144 ? 0.4391 0.7929 0.8488 0.0126  -0.0651 0.1311  300 ARG   A C   
973  O  O   . ARG   A 144 ? 0.5358 0.8952 0.9572 0.0157  -0.0555 0.1307  300 ARG   A O   
974  C  CB  . ARG   A 144 ? 0.4598 0.8732 0.8963 0.0038  -0.0850 0.1515  300 ARG   A CB  
975  N  N   . LYS   A 145 ? 0.4378 0.7637 0.8213 0.0052  -0.0684 0.1203  301 LYS   A N   
976  C  CA  . LYS   A 145 ? 0.5348 0.8359 0.9029 0.0007  -0.0609 0.1083  301 LYS   A CA  
977  C  C   . LYS   A 145 ? 0.5207 0.8276 0.8841 -0.0168 -0.0666 0.1043  301 LYS   A C   
978  O  O   . LYS   A 145 ? 0.5578 0.8687 0.9132 -0.0284 -0.0778 0.1038  301 LYS   A O   
979  C  CB  . LYS   A 145 ? 0.5184 0.7860 0.8618 0.0028  -0.0601 0.0993  301 LYS   A CB  
980  C  CG  . LYS   A 145 ? 0.5568 0.7995 0.8832 -0.0024 -0.0537 0.0878  301 LYS   A CG  
981  C  CD  . LYS   A 145 ? 0.4826 0.7152 0.8126 0.0094  -0.0397 0.0853  301 LYS   A CD  
982  C  CE  . LYS   A 145 ? 0.4515 0.6650 0.7728 0.0207  -0.0360 0.0834  301 LYS   A CE  
983  N  NZ  . LYS   A 145 ? 0.5178 0.7055 0.8236 0.0231  -0.0264 0.0736  301 LYS   A NZ  
984  N  N   . GLY   A 148 ? 0.3904 0.6214 0.6636 -0.0733 -0.0948 0.0682  304 GLY   A N   
985  C  CA  . GLY   A 148 ? 0.3167 0.5529 0.5850 -0.0716 -0.1030 0.0709  304 GLY   A CA  
986  C  C   . GLY   A 148 ? 0.4013 0.6193 0.6606 -0.0576 -0.0992 0.0700  304 GLY   A C   
987  O  O   . GLY   A 148 ? 0.4756 0.7050 0.7397 -0.0508 -0.1034 0.0766  304 GLY   A O   
988  N  N   . SER   A 149 ? 0.4257 0.6166 0.6723 -0.0536 -0.0914 0.0624  305 SER   A N   
989  C  CA  . SER   A 149 ? 0.3953 0.5675 0.6325 -0.0414 -0.0870 0.0606  305 SER   A CA  
990  C  C   . SER   A 149 ? 0.5324 0.6962 0.7748 -0.0313 -0.0754 0.0597  305 SER   A C   
991  O  O   . SER   A 149 ? 0.4819 0.6316 0.7167 -0.0355 -0.0705 0.0536  305 SER   A O   
992  C  CB  . SER   A 149 ? 0.3545 0.5009 0.5683 -0.0468 -0.0891 0.0515  305 SER   A CB  
993  O  OG  . SER   A 149 ? 0.3397 0.4918 0.5461 -0.0554 -0.0990 0.0512  305 SER   A OG  
994  N  N   . PRO   A 150 ? 0.4259 0.5961 0.6797 -0.0180 -0.0703 0.0653  306 PRO   A N   
995  C  CA  . PRO   A 150 ? 0.4272 0.6114 0.6905 -0.0101 -0.0745 0.0738  306 PRO   A CA  
996  C  C   . PRO   A 150 ? 0.4291 0.6450 0.7107 -0.0147 -0.0814 0.0830  306 PRO   A C   
997  O  O   . PRO   A 150 ? 0.4281 0.6564 0.7197 -0.0207 -0.0798 0.0835  306 PRO   A O   
998  C  CB  . PRO   A 150 ? 0.4241 0.6028 0.6957 0.0050  -0.0634 0.0758  306 PRO   A CB  
999  C  CG  . PRO   A 150 ? 0.4215 0.5787 0.6812 0.0038  -0.0546 0.0661  306 PRO   A CG  
1000 C  CD  . PRO   A 150 ? 0.4218 0.5853 0.6805 -0.0096 -0.0585 0.0636  306 PRO   A CD  
1001 N  N   . ALA   A 151 ? 0.4353 0.6661 0.7220 -0.0126 -0.0891 0.0908  307 ALA   A N   
1002 C  CA  . ALA   A 151 ? 0.3589 0.6228 0.6627 -0.0179 -0.0972 0.1005  307 ALA   A CA  
1003 C  C   . ALA   A 151 ? 0.4067 0.6925 0.7364 -0.0046 -0.0918 0.1121  307 ALA   A C   
1004 O  O   . ALA   A 151 ? 0.3899 0.7029 0.7380 -0.0083 -0.0939 0.1188  307 ALA   A O   
1005 C  CB  . ALA   A 151 ? 0.3636 0.6350 0.6589 -0.0235 -0.1092 0.1039  307 ALA   A CB  
1006 N  N   . VAL   A 152 ? 0.4524 0.7268 0.7844 0.0107  -0.0847 0.1148  308 VAL   A N   
1007 C  CA  . VAL   A 152 ? 0.3852 0.6763 0.7418 0.0250  -0.0776 0.1254  308 VAL   A CA  
1008 C  C   . VAL   A 152 ? 0.3440 0.6091 0.6965 0.0379  -0.0640 0.1199  308 VAL   A C   
1009 O  O   . VAL   A 152 ? 0.3816 0.6187 0.7129 0.0368  -0.0622 0.1105  308 VAL   A O   
1010 C  CB  . VAL   A 152 ? 0.3541 0.6671 0.7233 0.0312  -0.0851 0.1395  308 VAL   A CB  
1011 C  CG1 . VAL   A 152 ? 0.3861 0.7297 0.7613 0.0178  -0.0987 0.1458  308 VAL   A CG1 
1012 C  CG2 . VAL   A 152 ? 0.3385 0.6294 0.6901 0.0355  -0.0872 0.1376  308 VAL   A CG2 
1013 N  N   . THR   A 153 ? 0.4077 0.6832 0.7810 0.0500  -0.0541 0.1260  309 THR   A N   
1014 C  CA  . THR   A 153 ? 0.4225 0.6762 0.7949 0.0632  -0.0403 0.1221  309 THR   A CA  
1015 C  C   . THR   A 153 ? 0.4562 0.7241 0.8509 0.0785  -0.0365 0.1353  309 THR   A C   
1016 O  O   . THR   A 153 ? 0.4755 0.7713 0.8940 0.0821  -0.0358 0.1452  309 THR   A O   
1017 C  CB  . THR   A 153 ? 0.4615 0.7102 0.8365 0.0631  -0.0286 0.1145  309 THR   A CB  
1018 O  OG1 . THR   A 153 ? 0.4381 0.6738 0.7932 0.0492  -0.0322 0.1036  309 THR   A OG1 
1019 C  CG2 . THR   A 153 ? 0.3739 0.6008 0.7473 0.0757  -0.0141 0.1097  309 THR   A CG2 
1020 N  N   . LEU   A 154 ? 0.4965 0.7457 0.8844 0.0876  -0.0337 0.1361  310 LEU   A N   
1021 C  CA  . LEU   A 154 ? 0.4619 0.7200 0.8704 0.1035  -0.0284 0.1487  310 LEU   A CA  
1022 C  C   . LEU   A 154 ? 0.4410 0.6809 0.8549 0.1154  -0.0105 0.1432  310 LEU   A C   
1023 O  O   . LEU   A 154 ? 0.5044 0.7152 0.8986 0.1134  -0.0040 0.1302  310 LEU   A O   
1024 C  CB  . LEU   A 154 ? 0.4399 0.6876 0.8389 0.1070  -0.0347 0.1538  310 LEU   A CB  
1025 C  CG  . LEU   A 154 ? 0.4099 0.6668 0.7954 0.0944  -0.0516 0.1560  310 LEU   A CG  
1026 C  CD1 . LEU   A 154 ? 0.4044 0.6433 0.7775 0.0995  -0.0537 0.1582  310 LEU   A CD1 
1027 C  CD2 . LEU   A 154 ? 0.4963 0.7926 0.9010 0.0908  -0.0624 0.1697  310 LEU   A CD2 
1028 N  N   . LEU   A 155 ? 0.5041 0.7615 0.9447 0.1276  -0.0022 0.1531  311 LEU   A N   
1029 C  CA  . LEU   A 155 ? 0.5173 0.7575 0.9655 0.1411  0.0159  0.1496  311 LEU   A CA  
1030 C  C   . LEU   A 155 ? 0.5655 0.7991 1.0229 0.1553  0.0189  0.1601  311 LEU   A C   
1031 O  O   . LEU   A 155 ? 0.6108 0.8696 1.0901 0.1627  0.0142  0.1765  311 LEU   A O   
1032 C  CB  . LEU   A 155 ? 0.4996 0.7607 0.9718 0.1468  0.0258  0.1531  311 LEU   A CB  
1033 C  CG  . LEU   A 155 ? 0.5286 0.7920 0.9927 0.1350  0.0277  0.1418  311 LEU   A CG  
1034 C  CD1 . LEU   A 155 ? 0.5385 0.7688 0.9719 0.1264  0.0299  0.1249  311 LEU   A CD1 
1035 C  CD2 . LEU   A 155 ? 0.5649 0.8573 1.0335 0.1222  0.0127  0.1476  311 LEU   A CD2 
1036 N  N   . ILE   A 156 ? 0.6469 0.8472 1.0876 0.1586  0.0264  0.1512  312 ILE   A N   
1037 C  CA  . ILE   A 156 ? 0.5298 0.7176 0.9761 0.1714  0.0308  0.1594  312 ILE   A CA  
1038 C  C   . ILE   A 156 ? 0.5786 0.7468 1.0329 0.1836  0.0514  0.1536  312 ILE   A C   
1039 O  O   . ILE   A 156 ? 0.7350 0.8814 1.1726 0.1783  0.0599  0.1374  312 ILE   A O   
1040 C  CB  . ILE   A 156 ? 0.5496 0.7138 0.9693 0.1644  0.0230  0.1535  312 ILE   A CB  
1041 C  CG1 . ILE   A 156 ? 0.5222 0.7073 0.9374 0.1551  0.0037  0.1621  312 ILE   A CG1 
1042 C  CG2 . ILE   A 156 ? 0.6657 0.8088 1.0883 0.1774  0.0320  0.1582  312 ILE   A CG2 
1043 C  CD1 . ILE   A 156 ? 0.5286 0.6931 0.9136 0.1432  -0.0048 0.1518  312 ILE   A CD1 
1044 N  N   . SER   A 157 ? 0.6811 0.8521 1.1469 0.1937  0.0580  0.1624  313 SER   A N   
1045 C  CA  . SER   A 157 ? 0.7211 0.8700 1.1881 0.2026  0.0774  0.1550  313 SER   A CA  
1046 C  C   . SER   A 157 ? 0.7654 0.9207 1.2384 0.2005  0.0869  0.1454  313 SER   A C   
1047 O  O   . SER   A 157 ? 0.7797 0.9630 1.2631 0.1950  0.0791  0.1493  313 SER   A O   
1048 C  CB  . SER   A 157 ? 0.7347 0.8464 1.1815 0.2029  0.0837  0.1451  313 SER   A CB  
1049 O  OG  . SER   A 157 ? 0.6893 0.7907 1.1380 0.2111  0.0870  0.1534  313 SER   A OG  
1050 N  N   . GLU   A 158 ? 0.8458 0.9754 1.3111 0.2036  0.1038  0.1323  314 GLU   A N   
1051 C  CA  . GLU   A 158 ? 0.7460 0.8821 1.2180 0.2031  0.1152  0.1242  314 GLU   A CA  
1052 C  C   . GLU   A 158 ? 0.7239 0.8649 1.1878 0.1920  0.1102  0.1149  314 GLU   A C   
1053 O  O   . GLU   A 158 ? 0.8224 0.9871 1.2947 0.1869  0.1075  0.1160  314 GLU   A O   
1054 C  CB  . GLU   A 158 ? 0.7383 0.8455 1.2031 0.2089  0.1349  0.1126  314 GLU   A CB  
1055 C  CG  . GLU   A 158 ? 0.8621 0.9343 1.3038 0.2058  0.1382  0.1016  314 GLU   A CG  
1056 C  CD  . GLU   A 158 ? 0.8786 0.9235 1.3127 0.2099  0.1573  0.0901  314 GLU   A CD  
1057 O  OE1 . GLU   A 158 ? 0.8473 0.9002 1.2945 0.2158  0.1683  0.0907  314 GLU   A OE1 
1058 O  OE2 . GLU   A 158 ? 0.9416 0.9573 1.3564 0.2067  0.1613  0.0803  314 GLU   A OE2 
1059 N  N   . LYS   A 159 ? 0.6649 0.7805 1.1008 0.1826  0.1061  0.1035  315 LYS   A N   
1060 C  CA  . LYS   A 159 ? 0.7261 0.8385 1.1396 0.1669  0.1011  0.0904  315 LYS   A CA  
1061 C  C   . LYS   A 159 ? 0.6896 0.7920 1.0792 0.1551  0.0854  0.0873  315 LYS   A C   
1062 O  O   . LYS   A 159 ? 0.7205 0.8068 1.0867 0.1445  0.0852  0.0742  315 LYS   A O   
1063 C  CB  . LYS   A 159 ? 0.7056 0.7951 1.1062 0.1658  0.1179  0.0742  315 LYS   A CB  
1064 N  N   . ILE   A 160 ? 0.6925 0.8050 1.0871 0.1564  0.0722  0.0994  316 ILE   A N   
1065 C  CA  . ILE   A 160 ? 0.6233 0.7287 0.9960 0.1449  0.0571  0.0968  316 ILE   A CA  
1066 C  C   . ILE   A 160 ? 0.5211 0.6549 0.8991 0.1361  0.0419  0.1039  316 ILE   A C   
1067 O  O   . ILE   A 160 ? 0.5684 0.7275 0.9685 0.1418  0.0378  0.1175  316 ILE   A O   
1068 C  CB  . ILE   A 160 ? 0.6385 0.7308 1.0081 0.1510  0.0535  0.1033  316 ILE   A CB  
1069 C  CG1 . ILE   A 160 ? 0.6671 0.7255 1.0217 0.1539  0.0656  0.0924  316 ILE   A CG1 
1070 C  CG2 . ILE   A 160 ? 0.5553 0.6510 0.9087 0.1398  0.0357  0.1048  316 ILE   A CG2 
1071 C  CD1 . ILE   A 160 ? 0.6641 0.7126 1.0277 0.1620  0.0848  0.0859  316 ILE   A CD1 
1072 N  N   . SER   A 161 ? 0.5331 0.6629 0.8911 0.1219  0.0338  0.0949  317 SER   A N   
1073 C  CA  . SER   A 161 ? 0.4782 0.6296 0.8364 0.1112  0.0190  0.0994  317 SER   A CA  
1074 C  C   . SER   A 161 ? 0.4417 0.5810 0.7785 0.1026  0.0066  0.0968  317 SER   A C   
1075 O  O   . SER   A 161 ? 0.4028 0.5165 0.7207 0.1015  0.0099  0.0878  317 SER   A O   
1076 C  CB  . SER   A 161 ? 0.4171 0.5748 0.7713 0.1012  0.0205  0.0916  317 SER   A CB  
1077 O  OG  . SER   A 161 ? 0.5833 0.7170 0.9203 0.0992  0.0302  0.0783  317 SER   A OG  
1078 N  N   . VAL   A 162 ? 0.4429 0.6014 0.7824 0.0961  -0.0074 0.1044  318 VAL   A N   
1079 C  CA  . VAL   A 162 ? 0.4515 0.6010 0.7708 0.0869  -0.0194 0.1017  318 VAL   A CA  
1080 C  C   . VAL   A 162 ? 0.3879 0.5558 0.7055 0.0736  -0.0312 0.1021  318 VAL   A C   
1081 O  O   . VAL   A 162 ? 0.4081 0.6019 0.7406 0.0729  -0.0390 0.1128  318 VAL   A O   
1082 C  CB  . VAL   A 162 ? 0.4338 0.5847 0.7561 0.0937  -0.0250 0.1119  318 VAL   A CB  
1083 C  CG1 . VAL   A 162 ? 0.4134 0.5490 0.7116 0.0849  -0.0341 0.1064  318 VAL   A CG1 
1084 C  CG2 . VAL   A 162 ? 0.4380 0.5749 0.7687 0.1084  -0.0123 0.1145  318 VAL   A CG2 
1085 N  N   . ASP   A 163 ? 0.3978 0.5528 0.6974 0.0627  -0.0324 0.0909  319 ASP   A N   
1086 C  CA  . ASP   A 163 ? 0.4151 0.5815 0.7090 0.0489  -0.0434 0.0897  319 ASP   A CA  
1087 C  C   . ASP   A 163 ? 0.3464 0.5083 0.6260 0.0433  -0.0548 0.0904  319 ASP   A C   
1088 O  O   . ASP   A 163 ? 0.3781 0.5177 0.6410 0.0446  -0.0537 0.0849  319 ASP   A O   
1089 C  CB  . ASP   A 163 ? 0.3461 0.4991 0.6266 0.0401  -0.0397 0.0783  319 ASP   A CB  
1090 C  CG  . ASP   A 163 ? 0.4644 0.6284 0.7595 0.0420  -0.0307 0.0784  319 ASP   A CG  
1091 O  OD1 . ASP   A 163 ? 0.3953 0.5799 0.7121 0.0490  -0.0282 0.0872  319 ASP   A OD1 
1092 O  OD2 . ASP   A 163 ? 0.5411 0.6943 0.8262 0.0364  -0.0262 0.0701  319 ASP   A OD2 
1093 N  N   . ILE   A 164 ? 0.3633 0.5474 0.6492 0.0364  -0.0657 0.0973  320 ILE   A N   
1094 C  CA  . ILE   A 164 ? 0.3849 0.5680 0.6576 0.0302  -0.0768 0.0983  320 ILE   A CA  
1095 C  C   . ILE   A 164 ? 0.3877 0.5736 0.6492 0.0140  -0.0847 0.0918  320 ILE   A C   
1096 O  O   . ILE   A 164 ? 0.3557 0.5620 0.6291 0.0075  -0.0877 0.0947  320 ILE   A O   
1097 C  CB  . ILE   A 164 ? 0.3330 0.5399 0.6209 0.0357  -0.0833 0.1127  320 ILE   A CB  
1098 C  CG1 . ILE   A 164 ? 0.3511 0.5507 0.6493 0.0524  -0.0741 0.1189  320 ILE   A CG1 
1099 C  CG2 . ILE   A 164 ? 0.3250 0.5329 0.5976 0.0273  -0.0952 0.1133  320 ILE   A CG2 
1100 C  CD1 . ILE   A 164 ? 0.3346 0.5600 0.6528 0.0602  -0.0787 0.1354  320 ILE   A CD1 
1101 N  N   . THR   A 165 ? 0.3992 0.5638 0.6383 0.0076  -0.0873 0.0828  321 THR   A N   
1102 C  CA  . THR   A 165 ? 0.3752 0.5374 0.6012 -0.0074 -0.0940 0.0756  321 THR   A CA  
1103 C  C   . THR   A 165 ? 0.4149 0.5832 0.6312 -0.0136 -0.1048 0.0780  321 THR   A C   
1104 O  O   . THR   A 165 ? 0.3474 0.5054 0.5552 -0.0074 -0.1052 0.0793  321 THR   A O   
1105 C  CB  . THR   A 165 ? 0.4207 0.5545 0.6289 -0.0102 -0.0881 0.0637  321 THR   A CB  
1106 O  OG1 . THR   A 165 ? 0.3372 0.4681 0.5539 -0.0057 -0.0785 0.0619  321 THR   A OG1 
1107 C  CG2 . THR   A 165 ? 0.3369 0.4659 0.5318 -0.0250 -0.0940 0.0563  321 THR   A CG2 
1108 N  N   . LEU   A 166 ? 0.2960 0.4818 0.5135 -0.0262 -0.1134 0.0788  322 LEU   A N   
1109 C  CA  . LEU   A 166 ? 0.3610 0.5503 0.5648 -0.0358 -0.1235 0.0778  322 LEU   A CA  
1110 C  C   . LEU   A 166 ? 0.3460 0.5089 0.5268 -0.0450 -0.1225 0.0642  322 LEU   A C   
1111 O  O   . LEU   A 166 ? 0.3815 0.5356 0.5606 -0.0512 -0.1187 0.0571  322 LEU   A O   
1112 C  CB  . LEU   A 166 ? 0.4261 0.6462 0.6405 -0.0468 -0.1330 0.0838  322 LEU   A CB  
1113 C  CG  . LEU   A 166 ? 0.3804 0.6055 0.5789 -0.0609 -0.1437 0.0806  322 LEU   A CG  
1114 C  CD1 . LEU   A 166 ? 0.3154 0.5420 0.5083 -0.0534 -0.1474 0.0872  322 LEU   A CD1 
1115 C  CD2 . LEU   A 166 ? 0.4306 0.6877 0.6405 -0.0733 -0.1526 0.0859  322 LEU   A CD2 
1116 N  N   . ALA   A 167 ? 0.3278 0.4784 0.4916 -0.0457 -0.1255 0.0611  323 ALA   A N   
1117 C  CA  . ALA   A 167 ? 0.3400 0.4652 0.4825 -0.0529 -0.1237 0.0487  323 ALA   A CA  
1118 C  C   . ALA   A 167 ? 0.4548 0.5827 0.5819 -0.0623 -0.1322 0.0465  323 ALA   A C   
1119 O  O   . ALA   A 167 ? 0.4172 0.5496 0.5414 -0.0567 -0.1355 0.0523  323 ALA   A O   
1120 C  CB  . ALA   A 167 ? 0.3542 0.4544 0.4892 -0.0417 -0.1150 0.0449  323 ALA   A CB  
1121 N  N   . LEU   A 168 ? 0.4148 0.5397 0.5316 -0.0769 -0.1354 0.0381  324 LEU   A N   
1122 C  CA  . LEU   A 168 ? 0.3582 0.4804 0.4565 -0.0869 -0.1416 0.0328  324 LEU   A CA  
1123 C  C   . LEU   A 168 ? 0.4103 0.5042 0.4912 -0.0815 -0.1359 0.0254  324 LEU   A C   
1124 O  O   . LEU   A 168 ? 0.4122 0.4852 0.4912 -0.0771 -0.1276 0.0197  324 LEU   A O   
1125 C  CB  . LEU   A 168 ? 0.3595 0.4821 0.4509 -0.1044 -0.1447 0.0241  324 LEU   A CB  
1126 C  CG  . LEU   A 168 ? 0.4241 0.5723 0.5311 -0.1132 -0.1497 0.0289  324 LEU   A CG  
1127 C  CD1 . LEU   A 168 ? 0.4612 0.6030 0.5565 -0.1317 -0.1516 0.0177  324 LEU   A CD1 
1128 C  CD2 . LEU   A 168 ? 0.3982 0.5803 0.5167 -0.1124 -0.1592 0.0417  324 LEU   A CD2 
1129 N  N   . GLU   A 169 ? 0.3696 0.4639 0.4381 -0.0819 -0.1402 0.0262  325 GLU   A N   
1130 C  CA  . GLU   A 169 ? 0.3724 0.4422 0.4237 -0.0781 -0.1354 0.0192  325 GLU   A CA  
1131 C  C   . GLU   A 169 ? 0.4807 0.5428 0.5121 -0.0920 -0.1383 0.0088  325 GLU   A C   
1132 O  O   . GLU   A 169 ? 0.4758 0.5559 0.5031 -0.1019 -0.1466 0.0105  325 GLU   A O   
1133 C  CB  . GLU   A 169 ? 0.4150 0.4883 0.4660 -0.0672 -0.1364 0.0277  325 GLU   A CB  
1134 C  CG  . GLU   A 169 ? 0.5215 0.5716 0.5545 -0.0639 -0.1319 0.0211  325 GLU   A CG  
1135 C  CD  . GLU   A 169 ? 0.5063 0.5604 0.5397 -0.0538 -0.1330 0.0303  325 GLU   A CD  
1136 O  OE1 . GLU   A 169 ? 0.4911 0.5600 0.5192 -0.0580 -0.1405 0.0353  325 GLU   A OE1 
1137 O  OE2 . GLU   A 169 ? 0.4716 0.5146 0.5106 -0.0423 -0.1264 0.0326  325 GLU   A OE2 
1138 N  N   . SER   A 170 ? 0.3965 0.4324 0.4157 -0.0928 -0.1311 -0.0018 326 SER   A N   
1139 C  CA  . SER   A 170 ? 0.5402 0.5642 0.5396 -0.1042 -0.1315 -0.0128 326 SER   A CA  
1140 C  C   . SER   A 170 ? 0.5963 0.5994 0.5826 -0.0965 -0.1257 -0.0169 326 SER   A C   
1141 O  O   . SER   A 170 ? 0.4898 0.4762 0.4793 -0.0877 -0.1179 -0.0183 326 SER   A O   
1142 C  CB  . SER   A 170 ? 0.4474 0.4591 0.4449 -0.1144 -0.1277 -0.0226 326 SER   A CB  
1143 O  OG  . SER   A 170 ? 0.5223 0.5184 0.5003 -0.1242 -0.1260 -0.0343 326 SER   A OG  
1144 N  N   . LYS   A 171 ? 0.5092 0.5146 0.4807 -0.1004 -0.1294 -0.0184 327 LYS   A N   
1145 C  CA  . LYS   A 171 ? 0.5789 0.5653 0.5367 -0.0947 -0.1238 -0.0230 327 LYS   A CA  
1146 C  C   . LYS   A 171 ? 0.5528 0.5180 0.4954 -0.1029 -0.1181 -0.0368 327 LYS   A C   
1147 O  O   . LYS   A 171 ? 0.6052 0.5563 0.5348 -0.1002 -0.1138 -0.0416 327 LYS   A O   
1148 C  CB  . LYS   A 171 ? 0.5607 0.5592 0.5100 -0.0941 -0.1296 -0.0174 327 LYS   A CB  
1149 C  CG  . LYS   A 171 ? 0.5582 0.5718 0.5226 -0.0826 -0.1326 -0.0033 327 LYS   A CG  
1150 C  CD  . LYS   A 171 ? 0.6406 0.6658 0.5969 -0.0817 -0.1382 0.0036  327 LYS   A CD  
1151 C  CE  . LYS   A 171 ? 0.7286 0.7603 0.6992 -0.0677 -0.1378 0.0166  327 LYS   A CE  
1152 N  NZ  . LYS   A 171 ? 0.6399 0.6924 0.6305 -0.0656 -0.1424 0.0264  327 LYS   A NZ  
1153 N  N   . SER   A 172 ? 0.5727 0.5348 0.5174 -0.1123 -0.1173 -0.0429 328 SER   A N   
1154 C  CA  . SER   A 172 ? 0.5506 0.4908 0.4824 -0.1199 -0.1107 -0.0559 328 SER   A CA  
1155 C  C   . SER   A 172 ? 0.6441 0.5627 0.5815 -0.1100 -0.1008 -0.0576 328 SER   A C   
1156 O  O   . SER   A 172 ? 0.5926 0.5140 0.5430 -0.0987 -0.0994 -0.0496 328 SER   A O   
1157 C  CB  . SER   A 172 ? 0.6267 0.5723 0.5583 -0.1353 -0.1139 -0.0616 328 SER   A CB  
1158 O  OG  . SER   A 172 ? 0.6685 0.6178 0.6179 -0.1330 -0.1130 -0.0568 328 SER   A OG  
1159 N  N   . SER   A 173 ? 0.5516 0.4487 0.4786 -0.1146 -0.0936 -0.0682 329 SER   A N   
1160 C  CA  . SER   A 173 ? 0.6043 0.4813 0.5360 -0.1064 -0.0841 -0.0698 329 SER   A CA  
1161 C  C   . SER   A 173 ? 0.5398 0.4210 0.4884 -0.1051 -0.0838 -0.0646 329 SER   A C   
1162 O  O   . SER   A 173 ? 0.4875 0.3791 0.4409 -0.1149 -0.0884 -0.0649 329 SER   A O   
1163 C  CB  . SER   A 173 ? 0.7035 0.5580 0.6222 -0.1132 -0.0765 -0.0819 329 SER   A CB  
1164 O  OG  . SER   A 173 ? 0.8156 0.6607 0.7223 -0.1079 -0.0726 -0.0850 329 SER   A OG  
1165 N  N   . TRP   A 174 ? 0.5543 0.4289 0.5119 -0.0934 -0.0786 -0.0595 330 TRP   A N   
1166 C  CA  . TRP   A 174 ? 0.5285 0.4070 0.5015 -0.0915 -0.0775 -0.0544 330 TRP   A CA  
1167 C  C   . TRP   A 174 ? 0.4476 0.3132 0.4199 -0.1014 -0.0734 -0.0611 330 TRP   A C   
1168 O  O   . TRP   A 174 ? 0.4986 0.3456 0.4597 -0.1049 -0.0680 -0.0693 330 TRP   A O   
1169 C  CB  . TRP   A 174 ? 0.4518 0.3242 0.4319 -0.0784 -0.0719 -0.0489 330 TRP   A CB  
1170 C  CG  . TRP   A 174 ? 0.4500 0.3341 0.4330 -0.0686 -0.0749 -0.0419 330 TRP   A CG  
1171 C  CD1 . TRP   A 174 ? 0.4583 0.3548 0.4369 -0.0690 -0.0812 -0.0398 330 TRP   A CD1 
1172 C  CD2 . TRP   A 174 ? 0.4374 0.3213 0.4282 -0.0575 -0.0712 -0.0361 330 TRP   A CD2 
1173 N  NE1 . TRP   A 174 ? 0.4529 0.3551 0.4368 -0.0585 -0.0811 -0.0330 330 TRP   A NE1 
1174 C  CE2 . TRP   A 174 ? 0.4494 0.3439 0.4403 -0.0518 -0.0750 -0.0313 330 TRP   A CE2 
1175 C  CE3 . TRP   A 174 ? 0.4493 0.3254 0.4466 -0.0525 -0.0650 -0.0342 330 TRP   A CE3 
1176 C  CZ2 . TRP   A 174 ? 0.4215 0.3173 0.4181 -0.0419 -0.0722 -0.0260 330 TRP   A CZ2 
1177 C  CZ3 . TRP   A 174 ? 0.4867 0.3664 0.4893 -0.0429 -0.0630 -0.0288 330 TRP   A CZ3 
1178 C  CH2 . TRP   A 174 ? 0.4967 0.3854 0.4987 -0.0380 -0.0664 -0.0254 330 TRP   A CH2 
1179 N  N   . PRO   A 175 ? 0.4701 0.3445 0.4542 -0.1060 -0.0753 -0.0578 331 PRO   A N   
1180 C  CA  . PRO   A 175 ? 0.4942 0.3563 0.4778 -0.1167 -0.0716 -0.0639 331 PRO   A CA  
1181 C  C   . PRO   A 175 ? 0.5469 0.3854 0.5302 -0.1107 -0.0614 -0.0656 331 PRO   A C   
1182 O  O   . PRO   A 175 ? 0.5335 0.3695 0.5211 -0.0984 -0.0579 -0.0601 331 PRO   A O   
1183 C  CB  . PRO   A 175 ? 0.5340 0.4138 0.5330 -0.1201 -0.0758 -0.0573 331 PRO   A CB  
1184 C  CG  . PRO   A 175 ? 0.5297 0.4340 0.5338 -0.1155 -0.0840 -0.0501 331 PRO   A CG  
1185 C  CD  . PRO   A 175 ? 0.5283 0.4257 0.5263 -0.1030 -0.0814 -0.0486 331 PRO   A CD  
1186 N  N   . ALA   A 176 ? 0.5082 0.3299 0.4873 -0.1202 -0.0565 -0.0729 332 ALA   A N   
1187 C  CA  . ALA   A 176 ? 0.5192 0.3163 0.4968 -0.1154 -0.0461 -0.0751 332 ALA   A CA  
1188 C  C   . ALA   A 176 ? 0.4726 0.2709 0.4642 -0.1056 -0.0426 -0.0653 332 ALA   A C   
1189 O  O   . ALA   A 176 ? 0.5396 0.3250 0.5311 -0.0960 -0.0358 -0.0631 332 ALA   A O   
1190 C  CB  . ALA   A 176 ? 0.5765 0.3559 0.5486 -0.1287 -0.0414 -0.0844 332 ALA   A CB  
1191 N  N   . SER   A 177 ? 0.5109 0.3257 0.5143 -0.1078 -0.0470 -0.0591 333 SER   A N   
1192 C  CA  . SER   A 177 ? 0.5613 0.3794 0.5772 -0.0997 -0.0439 -0.0499 333 SER   A CA  
1193 C  C   . SER   A 177 ? 0.5632 0.3867 0.5798 -0.0857 -0.0435 -0.0441 333 SER   A C   
1194 O  O   . SER   A 177 ? 0.4733 0.2968 0.4976 -0.0783 -0.0396 -0.0373 333 SER   A O   
1195 C  CB  . SER   A 177 ? 0.5872 0.4254 0.6150 -0.1050 -0.0493 -0.0449 333 SER   A CB  
1196 O  OG  . SER   A 177 ? 0.5090 0.3687 0.5384 -0.1026 -0.0572 -0.0423 333 SER   A OG  
1197 N  N   . THR   A 178 ? 0.5285 0.3573 0.5372 -0.0825 -0.0473 -0.0465 334 THR   A N   
1198 C  CA  . THR   A 178 ? 0.5772 0.4108 0.5861 -0.0704 -0.0469 -0.0416 334 THR   A CA  
1199 C  C   . THR   A 178 ? 0.4880 0.3046 0.4881 -0.0645 -0.0408 -0.0445 334 THR   A C   
1200 O  O   . THR   A 178 ? 0.4440 0.2635 0.4439 -0.0552 -0.0398 -0.0407 334 THR   A O   
1201 C  CB  . THR   A 178 ? 0.5354 0.3855 0.5420 -0.0694 -0.0544 -0.0409 334 THR   A CB  
1202 O  OG1 . THR   A 178 ? 0.5319 0.3760 0.5258 -0.0748 -0.0562 -0.0482 334 THR   A OG1 
1203 C  CG2 . THR   A 178 ? 0.4187 0.2871 0.4350 -0.0752 -0.0605 -0.0376 334 THR   A CG2 
1204 N  N   . GLN   A 179 ? 0.5648 0.3636 0.5584 -0.0701 -0.0360 -0.0512 335 GLN   A N   
1205 C  CA  . GLN   A 179 ? 0.5855 0.3687 0.5704 -0.0649 -0.0299 -0.0549 335 GLN   A CA  
1206 C  C   . GLN   A 179 ? 0.6016 0.3822 0.5925 -0.0534 -0.0246 -0.0475 335 GLN   A C   
1207 O  O   . GLN   A 179 ? 0.5279 0.3054 0.5136 -0.0463 -0.0223 -0.0476 335 GLN   A O   
1208 C  CB  . GLN   A 179 ? 0.5636 0.3261 0.5425 -0.0725 -0.0238 -0.0631 335 GLN   A CB  
1209 C  CG  . GLN   A 179 ? 0.6481 0.3962 0.6160 -0.0685 -0.0180 -0.0690 335 GLN   A CG  
1210 C  CD  . GLN   A 179 ? 0.8731 0.5974 0.8359 -0.0741 -0.0094 -0.0769 335 GLN   A CD  
1211 O  OE1 . GLN   A 179 ? 0.8724 0.5908 0.8368 -0.0842 -0.0090 -0.0805 335 GLN   A OE1 
1212 N  NE2 . GLN   A 179 ? 0.9602 0.6703 0.9177 -0.0674 -0.0016 -0.0796 335 GLN   A NE2 
1213 N  N   . GLU   A 180 ? 0.5475 0.3299 0.5491 -0.0520 -0.0226 -0.0408 336 GLU   A N   
1214 C  CA  . GLU   A 180 ? 0.5249 0.3065 0.5321 -0.0421 -0.0178 -0.0331 336 GLU   A CA  
1215 C  C   . GLU   A 180 ? 0.5303 0.3308 0.5433 -0.0371 -0.0222 -0.0262 336 GLU   A C   
1216 O  O   . GLU   A 180 ? 0.5312 0.3343 0.5490 -0.0303 -0.0191 -0.0193 336 GLU   A O   
1217 C  CB  . GLU   A 180 ? 0.5738 0.3434 0.5881 -0.0433 -0.0114 -0.0295 336 GLU   A CB  
1218 C  CG  . GLU   A 180 ? 0.5971 0.3453 0.6058 -0.0483 -0.0056 -0.0369 336 GLU   A CG  
1219 C  CD  . GLU   A 180 ? 0.7564 0.4939 0.7581 -0.0411 -0.0004 -0.0396 336 GLU   A CD  
1220 O  OE1 . GLU   A 180 ? 0.7623 0.5084 0.7659 -0.0317 -0.0004 -0.0336 336 GLU   A OE1 
1221 O  OE2 . GLU   A 180 ? 0.8097 0.5309 0.8037 -0.0456 0.0038  -0.0483 336 GLU   A OE2 
1222 N  N   . GLY   A 181 ? 0.4598 0.2738 0.4726 -0.0403 -0.0290 -0.0277 337 GLY   A N   
1223 C  CA  . GLY   A 181 ? 0.4545 0.2849 0.4730 -0.0359 -0.0322 -0.0221 337 GLY   A CA  
1224 C  C   . GLY   A 181 ? 0.4567 0.2914 0.4696 -0.0291 -0.0334 -0.0220 337 GLY   A C   
1225 O  O   . GLY   A 181 ? 0.4484 0.2742 0.4537 -0.0267 -0.0313 -0.0251 337 GLY   A O   
1226 N  N   . LEU   A 182 ? 0.4172 0.2656 0.4343 -0.0261 -0.0362 -0.0184 338 LEU   A N   
1227 C  CA  . LEU   A 182 ? 0.4363 0.2897 0.4491 -0.0204 -0.0374 -0.0179 338 LEU   A CA  
1228 C  C   . LEU   A 182 ? 0.4351 0.2808 0.4432 -0.0151 -0.0328 -0.0171 338 LEU   A C   
1229 O  O   . LEU   A 182 ? 0.3958 0.2378 0.3964 -0.0130 -0.0329 -0.0198 338 LEU   A O   
1230 C  CB  . LEU   A 182 ? 0.4239 0.2794 0.4308 -0.0229 -0.0425 -0.0221 338 LEU   A CB  
1231 C  CG  . LEU   A 182 ? 0.4050 0.2670 0.4087 -0.0181 -0.0447 -0.0211 338 LEU   A CG  
1232 C  CD1 . LEU   A 182 ? 0.3616 0.2357 0.3739 -0.0155 -0.0456 -0.0167 338 LEU   A CD1 
1233 C  CD2 . LEU   A 182 ? 0.3886 0.2515 0.3855 -0.0214 -0.0496 -0.0245 338 LEU   A CD2 
1234 N  N   . ARG   A 183 ? 0.4292 0.2740 0.4423 -0.0129 -0.0285 -0.0123 339 ARG   A N   
1235 C  CA  . ARG   A 183 ? 0.4634 0.3024 0.4741 -0.0079 -0.0239 -0.0100 339 ARG   A CA  
1236 C  C   . ARG   A 183 ? 0.4379 0.2861 0.4465 -0.0031 -0.0243 -0.0076 339 ARG   A C   
1237 O  O   . ARG   A 183 ? 0.4670 0.3212 0.4788 -0.0002 -0.0219 -0.0023 339 ARG   A O   
1238 C  CB  . ARG   A 183 ? 0.5305 0.3663 0.5479 -0.0075 -0.0195 -0.0045 339 ARG   A CB  
1239 C  CG  . ARG   A 183 ? 0.5929 0.4147 0.6110 -0.0118 -0.0171 -0.0074 339 ARG   A CG  
1240 C  CD  . ARG   A 183 ? 0.7516 0.5610 0.7689 -0.0074 -0.0108 -0.0059 339 ARG   A CD  
1241 N  NE  . ARG   A 183 ? 0.7941 0.6035 0.8048 -0.0027 -0.0104 -0.0080 339 ARG   A NE  
1242 C  CZ  . ARG   A 183 ? 0.8031 0.6071 0.8140 0.0032  -0.0051 -0.0050 339 ARG   A CZ  
1243 N  NH1 . ARG   A 183 ? 0.8066 0.6035 0.8241 0.0056  0.0004  0.0006  339 ARG   A NH1 
1244 N  NH2 . ARG   A 183 ? 0.8380 0.6440 0.8432 0.0069  -0.0051 -0.0070 339 ARG   A NH2 
1245 N  N   . ILE   A 184 ? 0.4087 0.2581 0.4114 -0.0028 -0.0273 -0.0115 340 ILE   A N   
1246 C  CA  . ILE   A 184 ? 0.3795 0.2360 0.3792 0.0004  -0.0279 -0.0105 340 ILE   A CA  
1247 C  C   . ILE   A 184 ? 0.4171 0.2693 0.4110 0.0038  -0.0254 -0.0110 340 ILE   A C   
1248 O  O   . ILE   A 184 ? 0.4113 0.2687 0.4020 0.0058  -0.0259 -0.0106 340 ILE   A O   
1249 C  CB  . ILE   A 184 ? 0.4016 0.2623 0.3994 -0.0010 -0.0323 -0.0134 340 ILE   A CB  
1250 C  CG1 . ILE   A 184 ? 0.4115 0.2654 0.4028 -0.0031 -0.0347 -0.0180 340 ILE   A CG1 
1251 C  CG2 . ILE   A 184 ? 0.3926 0.2599 0.3977 -0.0036 -0.0343 -0.0122 340 ILE   A CG2 
1252 C  CD1 . ILE   A 184 ? 0.3351 0.1944 0.3248 -0.0043 -0.0395 -0.0192 340 ILE   A CD1 
1253 N  N   . GLN   A 185 ? 0.3652 0.2078 0.3579 0.0045  -0.0223 -0.0119 341 GLN   A N   
1254 C  CA  . GLN   A 185 ? 0.4235 0.2617 0.4106 0.0078  -0.0196 -0.0132 341 GLN   A CA  
1255 C  C   . GLN   A 185 ? 0.4906 0.3375 0.4796 0.0120  -0.0175 -0.0078 341 GLN   A C   
1256 O  O   . GLN   A 185 ? 0.4170 0.2660 0.4011 0.0139  -0.0172 -0.0087 341 GLN   A O   
1257 C  CB  . GLN   A 185 ? 0.4477 0.2733 0.4347 0.0084  -0.0150 -0.0148 341 GLN   A CB  
1258 C  CG  . GLN   A 185 ? 0.5702 0.3862 0.5532 0.0030  -0.0165 -0.0215 341 GLN   A CG  
1259 C  CD  . GLN   A 185 ? 0.5802 0.3935 0.5698 -0.0008 -0.0166 -0.0203 341 GLN   A CD  
1260 O  OE1 . GLN   A 185 ? 0.5551 0.3764 0.5518 0.0002  -0.0171 -0.0146 341 GLN   A OE1 
1261 N  NE2 . GLN   A 185 ? 0.6516 0.4542 0.6384 -0.0058 -0.0159 -0.0259 341 GLN   A NE2 
1262 N  N   . ASN   A 186 ? 0.3598 0.2128 0.3556 0.0131  -0.0159 -0.0018 342 ASN   A N   
1263 C  CA  . ASN   A 186 ? 0.4148 0.2783 0.4119 0.0160  -0.0144 0.0036  342 ASN   A CA  
1264 C  C   . ASN   A 186 ? 0.4116 0.2854 0.4064 0.0136  -0.0174 0.0029  342 ASN   A C   
1265 O  O   . ASN   A 186 ? 0.4006 0.2839 0.3948 0.0145  -0.0166 0.0060  342 ASN   A O   
1266 C  CB  . ASN   A 186 ? 0.4597 0.3273 0.4644 0.0179  -0.0114 0.0113  342 ASN   A CB  
1267 C  CG  . ASN   A 186 ? 0.6074 0.4637 0.6155 0.0213  -0.0068 0.0129  342 ASN   A CG  
1268 O  OD1 . ASN   A 186 ? 0.6849 0.5341 0.6894 0.0238  -0.0046 0.0098  342 ASN   A OD1 
1269 N  ND2 . ASN   A 186 ? 0.7325 0.5867 0.7474 0.0216  -0.0046 0.0181  342 ASN   A ND2 
1270 N  N   . TRP   A 187 ? 0.3822 0.2545 0.3759 0.0106  -0.0206 -0.0012 343 TRP   A N   
1271 C  CA  . TRP   A 187 ? 0.4054 0.2852 0.3979 0.0086  -0.0223 -0.0023 343 TRP   A CA  
1272 C  C   . TRP   A 187 ? 0.4118 0.2874 0.3985 0.0083  -0.0247 -0.0070 343 TRP   A C   
1273 O  O   . TRP   A 187 ? 0.3933 0.2715 0.3757 0.0087  -0.0241 -0.0073 343 TRP   A O   
1274 C  CB  . TRP   A 187 ? 0.3662 0.2486 0.3639 0.0063  -0.0232 -0.0019 343 TRP   A CB  
1275 C  CG  . TRP   A 187 ? 0.3399 0.2270 0.3374 0.0046  -0.0244 -0.0043 343 TRP   A CG  
1276 C  CD1 . TRP   A 187 ? 0.3701 0.2609 0.3635 0.0044  -0.0238 -0.0057 343 TRP   A CD1 
1277 C  CD2 . TRP   A 187 ? 0.3221 0.2097 0.3241 0.0031  -0.0259 -0.0057 343 TRP   A CD2 
1278 N  NE1 . TRP   A 187 ? 0.3581 0.2503 0.3535 0.0033  -0.0240 -0.0080 343 TRP   A NE1 
1279 C  CE2 . TRP   A 187 ? 0.3722 0.2634 0.3733 0.0029  -0.0255 -0.0077 343 TRP   A CE2 
1280 C  CE3 . TRP   A 187 ? 0.3644 0.2500 0.3716 0.0017  -0.0272 -0.0053 343 TRP   A CE3 
1281 C  CZ2 . TRP   A 187 ? 0.3957 0.2890 0.4019 0.0025  -0.0261 -0.0088 343 TRP   A CZ2 
1282 C  CZ3 . TRP   A 187 ? 0.3591 0.2484 0.3712 0.0004  -0.0285 -0.0063 343 TRP   A CZ3 
1283 C  CH2 . TRP   A 187 ? 0.3378 0.2312 0.3499 0.0014  -0.0278 -0.0077 343 TRP   A CH2 
1284 N  N   . LEU   A 188 ? 0.3566 0.2266 0.3432 0.0071  -0.0273 -0.0100 344 LEU   A N   
1285 C  CA  . LEU   A 188 ? 0.4251 0.2925 0.4066 0.0068  -0.0298 -0.0131 344 LEU   A CA  
1286 C  C   . LEU   A 188 ? 0.3920 0.2526 0.3671 0.0075  -0.0297 -0.0153 344 LEU   A C   
1287 O  O   . LEU   A 188 ? 0.3825 0.2419 0.3522 0.0074  -0.0313 -0.0169 344 LEU   A O   
1288 C  CB  . LEU   A 188 ? 0.4113 0.2791 0.3962 0.0050  -0.0331 -0.0143 344 LEU   A CB  
1289 C  CG  . LEU   A 188 ? 0.3969 0.2714 0.3882 0.0047  -0.0323 -0.0126 344 LEU   A CG  
1290 C  CD1 . LEU   A 188 ? 0.3960 0.2726 0.3926 0.0035  -0.0353 -0.0129 344 LEU   A CD1 
1291 C  CD2 . LEU   A 188 ? 0.3828 0.2597 0.3713 0.0058  -0.0308 -0.0128 344 LEU   A CD2 
1292 N  N   . SER   A 189 ? 0.3626 0.2183 0.3384 0.0081  -0.0273 -0.0152 345 SER   A N   
1293 C  CA  . SER   A 189 ? 0.4057 0.2545 0.3760 0.0094  -0.0251 -0.0175 345 SER   A CA  
1294 C  C   . SER   A 189 ? 0.4230 0.2631 0.3909 0.0065  -0.0260 -0.0218 345 SER   A C   
1295 O  O   . SER   A 189 ? 0.4012 0.2421 0.3702 0.0031  -0.0299 -0.0233 345 SER   A O   
1296 C  CB  . SER   A 189 ? 0.4662 0.3159 0.4291 0.0100  -0.0258 -0.0189 345 SER   A CB  
1297 O  OG  . SER   A 189 ? 0.4271 0.2752 0.3857 0.0072  -0.0300 -0.0218 345 SER   A OG  
1298 N  N   . ALA   A 190 ? 0.4213 0.2534 0.3860 0.0078  -0.0220 -0.0239 346 ALA   A N   
1299 C  CA  . ALA   A 190 ? 0.4212 0.2436 0.3816 0.0041  -0.0218 -0.0294 346 ALA   A CA  
1300 C  C   . ALA   A 190 ? 0.4402 0.2635 0.3918 0.0005  -0.0262 -0.0336 346 ALA   A C   
1301 O  O   . ALA   A 190 ? 0.4588 0.2789 0.4074 -0.0047 -0.0288 -0.0376 346 ALA   A O   
1302 C  CB  . ALA   A 190 ? 0.4134 0.2260 0.3722 0.0069  -0.0149 -0.0311 346 ALA   A CB  
1303 N  N   . LYS   A 191 ? 0.4216 0.2499 0.3689 0.0027  -0.0269 -0.0323 347 LYS   A N   
1304 C  CA  . LYS   A 191 ? 0.4606 0.2915 0.4002 -0.0002 -0.0314 -0.0343 347 LYS   A CA  
1305 C  C   . LYS   A 191 ? 0.4985 0.3360 0.4426 -0.0029 -0.0373 -0.0324 347 LYS   A C   
1306 O  O   . LYS   A 191 ? 0.4520 0.2903 0.3921 -0.0073 -0.0415 -0.0347 347 LYS   A O   
1307 C  CB  . LYS   A 191 ? 0.5045 0.3397 0.4405 0.0029  -0.0306 -0.0318 347 LYS   A CB  
1308 C  CG  . LYS   A 191 ? 0.6701 0.5026 0.5948 0.0013  -0.0304 -0.0353 347 LYS   A CG  
1309 C  CD  . LYS   A 191 ? 0.6237 0.4617 0.5456 0.0033  -0.0308 -0.0318 347 LYS   A CD  
1310 C  CE  . LYS   A 191 ? 0.5562 0.3968 0.4835 0.0075  -0.0265 -0.0286 347 LYS   A CE  
1311 N  NZ  . LYS   A 191 ? 0.7566 0.5929 0.6822 0.0099  -0.0204 -0.0306 347 LYS   A NZ  
1312 N  N   . VAL   A 192 ? 0.4666 0.3098 0.4189 -0.0004 -0.0377 -0.0280 348 VAL   A N   
1313 C  CA  . VAL   A 192 ? 0.4019 0.2518 0.3598 -0.0019 -0.0423 -0.0258 348 VAL   A CA  
1314 C  C   . VAL   A 192 ? 0.4115 0.2605 0.3732 -0.0061 -0.0441 -0.0277 348 VAL   A C   
1315 O  O   . VAL   A 192 ? 0.4355 0.2893 0.3977 -0.0095 -0.0489 -0.0277 348 VAL   A O   
1316 C  CB  . VAL   A 192 ? 0.4605 0.3157 0.4257 0.0014  -0.0408 -0.0218 348 VAL   A CB  
1317 C  CG1 . VAL   A 192 ? 0.4136 0.2751 0.3864 0.0004  -0.0440 -0.0197 348 VAL   A CG1 
1318 C  CG2 . VAL   A 192 ? 0.4680 0.3243 0.4287 0.0038  -0.0400 -0.0204 348 VAL   A CG2 
1319 N  N   . ARG   A 193 ? 0.4065 0.2497 0.3710 -0.0063 -0.0402 -0.0288 349 ARG   A N   
1320 C  CA  . ARG   A 193 ? 0.4373 0.2782 0.4051 -0.0111 -0.0414 -0.0308 349 ARG   A CA  
1321 C  C   . ARG   A 193 ? 0.4331 0.2713 0.3926 -0.0169 -0.0444 -0.0360 349 ARG   A C   
1322 O  O   . ARG   A 193 ? 0.3875 0.2306 0.3492 -0.0222 -0.0489 -0.0366 349 ARG   A O   
1323 C  CB  . ARG   A 193 ? 0.4533 0.2860 0.4244 -0.0103 -0.0358 -0.0310 349 ARG   A CB  
1324 C  CG  . ARG   A 193 ? 0.4313 0.2613 0.4068 -0.0159 -0.0366 -0.0326 349 ARG   A CG  
1325 C  CD  . ARG   A 193 ? 0.4723 0.2928 0.4518 -0.0147 -0.0305 -0.0318 349 ARG   A CD  
1326 N  NE  . ARG   A 193 ? 0.5004 0.3187 0.4854 -0.0204 -0.0310 -0.0324 349 ARG   A NE  
1327 C  CZ  . ARG   A 193 ? 0.5857 0.3946 0.5668 -0.0269 -0.0304 -0.0382 349 ARG   A CZ  
1328 N  NH1 . ARG   A 193 ? 0.5529 0.3539 0.5237 -0.0290 -0.0294 -0.0445 349 ARG   A NH1 
1329 N  NH2 . ARG   A 193 ? 0.5462 0.3535 0.5334 -0.0322 -0.0304 -0.0379 349 ARG   A NH2 
1330 N  N   . LYS   A 194 ? 0.4075 0.2391 0.3570 -0.0165 -0.0421 -0.0396 350 LYS   A N   
1331 C  CA  . LYS   A 194 ? 0.4316 0.2610 0.3712 -0.0230 -0.0447 -0.0452 350 LYS   A CA  
1332 C  C   . LYS   A 194 ? 0.4476 0.2892 0.3858 -0.0250 -0.0520 -0.0424 350 LYS   A C   
1333 O  O   . LYS   A 194 ? 0.4700 0.3163 0.4063 -0.0318 -0.0568 -0.0443 350 LYS   A O   
1334 C  CB  . LYS   A 194 ? 0.5133 0.3337 0.4425 -0.0216 -0.0397 -0.0496 350 LYS   A CB  
1335 C  CG  . LYS   A 194 ? 0.5054 0.3230 0.4222 -0.0290 -0.0414 -0.0565 350 LYS   A CG  
1336 C  CD  . LYS   A 194 ? 0.5636 0.3719 0.4703 -0.0272 -0.0352 -0.0613 350 LYS   A CD  
1337 C  CE  . LYS   A 194 ? 0.7890 0.5944 0.6818 -0.0356 -0.0364 -0.0692 350 LYS   A CE  
1338 N  NZ  . LYS   A 194 ? 0.9211 0.7170 0.8035 -0.0340 -0.0292 -0.0746 350 LYS   A NZ  
1339 N  N   . GLN   A 195 ? 0.4105 0.2576 0.3496 -0.0196 -0.0529 -0.0375 351 GLN   A N   
1340 C  CA  . GLN   A 195 ? 0.4558 0.3142 0.3962 -0.0200 -0.0591 -0.0330 351 GLN   A CA  
1341 C  C   . GLN   A 195 ? 0.5086 0.3758 0.4599 -0.0219 -0.0632 -0.0298 351 GLN   A C   
1342 O  O   . GLN   A 195 ? 0.4225 0.2991 0.3738 -0.0259 -0.0691 -0.0282 351 GLN   A O   
1343 C  CB  . GLN   A 195 ? 0.4488 0.3093 0.3904 -0.0135 -0.0579 -0.0281 351 GLN   A CB  
1344 C  CG  . GLN   A 195 ? 0.6599 0.5157 0.5897 -0.0129 -0.0557 -0.0302 351 GLN   A CG  
1345 C  CD  . GLN   A 195 ? 0.6516 0.5064 0.5824 -0.0072 -0.0523 -0.0268 351 GLN   A CD  
1346 O  OE1 . GLN   A 195 ? 0.7413 0.5997 0.6802 -0.0038 -0.0524 -0.0225 351 GLN   A OE1 
1347 N  NE2 . GLN   A 195 ? 0.5250 0.3753 0.4466 -0.0066 -0.0492 -0.0290 351 GLN   A NE2 
1348 N  N   . LEU   A 196 ? 0.4270 0.2932 0.3881 -0.0192 -0.0602 -0.0283 352 LEU   A N   
1349 C  CA  . LEU   A 196 ? 0.4469 0.3226 0.4190 -0.0206 -0.0635 -0.0249 352 LEU   A CA  
1350 C  C   . LEU   A 196 ? 0.4390 0.3160 0.4100 -0.0290 -0.0666 -0.0286 352 LEU   A C   
1351 O  O   . LEU   A 196 ? 0.4292 0.3179 0.4057 -0.0322 -0.0720 -0.0259 352 LEU   A O   
1352 C  CB  . LEU   A 196 ? 0.4001 0.2745 0.3815 -0.0163 -0.0590 -0.0227 352 LEU   A CB  
1353 C  CG  . LEU   A 196 ? 0.4384 0.3135 0.4220 -0.0094 -0.0561 -0.0192 352 LEU   A CG  
1354 C  CD1 . LEU   A 196 ? 0.4279 0.3021 0.4185 -0.0070 -0.0515 -0.0181 352 LEU   A CD1 
1355 C  CD2 . LEU   A 196 ? 0.4396 0.3235 0.4277 -0.0067 -0.0593 -0.0146 352 LEU   A CD2 
1356 N  N   . ARG   A 197 ? 0.3695 0.2348 0.3337 -0.0328 -0.0631 -0.0348 353 ARG   A N   
1357 C  CA  . ARG   A 197 ? 0.4412 0.3055 0.4035 -0.0419 -0.0651 -0.0395 353 ARG   A CA  
1358 C  C   . ARG   A 197 ? 0.4398 0.3095 0.3916 -0.0486 -0.0706 -0.0424 353 ARG   A C   
1359 O  O   . ARG   A 197 ? 0.4203 0.2929 0.3703 -0.0577 -0.0737 -0.0461 353 ARG   A O   
1360 C  CB  . ARG   A 197 ? 0.4933 0.3411 0.4522 -0.0434 -0.0582 -0.0452 353 ARG   A CB  
1361 C  CG  . ARG   A 197 ? 0.4994 0.3444 0.4699 -0.0398 -0.0540 -0.0417 353 ARG   A CG  
1362 C  CD  . ARG   A 197 ? 0.5476 0.3759 0.5156 -0.0402 -0.0467 -0.0458 353 ARG   A CD  
1363 N  NE  . ARG   A 197 ? 0.6834 0.5035 0.6447 -0.0496 -0.0465 -0.0532 353 ARG   A NE  
1364 C  CZ  . ARG   A 197 ? 0.6455 0.4659 0.6116 -0.0571 -0.0478 -0.0546 353 ARG   A CZ  
1365 N  NH1 . ARG   A 197 ? 0.6216 0.4503 0.5999 -0.0560 -0.0491 -0.0487 353 ARG   A NH1 
1366 N  NH2 . ARG   A 197 ? 0.7365 0.5494 0.6946 -0.0668 -0.0476 -0.0624 353 ARG   A NH2 
1367 N  N   . LEU   A 198 ? 0.4720 0.3442 0.4168 -0.0448 -0.0718 -0.0406 354 LEU   A N   
1368 C  CA  . LEU   A 198 ? 0.5760 0.4575 0.5121 -0.0506 -0.0781 -0.0409 354 LEU   A CA  
1369 C  C   . LEU   A 198 ? 0.5678 0.4677 0.5136 -0.0495 -0.0853 -0.0323 354 LEU   A C   
1370 O  O   . LEU   A 198 ? 0.4582 0.3699 0.3994 -0.0553 -0.0918 -0.0309 354 LEU   A O   
1371 C  CB  . LEU   A 198 ? 0.5198 0.3961 0.4439 -0.0473 -0.0760 -0.0420 354 LEU   A CB  
1372 C  CG  . LEU   A 198 ? 0.5119 0.3717 0.4247 -0.0487 -0.0689 -0.0507 354 LEU   A CG  
1373 C  CD1 . LEU   A 198 ? 0.5822 0.4397 0.4865 -0.0436 -0.0667 -0.0496 354 LEU   A CD1 
1374 C  CD2 . LEU   A 198 ? 0.6015 0.4592 0.5032 -0.0603 -0.0705 -0.0591 354 LEU   A CD2 
1375 N  N   . LYS   A 199 ? 0.4577 0.3612 0.4171 -0.0422 -0.0839 -0.0262 355 LYS   A N   
1376 C  CA  . LYS   A 199 ? 0.4854 0.4058 0.4562 -0.0406 -0.0894 -0.0181 355 LYS   A CA  
1377 C  C   . LYS   A 199 ? 0.5071 0.4370 0.4837 -0.0492 -0.0936 -0.0193 355 LYS   A C   
1378 O  O   . LYS   A 199 ? 0.4734 0.3940 0.4469 -0.0551 -0.0909 -0.0262 355 LYS   A O   
1379 C  CB  . LYS   A 199 ? 0.4776 0.3974 0.4605 -0.0310 -0.0854 -0.0128 355 LYS   A CB  
1380 C  CG  . LYS   A 199 ? 0.5146 0.4268 0.4919 -0.0240 -0.0819 -0.0114 355 LYS   A CG  
1381 C  CD  . LYS   A 199 ? 0.5164 0.4289 0.5046 -0.0155 -0.0781 -0.0065 355 LYS   A CD  
1382 C  CE  . LYS   A 199 ? 0.5847 0.4900 0.5661 -0.0102 -0.0752 -0.0053 355 LYS   A CE  
1383 N  NZ  . LYS   A 199 ? 0.7036 0.6110 0.6946 -0.0029 -0.0727 0.0004  355 LYS   A NZ  
1384 N  N   . PRO   A 200 ? 0.4907 0.4392 0.4755 -0.0504 -0.1002 -0.0123 356 PRO   A N   
1385 C  CA  . PRO   A 200 ? 0.4877 0.4479 0.4794 -0.0591 -0.1046 -0.0127 356 PRO   A CA  
1386 C  C   . PRO   A 200 ? 0.5006 0.4583 0.5055 -0.0564 -0.1001 -0.0122 356 PRO   A C   
1387 O  O   . PRO   A 200 ? 0.4719 0.4217 0.4820 -0.0475 -0.0943 -0.0105 356 PRO   A O   
1388 C  CB  . PRO   A 200 ? 0.4453 0.4283 0.4443 -0.0587 -0.1125 -0.0031 356 PRO   A CB  
1389 C  CG  . PRO   A 200 ? 0.5121 0.4936 0.5132 -0.0472 -0.1105 0.0036  356 PRO   A CG  
1390 C  CD  . PRO   A 200 ? 0.5260 0.4865 0.5130 -0.0450 -0.1044 -0.0036 356 PRO   A CD  
1391 N  N   . PHE   A 201 ? 0.4729 0.4382 0.4830 -0.0653 -0.1028 -0.0138 357 PHE   A N   
1392 C  CA  . PHE   A 201 ? 0.4828 0.4500 0.5068 -0.0638 -0.0996 -0.0119 357 PHE   A CA  
1393 C  C   . PHE   A 201 ? 0.5110 0.5019 0.5479 -0.0679 -0.1062 -0.0054 357 PHE   A C   
1394 O  O   . PHE   A 201 ? 0.4224 0.4274 0.4562 -0.0734 -0.1136 -0.0032 357 PHE   A O   
1395 C  CB  . PHE   A 201 ? 0.4617 0.4131 0.4811 -0.0707 -0.0948 -0.0201 357 PHE   A CB  
1396 C  CG  . PHE   A 201 ? 0.4282 0.3827 0.4417 -0.0848 -0.0991 -0.0257 357 PHE   A CG  
1397 C  CD1 . PHE   A 201 ? 0.5207 0.4652 0.5175 -0.0913 -0.0997 -0.0333 357 PHE   A CD1 
1398 C  CD2 . PHE   A 201 ? 0.4076 0.3748 0.4319 -0.0922 -0.1020 -0.0238 357 PHE   A CD2 
1399 C  CE1 . PHE   A 201 ? 0.5825 0.5295 0.5726 -0.1056 -0.1034 -0.0396 357 PHE   A CE1 
1400 C  CE2 . PHE   A 201 ? 0.4947 0.4653 0.5133 -0.1066 -0.1061 -0.0295 357 PHE   A CE2 
1401 C  CZ  . PHE   A 201 ? 0.5746 0.5345 0.5754 -0.1137 -0.1067 -0.0378 357 PHE   A CZ  
1402 N  N   . TYR   A 202 ? 0.4090 0.4057 0.4606 -0.0654 -0.1035 -0.0019 358 TYR   A N   
1403 C  CA  . TYR   A 202 ? 0.3745 0.3953 0.4420 -0.0661 -0.1085 0.0061  358 TYR   A CA  
1404 C  C   . TYR   A 202 ? 0.3741 0.3992 0.4496 -0.0745 -0.1078 0.0041  358 TYR   A C   
1405 O  O   . TYR   A 202 ? 0.4135 0.4221 0.4859 -0.0759 -0.1017 -0.0015 358 TYR   A O   
1406 C  CB  . TYR   A 202 ? 0.3692 0.3963 0.4493 -0.0523 -0.1053 0.0144  358 TYR   A CB  
1407 C  CG  . TYR   A 202 ? 0.3873 0.4109 0.4592 -0.0457 -0.1067 0.0170  358 TYR   A CG  
1408 C  CD1 . TYR   A 202 ? 0.3979 0.4007 0.4576 -0.0410 -0.1014 0.0119  358 TYR   A CD1 
1409 C  CD2 . TYR   A 202 ? 0.4267 0.4688 0.5026 -0.0453 -0.1137 0.0247  358 TYR   A CD2 
1410 C  CE1 . TYR   A 202 ? 0.4903 0.4900 0.5421 -0.0359 -0.1026 0.0142  358 TYR   A CE1 
1411 C  CE2 . TYR   A 202 ? 0.4434 0.4823 0.5115 -0.0399 -0.1150 0.0276  358 TYR   A CE2 
1412 C  CZ  . TYR   A 202 ? 0.4866 0.5040 0.5424 -0.0356 -0.1094 0.0220  358 TYR   A CZ  
1413 O  OH  . TYR   A 202 ? 0.4801 0.4950 0.5283 -0.0309 -0.1108 0.0253  358 TYR   A OH  
1414 N  N   . LEU   A 203 ? 0.3652 0.4137 0.4516 -0.0804 -0.1142 0.0094  359 LEU   A N   
1415 C  CA  . LEU   A 203 ? 0.3486 0.4054 0.4444 -0.0895 -0.1146 0.0087  359 LEU   A CA  
1416 C  C   . LEU   A 203 ? 0.3689 0.4514 0.4854 -0.0843 -0.1167 0.0193  359 LEU   A C   
1417 O  O   . LEU   A 203 ? 0.3834 0.4859 0.5052 -0.0833 -0.1234 0.0264  359 LEU   A O   
1418 C  CB  . LEU   A 203 ? 0.4999 0.5606 0.5863 -0.1059 -0.1210 0.0028  359 LEU   A CB  
1419 C  CG  . LEU   A 203 ? 0.4788 0.5131 0.5455 -0.1124 -0.1175 -0.0088 359 LEU   A CG  
1420 C  CD1 . LEU   A 203 ? 0.4805 0.5216 0.5363 -0.1278 -0.1246 -0.0142 359 LEU   A CD1 
1421 C  CD2 . LEU   A 203 ? 0.4230 0.4424 0.4924 -0.1155 -0.1106 -0.0132 359 LEU   A CD2 
1422 N  N   . VAL   A 204 ? 0.3305 0.4134 0.4591 -0.0811 -0.1109 0.0210  360 VAL   A N   
1423 C  CA  . VAL   A 204 ? 0.3353 0.4419 0.4847 -0.0753 -0.1112 0.0307  360 VAL   A CA  
1424 C  C   . VAL   A 204 ? 0.3481 0.4689 0.5070 -0.0873 -0.1135 0.0309  360 VAL   A C   
1425 O  O   . VAL   A 204 ? 0.3705 0.4762 0.5222 -0.0956 -0.1104 0.0236  360 VAL   A O   
1426 C  CB  . VAL   A 204 ? 0.3566 0.4549 0.5133 -0.0616 -0.1019 0.0330  360 VAL   A CB  
1427 C  CG1 . VAL   A 204 ? 0.3359 0.4204 0.4831 -0.0508 -0.0997 0.0327  360 VAL   A CG1 
1428 C  CG2 . VAL   A 204 ? 0.3503 0.4313 0.5032 -0.0645 -0.0946 0.0267  360 VAL   A CG2 
1429 N  N   . PRO   A 205 ? 0.3110 0.4605 0.4866 -0.0884 -0.1185 0.0395  361 PRO   A N   
1430 C  CA  . PRO   A 205 ? 0.3813 0.5461 0.5670 -0.1005 -0.1207 0.0400  361 PRO   A CA  
1431 C  C   . PRO   A 205 ? 0.4343 0.5922 0.6289 -0.0964 -0.1115 0.0397  361 PRO   A C   
1432 O  O   . PRO   A 205 ? 0.3930 0.5541 0.5982 -0.0832 -0.1056 0.0450  361 PRO   A O   
1433 C  CB  . PRO   A 205 ? 0.3436 0.5431 0.5468 -0.0996 -0.1279 0.0513  361 PRO   A CB  
1434 C  CG  . PRO   A 205 ? 0.3199 0.5197 0.5282 -0.0819 -0.1249 0.0581  361 PRO   A CG  
1435 C  CD  . PRO   A 205 ? 0.3690 0.5386 0.5567 -0.0778 -0.1216 0.0501  361 PRO   A CD  
1436 N  N   . LYS   A 206 ? 0.3947 0.5424 0.5845 -0.1081 -0.1096 0.0334  362 LYS   A N   
1437 C  CA  . LYS   A 206 ? 0.3977 0.5347 0.5921 -0.1048 -0.1005 0.0325  362 LYS   A CA  
1438 C  C   . LYS   A 206 ? 0.4822 0.6165 0.6755 -0.1207 -0.1009 0.0282  362 LYS   A C   
1439 O  O   . LYS   A 206 ? 0.4093 0.5238 0.5870 -0.1295 -0.1017 0.0201  362 LYS   A O   
1440 C  CB  . LYS   A 206 ? 0.3803 0.4887 0.5605 -0.0958 -0.0937 0.0272  362 LYS   A CB  
1441 C  CG  . LYS   A 206 ? 0.4450 0.5475 0.6315 -0.0878 -0.0843 0.0289  362 LYS   A CG  
1442 C  CD  . LYS   A 206 ? 0.4027 0.5191 0.6014 -0.0739 -0.0816 0.0357  362 LYS   A CD  
1443 C  CE  . LYS   A 206 ? 0.5176 0.6278 0.7205 -0.0662 -0.0716 0.0363  362 LYS   A CE  
1444 N  NZ  . LYS   A 206 ? 0.5288 0.6507 0.7431 -0.0530 -0.0678 0.0417  362 LYS   A NZ  
1445 N  N   . HIS   A 207 ? 0.5213 0.6748 0.7315 -0.1243 -0.0997 0.0335  363 HIS   A N   
1446 C  CA  . HIS   A 207 ? 0.5355 0.6859 0.7456 -0.1397 -0.0994 0.0300  363 HIS   A CA  
1447 C  C   . HIS   A 207 ? 0.5290 0.6515 0.7303 -0.1381 -0.0904 0.0253  363 HIS   A C   
1448 O  O   . HIS   A 207 ? 0.4489 0.5625 0.6500 -0.1251 -0.0838 0.0270  363 HIS   A O   
1449 C  CB  . HIS   A 207 ? 0.5442 0.7252 0.7755 -0.1449 -0.1010 0.0376  363 HIS   A CB  
1450 C  CG  . HIS   A 207 ? 0.5519 0.7412 0.7979 -0.1331 -0.0931 0.0441  363 HIS   A CG  
1451 N  ND1 . HIS   A 207 ? 0.5431 0.7584 0.8087 -0.1366 -0.0925 0.0510  363 HIS   A ND1 
1452 C  CD2 . HIS   A 207 ? 0.5792 0.7557 0.8231 -0.1184 -0.0852 0.0446  363 HIS   A CD2 
1453 C  CE1 . HIS   A 207 ? 0.6111 0.8282 0.8856 -0.1244 -0.0840 0.0550  363 HIS   A CE1 
1454 N  NE2 . HIS   A 207 ? 0.6625 0.8562 0.9237 -0.1135 -0.0796 0.0510  363 HIS   A NE2 
1455 N  N   . ALA   A 208 ? 0.6061 0.7140 0.7993 -0.1518 -0.0901 0.0192  364 ALA   A N   
1456 C  CA  . ALA   A 208 ? 0.6319 0.7136 0.8174 -0.1523 -0.0820 0.0157  364 ALA   A CA  
1457 C  C   . ALA   A 208 ? 0.6152 0.7040 0.8116 -0.1633 -0.0792 0.0182  364 ALA   A C   
1458 O  O   . ALA   A 208 ? 0.7206 0.8287 0.9255 -0.1752 -0.0847 0.0194  364 ALA   A O   
1459 C  CB  . ALA   A 208 ? 0.6378 0.6918 0.8041 -0.1582 -0.0822 0.0063  364 ALA   A CB  
1460 N  N   . LYS   A 209 ? 0.7924 0.8661 0.9884 -0.1599 -0.0709 0.0196  365 LYS   A N   
1461 C  CA  . LYS   A 209 ? 0.6830 0.7611 0.8887 -0.1697 -0.0671 0.0227  365 LYS   A CA  
1462 C  C   . LYS   A 209 ? 0.7473 0.8131 0.9470 -0.1879 -0.0689 0.0167  365 LYS   A C   
1463 O  O   . LYS   A 209 ? 0.8205 0.8765 1.0086 -0.1940 -0.0736 0.0094  365 LYS   A O   
1464 C  CB  . LYS   A 209 ? 0.6941 0.7576 0.8987 -0.1615 -0.0577 0.0260  365 LYS   A CB  
1465 N  N   . GLY   A 213 ? 0.7804 0.9698 1.0566 -0.2322 -0.0787 0.0409  369 GLY   A N   
1466 C  CA  . GLY   A 213 ? 0.5726 0.7747 0.8531 -0.2135 -0.0794 0.0452  369 GLY   A CA  
1467 C  C   . GLY   A 213 ? 0.7063 0.8841 0.9685 -0.2035 -0.0803 0.0389  369 GLY   A C   
1468 O  O   . GLY   A 213 ? 0.7426 0.8936 0.9936 -0.1958 -0.0735 0.0364  369 GLY   A O   
1469 N  N   . PHE   A 214 ? 0.7320 0.9204 0.9912 -0.2037 -0.0889 0.0371  370 PHE   A N   
1470 C  CA  . PHE   A 214 ? 0.7123 0.8817 0.9555 -0.1935 -0.0902 0.0321  370 PHE   A CA  
1471 C  C   . PHE   A 214 ? 0.6559 0.8285 0.8898 -0.2045 -0.0998 0.0265  370 PHE   A C   
1472 O  O   . PHE   A 214 ? 0.7069 0.9075 0.9512 -0.2141 -0.1072 0.0298  370 PHE   A O   
1473 C  CB  . PHE   A 214 ? 0.6791 0.8610 0.9298 -0.1741 -0.0887 0.0384  370 PHE   A CB  
1474 N  N   . GLN   A 215 ? 0.6535 0.7983 0.8678 -0.2033 -0.0994 0.0183  371 GLN   A N   
1475 C  CA  . GLN   A 215 ? 0.6693 0.8150 0.8717 -0.2114 -0.1078 0.0123  371 GLN   A CA  
1476 C  C   . GLN   A 215 ? 0.6113 0.7769 0.8181 -0.1982 -0.1134 0.0182  371 GLN   A C   
1477 O  O   . GLN   A 215 ? 0.5911 0.7443 0.7931 -0.1822 -0.1094 0.0191  371 GLN   A O   
1478 C  CB  . GLN   A 215 ? 0.6854 0.7937 0.8659 -0.2135 -0.1039 0.0016  371 GLN   A CB  
1479 C  CG  . GLN   A 215 ? 0.6149 0.7215 0.7806 -0.2219 -0.1114 -0.0058 371 GLN   A CG  
1480 C  CD  . GLN   A 215 ? 0.6760 0.8103 0.8481 -0.2393 -0.1205 -0.0054 371 GLN   A CD  
1481 O  OE1 . GLN   A 215 ? 0.6836 0.8409 0.8569 -0.2390 -0.1292 -0.0023 371 GLN   A OE1 
1482 N  NE2 . GLN   A 215 ? 0.6826 0.8155 0.8588 -0.2551 -0.1186 -0.0080 371 GLN   A NE2 
1483 N  N   . GLU   A 216 ? 0.6256 0.8226 0.8418 -0.2053 -0.1226 0.0228  372 GLU   A N   
1484 C  CA  . GLU   A 216 ? 0.5723 0.7945 0.7995 -0.1922 -0.1271 0.0321  372 GLU   A CA  
1485 C  C   . GLU   A 216 ? 0.5585 0.7804 0.7720 -0.1918 -0.1347 0.0294  372 GLU   A C   
1486 O  O   . GLU   A 216 ? 0.5771 0.8221 0.7999 -0.1828 -0.1398 0.0379  372 GLU   A O   
1487 C  CB  . GLU   A 216 ? 0.5337 0.7954 0.7836 -0.1975 -0.1322 0.0418  372 GLU   A CB  
1488 C  CG  . GLU   A 216 ? 0.5467 0.8154 0.8143 -0.1917 -0.1240 0.0479  372 GLU   A CG  
1489 C  CD  . GLU   A 216 ? 0.6508 0.9155 0.9249 -0.1696 -0.1165 0.0534  372 GLU   A CD  
1490 O  OE1 . GLU   A 216 ? 0.6690 0.9200 0.9326 -0.1579 -0.1163 0.0518  372 GLU   A OE1 
1491 O  OE2 . GLU   A 216 ? 0.7390 1.0142 1.0287 -0.1644 -0.1101 0.0590  372 GLU   A OE2 
1492 N  N   . GLU   A 217 ? 0.5257 0.7221 0.7178 -0.2008 -0.1351 0.0182  373 GLU   A N   
1493 C  CA  . GLU   A 217 ? 0.4349 0.6306 0.6128 -0.2004 -0.1416 0.0154  373 GLU   A CA  
1494 C  C   . GLU   A 217 ? 0.4827 0.6420 0.6412 -0.1923 -0.1353 0.0071  373 GLU   A C   
1495 O  O   . GLU   A 217 ? 0.4376 0.5864 0.5786 -0.1978 -0.1387 0.0000  373 GLU   A O   
1496 C  CB  . GLU   A 217 ? 0.4237 0.6309 0.5932 -0.2217 -0.1505 0.0098  373 GLU   A CB  
1497 C  CG  . GLU   A 217 ? 0.5477 0.7946 0.7360 -0.2313 -0.1583 0.0184  373 GLU   A CG  
1498 C  CD  . GLU   A 217 ? 0.5319 0.8092 0.7392 -0.2154 -0.1619 0.0331  373 GLU   A CD  
1499 O  OE1 . GLU   A 217 ? 0.4803 0.7532 0.6817 -0.2021 -0.1627 0.0357  373 GLU   A OE1 
1500 O  OE2 . GLU   A 217 ? 0.4452 0.7520 0.6740 -0.2169 -0.1639 0.0423  373 GLU   A OE2 
1501 N  N   . THR   A 218 ? 0.4203 0.5615 0.5817 -0.1794 -0.1259 0.0081  374 THR   A N   
1502 C  CA  . THR   A 218 ? 0.4393 0.5482 0.5843 -0.1710 -0.1196 0.0015  374 THR   A CA  
1503 C  C   . THR   A 218 ? 0.3896 0.5020 0.5359 -0.1531 -0.1196 0.0073  374 THR   A C   
1504 O  O   . THR   A 218 ? 0.4315 0.5652 0.5942 -0.1438 -0.1203 0.0169  374 THR   A O   
1505 C  CB  . THR   A 218 ? 0.4825 0.5694 0.6286 -0.1685 -0.1095 -0.0007 374 THR   A CB  
1506 O  OG1 . THR   A 218 ? 0.5085 0.6147 0.6744 -0.1644 -0.1074 0.0080  374 THR   A OG1 
1507 C  CG2 . THR   A 218 ? 0.5298 0.5992 0.6665 -0.1855 -0.1078 -0.0099 374 THR   A CG2 
1508 N  N   . TRP   A 219 ? 0.3635 0.4542 0.4928 -0.1485 -0.1180 0.0014  375 TRP   A N   
1509 C  CA  . TRP   A 219 ? 0.3911 0.4789 0.5186 -0.1323 -0.1166 0.0053  375 TRP   A CA  
1510 C  C   . TRP   A 219 ? 0.3700 0.4279 0.4881 -0.1239 -0.1074 0.0003  375 TRP   A C   
1511 O  O   . TRP   A 219 ? 0.4041 0.4401 0.5093 -0.1310 -0.1043 -0.0081 375 TRP   A O   
1512 C  CB  . TRP   A 219 ? 0.3665 0.4583 0.4818 -0.1345 -0.1239 0.0037  375 TRP   A CB  
1513 C  CG  . TRP   A 219 ? 0.4562 0.5793 0.5791 -0.1436 -0.1341 0.0092  375 TRP   A CG  
1514 C  CD1 . TRP   A 219 ? 0.4232 0.5556 0.5433 -0.1616 -0.1396 0.0048  375 TRP   A CD1 
1515 C  CD2 . TRP   A 219 ? 0.3819 0.5307 0.5157 -0.1355 -0.1400 0.0201  375 TRP   A CD2 
1516 N  NE1 . TRP   A 219 ? 0.4794 0.6445 0.6086 -0.1654 -0.1492 0.0129  375 TRP   A NE1 
1517 C  CE2 . TRP   A 219 ? 0.5054 0.6809 0.6434 -0.1490 -0.1496 0.0229  375 TRP   A CE2 
1518 C  CE3 . TRP   A 219 ? 0.4989 0.6506 0.6397 -0.1182 -0.1378 0.0281  375 TRP   A CE3 
1519 C  CZ2 . TRP   A 219 ? 0.4101 0.6165 0.5601 -0.1448 -0.1573 0.0347  375 TRP   A CZ2 
1520 C  CZ3 . TRP   A 219 ? 0.4006 0.5806 0.5532 -0.1138 -0.1447 0.0393  375 TRP   A CZ3 
1521 C  CH2 . TRP   A 219 ? 0.4704 0.6779 0.6279 -0.1266 -0.1545 0.0431  375 TRP   A CH2 
1522 N  N   . ARG   A 220 ? 0.3476 0.4046 0.4720 -0.1091 -0.1027 0.0055  376 ARG   A N   
1523 C  CA  . ARG   A 220 ? 0.3457 0.3784 0.4629 -0.1013 -0.0941 0.0021  376 ARG   A CA  
1524 C  C   . ARG   A 220 ? 0.3513 0.3726 0.4570 -0.0917 -0.0937 0.0006  376 ARG   A C   
1525 O  O   . ARG   A 220 ? 0.3466 0.3813 0.4559 -0.0854 -0.0977 0.0056  376 ARG   A O   
1526 C  CB  . ARG   A 220 ? 0.3460 0.3842 0.4770 -0.0931 -0.0880 0.0079  376 ARG   A CB  
1527 C  CG  . ARG   A 220 ? 0.3886 0.4042 0.5132 -0.0898 -0.0796 0.0046  376 ARG   A CG  
1528 C  CD  . ARG   A 220 ? 0.3687 0.3905 0.5037 -0.0792 -0.0737 0.0101  376 ARG   A CD  
1529 N  NE  . ARG   A 220 ? 0.4642 0.4857 0.5961 -0.0678 -0.0738 0.0115  376 ARG   A NE  
1530 C  CZ  . ARG   A 220 ? 0.4665 0.5023 0.6093 -0.0590 -0.0726 0.0170  376 ARG   A CZ  
1531 N  NH1 . ARG   A 220 ? 0.3632 0.4149 0.5211 -0.0588 -0.0703 0.0218  376 ARG   A NH1 
1532 N  NH2 . ARG   A 220 ? 0.4793 0.5122 0.6178 -0.0500 -0.0728 0.0177  376 ARG   A NH2 
1533 N  N   . LEU   A 221 ? 0.3394 0.3365 0.4318 -0.0907 -0.0889 -0.0057 377 LEU   A N   
1534 C  CA  . LEU   A 221 ? 0.3453 0.3312 0.4266 -0.0821 -0.0879 -0.0073 377 LEU   A CA  
1535 C  C   . LEU   A 221 ? 0.4000 0.3905 0.4893 -0.0686 -0.0843 -0.0013 377 LEU   A C   
1536 O  O   . LEU   A 221 ? 0.4050 0.3988 0.5044 -0.0652 -0.0797 0.0019  377 LEU   A O   
1537 C  CB  . LEU   A 221 ? 0.3545 0.3147 0.4222 -0.0830 -0.0824 -0.0145 377 LEU   A CB  
1538 C  CG  . LEU   A 221 ? 0.4271 0.3763 0.4832 -0.0952 -0.0840 -0.0225 377 LEU   A CG  
1539 C  CD1 . LEU   A 221 ? 0.3763 0.3001 0.4231 -0.0938 -0.0765 -0.0279 377 LEU   A CD1 
1540 C  CD2 . LEU   A 221 ? 0.5048 0.4595 0.5507 -0.0982 -0.0905 -0.0250 377 LEU   A CD2 
1541 N  N   . SER   A 222 ? 0.3575 0.3473 0.4413 -0.0614 -0.0859 -0.0001 378 SER   A N   
1542 C  CA  . SER   A 222 ? 0.3551 0.3470 0.4447 -0.0492 -0.0820 0.0046  378 SER   A CA  
1543 C  C   . SER   A 222 ? 0.4068 0.3840 0.4828 -0.0439 -0.0808 0.0016  378 SER   A C   
1544 O  O   . SER   A 222 ? 0.3509 0.3279 0.4181 -0.0470 -0.0857 0.0000  378 SER   A O   
1545 C  CB  . SER   A 222 ? 0.3600 0.3737 0.4630 -0.0452 -0.0859 0.0124  378 SER   A CB  
1546 O  OG  . SER   A 222 ? 0.3952 0.4079 0.5026 -0.0334 -0.0814 0.0160  378 SER   A OG  
1547 N  N   . PHE   A 223 ? 0.3925 0.3584 0.4666 -0.0366 -0.0742 0.0009  379 PHE   A N   
1548 C  CA  . PHE   A 223 ? 0.4608 0.4134 0.5233 -0.0313 -0.0720 -0.0016 379 PHE   A CA  
1549 C  C   . PHE   A 223 ? 0.4240 0.3785 0.4915 -0.0214 -0.0681 0.0021  379 PHE   A C   
1550 O  O   . PHE   A 223 ? 0.4153 0.3585 0.4750 -0.0169 -0.0644 0.0001  379 PHE   A O   
1551 C  CB  . PHE   A 223 ? 0.4933 0.4287 0.5466 -0.0335 -0.0675 -0.0069 379 PHE   A CB  
1552 C  CG  . PHE   A 223 ? 0.4211 0.3508 0.4679 -0.0431 -0.0701 -0.0117 379 PHE   A CG  
1553 C  CD1 . PHE   A 223 ? 0.4550 0.3795 0.4902 -0.0461 -0.0734 -0.0156 379 PHE   A CD1 
1554 C  CD2 . PHE   A 223 ? 0.4305 0.3607 0.4829 -0.0498 -0.0691 -0.0124 379 PHE   A CD2 
1555 C  CE1 . PHE   A 223 ? 0.4554 0.3739 0.4837 -0.0560 -0.0751 -0.0212 379 PHE   A CE1 
1556 C  CE2 . PHE   A 223 ? 0.4618 0.3853 0.5080 -0.0596 -0.0708 -0.0176 379 PHE   A CE2 
1557 C  CZ  . PHE   A 223 ? 0.5043 0.4217 0.5382 -0.0628 -0.0737 -0.0224 379 PHE   A CZ  
1558 N  N   . SER   A 224 ? 0.4054 0.3745 0.4863 -0.0182 -0.0684 0.0074  380 SER   A N   
1559 C  CA  . SER   A 224 ? 0.4220 0.3921 0.5087 -0.0091 -0.0635 0.0104  380 SER   A CA  
1560 C  C   . SER   A 224 ? 0.4328 0.3953 0.5112 -0.0039 -0.0637 0.0106  380 SER   A C   
1561 O  O   . SER   A 224 ? 0.4889 0.4437 0.5654 0.0019  -0.0581 0.0097  380 SER   A O   
1562 C  CB  . SER   A 224 ? 0.5427 0.5306 0.6459 -0.0066 -0.0642 0.0166  380 SER   A CB  
1563 O  OG  . SER   A 224 ? 0.6645 0.6568 0.7756 -0.0087 -0.0602 0.0162  380 SER   A OG  
1564 N  N   . HIS   A 225 ? 0.4019 0.3662 0.4744 -0.0066 -0.0700 0.0114  381 HIS   A N   
1565 C  CA  . HIS   A 225 ? 0.3876 0.3444 0.4515 -0.0021 -0.0701 0.0120  381 HIS   A CA  
1566 C  C   . HIS   A 225 ? 0.3897 0.3297 0.4406 -0.0024 -0.0660 0.0058  381 HIS   A C   
1567 O  O   . HIS   A 225 ? 0.3730 0.3053 0.4193 0.0026  -0.0627 0.0057  381 HIS   A O   
1568 C  CB  . HIS   A 225 ? 0.4067 0.3709 0.4663 -0.0060 -0.0780 0.0145  381 HIS   A CB  
1569 C  CG  . HIS   A 225 ? 0.3935 0.3538 0.4427 -0.0154 -0.0816 0.0087  381 HIS   A CG  
1570 N  ND1 . HIS   A 225 ? 0.3882 0.3517 0.4414 -0.0221 -0.0822 0.0060  381 HIS   A ND1 
1571 C  CD2 . HIS   A 225 ? 0.4198 0.3728 0.4547 -0.0195 -0.0843 0.0048  381 HIS   A CD2 
