data_9CLL
# 
_entry.id   9CLL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9CLL         pdb_00009cll 10.2210/pdb9cll/pdb 
WWPDB D_1000285485 ?            ?                   
# 
_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       2024-11-27 
# 
_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                        9CLL 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ltilley@unimelb.edu.au 
_pdbx_contact_author.name_first         Leann 
_pdbx_contact_author.name_last          Tilley 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9910-0199 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tai, C.W.'       1 0000-0002-1870-8678 
'Dogovski, C.'    2 ?                   
'Xie, S.C.'       3 0000-0001-7003-4677 
'Tilley, L.'      4 0000-0001-9910-0199 
'Griffin, M.D.W.' 5 0000-0001-9845-7735 
# 
_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                     'Plasmodium falciparum tyrosyl-tRNA synthetase in complex with ML471-Tyr' 
_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 'Tai, C.W.'       1 0000-0002-1870-8678 
primary 'Dogovski, C.'    2 ?                   
primary 'Xie, S.C.'       3 0000-0001-7003-4677 
primary 'Tilley, L.'      4 0000-0001-9910-0199 
primary 'Griffin, M.D.W.' 5 0000-0001-9845-7735 
# 
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 'tyrosine--tRNA ligase' 43514.227 2   6.1.1.1 ? ? ? 
2 non-polymer syn 
;{(2R,3S,4R,5R)-5-[4-amino-3-(propan-2-yl)-1H-pyrazolo[3,4-d]pyrimidin-1-yl]-3,4-dihydroxyoxolan-2-yl}methyl [(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]sulfamate
;
551.573   2   ?       ? ? ? 
3 non-polymer syn 'MALONATE ION' 102.046   2   ?       ? ? ? 
4 non-polymer nat 'CHLORIDE ION' 35.453    2   ?       ? ? ? 
5 non-polymer syn 'SODIUM ION' 22.990    4   ?       ? ? ? 
6 water       nat water 18.015    380 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Tyrosyl-tRNA synthetase' 
# 
_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       
;METTDTKREEQEIEEKKAQEESKIEDVDKILNDILSISSECIQPDELRVKLLLKRKLICYDGFEPSGRMHIAQGLLKSII
VNKLTSNGCTFIFWIADWFAHLNNKMSGDLKKIKKVGSYFIEVWKSCGMNMENVQFLWASEEINKKPNEYWSLVLDISRS
FNINRMKRCLKIMGRSEGEENYCSQILYPCMQCADIFFLNVDICQLGIDQRKVNMLAREYCDIKKIKKKPVILSHGMLPG
LLEGQEKMSKSDENSAIFMDDSESDVNRKIKKAYCPPNVIENNPIYAYAKSIIFPSYNEFNLVRKEKNGGDKTYYTLQEL
EHDYVNGFIHPLDLKDNVAMYINKLLQPVRDHFQNNIEAKNLLNEIKKYKVTK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;METTDTKREEQEIEEKKAQEESKIEDVDKILNDILSISSECIQPDELRVKLLLKRKLICYDGFEPSGRMHIAQGLLKSII
VNKLTSNGCTFIFWIADWFAHLNNKMSGDLKKIKKVGSYFIEVWKSCGMNMENVQFLWASEEINKKPNEYWSLVLDISRS
FNINRMKRCLKIMGRSEGEENYCSQILYPCMQCADIFFLNVDICQLGIDQRKVNMLAREYCDIKKIKKKPVILSHGMLPG
LLEGQEKMSKSDENSAIFMDDSESDVNRKIKKAYCPPNVIENNPIYAYAKSIIFPSYNEFNLVRKEKNGGDKTYYTLQEL
EHDYVNGFIHPLDLKDNVAMYINKLLQPVRDHFQNNIEAKNLLNEIKKYKVTK
;
_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 
;{(2R,3S,4R,5R)-5-[4-amino-3-(propan-2-yl)-1H-pyrazolo[3,4-d]pyrimidin-1-yl]-3,4-dihydroxyoxolan-2-yl}methyl [(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]sulfamate
;
A1AZG 
3 'MALONATE ION' MLI   
4 'CHLORIDE ION' CL    
5 'SODIUM ION' NA    
6 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLU n 
1 3   THR n 
1 4   THR n 
1 5   ASP n 
1 6   THR n 
1 7   LYS n 
1 8   ARG n 
1 9   GLU n 
1 10  GLU n 
1 11  GLN n 
1 12  GLU n 
1 13  ILE n 
1 14  GLU n 
1 15  GLU n 
1 16  LYS n 
1 17  LYS n 
1 18  ALA n 
1 19  GLN n 
1 20  GLU n 
1 21  GLU n 
1 22  SER n 
1 23  LYS n 
1 24  ILE n 
1 25  GLU n 
1 26  ASP n 
1 27  VAL n 
1 28  ASP n 
1 29  LYS n 
1 30  ILE n 
1 31  LEU n 
1 32  ASN n 
1 33  ASP n 
1 34  ILE n 
1 35  LEU n 
1 36  SER n 
1 37  ILE n 
1 38  SER n 
1 39  SER n 
1 40  GLU n 
1 41  CYS n 
1 42  ILE n 
1 43  GLN n 
1 44  PRO n 
1 45  ASP n 
1 46  GLU n 
1 47  LEU n 
1 48  ARG n 
1 49  VAL n 
1 50  LYS n 
1 51  LEU n 
1 52  LEU n 
1 53  LEU n 
1 54  LYS n 
1 55  ARG n 
1 56  LYS n 
1 57  LEU n 
1 58  ILE n 
1 59  CYS n 
1 60  TYR n 
1 61  ASP n 
1 62  GLY n 
1 63  PHE n 
1 64  GLU n 
1 65  PRO n 
1 66  SER n 
1 67  GLY n 
1 68  ARG n 
1 69  MET n 
1 70  HIS n 
1 71  ILE n 
1 72  ALA n 
1 73  GLN n 
1 74  GLY n 
1 75  LEU n 
1 76  LEU n 
1 77  LYS n 
1 78  SER n 
1 79  ILE n 
1 80  ILE n 
1 81  VAL n 
1 82  ASN n 
1 83  LYS n 
1 84  LEU n 
1 85  THR n 
1 86  SER n 
1 87  ASN n 
1 88  GLY n 
1 89  CYS n 
1 90  THR n 
1 91  PHE n 
1 92  ILE n 
1 93  PHE n 
1 94  TRP n 
1 95  ILE n 
1 96  ALA n 
1 97  ASP n 
1 98  TRP n 
1 99  PHE n 
1 100 ALA n 
1 101 HIS n 
1 102 LEU n 
1 103 ASN n 
1 104 ASN n 
1 105 LYS n 
1 106 MET n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 LEU n 
1 111 LYS n 
1 112 LYS n 
1 113 ILE n 
1 114 LYS n 
1 115 LYS n 
1 116 VAL n 
1 117 GLY n 
1 118 SER n 
1 119 TYR n 
1 120 PHE n 
1 121 ILE n 
1 122 GLU n 
1 123 VAL n 
1 124 TRP n 
1 125 LYS n 
1 126 SER n 
1 127 CYS n 
1 128 GLY n 
1 129 MET n 
1 130 ASN n 
1 131 MET n 
1 132 GLU n 
1 133 ASN n 
1 134 VAL n 
1 135 GLN n 
1 136 PHE n 
1 137 LEU n 
1 138 TRP n 
1 139 ALA n 
1 140 SER n 
1 141 GLU n 
1 142 GLU n 
1 143 ILE n 
1 144 ASN n 
1 145 LYS n 
1 146 LYS n 
1 147 PRO n 
1 148 ASN n 
1 149 GLU n 
1 150 TYR n 
1 151 TRP n 
1 152 SER n 
1 153 LEU n 
1 154 VAL n 
1 155 LEU n 
1 156 ASP n 
1 157 ILE n 
1 158 SER n 
1 159 ARG n 
1 160 SER n 
1 161 PHE n 
1 162 ASN n 
1 163 ILE n 
1 164 ASN n 
1 165 ARG n 
1 166 MET n 
1 167 LYS n 
1 168 ARG n 
1 169 CYS n 
1 170 LEU n 
1 171 LYS n 
1 172 ILE n 
1 173 MET n 
1 174 GLY n 
1 175 ARG n 
1 176 SER n 
1 177 GLU n 
1 178 GLY n 
1 179 GLU n 
1 180 GLU n 
1 181 ASN n 
1 182 TYR n 
1 183 CYS n 
1 184 SER n 
1 185 GLN n 
1 186 ILE n 
1 187 LEU n 
1 188 TYR n 
1 189 PRO n 
1 190 CYS n 
1 191 MET n 
1 192 GLN n 
1 193 CYS n 
1 194 ALA n 
1 195 ASP n 
1 196 ILE n 
1 197 PHE n 
1 198 PHE n 
1 199 LEU n 
1 200 ASN n 
1 201 VAL n 
1 202 ASP n 
1 203 ILE n 
1 204 CYS n 
1 205 GLN n 
1 206 LEU n 
1 207 GLY n 
1 208 ILE n 
1 209 ASP n 
1 210 GLN n 
1 211 ARG n 
1 212 LYS n 
1 213 VAL n 
1 214 ASN n 
1 215 MET n 
1 216 LEU n 
1 217 ALA n 
1 218 ARG n 
1 219 GLU n 
1 220 TYR n 
1 221 CYS n 
1 222 ASP n 
1 223 ILE n 
1 224 LYS n 
1 225 LYS n 
1 226 ILE n 
1 227 LYS n 
1 228 LYS n 
1 229 LYS n 
1 230 PRO n 
1 231 VAL n 
1 232 ILE n 
1 233 LEU n 
1 234 SER n 
1 235 HIS n 
1 236 GLY n 
1 237 MET n 
1 238 LEU n 
1 239 PRO n 
1 240 GLY n 
1 241 LEU n 
1 242 LEU n 
1 243 GLU n 
1 244 GLY n 
1 245 GLN n 
1 246 GLU n 
1 247 LYS n 
1 248 MET n 
1 249 SER n 
1 250 LYS n 
1 251 SER n 
1 252 ASP n 
1 253 GLU n 
1 254 ASN n 
1 255 SER n 
1 256 ALA n 
1 257 ILE n 
1 258 PHE n 
1 259 MET n 
1 260 ASP n 
1 261 ASP n 
1 262 SER n 
1 263 GLU n 
1 264 SER n 
1 265 ASP n 
1 266 VAL n 
1 267 ASN n 
1 268 ARG n 
1 269 LYS n 
1 270 ILE n 
1 271 LYS n 
1 272 LYS n 
1 273 ALA n 
1 274 TYR n 
1 275 CYS n 
1 276 PRO n 
1 277 PRO n 
1 278 ASN n 
1 279 VAL n 
1 280 ILE n 
1 281 GLU n 
1 282 ASN n 
1 283 ASN n 
1 284 PRO n 
1 285 ILE n 
1 286 TYR n 
1 287 ALA n 
1 288 TYR n 
1 289 ALA n 
1 290 LYS n 
1 291 SER n 
1 292 ILE n 
1 293 ILE n 
1 294 PHE n 
1 295 PRO n 
1 296 SER n 
1 297 TYR n 
1 298 ASN n 
1 299 GLU n 
1 300 PHE n 
1 301 ASN n 
1 302 LEU n 
1 303 VAL n 
1 304 ARG n 
1 305 LYS n 
1 306 GLU n 
1 307 LYS n 
1 308 ASN n 
1 309 GLY n 
1 310 GLY n 
1 311 ASP n 
1 312 LYS n 
1 313 THR n 
1 314 TYR n 
1 315 TYR n 
1 316 THR n 
1 317 LEU n 
1 318 GLN n 
1 319 GLU n 
1 320 LEU n 
1 321 GLU n 
1 322 HIS n 
1 323 ASP n 
1 324 TYR n 
1 325 VAL n 
1 326 ASN n 
1 327 GLY n 
1 328 PHE n 
1 329 ILE n 
1 330 HIS n 
1 331 PRO n 
1 332 LEU n 
1 333 ASP n 
1 334 LEU n 
1 335 LYS n 
1 336 ASP n 
1 337 ASN n 
1 338 VAL n 
1 339 ALA n 
1 340 MET n 
1 341 TYR n 
1 342 ILE n 
1 343 ASN n 
1 344 LYS n 
1 345 LEU n 
1 346 LEU n 
1 347 GLN n 
1 348 PRO n 
1 349 VAL n 
1 350 ARG n 
1 351 ASP n 
1 352 HIS n 
1 353 PHE n 
1 354 GLN n 
1 355 ASN n 
1 356 ASN n 
1 357 ILE n 
1 358 GLU n 
1 359 ALA n 
1 360 LYS n 
1 361 ASN n 
1 362 LEU n 
1 363 LEU n 
1 364 ASN n 
1 365 GLU n 
1 366 ILE n 
1 367 LYS n 
1 368 LYS n 
1 369 TYR n 
1 370 LYS n 
1 371 VAL n 
1 372 THR n 
1 373 LYS 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                   373 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PF3D7_0807900 
_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      'Plasmodium falciparum 3D7' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     36329 
_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 
A1AZG non-polymer         . 
;{(2R,3S,4R,5R)-5-[4-amino-3-(propan-2-yl)-1H-pyrazolo[3,4-d]pyrimidin-1-yl]-3,4-dihydroxyoxolan-2-yl}methyl [(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]sulfamate
;
? 'C22 H29 N7 O8 S' 551.573 
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 
CL    non-polymer         . 'CHLORIDE ION' ? 'Cl -1'           35.453  
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 
MLI   non-polymer         . 'MALONATE ION' ? 'C3 H2 O4 -2'     102.046 
NA    non-polymer         . 'SODIUM ION' ? 'Na 1'            22.990  
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLU 2   2   ?   ?   ?   A . n 
A 1 3   THR 3   3   ?   ?   ?   A . n 
A 1 4   THR 4   4   ?   ?   ?   A . n 
A 1 5   ASP 5   5   ?   ?   ?   A . n 
A 1 6   THR 6   6   ?   ?   ?   A . n 
A 1 7   LYS 7   7   ?   ?   ?   A . n 
A 1 8   ARG 8   8   ?   ?   ?   A . n 
A 1 9   GLU 9   9   ?   ?   ?   A . n 
A 1 10  GLU 10  10  ?   ?   ?   A . n 
A 1 11  GLN 11  11  ?   ?   ?   A . n 
A 1 12  GLU 12  12  ?   ?   ?   A . n 
A 1 13  ILE 13  13  ?   ?   ?   A . n 
A 1 14  GLU 14  14  ?   ?   ?   A . n 
A 1 15  GLU 15  15  ?   ?   ?   A . n 
A 1 16  LYS 16  16  ?   ?   ?   A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  GLU 20  20  20  GLU GLU A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  SER 22  22  22  SER SER A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  ASP 26  26  26  ASP ASP A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  ASN 32  32  32  ASN ASN A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ILE 34  34  34  ILE ILE A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  SER 36  36  36  SER SER A . n 
A 1 37  ILE 37  37  37  ILE ILE A . n 
A 1 38  SER 38  38  38  SER SER A . n 
A 1 39  SER 39  39  39  SER SER A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  CYS 41  41  41  CYS CYS A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  GLN 43  43  43  GLN GLN A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  GLU 46  46  46  GLU GLU A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  ARG 48  48  48  ARG ARG A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  LYS 54  54  54  LYS LYS A . n 
A 1 55  ARG 55  55  55  ARG ARG A . n 
A 1 56  LYS 56  56  56  LYS LYS A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ILE 58  58  58  ILE ILE A . n 
A 1 59  CYS 59  59  59  CYS CYS A . n 
A 1 60  TYR 60  60  60  TYR TYR A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  PHE 63  63  63  PHE PHE A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  PRO 65  65  65  PRO PRO A . n 
A 1 66  SER 66  66  66  SER SER A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  MET 69  69  69  MET MET A . n 
A 1 70  HIS 70  70  70  HIS HIS A . n 
A 1 71  ILE 71  71  71  ILE ILE A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  GLN 73  73  73  GLN GLN A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  SER 78  78  78  SER SER A . n 
A 1 79  ILE 79  79  79  ILE ILE A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  ASN 82  82  82  ASN ASN A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  CYS 89  89  89  CYS CYS A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  PHE 91  91  91  PHE PHE A . n 
A 1 92  ILE 92  92  92  ILE ILE A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  TRP 94  94  94  TRP TRP A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  TRP 98  98  98  TRP TRP A . n 
A 1 99  PHE 99  99  99  PHE PHE A . n 
A 1 100 ALA 100 100 100 ALA ALA A . n 
A 1 101 HIS 101 101 101 HIS HIS A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 ASN 104 104 104 ASN ASN A . n 
A 1 105 LYS 105 105 105 LYS LYS A . n 
A 1 106 MET 106 106 106 MET MET A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 LYS 115 115 115 LYS LYS A . n 
A 1 116 VAL 116 116 116 VAL VAL A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 TYR 119 119 119 TYR TYR A . n 
A 1 120 PHE 120 120 120 PHE PHE A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 TRP 124 124 124 TRP TRP A . n 
A 1 125 LYS 125 125 125 LYS LYS A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 CYS 127 127 127 CYS CYS A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 MET 129 129 129 MET MET A . n 
A 1 130 ASN 130 130 130 ASN ASN A . n 
A 1 131 MET 131 131 131 MET MET A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 PHE 136 136 136 PHE PHE A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 TRP 138 138 138 TRP TRP A . n 
A 1 139 ALA 139 139 139 ALA ALA A . n 
A 1 140 SER 140 140 140 SER SER A . n 
A 1 141 GLU 141 141 141 GLU GLU A . n 
A 1 142 GLU 142 142 142 GLU GLU A . n 
A 1 143 ILE 143 143 143 ILE ILE A . n 
A 1 144 ASN 144 144 144 ASN ASN A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 LYS 146 146 146 LYS LYS A . n 
A 1 147 PRO 147 147 147 PRO PRO A . n 
A 1 148 ASN 148 148 148 ASN ASN A . n 
A 1 149 GLU 149 149 149 GLU GLU A . n 
A 1 150 TYR 150 150 150 TYR TYR A . n 
A 1 151 TRP 151 151 151 TRP TRP A . n 
A 1 152 SER 152 152 152 SER SER A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 VAL 154 154 154 VAL VAL A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 ILE 157 157 157 ILE ILE A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 ARG 159 159 159 ARG ARG A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 PHE 161 161 161 PHE PHE A . n 
A 1 162 ASN 162 162 162 ASN ASN A . n 
A 1 163 ILE 163 163 163 ILE ILE A . n 
A 1 164 ASN 164 164 164 ASN ASN A . n 
A 1 165 ARG 165 165 165 ARG ARG A . n 
A 1 166 MET 166 166 166 MET MET A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 ARG 168 168 168 ARG ARG A . n 
A 1 169 CYS 169 169 169 CYS CYS A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 LYS 171 171 171 LYS LYS A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 MET 173 173 173 MET MET A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 ARG 175 175 175 ARG ARG A . n 
A 1 176 SER 176 176 176 SER SER A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 GLU 179 179 179 GLU GLU A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 ASN 181 181 181 ASN ASN A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 CYS 183 183 183 CYS CYS A . n 
A 1 184 SER 184 184 184 SER SER A . n 
A 1 185 GLN 185 185 185 GLN GLN A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 TYR 188 188 188 TYR TYR A . n 
A 1 189 PRO 189 189 189 PRO PRO A . n 
A 1 190 CYS 190 190 190 CYS CYS A . n 
A 1 191 MET 191 191 191 MET MET A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 CYS 193 193 193 CYS CYS A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 PHE 197 197 197 PHE PHE A . n 
A 1 198 PHE 198 198 198 PHE PHE A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 ASN 200 200 200 ASN ASN A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 ASP 202 202 202 ASP ASP A . n 
A 1 203 ILE 203 203 203 ILE ILE A . n 
A 1 204 CYS 204 204 204 CYS CYS A . n 
A 1 205 GLN 205 205 205 GLN GLN A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 GLY 207 207 207 GLY GLY A . n 
A 1 208 ILE 208 208 208 ILE ILE A . n 
A 1 209 ASP 209 209 209 ASP ASP A . n 
A 1 210 GLN 210 210 210 GLN GLN A . n 
A 1 211 ARG 211 211 211 ARG ARG A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 VAL 213 213 213 VAL VAL A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 MET 215 215 215 MET MET A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 ALA 217 217 217 ALA ALA A . n 
A 1 218 ARG 218 218 218 ARG ARG A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 TYR 220 220 220 TYR TYR A . n 
A 1 221 CYS 221 221 221 CYS CYS A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 ILE 223 223 223 ILE ILE A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 LYS 225 225 225 LYS LYS A . n 
A 1 226 ILE 226 226 226 ILE ILE A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 LYS 228 228 228 LYS LYS A . n 
A 1 229 LYS 229 229 229 LYS LYS A . n 
A 1 230 PRO 230 230 230 PRO PRO A . n 
A 1 231 VAL 231 231 231 VAL VAL A . n 
A 1 232 ILE 232 232 232 ILE ILE A . n 
A 1 233 LEU 233 233 233 LEU LEU A . n 
A 1 234 SER 234 234 234 SER SER A . n 
A 1 235 HIS 235 235 235 HIS HIS A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 MET 237 237 237 MET MET A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 GLY 244 244 244 GLY GLY A . n 
A 1 245 GLN 245 245 245 GLN GLN A . n 
A 1 246 GLU 246 246 ?   ?   ?   A . n 
A 1 247 LYS 247 247 ?   ?   ?   A . n 
A 1 248 MET 248 248 ?   ?   ?   A . n 
A 1 249 SER 249 249 ?   ?   ?   A . n 
A 1 250 LYS 250 250 ?   ?   ?   A . n 
A 1 251 SER 251 251 ?   ?   ?   A . n 
A 1 252 ASP 252 252 ?   ?   ?   A . n 
A 1 253 GLU 253 253 253 GLU GLU A . n 
A 1 254 ASN 254 254 254 ASN ASN A . n 
A 1 255 SER 255 255 255 SER SER A . n 
A 1 256 ALA 256 256 256 ALA ALA A . n 
A 1 257 ILE 257 257 257 ILE ILE A . n 
A 1 258 PHE 258 258 258 PHE PHE A . n 
A 1 259 MET 259 259 259 MET MET A . n 
A 1 260 ASP 260 260 260 ASP ASP A . n 
A 1 261 ASP 261 261 261 ASP ASP A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 GLU 263 263 263 GLU GLU A . n 
A 1 264 SER 264 264 264 SER SER A . n 
A 1 265 ASP 265 265 265 ASP ASP A . n 
A 1 266 VAL 266 266 266 VAL VAL A . n 
A 1 267 ASN 267 267 267 ASN ASN A . n 
A 1 268 ARG 268 268 268 ARG ARG A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 ILE 270 270 270 ILE ILE A . n 
A 1 271 LYS 271 271 271 LYS LYS A . n 
A 1 272 LYS 272 272 272 LYS LYS A . n 
A 1 273 ALA 273 273 273 ALA ALA A . n 
A 1 274 TYR 274 274 274 TYR TYR A . n 
A 1 275 CYS 275 275 275 CYS CYS A . n 
A 1 276 PRO 276 276 276 PRO PRO A . n 
A 1 277 PRO 277 277 277 PRO PRO A . n 
A 1 278 ASN 278 278 278 ASN ASN A . n 
A 1 279 VAL 279 279 279 VAL VAL A . n 
A 1 280 ILE 280 280 280 ILE ILE A . n 
A 1 281 GLU 281 281 281 GLU GLU A . n 
A 1 282 ASN 282 282 282 ASN ASN A . n 
A 1 283 ASN 283 283 283 ASN ASN A . n 
A 1 284 PRO 284 284 284 PRO PRO A . n 
A 1 285 ILE 285 285 285 ILE ILE A . n 
A 1 286 TYR 286 286 286 TYR TYR A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 TYR 288 288 288 TYR TYR A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 LYS 290 290 290 LYS LYS A . n 
A 1 291 SER 291 291 291 SER SER A . n 
A 1 292 ILE 292 292 292 ILE ILE A . n 
A 1 293 ILE 293 293 293 ILE ILE A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 PRO 295 295 295 PRO PRO A . n 
A 1 296 SER 296 296 296 SER SER A . n 
A 1 297 TYR 297 297 297 TYR TYR A . n 
A 1 298 ASN 298 298 298 ASN ASN A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 PHE 300 300 300 PHE PHE A . n 
A 1 301 ASN 301 301 301 ASN ASN A . n 
A 1 302 LEU 302 302 302 LEU LEU A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 ARG 304 304 304 ARG ARG A . n 
A 1 305 LYS 305 305 305 LYS LYS A . n 
A 1 306 GLU 306 306 306 GLU GLU A . n 
A 1 307 LYS 307 307 307 LYS LYS A . n 
A 1 308 ASN 308 308 308 ASN ASN A . n 
A 1 309 GLY 309 309 309 GLY GLY A . n 
A 1 310 GLY 310 310 310 GLY GLY A . n 
A 1 311 ASP 311 311 311 ASP ASP A . n 
A 1 312 LYS 312 312 312 LYS LYS A . n 
A 1 313 THR 313 313 313 THR THR A . n 
A 1 314 TYR 314 314 314 TYR TYR A . n 
A 1 315 TYR 315 315 315 TYR TYR A . n 
A 1 316 THR 316 316 316 THR THR A . n 
A 1 317 LEU 317 317 317 LEU LEU A . n 
A 1 318 GLN 318 318 318 GLN GLN A . n 
A 1 319 GLU 319 319 319 GLU GLU A . n 
A 1 320 LEU 320 320 320 LEU LEU A . n 
A 1 321 GLU 321 321 321 GLU GLU A . n 
A 1 322 HIS 322 322 322 HIS HIS A . n 
A 1 323 ASP 323 323 323 ASP ASP A . n 
A 1 324 TYR 324 324 324 TYR TYR A . n 
A 1 325 VAL 325 325 325 VAL VAL A . n 
A 1 326 ASN 326 326 326 ASN ASN A . n 
A 1 327 GLY 327 327 327 GLY GLY A . n 
A 1 328 PHE 328 328 328 PHE PHE A . n 
A 1 329 ILE 329 329 329 ILE ILE A . n 
A 1 330 HIS 330 330 330 HIS HIS A . n 
A 1 331 PRO 331 331 331 PRO PRO A . n 
A 1 332 LEU 332 332 332 LEU LEU A . n 
A 1 333 ASP 333 333 333 ASP ASP A . n 
A 1 334 LEU 334 334 334 LEU LEU A . n 
A 1 335 LYS 335 335 335 LYS LYS A . n 
A 1 336 ASP 336 336 336 ASP ASP A . n 
A 1 337 ASN 337 337 337 ASN ASN A . n 
A 1 338 VAL 338 338 338 VAL VAL A . n 
A 1 339 ALA 339 339 339 ALA ALA A . n 
A 1 340 MET 340 340 340 MET MET A . n 
A 1 341 TYR 341 341 341 TYR TYR A . n 
A 1 342 ILE 342 342 342 ILE ILE A . n 
A 1 343 ASN 343 343 343 ASN ASN A . n 
A 1 344 LYS 344 344 344 LYS LYS A . n 
A 1 345 LEU 345 345 345 LEU LEU A . n 
A 1 346 LEU 346 346 346 LEU LEU A . n 
A 1 347 GLN 347 347 347 GLN GLN A . n 
A 1 348 PRO 348 348 348 PRO PRO A . n 
A 1 349 VAL 349 349 349 VAL VAL A . n 
A 1 350 ARG 350 350 350 ARG ARG A . n 
A 1 351 ASP 351 351 351 ASP ASP A . n 
A 1 352 HIS 352 352 352 HIS HIS A . n 
A 1 353 PHE 353 353 353 PHE PHE A . n 
A 1 354 GLN 354 354 354 GLN GLN A . n 
A 1 355 ASN 355 355 355 ASN ASN A . n 
A 1 356 ASN 356 356 356 ASN ASN A . n 
A 1 357 ILE 357 357 357 ILE ILE A . n 
A 1 358 GLU 358 358 358 GLU GLU A . n 
A 1 359 ALA 359 359 359 ALA ALA A . n 
A 1 360 LYS 360 360 360 LYS LYS A . n 
A 1 361 ASN 361 361 361 ASN ASN A . n 
A 1 362 LEU 362 362 362 LEU LEU A . n 
A 1 363 LEU 363 363 363 LEU LEU A . n 
A 1 364 ASN 364 364 364 ASN ASN A . n 
A 1 365 GLU 365 365 365 GLU GLU A . n 
A 1 366 ILE 366 366 366 ILE ILE A . n 
A 1 367 LYS 367 367 367 LYS LYS A . n 
A 1 368 LYS 368 368 368 LYS LYS A . n 
A 1 369 TYR 369 369 369 TYR TYR A . n 
A 1 370 LYS 370 370 370 LYS LYS A . n 
A 1 371 VAL 371 371 371 VAL VAL A . n 
A 1 372 THR 372 372 372 THR THR A . n 
A 1 373 LYS 373 373 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   GLU 2   2   ?   ?   ?   B . n 
B 1 3   THR 3   3   ?   ?   ?   B . n 
B 1 4   THR 4   4   ?   ?   ?   B . n 
B 1 5   ASP 5   5   ?   ?   ?   B . n 
B 1 6   THR 6   6   ?   ?   ?   B . n 
B 1 7   LYS 7   7   ?   ?   ?   B . n 
B 1 8   ARG 8   8   ?   ?   ?   B . n 
B 1 9   GLU 9   9   ?   ?   ?   B . n 
B 1 10  GLU 10  10  ?   ?   ?   B . n 
B 1 11  GLN 11  11  ?   ?   ?   B . n 
B 1 12  GLU 12  12  ?   ?   ?   B . n 
B 1 13  ILE 13  13  ?   ?   ?   B . n 
B 1 14  GLU 14  14  ?   ?   ?   B . n 
B 1 15  GLU 15  15  ?   ?   ?   B . n 
B 1 16  LYS 16  16  ?   ?   ?   B . n 
B 1 17  LYS 17  17  17  LYS LYS B . n 
B 1 18  ALA 18  18  18  ALA ALA B . n 
B 1 19  GLN 19  19  19  GLN GLN B . n 
B 1 20  GLU 20  20  20  GLU GLU B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  SER 22  22  22  SER SER B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  ILE 24  24  24  ILE ILE B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  ASP 26  26  26  ASP ASP B . n 
B 1 27  VAL 27  27  27  VAL VAL B . n 
B 1 28  ASP 28  28  28  ASP ASP B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  ILE 30  30  30  ILE ILE B . n 
B 1 31  LEU 31  31  31  LEU LEU B . n 
B 1 32  ASN 32  32  32  ASN ASN B . n 
B 1 33  ASP 33  33  33  ASP ASP B . n 
B 1 34  ILE 34  34  34  ILE ILE B . n 
B 1 35  LEU 35  35  35  LEU LEU B . n 
B 1 36  SER 36  36  36  SER SER B . n 
B 1 37  ILE 37  37  37  ILE ILE B . n 
B 1 38  SER 38  38  38  SER SER B . n 
B 1 39  SER 39  39  39  SER SER B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  CYS 41  41  41  CYS CYS B . n 
B 1 42  ILE 42  42  42  ILE ILE B . n 
B 1 43  GLN 43  43  43  GLN GLN B . n 
B 1 44  PRO 44  44  44  PRO PRO B . n 
B 1 45  ASP 45  45  45  ASP ASP B . n 
B 1 46  GLU 46  46  46  GLU GLU B . n 
B 1 47  LEU 47  47  47  LEU LEU B . n 
B 1 48  ARG 48  48  48  ARG ARG B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  LYS 50  50  50  LYS LYS B . n 
B 1 51  LEU 51  51  51  LEU LEU B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  LYS 54  54  54  LYS LYS B . n 
B 1 55  ARG 55  55  55  ARG ARG B . n 
B 1 56  LYS 56  56  56  LYS LYS B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  ILE 58  58  58  ILE ILE B . n 
B 1 59  CYS 59  59  59  CYS CYS B . n 
B 1 60  TYR 60  60  60  TYR TYR B . n 
B 1 61  ASP 61  61  61  ASP ASP B . n 
B 1 62  GLY 62  62  62  GLY GLY B . n 
B 1 63  PHE 63  63  63  PHE PHE B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  PRO 65  65  65  PRO PRO B . n 
B 1 66  SER 66  66  66  SER SER B . n 
B 1 67  GLY 67  67  67  GLY GLY B . n 
B 1 68  ARG 68  68  68  ARG ARG B . n 
B 1 69  MET 69  69  69  MET MET B . n 
B 1 70  HIS 70  70  70  HIS HIS B . n 
B 1 71  ILE 71  71  71  ILE ILE B . n 
B 1 72  ALA 72  72  72  ALA ALA B . n 
B 1 73  GLN 73  73  73  GLN GLN B . n 
B 1 74  GLY 74  74  74  GLY GLY B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  LYS 77  77  77  LYS LYS B . n 
B 1 78  SER 78  78  78  SER SER B . n 
B 1 79  ILE 79  79  79  ILE ILE B . n 
B 1 80  ILE 80  80  80  ILE ILE B . n 
B 1 81  VAL 81  81  81  VAL VAL B . n 
B 1 82  ASN 82  82  82  ASN ASN B . n 
B 1 83  LYS 83  83  83  LYS LYS B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  THR 85  85  85  THR THR B . n 
B 1 86  SER 86  86  86  SER SER B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  GLY 88  88  88  GLY GLY B . n 
B 1 89  CYS 89  89  89  CYS CYS B . n 
B 1 90  THR 90  90  90  THR THR B . n 
B 1 91  PHE 91  91  91  PHE PHE B . n 
B 1 92  ILE 92  92  92  ILE ILE B . n 
B 1 93  PHE 93  93  93  PHE PHE B . n 
B 1 94  TRP 94  94  94  TRP TRP B . n 
B 1 95  ILE 95  95  95  ILE ILE B . n 
B 1 96  ALA 96  96  96  ALA ALA B . n 
B 1 97  ASP 97  97  97  ASP ASP B . n 
B 1 98  TRP 98  98  98  TRP TRP B . n 
B 1 99  PHE 99  99  99  PHE PHE B . n 
B 1 100 ALA 100 100 100 ALA ALA B . n 
B 1 101 HIS 101 101 101 HIS HIS B . n 
B 1 102 LEU 102 102 102 LEU LEU B . n 
B 1 103 ASN 103 103 103 ASN ASN B . n 
B 1 104 ASN 104 104 104 ASN ASN B . n 
B 1 105 LYS 105 105 105 LYS LYS B . n 
B 1 106 MET 106 106 106 MET MET B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 LYS 112 112 112 LYS LYS B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 LYS 114 114 114 LYS LYS B . n 
B 1 115 LYS 115 115 115 LYS LYS B . n 
B 1 116 VAL 116 116 116 VAL VAL B . n 
B 1 117 GLY 117 117 117 GLY GLY B . n 
B 1 118 SER 118 118 118 SER SER B . n 
B 1 119 TYR 119 119 119 TYR TYR B . n 
B 1 120 PHE 120 120 120 PHE PHE B . n 
B 1 121 ILE 121 121 121 ILE ILE B . n 
B 1 122 GLU 122 122 122 GLU GLU B . n 
B 1 123 VAL 123 123 123 VAL VAL B . n 
B 1 124 TRP 124 124 124 TRP TRP B . n 
B 1 125 LYS 125 125 125 LYS LYS B . n 
B 1 126 SER 126 126 126 SER SER B . n 
B 1 127 CYS 127 127 127 CYS CYS B . n 
B 1 128 GLY 128 128 128 GLY GLY B . n 
B 1 129 MET 129 129 129 MET MET B . n 
B 1 130 ASN 130 130 130 ASN ASN B . n 
B 1 131 MET 131 131 131 MET MET B . n 
B 1 132 GLU 132 132 132 GLU GLU B . n 
B 1 133 ASN 133 133 133 ASN ASN B . n 
B 1 134 VAL 134 134 134 VAL VAL B . n 
B 1 135 GLN 135 135 135 GLN GLN B . n 
B 1 136 PHE 136 136 136 PHE PHE B . n 
B 1 137 LEU 137 137 137 LEU LEU B . n 
B 1 138 TRP 138 138 138 TRP TRP B . n 
B 1 139 ALA 139 139 139 ALA ALA B . n 
B 1 140 SER 140 140 140 SER SER B . n 
B 1 141 GLU 141 141 141 GLU GLU B . n 
B 1 142 GLU 142 142 142 GLU GLU B . n 
B 1 143 ILE 143 143 143 ILE ILE B . n 
B 1 144 ASN 144 144 144 ASN ASN B . n 
B 1 145 LYS 145 145 145 LYS LYS B . n 
B 1 146 LYS 146 146 146 LYS LYS B . n 
B 1 147 PRO 147 147 147 PRO PRO B . n 
B 1 148 ASN 148 148 148 ASN ASN B . n 
B 1 149 GLU 149 149 149 GLU GLU B . n 
B 1 150 TYR 150 150 150 TYR TYR B . n 
B 1 151 TRP 151 151 151 TRP TRP B . n 
B 1 152 SER 152 152 152 SER SER B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 VAL 154 154 154 VAL VAL B . n 
B 1 155 LEU 155 155 155 LEU LEU B . n 
B 1 156 ASP 156 156 156 ASP ASP B . n 
B 1 157 ILE 157 157 157 ILE ILE B . n 
B 1 158 SER 158 158 158 SER SER B . n 
B 1 159 ARG 159 159 159 ARG ARG B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 PHE 161 161 161 PHE PHE B . n 
B 1 162 ASN 162 162 162 ASN ASN B . n 
B 1 163 ILE 163 163 163 ILE ILE B . n 
B 1 164 ASN 164 164 164 ASN ASN B . n 
B 1 165 ARG 165 165 165 ARG ARG B . n 
B 1 166 MET 166 166 166 MET MET B . n 
B 1 167 LYS 167 167 167 LYS LYS B . n 
B 1 168 ARG 168 168 168 ARG ARG B . n 
B 1 169 CYS 169 169 169 CYS CYS B . n 
B 1 170 LEU 170 170 170 LEU LEU B . n 
B 1 171 LYS 171 171 171 LYS LYS B . n 
B 1 172 ILE 172 172 172 ILE ILE B . n 
B 1 173 MET 173 173 173 MET MET B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 ARG 175 175 175 ARG ARG B . n 
B 1 176 SER 176 176 176 SER SER B . n 
B 1 177 GLU 177 177 177 GLU GLU B . n 
B 1 178 GLY 178 178 178 GLY GLY B . n 
B 1 179 GLU 179 179 179 GLU GLU B . n 
B 1 180 GLU 180 180 180 GLU GLU B . n 
B 1 181 ASN 181 181 181 ASN ASN B . n 
B 1 182 TYR 182 182 182 TYR TYR B . n 
B 1 183 CYS 183 183 183 CYS CYS B . n 
B 1 184 SER 184 184 184 SER SER B . n 
B 1 185 GLN 185 185 185 GLN GLN B . n 
B 1 186 ILE 186 186 186 ILE ILE B . n 
B 1 187 LEU 187 187 187 LEU LEU B . n 
B 1 188 TYR 188 188 188 TYR TYR B . n 
B 1 189 PRO 189 189 189 PRO PRO B . n 
B 1 190 CYS 190 190 190 CYS CYS B . n 
B 1 191 MET 191 191 191 MET MET B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 CYS 193 193 193 CYS CYS B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 ASP 195 195 195 ASP ASP B . n 
B 1 196 ILE 196 196 196 ILE ILE B . n 
B 1 197 PHE 197 197 197 PHE PHE B . n 
B 1 198 PHE 198 198 198 PHE PHE B . n 
B 1 199 LEU 199 199 199 LEU LEU B . n 
B 1 200 ASN 200 200 200 ASN ASN B . n 
B 1 201 VAL 201 201 201 VAL VAL B . n 
B 1 202 ASP 202 202 202 ASP ASP B . n 
B 1 203 ILE 203 203 203 ILE ILE B . n 
B 1 204 CYS 204 204 204 CYS CYS B . n 
B 1 205 GLN 205 205 205 GLN GLN B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 GLY 207 207 207 GLY GLY B . n 
B 1 208 ILE 208 208 208 ILE ILE B . n 
B 1 209 ASP 209 209 209 ASP ASP B . n 
B 1 210 GLN 210 210 210 GLN GLN B . n 
B 1 211 ARG 211 211 211 ARG ARG B . n 
B 1 212 LYS 212 212 212 LYS LYS B . n 
B 1 213 VAL 213 213 213 VAL VAL B . n 
B 1 214 ASN 214 214 214 ASN ASN B . n 
B 1 215 MET 215 215 215 MET MET B . n 
B 1 216 LEU 216 216 216 LEU LEU B . n 
B 1 217 ALA 217 217 217 ALA ALA B . n 
B 1 218 ARG 218 218 218 ARG ARG B . n 
B 1 219 GLU 219 219 219 GLU GLU B . n 
B 1 220 TYR 220 220 220 TYR TYR B . n 
B 1 221 CYS 221 221 221 CYS CYS B . n 
B 1 222 ASP 222 222 222 ASP ASP B . n 
B 1 223 ILE 223 223 223 ILE ILE B . n 
B 1 224 LYS 224 224 224 LYS LYS B . n 
B 1 225 LYS 225 225 225 LYS LYS B . n 
B 1 226 ILE 226 226 226 ILE ILE B . n 
B 1 227 LYS 227 227 227 LYS LYS B . n 
B 1 228 LYS 228 228 228 LYS LYS B . n 
B 1 229 LYS 229 229 229 LYS LYS B . n 
B 1 230 PRO 230 230 230 PRO PRO B . n 
B 1 231 VAL 231 231 231 VAL VAL B . n 
B 1 232 ILE 232 232 232 ILE ILE B . n 
B 1 233 LEU 233 233 233 LEU LEU B . n 
B 1 234 SER 234 234 234 SER SER B . n 
B 1 235 HIS 235 235 235 HIS HIS B . n 
B 1 236 GLY 236 236 236 GLY GLY B . n 
B 1 237 MET 237 237 237 MET MET B . n 
B 1 238 LEU 238 238 238 LEU LEU B . n 
B 1 239 PRO 239 239 239 PRO PRO B . n 
B 1 240 GLY 240 240 240 GLY GLY B . n 
B 1 241 LEU 241 241 241 LEU LEU B . n 
B 1 242 LEU 242 242 242 LEU LEU B . n 
B 1 243 GLU 243 243 243 GLU GLU B . n 
B 1 244 GLY 244 244 ?   ?   ?   B . n 
B 1 245 GLN 245 245 ?   ?   ?   B . n 
B 1 246 GLU 246 246 ?   ?   ?   B . n 
B 1 247 LYS 247 247 ?   ?   ?   B . n 
B 1 248 MET 248 248 ?   ?   ?   B . n 
B 1 249 SER 249 249 ?   ?   ?   B . n 
B 1 250 LYS 250 250 ?   ?   ?   B . n 
B 1 251 SER 251 251 ?   ?   ?   B . n 
B 1 252 ASP 252 252 ?   ?   ?   B . n 
B 1 253 GLU 253 253 253 GLU GLU B . n 
B 1 254 ASN 254 254 254 ASN ASN B . n 
B 1 255 SER 255 255 255 SER SER B . n 
B 1 256 ALA 256 256 256 ALA ALA B . n 
B 1 257 ILE 257 257 257 ILE ILE B . n 
B 1 258 PHE 258 258 258 PHE PHE B . n 
B 1 259 MET 259 259 259 MET MET B . n 
B 1 260 ASP 260 260 260 ASP ASP B . n 
B 1 261 ASP 261 261 261 ASP ASP B . n 
B 1 262 SER 262 262 262 SER SER B . n 
B 1 263 GLU 263 263 263 GLU GLU B . n 
B 1 264 SER 264 264 264 SER SER B . n 
B 1 265 ASP 265 265 265 ASP ASP B . n 
B 1 266 VAL 266 266 266 VAL VAL B . n 
B 1 267 ASN 267 267 267 ASN ASN B . n 
B 1 268 ARG 268 268 268 ARG ARG B . n 
B 1 269 LYS 269 269 269 LYS LYS B . n 
B 1 270 ILE 270 270 270 ILE ILE B . n 
B 1 271 LYS 271 271 271 LYS LYS B . n 
B 1 272 LYS 272 272 272 LYS LYS B . n 
B 1 273 ALA 273 273 273 ALA ALA B . n 
B 1 274 TYR 274 274 274 TYR TYR B . n 
B 1 275 CYS 275 275 275 CYS CYS B . n 
B 1 276 PRO 276 276 276 PRO PRO B . n 
B 1 277 PRO 277 277 277 PRO PRO B . n 
B 1 278 ASN 278 278 278 ASN ASN B . n 
B 1 279 VAL 279 279 279 VAL VAL B . n 
B 1 280 ILE 280 280 280 ILE ILE B . n 
B 1 281 GLU 281 281 281 GLU GLU B . n 
B 1 282 ASN 282 282 282 ASN ASN B . n 
B 1 283 ASN 283 283 283 ASN ASN B . n 
B 1 284 PRO 284 284 284 PRO PRO B . n 
B 1 285 ILE 285 285 285 ILE ILE B . n 
B 1 286 TYR 286 286 286 TYR TYR B . n 
B 1 287 ALA 287 287 287 ALA ALA B . n 
B 1 288 TYR 288 288 288 TYR TYR B . n 
B 1 289 ALA 289 289 289 ALA ALA B . n 
B 1 290 LYS 290 290 290 LYS LYS B . n 
B 1 291 SER 291 291 291 SER SER B . n 
B 1 292 ILE 292 292 292 ILE ILE B . n 
B 1 293 ILE 293 293 293 ILE ILE B . n 
B 1 294 PHE 294 294 294 PHE PHE B . n 
B 1 295 PRO 295 295 295 PRO PRO B . n 
B 1 296 SER 296 296 296 SER SER B . n 
B 1 297 TYR 297 297 297 TYR TYR B . n 
B 1 298 ASN 298 298 298 ASN ASN B . n 
B 1 299 GLU 299 299 299 GLU GLU B . n 
B 1 300 PHE 300 300 300 PHE PHE B . n 
B 1 301 ASN 301 301 301 ASN ASN B . n 
B 1 302 LEU 302 302 302 LEU LEU B . n 
B 1 303 VAL 303 303 303 VAL VAL B . n 
B 1 304 ARG 304 304 304 ARG ARG B . n 
B 1 305 LYS 305 305 305 LYS LYS B . n 
B 1 306 GLU 306 306 306 GLU GLU B . n 
B 1 307 LYS 307 307 307 LYS LYS B . n 
B 1 308 ASN 308 308 308 ASN ASN B . n 
B 1 309 GLY 309 309 309 GLY GLY B . n 
B 1 310 GLY 310 310 310 GLY GLY B . n 
B 1 311 ASP 311 311 311 ASP ASP B . n 
B 1 312 LYS 312 312 312 LYS LYS B . n 
B 1 313 THR 313 313 313 THR THR B . n 
B 1 314 TYR 314 314 314 TYR TYR B . n 
B 1 315 TYR 315 315 315 TYR TYR B . n 
B 1 316 THR 316 316 316 THR THR B . n 
B 1 317 LEU 317 317 317 LEU LEU B . n 
B 1 318 GLN 318 318 318 GLN GLN B . n 
B 1 319 GLU 319 319 319 GLU GLU B . n 
B 1 320 LEU 320 320 320 LEU LEU B . n 
B 1 321 GLU 321 321 321 GLU GLU B . n 
B 1 322 HIS 322 322 322 HIS HIS B . n 
B 1 323 ASP 323 323 323 ASP ASP B . n 
B 1 324 TYR 324 324 324 TYR TYR B . n 
B 1 325 VAL 325 325 325 VAL VAL B . n 
B 1 326 ASN 326 326 326 ASN ASN B . n 
B 1 327 GLY 327 327 327 GLY GLY B . n 
B 1 328 PHE 328 328 328 PHE PHE B . n 
B 1 329 ILE 329 329 329 ILE ILE B . n 
B 1 330 HIS 330 330 330 HIS HIS B . n 
B 1 331 PRO 331 331 331 PRO PRO B . n 
B 1 332 LEU 332 332 332 LEU LEU B . n 
B 1 333 ASP 333 333 333 ASP ASP B . n 
B 1 334 LEU 334 334 334 LEU LEU B . n 
B 1 335 LYS 335 335 335 LYS LYS B . n 
B 1 336 ASP 336 336 336 ASP ASP B . n 
B 1 337 ASN 337 337 337 ASN ASN B . n 
B 1 338 VAL 338 338 338 VAL VAL B . n 
B 1 339 ALA 339 339 339 ALA ALA B . n 
B 1 340 MET 340 340 340 MET MET B . n 
B 1 341 TYR 341 341 341 TYR TYR B . n 
B 1 342 ILE 342 342 342 ILE ILE B . n 
B 1 343 ASN 343 343 343 ASN ASN B . n 
B 1 344 LYS 344 344 344 LYS LYS B . n 
B 1 345 LEU 345 345 345 LEU LEU B . n 
B 1 346 LEU 346 346 346 LEU LEU B . n 
B 1 347 GLN 347 347 347 GLN GLN B . n 
B 1 348 PRO 348 348 348 PRO PRO B . n 
B 1 349 VAL 349 349 349 VAL VAL B . n 
B 1 350 ARG 350 350 350 ARG ARG B . n 
B 1 351 ASP 351 351 351 ASP ASP B . n 
B 1 352 HIS 352 352 352 HIS HIS B . n 
B 1 353 PHE 353 353 353 PHE PHE B . n 
B 1 354 GLN 354 354 354 GLN GLN B . n 
B 1 355 ASN 355 355 355 ASN ASN B . n 
B 1 356 ASN 356 356 356 ASN ASN B . n 
B 1 357 ILE 357 357 357 ILE ILE B . n 
B 1 358 GLU 358 358 358 GLU GLU B . n 
B 1 359 ALA 359 359 359 ALA ALA B . n 
B 1 360 LYS 360 360 360 LYS LYS B . n 
B 1 361 ASN 361 361 361 ASN ASN B . n 
B 1 362 LEU 362 362 362 LEU LEU B . n 
B 1 363 LEU 363 363 363 LEU LEU B . n 
B 1 364 ASN 364 364 364 ASN ASN B . n 
B 1 365 GLU 365 365 365 GLU GLU B . n 
B 1 366 ILE 366 366 366 ILE ILE B . n 
B 1 367 LYS 367 367 367 LYS LYS B . n 
B 1 368 LYS 368 368 368 LYS LYS B . n 
B 1 369 TYR 369 369 369 TYR TYR B . n 
B 1 370 LYS 370 370 370 LYS LYS B . n 
B 1 371 VAL 371 371 371 VAL VAL B . n 
B 1 372 THR 372 372 372 THR THR B . n 
B 1 373 LYS 373 373 373 LYS LYS B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AZG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AZG 
_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 A1AZG 1   401 401  A1AZG 471 A . 
D 3 MLI   1   402 402  MLI   MLI A . 
E 4 CL    1   403 2    CL    CL  A . 
F 5 NA    1   404 4    NA    NA  A . 
G 2 A1AZG 1   401 401  A1AZG 471 B . 
H 3 MLI   1   402 402  MLI   MLI B . 
I 4 CL    1   403 1    CL    CL  B . 
J 5 NA    1   404 1    NA    NA  B . 
K 5 NA    1   405 2    NA    NA  B . 
L 5 NA    1   406 3    NA    NA  B . 
M 6 HOH   1   501 1408 HOH   HOH A . 
M 6 HOH   2   502 1474 HOH   HOH A . 
M 6 HOH   3   503 66   HOH   HOH A . 
M 6 HOH   4   504 692  HOH   HOH A . 
M 6 HOH   5   505 1481 HOH   HOH A . 
M 6 HOH   6   506 675  HOH   HOH A . 
M 6 HOH   7   507 70   HOH   HOH A . 
M 6 HOH   8   508 409  HOH   HOH A . 
M 6 HOH   9   509 404  HOH   HOH A . 
M 6 HOH   10  510 306  HOH   HOH A . 
M 6 HOH   11  511 1438 HOH   HOH A . 
M 6 HOH   12  512 892  HOH   HOH A . 
M 6 HOH   13  513 176  HOH   HOH A . 
M 6 HOH   14  514 38   HOH   HOH A . 
M 6 HOH   15  515 1419 HOH   HOH A . 
M 6 HOH   16  516 151  HOH   HOH A . 
M 6 HOH   17  517 1204 HOH   HOH A . 
M 6 HOH   18  518 39   HOH   HOH A . 
M 6 HOH   19  519 153  HOH   HOH A . 
M 6 HOH   20  520 504  HOH   HOH A . 
M 6 HOH   21  521 279  HOH   HOH A . 
M 6 HOH   22  522 79   HOH   HOH A . 
M 6 HOH   23  523 280  HOH   HOH A . 
M 6 HOH   24  524 221  HOH   HOH A . 
M 6 HOH   25  525 91   HOH   HOH A . 
M 6 HOH   26  526 1410 HOH   HOH A . 
M 6 HOH   27  527 684  HOH   HOH A . 
M 6 HOH   28  528 82   HOH   HOH A . 
M 6 HOH   29  529 179  HOH   HOH A . 
M 6 HOH   30  530 973  HOH   HOH A . 
M 6 HOH   31  531 1029 HOH   HOH A . 
M 6 HOH   32  532 558  HOH   HOH A . 
M 6 HOH   33  533 84   HOH   HOH A . 
M 6 HOH   34  534 88   HOH   HOH A . 
M 6 HOH   35  535 145  HOH   HOH A . 
M 6 HOH   36  536 804  HOH   HOH A . 
M 6 HOH   37  537 1494 HOH   HOH A . 
M 6 HOH   38  538 96   HOH   HOH A . 
M 6 HOH   39  539 21   HOH   HOH A . 
M 6 HOH   40  540 111  HOH   HOH A . 
M 6 HOH   41  541 37   HOH   HOH A . 
M 6 HOH   42  542 1018 HOH   HOH A . 
M 6 HOH   43  543 445  HOH   HOH A . 
M 6 HOH   44  544 1409 HOH   HOH A . 
M 6 HOH   45  545 99   HOH   HOH A . 
M 6 HOH   46  546 732  HOH   HOH A . 
M 6 HOH   47  547 1450 HOH   HOH A . 
M 6 HOH   48  548 866  HOH   HOH A . 
M 6 HOH   49  549 209  HOH   HOH A . 
M 6 HOH   50  550 1393 HOH   HOH A . 
M 6 HOH   51  551 103  HOH   HOH A . 
M 6 HOH   52  552 321  HOH   HOH A . 
M 6 HOH   53  553 49   HOH   HOH A . 
M 6 HOH   54  554 824  HOH   HOH A . 
M 6 HOH   55  555 1007 HOH   HOH A . 
M 6 HOH   56  556 167  HOH   HOH A . 
M 6 HOH   57  557 102  HOH   HOH A . 
M 6 HOH   58  558 407  HOH   HOH A . 
M 6 HOH   59  559 26   HOH   HOH A . 
M 6 HOH   60  560 297  HOH   HOH A . 
M 6 HOH   61  561 219  HOH   HOH A . 
M 6 HOH   62  562 53   HOH   HOH A . 
M 6 HOH   63  563 165  HOH   HOH A . 
M 6 HOH   64  564 1167 HOH   HOH A . 
M 6 HOH   65  565 19   HOH   HOH A . 
M 6 HOH   66  566 385  HOH   HOH A . 
M 6 HOH   67  567 1454 HOH   HOH A . 
M 6 HOH   68  568 774  HOH   HOH A . 
M 6 HOH   69  569 1484 HOH   HOH A . 
M 6 HOH   70  570 169  HOH   HOH A . 
M 6 HOH   71  571 604  HOH   HOH A . 
M 6 HOH   72  572 875  HOH   HOH A . 
M 6 HOH   73  573 764  HOH   HOH A . 
M 6 HOH   74  574 1422 HOH   HOH A . 
M 6 HOH   75  575 191  HOH   HOH A . 
M 6 HOH   76  576 718  HOH   HOH A . 
M 6 HOH   77  577 1418 HOH   HOH A . 
M 6 HOH   78  578 1455 HOH   HOH A . 
M 6 HOH   79  579 1413 HOH   HOH A . 
M 6 HOH   80  580 707  HOH   HOH A . 
M 6 HOH   81  581 1469 HOH   HOH A . 
M 6 HOH   82  582 193  HOH   HOH A . 
M 6 HOH   83  583 98   HOH   HOH A . 
M 6 HOH   84  584 1472 HOH   HOH A . 
M 6 HOH   85  585 1449 HOH   HOH A . 
M 6 HOH   86  586 1427 HOH   HOH A . 
M 6 HOH   87  587 794  HOH   HOH A . 
M 6 HOH   88  588 206  HOH   HOH A . 
M 6 HOH   89  589 241  HOH   HOH A . 
M 6 HOH   90  590 798  HOH   HOH A . 
M 6 HOH   91  591 526  HOH   HOH A . 
M 6 HOH   92  592 610  HOH   HOH A . 
M 6 HOH   93  593 1463 HOH   HOH A . 
M 6 HOH   94  594 1414 HOH   HOH A . 
M 6 HOH   95  595 891  HOH   HOH A . 
M 6 HOH   96  596 439  HOH   HOH A . 
M 6 HOH   97  597 1483 HOH   HOH A . 
M 6 HOH   98  598 1420 HOH   HOH A . 
M 6 HOH   99  599 94   HOH   HOH A . 
M 6 HOH   100 600 394  HOH   HOH A . 
M 6 HOH   101 601 1113 HOH   HOH A . 
M 6 HOH   102 602 284  HOH   HOH A . 
M 6 HOH   103 603 1435 HOH   HOH A . 
M 6 HOH   104 604 1473 HOH   HOH A . 
M 6 HOH   105 605 1424 HOH   HOH A . 
M 6 HOH   106 606 1482 HOH   HOH A . 
M 6 HOH   107 607 1417 HOH   HOH A . 
M 6 HOH   108 608 491  HOH   HOH A . 
M 6 HOH   109 609 825  HOH   HOH A . 
M 6 HOH   110 610 85   HOH   HOH A . 
M 6 HOH   111 611 1388 HOH   HOH A . 
M 6 HOH   112 612 1467 HOH   HOH A . 
M 6 HOH   113 613 1480 HOH   HOH A . 
M 6 HOH   114 614 1412 HOH   HOH A . 
M 6 HOH   115 615 1154 HOH   HOH A . 
M 6 HOH   116 616 1143 HOH   HOH A . 
M 6 HOH   117 617 1207 HOH   HOH A . 
M 6 HOH   118 618 779  HOH   HOH A . 
M 6 HOH   119 619 906  HOH   HOH A . 
M 6 HOH   120 620 1475 HOH   HOH A . 
M 6 HOH   121 621 1464 HOH   HOH A . 
M 6 HOH   122 622 1421 HOH   HOH A . 
M 6 HOH   123 623 856  HOH   HOH A . 
N 6 HOH   1   501 1489 HOH   HOH B . 
N 6 HOH   2   502 1490 HOH   HOH B . 
N 6 HOH   3   503 772  HOH   HOH B . 
N 6 HOH   4   504 127  HOH   HOH B . 
N 6 HOH   5   505 1453 HOH   HOH B . 
N 6 HOH   6   506 57   HOH   HOH B . 
N 6 HOH   7   507 645  HOH   HOH B . 
N 6 HOH   8   508 1040 HOH   HOH B . 
N 6 HOH   9   509 227  HOH   HOH B . 
N 6 HOH   10  510 882  HOH   HOH B . 
N 6 HOH   11  511 56   HOH   HOH B . 
N 6 HOH   12  512 159  HOH   HOH B . 
N 6 HOH   13  513 36   HOH   HOH B . 
N 6 HOH   14  514 845  HOH   HOH B . 
N 6 HOH   15  515 871  HOH   HOH B . 
N 6 HOH   16  516 109  HOH   HOH B . 
N 6 HOH   17  517 311  HOH   HOH B . 
N 6 HOH   18  518 73   HOH   HOH B . 
N 6 HOH   19  519 113  HOH   HOH B . 
N 6 HOH   20  520 475  HOH   HOH B . 
N 6 HOH   21  521 1479 HOH   HOH B . 
N 6 HOH   22  522 47   HOH   HOH B . 
N 6 HOH   23  523 835  HOH   HOH B . 
N 6 HOH   24  524 188  HOH   HOH B . 
N 6 HOH   25  525 1493 HOH   HOH B . 
N 6 HOH   26  526 161  HOH   HOH B . 
N 6 HOH   27  527 25   HOH   HOH B . 
N 6 HOH   28  528 1396 HOH   HOH B . 
N 6 HOH   29  529 9    HOH   HOH B . 
N 6 HOH   30  530 731  HOH   HOH B . 
N 6 HOH   31  531 1501 HOH   HOH B . 
N 6 HOH   32  532 27   HOH   HOH B . 
N 6 HOH   33  533 122  HOH   HOH B . 
N 6 HOH   34  534 2    HOH   HOH B . 
N 6 HOH   35  535 336  HOH   HOH B . 
N 6 HOH   36  536 50   HOH   HOH B . 
N 6 HOH   37  537 141  HOH   HOH B . 
N 6 HOH   38  538 1434 HOH   HOH B . 
N 6 HOH   39  539 700  HOH   HOH B . 
N 6 HOH   40  540 1440 HOH   HOH B . 
N 6 HOH   41  541 54   HOH   HOH B . 
N 6 HOH   42  542 67   HOH   HOH B . 