1572 C  CE1 . HIS   A 225 ? 0.3630 0.3196 0.4047 -0.0298 -0.0845 0.0003  381 HIS   A CE1 
1573 N  NE2 . HIS   A 225 ? 0.4208 0.3714 0.4513 -0.0284 -0.0857 -0.0008 381 HIS   A NE2 
1574 N  N   . ILE   A 226 ? 0.3731 0.3076 0.4184 -0.0085 -0.0661 0.0010  382 ILE   A N   
1575 C  CA  . ILE   A 226 ? 0.3808 0.3010 0.4153 -0.0083 -0.0622 -0.0037 382 ILE   A CA  
1576 C  C   . ILE   A 226 ? 0.4468 0.3641 0.4853 -0.0041 -0.0557 -0.0037 382 ILE   A C   
1577 O  O   . ILE   A 226 ? 0.3791 0.2884 0.4111 -0.0010 -0.0521 -0.0052 382 ILE   A O   
1578 C  CB  . ILE   A 226 ? 0.4041 0.3186 0.4327 -0.0155 -0.0635 -0.0082 382 ILE   A CB  
1579 C  CG1 . ILE   A 226 ? 0.4101 0.3281 0.4332 -0.0212 -0.0699 -0.0093 382 ILE   A CG1 
1580 C  CG2 . ILE   A 226 ? 0.4379 0.3386 0.4569 -0.0144 -0.0591 -0.0120 382 ILE   A CG2 
1581 C  CD1 . ILE   A 226 ? 0.3748 0.2894 0.3879 -0.0189 -0.0716 -0.0094 382 ILE   A CD1 
1582 N  N   . GLU   A 227 ? 0.4087 0.3338 0.4578 -0.0046 -0.0541 -0.0019 383 GLU   A N   
1583 C  CA  . GLU   A 227 ? 0.4066 0.3313 0.4596 -0.0012 -0.0477 -0.0018 383 GLU   A CA  
1584 C  C   . GLU   A 227 ? 0.4156 0.3388 0.4685 0.0050  -0.0447 -0.0008 383 GLU   A C   
1585 O  O   . GLU   A 227 ? 0.3645 0.2810 0.4120 0.0068  -0.0401 -0.0030 383 GLU   A O   
1586 C  CB  . GLU   A 227 ? 0.4772 0.4130 0.5426 -0.0027 -0.0469 0.0006  383 GLU   A CB  
1587 C  CG  . GLU   A 227 ? 0.5010 0.4364 0.5663 -0.0097 -0.0489 -0.0005 383 GLU   A CG  
1588 C  CD  . GLU   A 227 ? 0.5233 0.4717 0.6011 -0.0129 -0.0503 0.0024  383 GLU   A CD  
1589 O  OE1 . GLU   A 227 ? 0.5623 0.5213 0.6498 -0.0091 -0.0498 0.0057  383 GLU   A OE1 
1590 O  OE2 . GLU   A 227 ? 0.6287 0.5767 0.7069 -0.0195 -0.0520 0.0015  383 GLU   A OE2 
1591 N  N   . LYS   A 228 ? 0.3721 0.3018 0.4314 0.0079  -0.0472 0.0028  384 LYS   A N   
1592 C  CA  . LYS   A 228 ? 0.4465 0.3731 0.5062 0.0139  -0.0442 0.0043  384 LYS   A CA  
1593 C  C   . LYS   A 228 ? 0.4361 0.3511 0.4827 0.0140  -0.0439 0.0015  384 LYS   A C   
1594 O  O   . LYS   A 228 ? 0.4429 0.3511 0.4860 0.0165  -0.0387 -0.0004 384 LYS   A O   
1595 C  CB  . LYS   A 228 ? 0.3952 0.3313 0.4640 0.0170  -0.0481 0.0103  384 LYS   A CB  
1596 C  CG  . LYS   A 228 ? 0.4881 0.4210 0.5592 0.0238  -0.0454 0.0138  384 LYS   A CG  
1597 C  CD  . LYS   A 228 ? 0.6288 0.5523 0.6873 0.0234  -0.0478 0.0131  384 LYS   A CD  
1598 C  CE  . LYS   A 228 ? 0.7456 0.6719 0.8084 0.0284  -0.0498 0.0201  384 LYS   A CE  
1599 N  NZ  . LYS   A 228 ? 0.7494 0.6701 0.7994 0.0261  -0.0541 0.0199  384 LYS   A NZ  
1600 N  N   . GLU   A 229 ? 0.4205 0.3333 0.4593 0.0105  -0.0492 0.0009  385 GLU   A N   
1601 C  CA  . GLU   A 229 ? 0.4517 0.3548 0.4787 0.0109  -0.0487 -0.0012 385 GLU   A CA  
1602 C  C   . GLU   A 229 ? 0.4918 0.3879 0.5130 0.0100  -0.0439 -0.0052 385 GLU   A C   
1603 O  O   . GLU   A 229 ? 0.4358 0.3257 0.4511 0.0117  -0.0408 -0.0064 385 GLU   A O   
1604 C  CB  . GLU   A 229 ? 0.4558 0.3583 0.4752 0.0070  -0.0544 -0.0019 385 GLU   A CB  
1605 C  CG  . GLU   A 229 ? 0.6958 0.5925 0.7065 0.0089  -0.0549 -0.0012 385 GLU   A CG  
1606 C  CD  . GLU   A 229 ? 0.6190 0.5192 0.6245 0.0058  -0.0611 0.0001  385 GLU   A CD  
1607 O  OE1 . GLU   A 229 ? 0.7801 0.6886 0.7914 0.0075  -0.0646 0.0054  385 GLU   A OE1 
1608 O  OE2 . GLU   A 229 ? 0.8378 0.7334 0.8340 0.0017  -0.0623 -0.0040 385 GLU   A OE2 
1609 N  N   . ILE   A 230 ? 0.3847 0.2824 0.4077 0.0070  -0.0432 -0.0068 386 ILE   A N   
1610 C  CA  . ILE   A 230 ? 0.4224 0.3155 0.4405 0.0063  -0.0391 -0.0091 386 ILE   A CA  
1611 C  C   . ILE   A 230 ? 0.5050 0.3996 0.5259 0.0085  -0.0336 -0.0094 386 ILE   A C   
1612 O  O   . ILE   A 230 ? 0.5431 0.4336 0.5577 0.0087  -0.0306 -0.0111 386 ILE   A O   
1613 C  CB  . ILE   A 230 ? 0.4373 0.3316 0.4574 0.0028  -0.0394 -0.0094 386 ILE   A CB  
1614 C  CG1 . ILE   A 230 ? 0.4293 0.3184 0.4435 0.0000  -0.0430 -0.0109 386 ILE   A CG1 
1615 C  CG2 . ILE   A 230 ? 0.5455 0.4389 0.5638 0.0027  -0.0349 -0.0098 386 ILE   A CG2 
1616 C  CD1 . ILE   A 230 ? 0.4833 0.3726 0.5011 -0.0039 -0.0435 -0.0112 386 ILE   A CD1 
1617 N  N   . LEU   A 231 ? 0.4684 0.3691 0.4986 0.0099  -0.0321 -0.0081 387 LEU   A N   
1618 C  CA  . LEU   A 231 ? 0.4143 0.3156 0.4465 0.0114  -0.0259 -0.0095 387 LEU   A CA  
1619 C  C   . LEU   A 231 ? 0.4962 0.3907 0.5237 0.0139  -0.0232 -0.0108 387 LEU   A C   
1620 O  O   . LEU   A 231 ? 0.4382 0.3299 0.4613 0.0130  -0.0182 -0.0138 387 LEU   A O   
1621 C  CB  . LEU   A 231 ? 0.3787 0.2878 0.4227 0.0132  -0.0241 -0.0077 387 LEU   A CB  
1622 C  CG  . LEU   A 231 ? 0.5204 0.4361 0.5684 0.0100  -0.0233 -0.0075 387 LEU   A CG  
1623 C  CD1 . LEU   A 231 ? 0.4843 0.4091 0.5450 0.0118  -0.0223 -0.0051 387 LEU   A CD1 
1624 C  CD2 . LEU   A 231 ? 0.5347 0.4490 0.5771 0.0086  -0.0175 -0.0104 387 LEU   A CD2 
1625 N  N   . ASN   A 232 ? 0.4316 0.3239 0.4601 0.0166  -0.0265 -0.0083 388 ASN   A N   
1626 C  CA  . ASN   A 232 ? 0.4487 0.3337 0.4737 0.0192  -0.0241 -0.0083 388 ASN   A CA  
1627 C  C   . ASN   A 232 ? 0.4466 0.3252 0.4603 0.0171  -0.0259 -0.0096 388 ASN   A C   
1628 O  O   . ASN   A 232 ? 0.4935 0.3656 0.5035 0.0184  -0.0238 -0.0096 388 ASN   A O   
1629 C  CB  . ASN   A 232 ? 0.4742 0.3612 0.5067 0.0235  -0.0267 -0.0032 388 ASN   A CB  
1630 C  CG  . ASN   A 232 ? 0.6449 0.5373 0.6899 0.0271  -0.0230 -0.0015 388 ASN   A CG  
1631 O  OD1 . ASN   A 232 ? 0.5517 0.4429 0.5980 0.0268  -0.0166 -0.0051 388 ASN   A OD1 
1632 N  ND2 . ASN   A 232 ? 0.5903 0.4895 0.6446 0.0305  -0.0266 0.0043  388 ASN   A ND2 
1633 N  N   . ASN   A 233 ? 0.3806 0.2607 0.3894 0.0142  -0.0294 -0.0103 389 ASN   A N   
1634 C  CA  . ASN   A 233 ? 0.4051 0.2803 0.4040 0.0126  -0.0303 -0.0115 389 ASN   A CA  
1635 C  C   . ASN   A 233 ? 0.4135 0.2913 0.4103 0.0098  -0.0298 -0.0131 389 ASN   A C   
1636 O  O   . ASN   A 233 ? 0.3716 0.2496 0.3670 0.0087  -0.0330 -0.0128 389 ASN   A O   
1637 C  CB  . ASN   A 233 ? 0.3992 0.2730 0.3948 0.0131  -0.0356 -0.0094 389 ASN   A CB  
1638 C  CG  . ASN   A 233 ? 0.4347 0.3034 0.4201 0.0119  -0.0356 -0.0105 389 ASN   A CG  
1639 O  OD1 . ASN   A 233 ? 0.3968 0.2635 0.3784 0.0108  -0.0319 -0.0124 389 ASN   A OD1 
1640 N  ND2 . ASN   A 233 ? 0.4887 0.3565 0.4697 0.0117  -0.0396 -0.0092 389 ASN   A ND2 
1641 N  N   . HIS   A 234 ? 0.4603 0.3400 0.4571 0.0085  -0.0254 -0.0147 390 HIS   A N   
1642 C  CA  . HIS   A 234 ? 0.4160 0.3009 0.4143 0.0065  -0.0246 -0.0146 390 HIS   A CA  
1643 C  C   . HIS   A 234 ? 0.4493 0.3352 0.4412 0.0045  -0.0230 -0.0148 390 HIS   A C   
1644 O  O   . HIS   A 234 ? 0.3722 0.2632 0.3656 0.0032  -0.0222 -0.0134 390 HIS   A O   
1645 C  CB  . HIS   A 234 ? 0.3895 0.2791 0.3934 0.0060  -0.0207 -0.0154 390 HIS   A CB  
1646 C  CG  . HIS   A 234 ? 0.3772 0.2646 0.3778 0.0054  -0.0159 -0.0183 390 HIS   A CG  
1647 N  ND1 . HIS   A 234 ? 0.4471 0.3314 0.4519 0.0077  -0.0130 -0.0194 390 HIS   A ND1 
1648 C  CD2 . HIS   A 234 ? 0.3711 0.2582 0.3643 0.0025  -0.0133 -0.0203 390 HIS   A CD2 
1649 C  CE1 . HIS   A 234 ? 0.3692 0.2496 0.3688 0.0059  -0.0082 -0.0228 390 HIS   A CE1 
1650 N  NE2 . HIS   A 234 ? 0.4126 0.2954 0.4049 0.0021  -0.0087 -0.0236 390 HIS   A NE2 
1651 N  N   . GLY   A 235 ? 0.3867 0.2695 0.3723 0.0042  -0.0222 -0.0159 391 GLY   A N   
1652 C  CA  . GLY   A 235 ? 0.3982 0.2848 0.3789 0.0020  -0.0206 -0.0156 391 GLY   A CA  
1653 C  C   . GLY   A 235 ? 0.4746 0.3597 0.4527 0.0034  -0.0229 -0.0136 391 GLY   A C   
1654 O  O   . GLY   A 235 ? 0.3713 0.2508 0.3489 0.0052  -0.0255 -0.0138 391 GLY   A O   
1655 N  N   . LYS   A 236 ? 0.3623 0.2532 0.3390 0.0024  -0.0216 -0.0116 392 LYS   A N   
1656 C  CA  . LYS   A 236 ? 0.3626 0.2519 0.3366 0.0042  -0.0223 -0.0100 392 LYS   A CA  
1657 C  C   . LYS   A 236 ? 0.4045 0.2910 0.3726 0.0035  -0.0221 -0.0118 392 LYS   A C   
1658 O  O   . LYS   A 236 ? 0.3937 0.2750 0.3589 0.0053  -0.0232 -0.0121 392 LYS   A O   
1659 C  CB  . LYS   A 236 ? 0.3587 0.2561 0.3345 0.0043  -0.0207 -0.0059 392 LYS   A CB  
1660 C  CG  . LYS   A 236 ? 0.4402 0.3369 0.4140 0.0067  -0.0201 -0.0042 392 LYS   A CG  
1661 C  CD  . LYS   A 236 ? 0.4214 0.3241 0.3997 0.0089  -0.0185 0.0012  392 LYS   A CD  
1662 C  CE  . LYS   A 236 ? 0.5275 0.4215 0.5096 0.0116  -0.0186 0.0014  392 LYS   A CE  
1663 N  NZ  . LYS   A 236 ? 0.6808 0.5787 0.6676 0.0148  -0.0160 0.0072  392 LYS   A NZ  
1664 N  N   . SER   A 237 ? 0.3693 0.2585 0.3349 0.0004  -0.0202 -0.0133 393 SER   A N   
1665 C  CA  . SER   A 237 ? 0.4014 0.2861 0.3619 -0.0008 -0.0197 -0.0150 393 SER   A CA  
1666 C  C   . SER   A 237 ? 0.4036 0.2794 0.3648 0.0011  -0.0210 -0.0165 393 SER   A C   
1667 O  O   . SER   A 237 ? 0.3640 0.2388 0.3295 0.0014  -0.0205 -0.0175 393 SER   A O   
1668 C  CB  . SER   A 237 ? 0.3581 0.2472 0.3156 -0.0057 -0.0167 -0.0168 393 SER   A CB  
1669 O  OG  . SER   A 237 ? 0.3901 0.2730 0.3429 -0.0073 -0.0157 -0.0185 393 SER   A OG  
1670 N  N   . LYS   A 238 ? 0.3602 0.2308 0.3175 0.0022  -0.0223 -0.0162 394 LYS   A N   
1671 C  CA  . LYS   A 238 ? 0.4023 0.2662 0.3604 0.0039  -0.0237 -0.0161 394 LYS   A CA  
1672 C  C   . LYS   A 238 ? 0.4513 0.3117 0.4103 0.0025  -0.0204 -0.0174 394 LYS   A C   
1673 O  O   . LYS   A 238 ? 0.3911 0.2472 0.3542 0.0048  -0.0206 -0.0167 394 LYS   A O   
1674 C  CB  . LYS   A 238 ? 0.3541 0.2142 0.3066 0.0048  -0.0256 -0.0148 394 LYS   A CB  
1675 C  CG  . LYS   A 238 ? 0.3308 0.1920 0.2823 0.0063  -0.0283 -0.0146 394 LYS   A CG  
1676 C  CD  . LYS   A 238 ? 0.3732 0.2318 0.3175 0.0064  -0.0292 -0.0140 394 LYS   A CD  
1677 C  CE  . LYS   A 238 ? 0.3673 0.2260 0.3094 0.0073  -0.0302 -0.0151 394 LYS   A CE  
1678 N  NZ  . LYS   A 238 ? 0.3950 0.2523 0.3295 0.0070  -0.0295 -0.0152 394 LYS   A NZ  
1679 N  N   . THR   A 239 ? 0.4123 0.2744 0.3679 -0.0015 -0.0170 -0.0193 395 THR   A N   
1680 C  CA  . THR   A 239 ? 0.4797 0.3365 0.4349 -0.0039 -0.0126 -0.0219 395 THR   A CA  
1681 C  C   . THR   A 239 ? 0.4706 0.3319 0.4287 -0.0061 -0.0097 -0.0248 395 THR   A C   
1682 O  O   . THR   A 239 ? 0.4171 0.2750 0.3733 -0.0098 -0.0050 -0.0284 395 THR   A O   
1683 C  CB  . THR   A 239 ? 0.5073 0.3625 0.4559 -0.0086 -0.0101 -0.0231 395 THR   A CB  
1684 O  OG1 . THR   A 239 ? 0.4249 0.2905 0.3707 -0.0117 -0.0108 -0.0229 395 THR   A OG1 
1685 C  CG2 . THR   A 239 ? 0.4577 0.3060 0.4036 -0.0065 -0.0116 -0.0202 395 THR   A CG2 
1686 N  N   . CYS   A 240 ? 0.4590 0.3271 0.4211 -0.0045 -0.0119 -0.0236 396 CYS   A N   
1687 C  CA  . CYS   A 240 ? 0.4083 0.2815 0.3727 -0.0068 -0.0091 -0.0259 396 CYS   A CA  
1688 C  C   . CYS   A 240 ? 0.4481 0.3140 0.4166 -0.0052 -0.0053 -0.0283 396 CYS   A C   
1689 O  O   . CYS   A 240 ? 0.4231 0.2840 0.3967 -0.0003 -0.0070 -0.0260 396 CYS   A O   
1690 C  CB  . CYS   A 240 ? 0.4105 0.2914 0.3794 -0.0048 -0.0121 -0.0230 396 CYS   A CB  
1691 S  SG  . CYS   A 240 ? 0.3706 0.2585 0.3437 -0.0067 -0.0091 -0.0245 396 CYS   A SG  
1692 N  N   . CYS   A 241 ? 0.3930 0.2588 0.3591 -0.0096 0.0001  -0.0329 397 CYS   A N   
1693 C  CA  . CYS   A 241 ? 0.3889 0.2465 0.3578 -0.0089 0.0061  -0.0365 397 CYS   A CA  
1694 C  C   . CYS   A 241 ? 0.3976 0.2422 0.3660 -0.0070 0.0084  -0.0365 397 CYS   A C   
1695 O  O   . CYS   A 241 ? 0.4150 0.2513 0.3875 -0.0050 0.0139  -0.0386 397 CYS   A O   
1696 C  CB  . CYS   A 241 ? 0.3811 0.2408 0.3594 -0.0038 0.0060  -0.0349 397 CYS   A CB  
1697 S  SG  . CYS   A 241 ? 0.3964 0.2696 0.3759 -0.0068 0.0061  -0.0357 397 CYS   A SG  
1698 N  N   . GLU   A 242 ? 0.3727 0.2150 0.3362 -0.0079 0.0055  -0.0343 398 GLU   A N   
1699 C  CA  . GLU   A 242 ? 0.4439 0.2736 0.4066 -0.0068 0.0082  -0.0337 398 GLU   A CA  
1700 C  C   . GLU   A 242 ? 0.4915 0.3156 0.4464 -0.0144 0.0139  -0.0391 398 GLU   A C   
1701 O  O   . GLU   A 242 ? 0.4208 0.2332 0.3744 -0.0144 0.0170  -0.0388 398 GLU   A O   
1702 C  CB  . GLU   A 242 ? 0.4127 0.2423 0.3745 -0.0034 0.0021  -0.0278 398 GLU   A CB  
1703 C  CG  . GLU   A 242 ? 0.3664 0.1998 0.3355 0.0034  -0.0033 -0.0228 398 GLU   A CG  
1704 C  CD  . GLU   A 242 ? 0.5192 0.3506 0.4866 0.0063  -0.0081 -0.0174 398 GLU   A CD  
1705 O  OE1 . GLU   A 242 ? 0.4676 0.2959 0.4282 0.0034  -0.0078 -0.0172 398 GLU   A OE1 
1706 O  OE2 . GLU   A 242 ? 0.4668 0.3005 0.4396 0.0110  -0.0122 -0.0133 398 GLU   A OE2 
1707 N  N   . ASN   A 243 ? 0.5133 0.3460 0.4628 -0.0214 0.0152  -0.0435 399 ASN   A N   
1708 C  CA  . ASN   A 243 ? 0.5040 0.3335 0.4453 -0.0305 0.0203  -0.0492 399 ASN   A CA  
1709 C  C   . ASN   A 243 ? 0.5002 0.3397 0.4381 -0.0369 0.0228  -0.0546 399 ASN   A C   
1710 O  O   . ASN   A 243 ? 0.4571 0.3071 0.3987 -0.0341 0.0197  -0.0525 399 ASN   A O   
1711 C  CB  . ASN   A 243 ? 0.4706 0.3051 0.4062 -0.0342 0.0164  -0.0466 399 ASN   A CB  
1712 C  CG  . ASN   A 243 ? 0.5137 0.3652 0.4496 -0.0337 0.0099  -0.0427 399 ASN   A CG  
1713 O  OD1 . ASN   A 243 ? 0.4636 0.3265 0.3979 -0.0379 0.0100  -0.0446 399 ASN   A OD1 
1714 N  ND2 . ASN   A 243 ? 0.4759 0.3290 0.4136 -0.0285 0.0047  -0.0369 399 ASN   A ND2 
1715 N  N   . LYS   A 244 ? 0.5080 0.3445 0.4382 -0.0462 0.0286  -0.0615 400 LYS   A N   
1716 C  CA  . LYS   A 244 ? 0.5663 0.4136 0.4914 -0.0540 0.0312  -0.0670 400 LYS   A CA  
1717 C  C   . LYS   A 244 ? 0.4830 0.3509 0.4071 -0.0556 0.0241  -0.0620 400 LYS   A C   
1718 O  O   . LYS   A 244 ? 0.5246 0.4028 0.4500 -0.0556 0.0234  -0.0618 400 LYS   A O   
1719 C  CB  . LYS   A 244 ? 0.5678 0.4101 0.4830 -0.0657 0.0377  -0.0754 400 LYS   A CB  
1720 C  CG  . LYS   A 244 ? 0.7005 0.5240 0.6158 -0.0661 0.0474  -0.0827 400 LYS   A CG  
1721 C  CD  . LYS   A 244 ? 0.6409 0.4589 0.5452 -0.0792 0.0537  -0.0914 400 LYS   A CD  
1722 C  CE  . LYS   A 244 ? 0.7603 0.5796 0.6588 -0.0864 0.0609  -0.1009 400 LYS   A CE  
1723 N  NZ  . LYS   A 244 ? 0.6776 0.5102 0.5629 -0.1025 0.0619  -0.1079 400 LYS   A NZ  
1724 N  N   . GLU   A 245 ? 0.5226 0.3972 0.4447 -0.0571 0.0192  -0.0576 401 GLU   A N   
1725 C  CA  . GLU   A 245 ? 0.4778 0.3720 0.3999 -0.0581 0.0133  -0.0521 401 GLU   A CA  
1726 C  C   . GLU   A 245 ? 0.4865 0.3855 0.4166 -0.0491 0.0091  -0.0464 401 GLU   A C   
1727 O  O   . GLU   A 245 ? 0.4728 0.3873 0.4037 -0.0501 0.0060  -0.0425 401 GLU   A O   
1728 C  CB  . GLU   A 245 ? 0.5690 0.4674 0.4901 -0.0585 0.0095  -0.0476 401 GLU   A CB  
1729 C  CG  . GLU   A 245 ? 0.5835 0.5035 0.5041 -0.0615 0.0050  -0.0423 401 GLU   A CG  
1730 C  CD  . GLU   A 245 ? 0.7175 0.6504 0.6302 -0.0742 0.0071  -0.0464 401 GLU   A CD  
1731 O  OE1 . GLU   A 245 ? 0.7469 0.6714 0.6531 -0.0821 0.0116  -0.0531 401 GLU   A OE1 
1732 O  OE2 . GLU   A 245 ? 0.7005 0.6521 0.6135 -0.0767 0.0045  -0.0427 401 GLU   A OE2 
1733 N  N   . GLU   A 246 ? 0.5207 0.4075 0.4570 -0.0408 0.0090  -0.0452 402 GLU   A N   
1734 C  CA  . GLU   A 246 ? 0.5000 0.3908 0.4436 -0.0330 0.0044  -0.0395 402 GLU   A CA  
1735 C  C   . GLU   A 246 ? 0.4827 0.3689 0.4319 -0.0292 0.0068  -0.0413 402 GLU   A C   
1736 O  O   . GLU   A 246 ? 0.4280 0.3132 0.3839 -0.0224 0.0034  -0.0372 402 GLU   A O   
1737 C  CB  . GLU   A 246 ? 0.4862 0.3705 0.4327 -0.0266 0.0003  -0.0350 402 GLU   A CB  
1738 C  CG  . GLU   A 246 ? 0.4669 0.3571 0.4091 -0.0294 -0.0020 -0.0325 402 GLU   A CG  
1739 C  CD  . GLU   A 246 ? 0.4571 0.3419 0.4018 -0.0227 -0.0058 -0.0282 402 GLU   A CD  
1740 O  OE1 . GLU   A 246 ? 0.4044 0.2932 0.3533 -0.0179 -0.0092 -0.0245 402 GLU   A OE1 
1741 O  OE2 . GLU   A 246 ? 0.4667 0.3432 0.4085 -0.0229 -0.0051 -0.0286 402 GLU   A OE2 
1742 N  N   . LYS   A 247 ? 0.4202 0.3037 0.3667 -0.0338 0.0130  -0.0475 403 LYS   A N   
1743 C  CA  . LYS   A 247 ? 0.4456 0.3267 0.3982 -0.0299 0.0157  -0.0488 403 LYS   A CA  
1744 C  C   . LYS   A 247 ? 0.4748 0.3702 0.4300 -0.0295 0.0122  -0.0447 403 LYS   A C   
1745 O  O   . LYS   A 247 ? 0.4541 0.3617 0.4039 -0.0356 0.0116  -0.0444 403 LYS   A O   
1746 C  CB  . LYS   A 247 ? 0.4096 0.2845 0.3583 -0.0349 0.0243  -0.0570 403 LYS   A CB  
1747 C  CG  . LYS   A 247 ? 0.5225 0.3805 0.4701 -0.0345 0.0291  -0.0607 403 LYS   A CG  
1748 C  CD  . LYS   A 247 ? 0.5674 0.4151 0.5255 -0.0242 0.0286  -0.0568 403 LYS   A CD  
1749 C  CE  . LYS   A 247 ? 0.6130 0.4437 0.5709 -0.0230 0.0338  -0.0590 403 LYS   A CE  
1750 N  NZ  . LYS   A 247 ? 0.5330 0.3559 0.5019 -0.0127 0.0329  -0.0536 403 LYS   A NZ  
1751 N  N   . CYS   A 248 ? 0.4702 0.3648 0.4341 -0.0227 0.0098  -0.0409 404 CYS   A N   
1752 C  CA  . CYS   A 248 ? 0.4073 0.3136 0.3746 -0.0221 0.0071  -0.0367 404 CYS   A CA  
1753 C  C   . CYS   A 248 ? 0.3933 0.2992 0.3662 -0.0205 0.0113  -0.0389 404 CYS   A C   
1754 O  O   . CYS   A 248 ? 0.4087 0.3050 0.3840 -0.0184 0.0158  -0.0429 404 CYS   A O   
1755 C  CB  . CYS   A 248 ? 0.3923 0.2992 0.3647 -0.0167 0.0005  -0.0300 404 CYS   A CB  
1756 S  SG  . CYS   A 248 ? 0.3764 0.2768 0.3594 -0.0092 -0.0018 -0.0276 404 CYS   A SG  
1757 N  N   . CYS   A 249 ? 0.3407 0.2571 0.3163 -0.0211 0.0102  -0.0358 405 CYS   A N   
1758 C  CA  . CYS   A 249 ? 0.3605 0.2784 0.3418 -0.0199 0.0144  -0.0375 405 CYS   A CA  
1759 C  C   . CYS   A 249 ? 0.3386 0.2588 0.3298 -0.0145 0.0101  -0.0315 405 CYS   A C   
1760 O  O   . CYS   A 249 ? 0.3616 0.2875 0.3579 -0.0143 0.0124  -0.0310 405 CYS   A O   
1761 C  CB  . CYS   A 249 ? 0.4481 0.3771 0.4232 -0.0269 0.0187  -0.0401 405 CYS   A CB  
1762 S  SG  . CYS   A 249 ? 0.3992 0.3444 0.3727 -0.0297 0.0131  -0.0319 405 CYS   A SG  
1763 N  N   . ARG   A 250 ? 0.3718 0.2876 0.3658 -0.0106 0.0042  -0.0274 406 ARG   A N   
1764 C  CA  . ARG   A 250 ? 0.3701 0.2875 0.3728 -0.0068 0.0001  -0.0226 406 ARG   A CA  
1765 C  C   . ARG   A 250 ? 0.3650 0.2805 0.3766 -0.0034 0.0026  -0.0238 406 ARG   A C   
1766 O  O   . ARG   A 250 ? 0.3323 0.2545 0.3502 -0.0034 0.0033  -0.0219 406 ARG   A O   
1767 C  CB  . ARG   A 250 ? 0.3181 0.2296 0.3206 -0.0040 -0.0058 -0.0196 406 ARG   A CB  
1768 C  CG  . ARG   A 250 ? 0.3912 0.3065 0.3887 -0.0059 -0.0086 -0.0163 406 ARG   A CG  
1769 C  CD  . ARG   A 250 ? 0.4228 0.3307 0.4203 -0.0027 -0.0133 -0.0146 406 ARG   A CD  
1770 N  NE  . ARG   A 250 ? 0.3565 0.2661 0.3506 -0.0030 -0.0154 -0.0113 406 ARG   A NE  
1771 C  CZ  . ARG   A 250 ? 0.3680 0.2770 0.3560 -0.0037 -0.0154 -0.0118 406 ARG   A CZ  
1772 N  NH1 . ARG   A 250 ? 0.3154 0.2214 0.2991 -0.0051 -0.0135 -0.0157 406 ARG   A NH1 
1773 N  NH2 . ARG   A 250 ? 0.3870 0.2982 0.3738 -0.0030 -0.0169 -0.0081 406 ARG   A NH2 
1774 N  N   . LYS   A 251 ? 0.3490 0.2562 0.3621 -0.0001 0.0043  -0.0263 407 LYS   A N   
1775 C  CA  . LYS   A 251 ? 0.3620 0.2688 0.3855 0.0043  0.0066  -0.0260 407 LYS   A CA  
1776 C  C   . LYS   A 251 ? 0.3635 0.2753 0.3889 0.0026  0.0141  -0.0295 407 LYS   A C   
1777 O  O   . LYS   A 251 ? 0.3330 0.2509 0.3680 0.0048  0.0152  -0.0275 407 LYS   A O   
1778 C  CB  . LYS   A 251 ? 0.4106 0.3075 0.4358 0.0087  0.0075  -0.0267 407 LYS   A CB  
1779 C  CG  . LYS   A 251 ? 0.3832 0.2764 0.4077 0.0108  -0.0002 -0.0226 407 LYS   A CG  
1780 C  CD  . LYS   A 251 ? 0.4791 0.3634 0.5052 0.0151  0.0008  -0.0220 407 LYS   A CD  
1781 C  CE  . LYS   A 251 ? 0.6307 0.5178 0.6696 0.0209  0.0005  -0.0181 407 LYS   A CE  
1782 N  NZ  . LYS   A 251 ? 0.6792 0.5577 0.7201 0.0254  0.0020  -0.0163 407 LYS   A NZ  
1783 N  N   . ASP   A 252 ? 0.3504 0.2606 0.3666 -0.0019 0.0197  -0.0350 408 ASP   A N   
1784 C  CA  . ASP   A 252 ? 0.3291 0.2444 0.3451 -0.0046 0.0275  -0.0393 408 ASP   A CA  
1785 C  C   . ASP   A 252 ? 0.3368 0.2651 0.3549 -0.0073 0.0256  -0.0355 408 ASP   A C   
1786 O  O   . ASP   A 252 ? 0.3424 0.2765 0.3663 -0.0069 0.0303  -0.0363 408 ASP   A O   
1787 C  CB  . ASP   A 252 ? 0.3506 0.2631 0.3541 -0.0110 0.0329  -0.0462 408 ASP   A CB  
1788 C  CG  . ASP   A 252 ? 0.4954 0.3940 0.4981 -0.0089 0.0386  -0.0516 408 ASP   A CG  
1789 O  OD1 . ASP   A 252 ? 0.4672 0.3602 0.4805 -0.0018 0.0405  -0.0501 408 ASP   A OD1 
1790 O  OD2 . ASP   A 252 ? 0.5892 0.4830 0.5812 -0.0144 0.0414  -0.0568 408 ASP   A OD2 
1791 N  N   . CYS   A 253 ? 0.3315 0.2643 0.3451 -0.0101 0.0193  -0.0311 409 CYS   A N   
1792 C  CA  . CYS   A 253 ? 0.3294 0.2731 0.3459 -0.0122 0.0173  -0.0262 409 CYS   A CA  
1793 C  C   . CYS   A 253 ? 0.3710 0.3164 0.4001 -0.0080 0.0154  -0.0224 409 CYS   A C   
1794 O  O   . CYS   A 253 ? 0.3362 0.2901 0.3701 -0.0094 0.0182  -0.0210 409 CYS   A O   
1795 C  CB  . CYS   A 253 ? 0.3255 0.2715 0.3367 -0.0144 0.0112  -0.0211 409 CYS   A CB  
1796 S  SG  . CYS   A 253 ? 0.3531 0.3064 0.3506 -0.0217 0.0138  -0.0234 409 CYS   A SG  
1797 N  N   . LEU   A 254 ? 0.3404 0.2791 0.3748 -0.0036 0.0104  -0.0203 410 LEU   A N   
1798 C  CA  . LEU   A 254 ? 0.3547 0.2970 0.4012 -0.0006 0.0080  -0.0167 410 LEU   A CA  
1799 C  C   . LEU   A 254 ? 0.3322 0.2779 0.3869 0.0021  0.0146  -0.0190 410 LEU   A C   
1800 O  O   . LEU   A 254 ? 0.3435 0.2978 0.4071 0.0021  0.0156  -0.0164 410 LEU   A O   
1801 C  CB  . LEU   A 254 ? 0.3149 0.2507 0.3644 0.0027  0.0013  -0.0143 410 LEU   A CB  
1802 C  CG  . LEU   A 254 ? 0.3626 0.3038 0.4245 0.0048  -0.0018 -0.0106 410 LEU   A CG  
1803 C  CD1 . LEU   A 254 ? 0.3242 0.2731 0.3897 0.0007  -0.0034 -0.0070 410 LEU   A CD1 
1804 C  CD2 . LEU   A 254 ? 0.3985 0.3343 0.4613 0.0071  -0.0085 -0.0087 410 LEU   A CD2 
1805 N  N   . LYS   A 255 ? 0.3382 0.2768 0.3909 0.0047  0.0198  -0.0238 411 LYS   A N   
1806 C  CA  . LYS   A 255 ? 0.3449 0.2854 0.4061 0.0082  0.0276  -0.0263 411 LYS   A CA  
1807 C  C   . LYS   A 255 ? 0.3616 0.3115 0.4216 0.0041  0.0339  -0.0284 411 LYS   A C   
1808 O  O   . LYS   A 255 ? 0.3606 0.3185 0.4313 0.0062  0.0373  -0.0269 411 LYS   A O   
1809 C  CB  . LYS   A 255 ? 0.3476 0.2764 0.4047 0.0108  0.0336  -0.0318 411 LYS   A CB  
1810 C  CG  . LYS   A 255 ? 0.4399 0.3603 0.5007 0.0161  0.0285  -0.0286 411 LYS   A CG  
1811 C  CD  . LYS   A 255 ? 0.4799 0.3871 0.5366 0.0183  0.0348  -0.0334 411 LYS   A CD  
1812 C  CE  . LYS   A 255 ? 0.5623 0.4627 0.6226 0.0234  0.0289  -0.0285 411 LYS   A CE  
1813 N  NZ  . LYS   A 255 ? 0.6539 0.5403 0.7102 0.0253  0.0348  -0.0323 411 LYS   A NZ  
1814 N  N   . LEU   A 256 ? 0.3298 0.2804 0.3768 -0.0021 0.0355  -0.0317 412 LEU   A N   
1815 C  CA  . LEU   A 256 ? 0.3503 0.3111 0.3940 -0.0072 0.0410  -0.0333 412 LEU   A CA  
1816 C  C   . LEU   A 256 ? 0.3433 0.3151 0.3947 -0.0082 0.0368  -0.0261 412 LEU   A C   
1817 O  O   . LEU   A 256 ? 0.3483 0.3289 0.4055 -0.0087 0.0420  -0.0260 412 LEU   A O   
1818 C  CB  . LEU   A 256 ? 0.3442 0.3056 0.3721 -0.0143 0.0417  -0.0365 412 LEU   A CB  
1819 C  CG  . LEU   A 256 ? 0.3452 0.2964 0.3646 -0.0154 0.0479  -0.0451 412 LEU   A CG  
1820 C  CD1 . LEU   A 256 ? 0.3578 0.3109 0.3616 -0.0232 0.0463  -0.0473 412 LEU   A CD1 
1821 C  CD2 . LEU   A 256 ? 0.3703 0.3210 0.3915 -0.0151 0.0594  -0.0523 412 LEU   A CD2 
1822 N  N   . MET   A 257 ? 0.3674 0.3382 0.4190 -0.0086 0.0279  -0.0203 413 MET   A N   
1823 C  CA  . MET   A 257 ? 0.3634 0.3422 0.4228 -0.0099 0.0241  -0.0137 413 MET   A CA  
1824 C  C   . MET   A 257 ? 0.3800 0.3631 0.4542 -0.0058 0.0252  -0.0122 413 MET   A C   
1825 O  O   . MET   A 257 ? 0.3686 0.3619 0.4496 -0.0077 0.0274  -0.0094 413 MET   A O   
1826 C  CB  . MET   A 257 ? 0.3498 0.3236 0.4073 -0.0105 0.0154  -0.0088 413 MET   A CB  
1827 C  CG  . MET   A 257 ? 0.4019 0.3744 0.4474 -0.0141 0.0136  -0.0078 413 MET   A CG  
1828 S  SD  . MET   A 257 ? 0.5047 0.4691 0.5495 -0.0131 0.0048  -0.0028 413 MET   A SD  
1829 C  CE  . MET   A 257 ? 0.3876 0.3580 0.4404 -0.0159 0.0030  0.0043  413 MET   A CE  
1830 N  N   . LYS   A 258 ? 0.3632 0.3400 0.4431 -0.0004 0.0234  -0.0131 414 LYS   A N   
1831 C  CA  . LYS   A 258 ? 0.3821 0.3653 0.4773 0.0039  0.0242  -0.0107 414 LYS   A CA  
1832 C  C   . LYS   A 258 ? 0.3612 0.3510 0.4615 0.0054  0.0345  -0.0139 414 LYS   A C   
1833 O  O   . LYS   A 258 ? 0.3537 0.3549 0.4655 0.0057  0.0364  -0.0108 414 LYS   A O   
1834 C  CB  . LYS   A 258 ? 0.3472 0.3232 0.4470 0.0098  0.0207  -0.0102 414 LYS   A CB  
1835 C  CG  . LYS   A 258 ? 0.3843 0.3565 0.4825 0.0086  0.0104  -0.0064 414 LYS   A CG  
1836 C  CD  . LYS   A 258 ? 0.4989 0.4665 0.6022 0.0144  0.0075  -0.0052 414 LYS   A CD  
1837 C  CE  . LYS   A 258 ? 0.5154 0.4804 0.6167 0.0127  -0.0024 -0.0020 414 LYS   A CE  
1838 N  NZ  . LYS   A 258 ? 0.7106 0.6737 0.8172 0.0181  -0.0051 0.0002  414 LYS   A NZ  
1839 N  N   . TYR   A 259 ? 0.3542 0.3370 0.4465 0.0062  0.0417  -0.0206 415 TYR   A N   
1840 C  CA  . TYR   A 259 ? 0.3580 0.3451 0.4540 0.0077  0.0529  -0.0251 415 TYR   A CA  
1841 C  C   . TYR   A 259 ? 0.3702 0.3694 0.4634 0.0015  0.0562  -0.0245 415 TYR   A C   
1842 O  O   . TYR   A 259 ? 0.3557 0.3641 0.4578 0.0028  0.0632  -0.0248 415 TYR   A O   
1843 C  CB  . TYR   A 259 ? 0.3676 0.3424 0.4530 0.0082  0.0600  -0.0334 415 TYR   A CB  
1844 C  CG  . TYR   A 259 ? 0.4483 0.4239 0.5369 0.0102  0.0731  -0.0397 415 TYR   A CG  
1845 C  CD1 . TYR   A 259 ? 0.4140 0.3900 0.5186 0.0187  0.0779  -0.0382 415 TYR   A CD1 
1846 C  CD2 . TYR   A 259 ? 0.4944 0.4704 0.5697 0.0037  0.0810  -0.0472 415 TYR   A CD2 
1847 C  CE1 . TYR   A 259 ? 0.4852 0.4608 0.5936 0.0215  0.0910  -0.0441 415 TYR   A CE1 
1848 C  CE2 . TYR   A 259 ? 0.5142 0.4897 0.5916 0.0053  0.0940  -0.0541 415 TYR   A CE2 
1849 C  CZ  . TYR   A 259 ? 0.5694 0.5439 0.6638 0.0146  0.0994  -0.0527 415 TYR   A CZ  
1850 O  OH  . TYR   A 259 ? 0.6001 0.5733 0.6978 0.0172  0.1135  -0.0596 415 TYR   A OH  
1851 N  N   . LEU   A 260 ? 0.3834 0.3836 0.4652 -0.0051 0.0511  -0.0227 416 LEU   A N   
1852 C  CA  . LEU   A 260 ? 0.4365 0.4488 0.5155 -0.0112 0.0534  -0.0204 416 LEU   A CA  
1853 C  C   . LEU   A 260 ? 0.4020 0.4245 0.4957 -0.0104 0.0509  -0.0135 416 LEU   A C   
1854 O  O   . LEU   A 260 ? 0.3938 0.4273 0.4933 -0.0114 0.0576  -0.0134 416 LEU   A O   
1855 C  CB  . LEU   A 260 ? 0.3732 0.3846 0.4392 -0.0172 0.0475  -0.0176 416 LEU   A CB  
1856 C  CG  . LEU   A 260 ? 0.4653 0.4891 0.5277 -0.0237 0.0484  -0.0128 416 LEU   A CG  
1857 C  CD1 . LEU   A 260 ? 0.3732 0.4056 0.4298 -0.0273 0.0589  -0.0183 416 LEU   A CD1 
1858 C  CD2 . LEU   A 260 ? 0.3933 0.4156 0.4448 -0.0279 0.0422  -0.0086 416 LEU   A CD2 
1859 N  N   . LEU   A 261 ? 0.3680 0.3875 0.4679 -0.0090 0.0416  -0.0081 417 LEU   A N   
1860 C  CA  . LEU   A 261 ? 0.3545 0.3836 0.4679 -0.0097 0.0385  -0.0018 417 LEU   A CA  
1861 C  C   . LEU   A 261 ? 0.4141 0.4511 0.5423 -0.0043 0.0442  -0.0026 417 LEU   A C   
1862 O  O   . LEU   A 261 ? 0.3758 0.4256 0.5136 -0.0060 0.0475  0.0004  417 LEU   A O   
1863 C  CB  . LEU   A 261 ? 0.3670 0.3900 0.4831 -0.0096 0.0279  0.0024  417 LEU   A CB  
1864 C  CG  . LEU   A 261 ? 0.3485 0.3811 0.4776 -0.0120 0.0241  0.0084  417 LEU   A CG  
1865 C  CD1 . LEU   A 261 ? 0.3543 0.3932 0.4809 -0.0187 0.0255  0.0123  417 LEU   A CD1 
1866 C  CD2 . LEU   A 261 ? 0.4619 0.4878 0.5929 -0.0124 0.0144  0.0110  417 LEU   A CD2 
1867 N  N   . GLU   A 262 ? 0.3769 0.4065 0.5076 0.0024  0.0461  -0.0062 418 GLU   A N   
1868 C  CA  . GLU   A 262 ? 0.4368 0.4738 0.5835 0.0089  0.0515  -0.0056 418 GLU   A CA  
1869 C  C   . GLU   A 262 ? 0.3786 0.4231 0.5264 0.0087  0.0637  -0.0097 418 GLU   A C   
1870 O  O   . GLU   A 262 ? 0.3815 0.4392 0.5436 0.0106  0.0678  -0.0067 418 GLU   A O   
1871 C  CB  . GLU   A 262 ? 0.3997 0.4256 0.5480 0.0164  0.0517  -0.0080 418 GLU   A CB  
1872 C  CG  . GLU   A 262 ? 0.4723 0.4944 0.6234 0.0176  0.0400  -0.0029 418 GLU   A CG  
1873 C  CD  . GLU   A 262 ? 0.4992 0.5089 0.6484 0.0241  0.0401  -0.0050 418 GLU   A CD  
1874 O  OE1 . GLU   A 262 ? 0.5200 0.5270 0.6738 0.0300  0.0495  -0.0083 418 GLU   A OE1 
1875 O  OE2 . GLU   A 262 ? 0.4225 0.4238 0.5644 0.0228  0.0317  -0.0040 418 GLU   A OE2 
1876 N  N   . GLN   A 263 ? 0.3966 0.4339 0.5291 0.0058  0.0698  -0.0167 419 GLN   A N   
1877 C  CA  . GLN   A 263 ? 0.4682 0.5125 0.5992 0.0043  0.0819  -0.0217 419 GLN   A CA  
1878 C  C   . GLN   A 263 ? 0.4032 0.4630 0.5368 -0.0019 0.0815  -0.0165 419 GLN   A C   
1879 O  O   . GLN   A 263 ? 0.4055 0.4769 0.5486 -0.0008 0.0897  -0.0165 419 GLN   A O   
1880 C  CB  . GLN   A 263 ? 0.4548 0.4888 0.5665 0.0004  0.0872  -0.0303 419 GLN   A CB  
1881 C  CG  . GLN   A 263 ? 0.4492 0.4678 0.5596 0.0065  0.0907  -0.0363 419 GLN   A CG  
1882 C  CD  . GLN   A 263 ? 0.5244 0.5438 0.6457 0.0131  0.1035  -0.0407 419 GLN   A CD  
1883 O  OE1 . GLN   A 263 ? 0.5209 0.5429 0.6597 0.0213  0.1033  -0.0361 419 GLN   A OE1 
1884 N  NE2 . GLN   A 263 ? 0.6116 0.6292 0.7225 0.0095  0.1151  -0.0498 419 GLN   A NE2 
1885 N  N   . LEU   A 264 ? 0.4061 0.4660 0.5325 -0.0081 0.0724  -0.0115 420 LEU   A N   
1886 C  CA  . LEU   A 264 ? 0.4160 0.4893 0.5452 -0.0143 0.0717  -0.0055 420 LEU   A CA  
1887 C  C   . LEU   A 264 ? 0.4484 0.5323 0.5972 -0.0120 0.0692  0.0009  420 LEU   A C   
1888 O  O   . LEU   A 264 ? 0.4147 0.5127 0.5711 -0.0144 0.0744  0.0035  420 LEU   A O   
1889 C  CB  . LEU   A 264 ? 0.3841 0.4532 0.5018 -0.0207 0.0631  -0.0010 420 LEU   A CB  
1890 C  CG  . LEU   A 264 ? 0.4218 0.4866 0.5205 -0.0250 0.0659  -0.0053 420 LEU   A CG  
1891 C  CD1 . LEU   A 264 ? 0.4683 0.5285 0.5586 -0.0294 0.0566  0.0007  420 LEU   A CD1 
1892 C  CD2 . LEU   A 264 ? 0.3903 0.4676 0.4841 -0.0296 0.0759  -0.0076 420 LEU   A CD2 
1893 N  N   . LYS   A 265 ? 0.4268 0.5058 0.5841 -0.0079 0.0612  0.0037  421 LYS   A N   
1894 C  CA  . LYS   A 265 ? 0.4275 0.5190 0.6036 -0.0066 0.0585  0.0097  421 LYS   A CA  
1895 C  C   . LYS   A 265 ? 0.4333 0.5357 0.6226 -0.0005 0.0690  0.0080  421 LYS   A C   
1896 O  O   . LYS   A 265 ? 0.4010 0.5193 0.6030 -0.0022 0.0718  0.0123  421 LYS   A O   
1897 C  CB  . LYS   A 265 ? 0.4192 0.5049 0.6011 -0.0038 0.0482  0.0128  421 LYS   A CB  
1898 C  CG  . LYS   A 265 ? 0.4656 0.5437 0.6384 -0.0105 0.0383  0.0157  421 LYS   A CG  
1899 C  CD  . LYS   A 265 ? 0.4789 0.5525 0.6567 -0.0089 0.0285  0.0181  421 LYS   A CD  
1900 C  CE  . LYS   A 265 ? 0.4136 0.5036 0.6096 -0.0101 0.0264  0.0238  421 LYS   A CE  
1901 N  NZ  . LYS   A 265 ? 0.5462 0.6341 0.7455 -0.0116 0.0159  0.0266  421 LYS   A NZ  
1902 N  N   . GLU   A 266 ? 0.4229 0.5167 0.6096 0.0064  0.0758  0.0016  422 GLU   A N   
1903 C  CA  . GLU   A 266 ? 0.5025 0.6045 0.7012 0.0128  0.0878  -0.0009 422 GLU   A CA  
1904 C  C   . GLU   A 266 ? 0.5225 0.6346 0.7167 0.0075  0.0974  -0.0033 422 GLU   A C   
1905 O  O   . GLU   A 266 ? 0.5073 0.6355 0.7161 0.0085  0.1028  0.0000  422 GLU   A O   
1906 C  CB  . GLU   A 266 ? 0.4950 0.5820 0.6889 0.0202  0.0944  -0.0082 422 GLU   A CB  
1907 C  CG  . GLU   A 266 ? 0.5588 0.6515 0.7690 0.0298  0.1064  -0.0097 422 GLU   A CG  
1908 C  CD  . GLU   A 266 ? 0.5771 0.6858 0.8114 0.0353  0.1021  0.0000  422 GLU   A CD  
1909 O  OE1 . GLU   A 266 ? 0.6072 0.7166 0.8447 0.0340  0.0892  0.0064  422 GLU   A OE1 
1910 O  OE2 . GLU   A 266 ? 0.6688 0.7903 0.9189 0.0405  0.1118  0.0012  422 GLU   A OE2 
1911 N  N   . ARG   A 267 ? 0.5348 0.6392 0.7090 0.0011  0.0992  -0.0085 423 ARG   A N   
1912 C  CA  . ARG   A 267 ? 0.5210 0.6352 0.6882 -0.0047 0.1085  -0.0111 423 ARG   A CA  
1913 C  C   . ARG   A 267 ? 0.5030 0.6345 0.6805 -0.0098 0.1058  -0.0025 423 ARG   A C   
1914 O  O   . ARG   A 267 ? 0.4990 0.6440 0.6820 -0.0109 0.1153  -0.0029 423 ARG   A O   
1915 C  CB  . ARG   A 267 ? 0.5030 0.6084 0.6469 -0.0120 0.1076  -0.0156 423 ARG   A CB  
1916 C  CG  . ARG   A 267 ? 0.5960 0.7130 0.7309 -0.0192 0.1163  -0.0175 423 ARG   A CG  
1917 C  CD  . ARG   A 267 ? 0.6189 0.7277 0.7322 -0.0235 0.1218  -0.0266 423 ARG   A CD  
1918 N  NE  . ARG   A 267 ? 0.6816 0.7866 0.7952 -0.0189 0.1354  -0.0371 423 ARG   A NE  
1919 C  CZ  . ARG   A 267 ? 0.7069 0.8232 0.8255 -0.0188 0.1477  -0.0403 423 ARG   A CZ  
1920 N  NH1 . ARG   A 267 ? 0.7625 0.8960 0.8866 -0.0232 0.1480  -0.0334 423 ARG   A NH1 
1921 N  NH2 . ARG   A 267 ? 0.7303 0.8399 0.8484 -0.0142 0.1608  -0.0507 423 ARG   A NH2 
1922 N  N   . PHE   A 268 ? 0.5320 0.6629 0.7121 -0.0134 0.0935  0.0051  424 PHE   A N   
1923 C  CA  . PHE   A 268 ? 0.5307 0.6759 0.7196 -0.0195 0.0904  0.0133  424 PHE   A CA  
1924 C  C   . PHE   A 268 ? 0.5647 0.7181 0.7743 -0.0164 0.0844  0.0195  424 PHE   A C   
1925 O  O   . PHE   A 268 ? 0.6448 0.8038 0.8595 -0.0225 0.0770  0.0264  424 PHE   A O   
1926 C  CB  . PHE   A 268 ? 0.5736 0.7126 0.7490 -0.0279 0.0822  0.0175  424 PHE   A CB  
1927 C  CG  . PHE   A 268 ? 0.5152 0.6516 0.6716 -0.0323 0.0876  0.0136  424 PHE   A CG  
1928 C  CD1 . PHE   A 268 ? 0.5348 0.6848 0.6892 -0.0369 0.0966  0.0141  424 PHE   A CD1 
1929 C  CD2 . PHE   A 268 ? 0.5687 0.6905 0.7091 -0.0323 0.0840  0.0096  424 PHE   A CD2 
1930 C  CE1 . PHE   A 268 ? 0.5340 0.6837 0.6701 -0.0418 0.1012  0.0108  424 PHE   A CE1 
1931 C  CE2 . PHE   A 268 ? 0.5102 0.6320 0.6331 -0.0372 0.0884  0.0064  424 PHE   A CE2 
1932 C  CZ  . PHE   A 268 ? 0.5316 0.6676 0.6520 -0.0422 0.0969  0.0070  424 PHE   A CZ  
1933 N  N   . LYS   A 269 ? 0.5243 0.6791 0.7461 -0.0072 0.0878  0.0173  425 LYS   A N   
1934 C  CA  . LYS   A 269 ? 0.5871 0.7525 0.8291 -0.0041 0.0819  0.0238  425 LYS   A CA  
1935 C  C   . LYS   A 269 ? 0.6185 0.8047 0.8746 -0.0095 0.0832  0.0305  425 LYS   A C   
1936 O  O   . LYS   A 269 ? 0.6097 0.8048 0.8790 -0.0116 0.0750  0.0371  425 LYS   A O   
1937 C  CB  . LYS   A 269 ? 0.5740 0.7405 0.8284 0.0076  0.0880  0.0215  425 LYS   A CB  
1938 C  CG  . LYS   A 269 ? 0.6099 0.7942 0.8804 0.0120  0.1003  0.0222  425 LYS   A CG  
1939 C  CD  . LYS   A 269 ? 0.5610 0.7438 0.8439 0.0247  0.1071  0.0203  425 LYS   A CD  
1940 C  CE  . LYS   A 269 ? 0.5687 0.7299 0.8344 0.0286  0.1139  0.0103  425 LYS   A CE  
1941 N  NZ  . LYS   A 269 ? 0.6068 0.7688 0.8826 0.0390  0.1288  0.0058  425 LYS   A NZ  
1942 N  N   . ASP   A 270 ? 0.6399 0.8343 0.8928 -0.0127 0.0932  0.0290  426 ASP   A N   
1943 C  CA  . ASP   A 270 ? 0.6545 0.8696 0.9210 -0.0178 0.0961  0.0353  426 ASP   A CA  
1944 C  C   . ASP   A 270 ? 0.6481 0.8628 0.9076 -0.0294 0.0884  0.0410  426 ASP   A C   
1945 O  O   . ASP   A 270 ? 0.6653 0.8963 0.9362 -0.0351 0.0893  0.0471  426 ASP   A O   
1946 C  CB  . ASP   A 270 ? 0.7006 0.9252 0.9664 -0.0161 0.1113  0.0311  426 ASP   A CB  
1947 C  CG  . ASP   A 270 ? 0.7524 0.9786 1.0289 -0.0041 0.1210  0.0261  426 ASP   A CG  
1948 O  OD1 . ASP   A 270 ? 0.7784 1.0063 1.0696 0.0025  0.1156  0.0295  426 ASP   A OD1 
1949 O  OD2 . ASP   A 270 ? 0.7743 0.9999 1.0443 -0.0015 0.1342  0.0190  426 ASP   A OD2 
1950 N  N   . LYS   A 271 ? 0.6488 0.8456 0.8906 -0.0330 0.0816  0.0394  427 LYS   A N   
1951 C  CA  . LYS   A 271 ? 0.6257 0.8188 0.8614 -0.0429 0.0740  0.0452  427 LYS   A CA  
1952 C  C   . LYS   A 271 ? 0.6649 0.8494 0.9048 -0.0438 0.0616  0.0475  427 LYS   A C   
1953 O  O   . LYS   A 271 ? 0.7012 0.8779 0.9415 -0.0369 0.0582  0.0438  427 LYS   A O   
1954 C  CB  . LYS   A 271 ? 0.6905 0.8702 0.9044 -0.0461 0.0749  0.0428  427 LYS   A CB  
1955 C  CG  . LYS   A 271 ? 0.7521 0.9416 0.9593 -0.0479 0.0865  0.0410  427 LYS   A CG  
1956 C  CD  . LYS   A 271 ? 0.6280 0.8064 0.8137 -0.0516 0.0861  0.0397  427 LYS   A CD  
1957 C  CE  . LYS   A 271 ? 0.7023 0.8923 0.8803 -0.0552 0.0968  0.0386  427 LYS   A CE  
1958 N  NZ  . LYS   A 271 ? 0.7513 0.9543 0.9358 -0.0631 0.0972  0.0479  427 LYS   A NZ  
1959 N  N   . LYS   A 272 ? 0.6884 0.8745 0.9315 -0.0527 0.0555  0.0537  428 LYS   A N   
1960 C  CA  . LYS   A 272 ? 0.6209 0.7966 0.8644 -0.0555 0.0441  0.0549  428 LYS   A CA  
1961 C  C   . LYS   A 272 ? 0.5987 0.7521 0.8233 -0.0563 0.0393  0.0525  428 LYS   A C   
1962 O  O   . LYS   A 272 ? 0.6376 0.7798 0.8602 -0.0577 0.0306  0.0521  428 LYS   A O   
1963 C  CB  . LYS   A 272 ? 0.5811 0.7659 0.8355 -0.0656 0.0399  0.0616  428 LYS   A CB  
1964 C  CG  . LYS   A 272 ? 0.6497 0.8585 0.9253 -0.0655 0.0424  0.0649  428 LYS   A CG  
1965 C  CD  . LYS   A 272 ? 0.6634 0.8762 0.9489 -0.0586 0.0370  0.0631  428 LYS   A CD  
1966 C  CE  . LYS   A 272 ? 0.6478 0.8509 0.9311 -0.0648 0.0250  0.0638  428 LYS   A CE  
1967 N  NZ  . LYS   A 272 ? 0.6759 0.8825 0.9665 -0.0584 0.0190  0.0626  428 LYS   A NZ  
1968 N  N   . HIS   A 273 ? 0.5266 0.6744 0.7374 -0.0554 0.0450  0.0507  429 HIS   A N   
1969 C  CA  . HIS   A 273 ? 0.5163 0.6463 0.7108 -0.0576 0.0409  0.0509  429 HIS   A CA  
1970 C  C   . HIS   A 273 ? 0.5125 0.6272 0.6993 -0.0516 0.0354  0.0454  429 HIS   A C   
1971 O  O   . HIS   A 273 ? 0.4877 0.5877 0.6657 -0.0537 0.0294  0.0462  429 HIS   A O   
1972 C  CB  . HIS   A 273 ? 0.5417 0.6734 0.7238 -0.0584 0.0483  0.0510  429 HIS   A CB  
1973 C  CG  . HIS   A 273 ? 0.5274 0.6702 0.7128 -0.0660 0.0523  0.0581  429 HIS   A CG  
1974 N  ND1 . HIS   A 273 ? 0.6409 0.8012 0.8407 -0.0682 0.0570  0.0605  429 HIS   A ND1 
1975 C  CD2 . HIS   A 273 ? 0.5227 0.6621 0.6992 -0.0718 0.0526  0.0643  429 HIS   A CD2 
1976 C  CE1 . HIS   A 273 ? 0.5573 0.7241 0.7565 -0.0755 0.0599  0.0674  429 HIS   A CE1 
1977 N  NE2 . HIS   A 273 ? 0.6487 0.8028 0.8339 -0.0777 0.0573  0.0701  429 HIS   A NE2 
1978 N  N   . LEU   A 274 ? 0.4477 0.5649 0.6376 -0.0439 0.0379  0.0400  430 LEU   A N   
1979 C  CA  . LEU   A 274 ? 0.4811 0.5838 0.6628 -0.0382 0.0335  0.0350  430 LEU   A CA  
1980 C  C   . LEU   A 274 ? 0.4586 0.5625 0.6515 -0.0351 0.0271  0.0348  430 LEU   A C   
1981 O  O   . LEU   A 274 ? 0.4453 0.5388 0.6330 -0.0298 0.0238  0.0311  430 LEU   A O   
1982 C  CB  . LEU   A 274 ? 0.4626 0.5635 0.6365 -0.0319 0.0410  0.0288  430 LEU   A CB  
1983 C  CG  . LEU   A 274 ? 0.4247 0.5258 0.5852 -0.0352 0.0473  0.0280  430 LEU   A CG  
1984 C  CD1 . LEU   A 274 ? 0.4417 0.5387 0.5938 -0.0297 0.0538  0.0201  430 LEU   A CD1 
1985 C  CD2 . LEU   A 274 ? 0.3802 0.4702 0.5288 -0.0401 0.0412  0.0315  430 LEU   A CD2 
1986 N  N   . ASP   A 275 ? 0.4626 0.5798 0.6704 -0.0388 0.0250  0.0393  431 ASP   A N   
1987 C  CA  . ASP   A 275 ? 0.4969 0.6200 0.7167 -0.0360 0.0194  0.0400  431 ASP   A CA  
1988 C  C   . ASP   A 275 ? 0.5096 0.6183 0.7219 -0.0383 0.0094  0.0390  431 ASP   A C   
1989 O  O   . ASP   A 275 ? 0.5051 0.6136 0.7209 -0.0337 0.0048  0.0379  431 ASP   A O   
1990 C  CB  . ASP   A 275 ? 0.4555 0.5982 0.6929 -0.0410 0.0190  0.0455  431 ASP   A CB  
1991 C  CG  . ASP   A 275 ? 0.5640 0.7233 0.8118 -0.0372 0.0292  0.0465  431 ASP   A CG  
1992 O  OD1 . ASP   A 275 ? 0.6235 0.7786 0.8653 -0.0300 0.0366  0.0420  431 ASP   A OD1 
1993 O  OD2 . ASP   A 275 ? 0.6102 0.7869 0.8721 -0.0417 0.0302  0.0513  431 ASP   A OD2 
1994 N  N   . LYS   A 276 ? 0.3768 0.4740 0.5793 -0.0454 0.0062  0.0398  432 LYS   A N   
1995 C  CA  . LYS   A 276 ? 0.4057 0.4890 0.6013 -0.0485 -0.0024 0.0384  432 LYS   A CA  
1996 C  C   . LYS   A 276 ? 0.4796 0.5454 0.6599 -0.0431 -0.0031 0.0340  432 LYS   A C   
1997 O  O   . LYS   A 276 ? 0.4688 0.5224 0.6424 -0.0448 -0.0095 0.0322  432 LYS   A O   
1998 C  CB  . LYS   A 276 ? 0.4654 0.5434 0.6593 -0.0587 -0.0046 0.0414  432 LYS   A CB  
1999 C  CG  . LYS   A 276 ? 0.5384 0.6333 0.7478 -0.0660 -0.0055 0.0457  432 LYS   A CG  
2000 C  CD  . LYS   A 276 ? 0.5421 0.6291 0.7495 -0.0768 -0.0073 0.0483  432 LYS   A CD  
2001 C  CE  . LYS   A 276 ? 0.5106 0.6137 0.7329 -0.0854 -0.0096 0.0517  432 LYS   A CE  
2002 N  NZ  . LYS   A 276 ? 0.6103 0.7029 0.8299 -0.0965 -0.0105 0.0538  432 LYS   A NZ  
2003 N  N   . PHE   A 277 ? 0.4409 0.5054 0.6151 -0.0373 0.0034  0.0317  433 PHE   A N   
2004 C  CA  . PHE   A 277 ? 0.3971 0.4467 0.5574 -0.0326 0.0027  0.0275  433 PHE   A CA  
2005 C  C   . PHE   A 277 ? 0.4375 0.4879 0.6012 -0.0251 0.0016  0.0244  433 PHE   A C   
2006 O  O   . PHE   A 277 ? 0.3898 0.4526 0.5649 -0.0212 0.0055  0.0250  433 PHE   A O   
2007 C  CB  . PHE   A 277 ? 0.3579 0.4061 0.5089 -0.0315 0.0100  0.0264  433 PHE   A CB  
2008 C  CG  . PHE   A 277 ? 0.3579 0.4052 0.5049 -0.0382 0.0109  0.0310  433 PHE   A CG  
2009 C  CD1 . PHE   A 277 ? 0.3579 0.3913 0.4956 -0.0407 0.0066  0.0323  433 PHE   A CD1 
2010 C  CD2 . PHE   A 277 ? 0.3691 0.4294 0.5224 -0.0418 0.0165  0.0345  433 PHE   A CD2 
2011 C  CE1 . PHE   A 277 ? 0.4215 0.4535 0.5570 -0.0463 0.0079  0.0378  433 PHE   A CE1 
2012 C  CE2 . PHE   A 277 ? 0.3612 0.4208 0.5114 -0.0479 0.0174  0.0400  433 PHE   A CE2 
2013 C  CZ  . PHE   A 277 ? 0.3737 0.4188 0.5153 -0.0500 0.0131  0.0420  433 PHE   A CZ  
2014 N  N   . SER   A 278 ? 0.4216 0.4588 0.5762 -0.0229 -0.0033 0.0217  434 SER   A N   
2015 C  CA  . SER   A 278 ? 0.4100 0.4464 0.5668 -0.0159 -0.0047 0.0196  434 SER   A CA  
2016 C  C   . SER   A 278 ? 0.3527 0.3734 0.4949 -0.0126 -0.0050 0.0154  434 SER   A C   
2017 O  O   . SER   A 278 ? 0.3474 0.3587 0.4784 -0.0157 -0.0054 0.0145  434 SER   A O   
2018 C  CB  . SER   A 278 ? 0.4306 0.4716 0.5952 -0.0177 -0.0129 0.0220  434 SER   A CB  
2019 O  OG  . SER   A 278 ? 0.4016 0.4293 0.5552 -0.0214 -0.0193 0.0204  434 SER   A OG  
2020 N  N   . SER   A 279 ? 0.3674 0.3860 0.5107 -0.0060 -0.0049 0.0136  435 SER   A N   
2021 C  CA  . SER   A 279 ? 0.3911 0.3954 0.5214 -0.0031 -0.0055 0.0097  435 SER   A CA  
2022 C  C   . SER   A 279 ? 0.3478 0.3421 0.4693 -0.0070 -0.0130 0.0098  435 SER   A C   
2023 O  O   . SER   A 279 ? 0.3535 0.3364 0.4631 -0.0061 -0.0132 0.0070  435 SER   A O   
2024 C  CB  . SER   A 279 ? 0.4035 0.4068 0.5379 0.0042  -0.0048 0.0090  435 SER   A CB  
2025 O  OG  . SER   A 279 ? 0.4011 0.4082 0.5416 0.0038  -0.0127 0.0124  435 SER   A OG  
2026 N  N   . TYR   A 280 ? 0.3658 0.3643 0.4929 -0.0116 -0.0189 0.0125  436 TYR   A N   
2027 C  CA  . TYR   A 280 ? 0.3847 0.3724 0.5029 -0.0157 -0.0249 0.0115  436 TYR   A CA  
2028 C  C   . TYR   A 280 ? 0.3519 0.3314 0.4617 -0.0193 -0.0225 0.0113  436 TYR   A C   
2029 O  O   . TYR   A 280 ? 0.3285 0.2959 0.4279 -0.0194 -0.0243 0.0095  436 TYR   A O   
2030 C  CB  . TYR   A 280 ? 0.3614 0.3556 0.4871 -0.0211 -0.0312 0.0136  436 TYR   A CB  
2031 C  CG  . TYR   A 280 ? 0.3786 0.3612 0.4948 -0.0249 -0.0371 0.0114  436 TYR   A CG  
2032 C  CD1 . TYR   A 280 ? 0.4571 0.4345 0.5672 -0.0214 -0.0407 0.0095  436 TYR   A CD1 
2033 C  CD2 . TYR   A 280 ? 0.3531 0.3292 0.4661 -0.0321 -0.0382 0.0110  436 TYR   A CD2 
2034 C  CE1 . TYR   A 280 ? 0.3731 0.3400 0.4737 -0.0251 -0.0454 0.0069  436 TYR   A CE1 
2035 C  CE2 . TYR   A 280 ? 0.4183 0.3824 0.5222 -0.0355 -0.0423 0.0080  436 TYR   A CE2 
2036 C  CZ  . TYR   A 280 ? 0.3840 0.3441 0.4815 -0.0321 -0.0458 0.0057  436 TYR   A CZ  
2037 O  OH  . TYR   A 280 ? 0.4216 0.3701 0.5095 -0.0357 -0.0492 0.0022  436 TYR   A OH  
2038 N  N   . HIS   A 281 ? 0.3353 0.3220 0.4500 -0.0221 -0.0183 0.0138  437 HIS   A N   
2039 C  CA  . HIS   A 281 ? 0.3568 0.3375 0.4641 -0.0248 -0.0154 0.0152  437 HIS   A CA  
2040 C  C   . HIS   A 281 ? 0.3211 0.2960 0.4178 -0.0205 -0.0123 0.0128  437 HIS   A C   
2041 O  O   . HIS   A 281 ? 0.3415 0.3069 0.4294 -0.0210 -0.0134 0.0130  437 HIS   A O   
2042 C  CB  . HIS   A 281 ? 0.3278 0.3197 0.4426 -0.0282 -0.0109 0.0188  437 HIS   A CB  
2043 C  CG  . HIS   A 281 ? 0.3284 0.3262 0.4535 -0.0338 -0.0139 0.0214  437 HIS   A CG  
2044 N  ND1 . HIS   A 281 ? 0.3448 0.3578 0.4822 -0.0344 -0.0118 0.0232  437 HIS   A ND1 
2045 C  CD2 . HIS   A 281 ? 0.3135 0.3045 0.4387 -0.0395 -0.0183 0.0223  437 HIS   A CD2 
2046 C  CE1 . HIS   A 281 ? 0.3740 0.3905 0.5186 -0.0406 -0.0157 0.0254  437 HIS   A CE1 
2047 N  NE2 . HIS   A 281 ? 0.4185 0.4211 0.5555 -0.0442 -0.0196 0.0244  437 HIS   A NE2 
2048 N  N   . VAL   A 282 ? 0.3308 0.3116 0.4288 -0.0166 -0.0080 0.0105  438 VAL   A N   
2049 C  CA  . VAL   A 282 ? 0.3311 0.3071 0.4187 -0.0138 -0.0047 0.0074  438 VAL   A CA  
2050 C  C   . VAL   A 282 ? 0.4022 0.3666 0.4823 -0.0113 -0.0093 0.0051  438 VAL   A C   
2051 O  O   . VAL   A 282 ? 0.3199 0.2780 0.3903 -0.0116 -0.0093 0.0047  438 VAL   A O   
2052 C  CB  . VAL   A 282 ? 0.4107 0.3933 0.5018 -0.0103 0.0014  0.0042  438 VAL   A CB  
2053 C  CG1 . VAL   A 282 ? 0.4666 0.4420 0.5479 -0.0075 0.0037  -0.0002 438 VAL   A CG1 
2054 C  CG2 . VAL   A 282 ? 0.4252 0.4183 0.5186 -0.0134 0.0075  0.0057  438 VAL   A CG2 
2055 N  N   . LYS   A 283 ? 0.3500 0.3129 0.4348 -0.0092 -0.0133 0.0042  439 LYS   A N   
2056 C  CA  . LYS   A 283 ? 0.3530 0.3058 0.4304 -0.0070 -0.0173 0.0021  439 LYS   A CA  
2057 C  C   . LYS   A 283 ? 0.3163 0.2611 0.3878 -0.0103 -0.0211 0.0032  439 LYS   A C   
2058 O  O   . LYS   A 283 ? 0.3702 0.3070 0.4326 -0.0092 -0.0215 0.0019  439 LYS   A O   
2059 C  CB  . LYS   A 283 ? 0.3371 0.2924 0.4214 -0.0044 -0.0210 0.0022  439 LYS   A CB  
2060 C  CG  . LYS   A 283 ? 0.4779 0.4245 0.5552 -0.0015 -0.0243 0.0003  439 LYS   A CG  
2061 C  CD  . LYS   A 283 ? 0.4944 0.4461 0.5797 0.0027  -0.0258 0.0015  439 LYS   A CD  
2062 C  CE  . LYS   A 283 ? 0.5899 0.5522 0.6861 0.0001  -0.0303 0.0050  439 LYS   A CE  
2063 N  NZ  . LYS   A 283 ? 0.6120 0.5737 0.7068 -0.0010 -0.0378 0.0061  439 LYS   A NZ  
2064 N  N   . THR   A 284 ? 0.3222 0.2689 0.3992 -0.0147 -0.0231 0.0057  440 THR   A N   
2065 C  CA  . THR   A 284 ? 0.3363 0.2737 0.4083 -0.0178 -0.0250 0.0066  440 THR   A CA  
2066 C  C   . THR   A 284 ? 0.3474 0.2821 0.4131 -0.0170 -0.0211 0.0086  440 THR   A C   
2067 O  O   . THR   A 284 ? 0.3490 0.2751 0.4074 -0.0157 -0.0218 0.0082  440 THR   A O   
2068 C  CB  . THR   A 284 ? 0.3978 0.3372 0.4771 -0.0235 -0.0266 0.0087  440 THR   A CB  
2069 O  OG1 . THR   A 284 ? 0.3883 0.3327 0.4733 -0.0248 -0.0310 0.0072  440 THR   A OG1 
2070 C  CG2 . THR   A 284 ? 0.3632 0.2899 0.4372 -0.0264 -0.0276 0.0089  440 THR   A CG2 
2071 N  N   . ALA   A 285 ? 0.3397 0.2833 0.4084 -0.0179 -0.0169 0.0112  441 ALA   A N   
2072 C  CA  . ALA   A 285 ? 0.3811 0.3255 0.4437 -0.0177 -0.0136 0.0140  441 ALA   A CA  
2073 C  C   . ALA   A 285 ? 0.3277 0.2684 0.3814 -0.0143 -0.0136 0.0109  441 ALA   A C   
2074 O  O   . ALA   A 285 ? 0.3608 0.2975 0.4087 -0.0136 -0.0137 0.0131  441 ALA   A O   
2075 C  CB  . ALA   A 285 ? 0.2991 0.2557 0.3647 -0.0195 -0.0089 0.0160  441 ALA   A CB  
2076 N  N   . PHE   A 286 ? 0.3068 0.2490 0.3602 -0.0119 -0.0132 0.0064  442 PHE   A N   
2077 C  CA  . PHE   A 286 ? 0.3159 0.2545 0.3611 -0.0094 -0.0128 0.0031  442 PHE   A CA  
2078 C  C   . PHE   A 286 ? 0.3498 0.2784 0.3902 -0.0080 -0.0167 0.0029  442 PHE   A C   
2079 O  O   . PHE   A 286 ? 0.2950 0.2215 0.3284 -0.0073 -0.0162 0.0033  442 PHE   A O   
2080 C  CB  . PHE   A 286 ? 0.3119 0.2516 0.3592 -0.0069 -0.0113 -0.0013 442 PHE   A CB  
2081 C  CG  . PHE   A 286 ? 0.3523 0.2861 0.3917 -0.0046 -0.0110 -0.0049 442 PHE   A CG  
2082 C  CD1 . PHE   A 286 ? 0.4524 0.3888 0.4849 -0.0060 -0.0069 -0.0069 442 PHE   A CD1 
2083 C  CD2 . PHE   A 286 ? 0.4420 0.3682 0.4804 -0.0021 -0.0149 -0.0062 442 PHE   A CD2 
2084 C  CE1 . PHE   A 286 ? 0.4355 0.3663 0.4607 -0.0049 -0.0064 -0.0103 442 PHE   A CE1 
2085 C  CE2 . PHE   A 286 ? 0.4771 0.3979 0.5085 -0.0004 -0.0144 -0.0091 442 PHE   A CE2 
2086 C  CZ  . PHE   A 286 ? 0.4758 0.3985 0.5008 -0.0020 -0.0100 -0.0112 442 PHE   A CZ  
2087 N  N   . PHE   A 287 ? 0.3333 0.2565 0.3771 -0.0078 -0.0206 0.0019  443 PHE   A N   
2088 C  CA  . PHE   A 287 ? 0.3248 0.2383 0.3629 -0.0068 -0.0236 0.0009  443 PHE   A CA  
2089 C  C   . PHE   A 287 ? 0.3483 0.2579 0.3840 -0.0076 -0.0225 0.0044  443 PHE   A C   
2090 O  O   . PHE   A 287 ? 0.2916 0.1958 0.3214 -0.0056 -0.0227 0.0042  443 PHE   A O   
2091 C  CB  . PHE   A 287 ? 0.3143 0.2240 0.3555 -0.0079 -0.0279 -0.0009 443 PHE   A CB  
2092 C  CG  . PHE   A 287 ? 0.4124 0.3256 0.4557 -0.0058 -0.0296 -0.0030 443 PHE   A CG  
2093 C  CD1 . PHE   A 287 ? 0.3652 0.2769 0.4034 -0.0025 -0.0283 -0.0049 443 PHE   A CD1 
2094 C  CD2 . PHE   A 287 ? 0.4425 0.3610 0.4936 -0.0073 -0.0323 -0.0026 443 PHE   A CD2 
2095 C  CE1 . PHE   A 287 ? 0.4237 0.3374 0.4648 0.0001  -0.0291 -0.0059 443 PHE   A CE1 
2096 C  CE2 . PHE   A 287 ? 0.4571 0.3798 0.5116 -0.0044 -0.0336 -0.0030 443 PHE   A CE2 
2097 C  CZ  . PHE   A 287 ? 0.4564 0.3759 0.5060 -0.0004 -0.0318 -0.0045 443 PHE   A CZ  
2098 N  N   . HIS   A 288 ? 0.3271 0.2396 0.3681 -0.0101 -0.0210 0.0083  444 HIS   A N   
2099 C  CA  . HIS   A 288 ? 0.3596 0.2689 0.3995 -0.0101 -0.0190 0.0133  444 HIS   A CA  
2100 C  C   . HIS   A 288 ? 0.3640 0.2797 0.3988 -0.0081 -0.0169 0.0157  444 HIS   A C   
2101 O  O   . HIS   A 288 ? 0.3791 0.2915 0.4110 -0.0060 -0.0163 0.0187  444 HIS   A O   
2102 C  CB  . HIS   A 288 ? 0.3647 0.2767 0.4116 -0.0134 -0.0174 0.0180  444 HIS   A CB  
2103 C  CG  . HIS   A 288 ? 0.4386 0.3424 0.4898 -0.0165 -0.0193 0.0163  444 HIS   A CG  
2104 N  ND1 . HIS   A 288 ? 0.3977 0.2885 0.4462 -0.0164 -0.0200 0.0148  444 HIS   A ND1 
2105 C  CD2 . HIS   A 288 ? 0.3606 0.2680 0.4184 -0.0206 -0.0204 0.0155  444 HIS   A CD2 
2106 C  CE1 . HIS   A 288 ? 0.3779 0.2639 0.4302 -0.0209 -0.0215 0.0127  444 HIS   A CE1 
2107 N  NE2 . HIS   A 288 ? 0.3982 0.2949 0.4566 -0.0236 -0.0222 0.0135  444 HIS   A NE2 
2108 N  N   . VAL   A 289 ? 0.3467 0.2721 0.3804 -0.0089 -0.0153 0.0143  445 VAL   A N   
2109 C  CA  . VAL   A 289 ? 0.3483 0.2807 0.3759 -0.0087 -0.0135 0.0158  445 VAL   A CA  
2110 C  C   . VAL   A 289 ? 0.3475 0.2745 0.3690 -0.0062 -0.0151 0.0121  445 VAL   A C   
2111 O  O   . VAL   A 289 ? 0.3728 0.3027 0.3903 -0.0054 -0.0146 0.0150  445 VAL   A O   
2112 C  CB  . VAL   A 289 ? 0.3346 0.2774 0.3613 -0.0112 -0.0106 0.0137  445 VAL   A CB  
2113 C  CG1 . VAL   A 289 ? 0.3360 0.2865 0.3549 -0.0125 -0.0090 0.0139  445 VAL   A CG1 
2114 C  CG2 . VAL   A 289 ? 0.3341 0.2837 0.3668 -0.0138 -0.0087 0.0182  445 VAL   A CG2 
2115 N  N   . CYS   A 290 ? 0.3362 0.2566 0.3574 -0.0050 -0.0170 0.0066  446 CYS   A N   
2116 C  CA  . CYS   A 290 ? 0.3444 0.2589 0.3598 -0.0028 -0.0185 0.0037  446 CYS   A CA  
2117 C  C   . CYS   A 290 ? 0.3383 0.2467 0.3528 -0.0010 -0.0194 0.0066  446 CYS   A C   
2118 O  O   . CYS   A 290 ? 0.3632 0.2715 0.3729 0.0006  -0.0191 0.0071  446 CYS   A O   
2119 C  CB  . CYS   A 290 ? 0.3130 0.2216 0.3290 -0.0018 -0.0207 -0.0012 446 CYS   A CB  
2120 S  SG  . CYS   A 290 ? 0.4034 0.3168 0.4201 -0.0021 -0.0184 -0.0050 446 CYS   A SG  
2121 N  N   . THR   A 291 ? 0.3294 0.2322 0.3486 -0.0013 -0.0199 0.0085  447 THR   A N   
2122 C  CA  . THR   A 291 ? 0.3286 0.2237 0.3475 0.0008  -0.0193 0.0110  447 THR   A CA  
2123 C  C   . THR   A 291 ? 0.4122 0.3140 0.4319 0.0022  -0.0166 0.0181  447 THR   A C   
2124 O  O   . THR   A 291 ? 0.3337 0.2336 0.3515 0.0053  -0.0156 0.0201  447 THR   A O   
2125 C  CB  . THR   A 291 ? 0.4117 0.2985 0.4353 -0.0010 -0.0196 0.0109  447 THR   A CB  
2126 O  OG1 . THR   A 291 ? 0.4338 0.3159 0.4561 -0.0026 -0.0228 0.0048  447 THR   A OG1 
2127 C  CG2 . THR   A 291 ? 0.4047 0.2822 0.4288 0.0012  -0.0171 0.0139  447 THR   A CG2 
2128 N  N   . GLN   A 292 ? 0.4442 0.3552 0.4673 0.0001  -0.0153 0.0226  448 GLN   A N   
2129 C  CA  . GLN   A 292 ? 0.4865 0.4066 0.5105 0.0011  -0.0132 0.0307  448 GLN   A CA  
2130 C  C   . GLN   A 292 ? 0.3526 0.2827 0.3707 0.0011  -0.0135 0.0303  448 GLN   A C   
2131 O  O   . GLN   A 292 ? 0.4142 0.3514 0.4327 0.0029  -0.0126 0.0370  448 GLN   A O   
2132 C  CB  . GLN   A 292 ? 0.4887 0.4178 0.5165 -0.0020 -0.0119 0.0356  448 GLN   A CB  
2133 C  CG  . GLN   A 292 ? 0.5136 0.4343 0.5481 -0.0027 -0.0110 0.0379  448 GLN   A CG  
2134 C  CD  . GLN   A 292 ? 0.7544 0.6847 0.7931 -0.0049 -0.0089 0.0462  448 GLN   A CD  
2135 O  OE1 . GLN   A 292 ? 0.7697 0.7138 0.8056 -0.0075 -0.0085 0.0473  448 GLN   A OE1 
2136 N  NE2 . GLN   A 292 ? 0.7268 0.6495 0.7716 -0.0042 -0.0071 0.0521  448 GLN   A NE2 
2137 N  N   . ASN   A 293 ? 0.3762 0.3070 0.3893 -0.0008 -0.0147 0.0231  449 ASN   A N   
2138 C  CA  . ASN   A 293 ? 0.3788 0.3182 0.3856 -0.0023 -0.0146 0.0216  449 ASN   A CA  
2139 C  C   . ASN   A 293 ? 0.3719 0.3023 0.3746 -0.0009 -0.0160 0.0148  449 ASN   A C   
2140 O  O   . ASN   A 293 ? 0.3337 0.2629 0.3332 -0.0029 -0.0160 0.0088  449 ASN   A O   
2141 C  CB  . ASN   A 293 ? 0.3493 0.2990 0.3534 -0.0071 -0.0132 0.0196  449 ASN   A CB  
2142 C  CG  . ASN   A 293 ? 0.4229 0.3829 0.4305 -0.0089 -0.0118 0.0269  449 ASN   A CG  
2143 O  OD1 . ASN   A 293 ? 0.3654 0.3363 0.3720 -0.0096 -0.0116 0.0336  449 ASN   A OD1 
2144 N  ND2 . ASN   A 293 ? 0.4329 0.3903 0.4448 -0.0098 -0.0110 0.0264  449 ASN   A ND2 
2145 N  N   . PRO   A 294 ? 0.3277 0.2517 0.3303 0.0026  -0.0165 0.0160  450 PRO   A N   
2146 C  CA  . PRO   A 294 ? 0.4004 0.3152 0.3989 0.0038  -0.0179 0.0099  450 PRO   A CA  
2147 C  C   . PRO   A 294 ? 0.4179 0.3377 0.4103 0.0023  -0.0178 0.0075  450 PRO   A C   
2148 O  O   . PRO   A 294 ? 0.4113 0.3238 0.4001 0.0025  -0.0188 0.0024  450 PRO   A O   
2149 C  CB  . PRO   A 294 ? 0.4051 0.3116 0.4053 0.0078  -0.0175 0.0120  450 PRO   A CB  
2150 C  CG  . PRO   A 294 ? 0.4232 0.3384 0.4280 0.0094  -0.0154 0.0206  450 PRO   A CG  
2151 C  CD  . PRO   A 294 ? 0.3443 0.2673 0.3516 0.0060  -0.0153 0.0229  450 PRO   A CD  
2152 N  N   . GLN   A 295 ? 0.4017 0.3338 0.3925 0.0002  -0.0168 0.0112  451 GLN   A N   
2153 C  CA  . GLN   A 295 ? 0.3471 0.2838 0.3319 -0.0024 -0.0166 0.0086  451 GLN   A CA  
2154 C  C   . GLN   A 295 ? 0.3539 0.2914 0.3345 -0.0072 -0.0156 0.0026  451 GLN   A C   
2155 O  O   . GLN   A 295 ? 0.3539 0.2966 0.3355 -0.0098 -0.0145 0.0027  451 GLN   A O   
2156 C  CB  . GLN   A 295 ? 0.3983 0.3500 0.3832 -0.0036 -0.0161 0.0151  451 GLN   A CB  
2157 C  CG  . GLN   A 295 ? 0.4550 0.4072 0.4454 0.0021  -0.0158 0.0221  451 GLN   A CG  
2158 C  CD  . GLN   A 295 ? 0.4984 0.4389 0.4874 0.0060  -0.0158 0.0188  451 GLN   A CD  
2159 O  OE1 . GLN   A 295 ? 0.5455 0.4843 0.5291 0.0039  -0.0163 0.0141  451 GLN   A OE1 
2160 N  NE2 . GLN   A 295 ? 0.4837 0.4169 0.4776 0.0114  -0.0146 0.0219  451 GLN   A NE2 
2161 N  N   . ASP   A 296 ? 0.3465 0.2782 0.3222 -0.0084 -0.0155 -0.0025 452 ASP   A N   
2162 C  CA  . ASP   A 296 ? 0.3602 0.2899 0.3322 -0.0124 -0.0134 -0.0085 452 ASP   A CA  
2163 C  C   . ASP   A 296 ? 0.3975 0.3404 0.3655 -0.0188 -0.0113 -0.0085 452 ASP   A C   
2164 O  O   . ASP   A 296 ? 0.3584 0.3013 0.3244 -0.0223 -0.0085 -0.0129 452 ASP   A O   
2165 C  CB  . ASP   A 296 ? 0.3554 0.2764 0.3231 -0.0126 -0.0132 -0.0127 452 ASP   A CB  
2166 C  CG  . ASP   A 296 ? 0.3852 0.2939 0.3557 -0.0072 -0.0153 -0.0133 452 ASP   A CG  
2167 O  OD1 . ASP   A 296 ? 0.3769 0.2831 0.3526 -0.0042 -0.0167 -0.0119 452 ASP   A OD1 
2168 O  OD2 . ASP   A 296 ? 0.3905 0.2932 0.3575 -0.0067 -0.0157 -0.0149 452 ASP   A OD2 
2169 N  N   . SER   A 297 ? 0.3606 0.3154 0.3272 -0.0206 -0.0123 -0.0036 453 SER   A N   
2170 C  CA  . SER   A 297 ? 0.3886 0.3586 0.3507 -0.0278 -0.0110 -0.0030 453 SER   A CA  
2171 C  C   . SER   A 297 ? 0.4470 0.4244 0.4117 -0.0286 -0.0103 0.0000  453 SER   A C   
2172 O  O   . SER   A 297 ? 0.4362 0.4254 0.3960 -0.0354 -0.0087 -0.0009 453 SER   A O   
2173 C  CB  . SER   A 297 ? 0.3770 0.3610 0.3388 -0.0290 -0.0129 0.0035  453 SER   A CB  
2174 O  OG  . SER   A 297 ? 0.3873 0.3744 0.3568 -0.0225 -0.0146 0.0121  453 SER   A OG  
2175 N  N   . GLN   A 298 ? 0.3697 0.3408 0.3416 -0.0227 -0.0113 0.0035  454 GLN   A N   
2176 C  CA  . GLN   A 298 ? 0.3700 0.3474 0.3447 -0.0237 -0.0103 0.0063  454 GLN   A CA  
2177 C  C   . GLN   A 298 ? 0.3702 0.3405 0.3437 -0.0255 -0.0074 -0.0012 454 GLN   A C   
2178 O  O   . GLN   A 298 ? 0.4237 0.3987 0.3996 -0.0266 -0.0059 0.0003  454 GLN   A O   
2179 C  CB  . GLN   A 298 ? 0.3673 0.3409 0.3505 -0.0174 -0.0120 0.0134  454 GLN   A CB  
2180 C  CG  . GLN   A 298 ? 0.4263 0.4079 0.4122 -0.0148 -0.0137 0.0222  454 GLN   A CG  
2181 C  CD  . GLN   A 298 ? 0.4975 0.4706 0.4916 -0.0081 -0.0143 0.0277  454 GLN   A CD  
2182 O  OE1 . GLN   A 298 ? 0.4415 0.4003 0.4372 -0.0043 -0.0148 0.0240  454 GLN   A OE1 
2183 N  NE2 . GLN   A 298 ? 0.4148 0.3966 0.4137 -0.0072 -0.0139 0.0368  454 GLN   A NE2 
2184 N  N   . TRP   A 299 ? 0.3655 0.3249 0.3361 -0.0256 -0.0060 -0.0086 455 TRP   A N   
2185 C  CA  . TRP   A 299 ? 0.3621 0.3136 0.3334 -0.0258 -0.0026 -0.0152 455 TRP   A CA  
2186 C  C   . TRP   A 299 ? 0.4385 0.3874 0.4021 -0.0311 0.0014  -0.0230 455 TRP   A C   
2187 O  O   . TRP   A 299 ? 0.4124 0.3501 0.3772 -0.0295 0.0045  -0.0287 455 TRP   A O   
2188 C  CB  . TRP   A 299 ? 0.3930 0.3310 0.3709 -0.0191 -0.0044 -0.0158 455 TRP   A CB  
2189 C  CG  . TRP   A 299 ? 0.3366 0.2750 0.3216 -0.0151 -0.0074 -0.0099 455 TRP   A CG  
2190 C  CD1 . TRP   A 299 ? 0.3677 0.3047 0.3549 -0.0119 -0.0109 -0.0049 455 TRP   A CD1 
2191 C  CD2 . TRP   A 299 ? 0.3420 0.2818 0.3333 -0.0142 -0.0065 -0.0087 455 TRP   A CD2 
2192 N  NE1 . TRP   A 299 ? 0.3536 0.2893 0.3475 -0.0094 -0.0121 -0.0010 455 TRP   A NE1 
2193 C  CE2 . TRP   A 299 ? 0.3371 0.2750 0.3338 -0.0110 -0.0099 -0.0031 455 TRP   A CE2 
2194 C  CE3 . TRP   A 299 ? 0.3383 0.2804 0.3314 -0.0159 -0.0027 -0.0120 455 TRP   A CE3 
2195 C  CZ2 . TRP   A 299 ? 0.3636 0.3023 0.3672 -0.0102 -0.0100 -0.0005 455 TRP   A CZ2 
2196 C  CZ3 . TRP   A 299 ? 0.3678 0.3119 0.3684 -0.0145 -0.0030 -0.0091 455 TRP   A CZ3 
2197 C  CH2 . TRP   A 299 ? 0.3383 0.2810 0.3439 -0.0121 -0.0068 -0.0032 455 TRP   A CH2 
2198 N  N   . ASP   A 300 ? 0.4338 0.3928 0.3900 -0.0375 0.0016  -0.0231 456 ASP   A N   
2199 C  CA  . ASP   A 300 ? 0.3847 0.3412 0.3324 -0.0443 0.0058  -0.0311 456 ASP   A CA  
2200 C  C   . ASP   A 300 ? 0.4650 0.4168 0.4114 -0.0466 0.0120  -0.0383 456 ASP   A C   
2201 O  O   . ASP   A 300 ? 0.4487 0.4090 0.3963 -0.0478 0.0133  -0.0368 456 ASP   A O   
2202 C  CB  . ASP   A 300 ? 0.4815 0.4547 0.4216 -0.0526 0.0047  -0.0293 456 ASP   A CB  
2203 C  CG  . ASP   A 300 ? 0.6562 0.6258 0.5869 -0.0606 0.0082  -0.0374 456 ASP   A CG  
2204 O  OD1 . ASP   A 300 ? 0.6242 0.5834 0.5514 -0.0635 0.0141  -0.0463 456 ASP   A OD1 
2205 O  OD2 . ASP   A 300 ? 0.7402 0.7173 0.6678 -0.0641 0.0054  -0.0350 456 ASP   A OD2 
2206 N  N   . ARG   A 301 ? 0.4853 0.4228 0.4300 -0.0467 0.0164  -0.0458 457 ARG   A N   
2207 C  CA  . ARG   A 301 ? 0.5642 0.4944 0.5092 -0.0471 0.0236  -0.0528 457 ARG   A CA  
2208 C  C   . ARG   A 301 ? 0.5138 0.4555 0.4498 -0.0568 0.0283  -0.0577 457 ARG   A C   
2209 O  O   . ARG   A 301 ? 0.5904 0.5330 0.5276 -0.0570 0.0333  -0.0609 457 ARG   A O   
2210 C  CB  . ARG   A 301 ? 0.6739 0.5863 0.6185 -0.0456 0.0280  -0.0591 457 ARG   A CB  
2211 C  CG  . ARG   A 301 ? 0.6006 0.5014 0.5494 -0.0427 0.0360  -0.0653 457 ARG   A CG  
2212 C  CD  . ARG   A 301 ? 0.7912 0.6942 0.7515 -0.0346 0.0347  -0.0605 457 ARG   A CD  
2213 N  NE  . ARG   A 301 ? 0.8297 0.7217 0.7961 -0.0302 0.0422  -0.0651 457 ARG   A NE  
2214 C  CZ  . ARG   A 301 ? 0.6219 0.5153 0.5871 -0.0330 0.0503  -0.0711 457 ARG   A CZ  
2215 N  NH1 . ARG   A 301 ? 0.8058 0.7114 0.7622 -0.0413 0.0520  -0.0739 457 ARG   A NH1 
2216 N  NH2 . ARG   A 301 ? 0.7034 0.5862 0.6764 -0.0272 0.0572  -0.0742 457 ARG   A NH2 
2217 N  N   . LYS   A 302 ? 0.5100 0.4620 0.4368 -0.0652 0.0266  -0.0580 458 LYS   A N   
2218 C  CA  . LYS   A 302 ? 0.5856 0.5517 0.5022 -0.0759 0.0299  -0.0619 458 LYS   A CA  
2219 C  C   . LYS   A 302 ? 0.6245 0.6071 0.5440 -0.0751 0.0272  -0.0544 458 LYS   A C   
2220 O  O   . LYS   A 302 ? 0.5566 0.5507 0.4684 -0.0831 0.0308  -0.0577 458 LYS   A O   
2221 C  CB  . LYS   A 302 ? 0.5297 0.5054 0.4371 -0.0849 0.0273  -0.0622 458 LYS   A CB  
2222 C  CG  . LYS   A 302 ? 0.5992 0.5954 0.5083 -0.0850 0.0193  -0.0506 458 LYS   A CG  
2223 C  CD  . LYS   A 302 ? 0.6642 0.6713 0.5656 -0.0937 0.0167  -0.0504 458 LYS   A CD  
2224 C  CE  . LYS   A 302 ? 0.7162 0.7489 0.6181 -0.0961 0.0105  -0.0392 458 LYS   A CE  
2225 N  NZ  . LYS   A 302 ? 0.6930 0.7284 0.6031 -0.0888 0.0041  -0.0293 458 LYS   A NZ  
2226 N  N   . ASP   A 303 ? 0.4464 0.4298 0.3765 -0.0660 0.0214  -0.0448 459 ASP   A N   
2227 C  CA  . ASP   A 303 ? 0.4776 0.4745 0.4121 -0.0643 0.0185  -0.0363 459 ASP   A CA  
2228 C  C   . ASP   A 303 ? 0.4550 0.4441 0.3987 -0.0575 0.0209  -0.0362 459 ASP   A C   
2229 O  O   . ASP   A 303 ? 0.4106 0.4058 0.3612 -0.0535 0.0174  -0.0278 459 ASP   A O   
2230 C  CB  . ASP   A 303 ? 0.4191 0.4226 0.3589 -0.0598 0.0109  -0.0252 459 ASP   A CB  
2231 C  CG  . ASP   A 303 ? 0.5788 0.5964 0.5108 -0.0670 0.0083  -0.0229 459 ASP   A CG  
2232 O  OD1 . ASP   A 303 ? 0.5675 0.5886 0.5040 -0.0631 0.0031  -0.0151 459 ASP   A OD1 
2233 O  OD2 . ASP   A 303 ? 0.5654 0.5918 0.4870 -0.0770 0.0117  -0.0288 459 ASP   A OD2 
2234 N  N   . LEU   A 304 ? 0.4486 0.4240 0.3932 -0.0560 0.0269  -0.0449 460 LEU   A N   
2235 C  CA  . LEU   A 304 ? 0.4570 0.4261 0.4114 -0.0493 0.0295  -0.0449 460 LEU   A CA  
2236 C  C   . LEU   A 304 ? 0.4071 0.3903 0.3626 -0.0517 0.0306  -0.0409 460 LEU   A C   
2237 O  O   . LEU   A 304 ? 0.3748 0.3583 0.3403 -0.0460 0.0284  -0.0351 460 LEU   A O   
2238 C  CB  . LEU   A 304 ? 0.5052 0.4612 0.4589 -0.0492 0.0378  -0.0553 460 LEU   A CB  
2239 C  CG  . LEU   A 304 ? 0.4175 0.3694 0.3820 -0.0426 0.0416  -0.0554 460 LEU   A CG  
2240 C  CD1 . LEU   A 304 ? 0.4230 0.3682 0.3998 -0.0332 0.0350  -0.0483 460 LEU   A CD1 
2241 C  CD2 . LEU   A 304 ? 0.5330 0.4738 0.4964 -0.0429 0.0518  -0.0657 460 LEU   A CD2 
2242 N  N   . GLY   A 305 ? 0.4007 0.3960 0.3453 -0.0609 0.0341  -0.0441 461 GLY   A N   
2243 C  CA  . GLY   A 305 ? 0.3824 0.3920 0.3265 -0.0640 0.0359  -0.0405 461 GLY   A CA  
2244 C  C   . GLY   A 305 ? 0.3741 0.3931 0.3248 -0.0606 0.0285  -0.0275 461 GLY   A C   
2245 O  O   . GLY   A 305 ? 0.3686 0.3890 0.3279 -0.0566 0.0284  -0.0227 461 GLY   A O   
2246 N  N   . LEU   A 306 ? 0.3946 0.4196 0.3423 -0.0619 0.0225  -0.0215 462 LEU   A N   
2247 C  CA  . LEU   A 306 ? 0.4024 0.4353 0.3569 -0.0582 0.0164  -0.0087 462 LEU   A CA  
2248 C  C   . LEU   A 306 ? 0.3743 0.3924 0.3409 -0.0485 0.0130  -0.0055 462 LEU   A C   
2249 O  O   . LEU   A 306 ? 0.3739 0.3942 0.3482 -0.0450 0.0105  0.0029  462 LEU   A O   
2250 C  CB  . LEU   A 306 ? 0.4272 0.4721 0.3763 -0.0617 0.0117  -0.0024 462 LEU   A CB  
2251 C  CG  . LEU   A 306 ? 0.6186 0.6854 0.5581 -0.0712 0.0127  0.0006  462 LEU   A CG  
2252 C  CD1 . LEU   A 306 ? 0.7076 0.7885 0.6484 -0.0709 0.0065  0.0131  462 LEU   A CD1 
2253 C  CD2 . LEU   A 306 ? 0.5015 0.5758 0.4418 -0.0731 0.0164  0.0026  462 LEU   A CD2 
2254 N  N   . CYS   A 307 ? 0.3758 0.3789 0.3437 -0.0449 0.0129  -0.0119 463 CYS   A N   
2255 C  CA  . CYS   A 307 ? 0.3897 0.3798 0.3677 -0.0367 0.0096  -0.0096 463 CYS   A CA  
2256 C  C   . CYS   A 307 ? 0.3720 0.3596 0.3585 -0.0338 0.0118  -0.0095 463 CYS   A C   
2257 O  O   . CYS   A 307 ? 0.3719 0.3588 0.3663 -0.0303 0.0087  -0.0029 463 CYS   A O   
2258 C  CB  . CYS   A 307 ? 0.3576 0.3339 0.3344 -0.0341 0.0095  -0.0162 463 CYS   A CB  
2259 S  SG  . CYS   A 307 ? 0.3826 0.3610 0.3523 -0.0361 0.0056  -0.0144 463 CYS   A SG  
2260 N  N   . PHE   A 308 ? 0.3440 0.3307 0.3291 -0.0357 0.0179  -0.0170 464 PHE   A N   
2261 C  CA  . PHE   A 308 ? 0.3409 0.3282 0.3347 -0.0334 0.0207  -0.0165 464 PHE   A CA  
2262 C  C   . PHE   A 308 ? 0.3500 0.3507 0.3451 -0.0364 0.0202  -0.0088 464 PHE   A C   
2263 O  O   . PHE   A 308 ? 0.3391 0.3395 0.3436 -0.0335 0.0190  -0.0042 464 PHE   A O   
2264 C  CB  . PHE   A 308 ? 0.3496 0.3348 0.3415 -0.0348 0.0288  -0.0258 464 PHE   A CB  
2265 C  CG  . PHE   A 308 ? 0.3565 0.3442 0.3582 -0.0322 0.0323  -0.0253 464 PHE   A CG  
2266 C  CD1 . PHE   A 308 ? 0.3502 0.3318 0.3643 -0.0257 0.0288  -0.0218 464 PHE   A CD1 
2267 C  CD2 . PHE   A 308 ? 0.3565 0.3540 0.3549 -0.0368 0.0393  -0.0283 464 PHE   A CD2 
2268 C  CE1 . PHE   A 308 ? 0.3446 0.3304 0.3686 -0.0238 0.0318  -0.0209 464 PHE   A CE1 
2269 C  CE2 . PHE   A 308 ? 0.3626 0.3636 0.3708 -0.0344 0.0431  -0.0275 464 PHE   A CE2 
2270 C  CZ  . PHE   A 308 ? 0.3503 0.3457 0.3721 -0.0277 0.0391  -0.0235 464 PHE   A CZ  
2271 N  N   . ASP   A 309 ? 0.3490 0.3621 0.3344 -0.0428 0.0214  -0.0073 465 ASP   A N   
2272 C  CA  . ASP   A 309 ? 0.3556 0.3822 0.3420 -0.0457 0.0207  0.0016  465 ASP   A CA  
2273 C  C   . ASP   A 309 ? 0.3347 0.3577 0.3293 -0.0409 0.0146  0.0117  465 ASP   A C   
2274 O  O   . ASP   A 309 ? 0.3417 0.3682 0.3431 -0.0404 0.0144  0.0183  465 ASP   A O   
2275 C  CB  . ASP   A 309 ? 0.3425 0.3847 0.3166 -0.0536 0.0217  0.0030  465 ASP   A CB  
2276 C  CG  . ASP   A 309 ? 0.3455 0.4038 0.3197 -0.0572 0.0218  0.0128  465 ASP   A CG  
2277 O  OD1 . ASP   A 309 ? 0.3704 0.4322 0.3472 -0.0585 0.0264  0.0115  465 ASP   A OD1 
2278 O  OD2 . ASP   A 309 ? 0.3456 0.4145 0.3169 -0.0590 0.0177  0.0222  465 ASP   A OD2 
2279 N  N   . ASN   A 310 ? 0.3598 0.3754 0.3540 -0.0378 0.0101  0.0127  466 ASN   A N   
2280 C  CA  . ASN   A 310 ? 0.3503 0.3611 0.3516 -0.0332 0.0053  0.0213  466 ASN   A CA  
2281 C  C   . ASN   A 310 ? 0.3662 0.3637 0.3773 -0.0284 0.0042  0.0195  466 ASN   A C   
2282 O  O   . ASN   A 310 ? 0.3522 0.3467 0.3702 -0.0264 0.0020  0.0263  466 ASN   A O   
2283 C  CB  . ASN   A 310 ? 0.3446 0.3532 0.3419 -0.0316 0.0016  0.0230  466 ASN   A CB  
2284 C  CG  . ASN   A 310 ? 0.4410 0.4666 0.4301 -0.0369 0.0017  0.0277  466 ASN   A CG  
2285 O  OD1 . ASN   A 310 ? 0.3577 0.3966 0.3451 -0.0410 0.0033  0.0327  466 ASN   A OD1 
2286 N  ND2 . ASN   A 310 ? 0.3871 0.4134 0.3712 -0.0372 -0.0004 0.0265  466 ASN   A ND2 
2287 N  N   . CYS   A 311 ? 0.3468 0.3370 0.3588 -0.0270 0.0059  0.0109  467 CYS   A N   
2288 C  CA  . CYS   A 311 ? 0.3526 0.3344 0.3744 -0.0234 0.0048  0.0098  467 CYS   A CA  
2289 C  C   . CYS   A 311 ? 0.3562 0.3459 0.3840 -0.0256 0.0076  0.0129  467 CYS   A C   
2290 O  O   . CYS   A 311 ? 0.3416 0.3285 0.3774 -0.0247 0.0055  0.0176  467 CYS   A O   
2291 C  CB  . CYS   A 311 ? 0.3413 0.3155 0.3637 -0.0208 0.0062  0.0014  467 CYS   A CB  
2292 S  SG  . CYS   A 311 ? 0.3519 0.3154 0.3685 -0.0180 0.0025  -0.0018 467 CYS   A SG  
2293 N  N   . VAL   A 312 ? 0.3282 0.3282 0.3516 -0.0294 0.0129  0.0104  468 VAL   A N   
2294 C  CA  . VAL   A 312 ? 0.3247 0.3339 0.3530 -0.0321 0.0164  0.0135  468 VAL   A CA  
2295 C  C   . VAL   A 312 ? 0.3155 0.3291 0.3461 -0.0337 0.0137  0.0241  468 VAL   A C   
2296 O  O   . VAL   A 312 ? 0.3084 0.3221 0.3477 -0.0338 0.0135  0.0285  468 VAL   A O   
2297 C  CB  . VAL   A 312 ? 0.3279 0.3479 0.3486 -0.0366 0.0230  0.0086  468 VAL   A CB  
2298 C  CG1 . VAL   A 312 ? 0.3331 0.3646 0.3577 -0.0399 0.0267  0.0131  468 VAL   A CG1 
2299 C  CG2 . VAL   A 312 ? 0.3349 0.3482 0.3559 -0.0342 0.0272  -0.0017 468 VAL   A CG2 
2300 N  N   . THR   A 313 ? 0.3497 0.3671 0.3731 -0.0350 0.0118  0.0287  469 THR   A N   
2301 C  CA  . THR   A 313 ? 0.3402 0.3620 0.3660 -0.0358 0.0099  0.0401  469 THR   A CA  
2302 C  C   . THR   A 313 ? 0.3270 0.3352 0.3619 -0.0317 0.0063  0.0436  469 THR   A C   
2303 O  O   . THR   A 313 ? 0.3243 0.3327 0.3655 -0.0327 0.0065  0.0509  469 THR   A O   
2304 C  CB  . THR   A 313 ? 0.3416 0.3711 0.3588 -0.0371 0.0083  0.0445  469 THR   A CB  
2305 O  OG1 . THR   A 313 ? 0.4392 0.4840 0.4473 -0.0430 0.0120  0.0423  469 THR   A OG1 
2306 C  CG2 . THR   A 313 ? 0.3264 0.3574 0.3479 -0.0356 0.0059  0.0573  469 THR   A CG2 
2307 N  N   . TYR   A 314 ? 0.3555 0.3513 0.3905 -0.0278 0.0033  0.0381  470 TYR   A N   
2308 C  CA  . TYR   A 314 ? 0.3402 0.3227 0.3822 -0.0248 0.0001  0.0400  470 TYR   A CA  
2309 C  C   . TYR   A 314 ? 0.3404 0.3209 0.3911 -0.0263 0.0008  0.0386  470 TYR   A C   
2310 O  O   . TYR   A 314 ? 0.3363 0.3123 0.3932 -0.0273 0.0002  0.0441  470 TYR   A O   
2311 C  CB  . TYR   A 314 ? 0.3431 0.3143 0.3823 -0.0210 -0.0030 0.0340  470 TYR   A CB  
2312 C  CG  . TYR   A 314 ? 0.4073 0.3650 0.4520 -0.0188 -0.0057 0.0357  470 TYR   A CG  
2313 C  CD1 . TYR   A 314 ? 0.4723 0.4252 0.5173 -0.0170 -0.0062 0.0426  470 TYR   A CD1 
2314 C  CD2 . TYR   A 314 ? 0.3295 0.2799 0.3793 -0.0188 -0.0075 0.0306  470 TYR   A CD2 
2315 C  CE1 . TYR   A 314 ? 0.5195 0.4584 0.5689 -0.0156 -0.0075 0.0430  470 TYR   A CE1 
2316 C  CE2 . TYR   A 314 ? 0.4519 0.3900 0.5053 -0.0184 -0.0097 0.0311  470 TYR   A CE2 
2317 C  CZ  . TYR   A 314 ? 0.5162 0.4476 0.5689 -0.0169 -0.0093 0.0367  470 TYR   A CZ  
2318 O  OH  . TYR   A 314 ? 0.5610 0.4787 0.6165 -0.0168 -0.0104 0.0362  470 TYR   A OH  
2319 N  N   . PHE   A 315 ? 0.3436 0.3278 0.3953 -0.0266 0.0025  0.0316  471 PHE   A N   
2320 C  CA  . PHE   A 315 ? 0.3576 0.3431 0.4188 -0.0280 0.0032  0.0308  471 PHE   A CA  
2321 C  C   . PHE   A 315 ? 0.3503 0.3446 0.4153 -0.0322 0.0060  0.0382  471 PHE   A C   
2322 O  O   . PHE   A 315 ? 0.3386 0.3299 0.4117 -0.0341 0.0051  0.0416  471 PHE   A O   
2323 C  CB  . PHE   A 315 ? 0.3426 0.3325 0.4048 -0.0267 0.0058  0.0232  471 PHE   A CB  
2324 C  CG  . PHE   A 315 ? 0.3731 0.3663 0.4464 -0.0274 0.0063  0.0226  471 PHE   A CG  
2325 C  CD1 . PHE   A 315 ? 0.3624 0.3480 0.4422 -0.0261 0.0016  0.0214  471 PHE   A CD1 
2326 C  CD2 . PHE   A 315 ? 0.3481 0.3533 0.4253 -0.0294 0.0116  0.0227  471 PHE   A CD2 
2327 C  CE1 . PHE   A 315 ? 0.3864 0.3776 0.4770 -0.0272 0.0016  0.0214  471 PHE   A CE1 
2328 C  CE2 . PHE   A 315 ? 0.3464 0.3567 0.4350 -0.0298 0.0123  0.0226  471 PHE   A CE2 
2329 C  CZ  . PHE   A 315 ? 0.3314 0.3353 0.4272 -0.0288 0.0070  0.0223  471 PHE   A CZ  
2330 N  N   . LEU   A 316 ? 0.3052 0.3107 0.3640 -0.0344 0.0095  0.0411  472 LEU   A N   
2331 C  CA  . LEU   A 316 ? 0.2989 0.3141 0.3602 -0.0385 0.0124  0.0492  472 LEU   A CA  
2332 C  C   . LEU   A 316 ? 0.2935 0.3009 0.3583 -0.0386 0.0099  0.0585  472 LEU   A C   
2333 O  O   . LEU   A 316 ? 0.2923 0.3008 0.3640 -0.0415 0.0111  0.0643  472 LEU   A O   
2334 C  CB  . LEU   A 316 ? 0.3056 0.3348 0.3571 -0.0413 0.0159  0.0507  472 LEU   A CB  
2335 C  CG  . LEU   A 316 ? 0.3107 0.3490 0.3588 -0.0428 0.0209  0.0421  472 LEU   A CG  
2336 C  CD1 . LEU   A 316 ? 0.3180 0.3683 0.3534 -0.0465 0.0237  0.0424  472 LEU   A CD1 
2337 C  CD2 . LEU   A 316 ? 0.3061 0.3516 0.3626 -0.0455 0.0247  0.0441  472 LEU   A CD2 
2338 N  N   . GLN   A 317 ? 0.3136 0.3135 0.3739 -0.0353 0.0071  0.0603  473 GLN   A N   
2339 C  CA  . GLN   A 317 ? 0.3120 0.3028 0.3764 -0.0343 0.0059  0.0689  473 GLN   A CA  
2340 C  C   . GLN   A 317 ? 0.3468 0.3238 0.4194 -0.0349 0.0044  0.0662  473 GLN   A C   
2341 O  O   . GLN   A 317 ? 0.3723 0.3437 0.4508 -0.0369 0.0054  0.0730  473 GLN   A O   
2342 C  CB  . GLN   A 317 ? 0.3195 0.3051 0.3785 -0.0299 0.0037  0.0704  473 GLN   A CB  
2343 C  CG  . GLN   A 317 ? 0.3207 0.2964 0.3846 -0.0279 0.0039  0.0801  473 GLN   A CG  
2344 C  CD  . GLN   A 317 ? 0.4264 0.3985 0.4862 -0.0228 0.0024  0.0825  473 GLN   A CD  
2345 O  OE1 . GLN   A 317 ? 0.3773 0.3599 0.4350 -0.0218 0.0031  0.0916  473 GLN   A OE1 
2346 N  NE2 . GLN   A 317 ? 0.3528 0.3125 0.4115 -0.0198 0.0002  0.0744  473 GLN   A NE2 
2347 N  N   . CYS   A 318 ? 0.3032 0.2750 0.3762 -0.0336 0.0020  0.0564  474 CYS   A N   
2348 C  CA  . CYS   A 318 ? 0.3147 0.2767 0.3950 -0.0356 0.0001  0.0534  474 CYS   A CA  
2349 C  C   . CYS   A 318 ? 0.3207 0.2912 0.4088 -0.0408 0.0025  0.0565  474 CYS   A C   
2350 O  O   . CYS   A 318 ? 0.3049 0.2684 0.3993 -0.0444 0.0023  0.0597  474 CYS   A O   
2351 C  CB  . CYS   A 318 ? 0.2951 0.2539 0.3744 -0.0333 -0.0031 0.0437  474 CYS   A CB  
2352 S  SG  . CYS   A 318 ? 0.3687 0.3159 0.4393 -0.0280 -0.0059 0.0403  474 CYS   A SG  
2353 N  N   . LEU   A 319 ? 0.3029 0.2885 0.3906 -0.0416 0.0053  0.0554  475 LEU   A N   
2354 C  CA  . LEU   A 319 ? 0.3079 0.3038 0.4031 -0.0464 0.0083  0.0584  475 LEU   A CA  
2355 C  C   . LEU   A 319 ? 0.3763 0.3723 0.4734 -0.0500 0.0106  0.0692  475 LEU   A C   
2356 O  O   . LEU   A 319 ? 0.3583 0.3524 0.4635 -0.0546 0.0112  0.0725  475 LEU   A O   
2357 C  CB  . LEU   A 319 ? 0.3090 0.3206 0.4018 -0.0461 0.0122  0.0551  475 LEU   A CB  
2358 C  CG  . LEU   A 319 ? 0.3716 0.3849 0.4663 -0.0430 0.0117  0.0456  475 LEU   A CG  
2359 C  CD1 . LEU   A 319 ? 0.3102 0.3357 0.4000 -0.0419 0.0170  0.0415  475 LEU   A CD1 
2360 C  CD2 . LEU   A 319 ? 0.3030 0.3179 0.4098 -0.0452 0.0104  0.0445  475 LEU   A CD2 
2361 N  N   . ARG   A 320 ? 0.3258 0.3246 0.4158 -0.0483 0.0119  0.0754  476 ARG   A N   
2362 C  CA  . ARG   A 320 ? 0.3214 0.3225 0.4137 -0.0513 0.0146  0.0872  476 ARG   A CA  
2363 C  C   . ARG   A 320 ? 0.3248 0.3077 0.4226 -0.0515 0.0133  0.0915  476 ARG   A C   
2364 O  O   . ARG   A 320 ? 0.3255 0.3068 0.4297 -0.0558 0.0157  0.0988  476 ARG   A O   
2365 C  CB  . ARG   A 320 ? 0.4060 0.4166 0.4898 -0.0494 0.0158  0.0941  476 ARG   A CB  
2366 C  CG  . ARG   A 320 ? 0.3249 0.3544 0.4016 -0.0512 0.0184  0.0909  476 ARG   A CG  
2367 C  CD  . ARG   A 320 ? 0.3296 0.3703 0.3982 -0.0513 0.0192  0.0998  476 ARG   A CD  
2368 N  NE  . ARG   A 320 ? 0.3338 0.3882 0.3926 -0.0525 0.0207  0.0928  476 ARG   A NE  
2369 C  CZ  . ARG   A 320 ? 0.3384 0.3899 0.3905 -0.0494 0.0185  0.0852  476 ARG   A CZ  
2370 N  NH1 . ARG   A 320 ? 0.3308 0.3679 0.3846 -0.0446 0.0146  0.0842  476 ARG   A NH1 
2371 N  NH2 . ARG   A 320 ? 0.3365 0.3994 0.3796 -0.0516 0.0209  0.0782  476 ARG   A NH2 
2372 N  N   . THR   A 321 ? 0.3411 0.3100 0.4362 -0.0471 0.0103  0.0871  477 THR   A N   
2373 C  CA  . THR   A 321 ? 0.3600 0.3095 0.4594 -0.0472 0.0101  0.0893  477 THR   A CA  
2374 C  C   . THR   A 321 ? 0.4516 0.3924 0.5566 -0.0517 0.0081  0.0813  477 THR   A C   
2375 O  O   . THR   A 321 ? 0.4001 0.3243 0.5083 -0.0538 0.0085  0.0819  477 THR   A O   
2376 C  CB  . THR   A 321 ? 0.3293 0.2681 0.4231 -0.0407 0.0084  0.0878  477 THR   A CB  
2377 O  OG1 . THR   A 321 ? 0.3375 0.2769 0.4266 -0.0386 0.0048  0.0766  477 THR   A OG1 
2378 C  CG2 . THR   A 321 ? 0.3750 0.3239 0.4641 -0.0367 0.0098  0.0967  477 THR   A CG2 
2379 N  N   . GLU   A 322 ? 0.3795 0.3314 0.4858 -0.0535 0.0064  0.0741  478 GLU   A N   
2380 C  CA  . GLU   A 322 ? 0.4319 0.3802 0.5441 -0.0580 0.0037  0.0671  478 GLU   A CA  
2381 C  C   . GLU   A 322 ? 0.4525 0.3840 0.5613 -0.0563 0.0002  0.0603  478 GLU   A C   
2382 O  O   . GLU   A 322 ? 0.4195 0.3412 0.5321 -0.0615 -0.0013 0.0572  478 GLU   A O   
2383 C  CB  . GLU   A 322 ? 0.4610 0.4084 0.5818 -0.0657 0.0061  0.0724  478 GLU   A CB  
2384 C  CG  . GLU   A 322 ? 0.4070 0.3722 0.5313 -0.0681 0.0099  0.0791  478 GLU   A CG  
2385 C  CD  . GLU   A 322 ? 0.4542 0.4199 0.5878 -0.0764 0.0120  0.0838  478 GLU   A CD  
2386 O  OE1 . GLU   A 322 ? 0.5101 0.4816 0.6503 -0.0810 0.0101  0.0786  478 GLU   A OE1 
2387 O  OE2 . GLU   A 322 ? 0.6216 0.5825 0.7565 -0.0786 0.0156  0.0933  478 GLU   A OE2 
2388 N  N   . LYS   A 323 ? 0.3795 0.3084 0.4805 -0.0497 -0.0011 0.0575  479 LYS   A N   
2389 C  CA  . LYS   A 323 ? 0.4134 0.3273 0.5100 -0.0473 -0.0039 0.0515  479 LYS   A CA  
2390 C  C   . LYS   A 323 ? 0.3915 0.3122 0.4828 -0.0427 -0.0071 0.0444  479 LYS   A C   
2391 O  O   . LYS   A 323 ? 0.3781 0.3064 0.4646 -0.0381 -0.0061 0.0460  479 LYS   A O   
2392 C  CB  . LYS   A 323 ? 0.4769 0.3782 0.5697 -0.0431 -0.0012 0.0569  479 LYS   A CB  
2393 C  CG  . LYS   A 323 ? 0.6161 0.4982 0.7065 -0.0429 -0.0020 0.0517  479 LYS   A CG  
2394 C  CD  . LYS   A 323 ? 0.6480 0.5234 0.7320 -0.0354 -0.0013 0.0523  479 LYS   A CD  
2395 C  CE  . LYS   A 323 ? 0.5558 0.4167 0.6353 -0.0354 -0.0035 0.0429  479 LYS   A CE  
2396 N  NZ  . LYS   A 323 ? 0.6842 0.5462 0.7565 -0.0286 -0.0050 0.0400  479 LYS   A NZ  
2397 N  N   . LEU   A 324 ? 0.3651 0.2839 0.4573 -0.0446 -0.0110 0.0371  480 LEU   A N   
2398 C  CA  . LEU   A 324 ? 0.3514 0.2740 0.4391 -0.0402 -0.0142 0.0307  480 LEU   A CA  
2399 C  C   . LEU   A 324 ? 0.4137 0.3257 0.4999 -0.0425 -0.0182 0.0245  480 LEU   A C   
2400 O  O   . LEU   A 324 ? 0.3731 0.2903 0.4645 -0.0470 -0.0211 0.0217  480 LEU   A O   
2401 C  CB  . LEU   A 324 ? 0.3348 0.2738 0.4271 -0.0399 -0.0143 0.0293  480 LEU   A CB  
2402 C  CG  . LEU   A 324 ? 0.3382 0.2794 0.4263 -0.0349 -0.0168 0.0235  480 LEU   A CG  
2403 C  CD1 . LEU   A 324 ? 0.3538 0.2919 0.4329 -0.0297 -0.0151 0.0237  480 LEU   A CD1 
2404 C  CD2 . LEU   A 324 ? 0.3439 0.2997 0.4384 -0.0341 -0.0162 0.0220  480 LEU   A CD2 
2405 N  N   . GLU   A 325 ? 0.4052 0.3032 0.4845 -0.0400 -0.0182 0.0229  481 GLU   A N   
2406 C  CA  . GLU   A 325 ? 0.4997 0.3873 0.5759 -0.0428 -0.0215 0.0164  481 GLU   A CA  
2407 C  C   . GLU   A 325 ? 0.3551 0.2511 0.4293 -0.0410 -0.0262 0.0112  481 GLU   A C   
2408 O  O   . GLU   A 325 ? 0.3727 0.2744 0.4438 -0.0350 -0.0262 0.0112  481 GLU   A O   
2409 C  CB  . GLU   A 325 ? 0.4953 0.3667 0.5641 -0.0396 -0.0196 0.0152  481 GLU   A CB  
2410 C  CG  . GLU   A 325 ? 0.4886 0.3488 0.5597 -0.0407 -0.0146 0.0205  481 GLU   A CG  
2411 C  CD  . GLU   A 325 ? 0.5913 0.4363 0.6562 -0.0363 -0.0121 0.0192  481 GLU   A CD  
2412 O  OE1 . GLU   A 325 ? 0.5869 0.4332 0.6455 -0.0317 -0.0142 0.0154  481 GLU   A OE1 
2413 O  OE2 . GLU   A 325 ? 0.8409 0.6721 0.9076 -0.0376 -0.0076 0.0219  481 GLU   A OE2 
2414 N  N   . ASN   A 326 ? 0.4117 0.3086 0.4880 -0.0466 -0.0303 0.0071  482 ASN   A N   
2415 C  CA  . ASN   A 326 ? 0.3532 0.2560 0.4269 -0.0445 -0.0351 0.0030  482 ASN   A CA  
2416 C  C   . ASN   A 326 ? 0.3452 0.2371 0.4084 -0.0394 -0.0349 -0.0001 482 ASN   A C   
2417 O  O   . ASN   A 326 ? 0.3537 0.2315 0.4116 -0.0407 -0.0331 -0.0018 482 ASN   A O   
2418 C  CB  . ASN   A 326 ? 0.3806 0.2855 0.4565 -0.0524 -0.0399 -0.0006 482 ASN   A CB  
2419 C  CG  . ASN   A 326 ? 0.4096 0.3233 0.4841 -0.0501 -0.0452 -0.0030 482 ASN   A CG  
2420 O  OD1 . ASN   A 326 ? 0.3770 0.2836 0.4426 -0.0464 -0.0463 -0.0060 482 ASN   A OD1 
2421 N  ND2 . ASN   A 326 ? 0.3904 0.3204 0.4744 -0.0518 -0.0481 -0.0009 482 ASN   A ND2 
2422 N  N   . TYR   A 327 ? 0.3529 0.2511 0.4136 -0.0336 -0.0363 -0.0006 483 TYR   A N   
2423 C  CA  . TYR   A 327 ? 0.3790 0.2688 0.4303 -0.0285 -0.0356 -0.0027 483 TYR   A CA  
2424 C  C   . TYR   A 327 ? 0.3820 0.2623 0.4263 -0.0313 -0.0386 -0.0079 483 TYR   A C   
2425 O  O   . TYR   A 327 ? 0.3835 0.2534 0.4201 -0.0286 -0.0369 -0.0098 483 TYR   A O   
2426 C  CB  . TYR   A 327 ? 0.3696 0.2680 0.4201 -0.0228 -0.0362 -0.0024 483 TYR   A CB  
2427 C  CG  . TYR   A 327 ? 0.3495 0.2414 0.3916 -0.0177 -0.0342 -0.0030 483 TYR   A CG  
2428 C  CD1 . TYR   A 327 ? 0.3575 0.2474 0.3984 -0.0155 -0.0300 0.0003  483 TYR   A CD1 
2429 C  CD2 . TYR   A 327 ? 0.3904 0.2797 0.4262 -0.0153 -0.0368 -0.0062 483 TYR   A CD2 
2430 C  CE1 . TYR   A 327 ? 0.3325 0.2188 0.3667 -0.0114 -0.0285 0.0002  483 TYR   A CE1 
2431 C  CE2 . TYR   A 327 ? 0.4062 0.2907 0.4350 -0.0112 -0.0350 -0.0067 483 TYR   A CE2 
2432 C  CZ  . TYR   A 327 ? 0.4033 0.2868 0.4315 -0.0093 -0.0308 -0.0035 483 TYR   A CZ  
2433 O  OH  . TYR   A 327 ? 0.3751 0.2558 0.3971 -0.0058 -0.0294 -0.0036 483 TYR   A OH  
2434 N  N   . PHE   A 328 ? 0.3795 0.2646 0.4263 -0.0371 -0.0430 -0.0101 484 PHE   A N   
2435 C  CA  . PHE   A 328 ? 0.3987 0.2772 0.4379 -0.0412 -0.0464 -0.0156 484 PHE   A CA  
2436 C  C   . PHE   A 328 ? 0.4106 0.2794 0.4492 -0.0495 -0.0454 -0.0187 484 PHE   A C   
2437 O  O   . PHE   A 328 ? 0.4539 0.3117 0.4837 -0.0528 -0.0456 -0.0242 484 PHE   A O   
2438 C  CB  . PHE   A 328 ? 0.3947 0.2869 0.4363 -0.0426 -0.0526 -0.0157 484 PHE   A CB  
2439 C  CG  . PHE   A 328 ? 0.3847 0.2836 0.4263 -0.0345 -0.0530 -0.0131 484 PHE   A CG  
2440 C  CD1 . PHE   A 328 ? 0.4134 0.3071 0.4456 -0.0312 -0.0542 -0.0154 484 PHE   A CD1 
2441 C  CD2 . PHE   A 328 ? 0.4022 0.3116 0.4528 -0.0304 -0.0513 -0.0088 484 PHE   A CD2 
2442 C  CE1 . PHE   A 328 ? 0.4410 0.3394 0.4732 -0.0243 -0.0540 -0.0131 484 PHE   A CE1 
2443 C  CE2 . PHE   A 328 ? 0.4688 0.3822 0.5191 -0.0234 -0.0506 -0.0072 484 PHE   A CE2 
2444 C  CZ  . PHE   A 328 ? 0.3817 0.2894 0.4230 -0.0205 -0.0520 -0.0092 484 PHE   A CZ  
2445 N  N   . ILE   A 329 ? 0.4152 0.2873 0.4625 -0.0534 -0.0437 -0.0155 485 ILE   A N   
2446 C  CA  . ILE   A 329 ? 0.4177 0.2807 0.4659 -0.0624 -0.0423 -0.0181 485 ILE   A CA  
2447 C  C   . ILE   A 329 ? 0.4661 0.3220 0.5193 -0.0602 -0.0359 -0.0130 485 ILE   A C   
2448 O  O   . ILE   A 329 ? 0.4035 0.2689 0.4659 -0.0622 -0.0354 -0.0082 485 ILE   A O   
2449 C  CB  . ILE   A 329 ? 0.4301 0.3071 0.4855 -0.0708 -0.0475 -0.0182 485 ILE   A CB  
2450 C  CG1 . ILE   A 329 ? 0.4764 0.3653 0.5287 -0.0712 -0.0544 -0.0205 485 ILE   A CG1 
2451 C  CG2 . ILE   A 329 ? 0.4133 0.2797 0.4681 -0.0818 -0.0461 -0.0221 485 ILE   A CG2 
2452 C  CD1 . ILE   A 329 ? 0.4373 0.3452 0.4994 -0.0772 -0.0598 -0.0181 485 ILE   A CD1 
2453 N  N   . PRO   A 330 ? 0.4789 0.3196 0.5268 -0.0558 -0.0307 -0.0129 486 PRO   A N   
2454 C  CA  . PRO   A 330 ? 0.4831 0.3210 0.5363 -0.0517 -0.0251 -0.0057 486 PRO   A CA  
2455 C  C   . PRO   A 330 ? 0.4806 0.3130 0.5405 -0.0590 -0.0221 -0.0034 486 PRO   A C   
2456 O  O   . PRO   A 330 ? 0.4754 0.3106 0.5414 -0.0566 -0.0186 0.0040  486 PRO   A O   
2457 C  CB  . PRO   A 330 ? 0.5908 0.4145 0.6373 -0.0453 -0.0206 -0.0061 486 PRO   A CB  
2458 C  CG  . PRO   A 330 ? 0.6312 0.4440 0.6689 -0.0496 -0.0222 -0.0152 486 PRO   A CG  
2459 C  CD  . PRO   A 330 ? 0.4423 0.2696 0.4797 -0.0540 -0.0296 -0.0187 486 PRO   A CD  
2460 N  N   . GLU   A 331 ? 0.4740 0.2995 0.5327 -0.0685 -0.0235 -0.0093 487 GLU   A N   
2461 C  CA  . GLU   A 331 ? 0.4500 0.2705 0.5155 -0.0765 -0.0207 -0.0071 487 GLU   A CA  
2462 C  C   . GLU   A 331 ? 0.4155 0.2560 0.4903 -0.0809 -0.0246 -0.0036 487 GLU   A C   
2463 O  O   . GLU   A 331 ? 0.4501 0.2896 0.5318 -0.0875 -0.0223 -0.0006 487 GLU   A O   
2464 C  CB  . GLU   A 331 ? 0.5014 0.3054 0.5614 -0.0863 -0.0198 -0.0155 487 GLU   A CB  
2465 C  CG  . GLU   A 331 ? 0.5104 0.2918 0.5624 -0.0823 -0.0137 -0.0189 487 GLU   A CG  
2466 C  CD  . GLU   A 331 ? 0.6515 0.4178 0.6954 -0.0923 -0.0132 -0.0297 487 GLU   A CD  
2467 O  OE1 . GLU   A 331 ? 0.7350 0.5067 0.7708 -0.0943 -0.0184 -0.0367 487 GLU   A OE1 
2468 O  OE2 . GLU   A 331 ? 0.6861 0.4351 0.7313 -0.0987 -0.0074 -0.0312 487 GLU   A OE2 
2469 N  N   . PHE   A 332 ? 0.4151 0.2736 0.4910 -0.0771 -0.0298 -0.0035 488 PHE   A N   
2470 C  CA  . PHE   A 332 ? 0.4340 0.3129 0.5199 -0.0797 -0.0328 0.0002  488 PHE   A CA  
2471 C  C   . PHE   A 332 ? 0.4041 0.2915 0.4946 -0.0716 -0.0292 0.0076  488 PHE   A C   
2472 O  O   . PHE   A 332 ? 0.3334 0.2258 0.4205 -0.0633 -0.0297 0.0081  488 PHE   A O   
2473 C  CB  . PHE   A 332 ? 0.3837 0.2770 0.4691 -0.0796 -0.0398 -0.0034 488 PHE   A CB  
2474 C  CG  . PHE   A 332 ? 0.4228 0.3367 0.5196 -0.0836 -0.0430 -0.0003 488 PHE   A CG  
2475 C  CD1 . PHE   A 332 ? 0.4970 0.4258 0.6014 -0.0770 -0.0416 0.0052  488 PHE   A CD1 
2476 C  CD2 . PHE   A 332 ? 0.4092 0.3280 0.5095 -0.0948 -0.0469 -0.0030 488 PHE   A CD2 
2477 C  CE1 . PHE   A 332 ? 0.4327 0.3810 0.5488 -0.0802 -0.0437 0.0083  488 PHE   A CE1 
2478 C  CE2 . PHE   A 332 ? 0.4848 0.4245 0.5970 -0.0986 -0.0499 0.0006  488 PHE   A CE2 
2479 C  CZ  . PHE   A 332 ? 0.5237 0.4782 0.6444 -0.0907 -0.0480 0.0065  488 PHE   A CZ  
2480 N  N   . ASN   A 333 ? 0.4122 0.3018 0.5101 -0.0751 -0.0255 0.0133  489 ASN   A N   
2481 C  CA  . ASN   A 333 ? 0.4845 0.3832 0.5862 -0.0692 -0.0218 0.0205  489 ASN   A CA  
2482 C  C   . ASN   A 333 ? 0.3763 0.2966 0.4863 -0.0696 -0.0238 0.0220  489 ASN   A C   
2483 O  O   . ASN   A 333 ? 0.4144 0.3424 0.5329 -0.0765 -0.0236 0.0243  489 ASN   A O   
2484 C  CB  . ASN   A 333 ? 0.4250 0.3150 0.5300 -0.0724 -0.0162 0.0269  489 ASN   A CB  
2485 C  CG  . ASN   A 333 ? 0.4087 0.3085 0.5157 -0.0666 -0.0123 0.0349  489 ASN   A CG  
2486 O  OD1 . ASN   A 333 ? 0.3926 0.3039 0.4975 -0.0604 -0.0134 0.0344  489 ASN   A OD1 
2487 N  ND2 . ASN   A 333 ? 0.3723 0.2673 0.4829 -0.0691 -0.0076 0.0421  489 ASN   A ND2 
2488 N  N   . LEU   A 334 ? 0.3670 0.2967 0.4750 -0.0620 -0.0248 0.0213  490 LEU   A N   
2489 C  CA  . LEU   A 334 ? 0.3718 0.3209 0.4879 -0.0606 -0.0253 0.0226  490 LEU   A CA  
2490 C  C   . LEU   A 334 ? 0.3601 0.3180 0.4826 -0.0620 -0.0202 0.0288  490 LEU   A C   
2491 O  O   . LEU   A 334 ? 0.3859 0.3592 0.5178 -0.0643 -0.0199 0.0305  490 LEU   A O   
2492 C  CB  . LEU   A 334 ? 0.3462 0.2997 0.4578 -0.0519 -0.0259 0.0203  490 LEU   A CB  
2493 C  CG  . LEU   A 334 ? 0.3604 0.3082 0.4662 -0.0500 -0.0311 0.0149  490 LEU   A CG  
2494 C  CD1 . LEU   A 334 ? 0.3527 0.3021 0.4533 -0.0415 -0.0305 0.0133  490 LEU   A CD1 
2495 C  CD2 . LEU   A 334 ? 0.3892 0.3476 0.5026 -0.0549 -0.0361 0.0135  490 LEU   A CD2 
2496 N  N   . PHE   A 335 ? 0.3885 0.3382 0.5063 -0.0605 -0.0160 0.0330  491 PHE   A N   
2497 C  CA  . PHE   A 335 ? 0.3956 0.3540 0.5182 -0.0622 -0.0111 0.0397  491 PHE   A CA  
2498 C  C   . PHE   A 335 ? 0.4554 0.4069 0.5829 -0.0702 -0.0094 0.0441  491 PHE   A C   
2499 O  O   . PHE   A 335 ? 0.4607 0.4140 0.5896 -0.0713 -0.0049 0.0511  491 PHE   A O   
2500 C  CB  . PHE   A 335 ? 0.3720 0.3299 0.4872 -0.0560 -0.0074 0.0432  491 PHE   A CB  
2501 C  CG  . PHE   A 335 ? 0.3709 0.3405 0.4838 -0.0503 -0.0067 0.0402  491 PHE   A CG  
2502 C  CD1 . PHE   A 335 ? 0.3341 0.3144 0.4532 -0.0499 -0.0084 0.0360  491 PHE   A CD1 
2503 C  CD2 . PHE   A 335 ? 0.3432 0.3142 0.4483 -0.0457 -0.0040 0.0419  491 PHE   A CD2 
2504 C  CE1 . PHE   A 335 ? 0.3279 0.3170 0.4453 -0.0443 -0.0065 0.0331  491 PHE   A CE1 
2505 C  CE2 . PHE   A 335 ? 0.3210 0.3015 0.4233 -0.0414 -0.0025 0.0382  491 PHE   A CE2 
2506 C  CZ  . PHE   A 335 ? 0.3697 0.3580 0.4782 -0.0405 -0.0033 0.0336  491 PHE   A CZ  
2507 N  N   . SER   A 336 ? 0.4852 0.4291 0.6150 -0.0767 -0.0127 0.0402  492 SER   A N   
2508 C  CA  . SER   A 336 ? 0.4963 0.4330 0.6312 -0.0856 -0.0107 0.0437  492 SER   A CA  
2509 C  C   . SER   A 336 ? 0.4708 0.4251 0.6158 -0.0899 -0.0082 0.0492  492 SER   A C   
2510 O  O   . SER   A 336 ? 0.4917 0.4642 0.6420 -0.0882 -0.0095 0.0479  492 SER   A O   
2511 C  CB  . SER   A 336 ? 0.4427 0.3710 0.5779 -0.0934 -0.0150 0.0370  492 SER   A CB  
2512 O  OG  . SER   A 336 ? 0.5880 0.5112 0.7291 -0.1038 -0.0130 0.0395  492 SER   A OG  
2513 N  N   . SER   A 337 ? 0.5008 0.4494 0.6490 -0.0954 -0.0040 0.0557  493 SER   A N   
2514 C  CA  . SER   A 337 ? 0.5077 0.4734 0.6659 -0.1006 -0.0015 0.0608  493 SER   A CA  
2515 C  C   . SER   A 337 ? 0.5287 0.5022 0.6958 -0.1097 -0.0053 0.0570  493 SER   A C   
2516 O  O   . SER   A 337 ? 0.5302 0.5220 0.7070 -0.1133 -0.0040 0.0602  493 SER   A O   
2517 C  CB  . SER   A 337 ? 0.5121 0.4706 0.6713 -0.1038 0.0043  0.0701  493 SER   A CB  
2518 O  OG  . SER   A 337 ? 0.6149 0.5530 0.7739 -0.1105 0.0048  0.0699  493 SER   A OG  
2519 N  N   . ASN   A 338 ? 0.5899 0.5515 0.7540 -0.1139 -0.0098 0.0502  494 ASN   A N   
2520 C  CA  . ASN   A 338 ? 0.5403 0.5129 0.7120 -0.1225 -0.0148 0.0460  494 ASN   A CA  
2521 C  C   . ASN   A 338 ? 0.5207 0.5142 0.6965 -0.1163 -0.0187 0.0436  494 ASN   A C   
2522 O  O   . ASN   A 338 ? 0.5899 0.6004 0.7757 -0.1220 -0.0221 0.0431  494 ASN   A O   
2523 C  CB  . ASN   A 338 ? 0.5463 0.5006 0.7116 -0.1293 -0.0185 0.0388  494 ASN   A CB  
2524 C  CG  . ASN   A 338 ? 0.6734 0.6054 0.8362 -0.1365 -0.0136 0.0408  494 ASN   A CG  
2525 O  OD1 . ASN   A 338 ? 0.7773 0.7121 0.9470 -0.1410 -0.0091 0.0478  494 ASN   A OD1 
2526 N  ND2 . ASN   A 338 ? 0.6896 0.5989 0.8428 -0.1371 -0.0137 0.0351  494 ASN   A ND2 
2527 N  N   . LEU   A 339 ? 0.4707 0.4636 0.6398 -0.1050 -0.0182 0.0424  495 LEU   A N   
2528 C  CA  . LEU   A 339 ? 0.4764 0.4861 0.6490 -0.0979 -0.0208 0.0403  495 LEU   A CA  
2529 C  C   . LEU   A 339 ? 0.5182 0.5427 0.6954 -0.0915 -0.0152 0.0448  495 LEU   A C   
2530 O  O   . LEU   A 339 ? 0.5274 0.5713 0.7149 -0.0903 -0.0152 0.0456  495 LEU   A O   
2531 C  CB  . LEU   A 339 ? 0.5161 0.5143 0.6775 -0.0903 -0.0240 0.0349  495 LEU   A CB  
2532 C  CG  . LEU   A 339 ? 0.5196 0.5047 0.6753 -0.0962 -0.0294 0.0293  495 LEU   A CG  
2533 C  CD1 . LEU   A 339 ? 0.4732 0.4474 0.6175 -0.0879 -0.0315 0.0247  495 LEU   A CD1 
2534 C  CD2 . LEU   A 339 ? 0.4835 0.4845 0.6486 -0.1037 -0.0351 0.0278  495 LEU   A CD2 
2535 N  N   . ILE   A 340 ? 0.4561 0.4726 0.6260 -0.0874 -0.0101 0.0478  496 ILE   A N   
2536 C  CA  . ILE   A 340 ? 0.4379 0.4678 0.6098 -0.0823 -0.0044 0.0512  496 ILE   A CA  
2537 C  C   . ILE   A 340 ? 0.5146 0.5401 0.6847 -0.0864 0.0007  0.0581  496 ILE   A C   
2538 O  O   . ILE   A 340 ? 0.4908 0.4992 0.6525 -0.0863 0.0009  0.0596  496 ILE   A O   
2539 C  CB  . ILE   A 340 ? 0.5072 0.5342 0.6696 -0.0721 -0.0036 0.0475  496 ILE   A CB  
2540 C  CG1 . ILE   A 340 ? 0.4894 0.5194 0.6537 -0.0678 -0.0085 0.0417  496 ILE   A CG1 
2541 C  CG2 . ILE   A 340 ? 0.4587 0.4990 0.6218 -0.0681 0.0030  0.0497  496 ILE   A CG2 
2542 C  CD1 . ILE   A 340 ? 0.4233 0.4470 0.5776 -0.0587 -0.0081 0.0377  496 ILE   A CD1 
2543 N  N   . ASP   A 341 ? 0.4749 0.5159 0.6531 -0.0898 0.0051  0.0629  497 ASP   A N   
2544 C  CA  . ASP   A 341 ? 0.4170 0.4535 0.5938 -0.0946 0.0096  0.0705  497 ASP   A CA  
2545 C  C   . ASP   A 341 ? 0.5185 0.5549 0.6853 -0.0882 0.0140  0.0737  497 ASP   A C   
2546 O  O   . ASP   A 341 ? 0.4272 0.4708 0.5896 -0.0812 0.0150  0.0696  497 ASP   A O   
2547 C  CB  . ASP   A 341 ? 0.5574 0.6099 0.7464 -0.1022 0.0127  0.0754  497 ASP   A CB  
2548 C  CG  . ASP   A 341 ? 0.5380 0.6124 0.7321 -0.0979 0.0169  0.0750  497 ASP   A CG  
2549 O  OD1 . ASP   A 341 ? 0.6246 0.7008 0.8111 -0.0898 0.0190  0.0722  497 ASP   A OD1 
2550 O  OD2 . ASP   A 341 ? 0.7205 0.8107 0.9269 -0.1032 0.0186  0.0774  497 ASP   A OD2 
2551 N  N   . LYS   A 342 ? 0.5160 0.5442 0.6792 -0.0911 0.0167  0.0813  498 LYS   A N   
2552 C  CA  . LYS   A 342 ? 0.5570 0.5846 0.7100 -0.0860 0.0198  0.0856  498 LYS   A CA  
2553 C  C   . LYS   A 342 ? 0.4672 0.5149 0.6192 -0.0834 0.0244  0.0851  498 LYS   A C   
2554 O  O   . LYS   A 342 ? 0.4537 0.5033 0.5964 -0.0775 0.0251  0.0821  498 LYS   A O   
2555 C  CB  . LYS   A 342 ? 0.5790 0.5982 0.7314 -0.0902 0.0226  0.0962  498 LYS   A CB  
2556 C  CG  . LYS   A 342 ? 0.4909 0.5152 0.6344 -0.0863 0.0261  0.1032  498 LYS   A CG  
2557 C  CD  . LYS   A 342 ? 0.5848 0.5947 0.7193 -0.0797 0.0232  0.1019  498 LYS   A CD  
2558 C  CE  . LYS   A 342 ? 0.5903 0.6012 0.7187 -0.0780 0.0260  0.1129  498 LYS   A CE  
2559 N  NZ  . LYS   A 342 ? 0.6624 0.6709 0.7975 -0.0841 0.0294  0.1240  498 LYS   A NZ  
2560 N  N   . ARG   A 343 ? 0.4478 0.5107 0.6092 -0.0884 0.0278  0.0873  499 ARG   A N   
2561 C  CA  . ARG   A 343 ? 0.5080 0.5899 0.6686 -0.0865 0.0335  0.0866  499 ARG   A CA  
2562 C  C   . ARG   A 343 ? 0.4823 0.5674 0.6397 -0.0790 0.0329  0.0767  499 ARG   A C   
2563 O  O   . ARG   A 343 ? 0.4662 0.5582 0.6155 -0.0754 0.0371  0.0746  499 ARG   A O   
2564 C  CB  . ARG   A 343 ? 0.5543 0.6518 0.7277 -0.0927 0.0371  0.0896  499 ARG   A CB  
2565 C  CG  . ARG   A 343 ? 0.5789 0.6963 0.7531 -0.0904 0.0439  0.0873  499 ARG   A CG  
2566 C  CD  . ARG   A 343 ? 0.6498 0.7738 0.8136 -0.0917 0.0496  0.0932  499 ARG   A CD  
2567 N  NE  . ARG   A 343 ? 0.5482 0.6748 0.7002 -0.0856 0.0520  0.0870  499 ARG   A NE  
2568 C  CZ  . ARG   A 343 ? 0.7274 0.8517 0.8658 -0.0850 0.0527  0.0903  499 ARG   A CZ  
2569 N  NH1 . ARG   A 343 ? 0.6255 0.7445 0.7609 -0.0890 0.0514  0.1007  499 ARG   A NH1 
2570 N  NH2 . ARG   A 343 ? 0.6070 0.7348 0.7349 -0.0807 0.0552  0.0834  499 ARG   A NH2 
2571 N  N   . SER   A 344 ? 0.4723 0.5523 0.6357 -0.0770 0.0280  0.0708  500 SER   A N   
2572 C  CA  . SER   A 344 ? 0.3870 0.4694 0.5487 -0.0695 0.0277  0.0624  500 SER   A CA  
2573 C  C   . SER   A 344 ? 0.3719 0.4424 0.5192 -0.0643 0.0263  0.0595  500 SER   A C   
2574 O  O   . SER   A 344 ? 0.3754 0.4502 0.5168 -0.0594 0.0296  0.0544  500 SER   A O   
2575 C  CB  . SER   A 344 ? 0.4184 0.4987 0.5897 -0.0690 0.0219  0.0584  500 SER   A CB  
2576 O  OG  . SER   A 344 ? 0.4658 0.5607 0.6513 -0.0739 0.0235  0.0613  500 SER   A OG  
2577 N  N   . LYS   A 345 ? 0.3674 0.4227 0.5092 -0.0655 0.0219  0.0624  501 LYS   A N   
2578 C  CA  . LYS   A 345 ? 0.3734 0.4185 0.5026 -0.0608 0.0204  0.0606  501 LYS   A CA  
2579 C  C   . LYS   A 345 ? 0.4070 0.4608 0.5275 -0.0612 0.0256  0.0646  501 LYS   A C   
2580 O  O   . LYS   A 345 ? 0.3711 0.4254 0.4819 -0.0573 0.0266  0.0606  501 LYS   A O   
2581 C  CB  . LYS   A 345 ? 0.4077 0.4354 0.5348 -0.0620 0.0156  0.0637  501 LYS   A CB  
2582 C  CG  . LYS   A 345 ? 0.4776 0.4962 0.6107 -0.0625 0.0100  0.0586  501 LYS   A CG  
2583 C  CD  . LYS   A 345 ? 0.4771 0.4786 0.6087 -0.0656 0.0074  0.0622  501 LYS   A CD  
2584 C  CE  . LYS   A 345 ? 0.5622 0.5582 0.7012 -0.0702 0.0033  0.0587  501 LYS   A CE  
2585 N  NZ  . LYS   A 345 ? 0.5317 0.5104 0.6704 -0.0751 0.0023  0.0616  501 LYS   A NZ  
2586 N  N   . GLU   A 346 ? 0.3767 0.4384 0.5003 -0.0667 0.0291  0.0728  502 GLU   A N   
2587 C  CA  . GLU   A 346 ? 0.4627 0.5353 0.5777 -0.0681 0.0339  0.0775  502 GLU   A CA  
2588 C  C   . GLU   A 346 ? 0.3777 0.4644 0.4900 -0.0666 0.0395  0.0704  502 GLU   A C   
2589 O  O   . GLU   A 346 ? 0.4031 0.4954 0.5039 -0.0660 0.0423  0.0691  502 GLU   A O   
2590 C  CB  . GLU   A 346 ? 0.4420 0.5202 0.5616 -0.0745 0.0366  0.0886  502 GLU   A CB  
2591 C  CG  . GLU   A 346 ? 0.4850 0.5479 0.6045 -0.0755 0.0329  0.0969  502 GLU   A CG  
2592 C  CD  . GLU   A 346 ? 0.5845 0.6500 0.7102 -0.0819 0.0356  0.1083  502 GLU   A CD  
2593 O  OE1 . GLU   A 346 ? 0.5269 0.6047 0.6598 -0.0866 0.0392  0.1090  502 GLU   A OE1 
2594 O  OE2 . GLU   A 346 ? 0.6883 0.7435 0.8125 -0.0822 0.0346  0.1171  502 GLU   A OE2 
2595 N  N   . PHE   A 347 ? 0.3768 0.4698 0.4998 -0.0663 0.0415  0.0658  503 PHE   A N   
2596 C  CA  . PHE   A 347 ? 0.3890 0.4937 0.5110 -0.0639 0.0479  0.0585  503 PHE   A CA  
2597 C  C   . PHE   A 347 ? 0.3803 0.4764 0.4939 -0.0579 0.0465  0.0497  503 PHE   A C   
2598 O  O   . PHE   A 347 ? 0.4137 0.5145 0.5167 -0.0573 0.0513  0.0453  503 PHE   A O   
2599 C  CB  . PHE   A 347 ? 0.3970 0.5102 0.5345 -0.0636 0.0501  0.0564  503 PHE   A CB  
2600 C  CG  . PHE   A 347 ? 0.4854 0.6099 0.6240 -0.0601 0.0581  0.0490  503 PHE   A CG  
2601 C  CD1 . PHE   A 347 ? 0.4775 0.6169 0.6137 -0.0637 0.0666  0.0503  503 PHE   A CD1 
2602 C  CD2 . PHE   A 347 ? 0.4998 0.6190 0.6408 -0.0532 0.0578  0.0408  503 PHE   A CD2 
2603 C  CE1 . PHE   A 347 ? 0.5042 0.6523 0.6410 -0.0603 0.0752  0.0427  503 PHE   A CE1 
2604 C  CE2 . PHE   A 347 ? 0.5175 0.6449 0.6599 -0.0494 0.0663  0.0340  503 PHE   A CE2 
2605 C  CZ  . PHE   A 347 ? 0.4675 0.6088 0.6077 -0.0530 0.0753  0.0344  503 PHE   A CZ  
2606 N  N   . LEU   A 348 ? 0.3792 0.4626 0.4966 -0.0541 0.0401  0.0468  504 LEU   A N   
2607 C  CA  . LEU   A 348 ? 0.3697 0.4443 0.4795 -0.0485 0.0387  0.0390  504 LEU   A CA  
2608 C  C   . LEU   A 348 ? 0.3510 0.4217 0.4457 -0.0496 0.0379  0.0405  504 LEU   A C   
2609 O  O   . LEU   A 348 ? 0.3475 0.4183 0.4327 -0.0477 0.0407  0.0342  504 LEU   A O   
2610 C  CB  . LEU   A 348 ? 0.3432 0.4056 0.4592 -0.0451 0.0314  0.0372  504 LEU   A CB  
2611 C  CG  . LEU   A 348 ? 0.3751 0.4275 0.4852 -0.0393 0.0291  0.0299  504 LEU   A CG  
2612 C  CD1 . LEU   A 348 ? 0.4047 0.4636 0.5163 -0.0354 0.0359  0.0229  504 LEU   A CD1 
2613 C  CD2 . LEU   A 348 ? 0.3164 0.3589 0.4330 -0.0373 0.0217  0.0297  504 LEU   A CD2 
2614 N  N   . THR   A 349 ? 0.3316 0.3993 0.4244 -0.0528 0.0345  0.0492  505 THR   A N   
2615 C  CA  . THR   A 349 ? 0.3551 0.4220 0.4353 -0.0537 0.0337  0.0526  505 THR   A CA  
2616 C  C   . THR   A 349 ? 0.3425 0.4245 0.4137 -0.0570 0.0403  0.0514  505 THR   A C   
2617 O  O   . THR   A 349 ? 0.3389 0.4217 0.3986 -0.0566 0.0411  0.0469  505 THR   A O   
2618 C  CB  . THR   A 349 ? 0.4174 0.4800 0.4998 -0.0562 0.0303  0.0639  505 THR   A CB  
2619 O  OG1 . THR   A 349 ? 0.3363 0.3827 0.4239 -0.0532 0.0244  0.0631  505 THR   A OG1 
2620 C  CG2 . THR   A 349 ? 0.3329 0.4004 0.4037 -0.0576 0.0303  0.0704  505 THR   A CG2 
2621 N  N   . LYS   A 350 ? 0.3619 0.4563 0.4378 -0.0610 0.0455  0.0546  506 LYS   A N   
2622 C  CA  . LYS   A 350 ? 0.4572 0.5669 0.5238 -0.0652 0.0526  0.0534  506 LYS   A CA  
2623 C  C   . LYS   A 350 ? 0.3865 0.4966 0.4481 -0.0627 0.0577  0.0405  506 LYS   A C   
2624 O  O   . LYS   A 350 ? 0.3727 0.4885 0.4208 -0.0654 0.0611  0.0365  506 LYS   A O   
2625 C  CB  . LYS   A 350 ? 0.4766 0.5987 0.5514 -0.0695 0.0575  0.0588  506 LYS   A CB  
2626 C  CG  . LYS   A 350 ? 0.5664 0.7058 0.6319 -0.0747 0.0654  0.0585  506 LYS   A CG  
2627 C  CD  . LYS   A 350 ? 0.6192 0.7704 0.6949 -0.0786 0.0702  0.0641  506 LYS   A CD  
2628 C  CE  . LYS   A 350 ? 0.5417 0.6889 0.6339 -0.0747 0.0706  0.0596  506 LYS   A CE  
2629 N  NZ  . LYS   A 350 ? 0.6340 0.7951 0.7364 -0.0787 0.0763  0.0640  506 LYS   A NZ  
2630 N  N   . GLN   A 351 ? 0.3945 0.4983 0.4669 -0.0577 0.0583  0.0341  507 GLN   A N   
2631 C  CA  . GLN   A 351 ? 0.3777 0.4807 0.4476 -0.0544 0.0644  0.0225  507 GLN   A CA  
2632 C  C   . GLN   A 351 ? 0.4089 0.5009 0.4676 -0.0523 0.0614  0.0166  507 GLN   A C   
2633 O  O   . GLN   A 351 ? 0.3760 0.4703 0.4236 -0.0540 0.0671  0.0089  507 GLN   A O   
2634 C  CB  . GLN   A 351 ? 0.4174 0.5174 0.5034 -0.0488 0.0652  0.0193  507 GLN   A CB  
2635 C  CG  . GLN   A 351 ? 0.4619 0.5753 0.5594 -0.0512 0.0698  0.0236  507 GLN   A CG  
2636 C  CD  . GLN   A 351 ? 0.5724 0.6991 0.6622 -0.0551 0.0801  0.0203  507 GLN   A CD  
2637 O  OE1 . GLN   A 351 ? 0.6665 0.7917 0.7492 -0.0533 0.0866  0.0107  507 GLN   A OE1 
2638 N  NE2 . GLN   A 351 ? 0.5744 0.7136 0.6648 -0.0611 0.0820  0.0281  507 GLN   A NE2 
2639 N  N   . ILE   A 352 ? 0.3339 0.4138 0.3950 -0.0491 0.0528  0.0197  508 ILE   A N   
2640 C  CA  . ILE   A 352 ? 0.3350 0.4050 0.3861 -0.0473 0.0495  0.0151  508 ILE   A CA  
2641 C  C   . ILE   A 352 ? 0.3394 0.4173 0.3753 -0.0531 0.0502  0.0174  508 ILE   A C   
2642 O  O   . ILE   A 352 ? 0.3467 0.4237 0.3714 -0.0545 0.0527  0.0101  508 ILE   A O   
2643 C  CB  . ILE   A 352 ? 0.3357 0.3926 0.3925 -0.0433 0.0405  0.0190  508 ILE   A CB  
2644 C  CG1 . ILE   A 352 ? 0.3300 0.3801 0.3998 -0.0379 0.0394  0.0153  508 ILE   A CG1 
2645 C  CG2 . ILE   A 352 ? 0.3321 0.3806 0.3784 -0.0421 0.0367  0.0165  508 ILE   A CG2 
2646 C  CD1 . ILE   A 352 ? 0.3207 0.3597 0.3965 -0.0356 0.0307  0.0197  508 ILE   A CD1 
2647 N  N   . GLU   A 353 ? 0.3420 0.4284 0.3774 -0.0571 0.0481  0.0280  509 GLU   A N   
2648 C  CA  . GLU   A 353 ? 0.3457 0.4428 0.3676 -0.0628 0.0483  0.0321  509 GLU   A CA  
2649 C  C   . GLU   A 353 ? 0.3445 0.4535 0.3560 -0.0681 0.0569  0.0244  509 GLU   A C   
2650 O  O   . GLU   A 353 ? 0.3419 0.4554 0.3397 -0.0722 0.0577  0.0206  509 GLU   A O   
2651 C  CB  . GLU   A 353 ? 0.3318 0.4366 0.3568 -0.0656 0.0454  0.0463  509 GLU   A CB  
2652 C  CG  . GLU   A 353 ? 0.3289 0.4215 0.3596 -0.0614 0.0375  0.0541  509 GLU   A CG  
2653 C  CD  . GLU   A 353 ? 0.3562 0.4537 0.3912 -0.0636 0.0356  0.0683  509 GLU   A CD  
2654 O  OE1 . GLU   A 353 ? 0.3222 0.4278 0.3621 -0.0669 0.0395  0.0721  509 GLU   A OE1 
2655 O  OE2 . GLU   A 353 ? 0.3275 0.4207 0.3614 -0.0618 0.0308  0.0761  509 GLU   A OE2 
2656 N  N   . TYR   A 354 ? 0.3642 0.4787 0.3821 -0.0685 0.0636  0.0216  510 TYR   A N   
2657 C  CA  . TYR   A 354 ? 0.4051 0.5287 0.4139 -0.0728 0.0733  0.0122  510 TYR   A CA  
2658 C  C   . TYR   A 354 ? 0.4403 0.5525 0.4433 -0.0703 0.0761  -0.0009 510 TYR   A C   
2659 O  O   . TYR   A 354 ? 0.4491 0.5659 0.4371 -0.0760 0.0801  -0.0077 510 TYR   A O   
2660 C  CB  . TYR   A 354 ? 0.3665 0.4963 0.3864 -0.0719 0.0804  0.0114  510 TYR   A CB  
2661 C  CG  . TYR   A 354 ? 0.5174 0.6541 0.5295 -0.0750 0.0920  0.0002  510 TYR   A CG  
2662 C  CD1 . TYR   A 354 ? 0.4591 0.6125 0.4589 -0.0836 0.0975  0.0013  510 TYR   A CD1 
2663 C  CD2 . TYR   A 354 ? 0.5708 0.6969 0.5872 -0.0696 0.0978  -0.0117 510 TYR   A CD2 
2664 C  CE1 . TYR   A 354 ? 0.5518 0.7107 0.5435 -0.0870 0.1090  -0.0101 510 TYR   A CE1 
2665 C  CE2 . TYR   A 354 ? 0.6289 0.7593 0.6383 -0.0722 0.1098  -0.0228 510 TYR   A CE2 
2666 C  CZ  . TYR   A 354 ? 0.5394 0.6857 0.5359 -0.0811 0.1155  -0.0226 510 TYR   A CZ  
2667 O  OH  . TYR   A 354 ? 0.7424 0.8922 0.7310 -0.0842 0.1283  -0.0347 510 TYR   A OH  
2668 N  N   . GLU   A 355 ? 0.4129 0.5106 0.4275 -0.0624 0.0742  -0.0047 511 GLU   A N   
2669 C  CA  . GLU   A 355 ? 0.4072 0.4928 0.4174 -0.0595 0.0771  -0.0162 511 GLU   A CA  
2670 C  C   . GLU   A 355 ? 0.4229 0.5063 0.4185 -0.0637 0.0725  -0.0172 511 GLU   A C   
2671 O  O   . GLU   A 355 ? 0.4293 0.5124 0.4124 -0.0680 0.0781  -0.0267 511 GLU   A O   
2672 C  CB  . GLU   A 355 ? 0.4370 0.5084 0.4620 -0.0504 0.0735  -0.0169 511 GLU   A CB  
2673 C  CG  . GLU   A 355 ? 0.4026 0.4768 0.4424 -0.0460 0.0792  -0.0179 511 GLU   A CG  
2674 C  CD  . GLU   A 355 ? 0.4267 0.5027 0.4626 -0.0465 0.0916  -0.0288 511 GLU   A CD  
2675 O  OE1 . GLU   A 355 ? 0.4763 0.5421 0.5042 -0.0458 0.0949  -0.0379 511 GLU   A OE1 
2676 O  OE2 . GLU   A 355 ? 0.4949 0.5819 0.5361 -0.0476 0.0986  -0.0285 511 GLU   A OE2 
2677 N  N   . ARG   A 356 ? 0.3592 0.4417 0.3562 -0.0628 0.0629  -0.0073 512 ARG   A N   
2678 C  CA  . ARG   A 356 ? 0.3598 0.4406 0.3455 -0.0656 0.0578  -0.0071 512 ARG   A CA  
2679 C  C   . ARG   A 356 ? 0.4278 0.5252 0.3978 -0.0753 0.0607  -0.0069 512 ARG   A C   
2680 O  O   . ARG   A 356 ? 0.5049 0.6026 0.4627 -0.0797 0.0608  -0.0126 512 ARG   A O   
2681 C  CB  . ARG   A 356 ? 0.3581 0.4345 0.3506 -0.0616 0.0479  0.0040  512 ARG   A CB  
2682 C  CG  . ARG   A 356 ? 0.3525 0.4249 0.3374 -0.0619 0.0419  0.0049  512 ARG   A CG  
2683 C  CD  . ARG   A 356 ? 0.3977 0.4849 0.3758 -0.0670 0.0381  0.0158  512 ARG   A CD  
2684 N  NE  . ARG   A 356 ? 0.3697 0.4573 0.3587 -0.0637 0.0340  0.0281  512 ARG   A NE  
2685 C  CZ  . ARG   A 356 ? 0.3416 0.4186 0.3386 -0.0579 0.0278  0.0340  512 ARG   A CZ  
2686 N  NH1 . ARG   A 356 ? 0.3465 0.4135 0.3416 -0.0547 0.0242  0.0301  512 ARG   A NH1 
2687 N  NH2 . ARG   A 356 ? 0.3315 0.4073 0.3383 -0.0557 0.0257  0.0438  512 ARG   A NH2 
2688 N  N   . ASN   A 357 ? 0.4081 0.5203 0.3778 -0.0795 0.0631  -0.0002 513 ASN   A N   
2689 C  CA  . ASN   A 357 ? 0.3952 0.5253 0.3491 -0.0895 0.0662  0.0002  513 ASN   A CA  
2690 C  C   . ASN   A 357 ? 0.4767 0.6076 0.4197 -0.0948 0.0765  -0.0150 513 ASN   A C   
2691 O  O   . ASN   A 357 ? 0.4511 0.5943 0.3777 -0.1043 0.0788  -0.0182 513 ASN   A O   
2692 C  CB  . ASN   A 357 ? 0.3936 0.5394 0.3504 -0.0925 0.0663  0.0121  513 ASN   A CB  
2693 C  CG  . ASN   A 357 ? 0.3769 0.5258 0.3384 -0.0906 0.0569  0.0278  513 ASN   A CG  
2694 O  OD1 . ASN   A 357 ? 0.4049 0.5530 0.3612 -0.0908 0.0512  0.0301  513 ASN   A OD1 
2695 N  ND2 . ASN   A 357 ? 0.3679 0.5191 0.3405 -0.0883 0.0556  0.0386  513 ASN   A ND2 
2696 N  N   . ASN   A 358 ? 0.4288 0.5473 0.3806 -0.0890 0.0832  -0.0243 514 ASN   A N   
2697 C  CA  . ASN   A 358 ? 0.4423 0.5598 0.3858 -0.0929 0.0950  -0.0386 514 ASN   A CA  
2698 C  C   . ASN   A 358 ? 0.4845 0.5826 0.4282 -0.0887 0.0978  -0.0506 514 ASN   A C   
2699 O  O   . ASN   A 358 ? 0.4656 0.5569 0.4087 -0.0880 0.1085  -0.0624 514 ASN   A O   
2700 C  CB  . ASN   A 358 ? 0.4314 0.5536 0.3849 -0.0903 0.1030  -0.0390 514 ASN   A CB  
2701 C  CG  . ASN   A 358 ? 0.4652 0.6086 0.4140 -0.0973 0.1031  -0.0294 514 ASN   A CG  
2702 O  OD1 . ASN   A 358 ? 0.4947 0.6511 0.4277 -0.1069 0.1091  -0.0339 514 ASN   A OD1 
2703 N  ND2 . ASN   A 358 ? 0.4291 0.5759 0.3909 -0.0932 0.0968  -0.0161 514 ASN   A ND2 
2704 N  N   . GLU   A 359 ? 0.4289 0.5181 0.3732 -0.0859 0.0888  -0.0474 515 GLU   A N   
2705 C  CA  . GLU   A 359 ? 0.5506 0.6211 0.4951 -0.0820 0.0900  -0.0568 515 GLU   A CA  
2706 C  C   . GLU   A 359 ? 0.5620 0.6185 0.5226 -0.0717 0.0948  -0.0606 515 GLU   A C   
2707 O  O   . GLU   A 359 ? 0.5820 0.6254 0.5417 -0.0696 0.1023  -0.0717 515 GLU   A O   
2708 C  CB  . GLU   A 359 ? 0.6049 0.6752 0.5314 -0.0914 0.0974  -0.0697 515 GLU   A CB  
2709 C  CG  . GLU   A 359 ? 0.6116 0.6999 0.5221 -0.1027 0.0927  -0.0654 515 GLU   A CG  
2710 C  CD  . GLU   A 359 ? 0.7503 0.8372 0.6427 -0.1130 0.0986  -0.0786 515 GLU   A CD  
2711 O  OE1 . GLU   A 359 ? 0.7906 0.8642 0.6816 -0.1124 0.1094  -0.0920 515 GLU   A OE1 
2712 O  OE2 . GLU   A 359 ? 0.7480 0.8463 0.6283 -0.1214 0.0926  -0.0756 515 GLU   A OE2 
2713 N  N   . PHE   A 360 ? 0.4447 0.5041 0.4203 -0.0653 0.0902  -0.0509 516 PHE   A N   
2714 C  CA  . PHE   A 360 ? 0.4891 0.5382 0.4822 -0.0552 0.0917  -0.0511 516 PHE   A CA  
2715 C  C   . PHE   A 360 ? 0.5480 0.5932 0.5435 -0.0532 0.1049  -0.0618 516 PHE   A C   
2716 O  O   . PHE   A 360 ? 0.5902 0.6207 0.5895 -0.0478 0.1089  -0.0688 516 PHE   A O   
2717 C  CB  . PHE   A 360 ? 0.4834 0.5167 0.4810 -0.0490 0.0843  -0.0505 516 PHE   A CB  
2718 C  CG  . PHE   A 360 ? 0.4346 0.4704 0.4312 -0.0498 0.0724  -0.0403 516 PHE   A CG  
2719 C  CD1 . PHE   A 360 ? 0.4550 0.4932 0.4642 -0.0455 0.0657  -0.0303 516 PHE   A CD1 
2720 C  CD2 . PHE   A 360 ? 0.4579 0.4938 0.4412 -0.0551 0.0683  -0.0409 516 PHE   A CD2 
2721 C  CE1 . PHE   A 360 ? 0.4042 0.4430 0.4128 -0.0459 0.0560  -0.0214 516 PHE   A CE1 
2722 C  CE2 . PHE   A 360 ? 0.4663 0.5045 0.4500 -0.0549 0.0581  -0.0310 516 PHE   A CE2 
2723 C  CZ  . PHE   A 360 ? 0.3951 0.4339 0.3915 -0.0500 0.0524  -0.0215 516 PHE   A CZ  
2724 N  N   . PRO   A 361 ? 0.4818 0.5403 0.4755 -0.0574 0.1127  -0.0630 517 PRO   A N   
2725 C  CA  . PRO   A 361 ? 0.4866 0.5419 0.4856 -0.0541 0.1262  -0.0724 517 PRO   A CA  
2726 C  C   . PRO   A 361 ? 0.5385 0.5858 0.5590 -0.0421 0.1262  -0.0694 517 PRO   A C   
2727 O  O   . PRO   A 361 ? 0.5180 0.5554 0.5437 -0.0367 0.1361  -0.0777 517 PRO   A O   
2728 C  CB  . PRO   A 361 ? 0.5358 0.6099 0.5311 -0.0604 0.1319  -0.0704 517 PRO   A CB  
2729 C  CG  . PRO   A 361 ? 0.5168 0.6026 0.5128 -0.0635 0.1197  -0.0565 517 PRO   A CG  
2730 C  CD  . PRO   A 361 ? 0.5043 0.5812 0.4923 -0.0647 0.1097  -0.0548 517 PRO   A CD  
2731 N  N   . VAL   A 362 ? 0.5045 0.5554 0.5375 -0.0379 0.1155  -0.0578 518 VAL   A N   
2732 C  CA  . VAL   A 362 ? 0.4856 0.5325 0.5392 -0.0276 0.1146  -0.0541 518 VAL   A CA  
2733 C  C   . VAL   A 362 ? 0.4904 0.5194 0.5466 -0.0207 0.1152  -0.0594 518 VAL   A C   
2734 O  O   . VAL   A 362 ? 0.6227 0.6478 0.6945 -0.0119 0.1190  -0.0593 518 VAL   A O   
2735 C  CB  . VAL   A 362 ? 0.4735 0.5265 0.5374 -0.0263 0.1021  -0.0415 518 VAL   A CB  
2736 C  CG1 . VAL   A 362 ? 0.4658 0.5067 0.5263 -0.0247 0.0912  -0.0389 518 VAL   A CG1 
2737 C  CG2 . VAL   A 362 ? 0.4875 0.5457 0.5727 -0.0188 0.1034  -0.0370 518 VAL   A CG2 
2738 N  N   . PHE   A 363 ? 0.4819 0.5007 0.5236 -0.0247 0.1119  -0.0636 519 PHE   A N   
2739 C  CA  . PHE   A 363 ? 0.5974 0.5986 0.6412 -0.0187 0.1125  -0.0682 519 PHE   A CA  
2740 C  C   . PHE   A 363 ? 0.7346 0.7279 0.7816 -0.0147 0.1274  -0.0781 519 PHE   A C   
2741 O  O   . PHE   A 363 ? 0.7332 0.7165 0.7933 -0.0052 0.1297  -0.0779 519 PHE   A O   
2742 C  CB  . PHE   A 363 ? 0.5101 0.5033 0.5370 -0.0249 0.1070  -0.0711 519 PHE   A CB  
2743 C  CG  . PHE   A 363 ? 0.5002 0.4950 0.5286 -0.0246 0.0926  -0.0612 519 PHE   A CG  
2744 C  CD1 . PHE   A 363 ? 0.5177 0.5170 0.5617 -0.0187 0.0859  -0.0519 519 PHE   A CD1 
2745 C  CD2 . PHE   A 363 ? 0.4694 0.4611 0.4841 -0.0303 0.0864  -0.0615 519 PHE   A CD2 
2746 C  CE1 . PHE   A 363 ? 0.5263 0.5255 0.5712 -0.0186 0.0737  -0.0438 519 PHE   A CE1 
2747 C  CE2 . PHE   A 363 ? 0.4493 0.4416 0.4660 -0.0292 0.0744  -0.0526 519 PHE   A CE2 
2748 C  CZ  . PHE   A 363 ? 0.4364 0.4315 0.4677 -0.0234 0.0683  -0.0442 519 PHE   A CZ  
2749 N  N   . ASP   A 364 ? 0.7310 0.7292 0.7668 -0.0216 0.1381  -0.0865 520 ASP   A N   
2750 C  CA  . ASP   A 364 ? 0.7924 0.7830 0.8317 -0.0178 0.1539  -0.0966 520 ASP   A CA  
2751 C  C   . ASP   A 364 ? 0.7053 0.7089 0.7610 -0.0122 0.1604  -0.0928 520 ASP   A C   
2752 O  O   . ASP   A 364 ? 0.7985 0.8090 0.8490 -0.0164 0.1719  -0.0995 520 ASP   A O   
2753 C  CB  . ASP   A 364 ? 0.7350 0.7227 0.7528 -0.0286 0.1637  -0.1095 520 ASP   A CB  
2754 C  CG  . ASP   A 364 ? 0.9223 0.8886 0.9369 -0.0260 0.1746  -0.1211 520 ASP   A CG  
2755 O  OD1 . ASP   A 364 ? 0.9038 0.8614 0.9350 -0.0149 0.1823  -0.1215 520 ASP   A OD1 
2756 O  OD2 . ASP   A 364 ? 0.9890 0.9473 0.9851 -0.0351 0.1755  -0.1294 520 ASP   A OD2 
2757 N  N   . GLY   B 5   ? 0.7090 0.8377 0.7420 0.0581  0.0811  0.0653  161 GLY   B N   
2758 C  CA  . GLY   B 5   ? 0.6490 0.7549 0.6765 0.0674  0.0893  0.0579  161 GLY   B CA  
2759 C  C   . GLY   B 5   ? 0.6318 0.7096 0.6466 0.0656  0.0840  0.0491  161 GLY   B C   
2760 O  O   . GLY   B 5   ? 0.6595 0.7156 0.6599 0.0651  0.0863  0.0393  161 GLY   B O   
2761 N  N   . ALA   B 6   ? 0.6085 0.6881 0.6282 0.0640  0.0765  0.0528  162 ALA   B N   
2762 C  CA  . ALA   B 6   ? 0.6954 0.7505 0.7049 0.0626  0.0714  0.0454  162 ALA   B CA  
2763 C  C   . ALA   B 6   ? 0.6807 0.7171 0.6916 0.0734  0.0794  0.0411  162 ALA   B C   
2764 O  O   . ALA   B 6   ? 0.5781 0.5908 0.5754 0.0717  0.0788  0.0313  162 ALA   B O   
2765 C  CB  . ALA   B 6   ? 0.4792 0.5423 0.4950 0.0591  0.0628  0.0509  162 ALA   B CB  
2766 N  N   . SER   B 7   ? 0.5460 0.5930 0.5733 0.0844  0.0875  0.0485  163 SER   B N   
2767 C  CA  . SER   B 7   ? 0.6273 0.6552 0.6565 0.0948  0.0968  0.0442  163 SER   B CA  
2768 C  C   . SER   B 7   ? 0.5419 0.5537 0.5567 0.0942  0.1038  0.0331  163 SER   B C   
2769 O  O   . SER   B 7   ? 0.5337 0.5224 0.5417 0.0979  0.1089  0.0248  163 SER   B O   
2770 C  CB  . SER   B 7   ? 0.5024 0.5459 0.5532 0.1075  0.1056  0.0553  163 SER   B CB  
2771 O  OG  . SER   B 7   ? 0.5667 0.6294 0.6236 0.1096  0.1120  0.0595  163 SER   B OG  