N 6 HOH   43  543 158  HOH   HOH B . 
N 6 HOH   44  544 356  HOH   HOH B . 
N 6 HOH   45  545 18   HOH   HOH B . 
N 6 HOH   46  546 55   HOH   HOH B . 
N 6 HOH   47  547 792  HOH   HOH B . 
N 6 HOH   48  548 107  HOH   HOH B . 
N 6 HOH   49  549 960  HOH   HOH B . 
N 6 HOH   50  550 64   HOH   HOH B . 
N 6 HOH   51  551 41   HOH   HOH B . 
N 6 HOH   52  552 12   HOH   HOH B . 
N 6 HOH   53  553 125  HOH   HOH B . 
N 6 HOH   54  554 40   HOH   HOH B . 
N 6 HOH   55  555 273  HOH   HOH B . 
N 6 HOH   56  556 171  HOH   HOH B . 
N 6 HOH   57  557 86   HOH   HOH B . 
N 6 HOH   58  558 1391 HOH   HOH B . 
N 6 HOH   59  559 446  HOH   HOH B . 
N 6 HOH   60  560 108  HOH   HOH B . 
N 6 HOH   61  561 1451 HOH   HOH B . 
N 6 HOH   62  562 16   HOH   HOH B . 
N 6 HOH   63  563 1395 HOH   HOH B . 
N 6 HOH   64  564 1402 HOH   HOH B . 
N 6 HOH   65  565 139  HOH   HOH B . 
N 6 HOH   66  566 6    HOH   HOH B . 
N 6 HOH   67  567 17   HOH   HOH B . 
N 6 HOH   68  568 14   HOH   HOH B . 
N 6 HOH   69  569 676  HOH   HOH B . 
N 6 HOH   70  570 101  HOH   HOH B . 
N 6 HOH   71  571 778  HOH   HOH B . 
N 6 HOH   72  572 796  HOH   HOH B . 
N 6 HOH   73  573 634  HOH   HOH B . 
N 6 HOH   74  574 133  HOH   HOH B . 
N 6 HOH   75  575 224  HOH   HOH B . 
N 6 HOH   76  576 540  HOH   HOH B . 
N 6 HOH   77  577 1458 HOH   HOH B . 
N 6 HOH   78  578 594  HOH   HOH B . 
N 6 HOH   79  579 142  HOH   HOH B . 
N 6 HOH   80  580 29   HOH   HOH B . 
N 6 HOH   81  581 396  HOH   HOH B . 
N 6 HOH   82  582 1445 HOH   HOH B . 
N 6 HOH   83  583 130  HOH   HOH B . 
N 6 HOH   84  584 381  HOH   HOH B . 
N 6 HOH   85  585 7    HOH   HOH B . 
N 6 HOH   86  586 189  HOH   HOH B . 
N 6 HOH   87  587 8    HOH   HOH B . 
N 6 HOH   88  588 430  HOH   HOH B . 
N 6 HOH   89  589 46   HOH   HOH B . 
N 6 HOH   90  590 217  HOH   HOH B . 
N 6 HOH   91  591 760  HOH   HOH B . 
N 6 HOH   92  592 1406 HOH   HOH B . 
N 6 HOH   93  593 134  HOH   HOH B . 
N 6 HOH   94  594 74   HOH   HOH B . 
N 6 HOH   95  595 71   HOH   HOH B . 
N 6 HOH   96  596 132  HOH   HOH B . 
N 6 HOH   97  597 1146 HOH   HOH B . 
N 6 HOH   98  598 851  HOH   HOH B . 
N 6 HOH   99  599 147  HOH   HOH B . 
N 6 HOH   100 600 1503 HOH   HOH B . 
N 6 HOH   101 601 68   HOH   HOH B . 
N 6 HOH   102 602 77   HOH   HOH B . 
N 6 HOH   103 603 81   HOH   HOH B . 
N 6 HOH   104 604 51   HOH   HOH B . 
N 6 HOH   105 605 104  HOH   HOH B . 
N 6 HOH   106 606 78   HOH   HOH B . 
N 6 HOH   107 607 136  HOH   HOH B . 
N 6 HOH   108 608 76   HOH   HOH B . 
N 6 HOH   109 609 11   HOH   HOH B . 
N 6 HOH   110 610 110  HOH   HOH B . 
N 6 HOH   111 611 15   HOH   HOH B . 
N 6 HOH   112 612 605  HOH   HOH B . 
N 6 HOH   113 613 140  HOH   HOH B . 
N 6 HOH   114 614 10   HOH   HOH B . 
N 6 HOH   115 615 106  HOH   HOH B . 
N 6 HOH   116 616 253  HOH   HOH B . 
N 6 HOH   117 617 48   HOH   HOH B . 
N 6 HOH   118 618 649  HOH   HOH B . 
N 6 HOH   119 619 339  HOH   HOH B . 
N 6 HOH   120 620 1461 HOH   HOH B . 
N 6 HOH   121 621 87   HOH   HOH B . 
N 6 HOH   122 622 432  HOH   HOH B . 
N 6 HOH   123 623 1499 HOH   HOH B . 
N 6 HOH   124 624 1496 HOH   HOH B . 
N 6 HOH   125 625 848  HOH   HOH B . 
N 6 HOH   126 626 785  HOH   HOH B . 
N 6 HOH   127 627 652  HOH   HOH B . 
N 6 HOH   128 628 1400 HOH   HOH B . 
N 6 HOH   129 629 318  HOH   HOH B . 
N 6 HOH   130 630 61   HOH   HOH B . 
N 6 HOH   131 631 92   HOH   HOH B . 
N 6 HOH   132 632 1505 HOH   HOH B . 
N 6 HOH   133 633 1462 HOH   HOH B . 
N 6 HOH   134 634 137  HOH   HOH B . 
N 6 HOH   135 635 575  HOH   HOH B . 
N 6 HOH   136 636 745  HOH   HOH B . 
N 6 HOH   137 637 1460 HOH   HOH B . 
N 6 HOH   138 638 596  HOH   HOH B . 
N 6 HOH   139 639 1507 HOH   HOH B . 
N 6 HOH   140 640 80   HOH   HOH B . 
N 6 HOH   141 641 1477 HOH   HOH B . 
N 6 HOH   142 642 307  HOH   HOH B . 
N 6 HOH   143 643 1446 HOH   HOH B . 
N 6 HOH   144 644 152  HOH   HOH B . 
N 6 HOH   145 645 1433 HOH   HOH B . 
N 6 HOH   146 646 157  HOH   HOH B . 
N 6 HOH   147 647 1116 HOH   HOH B . 
N 6 HOH   148 648 1500 HOH   HOH B . 
N 6 HOH   149 649 1389 HOH   HOH B . 
N 6 HOH   150 650 1432 HOH   HOH B . 
N 6 HOH   151 651 1508 HOH   HOH B . 
N 6 HOH   152 652 1430 HOH   HOH B . 
N 6 HOH   153 653 1485 HOH   HOH B . 
N 6 HOH   154 654 784  HOH   HOH B . 
N 6 HOH   155 655 309  HOH   HOH B . 
N 6 HOH   156 656 1390 HOH   HOH B . 
N 6 HOH   157 657 33   HOH   HOH B . 
N 6 HOH   158 658 436  HOH   HOH B . 
N 6 HOH   159 659 617  HOH   HOH B . 
N 6 HOH   160 660 1394 HOH   HOH B . 
N 6 HOH   161 661 72   HOH   HOH B . 
N 6 HOH   162 662 488  HOH   HOH B . 
N 6 HOH   163 663 1466 HOH   HOH B . 
N 6 HOH   164 664 138  HOH   HOH B . 
N 6 HOH   165 665 30   HOH   HOH B . 
N 6 HOH   166 666 1487 HOH   HOH B . 
N 6 HOH   167 667 1506 HOH   HOH B . 
N 6 HOH   168 668 1457 HOH   HOH B . 
N 6 HOH   169 669 448  HOH   HOH B . 
N 6 HOH   170 670 468  HOH   HOH B . 
N 6 HOH   171 671 198  HOH   HOH B . 
N 6 HOH   172 672 23   HOH   HOH B . 
N 6 HOH   173 673 1497 HOH   HOH B . 
N 6 HOH   174 674 388  HOH   HOH B . 
N 6 HOH   175 675 69   HOH   HOH B . 
N 6 HOH   176 676 121  HOH   HOH B . 
N 6 HOH   177 677 706  HOH   HOH B . 
N 6 HOH   178 678 537  HOH   HOH B . 
N 6 HOH   179 679 1448 HOH   HOH B . 
N 6 HOH   180 680 441  HOH   HOH B . 
N 6 HOH   181 681 1439 HOH   HOH B . 
N 6 HOH   182 682 876  HOH   HOH B . 
N 6 HOH   183 683 1456 HOH   HOH B . 
N 6 HOH   184 684 162  HOH   HOH B . 
N 6 HOH   185 685 900  HOH   HOH B . 
N 6 HOH   186 686 315  HOH   HOH B . 
N 6 HOH   187 687 1437 HOH   HOH B . 
N 6 HOH   188 688 1397 HOH   HOH B . 
N 6 HOH   189 689 1431 HOH   HOH B . 
N 6 HOH   190 690 451  HOH   HOH B . 
N 6 HOH   191 691 961  HOH   HOH B . 
N 6 HOH   192 692 194  HOH   HOH B . 
N 6 HOH   193 693 22   HOH   HOH B . 
N 6 HOH   194 694 576  HOH   HOH B . 
N 6 HOH   195 695 115  HOH   HOH B . 
N 6 HOH   196 696 1    HOH   HOH B . 
N 6 HOH   197 697 1079 HOH   HOH B . 
N 6 HOH   198 698 838  HOH   HOH B . 
N 6 HOH   199 699 527  HOH   HOH B . 
N 6 HOH   200 700 820  HOH   HOH B . 
N 6 HOH   201 701 214  HOH   HOH B . 
N 6 HOH   202 702 118  HOH   HOH B . 
N 6 HOH   203 703 1392 HOH   HOH B . 
N 6 HOH   204 704 83   HOH   HOH B . 
N 6 HOH   205 705 1184 HOH   HOH B . 
N 6 HOH   206 706 958  HOH   HOH B . 
N 6 HOH   207 707 1308 HOH   HOH B . 
N 6 HOH   208 708 474  HOH   HOH B . 
N 6 HOH   209 709 828  HOH   HOH B . 
N 6 HOH   210 710 1459 HOH   HOH B . 
N 6 HOH   211 711 1491 HOH   HOH B . 
N 6 HOH   212 712 725  HOH   HOH B . 
N 6 HOH   213 713 116  HOH   HOH B . 
N 6 HOH   214 714 257  HOH   HOH B . 
N 6 HOH   215 715 522  HOH   HOH B . 
N 6 HOH   216 716 1452 HOH   HOH B . 
N 6 HOH   217 717 31   HOH   HOH B . 
N 6 HOH   218 718 254  HOH   HOH B . 
N 6 HOH   219 719 120  HOH   HOH B . 
N 6 HOH   220 720 417  HOH   HOH B . 
N 6 HOH   221 721 274  HOH   HOH B . 
N 6 HOH   222 722 226  HOH   HOH B . 
N 6 HOH   223 723 1361 HOH   HOH B . 
N 6 HOH   224 724 1470 HOH   HOH B . 
N 6 HOH   225 725 768  HOH   HOH B . 
N 6 HOH   226 726 1108 HOH   HOH B . 
N 6 HOH   227 727 1488 HOH   HOH B . 
N 6 HOH   228 728 192  HOH   HOH B . 
N 6 HOH   229 729 237  HOH   HOH B . 
N 6 HOH   230 730 1486 HOH   HOH B . 
N 6 HOH   231 731 1447 HOH   HOH B . 
N 6 HOH   232 732 1387 HOH   HOH B . 
N 6 HOH   233 733 565  HOH   HOH B . 
N 6 HOH   234 734 114  HOH   HOH B . 
N 6 HOH   235 735 287  HOH   HOH B . 
N 6 HOH   236 736 235  HOH   HOH B . 
N 6 HOH   237 737 795  HOH   HOH B . 
N 6 HOH   238 738 535  HOH   HOH B . 
N 6 HOH   239 739 1399 HOH   HOH B . 
N 6 HOH   240 740 1436 HOH   HOH B . 
N 6 HOH   241 741 465  HOH   HOH B . 
N 6 HOH   242 742 150  HOH   HOH B . 
N 6 HOH   243 743 1110 HOH   HOH B . 
N 6 HOH   244 744 821  HOH   HOH B . 
N 6 HOH   245 745 97   HOH   HOH B . 
N 6 HOH   246 746 924  HOH   HOH B . 
N 6 HOH   247 747 1404 HOH   HOH B . 
N 6 HOH   248 748 105  HOH   HOH B . 
N 6 HOH   249 749 1504 HOH   HOH B . 
N 6 HOH   250 750 1502 HOH   HOH B . 
N 6 HOH   251 751 590  HOH   HOH B . 
N 6 HOH   252 752 1444 HOH   HOH B . 
N 6 HOH   253 753 1401 HOH   HOH B . 
N 6 HOH   254 754 1128 HOH   HOH B . 
N 6 HOH   255 755 269  HOH   HOH B . 
N 6 HOH   256 756 1498 HOH   HOH B . 
N 6 HOH   257 757 1495 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.21.1.5286 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   94.628 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CLL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     138.208 
_cell.length_a_esd                 ? 
_cell.length_b                     47.271 
_cell.length_b_esd                 ? 
_cell.length_c                     140.512 
_cell.length_c_esd                 ? 
_cell.volume                       915004.197 
_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                         9CLL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_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                   9CLL 
_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             2.63 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.20 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '2.5M sodium malonate, pH 6' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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         2024-06-04 
_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   0.9537 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9537 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          32.5 
_reflns.entry_id                                       9CLL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.8 
_reflns.d_resolution_low                               46.68 
_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                                     84432 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.8 
_reflns_shell.d_res_low                                     1.82 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4481 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.838 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_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                               50.31 
_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                                 9CLL 
_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                            1.80 
_refine.ls_d_res_low                             46.68 
_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                     84390 
_refine.ls_number_reflns_R_free                  4177 
_refine.ls_number_reflns_R_work                  80213 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.88 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1848 
_refine.ls_R_factor_R_free                       0.2198 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1830 
_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                          1.71 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 24.3284 
_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                            0.2321 
_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                       1.80 
_refine_hist.d_res_low                        46.68 
_refine_hist.number_atoms_solvent             380 
_refine_hist.number_atoms_total               6159 
_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        5683 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         96 
_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' ? 0.0172  ? 5887 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.5031  ? 7926 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0908  ? 854  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0115  ? 1003 ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 19.3965 ? 2265 ? f_dihedral_angle_d ? ? 
# 
_refine_ls_restr_ncs.pdbx_ordinal        1 
_refine_ls_restr_ncs.pdbx_refine_id      'X-RAY DIFFRACTION' 
_refine_ls_restr_ncs.dom_id              d_2 
_refine_ls_restr_ncs.pdbx_ens_id         ens_1 
_refine_ls_restr_ncs.rms_dev_position    1.5136648580524943 
_refine_ls_restr_ncs.weight_position     ? 
_refine_ls_restr_ncs.rms_dev_B_iso       ? 
_refine_ls_restr_ncs.weight_B_iso        ? 
_refine_ls_restr_ncs.pdbx_type           'Torsion NCS' 
_refine_ls_restr_ncs.pdbx_asym_id        A 
_refine_ls_restr_ncs.pdbx_auth_asym_id   A 
_refine_ls_restr_ncs.pdbx_number         ? 
_refine_ls_restr_ncs.pdbx_rms            ? 
_refine_ls_restr_ncs.pdbx_weight         ? 
_refine_ls_restr_ncs.ncs_model_details   ? 
# 
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' 1.80 1.82  . . 136 2698 99.93  . . . . 0.3172 . . . . . . . . . . . 0.3517 
'X-RAY DIFFRACTION' 1.82 1.84  . . 133 2579 99.85  . . . . 0.2993 . . . . . . . . . . . 0.3614 
'X-RAY DIFFRACTION' 1.84 1.86  . . 123 2688 99.82  . . . . 0.2890 . . . . . . . . . . . 0.3484 
'X-RAY DIFFRACTION' 1.86 1.89  . . 163 2626 99.96  . . . . 0.2688 . . . . . . . . . . . 0.2999 
'X-RAY DIFFRACTION' 1.89 1.91  . . 130 2641 99.89  . . . . 0.2493 . . . . . . . . . . . 0.3260 
'X-RAY DIFFRACTION' 1.91 1.94  . . 142 2652 99.96  . . . . 0.2362 . . . . . . . . . . . 0.2860 
'X-RAY DIFFRACTION' 1.94 1.97  . . 153 2699 100.00 . . . . 0.2270 . . . . . . . . . . . 0.2930 
'X-RAY DIFFRACTION' 1.97 2.00  . . 142 2608 99.96  . . . . 0.2200 . . . . . . . . . . . 0.2676 
'X-RAY DIFFRACTION' 2.00 2.03  . . 147 2654 99.79  . . . . 0.2288 . . . . . . . . . . . 0.2669 
'X-RAY DIFFRACTION' 2.03 2.06  . . 140 2665 99.96  . . . . 0.2075 . . . . . . . . . . . 0.2645 
'X-RAY DIFFRACTION' 2.06 2.10  . . 135 2660 100.00 . . . . 0.1916 . . . . . . . . . . . 0.2503 
'X-RAY DIFFRACTION' 2.10 2.13  . . 126 2665 100.00 . . . . 0.1926 . . . . . . . . . . . 0.2599 
'X-RAY DIFFRACTION' 2.13 2.18  . . 158 2640 99.96  . . . . 0.1872 . . . . . . . . . . . 0.2540 
'X-RAY DIFFRACTION' 2.18 2.22  . . 153 2640 99.96  . . . . 0.1877 . . . . . . . . . . . 0.2155 
'X-RAY DIFFRACTION' 2.22 2.27  . . 129 2704 99.96  . . . . 0.1879 . . . . . . . . . . . 0.2413 
'X-RAY DIFFRACTION' 2.27 2.32  . . 137 2641 100.00 . . . . 0.1884 . . . . . . . . . . . 0.2593 
'X-RAY DIFFRACTION' 2.32 2.38  . . 135 2667 99.96  . . . . 0.1849 . . . . . . . . . . . 0.2520 
'X-RAY DIFFRACTION' 2.38 2.44  . . 140 2662 99.82  . . . . 0.1868 . . . . . . . . . . . 0.2225 
'X-RAY DIFFRACTION' 2.44 2.51  . . 113 2716 99.79  . . . . 0.1886 . . . . . . . . . . . 0.2635 
'X-RAY DIFFRACTION' 2.51 2.60  . . 129 2694 99.96  . . . . 0.1982 . . . . . . . . . . . 0.2543 
'X-RAY DIFFRACTION' 2.60 2.69  . . 138 2658 99.96  . . . . 0.2231 . . . . . . . . . . . 0.2549 
'X-RAY DIFFRACTION' 2.69 2.80  . . 135 2688 99.89  . . . . 0.2096 . . . . . . . . . . . 0.2408 
'X-RAY DIFFRACTION' 2.80 2.92  . . 160 2652 99.86  . . . . 0.1959 . . . . . . . . . . . 0.2049 
'X-RAY DIFFRACTION' 2.92 3.08  . . 140 2657 99.89  . . . . 0.1980 . . . . . . . . . . . 0.2137 
'X-RAY DIFFRACTION' 3.08 3.27  . . 144 2694 99.89  . . . . 0.2005 . . . . . . . . . . . 0.2378 
'X-RAY DIFFRACTION' 3.27 3.52  . . 129 2713 99.93  . . . . 0.1804 . . . . . . . . . . . 0.2161 
'X-RAY DIFFRACTION' 3.52 3.88  . . 126 2693 99.72  . . . . 0.1639 . . . . . . . . . . . 0.2210 
'X-RAY DIFFRACTION' 3.88 4.44  . . 140 2717 99.86  . . . . 0.1433 . . . . . . . . . . . 0.1732 
'X-RAY DIFFRACTION' 4.44 5.59  . . 152 2717 99.14  . . . . 0.1514 . . . . . . . . . . . 0.1724 
'X-RAY DIFFRACTION' 5.59 46.68 . . 149 2825 99.77  . . . . 0.1635 . . . . . . . . . . . 0.1825 
# 
_struct_ncs_oper.id             1 
_struct_ncs_oper.code           given 
_struct_ncs_oper.matrix[1][1]   -0.7638535073355611 
_struct_ncs_oper.matrix[1][2]   0.6415370858108327 
_struct_ncs_oper.matrix[1][3]   -0.0704129736661223 
_struct_ncs_oper.matrix[2][1]   0.6245481435955915 
_struct_ncs_oper.matrix[2][2]   0.7072719333096729 
_struct_ncs_oper.matrix[2][3]   -0.3312190041101171 
_struct_ncs_oper.matrix[3][1]   -0.1626881546470494 
_struct_ncs_oper.matrix[3][2]   -0.2969790899739266 
_struct_ncs_oper.matrix[3][3]   -0.9409229428894782 
_struct_ncs_oper.vector[1]      -1.0094459572536056 
_struct_ncs_oper.vector[2]      14.705270512129225 
_struct_ncs_oper.vector[3]      72.9028067428768 
_struct_ncs_oper.details        ? 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
ens_1 d_1 
;(chain "A" and (resid 17 through 243 or resid 253 through 372 or resid 401 through 402))
;
ens_1 d_2 
;(chain "B" and (resid 17 through 372 or resid 401 through 402))
;
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
ens_1 d_1 1 A LYS   17  . A GLU   243 . A LYS   17  A GLU   243 ? ? 
ens_1 d_1 2 A GLU   253 . A THR   372 . A GLU   253 A THR   372 ? ? 
ens_1 d_1 3 C A1AZG .   . C A1AZG .   . A A1AZG 401 A A1AZG 401 ? ? 
ens_1 d_1 4 D MLI   .   . D MLI   .   . A MLI   402 A MLI   402 ? ? 
ens_1 d_2 1 B LYS   17  . B THR   372 . B LYS   17  B THR   372 ? ? 
ens_1 d_2 2 G A1AZG .   . G A1AZG .   . B A1AZG 401 B A1AZG 401 ? ? 
ens_1 d_2 3 H MLI   .   . H MLI   .   . B MLI   402 B MLI   402 ? ? 
# 
_struct_ncs_ens.id        ens_1 
_struct_ncs_ens.details   ? 
# 
_struct_ncs_ens_gen.ens_id     ens_1 
_struct_ncs_ens_gen.dom_id_1   d_2 
_struct_ncs_ens_gen.dom_id_2   d_1 
_struct_ncs_ens_gen.oper_id    1 
# 
_struct.entry_id                     9CLL 
_struct.title                        'Plasmodium falciparum tyrosyl-tRNA synthetase in complex with ML471-Tyr' 
_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        9CLL 
_struct_keywords.text            'Inhibitor complex, LIGASE, LIGASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   LIGASE/INHIBITOR 
# 
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 4 ? 
F N N 5 ? 
G N N 2 ? 
H N N 3 ? 
I N N 4 ? 
J N N 5 ? 
K N N 5 ? 
L N N 5 ? 
M N N 6 ? 
N N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q8IAR7_PLAF7 
_struct_ref.pdbx_db_accession          Q8IAR7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;METTDTKREEQEIEEKKAQEESKIEDVDKILNDILSISSECIQPDELRVKLLLKRKLICYDGFEPSGRMHIAQGLLKSII
VNKLTSNGCTFIFWIADWFAHLNNKMSGDLKKIKKVGSYFIEVWKSCGMNMENVQFLWASEEINKKPNEYWSLVLDISRS
FNINRMKRCLKIMGRSEGEENYCSQILYPCMQCADIFFLNVDICQLGIDQRKVNMLAREYCDIKKIKKKPVILSHGMLPG
LLEGQEKMSKSDENSAIFMDDSESDVNRKIKKAYCPPNVIENNPIYAYAKSIIFPSYNEFNLVRKEKNGGDKTYYTLQEL
EHDYVNGFIHPLDLKDNVAMYINKLLQPVRDHFQNNIEAKNLLNEIKKYKVTK
;
_struct_ref.pdbx_align_begin           1 
# 
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 9CLL A 1 ? 373 ? Q8IAR7 1 ? 373 ? 1 373 
2 1 9CLL B 1 ? 373 ? Q8IAR7 1 ? 373 ? 1 373 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5770  ? 
1 MORE         -80   ? 
1 'SSA (A^2)'  30590 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 LYS A 17  ? ILE A 37  ? LYS A 17  ILE A 37  1 ? 21 
HELX_P HELX_P2  AA2 GLN A 43  ? LEU A 52  ? GLN A 43  LEU A 52  1 ? 10 
HELX_P HELX_P3  AA3 HIS A 70  ? GLN A 73  ? HIS A 70  GLN A 73  5 ? 4  
HELX_P HELX_P4  AA4 GLY A 74  ? SER A 86  ? GLY A 74  SER A 86  1 ? 13 
HELX_P HELX_P5  AA5 ALA A 96  ? ASN A 103 ? ALA A 96  ASN A 103 1 ? 8  
HELX_P HELX_P6  AA6 ASN A 104 ? GLY A 108 ? ASN A 104 GLY A 108 5 ? 5  
HELX_P HELX_P7  AA7 ASP A 109 ? SER A 126 ? ASP A 109 SER A 126 1 ? 18 
HELX_P HELX_P8  AA8 ALA A 139 ? LYS A 146 ? ALA A 139 LYS A 146 1 ? 8  
HELX_P HELX_P9  AA9 LYS A 146 ? PHE A 161 ? LYS A 146 PHE A 161 1 ? 16 
HELX_P HELX_P10 AB1 ASN A 162 ? ARG A 168 ? ASN A 162 ARG A 168 1 ? 7  
HELX_P HELX_P11 AB2 CYS A 169 ? GLY A 174 ? CYS A 169 GLY A 174 5 ? 6  
HELX_P HELX_P12 AB3 CYS A 183 ? LEU A 199 ? CYS A 183 LEU A 199 1 ? 17 
HELX_P HELX_P13 AB4 GLY A 207 ? ASP A 209 ? GLY A 207 ASP A 209 5 ? 3  
HELX_P HELX_P14 AB5 GLN A 210 ? LYS A 225 ? GLN A 210 LYS A 225 1 ? 16 
HELX_P HELX_P15 AB6 SER A 262 ? LYS A 272 ? SER A 262 LYS A 272 1 ? 11 
HELX_P HELX_P16 AB7 ASN A 283 ? ILE A 292 ? ASN A 283 ILE A 292 1 ? 10 
HELX_P HELX_P17 AB8 ILE A 292 ? ASN A 298 ? ILE A 292 ASN A 298 1 ? 7  
HELX_P HELX_P18 AB9 LYS A 305 ? GLY A 309 ? LYS A 305 GLY A 309 5 ? 5  
HELX_P HELX_P19 AC1 THR A 316 ? ASN A 326 ? THR A 316 ASN A 326 1 ? 11 
HELX_P HELX_P20 AC2 HIS A 330 ? ASN A 356 ? HIS A 330 ASN A 356 1 ? 27 
HELX_P HELX_P21 AC3 ASN A 356 ? LYS A 368 ? ASN A 356 LYS A 368 1 ? 13 
HELX_P HELX_P22 AC4 ALA B 18  ? ILE B 37  ? ALA B 18  ILE B 37  1 ? 20 
HELX_P HELX_P23 AC5 GLN B 43  ? LEU B 53  ? GLN B 43  LEU B 53  1 ? 11 
HELX_P HELX_P24 AC6 HIS B 70  ? GLN B 73  ? HIS B 70  GLN B 73  5 ? 4  
HELX_P HELX_P25 AC7 GLY B 74  ? ASN B 87  ? GLY B 74  ASN B 87  1 ? 14 
HELX_P HELX_P26 AC8 ALA B 96  ? ASN B 103 ? ALA B 96  ASN B 103 1 ? 8  
HELX_P HELX_P27 AC9 ASN B 104 ? GLY B 108 ? ASN B 104 GLY B 108 5 ? 5  
HELX_P HELX_P28 AD1 ASP B 109 ? CYS B 127 ? ASP B 109 CYS B 127 1 ? 19 
HELX_P HELX_P29 AD2 ALA B 139 ? LYS B 146 ? ALA B 139 LYS B 146 1 ? 8  
HELX_P HELX_P30 AD3 LYS B 146 ? PHE B 161 ? LYS B 146 PHE B 161 1 ? 16 
HELX_P HELX_P31 AD4 ASN B 162 ? ARG B 168 ? ASN B 162 ARG B 168 1 ? 7  
HELX_P HELX_P32 AD5 CYS B 169 ? GLY B 174 ? CYS B 169 GLY B 174 5 ? 6  
HELX_P HELX_P33 AD6 CYS B 183 ? LEU B 199 ? CYS B 183 LEU B 199 1 ? 17 
HELX_P HELX_P34 AD7 GLY B 207 ? ASP B 209 ? GLY B 207 ASP B 209 5 ? 3  
HELX_P HELX_P35 AD8 GLN B 210 ? LYS B 225 ? GLN B 210 LYS B 225 1 ? 16 
HELX_P HELX_P36 AD9 SER B 262 ? LYS B 272 ? SER B 262 LYS B 272 1 ? 11 
HELX_P HELX_P37 AE1 ASN B 283 ? ILE B 292 ? ASN B 283 ILE B 292 1 ? 10 
HELX_P HELX_P38 AE2 ILE B 292 ? ASN B 298 ? ILE B 292 ASN B 298 1 ? 7  
HELX_P HELX_P39 AE3 LYS B 305 ? GLY B 309 ? LYS B 305 GLY B 309 5 ? 5  
HELX_P HELX_P40 AE4 THR B 316 ? ASN B 326 ? THR B 316 ASN B 326 1 ? 11 
HELX_P HELX_P41 AE5 HIS B 330 ? ASN B 356 ? HIS B 330 ASN B 356 1 ? 27 
HELX_P HELX_P42 AE6 ASN B 356 ? LYS B 368 ? ASN B 356 LYS B 368 1 ? 13 
# 
_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 ? ? C A1AZG .   O23 ? ? ? 1_555 F NA  . NA ? ? A A1AZG 401 A NA  404 1_555 ? ? ? ? ? ? ? 2.360 ? ? 
metalc2  metalc ? ? C A1AZG .   O25 ? ? ? 1_555 F NA  . NA ? ? A A1AZG 401 A NA  404 1_555 ? ? ? ? ? ? ? 2.436 ? ? 
metalc3  metalc ? ? F NA    .   NA  ? ? ? 1_555 M HOH . O  ? ? A NA    404 A HOH 526 1_555 ? ? ? ? ? ? ? 2.295 ? ? 
metalc4  metalc ? ? F NA    .   NA  ? ? ? 1_555 M HOH . O  ? ? A NA    404 A HOH 544 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
metalc5  metalc ? ? F NA    .   NA  ? ? ? 1_555 M HOH . O  ? ? A NA    404 A HOH 579 1_555 ? ? ? ? ? ? ? 2.334 ? ? 
metalc6  metalc ? ? F NA    .   NA  ? ? ? 1_555 M HOH . O  ? ? A NA    404 A HOH 614 1_555 ? ? ? ? ? ? ? 2.419 ? ? 
metalc7  metalc ? ? B MET   131 O   ? ? ? 1_555 K NA  . NA ? ? B MET   131 B NA  405 1_555 ? ? ? ? ? ? ? 2.324 ? ? 
metalc8  metalc ? ? B GLU   132 OE1 ? ? ? 1_555 J NA  . NA ? ? B GLU   132 B NA  404 4_556 ? ? ? ? ? ? ? 2.481 ? ? 
metalc9  metalc ? ? B VAL   134 O   ? ? ? 1_555 K NA  . NA ? ? B VAL   134 B NA  405 1_555 ? ? ? ? ? ? ? 2.360 ? ? 
metalc10 metalc ? ? B ARG   304 O   ? ? ? 1_555 J NA  . NA ? ? B ARG   304 B NA  404 1_555 ? ? ? ? ? ? ? 2.367 ? ? 
metalc11 metalc ? ? B ASP   311 OD1 ? ? ? 1_555 J NA  . NA ? ? B ASP   311 B NA  404 1_555 ? ? ? ? ? ? ? 2.464 ? ? 
metalc12 metalc ? ? G A1AZG .   O23 ? ? ? 1_555 L NA  . NA ? ? B A1AZG 401 B NA  406 1_555 ? ? ? ? ? ? ? 2.355 ? ? 
metalc13 metalc ? ? G A1AZG .   O25 ? ? ? 1_555 L NA  . NA ? ? B A1AZG 401 B NA  406 1_555 ? ? ? ? ? ? ? 2.435 ? ? 
metalc14 metalc ? ? J NA    .   NA  ? ? ? 1_555 N HOH . O  ? ? B NA    404 B HOH 554 4_546 ? ? ? ? ? ? ? 2.495 ? ? 
metalc15 metalc ? ? J NA    .   NA  ? ? ? 1_555 N HOH . O  ? ? B NA    404 B HOH 628 1_555 ? ? ? ? ? ? ? 2.500 ? ? 
metalc16 metalc ? ? J NA    .   NA  ? ? ? 1_555 N HOH . O  ? ? B NA    404 B HOH 687 1_555 ? ? ? ? ? ? ? 2.391 ? ? 
metalc17 metalc ? ? K NA    .   NA  ? ? ? 1_555 N HOH . O  ? ? B NA    405 B HOH 545 1_555 ? ? ? ? ? ? ? 2.677 ? ? 
metalc18 metalc ? ? K NA    .   NA  ? ? ? 1_555 N HOH . O  ? ? B NA    405 B HOH 637 1_555 ? ? ? ? ? ? ? 2.481 ? ? 
metalc19 metalc ? ? K NA    .   NA  ? ? ? 1_555 N HOH . O  ? ? B NA    405 B HOH 698 1_555 ? ? ? ? ? ? ? 2.373 ? ? 
metalc20 metalc ? ? K NA    .   NA  ? ? ? 1_555 N HOH . O  ? ? B NA    405 B HOH 710 1_555 ? ? ? ? ? ? ? 2.244 ? ? 
metalc21 metalc ? ? L NA    .   NA  ? ? ? 1_555 N HOH . O  ? ? B NA    406 B HOH 558 1_555 ? ? ? ? ? ? ? 2.463 ? ? 
metalc22 metalc ? ? L NA    .   NA  ? ? ? 1_555 N HOH . O  ? ? B NA    406 B HOH 649 1_555 ? ? ? ? ? ? ? 2.295 ? ? 
metalc23 metalc ? ? L NA    .   NA  ? ? ? 1_555 N HOH . O  ? ? B NA    406 B HOH 656 1_555 ? ? ? ? ? ? ? 2.363 ? ? 
metalc24 metalc ? ? L NA    .   NA  ? ? ? 1_555 N HOH . O  ? ? B NA    406 B HOH 703 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
# 
_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  O23 ? C A1AZG .   ? A A1AZG 401 ? 1_555 NA ? F NA . ? A NA 404 ? 1_555 O25 ? C A1AZG .   ? A A1AZG 401 ? 1_555 75.4  ? 
2  O23 ? C A1AZG .   ? A A1AZG 401 ? 1_555 NA ? F NA . ? A NA 404 ? 1_555 O   ? M HOH   .   ? A HOH   526 ? 1_555 95.1  ? 
3  O25 ? C A1AZG .   ? A A1AZG 401 ? 1_555 NA ? F NA . ? A NA 404 ? 1_555 O   ? M HOH   .   ? A HOH   526 ? 1_555 85.8  ? 
4  O23 ? C A1AZG .   ? A A1AZG 401 ? 1_555 NA ? F NA . ? A NA 404 ? 1_555 O   ? M HOH   .   ? A HOH   544 ? 1_555 100.4 ? 
5  O25 ? C A1AZG .   ? A A1AZG 401 ? 1_555 NA ? F NA . ? A NA 404 ? 1_555 O   ? M HOH   .   ? A HOH   544 ? 1_555 159.6 ? 
6  O   ? M HOH   .   ? A HOH   526 ? 1_555 NA ? F NA . ? A NA 404 ? 1_555 O   ? M HOH   .   ? A HOH   544 ? 1_555 74.6  ? 
7  O23 ? C A1AZG .   ? A A1AZG 401 ? 1_555 NA ? F NA . ? A NA 404 ? 1_555 O   ? M HOH   .   ? A HOH   579 ? 1_555 77.2  ? 
8  O25 ? C A1AZG .   ? A A1AZG 401 ? 1_555 NA ? F NA . ? A NA 404 ? 1_555 O   ? M HOH   .   ? A HOH   579 ? 1_555 94.9  ? 
9  O   ? M HOH   .   ? A HOH   526 ? 1_555 NA ? F NA . ? A NA 404 ? 1_555 O   ? M HOH   .   ? A HOH   579 ? 1_555 171.8 ? 
10 O   ? M HOH   .   ? A HOH   544 ? 1_555 NA ? F NA . ? A NA 404 ? 1_555 O   ? M HOH   .   ? A HOH   579 ? 1_555 103.7 ? 
11 O23 ? C A1AZG .   ? A A1AZG 401 ? 1_555 NA ? F NA . ? A NA 404 ? 1_555 O   ? M HOH   .   ? A HOH   614 ? 1_555 156.2 ? 
12 O25 ? C A1AZG .   ? A A1AZG 401 ? 1_555 NA ? F NA . ? A NA 404 ? 1_555 O   ? M HOH   .   ? A HOH   614 ? 1_555 87.6  ? 
13 O   ? M HOH   .   ? A HOH   526 ? 1_555 NA ? F NA . ? A NA 404 ? 1_555 O   ? M HOH   .   ? A HOH   614 ? 1_555 100.2 ? 
14 O   ? M HOH   .   ? A HOH   544 ? 1_555 NA ? F NA . ? A NA 404 ? 1_555 O   ? M HOH   .   ? A HOH   614 ? 1_555 101.2 ? 
15 O   ? M HOH   .   ? A HOH   579 ? 1_555 NA ? F NA . ? A NA 404 ? 1_555 O   ? M HOH   .   ? A HOH   614 ? 1_555 88.0  ? 
16 O   ? B MET   131 ? B MET   131 ? 1_555 NA ? K NA . ? B NA 405 ? 1_555 O   ? B VAL   134 ? B VAL   134 ? 1_555 90.1  ? 
17 O   ? B MET   131 ? B MET   131 ? 1_555 NA ? K NA . ? B NA 405 ? 1_555 O   ? N HOH   .   ? B HOH   545 ? 1_555 75.8  ? 
18 O   ? B VAL   134 ? B VAL   134 ? 1_555 NA ? K NA . ? B NA 405 ? 1_555 O   ? N HOH   .   ? B HOH   545 ? 1_555 97.3  ? 
19 O   ? B MET   131 ? B MET   131 ? 1_555 NA ? K NA . ? B NA 405 ? 1_555 O   ? N HOH   .   ? B HOH   637 ? 1_555 102.9 ? 
20 O   ? B VAL   134 ? B VAL   134 ? 1_555 NA ? K NA . ? B NA 405 ? 1_555 O   ? N HOH   .   ? B HOH   637 ? 1_555 84.5  ? 
21 O   ? N HOH   .   ? B HOH   545 ? 1_555 NA ? K NA . ? B NA 405 ? 1_555 O   ? N HOH   .   ? B HOH   637 ? 1_555 177.8 ? 
22 O   ? B MET   131 ? B MET   131 ? 1_555 NA ? K NA . ? B NA 405 ? 1_555 O   ? N HOH   .   ? B HOH   698 ? 1_555 87.7  ? 
23 O   ? B VAL   134 ? B VAL   134 ? 1_555 NA ? K NA . ? B NA 405 ? 1_555 O   ? N HOH   .   ? B HOH   698 ? 1_555 166.8 ? 
24 O   ? N HOH   .   ? B HOH   545 ? 1_555 NA ? K NA . ? B NA 405 ? 1_555 O   ? N HOH   .   ? B HOH   698 ? 1_555 94.8  ? 
25 O   ? N HOH   .   ? B HOH   637 ? 1_555 NA ? K NA . ? B NA 405 ? 1_555 O   ? N HOH   .   ? B HOH   698 ? 1_555 83.3  ? 
26 O   ? B MET   131 ? B MET   131 ? 1_555 NA ? K NA . ? B NA 405 ? 1_555 O   ? N HOH   .   ? B HOH   710 ? 1_555 156.2 ? 
27 O   ? B VAL   134 ? B VAL   134 ? 1_555 NA ? K NA . ? B NA 405 ? 1_555 O   ? N HOH   .   ? B HOH   710 ? 1_555 100.1 ? 
28 O   ? N HOH   .   ? B HOH   545 ? 1_555 NA ? K NA . ? B NA 405 ? 1_555 O   ? N HOH   .   ? B HOH   710 ? 1_555 81.6  ? 
29 O   ? N HOH   .   ? B HOH   637 ? 1_555 NA ? K NA . ? B NA 405 ? 1_555 O   ? N HOH   .   ? B HOH   710 ? 1_555 99.5  ? 
30 O   ? N HOH   .   ? B HOH   698 ? 1_555 NA ? K NA . ? B NA 405 ? 1_555 O   ? N HOH   .   ? B HOH   710 ? 1_555 86.9  ? 
31 OE1 ? B GLU   132 ? B GLU   132 ? 1_555 NA ? J NA . ? B NA 404 ? 4_556 O   ? B ARG   304 ? B ARG   304 ? 1_555 63.7  ? 
32 OE1 ? B GLU   132 ? B GLU   132 ? 1_555 NA ? J NA . ? B NA 404 ? 4_556 OD1 ? B ASP   311 ? B ASP   311 ? 1_555 65.7  ? 
33 O   ? B ARG   304 ? B ARG   304 ? 1_555 NA ? J NA . ? B NA 404 ? 4_556 OD1 ? B ASP   311 ? B ASP   311 ? 1_555 2.0   ? 
34 OE1 ? B GLU   132 ? B GLU   132 ? 1_555 NA ? J NA . ? B NA 404 ? 4_556 O   ? N HOH   .   ? B HOH   554 ? 4_546 67.1  ? 
35 O   ? B ARG   304 ? B ARG   304 ? 1_555 NA ? J NA . ? B NA 404 ? 4_556 O   ? N HOH   .   ? B HOH   554 ? 4_546 4.0   ? 
36 OD1 ? B ASP   311 ? B ASP   311 ? 1_555 NA ? J NA . ? B NA 404 ? 4_556 O   ? N HOH   .   ? B HOH   554 ? 4_546 2.6   ? 
37 OE1 ? B GLU   132 ? B GLU   132 ? 1_555 NA ? J NA . ? B NA 404 ? 4_556 O   ? N HOH   .   ? B HOH   628 ? 1_555 68.9  ? 
38 O   ? B ARG   304 ? B ARG   304 ? 1_555 NA ? J NA . ? B NA 404 ? 4_556 O   ? N HOH   .   ? B HOH   628 ? 1_555 5.9   ? 
39 OD1 ? B ASP   311 ? B ASP   311 ? 1_555 NA ? J NA . ? B NA 404 ? 4_556 O   ? N HOH   .   ? B HOH   628 ? 1_555 4.3   ? 
40 O   ? N HOH   .   ? B HOH   554 ? 4_546 NA ? J NA . ? B NA 404 ? 4_556 O   ? N HOH   .   ? B HOH   628 ? 1_555 1.9   ? 
41 OE1 ? B GLU   132 ? B GLU   132 ? 1_555 NA ? J NA . ? B NA 404 ? 4_556 O   ? N HOH   .   ? B HOH   687 ? 1_555 64.5  ? 
42 O   ? B ARG   304 ? B ARG   304 ? 1_555 NA ? J NA . ? B NA 404 ? 4_556 O   ? N HOH   .   ? B HOH   687 ? 1_555 3.9   ? 
43 OD1 ? B ASP   311 ? B ASP   311 ? 1_555 NA ? J NA . ? B NA 404 ? 4_556 O   ? N HOH   .   ? B HOH   687 ? 1_555 4.2   ? 
44 O   ? N HOH   .   ? B HOH   554 ? 4_546 NA ? J NA . ? B NA 404 ? 4_556 O   ? N HOH   .   ? B HOH   687 ? 1_555 3.2   ? 
45 O   ? N HOH   .   ? B HOH   628 ? 1_555 NA ? J NA . ? B NA 404 ? 4_556 O   ? N HOH   .   ? B HOH   687 ? 1_555 4.6   ? 
46 O23 ? G A1AZG .   ? B A1AZG 401 ? 1_555 NA ? L NA . ? B NA 406 ? 1_555 O25 ? G A1AZG .   ? B A1AZG 401 ? 1_555 78.5  ? 
47 O23 ? G A1AZG .   ? B A1AZG 401 ? 1_555 NA ? L NA . ? B NA 406 ? 1_555 O   ? N HOH   .   ? B HOH   558 ? 1_555 93.1  ? 
48 O25 ? G A1AZG .   ? B A1AZG 401 ? 1_555 NA ? L NA . ? B NA 406 ? 1_555 O   ? N HOH   .   ? B HOH   558 ? 1_555 84.6  ? 
49 O23 ? G A1AZG .   ? B A1AZG 401 ? 1_555 NA ? L NA . ? B NA 406 ? 1_555 O   ? N HOH   .   ? B HOH   649 ? 1_555 93.9  ? 
50 O25 ? G A1AZG .   ? B A1AZG 401 ? 1_555 NA ? L NA . ? B NA 406 ? 1_555 O   ? N HOH   .   ? B HOH   649 ? 1_555 159.1 ? 
51 O   ? N HOH   .   ? B HOH   558 ? 1_555 NA ? L NA . ? B NA 406 ? 1_555 O   ? N HOH   .   ? B HOH   649 ? 1_555 76.2  ? 
52 O23 ? G A1AZG .   ? B A1AZG 401 ? 1_555 NA ? L NA . ? B NA 406 ? 1_555 O   ? N HOH   .   ? B HOH   656 ? 1_555 81.9  ? 
53 O25 ? G A1AZG .   ? B A1AZG 401 ? 1_555 NA ? L NA . ? B NA 406 ? 1_555 O   ? N HOH   .   ? B HOH   656 ? 1_555 99.2  ? 
54 O   ? N HOH   .   ? B HOH   558 ? 1_555 NA ? L NA . ? B NA 406 ? 1_555 O   ? N HOH   .   ? B HOH   656 ? 1_555 172.9 ? 
55 O   ? N HOH   .   ? B HOH   649 ? 1_555 NA ? L NA . ? B NA 406 ? 1_555 O   ? N HOH   .   ? B HOH   656 ? 1_555 99.0  ? 
56 O23 ? G A1AZG .   ? B A1AZG 401 ? 1_555 NA ? L NA . ? B NA 406 ? 1_555 O   ? N HOH   .   ? B HOH   703 ? 1_555 162.1 ? 
57 O25 ? G A1AZG .   ? B A1AZG 401 ? 1_555 NA ? L NA . ? B NA 406 ? 1_555 O   ? N HOH   .   ? B HOH   703 ? 1_555 88.2  ? 
58 O   ? N HOH   .   ? B HOH   558 ? 1_555 NA ? L NA . ? B NA 406 ? 1_555 O   ? N HOH   .   ? B HOH   703 ? 1_555 97.6  ? 
59 O   ? N HOH   .   ? B HOH   649 ? 1_555 NA ? L NA . ? B NA 406 ? 1_555 O   ? N HOH   .   ? B HOH   703 ? 1_555 102.5 ? 
60 O   ? N HOH   .   ? B HOH   656 ? 1_555 NA ? L NA . ? B NA 406 ? 1_555 O   ? N HOH   .   ? B HOH   703 ? 1_555 88.5  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ILE 42 A . ? ILE 42 A GLN 43 A ? GLN 43 A 1 -9.04  
2 ILE 42 B . ? ILE 42 B GLN 43 B ? GLN 43 B 1 -10.16 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 6 ? 
AA4 ? 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 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA4 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 GLU A 40  ? ILE A 42  ? GLU A 40  ILE A 42  
AA1 2 VAL A 231 ? SER A 234 ? VAL A 231 SER A 234 
AA1 3 ILE A 203 ? CYS A 204 ? ILE A 203 CYS A 204 
AA1 4 LEU A 57  ? PHE A 63  ? LEU A 57  PHE A 63  
AA1 5 CYS A 89  ? ILE A 95  ? CYS A 89  ILE A 95  
AA1 6 VAL A 134 ? TRP A 138 ? VAL A 134 TRP A 138 
AA2 1 PHE A 300 ? LEU A 302 ? PHE A 300 LEU A 302 
AA2 2 LYS A 312 ? TYR A 314 ? LYS A 312 TYR A 314 
AA3 1 GLU B 40  ? ILE B 42  ? GLU B 40  ILE B 42  
AA3 2 VAL B 231 ? SER B 234 ? VAL B 231 SER B 234 
AA3 3 ILE B 203 ? CYS B 204 ? ILE B 203 CYS B 204 
AA3 4 ILE B 58  ? PHE B 63  ? ILE B 58  PHE B 63  
AA3 5 THR B 90  ? ILE B 95  ? THR B 90  ILE B 95  
AA3 6 VAL B 134 ? TRP B 138 ? VAL B 134 TRP B 138 
AA4 1 PHE B 300 ? LEU B 302 ? PHE B 300 LEU B 302 
AA4 2 LYS B 312 ? TYR B 314 ? LYS B 312 TYR B 314 
# 
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 ILE A 42  ? N ILE A 42  O ILE A 232 ? O ILE A 232 
AA1 2 3 O VAL A 231 ? O VAL A 231 N CYS A 204 ? N CYS A 204 
AA1 3 4 N ILE A 203 ? N ILE A 203 O ILE A 58  ? O ILE A 58  
AA1 4 5 N CYS A 59  ? N CYS A 59  O THR A 90  ? O THR A 90  
AA1 5 6 N PHE A 93  ? N PHE A 93  O GLN A 135 ? O GLN A 135 
AA2 1 2 N LEU A 302 ? N LEU A 302 O LYS A 312 ? O LYS A 312 
AA3 1 2 N ILE B 42  ? N ILE B 42  O ILE B 232 ? O ILE B 232 
AA3 2 3 O VAL B 231 ? O VAL B 231 N CYS B 204 ? N CYS B 204 
AA3 3 4 N ILE B 203 ? N ILE B 203 O ILE B 58  ? O ILE B 58  
AA3 4 5 N CYS B 59  ? N CYS B 59  O ILE B 92  ? O ILE B 92  
AA3 5 6 N ILE B 95  ? N ILE B 95  O LEU B 137 ? O LEU B 137 
AA4 1 2 N LEU B 302 ? N LEU B 302 O LYS B 312 ? O LYS B 312 
# 
_pdbx_entry_details.entry_id                   9CLL 
_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 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   B HOH 632 ? ? O   B HOH 667 ? ? 1.91 
2  1 OD1 A ASP 26  ? ? O   A HOH 501 ? ? 2.00 
3  1 O   B LEU 35  ? ? O   B HOH 501 ? ? 2.05 
4  1 OD1 B ASN 254 ? ? NH1 B ARG 268 ? ? 2.06 
5  1 NZ  A LYS 171 ? ? O   A HOH 502 ? ? 2.07 
6  1 NE2 A GLN 347 ? ? OD2 A ASP 351 ? ? 2.07 
7  1 O   B ASN 32  ? ? O   B HOH 502 ? ? 2.11 
8  1 O   A HOH 511 ? ? O   A HOH 578 ? ? 2.17 
9  1 NZ  A LYS 56  ? ? O   A HOH 503 ? ? 2.17 
10 1 O   B ASP 33  ? ? OG  B SER 36  ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 OD1 A ASN 361 ? ? 1_555 OD1 A ASN 361 ? ? 2_555 1.99 
2 1 O   B HOH 530 ? ? 1_555 O   B HOH 547 ? ? 4_546 2.06 
3 1 NZ  A LYS 228 ? ? 1_555 OE1 B GLU 20  ? ? 3_455 2.16 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              97 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_2              97 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             OD1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_3              97 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                124.97 
_pdbx_validate_rmsd_angle.angle_target_value         118.30 
_pdbx_validate_rmsd_angle.angle_deviation            6.67 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.90 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 96  ? ? -91.92  59.90 
2 1 LYS A 146 ? ? -140.60 59.14 
3 1 ASN A 298 ? ? 53.92   17.38 
4 1 ALA B 18  ? ? 88.84   -0.75 
5 1 LYS B 146 ? ? -140.25 59.70 
6 1 GLN B 205 ? ? -118.19 78.00 
7 1 CYS B 275 ? ? -154.59 73.55 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     697 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   N 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 -x,y,-z         
3 x+1/2,y+1/2,z   
4 -x+1/2,y+1/2,-z 
# 
_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         -2.5313305347518327 
_pdbx_refine_tls.origin_y         -0.8840572344560979 
_pdbx_refine_tls.origin_z         39.27176643647724 
_pdbx_refine_tls.T[1][1]          0.20772189955704853 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.005414554471691008 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0076010382049863205 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.36084058352957193 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0069099430198070935 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.2921189473710107 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.7590217302785468 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.3153025465252438 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.7971287507161685 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.5254196234415375 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.3859819869326225 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.2192803992719754 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0760033112584318 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.01813075895240059 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.15072082286854005 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.10229631506403263 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.07467473687632961 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.12972279024716343 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.05949364387377611 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.14492188848825902 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.13140297990417235 
_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   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     17 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   M 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    E 
_pdbx_refine_tls_group.end_auth_seq_id     4 
_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 MET 1   ? A MET 1   
2  1 Y 1 A GLU 2   ? A GLU 2   
3  1 Y 1 A THR 3   ? A THR 3   
4  1 Y 1 A THR 4   ? A THR 4   
5  1 Y 1 A ASP 5   ? A ASP 5   
6  1 Y 1 A THR 6   ? A THR 6   
7  1 Y 1 A LYS 7   ? A LYS 7   
8  1 Y 1 A ARG 8   ? A ARG 8   
9  1 Y 1 A GLU 9   ? A GLU 9   
10 1 Y 1 A GLU 10  ? A GLU 10  
11 1 Y 1 A GLN 11  ? A GLN 11  
12 1 Y 1 A GLU 12  ? A GLU 12  
13 1 Y 1 A ILE 13  ? A ILE 13  
14 1 Y 1 A GLU 14  ? A GLU 14  
15 1 Y 1 A GLU 15  ? A GLU 15  
16 1 Y 1 A LYS 16  ? A LYS 16  
17 1 Y 1 A GLU 246 ? A GLU 246 
18 1 Y 1 A LYS 247 ? A LYS 247 
19 1 Y 1 A MET 248 ? A MET 248 
20 1 Y 1 A SER 249 ? A SER 249 
21 1 Y 1 A LYS 250 ? A LYS 250 
22 1 Y 1 A SER 251 ? A SER 251 
23 1 Y 1 A ASP 252 ? A ASP 252 
24 1 Y 1 A LYS 373 ? A LYS 373 
25 1 Y 1 B MET 1   ? B MET 1   
26 1 Y 1 B GLU 2   ? B GLU 2   
27 1 Y 1 B THR 3   ? B THR 3   
28 1 Y 1 B THR 4   ? B THR 4   
29 1 Y 1 B ASP 5   ? B ASP 5   
30 1 Y 1 B THR 6   ? B THR 6   
31 1 Y 1 B LYS 7   ? B LYS 7   
32 1 Y 1 B ARG 8   ? B ARG 8   
33 1 Y 1 B GLU 9   ? B GLU 9   
34 1 Y 1 B GLU 10  ? B GLU 10  
35 1 Y 1 B GLN 11  ? B GLN 11  
36 1 Y 1 B GLU 12  ? B GLU 12  
37 1 Y 1 B ILE 13  ? B ILE 13  
38 1 Y 1 B GLU 14  ? B GLU 14  
39 1 Y 1 B GLU 15  ? B GLU 15  
40 1 Y 1 B LYS 16  ? B LYS 16  
41 1 Y 1 B GLY 244 ? B GLY 244 
42 1 Y 1 B GLN 245 ? B GLN 245 
43 1 Y 1 B GLU 246 ? B GLU 246 
44 1 Y 1 B LYS 247 ? B LYS 247 
45 1 Y 1 B MET 248 ? B MET 248 
46 1 Y 1 B SER 249 ? B SER 249 
47 1 Y 1 B LYS 250 ? B LYS 250 
48 1 Y 1 B SER 251 ? B SER 251 
49 1 Y 1 B ASP 252 ? B ASP 252 
# 
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 
A1AZG C02  C  N R 1   
A1AZG C03  C  N R 2   
A1AZG C05  C  N R 3   
A1AZG C06  C  N S 4   
A1AZG C08  C  N N 5   
A1AZG C12  C  N N 6   
A1AZG C13  C  N S 7   
A1AZG C15  C  N N 8   
A1AZG C16  C  Y N 9   
A1AZG C17  C  Y N 10  
A1AZG C18  C  Y N 11  
A1AZG C19  C  Y N 12  
A1AZG C20  C  Y N 13  
A1AZG C21  C  Y N 14  
A1AZG C27  C  Y N 15  
A1AZG C29  C  Y N 16  
A1AZG C31  C  Y N 17  
A1AZG C33  C  Y N 18  
A1AZG C34  C  Y N 19  
A1AZG C35  C  N N 20  
A1AZG C36  C  N N 21  
A1AZG C37  C  N N 22  
A1AZG N11  N  N N 23  
A1AZG N14  N  N N 24  
A1AZG N26  N  Y N 25  
A1AZG N28  N  Y N 26  
A1AZG N30  N  Y N 27  
A1AZG N32  N  N N 28  
A1AZG N38  N  Y N 29  
A1AZG O01  O  N N 30  
A1AZG O04  O  N N 31  
A1AZG O07  O  N N 32  
A1AZG O09  O  N N 33  
A1AZG O22  O  N N 34  
A1AZG O23  O  N N 35  
A1AZG O24  O  N N 36  
A1AZG O25  O  N N 37  
A1AZG S10  S  N N 38  
A1AZG H021 H  N N 39  
A1AZG H031 H  N N 40  
A1AZG H051 H  N N 41  
A1AZG H061 H  N N 42  
A1AZG H082 H  N N 43  
A1AZG H081 H  N N 44  
A1AZG H131 H  N N 45  
A1AZG H151 H  N N 46  
A1AZG H152 H  N N 47  
A1AZG H171 H  N N 48  
A1AZG H181 H  N N 49  
A1AZG H201 H  N N 50  
A1AZG H211 H  N N 51  
A1AZG H291 H  N N 52  
A1AZG H351 H  N N 53  
A1AZG H362 H  N N 54  
A1AZG H363 H  N N 55  
A1AZG H361 H  N N 56  
A1AZG H373 H  N N 57  
A1AZG H372 H  N N 58  
A1AZG H371 H  N N 59  
A1AZG H111 H  N N 60  
A1AZG H142 H  N N 61  
A1AZG H141 H  N N 62  
A1AZG H321 H  N N 63  
A1AZG H322 H  N N 64  
A1AZG H011 H  N N 65  
A1AZG H071 H  N N 66  
A1AZG H221 H  N N 67  
ALA   N    N  N N 68  
ALA   CA   C  N S 69  
ALA   C    C  N N 70  
ALA   O    O  N N 71  
ALA   CB   C  N N 72  
ALA   OXT  O  N N 73  
ALA   H    H  N N 74  
ALA   H2   H  N N 75  
ALA   HA   H  N N 76  
ALA   HB1  H  N N 77  
ALA   HB2  H  N N 78  
ALA   HB3  H  N N 79  
ALA   HXT  H  N N 80  
ARG   N    N  N N 81  
ARG   CA   C  N S 82  
ARG   C    C  N N 83  
ARG   O    O  N N 84  
ARG   CB   C  N N 85  
ARG   CG   C  N N 86  
ARG   CD   C  N N 87  
ARG   NE   N  N N 88  
ARG   CZ   C  N N 89  
ARG   NH1  N  N N 90  
ARG   NH2  N  N N 91  
ARG   OXT  O  N N 92  
ARG   H    H  N N 93  
ARG   H2   H  N N 94  
ARG   HA   H  N N 95  
ARG   HB2  H  N N 96  
ARG   HB3  H  N N 97  
ARG   HG2  H  N N 98  
ARG   HG3  H  N N 99  
ARG   HD2  H  N N 100 
ARG   HD3  H  N N 101 
ARG   HE   H  N N 102 
ARG   HH11 H  N N 103 
ARG   HH12 H  N N 104 
ARG   HH21 H  N N 105 
ARG   HH22 H  N N 106 
ARG   HXT  H  N N 107 
ASN   N    N  N N 108 
ASN   CA   C  N S 109 
ASN   C    C  N N 110 
ASN   O    O  N N 111 
ASN   CB   C  N N 112 
ASN   CG   C  N N 113 
ASN   OD1  O  N N 114 
ASN   ND2  N  N N 115 
ASN   OXT  O  N N 116 
ASN   H    H  N N 117 
ASN   H2   H  N N 118 
ASN   HA   H  N N 119 
ASN   HB2  H  N N 120 
ASN   HB3  H  N N 121 
ASN   HD21 H  N N 122 
ASN   HD22 H  N N 123 
ASN   HXT  H  N N 124 
ASP   N    N  N N 125 
ASP   CA   C  N S 126 
ASP   C    C  N N 127 
ASP   O    O  N N 128 
ASP   CB   C  N N 129 
ASP   CG   C  N N 130 
ASP   OD1  O  N N 131 
ASP   OD2  O  N N 132 
ASP   OXT  O  N N 133 
ASP   H    H  N N 134 
ASP   H2   H  N N 135 
ASP   HA   H  N N 136 
ASP   HB2  H  N N 137 
ASP   HB3  H  N N 138 
ASP   HD2  H  N N 139 
ASP   HXT  H  N N 140 
CL    CL   CL N N 141 
CYS   N    N  N N 142 
CYS   CA   C  N R 143 
CYS   C    C  N N 144 
CYS   O    O  N N 145 
CYS   CB   C  N N 146 
CYS   SG   S  N N 147 
CYS   OXT  O  N N 148 
CYS   H    H  N N 149 
CYS   H2   H  N N 150 
CYS   HA   H  N N 151 
CYS   HB2  H  N N 152 
CYS   HB3  H  N N 153 
CYS   HG   H  N N 154 
CYS   HXT  H  N N 155 
GLN   N    N  N N 156 
GLN   CA   C  N S 157 
GLN   C    C  N N 158 
GLN   O    O  N N 159 
GLN   CB   C  N N 160 
GLN   CG   C  N N 161 
GLN   CD   C  N N 162 
GLN   OE1  O  N N 163 
GLN   NE2  N  N N 164 
GLN   OXT  O  N N 165 
GLN   H    H  N N 166 
GLN   H2   H  N N 167 
GLN   HA   H  N N 168 
GLN   HB2  H  N N 169 
GLN   HB3  H  N N 170 
GLN   HG2  H  N N 171 
GLN   HG3  H  N N 172 
GLN   HE21 H  N N 173 
GLN   HE22 H  N N 174 
GLN   HXT  H  N N 175 
GLU   N    N  N N 176 
GLU   CA   C  N S 177 
GLU   C    C  N N 178 
GLU   O    O  N N 179 
GLU   CB   C  N N 180 
GLU   CG   C  N N 181 
GLU   CD   C  N N 182 
GLU   OE1  O  N N 183 
GLU   OE2  O  N N 184 
GLU   OXT  O  N N 185 
GLU   H    H  N N 186 
GLU   H2   H  N N 187 
GLU   HA   H  N N 188 
GLU   HB2  H  N N 189 
GLU   HB3  H  N N 190 
GLU   HG2  H  N N 191 
GLU   HG3  H  N N 192 
GLU   HE2  H  N N 193 
GLU   HXT  H  N N 194 
GLY   N    N  N N 195 
GLY   CA   C  N N 196 
GLY   C    C  N N 197 
GLY   O    O  N N 198 
GLY   OXT  O  N N 199 
GLY   H    H  N N 200 
GLY   H2   H  N N 201 
GLY   HA2  H  N N 202 
GLY   HA3  H  N N 203 
GLY   HXT  H  N N 204 
HIS   N    N  N N 205 
HIS   CA   C  N S 206 
HIS   C    C  N N 207 
HIS   O    O  N N 208 
HIS   CB   C  N N 209 
HIS   CG   C  Y N 210 
HIS   ND1  N  Y N 211 
HIS   CD2  C  Y N 212 
HIS   CE1  C  Y N 213 
HIS   NE2  N  Y N 214 
HIS   OXT  O  N N 215 
HIS   H    H  N N 216 
HIS   H2   H  N N 217 
HIS   HA   H  N N 218 
HIS   HB2  H  N N 219 
HIS   HB3  H  N N 220 
HIS   HD1  H  N N 221 
HIS   HD2  H  N N 222 
HIS   HE1  H  N N 223 
HIS   HE2  H  N N 224 
HIS   HXT  H  N N 225 
HOH   O    O  N N 226 
HOH   H1   H  N N 227 
HOH   H2   H  N N 228 
ILE   N    N  N N 229 
ILE   CA   C  N S 230 
ILE   C    C  N N 231 
ILE   O    O  N N 232 
ILE   CB   C  N S 233 
ILE   CG1  C  N N 234 
ILE   CG2  C  N N 235 
ILE   CD1  C  N N 236 
ILE   OXT  O  N N 237 
ILE   H    H  N N 238 
ILE   H2   H  N N 239 
ILE   HA   H  N N 240 
ILE   HB   H  N N 241 
ILE   HG12 H  N N 242 
ILE   HG13 H  N N 243 
ILE   HG21 H  N N 244 
ILE   HG22 H  N N 245 
ILE   HG23 H  N N 246 
ILE   HD11 H  N N 247 
ILE   HD12 H  N N 248 
ILE   HD13 H  N N 249 
ILE   HXT  H  N N 250 
LEU   N    N  N N 251 
LEU   CA   C  N S 252 
LEU   C    C  N N 253 
LEU   O    O  N N 254 
LEU   CB   C  N N 255 
LEU   CG   C  N N 256 
LEU   CD1  C  N N 257 
LEU   CD2  C  N N 258 
LEU   OXT  O  N N 259 
LEU   H    H  N N 260 
LEU   H2   H  N N 261 
LEU   HA   H  N N 262 
LEU   HB2  H  N N 263 
LEU   HB3  H  N N 264 
LEU   HG   H  N N 265 
LEU   HD11 H  N N 266 
LEU   HD12 H  N N 267 
LEU   HD13 H  N N 268 
LEU   HD21 H  N N 269 
LEU   HD22 H  N N 270 
LEU   HD23 H  N N 271 
LEU   HXT  H  N N 272 
LYS   N    N  N N 273 
LYS   CA   C  N S 274 
LYS   C    C  N N 275 
LYS   O    O  N N 276 
LYS   CB   C  N N 277 
LYS   CG   C  N N 278 
LYS   CD   C  N N 279 
LYS   CE   C  N N 280 
LYS   NZ   N  N N 281 
LYS   OXT  O  N N 282 
LYS   H    H  N N 283 
LYS   H2   H  N N 284 
LYS   HA   H  N N 285 
LYS   HB2  H  N N 286 
LYS   HB3  H  N N 287 
LYS   HG2  H  N N 288 
LYS   HG3  H  N N 289 
LYS   HD2  H  N N 290 
LYS   HD3  H  N N 291 
LYS   HE2  H  N N 292 
LYS   HE3  H  N N 293 
LYS   HZ1  H  N N 294 
LYS   HZ2  H  N N 295 
LYS   HZ3  H  N N 296 
LYS   HXT  H  N N 297 
MET   N    N  N N 298 
MET   CA   C  N S 299 
MET   C    C  N N 300 
MET   O    O  N N 301 
MET   CB   C  N N 302 
MET   CG   C  N N 303 
MET   SD   S  N N 304 
MET   CE   C  N N 305 
MET   OXT  O  N N 306 
MET   H    H  N N 307 
MET   H2   H  N N 308 
MET   HA   H  N N 309 
MET   HB2  H  N N 310 
MET   HB3  H  N N 311 
MET   HG2  H  N N 312 
MET   HG3  H  N N 313 
MET   HE1  H  N N 314 
MET   HE2  H  N N 315 
MET   HE3  H  N N 316 
MET   HXT  H  N N 317 
MLI   C1   C  N N 318 
MLI   C2   C  N N 319 
MLI   C3   C  N N 320 
MLI   O6   O  N N 321 
MLI   O7   O  N N 322 
MLI   O8   O  N N 323 
MLI   O9   O  N N 324 
MLI   H11  H  N N 325 
MLI   H12  H  N N 326 
NA    NA   NA N N 327 
PHE   N    N  N N 328 
PHE   CA   C  N S 329 
PHE   C    C  N N 330 
PHE   O    O  N N 331 
PHE   CB   C  N N 332 
PHE   CG   C  Y N 333 
PHE   CD1  C  Y N 334 
PHE   CD2  C  Y N 335 
PHE   CE1  C  Y N 336 
PHE   CE2  C  Y N 337 
PHE   CZ   C  Y N 338 
PHE   OXT  O  N N 339 
PHE   H    H  N N 340 
PHE   H2   H  N N 341 
PHE   HA   H  N N 342 
PHE   HB2  H  N N 343 
PHE   HB3  H  N N 344 
PHE   HD1  H  N N 345 
PHE   HD2  H  N N 346 
PHE   HE1  H  N N 347 
PHE   HE2  H  N N 348 
PHE   HZ   H  N N 349 
PHE   HXT  H  N N 350 
PRO   N    N  N N 351 
PRO   CA   C  N S 352 
PRO   C    C  N N 353 
PRO   O    O  N N 354 
PRO   CB   C  N N 355 
PRO   CG   C  N N 356 
PRO   CD   C  N N 357 
PRO   OXT  O  N N 358 
PRO   H    H  N N 359 
PRO   HA   H  N N 360 
PRO   HB2  H  N N 361 
PRO   HB3  H  N N 362 
PRO   HG2  H  N N 363 
PRO   HG3  H  N N 364 
PRO   HD2  H  N N 365 
PRO   HD3  H  N N 366 
PRO   HXT  H  N N 367 
SER   N    N  N N 368 
SER   CA   C  N S 369 
SER   C    C  N N 370 
SER   O    O  N N 371 
SER   CB   C  N N 372 
SER   OG   O  N N 373 
SER   OXT  O  N N 374 
SER   H    H  N N 375 
SER   H2   H  N N 376 
SER   HA   H  N N 377 
SER   HB2  H  N N 378 
SER   HB3  H  N N 379 
SER   HG   H  N N 380 
SER   HXT  H  N N 381 
THR   N    N  N N 382 
THR   CA   C  N S 383 
THR   C    C  N N 384 
THR   O    O  N N 385 
THR   CB   C  N R 386 
THR   OG1  O  N N 387 
THR   CG2  C  N N 388 
THR   OXT  O  N N 389 
THR   H    H  N N 390 
THR   H2   H  N N 391 
THR   HA   H  N N 392 
THR   HB   H  N N 393 
THR   HG1  H  N N 394 
THR   HG21 H  N N 395 
THR   HG22 H  N N 396 
THR   HG23 H  N N 397 
THR   HXT  H  N N 398 
TRP   N    N  N N 399 
TRP   CA   C  N S 400 
TRP   C    C  N N 401 
TRP   O    O  N N 402 
TRP   CB   C  N N 403 
TRP   CG   C  Y N 404 
TRP   CD1  C  Y N 405 
TRP   CD2  C  Y N 406 
TRP   NE1  N  Y N 407 
TRP   CE2  C  Y N 408 
TRP   CE3  C  Y N 409 
TRP   CZ2  C  Y N 410 
TRP   CZ3  C  Y N 411 
TRP   CH2  C  Y N 412 
TRP   OXT  O  N N 413 
TRP   H    H  N N 414 
TRP   H2   H  N N 415 
TRP   HA   H  N N 416 
TRP   HB2  H  N N 417 
TRP   HB3  H  N N 418 
TRP   HD1  H  N N 419 
TRP   HE1  H  N N 420 
TRP   HE3  H  N N 421 
TRP   HZ2  H  N N 422 
TRP   HZ3  H  N N 423 
TRP   HH2  H  N N 424 
TRP   HXT  H  N N 425 
TYR   N    N  N N 426 
TYR   CA   C  N S 427 
TYR   C    C  N N 428 
TYR   O    O  N N 429 
TYR   CB   C  N N 430 
TYR   CG   C  Y N 431 
TYR   CD1  C  Y N 432 
TYR   CD2  C  Y N 433 
TYR   CE1  C  Y N 434 
TYR   CE2  C  Y N 435 
TYR   CZ   C  Y N 436 
TYR   OH   O  N N 437 
TYR   OXT  O  N N 438 
TYR   H    H  N N 439 
TYR   H2   H  N N 440 
TYR   HA   H  N N 441 
TYR   HB2  H  N N 442 
TYR   HB3  H  N N 443 
TYR   HD1  H  N N 444 
TYR   HD2  H  N N 445 
TYR   HE1  H  N N 446 
TYR   HE2  H  N N 447 
TYR   HH   H  N N 448 
TYR   HXT  H  N N 449 
VAL   N    N  N N 450 
VAL   CA   C  N S 451 
VAL   C    C  N N 452 
VAL   O    O  N N 453 
VAL   CB   C  N N 454 
VAL   CG1  C  N N 455 
VAL   CG2  C  N N 456 
VAL   OXT  O  N N 457 
VAL   H    H  N N 458 
VAL   H2   H  N N 459 
VAL   HA   H  N N 460 
VAL   HB   H  N N 461 
VAL   HG11 H  N N 462 
VAL   HG12 H  N N 463 
VAL   HG13 H  N N 464 
VAL   HG21 H  N N 465 
VAL   HG22 H  N N 466 
VAL   HG23 H  N N 467 
VAL   HXT  H  N N 468 
# 
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 
A1AZG N32 C31  sing N N 1   
A1AZG C31 N30  doub Y N 2   
A1AZG C31 C33  sing Y N 3   
A1AZG N30 C29  sing Y N 4   
A1AZG C37 C35  sing N N 5   
A1AZG C35 C34  sing N N 6   
A1AZG C35 C36  sing N N 7   
A1AZG C29 N28  doub Y N 8   
A1AZG C33 C34  sing Y N 9   
A1AZG C33 C27  doub Y N 10  
A1AZG C34 N38  doub Y N 11  
A1AZG C27 N28  sing Y N 12  
A1AZG C27 N26  sing Y N 13  
A1AZG N38 N26  sing Y N 14  
A1AZG N26 C03  sing N N 15  
A1AZG O04 C03  sing N N 16  
A1AZG O04 C05  sing N N 17  
A1AZG O24 S10  doub N N 18  
A1AZG C03 C02  sing N N 19  
A1AZG C08 O09  sing N N 20  
A1AZG C08 C05  sing N N 21  
A1AZG O09 S10  sing N N 22  
A1AZG C05 C06  sing N N 23  
A1AZG O25 S10  doub N N 24  
A1AZG S10 N11  sing N N 25  
A1AZG C02 C06  sing N N 26  
A1AZG C02 O01  sing N N 27  
A1AZG C06 O07  sing N N 28  
A1AZG N11 C12  sing N N 29  
A1AZG O23 C12  doub N N 30  
A1AZG C12 C13  sing N N 31  
A1AZG C15 C13  sing N N 32  
A1AZG C15 C16  sing N N 33  
A1AZG C13 N14  sing N N 34  
A1AZG C16 C21  doub Y N 35  
A1AZG C16 C17  sing Y N 36  
A1AZG C21 C20  sing Y N 37  
A1AZG C17 C18  doub Y N 38  
A1AZG C20 C19  doub Y N 39  
A1AZG C18 C19  sing Y N 40  
A1AZG C19 O22  sing N N 41  
A1AZG C02 H021 sing N N 42  
A1AZG C03 H031 sing N N 43  
A1AZG C05 H051 sing N N 44  
A1AZG C06 H061 sing N N 45  
A1AZG C08 H082 sing N N 46  
A1AZG C08 H081 sing N N 47  
A1AZG C13 H131 sing N N 48  
A1AZG C15 H151 sing N N 49  
A1AZG C15 H152 sing N N 50  
A1AZG C17 H171 sing N N 51  
A1AZG C18 H181 sing N N 52  
A1AZG C20 H201 sing N N 53  
A1AZG C21 H211 sing N N 54  
A1AZG C29 H291 sing N N 55  
A1AZG C35 H351 sing N N 56  
A1AZG C36 H362 sing N N 57  
A1AZG C36 H363 sing N N 58  
A1AZG C36 H361 sing N N 59  
A1AZG C37 H373 sing N N 60  
A1AZG C37 H372 sing N N 61  
A1AZG C37 H371 sing N N 62  
A1AZG N11 H111 sing N N 63  
A1AZG N14 H142 sing N N 64  
A1AZG N14 H141 sing N N 65  
A1AZG N32 H321 sing N N 66  
A1AZG N32 H322 sing N N 67  
A1AZG O01 H011 sing N N 68  
A1AZG O07 H071 sing N N 69  
A1AZG O22 H221 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 
MLI   C1  C2   sing N N 307 
MLI   C1  C3   sing N N 308 
MLI   C1  H11  sing N N 309 
MLI   C1  H12  sing N N 310 
MLI   C2  O6   doub N N 311 
MLI   C2  O7   sing N N 312 
MLI   C3  O8   doub N N 313 
MLI   C3  O9   sing N N 314 
PHE   N   CA   sing N N 315 
PHE   N   H    sing N N 316 
PHE   N   H2   sing N N 317 
PHE   CA  C    sing N N 318 
PHE   CA  CB   sing N N 319 
PHE   CA  HA   sing N N 320 
PHE   C   O    doub N N 321 
PHE   C   OXT  sing N N 322 
PHE   CB  CG   sing N N 323 
PHE   CB  HB2  sing N N 324 
PHE   CB  HB3  sing N N 325 
PHE   CG  CD1  doub Y N 326 
PHE   CG  CD2  sing Y N 327 
PHE   CD1 CE1  sing Y N 328 
PHE   CD1 HD1  sing N N 329 
PHE   CD2 CE2  doub Y N 330 
PHE   CD2 HD2  sing N N 331 
PHE   CE1 CZ   doub Y N 332 
PHE   CE1 HE1  sing N N 333 
PHE   CE2 CZ   sing Y N 334 
PHE   CE2 HE2  sing N N 335 
PHE   CZ  HZ   sing N N 336 
PHE   OXT HXT  sing N N 337 
PRO   N   CA   sing N N 338 
PRO   N   CD   sing N N 339 
PRO   N   H    sing N N 340 
PRO   CA  C    sing N N 341 
PRO   CA  CB   sing N N 342 
PRO   CA  HA   sing N N 343 
PRO   C   O    doub N N 344 
PRO   C   OXT  sing N N 345 
PRO   CB  CG   sing N N 346 
PRO   CB  HB2  sing N N 347 
PRO   CB  HB3  sing N N 348 
PRO   CG  CD   sing N N 349 
PRO   CG  HG2  sing N N 350 
PRO   CG  HG3  sing N N 351 
PRO   CD  HD2  sing N N 352 
PRO   CD  HD3  sing N N 353 
PRO   OXT HXT  sing N N 354 
SER   N   CA   sing N N 355 
SER   N   H    sing N N 356 
SER   N   H2   sing N N 357 
SER   CA  C    sing N N 358 
SER   CA  CB   sing N N 359 
SER   CA  HA   sing N N 360 
SER   C   O    doub N N 361 
SER   C   OXT  sing N N 362 
SER   CB  OG   sing N N 363 
SER   CB  HB2  sing N N 364 
SER   CB  HB3  sing N N 365 
SER   OG  HG   sing N N 366 
SER   OXT HXT  sing N N 367 
THR   N   CA   sing N N 368 
THR   N   H    sing N N 369 
THR   N   H2   sing N N 370 
THR   CA  C    sing N N 371 
THR   CA  CB   sing N N 372 
THR   CA  HA   sing N N 373 
THR   C   O    doub N N 374 
THR   C   OXT  sing N N 375 
THR   CB  OG1  sing N N 376 
THR   CB  CG2  sing N N 377 
THR   CB  HB   sing N N 378 
THR   OG1 HG1  sing N N 379 
THR   CG2 HG21 sing N N 380 
THR   CG2 HG22 sing N N 381 
THR   CG2 HG23 sing N N 382 
THR   OXT HXT  sing N N 383 
TRP   N   CA   sing N N 384 
TRP   N   H    sing N N 385 
TRP   N   H2   sing N N 386 
TRP   CA  C    sing N N 387 
TRP   CA  CB   sing N N 388 
TRP   CA  HA   sing N N 389 
TRP   C   O    doub N N 390 
TRP   C   OXT  sing N N 391 
TRP   CB  CG   sing N N 392 
TRP   CB  HB2  sing N N 393 
TRP   CB  HB3  sing N N 394 
TRP   CG  CD1  doub Y N 395 
TRP   CG  CD2  sing Y N 396 
TRP   CD1 NE1  sing Y N 397 
TRP   CD1 HD1  sing N N 398 
TRP   CD2 CE2  doub Y N 399 
TRP   CD2 CE3  sing Y N 400 
TRP   NE1 CE2  sing Y N 401 
TRP   NE1 HE1  sing N N 402 
TRP   CE2 CZ2  sing Y N 403 
TRP   CE3 CZ3  doub Y N 404 
TRP   CE3 HE3  sing N N 405 
TRP   CZ2 CH2  doub Y N 406 
TRP   CZ2 HZ2  sing N N 407 
TRP   CZ3 CH2  sing Y N 408 
TRP   CZ3 HZ3  sing N N 409 
TRP   CH2 HH2  sing N N 410 
TRP   OXT HXT  sing N N 411 
TYR   N   CA   sing N N 412 
TYR   N   H    sing N N 413 
TYR   N   H2   sing N N 414 
TYR   CA  C    sing N N 415 
TYR   CA  CB   sing N N 416 
TYR   CA  HA   sing N N 417 
TYR   C   O    doub N N 418 
TYR   C   OXT  sing N N 419 
TYR   CB  CG   sing N N 420 
TYR   CB  HB2  sing N N 421 
TYR   CB  HB3  sing N N 422 
TYR   CG  CD1  doub Y N 423 
TYR   CG  CD2  sing Y N 424 
TYR   CD1 CE1  sing Y N 425 
TYR   CD1 HD1  sing N N 426 
TYR   CD2 CE2  doub Y N 427 
TYR   CD2 HD2  sing N N 428 
TYR   CE1 CZ   doub Y N 429 
TYR   CE1 HE1  sing N N 430 
TYR   CE2 CZ   sing Y N 431 
TYR   CE2 HE2  sing N N 432 
TYR   CZ  OH   sing N N 433 
TYR   OH  HH   sing N N 434 
TYR   OXT HXT  sing N N 435 
VAL   N   CA   sing N N 436 
VAL   N   H    sing N N 437 
VAL   N   H2   sing N N 438 
VAL   CA  C    sing N N 439 
VAL   CA  CB   sing N N 440 
VAL   CA  HA   sing N N 441 
VAL   C   O    doub N N 442 
VAL   C   OXT  sing N N 443 
VAL   CB  CG1  sing N N 444 
VAL   CB  CG2  sing N N 445 
VAL   CB  HB   sing N N 446 
VAL   CG1 HG11 sing N N 447 
VAL   CG1 HG12 sing N N 448 
VAL   CG1 HG13 sing N N 449 
VAL   CG2 HG21 sing N N 450 
VAL   CG2 HG22 sing N N 451 
VAL   CG2 HG23 sing N N 452 
VAL   OXT HXT  sing N N 453 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Global Health Innovative Technology Fund'                        Japan     H2019-104  1 
'National Health and Medical Research Council (NHMRC, Australia)' Australia APP2022075 2 
# 
_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   7ROS 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.crystal_system   monoclinic 
_space_group.IT_number        5 
_space_group.name_H-M_alt     'C 1 2 1' 
_space_group.name_Hall        'C 2y' 
_space_group.id               1 
# 
_atom_sites.entry_id                    9CLL 
_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]   0.007235 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000586 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021155 
_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]   0.007140 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? ?       ?       ? ? ?        ?        ? ? ?   ? ? 
H  ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MG ? ? 9.41153 2.53737 ? ? 2.59044  63.03566 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
NA ? ? ?       ?       ? ? ?        ?        ? ? ?   ? ? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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    . LYS   A 1 17  ? -46.80234 28.72562  32.99313  1.000 78.43022  ? 17  LYS   A N    1 
ATOM   2    C  CA   . LYS   A 1 17  ? -47.82938 27.67902  33.08640  1.000 82.57954  ? 17  LYS   A CA   1 
ATOM   3    C  C    . LYS   A 1 17  ? -47.91202 26.77533  31.80870  1.000 82.80289  ? 17  LYS   A C    1 
ATOM   4    O  O    . LYS   A 1 17  ? -47.63340 25.56919  31.88946  1.000 71.28645  ? 17  LYS   A O    1 
ATOM   5    C  CB   . LYS   A 1 17  ? -49.18866 28.31835  33.40313  1.000 76.41133  ? 17  LYS   A CB   1 
ATOM   6    C  CG   . LYS   A 1 17  ? -49.87311 29.08863  32.22288  1.000 85.27417  ? 17  LYS   A CG   1 
ATOM   7    C  CD   . LYS   A 1 17  ? -48.92108 30.07264  31.49798  1.000 85.48337  ? 17  LYS   A CD   1 
ATOM   8    C  CE   . LYS   A 1 17  ? -49.59864 30.75606  30.31582  1.000 82.41873  ? 17  LYS   A CE   1 
ATOM   9    N  NZ   . LYS   A 1 17  ? -48.66752 31.72742  29.69100  1.000 75.89149  ? 17  LYS   A NZ   1 
ATOM   10   N  N    . ALA   A 1 18  ? -48.25499 27.30902  30.62589  1.000 76.78365  ? 18  ALA   A N    1 
ATOM   11   C  CA   . ALA   A 1 18  ? -48.21359 26.40970  29.47176  1.000 74.04938  ? 18  ALA   A CA   1 
ATOM   12   C  C    . ALA   A 1 18  ? -46.77587 26.01136  29.15575  1.000 80.35715  ? 18  ALA   A C    1 
ATOM   13   O  O    . ALA   A 1 18  ? -46.53490 24.97854  28.51354  1.000 76.23595  ? 18  ALA   A O    1 
ATOM   14   C  CB   . ALA   A 1 18  ? -48.86576 27.06643  28.24856  1.000 74.24167  ? 18  ALA   A CB   1 
ATOM   15   N  N    . GLN   A 1 19  ? -45.82441 26.78766  29.67214  1.000 75.69929  ? 19  GLN   A N    1 
ATOM   16   C  CA   . GLN   A 1 19  ? -44.40478 26.50370  29.52566  1.000 75.91261  ? 19  GLN   A CA   1 
ATOM   17   C  C    . GLN   A 1 19  ? -43.98250 25.29161  30.34754  1.000 73.66261  ? 19  GLN   A C    1 
ATOM   18   O  O    . GLN   A 1 19  ? -43.15039 24.49702  29.89505  1.000 69.48965  ? 19  GLN   A O    1 
ATOM   19   C  CB   . GLN   A 1 19  ? -43.63061 27.76590  29.91120  1.000 85.50855  ? 19  GLN   A CB   1 
ATOM   20   C  CG   . GLN   A 1 19  ? -44.29849 28.51801  31.09033  1.000 92.44995  ? 19  GLN   A CG   1 
ATOM   21   C  CD   . GLN   A 1 19  ? -43.64781 29.85880  31.43821  1.000 101.71886 ? 19  GLN   A CD   1 
ATOM   22   O  OE1  . GLN   A 1 19  ? -42.42140 29.96938  31.56152  1.000 103.77678 ? 19  GLN   A OE1  1 
ATOM   23   N  NE2  . GLN   A 1 19  ? -44.48674 30.89235  31.59828  1.000 101.49700 ? 19  GLN   A NE2  1 
ATOM   24   N  N    . GLU   A 1 20  ? -44.54590 25.13237  31.55586  1.000 70.67370  ? 20  GLU   A N    1 
ATOM   25   C  CA   . GLU   A 1 20  ? -44.25005 23.96316  32.38963  1.000 70.62094  ? 20  GLU   A CA   1 
ATOM   26   C  C    . GLU   A 1 20  ? -44.62300 22.66383  31.68447  1.000 65.08215  ? 20  GLU   A C    1 
ATOM   27   O  O    . GLU   A 1 20  ? -43.81007 21.72542  31.58679  1.000 66.71598  ? 20  GLU   A O    1 
ATOM   28   C  CB   . GLU   A 1 20  ? -44.99425 24.08789  33.72359  1.000 70.72514  ? 20  GLU   A CB   1 
ATOM   29   C  CG   . GLU   A 1 20  ? -44.33378 25.06696  34.67819  1.000 69.06814  ? 20  GLU   A CG   1 
ATOM   30   C  CD   . GLU   A 1 20  ? -45.27229 25.65277  35.74532  1.000 71.74319  ? 20  GLU   A CD   1 
ATOM   31   O  OE1  . GLU   A 1 20  ? -44.73806 26.36428  36.63899  1.000 74.46943  ? 20  GLU   A OE1  1 
ATOM   32   O  OE2  . GLU   A 1 20  ? -46.50087 25.34107  35.76337  1.000 77.20236  ? 20  GLU   A OE2  1 
ATOM   33   N  N    . GLU   A 1 21  ? -45.85469 22.59978  31.16987  1.000 71.41217  ? 21  GLU   A N    1 
ATOM   34   C  CA   . GLU   A 1 21  ? -46.28611 21.41515  30.43392  1.000 72.27517  ? 21  GLU   A CA   1 
ATOM   35   C  C    . GLU   A 1 21  ? -45.38125 21.14893  29.24044  1.000 67.75595  ? 21  GLU   A C    1 
ATOM   36   O  O    . GLU   A 1 21  ? -44.93347 20.01177  29.03386  1.000 60.77378  ? 21  GLU   A O    1 
ATOM   37   C  CB   . GLU   A 1 21  ? -47.72556 21.58180  29.98065  1.000 63.04044  ? 21  GLU   A CB   1 
ATOM   38   C  CG   . GLU   A 1 21  ? -48.27687 20.44097  29.11223  1.000 74.83410  ? 21  GLU   A CG   1 
ATOM   39   C  CD   . GLU   A 1 21  ? -48.71923 19.20365  29.90986  1.000 72.08245  ? 21  GLU   A CD   1 
ATOM   40   O  OE1  . GLU   A 1 21  ? -48.92210 19.31301  31.15821  1.000 63.53919  ? 21  GLU   A OE1  1 
ATOM   41   O  OE2  . GLU   A 1 21  ? -48.89700 18.12378  29.27747  1.000 66.34529  ? 21  GLU   A OE2  1 
ATOM   42   N  N    . SER   A 1 22  ? -45.05993 22.19978  28.48439  1.000 66.85890  ? 22  SER   A N    1 
ATOM   43   C  CA   . SER   A 1 22  ? -44.23210 22.05173  27.28871  1.000 68.26178  ? 22  SER   A CA   1 
ATOM   44   C  C    . SER   A 1 22  ? -42.82467 21.56286  27.63713  1.000 66.65965  ? 22  SER   A C    1 
ATOM   45   O  O    . SER   A 1 22  ? -42.24896 20.74074  26.91522  1.000 71.60676  ? 22  SER   A O    1 
ATOM   46   C  CB   . SER   A 1 22  ? -44.21621 23.38466  26.52280  1.000 79.51798  ? 22  SER   A CB   1 
ATOM   47   O  OG   . SER   A 1 22  ? -43.76701 23.24892  25.17959  1.000 83.66395  ? 22  SER   A OG   1 
ATOM   48   N  N    . LYS   A 1 23  ? -42.25201 22.03324  28.74836  1.000 67.56042  ? 23  LYS   A N    1 
ATOM   49   C  CA   . LYS   A 1 23  ? -40.94607 21.52224  29.16842  1.000 61.92030  ? 23  LYS   A CA   1 
ATOM   50   C  C    . LYS   A 1 23  ? -41.01443 20.02233  29.45065  1.000 66.47460  ? 23  LYS   A C    1 
ATOM   51   O  O    . LYS   A 1 23  ? -40.12856 19.25269  29.03984  1.000 60.05650  ? 23  LYS   A O    1 
ATOM   52   C  CB   . LYS   A 1 23  ? -40.47660 22.25093  30.43625  1.000 72.05444  ? 23  LYS   A CB   1 
ATOM   53   C  CG   . LYS   A 1 23  ? -40.09582 23.73492  30.33485  1.000 75.55886  ? 23  LYS   A CG   1 
ATOM   54   C  CD   . LYS   A 1 23  ? -39.59911 24.26836  31.71869  1.000 83.63321  ? 23  LYS   A CD   1 
ATOM   55   C  CE   . LYS   A 1 23  ? -38.10668 24.59880  31.77033  1.000 80.90310  ? 23  LYS   A CE   1 
ATOM   56   N  NZ   . LYS   A 1 23  ? -37.25703 23.48569  32.29461  1.000 85.10371  ? 23  LYS   A NZ   1 
ATOM   57   N  N    . ILE   A 1 24  ? -42.06272 19.58531  30.16348  1.000 56.39369  ? 24  ILE   A N    1 
ATOM   58   C  CA   . ILE   A 1 24  ? -42.24104 18.15209  30.42718  1.000 58.54283  ? 24  ILE   A CA   1 
ATOM   59   C  C    . ILE   A 1 24  ? -42.34795 17.35330  29.12172  1.000 59.69687  ? 24  ILE   A C    1 
ATOM   60   O  O    . ILE   A 1 24  ? -41.71259 16.29877  28.95416  1.000 61.76983  ? 24  ILE   A O    1 
ATOM   61   C  CB   . ILE   A 1 24  ? -43.49320 17.93418  31.28392  1.000 58.96667  ? 24  ILE   A CB   1 
ATOM   62   C  CG1  . ILE   A 1 24  ? -43.39456 18.77049  32.57481  1.000 68.60740  ? 24  ILE   A CG1  1 
ATOM   63   C  CG2  . ILE   A 1 24  ? -43.63037 16.44273  31.53809  1.000 66.07555  ? 24  ILE   A CG2  1 
ATOM   64   C  CD1  . ILE   A 1 24  ? -44.67722 18.65558  33.50405  1.000 60.46650  ? 24  ILE   A CD1  1 
ATOM   65   N  N    . GLU   A 1 25  ? -43.18917 17.82015  28.20338  1.000 57.04657  ? 25  GLU   A N    1 
ATOM   66   C  CA   . GLU   A 1 25  ? -43.37545 17.09534  26.95336  1.000 58.60477  ? 25  GLU   A CA   1 
ATOM   67   C  C    . GLU   A 1 25  ? -42.05233 16.97457  26.20479  1.000 61.06931  ? 25  GLU   A C    1 
ATOM   68   O  O    . GLU   A 1 25  ? -41.74567 15.91873  25.63121  1.000 64.78045  ? 25  GLU   A O    1 
ATOM   69   C  CB   . GLU   A 1 25  ? -44.39158 17.82232  26.08327  1.000 61.74079  ? 25  GLU   A CB   1 
ATOM   70   C  CG   . GLU   A 1 25  ? -45.73623 18.05411  26.75738  1.000 66.96413  ? 25  GLU   A CG   1 
ATOM   71   C  CD   . GLU   A 1 25  ? -46.88858 17.98366  25.76880  1.000 81.59399  ? 25  GLU   A CD   1 
ATOM   72   O  OE1  . GLU   A 1 25  ? -47.83903 17.16605  25.96063  1.000 80.64663  ? 25  GLU   A OE1  1 
ATOM   73   O  OE2  . GLU   A 1 25  ? -46.86798 18.83859  24.84809  1.000 81.87325  ? 25  GLU   A OE2  1 
ATOM   74   N  N    . ASP   A 1 26  ? -41.25370 18.05455  26.20514  1.000 58.17088  ? 26  ASP   A N    1 
ATOM   75   C  CA   . ASP   A 1 26  ? -39.96694 18.02592  25.52075  1.000 59.40540  ? 26  ASP   A CA   1 
ATOM   76   C  C    . ASP   A 1 26  ? -39.07684 16.96961  26.13388  1.000 57.66794  ? 26  ASP   A C    1 
ATOM   77   O  O    . ASP   A 1 26  ? -38.46970 16.17244  25.41277  1.000 61.49009  ? 26  ASP   A O    1 
ATOM   78   C  CB   . ASP   A 1 26  ? -39.28602 19.40281  25.56452  1.000 64.31334  ? 26  ASP   A CB   1 
ATOM   79   C  CG   . ASP   A 1 26  ? -40.05833 20.49805  24.77706  1.000 75.35049  ? 26  ASP   A CG   1 
ATOM   80   O  OD1  . ASP   A 1 26  ? -40.86216 20.18258  23.85740  1.000 76.22384  ? 26  ASP   A OD1  1 
ATOM   81   O  OD2  . ASP   A 1 26  ? -39.85941 21.69914  25.08747  1.000 76.99618  ? 26  ASP   A OD2  1 
ATOM   82   N  N    . VAL   A 1 27  ? -39.00459 16.92890  27.47519  1.000 53.05215  ? 27  VAL   A N    1 
ATOM   83   C  CA   . VAL   A 1 27  ? -38.13682 15.94518  28.11200  1.000 50.53182  ? 27  VAL   A CA   1 
ATOM   84   C  C    . VAL   A 1 27  ? -38.58683 14.53885  27.74045  1.000 55.59330  ? 27  VAL   A C    1 
ATOM   85   O  O    . VAL   A 1 27  ? -37.76242 13.65764  27.48885  1.000 49.30538  ? 27  VAL   A O    1 
ATOM   86   C  CB   . VAL   A 1 27  ? -38.09706 16.11311  29.65294  1.000 55.09913  ? 27  VAL   A CB   1 
ATOM   87   C  CG1  . VAL   A 1 27  ? -37.29235 14.96826  30.26548  1.000 50.53490  ? 27  VAL   A CG1  1 
ATOM   88   C  CG2  . VAL   A 1 27  ? -37.47622 17.42057  30.05025  1.000 58.22921  ? 27  VAL   A CG2  1 
ATOM   89   N  N    . ASP   A 1 28  ? -39.89797 14.29116  27.73893  1.000 54.59374  ? 28  ASP   A N    1 
ATOM   90   C  CA   . ASP   A 1 28  ? -40.39124 12.94862  27.40169  1.000 63.12528  ? 28  ASP   A CA   1 
ATOM   91   C  C    . ASP   A 1 28  ? -39.98863 12.53541  25.98447  1.000 60.28045  ? 28  ASP   A C    1 
ATOM   92   O  O    . ASP   A 1 28  ? -39.55577 11.39077  25.75360  1.000 58.01154  ? 28  ASP   A O    1 
ATOM   93   C  CB   . ASP   A 1 28  ? -41.91081 12.88180  27.55295  1.000 59.34142  ? 28  ASP   A CB   1 
ATOM   94   C  CG   . ASP   A 1 28  ? -42.36661 13.04678  28.99776  1.000 67.82082  ? 28  ASP   A CG   1 
ATOM   95   O  OD1  . ASP   A 1 28  ? -41.60621 12.68842  29.93944  1.000 63.74734  ? 28  ASP   A OD1  1 
ATOM   96   O  OD2  . ASP   A 1 28  ? -43.51934 13.51198  29.17678  1.000 83.10607  ? 28  ASP   A OD2  1 
ATOM   97   N  N    . LYS   A 1 29  ? -40.08841 13.46988  25.03642  1.000 57.26140  ? 29  LYS   A N    1 
ATOM   98   C  CA   . LYS   A 1 29  ? -39.66216 13.19564  23.66144  1.000 59.34351  ? 29  LYS   A CA   1 
ATOM   99   C  C    . LYS   A 1 29  ? -38.15762 12.91445  23.59299  1.000 59.77838  ? 29  LYS   A C    1 
ATOM   100  O  O    . LYS   A 1 29  ? -37.72792 11.96646  22.92857  1.000 53.94779  ? 29  LYS   A O    1 
ATOM   101  C  CB   . LYS   A 1 29  ? -40.04945 14.38082  22.77292  1.000 59.82178  ? 29  LYS   A CB   1 
ATOM   102  C  CG   . LYS   A 1 29  ? -39.16724 14.70201  21.58615  1.000 66.03566  ? 29  LYS   A CG   1 
ATOM   103  C  CD   . LYS   A 1 29  ? -39.48932 16.14377  21.05643  1.000 68.71010  ? 29  LYS   A CD   1 
ATOM   104  C  CE   . LYS   A 1 29  ? -38.78681 16.51849  19.71032  1.000 77.32166  ? 29  LYS   A CE   1 
ATOM   105  N  NZ   . LYS   A 1 29  ? -37.27025 16.65614  19.68863  1.000 82.84656  ? 29  LYS   A NZ   1 
ATOM   106  N  N    . ILE   A 1 30  ? -37.34221 13.75293  24.24533  1.000 52.21017  ? 30  ILE   A N    1 
ATOM   107  C  CA   . ILE   A 1 30  ? -35.88949 13.54316  24.24747  1.000 55.66912  ? 30  ILE   A CA   1 
ATOM   108  C  C    . ILE   A 1 30  ? -35.52820 12.20714  24.89084  1.000 56.73523  ? 30  ILE   A C    1 
ATOM   109  O  O    . ILE   A 1 30  ? -34.60834 11.50823  24.43860  1.000 54.20088  ? 30  ILE   A O    1 
ATOM   110  C  CB   . ILE   A 1 30  ? -35.17056 14.70940  24.94786  1.000 53.49972  ? 30  ILE   A CB   1 
ATOM   111  C  CG1  . ILE   A 1 30  ? -35.31576 16.01338  24.15288  1.000 58.08046  ? 30  ILE   A CG1  1 
ATOM   112  C  CG2  . ILE   A 1 30  ? -33.68782 14.37678  25.25133  1.000 53.74982  ? 30  ILE   A CG2  1 
ATOM   113  C  CD1  . ILE   A 1 30  ? -34.74785 17.22838  24.91155  1.000 58.93627  ? 30  ILE   A CD1  1 
ATOM   114  N  N    . LEU   A 1 31  ? -36.21403 11.84729  25.97394  1.000 51.72663  ? 31  LEU   A N    1 
ATOM   115  C  CA   . LEU   A 1 31  ? -35.96558 10.57394  26.63674  1.000 57.11065  ? 31  LEU   A CA   1 
ATOM   116  C  C    . LEU   A 1 31  ? -36.26775 9.40550   25.70909  1.000 55.88817  ? 31  LEU   A C    1 
ATOM   117  O  O    . LEU   A 1 31  ? -35.40496 8.55974   25.45427  1.000 56.08674  ? 31  LEU   A O    1 
ATOM   118  C  CB   . LEU   A 1 31  ? -36.82055 10.48243  27.90592  1.000 49.79509  ? 31  LEU   A CB   1 
ATOM   119  C  CG   . LEU   A 1 31  ? -36.77370 9.14550   28.62233  1.000 50.30358  ? 31  LEU   A CG   1 
ATOM   120  C  CD1  . LEU   A 1 31  ? -35.38933 8.93785   29.26817  1.000 51.85420  ? 31  LEU   A CD1  1 
ATOM   121  C  CD2  . LEU   A 1 31  ? -37.83636 9.14806   29.67449  1.000 57.95675  ? 31  LEU   A CD2  1 
ATOM   122  N  N    . ASN   A 1 32  ? -37.46551 9.37342   25.13114  1.000 58.41964  ? 32  ASN   A N    1 
ATOM   123  C  CA   . ASN   A 1 32  ? -37.76708 8.27431   24.21676  1.000 53.33117  ? 32  ASN   A CA   1 
ATOM   124  C  C    . ASN   A 1 32  ? -36.82116 8.26238   23.00859  1.000 60.27591  ? 32  ASN   A C    1 
ATOM   125  O  O    . ASN   A 1 32  ? -36.47561 7.18991   22.49858  1.000 58.75383  ? 32  ASN   A O    1 
ATOM   126  C  CB   . ASN   A 1 32  ? -39.24058 8.32711   23.80462  1.000 64.76739  ? 32  ASN   A CB   1 
ATOM   127  C  CG   . ASN   A 1 32  ? -40.12047 7.49074   24.74161  1.000 70.34604  ? 32  ASN   A CG   1 
ATOM   128  O  OD1  . ASN   A 1 32  ? -39.77297 7.26294   25.92006  1.000 72.49434  ? 32  ASN   A OD1  1 
ATOM   129  N  ND2  . ASN   A 1 32  ? -41.23828 6.99512   24.21406  1.000 71.54975  ? 32  ASN   A ND2  1 
ATOM   130  N  N    . ASP   A 1 33  ? -36.35543 9.43147   22.56783  1.000 54.27570  ? 33  ASP   A N    1 
ATOM   131  C  CA   . ASP   A 1 33  ? -35.43695 9.48899   21.43845  1.000 61.62629  ? 33  ASP   A CA   1 
ATOM   132  C  C    . ASP   A 1 33  ? -34.07965 8.87907   21.80999  1.000 58.29874  ? 33  ASP   A C    1 
ATOM   133  O  O    . ASP   A 1 33  ? -33.54902 8.00956   21.10401  1.000 55.91203  ? 33  ASP   A O    1 
ATOM   134  C  CB   . ASP   A 1 33  ? -35.27963 10.95227  21.01142  1.000 66.32884  ? 33  ASP   A CB   1 
ATOM   135  C  CG   . ASP   A 1 33  ? -35.30413 11.13707  19.51314  1.000 76.41928  ? 33  ASP   A CG   1 
ATOM   136  O  OD1  . ASP   A 1 33  ? -35.40539 10.10929  18.80152  1.000 74.58746  ? 33  ASP   A OD1  1 
ATOM   137  O  OD2  . ASP   A 1 33  ? -35.21971 12.31163  19.05744  1.000 79.30723  ? 33  ASP   A OD2  1 
ATOM   138  N  N    . ILE   A 1 34  ? -33.49721 9.33876   22.90937  1.000 51.32913  ? 34  ILE   A N    1 
ATOM   139  C  CA   . ILE   A 1 34  ? -32.23208 8.77942   23.35610  1.000 51.22970  ? 34  ILE   A CA   1 
ATOM   140  C  C    . ILE   A 1 34  ? -32.35136 7.27428   23.55463  1.000 58.03553  ? 34  ILE   A C    1 
ATOM   141  O  O    . ILE   A 1 34  ? -31.47301 6.50691   23.14987  1.000 54.48636  ? 34  ILE   A O    1 
ATOM   142  C  CB   . ILE   A 1 34  ? -31.77975 9.50574   24.62961  1.000 52.80909  ? 34  ILE   A CB   1 
ATOM   143  C  CG1  . ILE   A 1 34  ? -31.43100 10.96023  24.27794  1.000 48.97079  ? 34  ILE   A CG1  1 
ATOM   144  C  CG2  . ILE   A 1 34  ? -30.67931 8.74350   25.27892  1.000 51.34950  ? 34  ILE   A CG2  1 
ATOM   145  C  CD1  . ILE   A 1 34  ? -30.84184 11.76016  25.39569  1.000 51.49917  ? 34  ILE   A CD1  1 
ATOM   146  N  N    . LEU   A 1 35  ? -33.45512 6.81834   24.14487  1.000 55.64786  ? 35  LEU   A N    1 
ATOM   147  C  CA   . LEU   A 1 35  ? -33.59907 5.39130   24.40758  1.000 57.15357  ? 35  LEU   A CA   1 
ATOM   148  C  C    . LEU   A 1 35  ? -33.73999 4.56458   23.13266  1.000 55.71428  ? 35  LEU   A C    1 
ATOM   149  O  O    . LEU   A 1 35  ? -33.38547 3.38088   23.13651  1.000 60.02293  ? 35  LEU   A O    1 
ATOM   150  C  CB   . LEU   A 1 35  ? -34.79439 5.15988   25.34404  1.000 60.84379  ? 35  LEU   A CB   1 
ATOM   151  C  CG   . LEU   A 1 35  ? -34.56396 5.61522   26.80315  1.000 53.17688  ? 35  LEU   A CG   1 
ATOM   152  C  CD1  . LEU   A 1 35  ? -35.87802 5.84043   27.54794  1.000 51.50919  ? 35  LEU   A CD1  1 
ATOM   153  C  CD2  . LEU   A 1 35  ? -33.68310 4.62883   27.57271  1.000 53.87588  ? 35  LEU   A CD2  1 
ATOM   154  N  N    . SER   A 1 36  ? -34.21801 5.15580   22.03750  1.000 51.24721  ? 36  SER   A N    1 
ATOM   155  C  CA   . SER   A 1 36  ? -34.44350 4.37582   20.82576  1.000 57.79125  ? 36  SER   A CA   1 
ATOM   156  C  C    . SER   A 1 36  ? -33.15014 3.73458   20.30277  1.000 59.77701  ? 36  SER   A C    1 
ATOM   157  O  O    . SER   A 1 36  ? -33.18451 2.63029   19.74630  1.000 63.18959  ? 36  SER   A O    1 