2772 N  N   . LYS   B 8   ? 0.5081 0.5321 0.5177 0.0891  0.1045  0.0329  164 LYS   B N   
2773 C  CA  . LYS   B 8   ? 0.6259 0.6357 0.6193 0.0866  0.1099  0.0225  164 LYS   B CA  
2774 C  C   . LYS   B 8   ? 0.5927 0.5805 0.5669 0.0779  0.1018  0.0125  164 LYS   B C   
2775 O  O   . LYS   B 8   ? 0.5789 0.5467 0.5412 0.0786  0.1063  0.0027  164 LYS   B O   
2776 C  CB  . LYS   B 8   ? 0.5926 0.6216 0.5845 0.0817  0.1112  0.0256  164 LYS   B CB  
2777 C  CG  . LYS   B 8   ? 0.6473 0.6949 0.6554 0.0915  0.1229  0.0325  164 LYS   B CG  
2778 C  CD  . LYS   B 8   ? 0.6350 0.6990 0.6393 0.0862  0.1256  0.0338  164 LYS   B CD  
2779 C  CE  . LYS   B 8   ? 0.7211 0.8179 0.7455 0.0881  0.1258  0.0474  164 LYS   B CE  
2780 N  NZ  . LYS   B 8   ? 0.5264 0.6407 0.5553 0.0903  0.1355  0.0501  164 LYS   B NZ  
2781 N  N   . LEU   B 9   ? 0.4955 0.4875 0.4667 0.0693  0.0901  0.0150  165 LEU   B N   
2782 C  CA  . LEU   B 9   ? 0.5272 0.5003 0.4830 0.0619  0.0820  0.0073  165 LEU   B CA  
2783 C  C   . LEU   B 9   ? 0.5718 0.5248 0.5268 0.0671  0.0841  0.0017  165 LEU   B C   
2784 O  O   . LEU   B 9   ? 0.4832 0.4177 0.4238 0.0642  0.0842  -0.0077 165 LEU   B O   
2785 C  CB  . LEU   B 9   ? 0.4837 0.4647 0.4409 0.0542  0.0706  0.0121  165 LEU   B CB  
2786 C  CG  . LEU   B 9   ? 0.5294 0.5284 0.4864 0.0472  0.0682  0.0169  165 LEU   B CG  
2787 C  CD1 . LEU   B 9   ? 0.4451 0.4492 0.4031 0.0394  0.0580  0.0203  165 LEU   B CD1 
2788 C  CD2 . LEU   B 9   ? 0.4684 0.4607 0.4100 0.0421  0.0700  0.0112  165 LEU   B CD2 
2789 N  N   . ARG   B 10  ? 0.5476 0.5046 0.5181 0.0745  0.0860  0.0078  166 ARG   B N   
2790 C  CA  . ARG   B 10  ? 0.5255 0.4631 0.4964 0.0792  0.0884  0.0032  166 ARG   B CA  
2791 C  C   . ARG   B 10  ? 0.5380 0.4603 0.5030 0.0843  0.1001  -0.0052 166 ARG   B C   
2792 O  O   . ARG   B 10  ? 0.5332 0.4345 0.4876 0.0823  0.1004  -0.0145 166 ARG   B O   
2793 C  CB  . ARG   B 10  ? 0.5706 0.5171 0.5604 0.0867  0.0892  0.0132  166 ARG   B CB  
2794 N  N   . ALA   B 11  ? 0.5161 0.4491 0.4878 0.0905  0.1100  -0.0024 167 ALA   B N   
2795 C  CA  . ALA   B 11  ? 0.5952 0.5137 0.5599 0.0949  0.1223  -0.0115 167 ALA   B CA  
2796 C  C   . ALA   B 11  ? 0.5831 0.4879 0.5247 0.0850  0.1191  -0.0233 167 ALA   B C   
2797 O  O   . ALA   B 11  ? 0.5630 0.4476 0.4940 0.0849  0.1245  -0.0339 167 ALA   B O   
2798 C  CB  . ALA   B 11  ? 0.5346 0.4704 0.5095 0.1019  0.1328  -0.0061 167 ALA   B CB  
2799 N  N   . VAL   B 12  ? 0.5455 0.4614 0.4790 0.0764  0.1104  -0.0213 168 VAL   B N   
2800 C  CA  . VAL   B 12  ? 0.5264 0.4320 0.4388 0.0667  0.1056  -0.0301 168 VAL   B CA  
2801 C  C   . VAL   B 12  ? 0.5319 0.4191 0.4365 0.0626  0.0987  -0.0363 168 VAL   B C   
2802 O  O   . VAL   B 12  ? 0.6196 0.4909 0.5100 0.0594  0.1013  -0.0465 168 VAL   B O   
2803 C  CB  . VAL   B 12  ? 0.5103 0.4313 0.4188 0.0588  0.0969  -0.0244 168 VAL   B CB  
2804 C  CG1 . VAL   B 12  ? 0.5856 0.4961 0.4738 0.0490  0.0901  -0.0312 168 VAL   B CG1 
2805 C  CG2 . VAL   B 12  ? 0.5122 0.4512 0.4268 0.0617  0.1043  -0.0193 168 VAL   B CG2 
2806 N  N   . LEU   B 13  ? 0.4992 0.3895 0.4125 0.0618  0.0898  -0.0302 169 LEU   B N   
2807 C  CA  . LEU   B 13  ? 0.5088 0.3843 0.4165 0.0577  0.0825  -0.0348 169 LEU   B CA  
2808 C  C   . LEU   B 13  ? 0.5996 0.4571 0.5077 0.0626  0.0907  -0.0419 169 LEU   B C   
2809 O  O   . LEU   B 13  ? 0.6279 0.4698 0.5244 0.0574  0.0881  -0.0503 169 LEU   B O   
2810 C  CB  . LEU   B 13  ? 0.5221 0.4059 0.4418 0.0576  0.0739  -0.0263 169 LEU   B CB  
2811 C  CG  . LEU   B 13  ? 0.4925 0.3903 0.4102 0.0510  0.0650  -0.0208 169 LEU   B CG  
2812 C  CD1 . LEU   B 13  ? 0.5182 0.4263 0.4494 0.0520  0.0593  -0.0125 169 LEU   B CD1 
2813 C  CD2 . LEU   B 13  ? 0.4864 0.3751 0.3886 0.0424  0.0572  -0.0263 169 LEU   B CD2 
2814 N  N   . GLU   B 14  ? 0.5637 0.4235 0.4859 0.0725  0.1009  -0.0381 170 GLU   B N   
2815 C  CA  . GLU   B 14  ? 0.6813 0.5224 0.6047 0.0779  0.1108  -0.0448 170 GLU   B CA  
2816 C  C   . GLU   B 14  ? 0.6703 0.4978 0.5752 0.0734  0.1173  -0.0578 170 GLU   B C   
2817 O  O   . GLU   B 14  ? 0.7541 0.5628 0.6489 0.0692  0.1178  -0.0675 170 GLU   B O   
2818 C  CB  . GLU   B 14  ? 0.6190 0.4672 0.5619 0.0903  0.1217  -0.0369 170 GLU   B CB  
2819 C  CG  . GLU   B 14  ? 0.7648 0.6123 0.7246 0.0962  0.1198  -0.0286 170 GLU   B CG  
2820 C  CD  . GLU   B 14  ? 0.9270 0.7523 0.8797 0.0920  0.1168  -0.0363 170 GLU   B CD  
2821 O  OE1 . GLU   B 14  ? 0.9288 0.7569 0.8861 0.0892  0.1070  -0.0311 170 GLU   B OE1 
2822 O  OE2 . GLU   B 14  ? 0.9254 0.7310 0.8674 0.0907  0.1245  -0.0478 170 GLU   B OE2 
2823 N  N   . LYS   B 15  ? 0.6233 0.4611 0.5227 0.0731  0.1219  -0.0583 171 LYS   B N   
2824 C  CA  . LYS   B 15  ? 0.7017 0.5285 0.5828 0.0689  0.1291  -0.0705 171 LYS   B CA  
2825 C  C   . LYS   B 15  ? 0.8057 0.6258 0.6671 0.0565  0.1183  -0.0774 171 LYS   B C   
2826 O  O   . LYS   B 15  ? 0.8498 0.6547 0.6961 0.0515  0.1221  -0.0892 171 LYS   B O   
2827 C  CB  . LYS   B 15  ? 0.7195 0.5614 0.5997 0.0710  0.1359  -0.0681 171 LYS   B CB  
2828 N  N   . LEU   B 16  ? 0.7536 0.5856 0.6151 0.0512  0.1052  -0.0702 172 LEU   B N   
2829 C  CA  . LEU   B 16  ? 0.8203 0.6478 0.6653 0.0404  0.0946  -0.0748 172 LEU   B CA  
2830 C  C   . LEU   B 16  ? 0.8485 0.6594 0.6915 0.0379  0.0918  -0.0811 172 LEU   B C   
2831 O  O   . LEU   B 16  ? 0.7823 0.5839 0.6090 0.0298  0.0894  -0.0901 172 LEU   B O   
2832 C  CB  . LEU   B 16  ? 0.6646 0.5065 0.5129 0.0366  0.0822  -0.0651 172 LEU   B CB  
2833 C  CG  . LEU   B 16  ? 0.6899 0.5480 0.5369 0.0359  0.0830  -0.0593 172 LEU   B CG  
2834 C  CD1 . LEU   B 16  ? 0.6130 0.4826 0.4652 0.0325  0.0719  -0.0499 172 LEU   B CD1 
2835 C  CD2 . LEU   B 16  ? 0.7394 0.5953 0.5668 0.0297  0.0857  -0.0663 172 LEU   B CD2 
2836 N  N   . LYS   B 17  ? 0.8459 0.6540 0.7053 0.0441  0.0919  -0.0762 173 LYS   B N   
2837 C  CA  . LYS   B 17  ? 0.8342 0.6268 0.6935 0.0419  0.0897  -0.0812 173 LYS   B CA  
2838 C  C   . LYS   B 17  ? 0.8962 0.6703 0.7464 0.0415  0.1011  -0.0936 173 LYS   B C   
2839 O  O   . LYS   B 17  ? 0.9159 0.6776 0.7542 0.0336  0.0983  -0.1025 173 LYS   B O   
2840 C  CB  . LYS   B 17  ? 0.8125 0.6071 0.6920 0.0495  0.0889  -0.0722 173 LYS   B CB  
2841 N  N   . LEU   B 18  ? 0.8264 0.5985 0.6821 0.0496  0.1147  -0.0947 174 LEU   B N   
2842 C  CA  . LEU   B 18  ? 0.8921 0.6451 0.7387 0.0493  0.1273  -0.1075 174 LEU   B CA  
2843 C  C   . LEU   B 18  ? 0.9721 0.7229 0.7945 0.0382  0.1258  -0.1184 174 LEU   B C   
2844 O  O   . LEU   B 18  ? 0.9985 0.7329 0.8077 0.0314  0.1291  -0.1306 174 LEU   B O   
2845 C  CB  . LEU   B 18  ? 0.9096 0.6623 0.7679 0.0612  0.1428  -0.1056 174 LEU   B CB  
2846 C  CG  . LEU   B 18  ? 0.9821 0.7269 0.8611 0.0717  0.1490  -0.0995 174 LEU   B CG  
2847 C  CD1 . LEU   B 18  ? 0.9415 0.6953 0.8365 0.0847  0.1612  -0.0922 174 LEU   B CD1 
2848 C  CD2 . LEU   B 18  ? 0.9468 0.6648 0.8198 0.0691  0.1563  -0.1115 174 LEU   B CD2 
2849 N  N   . SER   B 19  ? 0.9527 0.7206 0.7688 0.0355  0.1208  -0.1138 175 SER   B N   
2850 C  CA  . SER   B 19  ? 1.0465 0.8149 0.8395 0.0250  0.1189  -0.1224 175 SER   B CA  
2851 C  C   . SER   B 19  ? 1.0051 0.7690 0.7868 0.0139  0.1065  -0.1262 175 SER   B C   
2852 O  O   . SER   B 19  ? 1.1057 0.8614 0.8687 0.0047  0.1077  -0.1375 175 SER   B O   
2853 C  CB  . SER   B 19  ? 1.0508 0.8391 0.8414 0.0245  0.1150  -0.1144 175 SER   B CB  
2854 O  OG  . SER   B 19  ? 1.1150 0.9093 0.9155 0.0340  0.1269  -0.1113 175 SER   B OG  
2855 N  N   . ARG   B 20  ? 1.0407 0.8106 0.8338 0.0144  0.0948  -0.1170 176 ARG   B N   
2856 C  CA  . ARG   B 20  ? 1.0500 0.8171 0.8351 0.0048  0.0830  -0.1193 176 ARG   B CA  
2857 C  C   . ARG   B 20  ? 1.0538 0.8017 0.8374 0.0023  0.0877  -0.1294 176 ARG   B C   
2858 O  O   . ARG   B 20  ? 1.1357 0.8778 0.9037 -0.0083 0.0842  -0.1383 176 ARG   B O   
2859 C  CB  . ARG   B 20  ? 0.9483 0.7264 0.7468 0.0068  0.0707  -0.1070 176 ARG   B CB  
2860 N  N   . ASP   B 21  ? 1.0590 0.7973 0.8586 0.0114  0.0959  -0.1278 177 ASP   B N   
2861 C  CA  . ASP   B 21  ? 1.0971 0.8164 0.8980 0.0093  0.0997  -0.1355 177 ASP   B CA  
2862 C  C   . ASP   B 21  ? 1.0631 0.7662 0.8464 0.0029  0.1105  -0.1513 177 ASP   B C   
2863 O  O   . ASP   B 21  ? 1.2290 0.9194 1.0035 -0.0060 0.1091  -0.1606 177 ASP   B O   
2864 C  CB  . ASP   B 21  ? 1.0899 0.8031 0.9125 0.0214  0.1070  -0.1287 177 ASP   B CB  
2865 C  CG  . ASP   B 21  ? 1.1700 0.8965 1.0084 0.0252  0.0957  -0.1149 177 ASP   B CG  
2866 O  OD1 . ASP   B 21  ? 1.1773 0.9140 1.0098 0.0180  0.0827  -0.1122 177 ASP   B OD1 
2867 O  OD2 . ASP   B 21  ? 1.2950 1.0222 1.1515 0.0353  0.1001  -0.1067 177 ASP   B OD2 
2868 N  N   . ASP   B 22  ? 1.1341 0.8375 0.9120 0.0068  0.1217  -0.1552 178 ASP   B N   
2869 C  CA  . ASP   B 22  ? 1.0980 0.7859 0.8581 0.0006  0.1333  -0.1712 178 ASP   B CA  
2870 C  C   . ASP   B 22  ? 1.1431 0.8394 0.8790 -0.0133 0.1256  -0.1780 178 ASP   B C   
2871 O  O   . ASP   B 22  ? 1.0656 0.7569 0.7876 -0.0197 0.1323  -0.1891 178 ASP   B O   
2872 C  CB  . ASP   B 22  ? 1.1923 0.8765 0.9574 0.0113  0.1502  -0.1728 178 ASP   B CB  
2873 N  N   . ILE   B 23  ? 1.1760 0.8902 0.9113 -0.0176 0.1096  -0.1684 179 ILE   B N   
2874 C  CA  . ILE   B 23  ? 1.1285 0.8536 0.8428 -0.0300 0.1006  -0.1717 179 ILE   B CA  
2875 C  C   . ILE   B 23  ? 1.1848 0.9197 0.9019 -0.0361 0.0834  -0.1642 179 ILE   B C   
2876 O  O   . ILE   B 23  ? 1.1939 0.9293 0.8960 -0.0484 0.0766  -0.1705 179 ILE   B O   
2877 C  CB  . ILE   B 23  ? 1.1304 0.8719 0.8397 -0.0273 0.1014  -0.1658 179 ILE   B CB  
2878 C  CG1 . ILE   B 23  ? 1.1749 0.9078 0.8805 -0.0218 0.1194  -0.1740 179 ILE   B CG1 
2879 C  CG2 . ILE   B 23  ? 1.1724 0.9271 0.8614 -0.0398 0.0907  -0.1664 179 ILE   B CG2 
2880 C  CD1 . ILE   B 23  ? 1.1785 0.9276 0.8825 -0.0176 0.1217  -0.1672 179 ILE   B CD1 
2881 N  N   . THR   B 25  ? 1.0839 0.7926 0.7833 -0.0620 0.0771  -0.1877 181 THR   B N   
2882 C  CA  . THR   B 25  ? 1.0532 0.7619 0.7395 -0.0727 0.0792  -0.1984 181 THR   B CA  
2883 C  C   . THR   B 25  ? 1.1678 0.8942 0.8340 -0.0832 0.0703  -0.1984 181 THR   B C   
2884 O  O   . THR   B 25  ? 1.1301 0.8640 0.7866 -0.0954 0.0618  -0.2017 181 THR   B O   
2885 C  CB  . THR   B 25  ? 1.1028 0.8001 0.7899 -0.0670 0.0957  -0.2060 181 THR   B CB  
2886 O  OG1 . THR   B 25  ? 1.1328 0.8146 0.8396 -0.0567 0.1042  -0.2044 181 THR   B OG1 
2887 C  CG2 . THR   B 25  ? 0.9192 0.6149 0.5916 -0.0792 0.0979  -0.2177 181 THR   B CG2 
2888 N  N   . ALA   B 26  ? 1.1615 0.8952 0.8219 -0.0780 0.0727  -0.1939 182 ALA   B N   
2889 C  CA  . ALA   B 26  ? 1.1348 0.8866 0.7771 -0.0866 0.0642  -0.1913 182 ALA   B CA  
2890 C  C   . ALA   B 26  ? 1.0510 0.8160 0.6939 -0.0929 0.0470  -0.1826 182 ALA   B C   
2891 O  O   . ALA   B 26  ? 1.1777 0.9550 0.8061 -0.1049 0.0383  -0.1840 182 ALA   B O   
2892 C  CB  . ALA   B 26  ? 1.0694 0.8290 0.7124 -0.0776 0.0684  -0.1838 182 ALA   B CB  
2893 N  N   . ALA   B 27  ? 1.0435 0.8101 0.7086 -0.0835 0.0412  -0.1710 183 ALA   B N   
2894 C  CA  . ALA   B 27  ? 1.0270 0.8082 0.6987 -0.0866 0.0253  -0.1602 183 ALA   B CA  
2895 C  C   . ALA   B 27  ? 1.0017 0.7812 0.6643 -0.1000 0.0194  -0.1684 183 ALA   B C   
2896 O  O   . ALA   B 27  ? 1.0263 0.8218 0.6874 -0.1063 0.0060  -0.1613 183 ALA   B O   
2897 C  CB  . ALA   B 27  ? 0.9427 0.7226 0.6394 -0.0745 0.0227  -0.1491 183 ALA   B CB  
2898 N  N   . GLY   B 28  ? 0.9839 0.7448 0.6420 -0.1042 0.0293  -0.1825 184 GLY   B N   
2899 C  CA  . GLY   B 28  ? 0.9790 0.7436 0.6341 -0.1159 0.0238  -0.1880 184 GLY   B CA  
2900 C  C   . GLY   B 28  ? 0.9522 0.7319 0.5883 -0.1273 0.0201  -0.1916 184 GLY   B C   
2901 O  O   . GLY   B 28  ? 1.1359 0.9294 0.7670 -0.1380 0.0091  -0.1902 184 GLY   B O   
2902 N  N   . MET   B 29  ? 0.9342 0.7127 0.5600 -0.1252 0.0295  -0.1958 185 MET   B N   
2903 C  CA  . MET   B 29  ? 1.0667 0.8612 0.6738 -0.1354 0.0259  -0.1977 185 MET   B CA  
2904 C  C   . MET   B 29  ? 0.9852 0.8019 0.5872 -0.1389 0.0107  -0.1849 185 MET   B C   
2905 O  O   . MET   B 29  ? 1.0379 0.8713 0.6309 -0.1499 0.0009  -0.1831 185 MET   B O   
2906 C  CB  . MET   B 29  ? 1.0137 0.8036 0.6121 -0.1308 0.0387  -0.2028 185 MET   B CB  
2907 C  CG  . MET   B 29  ? 1.1235 0.9123 0.7080 -0.1402 0.0453  -0.2146 185 MET   B CG  
2908 S  SD  . MET   B 29  ? 1.5613 1.3317 1.1523 -0.1454 0.0513  -0.2268 185 MET   B SD  
2909 C  CE  . MET   B 29  ? 1.1785 0.9256 0.7762 -0.1330 0.0719  -0.2349 185 MET   B CE  
2910 N  N   . VAL   B 30  ? 0.9689 0.7861 0.5767 -0.1295 0.0088  -0.1751 186 VAL   B N   
2911 C  CA  . VAL   B 30  ? 0.9879 0.8247 0.5935 -0.1310 -0.0053 -0.1610 186 VAL   B CA  
2912 C  C   . VAL   B 30  ? 1.0085 0.8547 0.6208 -0.1376 -0.0185 -0.1565 186 VAL   B C   
2913 O  O   . VAL   B 30  ? 0.9869 0.8531 0.5910 -0.1465 -0.0296 -0.1507 186 VAL   B O   
2914 C  CB  . VAL   B 30  ? 0.9159 0.7531 0.5415 -0.1147 -0.0043 -0.1475 186 VAL   B CB  
2915 C  CG1 . VAL   B 30  ? 0.9055 0.7631 0.5381 -0.1130 -0.0183 -0.1300 186 VAL   B CG1 
2916 C  CG2 . VAL   B 30  ? 0.9861 0.8179 0.6043 -0.1095 0.0080  -0.1511 186 VAL   B CG2 
2917 N  N   . LYS   B 31  ? 0.9685 0.8022 0.5982 -0.1326 -0.0173 -0.1577 187 LYS   B N   
2918 C  CA  . LYS   B 31  ? 0.9269 0.7687 0.5645 -0.1387 -0.0286 -0.1541 187 LYS   B CA  
2919 C  C   . LYS   B 31  ? 1.0519 0.9068 0.6760 -0.1536 -0.0339 -0.1597 187 LYS   B C   
2920 O  O   . LYS   B 31  ? 1.1542 1.0293 0.7780 -0.1599 -0.0471 -0.1509 187 LYS   B O   
2921 C  CB  . LYS   B 31  ? 1.0676 0.8902 0.7210 -0.1340 -0.0229 -0.1596 187 LYS   B CB  
2922 C  CG  . LYS   B 31  ? 1.0941 0.9198 0.7480 -0.1457 -0.0294 -0.1644 187 LYS   B CG  
2923 C  CD  . LYS   B 31  ? 1.1556 0.9630 0.8260 -0.1409 -0.0244 -0.1679 187 LYS   B CD  
2924 C  CE  . LYS   B 31  ? 1.0037 0.7950 0.6725 -0.1436 -0.0117 -0.1815 187 LYS   B CE  
2925 N  NZ  . LYS   B 31  ? 1.0568 0.8599 0.7110 -0.1571 -0.0144 -0.1878 187 LYS   B NZ  
2926 N  N   . GLY   B 32  ? 1.0574 0.9027 0.6734 -0.1578 -0.0233 -0.1725 188 GLY   B N   
2927 C  CA  . GLY   B 32  ? 0.8885 0.7463 0.4937 -0.1713 -0.0272 -0.1775 188 GLY   B CA  
2928 C  C   . GLY   B 32  ? 1.0165 0.9000 0.6101 -0.1768 -0.0377 -0.1676 188 GLY   B C   
2929 O  O   . GLY   B 32  ? 1.1402 1.0430 0.7334 -0.1854 -0.0494 -0.1618 188 GLY   B O   
2930 N  N   . VAL   B 33  ? 1.0539 0.9391 0.6389 -0.1717 -0.0334 -0.1647 189 VAL   B N   
2931 C  CA  . VAL   B 33  ? 0.9973 0.9066 0.5710 -0.1765 -0.0422 -0.1546 189 VAL   B CA  
2932 C  C   . VAL   B 33  ? 0.9342 0.8607 0.5176 -0.1742 -0.0571 -0.1377 189 VAL   B C   
2933 O  O   . VAL   B 33  ? 1.0126 0.9620 0.5929 -0.1814 -0.0683 -0.1290 189 VAL   B O   
2934 C  CB  . VAL   B 33  ? 0.9527 0.8587 0.5163 -0.1707 -0.0335 -0.1544 189 VAL   B CB  
2935 C  CG1 . VAL   B 33  ? 0.9401 0.8696 0.4974 -0.1716 -0.0438 -0.1390 189 VAL   B CG1 
2936 C  CG2 . VAL   B 33  ? 1.0171 0.9138 0.5684 -0.1758 -0.0211 -0.1693 189 VAL   B CG2 
2937 N  N   . VAL   B 34  ? 0.9648 0.8805 0.5607 -0.1639 -0.0573 -0.1323 190 VAL   B N   
2938 C  CA  . VAL   B 34  ? 0.8482 0.7782 0.4542 -0.1608 -0.0708 -0.1161 190 VAL   B CA  
2939 C  C   . VAL   B 34  ? 0.9816 0.9244 0.5956 -0.1686 -0.0809 -0.1142 190 VAL   B C   
2940 O  O   . VAL   B 34  ? 0.9443 0.9094 0.5622 -0.1705 -0.0936 -0.1003 190 VAL   B O   
2941 C  CB  . VAL   B 34  ? 0.9581 0.8741 0.5884 -0.1434 -0.0660 -0.1093 190 VAL   B CB  
2942 C  CG1 . VAL   B 34  ? 0.8523 0.7821 0.5028 -0.1371 -0.0776 -0.0925 190 VAL   B CG1 
2943 C  CG2 . VAL   B 34  ? 0.9845 0.8948 0.6125 -0.1340 -0.0577 -0.1062 190 VAL   B CG2 
2944 N  N   . ASP   B 35  ? 1.0838 1.0134 0.7011 -0.1731 -0.0752 -0.1275 191 ASP   B N   
2945 C  CA  . ASP   B 35  ? 1.0331 0.9743 0.6580 -0.1813 -0.0839 -0.1266 191 ASP   B CA  
2946 C  C   . ASP   B 35  ? 0.9497 0.9150 0.5639 -0.1927 -0.0909 -0.1237 191 ASP   B C   
2947 O  O   . ASP   B 35  ? 1.1027 1.0899 0.7235 -0.1966 -0.1032 -0.1127 191 ASP   B O   
2948 C  CB  . ASP   B 35  ? 0.9904 0.9104 0.6201 -0.1839 -0.0747 -0.1417 191 ASP   B CB  
2949 C  CG  . ASP   B 35  ? 1.0560 0.9569 0.7011 -0.1738 -0.0712 -0.1414 191 ASP   B CG  
2950 O  OD1 . ASP   B 35  ? 1.1430 1.0496 0.7983 -0.1653 -0.0778 -0.1286 191 ASP   B OD1 
2951 O  OD2 . ASP   B 35  ? 1.1722 1.0522 0.8214 -0.1731 -0.0611 -0.1531 191 ASP   B OD2 
2952 N  N   . HIS   B 36  ? 1.0484 1.0102 0.6464 -0.1982 -0.0828 -0.1335 192 HIS   B N   
2953 C  CA  . HIS   B 36  ? 0.9816 0.9661 0.5674 -0.2091 -0.0888 -0.1307 192 HIS   B CA  
2954 C  C   . HIS   B 36  ? 1.0256 1.0346 0.6123 -0.2057 -0.1001 -0.1116 192 HIS   B C   
2955 O  O   . HIS   B 36  ? 0.8967 0.9303 0.4838 -0.2128 -0.1108 -0.1024 192 HIS   B O   
2956 C  CB  . HIS   B 36  ? 1.0648 1.0394 0.6325 -0.2139 -0.0770 -0.1440 192 HIS   B CB  
2957 C  CG  . HIS   B 36  ? 1.0933 1.0494 0.6579 -0.2208 -0.0672 -0.1619 192 HIS   B CG  
2958 N  ND1 . HIS   B 36  ? 1.1511 1.1170 0.7124 -0.2341 -0.0716 -0.1666 192 HIS   B ND1 
2959 C  CD2 . HIS   B 36  ? 1.0714 0.9997 0.6366 -0.2160 -0.0531 -0.1753 192 HIS   B CD2 
2960 C  CE1 . HIS   B 36  ? 1.0175 0.9615 0.5764 -0.2376 -0.0603 -0.1826 192 HIS   B CE1 
2961 N  NE2 . HIS   B 36  ? 1.2324 1.1534 0.7944 -0.2263 -0.0490 -0.1878 192 HIS   B NE2 
2962 N  N   . LEU   B 37  ? 0.8274 0.8303 0.4140 -0.1951 -0.0973 -0.1050 193 LEU   B N   
2963 C  CA  . LEU   B 37  ? 0.9113 0.9357 0.4988 -0.1913 -0.1068 -0.0862 193 LEU   B CA  
2964 C  C   . LEU   B 37  ? 0.8445 0.8840 0.4497 -0.1883 -0.1197 -0.0713 193 LEU   B C   
2965 O  O   . LEU   B 37  ? 0.7474 0.8123 0.3549 -0.1918 -0.1301 -0.0581 193 LEU   B O   
2966 C  CB  . LEU   B 37  ? 0.7756 0.7883 0.3602 -0.1806 -0.1005 -0.0823 193 LEU   B CB  
2967 C  CG  . LEU   B 37  ? 0.8494 0.8540 0.4165 -0.1827 -0.0891 -0.0924 193 LEU   B CG  
2968 C  CD1 . LEU   B 37  ? 0.8814 0.8736 0.4478 -0.1717 -0.0823 -0.0887 193 LEU   B CD1 
2969 C  CD2 . LEU   B 37  ? 0.9517 0.9792 0.5062 -0.1915 -0.0940 -0.0868 193 LEU   B CD2 
2970 N  N   . LEU   B 38  ? 0.7867 0.8112 0.4053 -0.1817 -0.1189 -0.0731 194 LEU   B N   
2971 C  CA  . LEU   B 38  ? 0.8095 0.8473 0.4462 -0.1780 -0.1304 -0.0591 194 LEU   B CA  
2972 C  C   . LEU   B 38  ? 0.8288 0.8869 0.4694 -0.1884 -0.1383 -0.0580 194 LEU   B C   
2973 O  O   . LEU   B 38  ? 0.8945 0.9753 0.5465 -0.1868 -0.1495 -0.0419 194 LEU   B O   
2974 C  CB  . LEU   B 38  ? 0.8228 0.8391 0.4737 -0.1697 -0.1264 -0.0633 194 LEU   B CB  
2975 C  CG  . LEU   B 38  ? 0.8041 0.8048 0.4640 -0.1536 -0.1181 -0.0580 194 LEU   B CG  
2976 C  CD1 . LEU   B 38  ? 0.8306 0.8092 0.5093 -0.1430 -0.1106 -0.0629 194 LEU   B CD1 
2977 C  CD2 . LEU   B 38  ? 0.7781 0.7964 0.4479 -0.1452 -0.1261 -0.0368 194 LEU   B CD2 
2978 N  N   . LEU   B 39  ? 0.9404 0.9912 0.5718 -0.1989 -0.1324 -0.0745 195 LEU   B N   
2979 C  CA  . LEU   B 39  ? 0.8438 0.9140 0.4770 -0.2104 -0.1395 -0.0742 195 LEU   B CA  
2980 C  C   . LEU   B 39  ? 0.8631 0.9615 0.4892 -0.2152 -0.1474 -0.0619 195 LEU   B C   
2981 O  O   . LEU   B 39  ? 0.8996 1.0225 0.5362 -0.2175 -0.1582 -0.0490 195 LEU   B O   
2982 C  CB  . LEU   B 39  ? 0.9530 1.0073 0.5762 -0.2210 -0.1304 -0.0947 195 LEU   B CB  
2983 C  CG  . LEU   B 39  ? 0.9397 0.9842 0.5764 -0.2230 -0.1302 -0.1014 195 LEU   B CG  
2984 C  CD1 . LEU   B 39  ? 0.8746 0.9017 0.5256 -0.2102 -0.1281 -0.0986 195 LEU   B CD1 
2985 C  CD2 . LEU   B 39  ? 0.9794 1.0055 0.6061 -0.2329 -0.1198 -0.1213 195 LEU   B CD2 
2986 N  N   . ARG   B 40  ? 0.8623 0.9585 0.4714 -0.2167 -0.1418 -0.0650 196 ARG   B N   
2987 C  CA  . ARG   B 40  ? 0.8251 0.9477 0.4273 -0.2210 -0.1488 -0.0525 196 ARG   B CA  
2988 C  C   . ARG   B 40  ? 0.8712 1.0102 0.4873 -0.2098 -0.1580 -0.0296 196 ARG   B C   
2989 O  O   . ARG   B 40  ? 0.9064 1.0722 0.5277 -0.2125 -0.1677 -0.0152 196 ARG   B O   
2990 C  CB  . ARG   B 40  ? 0.8171 0.9329 0.3987 -0.2242 -0.1402 -0.0604 196 ARG   B CB  
2991 C  CG  . ARG   B 40  ? 0.8703 1.0142 0.4433 -0.2319 -0.1474 -0.0498 196 ARG   B CG  
2992 C  CD  . ARG   B 40  ? 1.0646 1.2222 0.6308 -0.2479 -0.1504 -0.0575 196 ARG   B CD  
2993 N  NE  . ARG   B 40  ? 1.1384 1.2719 0.6987 -0.2539 -0.1406 -0.0793 196 ARG   B NE  
2994 C  CZ  . ARG   B 40  ? 1.2032 1.3361 0.7696 -0.2615 -0.1423 -0.0866 196 ARG   B CZ  
2995 N  NH1 . ARG   B 40  ? 1.1094 1.2678 0.6852 -0.2670 -0.1538 -0.0756 196 ARG   B NH1 
2996 N  NH2 . ARG   B 40  ? 1.2225 1.3292 0.7852 -0.2640 -0.1318 -0.1054 196 ARG   B NH2 
2997 N  N   . LEU   B 41  ? 0.7696 0.8929 0.3905 -0.1974 -0.1543 -0.0257 197 LEU   B N   
2998 C  CA  . LEU   B 41  ? 0.8199 0.9553 0.4547 -0.1859 -0.1617 -0.0040 197 LEU   B CA  
2999 C  C   . LEU   B 41  ? 0.8147 0.9677 0.4701 -0.1840 -0.1722 0.0083  197 LEU   B C   
3000 O  O   . LEU   B 41  ? 0.7563 0.9312 0.4216 -0.1797 -0.1804 0.0275  197 LEU   B O   
3001 C  CB  . LEU   B 41  ? 0.7295 0.8420 0.3679 -0.1737 -0.1557 -0.0039 197 LEU   B CB  
3002 C  CG  . LEU   B 41  ? 0.8164 0.9172 0.4377 -0.1723 -0.1467 -0.0086 197 LEU   B CG  
3003 C  CD1 . LEU   B 41  ? 0.7291 0.8043 0.3527 -0.1625 -0.1391 -0.0129 197 LEU   B CD1 
3004 C  CD2 . LEU   B 41  ? 0.7026 0.8242 0.3225 -0.1700 -0.1523 0.0099  197 LEU   B CD2 
3005 N  N   . LYS   B 42  ? 0.7273 0.8708 0.3908 -0.1865 -0.1715 -0.0019 198 LYS   B N   
3006 C  CA  . LYS   B 42  ? 0.8407 1.0010 0.5246 -0.1850 -0.1808 0.0088  198 LYS   B CA  
3007 C  C   . LYS   B 42  ? 0.8234 1.0124 0.5068 -0.1952 -0.1884 0.0148  198 LYS   B C   
3008 O  O   . LYS   B 42  ? 1.0087 1.2159 0.7099 -0.1936 -0.1965 0.0262  198 LYS   B O   
3009 C  CB  . LYS   B 42  ? 0.7797 0.9228 0.4712 -0.1866 -0.1777 -0.0046 198 LYS   B CB  
3010 C  CG  . LYS   B 42  ? 0.9447 1.0602 0.6388 -0.1766 -0.1709 -0.0098 198 LYS   B CG  
3011 C  CD  . LYS   B 42  ? 0.8481 0.9449 0.5482 -0.1794 -0.1666 -0.0245 198 LYS   B CD  
3012 C  CE  . LYS   B 42  ? 0.8215 0.9219 0.5461 -0.1701 -0.1723 -0.0132 198 LYS   B CE  
3013 N  NZ  . LYS   B 42  ? 0.9439 1.0477 0.6766 -0.1786 -0.1750 -0.0206 198 LYS   B NZ  
3014 N  N   . CYS   B 43  ? 0.7342 0.9285 0.3981 -0.2056 -0.1859 0.0080  199 CYS   B N   
3015 C  CA  . CYS   B 43  ? 0.8132 1.0361 0.4751 -0.2159 -0.1933 0.0148  199 CYS   B CA  
3016 C  C   . CYS   B 43  ? 0.7539 0.9990 0.4201 -0.2096 -0.1997 0.0365  199 CYS   B C   
3017 O  O   . CYS   B 43  ? 0.9086 1.1811 0.5792 -0.2153 -0.2076 0.0473  199 CYS   B O   
3018 C  CB  . CYS   B 43  ? 0.8908 1.1091 0.5294 -0.2313 -0.1873 -0.0034 199 CYS   B CB  
3019 S  SG  . CYS   B 43  ? 1.0893 1.2841 0.7245 -0.2404 -0.1798 -0.0278 199 CYS   B SG  
3020 N  N   . ASP   B 44  ? 0.7825 1.0165 0.4477 -0.1983 -0.1962 0.0434  200 ASP   B N   
3021 C  CA  . ASP   B 44  ? 0.7845 1.0368 0.4581 -0.1898 -0.2019 0.0660  200 ASP   B CA  
3022 C  C   . ASP   B 44  ? 0.7037 0.9633 0.4044 -0.1773 -0.2079 0.0827  200 ASP   B C   
3023 O  O   . ASP   B 44  ? 0.6936 0.9342 0.4037 -0.1686 -0.2048 0.0794  200 ASP   B O   
3024 C  CB  . ASP   B 44  ? 0.7780 1.0149 0.4407 -0.1827 -0.1952 0.0673  200 ASP   B CB  
3025 C  CG  . ASP   B 44  ? 0.7605 1.0170 0.4259 -0.1781 -0.1998 0.0879  200 ASP   B CG  
3026 O  OD1 . ASP   B 44  ? 0.8174 1.0764 0.5014 -0.1648 -0.2029 0.1055  200 ASP   B OD1 
3027 O  OD2 . ASP   B 44  ? 0.7995 1.0678 0.4489 -0.1875 -0.1998 0.0867  200 ASP   B OD2 
3028 N  N   . SER   B 45  ? 0.8057 1.0931 0.5194 -0.1762 -0.2162 0.1007  201 SER   B N   
3029 C  CA  . SER   B 45  ? 0.7103 1.0061 0.4514 -0.1638 -0.2212 0.1173  201 SER   B CA  
3030 C  C   . SER   B 45  ? 0.7172 0.9954 0.4675 -0.1472 -0.2172 0.1270  201 SER   B C   
3031 O  O   . SER   B 45  ? 0.7332 1.0049 0.5032 -0.1367 -0.2177 0.1326  201 SER   B O   
3032 C  CB  . SER   B 45  ? 0.7033 1.0321 0.4564 -0.1644 -0.2296 0.1364  201 SER   B CB  
3033 O  OG  . SER   B 45  ? 0.7287 1.0651 0.4778 -0.1597 -0.2297 0.1507  201 SER   B OG  
3034 N  N   . ALA   B 46  ? 0.7370 1.0066 0.4731 -0.1453 -0.2128 0.1286  202 ALA   B N   
3035 C  CA  . ALA   B 46  ? 0.7002 0.9522 0.4437 -0.1306 -0.2084 0.1376  202 ALA   B CA  
3036 C  C   . ALA   B 46  ? 0.6881 0.9107 0.4264 -0.1283 -0.2015 0.1217  202 ALA   B C   
3037 O  O   . ALA   B 46  ? 0.6715 0.8796 0.4215 -0.1157 -0.1988 0.1292  202 ALA   B O   
3038 C  CB  . ALA   B 46  ? 0.7248 0.9780 0.4550 -0.1299 -0.2057 0.1450  202 ALA   B CB  
3039 N  N   . PHE   B 47  ? 0.6773 0.8899 0.3987 -0.1401 -0.1980 0.1002  203 PHE   B N   
3040 C  CA  . PHE   B 47  ? 0.7051 0.8897 0.4214 -0.1385 -0.1910 0.0845  203 PHE   B CA  
3041 C  C   . PHE   B 47  ? 0.7290 0.9104 0.4541 -0.1427 -0.1928 0.0736  203 PHE   B C   
3042 O  O   . PHE   B 47  ? 0.6995 0.8586 0.4172 -0.1452 -0.1867 0.0567  203 PHE   B O   
3043 C  CB  . PHE   B 47  ? 0.7107 0.8804 0.4011 -0.1467 -0.1827 0.0675  203 PHE   B CB  
3044 C  CG  . PHE   B 47  ? 0.7033 0.8712 0.3849 -0.1416 -0.1794 0.0769  203 PHE   B CG  
3045 C  CD1 . PHE   B 47  ? 0.7437 0.8933 0.4294 -0.1305 -0.1748 0.0819  203 PHE   B CD1 
3046 C  CD2 . PHE   B 47  ? 0.7411 0.9253 0.4101 -0.1486 -0.1806 0.0805  203 PHE   B CD2 
3047 C  CE1 . PHE   B 47  ? 0.7583 0.9058 0.4364 -0.1263 -0.1713 0.0906  203 PHE   B CE1 
3048 C  CE2 . PHE   B 47  ? 0.7421 0.9246 0.4034 -0.1441 -0.1772 0.0892  203 PHE   B CE2 
3049 C  CZ  . PHE   B 47  ? 0.7157 0.8796 0.3819 -0.1329 -0.1723 0.0943  203 PHE   B CZ  
3050 N  N   . ARG   B 48  ? 0.7650 0.9683 0.5068 -0.1432 -0.2006 0.0835  204 ARG   B N   
3051 C  CA  . ARG   B 48  ? 0.7227 0.9272 0.4716 -0.1497 -0.2027 0.0732  204 ARG   B CA  
3052 C  C   . ARG   B 48  ? 0.7739 0.9535 0.5291 -0.1439 -0.1982 0.0642  204 ARG   B C   
3053 O  O   . ARG   B 48  ? 0.8619 1.0278 0.6095 -0.1521 -0.1943 0.0460  204 ARG   B O   
3054 C  CB  . ARG   B 48  ? 0.7303 0.9620 0.5013 -0.1469 -0.2114 0.0897  204 ARG   B CB  
3055 C  CG  . ARG   B 48  ? 0.7972 1.0349 0.5760 -0.1552 -0.2142 0.0806  204 ARG   B CG  
3056 C  CD  . ARG   B 48  ? 0.8031 1.0445 0.5615 -0.1728 -0.2131 0.0644  204 ARG   B CD  
3057 N  NE  . ARG   B 48  ? 0.8227 1.0949 0.5855 -0.1801 -0.2206 0.0740  204 ARG   B NE  
3058 C  CZ  . ARG   B 48  ? 0.8443 1.1281 0.5895 -0.1919 -0.2213 0.0704  204 ARG   B CZ  
3059 N  NH1 . ARG   B 48  ? 0.9576 1.2250 0.6799 -0.1971 -0.2146 0.0575  204 ARG   B NH1 
3060 N  NH2 . ARG   B 48  ? 0.8934 1.2065 0.6442 -0.1986 -0.2287 0.0802  204 ARG   B NH2 
3061 N  N   . GLY   B 49  ? 0.7324 0.9036 0.5027 -0.1290 -0.1970 0.0764  205 GLY   B N   
3062 C  CA  . GLY   B 49  ? 0.7349 0.8790 0.5194 -0.1190 -0.1874 0.0673  205 GLY   B CA  
3063 C  C   . GLY   B 49  ? 0.7224 0.8369 0.4954 -0.1151 -0.1754 0.0547  205 GLY   B C   
3064 O  O   . GLY   B 49  ? 0.6652 0.7596 0.4521 -0.1028 -0.1678 0.0539  205 GLY   B O   
3065 N  N   . VAL   B 50  ? 0.6940 0.8062 0.4420 -0.1254 -0.1734 0.0447  206 VAL   B N   
3066 C  CA  . VAL   B 50  ? 0.6424 0.7285 0.3801 -0.1215 -0.1616 0.0333  206 VAL   B CA  
3067 C  C   . VAL   B 50  ? 0.7233 0.7871 0.4626 -0.1229 -0.1537 0.0146  206 VAL   B C   
3068 O  O   . VAL   B 50  ? 0.7462 0.8147 0.4820 -0.1335 -0.1567 0.0052  206 VAL   B O   
3069 C  CB  . VAL   B 50  ? 0.6169 0.7084 0.3277 -0.1315 -0.1612 0.0292  206 VAL   B CB  
3070 C  CG1 . VAL   B 50  ? 0.7059 0.8021 0.3971 -0.1489 -0.1627 0.0129  206 VAL   B CG1 
3071 C  CG2 . VAL   B 50  ? 0.7107 0.7780 0.4150 -0.1244 -0.1492 0.0223  206 VAL   B CG2 
3072 N  N   . GLY   B 51  ? 0.6206 0.6606 0.3661 -0.1123 -0.1435 0.0101  207 GLY   B N   
3073 C  CA  . GLY   B 51  ? 0.7032 0.7216 0.4504 -0.1124 -0.1351 -0.0062 207 GLY   B CA  
3074 C  C   . GLY   B 51  ? 0.6991 0.6952 0.4451 -0.1034 -0.1239 -0.0111 207 GLY   B C   
3075 O  O   . GLY   B 51  ? 0.7524 0.7490 0.4973 -0.0970 -0.1226 -0.0021 207 GLY   B O   
3076 N  N   . LEU   B 52  ? 0.7465 0.7231 0.4934 -0.1030 -0.1158 -0.0250 208 LEU   B N   
3077 C  CA  . LEU   B 52  ? 0.7463 0.7032 0.4920 -0.0953 -0.1049 -0.0306 208 LEU   B CA  
3078 C  C   . LEU   B 52  ? 0.7279 0.6784 0.4943 -0.0816 -0.1031 -0.0210 208 LEU   B C   
3079 O  O   . LEU   B 52  ? 0.7756 0.7314 0.5584 -0.0779 -0.1079 -0.0145 208 LEU   B O   
3080 C  CB  . LEU   B 52  ? 0.8212 0.7600 0.5616 -0.0991 -0.0964 -0.0478 208 LEU   B CB  
3081 C  CG  . LEU   B 52  ? 0.8607 0.7904 0.5804 -0.1045 -0.0882 -0.0597 208 LEU   B CG  
3082 C  CD1 . LEU   B 52  ? 0.9378 0.8454 0.6606 -0.1020 -0.0775 -0.0731 208 LEU   B CD1 
3083 C  CD2 . LEU   B 52  ? 0.8161 0.7476 0.5297 -0.0990 -0.0854 -0.0526 208 LEU   B CD2 
3084 N  N   . LEU   B 53  ? 0.6968 0.6365 0.4620 -0.0745 -0.0958 -0.0204 209 LEU   B N   
3085 C  CA  . LEU   B 53  ? 0.7698 0.7003 0.5526 -0.0627 -0.0921 -0.0146 209 LEU   B CA  
3086 C  C   . LEU   B 53  ? 0.8097 0.7221 0.5915 -0.0591 -0.0815 -0.0251 209 LEU   B C   
3087 O  O   . LEU   B 53  ? 0.8310 0.7384 0.5979 -0.0635 -0.0762 -0.0337 209 LEU   B O   
3088 C  CB  . LEU   B 53  ? 0.6538 0.5904 0.4395 -0.0568 -0.0941 -0.0007 209 LEU   B CB  
3089 C  CG  . LEU   B 53  ? 0.8165 0.7445 0.6206 -0.0459 -0.0909 0.0056  209 LEU   B CG  
3090 C  CD1 . LEU   B 53  ? 0.7336 0.6629 0.5540 -0.0434 -0.0942 0.0064  209 LEU   B CD1 
3091 C  CD2 . LEU   B 53  ? 0.7239 0.6581 0.5311 -0.0413 -0.0934 0.0199  209 LEU   B CD2 
3092 N  N   . TYR   B 59  ? 1.0902 0.9508 0.8176 -0.0723 -0.0394 -0.0833 215 TYR   B N   
3093 C  CA  . TYR   B 59  ? 0.9264 0.7827 0.6461 -0.0688 -0.0303 -0.0858 215 TYR   B CA  
3094 C  C   . TYR   B 59  ? 0.9644 0.8163 0.7008 -0.0569 -0.0263 -0.0787 215 TYR   B C   
3095 O  O   . TYR   B 59  ? 1.0009 0.8463 0.7528 -0.0514 -0.0257 -0.0779 215 TYR   B O   
3096 C  CB  . TYR   B 59  ? 0.9578 0.8008 0.6662 -0.0728 -0.0196 -0.1011 215 TYR   B CB  
3097 C  CG  . TYR   B 59  ? 1.0195 0.8467 0.7421 -0.0646 -0.0108 -0.1056 215 TYR   B CG  
3098 C  CD1 . TYR   B 59  ? 0.9779 0.7969 0.7087 -0.0660 -0.0118 -0.1101 215 TYR   B CD1 
3099 C  CD2 . TYR   B 59  ? 1.0425 0.8643 0.7706 -0.0555 -0.0014 -0.1046 215 TYR   B CD2 
3100 C  CE1 . TYR   B 59  ? 0.9822 0.7875 0.7263 -0.0583 -0.0038 -0.1128 215 TYR   B CE1 
3101 C  CE2 . TYR   B 59  ? 0.9637 0.7732 0.7057 -0.0476 0.0062  -0.1071 215 TYR   B CE2 
3102 C  CZ  . TYR   B 59  ? 1.0949 0.8959 0.8446 -0.0489 0.0051  -0.1110 215 TYR   B CZ  
3103 O  OH  . TYR   B 59  ? 1.0928 0.8821 0.8564 -0.0409 0.0127  -0.1122 215 TYR   B OH  
3104 N  N   . GLU   B 60  ? 0.9536 0.8102 0.6861 -0.0539 -0.0236 -0.0734 216 GLU   B N   
3105 C  CA  . GLU   B 60  ? 0.8270 0.6810 0.5724 -0.0443 -0.0190 -0.0675 216 GLU   B CA  
3106 C  C   . GLU   B 60  ? 0.8246 0.6786 0.5593 -0.0439 -0.0103 -0.0705 216 GLU   B C   
3107 O  O   . GLU   B 60  ? 0.8095 0.6667 0.5267 -0.0509 -0.0091 -0.0755 216 GLU   B O   
3108 C  CB  . GLU   B 60  ? 0.9767 0.8394 0.7321 -0.0411 -0.0273 -0.0540 216 GLU   B CB  
3109 C  CG  . GLU   B 60  ? 0.8757 0.7403 0.6417 -0.0416 -0.0359 -0.0504 216 GLU   B CG  
3110 C  CD  . GLU   B 60  ? 1.0158 0.8730 0.7999 -0.0345 -0.0338 -0.0498 216 GLU   B CD  
3111 O  OE1 . GLU   B 60  ? 0.9990 0.8553 0.7918 -0.0282 -0.0307 -0.0448 216 GLU   B OE1 
3112 O  OE2 . GLU   B 60  ? 0.9891 0.8423 0.7783 -0.0359 -0.0355 -0.0543 216 GLU   B OE2 
3113 N  N   . HIS   B 61  ? 0.7781 0.6296 0.5232 -0.0360 -0.0040 -0.0675 217 HIS   B N   
3114 C  CA  . HIS   B 61  ? 0.8069 0.6601 0.5446 -0.0347 0.0046  -0.0689 217 HIS   B CA  
3115 C  C   . HIS   B 61  ? 0.8389 0.6998 0.5835 -0.0309 0.0025  -0.0573 217 HIS   B C   
3116 O  O   . HIS   B 61  ? 0.9291 0.7890 0.6896 -0.0251 0.0014  -0.0519 217 HIS   B O   
3117 C  CB  . HIS   B 61  ? 0.8740 0.7175 0.6172 -0.0291 0.0162  -0.0770 217 HIS   B CB  
3118 C  CG  . HIS   B 61  ? 0.7868 0.6206 0.5198 -0.0336 0.0211  -0.0897 217 HIS   B CG  
3119 N  ND1 . HIS   B 61  ? 0.8660 0.6929 0.6024 -0.0362 0.0169  -0.0939 217 HIS   B ND1 
3120 C  CD2 . HIS   B 61  ? 0.8641 0.6933 0.5832 -0.0366 0.0305  -0.0998 217 HIS   B CD2 
3121 C  CE1 . HIS   B 61  ? 0.8570 0.6748 0.5818 -0.0411 0.0233  -0.1062 217 HIS   B CE1 
3122 N  NE2 . HIS   B 61  ? 0.8180 0.6366 0.5319 -0.0413 0.0319  -0.1103 217 HIS   B NE2 
3123 N  N   . VAL   B 62  ? 0.8463 0.7151 0.5785 -0.0348 0.0022  -0.0537 218 VAL   B N   
3124 C  CA  . VAL   B 62  ? 0.8486 0.7237 0.5859 -0.0322 0.0019  -0.0434 218 VAL   B CA  
3125 C  C   . VAL   B 62  ? 0.8030 0.6772 0.5452 -0.0271 0.0125  -0.0459 218 VAL   B C   
3126 O  O   . VAL   B 62  ? 0.7590 0.6353 0.5140 -0.0226 0.0133  -0.0395 218 VAL   B O   
3127 C  CB  . VAL   B 62  ? 0.7545 0.6386 0.4768 -0.0384 -0.0022 -0.0375 218 VAL   B CB  
3128 C  CG1 . VAL   B 62  ? 0.8699 0.7588 0.5975 -0.0360 -0.0010 -0.0275 218 VAL   B CG1 
3129 C  CG2 . VAL   B 62  ? 0.7980 0.6856 0.5179 -0.0426 -0.0133 -0.0328 218 VAL   B CG2 
3130 N  N   . LYS   B 63  ? 0.6964 0.5684 0.4282 -0.0283 0.0212  -0.0551 219 LYS   B N   
3131 C  CA  . LYS   B 63  ? 0.6795 0.5519 0.4163 -0.0230 0.0323  -0.0576 219 LYS   B CA  
3132 C  C   . LYS   B 63  ? 0.8292 0.6917 0.5759 -0.0174 0.0382  -0.0654 219 LYS   B C   
3133 O  O   . LYS   B 63  ? 0.7316 0.5863 0.4693 -0.0197 0.0425  -0.0757 219 LYS   B O   
3134 C  CB  . LYS   B 63  ? 0.7796 0.6560 0.4993 -0.0269 0.0397  -0.0623 219 LYS   B CB  
3135 C  CG  . LYS   B 63  ? 0.7569 0.6439 0.4672 -0.0318 0.0357  -0.0534 219 LYS   B CG  
3136 C  CD  . LYS   B 63  ? 0.7291 0.6200 0.4222 -0.0357 0.0442  -0.0593 219 LYS   B CD  
3137 C  CE  . LYS   B 63  ? 0.7792 0.6719 0.4801 -0.0294 0.0563  -0.0611 219 LYS   B CE  
3138 N  NZ  . LYS   B 63  ? 0.9374 0.8345 0.6215 -0.0329 0.0657  -0.0669 219 LYS   B NZ  
3139 N  N   . ILE   B 64  ? 0.6806 0.5437 0.4456 -0.0106 0.0388  -0.0604 220 ILE   B N   
3140 C  CA  . ILE   B 64  ? 0.6446 0.5001 0.4216 -0.0041 0.0450  -0.0651 220 ILE   B CA  
3141 C  C   . ILE   B 64  ? 0.6381 0.4895 0.4093 -0.0017 0.0577  -0.0738 220 ILE   B C   
3142 O  O   . ILE   B 64  ? 0.6701 0.5106 0.4435 0.0009  0.0631  -0.0814 220 ILE   B O   
3143 C  CB  . ILE   B 64  ? 0.6477 0.5092 0.4439 0.0023  0.0444  -0.0565 220 ILE   B CB  
3144 C  CG1 . ILE   B 64  ? 0.6576 0.5117 0.4675 0.0077  0.0450  -0.0583 220 ILE   B CG1 
3145 C  CG2 . ILE   B 64  ? 0.6404 0.5108 0.4409 0.0064  0.0532  -0.0538 220 ILE   B CG2 
3146 C  CD1 . ILE   B 64  ? 0.8092 0.6585 0.6208 0.0045  0.0347  -0.0573 220 ILE   B CD1 
3147 N  N   . SER   B 65  ? 0.6777 0.5370 0.4414 -0.0026 0.0633  -0.0728 221 SER   B N   
3148 C  CA  . SER   B 65  ? 0.7399 0.5967 0.4992 0.0005  0.0767  -0.0803 221 SER   B CA  
3149 C  C   . SER   B 65  ? 0.7420 0.5927 0.4793 -0.0070 0.0797  -0.0910 221 SER   B C   
3150 O  O   . SER   B 65  ? 0.7892 0.6395 0.5191 -0.0060 0.0912  -0.0973 221 SER   B O   
3151 C  CB  . SER   B 65  ? 0.7953 0.6657 0.5590 0.0035  0.0821  -0.0735 221 SER   B CB  
3152 O  OG  . SER   B 65  ? 0.7835 0.6624 0.5340 -0.0039 0.0765  -0.0691 221 SER   B OG  
3153 N  N   . ALA   B 66  ? 0.7153 0.5628 0.4420 -0.0148 0.0699  -0.0930 222 ALA   B N   
3154 C  CA  . ALA   B 66  ? 0.8467 0.6905 0.5512 -0.0239 0.0709  -0.1027 222 ALA   B CA  
3155 C  C   . ALA   B 66  ? 0.9519 0.7851 0.6550 -0.0279 0.0649  -0.1087 222 ALA   B C   
3156 O  O   . ALA   B 66  ? 0.8970 0.7347 0.5941 -0.0348 0.0530  -0.1052 222 ALA   B O   
3157 C  CB  . ALA   B 66  ? 0.7965 0.6530 0.4868 -0.0315 0.0633  -0.0963 222 ALA   B CB  
3158 N  N   . PRO   B 67  ? 1.0337 0.8532 0.7436 -0.0237 0.0729  -0.1172 223 PRO   B N   
3159 C  CA  . PRO   B 67  ? 0.9392 0.7483 0.6498 -0.0275 0.0674  -0.1223 223 PRO   B CA  
3160 C  C   . PRO   B 67  ? 0.8956 0.7029 0.5840 -0.0400 0.0640  -0.1317 223 PRO   B C   
3161 O  O   . PRO   B 67  ? 0.9678 0.7723 0.6557 -0.0455 0.0553  -0.1328 223 PRO   B O   
3162 C  CB  . PRO   B 67  ? 0.9039 0.6980 0.6257 -0.0198 0.0795  -0.1292 223 PRO   B CB  
3163 C  CG  . PRO   B 67  ? 0.9019 0.6969 0.6197 -0.0154 0.0932  -0.1329 223 PRO   B CG  
3164 C  CD  . PRO   B 67  ? 0.9362 0.7490 0.6536 -0.0151 0.0880  -0.1219 223 PRO   B CD  
3165 N  N   . ASN   B 68  ? 0.9488 0.7587 0.6188 -0.0452 0.0706  -0.1383 224 ASN   B N   
3166 C  CA  . ASN   B 68  ? 0.9336 0.7442 0.5805 -0.0584 0.0673  -0.1471 224 ASN   B CA  
3167 C  C   . ASN   B 68  ? 0.9157 0.7440 0.5537 -0.0656 0.0535  -0.1369 224 ASN   B C   
3168 O  O   . ASN   B 68  ? 0.8631 0.6957 0.4814 -0.0771 0.0494  -0.1425 224 ASN   B O   
3169 C  CB  . ASN   B 68  ? 1.0408 0.8464 0.6700 -0.0617 0.0814  -0.1598 224 ASN   B CB  
3170 C  CG  . ASN   B 68  ? 1.1061 0.8913 0.7397 -0.0575 0.0955  -0.1728 224 ASN   B CG  
3171 O  OD1 . ASN   B 68  ? 1.0822 0.8560 0.7243 -0.0574 0.0932  -0.1759 224 ASN   B OD1 
3172 N  ND2 . ASN   B 68  ? 1.0895 0.8696 0.7169 -0.0543 0.1108  -0.1806 224 ASN   B ND2 
3173 N  N   . GLU   B 69  ? 0.8689 0.7073 0.5205 -0.0593 0.0464  -0.1222 225 GLU   B N   
3174 C  CA  . GLU   B 69  ? 0.7587 0.6127 0.4048 -0.0643 0.0341  -0.1106 225 GLU   B CA  
3175 C  C   . GLU   B 69  ? 0.7474 0.6030 0.4082 -0.0626 0.0218  -0.1019 225 GLU   B C   
3176 O  O   . GLU   B 69  ? 0.8432 0.6980 0.5230 -0.0539 0.0205  -0.0937 225 GLU   B O   
3177 C  CB  . GLU   B 69  ? 0.7666 0.6299 0.4151 -0.0594 0.0372  -0.1012 225 GLU   B CB  
3178 C  CG  . GLU   B 69  ? 0.7664 0.6296 0.3984 -0.0622 0.0494  -0.1103 225 GLU   B CG  
3179 C  CD  . GLU   B 69  ? 0.8689 0.7428 0.5013 -0.0589 0.0528  -0.1013 225 GLU   B CD  
3180 O  OE1 . GLU   B 69  ? 0.9418 0.8147 0.5666 -0.0581 0.0650  -0.1082 225 GLU   B OE1 
3181 O  OE2 . GLU   B 69  ? 0.8967 0.7788 0.5387 -0.0566 0.0443  -0.0876 225 GLU   B OE2 
3182 N  N   . PHE   B 70  ? 0.6727 0.5314 0.3249 -0.0714 0.0130  -0.1040 226 PHE   B N   
3183 C  CA  . PHE   B 70  ? 0.6943 0.5542 0.3599 -0.0704 0.0022  -0.0974 226 PHE   B CA  
3184 C  C   . PHE   B 70  ? 0.7731 0.6487 0.4381 -0.0728 -0.0099 -0.0833 226 PHE   B C   
3185 O  O   . PHE   B 70  ? 0.8118 0.6980 0.4612 -0.0787 -0.0119 -0.0804 226 PHE   B O   
3186 C  CB  . PHE   B 70  ? 0.7916 0.6456 0.4508 -0.0785 0.0001  -0.1081 226 PHE   B CB  
3187 C  CG  . PHE   B 70  ? 0.8305 0.6664 0.4935 -0.0754 0.0116  -0.1209 226 PHE   B CG  
3188 C  CD1 . PHE   B 70  ? 0.7958 0.6240 0.4441 -0.0786 0.0235  -0.1334 226 PHE   B CD1 
3189 C  CD2 . PHE   B 70  ? 0.8321 0.6588 0.5135 -0.0693 0.0111  -0.1201 226 PHE   B CD2 
3190 C  CE1 . PHE   B 70  ? 0.9484 0.7587 0.6010 -0.0752 0.0350  -0.1447 226 PHE   B CE1 
3191 C  CE2 . PHE   B 70  ? 0.9203 0.7300 0.6060 -0.0661 0.0220  -0.1307 226 PHE   B CE2 
3192 C  CZ  . PHE   B 70  ? 0.8635 0.6645 0.5353 -0.0687 0.0342  -0.1429 226 PHE   B CZ  
3193 N  N   . ASP   B 71  ? 0.7711 0.6479 0.4533 -0.0680 -0.0177 -0.0744 227 ASP   B N   
3194 C  CA  . ASP   B 71  ? 0.7584 0.6478 0.4443 -0.0682 -0.0284 -0.0600 227 ASP   B CA  
3195 C  C   . ASP   B 71  ? 0.7596 0.6520 0.4536 -0.0703 -0.0383 -0.0574 227 ASP   B C   
3196 O  O   . ASP   B 71  ? 0.6973 0.5811 0.4062 -0.0654 -0.0376 -0.0596 227 ASP   B O   
3197 C  CB  . ASP   B 71  ? 0.7775 0.6660 0.4780 -0.0588 -0.0267 -0.0498 227 ASP   B CB  
3198 C  CG  . ASP   B 71  ? 0.8461 0.7455 0.5492 -0.0588 -0.0358 -0.0353 227 ASP   B CG  
3199 O  OD1 . ASP   B 71  ? 0.8629 0.7634 0.5791 -0.0562 -0.0429 -0.0289 227 ASP   B OD1 
3200 O  OD2 . ASP   B 71  ? 0.9249 0.8322 0.6160 -0.0621 -0.0355 -0.0304 227 ASP   B OD2 
3201 N  N   . VAL   B 72  ? 0.7089 0.6149 0.3935 -0.0778 -0.0475 -0.0520 228 VAL   B N   
3202 C  CA  . VAL   B 72  ? 0.6545 0.5666 0.3431 -0.0824 -0.0569 -0.0509 228 VAL   B CA  
3203 C  C   . VAL   B 72  ? 0.7383 0.6660 0.4319 -0.0816 -0.0676 -0.0343 228 VAL   B C   
3204 O  O   . VAL   B 72  ? 0.6910 0.6286 0.3736 -0.0842 -0.0693 -0.0273 228 VAL   B O   
3205 C  CB  . VAL   B 72  ? 0.7906 0.7052 0.4601 -0.0949 -0.0569 -0.0633 228 VAL   B CB  
3206 C  CG1 . VAL   B 72  ? 0.7651 0.6956 0.4329 -0.1028 -0.0694 -0.0577 228 VAL   B CG1 
3207 C  CG2 . VAL   B 72  ? 0.8044 0.7015 0.4760 -0.0948 -0.0482 -0.0786 228 VAL   B CG2 
3208 N  N   . MET   B 73  ? 0.6202 0.5503 0.3306 -0.0778 -0.0742 -0.0276 229 MET   B N   
3209 C  CA  . MET   B 73  ? 0.6927 0.6372 0.4098 -0.0762 -0.0838 -0.0116 229 MET   B CA  
3210 C  C   . MET   B 73  ? 0.6952 0.6520 0.4138 -0.0828 -0.0934 -0.0105 229 MET   B C   
3211 O  O   . MET   B 73  ? 0.6893 0.6398 0.4165 -0.0829 -0.0932 -0.0178 229 MET   B O   
3212 C  CB  . MET   B 73  ? 0.6164 0.5539 0.3537 -0.0645 -0.0825 -0.0020 229 MET   B CB  
3213 C  CG  . MET   B 73  ? 0.7389 0.6880 0.4884 -0.0611 -0.0915 0.0136  229 MET   B CG  
3214 S  SD  . MET   B 73  ? 0.7974 0.7369 0.5663 -0.0486 -0.0880 0.0247  229 MET   B SD  
3215 C  CE  . MET   B 73  ? 0.7910 0.7171 0.5519 -0.0469 -0.0767 0.0166  229 MET   B CE  
3216 N  N   . PHE   B 74  ? 0.5974 0.5730 0.3070 -0.0889 -0.1018 -0.0014 230 PHE   B N   
3217 C  CA  . PHE   B 74  ? 0.6936 0.6860 0.4058 -0.0951 -0.1124 0.0033  230 PHE   B CA  
3218 C  C   . PHE   B 74  ? 0.7481 0.7503 0.4788 -0.0865 -0.1192 0.0219  230 PHE   B C   
3219 O  O   . PHE   B 74  ? 0.6990 0.7098 0.4269 -0.0842 -0.1216 0.0348  230 PHE   B O   
3220 C  CB  . PHE   B 74  ? 0.6438 0.6535 0.3338 -0.1084 -0.1178 0.0020  230 PHE   B CB  
3221 C  CG  . PHE   B 74  ? 0.6816 0.6831 0.3526 -0.1190 -0.1118 -0.0175 230 PHE   B CG  
3222 C  CD1 . PHE   B 74  ? 0.8429 0.8222 0.5174 -0.1156 -0.1016 -0.0318 230 PHE   B CD1 
3223 C  CD2 . PHE   B 74  ? 0.7996 0.8162 0.4492 -0.1330 -0.1164 -0.0213 230 PHE   B CD2 
3224 C  CE1 . PHE   B 74  ? 0.7818 0.7523 0.4394 -0.1250 -0.0952 -0.0494 230 PHE   B CE1 
3225 C  CE2 . PHE   B 74  ? 0.8232 0.8311 0.4545 -0.1435 -0.1100 -0.0402 230 PHE   B CE2 
3226 C  CZ  . PHE   B 74  ? 0.7721 0.7558 0.4081 -0.1389 -0.0990 -0.0542 230 PHE   B CZ  
3227 N  N   . LYS   B 75  ? 0.6864 0.6878 0.4356 -0.0820 -0.1220 0.0239  231 LYS   B N   
3228 C  CA  . LYS   B 75  ? 0.6833 0.6931 0.4514 -0.0733 -0.1274 0.0408  231 LYS   B CA  
3229 C  C   . LYS   B 75  ? 0.6169 0.6511 0.3870 -0.0792 -0.1390 0.0501  231 LYS   B C   
3230 O  O   . LYS   B 75  ? 0.5976 0.6399 0.3598 -0.0897 -0.1429 0.0413  231 LYS   B O   
3231 C  CB  . LYS   B 75  ? 0.5990 0.5948 0.3878 -0.0638 -0.1232 0.0387  231 LYS   B CB  
3232 C  CG  . LYS   B 75  ? 0.6839 0.6811 0.4770 -0.0691 -0.1256 0.0292  231 LYS   B CG  
3233 C  CD  . LYS   B 75  ? 0.7759 0.7750 0.5922 -0.0612 -0.1280 0.0366  231 LYS   B CD  
3234 C  CE  . LYS   B 75  ? 0.7561 0.7636 0.5760 -0.0686 -0.1330 0.0304  231 LYS   B CE  
3235 N  NZ  . LYS   B 75  ? 0.7129 0.7379 0.5505 -0.0651 -0.1408 0.0438  231 LYS   B NZ  
3236 N  N   . LEU   B 76  ? 0.6049 0.6504 0.3878 -0.0720 -0.1440 0.0683  232 LEU   B N   
3237 C  CA  . LEU   B 76  ? 0.6495 0.7209 0.4378 -0.0755 -0.1552 0.0811  232 LEU   B CA  
3238 C  C   . LEU   B 76  ? 0.6445 0.7181 0.4579 -0.0624 -0.1565 0.0971  232 LEU   B C   
3239 O  O   . LEU   B 76  ? 0.6096 0.6764 0.4276 -0.0538 -0.1530 0.1075  232 LEU   B O   
3240 C  CB  . LEU   B 76  ? 0.6260 0.7156 0.3965 -0.0829 -0.1609 0.0896  232 LEU   B CB  
3241 C  CG  . LEU   B 76  ? 0.6628 0.7830 0.4378 -0.0868 -0.1733 0.1054  232 LEU   B CG  
3242 C  CD1 . LEU   B 76  ? 0.6616 0.7945 0.4329 -0.0988 -0.1793 0.0952  232 LEU   B CD1 
3243 C  CD2 . LEU   B 76  ? 0.7396 0.8751 0.4967 -0.0927 -0.1774 0.1149  232 LEU   B CD2 
3244 N  N   . GLU   B 77  ? 0.6081 0.6909 0.4377 -0.0611 -0.1611 0.0994  233 GLU   B N   
3245 C  CA  . GLU   B 77  ? 0.6557 0.7380 0.5096 -0.0479 -0.1604 0.1133  233 GLU   B CA  
3246 C  C   . GLU   B 77  ? 0.7042 0.8078 0.5629 -0.0447 -0.1677 0.1349  233 GLU   B C   
3247 O  O   . GLU   B 77  ? 0.6783 0.8068 0.5298 -0.0534 -0.1773 0.1409  233 GLU   B O   
3248 C  CB  . GLU   B 77  ? 0.6482 0.7343 0.5196 -0.0463 -0.1622 0.1103  233 GLU   B CB  
3249 C  CG  . GLU   B 77  ? 0.7009 0.7851 0.5977 -0.0318 -0.1600 0.1242  233 GLU   B CG  
3250 C  CD  . GLU   B 77  ? 0.8300 0.9165 0.7456 -0.0289 -0.1602 0.1213  233 GLU   B CD  
3251 O  OE1 . GLU   B 77  ? 0.7838 0.8766 0.6945 -0.0386 -0.1636 0.1105  233 GLU   B OE1 
3252 O  OE2 . GLU   B 77  ? 0.8304 0.9102 0.7655 -0.0169 -0.1557 0.1288  233 GLU   B OE2 
3253 N  N   . VAL   B 78  ? 0.7191 0.8126 0.5899 -0.0325 -0.1628 0.1466  234 VAL   B N   
3254 C  CA  . VAL   B 78  ? 0.6694 0.7797 0.5491 -0.0266 -0.1680 0.1691  234 VAL   B CA  
3255 C  C   . VAL   B 78  ? 0.7076 0.8164 0.6152 -0.0137 -0.1660 0.1792  234 VAL   B C   
3256 O  O   . VAL   B 78  ? 0.7433 0.8309 0.6610 -0.0032 -0.1571 0.1807  234 VAL   B O   
3257 C  CB  . VAL   B 78  ? 0.6765 0.7756 0.5460 -0.0235 -0.1631 0.1755  234 VAL   B CB  
3258 C  CG1 . VAL   B 78  ? 0.7459 0.8578 0.6290 -0.0145 -0.1665 0.2005  234 VAL   B CG1 
3259 C  CG2 . VAL   B 78  ? 0.7729 0.8782 0.6150 -0.0366 -0.1657 0.1674  234 VAL   B CG2 
3260 N  N   . PRO   B 79  ? 0.7421 0.8729 0.6627 -0.0144 -0.1735 0.1857  235 PRO   B N   
3261 C  CA  . PRO   B 79  ? 0.8039 0.9340 0.7519 -0.0015 -0.1708 0.1955  235 PRO   B CA  
3262 C  C   . PRO   B 79  ? 0.7494 0.8810 0.7090 0.0100  -0.1694 0.2169  235 PRO   B C   
3263 O  O   . PRO   B 79  ? 0.7370 0.8812 0.6862 0.0069  -0.1744 0.2284  235 PRO   B O   
3264 C  CB  . PRO   B 79  ? 0.7954 0.9542 0.7520 -0.0071 -0.1808 0.1993  235 PRO   B CB  
3265 C  CG  . PRO   B 79  ? 0.8064 0.9819 0.7385 -0.0236 -0.1895 0.1927  235 PRO   B CG  
3266 C  CD  . PRO   B 79  ? 0.7894 0.9513 0.7014 -0.0257 -0.1857 0.1907  235 PRO   B CD  
3267 N  N   . ARG   B 80  ? 0.8289 0.9463 0.8100 0.0233  -0.1615 0.2218  236 ARG   B N   
3268 C  CA  . ARG   B 80  ? 0.7623 0.8807 0.7593 0.0359  -0.1592 0.2430  236 ARG   B CA  
3269 C  C   . ARG   B 80  ? 0.7246 0.8286 0.7069 0.0358  -0.1551 0.2468  236 ARG   B C   
3270 O  O   . ARG   B 80  ? 0.8361 0.9492 0.8217 0.0398  -0.1561 0.2629  236 ARG   B O   
3271 C  CB  . ARG   B 80  ? 0.8029 0.9538 0.8108 0.0362  -0.1675 0.2585  236 ARG   B CB  
3272 C  CG  . ARG   B 80  ? 0.8297 0.9976 0.8534 0.0360  -0.1716 0.2563  236 ARG   B CG  
3273 C  CD  . ARG   B 80  ? 0.8139 1.0130 0.8471 0.0349  -0.1778 0.2685  236 ARG   B CD  
3274 N  NE  . ARG   B 80  ? 0.9339 1.1520 0.9455 0.0207  -0.1866 0.2668  236 ARG   B NE  
3275 C  CZ  . ARG   B 80  ? 0.8135 1.0460 0.8121 0.0066  -0.1946 0.2552  236 ARG   B CZ  
3276 N  NH1 . ARG   B 80  ? 0.8649 1.0957 0.8696 0.0044  -0.1956 0.2448  236 ARG   B NH1 
3277 N  NH2 . ARG   B 80  ? 0.9050 1.1534 0.8839 -0.0060 -0.2011 0.2535  236 ARG   B NH2 
3278 N  N   . ILE   B 81  ? 0.6765 0.7573 0.6425 0.0305  -0.1486 0.2287  237 ILE   B N   
3279 C  CA  . ILE   B 81  ? 0.6285 0.6962 0.5797 0.0293  -0.1445 0.2311  237 ILE   B CA  
3280 C  C   . ILE   B 81  ? 0.7709 0.8211 0.7385 0.0425  -0.1358 0.2441  237 ILE   B C   
3281 O  O   . ILE   B 81  ? 0.7846 0.8234 0.7714 0.0517  -0.1295 0.2434  237 ILE   B O   
3282 C  CB  . ILE   B 81  ? 0.7770 0.8249 0.7089 0.0211  -0.1390 0.2089  237 ILE   B CB  
3283 C  CG1 . ILE   B 81  ? 0.7650 0.8126 0.6756 0.0146  -0.1396 0.2111  237 ILE   B CG1 
3284 C  CG2 . ILE   B 81  ? 0.7066 0.7252 0.6482 0.0285  -0.1271 0.1993  237 ILE   B CG2 
3285 C  CD1 . ILE   B 81  ? 0.6135 0.6397 0.5082 0.0091  -0.1321 0.1923  237 ILE   B CD1 
3286 N  N   . GLN   B 82  ? 0.8301 0.8787 0.7903 0.0433  -0.1351 0.2566  238 GLN   B N   
3287 C  CA  . GLN   B 82  ? 0.7231 0.7508 0.6951 0.0540  -0.1255 0.2673  238 GLN   B CA  
3288 C  C   . GLN   B 82  ? 0.6959 0.7084 0.6484 0.0483  -0.1210 0.2631  238 GLN   B C   
3289 O  O   . GLN   B 82  ? 0.7291 0.7566 0.6666 0.0419  -0.1273 0.2707  238 GLN   B O   
3290 C  CB  . GLN   B 82  ? 0.8136 0.8549 0.8019 0.0622  -0.1253 0.2837  238 GLN   B CB  
3291 C  CG  . GLN   B 82  ? 0.8954 0.9201 0.8860 0.0683  -0.1167 0.2938  238 GLN   B CG  
3292 C  CD  . GLN   B 82  ? 0.9905 0.9923 1.0028 0.0808  -0.1049 0.2954  238 GLN   B CD  
3293 O  OE1 . GLN   B 82  ? 0.9415 0.9400 0.9673 0.0854  -0.1027 0.2891  238 GLN   B OE1 
3294 N  NE2 . GLN   B 82  ? 0.8638 0.8500 0.8792 0.0860  -0.0969 0.3037  238 GLN   B NE2 
3295 N  N   . LEU   B 83  ? 0.6720 0.6561 0.6241 0.0499  -0.1102 0.2504  239 LEU   B N   
3296 C  CA  . LEU   B 83  ? 0.6681 0.6367 0.6025 0.0440  -0.1049 0.2438  239 LEU   B CA  
3297 C  C   . LEU   B 83  ? 0.7106 0.6638 0.6527 0.0513  -0.0976 0.2592  239 LEU   B C   
3298 O  O   . LEU   B 83  ? 0.7828 0.7232 0.7445 0.0615  -0.0912 0.2658  239 LEU   B O   
3299 C  CB  . LEU   B 83  ? 0.5428 0.4910 0.4719 0.0403  -0.0976 0.2210  239 LEU   B CB  
3300 C  CG  . LEU   B 83  ? 0.5890 0.5477 0.5043 0.0308  -0.1030 0.2036  239 LEU   B CG  
3301 C  CD1 . LEU   B 83  ? 0.6425 0.5803 0.5516 0.0275  -0.0948 0.1837  239 LEU   B CD1 
3302 C  CD2 . LEU   B 83  ? 0.6520 0.6297 0.5476 0.0216  -0.1109 0.2069  239 LEU   B CD2 
3303 N  N   . GLU   B 84  ? 0.6046 0.5577 0.5307 0.0457  -0.0978 0.2642  240 GLU   B N   
3304 C  CA  . GLU   B 84  ? 0.6506 0.5871 0.5807 0.0506  -0.0902 0.2775  240 GLU   B CA  
3305 C  C   . GLU   B 84  ? 0.7111 0.6321 0.6229 0.0420  -0.0843 0.2641  240 GLU   B C   
3306 O  O   . GLU   B 84  ? 0.6553 0.5894 0.5476 0.0329  -0.0894 0.2615  240 GLU   B O   
3307 C  CB  . GLU   B 84  ? 0.7454 0.7005 0.6753 0.0520  -0.0945 0.2930  240 GLU   B CB  
3308 C  CG  . GLU   B 84  ? 0.7736 0.7117 0.7079 0.0566  -0.0856 0.3030  240 GLU   B CG  
3309 C  CD  . GLU   B 84  ? 0.8727 0.8308 0.8078 0.0580  -0.0905 0.3188  240 GLU   B CD  
3310 O  OE1 . GLU   B 84  ? 0.9754 0.9472 0.9268 0.0649  -0.0937 0.3269  240 GLU   B OE1 
3311 O  OE2 . GLU   B 84  ? 1.0009 0.9613 0.9210 0.0521  -0.0908 0.3236  240 GLU   B OE2 
3312 N  N   . GLU   B 85  ? 0.6425 0.5368 0.5603 0.0443  -0.0735 0.2548  241 GLU   B N   
3313 C  CA  . GLU   B 85  ? 0.6758 0.5559 0.5785 0.0364  -0.0673 0.2424  241 GLU   B CA  
3314 C  C   . GLU   B 85  ? 0.6535 0.5373 0.5443 0.0326  -0.0678 0.2560  241 GLU   B C   
3315 O  O   . GLU   B 85  ? 0.7029 0.5863 0.6024 0.0386  -0.0673 0.2759  241 GLU   B O   
3316 C  CB  . GLU   B 85  ? 0.6404 0.4921 0.5535 0.0397  -0.0556 0.2341  241 GLU   B CB  
3317 C  CG  . GLU   B 85  ? 0.7187 0.5576 0.6179 0.0311  -0.0495 0.2197  241 GLU   B CG  
3318 C  CD  . GLU   B 85  ? 0.7139 0.5275 0.6225 0.0327  -0.0388 0.2094  241 GLU   B CD  
3319 O  OE1 . GLU   B 85  ? 0.8367 0.6415 0.7621 0.0407  -0.0355 0.2123  241 GLU   B OE1 
3320 O  OE2 . GLU   B 85  ? 0.7178 0.5214 0.6169 0.0257  -0.0336 0.1981  241 GLU   B OE2 
3321 N  N   . TYR   B 86  ? 0.6329 0.5207 0.5040 0.0228  -0.0683 0.2459  242 TYR   B N   
3322 C  CA  . TYR   B 86  ? 0.6817 0.5738 0.5394 0.0180  -0.0683 0.2571  242 TYR   B CA  
3323 C  C   . TYR   B 86  ? 0.6900 0.5577 0.5471 0.0161  -0.0572 0.2535  242 TYR   B C   
3324 O  O   . TYR   B 86  ? 0.7395 0.5990 0.5896 0.0106  -0.0528 0.2356  242 TYR   B O   
3325 C  CB  . TYR   B 86  ? 0.6260 0.5383 0.4618 0.0080  -0.0749 0.2494  242 TYR   B CB  
3326 C  CG  . TYR   B 86  ? 0.6802 0.5931 0.5003 0.0017  -0.0722 0.2562  242 TYR   B CG  
3327 C  CD1 . TYR   B 86  ? 0.7781 0.7009 0.5970 0.0032  -0.0756 0.2783  242 TYR   B CD1 
3328 C  CD2 . TYR   B 86  ? 0.7958 0.7004 0.6033 -0.0056 -0.0661 0.2416  242 TYR   B CD2 
3329 C  CE1 . TYR   B 86  ? 0.8439 0.7679 0.6484 -0.0029 -0.0730 0.2853  242 TYR   B CE1 
3330 C  CE2 . TYR   B 86  ? 0.7659 0.6720 0.5596 -0.0115 -0.0633 0.2482  242 TYR   B CE2 
3331 C  CZ  . TYR   B 86  ? 0.8695 0.7850 0.6613 -0.0104 -0.0667 0.2699  242 TYR   B CZ  
3332 O  OH  . TYR   B 86  ? 0.8309 0.7486 0.6087 -0.0165 -0.0638 0.2772  242 TYR   B OH  
3333 N  N   . SER   B 87  ? 0.6810 0.5377 0.5461 0.0207  -0.0525 0.2709  243 SER   B N   
3334 C  CA  . SER   B 87  ? 0.7402 0.5759 0.6027 0.0173  -0.0425 0.2714  243 SER   B CA  
3335 C  C   . SER   B 87  ? 0.7112 0.5275 0.5767 0.0147  -0.0345 0.2509  243 SER   B C   
3336 O  O   . SER   B 87  ? 0.8808 0.6922 0.7349 0.0067  -0.0303 0.2404  243 SER   B O   
3337 C  CB  . SER   B 87  ? 0.8667 0.7142 0.7089 0.0082  -0.0444 0.2746  243 SER   B CB  
3338 O  OG  . SER   B 87  ? 0.9178 0.7465 0.7574 0.0040  -0.0348 0.2750  243 SER   B OG  
3339 N  N   . ASN   B 88  ? 0.6626 0.4694 0.5439 0.0215  -0.0325 0.2454  244 ASN   B N   
3340 C  CA  . ASN   B 88  ? 0.7746 0.5626 0.6610 0.0199  -0.0247 0.2276  244 ASN   B CA  
3341 C  C   . ASN   B 88  ? 0.7223 0.5184 0.5951 0.0115  -0.0265 0.2081  244 ASN   B C   
3342 O  O   . ASN   B 88  ? 0.7960 0.5786 0.6691 0.0077  -0.0198 0.1948  244 ASN   B O   
3343 C  CB  . ASN   B 88  ? 0.7584 0.5212 0.6487 0.0184  -0.0135 0.2311  244 ASN   B CB  
3344 C  CG  . ASN   B 88  ? 0.8996 0.6475 0.8075 0.0281  -0.0087 0.2464  244 ASN   B CG  
3345 O  OD1 . ASN   B 88  ? 0.9733 0.7287 0.8929 0.0368  -0.0130 0.2520  244 ASN   B OD1 
3346 N  ND2 . ASN   B 88  ? 0.8483 0.5757 0.7587 0.0269  0.0004  0.2542  244 ASN   B ND2 
3347 N  N   . THR   B 89  ? 0.7946 0.6128 0.6556 0.0084  -0.0351 0.2061  245 THR   B N   
3348 C  CA  . THR   B 89  ? 0.6360 0.4608 0.4839 0.0009  -0.0356 0.1889  245 THR   B CA  
3349 C  C   . THR   B 89  ? 0.6618 0.4838 0.5166 0.0024  -0.0354 0.1724  245 THR   B C   
3350 O  O   . THR   B 89  ? 0.6493 0.4725 0.4965 -0.0029 -0.0337 0.1578  245 THR   B O   
3351 C  CB  . THR   B 89  ? 0.6969 0.5447 0.5292 -0.0033 -0.0438 0.1907  245 THR   B CB  
3352 O  OG1 . THR   B 89  ? 0.6521 0.5137 0.4898 0.0017  -0.0522 0.1981  245 THR   B OG1 
3353 C  CG2 . THR   B 89  ? 0.6290 0.4800 0.4508 -0.0073 -0.0427 0.2041  245 THR   B CG2 
3354 N  N   . ARG   B 90  ? 0.6442 0.4635 0.5135 0.0099  -0.0370 0.1750  246 ARG   B N   
3355 C  CA  . ARG   B 90  ? 0.6403 0.4572 0.5172 0.0118  -0.0369 0.1609  246 ARG   B CA  
3356 C  C   . ARG   B 90  ? 0.6057 0.4409 0.4745 0.0092  -0.0446 0.1515  246 ARG   B C   
3357 O  O   . ARG   B 90  ? 0.5899 0.4281 0.4668 0.0125  -0.0473 0.1454  246 ARG   B O   
3358 C  CB  . ARG   B 90  ? 0.7282 0.5286 0.6060 0.0080  -0.0282 0.1481  246 ARG   B CB  
3359 C  CG  . ARG   B 90  ? 0.7136 0.4935 0.5997 0.0097  -0.0197 0.1557  246 ARG   B CG  
3360 C  CD  . ARG   B 90  ? 0.7406 0.5070 0.6428 0.0161  -0.0153 0.1529  246 ARG   B CD  
3361 N  NE  . ARG   B 90  ? 0.9301 0.6968 0.8439 0.0249  -0.0171 0.1684  246 ARG   B NE  
3362 C  CZ  . ARG   B 90  ? 0.7515 0.5167 0.6794 0.0324  -0.0172 0.1685  246 ARG   B CZ  
3363 N  NH1 . ARG   B 90  ? 0.8536 0.6118 0.7865 0.0321  -0.0136 0.1543  246 ARG   B NH1 
3364 N  NH2 . ARG   B 90  ? 0.9109 0.6827 0.8484 0.0405  -0.0208 0.1840  246 ARG   B NH2 
3365 N  N   . ALA   B 91  ? 0.6699 0.5171 0.5227 0.0030  -0.0478 0.1504  247 ALA   B N   
3366 C  CA  . ALA   B 91  ? 0.6106 0.4734 0.4545 -0.0003 -0.0541 0.1408  247 ALA   B CA  
3367 C  C   . ALA   B 91  ? 0.6477 0.5294 0.4836 -0.0016 -0.0627 0.1508  247 ALA   B C   
3368 O  O   . ALA   B 91  ? 0.5542 0.4482 0.3856 -0.0037 -0.0685 0.1437  247 ALA   B O   
3369 C  CB  . ALA   B 91  ? 0.6332 0.4958 0.4638 -0.0072 -0.0503 0.1281  247 ALA   B CB  
3370 N  N   . TYR   B 92  ? 0.5993 0.4839 0.4326 -0.0011 -0.0636 0.1669  248 TYR   B N   
3371 C  CA  . TYR   B 92  ? 0.6345 0.5390 0.4585 -0.0034 -0.0718 0.1779  248 TYR   B CA  