ATOM   158  C  CB   . SER   A 1 36  ? -35.10693 5.25182   19.75466  1.000 60.88454  ? 36  SER   A CB   1 
ATOM   159  O  OG   . SER   A 1 36  ? -34.23720 6.31374   19.38626  1.000 66.64185  ? 36  SER   A OG   1 
ATOM   160  N  N    . ILE   A 1 37  ? -31.99956 4.41166   20.43151  1.000 61.90552  ? 37  ILE   A N    1 
ATOM   161  C  CA   . ILE   A 1 37  ? -30.77204 3.82217   19.88853  1.000 58.07716  ? 37  ILE   A CA   1 
ATOM   162  C  C    . ILE   A 1 37  ? -30.14487 2.78578   20.81186  1.000 59.45311  ? 37  ILE   A C    1 
ATOM   163  O  O    . ILE   A 1 37  ? -29.12875 2.17799   20.44530  1.000 55.75448  ? 37  ILE   A O    1 
ATOM   164  C  CB   . ILE   A 1 37  ? -29.75845 4.92084   19.50196  1.000 52.75391  ? 37  ILE   A CB   1 
ATOM   165  C  CG1  . ILE   A 1 37  ? -29.38194 5.82374   20.68813  1.000 58.45382  ? 37  ILE   A CG1  1 
ATOM   166  C  CG2  . ILE   A 1 37  ? -30.26386 5.69800   18.24045  1.000 58.59333  ? 37  ILE   A CG2  1 
ATOM   167  C  CD1  . ILE   A 1 37  ? -28.65301 5.12230   21.85692  1.000 50.32485  ? 37  ILE   A CD1  1 
ATOM   168  N  N    . SER   A 1 38  ? -30.74816 2.52514   21.97010  1.000 57.49691  ? 38  SER   A N    1 
ATOM   169  C  CA   . SER   A 1 38  ? -30.23559 1.60785   22.97675  1.000 48.75965  ? 38  SER   A CA   1 
ATOM   170  C  C    . SER   A 1 38  ? -30.99231 0.28500   22.98861  1.000 56.41428  ? 38  SER   A C    1 
ATOM   171  O  O    . SER   A 1 38  ? -32.20745 0.22891   22.77359  1.000 56.86981  ? 38  SER   A O    1 
ATOM   172  C  CB   . SER   A 1 38  ? -30.32968 2.23239   24.37138  1.000 52.04580  ? 38  SER   A CB   1 
ATOM   173  O  OG   . SER   A 1 38  ? -31.68016 2.09988   24.85701  1.000 60.15435  ? 38  SER   A OG   1 
ATOM   174  N  N    . SER   A 1 39  ? -30.26063 -0.78304  23.28105  1.000 49.98400  ? 39  SER   A N    1 
ATOM   175  C  CA   . SER   A 1 39  ? -30.85893 -2.07970  23.54691  1.000 54.86874  ? 39  SER   A CA   1 
ATOM   176  C  C    . SER   A 1 39  ? -31.09577 -2.30001  25.02472  1.000 52.00248  ? 39  SER   A C    1 
ATOM   177  O  O    . SER   A 1 39  ? -31.88897 -3.17575  25.39207  1.000 54.16968  ? 39  SER   A O    1 
ATOM   178  C  CB   . SER   A 1 39  ? -29.98623 -3.18212  22.94931  1.000 50.52897  ? 39  SER   A CB   1 
ATOM   179  O  OG   . SER   A 1 39  ? -28.85988 -3.41297  23.79840  1.000 57.48472  ? 39  SER   A OG   1 
ATOM   180  N  N    . GLU   A 1 40  ? -30.41209 -1.54595  25.88011  1.000 51.09221  ? 40  GLU   A N    1 
ATOM   181  C  CA   . GLU   A 1 40  ? -30.72608 -1.67503  27.29132  1.000 53.21276  ? 40  GLU   A CA   1 
ATOM   182  C  C    . GLU   A 1 40  ? -30.34808 -0.36571  27.96323  1.000 52.98172  ? 40  GLU   A C    1 
ATOM   183  O  O    . GLU   A 1 40  ? -29.32725 0.22687   27.63105  1.000 51.91152  ? 40  GLU   A O    1 
ATOM   184  C  CB   . GLU   A 1 40  ? -29.96211 -2.84848  27.94527  1.000 57.56649  ? 40  GLU   A CB   1 
ATOM   185  C  CG   . GLU   A 1 40  ? -30.19845 -2.97626  29.46131  1.000 56.76097  ? 40  GLU   A CG   1 
ATOM   186  C  CD   . GLU   A 1 40  ? -29.22202 -3.95029  30.17135  1.000 66.38257  ? 40  GLU   A CD   1 
ATOM   187  O  OE1  . GLU   A 1 40  ? -29.68071 -5.01678  30.66325  1.000 58.48528  ? 40  GLU   A OE1  1 
ATOM   188  O  OE2  . GLU   A 1 40  ? -27.98612 -3.67741  30.22620  1.000 59.20063  ? 40  GLU   A OE2  1 
ATOM   189  N  N    . CYS   A 1 41  ? -31.16177 0.07972   28.91309  1.000 48.90697  ? 41  CYS   A N    1 
ATOM   190  C  CA   . CYS   A 1 41  ? -30.84619 1.28554   29.66229  1.000 47.88015  ? 41  CYS   A CA   1 
ATOM   191  C  C    . CYS   A 1 41  ? -30.92735 0.98937   31.14715  1.000 52.15678  ? 41  CYS   A C    1 
ATOM   192  O  O    . CYS   A 1 41  ? -31.94827 0.48968   31.63253  1.000 50.85582  ? 41  CYS   A O    1 
ATOM   193  C  CB   . CYS   A 1 41  ? -31.78984 2.44664   29.31493  1.000 51.71213  ? 41  CYS   A CB   1 
ATOM   194  S  SG   . CYS   A 1 41  ? -31.35799 3.96700   30.26092  1.000 51.00114  ? 41  CYS   A SG   1 
ATOM   195  N  N    . ILE   A 1 42  ? -29.86062 1.30459   31.85744  1.000 47.03231  ? 42  ILE   A N    1 
ATOM   196  C  CA   . ILE   A 1 42  ? -29.79969 1.17139   33.29811  1.000 46.65919  ? 42  ILE   A CA   1 
ATOM   197  C  C    . ILE   A 1 42  ? -29.47871 2.55257   33.86202  1.000 49.73056  ? 42  ILE   A C    1 
ATOM   198  O  O    . ILE   A 1 42  ? -28.30524 2.95406   33.87969  1.000 45.35920  ? 42  ILE   A O    1 
ATOM   199  C  CB   . ILE   A 1 42  ? -28.75051 0.13255   33.70763  1.000 48.70971  ? 42  ILE   A CB   1 
ATOM   200  C  CG1  . ILE   A 1 42  ? -29.07683 -1.22530  33.07893  1.000 50.02064  ? 42  ILE   A CG1  1 
ATOM   201  C  CG2  . ILE   A 1 42  ? -28.54184 0.10286   35.23212  1.000 51.85556  ? 42  ILE   A CG2  1 
ATOM   202  C  CD1  . ILE   A 1 42  ? -27.85486 -2.10098  32.94667  1.000 58.51248  ? 42  ILE   A CD1  1 
ATOM   203  N  N    . GLN   A 1 43  ? -30.48157 3.29422   34.35003  1.000 48.06594  ? 43  GLN   A N    1 
ATOM   204  C  CA   . GLN   A 1 43  ? -31.93513 3.01926   34.25211  1.000 50.54407  ? 43  GLN   A CA   1 
ATOM   205  C  C    . GLN   A 1 43  ? -32.67777 4.18760   33.59213  1.000 54.68577  ? 43  GLN   A C    1 
ATOM   206  O  O    . GLN   A 1 43  ? -32.25350 5.32431   33.74552  1.000 52.01949  ? 43  GLN   A O    1 
ATOM   207  C  CB   . GLN   A 1 43  ? -32.51446 2.78318   35.65860  1.000 53.93760  ? 43  GLN   A CB   1 
ATOM   208  C  CG   . GLN   A 1 43  ? -31.85516 1.64082   36.42141  1.000 53.50988  ? 43  GLN   A CG   1 
ATOM   209  C  CD   . GLN   A 1 43  ? -32.38060 0.28907   35.97325  1.000 58.54400  ? 43  GLN   A CD   1 
ATOM   210  O  OE1  . GLN   A 1 43  ? -33.13283 0.18990   34.98924  1.000 62.00566  ? 43  GLN   A OE1  1 
ATOM   211  N  NE2  . GLN   A 1 43  ? -32.04013 -0.75129  36.72620  1.000 57.87600  ? 43  GLN   A NE2  1 
ATOM   212  N  N    . PRO   A 1 44  ? -33.81825 3.92654   32.91287  1.000 54.14255  ? 44  PRO   A N    1 
ATOM   213  C  CA   . PRO   A 1 44  ? -34.52786 5.03328   32.24269  1.000 56.73369  ? 44  PRO   A CA   1 
ATOM   214  C  C    . PRO   A 1 44  ? -34.92159 6.15848   33.18974  1.000 55.47887  ? 44  PRO   A C    1 
ATOM   215  O  O    . PRO   A 1 44  ? -34.89914 7.33412   32.80574  1.000 54.93217  ? 44  PRO   A O    1 
ATOM   216  C  CB   . PRO   A 1 44  ? -35.78324 4.35296   31.63344  1.000 57.03901  ? 44  PRO   A CB   1 
ATOM   217  C  CG   . PRO   A 1 44  ? -35.41151 2.90193   31.48902  1.000 60.13801  ? 44  PRO   A CG   1 
ATOM   218  C  CD   . PRO   A 1 44  ? -34.42316 2.61386   32.63051  1.000 55.79016  ? 44  PRO   A CD   1 
ATOM   219  N  N    . ASP   A 1 45  ? -35.35337 5.81349   34.40400  1.000 56.17114  ? 45  ASP   A N    1 
ATOM   220  C  CA   . ASP   A 1 45  ? -35.74145 6.80381   35.40829  1.000 53.91428  ? 45  ASP   A CA   1 
ATOM   221  C  C    . ASP   A 1 45  ? -34.57745 7.72690   35.74353  1.000 55.28262  ? 45  ASP   A C    1 
ATOM   222  O  O    . ASP   A 1 45  ? -34.72408 8.96001   35.84466  1.000 49.92368  ? 45  ASP   A O    1 
ATOM   223  C  CB   . ASP   A 1 45  ? -36.11750 6.02504   36.65124  1.000 65.15677  ? 45  ASP   A CB   1 
ATOM   224  C  CG   . ASP   A 1 45  ? -36.89103 4.77654   36.30323  1.000 78.49095  ? 45  ASP   A CG   1 
ATOM   225  O  OD1  . ASP   A 1 45  ? -38.00672 4.90636   35.71239  1.000 76.18062  ? 45  ASP   A OD1  1 
ATOM   226  O  OD2  . ASP   A 1 45  ? -36.30286 3.67622   36.51395  1.000 81.24402  ? 45  ASP   A OD2  1 
ATOM   227  N  N    . GLU   A 1 46  ? -33.39328 7.12850   35.86748  1.000 48.96062  ? 46  GLU   A N    1 
ATOM   228  C  CA   . GLU   A 1 46  ? -32.17500 7.88025   36.12762  1.000 46.05254  ? 46  GLU   A CA   1 
ATOM   229  C  C    . GLU   A 1 46  ? -31.81237 8.76325   34.93873  1.000 49.96685  ? 46  GLU   A C    1 
ATOM   230  O  O    . GLU   A 1 46  ? -31.28426 9.87690   35.10663  1.000 44.83079  ? 46  GLU   A O    1 
ATOM   231  C  CB   . GLU   A 1 46  ? -31.04574 6.89844   36.42906  1.000 48.80061  ? 46  GLU   A CB   1 
ATOM   232  C  CG   . GLU   A 1 46  ? -31.33970 5.92396   37.57821  1.000 51.64201  ? 46  GLU   A CG   1 
ATOM   233  C  CD   . GLU   A 1 46  ? -30.12093 5.07300   38.00755  1.000 58.51830  ? 46  GLU   A CD   1 
ATOM   234  O  OE1  . GLU   A 1 46  ? -28.93715 5.46374   37.72958  1.000 55.34921  ? 46  GLU   A OE1  1 
ATOM   235  O  OE2  . GLU   A 1 46  ? -30.34324 4.01150   38.64866  1.000 47.26806  ? 46  GLU   A OE2  1 
ATOM   236  N  N    . LEU   A 1 47  ? -32.03700 8.26060   33.72403  1.000 44.99412  ? 47  LEU   A N    1 
ATOM   237  C  CA   . LEU   A 1 47  ? -31.76066 9.07049   32.54556  1.000 47.92369  ? 47  LEU   A CA   1 
ATOM   238  C  C    . LEU   A 1 47  ? -32.70883 10.26316  32.47658  1.000 50.69880  ? 47  LEU   A C    1 
ATOM   239  O  O    . LEU   A 1 47  ? -32.26997 11.39173  32.22504  1.000 46.56732  ? 47  LEU   A O    1 
ATOM   240  C  CB   . LEU   A 1 47  ? -31.84358 8.20715   31.28369  1.000 49.11452  ? 47  LEU   A CB   1 
ATOM   241  C  CG   . LEU   A 1 47  ? -31.55656 8.96336   29.97570  1.000 49.61775  ? 47  LEU   A CG   1 
ATOM   242  C  CD1  . LEU   A 1 47  ? -30.24099 9.68220   30.02420  1.000 50.47071  ? 47  LEU   A CD1  1 
ATOM   243  C  CD2  . LEU   A 1 47  ? -31.69993 8.06719   28.72394  1.000 54.21108  ? 47  LEU   A CD2  1 
ATOM   244  N  N    . ARG   A 1 48  ? -33.99955 10.04686  32.75556  1.000 50.15039  ? 48  ARG   A N    1 
ATOM   245  C  CA   . ARG   A 1 48  ? -34.92776 11.17542  32.84296  1.000 46.53453  ? 48  ARG   A CA   1 
ATOM   246  C  C    . ARG   A 1 48  ? -34.39513 12.23612  33.79500  1.000 48.86252  ? 48  ARG   A C    1 
ATOM   247  O  O    . ARG   A 1 48  ? -34.35729 13.43415  33.45052  1.000 51.71641  ? 48  ARG   A O    1 
ATOM   248  C  CB   . ARG   A 1 48  ? -36.31287 10.70510  33.30041  1.000 55.73921  ? 48  ARG   A CB   1 
ATOM   249  C  CG   . ARG   A 1 48  ? -37.36089 11.78471  33.20110  1.000 58.41688  ? 48  ARG   A CG   1 
ATOM   250  C  CD   . ARG   A 1 48  ? -38.75502 11.19180  33.45246  1.000 60.14406  ? 48  ARG   A CD   1 
ATOM   251  N  NE   . ARG   A 1 48  ? -39.61905 11.25594  32.27405  1.000 78.11599  ? 48  ARG   A NE   1 
ATOM   252  C  CZ   . ARG   A 1 48  ? -40.27311 10.21148  31.77150  1.000 82.82613  ? 48  ARG   A CZ   1 
ATOM   253  N  NH1  . ARG   A 1 48  ? -40.21752 9.01872   32.35422  1.000 77.64880  ? 48  ARG   A NH1  1 
ATOM   254  N  NH2  . ARG   A 1 48  ? -41.00254 10.36620  30.65978  1.000 74.58286  ? 48  ARG   A NH2  1 
ATOM   255  N  N    . VAL   A 1 49  ? -33.93741 11.80043  34.98689  1.000 47.88471  ? 49  VAL   A N    1 
ATOM   256  C  CA   . VAL   A 1 49  ? -33.37774 12.74605  35.96584  1.000 55.79761  ? 49  VAL   A CA   1 
ATOM   257  C  C    . VAL   A 1 49  ? -32.17265 13.48676  35.39187  1.000 50.29617  ? 49  VAL   A C    1 
ATOM   258  O  O    . VAL   A 1 49  ? -32.07490 14.71426  35.50797  1.000 50.88947  ? 49  VAL   A O    1 
ATOM   259  C  CB   . VAL   A 1 49  ? -33.03340 12.05271  37.29533  1.000 46.13737  ? 49  VAL   A CB   1 
ATOM   260  C  CG1  . VAL   A 1 49  ? -32.06204 12.95527  38.14183  1.000 42.11946  ? 49  VAL   A CG1  1 
ATOM   261  C  CG2  . VAL   A 1 49  ? -34.35197 11.75543  38.05352  1.000 54.64017  ? 49  VAL   A CG2  1 
ATOM   262  N  N    . LYS   A 1 50  ? -31.22951 12.75971  34.77509  1.000 46.82250  ? 50  LYS   A N    1 
ATOM   263  C  CA   . LYS   A 1 50  ? -30.11549 13.43769  34.10054  1.000 51.70099  ? 50  LYS   A CA   1 
ATOM   264  C  C    . LYS   A 1 50  ? -30.62004 14.51236  33.12837  1.000 50.56766  ? 50  LYS   A C    1 
ATOM   265  O  O    . LYS   A 1 50  ? -30.04019 15.60486  33.02389  1.000 49.27517  ? 50  LYS   A O    1 
ATOM   266  C  CB   . LYS   A 1 50  ? -29.24573 12.43310  33.32421  1.000 46.74969  ? 50  LYS   A CB   1 
ATOM   267  C  CG   . LYS   A 1 50  ? -28.54563 11.38099  34.15510  1.000 48.91949  ? 50  LYS   A CG   1 
ATOM   268  C  CD   . LYS   A 1 50  ? -27.26857 11.86095  34.67493  1.000 47.82304  ? 50  LYS   A CD   1 
ATOM   269  C  CE   . LYS   A 1 50  ? -26.43838 10.73759  35.31592  1.000 49.24449  ? 50  LYS   A CE   1 
ATOM   270  N  NZ   . LYS   A 1 50  ? -25.26004 11.38789  35.89756  1.000 45.65079  ? 50  LYS   A NZ   1 
ATOM   271  N  N    . LEU   A 1 51  ? -31.65285 14.18503  32.35008  1.000 42.90041  ? 51  LEU   A N    1 
ATOM   272  C  CA   . LEU   A 1 51  ? -32.18140 15.11661  31.34852  1.000 51.82513  ? 51  LEU   A CA   1 
ATOM   273  C  C    . LEU   A 1 51  ? -32.77293 16.37648  31.97875  1.000 60.72716  ? 51  LEU   A C    1 
ATOM   274  O  O    . LEU   A 1 51  ? -32.99999 17.37312  31.27040  1.000 53.80527  ? 51  LEU   A O    1 
ATOM   275  C  CB   . LEU   A 1 51  ? -33.20472 14.41901  30.44383  1.000 45.15115  ? 51  LEU   A CB   1 
ATOM   276  C  CG   . LEU   A 1 51  ? -32.53749 13.40457  29.50438  1.000 56.09060  ? 51  LEU   A CG   1 
ATOM   277  C  CD1  . LEU   A 1 51  ? -33.53333 12.46480  28.81129  1.000 54.25374  ? 51  LEU   A CD1  1 
ATOM   278  C  CD2  . LEU   A 1 51  ? -31.66157 14.13957  28.47126  1.000 46.69944  ? 51  LEU   A CD2  1 
ATOM   279  N  N    . LEU   A 1 52  ? -33.23173 16.28118  33.22830  1.000 52.31333  ? 52  LEU   A N    1 
ATOM   280  C  CA   . LEU   A 1 52  ? -33.71876 17.48432  33.91982  1.000 52.44688  ? 52  LEU   A CA   1 
ATOM   281  C  C    . LEU   A 1 52  ? -32.59212 18.36882  34.48745  1.000 61.48260  ? 52  LEU   A C    1 
ATOM   282  O  O    . LEU   A 1 52  ? -32.88503 19.43504  35.03924  1.000 60.76598  ? 52  LEU   A O    1 
ATOM   283  C  CB   . LEU   A 1 52  ? -34.73557 17.09692  35.02236  1.000 54.01879  ? 52  LEU   A CB   1 
ATOM   284  C  CG   . LEU   A 1 52  ? -35.92962 16.27708  34.49132  1.000 54.39162  ? 52  LEU   A CG   1 
ATOM   285  C  CD1  . LEU   A 1 52  ? -36.65302 15.48795  35.57108  1.000 59.41996  ? 52  LEU   A CD1  1 
ATOM   286  C  CD2  . LEU   A 1 52  ? -36.85642 17.27444  33.92826  1.000 52.49363  ? 52  LEU   A CD2  1 
ATOM   287  N  N    . LEU   A 1 53  ? -31.31621 17.97647  34.35447  1.000 48.42591  ? 53  LEU   A N    1 
ATOM   288  C  CA   . LEU   A 1 53  ? -30.22158 18.73405  34.97439  1.000 61.75894  ? 53  LEU   A CA   1 
ATOM   289  C  C    . LEU   A 1 53  ? -29.93414 20.08417  34.34115  1.000 64.03690  ? 53  LEU   A C    1 
ATOM   290  O  O    . LEU   A 1 53  ? -29.28768 20.91189  34.98965  1.000 73.78210  ? 53  LEU   A O    1 
ATOM   291  C  CB   . LEU   A 1 53  ? -28.90453 17.94302  34.98180  1.000 52.64417  ? 53  LEU   A CB   1 
ATOM   292  C  CG   . LEU   A 1 53  ? -28.63546 16.85167  36.02358  1.000 57.02406  ? 53  LEU   A CG   1 
ATOM   293  C  CD1  . LEU   A 1 53  ? -29.85949 16.10073  36.36350  1.000 60.40096  ? 53  LEU   A CD1  1 
ATOM   294  C  CD2  . LEU   A 1 53  ? -27.52045 15.87956  35.60191  1.000 48.21931  ? 53  LEU   A CD2  1 
ATOM   295  N  N    . LYS   A 1 54  ? -30.38096 20.34067  33.11888  1.000 62.57595  ? 54  LYS   A N    1 
ATOM   296  C  CA   . LYS   A 1 54  ? -30.22241 21.66875  32.52208  1.000 69.74221  ? 54  LYS   A CA   1 
ATOM   297  C  C    . LYS   A 1 54  ? -28.74253 22.00702  32.29451  1.000 67.84035  ? 54  LYS   A C    1 
ATOM   298  O  O    . LYS   A 1 54  ? -28.26792 23.09831  32.61682  1.000 71.13460  ? 54  LYS   A O    1 
ATOM   299  C  CB   . LYS   A 1 54  ? -30.90331 22.72088  33.40247  1.000 79.73566  ? 54  LYS   A CB   1 
ATOM   300  C  CG   . LYS   A 1 54  ? -32.43866 22.53417  33.53125  1.000 73.69197  ? 54  LYS   A CG   1 
ATOM   301  C  CD   . LYS   A 1 54  ? -33.03993 23.47949  34.56425  1.000 80.47326  ? 54  LYS   A CD   1 
ATOM   302  C  CE   . LYS   A 1 54  ? -34.56487 23.33700  34.61910  1.000 88.56881  ? 54  LYS   A CE   1 
ATOM   303  N  NZ   . LYS   A 1 54  ? -35.19388 24.36461  35.49174  1.000 89.88523  ? 54  LYS   A NZ   1 
ATOM   304  N  N    . ARG   A 1 55  ? -28.01159 21.03440  31.76041  1.000 64.83056  ? 55  ARG   A N    1 
ATOM   305  C  CA   . ARG   A 1 55  ? -26.60815 21.11503  31.37143  1.000 57.17067  ? 55  ARG   A CA   1 
ATOM   306  C  C    . ARG   A 1 55  ? -26.41094 19.94149  30.43473  1.000 52.90548  ? 55  ARG   A C    1 
ATOM   307  O  O    . ARG   A 1 55  ? -27.13750 18.94821  30.52184  1.000 54.37710  ? 55  ARG   A O    1 
ATOM   308  C  CB   . ARG   A 1 55  ? -25.63101 21.00953  32.55461  1.000 60.88994  ? 55  ARG   A CB   1 
ATOM   309  C  CG   . ARG   A 1 55  ? -25.65477 19.63920  33.24225  1.000 56.74587  ? 55  ARG   A CG   1 
ATOM   310  C  CD   . ARG   A 1 55  ? -24.39263 19.42180  34.04135  1.000 58.74159  ? 55  ARG   A CD   1 
ATOM   311  N  NE   . ARG   A 1 55  ? -24.41001 18.23067  34.89197  1.000 57.40122  ? 55  ARG   A NE   1 
ATOM   312  C  CZ   . ARG   A 1 55  ? -24.10649 17.01074  34.46271  1.000 58.95789  ? 55  ARG   A CZ   1 
ATOM   313  N  NH1  . ARG   A 1 55  ? -23.84194 16.77396  33.18579  1.000 48.68889  ? 55  ARG   A NH1  1 
ATOM   314  N  NH2  . ARG   A 1 55  ? -24.05109 16.00485  35.33485  1.000 52.17096  ? 55  ARG   A NH2  1 
ATOM   315  N  N    . LYS   A 1 56  ? -25.41228 20.04583  29.55608  1.000 51.54010  ? 56  LYS   A N    1 
ATOM   316  C  CA   . LYS   A 1 56  ? -25.06756 18.93441  28.66843  1.000 46.00551  ? 56  LYS   A CA   1 
ATOM   317  C  C    . LYS   A 1 56  ? -24.68616 17.69266  29.47390  1.000 43.98539  ? 56  LYS   A C    1 
ATOM   318  O  O    . LYS   A 1 56  ? -23.97036 17.79053  30.47156  1.000 46.94468  ? 56  LYS   A O    1 
ATOM   319  C  CB   . LYS   A 1 56  ? -23.90406 19.33343  27.76046  1.000 48.15560  ? 56  LYS   A CB   1 
ATOM   320  C  CG   . LYS   A 1 56  ? -24.20686 20.45520  26.82008  1.000 53.70834  ? 56  LYS   A CG   1 
ATOM   321  C  CD   . LYS   A 1 56  ? -25.12070 20.01937  25.71115  1.000 52.16416  ? 56  LYS   A CD   1 
ATOM   322  C  CE   . LYS   A 1 56  ? -25.01511 21.04658  24.59041  1.000 58.46829  ? 56  LYS   A CE   1 
ATOM   323  N  NZ   . LYS   A 1 56  ? -25.49061 20.48547  23.31188  1.000 66.39079  ? 56  LYS   A NZ   1 
ATOM   324  N  N    . LEU   A 1 57  ? -25.20597 16.53478  29.07614  1.000 40.17705  ? 57  LEU   A N    1 
ATOM   325  C  CA   . LEU   A 1 57  ? -24.74022 15.26340  29.61636  1.000 38.30460  ? 57  LEU   A CA   1 
ATOM   326  C  C    . LEU   A 1 57  ? -23.50441 14.81074  28.84224  1.000 40.82705  ? 57  LEU   A C    1 
ATOM   327  O  O    . LEU   A 1 57  ? -23.47330 14.87309  27.60148  1.000 43.11881  ? 57  LEU   A O    1 
ATOM   328  C  CB   . LEU   A 1 57  ? -25.84675 14.22083  29.46447  1.000 44.21122  ? 57  LEU   A CB   1 
ATOM   329  C  CG   . LEU   A 1 57  ? -27.13733 14.74439  30.09454  1.000 44.44742  ? 57  LEU   A CG   1 
ATOM   330  C  CD1  . LEU   A 1 57  ? -28.27865 13.78593  29.84458  1.000 44.98376  ? 57  LEU   A CD1  1 
ATOM   331  C  CD2  . LEU   A 1 57  ? -26.90514 14.91172  31.60488  1.000 41.39867  ? 57  LEU   A CD2  1 
ATOM   332  N  N    . ILE   A 1 58  ? -22.51412 14.29554  29.56771  1.000 39.92710  ? 58  ILE   A N    1 
ATOM   333  C  CA   . ILE   A 1 58  ? -21.31204 13.75188  28.96650  1.000 39.03728  ? 58  ILE   A CA   1 
ATOM   334  C  C    . ILE   A 1 58  ? -21.54786 12.27337  28.67607  1.000 40.46587  ? 58  ILE   A C    1 
ATOM   335  O  O    . ILE   A 1 58  ? -21.85911 11.48993  29.58181  1.000 40.03130  ? 58  ILE   A O    1 
ATOM   336  C  CB   . ILE   A 1 58  ? -20.09697 13.94380  29.89197  1.000 41.95922  ? 58  ILE   A CB   1 
ATOM   337  C  CG1  . ILE   A 1 58  ? -19.82878 15.44436  30.07112  1.000 42.77509  ? 58  ILE   A CG1  1 
ATOM   338  C  CG2  . ILE   A 1 58  ? -18.88179 13.16979  29.30263  1.000 41.78815  ? 58  ILE   A CG2  1 
ATOM   339  C  CD1  . ILE   A 1 58  ? -18.65184 15.78304  31.01667  1.000 51.63542  ? 58  ILE   A CD1  1 
ATOM   340  N  N    . CYS   A 1 59  ? -21.41471 11.88830  27.41096  1.000 41.40995  ? 59  CYS   A N    1 
ATOM   341  C  CA   . CYS   A 1 59  ? -21.51810 10.49850  26.98487  1.000 33.50168  ? 59  CYS   A CA   1 
ATOM   342  C  C    . CYS   A 1 59  ? -20.16738 10.03506  26.48476  1.000 34.27447  ? 59  CYS   A C    1 
ATOM   343  O  O    . CYS   A 1 59  ? -19.39224 10.84427  25.96014  1.000 36.78521  ? 59  CYS   A O    1 
ATOM   344  C  CB   . CYS   A 1 59  ? -22.53650 10.35249  25.85409  1.000 35.91649  ? 59  CYS   A CB   1 
ATOM   345  S  SG   . CYS   A 1 59  ? -24.12291 11.13006  26.33144  1.000 46.76095  ? 59  CYS   A SG   1 
ATOM   346  N  N    . TYR   A 1 60  ? -19.92356 8.72201   26.52004  1.000 34.87039  ? 60  TYR   A N    1 
ATOM   347  C  CA   . TYR   A 1 60  ? -18.66572 8.30162   25.87283  1.000 32.09173  ? 60  TYR   A CA   1 
ATOM   348  C  C    . TYR   A 1 60  ? -18.75914 6.85195   25.40502  1.000 34.67625  ? 60  TYR   A C    1 
ATOM   349  O  O    . TYR   A 1 60  ? -19.58161 6.06217   25.87480  1.000 35.09325  ? 60  TYR   A O    1 
ATOM   350  C  CB   . TYR   A 1 60  ? -17.42697 8.49494   26.78593  1.000 32.65067  ? 60  TYR   A CB   1 
ATOM   351  C  CG   . TYR   A 1 60  ? -16.95857 7.29316   27.57815  1.000 37.97190  ? 60  TYR   A CG   1 
ATOM   352  C  CD1  . TYR   A 1 60  ? -17.80792 6.65725   28.49962  1.000 36.15522  ? 60  TYR   A CD1  1 
ATOM   353  C  CD2  . TYR   A 1 60  ? -15.61173 6.82809   27.47808  1.000 35.59774  ? 60  TYR   A CD2  1 
ATOM   354  C  CE1  . TYR   A 1 60  ? -17.35733 5.55731   29.26348  1.000 33.65923  ? 60  TYR   A CE1  1 
ATOM   355  C  CE2  . TYR   A 1 60  ? -15.17558 5.77438   28.22531  1.000 31.50817  ? 60  TYR   A CE2  1 
ATOM   356  C  CZ   . TYR   A 1 60  ? -16.01678 5.12052   29.10812  1.000 31.52172  ? 60  TYR   A CZ   1 
ATOM   357  O  OH   . TYR   A 1 60  ? -15.56421 4.04614   29.84571  1.000 35.63512  ? 60  TYR   A OH   1 
ATOM   358  N  N    . ASP   A 1 61  ? -17.85632 6.50803   24.49791  1.000 33.52164  ? 61  ASP   A N    1 
ATOM   359  C  CA   . ASP   A 1 61  ? -17.58938 5.13884   24.07564  1.000 34.88809  ? 61  ASP   A CA   1 
ATOM   360  C  C    . ASP   A 1 61  ? -16.07526 5.10857   23.94173  1.000 34.75078  ? 61  ASP   A C    1 
ATOM   361  O  O    . ASP   A 1 61  ? -15.46398 6.16033   23.73797  1.000 31.23648  ? 61  ASP   A O    1 
ATOM   362  C  CB   . ASP   A 1 61  ? -18.25611 4.83158   22.71876  1.000 32.23825  ? 61  ASP   A CB   1 
ATOM   363  C  CG   . ASP   A 1 61  ? -18.36980 3.33384   22.37618  1.000 39.59737  ? 61  ASP   A CG   1 
ATOM   364  O  OD1  . ASP   A 1 61  ? -17.74162 2.49566   23.04725  1.000 36.86562  ? 61  ASP   A OD1  1 
ATOM   365  O  OD2  . ASP   A 1 61  ? -19.15517 2.99432   21.41858  1.000 40.09714  ? 61  ASP   A OD2  1 
ATOM   366  N  N    . GLY   A 1 62  ? -15.49103 3.92414   24.01639  1.000 35.64234  ? 62  GLY   A N    1 
ATOM   367  C  CA   . GLY   A 1 62  ? -14.02826 3.79421   23.93354  1.000 33.98331  ? 62  GLY   A CA   1 
ATOM   368  C  C    . GLY   A 1 62  ? -13.65881 2.63995   23.02462  1.000 38.43020  ? 62  GLY   A C    1 
ATOM   369  O  O    . GLY   A 1 62  ? -14.43244 1.68813   22.84810  1.000 34.38593  ? 62  GLY   A O    1 
ATOM   370  N  N    . PHE   A 1 63  ? -12.44855 2.71810   22.45889  1.000 31.75867  ? 63  PHE   A N    1 
ATOM   371  C  CA   . PHE   A 1 63  ? -12.09309 1.86371   21.32747  1.000 35.52681  ? 63  PHE   A CA   1 
ATOM   372  C  C    . PHE   A 1 63  ? -10.63337 1.49238   21.43323  1.000 37.76672  ? 63  PHE   A C    1 
ATOM   373  O  O    . PHE   A 1 63  ? -9.79799  2.40134   21.47355  1.000 34.91252  ? 63  PHE   A O    1 
ATOM   374  C  CB   . PHE   A 1 63  ? -12.31815 2.58311   19.99446  1.000 35.37332  ? 63  PHE   A CB   1 
ATOM   375  C  CG   . PHE   A 1 63  ? -13.72707 3.09921   19.82556  1.000 32.15621  ? 63  PHE   A CG   1 
ATOM   376  C  CD1  . PHE   A 1 63  ? -14.11943 4.28389   20.44925  1.000 33.88772  ? 63  PHE   A CD1  1 
ATOM   377  C  CD2  . PHE   A 1 63  ? -14.65241 2.40349   19.03749  1.000 37.43517  ? 63  PHE   A CD2  1 
ATOM   378  C  CE1  . PHE   A 1 63  ? -15.42816 4.77046   20.29421  1.000 36.39378  ? 63  PHE   A CE1  1 
ATOM   379  C  CE2  . PHE   A 1 63  ? -15.98980 2.89123   18.90117  1.000 40.03569  ? 63  PHE   A CE2  1 
ATOM   380  C  CZ   . PHE   A 1 63  ? -16.35339 4.07897   19.54001  1.000 37.48528  ? 63  PHE   A CZ   1 
ATOM   381  N  N    . GLU   A 1 64  ? -10.34205 0.18365   21.43053  1.000 35.93708  ? 64  GLU   A N    1 
ATOM   382  C  CA   . GLU   A 1 64  ? -8.96189  -0.27643  21.30513  1.000 35.95215  ? 64  GLU   A CA   1 
ATOM   383  C  C    . GLU   A 1 64  ? -8.54426  -0.09722  19.84675  1.000 39.55387  ? 64  GLU   A C    1 
ATOM   384  O  O    . GLU   A 1 64  ? -9.16885  -0.69408  18.96562  1.000 35.19510  ? 64  GLU   A O    1 
ATOM   385  C  CB   . GLU   A 1 64  ? -8.84976  -1.75592  21.67448  1.000 34.03538  ? 64  GLU   A CB   1 
ATOM   386  C  CG   . GLU   A 1 64  ? -8.98089  -2.10998  23.17473  1.000 38.20451  ? 64  GLU   A CG   1 
ATOM   387  C  CD   . GLU   A 1 64  ? -8.73771  -3.59787  23.43269  1.000 39.82648  ? 64  GLU   A CD   1 
ATOM   388  O  OE1  . GLU   A 1 64  ? -8.00823  -4.24796  22.61701  1.000 39.90905  ? 64  GLU   A OE1  1 
ATOM   389  O  OE2  . GLU   A 1 64  ? -9.29240  -4.14087  24.41639  1.000 40.40995  ? 64  GLU   A OE2  1 
ATOM   390  N  N    . PRO   A 1 65  ? -7.48173  0.68041   19.53082  1.000 39.56222  ? 65  PRO   A N    1 
ATOM   391  C  CA   . PRO   A 1 65  ? -7.06452  0.71466   18.11343  1.000 40.78337  ? 65  PRO   A CA   1 
ATOM   392  C  C    . PRO   A 1 65  ? -6.35054  -0.58363  17.77684  1.000 40.89774  ? 65  PRO   A C    1 
ATOM   393  O  O    . PRO   A 1 65  ? -5.16374  -0.69166  18.02272  1.000 45.07721  ? 65  PRO   A O    1 
ATOM   394  C  CB   . PRO   A 1 65  ? -6.14737  1.94572   18.01957  1.000 41.57173  ? 65  PRO   A CB   1 
ATOM   395  C  CG   . PRO   A 1 65  ? -6.48251  2.77253   19.27923  1.000 40.64609  ? 65  PRO   A CG   1 
ATOM   396  C  CD   . PRO   A 1 65  ? -6.77125  1.70037   20.33591  1.000 34.91282  ? 65  PRO   A CD   1 
ATOM   397  N  N    . SER   A 1 66  ? -7.05819  -1.58687  17.25598  1.000 42.82940  ? 66  SER   A N    1 
ATOM   398  C  CA   . SER   A 1 66  ? -6.53919  -2.95634  17.16275  1.000 46.23451  ? 66  SER   A CA   1 
ATOM   399  C  C    . SER   A 1 66  ? -6.40092  -3.51418  15.75674  1.000 57.26034  ? 66  SER   A C    1 
ATOM   400  O  O    . SER   A 1 66  ? -5.90363  -4.63511  15.61374  1.000 63.47259  ? 66  SER   A O    1 
ATOM   401  C  CB   . SER   A 1 66  ? -7.45926  -3.91640  17.93883  1.000 48.74123  ? 66  SER   A CB   1 
ATOM   402  O  OG   . SER   A 1 66  ? -8.81828  -3.77254  17.45833  1.000 55.82241  ? 66  SER   A OG   1 
ATOM   403  N  N    . GLY   A 1 67  ? -6.83666  -2.79756  14.73488  1.000 45.73847  ? 67  GLY   A N    1 
ATOM   404  C  CA   . GLY   A 1 67  ? -6.90579  -3.31422  13.38723  1.000 57.74163  ? 67  GLY   A CA   1 
ATOM   405  C  C    . GLY   A 1 67  ? -7.94344  -2.51042  12.61359  1.000 52.43572  ? 67  GLY   A C    1 
ATOM   406  O  O    . GLY   A 1 67  ? -8.09756  -1.30867  12.82442  1.000 54.32398  ? 67  GLY   A O    1 
ATOM   407  N  N    . ARG   A 1 68  ? -8.59576  -3.16539  11.66989  1.000 53.75150  ? 68  ARG   A N    1 
ATOM   408  C  CA   . ARG   A 1 68  ? -9.63440  -2.47219  10.92120  1.000 54.09189  ? 68  ARG   A CA   1 
ATOM   409  C  C    . ARG   A 1 68  ? -10.82465 -2.08344  11.80766  1.000 50.98179  ? 68  ARG   A C    1 
ATOM   410  O  O    . ARG   A 1 68  ? -11.06900 -2.67943  12.86186  1.000 52.93664  ? 68  ARG   A O    1 
ATOM   411  C  CB   . ARG   A 1 68  ? -10.10258 -3.32635  9.74686   1.000 53.42825  ? 68  ARG   A CB   1 
ATOM   412  C  CG   . ARG   A 1 68  ? -9.07382  -3.42771  8.60701   1.000 57.46928  ? 68  ARG   A CG   1 
ATOM   413  C  CD   . ARG   A 1 68  ? -9.74464  -3.82850  7.26485   1.000 70.62472  ? 68  ARG   A CD   1 
ATOM   414  N  NE   . ARG   A 1 68  ? -10.25641 -5.19577  7.18638   1.000 71.81242  ? 68  ARG   A NE   1 
ATOM   415  C  CZ   . ARG   A 1 68  ? -11.08419 -5.63072  6.23678   1.000 70.89872  ? 68  ARG   A CZ   1 
ATOM   416  N  NH1  . ARG   A 1 68  ? -11.54430 -4.82508  5.28446   1.000 67.67048  ? 68  ARG   A NH1  1 
ATOM   417  N  NH2  . ARG   A 1 68  ? -11.45295 -6.90929  6.23242   1.000 76.14164  ? 68  ARG   A NH2  1 
ATOM   418  N  N    . MET   A 1 69  ? -11.54497 -1.03981  11.39119  1.000 52.45756  ? 69  MET   A N    1 
ATOM   419  C  CA   . MET   A 1 69  ? -12.69382 -0.55880  12.14907  1.000 46.26150  ? 69  MET   A CA   1 
ATOM   420  C  C    . MET   A 1 69  ? -13.95190 -1.32004  11.72657  1.000 48.94682  ? 69  MET   A C    1 
ATOM   421  O  O    . MET   A 1 69  ? -14.34298 -1.28225  10.56119  1.000 52.35714  ? 69  MET   A O    1 
ATOM   422  C  CB   . MET   A 1 69  ? -12.89191 0.94510   11.97277  1.000 47.31087  ? 69  MET   A CB   1 
ATOM   423  C  CG   . MET   A 1 69  ? -14.03634 1.43836   12.87767  1.000 42.00463  ? 69  MET   A CG   1 
ATOM   424  S  SD   . MET   A 1 69  ? -14.45894 3.15025   12.72114  1.000 43.14849  ? 69  MET   A SD   1 
ATOM   425  C  CE   . MET   A 1 69  ? -12.92992 3.80248   13.38287  1.000 40.95106  ? 69  MET   A CE   1 
ATOM   426  N  N    . HIS   A 1 70  ? -14.61022 -1.96117  12.68954  1.000 47.49730  ? 70  HIS   A N    1 
ATOM   427  C  CA   . HIS   A 1 70  ? -15.87000 -2.64958  12.42703  1.000 52.81797  ? 70  HIS   A CA   1 
ATOM   428  C  C    . HIS   A 1 70  ? -16.94054 -1.63126  12.02202  1.000 45.39129  ? 70  HIS   A C    1 
ATOM   429  O  O    . HIS   A 1 70  ? -16.95901 -0.50542  12.53058  1.000 44.60016  ? 70  HIS   A O    1 
ATOM   430  C  CB   . HIS   A 1 70  ? -16.27005 -3.42621  13.71071  1.000 47.94867  ? 70  HIS   A CB   1 
ATOM   431  C  CG   . HIS   A 1 70  ? -17.39548 -4.41834  13.51024  1.000 50.03418  ? 70  HIS   A CG   1 
ATOM   432  N  ND1  . HIS   A 1 70  ? -18.69260 -4.03096  13.20908  1.000 50.43735  ? 70  HIS   A ND1  1 
ATOM   433  C  CD2  . HIS   A 1 70  ? -17.42187 -5.77587  13.60306  1.000 50.44116  ? 70  HIS   A CD2  1 
ATOM   434  C  CE1  . HIS   A 1 70  ? -19.45582 -5.10209  13.08071  1.000 45.77362  ? 70  HIS   A CE1  1 
ATOM   435  N  NE2  . HIS   A 1 70  ? -18.71696 -6.17650  13.30843  1.000 49.17084  ? 70  HIS   A NE2  1 
ATOM   436  N  N    . ILE   A 1 71  ? -17.85883 -2.01552  11.10951  1.000 43.77522  ? 71  ILE   A N    1 
ATOM   437  C  CA   . ILE   A 1 71  ? -18.87440 -1.05080  10.70274  1.000 42.47700  ? 71  ILE   A CA   1 
ATOM   438  C  C    . ILE   A 1 71  ? -19.67672 -0.58157  11.91609  1.000 39.61917  ? 71  ILE   A C    1 
ATOM   439  O  O    . ILE   A 1 71  ? -20.10216 0.57248   11.97804  1.000 42.05593  ? 71  ILE   A O    1 
ATOM   440  C  CB   . ILE   A 1 71  ? -19.78387 -1.67029  9.60893   1.000 41.84327  ? 71  ILE   A CB   1 
ATOM   441  C  CG1  . ILE   A 1 71  ? -20.73313 -0.63554  9.00880   1.000 44.76753  ? 71  ILE   A CG1  1 
ATOM   442  C  CG2  . ILE   A 1 71  ? -20.61693 -2.79339  10.17326  1.000 46.87466  ? 71  ILE   A CG2  1 
ATOM   443  C  CD1  . ILE   A 1 71  ? -21.54027 -1.23389  7.83248   1.000 52.14088  ? 71  ILE   A CD1  1 
ATOM   444  N  N    . ALA   A 1 72  ? -19.83987 -1.43092  12.92506  1.000 41.80948  ? 72  ALA   A N    1 
ATOM   445  C  CA   . ALA   A 1 72  ? -20.52448 -0.98940  14.14949  1.000 48.45383  ? 72  ALA   A CA   1 
ATOM   446  C  C    . ALA   A 1 72  ? -19.81467 0.19133   14.81022  1.000 46.33478  ? 72  ALA   A C    1 
ATOM   447  O  O    . ALA   A 1 72  ? -20.46055 1.08139   15.37728  1.000 42.45738  ? 72  ALA   A O    1 
ATOM   448  C  CB   . ALA   A 1 72  ? -20.67552 -2.14118  15.15699  1.000 43.26877  ? 72  ALA   A CB   1 
ATOM   449  N  N    . GLN   A 1 73  ? -18.48931 0.22834   14.75217  1.000 42.41079  ? 73  GLN   A N    1 
ATOM   450  C  CA   . GLN   A 1 73  ? -17.75082 1.27048   15.43883  1.000 39.58880  ? 73  GLN   A CA   1 
ATOM   451  C  C    . GLN   A 1 73  ? -17.61308 2.55537   14.62949  1.000 43.41139  ? 73  GLN   A C    1 
ATOM   452  O  O    . GLN   A 1 73  ? -17.17900 3.58168   15.18637  1.000 38.27587  ? 73  GLN   A O    1 
ATOM   453  C  CB   . GLN   A 1 73  ? -16.34873 0.73593   15.78586  1.000 36.36196  ? 73  GLN   A CB   1 
ATOM   454  C  CG   . GLN   A 1 73  ? -16.47317 -0.45849  16.68085  1.000 41.10162  ? 73  GLN   A CG   1 
ATOM   455  C  CD   . GLN   A 1 73  ? -15.17613 -1.22336  16.76922  1.000 50.55175  ? 73  GLN   A CD   1 
ATOM   456  O  OE1  . GLN   A 1 73  ? -14.28886 -1.03502  15.92191  1.000 52.23761  ? 73  GLN   A OE1  1 
ATOM   457  N  NE2  . GLN   A 1 73  ? -15.05510 -2.10218  17.77798  1.000 41.85698  ? 73  GLN   A NE2  1 
ATOM   458  N  N    . GLY   A 1 74  ? -18.01866 2.53727   13.36328  1.000 46.72470  ? 74  GLY   A N    1 
ATOM   459  C  CA   . GLY   A 1 74  ? -17.97975 3.71926   12.51930  1.000 43.92053  ? 74  GLY   A CA   1 
ATOM   460  C  C    . GLY   A 1 74  ? -19.38123 4.15886   12.13575  1.000 45.94905  ? 74  GLY   A C    1 
ATOM   461  O  O    . GLY   A 1 74  ? -19.87693 5.15809   12.66183  1.000 52.48668  ? 74  GLY   A O    1 
ATOM   462  N  N    . LEU   A 1 75  ? -20.06218 3.42463   11.26476  1.000 44.63538  ? 75  LEU   A N    1 
ATOM   463  C  CA   . LEU   A 1 75  ? -21.37135 3.90162   10.79183  1.000 46.76839  ? 75  LEU   A CA   1 
ATOM   464  C  C    . LEU   A 1 75  ? -22.40813 3.92161   11.90805  1.000 48.44214  ? 75  LEU   A C    1 
ATOM   465  O  O    . LEU   A 1 75  ? -23.17262 4.89804   12.04985  1.000 49.04934  ? 75  LEU   A O    1 
ATOM   466  C  CB   . LEU   A 1 75  ? -21.89488 3.03315   9.64296   1.000 48.92428  ? 75  LEU   A CB   1 
ATOM   467  C  CG   . LEU   A 1 75  ? -21.15860 3.15562   8.31327   1.000 55.60417  ? 75  LEU   A CG   1 
ATOM   468  C  CD1  . LEU   A 1 75  ? -21.89501 2.32116   7.26874   1.000 52.88559  ? 75  LEU   A CD1  1 
ATOM   469  C  CD2  . LEU   A 1 75  ? -21.06787 4.61670   7.91093   1.000 54.97272  ? 75  LEU   A CD2  1 
ATOM   470  N  N    . LEU   A 1 76  ? -22.50776 2.81060   12.65781  1.000 46.13564  ? 76  LEU   A N    1 
ATOM   471  C  CA   . LEU   A 1 76  ? -23.50230 2.73758   13.71823  1.000 46.54272  ? 76  LEU   A CA   1 
ATOM   472  C  C    . LEU   A 1 76  ? -23.18737 3.75359   14.80367  1.000 44.93084  ? 76  LEU   A C    1 
ATOM   473  O  O    . LEU   A 1 76  ? -24.07773 4.44008   15.32833  1.000 45.55870  ? 76  LEU   A O    1 
ATOM   474  C  CB   . LEU   A 1 76  ? -23.60662 1.31074   14.25715  1.000 43.58843  ? 76  LEU   A CB   1 
ATOM   475  C  CG   . LEU   A 1 76  ? -24.49575 1.29868   15.51568  1.000 40.05680  ? 76  LEU   A CG   1 
ATOM   476  C  CD1  . LEU   A 1 76  ? -26.00543 1.49737   15.14681  1.000 47.33936  ? 76  LEU   A CD1  1 
ATOM   477  C  CD2  . LEU   A 1 76  ? -24.31344 0.05636   16.33498  1.000 51.19258  ? 76  LEU   A CD2  1 
ATOM   478  N  N    . LYS   A 1 77  ? -21.92249 3.86768   15.16611  1.000 44.44044  ? 77  LYS   A N    1 
ATOM   479  C  CA   . LYS   A 1 77  ? -21.57430 4.86650   16.15819  1.000 45.27062  ? 77  LYS   A CA   1 
ATOM   480  C  C    . LYS   A 1 77  ? -22.00849 6.25011   15.70212  1.000 46.43224  ? 77  LYS   A C    1 
ATOM   481  O  O    . LYS   A 1 77  ? -22.54030 7.03506   16.49193  1.000 43.36826  ? 77  LYS   A O    1 
ATOM   482  C  CB   . LYS   A 1 77  ? -20.07317 4.78209   16.42003  1.000 37.03191  ? 77  LYS   A CB   1 
ATOM   483  C  CG   . LYS   A 1 77  ? -19.49917 5.69061   17.48780  1.000 44.22136  ? 77  LYS   A CG   1 
ATOM   484  C  CD   . LYS   A 1 77  ? -20.11498 5.56570   18.87170  1.000 49.77201  ? 77  LYS   A CD   1 
ATOM   485  C  CE   . LYS   A 1 77  ? -20.76056 4.25667   19.12453  1.000 44.46094  ? 77  LYS   A CE   1 
ATOM   486  N  NZ   . LYS   A 1 77  ? -21.39834 4.37547   20.41074  1.000 38.91586  ? 77  LYS   A NZ   1 
ATOM   487  N  N    . SER   A 1 78  ? -21.79377 6.57819   14.42910  1.000 45.97002  ? 78  SER   A N    1 
ATOM   488  C  CA   . SER   A 1 78  ? -22.15494 7.92540   14.01304  1.000 47.04961  ? 78  SER   A CA   1 
ATOM   489  C  C    . SER   A 1 78  ? -23.66804 8.13911   14.07973  1.000 45.05112  ? 78  SER   A C    1 
ATOM   490  O  O    . SER   A 1 78  ? -24.11559 9.23230   14.45081  1.000 45.42803  ? 78  SER   A O    1 
ATOM   491  C  CB   . SER   A 1 78  ? -21.62132 8.23343   12.61084  1.000 54.84662  ? 78  SER   A CB   1 
ATOM   492  O  OG   . SER   A 1 78  ? -22.29666 7.49792   11.63319  1.000 55.58309  ? 78  SER   A OG   1 
ATOM   493  N  N    . ILE   A 1 79  ? -24.47009 7.11011   13.80498  1.000 47.77665  ? 79  ILE   A N    1 
ATOM   494  C  CA   . ILE   A 1 79  ? -25.92333 7.29667   13.95069  1.000 50.14639  ? 79  ILE   A CA   1 
ATOM   495  C  C    . ILE   A 1 79  ? -26.26911 7.62278   15.40952  1.000 49.65236  ? 79  ILE   A C    1 
ATOM   496  O  O    . ILE   A 1 79  ? -27.05398 8.54485   15.71247  1.000 45.80293  ? 79  ILE   A O    1 
ATOM   497  C  CB   . ILE   A 1 79  ? -26.69671 6.05269   13.48136  1.000 54.39441  ? 79  ILE   A CB   1 
ATOM   498  C  CG1  . ILE   A 1 79  ? -26.58132 5.82868   11.98203  1.000 58.08561  ? 79  ILE   A CG1  1 
ATOM   499  C  CG2  . ILE   A 1 79  ? -28.16181 6.16443   13.87876  1.000 51.26418  ? 79  ILE   A CG2  1 
ATOM   500  C  CD1  . ILE   A 1 79  ? -26.81582 4.40043   11.65785  1.000 55.42612  ? 79  ILE   A CD1  1 
ATOM   501  N  N    . ILE   A 1 80  ? -25.69681 6.84897   16.33744  1.000 43.60477  ? 80  ILE   A N    1 
ATOM   502  C  CA   . ILE   A 1 80  ? -25.98357 7.03721   17.76376  1.000 44.79771  ? 80  ILE   A CA   1 
ATOM   503  C  C    . ILE   A 1 80  ? -25.48371 8.39374   18.25490  1.000 46.80958  ? 80  ILE   A C    1 
ATOM   504  O  O    . ILE   A 1 80  ? -26.16672 9.10614   19.01472  1.000 39.56294  ? 80  ILE   A O    1 
ATOM   505  C  CB   . ILE   A 1 80  ? -25.34799 5.89926   18.58171  1.000 44.67341  ? 80  ILE   A CB   1 
ATOM   506  C  CG1  . ILE   A 1 80  ? -25.91654 4.54490   18.14358  1.000 45.52654  ? 80  ILE   A CG1  1 
ATOM   507  C  CG2  . ILE   A 1 80  ? -25.42849 6.19879   20.09401  1.000 46.12837  ? 80  ILE   A CG2  1 
ATOM   508  C  CD1  . ILE   A 1 80  ? -25.11850 3.37414   18.57194  1.000 46.90099  ? 80  ILE   A CD1  1 
ATOM   509  N  N    . VAL   A 1 81  ? -24.25081 8.74427   17.89325  1.000 39.07958  ? 81  VAL   A N    1 
ATOM   510  C  CA   . VAL   A 1 81  ? -23.70483 9.99727   18.38652  1.000 40.24548  ? 81  VAL   A CA   1 
ATOM   511  C  C    . VAL   A 1 81  ? -24.52841 11.17488  17.88036  1.000 38.72369  ? 81  VAL   A C    1 
ATOM   512  O  O    . VAL   A 1 81  ? -24.73628 12.14792  18.61160  1.000 41.42854  ? 81  VAL   A O    1 
ATOM   513  C  CB   . VAL   A 1 81  ? -22.22126 10.14092  18.01304  1.000 39.57023  ? 81  VAL   A CB   1 
ATOM   514  C  CG1  . VAL   A 1 81  ? -21.78988 11.58142  18.27068  1.000 40.62192  ? 81  VAL   A CG1  1 
ATOM   515  C  CG2  . VAL   A 1 81  ? -21.40350 9.19841   18.86458  1.000 43.13868  ? 81  VAL   A CG2  1 
ATOM   516  N  N    . ASN   A 1 82  ? -24.95240 11.14189  16.59617  1.000 39.78042  ? 82  ASN   A N    1 
ATOM   517  C  CA   . ASN   A 1 82  ? -25.75582 12.23689  16.06810  1.000 41.32100  ? 82  ASN   A CA   1 
ATOM   518  C  C    . ASN   A 1 82  ? -27.07823 12.37078  16.82593  1.000 43.95464  ? 82  ASN   A C    1 
ATOM   519  O  O    . ASN   A 1 82  ? -27.49789 13.49129  17.16291  1.000 47.53766  ? 82  ASN   A O    1 
ATOM   520  C  CB   . ASN   A 1 82  ? -26.01843 12.01352  14.57048  1.000 44.55750  ? 82  ASN   A CB   1 
ATOM   521  C  CG   . ASN   A 1 82  ? -24.88477 12.45467  13.73230  1.000 49.85790  ? 82  ASN   A CG   1 
ATOM   522  O  OD1  . ASN   A 1 82  ? -24.06801 13.28215  14.16289  1.000 52.50857  ? 82  ASN   A OD1  1 
ATOM   523  N  ND2  . ASN   A 1 82  ? -24.81787 11.93487  12.50942  1.000 50.50088  ? 82  ASN   A ND2  1 
ATOM   524  N  N    . LYS   A 1 83  ? -27.71354 11.23703  17.15043  1.000 45.93660  ? 83  LYS   A N    1 
ATOM   525  C  CA   . LYS   A 1 83  ? -28.88581 11.25060  18.03220  1.000 44.87530  ? 83  LYS   A CA   1 
ATOM   526  C  C    . LYS   A 1 83  ? -28.59311 11.95055  19.38009  1.000 47.95577  ? 83  LYS   A C    1 
ATOM   527  O  O    . LYS   A 1 83  ? -29.33556 12.84664  19.83153  1.000 47.84531  ? 83  LYS   A O    1 
ATOM   528  C  CB   . LYS   A 1 83  ? -29.30394 9.80192   18.26989  1.000 53.07541  ? 83  LYS   A CB   1 
ATOM   529  C  CG   . LYS   A 1 83  ? -30.70477 9.61293   18.82519  1.000 58.04291  ? 83  LYS   A CG   1 
ATOM   530  C  CD   . LYS   A 1 83  ? -31.70243 9.97527   17.71292  1.000 60.15241  ? 83  LYS   A CD   1 
ATOM   531  C  CE   . LYS   A 1 83  ? -32.89062 9.00893   17.64041  1.000 71.26026  ? 83  LYS   A CE   1 
ATOM   532  N  NZ   . LYS   A 1 83  ? -32.56600 7.73863   16.91465  1.000 72.19297  ? 83  LYS   A NZ   1 
ATOM   533  N  N    . LEU   A 1 84  ? -27.47780 11.58500  20.02679  1.000 42.21342  ? 84  LEU   A N    1 
ATOM   534  C  CA   . LEU   A 1 84  ? -27.22107 12.11239  21.36464  1.000 42.04420  ? 84  LEU   A CA   1 
ATOM   535  C  C    . LEU   A 1 84  ? -26.86554 13.60093  21.33589  1.000 45.58547  ? 84  LEU   A C    1 
ATOM   536  O  O    . LEU   A 1 84  ? -27.33571 14.37113  22.19154  1.000 42.48784  ? 84  LEU   A O    1 
ATOM   537  C  CB   . LEU   A 1 84  ? -26.10849 11.30454  22.03887  1.000 40.07552  ? 84  LEU   A CB   1 
ATOM   538  C  CG   . LEU   A 1 84  ? -26.45339 9.84379   22.36831  1.000 45.39626  ? 84  LEU   A CG   1 
ATOM   539  C  CD1  . LEU   A 1 84  ? -25.18508 9.08589   22.77979  1.000 45.96587  ? 84  LEU   A CD1  1 
ATOM   540  C  CD2  . LEU   A 1 84  ? -27.47076 9.72174   23.52639  1.000 50.61129  ? 84  LEU   A CD2  1 
ATOM   541  N  N    . THR   A 1 85  ? -26.00779 14.01868  20.38987  1.000 43.29784  ? 85  THR   A N    1 
ATOM   542  C  CA   . THR   A 1 85  ? -25.55422 15.40295  20.35360  1.000 43.17662  ? 85  THR   A CA   1 
ATOM   543  C  C    . THR   A 1 85  ? -26.65171 16.33882  19.88229  1.000 46.62098  ? 85  THR   A C    1 
ATOM   544  O  O    . THR   A 1 85  ? -26.59227 17.54457  20.16131  1.000 47.54893  ? 85  THR   A O    1 
ATOM   545  C  CB   . THR   A 1 85  ? -24.29511 15.57114  19.49778  1.000 43.21077  ? 85  THR   A CB   1 
ATOM   546  O  OG1  . THR   A 1 85  ? -24.54778 15.19353  18.14862  1.000 44.77384  ? 85  THR   A OG1  1 
ATOM   547  C  CG2  . THR   A 1 85  ? -23.10214 14.73397  20.08770  1.000 38.49477  ? 85  THR   A CG2  1 
ATOM   548  N  N    . SER   A 1 86  ? -27.61900 15.83584  19.13033  1.000 43.20712  ? 86  SER   A N    1 
ATOM   549  C  CA   . SER   A 1 86  ? -28.75718 16.68556  18.83927  1.000 49.07083  ? 86  SER   A CA   1 
ATOM   550  C  C    . SER   A 1 86  ? -29.77283 16.68036  19.97680  1.000 53.76891  ? 86  SER   A C    1 
ATOM   551  O  O    . SER   A 1 86  ? -30.80337 17.37999  19.87830  1.000 48.51626  ? 86  SER   A O    1 
ATOM   552  C  CB   . SER   A 1 86  ? -29.36608 16.27492  17.49560  1.000 48.84972  ? 86  SER   A CB   1 
ATOM   553  O  OG   . SER   A 1 86  ? -29.87275 14.95376  17.53799  1.000 55.19327  ? 86  SER   A OG   1 
ATOM   554  N  N    . ASN   A 1 87  ? -29.59469 15.80461  20.96849  1.000 46.65866  ? 87  ASN   A N    1 
ATOM   555  C  CA   . ASN   A 1 87  ? -30.49176 15.77328  22.13463  1.000 52.28890  ? 87  ASN   A CA   1 
ATOM   556  C  C    . ASN   A 1 87  ? -29.82827 16.20527  23.45838  1.000 53.34622  ? 87  ASN   A C    1 
ATOM   557  O  O    . ASN   A 1 87  ? -30.08692 15.62278  24.52305  1.000 50.92979  ? 87  ASN   A O    1 