3372 C  C   . TYR   B 92  ? 0.6174 0.5269 0.4561 0.0042  -0.0763 0.1950  248 TYR   B C   
3373 O  O   . TYR   B 92  ? 0.6344 0.5292 0.4871 0.0107  -0.0710 0.2036  248 TYR   B O   
3374 C  CB  . TYR   B 92  ? 0.6339 0.5408 0.4429 -0.0089 -0.0696 0.1849  248 TYR   B CB  
3375 C  CG  . TYR   B 92  ? 0.7149 0.6215 0.5086 -0.0164 -0.0657 0.1690  248 TYR   B CG  
3376 C  CD1 . TYR   B 92  ? 0.6634 0.5534 0.4606 -0.0168 -0.0571 0.1590  248 TYR   B CD1 
3377 C  CD2 . TYR   B 92  ? 0.6989 0.6223 0.4749 -0.0233 -0.0703 0.1640  248 TYR   B CD2 
3378 C  CE1 . TYR   B 92  ? 0.7627 0.6537 0.5479 -0.0227 -0.0532 0.1455  248 TYR   B CE1 
3379 C  CE2 . TYR   B 92  ? 0.6890 0.6112 0.4520 -0.0292 -0.0654 0.1495  248 TYR   B CE2 
3380 C  CZ  . TYR   B 92  ? 0.8011 0.7076 0.5697 -0.0283 -0.0570 0.1409  248 TYR   B CZ  
3381 O  OH  . TYR   B 92  ? 0.7930 0.6995 0.5510 -0.0332 -0.0518 0.1276  248 TYR   B OH  
3382 N  N   . TYR   B 93  ? 0.7200 0.6506 0.5557 0.0030  -0.0859 0.2002  249 TYR   B N   
3383 C  CA  . TYR   B 93  ? 0.5814 0.5210 0.4327 0.0105  -0.0912 0.2156  249 TYR   B CA  
3384 C  C   . TYR   B 93  ? 0.6760 0.6422 0.5173 0.0062  -0.1016 0.2272  249 TYR   B C   
3385 O  O   . TYR   B 93  ? 0.6064 0.5853 0.4296 -0.0029 -0.1059 0.2179  249 TYR   B O   
3386 C  CB  . TYR   B 93  ? 0.5457 0.4838 0.4115 0.0149  -0.0923 0.2063  249 TYR   B CB  
3387 C  CG  . TYR   B 93  ? 0.5973 0.5110 0.4742 0.0193  -0.0825 0.1958  249 TYR   B CG  
3388 C  CD1 . TYR   B 93  ? 0.5952 0.4986 0.4629 0.0138  -0.0776 0.1774  249 TYR   B CD1 
3389 C  CD2 . TYR   B 93  ? 0.6225 0.5246 0.5194 0.0288  -0.0782 0.2041  249 TYR   B CD2 
3390 C  CE1 . TYR   B 93  ? 0.6339 0.5174 0.5107 0.0167  -0.0693 0.1682  249 TYR   B CE1 
3391 C  CE2 . TYR   B 93  ? 0.5997 0.4798 0.5052 0.0316  -0.0690 0.1934  249 TYR   B CE2 
3392 C  CZ  . TYR   B 93  ? 0.6271 0.4989 0.5220 0.0251  -0.0651 0.1756  249 TYR   B CZ  
3393 O  OH  . TYR   B 93  ? 0.7104 0.5630 0.6125 0.0266  -0.0567 0.1650  249 TYR   B OH  
3394 N  N   . PHE   B 94  ? 0.6681 0.6429 0.5216 0.0129  -0.1053 0.2478  250 PHE   B N   
3395 C  CA  . PHE   B 94  ? 0.6931 0.6966 0.5429 0.0105  -0.1167 0.2600  250 PHE   B CA  
3396 C  C   . PHE   B 94  ? 0.7084 0.7213 0.5723 0.0139  -0.1219 0.2558  250 PHE   B C   
3397 O  O   . PHE   B 94  ? 0.6091 0.6073 0.4919 0.0225  -0.1166 0.2540  250 PHE   B O   
3398 C  CB  . PHE   B 94  ? 0.7226 0.7317 0.5816 0.0169  -0.1166 0.2819  250 PHE   B CB  
3399 C  CG  . PHE   B 94  ? 0.7307 0.7311 0.5771 0.0136  -0.1111 0.2865  250 PHE   B CG  
3400 C  CD1 . PHE   B 94  ? 0.6904 0.7064 0.5142 0.0031  -0.1152 0.2841  250 PHE   B CD1 
3401 C  CD2 . PHE   B 94  ? 0.7367 0.7124 0.5934 0.0203  -0.1010 0.2921  250 PHE   B CD2 
3402 C  CE1 . PHE   B 94  ? 0.8039 0.8129 0.6164 0.0000  -0.1098 0.2887  250 PHE   B CE1 
3403 C  CE2 . PHE   B 94  ? 0.8436 0.8115 0.6890 0.0166  -0.0958 0.2966  250 PHE   B CE2 
3404 C  CZ  . PHE   B 94  ? 0.8168 0.8020 0.6405 0.0067  -0.1003 0.2955  250 PHE   B CZ  
3405 N  N   . VAL   B 95  ? 0.7355 0.7729 0.5895 0.0063  -0.1318 0.2534  251 VAL   B N   
3406 C  CA  . VAL   B 95  ? 0.6084 0.6592 0.4749 0.0081  -0.1381 0.2512  251 VAL   B CA  
3407 C  C   . VAL   B 95  ? 0.6313 0.7043 0.5105 0.0128  -0.1440 0.2696  251 VAL   B C   
3408 O  O   . VAL   B 95  ? 0.6431 0.7346 0.5109 0.0067  -0.1486 0.2747  251 VAL   B O   
3409 C  CB  . VAL   B 95  ? 0.6238 0.6855 0.4735 -0.0039 -0.1432 0.2323  251 VAL   B CB  
3410 C  CG1 . VAL   B 95  ? 0.6341 0.7047 0.4984 -0.0019 -0.1478 0.2281  251 VAL   B CG1 
3411 C  CG2 . VAL   B 95  ? 0.7128 0.7509 0.5517 -0.0074 -0.1341 0.2112  251 VAL   B CG2 
3412 N  N   . LYS   B 96  ? 0.6420 0.7121 0.5459 0.0238  -0.1419 0.2764  252 LYS   B N   
3413 C  CA  . LYS   B 96  ? 0.8016 0.8922 0.7221 0.0293  -0.1458 0.2897  252 LYS   B CA  
3414 C  C   . LYS   B 96  ? 0.7640 0.8652 0.6983 0.0308  -0.1502 0.2846  252 LYS   B C   
3415 O  O   . LYS   B 96  ? 0.7772 0.8690 0.7076 0.0276  -0.1503 0.2711  252 LYS   B O   
3416 C  CB  . LYS   B 96  ? 0.7358 0.8122 0.6746 0.0420  -0.1373 0.3039  252 LYS   B CB  
3417 C  CG  . LYS   B 96  ? 0.7918 0.8587 0.7173 0.0398  -0.1331 0.3096  252 LYS   B CG  
3418 C  CD  . LYS   B 96  ? 0.8287 0.8783 0.7715 0.0516  -0.1238 0.3221  252 LYS   B CD  
3419 C  CE  . LYS   B 96  ? 0.8598 0.8989 0.7881 0.0481  -0.1196 0.3267  252 LYS   B CE  
3420 N  NZ  . LYS   B 96  ? 0.8614 0.8940 0.8039 0.0572  -0.1138 0.3427  252 LYS   B NZ  
3421 N  N   . PHE   B 97  ? 0.8488 0.9704 0.7994 0.0353  -0.1541 0.2958  253 PHE   B N   
3422 C  CA  . PHE   B 97  ? 0.8421 0.9792 0.8048 0.0350  -0.1595 0.2918  253 PHE   B CA  
3423 C  C   . PHE   B 97  ? 0.8685 1.0064 0.8601 0.0487  -0.1550 0.3038  253 PHE   B C   
3424 O  O   . PHE   B 97  ? 0.9183 1.0606 0.9191 0.0551  -0.1528 0.3186  253 PHE   B O   
3425 C  CB  . PHE   B 97  ? 0.8303 0.9995 0.7812 0.0226  -0.1708 0.2910  253 PHE   B CB  
3426 C  CG  . PHE   B 97  ? 0.8349 1.0036 0.7569 0.0084  -0.1744 0.2771  253 PHE   B CG  
3427 C  CD1 . PHE   B 97  ? 0.8598 1.0284 0.7639 0.0034  -0.1738 0.2803  253 PHE   B CD1 
3428 C  CD2 . PHE   B 97  ? 0.6971 0.8630 0.6099 0.0005  -0.1773 0.2602  253 PHE   B CD2 
3429 C  CE1 . PHE   B 97  ? 0.8935 1.0606 0.7708 -0.0094 -0.1757 0.2663  253 PHE   B CE1 
3430 C  CE2 . PHE   B 97  ? 0.7245 0.8876 0.6105 -0.0123 -0.1792 0.2462  253 PHE   B CE2 
3431 C  CZ  . PHE   B 97  ? 0.8056 0.9693 0.6739 -0.0171 -0.1780 0.2489  253 PHE   B CZ  
3432 N  N   . LYS   B 98  ? 0.8721 1.0062 0.8777 0.0529  -0.1536 0.2973  254 LYS   B N   
3433 C  CA  . LYS   B 98  ? 0.8582 0.9950 0.8912 0.0653  -0.1492 0.3068  254 LYS   B CA  
3434 C  C   . LYS   B 98  ? 0.7240 0.8959 0.7658 0.0623  -0.1583 0.3157  254 LYS   B C   
3435 O  O   . LYS   B 98  ? 0.8851 1.0737 0.9260 0.0614  -0.1618 0.3284  254 LYS   B O   
3436 C  CB  . LYS   B 98  ? 0.8047 0.9241 0.8492 0.0706  -0.1435 0.2959  254 LYS   B CB  
3437 C  CG  . LYS   B 98  ? 0.8745 0.9598 0.9110 0.0729  -0.1343 0.2871  254 LYS   B CG  
3438 C  CD  . LYS   B 98  ? 0.8552 0.9274 0.8959 0.0732  -0.1316 0.2733  254 LYS   B CD  
3439 C  CE  . LYS   B 98  ? 0.9212 0.9657 0.9784 0.0854  -0.1180 0.2726  254 LYS   B CE  
3440 N  NZ  . LYS   B 98  ? 0.8766 0.9307 0.9586 0.0957  -0.1147 0.2809  254 LYS   B NZ  
3441 N  N   . ASN   B 104 ? 0.8101 1.1417 0.7315 -0.0472 -0.2237 0.2694  260 ASN   B N   
3442 C  CA  . ASN   B 104 ? 0.8272 1.1286 0.7328 -0.0462 -0.2173 0.2577  260 ASN   B CA  
3443 C  C   . ASN   B 104 ? 0.7835 1.0874 0.6586 -0.0632 -0.2199 0.2426  260 ASN   B C   
3444 O  O   . ASN   B 104 ? 0.7416 1.0602 0.6056 -0.0692 -0.2225 0.2489  260 ASN   B O   
3445 C  CB  . ASN   B 104 ? 0.8112 1.0978 0.7228 -0.0330 -0.2109 0.2716  260 ASN   B CB  
3446 C  CG  . ASN   B 104 ? 0.7820 1.0369 0.6807 -0.0306 -0.2036 0.2610  260 ASN   B CG  
3447 O  OD1 . ASN   B 104 ? 0.7337 0.9798 0.6124 -0.0410 -0.2039 0.2435  260 ASN   B OD1 
3448 N  ND2 . ASN   B 104 ? 0.8719 1.1091 0.7817 -0.0172 -0.1965 0.2718  260 ASN   B ND2 
3449 N  N   . PRO   B 105 ? 0.7000 0.9901 0.5620 -0.0712 -0.2188 0.2226  261 PRO   B N   
3450 C  CA  . PRO   B 105 ? 0.7197 1.0110 0.5531 -0.0879 -0.2200 0.2061  261 PRO   B CA  
3451 C  C   . PRO   B 105 ? 0.7438 1.0231 0.5581 -0.0885 -0.2153 0.2057  261 PRO   B C   
3452 O  O   . PRO   B 105 ? 0.7223 1.0092 0.5148 -0.1013 -0.2164 0.1974  261 PRO   B O   
3453 C  CB  . PRO   B 105 ? 0.7214 0.9952 0.5490 -0.0929 -0.2178 0.1859  261 PRO   B CB  
3454 C  CG  . PRO   B 105 ? 0.8385 1.1155 0.6932 -0.0833 -0.2194 0.1931  261 PRO   B CG  
3455 C  CD  . PRO   B 105 ? 0.8010 1.0783 0.6754 -0.0669 -0.2172 0.2144  261 PRO   B CD  
3456 N  N   . LEU   B 106 ? 0.6839 0.9449 0.5057 -0.0754 -0.2096 0.2145  262 LEU   B N   
3457 C  CA  . LEU   B 106 ? 0.6876 0.9359 0.4927 -0.0753 -0.2045 0.2148  262 LEU   B CA  
3458 C  C   . LEU   B 106 ? 0.6344 0.8972 0.4449 -0.0706 -0.2058 0.2346  262 LEU   B C   
3459 O  O   . LEU   B 106 ? 0.6416 0.8943 0.4403 -0.0695 -0.2013 0.2372  262 LEU   B O   
3460 C  CB  . LEU   B 106 ? 0.6312 0.8493 0.4402 -0.0649 -0.1968 0.2124  262 LEU   B CB  
3461 C  CG  . LEU   B 106 ? 0.7064 0.9083 0.5108 -0.0687 -0.1951 0.1937  262 LEU   B CG  
3462 C  CD1 . LEU   B 106 ? 0.5957 0.7678 0.4001 -0.0603 -0.1874 0.1906  262 LEU   B CD1 
3463 C  CD2 . LEU   B 106 ? 0.6833 0.8894 0.4622 -0.0852 -0.1962 0.1748  262 LEU   B CD2 
3464 N  N   . SER   B 107 ? 0.6439 0.9304 0.4717 -0.0681 -0.2116 0.2489  263 SER   B N   
3465 C  CA  . SER   B 107 ? 0.6487 0.9470 0.4853 -0.0613 -0.2121 0.2696  263 SER   B CA  
3466 C  C   . SER   B 107 ? 0.7228 1.0301 0.5359 -0.0721 -0.2131 0.2686  263 SER   B C   
3467 O  O   . SER   B 107 ? 0.6804 0.9893 0.4956 -0.0665 -0.2113 0.2834  263 SER   B O   
3468 C  CB  . SER   B 107 ? 0.8636 1.1890 0.7216 -0.0585 -0.2185 0.2843  263 SER   B CB  
3469 O  OG  . SER   B 107 ? 0.9418 1.2871 0.7932 -0.0720 -0.2253 0.2741  263 SER   B OG  
3470 N  N   . GLN   B 108 ? 0.7180 1.0303 0.5088 -0.0874 -0.2152 0.2510  264 GLN   B N   
3471 C  CA  . GLN   B 108 ? 0.6963 1.0160 0.4636 -0.0980 -0.2151 0.2483  264 GLN   B CA  
3472 C  C   . GLN   B 108 ? 0.6935 0.9879 0.4477 -0.0943 -0.2068 0.2440  264 GLN   B C   
3473 O  O   . GLN   B 108 ? 0.8039 1.1026 0.5394 -0.1016 -0.2055 0.2428  264 GLN   B O   
3474 C  CB  . GLN   B 108 ? 0.7375 1.0669 0.4846 -0.1156 -0.2181 0.2289  264 GLN   B CB  
3475 C  CG  . GLN   B 108 ? 0.7092 1.0132 0.4443 -0.1192 -0.2125 0.2057  264 GLN   B CG  
3476 C  CD  . GLN   B 108 ? 0.8332 1.1455 0.5508 -0.1361 -0.2147 0.1866  264 GLN   B CD  
3477 O  OE1 . GLN   B 108 ? 0.7817 1.0887 0.4758 -0.1462 -0.2108 0.1733  264 GLN   B OE1 
3478 N  NE2 . GLN   B 108 ? 0.8385 1.1624 0.5679 -0.1392 -0.2200 0.1845  264 GLN   B NE2 
3479 N  N   . PHE   B 109 ? 0.7939 1.0630 0.5571 -0.0838 -0.2010 0.2415  265 PHE   B N   
3480 C  CA  . PHE   B 109 ? 0.7774 1.0226 0.5295 -0.0803 -0.1928 0.2380  265 PHE   B CA  
3481 C  C   . PHE   B 109 ? 0.7545 0.9896 0.5243 -0.0654 -0.1889 0.2573  265 PHE   B C   
3482 O  O   . PHE   B 109 ? 0.7302 0.9443 0.4939 -0.0614 -0.1816 0.2560  265 PHE   B O   
3483 C  CB  . PHE   B 109 ? 0.7330 0.9544 0.4789 -0.0809 -0.1879 0.2192  265 PHE   B CB  
3484 C  CG  . PHE   B 109 ? 0.7506 0.9769 0.4784 -0.0953 -0.1898 0.1984  265 PHE   B CG  
3485 C  CD1 . PHE   B 109 ? 0.8279 1.0630 0.5325 -0.1078 -0.1893 0.1898  265 PHE   B CD1 
3486 C  CD2 . PHE   B 109 ? 0.7247 0.9451 0.4589 -0.0963 -0.1911 0.1866  265 PHE   B CD2 
3487 C  CE1 . PHE   B 109 ? 0.8566 1.0936 0.5452 -0.1210 -0.1896 0.1696  265 PHE   B CE1 
3488 C  CE2 . PHE   B 109 ? 0.7746 0.9970 0.4927 -0.1096 -0.1918 0.1668  265 PHE   B CE2 
3489 C  CZ  . PHE   B 109 ? 0.7221 0.9518 0.4176 -0.1217 -0.1906 0.1579  265 PHE   B CZ  
3490 N  N   . LEU   B 110 ? 0.8293 1.0787 0.6208 -0.0575 -0.1928 0.2749  266 LEU   B N   
3491 C  CA  . LEU   B 110 ? 0.7866 1.0230 0.5968 -0.0427 -0.1877 0.2917  266 LEU   B CA  
3492 C  C   . LEU   B 110 ? 0.7474 0.9853 0.5479 -0.0433 -0.1851 0.3027  266 LEU   B C   
3493 O  O   . LEU   B 110 ? 0.7520 1.0114 0.5396 -0.0529 -0.1900 0.3050  266 LEU   B O   
3494 C  CB  . LEU   B 110 ? 0.6759 0.9268 0.5133 -0.0334 -0.1916 0.3072  266 LEU   B CB  
3495 C  CG  . LEU   B 110 ? 0.8516 1.0893 0.7090 -0.0241 -0.1894 0.3035  266 LEU   B CG  
3496 C  CD1 . LEU   B 110 ? 0.8203 1.0796 0.7016 -0.0182 -0.1944 0.3173  266 LEU   B CD1 
3497 C  CD2 . LEU   B 110 ? 0.7889 0.9935 0.6544 -0.0124 -0.1795 0.3036  266 LEU   B CD2 
3498 N  N   . GLU   B 111 ? 0.7485 0.9631 0.5553 -0.0334 -0.1772 0.3092  267 GLU   B N   
3499 C  CA  . GLU   B 111 ? 0.8615 1.0763 0.6690 -0.0294 -0.1743 0.3254  267 GLU   B CA  
3500 C  C   . GLU   B 111 ? 0.8248 1.0294 0.6603 -0.0138 -0.1705 0.3413  267 GLU   B C   
3501 O  O   . GLU   B 111 ? 0.7717 0.9495 0.6156 -0.0054 -0.1629 0.3383  267 GLU   B O   
3502 C  CB  . GLU   B 111 ? 0.9072 1.1021 0.6960 -0.0326 -0.1669 0.3186  267 GLU   B CB  
3503 C  CG  . GLU   B 111 ? 0.9176 1.1147 0.6803 -0.0462 -0.1677 0.2987  267 GLU   B CG  
3504 C  CD  . GLU   B 111 ? 0.9762 1.1790 0.7176 -0.0545 -0.1659 0.2993  267 GLU   B CD  
3505 O  OE1 . GLU   B 111 ? 0.9097 1.1341 0.6502 -0.0574 -0.1707 0.3117  267 GLU   B OE1 
3506 O  OE2 . GLU   B 111 ? 1.1229 1.3085 0.8490 -0.0580 -0.1594 0.2877  267 GLU   B OE2 
3507 N  N   . GLY   B 112 ? 0.8270 1.0531 0.6769 -0.0102 -0.1753 0.3578  268 GLY   B N   
3508 C  CA  . GLY   B 112 ? 0.7793 0.9987 0.6573 0.0045  -0.1719 0.3721  268 GLY   B CA  
3509 C  C   . GLY   B 112 ? 0.7986 1.0061 0.6904 0.0102  -0.1703 0.3622  268 GLY   B C   
3510 O  O   . GLY   B 112 ? 0.8034 1.0293 0.6985 0.0059  -0.1771 0.3570  268 GLY   B O   
3511 N  N   . GLU   B 113 ? 0.7746 0.9512 0.6739 0.0191  -0.1610 0.3590  269 GLU   B N   
3512 C  CA  . GLU   B 113 ? 0.7925 0.9556 0.7055 0.0252  -0.1583 0.3499  269 GLU   B CA  
3513 C  C   . GLU   B 113 ? 0.7788 0.9281 0.6745 0.0175  -0.1574 0.3296  269 GLU   B C   
3514 O  O   . GLU   B 113 ? 0.8236 0.9688 0.7276 0.0194  -0.1580 0.3204  269 GLU   B O   
3515 C  CB  . GLU   B 113 ? 0.8923 1.0293 0.8263 0.0398  -0.1479 0.3577  269 GLU   B CB  
3516 C  CG  . GLU   B 113 ? 0.9073 1.0539 0.8690 0.0509  -0.1479 0.3699  269 GLU   B CG  
3517 C  CD  . GLU   B 113 ? 1.0299 1.1480 1.0101 0.0628  -0.1377 0.3665  269 GLU   B CD  
3518 O  OE1 . GLU   B 113 ? 0.9491 1.0687 0.9401 0.0653  -0.1386 0.3591  269 GLU   B OE1 
3519 O  OE2 . GLU   B 113 ? 1.1275 1.2214 1.1111 0.0691  -0.1283 0.3710  269 GLU   B OE2 
3520 N  N   . ILE   B 114 ? 0.8149 0.9573 0.6874 0.0090  -0.1558 0.3225  270 ILE   B N   
3521 C  CA  . ILE   B 114 ? 0.7127 0.8377 0.5699 0.0032  -0.1529 0.3044  270 ILE   B CA  
3522 C  C   . ILE   B 114 ? 0.7386 0.8824 0.5750 -0.0110 -0.1606 0.2908  270 ILE   B C   
3523 O  O   . ILE   B 114 ? 0.7428 0.9091 0.5685 -0.0187 -0.1663 0.2945  270 ILE   B O   
3524 C  CB  . ILE   B 114 ? 0.7504 0.8528 0.5961 0.0032  -0.1444 0.3039  270 ILE   B CB  
3525 C  CG1 . ILE   B 114 ? 0.7901 0.9072 0.6139 -0.0070 -0.1472 0.3054  270 ILE   B CG1 
3526 C  CG2 . ILE   B 114 ? 0.7417 0.8242 0.6075 0.0163  -0.1360 0.3169  270 ILE   B CG2 
3527 C  CD1 . ILE   B 114 ? 0.8338 0.9337 0.6383 -0.0126 -0.1408 0.2965  270 ILE   B CD1 
3528 N  N   . LEU   B 115 ? 0.7149 0.8491 0.5459 -0.0146 -0.1604 0.2745  271 LEU   B N   
3529 C  CA  . LEU   B 115 ? 0.6915 0.8363 0.5005 -0.0286 -0.1652 0.2579  271 LEU   B CA  
3530 C  C   . LEU   B 115 ? 0.7249 0.8622 0.5098 -0.0361 -0.1609 0.2517  271 LEU   B C   
3531 O  O   . LEU   B 115 ? 0.7401 0.8543 0.5221 -0.0329 -0.1534 0.2485  271 LEU   B O   
3532 C  CB  . LEU   B 115 ? 0.6351 0.7675 0.4457 -0.0293 -0.1648 0.2427  271 LEU   B CB  
3533 C  CG  . LEU   B 115 ? 0.6483 0.7929 0.4454 -0.0416 -0.1708 0.2258  271 LEU   B CG  
3534 C  CD1 . LEU   B 115 ? 0.7770 0.9516 0.5716 -0.0492 -0.1789 0.2296  271 LEU   B CD1 
3535 C  CD2 . LEU   B 115 ? 0.6186 0.7520 0.4262 -0.0389 -0.1711 0.2158  271 LEU   B CD2 
3536 N  N   . SER   B 116 ? 0.6740 0.8306 0.4415 -0.0468 -0.1650 0.2494  272 SER   B N   
3537 C  CA  . SER   B 116 ? 0.7012 0.8520 0.4454 -0.0544 -0.1603 0.2423  272 SER   B CA  
3538 C  C   . SER   B 116 ? 0.7806 0.9208 0.5076 -0.0628 -0.1580 0.2199  272 SER   B C   
3539 O  O   . SER   B 116 ? 0.7556 0.9081 0.4742 -0.0718 -0.1627 0.2078  272 SER   B O   
3540 C  CB  . SER   B 116 ? 0.7536 0.9281 0.4851 -0.0629 -0.1648 0.2472  272 SER   B CB  
3541 O  OG  . SER   B 116 ? 0.7477 0.9172 0.4553 -0.0715 -0.1599 0.2370  272 SER   B OG  
3542 N  N   . ALA   B 117 ? 0.6976 0.8146 0.4198 -0.0603 -0.1501 0.2143  273 ALA   B N   
3543 C  CA  . ALA   B 117 ? 0.7090 0.8156 0.4125 -0.0687 -0.1465 0.1934  273 ALA   B CA  
3544 C  C   . ALA   B 117 ? 0.7576 0.8763 0.4371 -0.0805 -0.1457 0.1843  273 ALA   B C   
3545 O  O   . ALA   B 117 ? 0.6998 0.8204 0.3651 -0.0897 -0.1457 0.1663  273 ALA   B O   
3546 C  CB  . ALA   B 117 ? 0.6903 0.7692 0.3980 -0.0623 -0.1360 0.1882  273 ALA   B CB  
3547 N  N   . SER   B 118 ? 0.7031 0.8299 0.3786 -0.0803 -0.1445 0.1965  274 SER   B N   
3548 C  CA  . SER   B 118 ? 0.7900 0.9295 0.4436 -0.0913 -0.1436 0.1894  274 SER   B CA  
3549 C  C   . SER   B 118 ? 0.7793 0.9399 0.4280 -0.1001 -0.1513 0.1829  274 SER   B C   
3550 O  O   . SER   B 118 ? 0.8283 0.9921 0.4581 -0.1109 -0.1494 0.1660  274 SER   B O   
3551 C  CB  . SER   B 118 ? 0.7552 0.9021 0.4085 -0.0889 -0.1426 0.2068  274 SER   B CB  
3552 O  OG  . SER   B 118 ? 0.9143 1.0415 0.5688 -0.0830 -0.1344 0.2110  274 SER   B OG  
3553 N  N   . LYS   B 119 ? 0.7725 0.9481 0.4388 -0.0959 -0.1593 0.1964  275 LYS   B N   
3554 C  CA  . LYS   B 119 ? 0.7363 0.9336 0.4000 -0.1047 -0.1670 0.1919  275 LYS   B CA  
3555 C  C   . LYS   B 119 ? 0.7295 0.9191 0.3917 -0.1090 -0.1673 0.1730  275 LYS   B C   
3556 O  O   . LYS   B 119 ? 0.7718 0.9687 0.4189 -0.1208 -0.1681 0.1577  275 LYS   B O   
3557 C  CB  . LYS   B 119 ? 0.6979 0.9132 0.3830 -0.0981 -0.1748 0.2123  275 LYS   B CB  
3558 C  CG  . LYS   B 119 ? 0.7486 0.9766 0.4349 -0.0958 -0.1758 0.2314  275 LYS   B CG  
3559 C  CD  . LYS   B 119 ? 0.8093 1.0551 0.5186 -0.0889 -0.1832 0.2503  275 LYS   B CD  
3560 C  CE  . LYS   B 119 ? 0.8532 1.1129 0.5652 -0.0865 -0.1847 0.2701  275 LYS   B CE  
3561 N  NZ  . LYS   B 119 ? 0.9830 1.2613 0.7176 -0.0804 -0.1917 0.2871  275 LYS   B NZ  
3562 N  N   . MET   B 120 ? 0.6732 0.8474 0.3514 -0.0997 -0.1664 0.1740  276 MET   B N   
3563 C  CA  . MET   B 120 ? 0.7818 0.9475 0.4595 -0.1034 -0.1666 0.1568  276 MET   B CA  
3564 C  C   . MET   B 120 ? 0.7929 0.9457 0.4473 -0.1127 -0.1594 0.1348  276 MET   B C   
3565 O  O   . MET   B 120 ? 0.8244 0.9804 0.4695 -0.1223 -0.1602 0.1186  276 MET   B O   
3566 C  CB  . MET   B 120 ? 0.7880 0.9364 0.4847 -0.0917 -0.1654 0.1614  276 MET   B CB  
3567 C  CG  . MET   B 120 ? 0.8941 1.0398 0.5973 -0.0938 -0.1685 0.1494  276 MET   B CG  
3568 S  SD  . MET   B 120 ? 0.7715 0.9135 0.5059 -0.0797 -0.1721 0.1639  276 MET   B SD  
3569 C  CE  . MET   B 120 ? 0.7198 0.8530 0.4569 -0.0845 -0.1714 0.1420  276 MET   B CE  
3570 N  N   . LEU   B 121 ? 0.7749 0.9129 0.4203 -0.1099 -0.1515 0.1342  277 LEU   B N   
3571 C  CA  . LEU   B 121 ? 0.7683 0.8930 0.3933 -0.1171 -0.1430 0.1140  277 LEU   B CA  
3572 C  C   . LEU   B 121 ? 0.7888 0.9282 0.3952 -0.1291 -0.1427 0.1053  277 LEU   B C   
3573 O  O   . LEU   B 121 ? 0.7790 0.9126 0.3722 -0.1374 -0.1385 0.0854  277 LEU   B O   
3574 C  CB  . LEU   B 121 ? 0.7683 0.8764 0.3893 -0.1113 -0.1346 0.1174  277 LEU   B CB  
3575 C  CG  . LEU   B 121 ? 0.6751 0.7604 0.3118 -0.1011 -0.1297 0.1158  277 LEU   B CG  
3576 C  CD1 . LEU   B 121 ? 0.7880 0.8586 0.4212 -0.0969 -0.1196 0.1161  277 LEU   B CD1 
3577 C  CD2 . LEU   B 121 ? 0.7061 0.7799 0.3419 -0.1043 -0.1258 0.0937  277 LEU   B CD2 
3578 N  N   . SER   B 122 ? 0.7662 0.9234 0.3711 -0.1301 -0.1464 0.1199  278 SER   B N   
3579 C  CA  . SER   B 122 ? 0.7862 0.9585 0.3732 -0.1421 -0.1465 0.1125  278 SER   B CA  
3580 C  C   . SER   B 122 ? 0.7727 0.9535 0.3576 -0.1514 -0.1511 0.0996  278 SER   B C   
3581 O  O   . SER   B 122 ? 0.7439 0.9236 0.3114 -0.1620 -0.1466 0.0820  278 SER   B O   
3582 C  CB  . SER   B 122 ? 0.8466 1.0399 0.4359 -0.1417 -0.1520 0.1327  278 SER   B CB  
3583 O  OG  . SER   B 122 ? 0.9889 1.1737 0.5778 -0.1347 -0.1467 0.1435  278 SER   B OG  
3584 N  N   . LYS   B 123 ? 0.7143 0.9032 0.3175 -0.1477 -0.1593 0.1080  279 LYS   B N   
3585 C  CA  . LYS   B 123 ? 0.8190 1.0179 0.4215 -0.1571 -0.1641 0.0972  279 LYS   B CA  
3586 C  C   . LYS   B 123 ? 0.7682 0.9454 0.3659 -0.1595 -0.1577 0.0754  279 LYS   B C   
3587 O  O   . LYS   B 123 ? 0.7661 0.9436 0.3519 -0.1706 -0.1557 0.0585  279 LYS   B O   
3588 C  CB  . LYS   B 123 ? 0.8222 1.0375 0.4469 -0.1523 -0.1744 0.1130  279 LYS   B CB  
3589 C  CG  . LYS   B 123 ? 0.8700 1.1001 0.4934 -0.1637 -0.1800 0.1039  279 LYS   B CG  
3590 C  CD  . LYS   B 123 ? 0.8410 1.0902 0.4866 -0.1594 -0.1899 0.1198  279 LYS   B CD  
3591 C  CE  . LYS   B 123 ? 0.7940 1.0640 0.4341 -0.1736 -0.1956 0.1133  279 LYS   B CE  
3592 N  NZ  . LYS   B 123 ? 0.8368 1.1254 0.4989 -0.1703 -0.2047 0.1265  279 LYS   B NZ  
3593 N  N   . PHE   B 124 ? 0.8568 1.0146 0.4645 -0.1492 -0.1542 0.0762  280 PHE   B N   
3594 C  CA  . PHE   B 124 ? 0.7433 0.8784 0.3474 -0.1499 -0.1473 0.0568  280 PHE   B CA  
3595 C  C   . PHE   B 124 ? 0.7660 0.8905 0.3480 -0.1579 -0.1370 0.0381  280 PHE   B C   
3596 O  O   . PHE   B 124 ? 0.8011 0.9190 0.3755 -0.1658 -0.1333 0.0197  280 PHE   B O   
3597 C  CB  . PHE   B 124 ? 0.6911 0.8084 0.3072 -0.1375 -0.1448 0.0637  280 PHE   B CB  
3598 C  CG  . PHE   B 124 ? 0.6871 0.7813 0.3029 -0.1367 -0.1387 0.0465  280 PHE   B CG  
3599 C  CD1 . PHE   B 124 ? 0.6339 0.7273 0.2615 -0.1372 -0.1436 0.0423  280 PHE   B CD1 
3600 C  CD2 . PHE   B 124 ? 0.7202 0.7932 0.3282 -0.1338 -0.1271 0.0355  280 PHE   B CD2 
3601 C  CE1 . PHE   B 124 ? 0.6693 0.7393 0.3051 -0.1331 -0.1352 0.0265  280 PHE   B CE1 
3602 C  CE2 . PHE   B 124 ? 0.6289 0.6792 0.2459 -0.1292 -0.1188 0.0200  280 PHE   B CE2 
3603 C  CZ  . PHE   B 124 ? 0.6931 0.7416 0.3238 -0.1288 -0.1228 0.0157  280 PHE   B CZ  
3604 N  N   . ARG   B 125 ? 0.7026 0.8260 0.2749 -0.1558 -0.1318 0.0430  281 ARG   B N   
3605 C  CA  . ARG   B 125 ? 0.7599 0.8757 0.3122 -0.1627 -0.1217 0.0269  281 ARG   B CA  
3606 C  C   . ARG   B 125 ? 0.8246 0.9555 0.3647 -0.1758 -0.1238 0.0186  281 ARG   B C   
3607 O  O   . ARG   B 125 ? 0.8316 0.9522 0.3591 -0.1830 -0.1160 -0.0011 281 ARG   B O   
3608 C  CB  . ARG   B 125 ? 0.8230 0.9392 0.3688 -0.1583 -0.1172 0.0371  281 ARG   B CB  
3609 C  CG  . ARG   B 125 ? 0.7847 0.8858 0.3418 -0.1463 -0.1145 0.0461  281 ARG   B CG  
3610 C  CD  . ARG   B 125 ? 1.0200 1.1112 0.5655 -0.1446 -0.1039 0.0432  281 ARG   B CD  
3611 N  NE  . ARG   B 125 ? 1.1633 1.2642 0.7130 -0.1396 -0.1070 0.0640  281 ARG   B NE  
3612 C  CZ  . ARG   B 125 ? 0.9123 1.0018 0.4685 -0.1311 -0.1031 0.0733  281 ARG   B CZ  
3613 N  NH1 . ARG   B 125 ? 0.8308 0.9000 0.3885 -0.1270 -0.0959 0.0635  281 ARG   B NH1 
3614 N  NH2 . ARG   B 125 ? 1.0143 1.1127 0.5757 -0.1270 -0.1061 0.0929  281 ARG   B NH2 
3615 N  N   . LYS   B 126 ? 0.7831 0.9384 0.3269 -0.1790 -0.1339 0.0336  282 LYS   B N   
3616 C  CA  . LYS   B 126 ? 0.8264 0.9977 0.3577 -0.1924 -0.1363 0.0267  282 LYS   B CA  
3617 C  C   . LYS   B 126 ? 0.7995 0.9650 0.3320 -0.1995 -0.1364 0.0103  282 LYS   B C   
3618 O  O   . LYS   B 126 ? 0.8319 0.9924 0.3494 -0.2098 -0.1302 -0.0074 282 LYS   B O   
3619 C  CB  . LYS   B 126 ? 0.8920 1.0917 0.4297 -0.1939 -0.1477 0.0475  282 LYS   B CB  
3620 C  CG  . LYS   B 126 ? 0.8914 1.1096 0.4236 -0.2074 -0.1535 0.0421  282 LYS   B CG  
3621 C  CD  . LYS   B 126 ? 1.0610 1.3038 0.6104 -0.2056 -0.1663 0.0621  282 LYS   B CD  
3622 C  CE  . LYS   B 126 ? 1.0157 1.2754 0.5683 -0.2004 -0.1708 0.0844  282 LYS   B CE  
3623 N  NZ  . LYS   B 126 ? 0.9919 1.2627 0.5237 -0.2109 -0.1681 0.0812  282 LYS   B NZ  
3624 N  N   . ILE   B 127 ? 0.7597 0.9250 0.3105 -0.1942 -0.1429 0.0160  283 ILE   B N   
3625 C  CA  . ILE   B 127 ? 0.8656 1.0257 0.4191 -0.2009 -0.1434 0.0016  283 ILE   B CA  
3626 C  C   . ILE   B 127 ? 0.8682 1.0004 0.4122 -0.2018 -0.1307 -0.0207 283 ILE   B C   
3627 O  O   . ILE   B 127 ? 0.9113 1.0388 0.4451 -0.2122 -0.1262 -0.0375 283 ILE   B O   
3628 C  CB  . ILE   B 127 ? 0.7792 0.9431 0.3553 -0.1936 -0.1520 0.0124  283 ILE   B CB  
3629 C  CG1 . ILE   B 127 ? 0.8910 1.0846 0.4772 -0.1945 -0.1641 0.0326  283 ILE   B CG1 
3630 C  CG2 . ILE   B 127 ? 0.8447 0.9989 0.4236 -0.1997 -0.1507 -0.0038 283 ILE   B CG2 
3631 C  CD1 . ILE   B 127 ? 0.8109 1.0095 0.4213 -0.1847 -0.1719 0.0468  283 ILE   B CD1 
3632 N  N   . ILE   B 128 ? 0.8278 0.9410 0.3751 -0.1911 -0.1241 -0.0209 284 ILE   B N   
3633 C  CA  . ILE   B 128 ? 0.7961 0.8827 0.3365 -0.1904 -0.1113 -0.0408 284 ILE   B CA  
3634 C  C   . ILE   B 128 ? 0.9280 1.0123 0.4482 -0.1988 -0.1021 -0.0540 284 ILE   B C   
3635 O  O   . ILE   B 128 ? 0.8616 0.9321 0.3749 -0.2048 -0.0941 -0.0727 284 ILE   B O   
3636 C  CB  . ILE   B 128 ? 0.8107 0.8800 0.3584 -0.1775 -0.1063 -0.0365 284 ILE   B CB  
3637 C  CG1 . ILE   B 128 ? 0.7904 0.8562 0.3576 -0.1704 -0.1133 -0.0292 284 ILE   B CG1 
3638 C  CG2 . ILE   B 128 ? 0.8536 0.8981 0.3925 -0.1764 -0.0916 -0.0555 284 ILE   B CG2 
3639 C  CD1 . ILE   B 128 ? 0.7264 0.7784 0.3016 -0.1582 -0.1107 -0.0214 284 ILE   B CD1 
3640 N  N   . LYS   B 129 ? 0.8333 0.9307 0.3443 -0.1993 -0.1027 -0.0442 285 LYS   B N   
3641 C  CA  . LYS   B 129 ? 0.9617 1.0586 0.4531 -0.2074 -0.0941 -0.0558 285 LYS   B CA  
3642 C  C   . LYS   B 129 ? 0.9813 1.0870 0.4641 -0.2215 -0.0961 -0.0666 285 LYS   B C   
3643 O  O   . LYS   B 129 ? 0.9536 1.0476 0.4235 -0.2282 -0.0860 -0.0845 285 LYS   B O   
3644 C  CB  . LYS   B 129 ? 0.9690 1.0821 0.4532 -0.2064 -0.0964 -0.0409 285 LYS   B CB  
3645 C  CG  . LYS   B 129 ? 1.0184 1.1244 0.4844 -0.2099 -0.0844 -0.0523 285 LYS   B CG  
3646 C  CD  . LYS   B 129 ? 0.9867 1.1099 0.4459 -0.2096 -0.0872 -0.0368 285 LYS   B CD  
3647 C  CE  . LYS   B 129 ? 1.0404 1.1690 0.4789 -0.2199 -0.0803 -0.0470 285 LYS   B CE  
3648 N  NZ  . LYS   B 129 ? 1.0636 1.1700 0.4932 -0.2179 -0.0647 -0.0651 285 LYS   B NZ  
3649 N  N   . GLU   B 130 ? 1.0262 1.1524 0.5169 -0.2261 -0.1088 -0.0557 286 GLU   B N   
3650 C  CA  . GLU   B 130 ? 1.0172 1.1538 0.5006 -0.2404 -0.1116 -0.0648 286 GLU   B CA  
3651 C  C   . GLU   B 130 ? 0.9626 1.0791 0.4504 -0.2428 -0.1063 -0.0823 286 GLU   B C   
3652 O  O   . GLU   B 130 ? 1.0982 1.2105 0.5745 -0.2541 -0.1010 -0.0979 286 GLU   B O   
3653 C  CB  . GLU   B 130 ? 0.9694 1.1355 0.4614 -0.2440 -0.1266 -0.0464 286 GLU   B CB  
3654 C  CG  . GLU   B 130 ? 0.9872 1.1746 0.4722 -0.2446 -0.1310 -0.0305 286 GLU   B CG  
3655 C  CD  . GLU   B 130 ? 1.0336 1.2515 0.5267 -0.2490 -0.1449 -0.0129 286 GLU   B CD  
3656 O  OE1 . GLU   B 130 ? 1.1252 1.3483 0.6308 -0.2507 -0.1515 -0.0120 286 GLU   B OE1 
3657 O  OE2 . GLU   B 130 ? 1.0358 1.2731 0.5226 -0.2514 -0.1488 -0.0003 286 GLU   B OE2 
3658 N  N   . GLU   B 131 ? 1.0137 1.1167 0.5176 -0.2324 -0.1068 -0.0802 287 GLU   B N   
3659 C  CA  . GLU   B 131 ? 0.9957 1.0787 0.5049 -0.2339 -0.1013 -0.0960 287 GLU   B CA  
3660 C  C   . GLU   B 131 ? 1.0509 1.1056 0.5526 -0.2300 -0.0855 -0.1131 287 GLU   B C   
3661 O  O   . GLU   B 131 ? 1.0927 1.1295 0.5951 -0.2332 -0.0784 -0.1288 287 GLU   B O   
3662 C  CB  . GLU   B 131 ? 1.0064 1.0886 0.5364 -0.2252 -0.1090 -0.0861 287 GLU   B CB  
3663 C  CG  . GLU   B 131 ? 1.0013 1.0805 0.5380 -0.2322 -0.1110 -0.0950 287 GLU   B CG  
3664 C  CD  . GLU   B 131 ? 1.1190 1.2212 0.6475 -0.2466 -0.1179 -0.0941 287 GLU   B CD  
3665 O  OE1 . GLU   B 131 ? 1.1629 1.2913 0.6937 -0.2475 -0.1285 -0.0771 287 GLU   B OE1 
3666 O  OE2 . GLU   B 131 ? 1.2614 1.3556 0.7822 -0.2571 -0.1126 -0.1100 287 GLU   B OE2 
3667 N  N   . ILE   B 132 ? 1.0611 1.1121 0.5561 -0.2234 -0.0796 -0.1100 288 ILE   B N   
3668 C  CA  . ILE   B 132 ? 1.0388 1.0660 0.5259 -0.2203 -0.0640 -0.1259 288 ILE   B CA  
3669 C  C   . ILE   B 132 ? 1.0492 1.0777 0.5177 -0.2326 -0.0570 -0.1395 288 ILE   B C   
3670 O  O   . ILE   B 132 ? 1.0609 1.0684 0.5248 -0.2336 -0.0444 -0.1568 288 ILE   B O   
3671 C  CB  . ILE   B 132 ? 1.0075 1.0309 0.4955 -0.2087 -0.0599 -0.1171 288 ILE   B CB  
3672 C  CG1 . ILE   B 132 ? 1.0141 1.0268 0.5200 -0.1965 -0.0624 -0.1099 288 ILE   B CG1 
3673 C  CG2 . ILE   B 132 ? 1.0350 1.0420 0.5113 -0.2074 -0.0443 -0.1310 288 ILE   B CG2 
3674 C  CD1 . ILE   B 132 ? 0.9360 0.9310 0.4522 -0.1961 -0.0596 -0.1216 288 ILE   B CD1 
3675 N  N   . ASN   B 133 ? 1.0478 1.1006 0.5057 -0.2422 -0.0646 -0.1320 289 ASN   B N   
3676 C  CA  . ASN   B 133 ? 1.0835 1.1376 0.5225 -0.2545 -0.0577 -0.1451 289 ASN   B CA  
3677 C  C   . ASN   B 133 ? 1.0619 1.1057 0.4995 -0.2645 -0.0545 -0.1613 289 ASN   B C   
3678 O  O   . ASN   B 133 ? 1.1703 1.2051 0.5937 -0.2726 -0.0444 -0.1767 289 ASN   B O   
3679 C  CB  . ASN   B 133 ? 1.0490 1.1326 0.4769 -0.2638 -0.0671 -0.1334 289 ASN   B CB  
3680 C  CG  . ASN   B 133 ? 1.1703 1.2671 0.6028 -0.2541 -0.0731 -0.1136 289 ASN   B CG  
3681 O  OD1 . ASN   B 133 ? 1.2761 1.3592 0.7103 -0.2434 -0.0654 -0.1133 289 ASN   B OD1 
3682 N  ND2 . ASN   B 133 ? 1.0282 1.1522 0.4626 -0.2583 -0.0864 -0.0968 289 ASN   B ND2 
3683 N  N   . ASP   B 134 ? 1.1629 1.2070 0.6150 -0.2641 -0.0620 -0.1582 290 ASP   B N   
3684 C  CA  . ASP   B 134 ? 1.1783 1.2088 0.6304 -0.2725 -0.0574 -0.1740 290 ASP   B CA  
3685 C  C   . ASP   B 134 ? 1.1800 1.1778 0.6379 -0.2629 -0.0430 -0.1875 290 ASP   B C   
3686 O  O   . ASP   B 134 ? 1.4201 1.4015 0.8675 -0.2672 -0.0303 -0.2037 290 ASP   B O   
3687 C  CB  . ASP   B 134 ? 1.0677 1.1105 0.5337 -0.2756 -0.0702 -0.1660 290 ASP   B CB  
3688 C  CG  . ASP   B 134 ? 1.0852 1.1079 0.5569 -0.2794 -0.0642 -0.1808 290 ASP   B CG  
3689 O  OD1 . ASP   B 134 ? 1.2702 1.2734 0.7560 -0.2687 -0.0603 -0.1826 290 ASP   B OD1 
3690 O  OD2 . ASP   B 134 ? 1.2935 1.3197 0.7550 -0.2938 -0.0631 -0.1907 290 ASP   B OD2 
3691 N  N   . ILE   B 135 ? 1.1957 1.1843 0.6705 -0.2498 -0.0447 -0.1804 291 ILE   B N   
3692 C  CA  . ILE   B 135 ? 1.1304 1.0896 0.6146 -0.2396 -0.0327 -0.1905 291 ILE   B CA  
3693 C  C   . ILE   B 135 ? 1.2591 1.2005 0.7322 -0.2370 -0.0164 -0.2035 291 ILE   B C   
3694 O  O   . ILE   B 135 ? 1.3305 1.2776 0.7965 -0.2325 -0.0138 -0.1985 291 ILE   B O   
3695 C  CB  . ILE   B 135 ? 1.0500 1.0070 0.5504 -0.2251 -0.0372 -0.1777 291 ILE   B CB  
3696 N  N   . ASP   B 139 ? 1.2110 1.0749 0.6777 -0.2051 0.0470  -0.2408 295 ASP   B N   
3697 C  CA  . ASP   B 139 ? 1.1631 1.0534 0.6260 -0.2101 0.0306  -0.2260 295 ASP   B CA  
3698 C  C   . ASP   B 139 ? 1.1836 1.0787 0.6585 -0.1975 0.0251  -0.2110 295 ASP   B C   
3699 O  O   . ASP   B 139 ? 1.2120 1.0900 0.7005 -0.1859 0.0318  -0.2121 295 ASP   B O   
3700 C  CB  . ASP   B 139 ? 1.2631 1.1709 0.7057 -0.2201 0.0300  -0.2262 295 ASP   B CB  
3701 C  CG  . ASP   B 139 ? 1.1999 1.1046 0.6364 -0.2122 0.0411  -0.2267 295 ASP   B CG  
3702 O  OD1 . ASP   B 139 ? 1.3056 1.1975 0.7542 -0.1987 0.0478  -0.2246 295 ASP   B OD1 
3703 O  OD2 . ASP   B 139 ? 1.2299 1.1458 0.6496 -0.2200 0.0432  -0.2290 295 ASP   B OD2 
3704 N  N   . VAL   B 140 ? 1.2048 1.1231 0.6750 -0.2000 0.0129  -0.1966 296 VAL   B N   
3705 C  CA  . VAL   B 140 ? 0.9978 0.9225 0.4776 -0.1896 0.0067  -0.1812 296 VAL   B CA  
3706 C  C   . VAL   B 140 ? 1.0370 0.9859 0.5055 -0.1938 -0.0014 -0.1685 296 VAL   B C   
3707 O  O   . VAL   B 140 ? 1.1403 1.1064 0.5998 -0.2050 -0.0099 -0.1660 296 VAL   B O   
3708 C  CB  . VAL   B 140 ? 1.0106 0.9354 0.5066 -0.1867 -0.0043 -0.1734 296 VAL   B CB  
3709 C  CG1 . VAL   B 140 ? 1.1204 1.0610 0.6136 -0.1988 -0.0164 -0.1713 296 VAL   B CG1 
3710 C  CG2 . VAL   B 140 ? 0.9902 0.9242 0.4941 -0.1777 -0.0120 -0.1562 296 VAL   B CG2 
3711 N  N   . ILE   B 141 ? 0.9867 0.9370 0.4558 -0.1851 0.0020  -0.1604 297 ILE   B N   
3712 C  CA  . ILE   B 141 ? 0.9291 0.9003 0.3885 -0.1874 -0.0040 -0.1472 297 ILE   B CA  
3713 C  C   . ILE   B 141 ? 0.9416 0.9206 0.4131 -0.1794 -0.0142 -0.1289 297 ILE   B C   
3714 O  O   . ILE   B 141 ? 1.0205 0.9852 0.5039 -0.1694 -0.0104 -0.1284 297 ILE   B O   
3715 C  CB  . ILE   B 141 ? 1.0455 1.0124 0.4945 -0.1846 0.0093  -0.1526 297 ILE   B CB  
3716 C  CG1 . ILE   B 141 ? 1.0171 0.9733 0.4553 -0.1914 0.0210  -0.1717 297 ILE   B CG1 
3717 C  CG2 . ILE   B 141 ? 1.0079 0.9972 0.4466 -0.1878 0.0031  -0.1385 297 ILE   B CG2 
3718 C  CD1 . ILE   B 141 ? 0.9873 0.9588 0.4121 -0.2062 0.0137  -0.1741 297 ILE   B CD1 
3719 N  N   . MET   B 142 ? 0.9414 0.9426 0.4103 -0.1837 -0.0269 -0.1136 298 MET   B N   
3720 C  CA  . MET   B 142 ? 0.9407 0.9499 0.4197 -0.1760 -0.0356 -0.0947 298 MET   B CA  
3721 C  C   . MET   B 142 ? 0.9925 1.0080 0.4645 -0.1724 -0.0312 -0.0859 298 MET   B C   
3722 O  O   . MET   B 142 ? 1.1395 1.1650 0.5973 -0.1789 -0.0284 -0.0878 298 MET   B O   
3723 C  CB  . MET   B 142 ? 1.0667 1.0967 0.5504 -0.1808 -0.0518 -0.0802 298 MET   B CB  
3724 C  CG  . MET   B 142 ? 1.1085 1.1533 0.5962 -0.1754 -0.0597 -0.0582 298 MET   B CG  
3725 S  SD  . MET   B 142 ? 1.4086 1.4727 0.9108 -0.1744 -0.0778 -0.0371 298 MET   B SD  
3726 C  CE  . MET   B 142 ? 1.0605 1.1373 0.5632 -0.1682 -0.0811 -0.0146 298 MET   B CE  
3727 N  N   . LYS   B 143 ? 1.0182 1.0279 0.4999 -0.1624 -0.0307 -0.0761 299 LYS   B N   
3728 C  CA  . LYS   B 143 ? 1.0464 1.0635 0.5249 -0.1584 -0.0290 -0.0634 299 LYS   B CA  
3729 C  C   . LYS   B 143 ? 0.9763 1.0031 0.4664 -0.1540 -0.0418 -0.0426 299 LYS   B C   
3730 O  O   . LYS   B 143 ? 1.0004 1.0181 0.5035 -0.1485 -0.0456 -0.0403 299 LYS   B O   
3731 C  CB  . LYS   B 143 ? 1.0853 1.0851 0.5656 -0.1505 -0.0151 -0.0708 299 LYS   B CB  
3732 C  CG  . LYS   B 143 ? 1.0697 1.0747 0.5501 -0.1452 -0.0129 -0.0570 299 LYS   B CG  
3733 C  CD  . LYS   B 143 ? 0.9820 1.0072 0.4515 -0.1514 -0.0179 -0.0461 299 LYS   B CD  
3734 C  CE  . LYS   B 143 ? 1.2031 1.2300 0.6665 -0.1488 -0.0084 -0.0426 299 LYS   B CE  
3735 N  NZ  . LYS   B 143 ? 1.1663 1.1810 0.6231 -0.1481 0.0073  -0.0611 299 LYS   B NZ  
3736 N  N   . ARG   B 144 ? 1.0939 1.1389 0.5800 -0.1563 -0.0483 -0.0272 300 ARG   B N   
3737 C  CA  . ARG   B 144 ? 1.0619 1.1159 0.5600 -0.1511 -0.0593 -0.0058 300 ARG   B CA  
3738 C  C   . ARG   B 144 ? 1.0455 1.0914 0.5476 -0.1430 -0.0534 0.0031  300 ARG   B C   
3739 O  O   . ARG   B 144 ? 1.2097 1.2590 0.7023 -0.1441 -0.0465 0.0041  300 ARG   B O   
3740 C  CB  . ARG   B 144 ? 0.9528 1.0299 0.4465 -0.1569 -0.0690 0.0078  300 ARG   B CB  
3741 N  N   . LYS   B 145 ? 1.1292 1.1646 0.6453 -0.1354 -0.0560 0.0098  301 LYS   B N   
3742 C  CA  . LYS   B 145 ? 1.0971 1.1230 0.6221 -0.1268 -0.0498 0.0176  301 LYS   B CA  
3743 C  C   . LYS   B 145 ? 1.1657 1.2046 0.6901 -0.1263 -0.0555 0.0393  301 LYS   B C   
3744 O  O   . LYS   B 145 ? 1.1885 1.2200 0.7247 -0.1187 -0.0510 0.0479  301 LYS   B O   
3745 C  CB  . LYS   B 145 ? 1.0644 1.0742 0.6166 -0.1153 -0.0497 0.0176  301 LYS   B CB  
3746 N  N   . GLY   B 148 ? 0.6826 0.6970 0.3193 -0.0824 -0.0828 0.1029  304 GLY   B N   
3747 C  CA  . GLY   B 148 ? 0.6583 0.6796 0.2876 -0.0883 -0.0872 0.0903  304 GLY   B CA  
3748 C  C   . GLY   B 148 ? 0.7671 0.7749 0.4125 -0.0830 -0.0859 0.0784  304 GLY   B C   
3749 O  O   . GLY   B 148 ? 0.8327 0.8472 0.4812 -0.0852 -0.0930 0.0761  304 GLY   B O   
3750 N  N   . PRO   B 150 ? 0.8187 0.7847 0.4698 -0.0777 -0.0604 0.0299  306 PRO   B N   
3751 C  CA  . PRO   B 150 ? 0.7569 0.7288 0.3959 -0.0857 -0.0636 0.0188  306 PRO   B CA  
3752 C  C   . PRO   B 150 ? 0.7837 0.7744 0.4040 -0.0953 -0.0707 0.0255  306 PRO   B C   
3753 O  O   . PRO   B 150 ? 0.7988 0.7961 0.4063 -0.0983 -0.0682 0.0310  306 PRO   B O   
3754 C  CB  . PRO   B 150 ? 0.7997 0.7614 0.4289 -0.0876 -0.0522 0.0011  306 PRO   B CB  
3755 C  CG  . PRO   B 150 ? 0.8912 0.8459 0.5255 -0.0815 -0.0437 0.0042  306 PRO   B CG  
3756 C  CD  . PRO   B 150 ? 0.8535 0.8089 0.5030 -0.0752 -0.0486 0.0210  306 PRO   B CD  
3757 N  N   . ALA   B 151 ? 0.7779 0.7786 0.3962 -0.1007 -0.0797 0.0253  307 ALA   B N   
3758 C  CA  . ALA   B 151 ? 0.8032 0.8248 0.4044 -0.1105 -0.0878 0.0327  307 ALA   B CA  
3759 C  C   . ALA   B 151 ? 0.8269 0.8516 0.4027 -0.1221 -0.0829 0.0169  307 ALA   B C   
3760 O  O   . ALA   B 151 ? 0.8239 0.8618 0.3810 -0.1293 -0.0836 0.0213  307 ALA   B O   
3761 C  CB  . ALA   B 151 ? 0.6965 0.7302 0.3067 -0.1122 -0.0999 0.0396  307 ALA   B CB  
3762 N  N   . VAL   B 152 ? 0.8203 0.8325 0.3953 -0.1240 -0.0773 -0.0014 308 VAL   B N   
3763 C  CA  . VAL   B 152 ? 0.8520 0.8642 0.4038 -0.1350 -0.0714 -0.0186 308 VAL   B CA  
3764 C  C   . VAL   B 152 ? 0.8408 0.8304 0.3980 -0.1293 -0.0582 -0.0349 308 VAL   B C   
3765 O  O   . VAL   B 152 ? 0.7793 0.7561 0.3569 -0.1205 -0.0571 -0.0361 308 VAL   B O   
3766 C  CB  . VAL   B 152 ? 0.8081 0.8315 0.3531 -0.1457 -0.0798 -0.0243 308 VAL   B CB  
3767 C  CG1 . VAL   B 152 ? 0.9135 0.9297 0.4463 -0.1530 -0.0704 -0.0452 308 VAL   B CG1 
3768 C  CG2 . VAL   B 152 ? 0.7395 0.7878 0.2844 -0.1493 -0.0906 -0.0079 308 VAL   B CG2 
3769 N  N   . THR   B 153 ? 0.8693 0.8550 0.4083 -0.1340 -0.0477 -0.0466 309 THR   B N   
3770 C  CA  . THR   B 153 ? 0.9288 0.8948 0.4698 -0.1301 -0.0344 -0.0635 309 THR   B CA  
3771 C  C   . THR   B 153 ? 0.8907 0.8561 0.4117 -0.1419 -0.0301 -0.0810 309 THR   B C   
3772 O  O   . THR   B 153 ? 0.8694 0.8480 0.3785 -0.1483 -0.0301 -0.0804 309 THR   B O   
3773 C  CB  . THR   B 153 ? 0.8524 0.8135 0.3936 -0.1234 -0.0236 -0.0618 309 THR   B CB  
3774 O  OG1 . THR   B 153 ? 0.8153 0.7764 0.3771 -0.1129 -0.0274 -0.0459 309 THR   B OG1 
3775 C  CG2 . THR   B 153 ? 0.8340 0.7765 0.3782 -0.1189 -0.0095 -0.0784 309 THR   B CG2 
3776 N  N   . LEU   B 154 ? 0.9480 0.8987 0.4746 -0.1420 -0.0263 -0.0946 310 LEU   B N   
3777 C  CA  . LEU   B 154 ? 0.8495 0.7958 0.3689 -0.1491 -0.0200 -0.1111 310 LEU   B CA  
3778 C  C   . LEU   B 154 ? 0.9053 0.8321 0.4236 -0.1438 -0.0031 -0.1254 310 LEU   B C   
3779 O  O   . LEU   B 154 ? 0.8162 0.7282 0.3450 -0.1347 0.0024  -0.1262 310 LEU   B O   
3780 C  CB  . LEU   B 154 ? 0.7917 0.7341 0.3197 -0.1528 -0.0265 -0.1162 310 LEU   B CB  
3781 C  CG  . LEU   B 154 ? 0.9183 0.8796 0.4511 -0.1570 -0.0431 -0.1021 310 LEU   B CG  
3782 C  CD1 . LEU   B 154 ? 0.8966 0.8532 0.4377 -0.1612 -0.0472 -0.1095 310 LEU   B CD1 
3783 C  CD2 . LEU   B 154 ? 0.9170 0.9003 0.4368 -0.1656 -0.0483 -0.0962 310 LEU   B CD2 
3784 N  N   . LEU   B 155 ? 0.9086 0.8356 0.4151 -0.1492 0.0052  -0.1362 311 LEU   B N   
3785 C  CA  . LEU   B 155 ? 0.9742 0.8831 0.4806 -0.1445 0.0218  -0.1508 311 LEU   B CA  
3786 C  C   . LEU   B 155 ? 0.9137 0.8120 0.4199 -0.1506 0.0250  -0.1656 311 LEU   B C   
3787 O  O   . LEU   B 155 ? 1.0882 0.9942 0.5819 -0.1607 0.0244  -0.1715 311 LEU   B O   
3788 C  CB  . LEU   B 155 ? 0.8966 0.8124 0.3900 -0.1455 0.0303  -0.1518 311 LEU   B CB  
3789 C  CG  . LEU   B 155 ? 1.0410 0.9394 0.5345 -0.1405 0.0482  -0.1667 311 LEU   B CG  
3790 C  CD1 . LEU   B 155 ? 0.9782 0.8612 0.4878 -0.1277 0.0554  -0.1659 311 LEU   B CD1 
3791 C  CD2 . LEU   B 155 ? 1.0487 0.9561 0.5286 -0.1424 0.0559  -0.1676 311 LEU   B CD2 
3792 N  N   . ILE   B 156 ? 1.0052 0.8860 0.5253 -0.1449 0.0283  -0.1712 312 ILE   B N   
3793 C  CA  . ILE   B 156 ? 0.9957 0.8641 0.5177 -0.1500 0.0322  -0.1846 312 ILE   B CA  
3794 C  C   . ILE   B 156 ? 1.0887 0.9402 0.6089 -0.1459 0.0500  -0.1983 312 ILE   B C   
3795 O  O   . ILE   B 156 ? 1.1647 1.0044 0.6943 -0.1344 0.0598  -0.1984 312 ILE   B O   
3796 C  CB  . ILE   B 156 ? 1.0432 0.9010 0.5821 -0.1458 0.0273  -0.1832 312 ILE   B CB  
3797 C  CG1 . ILE   B 156 ? 0.9587 0.8340 0.4999 -0.1499 0.0097  -0.1697 312 ILE   B CG1 
3798 C  CG2 . ILE   B 156 ? 1.0745 0.9175 0.6165 -0.1503 0.0331  -0.1970 312 ILE   B CG2 
3799 C  CD1 . ILE   B 156 ? 0.9944 0.8605 0.5525 -0.1448 0.0047  -0.1666 312 ILE   B CD1 
3800 N  N   . SER   B 157 ? 1.1822 1.0327 0.6907 -0.1553 0.0545  -0.2096 313 SER   B N   
3801 C  CA  . SER   B 157 ? 1.0911 0.9270 0.5956 -0.1528 0.0716  -0.2228 313 SER   B CA  
3802 C  C   . SER   B 157 ? 1.2075 1.0508 0.7068 -0.1464 0.0777  -0.2175 313 SER   B C   
3803 O  O   . SER   B 157 ? 1.2739 1.1366 0.7608 -0.1524 0.0700  -0.2097 313 SER   B O   
3804 C  CB  . SER   B 157 ? 1.0638 0.8756 0.5847 -0.1443 0.0815  -0.2305 313 SER   B CB  
3805 O  OG  . SER   B 157 ? 1.3019 1.1078 0.8368 -0.1302 0.0860  -0.2236 313 SER   B OG  
3806 N  N   . GLU   B 158 ? 1.2032 1.0330 0.7120 -0.1344 0.0912  -0.2204 314 GLU   B N   
3807 C  CA  . GLU   B 158 ? 1.0951 0.9330 0.6006 -0.1281 0.0970  -0.2145 314 GLU   B CA  
3808 C  C   . GLU   B 158 ? 1.0868 0.9219 0.6079 -0.1157 0.0971  -0.2043 314 GLU   B C   
3809 O  O   . GLU   B 158 ? 1.1515 0.9981 0.6695 -0.1125 0.0969  -0.1952 314 GLU   B O   
3810 C  CB  . GLU   B 158 ? 1.2156 1.0438 0.7169 -0.1251 0.1146  -0.2262 314 GLU   B CB  
3811 C  CG  . GLU   B 158 ? 1.0222 0.8654 0.5036 -0.1337 0.1154  -0.2276 314 GLU   B CG  
3812 C  CD  . GLU   B 158 ? 1.2651 1.1114 0.7320 -0.1484 0.1100  -0.2357 314 GLU   B CD  
3813 O  OE1 . GLU   B 158 ? 1.3180 1.1484 0.7845 -0.1506 0.1193  -0.2495 314 GLU   B OE1 
3814 O  OE2 . GLU   B 158 ? 1.3189 1.1838 0.7750 -0.1578 0.0966  -0.2279 314 GLU   B OE2 
3815 N  N   . LYS   B 159 ? 1.1412 0.9620 0.6786 -0.1093 0.0973  -0.2052 315 LYS   B N   
3816 C  CA  . LYS   B 159 ? 1.0737 0.8898 0.6263 -0.0971 0.0995  -0.1970 315 LYS   B CA  
3817 C  C   . LYS   B 159 ? 1.1272 0.9487 0.6856 -0.0978 0.0844  -0.1857 315 LYS   B C   
3818 O  O   . LYS   B 159 ? 1.1685 0.9952 0.7310 -0.0919 0.0821  -0.1751 315 LYS   B O   
3819 C  CB  . LYS   B 159 ? 1.0724 0.8677 0.6415 -0.0867 0.1129  -0.2048 315 LYS   B CB  
3820 C  CG  . LYS   B 159 ? 1.1305 0.9157 0.6945 -0.0896 0.1247  -0.2188 315 LYS   B CG  
3821 C  CD  . LYS   B 159 ? 1.1910 0.9565 0.7732 -0.0777 0.1386  -0.2242 315 LYS   B CD  
3822 C  CE  . LYS   B 159 ? 1.1915 0.9442 0.7869 -0.0771 0.1333  -0.2247 315 LYS   B CE  
3823 N  NZ  . LYS   B 159 ? 1.2167 0.9553 0.8340 -0.0623 0.1434  -0.2225 315 LYS   B NZ  
3824 N  N   . ILE   B 160 ? 1.0387 0.8596 0.5974 -0.1052 0.0741  -0.1873 316 ILE   B N   
3825 C  CA  . ILE   B 160 ? 0.9447 0.7697 0.5105 -0.1052 0.0602  -0.1768 316 ILE   B CA  
3826 C  C   . ILE   B 160 ? 1.0357 0.8822 0.5896 -0.1123 0.0470  -0.1651 316 ILE   B C   
3827 O  O   . ILE   B 160 ? 0.9774 0.8361 0.5178 -0.1220 0.0431  -0.1668 316 ILE   B O   
3828 C  CB  . ILE   B 160 ? 1.0300 0.8473 0.6023 -0.1101 0.0546  -0.1824 316 ILE   B CB  
3829 C  CG1 . ILE   B 160 ? 1.1783 0.9747 0.7613 -0.1041 0.0684  -0.1939 316 ILE   B CG1 
3830 C  CG2 . ILE   B 160 ? 0.8599 0.6796 0.4437 -0.1075 0.0422  -0.1716 316 ILE   B CG2 
3831 C  CD1 . ILE   B 160 ? 1.1138 0.8999 0.7092 -0.1048 0.0634  -0.1957 316 ILE   B CD1 
3832 N  N   . SER   B 161 ? 0.9626 0.8171 0.5319 -0.1047 0.0385  -0.1492 317 SER   B N   
3833 C  CA  . SER   B 161 ? 0.8987 0.7732 0.4632 -0.1088 0.0255  -0.1348 317 SER   B CA  
3834 C  C   . SER   B 161 ? 0.8799 0.7581 0.4641 -0.1042 0.0125  -0.1223 317 SER   B C   
3835 O  O   . SER   B 161 ? 0.8342 0.7030 0.4396 -0.0936 0.0147  -0.1192 317 SER   B O   
3836 C  CB  . SER   B 161 ? 0.8167 0.6994 0.3808 -0.1031 0.0301  -0.1259 317 SER   B CB  
3837 O  OG  . SER   B 161 ? 0.8605 0.7447 0.4475 -0.0920 0.0255  -0.1116 317 SER   B OG  
3838 N  N   . VAL   B 162 ? 0.7997 0.6925 0.3772 -0.1123 -0.0007 -0.1149 318 VAL   B N   
3839 C  CA  . VAL   B 162 ? 0.8344 0.7317 0.4294 -0.1089 -0.0130 -0.1036 318 VAL   B CA  
3840 C  C   . VAL   B 162 ? 0.8280 0.7438 0.4219 -0.1095 -0.0235 -0.0864 318 VAL   B C   
3841 O  O   . VAL   B 162 ? 0.8020 0.7321 0.3781 -0.1198 -0.0294 -0.0847 318 VAL   B O   
3842 C  CB  . VAL   B 162 ? 0.8595 0.7562 0.4508 -0.1181 -0.0193 -0.1112 318 VAL   B CB  
3843 C  CG1 . VAL   B 162 ? 0.8606 0.7610 0.4730 -0.1127 -0.0303 -0.0995 318 VAL   B CG1 
3844 C  CG2 . VAL   B 162 ? 0.8435 0.7208 0.4319 -0.1195 -0.0076 -0.1293 318 VAL   B CG2 
3845 N  N   . ASP   B 163 ? 0.7603 0.6759 0.3733 -0.0989 -0.0259 -0.0735 319 ASP   B N   
3846 C  CA  . ASP   B 163 ? 0.7809 0.7112 0.3970 -0.0980 -0.0357 -0.0561 319 ASP   B CA  
3847 C  C   . ASP   B 163 ? 0.7445 0.6804 0.3725 -0.0983 -0.0477 -0.0488 319 ASP   B C   
3848 O  O   . ASP   B 163 ? 0.7996 0.7254 0.4440 -0.0927 -0.0475 -0.0515 319 ASP   B O   
3849 C  CB  . ASP   B 163 ? 0.7160 0.6424 0.3460 -0.0874 -0.0316 -0.0464 319 ASP   B CB  
3850 C  CG  . ASP   B 163 ? 0.8122 0.7415 0.4284 -0.0889 -0.0233 -0.0472 319 ASP   B CG  
3851 O  OD1 . ASP   B 163 ? 1.1430 1.0734 0.7676 -0.0827 -0.0216 -0.0372 319 ASP   B OD1 
3852 O  OD2 . ASP   B 163 ? 0.8323 0.7634 0.4289 -0.0967 -0.0183 -0.0578 319 ASP   B OD2 
3853 N  N   . ILE   B 164 ? 0.7336 0.6868 0.3538 -0.1047 -0.0580 -0.0389 320 ILE   B N   
3854 C  CA  . ILE   B 164 ? 0.6394 0.6013 0.2700 -0.1059 -0.0696 -0.0314 320 ILE   B CA  
3855 C  C   . ILE   B 164 ? 0.6688 0.6418 0.3088 -0.1004 -0.0771 -0.0114 320 ILE   B C   
3856 O  O   . ILE   B 164 ? 0.6011 0.5863 0.2285 -0.1043 -0.0793 -0.0032 320 ILE   B O   
3857 C  CB  . ILE   B 164 ? 0.7533 0.7278 0.3667 -0.1196 -0.0760 -0.0375 320 ILE   B CB  
3858 C  CG1 . ILE   B 164 ? 0.7003 0.6610 0.3029 -0.1256 -0.0670 -0.0584 320 ILE   B CG1 
3859 C  CG2 . ILE   B 164 ? 0.7574 0.7409 0.3850 -0.1196 -0.0874 -0.0298 320 ILE   B CG2 
3860 C  CD1 . ILE   B 164 ? 0.7294 0.7013 0.3106 -0.1413 -0.0713 -0.0670 320 ILE   B CD1 
3861 N  N   . THR   B 165 ? 0.6191 0.5875 0.2812 -0.0914 -0.0803 -0.0037 321 THR   B N   
3862 C  CA  . THR   B 165 ? 0.6241 0.5995 0.2990 -0.0848 -0.0862 0.0147  321 THR   B CA  
3863 C  C   . THR   B 165 ? 0.6378 0.6255 0.3224 -0.0858 -0.0974 0.0230  321 THR   B C   
3864 O  O   . THR   B 165 ? 0.5810 0.5638 0.2749 -0.0855 -0.0985 0.0157  321 THR   B O   
3865 C  CB  . THR   B 165 ? 0.5852 0.5446 0.2781 -0.0733 -0.0796 0.0166  321 THR   B CB  
3866 O  OG1 . THR   B 165 ? 0.6266 0.5789 0.3107 -0.0726 -0.0702 0.0121  321 THR   B OG1 
3867 C  CG2 . THR   B 165 ? 0.6129 0.5757 0.3219 -0.0661 -0.0849 0.0337  321 THR   B CG2 
3868 N  N   . LEU   B 166 ? 0.6118 0.6165 0.2944 -0.0873 -0.1055 0.0388  322 LEU   B N   
3869 C  CA  . LEU   B 166 ? 0.5616 0.5798 0.2572 -0.0860 -0.1159 0.0507  322 LEU   B CA  
3870 C  C   . LEU   B 166 ? 0.5906 0.5999 0.3100 -0.0730 -0.1149 0.0620  322 LEU   B C   
3871 O  O   . LEU   B 166 ? 0.5800 0.5812 0.3020 -0.0671 -0.1098 0.0685  322 LEU   B O   
3872 C  CB  . LEU   B 166 ? 0.6155 0.6574 0.2993 -0.0928 -0.1249 0.0642  322 LEU   B CB  
3873 C  CG  . LEU   B 166 ? 0.6699 0.7287 0.3691 -0.0896 -0.1357 0.0812  322 LEU   B CG  
3874 C  CD1 . LEU   B 166 ? 0.7137 0.7772 0.4191 -0.0940 -0.1406 0.0726  322 LEU   B CD1 
3875 C  CD2 . LEU   B 166 ? 0.7080 0.7916 0.3951 -0.0960 -0.1443 0.0963  322 LEU   B CD2 
3876 N  N   . ALA   B 167 ? 0.5932 0.6039 0.3297 -0.0693 -0.1194 0.0640  323 ALA   B N   
3877 C  CA  . ALA   B 167 ? 0.6093 0.6104 0.3683 -0.0574 -0.1175 0.0727  323 ALA   B CA  
3878 C  C   . ALA   B 167 ? 0.6951 0.7100 0.4695 -0.0548 -0.1263 0.0837  323 ALA   B C   
3879 O  O   . ALA   B 167 ? 0.6871 0.7069 0.4644 -0.0589 -0.1299 0.0763  323 ALA   B O   
3880 C  CB  . ALA   B 167 ? 0.5480 0.5286 0.3153 -0.0528 -0.1092 0.0591  323 ALA   B CB  
3881 N  N   . LEU   B 168 ? 0.6229 0.6429 0.4089 -0.0475 -0.1289 0.1013  324 LEU   B N   
3882 C  CA  . LEU   B 168 ? 0.5747 0.6057 0.3795 -0.0425 -0.1354 0.1125  324 LEU   B CA  
3883 C  C   . LEU   B 168 ? 0.6336 0.6480 0.4565 -0.0346 -0.1298 0.1057  324 LEU   B C   
3884 O  O   . LEU   B 168 ? 0.6148 0.6099 0.4412 -0.0290 -0.1214 0.1014  324 LEU   B O   
3885 C  CB  . LEU   B 168 ? 0.6198 0.6590 0.4330 -0.0357 -0.1382 0.1339  324 LEU   B CB  
3886 C  CG  . LEU   B 168 ? 0.6079 0.6634 0.4040 -0.0421 -0.1432 0.1440  324 LEU   B CG  
3887 C  CD1 . LEU   B 168 ? 0.6340 0.6946 0.4418 -0.0335 -0.1447 0.1665  324 LEU   B CD1 
3888 C  CD2 . LEU   B 168 ? 0.6044 0.6841 0.3893 -0.0534 -0.1530 0.1422  324 LEU   B CD2 
3889 N  N   . GLU   B 169 ? 0.6451 0.6682 0.4794 -0.0348 -0.1347 0.1047  325 GLU   B N   
3890 C  CA  . GLU   B 169 ? 0.5546 0.5646 0.4063 -0.0278 -0.1301 0.0992  325 GLU   B CA  
3891 C  C   . GLU   B 169 ? 0.6535 0.6706 0.5265 -0.0183 -0.1327 0.1152  325 GLU   B C   
3892 O  O   . GLU   B 169 ? 0.5908 0.6292 0.4675 -0.0199 -0.1412 0.1269  325 GLU   B O   
3893 C  CB  . GLU   B 169 ? 0.5778 0.5904 0.4282 -0.0346 -0.1322 0.0856  325 GLU   B CB  
3894 C  CG  . GLU   B 169 ? 0.5983 0.5984 0.4665 -0.0277 -0.1274 0.0800  325 GLU   B CG  
3895 C  CD  . GLU   B 169 ? 0.5530 0.5559 0.4198 -0.0349 -0.1295 0.0677  325 GLU   B CD  
3896 O  OE1 . GLU   B 169 ? 0.6648 0.6863 0.5352 -0.0396 -0.1376 0.0721  325 GLU   B OE1 
3897 O  OE2 . GLU   B 169 ? 0.6004 0.5874 0.4625 -0.0363 -0.1232 0.0540  325 GLU   B OE2 
3898 N  N   . SER   B 170 ? 0.6201 0.6201 0.5072 -0.0088 -0.1253 0.1157  326 SER   B N   
3899 C  CA  . SER   B 170 ? 0.6105 0.6137 0.5190 0.0012  -0.1256 0.1292  326 SER   B CA  
3900 C  C   . SER   B 170 ? 0.5849 0.5760 0.5076 0.0060  -0.1202 0.1203  326 SER   B C   
3901 O  O   . SER   B 170 ? 0.5621 0.5336 0.4824 0.0074  -0.1122 0.1099  326 SER   B O   
3902 C  CB  . SER   B 170 ? 0.5805 0.5739 0.4931 0.0089  -0.1207 0.1415  326 SER   B CB  
3903 O  OG  . SER   B 170 ? 0.6522 0.6462 0.5867 0.0192  -0.1194 0.1532  326 SER   B OG  
3904 N  N   . LYS   B 171 ? 0.5836 0.5875 0.5212 0.0084  -0.1245 0.1248  327 LYS   B N   
3905 C  CA  . LYS   B 171 ? 0.5932 0.5868 0.5447 0.0131  -0.1192 0.1173  327 LYS   B CA  
3906 C  C   . LYS   B 171 ? 0.5358 0.5212 0.5062 0.0250  -0.1133 0.1273  327 LYS   B C   
3907 O  O   . LYS   B 171 ? 0.7338 0.7160 0.7187 0.0298  -0.1099 0.1245  327 LYS   B O   
3908 C  CB  . LYS   B 171 ? 0.6318 0.6419 0.5890 0.0083  -0.1257 0.1140  327 LYS   B CB  
3909 C  CG  . LYS   B 171 ? 0.6874 0.7001 0.6260 -0.0040 -0.1292 0.1004  327 LYS   B CG  
3910 C  CD  . LYS   B 171 ? 0.7065 0.7346 0.6501 -0.0102 -0.1354 0.0967  327 LYS   B CD  
3911 C  CE  . LYS   B 171 ? 0.6527 0.6789 0.5773 -0.0225 -0.1371 0.0819  327 LYS   B CE  
3912 N  NZ  . LYS   B 171 ? 0.7652 0.8037 0.6937 -0.0298 -0.1422 0.0766  327 LYS   B NZ  
3913 N  N   . SER   B 172 ? 0.5633 0.5438 0.5332 0.0298  -0.1109 0.1382  328 SER   B N   
3914 C  CA  . SER   B 172 ? 0.5237 0.4924 0.5099 0.0408  -0.1037 0.1469  328 SER   B CA  
3915 C  C   . SER   B 172 ? 0.6321 0.5748 0.6135 0.0418  -0.0933 0.1357  328 SER   B C   
3916 O  O   . SER   B 172 ? 0.5379 0.4735 0.5041 0.0347  -0.0922 0.1232  328 SER   B O   
3917 C  CB  . SER   B 172 ? 0.6166 0.5932 0.6060 0.0455  -0.1062 0.1658  328 SER   B CB  
3918 O  OG  . SER   B 172 ? 0.6820 0.6521 0.6533 0.0403  -0.1058 0.1651  328 SER   B OG  
3919 N  N   . SER   B 173 ? 0.5398 0.4687 0.5350 0.0505  -0.0852 0.1403  329 SER   B N   
3920 C  CA  . SER   B 173 ? 0.6469 0.5524 0.6385 0.0508  -0.0753 0.1302  329 SER   B CA  
3921 C  C   . SER   B 173 ? 0.5764 0.4744 0.5515 0.0460  -0.0744 0.1302  329 SER   B C   
3922 O  O   . SER   B 173 ? 0.6143 0.5194 0.5864 0.0466  -0.0780 0.1428  329 SER   B O   
3923 C  CB  . SER   B 173 ? 0.6441 0.5358 0.6524 0.0604  -0.0664 0.1361  329 SER   B CB  
3924 O  OG  . SER   B 173 ? 0.7208 0.6190 0.7446 0.0651  -0.0661 0.1353  329 SER   B OG  
3925 N  N   . TRP   B 174 ? 0.5535 0.4383 0.5184 0.0411  -0.0695 0.1167  330 TRP   B N   
3926 C  CA  . TRP   B 174 ? 0.5583 0.4362 0.5081 0.0362  -0.0677 0.1155  330 TRP   B CA  
3927 C  C   . TRP   B 174 ? 0.5438 0.4114 0.4984 0.0413  -0.0628 0.1280  330 TRP   B C   
3928 O  O   . TRP   B 174 ? 0.6188 0.4774 0.5881 0.0484  -0.0574 0.1326  330 TRP   B O   
3929 C  CB  . TRP   B 174 ? 0.4650 0.3301 0.4072 0.0317  -0.0619 0.1001  330 TRP   B CB  
3930 C  CG  . TRP   B 174 ? 0.4924 0.3656 0.4285 0.0266  -0.0659 0.0884  330 TRP   B CG  
3931 C  CD1 . TRP   B 174 ? 0.4803 0.3688 0.4186 0.0255  -0.0732 0.0887  330 TRP   B CD1 
3932 C  CD2 . TRP   B 174 ? 0.4953 0.3620 0.4222 0.0216  -0.0626 0.0753  330 TRP   B CD2 
3933 N  NE1 . TRP   B 174 ? 0.5178 0.4073 0.4484 0.0200  -0.0740 0.0760  330 TRP   B NE1 
3934 C  CE2 . TRP   B 174 ? 0.4802 0.3567 0.4042 0.0182  -0.0675 0.0680  330 TRP   B CE2 
3935 C  CE3 . TRP   B 174 ? 0.5141 0.3682 0.4353 0.0195  -0.0559 0.0694  330 TRP   B CE3 
3936 C  CZ2 . TRP   B 174 ? 0.4921 0.3650 0.4086 0.0138  -0.0654 0.0558  330 TRP   B CZ2 
3937 C  CZ3 . TRP   B 174 ? 0.5038 0.3569 0.4179 0.0151  -0.0544 0.0573  330 TRP   B CZ3 
3938 C  CH2 . TRP   B 174 ? 0.4757 0.3376 0.3879 0.0128  -0.0589 0.0511  330 TRP   B CH2 
3939 N  N   . PRO   B 175 ? 0.6070 0.4754 0.5497 0.0378  -0.0640 0.1337  331 PRO   B N   
3940 C  CA  . PRO   B 175 ? 0.6272 0.4854 0.5746 0.0424  -0.0592 0.1469  331 PRO   B CA  
3941 C  C   . PRO   B 175 ? 0.5937 0.4286 0.5457 0.0437  -0.0482 0.1401  331 PRO   B C   
3942 O  O   . PRO   B 175 ? 0.6554 0.4831 0.6013 0.0389  -0.0448 0.1256  331 PRO   B O   
3943 C  CB  . PRO   B 175 ? 0.5529 0.4175 0.4835 0.0362  -0.0627 0.1513  331 PRO   B CB  
3944 C  CG  . PRO   B 175 ? 0.6155 0.4998 0.5364 0.0306  -0.0719 0.1461  331 PRO   B CG  
3945 C  CD  . PRO   B 175 ? 0.5637 0.4449 0.4890 0.0299  -0.0705 0.1309  331 PRO   B CD  
3946 N  N   . ALA   B 176 ? 0.6589 0.4823 0.6216 0.0501  -0.0425 0.1514  332 ALA   B N   
3947 C  CA  . ALA   B 176 ? 0.5927 0.3927 0.5608 0.0514  -0.0313 0.1459  332 ALA   B CA  
3948 C  C   . ALA   B 176 ? 0.6021 0.3921 0.5556 0.0426  -0.0273 0.1359  332 ALA   B C   
3949 O  O   . ALA   B 176 ? 0.6291 0.4053 0.5833 0.0402  -0.0201 0.1245  332 ALA   B O   
3950 C  CB  . ALA   B 176 ? 0.4989 0.2876 0.4790 0.0592  -0.0256 0.1615  332 ALA   B CB  
3951 N  N   . SER   B 177 ? 0.6544 0.4525 0.5944 0.0374  -0.0316 0.1398  333 SER   B N   
3952 C  CA  . SER   B 177 ? 0.5724 0.3635 0.4992 0.0292  -0.0279 0.1306  333 SER   B CA  
3953 C  C   . SER   B 177 ? 0.5307 0.3263 0.4517 0.0242  -0.0290 0.1138  333 SER   B C   
3954 O  O   . SER   B 177 ? 0.5495 0.3414 0.4609 0.0177  -0.0260 0.1060  333 SER   B O   
3955 C  CB  . SER   B 177 ? 0.6582 0.4591 0.5716 0.0249  -0.0324 0.1384  333 SER   B CB  
3956 O  OG  . SER   B 177 ? 0.6954 0.5160 0.6012 0.0228  -0.0414 0.1356  333 SER   B OG  
3957 N  N   . THR   B 178 ? 0.5431 0.3476 0.4701 0.0269  -0.0332 0.1087  334 THR   B N   
3958 C  CA  . THR   B 178 ? 0.6677 0.4746 0.5908 0.0229  -0.0333 0.0937  334 THR   B CA  
3959 C  C   . THR   B 178 ? 0.5594 0.3549 0.4929 0.0250  -0.0269 0.0860  334 THR   B C   
3960 O  O   . THR   B 178 ? 0.4629 0.2600 0.3940 0.0217  -0.0264 0.0742  334 THR   B O   
3961 C  CB  . THR   B 178 ? 0.5598 0.3840 0.4806 0.0228  -0.0418 0.0914  334 THR   B CB  
3962 O  OG1 . THR   B 178 ? 0.5730 0.4012 0.5073 0.0292  -0.0441 0.0964  334 THR   B OG1 
3963 C  CG2 . THR   B 178 ? 0.5377 0.3743 0.4467 0.0198  -0.0481 0.0984  334 THR   B CG2 
3964 N  N   . GLN   B 179 ? 0.5715 0.3553 0.5163 0.0303  -0.0216 0.0924  335 GLN   B N   
3965 C  CA  . GLN   B 179 ? 0.6306 0.4055 0.5858 0.0330  -0.0159 0.0853  335 GLN   B CA  
3966 C  C   . GLN   B 179 ? 0.6497 0.4156 0.5988 0.0261  -0.0101 0.0721  335 GLN   B C   
3967 O  O   . GLN   B 179 ? 0.6093 0.3749 0.5626 0.0259  -0.0081 0.0629  335 GLN   B O   
3968 C  CB  . GLN   B 179 ? 0.6889 0.4502 0.6567 0.0399  -0.0093 0.0942  335 GLN   B CB  
3969 C  CG  . GLN   B 179 ? 0.7934 0.5611 0.7756 0.0480  -0.0109 0.0977  335 GLN   B CG  
3970 C  CD  . GLN   B 179 ? 0.9175 0.6743 0.9133 0.0565  -0.0049 0.1096  335 GLN   B CD  
3971 O  OE1 . GLN   B 179 ? 0.9798 0.7174 0.9761 0.0558  0.0040  0.1101  335 GLN   B OE1 