ATOM   558  C  CB   . ASN   A 1 87  ? -31.13259 14.39702  22.24441  1.000 45.27666  ? 87  ASN   A CB   1 
ATOM   559  C  CG   . ASN   A 1 87  ? -32.26455 14.21485  21.25167  1.000 57.78846  ? 87  ASN   A CG   1 
ATOM   560  O  OD1  . ASN   A 1 87  ? -33.28506 14.88820  21.34743  1.000 55.02799  ? 87  ASN   A OD1  1 
ATOM   561  N  ND2  . ASN   A 1 87  ? -32.07576 13.33387  20.26703  1.000 53.44439  ? 87  ASN   A ND2  1 
ATOM   562  N  N    . GLY   A 1 88  ? -28.93604 17.20413  23.42945  1.000 48.58995  ? 88  GLY   A N    1 
ATOM   563  C  CA   . GLY   A 1 88  ? -28.44695 17.77517  24.67996  1.000 48.53345  ? 88  GLY   A CA   1 
ATOM   564  C  C    . GLY   A 1 88  ? -27.20706 17.14008  25.28664  1.000 46.02907  ? 88  GLY   A C    1 
ATOM   565  O  O    . GLY   A 1 88  ? -26.96199 17.32167  26.49464  1.000 50.17910  ? 88  GLY   A O    1 
ATOM   566  N  N    . CYS   A 1 89  ? -26.47661 16.32363  24.53029  1.000 44.06722  ? 89  CYS   A N    1 
ATOM   567  C  CA   . CYS   A 1 89  ? -25.30261 15.60329  25.01546  1.000 40.33207  ? 89  CYS   A CA   1 
ATOM   568  C  C    . CYS   A 1 89  ? -24.04520 16.08422  24.31581  1.000 46.80551  ? 89  CYS   A C    1 
ATOM   569  O  O    . CYS   A 1 89  ? -24.08913 16.61419  23.20699  1.000 44.01158  ? 89  CYS   A O    1 
ATOM   570  C  CB   . CYS   A 1 89  ? -25.42107 14.08987  24.79931  1.000 47.15840  ? 89  CYS   A CB   1 
ATOM   571  S  SG   . CYS   A 1 89  ? -26.88723 13.28790  25.58082  1.000 51.13831  ? 89  CYS   A SG   1 
ATOM   572  N  N    . THR   A 1 90  ? -22.91795 15.85620  24.98398  1.000 37.89758  ? 90  THR   A N    1 
ATOM   573  C  CA   . THR   A 1 90  ? -21.59245 15.98004  24.39971  1.000 43.22769  ? 90  THR   A CA   1 
ATOM   574  C  C    . THR   A 1 90  ? -20.98237 14.58647  24.43400  1.000 42.73399  ? 90  THR   A C    1 
ATOM   575  O  O    . THR   A 1 90  ? -21.32235 13.77916  25.30458  1.000 43.05965  ? 90  THR   A O    1 
ATOM   576  C  CB   . THR   A 1 90  ? -20.71267 16.97416  25.15476  1.000 42.78111  ? 90  THR   A CB   1 
ATOM   577  O  OG1  . THR   A 1 90  ? -20.54172 16.51004  26.48527  1.000 44.36482  ? 90  THR   A OG1  1 
ATOM   578  C  CG2  . THR   A 1 90  ? -21.38961 18.35045  25.20996  1.000 46.95380  ? 90  THR   A CG2  1 
ATOM   579  N  N    . PHE   A 1 91  ? -20.14203 14.26855  23.44566  1.000 39.73385  ? 91  PHE   A N    1 
ATOM   580  C  CA   . PHE   A 1 91  ? -19.75977 12.88705  23.22610  1.000 36.51486  ? 91  PHE   A CA   1 
ATOM   581  C  C    . PHE   A 1 91  ? -18.25060 12.80511  23.13000  1.000 38.49312  ? 91  PHE   A C    1 
ATOM   582  O  O    . PHE   A 1 91  ? -17.63269 13.59117  22.41318  1.000 39.31573  ? 91  PHE   A O    1 
ATOM   583  C  CB   . PHE   A 1 91  ? -20.43589 12.27018  21.95278  1.000 38.59309  ? 91  PHE   A CB   1 
ATOM   584  C  CG   . PHE   A 1 91  ? -20.38384 10.77336  21.98460  1.000 40.30016  ? 91  PHE   A CG   1 
ATOM   585  C  CD1  . PHE   A 1 91  ? -19.22732 10.10493  21.58314  1.000 38.37004  ? 91  PHE   A CD1  1 
ATOM   586  C  CD2  . PHE   A 1 91  ? -21.42257 10.04924  22.55274  1.000 43.70666  ? 91  PHE   A CD2  1 
ATOM   587  C  CE1  . PHE   A 1 91  ? -19.13823 8.70632   21.70495  1.000 36.15469  ? 91  PHE   A CE1  1 
ATOM   588  C  CE2  . PHE   A 1 91  ? -21.35501 8.67226   22.65774  1.000 44.61588  ? 91  PHE   A CE2  1 
ATOM   589  C  CZ   . PHE   A 1 91  ? -20.19637 8.00576   22.26518  1.000 35.41431  ? 91  PHE   A CZ   1 
ATOM   590  N  N    . ILE   A 1 92  ? -17.67156 11.90330  23.89252  1.000 34.21350  ? 92  ILE   A N    1 
ATOM   591  C  CA   . ILE   A 1 92  ? -16.23062 11.65335  23.87110  1.000 33.35175  ? 92  ILE   A CA   1 
ATOM   592  C  C    . ILE   A 1 92  ? -15.96932 10.32828  23.18293  1.000 36.27457  ? 92  ILE   A C    1 
ATOM   593  O  O    . ILE   A 1 92  ? -16.47780 9.29032   23.62422  1.000 38.43970  ? 92  ILE   A O    1 
ATOM   594  C  CB   . ILE   A 1 92  ? -15.65870 11.64716  25.29596  1.000 34.93464  ? 92  ILE   A CB   1 
ATOM   595  C  CG1  . ILE   A 1 92  ? -15.78385 13.05991  25.85815  1.000 36.12196  ? 92  ILE   A CG1  1 
ATOM   596  C  CG2  . ILE   A 1 92  ? -14.19620 11.07802  25.26171  1.000 30.30527  ? 92  ILE   A CG2  1 
ATOM   597  C  CD1  . ILE   A 1 92  ? -15.52002 13.14011  27.39941  1.000 36.66332  ? 92  ILE   A CD1  1 
ATOM   598  N  N    . PHE   A 1 93  ? -15.10670 10.33883  22.16337  1.000 30.93429  ? 93  PHE   A N    1 
ATOM   599  C  CA   . PHE   A 1 93  ? -14.53388 9.11200   21.64317  1.000 33.54449  ? 93  PHE   A CA   1 
ATOM   600  C  C    . PHE   A 1 93  ? -13.21592 8.91748   22.39123  1.000 32.63349  ? 93  PHE   A C    1 
ATOM   601  O  O    . PHE   A 1 93  ? -12.32162 9.75230   22.27304  1.000 35.50905  ? 93  PHE   A O    1 
ATOM   602  C  CB   . PHE   A 1 93  ? -14.25204 9.19997   20.14714  1.000 32.26061  ? 93  PHE   A CB   1 
ATOM   603  C  CG   . PHE   A 1 93  ? -15.45674 9.05200   19.26872  1.000 35.14010  ? 93  PHE   A CG   1 
ATOM   604  C  CD1  . PHE   A 1 93  ? -16.33484 10.10434  19.09861  1.000 37.25654  ? 93  PHE   A CD1  1 
ATOM   605  C  CD2  . PHE   A 1 93  ? -15.69379 7.86733   18.58785  1.000 34.93346  ? 93  PHE   A CD2  1 
ATOM   606  C  CE1  . PHE   A 1 93  ? -17.47097 9.96672   18.25426  1.000 35.57214  ? 93  PHE   A CE1  1 
ATOM   607  C  CE2  . PHE   A 1 93  ? -16.79182 7.72519   17.74969  1.000 37.17424  ? 93  PHE   A CE2  1 
ATOM   608  C  CZ   . PHE   A 1 93  ? -17.68263 8.78148   17.59350  1.000 40.59004  ? 93  PHE   A CZ   1 
ATOM   609  N  N    . TRP   A 1 94  ? -13.09246 7.83332   23.15102  1.000 32.34605  ? 94  TRP   A N    1 
ATOM   610  C  CA   . TRP   A 1 94  ? -11.89223 7.56203   23.95317  1.000 33.71823  ? 94  TRP   A CA   1 
ATOM   611  C  C    . TRP   A 1 94  ? -11.03019 6.55895   23.19253  1.000 36.24074  ? 94  TRP   A C    1 
ATOM   612  O  O    . TRP   A 1 94  ? -11.41404 5.38997   23.01971  1.000 34.95862  ? 94  TRP   A O    1 
ATOM   613  C  CB   . TRP   A 1 94  ? -12.35233 7.03659   25.29051  1.000 34.05592  ? 94  TRP   A CB   1 
ATOM   614  C  CG   . TRP   A 1 94  ? -11.38992 6.67593   26.35222  1.000 34.28788  ? 94  TRP   A CG   1 
ATOM   615  C  CD1  . TRP   A 1 94  ? -11.18740 5.44008   26.87122  1.000 31.32514  ? 94  TRP   A CD1  1 
ATOM   616  C  CD2  . TRP   A 1 94  ? -10.56953 7.57951   27.10329  1.000 29.70856  ? 94  TRP   A CD2  1 
ATOM   617  N  NE1  . TRP   A 1 94  ? -10.30421 5.51453   27.96777  1.000 30.84053  ? 94  TRP   A NE1  1 
ATOM   618  C  CE2  . TRP   A 1 94  ? -9.95665  6.83139   28.13773  1.000 33.72708  ? 94  TRP   A CE2  1 
ATOM   619  C  CE3  . TRP   A 1 94  ? -10.39736 8.96563   27.07821  1.000 32.86123  ? 94  TRP   A CE3  1 
ATOM   620  C  CZ2  . TRP   A 1 94  ? -9.08923  7.40913   29.07986  1.000 34.25230  ? 94  TRP   A CZ2  1 
ATOM   621  C  CZ3  . TRP   A 1 94  ? -9.54808  9.54344   28.05978  1.000 37.88749  ? 94  TRP   A CZ3  1 
ATOM   622  C  CH2  . TRP   A 1 94  ? -8.92043  8.76357   29.02725  1.000 34.44309  ? 94  TRP   A CH2  1 
ATOM   623  N  N    . ILE   A 1 95  ? -9.91366  7.03823   22.65146  1.000 33.91560  ? 95  ILE   A N    1 
ATOM   624  C  CA   . ILE   A 1 95  ? -9.00143  6.19126   21.91053  1.000 33.37482  ? 95  ILE   A CA   1 
ATOM   625  C  C    . ILE   A 1 95  ? -8.18023  5.44453   22.95061  1.000 36.32691  ? 95  ILE   A C    1 
ATOM   626  O  O    . ILE   A 1 95  ? -7.31965  6.04571   23.58959  1.000 34.37295  ? 95  ILE   A O    1 
ATOM   627  C  CB   . ILE   A 1 95  ? -8.09760  7.03064   21.01166  1.000 37.90602  ? 95  ILE   A CB   1 
ATOM   628  C  CG1  . ILE   A 1 95  ? -8.89624  8.10594   20.26946  1.000 41.45861  ? 95  ILE   A CG1  1 
ATOM   629  C  CG2  . ILE   A 1 95  ? -7.24664  6.11393   20.13644  1.000 36.39704  ? 95  ILE   A CG2  1 
ATOM   630  C  CD1  . ILE   A 1 95  ? -10.05949 7.63895   19.60092  1.000 43.37729  ? 95  ILE   A CD1  1 
ATOM   631  N  N    . ALA   A 1 96  ? -8.46278  4.14770   23.13467  1.000 33.32418  ? 96  ALA   A N    1 
ATOM   632  C  CA   . ALA   A 1 96  ? -8.00405  3.39141   24.29830  1.000 36.34838  ? 96  ALA   A CA   1 
ATOM   633  C  C    . ALA   A 1 96  ? -6.66090  2.72662   23.97023  1.000 34.02130  ? 96  ALA   A C    1 
ATOM   634  O  O    . ALA   A 1 96  ? -6.50370  1.51260   23.89643  1.000 33.05744  ? 96  ALA   A O    1 
ATOM   635  C  CB   . ALA   A 1 96  ? -9.06650  2.37714   24.71372  1.000 33.25971  ? 96  ALA   A CB   1 
ATOM   636  N  N    . ASP   A 1 97  ? -5.71082  3.59240   23.65160  1.000 34.65894  ? 97  ASP   A N    1 
ATOM   637  C  CA   . ASP   A 1 97  ? -4.44038  3.11648   23.11681  1.000 35.77361  ? 97  ASP   A CA   1 
ATOM   638  C  C    . ASP   A 1 97  ? -3.69974  2.28082   24.16442  1.000 33.50199  ? 97  ASP   A C    1 
ATOM   639  O  O    . ASP   A 1 97  ? -3.21281  1.16850   23.87438  1.000 35.71832  ? 97  ASP   A O    1 
ATOM   640  C  CB   . ASP   A 1 97  ? -3.61245  4.31299   22.61052  1.000 34.58940  ? 97  ASP   A CB   1 
ATOM   641  C  CG   . ASP   A 1 97  ? -3.41737  5.45096   23.67217  1.000 40.00885  ? 97  ASP   A CG   1 
ATOM   642  O  OD1  . ASP   A 1 97  ? -3.93051  5.41699   24.80503  1.000 37.12274  ? 97  ASP   A OD1  1 
ATOM   643  O  OD2  . ASP   A 1 97  ? -2.68358  6.40872   23.37809  1.000 38.07989  ? 97  ASP   A OD2  1 
ATOM   644  N  N    . TRP   A 1 98  ? -3.63471  2.77525   25.40985  1.000 36.27136  ? 98  TRP   A N    1 
ATOM   645  C  CA   . TRP   A 1 98  ? -2.98898  1.97928   26.46143  1.000 34.19020  ? 98  TRP   A CA   1 
ATOM   646  C  C    . TRP   A 1 98  ? -3.71218  0.67006   26.71300  1.000 38.26279  ? 98  TRP   A C    1 
ATOM   647  O  O    . TRP   A 1 98  ? -3.09741  -0.31671  27.09550  1.000 32.07864  ? 98  TRP   A O    1 
ATOM   648  C  CB   . TRP   A 1 98  ? -2.89735  2.77637   27.74589  1.000 39.80681  ? 98  TRP   A CB   1 
ATOM   649  C  CG   . TRP   A 1 98  ? -1.59299  3.41546   27.87265  1.000 53.51706  ? 98  TRP   A CG   1 
ATOM   650  C  CD1  . TRP   A 1 98  ? -0.59172  3.44619   26.91976  1.000 54.97249  ? 98  TRP   A CD1  1 
ATOM   651  C  CD2  . TRP   A 1 98  ? -1.11562  4.16268   28.98783  1.000 45.99911  ? 98  TRP   A CD2  1 
ATOM   652  N  NE1  . TRP   A 1 98  ? 0.48253   4.16005   27.39845  1.000 52.95396  ? 98  TRP   A NE1  1 
ATOM   653  C  CE2  . TRP   A 1 98  ? 0.18084   4.62264   28.65873  1.000 53.11341  ? 98  TRP   A CE2  1 
ATOM   654  C  CE3  . TRP   A 1 98  ? -1.67497  4.53586   30.20045  1.000 42.41337  ? 98  TRP   A CE3  1 
ATOM   655  C  CZ2  . TRP   A 1 98  ? 0.95402   5.38899   29.55205  1.000 52.50583  ? 98  TRP   A CZ2  1 
ATOM   656  C  CZ3  . TRP   A 1 98  ? -0.89698  5.32115   31.09816  1.000 49.19969  ? 98  TRP   A CZ3  1 
ATOM   657  C  CH2  . TRP   A 1 98  ? 0.38782   5.70878   30.77371  1.000 44.19401  ? 98  TRP   A CH2  1 
ATOM   658  N  N    . PHE   A 1 99  ? -5.03356  0.64729   26.52514  1.000 34.66380  ? 99  PHE   A N    1 
ATOM   659  C  CA   . PHE   A 1 99  ? -5.80148  -0.58473  26.71700  1.000 32.99950  ? 99  PHE   A CA   1 
ATOM   660  C  C    . PHE   A 1 99  ? -5.49665  -1.60248  25.63046  1.000 31.22826  ? 99  PHE   A C    1 
ATOM   661  O  O    . PHE   A 1 99  ? -5.39689  -2.79428  25.92205  1.000 35.43419  ? 99  PHE   A O    1 
ATOM   662  C  CB   . PHE   A 1 99  ? -7.30945  -0.26392  26.73907  1.000 32.46666  ? 99  PHE   A CB   1 
ATOM   663  C  CG   . PHE   A 1 99  ? -7.72394  0.54477   27.93151  1.000 31.20452  ? 99  PHE   A CG   1 
ATOM   664  C  CD1  . PHE   A 1 99  ? -7.53907  1.90929   27.93139  1.000 27.08569  ? 99  PHE   A CD1  1 
ATOM   665  C  CD2  . PHE   A 1 99  ? -8.21991  -0.08397  29.05993  1.000 31.73969  ? 99  PHE   A CD2  1 
ATOM   666  C  CE1  . PHE   A 1 99  ? -7.87877  2.68301   29.06443  1.000 29.75184  ? 99  PHE   A CE1  1 
ATOM   667  C  CE2  . PHE   A 1 99  ? -8.60813  0.63221   30.19571  1.000 27.58811  ? 99  PHE   A CE2  1 
ATOM   668  C  CZ   . PHE   A 1 99  ? -8.43247  2.03062   30.21779  1.000 31.17045  ? 99  PHE   A CZ   1 
ATOM   669  N  N    . ALA   A 1 100 ? -5.41745  -1.15679  24.35151  1.000 33.29387  ? 100 ALA   A N    1 
ATOM   670  C  CA   . ALA   A 1 100 ? -4.99720  -2.03383  23.26512  1.000 32.42534  ? 100 ALA   A CA   1 
ATOM   671  C  C    . ALA   A 1 100 ? -3.64676  -2.65291  23.58969  1.000 38.29898  ? 100 ALA   A C    1 
ATOM   672  O  O    . ALA   A 1 100 ? -3.41130  -3.84691  23.34905  1.000 37.10997  ? 100 ALA   A O    1 
ATOM   673  C  CB   . ALA   A 1 100 ? -4.84235  -1.23602  21.97541  1.000 33.90932  ? 100 ALA   A CB   1 
ATOM   674  N  N    . HIS   A 1 101 ? -2.73129  -1.81796  24.09349  1.000 34.03339  ? 101 HIS   A N    1 
ATOM   675  C  CA   . HIS   A 1 101 ? -1.39426  -2.32319  24.46093  1.000 34.86696  ? 101 HIS   A CA   1 
ATOM   676  C  C    . HIS   A 1 101 ? -1.49769  -3.34522  25.58380  1.000 33.93290  ? 101 HIS   A C    1 
ATOM   677  O  O    . HIS   A 1 101 ? -0.85723  -4.40894  25.55779  1.000 37.11470  ? 101 HIS   A O    1 
ATOM   678  C  CB   . HIS   A 1 101 ? -0.50981  -1.14742  24.85339  1.000 35.90719  ? 101 HIS   A CB   1 
ATOM   679  C  CG   . HIS   A 1 101 ? 0.82316   -1.54724  25.44713  1.000 43.70992  ? 101 HIS   A CG   1 
ATOM   680  N  ND1  . HIS   A 1 101 ? 1.90939   -1.89442  24.67340  1.000 47.82228  ? 101 HIS   A ND1  1 
ATOM   681  C  CD2  . HIS   A 1 101 ? 1.23318   -1.65102  26.73605  1.000 53.61138  ? 101 HIS   A CD2  1 
ATOM   682  C  CE1  . HIS   A 1 101 ? 2.94225   -2.16514  25.45805  1.000 50.21514  ? 101 HIS   A CE1  1 
ATOM   683  N  NE2  . HIS   A 1 101 ? 2.54887   -2.05057  26.71353  1.000 53.76637  ? 101 HIS   A NE2  1 
ATOM   684  N  N    . LEU   A 1 102 ? -2.28235  -3.02716  26.60562  1.000 35.14095  ? 102 LEU   A N    1 
ATOM   685  C  CA   . LEU   A 1 102 ? -2.44495  -3.95196  27.72311  1.000 32.47058  ? 102 LEU   A CA   1 
ATOM   686  C  C    . LEU   A 1 102 ? -3.04948  -5.25429  27.25990  1.000 37.97612  ? 102 LEU   A C    1 
ATOM   687  O  O    . LEU   A 1 102 ? -2.80276  -6.29883  27.85758  1.000 37.37126  ? 102 LEU   A O    1 
ATOM   688  C  CB   . LEU   A 1 102 ? -3.34180  -3.29275  28.77364  1.000 41.81124  ? 102 LEU   A CB   1 
ATOM   689  C  CG   . LEU   A 1 102 ? -3.45030  -3.83768  30.17987  1.000 35.48517  ? 102 LEU   A CG   1 
ATOM   690  C  CD1  . LEU   A 1 102 ? -1.99496  -3.90591  30.80252  1.000 29.92246  ? 102 LEU   A CD1  1 
ATOM   691  C  CD2  . LEU   A 1 102 ? -4.34306  -2.92833  31.00195  1.000 27.30987  ? 102 LEU   A CD2  1 
ATOM   692  N  N    . ASN   A 1 103 ? -3.89841  -5.20478  26.21220  1.000 34.08630  ? 103 ASN   A N    1 
ATOM   693  C  CA   . ASN   A 1 103 ? -4.62169  -6.35844  25.71917  1.000 36.64567  ? 103 ASN   A CA   1 
ATOM   694  C  C    . ASN   A 1 103 ? -3.88236  -7.04019  24.57315  1.000 40.65326  ? 103 ASN   A C    1 
ATOM   695  O  O    . ASN   A 1 103 ? -4.47386  -7.83803  23.82951  1.000 39.25939  ? 103 ASN   A O    1 
ATOM   696  C  CB   . ASN   A 1 103 ? -6.05204  -5.89566  25.31391  1.000 33.54730  ? 103 ASN   A CB   1 
ATOM   697  C  CG   . ASN   A 1 103 ? -7.04647  -7.02252  25.29292  1.000 41.67684  ? 103 ASN   A CG   1 
ATOM   698  O  OD1  . ASN   A 1 103 ? -6.73270  -8.15399  25.67414  1.000 36.98998  ? 103 ASN   A OD1  1 
ATOM   699  N  ND2  . ASN   A 1 103 ? -8.27663  -6.73208  24.80164  1.000 36.66728  ? 103 ASN   A ND2  1 
ATOM   700  N  N    . ASN   A 1 104 ? -2.59563  -6.70641  24.39801  1.000 35.46963  ? 104 ASN   A N    1 
ATOM   701  C  CA   . ASN   A 1 104 ? -1.72032  -7.40939  23.48001  1.000 37.31923  ? 104 ASN   A CA   1 
ATOM   702  C  C    . ASN   A 1 104 ? -2.13397  -7.23769  22.00530  1.000 43.09250  ? 104 ASN   A C    1 
ATOM   703  O  O    . ASN   A 1 104 ? -1.83336  -8.09203  21.17172  1.000 45.09436  ? 104 ASN   A O    1 
ATOM   704  C  CB   . ASN   A 1 104 ? -1.62031  -8.89282  23.85056  1.000 40.05866  ? 104 ASN   A CB   1 
ATOM   705  C  CG   . ASN   A 1 104 ? -0.91949  -9.11655  25.21021  1.000 55.05785  ? 104 ASN   A CG   1 
ATOM   706  O  OD1  . ASN   A 1 104 ? 0.01877   -8.39000  25.57021  1.000 52.33572  ? 104 ASN   A OD1  1 
ATOM   707  N  ND2  . ASN   A 1 104 ? -1.34657  -10.16004 25.95287  1.000 48.71137  ? 104 ASN   A ND2  1 
ATOM   708  N  N    . LYS   A 1 105 ? -2.75233  -6.10992  21.64871  1.000 41.36908  ? 105 LYS   A N    1 
ATOM   709  C  CA   . LYS   A 1 105 ? -3.14218  -5.88009  20.26596  1.000 47.40357  ? 105 LYS   A CA   1 
ATOM   710  C  C    . LYS   A 1 105 ? -1.95434  -5.35402  19.46920  1.000 48.79422  ? 105 LYS   A C    1 
ATOM   711  O  O    . LYS   A 1 105 ? -1.09823  -4.65878  19.99695  1.000 44.37053  ? 105 LYS   A O    1 
ATOM   712  C  CB   . LYS   A 1 105 ? -4.29612  -4.87352  20.17105  1.000 44.56858  ? 105 LYS   A CB   1 
ATOM   713  C  CG   . LYS   A 1 105 ? -5.54524  -5.26725  20.90786  1.000 38.54733  ? 105 LYS   A CG   1 
ATOM   714  C  CD   . LYS   A 1 105 ? -5.95166  -6.68758  20.50917  1.000 47.19529  ? 105 LYS   A CD   1 
ATOM   715  C  CE   . LYS   A 1 105 ? -7.17347  -7.17013  21.32275  1.000 53.15045  ? 105 LYS   A CE   1 
ATOM   716  N  NZ   . LYS   A 1 105 ? -8.35796  -6.29851  21.01745  1.000 53.39473  ? 105 LYS   A NZ   1 
ATOM   717  N  N    . MET   A 1 106 ? -1.91330  -5.66661  18.17933  1.000 49.45087  ? 106 MET   A N    1 
ATOM   718  C  CA   . MET   A 1 106 ? -0.87631  -5.08981  17.30992  1.000 51.87575  ? 106 MET   A CA   1 
ATOM   719  C  C    . MET   A 1 106 ? 0.51420   -5.40418  17.86004  1.000 55.15680  ? 106 MET   A C    1 
ATOM   720  O  O    . MET   A 1 106 ? 1.38384   -4.53196  17.90723  1.000 53.54801  ? 106 MET   A O    1 
ATOM   721  C  CB   . MET   A 1 106 ? -1.01684  -3.55589  17.18702  1.000 49.12269  ? 106 MET   A CB   1 
ATOM   722  C  CG   . MET   A 1 106 ? -2.31263  -2.94012  16.64602  1.000 50.23300  ? 106 MET   A CG   1 
ATOM   723  S  SD   . MET   A 1 106 ? -2.48569  -3.11476  14.87616  1.000 58.39668  ? 106 MET   A SD   1 
ATOM   724  C  CE   . MET   A 1 106 ? -2.78537  -4.86666  14.76764  1.000 70.24117  ? 106 MET   A CE   1 
ATOM   725  N  N    . SER   A 1 107 ? 0.71116   -6.62527  18.35998  1.000 47.74449  ? 107 SER   A N    1 
ATOM   726  C  CA   . SER   A 1 107 ? 1.99726   -7.03306  18.90575  1.000 59.64188  ? 107 SER   A CA   1 
ATOM   727  C  C    . SER   A 1 107 ? 2.37932   -6.20531  20.13857  1.000 62.89270  ? 107 SER   A C    1 
ATOM   728  O  O    . SER   A 1 107 ? 3.56344   -6.07688  20.46110  1.000 63.86194  ? 107 SER   A O    1 
ATOM   729  C  CB   . SER   A 1 107 ? 3.09304   -6.92567  17.82645  1.000 70.38621  ? 107 SER   A CB   1 
ATOM   730  O  OG   . SER   A 1 107 ? 2.67076   -7.37486  16.52504  1.000 68.53822  ? 107 SER   A OG   1 
ATOM   731  N  N    . GLY   A 1 108 ? 1.39737   -5.60065  20.81802  1.000 51.40836  ? 108 GLY   A N    1 
ATOM   732  C  CA   . GLY   A 1 108 ? 1.64667   -4.64343  21.87411  1.000 52.40947  ? 108 GLY   A CA   1 
ATOM   733  C  C    . GLY   A 1 108 ? 2.28428   -3.34511  21.42592  1.000 55.76260  ? 108 GLY   A C    1 
ATOM   734  O  O    . GLY   A 1 108 ? 2.42936   -2.43557  22.26117  1.000 53.10624  ? 108 GLY   A O    1 
ATOM   735  N  N    . ASP   A 1 109 ? 2.57577   -3.19389  20.11951  1.000 40.48432  ? 109 ASP   A N    1 
ATOM   736  C  CA   . ASP   A 1 109 ? 3.45325   -2.14018  19.61032  1.000 47.31040  ? 109 ASP   A CA   1 
ATOM   737  C  C    . ASP   A 1 109 ? 2.75126   -0.78053  19.66334  1.000 47.21918  ? 109 ASP   A C    1 
ATOM   738  O  O    . ASP   A 1 109 ? 1.82212   -0.50536  18.88706  1.000 46.30803  ? 109 ASP   A O    1 
ATOM   739  C  CB   . ASP   A 1 109 ? 3.89223   -2.52886  18.19500  1.000 48.91449  ? 109 ASP   A CB   1 
ATOM   740  C  CG   . ASP   A 1 109 ? 4.87397   -1.54892  17.57349  1.000 56.14698  ? 109 ASP   A CG   1 
ATOM   741  O  OD1  . ASP   A 1 109 ? 4.92934   -0.37378  18.00075  1.000 62.26306  ? 109 ASP   A OD1  1 
ATOM   742  O  OD2  . ASP   A 1 109 ? 5.58873   -1.95738  16.61554  1.000 67.19602  ? 109 ASP   A OD2  1 
ATOM   743  N  N    . LEU   A 1 110 ? 3.23713   0.10997   20.53451  1.000 45.75129  ? 110 LEU   A N    1 
ATOM   744  C  CA   . LEU   A 1 110 ? 2.53284   1.36952   20.77971  1.000 50.76102  ? 110 LEU   A CA   1 
ATOM   745  C  C    . LEU   A 1 110 ? 2.58377   2.29503   19.55822  1.000 46.79083  ? 110 LEU   A C    1 
ATOM   746  O  O    . LEU   A 1 110 ? 1.67528   3.11905   19.34908  1.000 41.14986  ? 110 LEU   A O    1 
ATOM   747  C  CB   . LEU   A 1 110 ? 3.12551   2.03846   22.02205  1.000 58.15378  ? 110 LEU   A CB   1 
ATOM   748  C  CG   . LEU   A 1 110 ? 2.50179   1.51109   23.33068  1.000 57.39393  ? 110 LEU   A CG   1 
ATOM   749  C  CD1  . LEU   A 1 110 ? 3.55731   1.40680   24.47455  1.000 64.23178  ? 110 LEU   A CD1  1 
ATOM   750  C  CD2  . LEU   A 1 110 ? 1.22041   2.28191   23.76630  1.000 63.42553  ? 110 LEU   A CD2  1 
ATOM   751  N  N    . LYS   A 1 111 ? 3.61598   2.15272   18.72516  1.000 45.84892  ? 111 LYS   A N    1 
ATOM   752  C  CA   . LYS   A 1 111 ? 3.68734   2.92416   17.48442  1.000 44.02649  ? 111 LYS   A CA   1 
ATOM   753  C  C    . LYS   A 1 111 ? 2.56109   2.54051   16.51715  1.000 40.75082  ? 111 LYS   A C    1 
ATOM   754  O  O    . LYS   A 1 111 ? 1.94397   3.41095   15.88765  1.000 42.39427  ? 111 LYS   A O    1 
ATOM   755  C  CB   . LYS   A 1 111 ? 5.03897   2.68732   16.79720  1.000 48.83553  ? 111 LYS   A CB   1 
ATOM   756  C  CG   . LYS   A 1 111 ? 6.26658   2.97539   17.68893  1.000 63.71818  ? 111 LYS   A CG   1 
ATOM   757  C  CD   . LYS   A 1 111 ? 6.74323   4.42303   17.59325  1.000 68.65559  ? 111 LYS   A CD   1 
ATOM   758  C  CE   . LYS   A 1 111 ? 7.41278   4.70037   16.26728  1.000 76.25030  ? 111 LYS   A CE   1 
ATOM   759  N  NZ   . LYS   A 1 111 ? 7.06194   6.06804   15.76497  1.000 83.24090  ? 111 LYS   A NZ   1 
ATOM   760  N  N    . LYS   A 1 112 ? 2.33940   1.23538   16.32376  1.000 41.70310  ? 112 LYS   A N    1 
ATOM   761  C  CA   . LYS   A 1 112 ? 1.26620   0.78966   15.42735  1.000 42.22346  ? 112 LYS   A CA   1 
ATOM   762  C  C    . LYS   A 1 112 ? -0.08659  1.18354   16.01090  1.000 40.05217  ? 112 LYS   A C    1 
ATOM   763  O  O    . LYS   A 1 112 ? -0.99638  1.58164   15.27714  1.000 40.45061  ? 112 LYS   A O    1 
ATOM   764  C  CB   . LYS   A 1 112 ? 1.34365   -0.72386  15.25006  1.000 41.78373  ? 112 LYS   A CB   1 
ATOM   765  C  CG   . LYS   A 1 112 ? 2.62015   -1.22997  14.63762  1.000 46.84112  ? 112 LYS   A CG   1 
ATOM   766  C  CD   . LYS   A 1 112 ? 2.54427   -2.71745  14.41900  1.000 54.92013  ? 112 LYS   A CD   1 
ATOM   767  C  CE   . LYS   A 1 112 ? 3.90902   -3.28366  13.99814  1.000 63.36541  ? 112 LYS   A CE   1 
ATOM   768  N  NZ   . LYS   A 1 112 ? 3.82938   -4.70584  13.64068  1.000 59.95237  ? 112 LYS   A NZ   1 
ATOM   769  N  N    . ILE   A 1 113 ? -0.23518  1.03938   17.33467  1.000 38.44518  ? 113 ILE   A N    1 
ATOM   770  C  CA   . ILE   A 1 113 ? -1.50649  1.36571   17.99269  1.000 39.95673  ? 113 ILE   A CA   1 
ATOM   771  C  C    . ILE   A 1 113 ? -1.82478  2.84477   17.81680  1.000 39.37299  ? 113 ILE   A C    1 
ATOM   772  O  O    . ILE   A 1 113 ? -2.95808  3.21899   17.50433  1.000 39.74451  ? 113 ILE   A O    1 
ATOM   773  C  CB   . ILE   A 1 113 ? -1.44808  0.95136   19.47138  1.000 39.58557  ? 113 ILE   A CB   1 
ATOM   774  C  CG1  . ILE   A 1 113 ? -1.47036  -0.56931  19.58708  1.000 37.18023  ? 113 ILE   A CG1  1 
ATOM   775  C  CG2  . ILE   A 1 113 ? -2.54623  1.64605   20.28843  1.000 37.66434  ? 113 ILE   A CG2  1 
ATOM   776  C  CD1  . ILE   A 1 113 ? -1.04186  -1.03013  21.07159  1.000 39.78597  ? 113 ILE   A CD1  1 
ATOM   777  N  N    . LYS   A 1 114 ? -0.81552  3.71220   17.95112  1.000 39.02439  ? 114 LYS   A N    1 
ATOM   778  C  CA   . LYS   A 1 114 ? -1.04161  5.13032   17.68274  1.000 41.66746  ? 114 LYS   A CA   1 
ATOM   779  C  C    . LYS   A 1 114 ? -1.42507  5.38487   16.22055  1.000 45.82338  ? 114 LYS   A C    1 
ATOM   780  O  O    . LYS   A 1 114 ? -2.28251  6.24591   15.93125  1.000 39.50060  ? 114 LYS   A O    1 
ATOM   781  C  CB   . LYS   A 1 114 ? 0.20071   5.94467   18.07860  1.000 50.89769  ? 114 LYS   A CB   1 
ATOM   782  C  CG   . LYS   A 1 114 ? 0.05690   7.44695   17.80564  1.000 55.82881  ? 114 LYS   A CG   1 
ATOM   783  C  CD   . LYS   A 1 114 ? 1.39233   8.21247   17.91448  1.000 65.32091  ? 114 LYS   A CD   1 
ATOM   784  C  CE   . LYS   A 1 114 ? 2.45332   7.81983   16.86381  1.000 67.06555  ? 114 LYS   A CE   1 
ATOM   785  N  NZ   . LYS   A 1 114 ? 3.86232   7.59122   17.43555  1.000 70.18788  ? 114 LYS   A NZ   1 
ATOM   786  N  N    . LYS   A 1 115 ? -0.77320  4.68499   15.27177  1.000 41.45859  ? 115 LYS   A N    1 
ATOM   787  C  CA   . LYS   A 1 115 ? -1.14057  4.86820   13.86606  1.000 40.69346  ? 115 LYS   A CA   1 
ATOM   788  C  C    . LYS   A 1 115 ? -2.59334  4.46515   13.61547  1.000 39.86849  ? 115 LYS   A C    1 
ATOM   789  O  O    . LYS   A 1 115 ? -3.34673  5.16723   12.91558  1.000 39.83590  ? 115 LYS   A O    1 
ATOM   790  C  CB   . LYS   A 1 115 ? -0.20196  4.05431   12.96280  1.000 45.90018  ? 115 LYS   A CB   1 
ATOM   791  C  CG   . LYS   A 1 115 ? 1.13769   4.76430   12.70898  1.000 54.78010  ? 115 LYS   A CG   1 
ATOM   792  C  CD   . LYS   A 1 115 ? 0.92048   5.62700   11.45135  1.000 64.40135  ? 115 LYS   A CD   1 
ATOM   793  C  CE   . LYS   A 1 115 ? 2.07247   6.54981   11.12521  1.000 69.77982  ? 115 LYS   A CE   1 
ATOM   794  N  NZ   . LYS   A 1 115 ? 1.63174   7.50539   10.04798  1.000 77.75712  ? 115 LYS   A NZ   1 
ATOM   795  N  N    . VAL   A 1 116 ? -2.98738  3.31620   14.15576  1.000 38.34451  ? 116 VAL   A N    1 
ATOM   796  C  CA   . VAL   A 1 116 ? -4.35273  2.84122   13.96251  1.000 42.95034  ? 116 VAL   A CA   1 
ATOM   797  C  C    . VAL   A 1 116 ? -5.33553  3.80330   14.60300  1.000 41.52595  ? 116 VAL   A C    1 
ATOM   798  O  O    . VAL   A 1 116 ? -6.40005  4.07279   14.04282  1.000 38.01394  ? 116 VAL   A O    1 
ATOM   799  C  CB   . VAL   A 1 116 ? -4.52033  1.41620   14.51070  1.000 41.88126  ? 116 VAL   A CB   1 
ATOM   800  C  CG1  . VAL   A 1 116 ? -6.02317  1.03450   14.50812  1.000 42.12512  ? 116 VAL   A CG1  1 
ATOM   801  C  CG2  . VAL   A 1 116 ? -3.69125  0.46206   13.65533  1.000 38.40772  ? 116 VAL   A CG2  1 
ATOM   802  N  N    . GLY   A 1 117 ? -5.01744  4.31633   15.80447  1.000 38.33833  ? 117 GLY   A N    1 
ATOM   803  C  CA   . GLY   A 1 117 ? -5.89540  5.30989   16.40924  1.000 38.39312  ? 117 GLY   A CA   1 
ATOM   804  C  C    . GLY   A 1 117 ? -6.06438  6.55190   15.54184  1.000 38.07220  ? 117 GLY   A C    1 
ATOM   805  O  O    . GLY   A 1 117 ? -7.15969  7.10500   15.43005  1.000 40.48008  ? 117 GLY   A O    1 
ATOM   806  N  N    . SER   A 1 118 ? -4.96280  7.03605   14.94030  1.000 35.94327  ? 118 SER   A N    1 
ATOM   807  C  CA   . SER   A 1 118 ? -5.07357  8.13951   13.97372  1.000 38.21947  ? 118 SER   A CA   1 
ATOM   808  C  C    . SER   A 1 118 ? -6.00505  7.78409   12.83495  1.000 37.37941  ? 118 SER   A C    1 
ATOM   809  O  O    . SER   A 1 118 ? -6.77124  8.63655   12.34783  1.000 42.45352  ? 118 SER   A O    1 
ATOM   810  C  CB   . SER   A 1 118 ? -3.68857  8.49449   13.39875  1.000 42.98641  ? 118 SER   A CB   1 
ATOM   811  O  OG   . SER   A 1 118 ? -2.87182  8.81993   14.54326  1.000 49.07541  ? 118 SER   A OG   1 
ATOM   812  N  N    . TYR   A 1 119 ? -5.89141  6.55046   12.32805  1.000 36.20131  ? 119 TYR   A N    1 
ATOM   813  C  CA   . TYR   A 1 119 ? -6.77823  6.14214   11.23978  1.000 36.12636  ? 119 TYR   A CA   1 
ATOM   814  C  C    . TYR   A 1 119 ? -8.25021  6.13140   11.69216  1.000 40.39460  ? 119 TYR   A C    1 
ATOM   815  O  O    . TYR   A 1 119 ? -9.14297  6.58039   10.95298  1.000 40.54022  ? 119 TYR   A O    1 
ATOM   816  C  CB   . TYR   A 1 119 ? -6.32650  4.77720   10.73161  1.000 39.16819  ? 119 TYR   A CB   1 
ATOM   817  C  CG   . TYR   A 1 119 ? -7.39131  4.04779   9.97600   1.000 39.40021  ? 119 TYR   A CG   1 
ATOM   818  C  CD1  . TYR   A 1 119 ? -7.66099  4.40434   8.66207   1.000 42.42088  ? 119 TYR   A CD1  1 
ATOM   819  C  CD2  . TYR   A 1 119 ? -8.07721  2.95894   10.52562  1.000 41.47403  ? 119 TYR   A CD2  1 
ATOM   820  C  CE1  . TYR   A 1 119 ? -8.63360  3.77458   7.94273   1.000 46.17637  ? 119 TYR   A CE1  1 
ATOM   821  C  CE2  . TYR   A 1 119 ? -9.10949  2.29813   9.75160   1.000 42.57970  ? 119 TYR   A CE2  1 
ATOM   822  C  CZ   . TYR   A 1 119 ? -9.32750  2.71629   8.48347   1.000 45.30124  ? 119 TYR   A CZ   1 
ATOM   823  O  OH   . TYR   A 1 119 ? -10.27115 2.10557   7.70429   1.000 49.00924  ? 119 TYR   A OH   1 
ATOM   824  N  N    . PHE   A 1 120 ? -8.51850  5.64909   12.91428  1.000 40.81405  ? 120 PHE   A N    1 
ATOM   825  C  CA   . PHE   A 1 120 ? -9.89789  5.66261   13.41525  1.000 41.80428  ? 120 PHE   A CA   1 
ATOM   826  C  C    . PHE   A 1 120 ? -10.44947 7.08537   13.39712  1.000 38.61817  ? 120 PHE   A C    1 
ATOM   827  O  O    . PHE   A 1 120 ? -11.60373 7.32234   13.01124  1.000 41.37401  ? 120 PHE   A O    1 
ATOM   828  C  CB   . PHE   A 1 120 ? -9.97155  5.08878   14.84105  1.000 38.45712  ? 120 PHE   A CB   1 
ATOM   829  C  CG   . PHE   A 1 120 ? -9.92511  3.57744   14.92270  1.000 36.56761  ? 120 PHE   A CG   1 
ATOM   830  C  CD1  . PHE   A 1 120 ? -9.56217  2.79392   13.84840  1.000 39.69374  ? 120 PHE   A CD1  1 
ATOM   831  C  CD2  . PHE   A 1 120 ? -10.23816 2.94777   16.11843  1.000 41.63224  ? 120 PHE   A CD2  1 
ATOM   832  C  CE1  . PHE   A 1 120 ? -9.50279  1.42004   13.94630  1.000 39.96501  ? 120 PHE   A CE1  1 
ATOM   833  C  CE2  . PHE   A 1 120 ? -10.18398 1.55646   16.22674  1.000 41.20926  ? 120 PHE   A CE2  1 
ATOM   834  C  CZ   . PHE   A 1 120 ? -9.84122  0.80063   15.13504  1.000 41.68949  ? 120 PHE   A CZ   1 
ATOM   835  N  N    . ILE   A 1 121 ? -9.65237  8.04587   13.86913  1.000 38.72153  ? 121 ILE   A N    1 
ATOM   836  C  CA   . ILE   A 1 121 ? -10.13775 9.42580   13.90506  1.000 40.65951  ? 121 ILE   A CA   1 
ATOM   837  C  C    . ILE   A 1 121 ? -10.43976 9.91846   12.50341  1.000 42.90168  ? 121 ILE   A C    1 
ATOM   838  O  O    . ILE   A 1 121 ? -11.41458 10.64446  12.27693  1.000 40.91427  ? 121 ILE   A O    1 
ATOM   839  C  CB   . ILE   A 1 121 ? -9.11110  10.32976  14.61981  1.000 38.65801  ? 121 ILE   A CB   1 
ATOM   840  C  CG1  . ILE   A 1 121 ? -9.14942  10.05499  16.12081  1.000 41.54922  ? 121 ILE   A CG1  1 
ATOM   841  C  CG2  . ILE   A 1 121 ? -9.40397  11.80993  14.37569  1.000 44.91011  ? 121 ILE   A CG2  1 
ATOM   842  C  CD1  . ILE   A 1 121 ? -8.00049  10.80902  16.87898  1.000 39.82784  ? 121 ILE   A CD1  1 
ATOM   843  N  N    . GLU   A 1 122 ? -9.57012  9.57138   11.54363  1.000 41.97987  ? 122 GLU   A N    1 
ATOM   844  C  CA   . GLU   A 1 122 ? -9.82412  9.94887   10.16039  1.000 43.86736  ? 122 GLU   A CA   1 
ATOM   845  C  C    . GLU   A 1 122 ? -11.16394 9.38843   9.67357   1.000 43.31226  ? 122 GLU   A C    1 
ATOM   846  O  O    . GLU   A 1 122 ? -11.95867 10.09525  9.03280   1.000 43.97686  ? 122 GLU   A O    1 
ATOM   847  C  CB   . GLU   A 1 122 ? -8.67197  9.43399   9.30269   1.000 42.71373  ? 122 GLU   A CB   1 
ATOM   848  C  CG   . GLU   A 1 122 ? -7.40863  10.24286  9.42109   1.000 57.14175  ? 122 GLU   A CG   1 
ATOM   849  C  CD   . GLU   A 1 122 ? -7.60940  11.64568  8.84564   1.000 71.04598  ? 122 GLU   A CD   1 
ATOM   850  O  OE1  . GLU   A 1 122 ? -7.59873  12.62914  9.63182   1.000 84.66002  ? 122 GLU   A OE1  1 
ATOM   851  O  OE2  . GLU   A 1 122 ? -7.72941  11.76077  7.59806   1.000 72.23642  ? 122 GLU   A OE2  1 
ATOM   852  N  N    . VAL   A 1 123 ? -11.41063 8.10113   9.94694   1.000 41.31677  ? 123 VAL   A N    1 
ATOM   853  C  CA   . VAL   A 1 123 ? -12.68953 7.47592   9.57622   1.000 42.83553  ? 123 VAL   A CA   1 
ATOM   854  C  C    . VAL   A 1 123 ? -13.84436 8.23134   10.21105  1.000 45.13123  ? 123 VAL   A C    1 
ATOM   855  O  O    . VAL   A 1 123 ? -14.80027 8.64383   9.53906   1.000 44.12724  ? 123 VAL   A O    1 
ATOM   856  C  CB   . VAL   A 1 123 ? -12.73115 5.99499   9.99202   1.000 40.65898  ? 123 VAL   A CB   1 
ATOM   857  C  CG1  . VAL   A 1 123 ? -14.13110 5.43913   9.70409   1.000 42.93045  ? 123 VAL   A CG1  1 
ATOM   858  C  CG2  . VAL   A 1 123 ? -11.66728 5.20286   9.31476   1.000 40.74172  ? 123 VAL   A CG2  1 
ATOM   859  N  N    . TRP   A 1 124 ? -13.77207 8.42998   11.52935  1.000 42.94394  ? 124 TRP   A N    1 
ATOM   860  C  CA   . TRP   A 1 124 ? -14.89887 9.03842   12.23559  1.000 43.51315  ? 124 TRP   A CA   1 
ATOM   861  C  C    . TRP   A 1 124 ? -15.18984 10.42917  11.70715  1.000 44.71422  ? 124 TRP   A C    1 
ATOM   862  O  O    . TRP   A 1 124 ? -16.35649 10.83436  11.62934  1.000 43.98799  ? 124 TRP   A O    1 
ATOM   863  C  CB   . TRP   A 1 124 ? -14.61915 9.10396   13.74300  1.000 36.66811  ? 124 TRP   A CB   1 
ATOM   864  C  CG   . TRP   A 1 124 ? -14.74633 7.79756   14.43969  1.000 41.08446  ? 124 TRP   A CG   1 
ATOM   865  C  CD1  . TRP   A 1 124 ? -15.67622 6.83590   14.21940  1.000 37.91413  ? 124 TRP   A CD1  1 
ATOM   866  C  CD2  . TRP   A 1 124 ? -13.89742 7.30922   15.50812  1.000 36.41198  ? 124 TRP   A CD2  1 
ATOM   867  N  NE1  . TRP   A 1 124 ? -15.46862 5.77373   15.07977  1.000 40.05863  ? 124 TRP   A NE1  1 
ATOM   868  C  CE2  . TRP   A 1 124 ? -14.38627 6.03585   15.87941  1.000 40.21707  ? 124 TRP   A CE2  1 
ATOM   869  C  CE3  . TRP   A 1 124 ? -12.77530 7.82138   16.16250  1.000 38.44204  ? 124 TRP   A CE3  1 
ATOM   870  C  CZ2  . TRP   A 1 124 ? -13.79878 5.26609   16.90326  1.000 38.27268  ? 124 TRP   A CZ2  1 
ATOM   871  C  CZ3  . TRP   A 1 124 ? -12.18705 7.06414   17.22428  1.000 38.45196  ? 124 TRP   A CZ3  1 
ATOM   872  C  CH2  . TRP   A 1 124 ? -12.68265 5.79369   17.55327  1.000 35.22795  ? 124 TRP   A CH2  1 
ATOM   873  N  N    . LYS   A 1 125 ? -14.13833 11.19962  11.37768  1.000 38.66945  ? 125 LYS   A N    1 
ATOM   874  C  CA   . LYS   A 1 125 ? -14.36563 12.51774  10.79879  1.000 41.91539  ? 125 LYS   A CA   1 
ATOM   875  C  C    . LYS   A 1 125 ? -14.97589 12.45878  9.40680   1.000 46.29639  ? 125 LYS   A C    1 
ATOM   876  O  O    . LYS   A 1 125 ? -15.50885 13.47021  8.94156   1.000 44.77964  ? 125 LYS   A O    1 
ATOM   877  C  CB   . LYS   A 1 125 ? -13.07582 13.32558  10.76156  1.000 46.34130  ? 125 LYS   A CB   1 
ATOM   878  C  CG   . LYS   A 1 125 ? -12.57119 13.60290  12.12876  1.000 44.86752  ? 125 LYS   A CG   1 
ATOM   879  C  CD   . LYS   A 1 125 ? -11.39174 14.55444  12.14031  1.000 56.07621  ? 125 LYS   A CD   1 
ATOM   880  C  CE   . LYS   A 1 125 ? -10.34368 14.12845  11.13515  1.000 60.20965  ? 125 LYS   A CE   1 
ATOM   881  N  NZ   . LYS   A 1 125 ? -9.12588  15.01814  11.22005  1.000 78.32044  ? 125 LYS   A NZ   1 
ATOM   882  N  N    . SER   A 1 126 ? -14.88946 11.33951  8.70142   1.000 42.36246  ? 126 SER   A N    1 
ATOM   883  C  CA   . SER   A 1 126 ? -15.66236 11.28124  7.44785   1.000 45.59335  ? 126 SER   A CA   1 
ATOM   884  C  C    . SER   A 1 126 ? -16.97594 10.50160  7.58657   1.000 51.60352  ? 126 SER   A C    1 
ATOM   885  O  O    . SER   A 1 126 ? -17.60097 10.15024  6.57085   1.000 52.80240  ? 126 SER   A O    1 
ATOM   886  C  CB   . SER   A 1 126 ? -14.79796 10.74033  6.30327   1.000 50.63073  ? 126 SER   A CB   1 
ATOM   887  O  OG   . SER   A 1 126 ? -14.35944 9.43396   6.61381   1.000 61.51961  ? 126 SER   A OG   1 
ATOM   888  N  N    . CYS   A 1 127 ? -17.44009 10.24753  8.80870   1.000 51.37174  ? 127 CYS   A N    1 
ATOM   889  C  CA   . CYS   A 1 127 ? -18.59300 9.36767   8.97153   1.000 56.14941  ? 127 CYS   A CA   1 
ATOM   890  C  C    . CYS   A 1 127 ? -19.91835 10.09799  9.05054   1.000 57.32834  ? 127 CYS   A C    1 
ATOM   891  O  O    . CYS   A 1 127 ? -20.96214 9.43838   9.21760   1.000 56.04470  ? 127 CYS   A O    1 
ATOM   892  C  CB   . CYS   A 1 127 ? -18.44367 8.54191   10.26481  1.000 48.82973  ? 127 CYS   A CB   1 
ATOM   893  S  SG   . CYS   A 1 127 ? -17.70651 6.92795   10.02208  1.000 54.00730  ? 127 CYS   A SG   1 
ATOM   894  N  N    . GLY   A 1 128 ? -19.93321 11.41747  8.88365   1.000 52.86275  ? 128 GLY   A N    1 
ATOM   895  C  CA   . GLY   A 1 128 ? -21.21291 12.08842  8.85285   1.000 58.71213  ? 128 GLY   A CA   1 
ATOM   896  C  C    . GLY   A 1 128 ? -21.69784 12.60806  10.18778  1.000 58.52487  ? 128 GLY   A C    1 
ATOM   897  O  O    . GLY   A 1 128 ? -22.91851 12.75656  10.36267  1.000 52.56664  ? 128 GLY   A O    1 
ATOM   898  N  N    . MET   A 1 129 ? -20.79978 12.86997  11.14906  1.000 52.74263  ? 129 MET   A N    1 
ATOM   899  C  CA   . MET   A 1 129 ? -21.22550 13.30957  12.46924  1.000 49.94550  ? 129 MET   A CA   1 
ATOM   900  C  C    . MET   A 1 129 ? -21.11635 14.82416  12.58224  1.000 51.89391  ? 129 MET   A C    1 
ATOM   901  O  O    . MET   A 1 129 ? -20.19147 15.43519  12.04385  1.000 52.39600  ? 129 MET   A O    1 
ATOM   902  C  CB   . MET   A 1 129 ? -20.36670 12.68145  13.57878  1.000 49.80258  ? 129 MET   A CB   1 
ATOM   903  C  CG   . MET   A 1 129 ? -20.68013 11.24719  13.91350  1.000 46.76551  ? 129 MET   A CG   1 
ATOM   904  S  SD   . MET   A 1 129 ? -19.62958 10.62890  15.25220  1.000 47.85947  ? 129 MET   A SD   1 
ATOM   905  C  CE   . MET   A 1 129 ? -17.95103 11.07232  14.73466  1.000 51.48274  ? 129 MET   A CE   1 
ATOM   906  N  N    . ASN   A 1 130 ? -22.05953 15.41549  13.31083  1.000 49.89470  ? 130 ASN   A N    1 
ATOM   907  C  CA   . ASN   A 1 130 ? -21.94758 16.80472  13.75106  1.000 51.85094  ? 130 ASN   A CA   1 
ATOM   908  C  C    . ASN   A 1 130 ? -20.88091 16.86020  14.82068  1.000 55.24383  ? 130 ASN   A C    1 
ATOM   909  O  O    . ASN   A 1 130 ? -20.96357 16.12860  15.80992  1.000 51.13802  ? 130 ASN   A O    1 
ATOM   910  C  CB   . ASN   A 1 130 ? -23.27613 17.31235  14.31062  1.000 52.96099  ? 130 ASN   A CB   1 
ATOM   911  C  CG   . ASN   A 1 130 ? -24.35958 17.27703  13.28457  1.000 67.34099  ? 130 ASN   A CG   1 
ATOM   912  O  OD1  . ASN   A 1 130 ? -24.09801 17.53605  12.11171  1.000 70.51131  ? 130 ASN   A OD1  1 
ATOM   913  N  ND2  . ASN   A 1 130 ? -25.57883 16.91899  13.69621  1.000 64.22931  ? 130 ASN   A ND2  1 
ATOM   914  N  N    . MET   A 1 131 ? -19.79477 17.57162  14.53659  1.000 54.34256  ? 131 MET   A N    1 
ATOM   915  C  CA   . MET   A 1 131 ? -18.62977 17.56237  15.40755  1.000 50.55441  ? 131 MET   A CA   1 
ATOM   916  C  C    . MET   A 1 131 ? -18.64197 18.66962  16.44604  1.000 50.11635  ? 131 MET   A C    1 
ATOM   917  O  O    . MET   A 1 131 ? -17.71513 18.72071  17.25977  1.000 45.01335  ? 131 MET   A O    1 
ATOM   918  C  CB   . MET   A 1 131 ? -17.34716 17.67727  14.56965  1.000 54.95630  ? 131 MET   A CB   1 
ATOM   919  C  CG   . MET   A 1 131 ? -17.26337 16.66206  13.43530  1.000 53.69080  ? 131 MET   A CG   1 
ATOM   920  S  SD   . MET   A 1 131 ? -17.20449 14.95779  14.04855  1.000 65.17734  ? 131 MET   A SD   1 
ATOM   921  C  CE   . MET   A 1 131 ? -15.60927 14.94437  14.81467  1.000 56.30896  ? 131 MET   A CE   1 
ATOM   922  N  N    . GLU   A 1 132 ? -19.62314 19.58767  16.45646  1.000 48.98706  ? 132 GLU   A N    1 
ATOM   923  C  CA   . GLU   A 1 132 ? -19.41665 20.69278  17.38653  1.000 53.71355  ? 132 GLU   A CA   1 
ATOM   924  C  C    . GLU   A 1 132 ? -19.33554 20.19644  18.83203  1.000 47.80314  ? 132 GLU   A C    1 
ATOM   925  O  O    . GLU   A 1 132 ? -18.65897 20.81651  19.66144  1.000 56.15698  ? 132 GLU   A O    1 
ATOM   926  C  CB   . GLU   A 1 132 ? -20.45535 21.80643  17.30102  1.000 61.01573  ? 132 GLU   A CB   1 
ATOM   927  C  CG   . GLU   A 1 132 ? -19.87174 22.90065  18.24746  1.000 71.60827  ? 132 GLU   A CG   1 
ATOM   928  C  CD   . GLU   A 1 132 ? -20.68249 24.15248  18.37337  1.000 89.78575  ? 132 GLU   A CD   1 
ATOM   929  O  OE1  . GLU   A 1 132 ? -21.77320 24.16397  17.76832  1.000 89.56040  ? 132 GLU   A OE1  1 
ATOM   930  O  OE2  . GLU   A 1 132 ? -20.22848 25.10640  19.07089  1.000 93.03304  ? 132 GLU   A OE2  1 
ATOM   931  N  N    . ASN   A 1 133 ? -20.06041 19.12599  19.16935  1.000 46.75583  ? 133 ASN   A N    1 
ATOM   932  C  CA   . ASN   A 1 133 ? -20.11800 18.58964  20.52967  1.000 43.87098  ? 133 ASN   A CA   1 
ATOM   933  C  C    . ASN   A 1 133 ? -19.46199 17.22578  20.65883  1.000 45.54596  ? 133 ASN   A C    1 
ATOM   934  O  O    . ASN   A 1 133 ? -19.86700 16.43728  21.51231  1.000 41.79075  ? 133 ASN   A O    1 
ATOM   935  C  CB   . ASN   A 1 133 ? -21.55383 18.53884  21.01527  1.000 47.63547  ? 133 ASN   A CB   1 
ATOM   936  C  CG   . ASN   A 1 133 ? -22.12334 19.90643  21.12991  1.000 43.48166  ? 133 ASN   A CG   1 
ATOM   937  O  OD1  . ASN   A 1 133 ? -23.05997 20.25900  20.41824  1.000 58.76826  ? 133 ASN   A OD1  1 
ATOM   938  N  ND2  . ASN   A 1 133 ? -21.55272 20.70627  21.99968  1.000 46.37302  ? 133 ASN   A ND2  1 
ATOM   939  N  N    . VAL   A 1 134 ? -18.49848 16.91286  19.78517  1.000 41.81161  ? 134 VAL   A N    1 
ATOM   940  C  CA   . VAL   A 1 134 ? -17.75453 15.65804  19.84140  1.000 38.63283  ? 134 VAL   A CA   1 
ATOM   941  C  C    . VAL   A 1 134 ? -16.27159 15.95213  20.08805  1.000 40.81819  ? 134 VAL   A C    1 
ATOM   942  O  O    . VAL   A 1 134 ? -15.73345 16.95138  19.60699  1.000 41.35063  ? 134 VAL   A O    1 
ATOM   943  C  CB   . VAL   A 1 134 ? -17.95488 14.84977  18.54327  1.000 39.37082  ? 134 VAL   A CB   1 
ATOM   944  C  CG1  . VAL   A 1 134 ? -17.14419 13.58075  18.52531  1.000 39.85940  ? 134 VAL   A CG1  1 
ATOM   945  C  CG2  . VAL   A 1 134 ? -19.45053 14.55071  18.30605  1.000 42.13714  ? 134 VAL   A CG2  1 
ATOM   946  N  N    . GLN   A 1 135 ? -15.64249 15.12201  20.90432  1.000 40.14004  ? 135 GLN   A N    1 
ATOM   947  C  CA   . GLN   A 1 135 ? -14.21059 15.19100  21.14790  1.000 40.50330  ? 135 GLN   A CA   1 
ATOM   948  C  C    . GLN   A 1 135 ? -13.59160 13.83390  20.91109  1.000 39.97766  ? 135 GLN   A C    1 
ATOM   949  O  O    . GLN   A 1 135 ? -14.20455 12.82140  21.21002  1.000 39.29134  ? 135 GLN   A O    1 
ATOM   950  C  CB   . GLN   A 1 135 ? -13.89392 15.54233  22.56606  1.000 44.19072  ? 135 GLN   A CB   1 
ATOM   951  C  CG   . GLN   A 1 135 ? -14.37379 16.83743  23.05057  1.000 46.70264  ? 135 GLN   A CG   1 
ATOM   952  C  CD   . GLN   A 1 135 ? -13.94548 16.95170  24.48833  1.000 54.19222  ? 135 GLN   A CD   1 
ATOM   953  O  OE1  . GLN   A 1 135 ? -14.72558 16.65814  25.40333  1.000 46.95256  ? 135 GLN   A OE1  1 
ATOM   954  N  NE2  . GLN   A 1 135 ? -12.67926 17.30489  24.70105  1.000 50.14569  ? 135 GLN   A NE2  1 
ATOM   955  N  N    . PHE   A 1 136 ? -12.34373 13.82494  20.44457  1.000 39.32398  ? 136 PHE   A N    1 
ATOM   956  C  CA   . PHE   A 1 136 ? -11.51738 12.62684  20.34562  1.000 39.46542  ? 136 PHE   A CA   1 
ATOM   957  C  C    . PHE   A 1 136 ? -10.42152 12.76881  21.39661  1.000 39.50479  ? 136 PHE   A C    1 
ATOM   958  O  O    . PHE   A 1 136 ? -9.59557  13.67852  21.29950  1.000 41.86024  ? 136 PHE   A O    1 
ATOM   959  C  CB   . PHE   A 1 136 ? -10.92729 12.48929  18.93472  1.000 38.64092  ? 136 PHE   A CB   1 
ATOM   960  C  CG   . PHE   A 1 136 ? -11.94220 12.40630  17.86570  1.000 40.25112  ? 136 PHE   A CG   1 
ATOM   961  C  CD1  . PHE   A 1 136 ? -12.68614 11.25504  17.72117  1.000 39.73761  ? 136 PHE   A CD1  1 
ATOM   962  C  CD2  . PHE   A 1 136 ? -12.16396 13.46866  16.99584  1.000 44.84049  ? 136 PHE   A CD2  1 
ATOM   963  C  CE1  . PHE   A 1 136 ? -13.65975 11.12315  16.72605  1.000 36.88020  ? 136 PHE   A CE1  1 
ATOM   964  C  CE2  . PHE   A 1 136 ? -13.13829 13.35759  15.96757  1.000 44.22177  ? 136 PHE   A CE2  1 
ATOM   965  C  CZ   . PHE   A 1 136 ? -13.89643 12.17609  15.86195  1.000 41.24037  ? 136 PHE   A CZ   1 
ATOM   966  N  N    . LEU   A 1 137 ? -10.44756 11.91981  22.43270  1.000 36.73686  ? 137 LEU   A N    1 
ATOM   967  C  CA   . LEU   A 1 137 ? -9.48808  11.98512  23.52800  1.000 36.36695  ? 137 LEU   A CA   1 
ATOM   968  C  C    . LEU   A 1 137 ? -8.67302  10.71482  23.50246  1.000 38.72469  ? 137 LEU   A C    1 
ATOM   969  O  O    . LEU   A 1 137 ? -9.23019  9.62017   23.43738  1.000 37.74575  ? 137 LEU   A O    1 
ATOM   970  C  CB   . LEU   A 1 137 ? -10.18534 12.14931  24.90167  1.000 35.00867  ? 137 LEU   A CB   1 
ATOM   971  C  CG   . LEU   A 1 137 ? -11.02219 13.42115  25.05068  1.000 41.14917  ? 137 LEU   A CG   1 
ATOM   972  C  CD1  . LEU   A 1 137 ? -11.63320 13.53972  26.43736  1.000 40.45576  ? 137 LEU   A CD1  1 
ATOM   973  C  CD2  . LEU   A 1 137 ? -10.23022 14.68421  24.70530  1.000 39.15894  ? 137 LEU   A CD2  1 
ATOM   974  N  N    . TRP   A 1 138 ? -7.36108  10.85429  23.60839  1.000 36.62341  ? 138 TRP   A N    1 
ATOM   975  C  CA   . TRP   A 1 138 ? -6.46913  9.70379   23.71082  1.000 39.37667  ? 138 TRP   A CA   1 
ATOM   976  C  C    . TRP   A 1 138 ? -6.24576  9.32851   25.17514  1.000 34.84422  ? 138 TRP   A C    1 
ATOM   977  O  O    . TRP   A 1 138 ? -5.91632  10.18876  25.99627  1.000 36.20589  ? 138 TRP   A O    1 
ATOM   978  C  CB   . TRP   A 1 138 ? -5.11772  10.02104  23.06708  1.000 37.71198  ? 138 TRP   A CB   1 
ATOM   979  C  CG   . TRP   A 1 138 ? -5.19528  10.20746  21.58789  1.000 37.40528  ? 138 TRP   A CG   1 
ATOM   980  C  CD1  . TRP   A 1 138 ? -5.66507  11.29669  20.89774  1.000 42.12587  ? 138 TRP   A CD1  1 
ATOM   981  C  CD2  . TRP   A 1 138 ? -4.73024  9.28155   20.60373  1.000 36.57719  ? 138 TRP   A CD2  1 
ATOM   982  N  NE1  . TRP   A 1 138 ? -5.55639  11.08081  19.54663  1.000 39.53760  ? 138 TRP   A NE1  1 
ATOM   983  C  CE2  . TRP   A 1 138 ? -4.97501  9.85419   19.33997  1.000 40.91307  ? 138 TRP   A CE2  1 
ATOM   984  C  CE3  . TRP   A 1 138 ? -4.18421  8.00351   20.67076  1.000 35.97891  ? 138 TRP   A CE3  1 
ATOM   985  C  CZ2  . TRP   A 1 138 ? -4.66086  9.19403   18.14320  1.000 44.55064  ? 138 TRP   A CZ2  1 
ATOM   986  C  CZ3  . TRP   A 1 138 ? -3.85679  7.35934   19.47459  1.000 35.40753  ? 138 TRP   A CZ3  1 
ATOM   987  C  CH2  . TRP   A 1 138 ? -4.09475  7.94905   18.24306  1.000 39.68659  ? 138 TRP   A CH2  1 
ATOM   988  N  N    . ALA   A 1 139 ? -6.39763  8.03473   25.49769  1.000 34.89686  ? 139 ALA   A N    1 
ATOM   989  C  CA   . ALA   A 1 139 ? -6.26945  7.60459   26.88795  1.000 34.61071  ? 139 ALA   A CA   1 
ATOM   990  C  C    . ALA   A 1 139 ? -4.90505  7.96895   27.45420  1.000 40.35173  ? 139 ALA   A C    1 
ATOM   991  O  O    . ALA   A 1 139 ? -4.80264  8.60333   28.50244  1.000 31.73751  ? 139 ALA   A O    1 
ATOM   992  C  CB   . ALA   A 1 139 ? -6.48610  6.10081   27.00293  1.000 31.92481  ? 139 ALA   A CB   1 
ATOM   993  N  N    . SER   A 1 140 ? -3.83611  7.58384   26.77251  1.000 39.12315  ? 140 SER   A N    1 
ATOM   994  C  CA   . SER   A 1 140 ? -2.52412  7.87016   27.34922  1.000 37.07395  ? 140 SER   A CA   1 
ATOM   995  C  C    . SER   A 1 140 ? -2.33263  9.37406   27.60127  1.000 41.13750  ? 140 SER   A C    1 
ATOM   996  O  O    . SER   A 1 140 ? -1.80493  9.77735   28.65157  1.000 42.63405  ? 140 SER   A O    1 
ATOM   997  C  CB   . SER   A 1 140 ? -1.44488  7.32814   26.42019  1.000 39.47957  ? 140 SER   A CB   1 
ATOM   998  O  OG   . SER   A 1 140 ? -1.57368  7.88467   25.13711  1.000 40.46419  ? 140 SER   A OG   1 
ATOM   999  N  N    . GLU   A 1 141 ? -2.71067  10.21971  26.63459  1.000 39.44631  ? 141 GLU   A N    1 
ATOM   1000 C  CA   . GLU   A 1 141 ? -2.51874  11.66258  26.79872  1.000 38.63354  ? 141 GLU   A CA   1 
ATOM   1001 C  C    . GLU   A 1 141 ? -3.28669  12.19804  27.99445  1.000 39.35778  ? 141 GLU   A C    1 
ATOM   1002 O  O    . GLU   A 1 141 ? -2.77410  13.00837  28.79181  1.000 40.53638  ? 141 GLU   A O    1 
ATOM   1003 C  CB   . GLU   A 1 141 ? -2.97645  12.40567  25.55557  1.000 42.74201  ? 141 GLU   A CB   1 
ATOM   1004 C  CG   . GLU   A 1 141 ? -2.16857  12.15451  24.33344  1.000 51.00812  ? 141 GLU   A CG   1 
ATOM   1005 C  CD   . GLU   A 1 141 ? -2.67663  12.98384  23.15373  1.000 48.73298  ? 141 GLU   A CD   1 
ATOM   1006 O  OE1  . GLU   A 1 141 ? -1.99315  12.93237  22.08318  1.000 73.04032  ? 141 GLU   A OE1  1 
ATOM   1007 O  OE2  . GLU   A 1 141 ? -3.71086  13.68822  23.28087  1.000 55.18924  ? 141 GLU   A OE2  1 
ATOM   1008 N  N    . GLU   A 1 142 ? -4.54388  11.79059  28.11861  1.000 38.08288  ? 142 GLU   A N    1 
ATOM   1009 C  CA   . GLU   A 1 142 ? -5.38175  12.35971  29.17580  1.000 37.04738  ? 142 GLU   A CA   1 
ATOM   1010 C  C    . GLU   A 1 142 ? -4.97268  11.83810  30.53624  1.000 34.43781  ? 142 GLU   A C    1 
ATOM   1011 O  O    . GLU   A 1 142 ? -4.94585  12.58595  31.51584  1.000 38.76001  ? 142 GLU   A O    1 
ATOM   1012 C  CB   . GLU   A 1 142 ? -6.85377  12.02960  28.89427  1.000 37.37491  ? 142 GLU   A CB   1 
ATOM   1013 C  CG   . GLU   A 1 142 ? -7.31024  12.61905  27.58069  1.000 36.95568  ? 142 GLU   A CG   1 
ATOM   1014 C  CD   . GLU   A 1 142 ? -7.19592  14.13062  27.56961  1.000 46.36870  ? 142 GLU   A CD   1 
ATOM   1015 O  OE1  . GLU   A 1 142 ? -7.62998  14.76137  28.56593  1.000 45.30526  ? 142 GLU   A OE1  1 
ATOM   1016 O  OE2  . GLU   A 1 142 ? -6.63411  14.68458  26.59258  1.000 44.33727  ? 142 GLU   A OE2  1 
ATOM   1017 N  N    . ILE   A 1 143 ? -4.61435  10.55718  30.61265  1.000 35.03121  ? 143 ILE   A N    1 
ATOM   1018 C  CA   . ILE   A 1 143 ? -4.16754  10.01060  31.86815  1.000 35.03560  ? 143 ILE   A CA   1 
ATOM   1019 C  C    . ILE   A 1 143 ? -2.89998  10.72147  32.31301  1.000 38.80603  ? 143 ILE   A C    1 
ATOM   1020 O  O    . ILE   A 1 143 ? -2.77440  11.09228  33.48220  1.000 32.89426  ? 143 ILE   A O    1 
ATOM   1021 C  CB   . ILE   A 1 143 ? -3.95871  8.49497   31.75506  1.000 34.51091  ? 143 ILE   A CB   1 
ATOM   1022 C  CG1  . ILE   A 1 143 ? -5.32112  7.78129   31.62906  1.000 32.38598  ? 143 ILE   A CG1  1 
ATOM   1023 C  CG2  . ILE   A 1 143 ? -3.18126  7.97829   32.95917  1.000 36.80968  ? 143 ILE   A CG2  1 
ATOM   1024 C  CD1  . ILE   A 1 143 ? -5.13277  6.40689   31.12836  1.000 35.67660  ? 143 ILE   A CD1  1 
ATOM   1025 N  N    . ASN   A 1 144 ? -1.96044  10.95247  31.38919  1.000 38.53867  ? 144 ASN   A N    1 
ATOM   1026 C  CA   . ASN   A 1 144 ? -0.71086  11.59793  31.80574  1.000 42.23901  ? 144 ASN   A CA   1 
ATOM   1027 C  C    . ASN   A 1 144 ? -0.85684  13.09450  32.08196  1.000 42.10713  ? 144 ASN   A C    1 
ATOM   1028 O  O    . ASN   A 1 144 ? 0.02802   13.66761  32.73379  1.000 47.19913  ? 144 ASN   A O    1 
ATOM   1029 C  CB   . ASN   A 1 144 ? 0.38224   11.37120  30.76795  1.000 37.67801  ? 144 ASN   A CB   1 
ATOM   1030 C  CG   . ASN   A 1 144 ? 0.91118   9.96470   30.81505  1.000 39.49502  ? 144 ASN   A CG   1 
ATOM   1031 O  OD1  . ASN   A 1 144 ? 1.16566   9.44001   31.89641  1.000 46.15038  ? 144 ASN   A OD1  1 
ATOM   1032 N  ND2  . ASN   A 1 144 ? 1.06214   9.33177   29.65108  1.000 44.90180  ? 144 ASN   A ND2  1 
ATOM   1033 N  N    . LYS   A 1 145 ? -1.94320  13.72979  31.64622  1.000 43.40125  ? 145 LYS   A N    1 
ATOM   1034 C  CA   . LYS   A 1 145 ? -2.23476  15.09143  32.11429  1.000 41.16078  ? 145 LYS   A CA   1 
ATOM   1035 C  C    . LYS   A 1 145 ? -2.62133  15.14405  33.60222  1.000 45.44504  ? 145 LYS   A C    1 
ATOM   1036 O  O    . LYS   A 1 145 ? -2.39923  16.17434  34.25145  1.000 43.23471  ? 145 LYS   A O    1 
ATOM   1037 C  CB   . LYS   A 1 145 ? -3.38298  15.71807  31.29790  1.000 43.51629  ? 145 LYS   A CB   1 
ATOM   1038 C  CG   . LYS   A 1 145 ? -3.05994  16.00100  29.81053  1.000 46.85934  ? 145 LYS   A CG   1 
ATOM   1039 C  CD   . LYS   A 1 145 ? -4.30128  16.47717  29.02891  1.000 49.12137  ? 145 LYS   A CD   1 
ATOM   1040 C  CE   . LYS   A 1 145 ? -3.97908  16.61410  27.54001  1.000 50.88049  ? 145 LYS   A CE   1 
ATOM   1041 N  NZ   . LYS   A 1 145 ? -5.23071  16.94206  26.77907  1.000 59.58712  ? 145 LYS   A NZ   1 
ATOM   1042 N  N    . LYS   A 1 146 ? -3.23548  14.08242  34.14640  1.000 38.71706  ? 146 LYS   A N    1 
ATOM   1043 C  CA   . LYS   A 1 146 ? -3.73354  14.06091  35.53712  1.000 41.16515  ? 146 LYS   A CA   1 
ATOM   1044 C  C    . LYS   A 1 146 ? -3.46594  12.69698  36.16063  1.000 34.66483  ? 146 LYS   A C    1 
ATOM   1045 O  O    . LYS   A 1 146 ? -4.36938  12.00098  36.62774  1.000 33.36666  ? 146 LYS   A O    1 
ATOM   1046 C  CB   . LYS   A 1 146 ? -5.22021  14.42450  35.57972  1.000 41.32322  ? 146 LYS   A CB   1 
ATOM   1047 C  CG   . LYS   A 1 146 ? -5.47464  15.79285  35.05778  1.000 38.46308  ? 146 LYS   A CG   1 
ATOM   1048 C  CD   . LYS   A 1 146 ? -6.87969  16.28918  35.42925  1.000 47.75394  ? 146 LYS   A CD   1 
ATOM   1049 C  CE   . LYS   A 1 146 ? -7.94525  15.76085  34.47252  1.000 60.63816  ? 146 LYS   A CE   1 
ATOM   1050 N  NZ   . LYS   A 1 146 ? -9.37115  16.12336  34.87688  1.000 62.56375  ? 146 LYS   A NZ   1 
ATOM   1051 N  N    . PRO   A 1 147 ? -2.20273  12.29590  36.21954  1.000 35.13265  ? 147 PRO   A N    1 
ATOM   1052 C  CA   . PRO   A 1 147 ? -1.91556  10.90357  36.59180  1.000 36.45042  ? 147 PRO   A CA   1 
ATOM   1053 C  C    . PRO   A 1 147 ? -2.12159  10.63262  38.06777  1.000 33.19487  ? 147 PRO   A C    1 
ATOM   1054 O  O    . PRO   A 1 147 ? -2.37310  9.48658   38.45206  1.000 35.15909  ? 147 PRO   A O    1 
ATOM   1055 C  CB   . PRO   A 1 147 ? -0.44168  10.72995  36.16827  1.000 44.41640  ? 147 PRO   A CB   1 
ATOM   1056 C  CG   . PRO   A 1 147 ? 0.13169   12.14270  36.28425  1.000 42.92799  ? 147 PRO   A CG   1 
ATOM   1057 C  CD   . PRO   A 1 147 ? -0.99345  13.04688  35.82630  1.000 36.54462  ? 147 PRO   A CD   1 
ATOM   1058 N  N    . ASN   A 1 148 ? -2.01202  11.63782  38.93914  1.000 32.76046  ? 148 ASN   A N    1 
ATOM   1059 C  CA   . ASN   A 1 148 ? -2.33872  11.37642  40.33189  1.000 37.85750  ? 148 ASN   A CA   1 
ATOM   1060 C  C    . ASN   A 1 148 ? -3.82898  11.08997  40.49676  1.000 38.52496  ? 148 ASN   A C    1 
ATOM   1061 O  O    . ASN   A 1 148 ? -4.23898  10.08653  41.11124  1.000 37.13649  ? 148 ASN   A O    1 
ATOM   1062 C  CB   . ASN   A 1 148 ? -1.90721  12.55887  41.21970  1.000 39.46590  ? 148 ASN   A CB   1 
ATOM   1063 C  CG   . ASN   A 1 148 ? -2.06713  12.23644  42.70948  1.000 44.83553  ? 148 ASN   A CG   1 
ATOM   1064 O  OD1  . ASN   A 1 148 ? -1.26375  11.52801  43.25673  1.000 42.29093  ? 148 ASN   A OD1  1 
ATOM   1065 N  ND2  . ASN   A 1 148 ? -3.12645  12.71101  43.33389  1.000 42.65848  ? 148 ASN   A ND2  1 
ATOM   1066 N  N    . GLU   A 1 149 ? -4.65840  11.96397  39.95655  1.000 35.82254  ? 149 GLU   A N    1 
ATOM   1067 C  CA   . GLU   A 1 149 ? -6.09256  11.69302  39.98412  1.000 38.82388  ? 149 GLU   A CA   1 
ATOM   1068 C  C    . GLU   A 1 149 ? -6.41225  10.31328  39.38296  1.000 39.22475  ? 149 GLU   A C    1 
ATOM   1069 O  O    . GLU   A 1 149 ? -7.14745  9.49854   39.98142  1.000 38.89400  ? 149 GLU   A O    1 
ATOM   1070 C  CB   . GLU   A 1 149 ? -6.81275  12.78421  39.18813  1.000 38.22812  ? 149 GLU   A CB   1 
ATOM   1071 C  CG   . GLU   A 1 149 ? -8.34129  12.60935  39.20936  1.000 39.53587  ? 149 GLU   A CG   1 
ATOM   1072 C  CD   . GLU   A 1 149 ? -9.05053  13.67877  38.35962  1.000 54.87715  ? 149 GLU   A CD   1 
ATOM   1073 O  OE1  . GLU   A 1 149 ? -8.47140  14.78648  38.18386  1.000 52.94133  ? 149 GLU   A OE1  1 
ATOM   1074 O  OE2  . GLU   A 1 149 ? -10.17061 13.40531  37.85490  1.000 56.45478  ? 149 GLU   A OE2  1 
ATOM   1075 N  N    . TYR   A 1 150 ? -5.85574  10.02878  38.19150  1.000 32.23758  ? 150 TYR   A N    1 
ATOM   1076 C  CA   . TYR   A 1 150 ? -6.26574  8.81681   37.48290  1.000 33.61819  ? 150 TYR   A CA   1 
ATOM   1077 C  C    . TYR   A 1 150 ? -5.83072  7.57931   38.24365  1.000 34.19821  ? 150 TYR   A C    1 
ATOM   1078 O  O    . TYR   A 1 150 ? -6.63516  6.69942   38.56228  1.000 31.13325  ? 150 TYR   A O    1 
ATOM   1079 C  CB   . TYR   A 1 150 ? -5.69965  8.79133   36.04749  1.000 33.03263  ? 150 TYR   A CB   1 
ATOM   1080 C  CG   . TYR   A 1 150 ? -6.18917  7.60092   35.26757  1.000 36.15734  ? 150 TYR   A CG   1 
ATOM   1081 C  CD1  . TYR   A 1 150 ? -7.46034  7.59366   34.69033  1.000 32.75458  ? 150 TYR   A CD1  1 
ATOM   1082 C  CD2  . TYR   A 1 150 ? -5.43590  6.47117   35.13705  1.000 30.31561  ? 150 TYR   A CD2  1 
ATOM   1083 C  CE1  . TYR   A 1 150 ? -7.89526  6.49077   33.96691  1.000 35.59110  ? 150 TYR   A CE1  1 
ATOM   1084 C  CE2  . TYR   A 1 150 ? -5.88686  5.34295   34.41288  1.000 30.00963  ? 150 TYR   A CE2  1 
ATOM   1085 C  CZ   . TYR   A 1 150 ? -7.12347  5.37697   33.82412  1.000 36.58147  ? 150 TYR   A CZ   1 
ATOM   1086 O  OH   . TYR   A 1 150 ? -7.56264  4.27619   33.10219  1.000 33.73413  ? 150 TYR   A OH   1 
ATOM   1087 N  N    . TRP   A 1 151 ? -4.53626  7.48326   38.55420  1.000 33.09785  ? 151 TRP   A N    1 
ATOM   1088 C  CA   . TRP   A 1 151 ? -4.11920  6.24453   39.17349  1.000 31.69035  ? 151 TRP   A CA   1 
ATOM   1089 C  C    . TRP   A 1 151 ? -4.63246  6.10670   40.58673  1.000 31.00772  ? 151 TRP   A C    1 
ATOM   1090 O  O    . TRP   A 1 151 ? -4.81266  4.97740   41.04646  1.000 33.19562  ? 151 TRP   A O    1 
ATOM   1091 C  CB   . TRP   A 1 151 ? -2.57220  6.13405   39.04986  1.000 29.05132  ? 151 TRP   A CB   1 
ATOM   1092 C  CG   . TRP   A 1 151 ? -2.19797  5.95496   37.56918  1.000 27.45048  ? 151 TRP   A CG   1 
ATOM   1093 C  CD1  . TRP   A 1 151 ? -1.65395  6.88682   36.73099  1.000 26.87219  ? 151 TRP   A CD1  1 
ATOM   1094 C  CD2  . TRP   A 1 151 ? -2.42962  4.77389   36.74397  1.000 27.22970  ? 151 TRP   A CD2  1 
ATOM   1095 N  NE1  . TRP   A 1 151 ? -1.50927  6.37359   35.47071  1.000 30.59134  ? 151 TRP   A NE1  1 
ATOM   1096 C  CE2  . TRP   A 1 151 ? -1.96957  5.07499   35.45864  1.000 27.65325  ? 151 TRP   A CE2  1 
ATOM   1097 C  CE3  . TRP   A 1 151 ? -2.95021  3.48439   37.00427  1.000 31.96007  ? 151 TRP   A CE3  1 
ATOM   1098 C  CZ2  . TRP   A 1 151 ? -2.00366  4.15279   34.39500  1.000 36.58372  ? 151 TRP   A CZ2  1 
ATOM   1099 C  CZ3  . TRP   A 1 151 ? -3.01402  2.53545   35.89705  1.000 27.61980  ? 151 TRP   A CZ3  1 
ATOM   1100 C  CH2  . TRP   A 1 151 ? -2.51303  2.88384   34.64242  1.000 33.14456  ? 151 TRP   A CH2  1 
ATOM   1101 N  N    . SER   A 1 152 ? -4.94869  7.21153   41.28050  1.000 32.81881  ? 152 SER   A N    1 
ATOM   1102 C  CA   . SER   A 1 152 ? -5.58758  7.07177   42.58412  1.000 34.73193  ? 152 SER   A CA   1 
ATOM   1103 C  C    . SER   A 1 152 ? -6.96202  6.44611   42.46554  1.000 34.60545  ? 152 SER   A C    1 
ATOM   1104 O  O    . SER   A 1 152 ? -7.34645  5.64945   43.32916  1.000 34.08049  ? 152 SER   A O    1 
ATOM   1105 C  CB   . SER   A 1 152 ? -5.67893  8.43197   43.27457  1.000 39.56095  ? 152 SER   A CB   1 
ATOM   1106 O  OG   . SER   A 1 152 ? -4.34828  8.91935   43.50700  1.000 38.45543  ? 152 SER   A OG   1 
ATOM   1107 N  N    . LEU   A 1 153 ? -7.71567  6.81999   41.41045  1.000 36.49478  ? 153 LEU   A N    1 
ATOM   1108 C  CA   . LEU   A 1 153 ? -8.99965  6.15640   41.14029  1.000 34.01593  ? 153 LEU   A CA   1 
ATOM   1109 C  C    . LEU   A 1 153 ? -8.78996  4.66390   40.90890  1.000 31.95679  ? 153 LEU   A C    1 
ATOM   1110 O  O    . LEU   A 1 153 ? -9.46575  3.82104   41.51334  1.000 33.46535  ? 153 LEU   A O    1 
ATOM   1111 C  CB   . LEU   A 1 153 ? -9.65116  6.77224   39.89546  1.000 37.17585  ? 153 LEU   A CB   1 
ATOM   1112 C  CG   . LEU   A 1 153 ? -10.67991 7.83370   40.05491  1.000 44.92781  ? 153 LEU   A CG   1 
ATOM   1113 C  CD1  . LEU   A 1 153 ? -11.08260 8.19845   38.62678  1.000 40.07590  ? 153 LEU   A CD1  1 
ATOM   1114 C  CD2  . LEU   A 1 153 ? -11.83806 7.32936   40.87406  1.000 42.58207  ? 153 LEU   A CD2  1 
ATOM   1115 N  N    . VAL   A 1 154 ? -7.85789  4.33576   40.00968  1.000 30.07591  ? 154 VAL   A N    1 
ATOM   1116 C  CA   . VAL   A 1 154 ? -7.58947  2.93436   39.68491  1.000 30.35895  ? 154 VAL   A CA   1 
ATOM   1117 C  C    . VAL   A 1 154 ? -7.30259  2.12370   40.95524  1.000 33.73280  ? 154 VAL   A C    1 
ATOM   1118 O  O    . VAL   A 1 154 ? -7.84050  1.02950   41.16413  1.000 35.21571  ? 154 VAL   A O    1 
ATOM   1119 C  CB   . VAL   A 1 154 ? -6.41288  2.83734   38.69909  1.000 28.68000  ? 154 VAL   A CB   1 
ATOM   1120 C  CG1  . VAL   A 1 154 ? -6.04538  1.37320   38.54229  1.000 31.91733  ? 154 VAL   A CG1  1 
ATOM   1121 C  CG2  . VAL   A 1 154 ? -6.76842  3.43859   37.30175  1.000 29.21178  ? 154 VAL   A CG2  1 
ATOM   1122 N  N    . LEU   A 1 155 ? -6.38860  2.62742   41.80217  1.000 31.64034  ? 155 LEU   A N    1 
ATOM   1123 C  CA   . LEU   A 1 155 ? -6.07294  1.92068   43.04523  1.000 32.29398  ? 155 LEU   A CA   1 
ATOM   1124 C  C    . LEU   A 1 155 ? -7.26080  1.84386   44.00414  1.000 35.19227  ? 155 LEU   A C    1 
ATOM   1125 O  O    . LEU   A 1 155 ? -7.47947  0.80375   44.64290  1.000 36.90289  ? 155 LEU   A O    1 
ATOM   1126 C  CB   . LEU   A 1 155 ? -4.86849  2.56805   43.73236  1.000 33.91810  ? 155 LEU   A CB   1 
ATOM   1127 C  CG   . LEU   A 1 155 ? -3.50215  2.10548   43.16817  1.000 35.40775  ? 155 LEU   A CG   1 
ATOM   1128 C  CD1  . LEU   A 1 155 ? -3.32754  2.35612   41.74637  1.000 38.41126  ? 155 LEU   A CD1  1 
ATOM   1129 C  CD2  . LEU   A 1 155 ? -2.40638  2.82324   43.99180  1.000 33.46934  ? 155 LEU   A CD2  1 
ATOM   1130 N  N    . ASP   A 1 156 ? -8.06231  2.91349   44.11211  1.000 30.74550  ? 156 ASP   A N    1 
ATOM   1131 C  CA   . ASP   A 1 156 ? -9.20736  2.82500   45.01588  1.000 34.31395  ? 156 ASP   A CA   1 
ATOM   1132 C  C    . ASP   A 1 156 ? -10.23294 1.78537   44.53158  1.000 35.60666  ? 156 ASP   A C    1 
ATOM   1133 O  O    . ASP   A 1 156 ? -10.77534 0.99756   45.32474  1.000 37.44107  ? 156 ASP   A O    1 
ATOM   1134 C  CB   . ASP   A 1 156 ? -9.83059  4.21741   45.22415  1.000 37.33417  ? 156 ASP   A CB   1 
ATOM   1135 C  CG   . ASP   A 1 156 ? -9.00698  5.07829   46.25727  1.000 56.50152  ? 156 ASP   A CG   1 
ATOM   1136 O  OD1  . ASP   A 1 156 ? -9.16380  6.33465   46.26124  1.000 53.44013  ? 156 ASP   A OD1  1 
ATOM   1137 O  OD2  . ASP   A 1 156 ? -8.16883  4.49286   47.05539  1.000 48.46669  ? 156 ASP   A OD2  1 
ATOM   1138 N  N    . ILE   A 1 157 ? -10.45867 1.73176   43.22721  1.000 34.15690  ? 157 ILE   A N    1 
ATOM   1139 C  CA   . ILE   A 1 157 ? -11.28664 0.68247   42.64825  1.000 35.56788  ? 157 ILE   A CA   1 
ATOM   1140 C  C    . ILE   A 1 157 ? -10.70907 -0.67631  42.96348  1.000 33.89885  ? 157 ILE   A C    1 
ATOM   1141 O  O    . ILE   A 1 157 ? -11.43568 -1.60589  43.32558  1.000 33.34024  ? 157 ILE   A O    1 
ATOM   1142 C  CB   . ILE   A 1 157 ? -11.43882 0.89684   41.13387  1.000 34.43710  ? 157 ILE   A CB   1 
ATOM   1143 C  CG1  . ILE   A 1 157 ? -12.29579 2.13955   40.92643  1.000 37.37739  ? 157 ILE   A CG1  1 
ATOM   1144 C  CG2  . ILE   A 1 157 ? -11.98538 -0.36975  40.48112  1.000 35.78771  ? 157 ILE   A CG2  1 
ATOM   1145 C  CD1  . ILE   A 1 157 ? -12.24096 2.67400   39.51684  1.000 38.21772  ? 157 ILE   A CD1  1 
ATOM   1146 N  N    . SER   A 1 158 ? -9.39545  -0.83105  42.81683  1.000 32.00083  ? 158 SER   A N    1 
ATOM   1147 C  CA   . SER   A 1 158 ? -8.83646  -2.15350  43.08999  1.000 35.36935  ? 158 SER   A CA   1 
ATOM   1148 C  C    . SER   A 1 158 ? -9.02611  -2.56568  44.55196  1.000 35.80293  ? 158 SER   A C    1 
ATOM   1149 O  O    . SER   A 1 158 ? -9.11228  -3.76973  44.84681  1.000 36.39907  ? 158 SER   A O    1 
ATOM   1150 C  CB   . SER   A 1 158 ? -7.35808  -2.20379  42.69279  1.000 33.22872  ? 158 SER   A CB   1 
ATOM   1151 O  OG   . SER   A 1 158 ? -6.52291  -1.58902  43.68528  1.000 34.85512  ? 158 SER   A OG   1 
ATOM   1152 N  N    . ARG   A 1 159 ? -9.05131  -1.59420  45.47650  1.000 32.01671  ? 159 ARG   A N    1 
ATOM   1153 C  CA   . ARG   A 1 159 ? -9.28704  -1.89003  46.89048  1.000 34.73089  ? 159 ARG   A CA   1 
ATOM   1154 C  C    . ARG   A 1 159 ? -10.69748 -2.30647  47.17326  1.000 38.31332  ? 159 ARG   A C    1 
ATOM   1155 O  O    . ARG   A 1 159 ? -10.93888 -2.90447  48.22090  1.000 38.57436  ? 159 ARG   A O    1 
ATOM   1156 C  CB   . ARG   A 1 159 ? -9.02651  -0.67543  47.78067  1.000 41.11886  ? 159 ARG   A CB   1 
ATOM   1157 C  CG   . ARG   A 1 159 ? -7.59753  -0.23637  47.82823  1.000 41.67143  ? 159 ARG   A CG   1 
ATOM   1158 C  CD   . ARG   A 1 159 ? -7.46562  1.14295   48.44761  1.000 43.50666  ? 159 ARG   A CD   1 
ATOM   1159 N  NE   . ARG   A 1 159 ? -7.75325  1.15324   49.87366  1.000 46.67153  ? 159 ARG   A NE   1 
ATOM   1160 C  CZ   . ARG   A 1 159 ? -8.39371  2.13851   50.48771  1.000 48.77668  ? 159 ARG   A CZ   1 
ATOM   1161 N  NH1  . ARG   A 1 159 ? -8.95891  3.13064   49.80831  1.000 49.18657  ? 159 ARG   A NH1  1 
ATOM   1162 N  NH2  . ARG   A 1 159 ? -8.46037  2.13625   51.81318  1.000 54.82303  ? 159 ARG   A NH2  1 
ATOM   1163 N  N    . SER   A 1 160 ? -11.61870 -1.94692  46.29774  1.000 38.18394  ? 160 SER   A N    1 
ATOM   1164 C  CA   . SER   A 1 160 ? -13.05027 -2.13475  46.55440  1.000 37.25986  ? 160 SER   A CA   1 
ATOM   1165 C  C    . SER   A 1 160 ? -13.62107 -3.47762  46.09349  1.000 41.31235  ? 160 SER   A C    1 
ATOM   1166 O  O    . SER   A 1 160 ? -14.77549 -3.79872  46.44673  1.000 42.14312  ? 160 SER   A O    1 
ATOM   1167 C  CB   . SER   A 1 160 ? -13.81399 -1.01690  45.85718  1.000 43.86174  ? 160 SER   A CB   1 
ATOM   1168 O  OG   . SER   A 1 160 ? -13.37125 0.23737   46.34870  1.000 47.30597  ? 160 SER   A OG   1 
ATOM   1169 N  N    . PHE   A 1 161 ? -12.90848 -4.24643  45.26656  1.000 37.91201  ? 161 PHE   A N    1 
ATOM   1170 C  CA   . PHE   A 1 161 ? -13.50551 -5.42112  44.62482  1.000 35.70500  ? 161 PHE   A CA   1 
ATOM   1171 C  C    . PHE   A 1 161 ? -12.57215 -6.61399  44.70380  1.000 39.69424  ? 161 PHE   A C    1 
ATOM   1172 O  O    . PHE   A 1 161 ? -11.35379 -6.45823  44.61841  1.000 40.19751  ? 161 PHE   A O    1 
ATOM   1173 C  CB   . PHE   A 1 161 ? -13.83663 -5.17041  43.14160  1.000 41.00527  ? 161 PHE   A CB   1 
ATOM   1174 C  CG   . PHE   A 1 161 ? -14.86626 -4.12207  42.91939  1.000 37.49386  ? 161 PHE   A CG   1 
ATOM   1175 C  CD1  . PHE   A 1 161 ? -16.19942 -4.40074  43.15339  1.000 44.52214  ? 161 PHE   A CD1  1 
ATOM   1176 C  CD2  . PHE   A 1 161 ? -14.49604 -2.83828  42.53733  1.000 35.48953  ? 161 PHE   A CD2  1 
ATOM   1177 C  CE1  . PHE   A 1 161 ? -17.14797 -3.44922  42.94995  1.000 45.15366  ? 161 PHE   A CE1  1 
ATOM   1178 C  CE2  . PHE   A 1 161 ? -15.44349 -1.85922  42.36298  1.000 42.06845  ? 161 PHE   A CE2  1 
ATOM   1179 C  CZ   . PHE   A 1 161 ? -16.77708 -2.17217  42.55995  1.000 42.85270  ? 161 PHE   A CZ   1 
ATOM   1180 N  N    . ASN   A 1 162 ? -13.13751 -7.81390  44.80802  1.000 38.20315  ? 162 ASN   A N    1 
ATOM   1181 C  CA   . ASN   A 1 162 ? -12.23650 -8.95417  44.88723  1.000 44.34365  ? 162 ASN   A CA   1 
ATOM   1182 C  C    . ASN   A 1 162 ? -11.87949 -9.47020  43.50112  1.000 43.86363  ? 162 ASN   A C    1 
ATOM   1183 O  O    . ASN   A 1 162 ? -12.45850 -9.06185  42.48524  1.000 43.05910  ? 162 ASN   A O    1 
ATOM   1184 C  CB   . ASN   A 1 162 ? -12.81553 -10.06231 45.77473  1.000 47.26763  ? 162 ASN   A CB   1 
ATOM   1185 C  CG   . ASN   A 1 162 ? -14.10382 -10.66262 45.22560  1.000 44.42795  ? 162 ASN   A CG   1 
ATOM   1186 O  OD1  . ASN   A 1 162 ? -14.29837 -10.74680 44.04207  1.000 49.86935  ? 162 ASN   A OD1  1 
ATOM   1187 N  ND2  . ASN   A 1 162 ? -14.99199 -11.09317 46.12965  1.000 53.01190  ? 162 ASN   A ND2  1 
ATOM   1188 N  N    . ILE   A 1 163 ? -10.85900 -10.34596 43.45815  1.000 41.12750  ? 163 ILE   A N    1 
ATOM   1189 C  CA   . ILE   A 1 163 ? -10.31605 -10.80687 42.17818  1.000 41.85739  ? 163 ILE   A CA   1 
ATOM   1190 C  C    . ILE   A 1 163 ? -11.38593 -11.51921 41.34204  1.000 47.03305  ? 163 ILE   A C    1 
ATOM   1191 O  O    . ILE   A 1 163 ? -11.46783 -11.34447 40.11391  1.000 43.12221  ? 163 ILE   A O    1 
ATOM   1192 C  CB   . ILE   A 1 163 ? -9.10244  -11.71353 42.43126  1.000 41.62495  ? 163 ILE   A CB   1 
ATOM   1193 C  CG1  . ILE   A 1 163 ? -7.94199  -10.85031 42.86864  1.000 36.28554  ? 163 ILE   A CG1  1 
ATOM   1194 C  CG2  . ILE   A 1 163 ? -8.72279  -12.47225 41.17303  1.000 43.64903  ? 163 ILE   A CG2  1 
ATOM   1195 C  CD1  . ILE   A 1 163 ? -6.76728  -11.67337 43.51842  1.000 36.41231  ? 163 ILE   A CD1  1 
ATOM   1196 N  N    . ASN   A 1 164 ? -12.21671 -12.34324 41.98114  1.000 46.46033  ? 164 ASN   A N    1 
ATOM   1197 C  CA   . ASN   A 1 164 ? -13.23082 -13.06486 41.20246  1.000 45.32493  ? 164 ASN   A CA   1 
ATOM   1198 C  C    . ASN   A 1 164 ? -14.22297 -12.10708 40.53943  1.000 48.89498  ? 164 ASN   A C    1 
ATOM   1199 O  O    . ASN   A 1 164 ? -14.63876 -12.31504 39.38426  1.000 51.49919  ? 164 ASN   A O    1 
ATOM   1200 C  CB   . ASN   A 1 164 ? -13.95673 -14.06315 42.09476  1.000 48.09728  ? 164 ASN   A CB   1 
ATOM   1201 C  CG   . ASN   A 1 164 ? -13.06381 -15.23165 42.45416  1.000 59.47920  ? 164 ASN   A CG   1 
ATOM   1202 O  OD1  . ASN   A 1 164 ? -12.14465 -15.58784 41.68646  1.000 59.73148  ? 164 ASN   A OD1  1 
ATOM   1203 N  ND2  . ASN   A 1 164 ? -13.32811 -15.85296 43.60259  1.000 69.18098  ? 164 ASN   A ND2  1 
ATOM   1204 N  N    . ARG   A 1 165 ? -14.60816 -11.04718 41.25382  1.000 47.13463  ? 165 ARG   A N    1 
ATOM   1205 C  CA   . ARG   A 1 165 ? -15.52495 -10.06878 40.68245  1.000 53.95270  ? 165 ARG   A CA   1 
ATOM   1206 C  C    . ARG   A 1 165 ? -14.91410 -9.41537  39.46431  1.000 50.53117  ? 165 ARG   A C    1 
ATOM   1207 O  O    . ARG   A 1 165 ? -15.59318 -9.19456  38.46104  1.000 46.17553  ? 165 ARG   A O    1 
ATOM   1208 C  CB   . ARG   A 1 165 ? -15.90040 -9.00009  41.69961  1.000 46.65565  ? 165 ARG   A CB   1 
ATOM   1209 C  CG   . ARG   A 1 165 ? -16.74978 -7.91483  41.08600  1.000 50.91434  ? 165 ARG   A CG   1 
ATOM   1210 C  CD   . ARG   A 1 165 ? -18.05564 -8.50008  40.49095  1.000 53.79242  ? 165 ARG   A CD   1 
ATOM   1211 N  NE   . ARG   A 1 165 ? -18.82217 -7.39737  39.93177  1.000 47.87050  ? 165 ARG   A NE   1 
ATOM   1212 C  CZ   . ARG   A 1 165 ? -19.55623 -6.58717  40.68640  1.000 68.51834  ? 165 ARG   A CZ   1 
ATOM   1213 N  NH1  . ARG   A 1 165 ? -19.61447 -6.74158  42.00867  1.000 62.27848  ? 165 ARG   A NH1  1 
ATOM   1214 N  NH2  . ARG   A 1 165 ? -20.25485 -5.60537  40.10583  1.000 61.24721  ? 165 ARG   A NH2  1 
ATOM   1215 N  N    . MET   A 1 166 ? -13.62110 -9.13328  39.52746  1.000 44.82652  ? 166 MET   A N    1 
ATOM   1216 C  CA   . MET   A 1 166 ? -12.96081 -8.47311  38.42459  1.000 45.70266  ? 166 MET   A CA   1 
ATOM   1217 C  C    . MET   A 1 166 ? -12.74316 -9.44034  37.26098  1.000 45.12104  ? 166 MET   A C    1 
ATOM   1218 O  O    . MET   A 1 166 ? -12.81142 -9.02727  36.10850  1.000 45.52351  ? 166 MET   A O    1 
ATOM   1219 C  CB   . MET   A 1 166 ? -11.63623 -7.87074  38.93912  1.000 41.96216  ? 166 MET   A CB   1 
ATOM   1220 C  CG   . MET   A 1 166 ? -11.14086 -6.75703  38.06933  1.000 42.75254  ? 166 MET   A CG   1 
ATOM   1221 S  SD   . MET   A 1 166 ? -12.20961 -5.31960  38.16574  1.000 46.39882  ? 166 MET   A SD   1 
ATOM   1222 C  CE   . MET   A 1 166 ? -12.56730 -5.18093  39.92858  1.000 37.80893  ? 166 MET   A CE   1 
ATOM   1223 N  N    . LYS   A 1 167 ? -12.48804 -10.72446 37.54113  1.000 44.67994  ? 167 LYS   A N    1 
ATOM   1224 C  CA   . LYS   A 1 167 ? -12.36981 -11.70442 36.47215  1.000 41.00883  ? 167 LYS   A CA   1 
ATOM   1225 C  C    . LYS   A 1 167 ? -13.66672 -11.84094 35.71395  1.000 47.08710  ? 167 LYS   A C    1 
ATOM   1226 O  O    . LYS   A 1 167 ? -13.65599 -12.13673 34.51289  1.000 45.41254  ? 167 LYS   A O    1 
ATOM   1227 C  CB   . LYS   A 1 167 ? -11.96589 -13.05705 37.02969  1.000 44.31352  ? 167 LYS   A CB   1 
ATOM   1228 C  CG   . LYS   A 1 167 ? -10.50625 -13.08016 37.50574  1.000 48.43705  ? 167 LYS   A CG   1 
ATOM   1229 C  CD   . LYS   A 1 167 ? -10.08756 -14.42763 38.10927  1.000 52.25312  ? 167 LYS   A CD   1 
ATOM   1230 C  CE   . LYS   A 1 167 ? -9.75541  -15.48966 37.11059  1.000 56.53710  ? 167 LYS   A CE   1 
ATOM   1231 N  NZ   . LYS   A 1 167 ? -9.78711  -16.79209 37.84571  1.000 67.80406  ? 167 LYS   A NZ   1 
ATOM   1232 N  N    . ARG   A 1 168 ? -14.79884 -11.64219 36.39763  1.000 46.54202  ? 168 ARG   A N    1 
ATOM   1233 C  CA   . ARG   A 1 168 ? -16.04907 -11.66913 35.64170  1.000 45.54260  ? 168 ARG   A CA   1 
ATOM   1234 C  C    . ARG   A 1 168 ? -16.20502 -10.50038 34.66850  1.000 49.74192  ? 168 ARG   A C    1 
ATOM   1235 O  O    . ARG   A 1 168 ? -17.18522 -10.49722 33.91304  1.000 45.90342  ? 168 ARG   A O    1 
ATOM   1236 C  CB   . ARG   A 1 168 ? -17.26096 -11.75683 36.58355  1.000 46.34451  ? 168 ARG   A CB   1 
ATOM   1237 C  CG   . ARG   A 1 168 ? -17.29150 -13.13050 37.27614  1.000 53.85546  ? 168 ARG   A CG   1 
ATOM   1238 C  CD   . ARG   A 1 168 ? -18.65450 -13.50134 37.84398  1.000 57.91323  ? 168 ARG   A CD   1 
ATOM   1239 N  NE   . ARG   A 1 168 ? -18.57553 -13.15206 39.25163  1.000 74.00256  ? 168 ARG   A NE   1 
ATOM   1240 C  CZ   . ARG   A 1 168 ? -18.94973 -11.98729 39.76386  1.000 70.64451  ? 168 ARG   A CZ   1 
ATOM   1241 N  NH1  . ARG   A 1 168 ? -19.58861 -11.08183 39.02492  1.000 72.27157  ? 168 ARG   A NH1  1 
ATOM   1242 N  NH2  . ARG   A 1 168 ? -18.61070 -11.69926 41.02664  1.000 65.10917  ? 168 ARG   A NH2  1 
ATOM   1243 N  N    . CYS   A 1 169 ? -15.29103 -9.52957  34.64045  1.000 44.43214  ? 169 CYS   A N    1 
ATOM   1244 C  CA   . CYS   A 1 169 ? -15.32437 -8.47733  33.63367  1.000 44.94895  ? 169 CYS   A CA   1 
ATOM   1245 C  C    . CYS   A 1 169 ? -14.54818 -8.82590  32.38466  1.000 38.67086  ? 169 CYS   A C    1 
ATOM   1246 O  O    . CYS   A 1 169 ? -14.38523 -7.94843  31.53913  1.000 40.42980  ? 169 CYS   A O    1 
ATOM   1247 C  CB   . CYS   A 1 169 ? -14.73221 -7.16904  34.16755  1.000 44.69443  ? 169 CYS   A CB   1 
ATOM   1248 S  SG   . CYS   A 1 169 ? -15.74479 -6.42144  35.37912  1.000 46.17384  ? 169 CYS   A SG   1 
ATOM   1249 N  N    . LEU   A 1 170 ? -14.08116 -10.07858 32.24512  1.000 40.95371  ? 170 LEU   A N    1 
ATOM   1250 C  CA   . LEU   A 1 170 ? -13.17003 -10.45162 31.15421  1.000 39.26434  ? 170 LEU   A CA   1 
ATOM   1251 C  C    . LEU   A 1 170 ? -13.79050 -10.20509 29.76383  1.000 41.23512  ? 170 LEU   A C    1 
ATOM   1252 O  O    . LEU   A 1 170 ? -13.06358 -9.92036  28.79656  1.000 38.54183  ? 170 LEU   A O    1 
ATOM   1253 C  CB   . LEU   A 1 170 ? -12.78368 -11.92009 31.28607  1.000 42.79193  ? 170 LEU   A CB   1 
ATOM   1254 C  CG   . LEU   A 1 170 ? -11.72907 -12.38871 30.28517  1.000 56.50765  ? 170 LEU   A CG   1 
ATOM   1255 C  CD1  . LEU   A 1 170 ? -10.41284 -11.61864 30.48950  1.000 51.52441  ? 170 LEU   A CD1  1 
ATOM   1256 C  CD2  . LEU   A 1 170 ? -11.54053 -13.89624 30.36781  1.000 63.04735  ? 170 LEU   A CD2  1 
ATOM   1257 N  N    . LYS   A 1 171 ? -15.12144 -10.27439 29.64353  1.000 42.19659  ? 171 LYS   A N    1 
ATOM   1258 C  CA   . LYS   A 1 171 ? -15.73619 -10.07870 28.32049  1.000 39.63439  ? 171 LYS   A CA   1 
ATOM   1259 C  C    . LYS   A 1 171 ? -15.37439 -8.71382  27.73664  1.000 42.63370  ? 171 LYS   A C    1 
ATOM   1260 O  O    . LYS   A 1 171 ? -15.34196 -8.55036  26.50198  1.000 40.02433  ? 171 LYS   A O    1 
ATOM   1261 C  CB   . LYS   A 1 171 ? -17.25815 -10.22466 28.39872  1.000 42.01951  ? 171 LYS   A CB   1 
ATOM   1262 C  CG   . LYS   A 1 171 ? -17.89949 -10.04851 27.05193  1.000 55.96217  ? 171 LYS   A CG   1 
ATOM   1263 C  CD   . LYS   A 1 171 ? -19.38516 -10.56467 26.92488  1.000 53.96821  ? 171 LYS   A CD   1 
ATOM   1264 C  CE   . LYS   A 1 171 ? -19.70918 -10.77935 25.40765  1.000 60.05615  ? 171 LYS   A CE   1 
ATOM   1265 N  NZ   . LYS   A 1 171 ? -21.19296 -10.63418 25.03470  1.000 64.84789  ? 171 LYS   A NZ   1 
ATOM   1266 N  N    . ILE   A 1 172 ? -15.11883 -7.71656  28.59828  1.000 38.20041  ? 172 ILE   A N    1 
ATOM   1267 C  CA   . ILE   A 1 172 ? -14.83444 -6.38729  28.06568  1.000 38.91618  ? 172 ILE   A CA   1 
ATOM   1268 C  C    . ILE   A 1 172 ? -13.50709 -6.36492  27.33200  1.000 42.64328  ? 172 ILE   A C    1 
ATOM   1269 O  O    . ILE   A 1 172 ? -13.25280 -5.43097  26.54481  1.000 37.03899  ? 172 ILE   A O    1 
ATOM   1270 C  CB   . ILE   A 1 172 ? -14.82642 -5.29448  29.14255  1.000 30.58220  ? 172 ILE   A CB   1 
ATOM   1271 C  CG1  . ILE   A 1 172 ? -13.51850 -5.36353  29.98830  1.000 35.26007  ? 172 ILE   A CG1  1 
ATOM   1272 C  CG2  . ILE   A 1 172 ? -16.04255 -5.41589  30.05254  1.000 35.64630  ? 172 ILE   A CG2  1 
ATOM   1273 C  CD1  . ILE   A 1 172 ? -13.41236 -4.31694  31.03097  1.000 34.32935  ? 172 ILE   A CD1  1 
ATOM   1274 N  N    . MET   A 1 173 ? -12.64653 -7.35862  27.58347  1.000 38.70316  ? 173 MET   A N    1 
ATOM   1275 C  CA   . MET   A 1 173 ? -11.37908 -7.49678  26.85787  1.000 36.05995  ? 173 MET   A CA   1 
ATOM   1276 C  C    . MET   A 1 173 ? -11.49074 -8.41831  25.65226  1.000 42.24712  ? 173 MET   A C    1 
ATOM   1277 O  O    . MET   A 1 173 ? -10.48883 -8.68124  24.98846  1.000 39.38136  ? 173 MET   A O    1 
ATOM   1278 C  CB   . MET   A 1 173 ? -10.25838 -8.00738  27.78579  1.000 36.06184  ? 173 MET   A CB   1 
ATOM   1279 C  CG   . MET   A 1 173 ? -10.09041 -7.15373  28.99360  1.000 36.16958  ? 173 MET   A CG   1 
ATOM   1280 S  SD   . MET   A 1 173 ? -8.86991  -7.88617  30.12460  1.000 36.82517  ? 173 MET   A SD   1 
ATOM   1281 C  CE   . MET   A 1 173 ? -7.33572  -7.72310  29.12591  1.000 40.00435  ? 173 MET   A CE   1 
ATOM   1282 N  N    . GLY   A 1 174 ? -12.68892 -8.90073  25.34563  1.000 39.15414  ? 174 GLY   A N    1 
ATOM   1283 C  CA   . GLY   A 1 174 ? -12.88326 -9.78982  24.21572  1.000 44.33910  ? 174 GLY   A CA   1 
ATOM   1284 C  C    . GLY   A 1 174 ? -12.18648 -11.12156 24.37080  1.000 51.76275  ? 174 GLY   A C    1 
ATOM   1285 O  O    . GLY   A 1 174 ? -11.69307 -11.67333 23.38550  1.000 58.20535  ? 174 GLY   A O    1 
ATOM   1286 N  N    . ARG   A 1 175 ? -12.12820 -11.65127 25.58251  1.000 49.99035  ? 175 ARG   A N    1 
ATOM   1287 C  CA   . ARG   A 1 175 ? -11.37572 -12.86026 25.85880  1.000 63.30324  ? 175 ARG   A CA   1 
ATOM   1288 C  C    . ARG   A 1 175 ? -12.27593 -13.87047 26.54354  1.000 66.80859  ? 175 ARG   A C    1 
ATOM   1289 O  O    . ARG   A 1 175 ? -13.20728 -13.49910 27.26460  1.000 56.19925  ? 175 ARG   A O    1 
ATOM   1290 C  CB   . ARG   A 1 175 ? -10.15042 -12.58428 26.73488  1.000 58.98938  ? 175 ARG   A CB   1 
ATOM   1291 C  CG   . ARG   A 1 175 ? -9.11779  -11.73560 26.03543  1.000 53.51623  ? 175 ARG   A CG   1 
ATOM   1292 C  CD   . ARG   A 1 175 ? -7.88141  -11.49176 26.91798  1.000 61.45102  ? 175 ARG   A CD   1 
ATOM   1293 N  NE   . ARG   A 1 175 ? -6.88265  -10.78519 26.12616  1.000 64.07760  ? 175 ARG   A NE   1 
ATOM   1294 C  CZ   . ARG   A 1 175 ? -5.94499  -11.38658 25.40703  1.000 69.79478  ? 175 ARG   A CZ   1 
ATOM   1295 N  NH1  . ARG   A 1 175 ? -5.75949  -12.69832 25.47422  1.000 66.56014  ? 175 ARG   A NH1  1 
ATOM   1296 N  NH2  . ARG   A 1 175 ? -5.18621  -10.65675 24.58628  1.000 67.37936  ? 175 ARG   A NH2  1 
ATOM   1297 N  N    . SER   A 1 176 ? -11.97285 -15.14993 26.30608  1.000 75.37510  ? 176 SER   A N    1 
ATOM   1298 C  CA   . SER   A 1 176 ? -12.68039 -16.28895 26.87341  1.000 85.35357  ? 176 SER   A CA   1 
ATOM   1299 C  C    . SER   A 1 176 ? -11.94463 -16.79634 28.10058  1.000 82.59878  ? 176 SER   A C    1 
ATOM   1300 O  O    . SER   A 1 176 ? -10.73018 -16.62618 28.21956  1.000 87.21632  ? 176 SER   A O    1 
ATOM   1301 C  CB   . SER   A 1 176 ? -12.80227 -17.40147 25.83606  1.000 90.40825  ? 176 SER   A CB   1 
ATOM   1302 O  OG   . SER   A 1 176 ? -13.46037 -16.90599 24.68197  1.000 86.31792  ? 176 SER   A OG   1 
ATOM   1303 N  N    . GLU   A 1 177 ? -12.68272 -17.42754 29.01709  1.000 89.13712  ? 177 GLU   A N    1 
ATOM   1304 C  CA   . GLU   A 1 177 ? -12.07654 -17.74438 30.30914  1.000 110.02222 ? 177 GLU   A CA   1 
ATOM   1305 C  C    . GLU   A 1 177 ? -11.09388 -18.91390 30.25341  1.000 112.36195 ? 177 GLU   A C    1 
ATOM   1306 O  O    . GLU   A 1 177 ? -10.22925 -19.01937 31.13347  1.000 109.13267 ? 177 GLU   A O    1 
ATOM   1307 C  CB   . GLU   A 1 177 ? -13.15510 -18.01761 31.36012  1.000 109.87337 ? 177 GLU   A CB   1 
ATOM   1308 C  CG   . GLU   A 1 177 ? -12.85805 -17.33060 32.69871  1.000 111.44484 ? 177 GLU   A CG   1 
ATOM   1309 C  CD   . GLU   A 1 177 ? -11.66684 -17.95941 33.42468  1.000 113.77763 ? 177 GLU   A CD   1 
ATOM   1310 O  OE1  . GLU   A 1 177 ? -11.43261 -19.16931 33.22115  1.000 122.07031 ? 177 GLU   A OE1  1 
ATOM   1311 O  OE2  . GLU   A 1 177 ? -10.96107 -17.25730 34.19016  1.000 105.50173 ? 177 GLU   A OE2  1 
ATOM   1312 N  N    . GLY   A 1 178 ? -11.15940 -19.75688 29.22424  1.000 99.38474  ? 178 GLY   A N    1 
ATOM   1313 C  CA   . GLY   A 1 178 ? -10.29543 -20.92649 29.18152  1.000 94.06732  ? 178 GLY   A CA   1 
ATOM   1314 C  C    . GLY   A 1 178 ? -8.80914  -20.63564 29.06307  1.000 87.17863  ? 178 GLY   A C    1 
ATOM   1315 O  O    . GLY   A 1 178 ? -8.01232  -21.56816 29.19698  1.000 86.76712  ? 178 GLY   A O    1 
ATOM   1316 N  N    . GLU   A 1 179 ? -8.41768  -19.38869 28.81762  1.000 82.36643  ? 179 GLU   A N    1 
ATOM   1317 C  CA   . GLU   A 1 179 ? -7.01963  -19.05391 28.60309  1.000 76.44790  ? 179 GLU   A CA   1 
ATOM   1318 C  C    . GLU   A 1 179 ? -6.32541  -18.64963 29.90702  1.000 69.72294  ? 179 GLU   A C    1 
ATOM   1319 O  O    . GLU   A 1 179 ? -6.94348  -18.49571 30.96744  1.000 62.31541  ? 179 GLU   A O    1 
ATOM   1320 C  CB   . GLU   A 1 179 ? -6.88514  -17.91496 27.59039  1.000 75.75044  ? 179 GLU   A CB   1 
ATOM   1321 C  CG   . GLU   A 1 179 ? -7.63891  -16.63867 27.99361  1.000 79.73762  ? 179 GLU   A CG   1 
ATOM   1322 C  CD   . GLU   A 1 179 ? -7.62268  -15.56196 26.90721  1.000 79.78726  ? 179 GLU   A CD   1 
ATOM   1323 O  OE1  . GLU   A 1 179 ? -8.15584  -15.80206 25.78610  1.000 78.77893  ? 179 GLU   A OE1  1 
ATOM   1324 O  OE2  . GLU   A 1 179 ? -7.07402  -14.46718 27.19263  1.000 72.27471  ? 179 GLU   A OE2  1 
ATOM   1325 N  N    . GLU   A 1 180 ? -5.01333  -18.46122 29.79704  1.000 63.09721  ? 180 GLU   A N    1 
ATOM   1326 C  CA   . GLU   A 1 180 ? -4.21820  -18.04082 30.93704  1.000 58.44682  ? 180 GLU   A CA   1 
ATOM   1327 C  C    . GLU   A 1 180 ? -4.66209  -16.65305 31.36613  1.000 52.42221  ? 180 GLU   A C    1 
ATOM   1328 O  O    . GLU   A 1 180 ? -4.90231  -15.77736 30.53335  1.000 48.65507  ? 180 GLU   A O    1 
ATOM   1329 C  CB   . GLU   A 1 180 ? -2.73829  -18.01253 30.57512  1.000 59.72499  ? 180 GLU   A CB   1 
ATOM   1330 C  CG   . GLU   A 1 180 ? -1.81840  -18.05509 31.81144  1.000 64.32942  ? 180 GLU   A CG   1 
ATOM   1331 C  CD   . GLU   A 1 180 ? -0.34992  -17.86642 31.46850  1.000 68.92963  ? 180 GLU   A CD   1 
ATOM   1332 O  OE1  . GLU   A 1 180 ? 0.49535   -17.93229 32.38739  1.000 67.88695  ? 180 GLU   A OE1  1 
ATOM   1333 O  OE2  . GLU   A 1 180 ? -0.04037  -17.69877 30.26745  1.000 75.56986  ? 180 GLU   A OE2  1 
ATOM   1334 N  N    . ASN   A 1 181 ? -4.77141  -16.44977 32.66948  1.000 50.92423  ? 181 ASN   A N    1 
ATOM   1335 C  CA   . ASN   A 1 181 ? -5.29925  -15.19890 33.20403  1.000 46.43100  ? 181 ASN   A CA   1 
ATOM   1336 C  C    . ASN   A 1 181 ? -4.13794  -14.31742 33.64349  1.000 44.12515  ? 181 ASN   A C    1 
ATOM   1337 O  O    . ASN   A 1 181 ? -3.67331  -14.41252 34.77222  1.000 42.53178  ? 181 ASN   A O    1 
ATOM   1338 C  CB   . ASN   A 1 181 ? -6.23051  -15.47059 34.36620  1.000 48.54744  ? 181 ASN   A CB   1 
ATOM   1339 C  CG   . ASN   A 1 181 ? -7.39164  -16.37600 33.97149  1.000 60.10928  ? 181 ASN   A CG   1 
ATOM   1340 O  OD1  . ASN   A 1 181 ? -8.19206  -16.02106 33.10433  1.000 63.32088  ? 181 ASN   A OD1  1 
ATOM   1341 N  ND2  . ASN   A 1 181 ? -7.48053  -17.54303 34.61021  1.000 64.71153  ? 181 ASN   A ND2  1 
ATOM   1342 N  N    . TYR   A 1 182 ? -3.65624  -13.46809 32.73940  1.000 41.79350  ? 182 TYR   A N    1 
ATOM   1343 C  CA   . TYR   A 1 182 ? -2.61442  -12.52620 33.11832  1.000 39.79815  ? 182 TYR   A CA   1 
ATOM   1344 C  C    . TYR   A 1 182 ? -3.17791  -11.45364 34.03015  1.000 42.08235  ? 182 TYR   A C    1 
ATOM   1345 O  O    . TYR   A 1 182 ? -4.37643  -11.16913 34.02142  1.000 38.56447  ? 182 TYR   A O    1 
ATOM   1346 C  CB   . TYR   A 1 182 ? -1.99438  -11.89598 31.88509  1.000 39.05837  ? 182 TYR   A CB   1 
ATOM   1347 C  CG   . TYR   A 1 182 ? -1.15685  -12.90285 31.12725  1.000 47.52217  ? 182 TYR   A CG   1 
ATOM   1348 C  CD1  . TYR   A 1 182 ? 0.13735   -13.21203 31.56346  1.000 51.64270  ? 182 TYR   A CD1  1 
ATOM   1349 C  CD2  . TYR   A 1 182 ? -1.65635  -13.55420 29.99315  1.000 57.52554  ? 182 TYR   A CD2  1 
ATOM   1350 C  CE1  . TYR   A 1 182 ? 0.91741   -14.13121 30.88967  1.000 55.50390  ? 182 TYR   A CE1  1 
ATOM   1351 C  CE2  . TYR   A 1 182 ? -0.88152  -14.48131 29.30374  1.000 60.24606  ? 182 TYR   A CE2  1 
ATOM   1352 C  CZ   . TYR   A 1 182 ? 0.40494   -14.76143 29.76087  1.000 55.82039  ? 182 TYR   A CZ   1 
ATOM   1353 O  OH   . TYR   A 1 182 ? 1.19941   -15.66973 29.10409  1.000 65.80660  ? 182 TYR   A OH   1 
ATOM   1354 N  N    . CYS   A 1 183 ? -2.29632  -10.88541 34.86792  1.000 31.53588  ? 183 CYS   A N    1 
ATOM   1355 C  CA   . CYS   A 1 183 ? -2.72476  -9.83355  35.79269  1.000 34.41323  ? 183 CYS   A CA   1 
ATOM   1356 C  C    . CYS   A 1 183 ? -3.24648  -8.61049  35.05328  1.000 32.46779  ? 183 CYS   A C    1 
ATOM   1357 O  O    . CYS   A 1 183 ? -3.97270  -7.80063  35.64584  1.000 33.30012  ? 183 CYS   A O    1 