3972 N  NE2 . GLN   B 179 ? 0.9312 0.7004 0.9387 0.0644  -0.0097 0.1200  335 GLN   B NE2 
3973 N  N   . GLU   B 180 ? 0.6070 0.3671 0.5467 0.0201  -0.0072 0.0714  336 GLU   B N   
3974 C  CA  . GLU   B 180 ? 0.5869 0.3412 0.5211 0.0128  -0.0022 0.0598  336 GLU   B CA  
3975 C  C   . GLU   B 180 ? 0.6353 0.4029 0.5590 0.0075  -0.0072 0.0534  336 GLU   B C   
3976 O  O   . GLU   B 180 ? 0.5560 0.3220 0.4751 0.0013  -0.0038 0.0449  336 GLU   B O   
3977 C  CB  . GLU   B 180 ? 0.6729 0.4112 0.6045 0.0086  0.0054  0.0620  336 GLU   B CB  
3978 C  CG  . GLU   B 180 ? 0.7335 0.4553 0.6760 0.0137  0.0125  0.0663  336 GLU   B CG  
3979 C  CD  . GLU   B 180 ? 0.7724 0.4903 0.7214 0.0143  0.0165  0.0560  336 GLU   B CD  
3980 O  OE1 . GLU   B 180 ? 0.8799 0.5992 0.8230 0.0071  0.0182  0.0447  336 GLU   B OE1 
3981 O  OE2 . GLU   B 180 ? 0.9046 0.6196 0.8648 0.0220  0.0179  0.0596  336 GLU   B OE2 
3982 N  N   . GLY   B 181 ? 0.5115 0.2926 0.4314 0.0095  -0.0147 0.0571  337 GLY   B N   
3983 C  CA  . GLY   B 181 ? 0.4909 0.2835 0.4014 0.0051  -0.0184 0.0510  337 GLY   B CA  
3984 C  C   . GLY   B 181 ? 0.4793 0.2786 0.3929 0.0057  -0.0205 0.0420  337 GLY   B C   
3985 O  O   . GLY   B 181 ? 0.4764 0.2721 0.3989 0.0087  -0.0189 0.0396  337 GLY   B O   
3986 N  N   . LEU   B 182 ? 0.4282 0.2376 0.3344 0.0031  -0.0238 0.0374  338 LEU   B N   
3987 C  CA  . LEU   B 182 ? 0.5146 0.3309 0.4231 0.0037  -0.0261 0.0298  338 LEU   B CA  
3988 C  C   . LEU   B 182 ? 0.5253 0.3362 0.4400 0.0026  -0.0213 0.0234  338 LEU   B C   
3989 O  O   . LEU   B 182 ? 0.4902 0.3017 0.4124 0.0054  -0.0219 0.0209  338 LEU   B O   
3990 C  CB  . LEU   B 182 ? 0.4132 0.2356 0.3263 0.0081  -0.0319 0.0330  338 LEU   B CB  
3991 C  CG  . LEU   B 182 ? 0.4456 0.2756 0.3594 0.0079  -0.0349 0.0257  338 LEU   B CG  
3992 C  CD1 . LEU   B 182 ? 0.4683 0.3042 0.3717 0.0045  -0.0359 0.0217  338 LEU   B CD1 
3993 C  CD2 . LEU   B 182 ? 0.5035 0.3396 0.4230 0.0113  -0.0404 0.0291  338 LEU   B CD2 
3994 N  N   . ARG   B 183 ? 0.5453 0.3518 0.4566 -0.0022 -0.0163 0.0207  339 ARG   B N   
3995 C  CA  . ARG   B 183 ? 0.5128 0.3138 0.4284 -0.0049 -0.0112 0.0150  339 ARG   B CA  
3996 C  C   . ARG   B 183 ? 0.4450 0.2557 0.3607 -0.0064 -0.0124 0.0079  339 ARG   B C   
3997 O  O   . ARG   B 183 ? 0.4776 0.2918 0.3901 -0.0113 -0.0100 0.0039  339 ARG   B O   
3998 C  CB  . ARG   B 183 ? 0.5406 0.3342 0.4521 -0.0108 -0.0057 0.0149  339 ARG   B CB  
3999 C  CG  . ARG   B 183 ? 0.6037 0.3839 0.5175 -0.0093 -0.0023 0.0215  339 ARG   B CG  
4000 C  CD  . ARG   B 183 ? 0.7979 0.5692 0.7077 -0.0166 0.0040  0.0203  339 ARG   B CD  
4001 N  NE  . ARG   B 183 ? 0.8636 0.6428 0.7652 -0.0211 0.0027  0.0215  339 ARG   B NE  
4002 C  CZ  . ARG   B 183 ? 0.9100 0.6966 0.8079 -0.0274 0.0041  0.0157  339 ARG   B CZ  
4003 N  NH1 . ARG   B 183 ? 0.9212 0.7083 0.8218 -0.0311 0.0067  0.0084  339 ARG   B NH1 
4004 N  NH2 . ARG   B 183 ? 0.7743 0.5692 0.6659 -0.0303 0.0030  0.0177  339 ARG   B NH2 
4005 N  N   . ILE   B 184 ? 0.3893 0.2049 0.3092 -0.0022 -0.0163 0.0071  340 ILE   B N   
4006 C  CA  . ILE   B 184 ? 0.4237 0.2482 0.3440 -0.0027 -0.0179 0.0018  340 ILE   B CA  
4007 C  C   . ILE   B 184 ? 0.4158 0.2396 0.3427 -0.0029 -0.0156 -0.0026 340 ILE   B C   
4008 O  O   . ILE   B 184 ? 0.4318 0.2628 0.3606 -0.0025 -0.0172 -0.0057 340 ILE   B O   
4009 C  CB  . ILE   B 184 ? 0.4931 0.3237 0.4131 0.0009  -0.0234 0.0030  340 ILE   B CB  
4010 C  CG1 . ILE   B 184 ? 0.4112 0.2397 0.3383 0.0052  -0.0259 0.0058  340 ILE   B CG1 
4011 C  CG2 . ILE   B 184 ? 0.4658 0.2987 0.3775 0.0003  -0.0254 0.0060  340 ILE   B CG2 
4012 C  CD1 . ILE   B 184 ? 0.4646 0.3000 0.3913 0.0073  -0.0317 0.0064  340 ILE   B CD1 
4013 N  N   . GLN   B 185 ? 0.4073 0.2222 0.3377 -0.0035 -0.0115 -0.0027 341 GLN   B N   
4014 C  CA  . GLN   B 185 ? 0.4662 0.2801 0.4030 -0.0027 -0.0093 -0.0065 341 GLN   B CA  
4015 C  C   . GLN   B 185 ? 0.4720 0.2927 0.4070 -0.0077 -0.0075 -0.0124 341 GLN   B C   
4016 O  O   . GLN   B 185 ? 0.4711 0.2968 0.4103 -0.0065 -0.0082 -0.0149 341 GLN   B O   
4017 C  CB  . GLN   B 185 ? 0.4614 0.2627 0.4019 -0.0022 -0.0038 -0.0059 341 GLN   B CB  
4018 C  CG  . GLN   B 185 ? 0.5483 0.3440 0.4934 0.0040  -0.0054 0.0015  341 GLN   B CG  
4019 C  CD  . GLN   B 185 ? 0.4969 0.2856 0.4369 0.0025  -0.0041 0.0064  341 GLN   B CD  
4020 O  OE1 . GLN   B 185 ? 0.5961 0.3886 0.5284 -0.0021 -0.0050 0.0054  341 GLN   B OE1 
4021 N  NE2 . GLN   B 185 ? 0.5317 0.3103 0.4765 0.0062  -0.0013 0.0119  341 GLN   B NE2 
4022 N  N   . ASN   B 186 ? 0.4324 0.2549 0.3616 -0.0135 -0.0053 -0.0140 342 ASN   B N   
4023 C  CA  . ASN   B 186 ? 0.4952 0.3268 0.4231 -0.0185 -0.0041 -0.0184 342 ASN   B CA  
4024 C  C   . ASN   B 186 ? 0.5078 0.3519 0.4351 -0.0169 -0.0081 -0.0171 342 ASN   B C   
4025 O  O   . ASN   B 186 ? 0.4151 0.2690 0.3425 -0.0201 -0.0077 -0.0190 342 ASN   B O   
4026 C  CB  . ASN   B 186 ? 0.4955 0.3253 0.4183 -0.0265 0.0003  -0.0207 342 ASN   B CB  
4027 C  CG  . ASN   B 186 ? 0.6749 0.4899 0.5981 -0.0287 0.0058  -0.0229 342 ASN   B CG  
4028 O  OD1 . ASN   B 186 ? 0.7349 0.5418 0.6544 -0.0327 0.0091  -0.0224 342 ASN   B OD1 
4029 N  ND2 . ASN   B 186 ? 0.7939 0.6048 0.7220 -0.0259 0.0075  -0.0254 342 ASN   B ND2 
4030 N  N   . TRP   B 187 ? 0.4474 0.2913 0.3742 -0.0121 -0.0117 -0.0136 343 TRP   B N   
4031 C  CA  . TRP   B 187 ? 0.4319 0.2848 0.3578 -0.0101 -0.0144 -0.0128 343 TRP   B CA  
4032 C  C   . TRP   B 187 ? 0.4841 0.3375 0.4143 -0.0052 -0.0177 -0.0127 343 TRP   B C   
4033 O  O   . TRP   B 187 ? 0.4536 0.3130 0.3875 -0.0047 -0.0180 -0.0141 343 TRP   B O   
4034 C  CB  . TRP   B 187 ? 0.3961 0.2485 0.3163 -0.0100 -0.0149 -0.0101 343 TRP   B CB  
4035 C  CG  . TRP   B 187 ? 0.4046 0.2628 0.3233 -0.0068 -0.0170 -0.0094 343 TRP   B CG  
4036 C  CD1 . TRP   B 187 ? 0.4113 0.2765 0.3335 -0.0049 -0.0174 -0.0107 343 TRP   B CD1 
4037 C  CD2 . TRP   B 187 ? 0.4155 0.2719 0.3289 -0.0049 -0.0185 -0.0076 343 TRP   B CD2 
4038 N  NE1 . TRP   B 187 ? 0.4052 0.2716 0.3246 -0.0020 -0.0183 -0.0103 343 TRP   B NE1 
4039 C  CE2 . TRP   B 187 ? 0.4413 0.3028 0.3548 -0.0023 -0.0191 -0.0089 343 TRP   B CE2 
4040 C  CE3 . TRP   B 187 ? 0.3984 0.2493 0.3067 -0.0055 -0.0191 -0.0047 343 TRP   B CE3 
4041 C  CZ2 . TRP   B 187 ? 0.4239 0.2847 0.3315 -0.0007 -0.0198 -0.0087 343 TRP   B CZ2 
4042 C  CZ3 . TRP   B 187 ? 0.4426 0.2946 0.3450 -0.0040 -0.0206 -0.0037 343 TRP   B CZ3 
4043 C  CH2 . TRP   B 187 ? 0.3879 0.2447 0.2896 -0.0019 -0.0208 -0.0063 343 TRP   B CH2 
4044 N  N   . LEU   B 188 ? 0.3859 0.2338 0.3159 -0.0018 -0.0204 -0.0105 344 LEU   B N   
4045 C  CA  . LEU   B 188 ? 0.4368 0.2856 0.3703 0.0018  -0.0240 -0.0103 344 LEU   B CA  
4046 C  C   . LEU   B 188 ? 0.4020 0.2476 0.3423 0.0035  -0.0242 -0.0102 344 LEU   B C   
4047 O  O   . LEU   B 188 ? 0.3737 0.2218 0.3182 0.0058  -0.0269 -0.0103 344 LEU   B O   
4048 C  CB  . LEU   B 188 ? 0.4420 0.2893 0.3710 0.0035  -0.0274 -0.0079 344 LEU   B CB  
4049 C  CG  . LEU   B 188 ? 0.4418 0.2921 0.3637 0.0025  -0.0269 -0.0084 344 LEU   B CG  
4050 C  CD1 . LEU   B 188 ? 0.4420 0.2908 0.3576 0.0032  -0.0300 -0.0063 344 LEU   B CD1 
4051 C  CD2 . LEU   B 188 ? 0.4323 0.2877 0.3564 0.0033  -0.0261 -0.0112 344 LEU   B CD2 
4052 N  N   . SER   B 189 ? 0.4077 0.2475 0.3494 0.0026  -0.0209 -0.0099 345 SER   B N   
4053 C  CA  . SER   B 189 ? 0.4546 0.2907 0.4032 0.0041  -0.0187 -0.0105 345 SER   B CA  
4054 C  C   . SER   B 189 ? 0.5056 0.3351 0.4575 0.0078  -0.0192 -0.0059 345 SER   B C   
4055 O  O   . SER   B 189 ? 0.4127 0.2429 0.3622 0.0096  -0.0230 -0.0017 345 SER   B O   
4056 C  CB  . SER   B 189 ? 0.4378 0.2798 0.3925 0.0060  -0.0207 -0.0119 345 SER   B CB  
4057 O  OG  . SER   B 189 ? 0.4180 0.2621 0.3748 0.0093  -0.0257 -0.0088 345 SER   B OG  
4058 N  N   . ALA   B 190 ? 0.4622 0.2857 0.4197 0.0089  -0.0148 -0.0065 346 ALA   B N   
4059 C  CA  . ALA   B 190 ? 0.4634 0.2810 0.4264 0.0136  -0.0144 -0.0011 346 ALA   B CA  
4060 C  C   . ALA   B 190 ? 0.5207 0.3460 0.4904 0.0181  -0.0199 0.0027  346 ALA   B C   
4061 O  O   . ALA   B 190 ? 0.4139 0.2394 0.3861 0.0217  -0.0228 0.0093  346 ALA   B O   
4062 C  CB  . ALA   B 190 ? 0.4278 0.2361 0.3959 0.0140  -0.0069 -0.0034 346 ALA   B CB  
4063 N  N   . LYS   B 191 ? 0.4970 0.3295 0.4696 0.0176  -0.0214 -0.0009 347 LYS   B N   
4064 C  CA  . LYS   B 191 ? 0.4836 0.3241 0.4621 0.0204  -0.0268 0.0021  347 LYS   B CA  
4065 C  C   . LYS   B 191 ? 0.4623 0.3070 0.4344 0.0195  -0.0330 0.0049  347 LYS   B C   
4066 O  O   . LYS   B 191 ? 0.4929 0.3422 0.4682 0.0218  -0.0375 0.0101  347 LYS   B O   
4067 C  CB  . LYS   B 191 ? 0.4811 0.3278 0.4625 0.0189  -0.0271 -0.0024 347 LYS   B CB  
4068 C  CG  . LYS   B 191 ? 0.6042 0.4522 0.5959 0.0215  -0.0239 -0.0026 347 LYS   B CG  
4069 C  CD  . LYS   B 191 ? 0.6421 0.4978 0.6361 0.0197  -0.0256 -0.0056 347 LYS   B CD  
4070 C  CE  . LYS   B 191 ? 0.5024 0.3572 0.4927 0.0161  -0.0211 -0.0109 347 LYS   B CE  
4071 N  NZ  . LYS   B 191 ? 0.6667 0.5277 0.6544 0.0137  -0.0247 -0.0122 347 LYS   B NZ  
4072 N  N   . VAL   B 192 ? 0.4348 0.2791 0.3978 0.0159  -0.0331 0.0015  348 VAL   B N   
4073 C  CA  . VAL   B 192 ? 0.5078 0.3552 0.4634 0.0146  -0.0378 0.0030  348 VAL   B CA  
4074 C  C   . VAL   B 192 ? 0.4801 0.3245 0.4325 0.0158  -0.0387 0.0089  348 VAL   B C   
4075 O  O   . VAL   B 192 ? 0.4695 0.3186 0.4198 0.0161  -0.0437 0.0129  348 VAL   B O   
4076 C  CB  . VAL   B 192 ? 0.4265 0.2741 0.3744 0.0113  -0.0365 -0.0018 348 VAL   B CB  
4077 C  CG1 . VAL   B 192 ? 0.4014 0.2506 0.3403 0.0099  -0.0396 -0.0011 348 VAL   B CG1 
4078 C  CG2 . VAL   B 192 ? 0.4252 0.2769 0.3770 0.0107  -0.0367 -0.0058 348 VAL   B CG2 
4079 N  N   . ARG   B 193 ? 0.4639 0.3005 0.4160 0.0160  -0.0338 0.0100  349 ARG   B N   
4080 C  CA  . ARG   B 193 ? 0.4868 0.3198 0.4369 0.0174  -0.0342 0.0168  349 ARG   B CA  
4081 C  C   . ARG   B 193 ? 0.4821 0.3189 0.4408 0.0221  -0.0374 0.0239  349 ARG   B C   
4082 O  O   . ARG   B 193 ? 0.5301 0.3715 0.4860 0.0228  -0.0421 0.0302  349 ARG   B O   
4083 C  CB  . ARG   B 193 ? 0.4317 0.2540 0.3815 0.0166  -0.0275 0.0166  349 ARG   B CB  
4084 C  CG  . ARG   B 193 ? 0.4610 0.2783 0.4083 0.0177  -0.0273 0.0242  349 ARG   B CG  
4085 C  CD  . ARG   B 193 ? 0.4783 0.2835 0.4241 0.0155  -0.0200 0.0233  349 ARG   B CD  
4086 N  NE  . ARG   B 193 ? 0.4399 0.2401 0.3820 0.0159  -0.0198 0.0310  349 ARG   B NE  
4087 C  CZ  . ARG   B 193 ? 0.5327 0.3267 0.4816 0.0205  -0.0181 0.0391  349 ARG   B CZ  
4088 N  NH1 . ARG   B 193 ? 0.5067 0.2989 0.4669 0.0258  -0.0165 0.0405  349 ARG   B NH1 
4089 N  NH2 . ARG   B 193 ? 0.5653 0.3547 0.5099 0.0202  -0.0176 0.0464  349 ARG   B NH2 
4090 N  N   . LYS   B 194 ? 0.4802 0.3167 0.4497 0.0253  -0.0351 0.0233  350 LYS   B N   
4091 C  CA  . LYS   B 194 ? 0.5199 0.3618 0.4998 0.0304  -0.0379 0.0307  350 LYS   B CA  
4092 C  C   . LYS   B 194 ? 0.5590 0.4141 0.5374 0.0289  -0.0462 0.0326  350 LYS   B C   
4093 O  O   . LYS   B 194 ? 0.5052 0.3674 0.4862 0.0311  -0.0509 0.0409  350 LYS   B O   
4094 C  CB  . LYS   B 194 ? 0.5163 0.3565 0.5079 0.0336  -0.0331 0.0284  350 LYS   B CB  
4095 C  CG  . LYS   B 194 ? 0.5018 0.3463 0.5065 0.0402  -0.0338 0.0372  350 LYS   B CG  
4096 C  CD  . LYS   B 194 ? 0.6522 0.4989 0.6684 0.0430  -0.0302 0.0343  350 LYS   B CD  
4097 C  CE  . LYS   B 194 ? 0.5305 0.3750 0.5606 0.0508  -0.0260 0.0421  350 LYS   B CE  
4098 N  NZ  . LYS   B 194 ? 0.8030 0.6550 0.8360 0.0543  -0.0320 0.0539  350 LYS   B NZ  
4099 N  N   . GLN   B 195 ? 0.4989 0.3576 0.4728 0.0249  -0.0480 0.0253  351 GLN   B N   
4100 C  CA  . GLN   B 195 ? 0.4973 0.3667 0.4690 0.0223  -0.0550 0.0255  351 GLN   B CA  
4101 C  C   . GLN   B 195 ? 0.4713 0.3430 0.4312 0.0193  -0.0591 0.0280  351 GLN   B C   
4102 O  O   . GLN   B 195 ? 0.4906 0.3722 0.4498 0.0181  -0.0653 0.0325  351 GLN   B O   
4103 C  CB  . GLN   B 195 ? 0.5141 0.3839 0.4835 0.0187  -0.0545 0.0169  351 GLN   B CB  
4104 C  CG  . GLN   B 195 ? 0.5655 0.4365 0.5458 0.0205  -0.0519 0.0146  351 GLN   B CG  
4105 C  CD  . GLN   B 195 ? 0.7421 0.6137 0.7192 0.0167  -0.0518 0.0075  351 GLN   B CD  
4106 O  OE1 . GLN   B 195 ? 0.8433 0.7171 0.8278 0.0171  -0.0503 0.0053  351 GLN   B OE1 
4107 N  NE2 . GLN   B 195 ? 0.6661 0.5361 0.6325 0.0132  -0.0534 0.0043  351 GLN   B NE2 
4108 N  N   . LEU   B 196 ? 0.4296 0.2936 0.3799 0.0173  -0.0556 0.0248  352 LEU   B N   
4109 C  CA  . LEU   B 196 ? 0.4903 0.3564 0.4289 0.0144  -0.0585 0.0269  352 LEU   B CA  
4110 C  C   . LEU   B 196 ? 0.5303 0.3995 0.4711 0.0172  -0.0611 0.0376  352 LEU   B C   
4111 O  O   . LEU   B 196 ? 0.5352 0.4137 0.4710 0.0152  -0.0670 0.0419  352 LEU   B O   
4112 C  CB  . LEU   B 196 ? 0.4095 0.2676 0.3390 0.0122  -0.0536 0.0221  352 LEU   B CB  
4113 C  CG  . LEU   B 196 ? 0.4528 0.3095 0.3792 0.0096  -0.0514 0.0129  352 LEU   B CG  
4114 C  CD1 . LEU   B 196 ? 0.4023 0.2533 0.3221 0.0081  -0.0463 0.0097  352 LEU   B CD1 
4115 C  CD2 . LEU   B 196 ? 0.5102 0.3729 0.4304 0.0063  -0.0557 0.0094  352 LEU   B CD2 
4116 N  N   . ARG   B 197 ? 0.4921 0.3541 0.4412 0.0218  -0.0565 0.0423  353 ARG   B N   
4117 C  CA  . ARG   B 197 ? 0.4789 0.3422 0.4317 0.0256  -0.0577 0.0538  353 ARG   B CA  
4118 C  C   . ARG   B 197 ? 0.4408 0.3171 0.4033 0.0286  -0.0637 0.0615  353 ARG   B C   
4119 O  O   . ARG   B 197 ? 0.4497 0.3307 0.4148 0.0315  -0.0663 0.0727  353 ARG   B O   
4120 C  CB  . ARG   B 197 ? 0.4964 0.3462 0.4562 0.0297  -0.0499 0.0559  353 ARG   B CB  
4121 C  CG  . ARG   B 197 ? 0.5577 0.3964 0.5074 0.0261  -0.0447 0.0519  353 ARG   B CG  
4122 C  CD  . ARG   B 197 ? 0.5687 0.3928 0.5249 0.0288  -0.0364 0.0530  353 ARG   B CD  
4123 N  NE  . ARG   B 197 ? 0.5938 0.4160 0.5588 0.0348  -0.0359 0.0647  353 ARG   B NE  
4124 C  CZ  . ARG   B 197 ? 0.5884 0.4101 0.5494 0.0353  -0.0373 0.0742  353 ARG   B CZ  
4125 N  NH1 . ARG   B 197 ? 0.5966 0.4201 0.5442 0.0299  -0.0393 0.0731  353 ARG   B NH1 
4126 N  NH2 . ARG   B 197 ? 0.6785 0.4988 0.6497 0.0417  -0.0364 0.0858  353 ARG   B NH2 
4127 N  N   . LEU   B 198 ? 0.4309 0.3139 0.3992 0.0279  -0.0660 0.0567  354 LEU   B N   
4128 C  CA  . LEU   B 198 ? 0.5424 0.4408 0.5189 0.0290  -0.0727 0.0635  354 LEU   B CA  
4129 C  C   . LEU   B 198 ? 0.4890 0.3995 0.4539 0.0221  -0.0806 0.0624  354 LEU   B C   
4130 O  O   . LEU   B 198 ? 0.5213 0.4469 0.4907 0.0216  -0.0874 0.0693  354 LEU   B O   
4131 C  CB  . LEU   B 198 ? 0.4954 0.3964 0.4839 0.0308  -0.0713 0.0590  354 LEU   B CB  
4132 C  CG  . LEU   B 198 ? 0.4784 0.3707 0.4804 0.0380  -0.0638 0.0613  354 LEU   B CG  
4133 C  CD1 . LEU   B 198 ? 0.6143 0.5089 0.6250 0.0381  -0.0619 0.0548  354 LEU   B CD1 
4134 C  CD2 . LEU   B 198 ? 0.6628 0.5620 0.6765 0.0447  -0.0653 0.0750  354 LEU   B CD2 
4135 N  N   . LYS   B 199 ? 0.4427 0.3474 0.3930 0.0165  -0.0797 0.0540  355 LYS   B N   
4136 C  CA  . LYS   B 199 ? 0.4871 0.4010 0.4246 0.0096  -0.0857 0.0519  355 LYS   B CA  
4137 C  C   . LYS   B 199 ? 0.4628 0.3834 0.3946 0.0097  -0.0894 0.0627  355 LYS   B C   
4138 O  O   . LYS   B 199 ? 0.4738 0.3880 0.4098 0.0150  -0.0858 0.0702  355 LYS   B O   
4139 C  CB  . LYS   B 199 ? 0.4320 0.3366 0.3564 0.0048  -0.0820 0.0403  355 LYS   B CB  
4140 C  CG  . LYS   B 199 ? 0.4585 0.3574 0.3880 0.0044  -0.0787 0.0307  355 LYS   B CG  
4141 C  CD  . LYS   B 199 ? 0.5865 0.4763 0.5050 0.0011  -0.0744 0.0208  355 LYS   B CD  
4142 C  CE  . LYS   B 199 ? 0.5237 0.4118 0.4455 -0.0010 -0.0733 0.0123  355 LYS   B CE  
4143 N  NZ  . LYS   B 199 ? 0.7443 0.6372 0.6573 -0.0077 -0.0772 0.0070  355 LYS   B NZ  
4144 N  N   . PRO   B 200 ? 0.4374 0.3706 0.3592 0.0034  -0.0962 0.0637  356 PRO   B N   
4145 C  CA  . PRO   B 200 ? 0.4572 0.3986 0.3727 0.0030  -0.1000 0.0748  356 PRO   B CA  
4146 C  C   . PRO   B 200 ? 0.5017 0.4316 0.4043 0.0018  -0.0949 0.0721  356 PRO   B C   
4147 O  O   . PRO   B 200 ? 0.5683 0.4871 0.4642 -0.0004 -0.0897 0.0608  356 PRO   B O   
4148 C  CB  . PRO   B 200 ? 0.4961 0.4550 0.4025 -0.0053 -0.1086 0.0742  356 PRO   B CB  
4149 C  CG  . PRO   B 200 ? 0.4516 0.4061 0.3541 -0.0106 -0.1073 0.0598  356 PRO   B CG  
4150 C  CD  . PRO   B 200 ? 0.4666 0.4089 0.3838 -0.0038 -0.1011 0.0561  356 PRO   B CD  
4151 N  N   . PHE   B 201 ? 0.5229 0.4560 0.4230 0.0037  -0.0961 0.0838  357 PHE   B N   
4152 C  CA  . PHE   B 201 ? 0.5244 0.4504 0.4109 0.0013  -0.0925 0.0830  357 PHE   B CA  
4153 C  C   . PHE   B 201 ? 0.5282 0.4691 0.4003 -0.0052 -0.0991 0.0877  357 PHE   B C   
4154 O  O   . PHE   B 201 ? 0.5617 0.5190 0.4362 -0.0070 -0.1068 0.0942  357 PHE   B O   
4155 C  CB  . PHE   B 201 ? 0.5776 0.4926 0.4715 0.0079  -0.0870 0.0923  357 PHE   B CB  
4156 C  CG  . PHE   B 201 ? 0.5364 0.4607 0.4384 0.0125  -0.0912 0.1093  357 PHE   B CG  
4157 C  CD1 . PHE   B 201 ? 0.5793 0.5055 0.4997 0.0196  -0.0916 0.1161  357 PHE   B CD1 
4158 C  CD2 . PHE   B 201 ? 0.5918 0.5231 0.4836 0.0102  -0.0940 0.1193  357 PHE   B CD2 
4159 C  CE1 . PHE   B 201 ? 0.6360 0.5715 0.5657 0.0249  -0.0950 0.1333  357 PHE   B CE1 
4160 C  CE2 . PHE   B 201 ? 0.5406 0.4815 0.4406 0.0149  -0.0980 0.1367  357 PHE   B CE2 
4161 C  CZ  . PHE   B 201 ? 0.6403 0.5832 0.5598 0.0226  -0.0984 0.1441  357 PHE   B CZ  
4162 N  N   . TYR   B 202 ? 0.5149 0.4514 0.3719 -0.0091 -0.0961 0.0847  358 TYR   B N   
4163 C  CA  . TYR   B 202 ? 0.5352 0.4847 0.3752 -0.0167 -0.1011 0.0861  358 TYR   B CA  
4164 C  C   . TYR   B 202 ? 0.5779 0.5268 0.4109 -0.0159 -0.0994 0.0966  358 TYR   B C   
4165 O  O   . TYR   B 202 ? 0.5502 0.4851 0.3882 -0.0112 -0.0926 0.0985  358 TYR   B O   
4166 C  CB  . TYR   B 202 ? 0.5207 0.4667 0.3463 -0.0240 -0.0985 0.0695  358 TYR   B CB  
4167 C  CG  . TYR   B 202 ? 0.4946 0.4421 0.3269 -0.0254 -0.1008 0.0607  358 TYR   B CG  
4168 C  CD1 . TYR   B 202 ? 0.5262 0.4610 0.3708 -0.0204 -0.0957 0.0540  358 TYR   B CD1 
4169 C  CD2 . TYR   B 202 ? 0.5764 0.5396 0.4037 -0.0321 -0.1086 0.0605  358 TYR   B CD2 
4170 C  CE1 . TYR   B 202 ? 0.5564 0.4927 0.4077 -0.0217 -0.0976 0.0472  358 TYR   B CE1 
4171 C  CE2 . TYR   B 202 ? 0.5925 0.5571 0.4268 -0.0340 -0.1106 0.0531  358 TYR   B CE2 
4172 C  CZ  . TYR   B 202 ? 0.5721 0.5227 0.4187 -0.0284 -0.1049 0.0467  358 TYR   B CZ  
4173 O  OH  . TYR   B 202 ? 0.5954 0.5472 0.4493 -0.0301 -0.1066 0.0401  358 TYR   B OH  
4174 N  N   . LEU   B 203 ? 0.5014 0.4661 0.3224 -0.0215 -0.1056 0.1035  359 LEU   B N   
4175 C  CA  . LEU   B 203 ? 0.5021 0.4693 0.3144 -0.0220 -0.1050 0.1147  359 LEU   B CA  
4176 C  C   . LEU   B 203 ? 0.5672 0.5449 0.3570 -0.0321 -0.1072 0.1088  359 LEU   B C   
4177 O  O   . LEU   B 203 ? 0.5945 0.5872 0.3773 -0.0385 -0.1141 0.1063  359 LEU   B O   
4178 C  CB  . LEU   B 203 ? 0.6511 0.6302 0.4740 -0.0172 -0.1110 0.1345  359 LEU   B CB  
4179 C  CG  . LEU   B 203 ? 0.5818 0.5479 0.4261 -0.0065 -0.1066 0.1421  359 LEU   B CG  
4180 C  CD1 . LEU   B 203 ? 0.6446 0.6258 0.5017 -0.0015 -0.1135 0.1598  359 LEU   B CD1 
4181 C  CD2 . LEU   B 203 ? 0.5672 0.5178 0.4098 -0.0037 -0.0988 0.1462  359 LEU   B CD2 
4182 N  N   . VAL   B 204 ? 0.5704 0.5407 0.3488 -0.0339 -0.1012 0.1068  360 VAL   B N   
4183 C  CA  . VAL   B 204 ? 0.5947 0.5713 0.3511 -0.0431 -0.1004 0.0985  360 VAL   B CA  
4184 C  C   . VAL   B 204 ? 0.6153 0.5996 0.3620 -0.0448 -0.1013 0.1121  360 VAL   B C   
4185 O  O   . VAL   B 204 ? 0.5461 0.5209 0.3006 -0.0390 -0.0970 0.1213  360 VAL   B O   
4186 C  CB  . VAL   B 204 ? 0.6718 0.6325 0.4240 -0.0436 -0.0909 0.0819  360 VAL   B CB  
4187 C  CG1 . VAL   B 204 ? 0.8204 0.7838 0.5524 -0.0502 -0.0869 0.0771  360 VAL   B CG1 
4188 C  CG2 . VAL   B 204 ? 0.5296 0.4875 0.2848 -0.0452 -0.0914 0.0673  360 VAL   B CG2 
4189 N  N   . PRO   B 205 ? 0.6585 0.6606 0.3881 -0.0531 -0.1070 0.1151  361 PRO   B N   
4190 C  CA  . PRO   B 205 ? 0.7222 0.7333 0.4421 -0.0550 -0.1083 0.1298  361 PRO   B CA  
4191 C  C   . PRO   B 205 ? 0.8017 0.8005 0.5121 -0.0559 -0.0985 0.1243  361 PRO   B C   
4192 O  O   . PRO   B 205 ? 0.7210 0.7170 0.4179 -0.0615 -0.0937 0.1090  361 PRO   B O   
4193 C  CB  . PRO   B 205 ? 0.6976 0.7312 0.3993 -0.0655 -0.1163 0.1299  361 PRO   B CB  
4194 C  CG  . PRO   B 205 ? 0.6844 0.7149 0.3809 -0.0707 -0.1154 0.1098  361 PRO   B CG  
4195 C  CD  . PRO   B 205 ? 0.6798 0.6944 0.3976 -0.0620 -0.1124 0.1047  361 PRO   B CD  
4196 N  N   . LYS   B 206 ? 0.8161 0.8074 0.5348 -0.0502 -0.0952 0.1372  362 LYS   B N   
4197 C  CA  . LYS   B 206 ? 0.7691 0.7474 0.4828 -0.0503 -0.0855 0.1328  362 LYS   B CA  
4198 C  C   . LYS   B 206 ? 0.8161 0.7938 0.5326 -0.0475 -0.0846 0.1514  362 LYS   B C   
4199 O  O   . LYS   B 206 ? 0.7222 0.6948 0.4555 -0.0404 -0.0864 0.1639  362 LYS   B O   
4200 C  CB  . LYS   B 206 ? 0.7173 0.6765 0.4449 -0.0447 -0.0783 0.1215  362 LYS   B CB  
4201 C  CG  . LYS   B 206 ? 0.7204 0.6694 0.4420 -0.0461 -0.0686 0.1141  362 LYS   B CG  
4202 C  CD  . LYS   B 206 ? 0.8198 0.7679 0.5325 -0.0500 -0.0648 0.0949  362 LYS   B CD  
4203 C  CE  . LYS   B 206 ? 0.9266 0.8669 0.6346 -0.0510 -0.0549 0.0876  362 LYS   B CE  
4204 N  NZ  . LYS   B 206 ? 0.9399 0.8850 0.6320 -0.0566 -0.0513 0.0732  362 LYS   B NZ  
4205 N  N   . HIS   B 207 ? 0.8445 0.8253 0.5452 -0.0530 -0.0805 0.1524  363 HIS   B N   
4206 C  CA  . HIS   B 207 ? 0.9110 0.8936 0.6110 -0.0522 -0.0801 0.1709  363 HIS   B CA  
4207 C  C   . HIS   B 207 ? 0.7898 0.7517 0.5063 -0.0454 -0.0727 0.1740  363 HIS   B C   
4208 O  O   . HIS   B 207 ? 0.8632 0.8119 0.5854 -0.0440 -0.0665 0.1600  363 HIS   B O   
4209 C  CB  . HIS   B 207 ? 0.9401 0.9312 0.6184 -0.0604 -0.0766 0.1694  363 HIS   B CB  
4210 C  CG  . HIS   B 207 ? 0.8018 0.8156 0.4630 -0.0675 -0.0848 0.1756  363 HIS   B CG  
4211 N  ND1 . HIS   B 207 ? 1.0823 1.1071 0.7210 -0.0763 -0.0825 0.1722  363 HIS   B ND1 
4212 C  CD2 . HIS   B 207 ? 0.9126 0.9416 0.5748 -0.0683 -0.0950 0.1811  363 HIS   B CD2 
4213 C  CE1 . HIS   B 207 ? 1.0479 1.0936 0.6737 -0.0825 -0.0912 0.1779  363 HIS   B CE1 
4214 N  NE2 . HIS   B 207 ? 1.1062 1.1552 0.7460 -0.0781 -0.0991 0.1827  363 HIS   B NE2 
4215 N  N   . ALA   B 208 ? 0.9003 0.8593 0.6247 -0.0415 -0.0731 0.1927  364 ALA   B N   
4216 C  CA  . ALA   B 208 ? 0.8484 0.7869 0.5856 -0.0371 -0.0649 0.1955  364 ALA   B CA  
4217 C  C   . ALA   B 208 ? 0.7753 0.7142 0.5040 -0.0405 -0.0612 0.2089  364 ALA   B C   
4218 O  O   . ALA   B 208 ? 1.0718 1.0252 0.7924 -0.0423 -0.0666 0.2238  364 ALA   B O   
4219 C  CB  . ALA   B 208 ? 0.7368 0.6648 0.4959 -0.0279 -0.0663 0.2040  364 ALA   B CB  
4220 N  N   . LYS   B 209 ? 1.0585 0.9827 0.7886 -0.0419 -0.0520 0.2038  365 LYS   B N   
4221 C  CA  . LYS   B 209 ? 0.9581 0.8811 0.6799 -0.0463 -0.0468 0.2139  365 LYS   B CA  
4222 C  C   . LYS   B 209 ? 1.0376 0.9589 0.7659 -0.0427 -0.0489 0.2373  365 LYS   B C   
4223 O  O   . LYS   B 209 ? 1.1048 1.0104 0.8506 -0.0360 -0.0468 0.2440  365 LYS   B O   
4224 C  CB  . LYS   B 209 ? 0.9867 0.8923 0.7142 -0.0475 -0.0368 0.2044  365 LYS   B CB  
4225 N  N   . PHE   B 214 ? 0.9436 0.9546 0.5957 -0.0684 -0.0706 0.2411  370 PHE   B N   
4226 C  CA  . PHE   B 214 ? 1.0077 1.0070 0.6817 -0.0590 -0.0718 0.2567  370 PHE   B CA  
4227 C  C   . PHE   B 214 ? 1.0133 1.0218 0.6987 -0.0537 -0.0813 0.2597  370 PHE   B C   
4228 O  O   . PHE   B 214 ? 1.0422 1.0715 0.7208 -0.0563 -0.0881 0.2616  370 PHE   B O   
4229 C  CB  . PHE   B 214 ? 0.9658 0.9400 0.6525 -0.0554 -0.0640 0.2518  370 PHE   B CB  
4230 N  N   . GLN   B 215 ? 1.0126 1.0065 0.7155 -0.0466 -0.0815 0.2602  371 GLN   B N   
4231 C  CA  . GLN   B 215 ? 0.8948 0.8964 0.6117 -0.0404 -0.0895 0.2642  371 GLN   B CA  
4232 C  C   . GLN   B 215 ? 0.9660 0.9819 0.6714 -0.0464 -0.0961 0.2490  371 GLN   B C   
4233 O  O   . GLN   B 215 ? 0.8197 0.8250 0.5241 -0.0478 -0.0917 0.2294  371 GLN   B O   
4234 C  CB  . GLN   B 215 ? 0.8761 0.8563 0.6157 -0.0308 -0.0862 0.2682  371 GLN   B CB  
4235 C  CG  . GLN   B 215 ? 0.8458 0.8337 0.6002 -0.0245 -0.0937 0.2704  371 GLN   B CG  
4236 C  CD  . GLN   B 215 ? 0.9083 0.9171 0.6667 -0.0220 -0.1003 0.2834  371 GLN   B CD  
4237 O  OE1 . GLN   B 215 ? 0.9343 0.9636 0.6874 -0.0257 -0.1085 0.2790  371 GLN   B OE1 
4238 N  NE2 . GLN   B 215 ? 0.9020 0.9063 0.6688 -0.0170 -0.0967 0.2988  371 GLN   B NE2 
4239 N  N   . GLU   B 216 ? 0.9396 0.9775 0.6418 -0.0484 -0.1040 0.2519  372 GLU   B N   
4240 C  CA  . GLU   B 216 ? 0.8376 0.8896 0.5250 -0.0566 -0.1090 0.2359  372 GLU   B CA  
4241 C  C   . GLU   B 216 ? 0.9417 0.9993 0.6409 -0.0535 -0.1165 0.2327  372 GLU   B C   
4242 O  O   . GLU   B 216 ? 0.9161 0.9827 0.6038 -0.0607 -0.1201 0.2181  372 GLU   B O   
4243 C  CB  . GLU   B 216 ? 0.8935 0.9671 0.5651 -0.0641 -0.1119 0.2377  372 GLU   B CB  
4244 C  CG  . GLU   B 216 ? 0.9806 1.0495 0.6323 -0.0714 -0.1040 0.2284  372 GLU   B CG  
4245 C  CD  . GLU   B 216 ? 1.1264 1.2114 0.7563 -0.0824 -0.1056 0.2129  372 GLU   B CD  
4246 O  OE1 . GLU   B 216 ? 1.2577 1.3532 0.8868 -0.0854 -0.1122 0.2051  372 GLU   B OE1 
4247 O  OE2 . GLU   B 216 ? 1.1663 1.2547 0.7806 -0.0881 -0.1003 0.2105  372 GLU   B OE2 
4248 N  N   . GLU   B 217 ? 0.8724 0.9228 0.5948 -0.0431 -0.1178 0.2445  373 GLU   B N   
4249 C  CA  . GLU   B 217 ? 0.7740 0.8339 0.5098 -0.0397 -0.1253 0.2442  373 GLU   B CA  
4250 C  C   . GLU   B 217 ? 0.7323 0.7715 0.4860 -0.0319 -0.1215 0.2382  373 GLU   B C   
4251 O  O   . GLU   B 217 ? 0.6482 0.6920 0.4187 -0.0259 -0.1263 0.2429  373 GLU   B O   
4252 C  CB  . GLU   B 217 ? 0.6603 0.7351 0.4112 -0.0335 -0.1301 0.2623  373 GLU   B CB  
4253 C  CG  . GLU   B 217 ? 0.8875 0.9883 0.6255 -0.0413 -0.1359 0.2662  373 GLU   B CG  
4254 C  CD  . GLU   B 217 ? 0.8734 0.9848 0.5869 -0.0544 -0.1380 0.2482  373 GLU   B CD  
4255 O  OE1 . GLU   B 217 ? 0.8677 0.9806 0.5799 -0.0577 -0.1413 0.2349  373 GLU   B OE1 
4256 O  OE2 . GLU   B 217 ? 0.8975 1.0159 0.5936 -0.0615 -0.1361 0.2472  373 GLU   B OE2 
4257 N  N   . THR   B 218 ? 0.6473 0.6640 0.4007 -0.0310 -0.1115 0.2251  374 THR   B N   
4258 C  CA  . THR   B 218 ? 0.6521 0.6488 0.4238 -0.0236 -0.1060 0.2155  374 THR   B CA  
4259 C  C   . THR   B 218 ? 0.7352 0.7311 0.5017 -0.0281 -0.1061 0.1932  374 THR   B C   
4260 O  O   . THR   B 218 ? 0.7875 0.7918 0.5349 -0.0371 -0.1071 0.1821  374 THR   B O   
4261 C  CB  . THR   B 218 ? 0.7259 0.6990 0.5021 -0.0202 -0.0952 0.2148  374 THR   B CB  
4262 O  OG1 . THR   B 218 ? 0.7464 0.7194 0.5030 -0.0284 -0.0909 0.2059  374 THR   B OG1 
4263 C  CG2 . THR   B 218 ? 0.7799 0.7492 0.5673 -0.0136 -0.0942 0.2373  374 THR   B CG2 
4264 N  N   . TRP   B 219 ? 0.6679 0.6533 0.4518 -0.0217 -0.1047 0.1870  375 TRP   B N   
4265 C  CA  . TRP   B 219 ? 0.6567 0.6384 0.4400 -0.0242 -0.1041 0.1674  375 TRP   B CA  
4266 C  C   . TRP   B 219 ? 0.6994 0.6574 0.4937 -0.0189 -0.0945 0.1579  375 TRP   B C   
4267 O  O   . TRP   B 219 ? 0.6833 0.6296 0.4922 -0.0116 -0.0908 0.1673  375 TRP   B O   
4268 C  CB  . TRP   B 219 ? 0.5816 0.5757 0.3764 -0.0220 -0.1121 0.1697  375 TRP   B CB  
4269 C  CG  . TRP   B 219 ? 0.6266 0.6468 0.4123 -0.0276 -0.1225 0.1805  375 TRP   B CG  
4270 C  CD1 . TRP   B 219 ? 0.6596 0.6929 0.4495 -0.0246 -0.1276 0.2021  375 TRP   B CD1 
4271 C  CD2 . TRP   B 219 ? 0.6521 0.6892 0.4240 -0.0373 -0.1292 0.1708  375 TRP   B CD2 
4272 N  NE1 . TRP   B 219 ? 0.5853 0.6446 0.3642 -0.0322 -0.1377 0.2067  375 TRP   B NE1 
4273 C  CE2 . TRP   B 219 ? 0.6635 0.7252 0.4309 -0.0406 -0.1388 0.1871  375 TRP   B CE2 
4274 C  CE3 . TRP   B 219 ? 0.6851 0.7187 0.4481 -0.0438 -0.1278 0.1502  375 TRP   B CE3 
4275 C  CZ2 . TRP   B 219 ? 0.7172 0.8006 0.4703 -0.0513 -0.1471 0.1824  375 TRP   B CZ2 
4276 C  CZ3 . TRP   B 219 ? 0.6301 0.6827 0.3793 -0.0540 -0.1352 0.1452  375 TRP   B CZ3 
4277 C  CH2 . TRP   B 219 ? 0.7259 0.8034 0.4697 -0.0582 -0.1449 0.1607  375 TRP   B CH2 
4278 N  N   . ARG   B 220 ? 0.6253 0.5763 0.4128 -0.0227 -0.0903 0.1397  376 ARG   B N   
4279 C  CA  . ARG   B 220 ? 0.5551 0.4864 0.3507 -0.0191 -0.0814 0.1305  376 ARG   B CA  
4280 C  C   . ARG   B 220 ? 0.5694 0.4959 0.3752 -0.0167 -0.0816 0.1182  376 ARG   B C   
4281 O  O   . ARG   B 220 ? 0.5424 0.4782 0.3417 -0.0210 -0.0858 0.1094  376 ARG   B O   
4282 C  CB  . ARG   B 220 ? 0.6299 0.5567 0.4107 -0.0247 -0.0751 0.1207  376 ARG   B CB  
4283 C  CG  . ARG   B 220 ? 0.6693 0.5784 0.4576 -0.0217 -0.0662 0.1171  376 ARG   B CG  
4284 C  CD  . ARG   B 220 ? 0.6455 0.5523 0.4231 -0.0264 -0.0606 0.1026  376 ARG   B CD  
4285 N  NE  . ARG   B 220 ? 0.7606 0.6678 0.5408 -0.0263 -0.0619 0.0891  376 ARG   B NE  
4286 C  CZ  . ARG   B 220 ? 0.7341 0.6467 0.5023 -0.0310 -0.0614 0.0775  376 ARG   B CZ  
4287 N  NH1 . ARG   B 220 ? 0.7698 0.6881 0.5218 -0.0363 -0.0589 0.0763  376 ARG   B NH1 
4288 N  NH2 . ARG   B 220 ? 0.6931 0.6047 0.4653 -0.0304 -0.0627 0.0668  376 ARG   B NH2 
4289 N  N   . LEU   B 221 ? 0.5152 0.4272 0.3366 -0.0105 -0.0768 0.1174  377 LEU   B N   
4290 C  CA  . LEU   B 221 ? 0.6433 0.5509 0.4753 -0.0079 -0.0765 0.1069  377 LEU   B CA  
4291 C  C   . LEU   B 221 ? 0.5888 0.4944 0.4109 -0.0128 -0.0736 0.0901  377 LEU   B C   
4292 O  O   . LEU   B 221 ? 0.6156 0.5170 0.4277 -0.0161 -0.0685 0.0855  377 LEU   B O   
4293 C  CB  . LEU   B 221 ? 0.5492 0.4408 0.3972 -0.0013 -0.0705 0.1079  377 LEU   B CB  
4294 C  CG  . LEU   B 221 ? 0.6688 0.5592 0.5313 0.0056  -0.0718 0.1229  377 LEU   B CG  
4295 C  CD1 . LEU   B 221 ? 0.5714 0.4427 0.4468 0.0107  -0.0636 0.1219  377 LEU   B CD1 
4296 C  CD2 . LEU   B 221 ? 0.5837 0.4875 0.4546 0.0082  -0.0794 0.1268  377 LEU   B CD2 
4297 N  N   . SER   B 222 ? 0.5273 0.4363 0.3531 -0.0132 -0.0766 0.0816  378 SER   B N   
4298 C  CA  . SER   B 222 ? 0.5067 0.4124 0.3253 -0.0169 -0.0734 0.0662  378 SER   B CA  
4299 C  C   . SER   B 222 ? 0.4837 0.3834 0.3159 -0.0133 -0.0726 0.0590  378 SER   B C   
4300 O  O   . SER   B 222 ? 0.5085 0.4143 0.3490 -0.0117 -0.0780 0.0621  378 SER   B O   
4301 C  CB  . SER   B 222 ? 0.5067 0.4243 0.3098 -0.0241 -0.0778 0.0612  378 SER   B CB  
4302 O  OG  . SER   B 222 ? 0.5169 0.4291 0.3151 -0.0267 -0.0735 0.0461  378 SER   B OG  
4303 N  N   . PHE   B 223 ? 0.4799 0.3690 0.3142 -0.0123 -0.0659 0.0499  379 PHE   B N   
4304 C  CA  . PHE   B 223 ? 0.5405 0.4238 0.3864 -0.0093 -0.0644 0.0427  379 PHE   B CA  
4305 C  C   . PHE   B 223 ? 0.5252 0.4065 0.3651 -0.0122 -0.0613 0.0298  379 PHE   B C   
4306 O  O   . PHE   B 223 ? 0.4901 0.3651 0.3383 -0.0098 -0.0581 0.0237  379 PHE   B O   
4307 C  CB  . PHE   B 223 ? 0.4764 0.3490 0.3334 -0.0047 -0.0591 0.0450  379 PHE   B CB  
4308 C  CG  . PHE   B 223 ? 0.4542 0.3260 0.3194 -0.0008 -0.0608 0.0572  379 PHE   B CG  
4309 C  CD1 . PHE   B 223 ? 0.4767 0.3517 0.3537 0.0030  -0.0647 0.0614  379 PHE   B CD1 
4310 C  CD2 . PHE   B 223 ? 0.4663 0.3344 0.3279 -0.0009 -0.0582 0.0651  379 PHE   B CD2 
4311 C  CE1 . PHE   B 223 ? 0.5226 0.3968 0.4087 0.0076  -0.0654 0.0735  379 PHE   B CE1 
4312 C  CE2 . PHE   B 223 ? 0.5361 0.4022 0.4060 0.0032  -0.0590 0.0773  379 PHE   B CE2 
4313 C  CZ  . PHE   B 223 ? 0.5362 0.4053 0.4187 0.0079  -0.0625 0.0816  379 PHE   B CZ  
4314 N  N   . SER   B 224 ? 0.5322 0.4185 0.3576 -0.0172 -0.0617 0.0257  380 SER   B N   
4315 C  CA  . SER   B 224 ? 0.5516 0.4341 0.3714 -0.0192 -0.0570 0.0137  380 SER   B CA  
4316 C  C   . SER   B 224 ? 0.5113 0.3916 0.3390 -0.0185 -0.0582 0.0068  380 SER   B C   
4317 O  O   . SER   B 224 ? 0.5603 0.4344 0.3896 -0.0175 -0.0531 -0.0014 380 SER   B O   
4318 C  CB  . SER   B 224 ? 0.6453 0.5335 0.4478 -0.0252 -0.0571 0.0101  380 SER   B CB  
4319 O  OG  . SER   B 224 ? 0.8012 0.6977 0.5995 -0.0293 -0.0641 0.0107  380 SER   B OG  
4320 N  N   . HIS   B 225 ? 0.4824 0.3684 0.3157 -0.0188 -0.0648 0.0106  381 HIS   B N   
4321 C  CA  . HIS   B 225 ? 0.5231 0.4072 0.3649 -0.0184 -0.0658 0.0046  381 HIS   B CA  
4322 C  C   . HIS   B 225 ? 0.4905 0.3671 0.3464 -0.0125 -0.0620 0.0048  381 HIS   B C   
4323 O  O   . HIS   B 225 ? 0.5136 0.3859 0.3747 -0.0119 -0.0597 -0.0019 381 HIS   B O   
4324 C  CB  . HIS   B 225 ? 0.5402 0.4343 0.3857 -0.0204 -0.0739 0.0096  381 HIS   B CB  
4325 C  CG  . HIS   B 225 ? 0.4810 0.3790 0.3368 -0.0156 -0.0770 0.0217  381 HIS   B CG  
4326 N  ND1 . HIS   B 225 ? 0.4943 0.3930 0.3463 -0.0142 -0.0764 0.0300  381 HIS   B ND1 
4327 C  CD2 . HIS   B 225 ? 0.4809 0.3816 0.3511 -0.0117 -0.0799 0.0269  381 HIS   B CD2 
4328 C  CE1 . HIS   B 225 ? 0.4984 0.3988 0.3622 -0.0093 -0.0785 0.0400  381 HIS   B CE1 
4329 N  NE2 . HIS   B 225 ? 0.4995 0.4017 0.3747 -0.0075 -0.0806 0.0382  381 HIS   B NE2 
4330 N  N   . ILE   B 226 ? 0.4806 0.3555 0.3427 -0.0087 -0.0611 0.0126  382 ILE   B N   
4331 C  CA  . ILE   B 226 ? 0.4484 0.3161 0.3218 -0.0044 -0.0568 0.0120  382 ILE   B CA  
4332 C  C   . ILE   B 226 ? 0.4863 0.3486 0.3559 -0.0047 -0.0503 0.0058  382 ILE   B C   
4333 O  O   . ILE   B 226 ? 0.4481 0.3067 0.3245 -0.0029 -0.0471 0.0011  382 ILE   B O   
4334 C  CB  . ILE   B 226 ? 0.4438 0.3094 0.3237 -0.0011 -0.0566 0.0213  382 ILE   B CB  
4335 C  CG1 . ILE   B 226 ? 0.4403 0.3127 0.3257 0.0004  -0.0627 0.0294  382 ILE   B CG1 
4336 C  CG2 . ILE   B 226 ? 0.4403 0.2983 0.3309 0.0022  -0.0516 0.0193  382 ILE   B CG2 
4337 C  CD1 . ILE   B 226 ? 0.4415 0.3175 0.3367 0.0016  -0.0657 0.0272  382 ILE   B CD1 
4338 N  N   . GLU   B 227 ? 0.4476 0.3106 0.3067 -0.0068 -0.0481 0.0063  383 GLU   B N   
4339 C  CA  . GLU   B 227 ? 0.5184 0.3784 0.3741 -0.0069 -0.0417 0.0010  383 GLU   B CA  
4340 C  C   . GLU   B 227 ? 0.5120 0.3707 0.3679 -0.0070 -0.0398 -0.0076 383 GLU   B C   
4341 O  O   . GLU   B 227 ? 0.4751 0.3312 0.3366 -0.0048 -0.0353 -0.0109 383 GLU   B O   
4342 C  CB  . GLU   B 227 ? 0.4880 0.3506 0.3315 -0.0096 -0.0400 0.0029  383 GLU   B CB  
4343 C  CG  . GLU   B 227 ? 0.6955 0.5599 0.5379 -0.0100 -0.0434 0.0127  383 GLU   B CG  
4344 C  CD  . GLU   B 227 ? 0.6503 0.5183 0.4799 -0.0132 -0.0422 0.0159  383 GLU   B CD  
4345 O  OE1 . GLU   B 227 ? 0.7680 0.6356 0.5977 -0.0131 -0.0428 0.0245  383 GLU   B OE1 
4346 O  OE2 . GLU   B 227 ? 0.6844 0.5551 0.5038 -0.0159 -0.0402 0.0100  383 GLU   B OE2 
4347 N  N   . LYS   B 228 ? 0.5120 0.3728 0.3621 -0.0098 -0.0433 -0.0108 384 LYS   B N   
4348 C  CA  . LYS   B 228 ? 0.5835 0.4411 0.4332 -0.0105 -0.0409 -0.0192 384 LYS   B CA  
4349 C  C   . LYS   B 228 ? 0.5208 0.3757 0.3838 -0.0074 -0.0412 -0.0199 384 LYS   B C   
4350 O  O   . LYS   B 228 ? 0.5145 0.3655 0.3815 -0.0055 -0.0365 -0.0243 384 LYS   B O   
4351 C  CB  . LYS   B 228 ? 0.5032 0.3637 0.3432 -0.0158 -0.0450 -0.0226 384 LYS   B CB  
4352 C  CG  . LYS   B 228 ? 0.5778 0.4332 0.4164 -0.0177 -0.0427 -0.0318 384 LYS   B CG  
4353 C  CD  . LYS   B 228 ? 0.6486 0.5036 0.4990 -0.0170 -0.0465 -0.0314 384 LYS   B CD  
4354 C  CE  . LYS   B 228 ? 0.7698 0.6316 0.6168 -0.0224 -0.0541 -0.0304 384 LYS   B CE  
4355 N  NZ  . LYS   B 228 ? 0.7417 0.6052 0.6015 -0.0215 -0.0580 -0.0287 384 LYS   B NZ  
4356 N  N   . GLU   B 229 ? 0.5197 0.3772 0.3901 -0.0067 -0.0462 -0.0149 385 GLU   B N   
4357 C  CA  . GLU   B 229 ? 0.5975 0.4532 0.4801 -0.0041 -0.0461 -0.0155 385 GLU   B CA  
4358 C  C   . GLU   B 229 ? 0.5732 0.4262 0.4619 -0.0008 -0.0410 -0.0150 385 GLU   B C   
4359 O  O   . GLU   B 229 ? 0.4899 0.3410 0.3843 0.0007  -0.0382 -0.0182 385 GLU   B O   
4360 C  CB  . GLU   B 229 ? 0.5418 0.4016 0.4318 -0.0035 -0.0517 -0.0100 385 GLU   B CB  
4361 C  CG  . GLU   B 229 ? 0.6271 0.4922 0.5126 -0.0076 -0.0574 -0.0105 385 GLU   B CG  
4362 C  CD  . GLU   B 229 ? 0.6995 0.5693 0.5960 -0.0067 -0.0620 -0.0071 385 GLU   B CD  
4363 O  OE1 . GLU   B 229 ? 0.6910 0.5580 0.5979 -0.0034 -0.0596 -0.0073 385 GLU   B OE1 
4364 O  OE2 . GLU   B 229 ? 0.8495 0.7270 0.7443 -0.0096 -0.0678 -0.0042 385 GLU   B OE2 
4365 N  N   . ILE   B 230 ? 0.5499 0.4032 0.4372 -0.0002 -0.0397 -0.0106 386 ILE   B N   
4366 C  CA  . ILE   B 230 ? 0.4827 0.3350 0.3746 0.0014  -0.0349 -0.0104 386 ILE   B CA  
4367 C  C   . ILE   B 230 ? 0.5553 0.4078 0.4448 0.0019  -0.0303 -0.0150 386 ILE   B C   
4368 O  O   . ILE   B 230 ? 0.5985 0.4516 0.4951 0.0036  -0.0277 -0.0164 386 ILE   B O   
4369 C  CB  . ILE   B 230 ? 0.4891 0.3410 0.3782 0.0006  -0.0339 -0.0055 386 ILE   B CB  
4370 C  CG1 . ILE   B 230 ? 0.4672 0.3172 0.3624 0.0016  -0.0367 -0.0007 386 ILE   B CG1 
4371 C  CG2 . ILE   B 230 ? 0.6385 0.4910 0.5297 0.0005  -0.0288 -0.0063 386 ILE   B CG2 
4372 C  CD1 . ILE   B 230 ? 0.5618 0.4096 0.4534 0.0007  -0.0359 0.0050  386 ILE   B CD1 
4373 N  N   . LEU   B 231 ? 0.5320 0.3848 0.4121 0.0005  -0.0287 -0.0169 387 LEU   B N   
4374 C  CA  . LEU   B 231 ? 0.4776 0.3306 0.3560 0.0019  -0.0230 -0.0207 387 LEU   B CA  
4375 C  C   . LEU   B 231 ? 0.5188 0.3689 0.4026 0.0037  -0.0216 -0.0250 387 LEU   B C   
4376 O  O   . LEU   B 231 ? 0.4938 0.3448 0.3826 0.0065  -0.0168 -0.0257 387 LEU   B O   
4377 C  CB  . LEU   B 231 ? 0.4524 0.3055 0.3187 -0.0002 -0.0212 -0.0229 387 LEU   B CB  
4378 C  CG  . LEU   B 231 ? 0.5585 0.4153 0.4207 -0.0009 -0.0186 -0.0191 387 LEU   B CG  
4379 C  CD1 . LEU   B 231 ? 0.6149 0.4722 0.4648 -0.0027 -0.0158 -0.0223 387 LEU   B CD1 
4380 C  CD2 . LEU   B 231 ? 0.6126 0.4728 0.4830 0.0016  -0.0139 -0.0180 387 LEU   B CD2 
4381 N  N   . ASN   B 232 ? 0.5073 0.3543 0.3900 0.0020  -0.0254 -0.0274 388 ASN   B N   
4382 C  CA  . ASN   B 232 ? 0.5533 0.3961 0.4405 0.0029  -0.0239 -0.0316 388 ASN   B CA  
4383 C  C   . ASN   B 232 ? 0.5430 0.3868 0.4418 0.0046  -0.0258 -0.0291 388 ASN   B C   
4384 O  O   . ASN   B 232 ? 0.5052 0.3456 0.4087 0.0053  -0.0247 -0.0315 388 ASN   B O   
4385 C  CB  . ASN   B 232 ? 0.4877 0.3272 0.3677 -0.0012 -0.0270 -0.0360 388 ASN   B CB  
4386 C  CG  . ASN   B 232 ? 0.6215 0.4584 0.4890 -0.0035 -0.0236 -0.0409 388 ASN   B CG  
4387 O  OD1 . ASN   B 232 ? 0.5229 0.3589 0.3886 -0.0009 -0.0174 -0.0420 388 ASN   B OD1 
4388 N  ND2 . ASN   B 232 ? 0.6616 0.4985 0.5203 -0.0088 -0.0276 -0.0438 388 ASN   B ND2 
4389 N  N   . ASN   B 233 ? 0.4592 0.3068 0.3620 0.0048  -0.0285 -0.0245 389 ASN   B N   
4390 C  CA  . ASN   B 233 ? 0.4901 0.3394 0.4030 0.0060  -0.0298 -0.0225 389 ASN   B CA  
4391 C  C   . ASN   B 233 ? 0.4390 0.2918 0.3541 0.0066  -0.0283 -0.0188 389 ASN   B C   
4392 O  O   . ASN   B 233 ? 0.4177 0.2709 0.3338 0.0058  -0.0306 -0.0162 389 ASN   B O   
4393 C  CB  . ASN   B 233 ? 0.4787 0.3280 0.3939 0.0043  -0.0352 -0.0218 389 ASN   B CB  
4394 C  CG  . ASN   B 233 ? 0.5274 0.3779 0.4527 0.0055  -0.0357 -0.0208 389 ASN   B CG  
4395 O  OD1 . ASN   B 233 ? 0.4861 0.3376 0.4161 0.0071  -0.0322 -0.0206 389 ASN   B OD1 
4396 N  ND2 . ASN   B 233 ? 0.4727 0.3247 0.4017 0.0045  -0.0398 -0.0196 389 ASN   B ND2 
4397 N  N   . HIS   B 234 ? 0.4031 0.2587 0.3190 0.0079  -0.0239 -0.0187 390 HIS   B N   
4398 C  CA  . HIS   B 234 ? 0.4371 0.2965 0.3513 0.0069  -0.0220 -0.0161 390 HIS   B CA  
4399 C  C   . HIS   B 234 ? 0.4309 0.2957 0.3521 0.0067  -0.0202 -0.0143 390 HIS   B C   
4400 O  O   . HIS   B 234 ? 0.4205 0.2888 0.3405 0.0046  -0.0187 -0.0125 390 HIS   B O   
4401 C  CB  . HIS   B 234 ? 0.4211 0.2821 0.3296 0.0076  -0.0182 -0.0169 390 HIS   B CB  
4402 C  CG  . HIS   B 234 ? 0.4591 0.3219 0.3720 0.0107  -0.0142 -0.0181 390 HIS   B CG  
4403 N  ND1 . HIS   B 234 ? 0.5135 0.3714 0.4234 0.0124  -0.0121 -0.0217 390 HIS   B ND1 
4404 C  CD2 . HIS   B 234 ? 0.4087 0.2779 0.3296 0.0125  -0.0118 -0.0157 390 HIS   B CD2 
4405 C  CE1 . HIS   B 234 ? 0.4861 0.3459 0.4027 0.0159  -0.0080 -0.0211 390 HIS   B CE1 
4406 N  NE2 . HIS   B 234 ? 0.4790 0.3469 0.4025 0.0161  -0.0081 -0.0168 390 HIS   B NE2 
4407 N  N   . GLY   B 235 ? 0.4657 0.3322 0.3937 0.0080  -0.0203 -0.0145 391 GLY   B N   
4408 C  CA  . GLY   B 235 ? 0.4191 0.2926 0.3526 0.0070  -0.0188 -0.0126 391 GLY   B CA  
4409 C  C   . GLY   B 235 ? 0.4166 0.2886 0.3525 0.0048  -0.0207 -0.0128 391 GLY   B C   
4410 O  O   . GLY   B 235 ? 0.3520 0.2183 0.2881 0.0052  -0.0233 -0.0137 391 GLY   B O   
4411 N  N   . LYS   B 236 ? 0.4187 0.2968 0.3567 0.0020  -0.0190 -0.0120 392 LYS   B N   
4412 C  CA  . LYS   B 236 ? 0.3666 0.2439 0.3078 0.0000  -0.0195 -0.0130 392 LYS   B CA  
4413 C  C   . LYS   B 236 ? 0.3719 0.2508 0.3188 0.0022  -0.0205 -0.0129 392 LYS   B C   
4414 O  O   . LYS   B 236 ? 0.3539 0.2292 0.3036 0.0025  -0.0218 -0.0140 392 LYS   B O   
4415 C  CB  . LYS   B 236 ? 0.3861 0.2702 0.3268 -0.0047 -0.0171 -0.0130 392 LYS   B CB  
4416 C  CG  . LYS   B 236 ? 0.4403 0.3230 0.3832 -0.0074 -0.0163 -0.0152 392 LYS   B CG  
4417 C  CD  . LYS   B 236 ? 0.5122 0.4008 0.4526 -0.0139 -0.0136 -0.0166 392 LYS   B CD  
4418 C  CE  . LYS   B 236 ? 0.5301 0.4109 0.4654 -0.0171 -0.0118 -0.0182 392 LYS   B CE  
4419 N  NZ  . LYS   B 236 ? 0.4855 0.3531 0.4213 -0.0144 -0.0119 -0.0191 392 LYS   B NZ  
4420 N  N   . SER   B 237 ? 0.3890 0.2737 0.3385 0.0040  -0.0196 -0.0109 393 SER   B N   
4421 C  CA  . SER   B 237 ? 0.4185 0.3033 0.3734 0.0064  -0.0202 -0.0101 393 SER   B CA  
4422 C  C   . SER   B 237 ? 0.4254 0.3013 0.3790 0.0088  -0.0219 -0.0119 393 SER   B C   
4423 O  O   . SER   B 237 ? 0.3823 0.2553 0.3320 0.0102  -0.0212 -0.0126 393 SER   B O   
4424 C  CB  . SER   B 237 ? 0.3869 0.2800 0.3455 0.0081  -0.0181 -0.0064 393 SER   B CB  
4425 O  OG  . SER   B 237 ? 0.4029 0.2938 0.3665 0.0109  -0.0181 -0.0051 393 SER   B OG  
4426 N  N   . LYS   B 238 ? 0.3805 0.2532 0.3375 0.0088  -0.0239 -0.0129 394 LYS   B N   
4427 C  CA  . LYS   B 238 ? 0.4344 0.3003 0.3905 0.0098  -0.0259 -0.0148 394 LYS   B CA  
4428 C  C   . LYS   B 238 ? 0.4763 0.3400 0.4329 0.0119  -0.0236 -0.0146 394 LYS   B C   
4429 O  O   . LYS   B 238 ? 0.4131 0.2703 0.3658 0.0120  -0.0240 -0.0173 394 LYS   B O   
4430 C  CB  . LYS   B 238 ? 0.4336 0.2989 0.3949 0.0089  -0.0282 -0.0151 394 LYS   B CB  
4431 C  CG  . LYS   B 238 ? 0.3880 0.2536 0.3496 0.0080  -0.0299 -0.0153 394 LYS   B CG  
4432 C  CD  . LYS   B 238 ? 0.3554 0.2226 0.3237 0.0076  -0.0312 -0.0151 394 LYS   B CD  
4433 C  CE  . LYS   B 238 ? 0.3380 0.2054 0.3078 0.0076  -0.0313 -0.0149 394 LYS   B CE  
4434 N  NZ  . LYS   B 238 ? 0.3745 0.2449 0.3519 0.0077  -0.0313 -0.0145 394 LYS   B NZ  
4435 N  N   . THR   B 239 ? 0.4487 0.3177 0.4100 0.0135  -0.0207 -0.0114 395 THR   B N   
4436 C  CA  . THR   B 239 ? 0.4578 0.3242 0.4211 0.0166  -0.0173 -0.0102 395 THR   B CA  
4437 C  C   . THR   B 239 ? 0.4282 0.2984 0.3892 0.0188  -0.0141 -0.0087 395 THR   B C   
4438 O  O   . THR   B 239 ? 0.4032 0.2738 0.3680 0.0225  -0.0102 -0.0062 395 THR   B O   
4439 C  CB  . THR   B 239 ? 0.4686 0.3391 0.4401 0.0180  -0.0158 -0.0059 395 THR   B CB  
4440 O  OG1 . THR   B 239 ? 0.4392 0.3213 0.4129 0.0166  -0.0162 -0.0022 395 THR   B OG1 
4441 C  CG2 . THR   B 239 ? 0.4401 0.3049 0.4144 0.0162  -0.0178 -0.0075 395 THR   B CG2 
4442 N  N   . CYS   B 240 ? 0.4124 0.2852 0.3679 0.0170  -0.0152 -0.0099 396 CYS   B N   
4443 C  CA  . CYS   B 240 ? 0.4397 0.3173 0.3936 0.0188  -0.0119 -0.0082 396 CYS   B CA  
4444 C  C   . CYS   B 240 ? 0.4437 0.3128 0.3950 0.0218  -0.0087 -0.0108 396 CYS   B C   
4445 O  O   . CYS   B 240 ? 0.4352 0.2948 0.3816 0.0204  -0.0102 -0.0154 396 CYS   B O   
4446 C  CB  . CYS   B 240 ? 0.4685 0.3492 0.4166 0.0154  -0.0134 -0.0090 396 CYS   B CB  
4447 S  SG  . CYS   B 240 ? 0.4342 0.3191 0.3780 0.0163  -0.0099 -0.0082 396 CYS   B SG  
4448 N  N   . CYS   B 241 ? 0.4022 0.2753 0.3574 0.0260  -0.0038 -0.0077 397 CYS   B N   
4449 C  CA  . CYS   B 241 ? 0.3871 0.2525 0.3414 0.0299  0.0015  -0.0099 397 CYS   B CA  
4450 C  C   . CYS   B 241 ? 0.4198 0.2737 0.3766 0.0311  0.0028  -0.0122 397 CYS   B C   
4451 O  O   . CYS   B 241 ? 0.4011 0.2457 0.3560 0.0334  0.0077  -0.0156 397 CYS   B O   
4452 C  CB  . CYS   B 241 ? 0.5248 0.3848 0.4685 0.0279  0.0017  -0.0153 397 CYS   B CB  
4453 S  SG  . CYS   B 241 ? 0.4110 0.2829 0.3528 0.0281  0.0037  -0.0122 397 CYS   B SG  
4454 N  N   . GLU   B 242 ? 0.3879 0.2420 0.3491 0.0292  -0.0007 -0.0107 398 GLU   B N   
4455 C  CA  . GLU   B 242 ? 0.4195 0.2631 0.3838 0.0297  0.0008  -0.0124 398 GLU   B CA  
4456 C  C   . GLU   B 242 ? 0.4705 0.3166 0.4455 0.0347  0.0053  -0.0056 398 GLU   B C   
4457 O  O   . GLU   B 242 ? 0.4538 0.2904 0.4324 0.0354  0.0074  -0.0060 398 GLU   B O   
4458 C  CB  . GLU   B 242 ? 0.4301 0.2720 0.3936 0.0246  -0.0052 -0.0144 398 GLU   B CB  
4459 C  CG  . GLU   B 242 ? 0.4568 0.2938 0.4107 0.0200  -0.0094 -0.0209 398 GLU   B CG  
4460 C  CD  . GLU   B 242 ? 0.5367 0.3714 0.4918 0.0158  -0.0143 -0.0226 398 GLU   B CD  
4461 O  OE1 . GLU   B 242 ? 0.4642 0.3014 0.4271 0.0163  -0.0143 -0.0191 398 GLU   B OE1 
4462 O  OE2 . GLU   B 242 ? 0.4501 0.2817 0.3989 0.0119  -0.0180 -0.0270 398 GLU   B OE2 
4463 N  N   . ASN   B 243 ? 0.5012 0.3602 0.4815 0.0382  0.0070  0.0012  399 ASN   B N   
4464 C  CA  . ASN   B 243 ? 0.5079 0.3722 0.4991 0.0435  0.0110  0.0096  399 ASN   B CA  
4465 C  C   . ASN   B 243 ? 0.5387 0.4170 0.5336 0.0475  0.0137  0.0155  399 ASN   B C   
4466 O  O   . ASN   B 243 ? 0.4746 0.3601 0.4638 0.0446  0.0113  0.0134  399 ASN   B O   
4467 C  CB  . ASN   B 243 ? 0.4379 0.3097 0.4341 0.0409  0.0068  0.0145  399 ASN   B CB  
4468 C  CG  . ASN   B 243 ? 0.4509 0.3368 0.4438 0.0362  0.0014  0.0152  399 ASN   B CG  
4469 O  OD1 . ASN   B 243 ? 0.4744 0.3733 0.4687 0.0371  0.0019  0.0194  399 ASN   B OD1 
4470 N  ND2 . ASN   B 243 ? 0.4204 0.3033 0.4089 0.0309  -0.0033 0.0108  399 ASN   B ND2 
4471 N  N   . LYS   B 244 ? 0.5329 0.4156 0.5383 0.0542  0.0190  0.0236  400 LYS   B N   
4472 C  CA  . LYS   B 244 ? 0.5489 0.4473 0.5597 0.0583  0.0218  0.0303  400 LYS   B CA  
4473 C  C   . LYS   B 244 ? 0.4210 0.3390 0.4305 0.0530  0.0157  0.0338  400 LYS   B C   
4474 O  O   . LYS   B 244 ? 0.4952 0.4240 0.5033 0.0525  0.0160  0.0346  400 LYS   B O   
4475 C  CB  . LYS   B 244 ? 0.5540 0.4572 0.5785 0.0668  0.0279  0.0408  400 LYS   B CB  
4476 C  CG  . LYS   B 244 ? 0.5210 0.4071 0.5488 0.0739  0.0368  0.0387  400 LYS   B CG  
4477 C  CD  . LYS   B 244 ? 0.5634 0.4575 0.6070 0.0826  0.0421  0.0519  400 LYS   B CD  
4478 C  CE  . LYS   B 244 ? 0.5405 0.4586 0.5913 0.0864  0.0428  0.0610  400 LYS   B CE  
4479 N  NZ  . LYS   B 244 ? 0.5107 0.4412 0.5785 0.0958  0.0479  0.0761  400 LYS   B NZ  
4480 N  N   . GLU   B 245 ? 0.5200 0.4430 0.5298 0.0485  0.0107  0.0357  401 GLU   B N   
4481 C  CA  . GLU   B 245 ? 0.4221 0.3634 0.4302 0.0428  0.0059  0.0384  401 GLU   B CA  
4482 C  C   . GLU   B 245 ? 0.4945 0.4324 0.4917 0.0367  0.0028  0.0298  401 GLU   B C   
4483 O  O   . GLU   B 245 ? 0.4616 0.4132 0.4568 0.0322  0.0006  0.0312  401 GLU   B O   
4484 C  CB  . GLU   B 245 ? 0.4577 0.4044 0.4675 0.0389  0.0020  0.0414  401 GLU   B CB  
4485 N  N   . GLU   B 246 ? 0.4897 0.4099 0.4796 0.0360  0.0027  0.0215  402 GLU   B N   
4486 C  CA  . GLU   B 246 ? 0.4577 0.3742 0.4378 0.0304  -0.0006 0.0146  402 GLU   B CA  
4487 C  C   . GLU   B 246 ? 0.4722 0.3808 0.4467 0.0322  0.0022  0.0101  402 GLU   B C   
4488 O  O   . GLU   B 246 ? 0.4678 0.3684 0.4337 0.0285  -0.0002 0.0040  402 GLU   B O   
4489 C  CB  . GLU   B 246 ? 0.4625 0.3686 0.4385 0.0266  -0.0046 0.0093  402 GLU   B CB  
4490 C  CG  . GLU   B 246 ? 0.4813 0.3951 0.4616 0.0241  -0.0071 0.0129  402 GLU   B CG  
4491 C  CD  . GLU   B 246 ? 0.4520 0.3569 0.4287 0.0204  -0.0106 0.0077  402 GLU   B CD  
4492 O  OE1 . GLU   B 246 ? 0.4513 0.3549 0.4221 0.0164  -0.0129 0.0035  402 GLU   B OE1 
4493 O  OE2 . GLU   B 246 ? 0.4343 0.3337 0.4148 0.0217  -0.0106 0.0082  402 GLU   B OE2 
4494 N  N   . LYS   B 247 ? 0.4590 0.3698 0.4383 0.0380  0.0077  0.0133  403 LYS   B N   
4495 C  CA  . LYS   B 247 ? 0.4722 0.3767 0.4454 0.0394  0.0111  0.0087  403 LYS   B CA  
4496 C  C   . LYS   B 247 ? 0.4635 0.3789 0.4323 0.0350  0.0093  0.0091  403 LYS   B C   
4497 O  O   . LYS   B 247 ? 0.4245 0.3564 0.3994 0.0349  0.0096  0.0155  403 LYS   B O   
4498 C  CB  . LYS   B 247 ? 0.4640 0.3680 0.4441 0.0472  0.0188  0.0119  403 LYS   B CB  
4499 C  CG  . LYS   B 247 ? 0.5391 0.4290 0.5230 0.0515  0.0222  0.0107  403 LYS   B CG  
4500 C  CD  . LYS   B 247 ? 0.6065 0.4777 0.5793 0.0478  0.0210  0.0004  403 LYS   B CD  
4501 C  CE  . LYS   B 247 ? 0.6387 0.4950 0.6149 0.0510  0.0252  -0.0015 403 LYS   B CE  
4502 N  NZ  . LYS   B 247 ? 0.6532 0.4927 0.6182 0.0476  0.0261  -0.0119 403 LYS   B NZ  
4503 N  N   . CYS   B 248 ? 0.4730 0.3801 0.4314 0.0310  0.0073  0.0029  404 CYS   B N   
4504 C  CA  . CYS   B 248 ? 0.4460 0.3610 0.3996 0.0267  0.0063  0.0032  404 CYS   B CA  
4505 C  C   . CYS   B 248 ? 0.4198 0.3308 0.3679 0.0288  0.0107  0.0004  404 CYS   B C   
4506 O  O   . CYS   B 248 ? 0.3999 0.3014 0.3475 0.0333  0.0146  -0.0025 404 CYS   B O   
4507 C  CB  . CYS   B 248 ? 0.4086 0.3185 0.3553 0.0202  0.0006  -0.0003 404 CYS   B CB  
4508 S  SG  . CYS   B 248 ? 0.4008 0.2941 0.3360 0.0186  -0.0012 -0.0072 404 CYS   B SG  
4509 N  N   . CYS   B 249 ? 0.4040 0.3217 0.3477 0.0252  0.0108  0.0009  405 CYS   B N   
4510 C  CA  . CYS   B 249 ? 0.3926 0.3086 0.3313 0.0272  0.0156  -0.0011 405 CYS   B CA  
4511 C  C   . CYS   B 249 ? 0.3644 0.2735 0.2911 0.0215  0.0126  -0.0050 405 CYS   B C   
4512 O  O   . CYS   B 249 ? 0.3751 0.2877 0.2971 0.0206  0.0156  -0.0051 405 CYS   B O   
4513 C  CB  . CYS   B 249 ? 0.4241 0.3567 0.3691 0.0287  0.0200  0.0044  405 CYS   B CB  
4514 S  SG  . CYS   B 249 ? 0.4717 0.4207 0.4188 0.0209  0.0158  0.0092  405 CYS   B SG  
4515 N  N   . ARG   B 250 ? 0.4110 0.3127 0.3341 0.0177  0.0068  -0.0070 406 ARG   B N   
4516 C  CA  . ARG   B 250 ? 0.4011 0.2970 0.3144 0.0129  0.0038  -0.0090 406 ARG   B CA  
4517 C  C   . ARG   B 250 ? 0.4032 0.2914 0.3073 0.0140  0.0059  -0.0130 406 ARG   B C   
4518 O  O   . ARG   B 250 ? 0.3983 0.2875 0.2950 0.0114  0.0068  -0.0129 406 ARG   B O   
4519 C  CB  . ARG   B 250 ? 0.4431 0.3319 0.3560 0.0103  -0.0019 -0.0101 406 ARG   B CB  
4520 C  CG  . ARG   B 250 ? 0.4001 0.2950 0.3185 0.0071  -0.0041 -0.0074 406 ARG   B CG  
4521 C  CD  . ARG   B 250 ? 0.4160 0.3019 0.3324 0.0050  -0.0088 -0.0092 406 ARG   B CD  
4522 N  NE  . ARG   B 250 ? 0.3990 0.2879 0.3193 0.0016  -0.0103 -0.0079 406 ARG   B NE  
4523 C  CZ  . ARG   B 250 ? 0.3887 0.2804 0.3154 0.0022  -0.0113 -0.0078 406 ARG   B CZ  
4524 N  NH1 . ARG   B 250 ? 0.3996 0.2926 0.3310 0.0065  -0.0105 -0.0075 406 ARG   B NH1 
4525 N  NH2 . ARG   B 250 ? 0.3893 0.2817 0.3175 -0.0017 -0.0125 -0.0079 406 ARG   B NH2 
4526 N  N   . LYS   B 251 ? 0.4091 0.2891 0.3128 0.0171  0.0068  -0.0169 407 LYS   B N   
4527 C  CA  . LYS   B 251 ? 0.4608 0.3331 0.3541 0.0168  0.0088  -0.0220 407 LYS   B CA  
4528 C  C   . LYS   B 251 ? 0.4699 0.3469 0.3619 0.0196  0.0165  -0.0223 407 LYS   B C   
4529 O  O   . LYS   B 251 ? 0.4286 0.3043 0.3104 0.0174  0.0181  -0.0246 407 LYS   B O   
4530 C  CB  . LYS   B 251 ? 0.5743 0.4362 0.4672 0.0182  0.0084  -0.0269 407 LYS   B CB  
4531 C  CG  . LYS   B 251 ? 0.5897 0.4461 0.4788 0.0141  0.0009  -0.0281 407 LYS   B CG  
4532 C  CD  . LYS   B 251 ? 0.6839 0.5340 0.5787 0.0155  -0.0001 -0.0304 407 LYS   B CD  
4533 C  CE  . LYS   B 251 ? 0.6726 0.5144 0.5587 0.0118  -0.0032 -0.0359 407 LYS   B CE  
4534 N  NZ  . LYS   B 251 ? 0.8600 0.6959 0.7383 0.0120  0.0028  -0.0420 407 LYS   B NZ  
4535 N  N   . ASP   B 252 ? 0.4575 0.3412 0.3602 0.0247  0.0214  -0.0194 408 ASP   B N   
4536 C  CA  . ASP   B 252 ? 0.4076 0.2979 0.3112 0.0281  0.0292  -0.0187 408 ASP   B CA  
4537 C  C   . ASP   B 252 ? 0.4047 0.3057 0.3052 0.0241  0.0286  -0.0150 408 ASP   B C   
4538 O  O   . ASP   B 252 ? 0.4099 0.3137 0.3054 0.0247  0.0341  -0.0161 408 ASP   B O   
4539 C  CB  . ASP   B 252 ? 0.4179 0.3151 0.3356 0.0350  0.0344  -0.0145 408 ASP   B CB  
4540 C  CG  . ASP   B 252 ? 0.5452 0.4299 0.4653 0.0399  0.0382  -0.0187 408 ASP   B CG  
4541 O  OD1 . ASP   B 252 ? 0.5367 0.4077 0.4462 0.0376  0.0380  -0.0261 408 ASP   B OD1 
4542 O  OD2 . ASP   B 252 ? 0.5415 0.4302 0.4740 0.0457  0.0413  -0.0142 408 ASP   B OD2 
4543 N  N   . CYS   B 253 ? 0.3793 0.2863 0.2828 0.0198  0.0230  -0.0106 409 CYS   B N   
4544 C  CA  . CYS   B 253 ? 0.4145 0.3294 0.3141 0.0149  0.0227  -0.0076 409 CYS   B CA  
4545 C  C   . CYS   B 253 ? 0.3835 0.2901 0.2692 0.0110  0.0212  -0.0106 409 CYS   B C   
4546 O  O   . CYS   B 253 ? 0.3909 0.3025 0.2713 0.0091  0.0246  -0.0095 409 CYS   B O   
4547 C  CB  . CYS   B 253 ? 0.3832 0.3037 0.2877 0.0101  0.0175  -0.0035 409 CYS   B CB  
4548 S  SG  . CYS   B 253 ? 0.4315 0.3692 0.3512 0.0121  0.0192  0.0022  409 CYS   B SG  
4549 N  N   . LEU   B 254 ? 0.4189 0.3142 0.2988 0.0093  0.0159  -0.0135 410 LEU   B N   
4550 C  CA  . LEU   B 254 ? 0.4122 0.3016 0.2789 0.0058  0.0142  -0.0155 410 LEU   B CA  
4551 C  C   . LEU   B 254 ? 0.4167 0.3049 0.2759 0.0079  0.0206  -0.0201 410 LEU   B C   
4552 O  O   . LEU   B 254 ? 0.4487 0.3396 0.2988 0.0051  0.0227  -0.0196 410 LEU   B O   
4553 C  CB  . LEU   B 254 ? 0.4108 0.2906 0.2739 0.0040  0.0074  -0.0172 410 LEU   B CB  
4554 C  CG  . LEU   B 254 ? 0.4999 0.3750 0.3498 0.0003  0.0044  -0.0183 410 LEU   B CG  
4555 C  CD1 . LEU   B 254 ? 0.4313 0.3109 0.2767 -0.0035 0.0042  -0.0129 410 LEU   B CD1 
4556 C  CD2 . LEU   B 254 ? 0.5116 0.3810 0.3630 -0.0009 -0.0027 -0.0177 410 LEU   B CD2 
4557 N  N   . LYS   B 255 ? 0.4210 0.3050 0.2840 0.0126  0.0245  -0.0245 411 LYS   B N   
4558 C  CA  . LYS   B 255 ? 0.4292 0.3105 0.2848 0.0146  0.0320  -0.0301 411 LYS   B CA  
4559 C  C   . LYS   B 255 ? 0.4424 0.3345 0.2991 0.0158  0.0388  -0.0271 411 LYS   B C   
4560 O  O   . LYS   B 255 ? 0.4371 0.3294 0.2830 0.0141  0.0429  -0.0300 411 LYS   B O   
4561 C  CB  . LYS   B 255 ? 0.4477 0.3219 0.3097 0.0202  0.0366  -0.0346 411 LYS   B CB  
4562 C  CG  . LYS   B 255 ? 0.5417 0.4040 0.3996 0.0180  0.0314  -0.0394 411 LYS   B CG  
4563 C  CD  . LYS   B 255 ? 0.7260 0.5802 0.5906 0.0233  0.0372  -0.0437 411 LYS   B CD  
4564 C  CE  . LYS   B 255 ? 0.6897 0.5342 0.5544 0.0209  0.0310  -0.0466 411 LYS   B CE  
4565 N  NZ  . LYS   B 255 ? 0.7618 0.6038 0.6404 0.0264  0.0333  -0.0446 411 LYS   B NZ  
4566 N  N   . LEU   B 256 ? 0.4082 0.3111 0.2780 0.0184  0.0399  -0.0211 412 LEU   B N   
4567 C  CA  . LEU   B 256 ? 0.4105 0.3262 0.2836 0.0197  0.0465  -0.0176 412 LEU   B CA  
4568 C  C   . LEU   B 256 ? 0.4036 0.3242 0.2681 0.0128  0.0439  -0.0145 412 LEU   B C   
4569 O  O   . LEU   B 256 ? 0.4377 0.3647 0.2975 0.0123  0.0498  -0.0142 412 LEU   B O   
4570 C  CB  . LEU   B 256 ? 0.4023 0.3306 0.2923 0.0235  0.0478  -0.0113 412 LEU   B CB  
4571 C  CG  . LEU   B 256 ? 0.4236 0.3509 0.3251 0.0319  0.0528  -0.0119 412 LEU   B CG  