ATOM   1358 C  CB   . CYS   A 1 183 ? -1.55119  -9.38758  36.67588  1.000 32.38633  ? 183 CYS   A CB   1 
ATOM   1359 S  SG   . CYS   A 1 183 ? -1.08560  -10.70752 37.86232  1.000 36.93325  ? 183 CYS   A SG   1 
ATOM   1360 N  N    . SER   A 1 184 ? -2.83628  -8.43309  33.79526  1.000 35.59105  ? 184 SER   A N    1 
ATOM   1361 C  CA   . SER   A 1 184 ? -3.37542  -7.36882  32.96434  1.000 31.82329  ? 184 SER   A CA   1 
ATOM   1362 C  C    . SER   A 1 184 ? -4.89793  -7.47013  32.88568  1.000 37.33177  ? 184 SER   A C    1 
ATOM   1363 O  O    . SER   A 1 184 ? -5.58360  -6.44207  32.76112  1.000 36.09827  ? 184 SER   A O    1 
ATOM   1364 C  CB   . SER   A 1 184 ? -2.74457  -7.42872  31.56434  1.000 34.16998  ? 184 SER   A CB   1 
ATOM   1365 O  OG   . SER   A 1 184 ? -2.85076  -8.73895  30.98747  1.000 37.32324  ? 184 SER   A OG   1 
ATOM   1366 N  N    . GLN   A 1 185 ? -5.44062  -8.68800  33.03814  1.000 35.73431  ? 185 GLN   A N    1 
ATOM   1367 C  CA   . GLN   A 1 185 ? -6.90911  -8.86387  33.01738  1.000 36.00931  ? 185 GLN   A CA   1 
ATOM   1368 C  C    . GLN   A 1 185 ? -7.59362  -8.36516  34.28557  1.000 37.97345  ? 185 GLN   A C    1 
ATOM   1369 O  O    . GLN   A 1 185 ? -8.84178  -8.33437  34.33078  1.000 38.27382  ? 185 GLN   A O    1 
ATOM   1370 C  CB   . GLN   A 1 185 ? -7.27619  -10.32521 32.79376  1.000 34.76377  ? 185 GLN   A CB   1 
ATOM   1371 C  CG   . GLN   A 1 185 ? -6.71469  -10.80996 31.48991  1.000 39.80261  ? 185 GLN   A CG   1 
ATOM   1372 C  CD   . GLN   A 1 185 ? -6.91022  -12.29569 31.30461  1.000 49.04526  ? 185 GLN   A CD   1 
ATOM   1373 O  OE1  . GLN   A 1 185 ? -7.65450  -12.94995 32.05809  1.000 46.93057  ? 185 GLN   A OE1  1 
ATOM   1374 N  NE2  . GLN   A 1 185 ? -6.25225  -12.84296 30.28883  1.000 55.42261  ? 185 GLN   A NE2  1 
ATOM   1375 N  N    . ILE   A 1 186 ? -6.81079  -7.99928  35.30015  1.000 36.38062  ? 186 ILE   A N    1 
ATOM   1376 C  CA   . ILE   A 1 186 ? -7.28259  -7.28233  36.46802  1.000 33.45313  ? 186 ILE   A CA   1 
ATOM   1377 C  C    . ILE   A 1 186 ? -7.07815  -5.78787  36.30362  1.000 35.36444  ? 186 ILE   A C    1 
ATOM   1378 O  O    . ILE   A 1 186 ? -7.96805  -5.00622  36.63501  1.000 34.05619  ? 186 ILE   A O    1 
ATOM   1379 C  CB   . ILE   A 1 186 ? -6.56962  -7.77856  37.75612  1.000 39.28719  ? 186 ILE   A CB   1 
ATOM   1380 C  CG1  . ILE   A 1 186 ? -6.77228  -9.27714  38.00439  1.000 34.26005  ? 186 ILE   A CG1  1 
ATOM   1381 C  CG2  . ILE   A 1 186 ? -6.90932  -6.85027  38.97700  1.000 37.14285  ? 186 ILE   A CG2  1 
ATOM   1382 C  CD1  . ILE   A 1 186 ? -8.28179  -9.76431  37.95978  1.000 39.01263  ? 186 ILE   A CD1  1 
ATOM   1383 N  N    . LEU   A 1 187 ? -5.90344  -5.35863  35.81377  1.000 31.53577  ? 187 LEU   A N    1 
ATOM   1384 C  CA   . LEU   A 1 187 ? -5.66536  -3.92103  35.69612  1.000 31.39133  ? 187 LEU   A CA   1 
ATOM   1385 C  C    . LEU   A 1 187 ? -6.63144  -3.29104  34.68544  1.000 32.53525  ? 187 LEU   A C    1 
ATOM   1386 O  O    . LEU   A 1 187 ? -7.13561  -2.17774  34.90263  1.000 30.27083  ? 187 LEU   A O    1 
ATOM   1387 C  CB   . LEU   A 1 187 ? -4.24611  -3.66576  35.21769  1.000 31.35027  ? 187 LEU   A CB   1 
ATOM   1388 C  CG   . LEU   A 1 187 ? -3.05779  -3.51802  36.15871  1.000 42.00892  ? 187 LEU   A CG   1 
ATOM   1389 C  CD1  . LEU   A 1 187 ? -3.19774  -2.18921  36.78320  1.000 51.41584  ? 187 LEU   A CD1  1 
ATOM   1390 C  CD2  . LEU   A 1 187 ? -3.05289  -4.65284  37.19164  1.000 39.02589  ? 187 LEU   A CD2  1 
ATOM   1391 N  N    . TYR   A 1 188 ? -6.82304  -3.94083  33.55271  1.000 33.86851  ? 188 TYR   A N    1 
ATOM   1392 C  CA   . TYR   A 1 188 ? -7.68646  -3.40229  32.45977  1.000 31.07917  ? 188 TYR   A CA   1 
ATOM   1393 C  C    . TYR   A 1 188 ? -9.07704  -3.02562  32.95436  1.000 29.46977  ? 188 TYR   A C    1 
ATOM   1394 O  O    . TYR   A 1 188 ? -9.48087  -1.86122  32.77480  1.000 30.01790  ? 188 TYR   A O    1 
ATOM   1395 C  CB   . TYR   A 1 188 ? -7.74583  -4.42490  31.34496  1.000 28.71902  ? 188 TYR   A CB   1 
ATOM   1396 C  CG   . TYR   A 1 188 ? -8.37725  -3.98058  30.03763  1.000 30.94102  ? 188 TYR   A CG   1 
ATOM   1397 C  CD1  . TYR   A 1 188 ? -9.74835  -3.64132  29.97289  1.000 31.33962  ? 188 TYR   A CD1  1 
ATOM   1398 C  CD2  . TYR   A 1 188 ? -7.62577  -3.94751  28.84043  1.000 34.01341  ? 188 TYR   A CD2  1 
ATOM   1399 C  CE1  . TYR   A 1 188 ? -10.34261 -3.27306  28.76550  1.000 33.47363  ? 188 TYR   A CE1  1 
ATOM   1400 C  CE2  . TYR   A 1 188 ? -8.24819  -3.57531  27.59818  1.000 32.68718  ? 188 TYR   A CE2  1 
ATOM   1401 C  CZ   . TYR   A 1 188 ? -9.60902  -3.25164  27.58676  1.000 35.97729  ? 188 TYR   A CZ   1 
ATOM   1402 O  OH   . TYR   A 1 188 ? -10.23180 -2.90750  26.38777  1.000 35.99144  ? 188 TYR   A OH   1 
ATOM   1403 N  N    . PRO   A 1 189 ? -9.86379  -3.94248  33.54582  1.000 32.45367  ? 189 PRO   A N    1 
ATOM   1404 C  CA   . PRO   A 1 189 ? -11.18648 -3.49484  34.03397  1.000 34.04201  ? 189 PRO   A CA   1 
ATOM   1405 C  C    . PRO   A 1 189 ? -11.08656 -2.44147  35.13627  1.000 35.53649  ? 189 PRO   A C    1 
ATOM   1406 O  O    . PRO   A 1 189 ? -11.93555 -1.53155  35.13305  1.000 34.32063  ? 189 PRO   A O    1 
ATOM   1407 C  CB   . PRO   A 1 189 ? -11.89451 -4.79376  34.48590  1.000 34.14320  ? 189 PRO   A CB   1 
ATOM   1408 C  CG   . PRO   A 1 189 ? -10.77548 -5.83026  34.65097  1.000 33.84624  ? 189 PRO   A CG   1 
ATOM   1409 C  CD   . PRO   A 1 189 ? -9.69210  -5.40939  33.66423  1.000 33.28637  ? 189 PRO   A CD   1 
ATOM   1410 N  N    . CYS   A 1 190 ? -10.07145 -2.48331  36.05459  1.000 31.46162  ? 190 CYS   A N    1 
ATOM   1411 C  CA   . CYS   A 1 190 ? -9.99175  -1.39795  37.03169  1.000 32.46984  ? 190 CYS   A CA   1 
ATOM   1412 C  C    . CYS   A 1 190 ? -9.86233  -0.08805  36.29954  1.000 29.41504  ? 190 CYS   A C    1 
ATOM   1413 O  O    . CYS   A 1 190 ? -10.43863 0.93263   36.70661  1.000 32.53974  ? 190 CYS   A O    1 
ATOM   1414 C  CB   . CYS   A 1 190 ? -8.80244  -1.58069  38.02743  1.000 31.15479  ? 190 CYS   A CB   1 
ATOM   1415 S  SG   . CYS   A 1 190 ? -9.03487  -3.02579  39.13520  1.000 36.89993  ? 190 CYS   A SG   1 
ATOM   1416 N  N    . MET   A 1 191 ? -9.05868  -0.09576  35.22202  1.000 28.48991  ? 191 MET   A N    1 
ATOM   1417 C  CA   . MET   A 1 191 ? -8.78346  1.13285   34.48585  1.000 30.33272  ? 191 MET   A CA   1 
ATOM   1418 C  C    . MET   A 1 191 ? -10.01723 1.57373   33.69002  1.000 31.20714  ? 191 MET   A C    1 
ATOM   1419 O  O    . MET   A 1 191 ? -10.33440 2.76978   33.63750  1.000 28.55126  ? 191 MET   A O    1 
ATOM   1420 C  CB   . MET   A 1 191 ? -7.58653  0.97188   33.53093  1.000 27.29453  ? 191 MET   A CB   1 
ATOM   1421 C  CG   . MET   A 1 191 ? -6.27670  0.88885   34.29394  1.000 30.53086  ? 191 MET   A CG   1 
ATOM   1422 S  SD   . MET   A 1 191 ? -4.94162  0.32233   33.20866  1.000 32.62521  ? 191 MET   A SD   1 
ATOM   1423 C  CE   . MET   A 1 191 ? -4.80391  1.72850   32.15868  1.000 29.82437  ? 191 MET   A CE   1 
ATOM   1424 N  N    . GLN   A 1 192 ? -10.70281 0.63665   33.04668  1.000 30.42166  ? 192 GLN   A N    1 
ATOM   1425 C  CA   . GLN   A 1 192 ? -11.88754 1.06499   32.30983  1.000 31.58193  ? 192 GLN   A CA   1 
ATOM   1426 C  C    . GLN   A 1 192 ? -12.91146 1.62128   33.28515  1.000 36.13542  ? 192 GLN   A C    1 
ATOM   1427 O  O    . GLN   A 1 192 ? -13.60412 2.62111   32.98425  1.000 36.21853  ? 192 GLN   A O    1 
ATOM   1428 C  CB   . GLN   A 1 192 ? -12.44699 -0.09645  31.47085  1.000 29.93890  ? 192 GLN   A CB   1 
ATOM   1429 C  CG   . GLN   A 1 192 ? -13.78515 0.28770   30.71613  1.000 33.42600  ? 192 GLN   A CG   1 
ATOM   1430 C  CD   . GLN   A 1 192 ? -14.07425 -0.63365  29.51378  1.000 35.57510  ? 192 GLN   A CD   1 
ATOM   1431 O  OE1  . GLN   A 1 192 ? -13.20030 -1.36780  29.03709  1.000 32.00356  ? 192 GLN   A OE1  1 
ATOM   1432 N  NE2  . GLN   A 1 192 ? -15.28074 -0.57183  29.02054  1.000 33.24528  ? 192 GLN   A NE2  1 
ATOM   1433 N  N    . CYS   A 1 193 ? -12.98535 1.02370   34.48921  1.000 35.00232  ? 193 CYS   A N    1 
ATOM   1434 C  CA   . CYS   A 1 193 ? -13.92819 1.54671   35.47065  1.000 31.42137  ? 193 CYS   A CA   1 
ATOM   1435 C  C    . CYS   A 1 193 ? -13.50787 2.96208   35.85763  1.000 37.93837  ? 193 CYS   A C    1 
ATOM   1436 O  O    . CYS   A 1 193 ? -14.32367 3.90440   35.86630  1.000 34.45574  ? 193 CYS   A O    1 
ATOM   1437 C  CB   . CYS   A 1 193 ? -13.96386 0.59802   36.66397  1.000 31.50168  ? 193 CYS   A CB   1 
ATOM   1438 S  SG   . CYS   A 1 193 ? -15.25212 0.99024   37.90451  1.000 36.94941  ? 193 CYS   A SG   1 
ATOM   1439 N  N    . ALA   A 1 194 ? -12.19463 3.15115   36.05206  1.000 32.81489  ? 194 ALA   A N    1 
ATOM   1440 C  CA   . ALA   A 1 194 ? -11.69743 4.47015   36.42608  1.000 34.86904  ? 194 ALA   A CA   1 
ATOM   1441 C  C    . ALA   A 1 194 ? -12.05114 5.50591   35.36804  1.000 34.89044  ? 194 ALA   A C    1 
ATOM   1442 O  O    . ALA   A 1 194 ? -12.37928 6.65945   35.70829  1.000 32.20624  ? 194 ALA   A O    1 
ATOM   1443 C  CB   . ALA   A 1 194 ? -10.15447 4.43541   36.62407  1.000 32.38546  ? 194 ALA   A CB   1 
ATOM   1444 N  N    . ASP   A 1 195 ? -11.97785 5.11726   34.06919  1.000 33.64670  ? 195 ASP   A N    1 
ATOM   1445 C  CA   . ASP   A 1 195 ? -12.24917 6.07250   32.99039  1.000 35.05209  ? 195 ASP   A CA   1 
ATOM   1446 C  C    . ASP   A 1 195 ? -13.60345 6.74850   33.17734  1.000 34.57288  ? 195 ASP   A C    1 
ATOM   1447 O  O    . ASP   A 1 195 ? -13.73835 7.96532   32.99458  1.000 30.72816  ? 195 ASP   A O    1 
ATOM   1448 C  CB   . ASP   A 1 195 ? -12.24208 5.37071   31.64823  1.000 30.46295  ? 195 ASP   A CB   1 
ATOM   1449 C  CG   . ASP   A 1 195 ? -10.85476 4.84183   31.25538  1.000 33.33091  ? 195 ASP   A CG   1 
ATOM   1450 O  OD1  . ASP   A 1 195 ? -9.82251  5.23926   31.87153  1.000 38.19697  ? 195 ASP   A OD1  1 
ATOM   1451 O  OD2  . ASP   A 1 195 ? -10.80903 4.01754   30.31522  1.000 36.47437  ? 195 ASP   A OD2  1 
ATOM   1452 N  N    . ILE   A 1 196 ? -14.59206 5.96322   33.60469  1.000 37.02156  ? 196 ILE   A N    1 
ATOM   1453 C  CA   . ILE   A 1 196 ? -15.96545 6.45667   33.72545  1.000 32.53533  ? 196 ILE   A CA   1 
ATOM   1454 C  C    . ILE   A 1 196 ? -16.00625 7.65281   34.66072  1.000 38.90920  ? 196 ILE   A C    1 
ATOM   1455 O  O    . ILE   A 1 196 ? -16.72750 8.62539   34.41080  1.000 40.58419  ? 196 ILE   A O    1 
ATOM   1456 C  CB   . ILE   A 1 196 ? -16.86537 5.31243   34.20862  1.000 36.19407  ? 196 ILE   A CB   1 
ATOM   1457 C  CG1  . ILE   A 1 196 ? -16.93049 4.19903   33.14813  1.000 34.46981  ? 196 ILE   A CG1  1 
ATOM   1458 C  CG2  . ILE   A 1 196 ? -18.32097 5.79438   34.51415  1.000 40.99847  ? 196 ILE   A CG2  1 
ATOM   1459 C  CD1  . ILE   A 1 196 ? -17.56761 2.96201   33.65170  1.000 31.36991  ? 196 ILE   A CD1  1 
ATOM   1460 N  N    . PHE   A 1 197 ? -15.23168 7.60382   35.75151  1.000 33.58083  ? 197 PHE   A N    1 
ATOM   1461 C  CA   . PHE   A 1 197 ? -15.19601 8.70029   36.71949  1.000 33.19658  ? 197 PHE   A CA   1 
ATOM   1462 C  C    . PHE   A 1 197 ? -14.22730 9.78339   36.27733  1.000 36.67277  ? 197 PHE   A C    1 
ATOM   1463 O  O    . PHE   A 1 197 ? -14.48907 10.98409  36.44597  1.000 37.67691  ? 197 PHE   A O    1 
ATOM   1464 C  CB   . PHE   A 1 197 ? -14.81666 8.13725   38.10711  1.000 38.00437  ? 197 PHE   A CB   1 
ATOM   1465 C  CG   . PHE   A 1 197 ? -15.80009 7.11741   38.58062  1.000 41.16997  ? 197 PHE   A CG   1 
ATOM   1466 C  CD1  . PHE   A 1 197 ? -17.04537 7.50808   39.01824  1.000 43.18126  ? 197 PHE   A CD1  1 
ATOM   1467 C  CD2  . PHE   A 1 197 ? -15.53851 5.77754   38.45533  1.000 38.87006  ? 197 PHE   A CD2  1 
ATOM   1468 C  CE1  . PHE   A 1 197 ? -17.98731 6.58776   39.38667  1.000 45.50948  ? 197 PHE   A CE1  1 
ATOM   1469 C  CE2  . PHE   A 1 197 ? -16.48321 4.84967   38.83540  1.000 42.96018  ? 197 PHE   A CE2  1 
ATOM   1470 C  CZ   . PHE   A 1 197 ? -17.70488 5.25930   39.29670  1.000 45.53022  ? 197 PHE   A CZ   1 
ATOM   1471 N  N    . PHE   A 1 198 ? -13.10545 9.36442   35.70294  1.000 35.44124  ? 198 PHE   A N    1 
ATOM   1472 C  CA   . PHE   A 1 198 ? -12.07567 10.32232  35.28923  1.000 41.01493  ? 198 PHE   A CA   1 
ATOM   1473 C  C    . PHE   A 1 198 ? -12.62831 11.28661  34.23103  1.000 40.07914  ? 198 PHE   A C    1 
ATOM   1474 O  O    . PHE   A 1 198 ? -12.29428 12.47548  34.19400  1.000 38.43406  ? 198 PHE   A O    1 
ATOM   1475 C  CB   . PHE   A 1 198 ? -10.87938 9.51974   34.74523  1.000 31.08193  ? 198 PHE   A CB   1 
ATOM   1476 C  CG   . PHE   A 1 198 ? -9.69629  10.34195  34.37709  1.000 35.55047  ? 198 PHE   A CG   1 
ATOM   1477 C  CD1  . PHE   A 1 198 ? -8.97508  11.01177  35.38487  1.000 37.36056  ? 198 PHE   A CD1  1 
ATOM   1478 C  CD2  . PHE   A 1 198 ? -9.20433  10.33427  33.06824  1.000 37.66950  ? 198 PHE   A CD2  1 
ATOM   1479 C  CE1  . PHE   A 1 198 ? -7.86177  11.77809  35.07987  1.000 35.19626  ? 198 PHE   A CE1  1 
ATOM   1480 C  CE2  . PHE   A 1 198 ? -8.04321  11.06281  32.73717  1.000 39.27983  ? 198 PHE   A CE2  1 
ATOM   1481 C  CZ   . PHE   A 1 198 ? -7.36644  11.79111  33.75291  1.000 36.75538  ? 198 PHE   A CZ   1 
ATOM   1482 N  N    . LEU   A 1 199 ? -13.43097 10.78182  33.32765  1.000 34.60714  ? 199 LEU   A N    1 
ATOM   1483 C  CA   . LEU   A 1 199 ? -14.04458 11.61456  32.29504  1.000 36.83636  ? 199 LEU   A CA   1 
ATOM   1484 C  C    . LEU   A 1 199 ? -15.35219 12.27124  32.75091  1.000 39.42007  ? 199 LEU   A C    1 
ATOM   1485 O  O    . LEU   A 1 199 ? -15.95738 13.02391  31.98043  1.000 38.99738  ? 199 LEU   A O    1 
ATOM   1486 C  CB   . LEU   A 1 199 ? -14.32415 10.76139  31.06667  1.000 35.61560  ? 199 LEU   A CB   1 
ATOM   1487 C  CG   . LEU   A 1 199 ? -13.04302 10.24280  30.43588  1.000 39.73101  ? 199 LEU   A CG   1 
ATOM   1488 C  CD1  . LEU   A 1 199 ? -13.34684 9.21913   29.34252  1.000 38.07983  ? 199 LEU   A CD1  1 
ATOM   1489 C  CD2  . LEU   A 1 199 ? -12.19306 11.41161  29.87145  1.000 39.12859  ? 199 LEU   A CD2  1 
ATOM   1490 N  N    . ASN   A 1 200 ? -15.77930 12.01897  33.98663  1.000 37.48107  ? 200 ASN   A N    1 
ATOM   1491 C  CA   . ASN   A 1 200 ? -17.01831 12.60124  34.52722  1.000 38.14505  ? 200 ASN   A CA   1 
ATOM   1492 C  C    . ASN   A 1 200 ? -18.20870 12.27417  33.62440  1.000 40.91334  ? 200 ASN   A C    1 
ATOM   1493 O  O    . ASN   A 1 200 ? -19.03731 13.13450  33.34006  1.000 41.49783  ? 200 ASN   A O    1 
ATOM   1494 C  CB   . ASN   A 1 200 ? -16.88703 14.11208  34.70562  1.000 39.96471  ? 200 ASN   A CB   1 
ATOM   1495 C  CG   . ASN   A 1 200 ? -17.96497 14.68306  35.60417  1.000 55.64654  ? 200 ASN   A CG   1 
ATOM   1496 O  OD1  . ASN   A 1 200 ? -18.54458 13.96522  36.44225  1.000 57.75405  ? 200 ASN   A OD1  1 
ATOM   1497 N  ND2  . ASN   A 1 200 ? -18.22746 15.98446  35.46117  1.000 58.89131  ? 200 ASN   A ND2  1 
ATOM   1498 N  N    . VAL   A 1 201 ? -18.30409 11.00443  33.20927  1.000 35.89479  ? 201 VAL   A N    1 
ATOM   1499 C  CA   . VAL   A 1 201 ? -19.34426 10.57231  32.26524  1.000 36.08170  ? 201 VAL   A CA   1 
ATOM   1500 C  C    . VAL   A 1 201 ? -20.69611 10.55173  32.96994  1.000 40.01907  ? 201 VAL   A C    1 
ATOM   1501 O  O    . VAL   A 1 201 ? -20.79450 10.14297  34.13889  1.000 39.34563  ? 201 VAL   A O    1 
ATOM   1502 C  CB   . VAL   A 1 201 ? -18.97103 9.16902   31.75232  1.000 38.33341  ? 201 VAL   A CB   1 
ATOM   1503 C  CG1  . VAL   A 1 201 ? -20.02180 8.57309   30.92746  1.000 45.63090  ? 201 VAL   A CG1  1 
ATOM   1504 C  CG2  . VAL   A 1 201 ? -17.60731 9.22393   31.00817  1.000 38.55375  ? 201 VAL   A CG2  1 
ATOM   1505 N  N    . ASP   A 1 202 ? -21.73418 11.01618  32.27173  1.000 37.64120  ? 202 ASP   A N    1 
ATOM   1506 C  CA   . ASP   A 1 202 ? -23.13582 10.82934  32.66436  1.000 38.68471  ? 202 ASP   A CA   1 
ATOM   1507 C  C    . ASP   A 1 202 ? -23.72085 9.56070   32.08351  1.000 38.03184  ? 202 ASP   A C    1 
ATOM   1508 O  O    . ASP   A 1 202 ? -24.53557 8.89472   32.74648  1.000 39.93477  ? 202 ASP   A O    1 
ATOM   1509 C  CB   . ASP   A 1 202 ? -23.99356 12.03073  32.22785  1.000 34.11511  ? 202 ASP   A CB   1 
ATOM   1510 C  CG   . ASP   A 1 202 ? -23.66740 13.26062  33.03803  1.000 43.98038  ? 202 ASP   A CG   1 
ATOM   1511 O  OD1  . ASP   A 1 202 ? -23.82662 13.19143  34.28487  1.000 43.58098  ? 202 ASP   A OD1  1 
ATOM   1512 O  OD2  . ASP   A 1 202 ? -23.15869 14.24640  32.46594  1.000 41.54453  ? 202 ASP   A OD2  1 
ATOM   1513 N  N    . ILE   A 1 203 ? -23.33464 9.23195   30.85053  1.000 32.30078  ? 203 ILE   A N    1 
ATOM   1514 C  CA   . ILE   A 1 203 ? -23.88391 8.10658   30.11527  1.000 39.04345  ? 203 ILE   A CA   1 
ATOM   1515 C  C    . ILE   A 1 203 ? -22.74099 7.31385   29.51441  1.000 38.86134  ? 203 ILE   A C    1 
ATOM   1516 O  O    . ILE   A 1 203 ? -21.98927 7.83687   28.67376  1.000 39.21785  ? 203 ILE   A O    1 
ATOM   1517 C  CB   . ILE   A 1 203 ? -24.85639 8.56407   29.00895  1.000 37.11522  ? 203 ILE   A CB   1 
ATOM   1518 C  CG1  . ILE   A 1 203 ? -26.06116 9.32778   29.59912  1.000 40.15739  ? 203 ILE   A CG1  1 
ATOM   1519 C  CG2  . ILE   A 1 203 ? -25.30058 7.37315   28.19008  1.000 37.59401  ? 203 ILE   A CG2  1 
ATOM   1520 C  CD1  . ILE   A 1 203 ? -26.92873 10.03077  28.49220  1.000 45.46519  ? 203 ILE   A CD1  1 
ATOM   1521 N  N    . CYS   A 1 204 ? -22.59412 6.06857   29.95631  1.000 40.11235  ? 204 CYS   A N    1 
ATOM   1522 C  CA   . CYS   A 1 204 ? -21.72581 5.10824   29.27490  1.000 41.07929  ? 204 CYS   A CA   1 
ATOM   1523 C  C    . CYS   A 1 204 ? -22.48822 4.54449   28.09086  1.000 38.98433  ? 204 CYS   A C    1 
ATOM   1524 O  O    . CYS   A 1 204 ? -23.49103 3.83915   28.27419  1.000 37.81401  ? 204 CYS   A O    1 
ATOM   1525 C  CB   . CYS   A 1 204 ? -21.33982 3.97358   30.19481  1.000 34.29348  ? 204 CYS   A CB   1 
ATOM   1526 S  SG   . CYS   A 1 204 ? -20.51391 4.60911   31.71411  1.000 38.05070  ? 204 CYS   A SG   1 
ATOM   1527 N  N    . GLN   A 1 205 ? -22.03839 4.85463   26.88351  1.000 37.25342  ? 205 GLN   A N    1 
ATOM   1528 C  CA   . GLN   A 1 205 ? -22.75572 4.43318   25.68246  1.000 35.85914  ? 205 GLN   A CA   1 
ATOM   1529 C  C    . GLN   A 1 205 ? -21.80445 3.51172   24.89166  1.000 40.11033  ? 205 GLN   A C    1 
ATOM   1530 O  O    . GLN   A 1 205 ? -21.12604 3.94592   23.96475  1.000 38.73496  ? 205 GLN   A O    1 
ATOM   1531 C  CB   . GLN   A 1 205 ? -23.18689 5.64209   24.92158  1.000 36.58324  ? 205 GLN   A CB   1 
ATOM   1532 C  CG   . GLN   A 1 205 ? -24.36334 5.39561   23.93454  1.000 37.98087  ? 205 GLN   A CG   1 
ATOM   1533 C  CD   . GLN   A 1 205 ? -23.93505 4.42583   22.85539  1.000 38.82691  ? 205 GLN   A CD   1 
ATOM   1534 O  OE1  . GLN   A 1 205 ? -23.29558 4.83064   21.87466  1.000 35.67608  ? 205 GLN   A OE1  1 
ATOM   1535 N  NE2  . GLN   A 1 205 ? -24.22263 3.14379   23.04302  1.000 34.69948  ? 205 GLN   A NE2  1 
ATOM   1536 N  N    . LEU   A 1 206 ? -21.73164 2.25239   25.31021  1.000 34.06421  ? 206 LEU   A N    1 
ATOM   1537 C  CA   . LEU   A 1 206 ? -20.88992 1.23170   24.71405  1.000 40.20774  ? 206 LEU   A CA   1 
ATOM   1538 C  C    . LEU   A 1 206 ? -21.73135 0.03389   24.33532  1.000 40.14726  ? 206 LEU   A C    1 
ATOM   1539 O  O    . LEU   A 1 206 ? -22.92381 -0.06111  24.65948  1.000 40.83897  ? 206 LEU   A O    1 
ATOM   1540 C  CB   . LEU   A 1 206 ? -19.76707 0.80069   25.70606  1.000 32.34805  ? 206 LEU   A CB   1 
ATOM   1541 C  CG   . LEU   A 1 206 ? -18.89331 1.96590   26.18444  1.000 39.95030  ? 206 LEU   A CG   1 
ATOM   1542 C  CD1  . LEU   A 1 206 ? -19.34313 2.52004   27.56155  1.000 37.65016  ? 206 LEU   A CD1  1 
ATOM   1543 C  CD2  . LEU   A 1 206 ? -17.36804 1.53402   26.28670  1.000 35.87745  ? 206 LEU   A CD2  1 
ATOM   1544 N  N    . GLY   A 1 207 ? -21.10574 -0.91757  23.66092  1.000 37.01991  ? 207 GLY   A N    1 
ATOM   1545 C  CA   . GLY   A 1 207 ? -21.81151 -2.13997  23.34555  1.000 39.11747  ? 207 GLY   A CA   1 
ATOM   1546 C  C    . GLY   A 1 207 ? -22.20070 -2.92251  24.59093  1.000 44.72377  ? 207 GLY   A C    1 
ATOM   1547 O  O    . GLY   A 1 207 ? -21.54317 -2.85101  25.62337  1.000 39.06769  ? 207 GLY   A O    1 
ATOM   1548 N  N    . ILE   A 1 208 ? -23.26038 -3.73994  24.46963  1.000 38.50750  ? 208 ILE   A N    1 
ATOM   1549 C  CA   . ILE   A 1 208 ? -23.69139 -4.54204  25.60394  1.000 40.84541  ? 208 ILE   A CA   1 
ATOM   1550 C  C    . ILE   A 1 208 ? -22.58189 -5.48367  26.07824  1.000 44.74839  ? 208 ILE   A C    1 
ATOM   1551 O  O    . ILE   A 1 208 ? -22.58618 -5.88739  27.24769  1.000 40.03585  ? 208 ILE   A O    1 
ATOM   1552 C  CB   . ILE   A 1 208 ? -24.98851 -5.32179  25.30155  1.000 47.80934  ? 208 ILE   A CB   1 
ATOM   1553 C  CG1  . ILE   A 1 208 ? -25.54049 -5.91243  26.58984  1.000 49.43538  ? 208 ILE   A CG1  1 
ATOM   1554 C  CG2  . ILE   A 1 208 ? -24.75557 -6.45306  24.33676  1.000 50.86427  ? 208 ILE   A CG2  1 
ATOM   1555 C  CD1  . ILE   A 1 208 ? -26.41399 -4.94107  27.34362  1.000 59.72708  ? 208 ILE   A CD1  1 
ATOM   1556 N  N    . ASP   A 1 209 ? -21.58231 -5.79604  25.23382  1.000 47.66743  ? 209 ASP   A N    1 
ATOM   1557 C  CA   . ASP   A 1 209 ? -20.49461 -6.62750  25.76459  1.000 46.33123  ? 209 ASP   A CA   1 
ATOM   1558 C  C    . ASP   A 1 209 ? -19.62447 -5.90773  26.78465  1.000 40.54973  ? 209 ASP   A C    1 
ATOM   1559 O  O    . ASP   A 1 209 ? -18.81471 -6.57892  27.43402  1.000 39.58473  ? 209 ASP   A O    1 
ATOM   1560 C  CB   . ASP   A 1 209 ? -19.60629 -7.20899  24.64136  1.000 45.88434  ? 209 ASP   A CB   1 
ATOM   1561 C  CG   . ASP   A 1 209 ? -18.79539 -6.14424  23.86393  1.000 45.40820  ? 209 ASP   A CG   1 
ATOM   1562 O  OD1  . ASP   A 1 209 ? -19.08717 -4.92601  23.93325  1.000 43.31677  ? 209 ASP   A OD1  1 
ATOM   1563 O  OD2  . ASP   A 1 209 ? -17.85512 -6.56618  23.13962  1.000 42.78893  ? 209 ASP   A OD2  1 
ATOM   1564 N  N    . GLN   A 1 210 ? -19.78504 -4.60200  26.99131  1.000 36.87022  ? 210 GLN   A N    1 
ATOM   1565 C  CA   . GLN   A 1 210 ? -19.03271 -3.90720  28.04921  1.000 37.94015  ? 210 GLN   A CA   1 
ATOM   1566 C  C    . GLN   A 1 210 ? -19.80976 -3.85076  29.37413  1.000 39.52677  ? 210 GLN   A C    1 
ATOM   1567 O  O    . GLN   A 1 210 ? -19.30537 -3.30290  30.36441  1.000 39.79611  ? 210 GLN   A O    1 
ATOM   1568 C  CB   . GLN   A 1 210 ? -18.67001 -2.48276  27.58371  1.000 34.59844  ? 210 GLN   A CB   1 
ATOM   1569 C  CG   . GLN   A 1 210 ? -18.05564 -2.41659  26.17441  1.000 35.98219  ? 210 GLN   A CG   1 
ATOM   1570 C  CD   . GLN   A 1 210 ? -16.67831 -3.05613  26.16056  1.000 37.46286  ? 210 GLN   A CD   1 
ATOM   1571 O  OE1  . GLN   A 1 210 ? -15.78859 -2.63589  26.90234  1.000 38.97090  ? 210 GLN   A OE1  1 
ATOM   1572 N  NE2  . GLN   A 1 210 ? -16.51991 -4.11944  25.37227  1.000 39.87968  ? 210 GLN   A NE2  1 
ATOM   1573 N  N    . ARG   A 1 211 ? -21.01621 -4.44846  29.41898  1.000 39.23051  ? 211 ARG   A N    1 
ATOM   1574 C  CA   . ARG   A 1 211 ? -21.92312 -4.21364  30.53618  1.000 42.10949  ? 211 ARG   A CA   1 
ATOM   1575 C  C    . ARG   A 1 211 ? -21.29058 -4.48807  31.91629  1.000 45.90772  ? 211 ARG   A C    1 
ATOM   1576 O  O    . ARG   A 1 211 ? -21.51014 -3.72487  32.86991  1.000 43.28381  ? 211 ARG   A O    1 
ATOM   1577 C  CB   . ARG   A 1 211 ? -23.17183 -5.07193  30.30195  1.000 38.18985  ? 211 ARG   A CB   1 
ATOM   1578 C  CG   . ARG   A 1 211 ? -24.27897 -4.86879  31.30623  1.000 54.09290  ? 211 ARG   A CG   1 
ATOM   1579 C  CD   . ARG   A 1 211 ? -25.34457 -5.91309  31.05081  1.000 54.47472  ? 211 ARG   A CD   1 
ATOM   1580 N  NE   . ARG   A 1 211 ? -26.60748 -5.55639  31.67501  1.000 58.63501  ? 211 ARG   A NE   1 
ATOM   1581 C  CZ   . ARG   A 1 211 ? -26.95168 -5.83915  32.92692  1.000 57.11643  ? 211 ARG   A CZ   1 
ATOM   1582 N  NH1  . ARG   A 1 211 ? -26.11754 -6.44620  33.76615  1.000 52.43064  ? 211 ARG   A NH1  1 
ATOM   1583 N  NH2  . ARG   A 1 211 ? -28.17962 -5.51841  33.34426  1.000 63.89725  ? 211 ARG   A NH2  1 
ATOM   1584 N  N    . LYS   A 1 212 ? -20.48831 -5.56123  32.04520  1.000 38.44360  ? 212 LYS   A N    1 
ATOM   1585 C  CA   . LYS   A 1 212 ? -19.98568 -5.95081  33.35661  1.000 42.47183  ? 212 LYS   A CA   1 
ATOM   1586 C  C    . LYS   A 1 212 ? -19.19731 -4.80857  33.99892  1.000 44.57914  ? 212 LYS   A C    1 
ATOM   1587 O  O    . LYS   A 1 212 ? -19.41709 -4.45896  35.17350  1.000 40.64289  ? 212 LYS   A O    1 
ATOM   1588 C  CB   . LYS   A 1 212 ? -19.13828 -7.22039  33.21363  1.000 44.44421  ? 212 LYS   A CB   1 
ATOM   1589 C  CG   . LYS   A 1 212 ? -19.99980 -8.50611  33.13590  1.000 45.11516  ? 212 LYS   A CG   1 
ATOM   1590 C  CD   . LYS   A 1 212 ? -20.60743 -8.72187  34.54827  1.000 59.69727  ? 212 LYS   A CD   1 
ATOM   1591 C  CE   . LYS   A 1 212 ? -21.51189 -9.94035  34.65924  1.000 69.85388  ? 212 LYS   A CE   1 
ATOM   1592 N  NZ   . LYS   A 1 212 ? -20.61169 -11.16326 34.67557  1.000 66.72588  ? 212 LYS   A NZ   1 
ATOM   1593 N  N    . VAL   A 1 213 ? -18.31282 -4.16362  33.22852  1.000 36.79018  ? 213 VAL   A N    1 
ATOM   1594 C  CA   . VAL   A 1 213 ? -17.51048 -3.14125  33.89166  1.000 34.73352  ? 213 VAL   A CA   1 
ATOM   1595 C  C    . VAL   A 1 213 ? -18.34746 -1.89176  34.09419  1.000 39.09049  ? 213 VAL   A C    1 
ATOM   1596 O  O    . VAL   A 1 213 ? -18.12895 -1.13336  35.03657  1.000 35.63408  ? 213 VAL   A O    1 
ATOM   1597 C  CB   . VAL   A 1 213 ? -16.23656 -2.83542  33.10220  1.000 33.31372  ? 213 VAL   A CB   1 
ATOM   1598 C  CG1  . VAL   A 1 213 ? -16.57468 -1.98748  31.88549  1.000 36.58666  ? 213 VAL   A CG1  1 
ATOM   1599 C  CG2  . VAL   A 1 213 ? -15.15725 -2.14628  33.98591  1.000 33.43244  ? 213 VAL   A CG2  1 
ATOM   1600 N  N    . ASN   A 1 214 ? -19.33741 -1.65772  33.22765  1.000 38.64745  ? 214 ASN   A N    1 
ATOM   1601 C  CA   . ASN   A 1 214 ? -20.24807 -0.55295  33.49137  1.000 41.24881  ? 214 ASN   A CA   1 
ATOM   1602 C  C    . ASN   A 1 214 ? -21.07250 -0.80862  34.75065  1.000 39.36784  ? 214 ASN   A C    1 
ATOM   1603 O  O    . ASN   A 1 214 ? -21.29160 0.11544   35.55004  1.000 37.77974  ? 214 ASN   A O    1 
ATOM   1604 C  CB   . ASN   A 1 214 ? -21.17285 -0.33296  32.31031  1.000 42.77846  ? 214 ASN   A CB   1 
ATOM   1605 C  CG   . ASN   A 1 214 ? -20.47570 0.30199   31.15648  1.000 38.67312  ? 214 ASN   A CG   1 
ATOM   1606 O  OD1  . ASN   A 1 214 ? -19.64888 1.18676   31.34223  1.000 40.17087  ? 214 ASN   A OD1  1 
ATOM   1607 N  ND2  . ASN   A 1 214 ? -20.87828 -0.08560  29.94071  1.000 41.68557  ? 214 ASN   A ND2  1 
ATOM   1608 N  N    . MET   A 1 215 ? -21.45869 -2.07312  34.98921  1.000 36.62815  ? 215 MET   A N    1 
ATOM   1609 C  CA   . MET   A 1 215 ? -22.16619 -2.35473  36.23764  1.000 43.99580  ? 215 MET   A CA   1 
ATOM   1610 C  C    . MET   A 1 215 ? -21.22752 -2.17775  37.42444  1.000 43.34023  ? 215 MET   A C    1 
ATOM   1611 O  O    . MET   A 1 215 ? -21.64345 -1.70419  38.50184  1.000 40.85488  ? 215 MET   A O    1 
ATOM   1612 C  CB   . MET   A 1 215 ? -22.77719 -3.76224  36.20212  1.000 40.40284  ? 215 MET   A CB   1 
ATOM   1613 C  CG   . MET   A 1 215 ? -23.88278 -4.00492  35.14824  1.000 43.10327  ? 215 MET   A CG   1 
ATOM   1614 S  SD   . MET   A 1 215 ? -25.41363 -3.10565  35.50415  1.000 58.74555  ? 215 MET   A SD   1 
ATOM   1615 C  CE   . MET   A 1 215 ? -25.12695 -1.44222  34.95092  1.000 53.24843  ? 215 MET   A CE   1 
ATOM   1616 N  N    . LEU   A 1 216 ? -19.94047 -2.48345  37.21470  1.000 40.10923  ? 216 LEU   A N    1 
ATOM   1617 C  CA   . LEU   A 1 216 ? -18.96075 -2.35075  38.28343  1.000 40.67578  ? 216 LEU   A CA   1 
ATOM   1618 C  C    . LEU   A 1 216 ? -18.88088 -0.90621  38.75216  1.000 38.81178  ? 216 LEU   A C    1 
ATOM   1619 O  O    . LEU   A 1 216 ? -18.83329 -0.64161  39.96353  1.000 43.08742  ? 216 LEU   A O    1 
ATOM   1620 C  CB   . LEU   A 1 216 ? -17.59784 -2.82559  37.77776  1.000 36.14639  ? 216 LEU   A CB   1 
ATOM   1621 C  CG   . LEU   A 1 216 ? -16.49327 -2.95259  38.85503  1.000 37.86307  ? 216 LEU   A CG   1 
ATOM   1622 C  CD1  . LEU   A 1 216 ? -16.68582 -4.25947  39.57294  1.000 47.45154  ? 216 LEU   A CD1  1 
ATOM   1623 C  CD2  . LEU   A 1 216 ? -15.06871 -2.90793  38.25458  1.000 43.26223  ? 216 LEU   A CD2  1 
ATOM   1624 N  N    . ALA   A 1 217 ? -18.92247 0.04357   37.80179  1.000 38.37618  ? 217 ALA   A N    1 
ATOM   1625 C  CA   . ALA   A 1 217 ? -18.82329 1.45224   38.16866  1.000 34.97878  ? 217 ALA   A CA   1 
ATOM   1626 C  C    . ALA   A 1 217 ? -20.02550 1.83748   39.01653  1.000 37.47411  ? 217 ALA   A C    1 
ATOM   1627 O  O    . ALA   A 1 217 ? -19.90770 2.58439   39.99730  1.000 38.52898  ? 217 ALA   A O    1 
ATOM   1628 C  CB   . ALA   A 1 217 ? -18.77795 2.32798   36.89757  1.000 41.53688  ? 217 ALA   A CB   1 
ATOM   1629 N  N    . ARG   A 1 218 ? -21.19061 1.34247   38.63557  1.000 37.89722  ? 218 ARG   A N    1 
ATOM   1630 C  CA   . ARG   A 1 218 ? -22.37474 1.67275   39.42541  1.000 41.74391  ? 218 ARG   A CA   1 
ATOM   1631 C  C    . ARG   A 1 218 ? -22.24258 1.12525   40.83575  1.000 45.68079  ? 218 ARG   A C    1 
ATOM   1632 O  O    . ARG   A 1 218 ? -22.50563 1.83627   41.81341  1.000 43.75269  ? 218 ARG   A O    1 
ATOM   1633 C  CB   . ARG   A 1 218 ? -23.62597 1.13463   38.75390  1.000 37.35363  ? 218 ARG   A CB   1 
ATOM   1634 C  CG   . ARG   A 1 218 ? -23.96181 1.94811   37.50690  1.000 38.44092  ? 218 ARG   A CG   1 
ATOM   1635 C  CD   . ARG   A 1 218 ? -25.21423 1.48580   36.74450  1.000 39.77836  ? 218 ARG   A CD   1 
ATOM   1636 N  NE   . ARG   A 1 218 ? -26.43048 1.48701   37.55027  1.000 43.43465  ? 218 ARG   A NE   1 
ATOM   1637 C  CZ   . ARG   A 1 218 ? -27.23158 2.52902   37.72104  1.000 46.66896  ? 218 ARG   A CZ   1 
ATOM   1638 N  NH1  . ARG   A 1 218 ? -26.97447 3.70252   37.17501  1.000 41.58411  ? 218 ARG   A NH1  1 
ATOM   1639 N  NH2  . ARG   A 1 218 ? -28.33672 2.38545   38.45462  1.000 44.56622  ? 218 ARG   A NH2  1 
ATOM   1640 N  N    . GLU   A 1 219 ? -21.79140 -0.12481  40.95221  1.000 42.30221  ? 219 GLU   A N    1 
ATOM   1641 C  CA   . GLU   A 1 219 ? -21.62530 -0.69020  42.26728  1.000 40.73344  ? 219 GLU   A CA   1 
ATOM   1642 C  C    . GLU   A 1 219 ? -20.58957 0.10767   43.04860  1.000 45.34300  ? 219 GLU   A C    1 
ATOM   1643 O  O    . GLU   A 1 219 ? -20.73287 0.32725   44.25933  1.000 45.86060  ? 219 GLU   A O    1 
ATOM   1644 C  CB   . GLU   A 1 219 ? -21.24153 -2.15658  42.14507  1.000 48.41597  ? 219 GLU   A CB   1 
ATOM   1645 C  CG   . GLU   A 1 219 ? -20.93727 -2.74784  43.51746  1.000 60.39042  ? 219 GLU   A CG   1 
ATOM   1646 C  CD   . GLU   A 1 219 ? -21.04565 -4.24816  43.52992  1.000 65.17414  ? 219 GLU   A CD   1 
ATOM   1647 O  OE1  . GLU   A 1 219 ? -21.68656 -4.79069  42.59987  1.000 79.32036  ? 219 GLU   A OE1  1 
ATOM   1648 O  OE2  . GLU   A 1 219 ? -20.48588 -4.87497  44.45841  1.000 76.27463  ? 219 GLU   A OE2  1 
ATOM   1649 N  N    . TYR   A 1 220 ? -19.55412 0.58996   42.36352  1.000 40.94960  ? 220 TYR   A N    1 
ATOM   1650 C  CA   . TYR   A 1 220 ? -18.52844 1.32878   43.08358  1.000 40.58141  ? 220 TYR   A CA   1 
ATOM   1651 C  C    . TYR   A 1 220 ? -19.09402 2.60368   43.69147  1.000 44.37187  ? 220 TYR   A C    1 
ATOM   1652 O  O    . TYR   A 1 220 ? -18.76066 2.94924   44.83372  1.000 43.28278  ? 220 TYR   A O    1 
ATOM   1653 C  CB   . TYR   A 1 220 ? -17.37312 1.63544   42.14560  1.000 37.47322  ? 220 TYR   A CB   1 
ATOM   1654 C  CG   . TYR   A 1 220 ? -16.26685 2.45025   42.75790  1.000 39.58537  ? 220 TYR   A CG   1 
ATOM   1655 C  CD1  . TYR   A 1 220 ? -15.35100 1.87842   43.66248  1.000 44.67794  ? 220 TYR   A CD1  1 
ATOM   1656 C  CD2  . TYR   A 1 220 ? -16.07325 3.78236   42.38546  1.000 43.34985  ? 220 TYR   A CD2  1 
ATOM   1657 C  CE1  . TYR   A 1 220 ? -14.32686 2.62051   44.19065  1.000 42.67205  ? 220 TYR   A CE1  1 
ATOM   1658 C  CE2  . TYR   A 1 220 ? -15.02032 4.53972   42.93374  1.000 44.89134  ? 220 TYR   A CE2  1 
ATOM   1659 C  CZ   . TYR   A 1 220 ? -14.15527 3.93947   43.82665  1.000 44.65028  ? 220 TYR   A CZ   1 
ATOM   1660 O  OH   . TYR   A 1 220 ? -13.12235 4.66609   44.38042  1.000 41.46350  ? 220 TYR   A OH   1 
ATOM   1661 N  N    . CYS   A 1 221 ? -20.01707 3.27632   42.97213  1.000 37.75228  ? 221 CYS   A N    1 
ATOM   1662 C  CA   . CYS   A 1 221 ? -20.66967 4.44977   43.53754  1.000 43.69338  ? 221 CYS   A CA   1 
ATOM   1663 C  C    . CYS   A 1 221 ? -21.41265 4.07642   44.81064  1.000 45.35722  ? 221 CYS   A C    1 
ATOM   1664 O  O    . CYS   A 1 221 ? -21.36043 4.80233   45.81435  1.000 46.68245  ? 221 CYS   A O    1 
ATOM   1665 C  CB   . CYS   A 1 221 ? -21.69151 5.04416   42.54072  1.000 41.68534  ? 221 CYS   A CB   1 
ATOM   1666 S  SG   . CYS   A 1 221 ? -20.97887 5.75576   41.00863  1.000 44.15637  ? 221 CYS   A SG   1 
ATOM   1667 N  N    . ASP   A 1 222 ? -22.12700 2.94491   44.78166  1.000 43.23309  ? 222 ASP   A N    1 
ATOM   1668 C  CA   . ASP   A 1 222 ? -22.89799 2.55816   45.94612  1.000 46.09825  ? 222 ASP   A CA   1 
ATOM   1669 C  C    . ASP   A 1 222 ? -21.95986 2.29701   47.11715  1.000 48.12092  ? 222 ASP   A C    1 
ATOM   1670 O  O    . ASP   A 1 222 ? -22.24278 2.66851   48.26193  1.000 47.49084  ? 222 ASP   A O    1 
ATOM   1671 C  CB   . ASP   A 1 222 ? -23.71801 1.31677   45.62700  1.000 46.40417  ? 222 ASP   A CB   1 
ATOM   1672 C  CG   . ASP   A 1 222 ? -24.90522 1.61245   44.72767  1.000 55.22489  ? 222 ASP   A CG   1 
ATOM   1673 O  OD1  . ASP   A 1 222 ? -25.18054 2.81196   44.43210  1.000 51.80152  ? 222 ASP   A OD1  1 
ATOM   1674 O  OD2  . ASP   A 1 222 ? -25.54885 0.62502   44.30771  1.000 56.09413  ? 222 ASP   A OD2  1 
ATOM   1675 N  N    . ILE   A 1 223 ? -20.81778 1.69789   46.82596  1.000 43.56143  ? 223 ILE   A N    1 
ATOM   1676 C  CA   . ILE   A 1 223 ? -19.85317 1.36834   47.86627  1.000 46.84665  ? 223 ILE   A CA   1 
ATOM   1677 C  C    . ILE   A 1 223 ? -19.31964 2.64469   48.50662  1.000 54.01892  ? 223 ILE   A C    1 
ATOM   1678 O  O    . ILE   A 1 223 ? -19.14788 2.71946   49.72866  1.000 51.24216  ? 223 ILE   A O    1 
ATOM   1679 C  CB   . ILE   A 1 223 ? -18.71567 0.51414   47.26536  1.000 42.70505  ? 223 ILE   A CB   1 
ATOM   1680 C  CG1  . ILE   A 1 223 ? -19.16912 -0.93287  46.97954  1.000 44.97274  ? 223 ILE   A CG1  1 
ATOM   1681 C  CG2  . ILE   A 1 223 ? -17.44132 0.56656   48.09595  1.000 45.13842  ? 223 ILE   A CG2  1 
ATOM   1682 C  CD1  . ILE   A 1 223 ? -18.08330 -1.65140  46.11866  1.000 48.10040  ? 223 ILE   A CD1  1 
ATOM   1683 N  N    . LYS   A 1 224 ? -19.06203 3.66703   47.69243  1.000 49.03364  ? 224 LYS   A N    1 
ATOM   1684 C  CA   . LYS   A 1 224 ? -18.44510 4.90440   48.13149  1.000 42.75805  ? 224 LYS   A CA   1 
ATOM   1685 C  C    . LYS   A 1 224 ? -19.44987 5.97082   48.53222  1.000 46.84432  ? 224 LYS   A C    1 
ATOM   1686 O  O    . LYS   A 1 224 ? -19.03644 7.09880   48.82513  1.000 48.94196  ? 224 LYS   A O    1 
ATOM   1687 C  CB   . LYS   A 1 224 ? -17.54561 5.42455   47.01831  1.000 41.67120  ? 224 LYS   A CB   1 
ATOM   1688 C  CG   . LYS   A 1 224 ? -16.33127 4.53616   46.74937  1.000 51.30713  ? 224 LYS   A CG   1 
ATOM   1689 C  CD   . LYS   A 1 224 ? -15.28964 4.71885   47.88313  1.000 53.90045  ? 224 LYS   A CD   1 
ATOM   1690 C  CE   . LYS   A 1 224 ? -14.11833 3.79335   47.75457  1.000 55.58271  ? 224 LYS   A CE   1 
ATOM   1691 N  NZ   . LYS   A 1 224 ? -12.88405 4.36743   48.35019  1.000 56.32457  ? 224 LYS   A NZ   1 
ATOM   1692 N  N    . LYS   A 1 225 ? -20.75496 5.67606   48.47329  1.000 45.54937  ? 225 LYS   A N    1 
ATOM   1693 C  CA   . LYS   A 1 225 ? -21.79598 6.66341   48.78493  1.000 52.56645  ? 225 LYS   A CA   1 
ATOM   1694 C  C    . LYS   A 1 225 ? -21.76577 7.83559   47.80927  1.000 54.91787  ? 225 LYS   A C    1 
ATOM   1695 O  O    . LYS   A 1 225 ? -22.10543 8.96528   48.16270  1.000 55.78069  ? 225 LYS   A O    1 
ATOM   1696 C  CB   . LYS   A 1 225 ? -21.63140 7.15529   50.22707  1.000 60.36597  ? 225 LYS   A CB   1 
ATOM   1697 C  CG   . LYS   A 1 225 ? -21.82973 6.06184   51.25242  1.000 60.85025  ? 225 LYS   A CG   1 
ATOM   1698 C  CD   . LYS   A 1 225 ? -22.95322 5.10409   50.83686  1.000 66.56695  ? 225 LYS   A CD   1 
ATOM   1699 C  CE   . LYS   A 1 225 ? -22.80777 3.73100   51.51291  1.000 75.70503  ? 225 LYS   A CE   1 
ATOM   1700 N  NZ   . LYS   A 1 225 ? -23.73578 2.73622   50.86122  1.000 72.77547  ? 225 LYS   A NZ   1 
ATOM   1701 N  N    . ILE   A 1 226 ? -21.35839 7.57646   46.56528  1.000 51.61700  ? 226 ILE   A N    1 
ATOM   1702 C  CA   . ILE   A 1 226 ? -21.37329 8.58708   45.52097  1.000 47.68619  ? 226 ILE   A CA   1 
ATOM   1703 C  C    . ILE   A 1 226 ? -22.74250 8.52788   44.88955  1.000 51.23911  ? 226 ILE   A C    1 
ATOM   1704 O  O    . ILE   A 1 226 ? -23.12160 7.49338   44.32784  1.000 48.76229  ? 226 ILE   A O    1 
ATOM   1705 C  CB   . ILE   A 1 226 ? -20.28986 8.33243   44.46066  1.000 48.36349  ? 226 ILE   A CB   1 
ATOM   1706 C  CG1  . ILE   A 1 226 ? -18.89508 8.37408   45.08921  1.000 48.35994  ? 226 ILE   A CG1  1 
ATOM   1707 C  CG2  . ILE   A 1 226 ? -20.42399 9.35585   43.31066  1.000 47.50018  ? 226 ILE   A CG2  1 
ATOM   1708 C  CD1  . ILE   A 1 226 ? -17.83987 7.79914   44.13312  1.000 45.01032  ? 226 ILE   A CD1  1 
ATOM   1709 N  N    . LYS   A 1 227 ? -23.47157 9.63441   44.98206  1.000 52.47029  ? 227 LYS   A N    1 
ATOM   1710 C  CA   . LYS   A 1 227 ? -24.83430 9.70120   44.49274  1.000 50.61995  ? 227 LYS   A CA   1 
ATOM   1711 C  C    . LYS   A 1 227 ? -24.88345 9.98846   42.99898  1.000 50.51063  ? 227 LYS   A C    1 
ATOM   1712 O  O    . LYS   A 1 227 ? -25.88546 9.68041   42.35293  1.000 51.12492  ? 227 LYS   A O    1 
ATOM   1713 C  CB   . LYS   A 1 227 ? -25.60274 10.78275  45.26499  1.000 54.09311  ? 227 LYS   A CB   1 
ATOM   1714 C  CG   . LYS   A 1 227 ? -25.77206 10.46339  46.74610  1.000 60.95370  ? 227 LYS   A CG   1 
ATOM   1715 C  CD   . LYS   A 1 227 ? -26.51740 9.13920   46.94486  1.000 66.07684  ? 227 LYS   A CD   1 
ATOM   1716 C  CE   . LYS   A 1 227 ? -26.64984 8.74491   48.44210  1.000 62.03431  ? 227 LYS   A CE   1 
ATOM   1717 N  NZ   . LYS   A 1 227 ? -25.35606 8.25841   49.00335  1.000 70.91636  ? 227 LYS   A NZ   1 
ATOM   1718 N  N    . LYS   A 1 228 ? -23.85024 10.62152  42.44745  1.000 47.67110  ? 228 LYS   A N    1 
ATOM   1719 C  CA   . LYS   A 1 228 ? -23.76910 10.85119  41.00817  1.000 54.25922  ? 228 LYS   A CA   1 
ATOM   1720 C  C    . LYS   A 1 228 ? -23.37441 9.54095   40.33320  1.000 52.06901  ? 228 LYS   A C    1 
ATOM   1721 O  O    . LYS   A 1 228 ? -22.21298 9.13944   40.36788  1.000 53.01831  ? 228 LYS   A O    1 
ATOM   1722 C  CB   . LYS   A 1 228 ? -22.77388 11.96118  40.69881  1.000 48.76921  ? 228 LYS   A CB   1 
ATOM   1723 C  CG   . LYS   A 1 228 ? -22.83314 12.31817  39.19971  1.000 50.03665  ? 228 LYS   A CG   1 
ATOM   1724 C  CD   . LYS   A 1 228 ? -21.91403 13.41609  38.78413  1.000 48.77413  ? 228 LYS   A CD   1 
ATOM   1725 C  CE   . LYS   A 1 228 ? -21.96574 13.56569  37.24160  1.000 52.60514  ? 228 LYS   A CE   1 
ATOM   1726 N  NZ   . LYS   A 1 228 ? -20.94778 14.55278  36.81482  1.000 60.87042  ? 228 LYS   A NZ   1 
ATOM   1727 N  N    . LYS   A 1 229 ? -24.34044 8.84659   39.74472  1.000 45.45414  ? 229 LYS   A N    1 
ATOM   1728 C  CA   . LYS   A 1 229 ? -24.09875 7.52527   39.15619  1.000 46.90542  ? 229 LYS   A CA   1 
ATOM   1729 C  C    . LYS   A 1 229 ? -24.31591 7.57882   37.64823  1.000 41.54285  ? 229 LYS   A C    1 
ATOM   1730 O  O    . LYS   A 1 229 ? -25.23262 8.25973   37.18634  1.000 41.74765  ? 229 LYS   A O    1 
ATOM   1731 C  CB   . LYS   A 1 229 ? -25.02766 6.43265   39.73803  1.000 42.80361  ? 229 LYS   A CB   1 
ATOM   1732 C  CG   . LYS   A 1 229 ? -24.74811 6.03684   41.16275  1.000 51.70791  ? 229 LYS   A CG   1 
ATOM   1733 C  CD   . LYS   A 1 229 ? -25.86131 5.19554   41.74810  1.000 53.58822  ? 229 LYS   A CD   1 
ATOM   1734 C  CE   . LYS   A 1 229 ? -25.90119 3.81652   41.13599  1.000 56.85226  ? 229 LYS   A CE   1 
ATOM   1735 N  NZ   . LYS   A 1 229 ? -26.73347 2.92381   42.00580  1.000 60.32890  ? 229 LYS   A NZ   1 
ATOM   1736 N  N    . PRO   A 1 230 ? -23.50058 6.85998   36.88211  1.000 42.43196  ? 230 PRO   A N    1 
ATOM   1737 C  CA   . PRO   A 1 230 ? -23.61993 6.86443   35.41959  1.000 39.75712  ? 230 PRO   A CA   1 
ATOM   1738 C  C    . PRO   A 1 230 ? -24.78131 6.01034   34.94264  1.000 39.39632  ? 230 PRO   A C    1 
ATOM   1739 O  O    . PRO   A 1 230 ? -25.04918 4.93384   35.48469  1.000 41.42219  ? 230 PRO   A O    1 
ATOM   1740 C  CB   . PRO   A 1 230 ? -22.27113 6.26191   34.96899  1.000 39.42967  ? 230 PRO   A CB   1 
ATOM   1741 C  CG   . PRO   A 1 230 ? -21.91003 5.34989   36.05051  1.000 42.77124  ? 230 PRO   A CG   1 
ATOM   1742 C  CD   . PRO   A 1 230 ? -22.34024 6.06808   37.34160  1.000 41.01626  ? 230 PRO   A CD   1 
ATOM   1743 N  N    . VAL   A 1 231 ? -25.46954 6.50436   33.91482  1.000 36.56761  ? 231 VAL   A N    1 
ATOM   1744 C  CA   . VAL   A 1 231 ? -26.47782 5.71259   33.22826  1.000 42.36425  ? 231 VAL   A CA   1 
ATOM   1745 C  C    . VAL   A 1 231 ? -25.77959 4.84182   32.20462  1.000 41.20603  ? 231 VAL   A C    1 
ATOM   1746 O  O    . VAL   A 1 231 ? -24.90317 5.32398   31.48062  1.000 39.67875  ? 231 VAL   A O    1 
ATOM   1747 C  CB   . VAL   A 1 231 ? -27.50754 6.64430   32.57430  1.000 41.03132  ? 231 VAL   A CB   1 
ATOM   1748 C  CG1  . VAL   A 1 231 ? -28.47056 5.87248   31.65305  1.000 45.58152  ? 231 VAL   A CG1  1 
ATOM   1749 C  CG2  . VAL   A 1 231 ? -28.22463 7.35709   33.68690  1.000 51.04962  ? 231 VAL   A CG2  1 
ATOM   1750 N  N    . ILE   A 1 232 ? -26.12405 3.55544   32.15916  1.000 41.10173  ? 232 ILE   A N    1 
ATOM   1751 C  CA   . ILE   A 1 232 ? -25.56854 2.63987   31.15599  1.000 45.58901  ? 232 ILE   A CA   1 
ATOM   1752 C  C    . ILE   A 1 232 ? -26.57001 2.55155   30.01734  1.000 48.19428  ? 232 ILE   A C    1 
ATOM   1753 O  O    . ILE   A 1 232 ? -27.61818 1.92008   30.16915  1.000 46.52355  ? 232 ILE   A O    1 
ATOM   1754 C  CB   . ILE   A 1 232 ? -25.29870 1.23672   31.71404  1.000 43.57201  ? 232 ILE   A CB   1 
ATOM   1755 C  CG1  . ILE   A 1 232 ? -24.61944 1.23763   33.11758  1.000 39.51553  ? 232 ILE   A CG1  1 
ATOM   1756 C  CG2  . ILE   A 1 232 ? -24.55615 0.44559   30.69467  1.000 41.63540  ? 232 ILE   A CG2  1 
ATOM   1757 C  CD1  . ILE   A 1 232 ? -23.48054 2.25292   33.35254  1.000 46.94058  ? 232 ILE   A CD1  1 