4572 C  CD1 . LEU   B 256 ? 0.4046 0.3459 0.3219 0.0338  0.0508  -0.0041 412 LEU   B CD1 
4573 C  CD2 . LEU   B 256 ? 0.4169 0.3456 0.3186 0.0378  0.0637  -0.0145 412 LEU   B CD2 
4574 N  N   . MET   B 257 ? 0.4250 0.3428 0.2878 0.0075  0.0357  -0.0116 413 MET   B N   
4575 C  CA  . MET   B 257 ? 0.4315 0.3505 0.2850 0.0010  0.0333  -0.0084 413 MET   B CA  
4576 C  C   . MET   B 257 ? 0.4661 0.3782 0.3040 -0.0009 0.0340  -0.0123 413 MET   B C   
4577 O  O   . MET   B 257 ? 0.4465 0.3635 0.2765 -0.0042 0.0368  -0.0103 413 MET   B O   
4578 C  CB  . MET   B 257 ? 0.4211 0.3358 0.2763 -0.0035 0.0253  -0.0048 413 MET   B CB  
4579 C  CG  . MET   B 257 ? 0.4142 0.3360 0.2818 -0.0042 0.0239  -0.0011 413 MET   B CG  
4580 S  SD  . MET   B 257 ? 0.5605 0.4720 0.4280 -0.0085 0.0155  0.0004  413 MET   B SD  
4581 C  CE  . MET   B 257 ? 0.4304 0.3435 0.2912 -0.0159 0.0158  0.0056  413 MET   B CE  
4582 N  N   . LYS   B 258 ? 0.4779 0.3796 0.3107 0.0002  0.0312  -0.0177 414 LYS   B N   
4583 C  CA  . LYS   B 258 ? 0.5449 0.4417 0.3619 -0.0025 0.0318  -0.0220 414 LYS   B CA  
4584 C  C   . LYS   B 258 ? 0.5202 0.4212 0.3331 -0.0001 0.0419  -0.0262 414 LYS   B C   
4585 O  O   . LYS   B 258 ? 0.5325 0.4363 0.3330 -0.0037 0.0445  -0.0267 414 LYS   B O   
4586 C  CB  . LYS   B 258 ? 0.4787 0.3649 0.2919 -0.0025 0.0272  -0.0274 414 LYS   B CB  
4587 C  CG  . LYS   B 258 ? 0.4927 0.3752 0.3061 -0.0058 0.0172  -0.0232 414 LYS   B CG  
4588 C  CD  . LYS   B 258 ? 0.5680 0.4421 0.3789 -0.0059 0.0129  -0.0286 414 LYS   B CD  
4589 C  CE  . LYS   B 258 ? 0.6855 0.5572 0.4807 -0.0092 0.0150  -0.0350 414 LYS   B CE  
4590 N  NZ  . LYS   B 258 ? 0.7601 0.6240 0.5527 -0.0104 0.0117  -0.0413 414 LYS   B NZ  
4591 N  N   . TYR   B 259 ? 0.5379 0.4402 0.3617 0.0064  0.0483  -0.0287 415 TYR   B N   
4592 C  CA  . TYR   B 259 ? 0.4844 0.3896 0.3055 0.0099  0.0592  -0.0331 415 TYR   B CA  
4593 C  C   . TYR   B 259 ? 0.5245 0.4437 0.3474 0.0088  0.0636  -0.0273 415 TYR   B C   
4594 O  O   . TYR   B 259 ? 0.4806 0.4030 0.2944 0.0082  0.0708  -0.0300 415 TYR   B O   
4595 C  CB  . TYR   B 259 ? 0.4899 0.3921 0.3238 0.0180  0.0652  -0.0361 415 TYR   B CB  
4596 C  CG  . TYR   B 259 ? 0.6196 0.5224 0.4519 0.0230  0.0778  -0.0413 415 TYR   B CG  
4597 C  CD1 . TYR   B 259 ? 0.6967 0.5893 0.5131 0.0206  0.0821  -0.0507 415 TYR   B CD1 
4598 C  CD2 . TYR   B 259 ? 0.5320 0.4459 0.3788 0.0298  0.0857  -0.0370 415 TYR   B CD2 
4599 C  CE1 . TYR   B 259 ? 0.7314 0.6231 0.5457 0.0251  0.0949  -0.0566 415 TYR   B CE1 
4600 C  CE2 . TYR   B 259 ? 0.6233 0.5375 0.4698 0.0352  0.0982  -0.0416 415 TYR   B CE2 
4601 C  CZ  . TYR   B 259 ? 0.7231 0.6251 0.5532 0.0330  0.1033  -0.0519 415 TYR   B CZ  
4602 O  OH  . TYR   B 259 ? 0.8273 0.7283 0.6566 0.0384  0.1171  -0.0574 415 TYR   B OH  
4603 N  N   . LEU   B 260 ? 0.5081 0.4361 0.3420 0.0078  0.0596  -0.0194 416 LEU   B N   
4604 C  CA  . LEU   B 260 ? 0.5027 0.4445 0.3384 0.0051  0.0630  -0.0135 416 LEU   B CA  
4605 C  C   . LEU   B 260 ? 0.4810 0.4214 0.3004 -0.0021 0.0611  -0.0125 416 LEU   B C   
4606 O  O   . LEU   B 260 ? 0.4724 0.4207 0.2863 -0.0033 0.0677  -0.0119 416 LEU   B O   
4607 C  CB  . LEU   B 260 ? 0.4561 0.4062 0.3052 0.0035  0.0582  -0.0062 416 LEU   B CB  
4608 C  CG  . LEU   B 260 ? 0.4578 0.4221 0.3085 -0.0011 0.0610  0.0001  416 LEU   B CG  
4609 C  CD1 . LEU   B 260 ? 0.4956 0.4724 0.3512 0.0039  0.0717  -0.0002 416 LEU   B CD1 
4610 C  CD2 . LEU   B 260 ? 0.5027 0.4742 0.3648 -0.0047 0.0558  0.0063  416 LEU   B CD2 
4611 N  N   . LEU   B 261 ? 0.5061 0.4374 0.3183 -0.0067 0.0522  -0.0114 417 LEU   B N   
4612 C  CA  . LEU   B 261 ? 0.4955 0.4260 0.2929 -0.0132 0.0497  -0.0088 417 LEU   B CA  
4613 C  C   . LEU   B 261 ? 0.5403 0.4685 0.3225 -0.0135 0.0548  -0.0155 417 LEU   B C   
4614 O  O   . LEU   B 261 ? 0.5474 0.4810 0.3185 -0.0177 0.0578  -0.0135 417 LEU   B O   
4615 C  CB  . LEU   B 261 ? 0.4907 0.4123 0.2851 -0.0169 0.0394  -0.0055 417 LEU   B CB  
4616 C  CG  . LEU   B 261 ? 0.6007 0.5223 0.3806 -0.0232 0.0367  -0.0009 417 LEU   B CG  
4617 C  CD1 . LEU   B 261 ? 0.5395 0.4698 0.3215 -0.0269 0.0400  0.0063  417 LEU   B CD1 
4618 C  CD2 . LEU   B 261 ? 0.5830 0.4960 0.3608 -0.0255 0.0270  0.0027  417 LEU   B CD2 
4619 N  N   . GLU   B 262 ? 0.5418 0.4619 0.3230 -0.0097 0.0562  -0.0236 418 GLU   B N   
4620 C  CA  . GLU   B 262 ? 0.5787 0.4947 0.3440 -0.0112 0.0607  -0.0316 418 GLU   B CA  
4621 C  C   . GLU   B 262 ? 0.6034 0.5273 0.3680 -0.0084 0.0730  -0.0344 418 GLU   B C   
4622 O  O   . GLU   B 262 ? 0.5819 0.5093 0.3318 -0.0126 0.0770  -0.0360 418 GLU   B O   
4623 C  CB  . GLU   B 262 ? 0.5799 0.4841 0.3455 -0.0085 0.0594  -0.0399 418 GLU   B CB  
4624 C  CG  . GLU   B 262 ? 0.6084 0.5061 0.3684 -0.0133 0.0477  -0.0383 418 GLU   B CG  
4625 C  CD  . GLU   B 262 ? 0.6693 0.5568 0.4356 -0.0103 0.0451  -0.0442 418 GLU   B CD  
4626 O  OE1 . GLU   B 262 ? 0.6082 0.4922 0.3788 -0.0115 0.0359  -0.0408 418 GLU   B OE1 
4627 O  OE2 . GLU   B 262 ? 0.7186 0.6007 0.4836 -0.0072 0.0530  -0.0528 418 GLU   B OE2 
4628 N  N   . GLN   B 263 ? 0.6073 0.5357 0.3885 -0.0013 0.0791  -0.0337 419 GLN   B N   
4629 C  CA  . GLN   B 263 ? 0.5784 0.5166 0.3625 0.0025  0.0912  -0.0347 419 GLN   B CA  
4630 C  C   . GLN   B 263 ? 0.5917 0.5426 0.3713 -0.0030 0.0918  -0.0274 419 GLN   B C   
4631 O  O   . GLN   B 263 ? 0.6326 0.5893 0.4034 -0.0038 0.1004  -0.0299 419 GLN   B O   
4632 C  CB  . GLN   B 263 ? 0.6111 0.5546 0.4163 0.0111  0.0959  -0.0325 419 GLN   B CB  
4633 C  CG  . GLN   B 263 ? 0.5941 0.5253 0.4039 0.0176  0.0991  -0.0400 419 GLN   B CG  
4634 C  CD  . GLN   B 263 ? 0.7338 0.6596 0.5339 0.0203  0.1113  -0.0497 419 GLN   B CD  
4635 O  OE1 . GLN   B 263 ? 0.6527 0.5675 0.4356 0.0156  0.1105  -0.0578 419 GLN   B OE1 
4636 N  NE2 . GLN   B 263 ? 0.7429 0.6773 0.5538 0.0277  0.1229  -0.0489 419 GLN   B NE2 
4637 N  N   . LEU   B 264 ? 0.6110 0.5660 0.3962 -0.0071 0.0833  -0.0186 420 LEU   B N   
4638 C  CA  . LEU   B 264 ? 0.6225 0.5884 0.4038 -0.0129 0.0841  -0.0112 420 LEU   B CA  
4639 C  C   . LEU   B 264 ? 0.6194 0.5816 0.3799 -0.0197 0.0822  -0.0118 420 LEU   B C   
4640 O  O   . LEU   B 264 ? 0.5611 0.5320 0.3133 -0.0229 0.0883  -0.0102 420 LEU   B O   
4641 C  CB  . LEU   B 264 ? 0.5222 0.4911 0.3143 -0.0164 0.0762  -0.0023 420 LEU   B CB  
4642 C  CG  . LEU   B 264 ? 0.5196 0.4973 0.3317 -0.0116 0.0782  0.0002  420 LEU   B CG  
4643 C  CD1 . LEU   B 264 ? 0.5756 0.5543 0.3955 -0.0168 0.0700  0.0075  420 LEU   B CD1 
4644 C  CD2 . LEU   B 264 ? 0.5768 0.5705 0.3946 -0.0092 0.0888  0.0017  420 LEU   B CD2 
4645 N  N   . LYS   B 265 ? 0.6003 0.5511 0.3525 -0.0224 0.0733  -0.0133 421 LYS   B N   
4646 C  CA  . LYS   B 265 ? 0.5696 0.5186 0.3020 -0.0289 0.0706  -0.0132 421 LYS   B CA  
4647 C  C   . LYS   B 265 ? 0.6636 0.6143 0.3824 -0.0286 0.0804  -0.0222 421 LYS   B C   
4648 O  O   . LYS   B 265 ? 0.7040 0.6605 0.4078 -0.0342 0.0826  -0.0205 421 LYS   B O   
4649 C  CB  . LYS   B 265 ? 0.5673 0.5054 0.2949 -0.0309 0.0598  -0.0136 421 LYS   B CB  
4650 C  CG  . LYS   B 265 ? 0.5820 0.5183 0.3177 -0.0331 0.0506  -0.0036 421 LYS   B CG  
4651 C  CD  . LYS   B 265 ? 0.6437 0.5717 0.3737 -0.0352 0.0406  -0.0027 421 LYS   B CD  
4652 C  CE  . LYS   B 265 ? 0.6264 0.5578 0.3369 -0.0415 0.0389  -0.0003 421 LYS   B CE  
4653 N  NZ  . LYS   B 265 ? 0.7483 0.6748 0.4545 -0.0440 0.0283  0.0040  421 LYS   B NZ  
4654 N  N   . GLU   B 266 ? 0.6188 0.5643 0.3428 -0.0223 0.0868  -0.0318 422 GLU   B N   
4655 C  CA  . GLU   B 266 ? 0.7198 0.6653 0.4323 -0.0214 0.0981  -0.0417 422 GLU   B CA  
4656 C  C   . GLU   B 266 ? 0.7233 0.6823 0.4388 -0.0198 0.1090  -0.0389 422 GLU   B C   
4657 O  O   . GLU   B 266 ? 0.7710 0.7337 0.4713 -0.0230 0.1166  -0.0434 422 GLU   B O   
4658 C  CB  . GLU   B 266 ? 0.7757 0.7106 0.4957 -0.0143 0.1031  -0.0517 422 GLU   B CB  
4659 C  CG  . GLU   B 266 ? 0.7576 0.6790 0.4674 -0.0176 0.0960  -0.0587 422 GLU   B CG  
4660 C  CD  . GLU   B 266 ? 0.8056 0.7257 0.4905 -0.0254 0.0980  -0.0659 422 GLU   B CD  
4661 O  OE1 . GLU   B 266 ? 0.7966 0.7249 0.4720 -0.0274 0.1065  -0.0668 422 GLU   B OE1 
4662 O  OE2 . GLU   B 266 ? 0.9781 0.8900 0.6528 -0.0301 0.0912  -0.0708 422 GLU   B OE2 
4663 N  N   . ARG   B 267 ? 0.7531 0.7206 0.4879 -0.0154 0.1103  -0.0318 423 ARG   B N   
4664 C  CA  . ARG   B 267 ? 0.7545 0.7368 0.4939 -0.0139 0.1207  -0.0287 423 ARG   B CA  
4665 C  C   . ARG   B 267 ? 0.8171 0.8075 0.5425 -0.0230 0.1188  -0.0220 423 ARG   B C   
4666 O  O   . ARG   B 267 ? 0.7321 0.7308 0.4482 -0.0245 0.1283  -0.0239 423 ARG   B O   
4667 C  CB  . ARG   B 267 ? 0.7899 0.7815 0.5533 -0.0084 0.1211  -0.0217 423 ARG   B CB  
4668 C  CG  . ARG   B 267 ? 0.8244 0.8348 0.5950 -0.0097 0.1276  -0.0142 423 ARG   B CG  
4669 C  CD  . ARG   B 267 ? 0.8135 0.8327 0.5909 -0.0017 0.1426  -0.0189 423 ARG   B CD  
4670 N  NE  . ARG   B 267 ? 0.7653 0.7817 0.5603 0.0084  0.1457  -0.0218 423 ARG   B NE  
4671 C  CZ  . ARG   B 267 ? 0.8221 0.8477 0.6378 0.0120  0.1425  -0.0144 423 ARG   B CZ  
4672 N  NH1 . ARG   B 267 ? 0.9008 0.9386 0.7225 0.0058  0.1364  -0.0046 423 ARG   B NH1 
4673 N  NH2 . ARG   B 267 ? 0.9163 0.9389 0.7467 0.0215  0.1456  -0.0167 423 ARG   B NH2 
4674 N  N   . PHE   B 268 ? 0.7382 0.7254 0.4610 -0.0290 0.1068  -0.0141 424 PHE   B N   
4675 C  CA  . PHE   B 268 ? 0.7628 0.7571 0.4751 -0.0373 0.1045  -0.0055 424 PHE   B CA  
4676 C  C   . PHE   B 268 ? 0.7398 0.7266 0.4318 -0.0438 0.0971  -0.0056 424 PHE   B C   
4677 O  O   . PHE   B 268 ? 0.8072 0.7961 0.4932 -0.0502 0.0910  0.0040  424 PHE   B O   
4678 C  CB  . PHE   B 268 ? 0.7441 0.7422 0.4707 -0.0396 0.0981  0.0057  424 PHE   B CB  
4679 C  CG  . PHE   B 268 ? 0.7894 0.7990 0.5354 -0.0351 0.1047  0.0075  424 PHE   B CG  
4680 C  CD1 . PHE   B 268 ? 0.7280 0.7347 0.4914 -0.0291 0.1019  0.0062  424 PHE   B CD1 
4681 C  CD2 . PHE   B 268 ? 0.6306 0.6556 0.3776 -0.0368 0.1139  0.0109  424 PHE   B CD2 
4682 C  CE1 . PHE   B 268 ? 0.7647 0.7847 0.5463 -0.0252 0.1074  0.0089  424 PHE   B CE1 
4683 C  CE2 . PHE   B 268 ? 0.7031 0.7414 0.4688 -0.0327 0.1197  0.0133  424 PHE   B CE2 
4684 C  CZ  . PHE   B 268 ? 0.6826 0.7189 0.4658 -0.0269 0.1162  0.0126  424 PHE   B CZ  
4685 N  N   . LYS   B 269 ? 0.8146 0.7932 0.4960 -0.0425 0.0977  -0.0161 425 LYS   B N   
4686 C  CA  . LYS   B 269 ? 0.8301 0.8034 0.4928 -0.0491 0.0897  -0.0162 425 LYS   B CA  
4687 C  C   . LYS   B 269 ? 0.8987 0.8819 0.5430 -0.0568 0.0920  -0.0111 425 LYS   B C   
4688 O  O   . LYS   B 269 ? 0.9088 0.8918 0.5425 -0.0630 0.0830  -0.0036 425 LYS   B O   
4689 C  CB  . LYS   B 269 ? 0.7999 0.7639 0.4539 -0.0474 0.0917  -0.0298 425 LYS   B CB  
4690 C  CG  . LYS   B 269 ? 0.7259 0.6928 0.3713 -0.0458 0.1060  -0.0408 425 LYS   B CG  
4691 C  CD  . LYS   B 269 ? 0.8953 0.8547 0.5208 -0.0500 0.1070  -0.0530 425 LYS   B CD  
4692 C  CE  . LYS   B 269 ? 0.8419 0.7875 0.4734 -0.0473 0.1005  -0.0594 425 LYS   B CE  
4693 N  NZ  . LYS   B 269 ? 0.8895 0.8268 0.5091 -0.0475 0.1099  -0.0756 425 LYS   B NZ  
4694 N  N   . ASP   B 270 ? 0.8069 0.7993 0.4474 -0.0565 0.1041  -0.0143 426 ASP   B N   
4695 C  CA  . ASP   B 270 ? 0.9212 0.9240 0.5440 -0.0641 0.1070  -0.0092 426 ASP   B CA  
4696 C  C   . ASP   B 270 ? 0.8856 0.8957 0.5157 -0.0675 0.1034  0.0059  426 ASP   B C   
4697 O  O   . ASP   B 270 ? 0.9090 0.9269 0.5249 -0.0745 0.1039  0.0128  426 ASP   B O   
4698 C  CB  . ASP   B 270 ? 0.9143 0.9245 0.5298 -0.0626 0.1224  -0.0187 426 ASP   B CB  
4699 C  CG  . ASP   B 270 ? 0.9277 0.9393 0.5649 -0.0531 0.1316  -0.0227 426 ASP   B CG  
4700 O  OD1 . ASP   B 270 ? 0.9285 0.9341 0.5844 -0.0479 0.1256  -0.0201 426 ASP   B OD1 
4701 O  OD2 . ASP   B 270 ? 1.0181 1.0376 0.6536 -0.0507 0.1450  -0.0281 426 ASP   B OD2 
4702 N  N   . LYS   B 271 ? 0.8479 0.8556 0.4991 -0.0635 0.1002  0.0112  427 LYS   B N   
4703 C  CA  . LYS   B 271 ? 0.8194 0.8300 0.4768 -0.0680 0.0950  0.0251  427 LYS   B CA  
4704 C  C   . LYS   B 271 ? 0.8899 0.8889 0.5473 -0.0696 0.0817  0.0310  427 LYS   B C   
4705 O  O   . LYS   B 271 ? 0.8213 0.8114 0.4784 -0.0663 0.0764  0.0243  427 LYS   B O   
4706 C  CB  . LYS   B 271 ? 0.8351 0.8503 0.5145 -0.0645 0.0985  0.0280  427 LYS   B CB  
4707 C  CG  . LYS   B 271 ? 0.8483 0.8724 0.5374 -0.0582 0.1103  0.0200  427 LYS   B CG  
4708 C  CD  . LYS   B 271 ? 0.8297 0.8634 0.5047 -0.0592 0.1218  0.0147  427 LYS   B CD  
4709 C  CE  . LYS   B 271 ? 0.8897 0.9233 0.5716 -0.0503 0.1313  0.0024  427 LYS   B CE  
4710 N  NZ  . LYS   B 271 ? 0.8959 0.9372 0.5639 -0.0506 0.1440  -0.0047 427 LYS   B NZ  
4711 N  N   . LYS   B 272 ? 0.8924 0.8915 0.5515 -0.0745 0.0767  0.0439  428 LYS   B N   
4712 C  CA  . LYS   B 272 ? 0.8242 0.8127 0.4839 -0.0756 0.0651  0.0512  428 LYS   B CA  
4713 C  C   . LYS   B 272 ? 0.7963 0.7756 0.4763 -0.0715 0.0604  0.0522  428 LYS   B C   
4714 O  O   . LYS   B 272 ? 0.7897 0.7591 0.4723 -0.0708 0.0514  0.0560  428 LYS   B O   
4715 C  CB  . LYS   B 272 ? 0.8425 0.8339 0.4933 -0.0827 0.0625  0.0653  428 LYS   B CB  
4716 C  CG  . LYS   B 272 ? 0.9097 0.9139 0.5419 -0.0879 0.0697  0.0659  428 LYS   B CG  
4717 C  CD  . LYS   B 272 ? 0.8845 0.8902 0.4965 -0.0919 0.0637  0.0687  428 LYS   B CD  
4718 C  CE  . LYS   B 272 ? 0.8635 0.8699 0.4650 -0.0897 0.0654  0.0537  428 LYS   B CE  
4719 N  NZ  . LYS   B 272 ? 0.8667 0.8799 0.4449 -0.0960 0.0622  0.0555  428 LYS   B NZ  
4720 N  N   . HIS   B 273 ? 0.7670 0.7503 0.4615 -0.0689 0.0664  0.0489  429 HIS   B N   
4721 C  CA  . HIS   B 273 ? 0.7148 0.6917 0.4273 -0.0675 0.0625  0.0520  429 HIS   B CA  
4722 C  C   . HIS   B 273 ? 0.6541 0.6193 0.3724 -0.0623 0.0548  0.0470  429 HIS   B C   
4723 O  O   . HIS   B 273 ? 0.7268 0.6824 0.4508 -0.0631 0.0477  0.0527  429 HIS   B O   
4724 C  CB  . HIS   B 273 ? 0.7592 0.7461 0.4852 -0.0656 0.0704  0.0485  429 HIS   B CB  
4725 C  CG  . HIS   B 273 ? 0.7438 0.7425 0.4672 -0.0715 0.0773  0.0550  429 HIS   B CG  
4726 N  ND1 . HIS   B 273 ? 0.8246 0.8208 0.5442 -0.0788 0.0747  0.0661  429 HIS   B ND1 
4727 C  CD2 . HIS   B 273 ? 0.7808 0.7940 0.5038 -0.0711 0.0871  0.0522  429 HIS   B CD2 
4728 C  CE1 . HIS   B 273 ? 0.8465 0.8554 0.5637 -0.0833 0.0824  0.0698  429 HIS   B CE1 
4729 N  NE2 . HIS   B 273 ? 0.8653 0.8853 0.5845 -0.0787 0.0900  0.0615  429 HIS   B NE2 
4730 N  N   . LEU   B 274 ? 0.6133 0.5785 0.3297 -0.0572 0.0566  0.0364  430 LEU   B N   
4731 C  CA  . LEU   B 274 ? 0.6336 0.5891 0.3582 -0.0521 0.0507  0.0309  430 LEU   B CA  
4732 C  C   . LEU   B 274 ? 0.6786 0.6274 0.3912 -0.0524 0.0438  0.0292  430 LEU   B C   
4733 O  O   . LEU   B 274 ? 0.6510 0.5924 0.3691 -0.0484 0.0393  0.0238  430 LEU   B O   
4734 C  CB  . LEU   B 274 ? 0.5830 0.5417 0.3164 -0.0458 0.0571  0.0207  430 LEU   B CB  
4735 C  CG  . LEU   B 274 ? 0.5917 0.5599 0.3394 -0.0447 0.0636  0.0225  430 LEU   B CG  
4736 C  CD1 . LEU   B 274 ? 0.6155 0.5864 0.3727 -0.0371 0.0692  0.0136  430 LEU   B CD1 
4737 C  CD2 . LEU   B 274 ? 0.5751 0.5402 0.3355 -0.0473 0.0581  0.0298  430 LEU   B CD2 
4738 N  N   . ASP   B 275 ? 0.6775 0.6299 0.3739 -0.0576 0.0425  0.0343  431 ASP   B N   
4739 C  CA  . ASP   B 275 ? 0.7530 0.7024 0.4367 -0.0590 0.0358  0.0329  431 ASP   B CA  
4740 C  C   . ASP   B 275 ? 0.6840 0.6242 0.3764 -0.0573 0.0256  0.0385  431 ASP   B C   
4741 O  O   . ASP   B 275 ? 0.7100 0.6466 0.3994 -0.0560 0.0201  0.0340  431 ASP   B O   
4742 C  CB  . ASP   B 275 ? 0.7721 0.7296 0.4371 -0.0656 0.0360  0.0395  431 ASP   B CB  
4743 C  CG  . ASP   B 275 ? 0.8168 0.7839 0.4704 -0.0676 0.0467  0.0329  431 ASP   B CG  
4744 O  OD1 . ASP   B 275 ? 0.8873 0.8564 0.5507 -0.0640 0.0548  0.0270  431 ASP   B OD1 
4745 O  OD2 . ASP   B 275 ? 1.0273 1.0013 0.6623 -0.0730 0.0471  0.0342  431 ASP   B OD2 
4746 N  N   . LYS   B 276 ? 0.5875 0.5237 0.2902 -0.0579 0.0234  0.0483  432 LYS   B N   
4747 C  CA  . LYS   B 276 ? 0.6499 0.5769 0.3609 -0.0561 0.0149  0.0545  432 LYS   B CA  
4748 C  C   . LYS   B 276 ? 0.7038 0.6233 0.4305 -0.0507 0.0134  0.0474  432 LYS   B C   
4749 O  O   . LYS   B 276 ? 0.7305 0.6424 0.4644 -0.0487 0.0069  0.0509  432 LYS   B O   
4750 C  CB  . LYS   B 276 ? 0.7054 0.6290 0.4208 -0.0591 0.0143  0.0674  432 LYS   B CB  
4751 C  CG  . LYS   B 276 ? 0.6825 0.6101 0.3843 -0.0633 0.0111  0.0787  432 LYS   B CG  
4752 C  CD  . LYS   B 276 ? 0.7798 0.7073 0.4819 -0.0677 0.0150  0.0897  432 LYS   B CD  
4753 C  CE  . LYS   B 276 ? 0.6891 0.6194 0.3796 -0.0711 0.0109  0.1031  432 LYS   B CE  
4754 N  NZ  . LYS   B 276 ? 0.9136 0.8360 0.6109 -0.0732 0.0117  0.1165  432 LYS   B NZ  
4755 N  N   . PHE   B 277 ? 0.6356 0.5575 0.3681 -0.0481 0.0195  0.0383  433 PHE   B N   
4756 C  CA  . PHE   B 277 ? 0.6238 0.5398 0.3707 -0.0432 0.0180  0.0324  433 PHE   B CA  
4757 C  C   . PHE   B 277 ? 0.6886 0.6025 0.4314 -0.0402 0.0153  0.0237  433 PHE   B C   
4758 O  O   . PHE   B 277 ? 0.6389 0.5573 0.3689 -0.0417 0.0181  0.0187  433 PHE   B O   
4759 C  CB  . PHE   B 277 ? 0.5890 0.5101 0.3457 -0.0417 0.0254  0.0286  433 PHE   B CB  
4760 C  CG  . PHE   B 277 ? 0.5769 0.4993 0.3398 -0.0456 0.0272  0.0365  433 PHE   B CG  
4761 C  CD1 . PHE   B 277 ? 0.5221 0.4364 0.2955 -0.0459 0.0230  0.0405  433 PHE   B CD1 
4762 C  CD2 . PHE   B 277 ? 0.5701 0.5014 0.3274 -0.0495 0.0334  0.0399  433 PHE   B CD2 
4763 C  CE1 . PHE   B 277 ? 0.6209 0.5349 0.3993 -0.0506 0.0251  0.0470  433 PHE   B CE1 
4764 C  CE2 . PHE   B 277 ? 0.5499 0.4822 0.3128 -0.0542 0.0352  0.0471  433 PHE   B CE2 
4765 C  CZ  . PHE   B 277 ? 0.5631 0.4861 0.3363 -0.0551 0.0310  0.0505  433 PHE   B CZ  
4766 N  N   . SER   B 278 ? 0.6279 0.5347 0.3809 -0.0367 0.0102  0.0216  434 SER   B N   
4767 C  CA  . SER   B 278 ? 0.7009 0.6049 0.4508 -0.0347 0.0072  0.0138  434 SER   B CA  
4768 C  C   . SER   B 278 ? 0.6173 0.5158 0.3822 -0.0297 0.0067  0.0088  434 SER   B C   
4769 O  O   . SER   B 278 ? 0.5525 0.4491 0.3295 -0.0283 0.0068  0.0123  434 SER   B O   
4770 C  CB  . SER   B 278 ? 0.6059 0.5083 0.3494 -0.0368 -0.0014 0.0188  434 SER   B CB  
4771 O  OG  . SER   B 278 ? 0.6206 0.5166 0.3769 -0.0343 -0.0069 0.0238  434 SER   B OG  
4772 N  N   . SER   B 279 ? 0.5938 0.4895 0.3571 -0.0277 0.0060  0.0005  435 SER   B N   
4773 C  CA  . SER   B 279 ? 0.6530 0.5435 0.4299 -0.0231 0.0051  -0.0037 435 SER   B CA  
4774 C  C   . SER   B 279 ? 0.6257 0.5115 0.4118 -0.0225 -0.0022 0.0024  435 SER   B C   
4775 O  O   . SER   B 279 ? 0.5331 0.4159 0.3318 -0.0193 -0.0023 0.0010  435 SER   B O   
4776 C  CB  . SER   B 279 ? 0.5634 0.4503 0.3364 -0.0219 0.0053  -0.0130 435 SER   B CB  
4777 O  OG  . SER   B 279 ? 0.6115 0.4967 0.3781 -0.0249 -0.0025 -0.0114 435 SER   B OG  
4778 N  N   . TYR   B 280 ? 0.5518 0.4375 0.3320 -0.0254 -0.0079 0.0094  436 TYR   B N   
4779 C  CA  . TYR   B 280 ? 0.6593 0.5401 0.4489 -0.0243 -0.0136 0.0159  436 TYR   B CA  
4780 C  C   . TYR   B 280 ? 0.5160 0.3945 0.3154 -0.0240 -0.0105 0.0201  436 TYR   B C   
4781 O  O   . TYR   B 280 ? 0.5076 0.3807 0.3178 -0.0221 -0.0128 0.0215  436 TYR   B O   
4782 C  CB  . TYR   B 280 ? 0.5347 0.4170 0.3169 -0.0268 -0.0195 0.0243  436 TYR   B CB  
4783 C  CG  . TYR   B 280 ? 0.6021 0.4791 0.3949 -0.0243 -0.0253 0.0300  436 TYR   B CG  
4784 C  CD1 . TYR   B 280 ? 0.6970 0.5728 0.4946 -0.0221 -0.0299 0.0259  436 TYR   B CD1 
4785 C  CD2 . TYR   B 280 ? 0.5673 0.4398 0.3659 -0.0241 -0.0254 0.0391  436 TYR   B CD2 
4786 C  CE1 . TYR   B 280 ? 0.6525 0.5243 0.4606 -0.0194 -0.0345 0.0310  436 TYR   B CE1 
4787 C  CE2 . TYR   B 280 ? 0.5143 0.3812 0.3233 -0.0212 -0.0295 0.0439  436 TYR   B CE2 
4788 C  CZ  . TYR   B 280 ? 0.6593 0.5266 0.4732 -0.0186 -0.0340 0.0400  436 TYR   B CZ  
4789 O  OH  . TYR   B 280 ? 0.6541 0.5167 0.4790 -0.0152 -0.0374 0.0446  436 TYR   B OH  
4790 N  N   . HIS   B 281 ? 0.4782 0.3610 0.2734 -0.0266 -0.0052 0.0223  437 HIS   B N   
4791 C  CA  . HIS   B 281 ? 0.4903 0.3719 0.2942 -0.0277 -0.0019 0.0254  437 HIS   B CA  
4792 C  C   . HIS   B 281 ? 0.4916 0.3745 0.3063 -0.0249 0.0007  0.0188  437 HIS   B C   
4793 O  O   . HIS   B 281 ? 0.4973 0.3766 0.3219 -0.0249 -0.0001 0.0198  437 HIS   B O   
4794 C  CB  . HIS   B 281 ? 0.4837 0.3714 0.2808 -0.0318 0.0033  0.0290  437 HIS   B CB  
4795 C  CG  . HIS   B 281 ? 0.5479 0.4349 0.3348 -0.0350 0.0010  0.0372  437 HIS   B CG  
4796 N  ND1 . HIS   B 281 ? 0.6420 0.5362 0.4158 -0.0375 0.0034  0.0379  437 HIS   B ND1 
4797 C  CD2 . HIS   B 281 ? 0.4934 0.3738 0.2815 -0.0359 -0.0031 0.0458  437 HIS   B CD2 
4798 C  CE1 . HIS   B 281 ? 0.5744 0.4674 0.3413 -0.0402 0.0003  0.0470  437 HIS   B CE1 
4799 N  NE2 . HIS   B 281 ? 0.5180 0.4023 0.2940 -0.0389 -0.0037 0.0523  437 HIS   B NE2 
4800 N  N   . VAL   B 282 ? 0.4875 0.3760 0.3003 -0.0227 0.0045  0.0124  438 VAL   B N   
4801 C  CA  . VAL   B 282 ? 0.4944 0.3852 0.3178 -0.0191 0.0071  0.0073  438 VAL   B CA  
4802 C  C   . VAL   B 282 ? 0.4991 0.3831 0.3301 -0.0166 0.0019  0.0055  438 VAL   B C   
4803 O  O   . VAL   B 282 ? 0.4800 0.3644 0.3216 -0.0156 0.0021  0.0050  438 VAL   B O   
4804 C  CB  . VAL   B 282 ? 0.5252 0.4205 0.3445 -0.0161 0.0121  0.0009  438 VAL   B CB  
4805 C  CG1 . VAL   B 282 ? 0.6162 0.5112 0.4459 -0.0114 0.0133  -0.0039 438 VAL   B CG1 
4806 C  CG2 . VAL   B 282 ? 0.6489 0.5532 0.4654 -0.0178 0.0189  0.0025  438 VAL   B CG2 
4807 N  N   . LYS   B 283 ? 0.4863 0.3652 0.3119 -0.0160 -0.0029 0.0047  439 LYS   B N   
4808 C  CA  . LYS   B 283 ? 0.4760 0.3495 0.3086 -0.0134 -0.0075 0.0026  439 LYS   B CA  
4809 C  C   . LYS   B 283 ? 0.4742 0.3432 0.3138 -0.0145 -0.0107 0.0080  439 LYS   B C   
4810 O  O   . LYS   B 283 ? 0.4321 0.2987 0.2813 -0.0128 -0.0116 0.0064  439 LYS   B O   
4811 C  CB  . LYS   B 283 ? 0.4929 0.3644 0.3173 -0.0134 -0.0116 0.0003  439 LYS   B CB  
4812 C  CG  . LYS   B 283 ? 0.5829 0.4502 0.4141 -0.0111 -0.0162 -0.0023 439 LYS   B CG  
4813 C  CD  . LYS   B 283 ? 0.6164 0.4834 0.4389 -0.0123 -0.0191 -0.0064 439 LYS   B CD  
4814 C  CE  . LYS   B 283 ? 0.7105 0.5796 0.5243 -0.0155 -0.0242 -0.0005 439 LYS   B CE  
4815 N  NZ  . LYS   B 283 ? 0.8344 0.7050 0.6400 -0.0178 -0.0276 -0.0051 439 LYS   B NZ  
4816 N  N   . THR   B 284 ? 0.4349 0.3022 0.2698 -0.0174 -0.0114 0.0145  440 THR   B N   
4817 C  CA  . THR   B 284 ? 0.4571 0.3181 0.2986 -0.0185 -0.0126 0.0195  440 THR   B CA  
4818 C  C   . THR   B 284 ? 0.4473 0.3095 0.2963 -0.0203 -0.0084 0.0177  440 THR   B C   
4819 O  O   . THR   B 284 ? 0.4147 0.2723 0.2718 -0.0201 -0.0091 0.0169  440 THR   B O   
4820 C  CB  . THR   B 284 ? 0.4439 0.3025 0.2787 -0.0212 -0.0132 0.0276  440 THR   B CB  
4821 O  OG1 . THR   B 284 ? 0.5125 0.3724 0.3403 -0.0199 -0.0179 0.0297  440 THR   B OG1 
4822 C  CG2 . THR   B 284 ? 0.4564 0.3059 0.2985 -0.0218 -0.0134 0.0325  440 THR   B CG2 
4823 N  N   . ALA   B 285 ? 0.4378 0.3072 0.2840 -0.0227 -0.0038 0.0172  441 ALA   B N   
4824 C  CA  . ALA   B 285 ? 0.4895 0.3633 0.3428 -0.0253 -0.0002 0.0159  441 ALA   B CA  
4825 C  C   . ALA   B 285 ? 0.4685 0.3450 0.3302 -0.0220 -0.0010 0.0107  441 ALA   B C   
4826 O  O   . ALA   B 285 ? 0.4506 0.3268 0.3193 -0.0239 -0.0008 0.0100  441 ALA   B O   
4827 C  CB  . ALA   B 285 ? 0.5030 0.3870 0.3530 -0.0278 0.0048  0.0166  441 ALA   B CB  
4828 N  N   . PHE   B 286 ? 0.4506 0.3292 0.3111 -0.0173 -0.0018 0.0071  442 PHE   B N   
4829 C  CA  . PHE   B 286 ? 0.4254 0.3063 0.2939 -0.0138 -0.0023 0.0030  442 PHE   B CA  
4830 C  C   . PHE   B 286 ? 0.4467 0.3202 0.3204 -0.0134 -0.0063 0.0027  442 PHE   B C   
4831 O  O   . PHE   B 286 ? 0.4423 0.3182 0.3236 -0.0138 -0.0060 0.0014  442 PHE   B O   
4832 C  CB  . PHE   B 286 ? 0.4258 0.3076 0.2911 -0.0093 -0.0017 -0.0010 442 PHE   B CB  
4833 C  CG  . PHE   B 286 ? 0.4131 0.2949 0.2864 -0.0055 -0.0024 -0.0045 442 PHE   B CG  
4834 C  CD1 . PHE   B 286 ? 0.4304 0.3208 0.3117 -0.0038 0.0012  -0.0048 442 PHE   B CD1 
4835 C  CD2 . PHE   B 286 ? 0.4417 0.3164 0.3152 -0.0036 -0.0067 -0.0066 442 PHE   B CD2 
4836 C  CE1 . PHE   B 286 ? 0.4058 0.2963 0.2946 -0.0001 0.0006  -0.0068 442 PHE   B CE1 
4837 C  CE2 . PHE   B 286 ? 0.5412 0.4156 0.4220 -0.0005 -0.0071 -0.0093 442 PHE   B CE2 
4838 C  CZ  . PHE   B 286 ? 0.4654 0.3473 0.3538 0.0014  -0.0034 -0.0093 442 PHE   B CZ  
4839 N  N   . PHE   B 287 ? 0.4034 0.2690 0.2734 -0.0128 -0.0101 0.0044  443 PHE   B N   
4840 C  CA  . PHE   B 287 ? 0.3957 0.2547 0.2715 -0.0118 -0.0134 0.0046  443 PHE   B CA  
4841 C  C   . PHE   B 287 ? 0.4285 0.2845 0.3088 -0.0155 -0.0112 0.0061  443 PHE   B C   
4842 O  O   . PHE   B 287 ? 0.3803 0.2343 0.2672 -0.0153 -0.0117 0.0040  443 PHE   B O   
4843 C  CB  . PHE   B 287 ? 0.4253 0.2785 0.2970 -0.0105 -0.0175 0.0079  443 PHE   B CB  
4844 C  CG  . PHE   B 287 ? 0.5076 0.3628 0.3758 -0.0078 -0.0205 0.0050  443 PHE   B CG  
4845 C  CD1 . PHE   B 287 ? 0.4734 0.3299 0.3468 -0.0053 -0.0209 0.0000  443 PHE   B CD1 
4846 C  CD2 . PHE   B 287 ? 0.6000 0.4559 0.4592 -0.0085 -0.0228 0.0073  443 PHE   B CD2 
4847 C  CE1 . PHE   B 287 ? 0.5541 0.4111 0.4241 -0.0039 -0.0231 -0.0033 443 PHE   B CE1 
4848 C  CE2 . PHE   B 287 ? 0.5066 0.3644 0.3615 -0.0075 -0.0254 0.0037  443 PHE   B CE2 
4849 C  CZ  . PHE   B 287 ? 0.5376 0.3951 0.3980 -0.0054 -0.0254 -0.0019 443 PHE   B CZ  
4850 N  N   . HIS   B 288 ? 0.3866 0.2422 0.2630 -0.0197 -0.0085 0.0094  444 HIS   B N   
4851 C  CA  . HIS   B 288 ? 0.4842 0.3367 0.3640 -0.0248 -0.0057 0.0097  444 HIS   B CA  
4852 C  C   . HIS   B 288 ? 0.4347 0.2971 0.3196 -0.0269 -0.0037 0.0057  444 HIS   B C   
4853 O  O   . HIS   B 288 ? 0.4023 0.2627 0.2916 -0.0300 -0.0028 0.0036  444 HIS   B O   
4854 C  CB  . HIS   B 288 ? 0.4457 0.2961 0.3201 -0.0295 -0.0028 0.0142  444 HIS   B CB  
4855 C  CG  . HIS   B 288 ? 0.5666 0.4065 0.4374 -0.0281 -0.0044 0.0197  444 HIS   B CG  
4856 N  ND1 . HIS   B 288 ? 0.5356 0.3644 0.4109 -0.0265 -0.0053 0.0211  444 HIS   B ND1 
4857 C  CD2 . HIS   B 288 ? 0.4667 0.3066 0.3302 -0.0278 -0.0051 0.0249  444 HIS   B CD2 
4858 C  CE1 . HIS   B 288 ? 0.5655 0.3883 0.4374 -0.0249 -0.0067 0.0277  444 HIS   B CE1 
4859 N  NE2 . HIS   B 288 ? 0.4700 0.2997 0.3342 -0.0260 -0.0069 0.0303  444 HIS   B NE2 
4860 N  N   . VAL   B 289 ? 0.4030 0.2765 0.2874 -0.0253 -0.0027 0.0049  445 VAL   B N   
4861 C  CA  . VAL   B 289 ? 0.4133 0.2983 0.3038 -0.0264 -0.0012 0.0028  445 VAL   B CA  
4862 C  C   . VAL   B 289 ? 0.4200 0.3036 0.3163 -0.0229 -0.0037 -0.0001 445 VAL   B C   
4863 O  O   . VAL   B 289 ? 0.4290 0.3183 0.3303 -0.0256 -0.0033 -0.0015 445 VAL   B O   
4864 C  CB  . VAL   B 289 ? 0.3980 0.2949 0.2883 -0.0239 0.0012  0.0035  445 VAL   B CB  
4865 C  CG1 . VAL   B 289 ? 0.4581 0.3686 0.3564 -0.0240 0.0024  0.0030  445 VAL   B CG1 
4866 C  CG2 . VAL   B 289 ? 0.4138 0.3136 0.2984 -0.0279 0.0042  0.0066  445 VAL   B CG2 
4867 N  N   . CYS   B 290 ? 0.3722 0.2492 0.2676 -0.0175 -0.0066 -0.0009 446 CYS   B N   
4868 C  CA  . CYS   B 290 ? 0.3956 0.2708 0.2966 -0.0145 -0.0089 -0.0034 446 CYS   B CA  
4869 C  C   . CYS   B 290 ? 0.4561 0.3244 0.3594 -0.0178 -0.0092 -0.0041 446 CYS   B C   
4870 O  O   . CYS   B 290 ? 0.4474 0.3186 0.3558 -0.0184 -0.0093 -0.0063 446 CYS   B O   
4871 C  CB  . CYS   B 290 ? 0.3602 0.2297 0.2595 -0.0094 -0.0120 -0.0042 446 CYS   B CB  
4872 S  SG  . CYS   B 290 ? 0.4321 0.3074 0.3295 -0.0052 -0.0106 -0.0057 446 CYS   B SG  
4873 N  N   . THR   B 291 ? 0.3725 0.2314 0.2722 -0.0198 -0.0088 -0.0021 447 THR   B N   
4874 C  CA  . THR   B 291 ? 0.4559 0.3064 0.3579 -0.0229 -0.0074 -0.0031 447 THR   B CA  
4875 C  C   . THR   B 291 ? 0.4678 0.3238 0.3706 -0.0301 -0.0041 -0.0054 447 THR   B C   
4876 O  O   . THR   B 291 ? 0.4631 0.3181 0.3692 -0.0323 -0.0032 -0.0087 447 THR   B O   
4877 C  CB  . THR   B 291 ? 0.5136 0.3525 0.4123 -0.0230 -0.0069 0.0007  447 THR   B CB  
4878 O  OG1 . THR   B 291 ? 0.4973 0.3332 0.3960 -0.0170 -0.0108 0.0031  447 THR   B OG1 
4879 C  CG2 . THR   B 291 ? 0.5187 0.3470 0.4203 -0.0263 -0.0038 -0.0006 447 THR   B CG2 
4880 N  N   . GLN   B 292 ? 0.4750 0.3381 0.3747 -0.0343 -0.0021 -0.0039 448 GLN   B N   
4881 C  CA  . GLN   B 292 ? 0.5005 0.3713 0.4010 -0.0423 0.0006  -0.0059 448 GLN   B CA  
4882 C  C   . GLN   B 292 ? 0.4278 0.3127 0.3332 -0.0418 -0.0007 -0.0077 448 GLN   B C   
4883 O  O   . GLN   B 292 ? 0.4309 0.3221 0.3373 -0.0486 0.0008  -0.0099 448 GLN   B O   
4884 C  CB  . GLN   B 292 ? 0.4979 0.3761 0.3951 -0.0472 0.0028  -0.0033 448 GLN   B CB  
4885 C  CG  . GLN   B 292 ? 0.7079 0.5749 0.6000 -0.0495 0.0047  -0.0004 448 GLN   B CG  
4886 C  CD  . GLN   B 292 ? 0.8211 0.6957 0.7110 -0.0583 0.0080  0.0006  448 GLN   B CD  
4887 O  OE1 . GLN   B 292 ? 0.7974 0.6861 0.6877 -0.0580 0.0082  0.0028  448 GLN   B OE1 
4888 N  NE2 . GLN   B 292 ? 0.7658 0.6316 0.6541 -0.0665 0.0111  -0.0013 448 GLN   B NE2 
4889 N  N   . ASN   B 293 ? 0.4304 0.3204 0.3386 -0.0344 -0.0030 -0.0065 449 ASN   B N   
4890 C  CA  . ASN   B 293 ? 0.4356 0.3394 0.3493 -0.0327 -0.0039 -0.0064 449 ASN   B CA  
4891 C  C   . ASN   B 293 ? 0.3930 0.2914 0.3098 -0.0261 -0.0065 -0.0076 449 ASN   B C   
4892 O  O   . ASN   B 293 ? 0.4183 0.3190 0.3369 -0.0198 -0.0075 -0.0063 449 ASN   B O   
4893 C  CB  . ASN   B 293 ? 0.4008 0.3173 0.3159 -0.0303 -0.0029 -0.0030 449 ASN   B CB  
4894 C  CG  . ASN   B 293 ? 0.5738 0.4977 0.4865 -0.0374 -0.0004 -0.0014 449 ASN   B CG  
4895 O  OD1 . ASN   B 293 ? 0.5165 0.4526 0.4316 -0.0437 0.0003  -0.0011 449 ASN   B OD1 
4896 N  ND2 . ASN   B 293 ? 0.5535 0.4702 0.4610 -0.0374 0.0008  -0.0003 449 ASN   B ND2 
4897 N  N   . PRO   B 294 ? 0.4327 0.3236 0.3504 -0.0275 -0.0069 -0.0104 450 PRO   B N   
4898 C  CA  . PRO   B 294 ? 0.4413 0.3256 0.3618 -0.0214 -0.0093 -0.0113 450 PRO   B CA  
4899 C  C   . PRO   B 294 ? 0.4759 0.3699 0.4018 -0.0186 -0.0105 -0.0108 450 PRO   B C   
4900 O  O   . PRO   B 294 ? 0.4380 0.3278 0.3664 -0.0133 -0.0125 -0.0110 450 PRO   B O   
4901 C  CB  . PRO   B 294 ? 0.4642 0.3379 0.3844 -0.0242 -0.0083 -0.0141 450 PRO   B CB  
4902 C  CG  . PRO   B 294 ? 0.4832 0.3616 0.4014 -0.0327 -0.0053 -0.0160 450 PRO   B CG  
4903 C  CD  . PRO   B 294 ? 0.4417 0.3277 0.3571 -0.0350 -0.0046 -0.0132 450 PRO   B CD  
4904 N  N   . GLN   B 295 ? 0.3900 0.2975 0.3181 -0.0223 -0.0095 -0.0098 451 GLN   B N   
4905 C  CA  . GLN   B 295 ? 0.3630 0.2801 0.2967 -0.0199 -0.0105 -0.0082 451 GLN   B CA  
4906 C  C   . GLN   B 295 ? 0.3438 0.2667 0.2811 -0.0135 -0.0105 -0.0045 451 GLN   B C   
4907 O  O   . GLN   B 295 ? 0.3512 0.2796 0.2876 -0.0134 -0.0090 -0.0024 451 GLN   B O   
4908 C  CB  . GLN   B 295 ? 0.4205 0.3517 0.3549 -0.0271 -0.0096 -0.0078 451 GLN   B CB  
4909 C  CG  . GLN   B 295 ? 0.3575 0.2820 0.2880 -0.0341 -0.0085 -0.0128 451 GLN   B CG  
4910 C  CD  . GLN   B 295 ? 0.4281 0.3444 0.3606 -0.0309 -0.0092 -0.0152 451 GLN   B CD  
4911 O  OE1 . GLN   B 295 ? 0.5094 0.4298 0.4466 -0.0256 -0.0109 -0.0127 451 GLN   B OE1 
4912 N  NE2 . GLN   B 295 ? 0.4887 0.3937 0.4182 -0.0341 -0.0073 -0.0198 451 GLN   B NE2 
4913 N  N   . ASP   B 296 ? 0.3438 0.2651 0.2855 -0.0082 -0.0116 -0.0037 452 ASP   B N   
4914 C  CA  . ASP   B 296 ? 0.3601 0.2843 0.3055 -0.0018 -0.0105 -0.0007 452 ASP   B CA  
4915 C  C   . ASP   B 296 ? 0.4496 0.3908 0.3996 -0.0021 -0.0085 0.0044  452 ASP   B C   
4916 O  O   . ASP   B 296 ? 0.3904 0.3347 0.3423 0.0022  -0.0061 0.0068  452 ASP   B O   
4917 C  CB  . ASP   B 296 ? 0.3772 0.2968 0.3270 0.0027  -0.0115 -0.0006 452 ASP   B CB  
4918 C  CG  . ASP   B 296 ? 0.4368 0.3414 0.3830 0.0035  -0.0137 -0.0049 452 ASP   B CG  
4919 O  OD1 . ASP   B 296 ? 0.3731 0.2710 0.3136 0.0022  -0.0140 -0.0071 452 ASP   B OD1 
4920 O  OD2 . ASP   B 296 ? 0.4063 0.3074 0.3558 0.0049  -0.0150 -0.0055 452 ASP   B OD2 
4921 N  N   . SER   B 297 ? 0.3871 0.3406 0.3392 -0.0073 -0.0094 0.0062  453 SER   B N   
4922 C  CA  . SER   B 297 ? 0.3698 0.3430 0.3270 -0.0086 -0.0083 0.0122  453 SER   B CA  
4923 C  C   . SER   B 297 ? 0.4244 0.4028 0.3793 -0.0109 -0.0064 0.0128  453 SER   B C   
4924 O  O   . SER   B 297 ? 0.4084 0.4026 0.3692 -0.0092 -0.0048 0.0186  453 SER   B O   
4925 C  CB  . SER   B 297 ? 0.4552 0.4409 0.4126 -0.0161 -0.0101 0.0129  453 SER   B CB  
4926 O  OG  . SER   B 297 ? 0.4086 0.3904 0.3585 -0.0251 -0.0103 0.0074  453 SER   B OG  
4927 N  N   . GLN   B 298 ? 0.3753 0.3415 0.3225 -0.0146 -0.0064 0.0078  454 GLN   B N   
4928 C  CA  . GLN   B 298 ? 0.3881 0.3590 0.3327 -0.0174 -0.0044 0.0087  454 GLN   B CA  
4929 C  C   . GLN   B 298 ? 0.3754 0.3417 0.3206 -0.0098 -0.0019 0.0098  454 GLN   B C   
4930 O  O   . GLN   B 298 ? 0.3913 0.3609 0.3342 -0.0113 0.0003  0.0105  454 GLN   B O   
4931 C  CB  . GLN   B 298 ? 0.3889 0.3481 0.3251 -0.0244 -0.0047 0.0038  454 GLN   B CB  
4932 C  CG  . GLN   B 298 ? 0.3968 0.3566 0.3309 -0.0325 -0.0059 0.0008  454 GLN   B CG  
4933 C  CD  . GLN   B 298 ? 0.4814 0.4265 0.4081 -0.0382 -0.0049 -0.0038 454 GLN   B CD  
4934 O  OE1 . GLN   B 298 ? 0.4797 0.4085 0.4038 -0.0356 -0.0055 -0.0069 454 GLN   B OE1 
4935 N  NE2 . GLN   B 298 ? 0.5682 0.5196 0.4920 -0.0464 -0.0033 -0.0038 454 GLN   B NE2 
4936 N  N   . TRP   B 299 ? 0.3824 0.3407 0.3301 -0.0023 -0.0018 0.0094  455 TRP   B N   
4937 C  CA  . TRP   B 299 ? 0.3883 0.3391 0.3351 0.0045  0.0010  0.0086  455 TRP   B CA  
4938 C  C   . TRP   B 299 ? 0.4564 0.4125 0.4121 0.0121  0.0035  0.0125  455 TRP   B C   
4939 O  O   . TRP   B 299 ? 0.4328 0.3783 0.3878 0.0180  0.0058  0.0104  455 TRP   B O   
4940 C  CB  . TRP   B 299 ? 0.3925 0.3241 0.3318 0.0052  -0.0009 0.0031  455 TRP   B CB  
4941 C  CG  . TRP   B 299 ? 0.3798 0.3048 0.3111 -0.0007 -0.0026 0.0005  455 TRP   B CG  
4942 C  CD1 . TRP   B 299 ? 0.3844 0.3046 0.3136 -0.0057 -0.0054 -0.0013 455 TRP   B CD1 
4943 C  CD2 . TRP   B 299 ? 0.3767 0.2988 0.3014 -0.0020 -0.0009 -0.0001 455 TRP   B CD2 
4944 N  NE1 . TRP   B 299 ? 0.3813 0.2947 0.3037 -0.0096 -0.0054 -0.0026 455 TRP   B NE1 
4945 C  CE2 . TRP   B 299 ? 0.3834 0.2984 0.3026 -0.0077 -0.0030 -0.0015 455 TRP   B CE2 
4946 C  CE3 . TRP   B 299 ? 0.3922 0.3169 0.3151 0.0013  0.0028  0.0006  455 TRP   B CE3 
4947 C  CZ2 . TRP   B 299 ? 0.3894 0.3000 0.3015 -0.0103 -0.0021 -0.0014 455 TRP   B CZ2 
4948 C  CZ3 . TRP   B 299 ? 0.3897 0.3111 0.3048 -0.0019 0.0037  0.0001  455 TRP   B CZ3 
4949 C  CH2 . TRP   B 299 ? 0.4124 0.3269 0.3223 -0.0077 0.0010  -0.0004 455 TRP   B CH2 
4950 N  N   . ASP   B 300 ? 0.3813 0.3538 0.3453 0.0118  0.0033  0.0185  456 ASP   B N   
4951 C  CA  . ASP   B 300 ? 0.3850 0.3626 0.3588 0.0195  0.0058  0.0237  456 ASP   B CA  
4952 C  C   . ASP   B 300 ? 0.4051 0.3820 0.3816 0.0265  0.0117  0.0249  456 ASP   B C   
4953 O  O   . ASP   B 300 ? 0.4035 0.3887 0.3789 0.0249  0.0138  0.0259  456 ASP   B O   
4954 C  CB  . ASP   B 300 ? 0.4590 0.4588 0.4415 0.0175  0.0046  0.0316  456 ASP   B CB  
4955 C  CG  . ASP   B 300 ? 0.5581 0.5617 0.5507 0.0250  0.0062  0.0380  456 ASP   B CG  
4956 O  OD1 . ASP   B 300 ? 0.5026 0.4965 0.4989 0.0333  0.0106  0.0382  456 ASP   B OD1 
4957 O  OD2 . ASP   B 300 ? 0.6657 0.6833 0.6629 0.0221  0.0034  0.0433  456 ASP   B OD2 
4958 N  N   . ARG   B 301 ? 0.4704 0.4368 0.4504 0.0341  0.0150  0.0245  457 ARG   B N   
4959 C  CA  . ARG   B 301 ? 0.5330 0.4942 0.5135 0.0406  0.0217  0.0233  457 ARG   B CA  
4960 C  C   . ARG   B 301 ? 0.5000 0.4809 0.4910 0.0448  0.0264  0.0315  457 ARG   B C   
4961 O  O   . ARG   B 301 ? 0.4964 0.4776 0.4862 0.0476  0.0317  0.0303  457 ARG   B O   
4962 C  CB  . ARG   B 301 ? 0.6171 0.5618 0.5993 0.0471  0.0250  0.0206  457 ARG   B CB  
4963 C  CG  . ARG   B 301 ? 0.6503 0.5874 0.6321 0.0535  0.0331  0.0180  457 ARG   B CG  
4964 C  CD  . ARG   B 301 ? 0.7875 0.7081 0.7718 0.0593  0.0371  0.0155  457 ARG   B CD  
4965 N  NE  . ARG   B 301 ? 0.8017 0.7318 0.8011 0.0668  0.0412  0.0249  457 ARG   B NE  
4966 C  CZ  . ARG   B 301 ? 0.7566 0.6875 0.7643 0.0755  0.0501  0.0283  457 ARG   B CZ  
4967 N  NH1 . ARG   B 301 ? 0.8316 0.7527 0.8331 0.0775  0.0566  0.0215  457 ARG   B NH1 
4968 N  NH2 . ARG   B 301 ? 0.8543 0.7967 0.8772 0.0824  0.0530  0.0389  457 ARG   B NH2 
4969 N  N   . LYS   B 302 ? 0.4641 0.4632 0.4654 0.0449  0.0245  0.0401  458 LYS   B N   
4970 C  CA  . LYS   B 302 ? 0.4880 0.5099 0.5002 0.0481  0.0280  0.0491  458 LYS   B CA  
4971 C  C   . LYS   B 302 ? 0.5427 0.5755 0.5495 0.0408  0.0269  0.0478  458 LYS   B C   
4972 O  O   . LYS   B 302 ? 0.5627 0.6117 0.5770 0.0437  0.0312  0.0534  458 LYS   B O   
4973 C  CB  . LYS   B 302 ? 0.5574 0.5994 0.5802 0.0476  0.0247  0.0591  458 LYS   B CB  
4974 C  CG  . LYS   B 302 ? 0.5609 0.6041 0.5758 0.0368  0.0167  0.0559  458 LYS   B CG  
4975 C  CD  . LYS   B 302 ? 0.6623 0.7324 0.6839 0.0316  0.0129  0.0646  458 LYS   B CD  
4976 C  CE  . LYS   B 302 ? 0.7231 0.7901 0.7359 0.0215  0.0063  0.0597  458 LYS   B CE  
4977 N  NZ  . LYS   B 302 ? 0.5011 0.5691 0.5033 0.0100  0.0032  0.0532  458 LYS   B NZ  
4978 N  N   . ASP   B 303 ? 0.4510 0.4763 0.4461 0.0313  0.0215  0.0412  459 ASP   B N   
4979 C  CA  . ASP   B 303 ? 0.4119 0.4454 0.4012 0.0231  0.0203  0.0398  459 ASP   B CA  
4980 C  C   . ASP   B 303 ? 0.4669 0.4850 0.4463 0.0235  0.0235  0.0330  459 ASP   B C   
4981 O  O   . ASP   B 303 ? 0.4061 0.4253 0.3780 0.0158  0.0219  0.0306  459 ASP   B O   
4982 C  CB  . ASP   B 303 ? 0.3867 0.4204 0.3693 0.0122  0.0136  0.0370  459 ASP   B CB  
4983 C  CG  . ASP   B 303 ? 0.5752 0.6288 0.5663 0.0097  0.0105  0.0440  459 ASP   B CG  
4984 O  OD1 . ASP   B 303 ? 0.4041 0.4790 0.4058 0.0126  0.0128  0.0524  459 ASP   B OD1 
4985 O  OD2 . ASP   B 303 ? 0.4642 0.5136 0.4516 0.0047  0.0060  0.0416  459 ASP   B OD2 
4986 N  N   . LEU   B 304 ? 0.4090 0.4127 0.3876 0.0316  0.0280  0.0298  460 LEU   B N   
4987 C  CA  . LEU   B 304 ? 0.4208 0.4112 0.3893 0.0321  0.0314  0.0235  460 LEU   B CA  
4988 C  C   . LEU   B 304 ? 0.4289 0.4326 0.3962 0.0283  0.0339  0.0257  460 LEU   B C   
4989 O  O   . LEU   B 304 ? 0.4046 0.4009 0.3608 0.0222  0.0323  0.0213  460 LEU   B O   
4990 C  CB  . LEU   B 304 ? 0.4464 0.4260 0.4171 0.0418  0.0383  0.0213  460 LEU   B CB  
4991 C  CG  . LEU   B 304 ? 0.4133 0.3821 0.3732 0.0420  0.0429  0.0148  460 LEU   B CG  
4992 C  CD1 . LEU   B 304 ? 0.4583 0.4113 0.4033 0.0348  0.0371  0.0076  460 LEU   B CD1 
4993 C  CD2 . LEU   B 304 ? 0.4338 0.3926 0.3962 0.0511  0.0512  0.0120  460 LEU   B CD2 
4994 N  N   . GLY   B 305 ? 0.3988 0.4235 0.3783 0.0315  0.0377  0.0333  461 GLY   B N   
4995 C  CA  . GLY   B 305 ? 0.3999 0.4393 0.3796 0.0279  0.0405  0.0360  461 GLY   B CA  
4996 C  C   . GLY   B 305 ? 0.4240 0.4658 0.3956 0.0156  0.0345  0.0345  461 GLY   B C   
4997 O  O   . GLY   B 305 ? 0.4074 0.4440 0.3697 0.0109  0.0356  0.0313  461 GLY   B O   
4998 N  N   . LEU   B 306 ? 0.4050 0.4538 0.3796 0.0100  0.0287  0.0367  462 LEU   B N   
4999 C  CA  . LEU   B 306 ? 0.3943 0.4444 0.3617 -0.0021 0.0239  0.0348  462 LEU   B CA  
5000 C  C   . LEU   B 306 ? 0.4170 0.4420 0.3710 -0.0053 0.0210  0.0269  462 LEU   B C   
5001 O  O   . LEU   B 306 ? 0.3801 0.4004 0.3259 -0.0129 0.0201  0.0247  462 LEU   B O   
5002 C  CB  . LEU   B 306 ? 0.3646 0.4286 0.3381 -0.0074 0.0191  0.0385  462 LEU   B CB  
5003 C  CG  . LEU   B 306 ? 0.4994 0.5929 0.4864 -0.0066 0.0206  0.0478  462 LEU   B CG  
5004 C  CD1 . LEU   B 306 ? 0.5108 0.6192 0.5001 -0.0157 0.0150  0.0504  462 LEU   B CD1 
5005 C  CD2 . LEU   B 306 ? 0.4911 0.5985 0.4798 -0.0094 0.0247  0.0506  462 LEU   B CD2 
5006 N  N   . CYS   B 307 ? 0.3968 0.4061 0.3490 0.0005  0.0197  0.0234  463 CYS   B N   
5007 C  CA  . CYS   B 307 ? 0.4108 0.3985 0.3516 -0.0019 0.0166  0.0170  463 CYS   B CA  
5008 C  C   . CYS   B 307 ? 0.4121 0.3912 0.3440 -0.0015 0.0197  0.0144  463 CYS   B C   
5009 O  O   . CYS   B 307 ? 0.4182 0.3888 0.3414 -0.0076 0.0176  0.0123  463 CYS   B O   
5010 C  CB  . CYS   B 307 ? 0.4109 0.3862 0.3528 0.0042  0.0148  0.0143  463 CYS   B CB  
5011 S  SG  . CYS   B 307 ? 0.4332 0.4150 0.3823 0.0021  0.0103  0.0166  463 CYS   B SG  
5012 N  N   . PHE   B 308 ? 0.4161 0.3979 0.3503 0.0056  0.0252  0.0149  464 PHE   B N   
5013 C  CA  . PHE   B 308 ? 0.4055 0.3813 0.3303 0.0053  0.0287  0.0125  464 PHE   B CA  
5014 C  C   . PHE   B 308 ? 0.4027 0.3897 0.3259 -0.0022 0.0295  0.0157  464 PHE   B C   
5015 O  O   . PHE   B 308 ? 0.3967 0.3754 0.3096 -0.0069 0.0289  0.0140  464 PHE   B O   
5016 C  CB  . PHE   B 308 ? 0.4717 0.4494 0.3995 0.0139  0.0359  0.0119  464 PHE   B CB  
5017 C  CG  . PHE   B 308 ? 0.4136 0.3858 0.3305 0.0132  0.0399  0.0088  464 PHE   B CG  
5018 C  CD1 . PHE   B 308 ? 0.4384 0.3941 0.3421 0.0102  0.0367  0.0038  464 PHE   B CD1 
5019 C  CD2 . PHE   B 308 ? 0.4118 0.3969 0.3319 0.0151  0.0469  0.0115  464 PHE   B CD2 
5020 C  CE1 . PHE   B 308 ? 0.4099 0.3620 0.3026 0.0088  0.0401  0.0015  464 PHE   B CE1 
5021 C  CE2 . PHE   B 308 ? 0.4700 0.4507 0.3792 0.0140  0.0510  0.0085  464 PHE   B CE2 
5022 C  CZ  . PHE   B 308 ? 0.4445 0.4087 0.3394 0.0106  0.0474  0.0035  464 PHE   B CZ  
5023 N  N   . ASP   B 309 ? 0.3707 0.3775 0.3041 -0.0038 0.0309  0.0211  465 ASP   B N   
5024 C  CA  . ASP   B 309 ? 0.3695 0.3880 0.3019 -0.0122 0.0317  0.0242  465 ASP   B CA  
5025 C  C   . ASP   B 309 ? 0.3630 0.3702 0.2871 -0.0217 0.0266  0.0218  465 ASP   B C   
5026 O  O   . ASP   B 309 ? 0.3688 0.3735 0.2859 -0.0280 0.0275  0.0221  465 ASP   B O   
5027 C  CB  . ASP   B 309 ? 0.3641 0.4077 0.3097 -0.0135 0.0327  0.0306  465 ASP   B CB  
5028 C  CG  . ASP   B 309 ? 0.3691 0.4267 0.3142 -0.0226 0.0343  0.0338  465 ASP   B CG  
5029 O  OD1 . ASP   B 309 ? 0.3550 0.4154 0.2978 -0.0209 0.0395  0.0347  465 ASP   B OD1 
5030 O  OD2 . ASP   B 309 ? 0.4005 0.4668 0.3475 -0.0320 0.0306  0.0354  465 ASP   B OD2 
5031 N  N   . ASN   B 310 ? 0.3795 0.3790 0.3043 -0.0226 0.0218  0.0197  466 ASN   B N   
5032 C  CA  . ASN   B 310 ? 0.3788 0.3669 0.2970 -0.0309 0.0178  0.0172  466 ASN   B CA  
5033 C  C   . ASN   B 310 ? 0.4004 0.3680 0.3078 -0.0295 0.0171  0.0141  466 ASN   B C   
5034 O  O   . ASN   B 310 ? 0.4039 0.3627 0.3049 -0.0361 0.0161  0.0139  466 ASN   B O   
5035 C  CB  . ASN   B 310 ? 0.3746 0.3615 0.2971 -0.0317 0.0137  0.0157  466 ASN   B CB  
5036 C  CG  . ASN   B 310 ? 0.3904 0.3998 0.3224 -0.0358 0.0136  0.0197  466 ASN   B CG  
5037 O  OD1 . ASN   B 310 ? 0.4205 0.4454 0.3551 -0.0408 0.0158  0.0231  466 ASN   B OD1 
5038 N  ND2 . ASN   B 310 ? 0.3713 0.3835 0.3082 -0.0341 0.0107  0.0195  466 ASN   B ND2 
5039 N  N   . CYS   B 311 ? 0.4054 0.3658 0.3109 -0.0212 0.0177  0.0121  467 CYS   B N   
5040 C  CA  . CYS   B 311 ? 0.4057 0.3500 0.3006 -0.0203 0.0167  0.0098  467 CYS   B CA  
5041 C  C   . CYS   B 311 ? 0.4147 0.3622 0.3031 -0.0233 0.0203  0.0120  467 CYS   B C   
5042 O  O   . CYS   B 311 ? 0.4186 0.3564 0.2989 -0.0277 0.0190  0.0128  467 CYS   B O   
5043 C  CB  . CYS   B 311 ? 0.4082 0.3452 0.3019 -0.0121 0.0166  0.0064  467 CYS   B CB  
5044 S  SG  . CYS   B 311 ? 0.4451 0.3743 0.3441 -0.0093 0.0116  0.0038  467 CYS   B SG  
5045 N  N   . VAL   B 312 ? 0.3802 0.3419 0.2728 -0.0210 0.0254  0.0138  468 VAL   B N   
5046 C  CA  . VAL   B 312 ? 0.3752 0.3426 0.2625 -0.0241 0.0297  0.0162  468 VAL   B CA  
5047 C  C   . VAL   B 312 ? 0.3791 0.3482 0.2651 -0.0341 0.0285  0.0194  468 VAL   B C   
5048 O  O   . VAL   B 312 ? 0.3828 0.3450 0.2601 -0.0384 0.0290  0.0209  468 VAL   B O   
5049 C  CB  . VAL   B 312 ? 0.3770 0.3616 0.2718 -0.0195 0.0360  0.0179  468 VAL   B CB  
5050 C  CG1 . VAL   B 312 ? 0.3790 0.3725 0.2698 -0.0242 0.0406  0.0211  468 VAL   B CG1 
5051 C  CG2 . VAL   B 312 ? 0.3869 0.3656 0.2804 -0.0097 0.0390  0.0138  468 VAL   B CG2 
5052 N  N   . THR   B 313 ? 0.3633 0.3417 0.2578 -0.0383 0.0271  0.0206  469 THR   B N   
5053 C  CA  . THR   B 313 ? 0.3597 0.3387 0.2532 -0.0490 0.0263  0.0224  469 THR   B CA  
5054 C  C   . THR   B 313 ? 0.3615 0.3195 0.2467 -0.0523 0.0232  0.0209  469 THR   B C   
5055 O  O   . THR   B 313 ? 0.3665 0.3194 0.2464 -0.0593 0.0245  0.0232  469 THR   B O   
5056 C  CB  . THR   B 313 ? 0.3649 0.3571 0.2679 -0.0530 0.0247  0.0227  469 THR   B CB  
5057 O  OG1 . THR   B 313 ? 0.3454 0.3602 0.2567 -0.0519 0.0282  0.0264  469 THR   B OG1 
5058 C  CG2 . THR   B 313 ? 0.3517 0.3385 0.2522 -0.0646 0.0231  0.0220  469 THR   B CG2 
5059 N  N   . TYR   B 314 ? 0.4014 0.3473 0.2863 -0.0476 0.0193  0.0177  470 TYR   B N   
5060 C  CA  . TYR   B 314 ? 0.4596 0.3864 0.3383 -0.0496 0.0167  0.0172  470 TYR   B CA  
5061 C  C   . TYR   B 314 ? 0.4422 0.3615 0.3117 -0.0484 0.0177  0.0199  470 TYR   B C   
5062 O  O   . TYR   B 314 ? 0.4250 0.3348 0.2896 -0.0536 0.0180  0.0228  470 TYR   B O   
5063 C  CB  . TYR   B 314 ? 0.4443 0.3614 0.3250 -0.0438 0.0126  0.0137  470 TYR   B CB  
5064 C  CG  . TYR   B 314 ? 0.4993 0.3986 0.3758 -0.0456 0.0104  0.0139  470 TYR   B CG  
5065 C  CD1 . TYR   B 314 ? 0.5982 0.4915 0.4768 -0.0524 0.0108  0.0130  470 TYR   B CD1 
5066 C  CD2 . TYR   B 314 ? 0.5320 0.4208 0.4023 -0.0410 0.0084  0.0153  470 TYR   B CD2 
5067 C  CE1 . TYR   B 314 ? 0.6334 0.5093 0.5092 -0.0532 0.0099  0.0137  470 TYR   B CE1 
5068 C  CE2 . TYR   B 314 ? 0.5316 0.4054 0.3996 -0.0419 0.0066  0.0171  470 TYR   B CE2 
5069 C  CZ  . TYR   B 314 ? 0.5551 0.4219 0.4265 -0.0474 0.0078  0.0164  470 TYR   B CZ  
5070 O  OH  . TYR   B 314 ? 0.6539 0.5051 0.5242 -0.0471 0.0070  0.0186  470 TYR   B OH  
5071 N  N   . PHE   B 315 ? 0.4142 0.3377 0.2809 -0.0418 0.0186  0.0192  471 PHE   B N   
5072 C  CA  . PHE   B 315 ? 0.4472 0.3657 0.3038 -0.0412 0.0196  0.0215  471 PHE   B CA  
5073 C  C   . PHE   B 315 ? 0.4513 0.3766 0.3052 -0.0480 0.0238  0.0260  471 PHE   B C   
5074 O  O   . PHE   B 315 ? 0.4204 0.3377 0.2668 -0.0515 0.0237  0.0299  471 PHE   B O   
5075 C  CB  . PHE   B 315 ? 0.4100 0.3326 0.2636 -0.0339 0.0209  0.0185  471 PHE   B CB  
5076 C  CG  . PHE   B 315 ? 0.4844 0.4023 0.3260 -0.0337 0.0214  0.0201  471 PHE   B CG  
5077 C  CD1 . PHE   B 315 ? 0.4379 0.3433 0.2731 -0.0327 0.0164  0.0208  471 PHE   B CD1 
5078 C  CD2 . PHE   B 315 ? 0.4316 0.3590 0.2682 -0.0344 0.0268  0.0211  471 PHE   B CD2 
5079 C  CE1 . PHE   B 315 ? 0.4397 0.3429 0.2633 -0.0331 0.0162  0.0229  471 PHE   B CE1 
5080 C  CE2 . PHE   B 315 ? 0.4701 0.3942 0.2941 -0.0348 0.0272  0.0224  471 PHE   B CE2 
5081 C  CZ  . PHE   B 315 ? 0.4580 0.3704 0.2753 -0.0345 0.0216  0.0234  471 PHE   B CZ  
5082 N  N   . LEU   B 316 ? 0.4206 0.3615 0.2816 -0.0505 0.0272  0.0261  472 LEU   B N   
5083 C  CA  . LEU   B 316 ? 0.4217 0.3706 0.2812 -0.0581 0.0313  0.0304  472 LEU   B CA  
5084 C  C   . LEU   B 316 ? 0.4534 0.3913 0.3116 -0.0669 0.0300  0.0327  472 LEU   B C   
5085 O  O   . LEU   B 316 ? 0.4367 0.3717 0.2892 -0.0727 0.0324  0.0371  472 LEU   B O   
5086 C  CB  . LEU   B 316 ? 0.4229 0.3929 0.2919 -0.0592 0.0348  0.0307  472 LEU   B CB  
5087 C  CG  . LEU   B 316 ? 0.4810 0.4625 0.3514 -0.0508 0.0388  0.0297  472 LEU   B CG  
5088 C  CD1 . LEU   B 316 ? 0.4257 0.4285 0.3088 -0.0504 0.0415  0.0309  472 LEU   B CD1 
5089 C  CD2 . LEU   B 316 ? 0.4612 0.4435 0.3221 -0.0525 0.0430  0.0324  472 LEU   B CD2 
5090 N  N   . GLN   B 317 ? 0.4351 0.3664 0.2984 -0.0685 0.0270  0.0298  473 GLN   B N   
5091 C  CA  . GLN   B 317 ? 0.4388 0.3574 0.3007 -0.0769 0.0270  0.0310  473 GLN   B CA  
5092 C  C   . GLN   B 317 ? 0.4668 0.3669 0.3209 -0.0749 0.0258  0.0345  473 GLN   B C   
5093 O  O   . GLN   B 317 ? 0.4719 0.3622 0.3228 -0.0816 0.0279  0.0383  473 GLN   B O   
5094 C  CB  . GLN   B 317 ? 0.4339 0.3482 0.3018 -0.0782 0.0245  0.0262  473 GLN   B CB  
5095 C  CG  . GLN   B 317 ? 0.4369 0.3386 0.3038 -0.0880 0.0261  0.0261  473 GLN   B CG  
5096 C  CD  . GLN   B 317 ? 0.5120 0.4121 0.3841 -0.0901 0.0244  0.0204  473 GLN   B CD  
5097 O  OE1 . GLN   B 317 ? 0.4807 0.3706 0.3535 -0.0834 0.0215  0.0180  473 GLN   B OE1 
5098 N  NE2 . GLN   B 317 ? 0.4903 0.4020 0.3658 -0.0997 0.0260  0.0183  473 GLN   B NE2 
5099 N  N   . CYS   B 318 ? 0.4554 0.3504 0.3069 -0.0660 0.0225  0.0335  474 CYS   B N   
5100 C  CA  . CYS   B 318 ? 0.4834 0.3645 0.3278 -0.0635 0.0206  0.0379  474 CYS   B CA  
5101 C  C   . CYS   B 318 ? 0.4865 0.3716 0.3229 -0.0664 0.0236  0.0438  474 CYS   B C   
5102 O  O   . CYS   B 318 ? 0.4997 0.3741 0.3317 -0.0697 0.0242  0.0499  474 CYS   B O   
5103 C  CB  . CYS   B 318 ? 0.4567 0.3358 0.3000 -0.0544 0.0162  0.0352  474 CYS   B CB  
5104 S  SG  . CYS   B 318 ? 0.4901 0.3616 0.3420 -0.0509 0.0125  0.0297  474 CYS   B SG  
5105 N  N   . LEU   B 319 ? 0.4750 0.3755 0.3098 -0.0650 0.0261  0.0426  475 LEU   B N   
5106 C  CA  . LEU   B 319 ? 0.4542 0.3604 0.2810 -0.0681 0.0296  0.0477  475 LEU   B CA  
5107 C  C   . LEU   B 319 ? 0.5323 0.4373 0.3603 -0.0779 0.0333  0.0524  475 LEU   B C   
5108 O  O   . LEU   B 319 ? 0.4782 0.3764 0.2993 -0.0815 0.0346  0.0592  475 LEU   B O   
5109 C  CB  . LEU   B 319 ? 0.4719 0.3956 0.2987 -0.0648 0.0330  0.0446  475 LEU   B CB  
5110 C  CG  . LEU   B 319 ? 0.5255 0.4496 0.3478 -0.0561 0.0311  0.0403  475 LEU   B CG  
5111 C  CD1 . LEU   B 319 ? 0.4669 0.4068 0.2926 -0.0522 0.0358  0.0359  475 LEU   B CD1 
5112 C  CD2 . LEU   B 319 ? 0.4723 0.3902 0.2817 -0.0557 0.0299  0.0444  475 LEU   B CD2 
5113 N  N   . ARG   B 320 ? 0.4817 0.3938 0.3181 -0.0831 0.0350  0.0493  476 ARG   B N   
5114 C  CA  . ARG   B 320 ? 0.4554 0.3680 0.2925 -0.0939 0.0390  0.0529  476 ARG   B CA  
5115 C  C   . ARG   B 320 ? 0.4567 0.3476 0.2921 -0.0983 0.0384  0.0559  476 ARG   B C   
5116 O  O   . ARG   B 320 ? 0.4891 0.3744 0.3209 -0.1055 0.0418  0.0616  476 ARG   B O   
5117 C  CB  . ARG   B 320 ? 0.4468 0.3742 0.2933 -0.0995 0.0405  0.0488  476 ARG   B CB  
5118 C  CG  . ARG   B 320 ? 0.4298 0.3805 0.2800 -0.0963 0.0428  0.0479  476 ARG   B CG  
5119 C  CD  . ARG   B 320 ? 0.4672 0.4346 0.3271 -0.1038 0.0442  0.0462  476 ARG   B CD  
5120 N  NE  . ARG   B 320 ? 0.4476 0.4353 0.3145 -0.0968 0.0449  0.0444  476 ARG   B NE  
5121 C  CZ  . ARG   B 320 ? 0.4418 0.4318 0.3148 -0.0903 0.0416  0.0402  476 ARG   B CZ  
5122 N  NH1 . ARG   B 320 ? 0.4170 0.3915 0.2896 -0.0902 0.0374  0.0367  476 ARG   B NH1 
5123 N  NH2 . ARG   B 320 ? 0.4624 0.4703 0.3424 -0.0833 0.0431  0.0398  476 ARG   B NH2 
5124 N  N   . THR   B 321 ? 0.4537 0.3319 0.2921 -0.0940 0.0348  0.0524  477 THR   B N   
5125 C  CA  . THR   B 321 ? 0.4836 0.3404 0.3218 -0.0971 0.0353  0.0550  477 THR   B CA  
5126 C  C   . THR   B 321 ? 0.5410 0.3856 0.3734 -0.0902 0.0329  0.0617  477 THR   B C   
5127 O  O   . THR   B 321 ? 0.5330 0.3593 0.3662 -0.0908 0.0334  0.0654  477 THR   B O   
5128 C  CB  . THR   B 321 ? 0.4566 0.3053 0.3015 -0.0962 0.0334  0.0481  477 THR   B CB  
5129 O  OG1 . THR   B 321 ? 0.4834 0.3340 0.3293 -0.0856 0.0285  0.0454  477 THR   B OG1 
5130 C  CG2 . THR   B 321 ? 0.4504 0.3124 0.3012 -0.1040 0.0351  0.0415  477 THR   B CG2 
5131 N  N   . GLU   B 322 ? 0.4869 0.3415 0.3141 -0.0834 0.0302  0.0631  478 GLU   B N   
5132 C  CA  . GLU   B 322 ? 0.5728 0.4201 0.3934 -0.0776 0.0272  0.0699  478 GLU   B CA  
5133 C  C   . GLU   B 322 ? 0.5874 0.4200 0.4124 -0.0718 0.0233  0.0697  478 GLU   B C   
5134 O  O   . GLU   B 322 ? 0.5807 0.4011 0.4040 -0.0702 0.0225  0.0776  478 GLU   B O   
5135 C  CB  . GLU   B 322 ? 0.5456 0.3872 0.3601 -0.0832 0.0306  0.0800  478 GLU   B CB  
5136 C  CG  . GLU   B 322 ? 0.5330 0.3897 0.3430 -0.0892 0.0349  0.0811  478 GLU   B CG  
5137 C  CD  . GLU   B 322 ? 0.6544 0.5062 0.4570 -0.0936 0.0376  0.0921  478 GLU   B CD  
5138 O  OE1 . GLU   B 322 ? 0.6352 0.4895 0.4295 -0.0891 0.0351  0.0977  478 GLU   B OE1 
5139 O  OE2 . GLU   B 322 ? 0.6768 0.5228 0.4815 -0.1023 0.0423  0.0953  478 GLU   B OE2 
5140 N  N   . LYS   B 323 ? 0.5194 0.3543 0.3507 -0.0683 0.0210  0.0614  479 LYS   B N   
5141 C  CA  . LYS   B 323 ? 0.5250 0.3478 0.3617 -0.0628 0.0178  0.0600  479 LYS   B CA  
5142 C  C   . LYS   B 323 ? 0.5510 0.3834 0.3894 -0.0560 0.0133  0.0532  479 LYS   B C   
5143 O  O   . LYS   B 323 ? 0.4586 0.3001 0.3010 -0.0571 0.0141  0.0459  479 LYS   B O   
5144 C  CB  . LYS   B 323 ? 0.5239 0.3351 0.3678 -0.0680 0.0213  0.0564  479 LYS   B CB  
5145 C  CG  . LYS   B 323 ? 0.6590 0.4562 0.5014 -0.0744 0.0262  0.0636  479 LYS   B CG  
5146 C  CD  . LYS   B 323 ? 0.8815 0.6648 0.7298 -0.0804 0.0306  0.0590  479 LYS   B CD  
5147 C  CE  . LYS   B 323 ? 0.8286 0.5963 0.6752 -0.0871 0.0364  0.0662  479 LYS   B CE  
5148 N  NZ  . LYS   B 323 ? 0.9411 0.6937 0.7922 -0.0947 0.0420  0.0605  479 LYS   B NZ  
5149 N  N   . LEU   B 324 ? 0.4796 0.3107 0.3152 -0.0494 0.0087  0.0561  480 LEU   B N   
5150 C  CA  . LEU   B 324 ? 0.4828 0.3198 0.3203 -0.0431 0.0043  0.0500  480 LEU   B CA  
5151 C  C   . LEU   B 324 ? 0.6159 0.4440 0.4550 -0.0377 -0.0002 0.0547  480 LEU   B C   
5152 O  O   . LEU   B 324 ? 0.5351 0.3661 0.3675 -0.0355 -0.0034 0.0603  480 LEU   B O   
5153 C  CB  . LEU   B 324 ? 0.5019 0.3525 0.3319 -0.0417 0.0037  0.0477  480 LEU   B CB  
5154 C  CG  . LEU   B 324 ? 0.4960 0.3516 0.3277 -0.0360 0.0001  0.0409  480 LEU   B CG  
5155 C  CD1 . LEU   B 324 ? 0.4614 0.3198 0.3019 -0.0361 0.0018  0.0338  480 LEU   B CD1 
5156 C  CD2 . LEU   B 324 ? 0.5273 0.3931 0.3498 -0.0348 0.0003  0.0392  480 LEU   B CD2 
5157 N  N   . GLU   B 325 ? 0.5900 0.4084 0.4379 -0.0360 -0.0003 0.0528  481 GLU   B N   
5158 C  CA  . GLU   B 325 ? 0.6439 0.4550 0.4957 -0.0302 -0.0041 0.0573  481 GLU   B CA  
5159 C  C   . GLU   B 325 ? 0.6070 0.4277 0.4570 -0.0251 -0.0100 0.0544  481 GLU   B C   
5160 O  O   . GLU   B 325 ? 0.5175 0.3454 0.3681 -0.0247 -0.0105 0.0461  481 GLU   B O   
5161 C  CB  . GLU   B 325 ? 0.6398 0.4397 0.5017 -0.0293 -0.0019 0.0538  481 GLU   B CB  
5162 C  CG  . GLU   B 325 ? 0.6351 0.4218 0.4995 -0.0346 0.0044  0.0561  481 GLU   B CG  
5163 C  CD  . GLU   B 325 ? 0.6959 0.4714 0.5693 -0.0335 0.0068  0.0513  481 GLU   B CD  
5164 O  OE1 . GLU   B 325 ? 0.5895 0.3709 0.4667 -0.0303 0.0040  0.0447  481 GLU   B OE1 
5165 O  OE2 . GLU   B 325 ? 0.9391 0.6996 0.8157 -0.0357 0.0120  0.0543  481 GLU   B OE2 
5166 N  N   . ASN   B 326 ? 0.5779 0.3985 0.4263 -0.0214 -0.0144 0.0616  482 ASN   B N   
5167 C  CA  . ASN   B 326 ? 0.5274 0.3551 0.3762 -0.0171 -0.0202 0.0585  482 ASN   B CA  
5168 C  C   . ASN   B 326 ? 0.5049 0.3276 0.3648 -0.0140 -0.0203 0.0526  482 ASN   B C   
5169 O  O   . ASN   B 326 ? 0.4545 0.2668 0.3224 -0.0127 -0.0180 0.0554  482 ASN   B O   
5170 C  CB  . ASN   B 326 ? 0.4960 0.3260 0.3422 -0.0143 -0.0253 0.0686  482 ASN   B CB  
5171 C  CG  . ASN   B 326 ? 0.5365 0.3756 0.3814 -0.0117 -0.0315 0.0653  482 ASN   B CG  
5172 O  OD1 . ASN   B 326 ? 0.5213 0.3584 0.3754 -0.0081 -0.0334 0.0623  482 ASN   B OD1 
5173 N  ND2 . ASN   B 326 ? 0.5515 0.4009 0.3848 -0.0140 -0.0345 0.0657  482 ASN   B ND2 
5174 N  N   . TYR   B 327 ? 0.4830 0.3128 0.3431 -0.0128 -0.0224 0.0445  483 TYR   B N   
5175 C  CA  . TYR   B 327 ? 0.4978 0.3247 0.3674 -0.0106 -0.0222 0.0381  483 TYR   B CA  
5176 C  C   . TYR   B 327 ? 0.5123 0.3351 0.3897 -0.0059 -0.0254 0.0424  483 TYR   B C   
5177 O  O   . TYR   B 327 ? 0.5129 0.3300 0.3992 -0.0042 -0.0237 0.0394  483 TYR   B O   
5178 C  CB  . TYR   B 327 ? 0.4312 0.2667 0.2990 -0.0102 -0.0237 0.0299  483 TYR   B CB  
5179 C  CG  . TYR   B 327 ? 0.4634 0.2977 0.3395 -0.0094 -0.0222 0.0231  483 TYR   B CG  
5180 C  CD1 . TYR   B 327 ? 0.4428 0.2757 0.3214 -0.0127 -0.0174 0.0199  483 TYR   B CD1 
5181 C  CD2 . TYR   B 327 ? 0.5088 0.3446 0.3901 -0.0059 -0.0257 0.0202  483 TYR   B CD2 
5182 C  CE1 . TYR   B 327 ? 0.4409 0.2745 0.3263 -0.0125 -0.0163 0.0142  483 TYR   B CE1 
5183 C  CE2 . TYR   B 327 ? 0.4625 0.2980 0.3512 -0.0053 -0.0242 0.0146  483 TYR   B CE2 
5184 C  CZ  . TYR   B 327 ? 0.5038 0.3385 0.3942 -0.0085 -0.0196 0.0118  483 TYR   B CZ  
5185 O  OH  . TYR   B 327 ? 0.4876 0.3235 0.3844 -0.0084 -0.0185 0.0069  483 TYR   B OH  
5186 N  N   . PHE   B 328 ? 0.4984 0.3253 0.3726 -0.0039 -0.0301 0.0497  484 PHE   B N   
5187 C  CA  . PHE   B 328 ? 0.4837 0.3100 0.3657 0.0009  -0.0339 0.0558  484 PHE   B CA  
5188 C  C   . PHE   B 328 ? 0.4780 0.2963 0.3636 0.0028  -0.0319 0.0668  484 PHE   B C   
5189 O  O   . PHE   B 328 ? 0.5143 0.3282 0.4102 0.0076  -0.0321 0.0715  484 PHE   B O   
5190 C  CB  . PHE   B 328 ? 0.4610 0.2996 0.3374 0.0013  -0.0410 0.0574  484 PHE   B CB  
5191 C  CG  . PHE   B 328 ? 0.4870 0.3313 0.3608 -0.0002 -0.0424 0.0467  484 PHE   B CG  
5192 C  CD1 . PHE   B 328 ? 0.4938 0.3414 0.3576 -0.0040 -0.0404 0.0408  484 PHE   B CD1 
5193 C  CD2 . PHE   B 328 ? 0.4685 0.3143 0.3507 0.0025  -0.0448 0.0428  484 PHE   B CD2 
5194 C  CE1 . PHE   B 328 ? 0.5060 0.3572 0.3685 -0.0047 -0.0405 0.0312  484 PHE   B CE1 
5195 C  CE2 . PHE   B 328 ? 0.4967 0.3462 0.3769 0.0010  -0.0453 0.0335  484 PHE   B CE2 
5196 C  CZ  . PHE   B 328 ? 0.4431 0.2947 0.3137 -0.0023 -0.0430 0.0278  484 PHE   B CZ  
5197 N  N   . ILE   B 329 ? 0.5062 0.3223 0.3840 -0.0007 -0.0293 0.0712  485 ILE   B N   
5198 C  CA  . ILE   B 329 ? 0.5474 0.3559 0.4271 0.0006  -0.0273 0.0832  485 ILE   B CA  
5199 C  C   . ILE   B 329 ? 0.5175 0.3152 0.3948 -0.0043 -0.0198 0.0812  485 ILE   B C   
5200 O  O   . ILE   B 329 ? 0.5127 0.3135 0.3805 -0.0088 -0.0189 0.0837  485 ILE   B O   
5201 C  CB  . ILE   B 329 ? 0.4935 0.3128 0.3644 0.0003  -0.0328 0.0929  485 ILE   B CB  
5202 C  CG1 . ILE   B 329 ? 0.5265 0.3590 0.3977 0.0030  -0.0407 0.0927  485 ILE   B CG1 
5203 C  CG2 . ILE   B 329 ? 0.4919 0.3037 0.3661 0.0026  -0.0309 0.1075  485 ILE   B CG2 
5204 C  CD1 . ILE   B 329 ? 0.5892 0.4353 0.4490 0.0008  -0.0467 0.1007  485 ILE   B CD1 
5205 N  N   . PRO   B 330 ? 0.5246 0.3102 0.4100 -0.0045 -0.0142 0.0765  486 PRO   B N   
5206 C  CA  . PRO   B 330 ? 0.5979 0.3766 0.4799 -0.0113 -0.0077 0.0711  486 PRO   B CA  
5207 C  C   . PRO   B 330 ? 0.5870 0.3572 0.4655 -0.0143 -0.0037 0.0803  486 PRO   B C   
5208 O  O   . PRO   B 330 ? 0.6240 0.3937 0.4966 -0.0212 0.0001  0.0773  486 PRO   B O   
5209 C  CB  . PRO   B 330 ? 0.6500 0.4183 0.5413 -0.0110 -0.0032 0.0638  486 PRO   B CB  
5210 C  CG  . PRO   B 330 ? 0.7096 0.4737 0.6106 -0.0030 -0.0051 0.0698  486 PRO   B CG  
5211 C  CD  . PRO   B 330 ? 0.6130 0.3919 0.5105 0.0008  -0.0134 0.0753  486 PRO   B CD  
5212 N  N   . GLU   B 331 ? 0.6267 0.3911 0.5091 -0.0095 -0.0044 0.0921  487 GLU   B N   
5213 C  CA  . GLU   B 331 ? 0.6973 0.4538 0.5763 -0.0121 -0.0007 0.1025  487 GLU   B CA  
5214 C  C   . GLU   B 331 ? 0.6078 0.3781 0.4743 -0.0154 -0.0047 0.1070  487 GLU   B C   
5215 O  O   . GLU   B 331 ? 0.6352 0.4008 0.4973 -0.0186 -0.0016 0.1153  487 GLU   B O   
5216 C  CB  . GLU   B 331 ? 0.6052 0.3524 0.4934 -0.0048 -0.0003 0.1153  487 GLU   B CB  
5217 C  CG  . GLU   B 331 ? 0.6823 0.4123 0.5824 -0.0022 0.0063  0.1111  487 GLU   B CG  
5218 C  CD  . GLU   B 331 ? 0.8068 0.5298 0.7185 0.0071  0.0066  0.1231  487 GLU   B CD  
5219 O  OE1 . GLU   B 331 ? 0.8817 0.6162 0.7985 0.0136  0.0003  0.1249  487 GLU   B OE1 
5220 O  OE2 . GLU   B 331 ? 0.8936 0.5996 0.8099 0.0078  0.0135  0.1310  487 GLU   B OE2 
5221 N  N   . PHE   B 332 ? 0.6354 0.4218 0.4959 -0.0150 -0.0107 0.1014  488 PHE   B N   
5222 C  CA  . PHE   B 332 ? 0.5981 0.3980 0.4459 -0.0180 -0.0140 0.1046  488 PHE   B CA  
5223 C  C   . PHE   B 332 ? 0.6043 0.4085 0.4454 -0.0245 -0.0103 0.0944  488 PHE   B C   
5224 O  O   . PHE   B 332 ? 0.5930 0.4033 0.4349 -0.0244 -0.0114 0.0835  488 PHE   B O   
5225 C  CB  . PHE   B 332 ? 0.5883 0.4025 0.4329 -0.0143 -0.0221 0.1044  488 PHE   B CB  
5226 C  CG  . PHE   B 332 ? 0.6480 0.4754 0.4787 -0.0174 -0.0255 0.1091  488 PHE   B CG  
5227 C  CD1 . PHE   B 332 ? 0.6376 0.4735 0.4580 -0.0222 -0.0242 0.1002  488 PHE   B CD1 
5228 C  CD2 . PHE   B 332 ? 0.7109 0.5429 0.5389 -0.0155 -0.0296 0.1229  488 PHE   B CD2 
5229 C  CE1 . PHE   B 332 ? 0.6620 0.5097 0.4688 -0.0253 -0.0265 0.1036  488 PHE   B CE1 
5230 C  CE2 . PHE   B 332 ? 0.7592 0.6044 0.5730 -0.0192 -0.0327 0.1271  488 PHE   B CE2 
5231 C  CZ  . PHE   B 332 ? 0.7032 0.5557 0.5058 -0.0244 -0.0308 0.1167  488 PHE   B CZ  
5232 N  N   . ASN   B 333 ? 0.5698 0.3718 0.4052 -0.0300 -0.0059 0.0987  489 ASN   B N   
5233 C  CA  . ASN   B 333 ? 0.6414 0.4489 0.4721 -0.0362 -0.0019 0.0903  489 ASN   B CA  
5234 C  C   . ASN   B 333 ? 0.5924 0.4158 0.4111 -0.0376 -0.0043 0.0896  489 ASN   B C   
5235 O  O   . ASN   B 333 ? 0.6209 0.4473 0.4315 -0.0406 -0.0033 0.0975  489 ASN   B O   
5236 C  CB  . ASN   B 333 ? 0.5314 0.3285 0.3630 -0.0425 0.0050  0.0940  489 ASN   B CB  
5237 C  CG  . ASN   B 333 ? 0.5265 0.3315 0.3546 -0.0492 0.0090  0.0860  489 ASN   B CG  
5238 O  OD1 . ASN   B 333 ? 0.5614 0.3783 0.3882 -0.0481 0.0071  0.0774  489 ASN   B OD1 
5239 N  ND2 . ASN   B 333 ? 0.5278 0.3270 0.3551 -0.0562 0.0147  0.0893  489 ASN   B ND2 
5240 N  N   . LEU   B 334 ? 0.5411 0.3740 0.3586 -0.0358 -0.0067 0.0795  490 LEU   B N   
5241 C  CA  . LEU   B 334 ? 0.5077 0.3543 0.3139 -0.0369 -0.0079 0.0768  490 LEU   B CA  
5242 C  C   . LEU   B 334 ? 0.5357 0.3872 0.3352 -0.0428 -0.0022 0.0777  490 LEU   B C   
5243 O  O   . LEU   B 334 ? 0.5983 0.4591 0.3865 -0.0445 -0.0023 0.0799  490 LEU   B O   
5244 C  CB  . LEU   B 334 ? 0.4869 0.3399 0.2949 -0.0343 -0.0093 0.0650  490 LEU   B CB  
5245 C  CG  . LEU   B 334 ? 0.5306 0.3815 0.3438 -0.0290 -0.0152 0.0633  490 LEU   B CG  
5246 C  CD1 . LEU   B 334 ? 0.5121 0.3674 0.3281 -0.0269 -0.0155 0.0517  490 LEU   B CD1 
5247 C  CD2 . LEU   B 334 ? 0.5934 0.4499 0.3978 -0.0282 -0.0206 0.0705  490 LEU   B CD2 
5248 N  N   . PHE   B 335 ? 0.5448 0.3914 0.3506 -0.0466 0.0030  0.0757  491 PHE   B N   
5249 C  CA  . PHE   B 335 ? 0.5568 0.4093 0.3581 -0.0527 0.0086  0.0765  491 PHE   B CA  
5250 C  C   . PHE   B 335 ? 0.6394 0.4831 0.4395 -0.0575 0.0116  0.0872  491 PHE   B C   
5251 O  O   . PHE   B 335 ? 0.6224 0.4677 0.4223 -0.0638 0.0169  0.0875  491 PHE   B O   
5252 C  CB  . PHE   B 335 ? 0.5502 0.4064 0.3590 -0.0551 0.0124  0.0675  491 PHE   B CB  
5253 C  CG  . PHE   B 335 ? 0.5663 0.4351 0.3741 -0.0518 0.0122  0.0586  491 PHE   B CG  
5254 C  CD1 . PHE   B 335 ? 0.5694 0.4444 0.3682 -0.0483 0.0096  0.0578  491 PHE   B CD1 
5255 C  CD2 . PHE   B 335 ? 0.5431 0.4177 0.3586 -0.0526 0.0149  0.0514  491 PHE   B CD2 
5256 C  CE1 . PHE   B 335 ? 0.5376 0.4219 0.3356 -0.0452 0.0106  0.0493  491 PHE   B CE1 
5257 C  CE2 . PHE   B 335 ? 0.5021 0.3875 0.3178 -0.0487 0.0154  0.0443  491 PHE   B CE2 
5258 C  CZ  . PHE   B 335 ? 0.5255 0.4144 0.3325 -0.0449 0.0137  0.0429  491 PHE   B CZ  
5259 N  N   . SER   B 336 ? 0.6268 0.4618 0.4264 -0.0548 0.0085  0.0967  492 SER   B N   
5260 C  CA  . SER   B 336 ? 0.6439 0.4688 0.4431 -0.0591 0.0122  0.1076  492 SER   B CA  
5261 C  C   . SER   B 336 ? 0.6884 0.5240 0.4760 -0.0639 0.0145  0.1132  492 SER   B C   
5262 O  O   . SER   B 336 ? 0.7054 0.5545 0.4836 -0.0624 0.0119  0.1116  492 SER   B O   
5263 C  CB  . SER   B 336 ? 0.7351 0.5489 0.5376 -0.0541 0.0088  0.1183  492 SER   B CB  
5264 O  OG  . SER   B 336 ? 0.8146 0.6389 0.6084 -0.0507 0.0031  0.1248  492 SER   B OG  
5265 N  N   . SER   B 337 ? 0.6708 0.4998 0.4585 -0.0704 0.0200  0.1195  493 SER   B N   
5266 C  CA  . SER   B 337 ? 0.7693 0.6079 0.5464 -0.0756 0.0229  0.1260  493 SER   B CA  
5267 C  C   . SER   B 337 ? 0.7645 0.6068 0.5321 -0.0724 0.0184  0.1373  493 SER   B C   
5268 O  O   . SER   B 337 ? 0.7056 0.5609 0.4615 -0.0752 0.0191  0.1401  493 SER   B O   
5269 C  CB  . SER   B 337 ? 0.8158 0.6449 0.5958 -0.0837 0.0297  0.1315  493 SER   B CB  
5270 O  OG  . SER   B 337 ? 0.9174 0.7265 0.7057 -0.0827 0.0304  0.1374  493 SER   B OG  
5271 N  N   . ASN   B 338 ? 0.7888 0.6214 0.5613 -0.0667 0.0138  0.1441  494 ASN   B N   
5272 C  CA  . ASN   B 338 ? 0.6900 0.5298 0.4543 -0.0631 0.0079  0.1543  494 ASN   B CA  
5273 C  C   . ASN   B 338 ? 0.7746 0.6319 0.5290 -0.0615 0.0035  0.1457  494 ASN   B C   
5274 O  O   . ASN   B 338 ? 0.7333 0.6019 0.4757 -0.0623 0.0004  0.1522  494 ASN   B O   
5275 C  CB  . ASN   B 338 ? 0.7729 0.6012 0.5474 -0.0561 0.0036  0.1611  494 ASN   B CB  
5276 C  CG  . ASN   B 338 ? 0.8145 0.6242 0.5974 -0.0571 0.0085  0.1720  494 ASN   B CG  
5277 O  OD1 . ASN   B 338 ? 0.8694 0.6761 0.6481 -0.0634 0.0139  0.1780  494 ASN   B OD1 
5278 N  ND2 . ASN   B 338 ? 0.8566 0.6527 0.6519 -0.0510 0.0075  0.1739  494 ASN   B ND2 
5279 N  N   . LEU   B 339 ? 0.7354 0.5949 0.4944 -0.0594 0.0033  0.1312  495 LEU   B N   
5280 C  CA  . LEU   B 339 ? 0.6676 0.5408 0.4184 -0.0576 -0.0003 0.1223  495 LEU   B CA  
5281 C  C   . LEU   B 339 ? 0.6951 0.5789 0.4389 -0.0615 0.0053  0.1128  495 LEU   B C   
5282 O  O   . LEU   B 339 ? 0.7810 0.6768 0.5130 -0.0620 0.0043  0.1090  495 LEU   B O   
5283 C  CB  . LEU   B 339 ? 0.6307 0.5000 0.3910 -0.0517 -0.0045 0.1131  495 LEU   B CB  
5284 C  CG  . LEU   B 339 ? 0.7542 0.6176 0.5204 -0.0465 -0.0111 0.1209  495 LEU   B CG  
5285 C  CD1 . LEU   B 339 ? 0.6967 0.5507 0.4771 -0.0417 -0.0123 0.1134  495 LEU   B CD1 
5286 C  CD2 . LEU   B 339 ? 0.7234 0.5996 0.4786 -0.0455 -0.0181 0.1245  495 LEU   B CD2 
5287 N  N   . ILE   B 340 ? 0.7897 0.6701 0.5409 -0.0644 0.0113  0.1085  496 ILE   B N   
5288 C  CA  . ILE   B 340 ? 0.6530 0.5446 0.4008 -0.0671 0.0170  0.0998  496 ILE   B CA  
5289 C  C   . ILE   B 340 ? 0.7876 0.6775 0.5385 -0.0736 0.0234  0.1047  496 ILE   B C   
5290 O  O   . ILE   B 340 ? 0.7263 0.6047 0.4878 -0.0751 0.0243  0.1065  496 ILE   B O   
5291 C  CB  . ILE   B 340 ? 0.7291 0.6218 0.4860 -0.0631 0.0171  0.0866  496 ILE   B CB  
5292 C  CG1 . ILE   B 340 ? 0.6249 0.5184 0.3793 -0.0573 0.0110  0.0811  496 ILE   B CG1 
5293 C  CG2 . ILE   B 340 ? 0.7651 0.6702 0.5201 -0.0650 0.0236  0.0793  496 ILE   B CG2 
5294 C  CD1 . ILE   B 340 ? 0.6658 0.5581 0.4305 -0.0530 0.0108  0.0695  496 ILE   B CD1 
5295 N  N   . ASP   B 341 ? 0.6755 0.5770 0.4172 -0.0781 0.0283  0.1062  497 ASP   B N   
5296 C  CA  . ASP   B 341 ? 0.6824 0.5842 0.4271 -0.0851 0.0347  0.1108  497 ASP   B CA  
5297 C  C   . ASP   B 341 ? 0.7220 0.6263 0.4787 -0.0863 0.0384  0.1014  497 ASP   B C   
5298 O  O   . ASP   B 341 ? 0.6610 0.5728 0.4207 -0.0818 0.0381  0.0912  497 ASP   B O   
5299 C  CB  . ASP   B 341 ? 0.6639 0.5794 0.3960 -0.0895 0.0394  0.1146  497 ASP   B CB  
5300 C  CG  . ASP   B 341 ? 0.8149 0.7289 0.5348 -0.0903 0.0361  0.1263  497 ASP   B CG  
5301 O  OD1 . ASP   B 341 ? 0.9722 0.8728 0.6964 -0.0899 0.0327  0.1355  497 ASP   B OD1 
5302 O  OD2 . ASP   B 341 ? 0.8552 0.7818 0.5616 -0.0914 0.0373  0.1267  497 ASP   B OD2 
5303 N  N   . LYS   B 342 ? 0.6570 0.5552 0.4207 -0.0928 0.0419  0.1053  498 LYS   B N   
5304 C  CA  . LYS   B 342 ? 0.7139 0.6170 0.4884 -0.0960 0.0454  0.0979  498 LYS   B CA  
5305 C  C   . LYS   B 342 ? 0.6832 0.6065 0.4558 -0.0954 0.0497  0.0920  498 LYS   B C   
5306 O  O   . LYS   B 342 ? 0.6150 0.5455 0.3948 -0.0914 0.0496  0.0831  498 LYS   B O   
5307 C  CB  . LYS   B 342 ? 0.6695 0.5650 0.4486 -0.1055 0.0495  0.1038  498 LYS   B CB  
5308 C  CG  . LYS   B 342 ? 0.6531 0.5569 0.4428 -0.1108 0.0529  0.0968  498 LYS   B CG  
5309 C  CD  . LYS   B 342 ? 0.6047 0.4936 0.4037 -0.1116 0.0506  0.0929  498 LYS   B CD  
5310 C  CE  . LYS   B 342 ? 0.6603 0.5582 0.4685 -0.1193 0.0539  0.0873  498 LYS   B CE  
5311 N  NZ  . LYS   B 342 ? 0.5426 0.4484 0.3577 -0.1129 0.0507  0.0778  498 LYS   B NZ  
5312 N  N   . ARG   B 343 ? 0.6299 0.5625 0.3926 -0.0987 0.0537  0.0974  499 ARG   B N   
5313 C  CA  . ARG   B 343 ? 0.6517 0.6035 0.4118 -0.0978 0.0591  0.0925  499 ARG   B CA  
5314 C  C   . ARG   B 343 ? 0.6707 0.6269 0.4310 -0.0886 0.0572  0.0823  499 ARG   B C   
5315 O  O   . ARG   B 343 ? 0.6782 0.6464 0.4457 -0.0861 0.0610  0.0754  499 ARG   B O   
5316 C  CB  . ARG   B 343 ? 0.7424 0.7008 0.4884 -0.1013 0.0627  0.0998  499 ARG   B CB  
5317 C  CG  . ARG   B 343 ? 0.7805 0.7532 0.5180 -0.0964 0.0661  0.0932  499 ARG   B CG  
5318 C  CD  . ARG   B 343 ? 0.7880 0.7657 0.5088 -0.0994 0.0682  0.0997  499 ARG   B CD  
5319 N  NE  . ARG   B 343 ? 0.7853 0.7780 0.5046 -0.1049 0.0767  0.1023  499 ARG   B NE  
5320 C  CZ  . ARG   B 343 ? 0.7054 0.7045 0.4111 -0.1095 0.0802  0.1092  499 ARG   B CZ  
5321 N  NH1 . ARG   B 343 ? 0.8086 0.8027 0.4998 -0.1087 0.0758  0.1135  499 ARG   B NH1 
5322 N  NH2 . ARG   B 343 ? 0.7560 0.7683 0.4626 -0.1152 0.0880  0.1124  499 ARG   B NH2 
5323 N  N   . SER   B 344 ? 0.6117 0.5589 0.3649 -0.0836 0.0514  0.0816  500 SER   B N   
5324 C  CA  . SER   B 344 ? 0.5741 0.5238 0.3270 -0.0758 0.0497  0.0718  500 SER   B CA  
5325 C  C   . SER   B 344 ? 0.5587 0.5059 0.3268 -0.0722 0.0480  0.0649  500 SER   B C   
5326 O  O   . SER   B 344 ? 0.5385 0.4946 0.3114 -0.0677 0.0511  0.0573  500 SER   B O   
5327 C  CB  . SER   B 344 ? 0.6834 0.6244 0.4260 -0.0727 0.0431  0.0732  500 SER   B CB  
5328 O  OG  . SER   B 344 ? 0.7258 0.6704 0.4541 -0.0768 0.0442  0.0809  500 SER   B OG  
5329 N  N   . LYS   B 345 ? 0.5798 0.5150 0.3555 -0.0741 0.0438  0.0679  501 LYS   B N   
5330 C  CA  . LYS   B 345 ? 0.6008 0.5342 0.3899 -0.0718 0.0421  0.0619  501 LYS   B CA  
5331 C  C   . LYS   B 345 ? 0.5705 0.5188 0.3682 -0.0748 0.0479  0.0597  501 LYS   B C   
5332 O  O   . LYS   B 345 ? 0.4950 0.4510 0.3010 -0.0703 0.0487  0.0533  501 LYS   B O   
5333 C  CB  . LYS   B 345 ? 0.5590 0.4768 0.3531 -0.0751 0.0382  0.0660  501 LYS   B CB  
5334 C  CG  . LYS   B 345 ? 0.6912 0.5957 0.4794 -0.0711 0.0322  0.0693  501 LYS   B CG  
5335 C  CD  . LYS   B 345 ? 0.7246 0.6134 0.5168 -0.0749 0.0306  0.0758  501 LYS   B CD  
5336 C  CE  . LYS   B 345 ? 0.6768 0.5560 0.4619 -0.0718 0.0260  0.0831  501 LYS   B CE  
5337 N  NZ  . LYS   B 345 ? 0.6748 0.5380 0.4630 -0.0745 0.0256  0.0917  501 LYS   B NZ  
5338 N  N   . GLU   B 346 ? 0.5583 0.5120 0.3544 -0.0826 0.0523  0.0659  502 GLU   B N   
5339 C  CA  . GLU   B 346 ? 0.5103 0.4808 0.3144 -0.0866 0.0580  0.0653  502 GLU   B CA  
5340 C  C   . GLU   B 346 ? 0.5265 0.5130 0.3304 -0.0802 0.0627  0.0605  502 GLU   B C   
5341 O  O   . GLU   B 346 ? 0.5176 0.5177 0.3326 -0.0785 0.0655  0.0573  502 GLU   B O   
5342 C  CB  . GLU   B 346 ? 0.5499 0.5225 0.3501 -0.0964 0.0619  0.0733  502 GLU   B CB  
5343 C  CG  . GLU   B 346 ? 0.5805 0.5402 0.3854 -0.1043 0.0597  0.0768  502 GLU   B CG  
5344 C  CD  . GLU   B 346 ? 0.6917 0.6508 0.4921 -0.1144 0.0639  0.0854  502 GLU   B CD  
5345 O  OE1 . GLU   B 346 ? 0.6727 0.6363 0.4632 -0.1143 0.0666  0.0902  502 GLU   B OE1 
5346 O  OE2 . GLU   B 346 ? 0.7570 0.7106 0.5634 -0.1231 0.0646  0.0870  502 GLU   B OE2 
5347 N  N   . PHE   B 347 ? 0.5635 0.5491 0.3549 -0.0767 0.0641  0.0602  503 PHE   B N   
5348 C  CA  . PHE   B 347 ? 0.4981 0.4967 0.2886 -0.0704 0.0699  0.0546  503 PHE   B CA  
5349 C  C   . PHE   B 347 ? 0.4792 0.4750 0.2772 -0.0618 0.0675  0.0467  503 PHE   B C   
5350 O  O   . PHE   B 347 ? 0.4915 0.4997 0.2987 -0.0571 0.0723  0.0429  503 PHE   B O   
5351 C  CB  . PHE   B 347 ? 0.5623 0.5594 0.3356 -0.0699 0.0720  0.0551  503 PHE   B CB  
5352 C  CG  . PHE   B 347 ? 0.5338 0.5425 0.3045 -0.0640 0.0795  0.0485  503 PHE   B CG  
5353 C  CD1 . PHE   B 347 ? 0.6376 0.6631 0.4104 -0.0660 0.0884  0.0504  503 PHE   B CD1 
5354 C  CD2 . PHE   B 347 ? 0.6078 0.6103 0.3747 -0.0566 0.0785  0.0402  503 PHE   B CD2 
5355 C  CE1 . PHE   B 347 ? 0.6416 0.6768 0.4124 -0.0599 0.0966  0.0440  503 PHE   B CE1 
5356 C  CE2 . PHE   B 347 ? 0.6097 0.6205 0.3742 -0.0511 0.0867  0.0334  503 PHE   B CE2 
5357 C  CZ  . PHE   B 347 ? 0.6060 0.6330 0.3727 -0.0524 0.0960  0.0352  503 PHE   B CZ  
5358 N  N   . LEU   B 348 ? 0.4627 0.4430 0.2581 -0.0594 0.0602  0.0448  504 LEU   B N   
5359 C  CA  . LEU   B 348 ? 0.4683 0.4454 0.2705 -0.0517 0.0579  0.0376  504 LEU   B CA  
5360 C  C   . LEU   B 348 ? 0.4876 0.4712 0.3062 -0.0519 0.0574  0.0374  504 LEU   B C   
5361 O  O   . LEU   B 348 ? 0.4516 0.4414 0.2790 -0.0455 0.0591  0.0328  504 LEU   B O   
5362 C  CB  . LEU   B 348 ? 0.4736 0.4340 0.2697 -0.0498 0.0501  0.0362  504 LEU   B CB  
5363 C  CG  . LEU   B 348 ? 0.5203 0.4759 0.3227 -0.0424 0.0473  0.0289  504 LEU   B CG  
5364 C  CD1 . LEU   B 348 ? 0.4616 0.4244 0.2626 -0.0361 0.0537  0.0221  504 LEU   B CD1 
5365 C  CD2 . LEU   B 348 ? 0.4794 0.4200 0.2761 -0.0414 0.0395  0.0285  504 LEU   B CD2 
5366 N  N   . THR   B 349 ? 0.4567 0.4394 0.2793 -0.0597 0.0554  0.0427  505 THR   B N   
5367 C  CA  . THR   B 349 ? 0.4507 0.4416 0.2875 -0.0619 0.0549  0.0425  505 THR   B CA  
5368 C  C   . THR   B 349 ? 0.4357 0.4483 0.2806 -0.0607 0.0618  0.0430  505 THR   B C   
5369 O  O   . THR   B 349 ? 0.4663 0.4886 0.3227 -0.0559 0.0623  0.0406  505 THR   B O   
5370 C  CB  . THR   B 349 ? 0.4783 0.4629 0.3159 -0.0720 0.0525  0.0472  505 THR   B CB  
5371 O  OG1 . THR   B 349 ? 0.4899 0.4545 0.3226 -0.0713 0.0466  0.0467  505 THR   B OG1 
5372 C  CG2 . THR   B 349 ? 0.4382 0.4344 0.2897 -0.0762 0.0523  0.0465  505 THR   B CG2 
5373 N  N   . LYS   B 350 ? 0.4531 0.4743 0.2926 -0.0646 0.0674  0.0468  506 LYS   B N   
5374 C  CA  . LYS   B 350 ? 0.4595 0.5026 0.3068 -0.0631 0.0749  0.0479  506 LYS   B CA  
5375 C  C   . LYS   B 350 ? 0.4683 0.5157 0.3194 -0.0513 0.0785  0.0423  506 LYS   B C   
5376 O  O   . LYS   B 350 ? 0.4485 0.5110 0.3134 -0.0472 0.0814  0.0424  506 LYS   B O   
5377 C  CB  . LYS   B 350 ? 0.4610 0.5098 0.2989 -0.0684 0.0805  0.0523  506 LYS   B CB  
5378 C  CG  . LYS   B 350 ? 0.4985 0.5710 0.3444 -0.0678 0.0891  0.0545  506 LYS   B CG  
5379 C  CD  . LYS   B 350 ? 0.5236 0.6020 0.3610 -0.0761 0.0939  0.0602  506 LYS   B CD  
5380 C  CE  . LYS   B 350 ? 0.7256 0.8296 0.5761 -0.0799 0.1001  0.0646  506 LYS   B CE  
5381 N  NZ  . LYS   B 350 ? 0.5866 0.6933 0.4441 -0.0918 0.0958  0.0694  506 LYS   B NZ  
5382 N  N   . GLN   B 351 ? 0.4590 0.4925 0.2982 -0.0461 0.0780  0.0376  507 GLN   B N   
5383 C  CA  . GLN   B 351 ? 0.5100 0.5450 0.3513 -0.0356 0.0826  0.0314  507 GLN   B CA  
5384 C  C   . GLN   B 351 ? 0.4534 0.4856 0.3070 -0.0299 0.0784  0.0287  507 GLN   B C   
5385 O  O   . GLN   B 351 ? 0.4519 0.4950 0.3170 -0.0226 0.0833  0.0276  507 GLN   B O   
5386 C  CB  . GLN   B 351 ? 0.4749 0.4954 0.2989 -0.0335 0.0827  0.0264  507 GLN   B CB  
5387 C  CG  . GLN   B 351 ? 0.5196 0.5441 0.3302 -0.0387 0.0875  0.0290  507 GLN   B CG  
5388 C  CD  . GLN   B 351 ? 0.5251 0.5689 0.3419 -0.0369 0.0980  0.0302  507 GLN   B CD  
5389 O  OE1 . GLN   B 351 ? 0.6047 0.6540 0.4281 -0.0285 0.1044  0.0254  507 GLN   B OE1 
5390 N  NE2 . GLN   B 351 ? 0.4951 0.5489 0.3097 -0.0446 0.1005  0.0368  507 GLN   B NE2 
5391 N  N   . ILE   B 352 ? 0.4369 0.4552 0.2888 -0.0327 0.0697  0.0283  508 ILE   B N   
5392 C  CA  . ILE   B 352 ? 0.4369 0.4528 0.2995 -0.0275 0.0659  0.0258  508 ILE   B CA  
5393 C  C   . ILE   B 352 ? 0.4349 0.4694 0.3136 -0.0292 0.0669  0.0304  508 ILE   B C   
5394 O  O   . ILE   B 352 ? 0.4248 0.4673 0.3152 -0.0222 0.0684  0.0297  508 ILE   B O   
5395 C  CB  . ILE   B 352 ? 0.5032 0.5008 0.3606 -0.0301 0.0569  0.0243  508 ILE   B CB  
5396 C  CG1 . ILE   B 352 ? 0.4542 0.4361 0.2982 -0.0268 0.0554  0.0196  508 ILE   B CG1 
5397 C  CG2 . ILE   B 352 ? 0.4230 0.4210 0.2926 -0.0271 0.0528  0.0232  508 ILE   B CG2 
5398 C  CD1 . ILE   B 352 ? 0.4580 0.4239 0.2974 -0.0296 0.0469  0.0196  508 ILE   B CD1 
5399 N  N   . GLU   B 353 ? 0.4227 0.4653 0.3024 -0.0388 0.0662  0.0355  509 GLU   B N   
5400 C  CA  . GLU   B 353 ? 0.4181 0.4808 0.3124 -0.0420 0.0667  0.0398  509 GLU   B CA  
5401 C  C   . GLU   B 353 ? 0.4272 0.5104 0.3316 -0.0351 0.0748  0.0419  509 GLU   B C   
5402 O  O   . GLU   B 353 ? 0.4135 0.5124 0.3325 -0.0317 0.0752  0.0445  509 GLU   B O   
5403 C  CB  . GLU   B 353 ? 0.4096 0.4770 0.3022 -0.0549 0.0653  0.0443  509 GLU   B CB  
5404 C  CG  . GLU   B 353 ? 0.4174 0.4673 0.3052 -0.0618 0.0579  0.0429  509 GLU   B CG  
5405 C  CD  . GLU   B 353 ? 0.4554 0.5074 0.3412 -0.0751 0.0576  0.0469  509 GLU   B CD  
5406 O  OE1 . GLU   B 353 ? 0.4639 0.5239 0.3465 -0.0790 0.0625  0.0505  509 GLU   B OE1 
5407 O  OE2 . GLU   B 353 ? 0.4149 0.4593 0.3017 -0.0819 0.0529  0.0459  509 GLU   B OE2 
5408 N  N   . TYR   B 354 ? 0.4278 0.5118 0.3247 -0.0327 0.0817  0.0411  510 TYR   B N   
5409 C  CA  . TYR   B 354 ? 0.4611 0.5622 0.3674 -0.0243 0.0908  0.0422  510 TYR   B CA  
5410 C  C   . TYR   B 354 ? 0.4611 0.5569 0.3743 -0.0123 0.0918  0.0382  510 TYR   B C   
5411 O  O   . TYR   B 354 ? 0.4292 0.5418 0.3586 -0.0061 0.0951  0.0418  510 TYR   B O   
5412 C  CB  . TYR   B 354 ? 0.4881 0.5876 0.3826 -0.0236 0.0985  0.0404  510 TYR   B CB  
5413 C  CG  . TYR   B 354 ? 0.5284 0.6431 0.4325 -0.0138 0.1091  0.0404  510 TYR   B CG  
5414 C  CD1 . TYR   B 354 ? 0.5443 0.6853 0.4626 -0.0150 0.1143  0.0474  510 TYR   B CD1 
5415 C  CD2 . TYR   B 354 ? 0.5131 0.6164 0.4132 -0.0034 0.1144  0.0336  510 TYR   B CD2 
5416 C  CE1 . TYR   B 354 ? 0.6285 0.7844 0.5575 -0.0049 0.1248  0.0482  510 TYR   B CE1 
5417 C  CE2 . TYR   B 354 ? 0.5541 0.6701 0.4641 0.0064  0.1255  0.0335  510 TYR   B CE2 
5418 C  CZ  . TYR   B 354 ? 0.6033 0.7457 0.5282 0.0061  0.1308  0.0412  510 TYR   B CZ  
5419 O  OH  . TYR   B 354 ? 0.6905 0.8463 0.6269 0.0167  0.1425  0.0419  510 TYR   B OH  
5420 N  N   . GLU   B 355 ? 0.4807 0.5537 0.3823 -0.0091 0.0889  0.0315  511 GLU   B N   
5421 C  CA  . GLU   B 355 ? 0.4695 0.5352 0.3767 0.0015  0.0902  0.0273  511 GLU   B CA  
5422 C  C   . GLU   B 355 ? 0.4643 0.5386 0.3869 0.0028  0.0850  0.0315  511 GLU   B C   
5423 O  O   . GLU   B 355 ? 0.4494 0.5347 0.3861 0.0114  0.0895  0.0338  511 GLU   B O   
5424 C  CB  . GLU   B 355 ? 0.4769 0.5174 0.3687 0.0021  0.0861  0.0198  511 GLU   B CB  
5425 C  CG  . GLU   B 355 ? 0.4758 0.5088 0.3521 0.0024  0.0922  0.0148  511 GLU   B CG  
5426 C  CD  . GLU   B 355 ? 0.5090 0.5489 0.3909 0.0120  0.1040  0.0120  511 GLU   B CD  
5427 O  OE1 . GLU   B 355 ? 0.5416 0.5782 0.4330 0.0206  0.1061  0.0098  511 GLU   B OE1 
5428 O  OE2 . GLU   B 355 ? 0.5491 0.5978 0.4266 0.0112  0.1117  0.0124  511 GLU   B OE2 
5429 N  N   . ARG   B 356 ? 0.4183 0.4884 0.3387 -0.0060 0.0760  0.0329  512 ARG   B N   
5430 C  CA  . ARG   B 356 ? 0.4278 0.5042 0.3601 -0.0058 0.0704  0.0357  512 ARG   B CA  
5431 C  C   . ARG   B 356 ? 0.4311 0.5359 0.3798 -0.0062 0.0734  0.0435  512 ARG   B C   
5432 O  O   . ARG   B 356 ? 0.3893 0.5042 0.3512 -0.0006 0.0726  0.0468  512 ARG   B O   
5433 C  CB  . ARG   B 356 ? 0.4053 0.4693 0.3298 -0.0157 0.0612  0.0344  512 ARG   B CB  
5434 C  CG  . ARG   B 356 ? 0.4046 0.4692 0.3370 -0.0162 0.0548  0.0351  512 ARG   B CG  
5435 C  CD  . ARG   B 356 ? 0.3848 0.4685 0.3249 -0.0261 0.0520  0.0405  512 ARG   B CD  
5436 N  NE  . ARG   B 356 ? 0.3787 0.4547 0.3084 -0.0377 0.0497  0.0397  512 ARG   B NE  
5437 C  CZ  . ARG   B 356 ? 0.3861 0.4442 0.3076 -0.0436 0.0439  0.0363  512 ARG   B CZ  
5438 N  NH1 . ARG   B 356 ? 0.3847 0.4325 0.3073 -0.0401 0.0393  0.0332  512 ARG   B NH1 
5439 N  NH2 . ARG   B 356 ? 0.3817 0.4322 0.2945 -0.0531 0.0433  0.0364  512 ARG   B NH2 
5440 N  N   . ASN   B 357 ? 0.3952 0.5146 0.3440 -0.0122 0.0772  0.0473  513 ASN   B N   
5441 C  CA  . ASN   B 357 ? 0.3836 0.5328 0.3488 -0.0126 0.0804  0.0553  513 ASN   B CA  
5442 C  C   . ASN   B 357 ? 0.4728 0.6337 0.4503 0.0011  0.0895  0.0577  513 ASN   B C   
5443 O  O   . ASN   B 357 ? 0.3716 0.5587 0.3659 0.0033  0.0919  0.0655  513 ASN   B O   
5444 C  CB  . ASN   B 357 ? 0.3708 0.5327 0.3330 -0.0233 0.0825  0.0587  513 ASN   B CB  
5445 C  CG  . ASN   B 357 ? 0.3723 0.5325 0.3300 -0.0378 0.0743  0.0594  513 ASN   B CG  
5446 O  OD1 . ASN   B 357 ? 0.3587 0.5233 0.3229 -0.0403 0.0684  0.0605  513 ASN   B OD1 
5447 N  ND2 . ASN   B 357 ? 0.3701 0.5230 0.3163 -0.0476 0.0745  0.0586  513 ASN   B ND2 
5448 N  N   . ASN   B 358 ? 0.4615 0.6044 0.4312 0.0100  0.0950  0.0514  514 ASN   B N   
5449 C  CA  . ASN   B 358 ? 0.5783 0.7297 0.5584 0.0229  0.1058  0.0527  514 ASN   B CA  
5450 C  C   . ASN   B 358 ? 0.5295 0.6630 0.5108 0.0338  0.1069  0.0479  514 ASN   B C   
5451 O  O   . ASN   B 358 ? 0.5701 0.7004 0.5546 0.0446  0.1168  0.0457  514 ASN   B O   
5452 C  CB  . ASN   B 358 ? 0.4475 0.5961 0.4174 0.0232  0.1146  0.0490  514 ASN   B CB  
5453 C  CG  . ASN   B 358 ? 0.4955 0.6661 0.4683 0.0142  0.1159  0.0553  514 ASN   B CG  
5454 O  OD1 . ASN   B 358 ? 0.5529 0.7488 0.5418 0.0180  0.1219  0.0624  514 ASN   B OD1 
5455 N  ND2 . ASN   B 358 ? 0.4922 0.6537 0.4501 0.0022  0.1106  0.0532  514 ASN   B ND2 
5456 N  N   . GLU   B 359 ? 0.4484 0.5692 0.4266 0.0310  0.0976  0.0460  515 GLU   B N   
5457 C  CA  . GLU   B 359 ? 0.5391 0.6423 0.5181 0.0398  0.0976  0.0418  515 GLU   B CA  
5458 C  C   . GLU   B 359 ? 0.5913 0.6698 0.5541 0.0428  0.1022  0.0315  515 GLU   B C   
5459 O  O   . GLU   B 359 ? 0.5563 0.6245 0.5216 0.0526  0.1087  0.0277  515 GLU   B O   
5460 C  CB  . GLU   B 359 ? 0.5469 0.6658 0.5465 0.0517  0.1038  0.0488  515 GLU   B CB  
5461 C  CG  . GLU   B 359 ? 0.5831 0.7338 0.5994 0.0485  0.1013  0.0604  515 GLU   B CG  
5462 C  CD  . GLU   B 359 ? 0.6663 0.8296 0.7020 0.0584  0.1023  0.0685  515 GLU   B CD  
5463 O  OE1 . GLU   B 359 ? 0.7507 0.9084 0.7937 0.0713  0.1116  0.0683  515 GLU   B OE1 
5464 O  OE2 . GLU   B 359 ? 0.7621 0.9398 0.8051 0.0530  0.0940  0.0749  515 GLU   B OE2 
5465 N  N   . PHE   B 360 ? 0.4628 0.5319 0.4086 0.0335  0.0988  0.0271  516 PHE   B N   
5466 C  CA  . PHE   B 360 ? 0.5297 0.5758 0.4572 0.0329  0.0998  0.0176  516 PHE   B CA  
5467 C  C   . PHE   B 360 ? 0.6156 0.6576 0.5412 0.0416  0.1121  0.0125  516 PHE   B C   
5468 O  O   . PHE   B 360 ? 0.6429 0.6663 0.5623 0.0463  0.1142  0.0050  516 PHE   B O   
5469 C  CB  . PHE   B 360 ? 0.5432 0.5699 0.4664 0.0331  0.0919  0.0131  516 PHE   B CB  
5470 C  CG  . PHE   B 360 ? 0.5517 0.5797 0.4753 0.0247  0.0807  0.0168  516 PHE   B CG  
5471 C  CD1 . PHE   B 360 ? 0.4694 0.4879 0.3787 0.0153  0.0745  0.0148  516 PHE   B CD1 
5472 C  CD2 . PHE   B 360 ? 0.5188 0.5577 0.4571 0.0261  0.0768  0.0226  516 PHE   B CD2 
5473 C  CE1 . PHE   B 360 ? 0.5144 0.5325 0.4244 0.0079  0.0656  0.0176  516 PHE   B CE1 
5474 C  CE2 . PHE   B 360 ? 0.4879 0.5275 0.4256 0.0177  0.0674  0.0248  516 PHE   B CE2 
5475 C  CZ  . PHE   B 360 ? 0.4965 0.5247 0.4201 0.0087  0.0622  0.0219  516 PHE   B CZ  
5476 N  N   . PRO   B 361 ? 0.5783 0.6366 0.5082 0.0433  0.1211  0.0156  517 PRO   B N   
5477 C  CA  . PRO   B 361 ? 0.5202 0.5733 0.4473 0.0516  0.1341  0.0096  517 PRO   B CA  
5478 C  C   . PRO   B 361 ? 0.6475 0.6777 0.5519 0.0480  0.1346  -0.0016 517 PRO   B C   
5479 O  O   . PRO   B 361 ? 0.7217 0.7406 0.6226 0.0549  0.1441  -0.0091 517 PRO   B O   
5480 C  CB  . PRO   B 361 ? 0.5582 0.6342 0.4911 0.0508  0.1417  0.0153  517 PRO   B CB  
5481 C  CG  . PRO   B 361 ? 0.6255 0.7117 0.5555 0.0387  0.1315  0.0214  517 PRO   B CG  
5482 C  CD  . PRO   B 361 ? 0.5551 0.6360 0.4908 0.0367  0.1201  0.0237  517 PRO   B CD  
5483 N  N   . VAL   B 362 ? 0.6731 0.6961 0.5620 0.0373  0.1251  -0.0028 518 VAL   B N   
5484 C  CA  . VAL   B 362 ? 0.6173 0.6217 0.4845 0.0333  0.1249  -0.0122 518 VAL   B CA  
5485 C  C   . VAL   B 362 ? 0.7496 0.7342 0.6145 0.0377  0.1233  -0.0197 518 VAL   B C   
5486 O  O   . VAL   B 362 ? 0.7951 0.7647 0.6438 0.0361  0.1257  -0.0290 518 VAL   B O   
5487 C  CB  . VAL   B 362 ? 0.5907 0.5919 0.4438 0.0216  0.1142  -0.0101 518 VAL   B CB  
5488 C  CG1 . VAL   B 362 ? 0.6794 0.6706 0.5350 0.0190  0.1019  -0.0088 518 VAL   B CG1 
5489 C  CG2 . VAL   B 362 ? 0.6795 0.6698 0.5104 0.0170  0.1164  -0.0175 518 VAL   B CG2 
5490 N  N   . PHE   B 363 ? 0.6727 0.6575 0.5530 0.0423  0.1190  -0.0159 519 PHE   B N   
5491 C  CA  . PHE   B 363 ? 0.7102 0.6771 0.5904 0.0468  0.1180  -0.0221 519 PHE   B CA  
5492 C  C   . PHE   B 363 ? 0.7583 0.7182 0.6404 0.0559  0.1319  -0.0288 519 PHE   B C   
5493 O  O   . PHE   B 363 ? 0.7861 0.7273 0.6623 0.0577  0.1331  -0.0369 519 PHE   B O   
5494 C  CB  . PHE   B 363 ? 0.6662 0.6378 0.5636 0.0499  0.1112  -0.0150 519 PHE   B CB  
5495 C  CG  . PHE   B 363 ? 0.6432 0.6113 0.5355 0.0413  0.0974  -0.0126 519 PHE   B CG  
5496 C  CD1 . PHE   B 363 ? 0.6753 0.6350 0.5498 0.0326  0.0916  -0.0163 519 PHE   B CD1 
5497 C  CD2 . PHE   B 363 ? 0.5740 0.5487 0.4799 0.0420  0.0907  -0.0061 519 PHE   B CD2 
5498 C  CE1 . PHE   B 363 ? 0.6979 0.6541 0.5694 0.0257  0.0799  -0.0136 519 PHE   B CE1 
5499 C  CE2 . PHE   B 363 ? 0.5198 0.4908 0.4215 0.0344  0.0792  -0.0044 519 PHE   B CE2 
5500 C  CZ  . PHE   B 363 ? 0.5809 0.5423 0.4662 0.0267  0.0742  -0.0080 519 PHE   B CZ  
5501 N  N   . ASP   B 364 ? 0.7347 0.7090 0.6255 0.0615  0.1428  -0.0255 520 ASP   B N   
5502 C  CA  . ASP   B 364 ? 0.8193 0.7868 0.7120 0.0705  0.1579  -0.0321 520 ASP   B CA  
5503 C  C   . ASP   B 364 ? 0.7985 0.7727 0.6805 0.0687  0.1678  -0.0358 520 ASP   B C   
5504 O  O   . ASP   B 364 ? 0.7570 0.7235 0.6365 0.0748  0.1814  -0.0434 520 ASP   B O   
5505 C  CB  . ASP   B 364 ? 0.7552 0.7334 0.6731 0.0826  0.1644  -0.0241 520 ASP   B CB  
5506 C  CG  . ASP   B 364 ? 0.8764 0.8395 0.8014 0.0874  0.1611  -0.0252 520 ASP   B CG  
5507 O  OD1 . ASP   B 364 ? 0.8691 0.8134 0.7901 0.0925  0.1703  -0.0343 520 ASP   B OD1 
5508 O  OD2 . ASP   B 364 ? 0.8691 0.8384 0.8026 0.0852  0.1498  -0.0177 520 ASP   B OD2 
5509 N  N1  . A1EKD C .   ? 0.4543 0.4698 0.5921 -0.0316 -0.0540 0.0173  601 A1EKD A N1  
5510 N  N3  . A1EKD C .   ? 0.4258 0.4737 0.6036 -0.0007 -0.0188 0.0245  601 A1EKD A N3  
5511 C  C4  . A1EKD C .   ? 0.3724 0.3757 0.5004 -0.0395 -0.0560 0.0134  601 A1EKD A C4  
5512 C  C5  . A1EKD C .   ? 0.5156 0.5424 0.6631 -0.0179 -0.0524 0.0220  601 A1EKD A C5  
5513 C  C6  . A1EKD C .   ? 0.4652 0.4923 0.6135 -0.0091 -0.0524 0.0242  601 A1EKD A C6  
5514 C  C7  . A1EKD C .   ? 0.3966 0.4336 0.5547 -0.0206 -0.0486 0.0239  601 A1EKD A C7  
5515 C  C8  . A1EKD C .   ? 0.4467 0.4994 0.6209 -0.0150 -0.0433 0.0283  601 A1EKD A C8  
5516 C  C10 . A1EKD C .   ? 0.4467 0.5272 0.6373 -0.0173 -0.0564 0.0373  601 A1EKD A C10 
5517 C  C13 . A1EKD C .   ? 0.4499 0.5443 0.6555 -0.0008 -0.0560 0.0467  601 A1EKD A C13 
5518 C  C15 . A1EKD C .   ? 0.4269 0.4931 0.6159 0.0003  -0.0432 0.0357  601 A1EKD A C15 
5519 C  C17 . A1EKD C .   ? 0.4483 0.5064 0.6332 -0.0052 -0.0268 0.0284  601 A1EKD A C17 
5520 C  C20 . A1EKD C .   ? 0.5782 0.6260 0.7537 0.0088  0.0160  0.0146  601 A1EKD A C20 
5521 C  C21 . A1EKD C .   ? 0.5196 0.5781 0.7048 0.0115  0.0253  0.0144  601 A1EKD A C21 
5522 C  C22 . A1EKD C .   ? 0.5364 0.6115 0.7402 0.0139  0.0254  0.0198  601 A1EKD A C22 
5523 C  C24 . A1EKD C .   ? 0.5699 0.6412 0.7717 0.0094  0.0067  0.0249  601 A1EKD A C24 
5524 C  C26 . A1EKD C .   ? 0.3808 0.3927 0.5234 -0.0059 -0.0325 0.0174  601 A1EKD A C26 
5525 C  C28 . A1EKD C .   ? 0.4058 0.3802 0.5188 -0.0635 -0.0570 0.0054  601 A1EKD A C28 
5526 C  C1  . A1EKD C .   ? 0.4346 0.4017 0.5312 -0.0535 -0.0629 0.0012  601 A1EKD A C1  
5527 C  C11 . A1EKD C .   ? 0.5122 0.5934 0.6991 -0.0301 -0.0613 0.0350  601 A1EKD A C11 
5528 C  C12 . A1EKD C .   ? 0.4320 0.5274 0.6328 -0.0127 -0.0607 0.0437  601 A1EKD A C12 
5529 C  C14 . A1EKD C .   ? 0.4759 0.5547 0.6755 0.0055  -0.0469 0.0422  601 A1EKD A C14 
5530 C  C16 . A1EKD C .   ? 0.4463 0.4924 0.6188 -0.0084 -0.0336 0.0261  601 A1EKD A C16 
5531 C  C18 . A1EKD C .   ? 0.4687 0.5225 0.6530 0.0032  -0.0094 0.0241  601 A1EKD A C18 
5532 C  C19 . A1EKD C .   ? 0.5009 0.5542 0.6842 0.0077  0.0070  0.0194  601 A1EKD A C19 
5533 C  C2  . A1EKD C .   ? 0.4919 0.4730 0.6014 -0.0499 -0.0604 0.0062  601 A1EKD A C2  
5534 C  C23 . A1EKD C .   ? 0.5600 0.6429 0.7731 0.0128  0.0160  0.0255  601 A1EKD A C23 
5535 C  C25 . A1EKD C .   ? 0.4425 0.4715 0.6012 -0.0051 -0.0293 0.0213  601 A1EKD A C25 
5536 C  C27 . A1EKD C .   ? 0.4518 0.4815 0.6034 -0.0296 -0.0502 0.0211  601 A1EKD A C27 
5537 C  C29 . A1EKD C .   ? 0.4424 0.4018 0.5429 -0.0665 -0.0591 0.0001  601 A1EKD A C29 
5538 C  C3  . A1EKD C .   ? 0.4108 0.3961 0.5282 -0.0549 -0.0574 0.0081  601 A1EKD A C3  
5539 C  C30 . A1EKD C .   ? 0.4518 0.4078 0.5439 -0.0618 -0.0620 -0.0022 601 A1EKD A C30 
5540 C  C9  . A1EKD C .   ? 0.4066 0.4735 0.5916 -0.0104 -0.0477 0.0338  601 A1EKD A C9  
5541 F  F1  . A1EKD C .   ? 0.4753 0.4389 0.5640 -0.0489 -0.0655 -0.0002 601 A1EKD A F1  
5542 F  F2  . A1EKD C .   ? 0.5779 0.6109 0.7365 0.0068  0.0159  0.0100  601 A1EKD A F2  
5543 F  F3  . A1EKD C .   ? 0.6567 0.7425 0.8704 0.0170  0.0354  0.0196  601 A1EKD A F3  
5544 F  F4  . A1EKD C .   ? 0.5284 0.4745 0.6244 -0.0744 -0.0575 -0.0030 601 A1EKD A F4  
5545 N  N2  . A1EKD C .   ? 0.4475 0.4620 0.5826 -0.0246 -0.0556 0.0178  601 A1EKD A N2  
5546 N  N4  . A1EKD C .   ? 0.5088 0.5524 0.6830 0.0046  -0.0022 0.0193  601 A1EKD A N4  
5547 N  N5  . A1EKD C .   ? 0.4265 0.4570 0.5882 -0.0009 -0.0207 0.0203  601 A1EKD A N5  
5548 N  N6  . A1EKD C .   ? 0.5076 0.4988 0.6232 -0.0410 -0.0596 0.0096  601 A1EKD A N6  
5549 O  O1  . A1EKD C .   ? 0.4664 0.5383 0.6410 -0.0360 -0.0674 0.0315  601 A1EKD A O1  
5550 O  O2  . A1EKD C .   ? 0.5178 0.6085 0.7140 -0.0345 -0.0588 0.0364  601 A1EKD A O2  
5551 O  O3  . A1EKD C .   ? 0.4305 0.5076 0.6316 -0.0064 -0.0273 0.0334  601 A1EKD A O3  
5552 O  O4  . A1EKD C .   ? 0.4780 0.5121 0.6348 -0.0356 -0.0479 0.0219  601 A1EKD A O4  
5553 S  S1  . A1EKD C .   ? 0.4450 0.4488 0.5775 -0.0485 -0.0537 0.0138  601 A1EKD A S1  
5554 S  S2  . A1EKD C .   ? 0.5497 0.6264 0.7563 0.0059  -0.0060 0.0299  601 A1EKD A S2  
5555 ZN ZN  . ZN    D .   ? 0.4161 0.3006 0.3969 -0.0051 -0.0037 -0.0282 602 ZN    A ZN  
5556 N  N1  . A1EKD E .   ? 0.7440 0.6395 0.5128 -0.0307 -0.0440 0.0421  601 A1EKD B N1  
5557 N  N3  . A1EKD E .   ? 0.7442 0.6453 0.4714 -0.0392 -0.0100 0.0009  601 A1EKD B N3  
5558 C  C4  . A1EKD E .   ? 0.6938 0.5839 0.4745 -0.0271 -0.0449 0.0519  601 A1EKD B C4  
5559 C  C5  . A1EKD E .   ? 0.8174 0.7179 0.5737 -0.0352 -0.0444 0.0254  601 A1EKD B C5  
5560 C  C6  . A1EKD E .   ? 0.8087 0.7093 0.5624 -0.0371 -0.0459 0.0146  601 A1EKD B C6  
5561 C  C7  . A1EKD E .   ? 0.6673 0.5703 0.4137 -0.0375 -0.0395 0.0283  601 A1EKD B C7  
5562 C  C8  . A1EKD E .   ? 0.7564 0.6640 0.4861 -0.0423 -0.0343 0.0213  601 A1EKD B C8  
5563 C  C10 . A1EKD E .   ? 0.7466 0.6705 0.4578 -0.0514 -0.0474 0.0246  601 A1EKD B C10 
5564 C  C13 . A1EKD E .   ? 0.8691 0.7955 0.5616 -0.0604 -0.0466 0.0033  601 A1EKD B C13 
5565 C  C15 . A1EKD E .   ? 0.7789 0.6895 0.4905 -0.0493 -0.0340 0.0014  601 A1EKD B C15 
5566 C  C17 . A1EKD E .   ? 0.7986 0.7045 0.5182 -0.0430 -0.0179 0.0081  601 A1EKD B C17 
5567 C  C20 . A1EKD E .   ? 0.8173 0.7218 0.5468 -0.0314 0.0250  -0.0198 601 A1EKD B C20 
5568 C  C21 . A1EKD E .   ? 0.7346 0.6434 0.4538 -0.0325 0.0341  -0.0252 601 A1EKD B C21 
5569 C  C22 . A1EKD E .   ? 0.8311 0.7438 0.5311 -0.0388 0.0338  -0.0263 601 A1EKD B C22 
5570 C  C24 . A1EKD E .   ? 0.7555 0.6652 0.4584 -0.0421 0.0150  -0.0152 601 A1EKD B C24 
5571 C  C26 . A1EKD E .   ? 0.6712 0.5595 0.4334 -0.0304 -0.0243 0.0066  601 A1EKD B C26 
5572 C  C28 . A1EKD E .   ? 0.5871 0.4602 0.3885 -0.0211 -0.0424 0.0818  601 A1EKD B C28 
5573 C  C1  . A1EKD E .   ? 0.7575 0.6333 0.5735 -0.0155 -0.0506 0.0707  601 A1EKD B C1  
5574 C  C11 . A1EKD E .   ? 0.8158 0.7433 0.5330 -0.0493 -0.0524 0.0412  601 A1EKD B C11 
5575 C  C12 . A1EKD E .   ? 0.8116 0.7428 0.5107 -0.0578 -0.0517 0.0186  601 A1EKD B C12 
5576 C  C14 . A1EKD E .   ? 0.7699 0.6853 0.4693 -0.0556 -0.0375 -0.0050 601 A1EKD B C14 
5577 C  C16 . A1EKD E .   ? 0.8203 0.7225 0.5522 -0.0401 -0.0247 0.0119  601 A1EKD B C16 
5578 C  C18 . A1EKD E .   ? 0.7538 0.6570 0.4745 -0.0395 -0.0007 -0.0048 601 A1EKD B C18 
5579 C  C19 . A1EKD E .   ? 0.8312 0.7356 0.5530 -0.0359 0.0158  -0.0150 601 A1EKD B C19 
5580 C  C2  . A1EKD E .   ? 0.7570 0.6379 0.5588 -0.0203 -0.0482 0.0655  601 A1EKD B C2  
5581 C  C23 . A1EKD E .   ? 0.8892 0.8031 0.5803 -0.0441 0.0241  -0.0213 601 A1EKD B C23 
5582 C  C25 . A1EKD E .   ? 0.6402 0.5347 0.3862 -0.0349 -0.0207 0.0062  601 A1EKD B C25 
5583 C  C27 . A1EKD E .   ? 0.7510 0.6510 0.5057 -0.0349 -0.0398 0.0392  601 A1EKD B C27 
5584 C  C29 . A1EKD E .   ? 0.5827 0.4496 0.3980 -0.0161 -0.0446 0.0863  601 A1EKD B C29 
5585 C  C3  . A1EKD E .   ? 0.6824 0.5626 0.4771 -0.0229 -0.0441 0.0710  601 A1EKD B C3  
5586 C  C30 . A1EKD E .   ? 0.6754 0.5441 0.4982 -0.0131 -0.0486 0.0811  601 A1EKD B C30 
5587 C  C9  . A1EKD E .   ? 0.7450 0.6591 0.4619 -0.0478 -0.0387 0.0156  601 A1EKD B C9  
5588 F  F1  . A1EKD E .   ? 0.6258 0.5032 0.4491 -0.0132 -0.0543 0.0657  601 A1EKD B F1  
5589 F  F2  . A1EKD E .   ? 0.7229 0.6244 0.4699 -0.0261 0.0253  -0.0190 601 A1EKD B F2  
5590 F  F3  . A1EKD E .   ? 1.0147 0.9316 0.7041 -0.0400 0.0436  -0.0323 601 A1EKD B F3  
5591 F  F4  . A1EKD E .   ? 0.8564 0.7139 0.6789 -0.0141 -0.0418 0.0962  601 A1EKD B F4  
5592 N  N2  . A1EKD E .   ? 0.7524 0.6490 0.5224 -0.0309 -0.0470 0.0338  601 A1EKD B N2  
5593 N  N4  . A1EKD E .   ? 0.6910 0.5914 0.4223 -0.0349 0.0066  -0.0091 601 A1EKD B N4  
5594 N  N5  . A1EKD E .   ? 0.7030 0.5974 0.4462 -0.0343 -0.0122 0.0001  601 A1EKD B N5  
5595 N  N6  . A1EKD E .   ? 0.7816 0.6680 0.5753 -0.0230 -0.0486 0.0543  601 A1EKD B N6  
5596 O  O1  . A1EKD E .   ? 0.8097 0.7377 0.5386 -0.0462 -0.0590 0.0477  601 A1EKD B O1  
5597 O  O2  . A1EKD E .   ? 0.8726 0.8024 0.5834 -0.0506 -0.0493 0.0479  601 A1EKD B O2  
5598 O  O3  . A1EKD E .   ? 0.7011 0.6152 0.4046 -0.0486 -0.0186 0.0113  601 A1EKD B O3  
5599 O  O4  . A1EKD E .   ? 0.7258 0.6262 0.4771 -0.0360 -0.0361 0.0461  601 A1EKD B O4  
5600 S  S1  . A1EKD E .   ? 0.6890 0.5769 0.4667 -0.0284 -0.0406 0.0622  601 A1EKD B S1  
5601 S  S2  . A1EKD E .   ? 0.8908 0.8024 0.5888 -0.0464 0.0024  -0.0067 601 A1EKD B S2  
5602 ZN ZN  . ZN    F .   ? 0.4375 0.3161 0.3745 0.0204  -0.0042 -0.0112 602 ZN    B ZN  
5603 O  O   . HOH   G .   ? 0.4805 0.5219 0.6467 -0.0312 -0.0361 0.0243  701 HOH   A O   
5604 O  O   . HOH   G .   ? 0.5303 0.6516 0.8812 0.1154  0.0582  0.0723  702 HOH   A O   
5605 O  O   . HOH   G .   ? 0.3895 0.4550 0.3807 -0.0496 0.0107  0.0456  703 HOH   A O   
5606 O  O   . HOH   G .   ? 0.4177 0.4687 0.4149 -0.0401 0.0027  0.0524  704 HOH   A O   
5607 O  O   . HOH   G .   ? 0.5382 0.5520 0.5088 -0.0283 -0.0145 0.0217  705 HOH   A O   
5608 O  O   . HOH   G .   ? 0.3886 0.5721 0.5884 -0.1465 -0.1232 0.0319  706 HOH   A O   
5609 O  O   . HOH   G .   ? 0.4652 0.3043 0.4444 0.0197  -0.0099 -0.0100 707 HOH   A O   
5610 O  O   . HOH   G .   ? 0.4107 0.4563 0.5729 -0.0703 -0.0631 0.0206  708 HOH   A O   
5611 O  O   . HOH   G .   ? 0.5464 0.4627 0.4958 -0.0773 -0.0954 -0.0409 709 HOH   A O   
5612 O  O   . HOH   G .   ? 0.4690 0.3271 0.4747 0.0080  -0.0179 0.0017  710 HOH   A O   
5613 O  O   . HOH   G .   ? 0.6459 0.4935 0.6956 -0.2153 -0.0573 -0.0688 711 HOH   A O   
5614 O  O   . HOH   G .   ? 0.5350 0.3362 0.4855 -0.0100 -0.0226 -0.0441 712 HOH   A O   
5615 O  O   . HOH   G .   ? 0.3693 0.4681 0.3838 -0.0618 0.0267  0.0721  713 HOH   A O   
5616 O  O   . HOH   G .   ? 0.7312 0.5514 0.7138 -0.0057 0.0437  -0.0575 714 HOH   A O   
5617 O  O   . HOH   G .   ? 0.4370 0.3417 0.3950 -0.0207 -0.0049 -0.0275 715 HOH   A O   
5618 O  O   . HOH   G .   ? 0.5726 0.4815 0.7123 -0.0962 0.0015  0.0605  716 HOH   A O   
5619 O  O   . HOH   G .   ? 0.4474 0.3079 0.4249 0.0066  -0.0169 -0.0189 717 HOH   A O   
5620 O  O   . HOH   G .   ? 0.3293 0.4336 0.3635 -0.0641 0.0276  0.1032  718 HOH   A O   
5621 O  O   . HOH   G .   ? 0.5155 0.5015 0.6291 -0.0096 -0.0482 0.0124  719 HOH   A O   
5622 O  O   . HOH   G .   ? 0.5579 0.7405 0.7833 -0.0114 0.1127  0.0143  720 HOH   A O   
5623 O  O   . HOH   G .   ? 0.3575 0.5012 0.3849 -0.0782 0.0666  0.0465  721 HOH   A O   
5624 O  O   . HOH   G .   ? 0.5491 0.3905 0.5565 -0.1362 -0.0601 -0.0645 722 HOH   A O   
5625 O  O   . HOH   G .   ? 0.7531 0.8132 0.9251 -0.2575 -0.0914 -0.0135 723 HOH   A O   
5626 O  O   . HOH   G .   ? 0.3219 0.4323 0.3142 -0.0707 0.0412  0.0384  724 HOH   A O   
5627 O  O   . HOH   G .   ? 0.5011 0.6521 0.6100 -0.2080 -0.1519 -0.0086 725 HOH   A O   
5628 O  O   . HOH   G .   ? 0.3849 0.4134 0.4259 -0.0380 0.0094  0.0712  726 HOH   A O   
5629 O  O   . HOH   G .   ? 0.5130 0.3658 0.4600 -0.0725 -0.0678 -0.0588 727 HOH   A O   
5630 O  O   . HOH   G .   ? 0.4824 0.4753 0.4363 -0.0444 -0.0010 -0.0108 728 HOH   A O   
5631 O  O   . HOH   G .   ? 0.6794 0.4536 0.6438 -0.0446 -0.0234 -0.0578 729 HOH   A O   
5632 O  O   . HOH   G .   ? 0.4748 0.2858 0.5151 -0.0806 -0.0293 -0.0283 730 HOH   A O   
5633 O  O   . HOH   G .   ? 0.4069 0.3020 0.4059 -0.0064 0.0209  -0.0411 731 HOH   A O   
5634 O  O   . HOH   G .   ? 0.4777 0.5050 0.6101 -0.0286 -0.0716 0.0212  732 HOH   A O   
5635 O  O   . HOH   G .   ? 0.4412 0.3707 0.4147 -0.0036 -0.0170 0.0011  733 HOH   A O   
5636 O  O   . HOH   G .   ? 0.5387 0.3455 0.4933 -0.0240 -0.0323 -0.0474 734 HOH   A O   
5637 O  O   . HOH   G .   ? 0.6905 0.7443 0.6340 -0.0612 -0.0044 0.0079  735 HOH   A O   
5638 O  O   . HOH   G .   ? 0.3413 0.2689 0.4170 -0.0311 -0.0395 0.0021  736 HOH   A O   
5639 O  O   . HOH   G .   ? 0.5485 0.3812 0.4661 -0.0129 -0.0418 -0.0426 737 HOH   A O   
5640 O  O   . HOH   G .   ? 0.4408 0.6211 0.3636 -0.1101 0.0553  0.0243  738 HOH   A O   
5641 O  O   . HOH   G .   ? 0.3978 0.5185 0.6283 0.0198  -0.0612 0.0665  739 HOH   A O   
5642 O  O   . HOH   G .   ? 0.4488 0.4491 0.5946 -0.0616 -0.0264 0.0265  740 HOH   A O   
5643 O  O   . HOH   G .   ? 0.4726 0.5009 0.4353 -0.0592 0.0409  -0.0285 741 HOH   A O   
5644 O  O   . HOH   G .   ? 0.5151 0.4096 0.5536 -0.0053 -0.0140 0.0259  742 HOH   A O   
5645 O  O   . HOH   G .   ? 0.6378 0.6713 0.6005 -0.1480 -0.1435 -0.0343 743 HOH   A O   
5646 O  O   . HOH   G .   ? 0.6580 0.4841 0.6220 -0.1512 -0.0639 -0.0887 744 HOH   A O   
5647 O  O   . HOH   G .   ? 0.5304 0.4209 0.4698 -0.0263 -0.0777 -0.0214 745 HOH   A O   
5648 O  O   . HOH   G .   ? 0.3738 0.2320 0.3412 0.0097  -0.0299 -0.0124 746 HOH   A O   
5649 O  O   . HOH   G .   ? 0.7881 0.5585 0.8341 -0.1433 -0.0224 -0.0486 747 HOH   A O   
5650 O  O   . HOH   G .   ? 0.4923 0.4865 0.5116 -0.0224 -0.0030 0.0427  748 HOH   A O   
5651 O  O   . HOH   G .   ? 0.4625 0.5157 0.4284 -0.0632 0.0399  -0.0136 749 HOH   A O   
5652 O  O   . HOH   G .   ? 0.4700 0.3303 0.4333 0.0099  -0.0383 -0.0110 750 HOH   A O   
5653 O  O   . HOH   G .   ? 0.3308 0.2414 0.3295 -0.0006 -0.0189 -0.0019 751 HOH   A O   
5654 O  O   . HOH   G .   ? 0.4493 0.3024 0.3817 0.0068  -0.0359 -0.0116 752 HOH   A O   
5655 O  O   . HOH   G .   ? 0.3993 0.4161 0.5146 -0.0649 0.0192  0.0857  753 HOH   A O   
5656 O  O   . HOH   G .   ? 0.5231 0.3062 0.5371 -0.0691 -0.0241 -0.0405 754 HOH   A O   
5657 O  O   . HOH   G .   ? 0.4811 0.3431 0.5950 -0.0840 -0.0040 0.0401  755 HOH   A O   
5658 O  O   . HOH   G .   ? 0.4464 0.5717 0.7438 0.0721  0.0003  0.0722  756 HOH   A O   
5659 O  O   . HOH   G .   ? 0.6726 0.6101 0.6813 0.0181  -0.0111 0.0374  757 HOH   A O   
5660 O  O   . HOH   G .   ? 0.5498 0.3787 0.4754 -0.0468 -0.0531 -0.0590 758 HOH   A O   
5661 O  O   . HOH   G .   ? 0.6405 0.5740 0.7212 -0.2543 -0.0813 -0.0604 759 HOH   A O   
5662 O  O   . HOH   G .   ? 0.4228 0.3292 0.3787 -0.0174 -0.0103 -0.0212 760 HOH   A O   
5663 O  O   . HOH   G .   ? 0.3781 0.2485 0.3551 0.0062  -0.0235 -0.0167 761 HOH   A O   
5664 O  O   . HOH   G .   ? 0.5838 0.5118 0.4803 -0.0980 0.0129  -0.0555 762 HOH   A O   
5665 O  O   . HOH   G .   ? 0.3654 0.4251 0.3894 -0.0478 0.0166  0.0632  763 HOH   A O   
5666 O  O   . HOH   G .   ? 0.4246 0.3540 0.3794 -0.0301 -0.0020 -0.0269 764 HOH   A O   
5667 O  O   . HOH   G .   ? 0.5042 0.5370 0.4273 -0.0790 0.0265  -0.0353 765 HOH   A O   
5668 O  O   . HOH   G .   ? 0.4738 0.5681 0.6837 -0.0238 -0.0065 0.0341  766 HOH   A O   
5669 O  O   . HOH   G .   ? 0.4114 0.2696 0.4411 -0.0179 -0.0281 -0.0048 767 HOH   A O   
5670 O  O   . HOH   G .   ? 0.4292 0.3831 0.3967 -0.0147 -0.0151 0.0022  768 HOH   A O   
5671 O  O   . HOH   G .   ? 0.4071 0.4473 0.5053 -0.0605 0.0238  0.0836  769 HOH   A O   
5672 O  O   . HOH   G .   ? 0.4182 0.2886 0.4117 0.0097  -0.0176 -0.0178 770 HOH   A O   
5673 O  O   . HOH   G .   ? 0.5209 0.5167 0.4383 -0.0801 0.0410  -0.0615 771 HOH   A O   
5674 O  O   . HOH   G .   ? 0.4993 0.5713 0.6969 0.0215  0.0575  0.0060  772 HOH   A O   
5675 O  O   . HOH   G .   ? 0.5206 0.5887 0.6843 -0.0256 -0.0755 0.0343  773 HOH   A O   
5676 O  O   . HOH   G .   ? 0.3694 0.3811 0.4357 -0.0388 0.0114  0.1014  774 HOH   A O   
5677 O  O   . HOH   G .   ? 0.6107 0.4012 0.5767 -0.0069 -0.0144 -0.0387 775 HOH   A O   
5678 O  O   . HOH   G .   ? 0.4374 0.3278 0.4354 -0.0021 0.0066  -0.0322 776 HOH   A O   
5679 O  O   . HOH   G .   ? 0.4704 0.3889 0.5491 -0.0276 0.0011  0.0688  777 HOH   A O   
5680 O  O   . HOH   G .   ? 0.5942 0.3998 0.5342 -0.0418 -0.0396 -0.0597 778 HOH   A O   
5681 O  O   . HOH   G .   ? 0.4922 0.4688 0.5888 -0.0300 -0.0632 0.0066  779 HOH   A O   
5682 O  O   . HOH   G .   ? 0.4154 0.2925 0.4086 0.0062  -0.0427 -0.0122 780 HOH   A O   
5683 O  O   . HOH   G .   ? 0.5392 0.3678 0.4776 -0.0210 0.0047  -0.0309 781 HOH   A O   
5684 O  O   . HOH   G .   ? 0.6910 0.5753 0.5786 -0.1415 -0.0933 -0.0917 782 HOH   A O   
5685 O  O   . HOH   G .   ? 0.5750 0.4669 0.6970 -0.0737 0.0058  0.0679  783 HOH   A O   
5686 O  O   . HOH   G .   ? 0.5769 0.4502 0.5911 0.0244  -0.0333 0.0016  784 HOH   A O   
5687 O  O   . HOH   G .   ? 0.6054 0.6316 0.5479 -0.0716 0.0600  -0.0533 785 HOH   A O   
5688 O  O   . HOH   G .   ? 0.4581 0.3206 0.4220 0.0072  -0.0414 -0.0146 786 HOH   A O   
5689 O  O   . HOH   G .   ? 0.4311 0.4182 0.4677 -0.0211 -0.0019 0.0593  787 HOH   A O   
5690 O  O   . HOH   G .   ? 0.5436 0.4300 0.5811 0.0029  -0.0094 0.0352  788 HOH   A O   
5691 O  O   . HOH   G .   ? 0.5301 0.4647 0.4811 -0.0273 -0.0098 -0.0172 789 HOH   A O   
5692 O  O   . HOH   H .   ? 0.8451 0.7764 0.5655 -0.0462 -0.0522 0.1389  701 HOH   B O   
5693 O  O   . HOH   H .   ? 0.7384 0.8236 0.5640 -0.0790 -0.1643 0.0715  702 HOH   B O   
5694 O  O   . HOH   H .   ? 0.7266 0.6287 0.4669 -0.0392 -0.0231 0.0385  703 HOH   B O   
5695 O  O   . HOH   H .   ? 0.5510 0.5519 0.4981 -0.0359 -0.0087 0.0094  704 HOH   B O   
5696 O  O   . HOH   H .   ? 0.6674 0.7155 0.6099 0.0146  -0.1401 0.1759  705 HOH   B O   
5697 O  O   . HOH   H .   ? 0.3672 0.4191 0.2989 -0.0525 0.0270  0.0314  706 HOH   B O   
5698 O  O   . HOH   H .   ? 0.7905 0.6103 0.6984 0.0389  -0.0403 0.2674  707 HOH   B O   
5699 O  O   . HOH   H .   ? 0.5304 0.4425 0.3441 -0.0939 0.0436  0.0689  708 HOH   B O   
5700 O  O   . HOH   H .   ? 0.7836 0.6745 0.4027 -0.0834 0.0052  -0.0883 709 HOH   B O   
5701 O  O   . HOH   H .   ? 0.5438 0.4118 0.5187 0.0411  -0.0595 0.0912  710 HOH   B O   
5702 O  O   . HOH   H .   ? 0.7467 0.6201 0.4431 -0.0490 0.0042  -0.0657 711 HOH   B O   
5703 O  O   . HOH   H .   ? 0.6060 0.5154 0.4194 -0.0259 -0.0767 0.0308  712 HOH   B O   
5704 O  O   . HOH   H .   ? 0.4335 0.4650 0.4077 -0.0110 -0.0065 0.0310  713 HOH   B O   
5705 O  O   . HOH   H .   ? 0.4349 0.3531 0.3799 -0.0119 -0.0137 -0.0075 714 HOH   B O   
5706 O  O   . HOH   H .   ? 0.5218 0.5258 0.4871 -0.0022 0.0014  0.0238  715 HOH   B O   
5707 O  O   . HOH   H .   ? 0.6544 0.7210 0.4579 -0.0160 -0.1389 0.2538  716 HOH   B O   
5708 O  O   . HOH   H .   ? 0.5700 0.3925 0.4886 -0.0175 -0.0057 -0.0086 717 HOH   B O   
5709 O  O   . HOH   H .   ? 0.6340 0.4863 0.5440 0.0467  0.0544  -0.0353 718 HOH   B O   
5710 O  O   . HOH   H .   ? 0.5298 0.3846 0.5260 0.0419  -0.0457 0.0579  719 HOH   B O   
5711 O  O   . HOH   H .   ? 0.5374 0.4018 0.5547 0.0587  0.0240  0.0286  720 HOH   B O   
5712 O  O   . HOH   H .   ? 0.6416 0.4719 0.5776 0.0419  -0.0471 0.1732  721 HOH   B O   
5713 O  O   . HOH   H .   ? 0.5311 0.3707 0.4439 -0.0287 -0.0028 -0.0130 722 HOH   B O   
5714 O  O   . HOH   H .   ? 0.5143 0.3336 0.4619 -0.0071 -0.0006 -0.0216 723 HOH   B O   
5715 O  O   . HOH   H .   ? 0.4021 0.3190 0.3659 0.0114  -0.0123 0.0036  724 HOH   B O   
5716 O  O   . HOH   H .   ? 0.4702 0.5749 0.3584 -0.0566 0.0872  0.0528  725 HOH   B O   
5717 O  O   . HOH   H .   ? 0.6047 0.3709 0.5068 0.0079  -0.0119 0.1071  726 HOH   B O   
5718 O  O   . HOH   H .   ? 0.5804 0.4578 0.3517 -0.0410 -0.0103 0.0743  727 HOH   B O   
5719 O  O   . HOH   H .   ? 0.6250 0.4425 0.5585 0.0114  -0.0116 -0.0364 728 HOH   B O   
5720 O  O   . HOH   H .   ? 0.4092 0.2779 0.3882 0.0069  -0.0385 -0.0145 729 HOH   B O   
5721 O  O   . HOH   H .   ? 0.5182 0.5726 0.5303 0.0471  0.0421  0.0513  730 HOH   B O   
5722 O  O   . HOH   H .   ? 0.4810 0.3345 0.4198 0.0137  -0.0196 -0.0201 731 HOH   B O   
5723 O  O   . HOH   H .   ? 0.7339 0.6401 0.4875 -0.0355 -0.0475 0.0872  732 HOH   B O   
5724 O  O   . HOH   H .   ? 0.7261 0.9131 0.5668 -0.0663 -0.1983 0.1675  733 HOH   B O   
5725 O  O   . HOH   H .   ? 0.8618 0.9859 0.5573 -0.0580 -0.1316 0.2766  734 HOH   B O   
5726 O  O   . HOH   H .   ? 0.7165 0.9178 0.6510 -0.0118 -0.1926 0.2374  735 HOH   B O   
5727 O  O   . HOH   H .   ? 0.5954 0.4593 0.4596 -0.0699 0.0183  0.0244  736 HOH   B O   
5728 O  O   . HOH   H .   ? 0.3929 0.6144 0.3927 -0.0325 0.0723  0.0751  737 HOH   B O   
5729 O  O   . HOH   H .   ? 0.4260 0.2790 0.3710 0.0080  -0.0318 -0.0204 738 HOH   B O   
5730 O  O   . HOH   H .   ? 0.4842 0.3337 0.3238 -0.0149 -0.0270 0.0397  739 HOH   B O   
5731 O  O   . HOH   H .   ? 0.7534 0.5874 0.7055 0.0504  0.0365  -0.0206 740 HOH   B O   
5732 O  O   . HOH   H .   ? 0.6578 0.6636 0.3249 -0.0847 -0.0980 0.0543  741 HOH   B O   
5733 O  O   . HOH   H .   ? 0.4051 0.4342 0.3307 -0.0604 0.0188  0.0240  742 HOH   B O   
5734 O  O   . HOH   H .   ? 0.6124 0.6679 0.5568 0.0032  -0.1442 0.1487  743 HOH   B O   
5735 O  O   . HOH   H .   ? 0.4665 0.3176 0.3874 0.0118  -0.0188 -0.0232 744 HOH   B O   
5736 O  O   . HOH   H .   ? 0.4435 0.3878 0.4085 0.0162  -0.0024 0.0128  745 HOH   B O   
5737 O  O   . HOH   H .   ? 0.3967 0.2786 0.3124 -0.0092 -0.0117 -0.0076 746 HOH   B O   
5738 O  O   . HOH   H .   ? 0.5470 0.4992 0.4478 -0.0530 0.0128  0.0118  747 HOH   B O   
5739 O  O   . HOH   H .   ? 0.3989 0.3733 0.2828 -0.0790 0.0299  0.0283  748 HOH   B O   
5740 O  O   . HOH   H .   ? 0.4396 0.3238 0.3634 0.0309  0.0196  -0.0147 749 HOH   B O   
5741 O  O   . HOH   H .   ? 0.5029 0.3123 0.4780 0.0312  -0.0221 0.0357  750 HOH   B O   
5742 O  O   . HOH   H .   ? 0.6908 0.5753 0.5030 -0.0183 -0.0551 0.0403  751 HOH   B O   
5743 O  O   . HOH   H .   ? 0.7360 0.6189 0.5270 -0.0242 -0.0422 0.0154  752 HOH   B O   
5744 O  O   . HOH   H .   ? 0.4734 0.5354 0.4274 0.0030  0.0504  0.0350  753 HOH   B O   
5745 O  O   . HOH   H .   ? 0.6803 0.4374 0.6077 0.0175  -0.0082 0.0912  754 HOH   B O   
5746 O  O   . HOH   H .   ? 0.4401 0.4837 0.3989 0.0164  0.0493  0.0312  755 HOH   B O   
5747 O  O   . HOH   H .   ? 0.3484 0.2089 0.2848 0.0103  -0.0235 -0.0171 756 HOH   B O   
5748 O  O   . HOH   H .   ? 0.4938 0.3022 0.3877 -0.0102 -0.0138 0.0266  757 HOH   B O   
5749 O  O   . HOH   H .   ? 0.6609 0.6909 0.3607 -0.0565 -0.1087 0.1800  758 HOH   B O   
5750 O  O   . HOH   H .   ? 0.4987 0.3598 0.4882 0.0270  -0.0055 0.0043  759 HOH   B O   
5751 O  O   . HOH   H .   ? 0.4356 0.3841 0.3859 -0.0147 -0.0125 0.0009  760 HOH   B O   
5752 O  O   . HOH   H .   ? 0.5139 0.5252 0.4081 -0.0716 0.0358  0.0327  761 HOH   B O   
5753 O  O   . HOH   H .   ? 0.4665 0.3421 0.3877 0.0237  0.0068  -0.0163 762 HOH   B O   
5754 O  O   . HOH   H .   ? 0.7361 0.6259 0.4920 -0.0401 -0.0444 -0.0167 763 HOH   B O   
5755 O  O   . HOH   H .   ? 0.5010 0.4524 0.3268 -0.0911 0.0489  0.0593  764 HOH   B O   
5756 O  O   . HOH   H .   ? 0.6079 0.4300 0.5957 0.0410  -0.0303 0.0553  765 HOH   B O   
5757 O  O   . HOH   H .   ? 0.4275 0.2797 0.3436 0.0047  -0.0394 -0.0103 766 HOH   B O   
5758 O  O   . HOH   H .   ? 0.7513 1.0780 0.4313 -0.2025 -0.2209 0.1004  767 HOH   B O   
5759 O  O   . HOH   H .   ? 0.5576 0.4050 0.4522 -0.0033 -0.0411 -0.0277 768 HOH   B O   
5760 O  O   . HOH   H .   ? 0.5827 0.4207 0.5157 0.0192  -0.0074 -0.0270 769 HOH   B O   
5761 O  O   . HOH   H .   ? 0.6242 0.4038 0.6018 0.0388  -0.0123 0.0635  770 HOH   B O   
5762 O  O   . HOH   H .   ? 0.6327 0.4893 0.5511 0.0022  -0.0485 -0.0122 771 HOH   B O   
5763 O  O   . HOH   H .   ? 0.4242 0.3595 0.2896 -0.1065 0.0359  0.0354  772 HOH   B O   
5764 O  O   . HOH   H .   ? 0.6432 0.4757 0.5307 -0.0370 0.0013  0.0074  773 HOH   B O   
5765 O  O   . HOH   H .   ? 0.4300 0.2869 0.3793 0.0065  -0.0392 -0.0172 774 HOH   B O   
5766 O  O   . HOH   H .   ? 0.6680 0.5829 0.3833 -0.0267 0.0602  -0.0398 775 HOH   B O   
5767 O  O   . HOH   H .   ? 0.5864 0.6535 0.5720 0.0376  0.0644  0.0406  776 HOH   B O   
5768 O  O   . HOH   H .   ? 0.5230 0.3798 0.4698 0.0078  -0.0400 -0.0127 777 HOH   B O   
5769 O  O   . HOH   H .   ? 0.5948 0.5332 0.4853 -0.0687 0.0163  0.0135  778 HOH   B O   
5770 O  O   . HOH   H .   ? 0.5284 0.3833 0.4497 0.0263  0.0078  -0.0240 779 HOH   B O   
5771 O  O   . HOH   H .   ? 0.6148 0.4852 0.5805 0.0553  0.0361  -0.0047 780 HOH   B O   
# 