ATOM   1758 N  N    . LEU   A 1 233 ? -26.23601 3.13396   28.86015  1.000 37.40529  ? 233 LEU   A N    1 
ATOM   1759 C  CA   . LEU   A 1 233 ? -27.12473 3.13724   27.67803  1.000 39.17993  ? 233 LEU   A CA   1 
ATOM   1760 C  C    . LEU   A 1 233 ? -26.44240 2.26333   26.64194  1.000 40.75581  ? 233 LEU   A C    1 
ATOM   1761 O  O    . LEU   A 1 233 ? -25.62669 2.75468   25.86292  1.000 37.97232  ? 233 LEU   A O    1 
ATOM   1762 C  CB   . LEU   A 1 233 ? -27.28317 4.53408   27.19717  1.000 39.71946  ? 233 LEU   A CB   1 
ATOM   1763 C  CG   . LEU   A 1 233 ? -28.28545 4.78245   26.06501  1.000 39.94661  ? 233 LEU   A CG   1 
ATOM   1764 C  CD1  . LEU   A 1 233 ? -29.71449 4.50305   26.55590  1.000 48.21050  ? 233 LEU   A CD1  1 
ATOM   1765 C  CD2  . LEU   A 1 233 ? -28.06574 6.20556   25.58474  1.000 41.77881  ? 233 LEU   A CD2  1 
ATOM   1766 N  N    . SER   A 1 234 ? -26.66846 0.95007   26.71427  1.000 42.14922  ? 234 SER   A N    1 
ATOM   1767 C  CA   . SER   A 1 234 ? -25.89776 0.02949   25.87685  1.000 43.73663  ? 234 SER   A CA   1 
ATOM   1768 C  C    . SER   A 1 234 ? -26.58800 -0.16279  24.52530  1.000 49.94372  ? 234 SER   A C    1 
ATOM   1769 O  O    . SER   A 1 234 ? -27.83786 -0.26815  24.43072  1.000 46.26800  ? 234 SER   A O    1 
ATOM   1770 C  CB   . SER   A 1 234 ? -25.71877 -1.33251  26.55976  1.000 43.57273  ? 234 SER   A CB   1 
ATOM   1771 O  OG   . SER   A 1 234 ? -25.10340 -1.21346  27.83492  1.000 43.12487  ? 234 SER   A OG   1 
ATOM   1772 N  N    . HIS   A 1 235 ? -25.76861 -0.18482  23.46894  1.000 41.52163  ? 235 HIS   A N    1 
ATOM   1773 C  CA   . HIS   A 1 235 ? -26.32757 -0.52149  22.16154  1.000 45.89905  ? 235 HIS   A CA   1 
ATOM   1774 C  C    . HIS   A 1 235 ? -26.13473 -2.01212  21.92209  1.000 44.46428  ? 235 HIS   A C    1 
ATOM   1775 O  O    . HIS   A 1 235 ? -25.29700 -2.66323  22.56929  1.000 46.06226  ? 235 HIS   A O    1 
ATOM   1776 C  CB   . HIS   A 1 235 ? -25.69930 0.32832   21.03760  1.000 43.49246  ? 235 HIS   A CB   1 
ATOM   1777 C  CG   . HIS   A 1 235 ? -24.23243 0.07338   20.81576  1.000 42.60563  ? 235 HIS   A CG   1 
ATOM   1778 N  ND1  . HIS   A 1 235 ? -23.24810 0.90355   21.31522  1.000 40.45519  ? 235 HIS   A ND1  1 
ATOM   1779 C  CD2  . HIS   A 1 235 ? -23.58645 -0.89683  20.12725  1.000 40.35542  ? 235 HIS   A CD2  1 
ATOM   1780 C  CE1  . HIS   A 1 235 ? -22.05592 0.43090   20.98671  1.000 42.99433  ? 235 HIS   A CE1  1 
ATOM   1781 N  NE2  . HIS   A 1 235 ? -22.23131 -0.66140  20.26293  1.000 40.49071  ? 235 HIS   A NE2  1 
ATOM   1782 N  N    . GLY   A 1 236 ? -26.97590 -2.56707  21.03939  1.000 43.12616  ? 236 GLY   A N    1 
ATOM   1783 C  CA   . GLY   A 1 236 ? -26.89380 -3.98911  20.76442  1.000 48.00650  ? 236 GLY   A CA   1 
ATOM   1784 C  C    . GLY   A 1 236 ? -25.67626 -4.34761  19.92732  1.000 47.09204  ? 236 GLY   A C    1 
ATOM   1785 O  O    . GLY   A 1 236 ? -25.18622 -3.55831  19.10991  1.000 43.61845  ? 236 GLY   A O    1 
ATOM   1786 N  N    . MET   A 1 237 ? -25.20288 -5.58146  20.09452  1.000 49.68727  ? 237 MET   A N    1 
ATOM   1787 C  CA   . MET   A 1 237 ? -24.08665 -6.04297  19.28003  1.000 49.20536  ? 237 MET   A CA   1 
ATOM   1788 C  C    . MET   A 1 237 ? -24.58890 -6.36206  17.88035  1.000 49.13690  ? 237 MET   A C    1 
ATOM   1789 O  O    . MET   A 1 237 ? -25.59049 -7.07210  17.70849  1.000 52.43561  ? 237 MET   A O    1 
ATOM   1790 C  CB   . MET   A 1 237 ? -23.41632 -7.26675  19.89428  1.000 47.37728  ? 237 MET   A CB   1 
ATOM   1791 C  CG   . MET   A 1 237 ? -22.91182 -7.06403  21.31878  1.000 49.71029  ? 237 MET   A CG   1 
ATOM   1792 S  SD   . MET   A 1 237 ? -21.76811 -5.68106  21.50697  1.000 47.71755  ? 237 MET   A SD   1 
ATOM   1793 C  CE   . MET   A 1 237 ? -20.27381 -6.41459  20.83919  1.000 44.63816  ? 237 MET   A CE   1 
ATOM   1794 N  N    . LEU   A 1 238 ? -23.90869 -5.83657  16.88284  1.000 47.50682  ? 238 LEU   A N    1 
ATOM   1795 C  CA   . LEU   A 1 238 ? -24.29513 -6.13780  15.51371  1.000 50.74529  ? 238 LEU   A CA   1 
ATOM   1796 C  C    . LEU   A 1 238 ? -23.89260 -7.58020  15.21501  1.000 53.57761  ? 238 LEU   A C    1 
ATOM   1797 O  O    . LEU   A 1 238 ? -22.74275 -7.95918  15.46752  1.000 53.13796  ? 238 LEU   A O    1 
ATOM   1798 C  CB   . LEU   A 1 238 ? -23.61870 -5.13791  14.57295  1.000 47.26931  ? 238 LEU   A CB   1 
ATOM   1799 C  CG   . LEU   A 1 238 ? -24.17680 -5.05255  13.15253  1.000 53.54110  ? 238 LEU   A CG   1 
ATOM   1800 C  CD1  . LEU   A 1 238 ? -25.55428 -4.37792  13.13695  1.000 53.66506  ? 238 LEU   A CD1  1 
ATOM   1801 C  CD2  . LEU   A 1 238 ? -23.18025 -4.29213  12.25922  1.000 57.63892  ? 238 LEU   A CD2  1 
ATOM   1802 N  N    . PRO   A 1 239 ? -24.80626 -8.42721  14.74893  1.000 59.16624  ? 239 PRO   A N    1 
ATOM   1803 C  CA   . PRO   A 1 239 ? -24.46277 -9.84023  14.54880  1.000 61.17374  ? 239 PRO   A CA   1 
ATOM   1804 C  C    . PRO   A 1 239 ? -23.48322 -10.04997 13.39983  1.000 60.88633  ? 239 PRO   A C    1 
ATOM   1805 O  O    . PRO   A 1 239 ? -23.33367 -9.21539  12.50618  1.000 56.37485  ? 239 PRO   A O    1 
ATOM   1806 C  CB   . PRO   A 1 239 ? -25.80521 -10.50070 14.23980  1.000 60.18621  ? 239 PRO   A CB   1 
ATOM   1807 C  CG   . PRO   A 1 239 ? -26.79216 -9.40024  14.00426  1.000 64.89178  ? 239 PRO   A CG   1 
ATOM   1808 C  CD   . PRO   A 1 239 ? -26.24766 -8.15274  14.58004  1.000 56.21203  ? 239 PRO   A CD   1 
ATOM   1809 N  N    . GLY   A 1 240 ? -22.76880 -11.17426 13.47031  1.000 65.12120  ? 240 GLY   A N    1 
ATOM   1810 C  CA   . GLY   A 1 240 ? -21.95326 -11.60033 12.35115  1.000 60.89101  ? 240 GLY   A CA   1 
ATOM   1811 C  C    . GLY   A 1 240 ? -22.79151 -11.99598 11.14519  1.000 70.07458  ? 240 GLY   A C    1 
ATOM   1812 O  O    . GLY   A 1 240 ? -23.90423 -12.50680 11.25681  1.000 67.16880  ? 240 GLY   A O    1 
ATOM   1813 N  N    . LEU   A 1 241 ? -22.21853 -11.77760 9.96572   1.000 66.77824  ? 241 LEU   A N    1 
ATOM   1814 C  CA   . LEU   A 1 241 ? -22.92245 -12.02354 8.71443   1.000 72.36490  ? 241 LEU   A CA   1 
ATOM   1815 C  C    . LEU   A 1 241 ? -23.29343 -13.49062 8.52639   1.000 75.06432  ? 241 LEU   A C    1 
ATOM   1816 O  O    . LEU   A 1 241 ? -24.25595 -13.79740 7.81398   1.000 80.51666  ? 241 LEU   A O    1 
ATOM   1817 C  CB   . LEU   A 1 241 ? -22.08349 -11.50716 7.55094   1.000 74.96485  ? 241 LEU   A CB   1 
ATOM   1818 C  CG   . LEU   A 1 241 ? -22.03088 -9.98520  7.64550   1.000 64.04737  ? 241 LEU   A CG   1 
ATOM   1819 C  CD1  . LEU   A 1 241 ? -21.25376 -9.41370  6.48884   1.000 65.55757  ? 241 LEU   A CD1  1 
ATOM   1820 C  CD2  . LEU   A 1 241 ? -23.45845 -9.45998  7.66156   1.000 68.30688  ? 241 LEU   A CD2  1 
ATOM   1821 N  N    . LEU   A 1 242 ? -22.56047 -14.40749 9.14390   1.000 84.04569  ? 242 LEU   A N    1 
ATOM   1822 C  CA   . LEU   A 1 242 ? -22.80708 -15.82972 8.94935   1.000 89.23678  ? 242 LEU   A CA   1 
ATOM   1823 C  C    . LEU   A 1 242 ? -23.69953 -16.39613 10.05897  1.000 95.87832  ? 242 LEU   A C    1 
ATOM   1824 O  O    . LEU   A 1 242 ? -23.80522 -15.83600 11.15538  1.000 93.21421  ? 242 LEU   A O    1 
ATOM   1825 C  CB   . LEU   A 1 242 ? -21.47873 -16.58967 8.86738   1.000 86.47667  ? 242 LEU   A CB   1 
ATOM   1826 C  CG   . LEU   A 1 242 ? -20.59941 -16.10622 7.70868   1.000 81.65718  ? 242 LEU   A CG   1 
ATOM   1827 C  CD1  . LEU   A 1 242 ? -19.28782 -16.85445 7.63751   1.000 86.40995  ? 242 LEU   A CD1  1 
ATOM   1828 C  CD2  . LEU   A 1 242 ? -21.35578 -16.22757 6.40280   1.000 87.19694  ? 242 LEU   A CD2  1 
ATOM   1829 N  N    . GLU   A 1 243 ? -24.38291 -17.50342 9.73428   1.000 97.07817  ? 243 GLU   A N    1 
ATOM   1830 C  CA   . GLU   A 1 243 ? -25.39529 -18.07395 10.62241  1.000 95.74538  ? 243 GLU   A CA   1 
ATOM   1831 C  C    . GLU   A 1 243 ? -24.78571 -18.47658 11.96015  1.000 101.84230 ? 243 GLU   A C    1 
ATOM   1832 O  O    . GLU   A 1 243 ? -23.73551 -19.12590 12.01088  1.000 99.88337  ? 243 GLU   A O    1 
ATOM   1833 C  CB   . GLU   A 1 243 ? -26.05356 -19.28122 9.94239   1.000 94.98091  ? 243 GLU   A CB   1 
ATOM   1834 C  CG   . GLU   A 1 243 ? -27.30095 -19.84092 10.63836  1.000 95.58909  ? 243 GLU   A CG   1 
ATOM   1835 C  CD   . GLU   A 1 243 ? -27.91969 -21.03706 9.89624   1.000 98.76682  ? 243 GLU   A CD   1 
ATOM   1836 O  OE1  . GLU   A 1 243 ? -27.34108 -21.49259 8.87765   1.000 98.71077  ? 243 GLU   A OE1  1 
ATOM   1837 O  OE2  . GLU   A 1 243 ? -29.00024 -21.51551 10.32161  1.000 93.16728  ? 243 GLU   A OE2  1 
ATOM   1838 N  N    . GLY   A 1 244 ? -25.43492 -18.05471 13.04660  1.000 101.84224 ? 244 GLY   A N    1 
ATOM   1839 C  CA   . GLY   A 1 244 ? -24.98327 -18.36551 14.38938  1.000 98.13013  ? 244 GLY   A CA   1 
ATOM   1840 C  C    . GLY   A 1 244 ? -23.99847 -17.39560 15.00517  1.000 103.36535 ? 244 GLY   A C    1 
ATOM   1841 O  O    . GLY   A 1 244 ? -23.45017 -17.70013 16.07353  1.000 109.80909 ? 244 GLY   A O    1 
ATOM   1842 N  N    . GLN   A 1 245 ? -23.76039 -16.23787 14.38651  1.000 100.00641 ? 245 GLN   A N    1 
ATOM   1843 C  CA   . GLN   A 1 245 ? -22.74160 -15.30221 14.87751  1.000 93.11798  ? 245 GLN   A CA   1 
ATOM   1844 C  C    . GLN   A 1 245 ? -23.34652 -14.10198 15.61431  1.000 89.66883  ? 245 GLN   A C    1 
ATOM   1845 O  O    . GLN   A 1 245 ? -24.56606 -14.00880 15.78496  1.000 87.16715  ? 245 GLN   A O    1 
ATOM   1846 C  CB   . GLN   A 1 245 ? -21.86648 -14.81024 13.71779  1.000 89.26198  ? 245 GLN   A CB   1 
ATOM   1847 C  CG   . GLN   A 1 245 ? -21.49102 -15.90016 12.70759  1.000 92.80972  ? 245 GLN   A CG   1 
ATOM   1848 C  CD   . GLN   A 1 245 ? -20.25995 -15.55533 11.85834  1.000 91.25096  ? 245 GLN   A CD   1 
ATOM   1849 O  OE1  . GLN   A 1 245 ? -19.98092 -14.38398 11.57679  1.000 80.30593  ? 245 GLN   A OE1  1 
ATOM   1850 N  NE2  . GLN   A 1 245 ? -19.50970 -16.58630 11.46188  1.000 95.99076  ? 245 GLN   A NE2  1 
ATOM   1851 N  N    . GLU   A 1 253 ? -13.49188 -11.22923 9.35595   1.000 91.88547  ? 253 GLU   A N    1 
ATOM   1852 C  CA   . GLU   A 1 253 ? -13.17531 -11.36906 7.93294   1.000 93.06207  ? 253 GLU   A CA   1 
ATOM   1853 C  C    . GLU   A 1 253 ? -14.42363 -11.25280 7.06156   1.000 89.28879  ? 253 GLU   A C    1 
ATOM   1854 O  O    . GLU   A 1 253 ? -14.90724 -10.15129 6.79331   1.000 79.49617  ? 253 GLU   A O    1 
ATOM   1855 C  CB   . GLU   A 1 253 ? -12.45321 -12.70483 7.66541   1.000 102.11656 ? 253 GLU   A CB   1 
ATOM   1856 C  CG   . GLU   A 1 253 ? -13.19310 -14.01741 8.06197   1.000 104.22665 ? 253 GLU   A CG   1 
ATOM   1857 C  CD   . GLU   A 1 253 ? -13.40857 -14.18731 9.56942   1.000 101.93860 ? 253 GLU   A CD   1 
ATOM   1858 O  OE1  . GLU   A 1 253 ? -13.34687 -13.18750 10.31536  1.000 101.23817 ? 253 GLU   A OE1  1 
ATOM   1859 O  OE2  . GLU   A 1 253 ? -13.61761 -15.33673 10.01105  1.000 100.91095 ? 253 GLU   A OE2  1 
ATOM   1860 N  N    . ASN   A 1 254 ? -14.94620 -12.39117 6.61544   1.000 94.39558  ? 254 ASN   A N    1 
ATOM   1861 C  CA   . ASN   A 1 254 ? -16.25646 -12.43062 5.98559   1.000 88.80212  ? 254 ASN   A CA   1 
ATOM   1862 C  C    . ASN   A 1 254 ? -17.40139 -12.41097 7.01196   1.000 83.12649  ? 254 ASN   A C    1 
ATOM   1863 O  O    . ASN   A 1 254 ? -18.56990 -12.52363 6.63609   1.000 80.99903  ? 254 ASN   A O    1 
ATOM   1864 C  CB   . ASN   A 1 254 ? -16.34806 -13.64633 5.05077   1.000 96.15987  ? 254 ASN   A CB   1 
ATOM   1865 C  CG   . ASN   A 1 254 ? -15.54742 -13.45708 3.75080   1.000 99.18694  ? 254 ASN   A CG   1 
ATOM   1866 O  OD1  . ASN   A 1 254 ? -14.88866 -12.43322 3.55491   1.000 95.62644  ? 254 ASN   A OD1  1 
ATOM   1867 N  ND2  . ASN   A 1 254 ? -15.61799 -14.44259 2.85752   1.000 100.49548 ? 254 ASN   A ND2  1 
ATOM   1868 N  N    . SER   A 1 255 ? -17.10290 -12.24122 8.29859   1.000 86.68198  ? 255 SER   A N    1 
ATOM   1869 C  CA   . SER   A 1 255 ? -18.16592 -12.23216 9.28755   1.000 79.58025  ? 255 SER   A CA   1 
ATOM   1870 C  C    . SER   A 1 255 ? -18.70010 -10.82961 9.56470   1.000 70.99221  ? 255 SER   A C    1 
ATOM   1871 O  O    . SER   A 1 255 ? -19.76938 -10.70350 10.16934  1.000 68.86728  ? 255 SER   A O    1 
ATOM   1872 C  CB   . SER   A 1 255 ? -17.68673 -12.88956 10.59005  1.000 72.34661  ? 255 SER   A CB   1 
ATOM   1873 O  OG   . SER   A 1 255 ? -16.73167 -12.09336 11.26404  1.000 77.88061  ? 255 SER   A OG   1 
ATOM   1874 N  N    . ALA   A 1 256 ? -18.04697 -9.78184  9.06731   1.000 65.30827  ? 256 ALA   A N    1 
ATOM   1875 C  CA   . ALA   A 1 256 ? -18.56135 -8.44291  9.30797   1.000 57.22059  ? 256 ALA   A CA   1 
ATOM   1876 C  C    . ALA   A 1 256 ? -18.07728 -7.50308  8.21350   1.000 53.29879  ? 256 ALA   A C    1 
ATOM   1877 O  O    . ALA   A 1 256 ? -17.10364 -7.78411  7.51562   1.000 60.62184  ? 256 ALA   A O    1 
ATOM   1878 C  CB   . ALA   A 1 256 ? -18.14331 -7.94479  10.69710  1.000 57.72549  ? 256 ALA   A CB   1 
ATOM   1879 N  N    . ILE   A 1 257 ? -18.81643 -6.41251  8.02996   1.000 52.18932  ? 257 ILE   A N    1 
ATOM   1880 C  CA   . ILE   A 1 257 ? -18.36788 -5.30338  7.19825   1.000 49.87271  ? 257 ILE   A CA   1 
ATOM   1881 C  C    . ILE   A 1 257 ? -17.40638 -4.44460  8.01915   1.000 51.50754  ? 257 ILE   A C    1 
ATOM   1882 O  O    . ILE   A 1 257 ? -17.68144 -4.14035  9.18267   1.000 53.37179  ? 257 ILE   A O    1 
ATOM   1883 C  CB   . ILE   A 1 257 ? -19.55254 -4.45065  6.72861   1.000 45.66674  ? 257 ILE   A CB   1 
ATOM   1884 C  CG1  . ILE   A 1 257 ? -20.58167 -5.32421  5.99747   1.000 51.40101  ? 257 ILE   A CG1  1 
ATOM   1885 C  CG2  . ILE   A 1 257 ? -19.04344 -3.29186  5.86634   1.000 48.85315  ? 257 ILE   A CG2  1 
ATOM   1886 C  CD1  . ILE   A 1 257 ? -19.95828 -6.05620  4.87781   1.000 53.77589  ? 257 ILE   A CD1  1 
ATOM   1887 N  N    . PHE   A 1 258 ? -16.27294 -4.07923  7.41809   1.000 47.14884  ? 258 PHE   A N    1 
ATOM   1888 C  CA   . PHE   A 1 258 ? -15.32313 -3.11183  7.95008   1.000 53.98131  ? 258 PHE   A CA   1 
ATOM   1889 C  C    . PHE   A 1 258 ? -15.38759 -1.80366  7.16267   1.000 52.15567  ? 258 PHE   A C    1 
ATOM   1890 O  O    . PHE   A 1 258 ? -15.90110 -1.75381  6.04923   1.000 52.53020  ? 258 PHE   A O    1 
ATOM   1891 C  CB   . PHE   A 1 258 ? -13.92050 -3.71292  7.96637   1.000 56.18931  ? 258 PHE   A CB   1 
ATOM   1892 C  CG   . PHE   A 1 258 ? -13.81530 -4.92797  8.85125   1.000 55.96497  ? 258 PHE   A CG   1 
ATOM   1893 C  CD1  . PHE   A 1 258 ? -13.60178 -4.77731  10.22434  1.000 57.40446  ? 258 PHE   A CD1  1 
ATOM   1894 C  CD2  . PHE   A 1 258 ? -14.04225 -6.20656  8.33653   1.000 58.73099  ? 258 PHE   A CD2  1 
ATOM   1895 C  CE1  . PHE   A 1 258 ? -13.53537 -5.87516  11.07370  1.000 57.60585  ? 258 PHE   A CE1  1 
ATOM   1896 C  CE2  . PHE   A 1 258 ? -13.98637 -7.32020  9.16626   1.000 62.74716  ? 258 PHE   A CE2  1 
ATOM   1897 C  CZ   . PHE   A 1 258 ? -13.72978 -7.15164  10.55049  1.000 63.77842  ? 258 PHE   A CZ   1 
ATOM   1898 N  N    . MET   A 1 259 ? -14.86893 -0.72975  7.77366   1.000 49.00559  ? 259 MET   A N    1 
ATOM   1899 C  CA   . MET   A 1 259 ? -15.01376 0.63887   7.25992   1.000 45.39075  ? 259 MET   A CA   1 
ATOM   1900 C  C    . MET   A 1 259 ? -14.19602 0.88830   5.99495   1.000 48.84235  ? 259 MET   A C    1 
ATOM   1901 O  O    . MET   A 1 259 ? -14.46224 1.86240   5.28677   1.000 54.34213  ? 259 MET   A O    1 
ATOM   1902 C  CB   . MET   A 1 259 ? -14.61471 1.68759   8.32887   1.000 51.86423  ? 259 MET   A CB   1 
ATOM   1903 C  CG   . MET   A 1 259 ? -15.57330 1.75708   9.48372   1.000 46.63116  ? 259 MET   A CG   1 
ATOM   1904 S  SD   . MET   A 1 259 ? -17.32572 1.95466   8.98492   1.000 46.34296  ? 259 MET   A SD   1 
ATOM   1905 C  CE   . MET   A 1 259 ? -17.32790 3.60146   8.34164   1.000 40.71243  ? 259 MET   A CE   1 
ATOM   1906 N  N    . ASP   A 1 260 ? -13.19101 0.06978   5.71155   1.000 56.01557  ? 260 ASP   A N    1 
ATOM   1907 C  CA   . ASP   A 1 260 ? -12.44050 0.24337   4.47732   1.000 66.09913  ? 260 ASP   A CA   1 
ATOM   1908 C  C    . ASP   A 1 260 ? -12.92919 -0.65766  3.35000   1.000 67.27350  ? 260 ASP   A C    1 
ATOM   1909 O  O    . ASP   A 1 260 ? -12.49415 -0.46890  2.21249   1.000 80.27337  ? 260 ASP   A O    1 
ATOM   1910 C  CB   . ASP   A 1 260 ? -10.95129 -0.00042  4.74626   1.000 60.06305  ? 260 ASP   A CB   1 
ATOM   1911 C  CG   . ASP   A 1 260 ? -10.68380 -1.37359  5.30046   1.000 67.24042  ? 260 ASP   A CG   1 
ATOM   1912 O  OD1  . ASP   A 1 260 ? -11.33174 -1.72221  6.30245   1.000 70.47273  ? 260 ASP   A OD1  1 
ATOM   1913 O  OD2  . ASP   A 1 260 ? -9.77484  -2.07474  4.80403   1.000 76.96634  ? 260 ASP   A OD2  1 
ATOM   1914 N  N    . ASP   A 1 261 ? -13.86668 -1.57101  3.61563   1.000 63.17859  ? 261 ASP   A N    1 
ATOM   1915 C  CA   . ASP   A 1 261 ? -14.34684 -2.49056  2.57782   1.000 70.47705  ? 261 ASP   A CA   1 
ATOM   1916 C  C    . ASP   A 1 261 ? -14.84052 -1.71569  1.35158   1.000 73.69907  ? 261 ASP   A C    1 
ATOM   1917 O  O    . ASP   A 1 261 ? -15.46793 -0.65818  1.47535   1.000 80.93356  ? 261 ASP   A O    1 
ATOM   1918 C  CB   . ASP   A 1 261 ? -15.48194 -3.36550  3.14292   1.000 56.39519  ? 261 ASP   A CB   1 
ATOM   1919 C  CG   . ASP   A 1 261 ? -14.97703 -4.62694  3.86803   1.000 62.82699  ? 261 ASP   A CG   1 
ATOM   1920 O  OD1  . ASP   A 1 261 ? -13.81506 -5.05427  3.64598   1.000 69.94776  ? 261 ASP   A OD1  1 
ATOM   1921 O  OD2  . ASP   A 1 261 ? -15.76180 -5.21179  4.66104   1.000 60.28760  ? 261 ASP   A OD2  1 
ATOM   1922 N  N    . SER   A 1 262 ? -14.56602 -2.24714  0.15322   1.000 81.62096  ? 262 SER   A N    1 
ATOM   1923 C  CA   . SER   A 1 262 ? -15.03335 -1.66825  -1.11123  1.000 83.59280  ? 262 SER   A CA   1 
ATOM   1924 C  C    . SER   A 1 262 ? -16.48632 -2.05602  -1.42527  1.000 83.30449  ? 262 SER   A C    1 
ATOM   1925 O  O    . SER   A 1 262 ? -17.08549 -2.91479  -0.77017  1.000 81.74929  ? 262 SER   A O    1 
ATOM   1926 C  CB   . SER   A 1 262 ? -14.12966 -2.09779  -2.26045  1.000 81.94571  ? 262 SER   A CB   1 
ATOM   1927 O  OG   . SER   A 1 262 ? -14.27580 -3.48053  -2.48795  1.000 83.09620  ? 262 SER   A OG   1 
ATOM   1928 N  N    . GLU   A 1 263 ? -17.05924 -1.42469  -2.46711  1.000 78.79936  ? 263 GLU   A N    1 
ATOM   1929 C  CA   . GLU   A 1 263 ? -18.43598 -1.75791  -2.83066  1.000 76.81716  ? 263 GLU   A CA   1 
ATOM   1930 C  C    . GLU   A 1 263 ? -18.55791 -3.23582  -3.15975  1.000 75.50528  ? 263 GLU   A C    1 
ATOM   1931 O  O    . GLU   A 1 263 ? -19.56557 -3.86691  -2.81843  1.000 72.00217  ? 263 GLU   A O    1 
ATOM   1932 C  CB   . GLU   A 1 263 ? -18.96635 -0.91307  -4.00879  1.000 81.62495  ? 263 GLU   A CB   1 
ATOM   1933 C  CG   . GLU   A 1 263 ? -19.12687 0.58818   -3.71442  1.000 81.30046  ? 263 GLU   A CG   1 
ATOM   1934 C  CD   . GLU   A 1 263 ? -20.24210 1.27104   -4.52811  1.000 89.03553  ? 263 GLU   A CD   1 
ATOM   1935 O  OE1  . GLU   A 1 263 ? -20.84710 2.23130   -3.98072  1.000 83.28135  ? 263 GLU   A OE1  1 
ATOM   1936 O  OE2  . GLU   A 1 263 ? -20.52464 0.85447   -5.68391  1.000 79.38987  ? 263 GLU   A OE2  1 
ATOM   1937 N  N    . SER   A 1 264 ? -17.55237 -3.80660  -3.83436  1.000 78.57151  ? 264 SER   A N    1 
ATOM   1938 C  CA   . SER   A 1 264 ? -17.62520 -5.23335  -4.14342  1.000 84.37593  ? 264 SER   A CA   1 
ATOM   1939 C  C    . SER   A 1 264 ? -17.35649 -6.07560  -2.89978  1.000 76.73246  ? 264 SER   A C    1 
ATOM   1940 O  O    . SER   A 1 264 ? -17.91087 -7.16775  -2.77401  1.000 73.78946  ? 264 SER   A O    1 
ATOM   1941 C  CB   . SER   A 1 264 ? -16.66498 -5.62159  -5.28071  1.000 83.47741  ? 264 SER   A CB   1 
ATOM   1942 O  OG   . SER   A 1 264 ? -15.31606 -5.69889  -4.82717  1.000 84.16129  ? 264 SER   A OG   1 
ATOM   1943 N  N    . ASP   A 1 265 ? -16.50072 -5.60843  -1.98396  1.000 81.29846  ? 265 ASP   A N    1 
ATOM   1944 C  CA   . ASP   A 1 265 ? -16.33131 -6.31387  -0.71213  1.000 70.80073  ? 265 ASP   A CA   1 
ATOM   1945 C  C    . ASP   A 1 265 ? -17.66566 -6.43293  0.00174   1.000 63.61183  ? 265 ASP   A C    1 
ATOM   1946 O  O    . ASP   A 1 265 ? -18.04679 -7.51396  0.45556   1.000 67.31499  ? 265 ASP   A O    1 
ATOM   1947 C  CB   . ASP   A 1 265 ? -15.34831 -5.57084  0.20443   1.000 75.55512  ? 265 ASP   A CB   1 
ATOM   1948 C  CG   . ASP   A 1 265 ? -13.88220 -5.85849  -0.09615  1.000 79.20704  ? 265 ASP   A CG   1 
ATOM   1949 O  OD1  . ASP   A 1 265 ? -13.57195 -6.97994  -0.55891  1.000 79.38724  ? 265 ASP   A OD1  1 
ATOM   1950 O  OD2  . ASP   A 1 265 ? -13.03261 -4.97654  0.22003   1.000 79.75478  ? 265 ASP   A OD2  1 
ATOM   1951 N  N    . VAL   A 1 266 ? -18.38205 -5.31215  0.12051   1.000 62.19419  ? 266 VAL   A N    1 
ATOM   1952 C  CA   . VAL   A 1 266 ? -19.69405 -5.30818  0.75925   1.000 65.55078  ? 266 VAL   A CA   1 
ATOM   1953 C  C    . VAL   A 1 266 ? -20.64630 -6.22100  0.00851   1.000 68.93945  ? 266 VAL   A C    1 
ATOM   1954 O  O    . VAL   A 1 266 ? -21.37659 -7.02396  0.60443   1.000 61.92571  ? 266 VAL   A O    1 
ATOM   1955 C  CB   . VAL   A 1 266 ? -20.23524 -3.87244  0.86122   1.000 57.50725  ? 266 VAL   A CB   1 
ATOM   1956 C  CG1  . VAL   A 1 266 ? -21.70262 -3.87001  1.21702   1.000 62.56346  ? 266 VAL   A CG1  1 
ATOM   1957 C  CG2  . VAL   A 1 266 ? -19.41169 -3.10663  1.93766   1.000 57.59310  ? 266 VAL   A CG2  1 
ATOM   1958 N  N    . ASN   A 1 267 ? -20.66511 -6.09290  -1.31346  1.000 68.00574  ? 267 ASN   A N    1 
ATOM   1959 C  CA   . ASN   A 1 267 ? -21.56244 -6.90555  -2.12437  1.000 60.92934  ? 267 ASN   A CA   1 
ATOM   1960 C  C    . ASN   A 1 267 ? -21.26848 -8.40136  -1.95058  1.000 64.95273  ? 267 ASN   A C    1 
ATOM   1961 O  O    . ASN   A 1 267 ? -22.16263 -9.17555  -1.59469  1.000 62.88058  ? 267 ASN   A O    1 
ATOM   1962 C  CB   . ASN   A 1 267 ? -21.47007 -6.39900  -3.56460  1.000 55.35189  ? 267 ASN   A CB   1 
ATOM   1963 C  CG   . ASN   A 1 267 ? -22.26342 -5.08195  -3.75545  1.000 71.92928  ? 267 ASN   A CG   1 
ATOM   1964 O  OD1  . ASN   A 1 267 ? -23.11079 -4.74711  -2.92156  1.000 70.24659  ? 267 ASN   A OD1  1 
ATOM   1965 N  ND2  . ASN   A 1 267 ? -22.03198 -4.37262  -4.85608  1.000 74.29862  ? 267 ASN   A ND2  1 
ATOM   1966 N  N    . ARG   A 1 268 ? -19.99510 -8.79988  -2.03095  1.000 67.76310  ? 268 ARG   A N    1 
ATOM   1967 C  CA   . ARG   A 1 268 ? -19.61959 -10.20018 -1.81111  1.000 70.30850  ? 268 ARG   A CA   1 
ATOM   1968 C  C    . ARG   A 1 268 ? -19.97013 -10.69288 -0.39852  1.000 73.83345  ? 268 ARG   A C    1 
ATOM   1969 O  O    . ARG   A 1 268 ? -20.42195 -11.83590 -0.23540  1.000 71.40846  ? 268 ARG   A O    1 
ATOM   1970 C  CB   . ARG   A 1 268 ? -18.12722 -10.39786 -2.08292  1.000 67.33853  ? 268 ARG   A CB   1 
ATOM   1971 C  CG   . ARG   A 1 268 ? -17.54718 -11.72602 -1.54486  1.000 77.04335  ? 268 ARG   A CG   1 
ATOM   1972 C  CD   . ARG   A 1 268 ? -16.09878 -11.92514 -1.97872  1.000 86.92611  ? 268 ARG   A CD   1 
ATOM   1973 N  NE   . ARG   A 1 268 ? -15.18322 -10.86995 -1.54319  1.000 92.21424  ? 268 ARG   A NE   1 
ATOM   1974 C  CZ   . ARG   A 1 268 ? -14.45059 -10.88341 -0.43717  1.000 93.49811  ? 268 ARG   A CZ   1 
ATOM   1975 N  NH1  . ARG   A 1 268 ? -14.55497 -11.85493 0.45682   1.000 94.98075  ? 268 ARG   A NH1  1 
ATOM   1976 N  NH2  . ARG   A 1 268 ? -13.56679 -9.90991  -0.23834  1.000 92.88748  ? 268 ARG   A NH2  1 
ATOM   1977 N  N    . LYS   A 1 269 ? -19.72016 -9.88737  0.64608   1.000 65.05719  ? 269 LYS   A N    1 
ATOM   1978 C  CA   . LYS   A 1 269 ? -20.01575 -10.38080 1.99067   1.000 64.50035  ? 269 LYS   A CA   1 
ATOM   1979 C  C    . LYS   A 1 269 ? -21.50964 -10.43103 2.27752   1.000 68.60209  ? 269 LYS   A C    1 
ATOM   1980 O  O    . LYS   A 1 269 ? -21.97756 -11.33974 2.96989   1.000 68.87344  ? 269 LYS   A O    1 
ATOM   1981 C  CB   . LYS   A 1 269 ? -19.32473 -9.53426  3.06845   1.000 64.86722  ? 269 LYS   A CB   1 
ATOM   1982 C  CG   . LYS   A 1 269 ? -17.84375 -9.71186  3.12292   1.000 62.06609  ? 269 LYS   A CG   1 
ATOM   1983 C  CD   . LYS   A 1 269 ? -17.22339 -8.67988  4.07906   1.000 68.80703  ? 269 LYS   A CD   1 
ATOM   1984 C  CE   . LYS   A 1 269 ? -15.73810 -8.83085  4.17760   1.000 65.53332  ? 269 LYS   A CE   1 
ATOM   1985 N  NZ   . LYS   A 1 269 ? -15.17670 -7.84244  5.15819   1.000 61.73267  ? 269 LYS   A NZ   1 
ATOM   1986 N  N    . ILE   A 1 270 ? -22.26728 -9.43890  1.81504   1.000 65.00002  ? 270 ILE   A N    1 
ATOM   1987 C  CA   . ILE   A 1 270 ? -23.70022 -9.43730  2.06467   1.000 68.08575  ? 270 ILE   A CA   1 
ATOM   1988 C  C    . ILE   A 1 270 ? -24.37090 -10.55366 1.28126   1.000 67.47050  ? 270 ILE   A C    1 
ATOM   1989 O  O    . ILE   A 1 270 ? -25.29623 -11.20855 1.76863   1.000 70.09118  ? 270 ILE   A O    1 
ATOM   1990 C  CB   . ILE   A 1 270 ? -24.29727 -8.06802  1.70999   1.000 73.10763  ? 270 ILE   A CB   1 
ATOM   1991 C  CG1  . ILE   A 1 270 ? -23.69805 -6.98430  2.60410   1.000 62.51942  ? 270 ILE   A CG1  1 
ATOM   1992 C  CG2  . ILE   A 1 270 ? -25.80223 -8.11791  1.89944   1.000 71.17125  ? 270 ILE   A CG2  1 
ATOM   1993 C  CD1  . ILE   A 1 270 ? -23.57229 -7.40241  4.02526   1.000 66.90481  ? 270 ILE   A CD1  1 
ATOM   1994 N  N    . LYS   A 1 271 ? -23.90807 -10.78217 0.05522   1.000 69.11762  ? 271 LYS   A N    1 
ATOM   1995 C  CA   . LYS   A 1 271 ? -24.52966 -11.77062 -0.82172  1.000 80.00739  ? 271 LYS   A CA   1 
ATOM   1996 C  C    . LYS   A 1 271 ? -24.48704 -13.14823 -0.18517  1.000 79.17873  ? 271 LYS   A C    1 
ATOM   1997 O  O    . LYS   A 1 271 ? -25.43758 -13.92291 -0.31420  1.000 77.57842  ? 271 LYS   A O    1 
ATOM   1998 C  CB   . LYS   A 1 271 ? -23.79183 -11.79142 -2.16282  1.000 80.44518  ? 271 LYS   A CB   1 
ATOM   1999 C  CG   . LYS   A 1 271 ? -24.36013 -12.66825 -3.29453  1.000 85.01674  ? 271 LYS   A CG   1 
ATOM   2000 C  CD   . LYS   A 1 271 ? -23.24777 -13.00764 -4.31784  1.000 91.93289  ? 271 LYS   A CD   1 
ATOM   2001 C  CE   . LYS   A 1 271 ? -23.75212 -13.99717 -5.38467  1.000 102.13255 ? 271 LYS   A CE   1 
ATOM   2002 N  NZ   . LYS   A 1 271 ? -22.85727 -14.07252 -6.57856  1.000 102.57107 ? 271 LYS   A NZ   1 
ATOM   2003 N  N    . LYS   A 1 272 ? -23.40406 -13.45676 0.52483   1.000 78.32255  ? 272 LYS   A N    1 
ATOM   2004 C  CA   . LYS   A 1 272 ? -23.23492 -14.74776 1.16923   1.000 77.44062  ? 272 LYS   A CA   1 
ATOM   2005 C  C    . LYS   A 1 272 ? -23.74433 -14.74951 2.60311   1.000 70.17053  ? 272 LYS   A C    1 
ATOM   2006 O  O    . LYS   A 1 272 ? -23.69783 -15.78894 3.25959   1.000 72.39423  ? 272 LYS   A O    1 
ATOM   2007 C  CB   . LYS   A 1 272 ? -21.75353 -15.16141 1.10798   1.000 74.14375  ? 272 LYS   A CB   1 
ATOM   2008 C  CG   . LYS   A 1 272 ? -21.20637 -15.86337 2.33116   1.000 88.14249  ? 272 LYS   A CG   1 
ATOM   2009 C  CD   . LYS   A 1 272 ? -21.56564 -17.35904 2.39233   1.000 91.56144  ? 272 LYS   A CD   1 
ATOM   2010 C  CE   . LYS   A 1 272 ? -21.06430 -17.93487 3.72536   1.000 91.53183  ? 272 LYS   A CE   1 
ATOM   2011 N  NZ   . LYS   A 1 272 ? -21.06084 -19.42394 3.79160   1.000 98.99449  ? 272 LYS   A NZ   1 
ATOM   2012 N  N    . ALA   A 1 273 ? -24.26166 -13.63219 3.10023   1.000 72.96796  ? 273 ALA   A N    1 
ATOM   2013 C  CA   . ALA   A 1 273 ? -24.66757 -13.58915 4.49547   1.000 69.63329  ? 273 ALA   A CA   1 
ATOM   2014 C  C    . ALA   A 1 273 ? -25.91201 -14.44418 4.73025   1.000 76.88819  ? 273 ALA   A C    1 
ATOM   2015 O  O    . ALA   A 1 273 ? -26.64768 -14.81615 3.79886   1.000 80.78268  ? 273 ALA   A O    1 
ATOM   2016 C  CB   . ALA   A 1 273 ? -24.93862 -12.15321 4.93658   1.000 72.28477  ? 273 ALA   A CB   1 
ATOM   2017 N  N    . TYR   A 1 274 ? -26.13774 -14.76079 6.00149   1.000 80.74292  ? 274 TYR   A N    1 
ATOM   2018 C  CA   . TYR   A 1 274 ? -27.35451 -15.45423 6.39236   1.000 82.48519  ? 274 TYR   A CA   1 
ATOM   2019 C  C    . TYR   A 1 274 ? -28.53484 -14.49633 6.29698   1.000 80.80030  ? 274 TYR   A C    1 
ATOM   2020 O  O    . TYR   A 1 274 ? -28.54402 -13.43634 6.93169   1.000 82.52814  ? 274 TYR   A O    1 
ATOM   2021 C  CB   . TYR   A 1 274 ? -27.22352 -16.01658 7.80983   1.000 80.93608  ? 274 TYR   A CB   1 
ATOM   2022 C  CG   . TYR   A 1 274 ? -28.34990 -16.96234 8.17043   1.000 85.86065  ? 274 TYR   A CG   1 
ATOM   2023 C  CD1  . TYR   A 1 274 ? -28.74632 -17.95679 7.26937   1.000 88.01791  ? 274 TYR   A CD1  1 
ATOM   2024 C  CD2  . TYR   A 1 274 ? -28.96727 -16.91419 9.42353   1.000 86.89754  ? 274 TYR   A CD2  1 
ATOM   2025 C  CE1  . TYR   A 1 274 ? -29.75688 -18.84585 7.57905   1.000 86.70110  ? 274 TYR   A CE1  1 
ATOM   2026 C  CE2  . TYR   A 1 274 ? -29.97428 -17.80134 9.75149   1.000 86.23677  ? 274 TYR   A CE2  1 
ATOM   2027 C  CZ   . TYR   A 1 274 ? -30.36814 -18.76699 8.81826   1.000 90.23176  ? 274 TYR   A CZ   1 
ATOM   2028 O  OH   . TYR   A 1 274 ? -31.36886 -19.66088 9.11964   1.000 90.79368  ? 274 TYR   A OH   1 
ATOM   2029 N  N    . CYS   A 1 275 ? -29.55487 -14.89714 5.54147   1.000 84.53313  ? 275 CYS   A N    1 
ATOM   2030 C  CA   . CYS   A 1 275 ? -30.73179 -14.05850 5.30323   1.000 86.72896  ? 275 CYS   A CA   1 
ATOM   2031 C  C    . CYS   A 1 275 ? -31.93263 -14.97090 5.10447   1.000 91.07818  ? 275 CYS   A C    1 
ATOM   2032 O  O    . CYS   A 1 275 ? -32.42765 -15.16097 3.97848   1.000 98.08879  ? 275 CYS   A O    1 
ATOM   2033 C  CB   . CYS   A 1 275 ? -30.50184 -13.14749 4.09472   1.000 81.20030  ? 275 CYS   A CB   1 
ATOM   2034 S  SG   . CYS   A 1 275 ? -31.72449 -11.84325 3.83898   1.000 83.16343  ? 275 CYS   A SG   1 
ATOM   2035 N  N    . PRO   A 1 276 ? -32.43163 -15.56994 6.18511   1.000 90.32158  ? 276 PRO   A N    1 
ATOM   2036 C  CA   . PRO   A 1 276 ? -33.49313 -16.57145 6.06115   1.000 95.77189  ? 276 PRO   A CA   1 
ATOM   2037 C  C    . PRO   A 1 276 ? -34.72977 -15.97989 5.40454   1.000 101.38773 ? 276 PRO   A C    1 
ATOM   2038 O  O    . PRO   A 1 276 ? -35.24152 -14.94140 5.85246   1.000 97.93662  ? 276 PRO   A O    1 
ATOM   2039 C  CB   . PRO   A 1 276 ? -33.75316 -16.98477 7.52091   1.000 89.56472  ? 276 PRO   A CB   1 
ATOM   2040 C  CG   . PRO   A 1 276 ? -33.18892 -15.85474 8.35950   1.000 83.95255  ? 276 PRO   A CG   1 
ATOM   2041 C  CD   . PRO   A 1 276 ? -32.01082 -15.37200 7.58666   1.000 82.75470  ? 276 PRO   A CD   1 
ATOM   2042 N  N    . PRO   A 1 277 ? -35.24345 -16.61089 4.34043   1.000 115.40488 ? 277 PRO   A N    1 
ATOM   2043 C  CA   . PRO   A 1 277 ? -36.44920 -16.07769 3.68535   1.000 123.58743 ? 277 PRO   A CA   1 
ATOM   2044 C  C    . PRO   A 1 277 ? -37.62067 -16.00299 4.65654   1.000 126.93937 ? 277 PRO   A C    1 
ATOM   2045 O  O    . PRO   A 1 277 ? -37.88853 -16.94512 5.40834   1.000 131.31256 ? 277 PRO   A O    1 
ATOM   2046 C  CB   . PRO   A 1 277 ? -36.71472 -17.07217 2.54142   1.000 113.63352 ? 277 PRO   A CB   1 
ATOM   2047 C  CG   . PRO   A 1 277 ? -35.43638 -17.82286 2.34735   1.000 117.00667 ? 277 PRO   A CG   1 
ATOM   2048 C  CD   . PRO   A 1 277 ? -34.69890 -17.79576 3.64709   1.000 110.93146 ? 277 PRO   A CD   1 
ATOM   2049 N  N    . ASN   A 1 278 ? -38.31196 -14.85824 4.65020   1.000 99.62034  ? 278 ASN   A N    1 
ATOM   2050 C  CA   . ASN   A 1 278 ? -39.55759 -14.66767 5.39052   1.000 95.32483  ? 278 ASN   A CA   1 
ATOM   2051 C  C    . ASN   A 1 278 ? -39.37394 -14.71438 6.91411   1.000 90.53078  ? 278 ASN   A C    1 
ATOM   2052 O  O    . ASN   A 1 278 ? -40.36395 -14.74458 7.66177   1.000 88.98366  ? 278 ASN   A O    1 
ATOM   2053 C  CB   . ASN   A 1 278 ? -40.60802 -15.67710 4.90758   1.000 88.09996  ? 278 ASN   A CB   1 
ATOM   2054 C  CG   . ASN   A 1 278 ? -40.86371 -15.57629 3.37682   1.000 89.64388  ? 278 ASN   A CG   1 
ATOM   2055 O  OD1  . ASN   A 1 278 ? -41.75665 -14.85473 2.95804   1.000 95.11667  ? 278 ASN   A OD1  1 
ATOM   2056 N  ND2  . ASN   A 1 278 ? -40.07501 -16.28406 2.56013   1.000 78.09247  ? 278 ASN   A ND2  1 
ATOM   2057 N  N    . VAL   A 1 279 ? -38.13535 -14.74041 7.39632   1.000 85.10684  ? 279 VAL   A N    1 
ATOM   2058 C  CA   . VAL   A 1 279 ? -37.83045 -14.83355 8.81687   1.000 82.47592  ? 279 VAL   A CA   1 
ATOM   2059 C  C    . VAL   A 1 279 ? -36.96027 -13.64377 9.19875   1.000 97.54681  ? 279 VAL   A C    1 
ATOM   2060 O  O    . VAL   A 1 279 ? -35.94900 -13.37370 8.53917   1.000 89.58989  ? 279 VAL   A O    1 
ATOM   2061 C  CB   . VAL   A 1 279 ? -37.12347 -16.15269 9.14364   1.000 80.55415  ? 279 VAL   A CB   1 
ATOM   2062 C  CG1  . VAL   A 1 279 ? -36.88661 -16.26452 10.68937  1.000 85.00481  ? 279 VAL   A CG1  1 
ATOM   2063 C  CG2  . VAL   A 1 279 ? -37.89622 -17.32185 8.51031   1.000 87.61919  ? 279 VAL   A CG2  1 
ATOM   2064 N  N    . ILE   A 1 280 ? -37.34835 -12.93316 10.25492  1.000 106.50536 ? 280 ILE   A N    1 
ATOM   2065 C  CA   . ILE   A 1 280 ? -36.57319 -11.77232 10.69164  1.000 107.65969 ? 280 ILE   A CA   1 
ATOM   2066 C  C    . ILE   A 1 280 ? -35.53988 -12.13004 11.74530  1.000 109.79913 ? 280 ILE   A C    1 
ATOM   2067 O  O    . ILE   A 1 280 ? -34.42581 -11.59957 11.72922  1.000 108.19889 ? 280 ILE   A O    1 
ATOM   2068 C  CB   . ILE   A 1 280 ? -37.50522 -10.66761 11.22449  1.000 109.60267 ? 280 ILE   A CB   1 
ATOM   2069 C  CG1  . ILE   A 1 280 ? -38.08387 -9.83964  10.07604  1.000 110.63591 ? 280 ILE   A CG1  1 
ATOM   2070 C  CG2  . ILE   A 1 280 ? -36.77133 -9.82166  12.27904  1.000 110.26040 ? 280 ILE   A CG2  1 
ATOM   2071 C  CD1  . ILE   A 1 280 ? -39.08837 -8.80005  10.50351  1.000 112.83909 ? 280 ILE   A CD1  1 
ATOM   2072 N  N    . GLU   A 1 281 ? -35.88185 -13.00239 12.68342  1.000 111.29722 ? 281 GLU   A N    1 
ATOM   2073 C  CA   . GLU   A 1 281 ? -34.99130 -13.21365 13.81156  1.000 116.86710 ? 281 GLU   A CA   1 
ATOM   2074 C  C    . GLU   A 1 281 ? -33.65666 -13.81738 13.38952  1.000 120.88709 ? 281 GLU   A C    1 
ATOM   2075 O  O    . GLU   A 1 281 ? -33.61002 -14.76545 12.59756  1.000 114.44206 ? 281 GLU   A O    1 
ATOM   2076 C  CB   . GLU   A 1 281 ? -35.65200 -14.07062 14.87700  1.000 121.36927 ? 281 GLU   A CB   1 
ATOM   2077 C  CG   . GLU   A 1 281 ? -34.68343 -14.28223 16.00960  1.000 128.69398 ? 281 GLU   A CG   1 
ATOM   2078 C  CD   . GLU   A 1 281 ? -34.20540 -12.96030 16.59716  1.000 130.29751 ? 281 GLU   A CD   1 
ATOM   2079 O  OE1  . GLU   A 1 281 ? -34.72646 -11.89505 16.19174  1.000 129.31575 ? 281 GLU   A OE1  1 
ATOM   2080 O  OE2  . GLU   A 1 281 ? -33.28265 -12.98532 17.43975  1.000 130.88930 ? 281 GLU   A OE2  1 
ATOM   2081 N  N    . ASN   A 1 282 ? -32.56928 -13.23130 13.91344  1.000 118.60157 ? 282 ASN   A N    1 
ATOM   2082 C  CA   . ASN   A 1 282 ? -31.17368 -13.62298 13.71089  1.000 111.64921 ? 282 ASN   A CA   1 
ATOM   2083 C  C    . ASN   A 1 282 ? -30.69341 -13.39107 12.28578  1.000 104.34204 ? 282 ASN   A C    1 
ATOM   2084 O  O    . ASN   A 1 282 ? -29.57435 -13.80048 11.93759  1.000 101.27031 ? 282 ASN   A O    1 
ATOM   2085 C  CB   . ASN   A 1 282 ? -30.93150 -15.08284 14.09905  1.000 117.21762 ? 282 ASN   A CB   1 
ATOM   2086 C  CG   . ASN   A 1 282 ? -30.94908 -15.29467 15.60022  1.000 120.57641 ? 282 ASN   A CG   1 
ATOM   2087 O  OD1  . ASN   A 1 282 ? -31.77397 -16.04773 16.11986  1.000 118.37959 ? 282 ASN   A OD1  1 
ATOM   2088 N  ND2  . ASN   A 1 282 ? -30.02908 -14.63591 16.30655  1.000 119.96336 ? 282 ASN   A ND2  1 
ATOM   2089 N  N    . ASN   A 1 283 ? -31.48376 -12.69935 11.47001  1.000 101.01541 ? 283 ASN   A N    1 
ATOM   2090 C  CA   . ASN   A 1 283 ? -31.16728 -12.42216 10.08068  1.000 94.25648  ? 283 ASN   A CA   1 
ATOM   2091 C  C    . ASN   A 1 283 ? -30.30816 -11.16950 10.11290  1.000 85.89040  ? 283 ASN   A C    1 
ATOM   2092 O  O    . ASN   A 1 283 ? -30.84802 -10.05600 10.07018  1.000 88.16313  ? 283 ASN   A O    1 
ATOM   2093 C  CB   . ASN   A 1 283 ? -32.45810 -12.19864 9.27990   1.000 87.37759  ? 283 ASN   A CB   1 
ATOM   2094 C  CG   . ASN   A 1 283 ? -32.21772 -12.00260 7.78668   1.000 87.30296  ? 283 ASN   A CG   1 
ATOM   2095 O  OD1  . ASN   A 1 283 ? -31.14204 -11.59990 7.35730   1.000 82.01622  ? 283 ASN   A OD1  1 
ATOM   2096 N  ND2  . ASN   A 1 283 ? -33.24611 -12.24170 6.99678   1.000 84.13626  ? 283 ASN   A ND2  1 
ATOM   2097 N  N    . PRO   A 1 284 ? -28.97858 -11.30340 10.09317  1.000 85.11459  ? 284 PRO   A N    1 
ATOM   2098 C  CA   . PRO   A 1 284 ? -28.11822 -10.12392 10.31525  1.000 78.29976  ? 284 PRO   A CA   1 
ATOM   2099 C  C    . PRO   A 1 284 ? -28.30648 -9.05863  9.25178   1.000 73.83415  ? 284 PRO   A C    1 
ATOM   2100 O  O    . PRO   A 1 284 ? -28.01453 -7.88617  9.50847   1.000 76.76584  ? 284 PRO   A O    1 
ATOM   2101 C  CB   . PRO   A 1 284 ? -26.69876 -10.71037 10.31733  1.000 72.54778  ? 284 PRO   A CB   1 
ATOM   2102 C  CG   . PRO   A 1 284 ? -26.81908 -11.92933 9.46115   1.000 73.09804  ? 284 PRO   A CG   1 
ATOM   2103 C  CD   . PRO   A 1 284 ? -28.19873 -12.49839 9.72999   1.000 82.62241  ? 284 PRO   A CD   1 
ATOM   2104 N  N    . ILE   A 1 285 ? -28.76443 -9.43100  8.05424   1.000 77.74807  ? 285 ILE   A N    1 
ATOM   2105 C  CA   . ILE   A 1 285 ? -29.13593 -8.42848  7.06506   1.000 76.20615  ? 285 ILE   A CA   1 
ATOM   2106 C  C    . ILE   A 1 285 ? -30.20342 -7.50664  7.64634   1.000 78.88972  ? 285 ILE   A C    1 
ATOM   2107 O  O    . ILE   A 1 285 ? -30.10616 -6.27228  7.58321   1.000 68.79177  ? 285 ILE   A O    1 
ATOM   2108 C  CB   . ILE   A 1 285 ? -29.61702 -9.12317  5.78261   1.000 77.66713  ? 285 ILE   A CB   1 
ATOM   2109 C  CG1  . ILE   A 1 285 ? -28.50533 -10.03201 5.23980   1.000 76.68138  ? 285 ILE   A CG1  1 
ATOM   2110 C  CG2  . ILE   A 1 285 ? -30.08028 -8.11840  4.75770   1.000 71.78663  ? 285 ILE   A CG2  1 
ATOM   2111 C  CD1  . ILE   A 1 285 ? -27.14405 -9.39124  5.21327   1.000 68.89202  ? 285 ILE   A CD1  1 
ATOM   2112 N  N    . TYR   A 1 286 ? -31.24208 -8.09908  8.22405   1.000 81.27801  ? 286 TYR   A N    1 
ATOM   2113 C  CA   . TYR   A 1 286 ? -32.26449 -7.29697  8.86857   1.000 82.39050  ? 286 TYR   A CA   1 
ATOM   2114 C  C    . TYR   A 1 286 ? -31.67876 -6.51076  10.02443  1.000 76.44782  ? 286 TYR   A C    1 
ATOM   2115 O  O    . TYR   A 1 286 ? -32.11658 -5.39060  10.30162  1.000 78.87576  ? 286 TYR   A O    1 
ATOM   2116 C  CB   . TYR   A 1 286 ? -33.42142 -8.18329  9.33036   1.000 90.54380  ? 286 TYR   A CB   1 
ATOM   2117 C  CG   . TYR   A 1 286 ? -34.51509 -7.40689  10.02267  1.000 97.33917  ? 286 TYR   A CG   1 
ATOM   2118 C  CD1  . TYR   A 1 286 ? -34.42870 -7.11805  11.38544  1.000 94.90583  ? 286 TYR   A CD1  1 
ATOM   2119 C  CD2  . TYR   A 1 286 ? -35.62262 -6.94203  9.31826   1.000 96.97602  ? 286 TYR   A CD2  1 
ATOM   2120 C  CE1  . TYR   A 1 286 ? -35.41654 -6.39064  12.02582  1.000 98.65174  ? 286 TYR   A CE1  1 
ATOM   2121 C  CE2  . TYR   A 1 286 ? -36.61655 -6.21814  9.94843   1.000 99.77128  ? 286 TYR   A CE2  1 
ATOM   2122 C  CZ   . TYR   A 1 286 ? -36.50929 -5.94302  11.30093  1.000 98.19945  ? 286 TYR   A CZ   1 
ATOM   2123 O  OH   . TYR   A 1 286 ? -37.49910 -5.22124  11.92854  1.000 99.64939  ? 286 TYR   A OH   1 
ATOM   2124 N  N    . ALA   A 1 287 ? -30.70847 -7.07961  10.73441  1.000 79.35774  ? 287 ALA   A N    1 
ATOM   2125 C  CA   . ALA   A 1 287 ? -30.06336 -6.31986  11.79355  1.000 67.67937  ? 287 ALA   A CA   1 
ATOM   2126 C  C    . ALA   A 1 287 ? -29.43165 -5.03468  11.24726  1.000 65.20898  ? 287 ALA   A C    1 
ATOM   2127 O  O    . ALA   A 1 287 ? -29.51919 -3.96947  11.87896  1.000 63.35310  ? 287 ALA   A O    1 
ATOM   2128 C  CB   . ALA   A 1 287 ? -29.02685 -7.20048  12.48949  1.000 76.16098  ? 287 ALA   A CB   1 
ATOM   2129 N  N    . TYR   A 1 288 ? -28.78435 -5.11512  10.07684  1.000 59.83017  ? 288 TYR   A N    1 
ATOM   2130 C  CA   . TYR   A 1 288 ? -28.23443 -3.91166  9.45046   1.000 62.12628  ? 288 TYR   A CA   1 
ATOM   2131 C  C    . TYR   A 1 288 ? -29.34808 -2.94371  9.03913   1.000 63.57420  ? 288 TYR   A C    1 
ATOM   2132 O  O    . TYR   A 1 288 ? -29.29820 -1.74961  9.35431   1.000 60.98111  ? 288 TYR   A O    1 
ATOM   2133 C  CB   . TYR   A 1 288 ? -27.35604 -4.26978  8.23942   1.000 55.90193  ? 288 TYR   A CB   1 
ATOM   2134 C  CG   . TYR   A 1 288 ? -25.96945 -4.87996  8.56587   1.000 55.38816  ? 288 TYR   A CG   1 
ATOM   2135 C  CD1  . TYR   A 1 288 ? -24.90695 -4.70564  7.69080   1.000 60.90933  ? 288 TYR   A CD1  1 
ATOM   2136 C  CD2  . TYR   A 1 288 ? -25.72297 -5.54332  9.74776   1.000 60.70466  ? 288 TYR   A CD2  1 
ATOM   2137 C  CE1  . TYR   A 1 288 ? -23.64272 -5.20708  7.96245   1.000 61.53715  ? 288 TYR   A CE1  1 
ATOM   2138 C  CE2  . TYR   A 1 288 ? -24.44494 -6.06304  10.02979  1.000 61.63867  ? 288 TYR   A CE2  1 
ATOM   2139 C  CZ   . TYR   A 1 288 ? -23.41819 -5.88087  9.13442   1.000 56.31316  ? 288 TYR   A CZ   1 
ATOM   2140 O  OH   . TYR   A 1 288 ? -22.15466 -6.37444  9.40593   1.000 60.53489  ? 288 TYR   A OH   1 
ATOM   2141 N  N    . ALA   A 1 289 ? -30.39456 -3.45242  8.39077   1.000 64.14213  ? 289 ALA   A N    1 
ATOM   2142 C  CA   . ALA   A 1 289 ? -31.49954 -2.56591  8.00298   1.000 57.64579  ? 289 ALA   A CA   1 
ATOM   2143 C  C    . ALA   A 1 289 ? -32.01793 -1.79642  9.22013   1.000 57.96626  ? 289 ALA   A C    1 
ATOM   2144 O  O    . ALA   A 1 289 ? -32.04252 -0.56287  9.23717   1.000 65.38691  ? 289 ALA   A O    1 
ATOM   2145 C  CB   . ALA   A 1 289 ? -32.61084 -3.38415  7.34268   1.000 64.87848  ? 289 ALA   A CB   1 
ATOM   2146 N  N    . LYS   A 1 290 ? -32.30743 -2.50293  10.29875  1.000 64.02403  ? 290 LYS   A N    1 
ATOM   2147 C  CA   . LYS   A 1 290 ? -32.95105 -1.87480  11.44447  1.000 71.23111  ? 290 LYS   A CA   1 
ATOM   2148 C  C    . LYS   A 1 290 ? -32.01331 -0.95490  12.25611  1.000 70.49224  ? 290 LYS   A C    1 
ATOM   2149 O  O    . LYS   A 1 290 ? -32.49408 0.01819   12.86118  1.000 64.68143  ? 290 LYS   A O    1 
ATOM   2150 C  CB   . LYS   A 1 290 ? -33.54705 -2.95770  12.33935  1.000 70.92434  ? 290 LYS   A CB   1 
ATOM   2151 C  CG   . LYS   A 1 290 ? -33.50806 -2.55946  13.79884  1.000 72.39924  ? 290 LYS   A CG   1 
ATOM   2152 C  CD   . LYS   A 1 290 ? -33.87007 -3.68681  14.75587  1.000 84.60012  ? 290 LYS   A CD   1 
ATOM   2153 C  CE   . LYS   A 1 290 ? -34.74770 -3.18669  15.90494  1.000 88.48717  ? 290 LYS   A CE   1 
ATOM   2154 N  NZ   . LYS   A 1 290 ? -34.99161 -4.27404  16.90000  1.000 82.99005  ? 290 LYS   A NZ   1 
ATOM   2155 N  N    . SER   A 1 291 ? -30.70173 -1.25598  12.36132  1.000 64.73036  ? 291 SER   A N    1 
ATOM   2156 C  CA   . SER   A 1 291 ? -29.88471 -0.49659  13.31140  1.000 68.45702  ? 291 SER   A CA   1 
ATOM   2157 C  C    . SER   A 1 291 ? -29.01321 0.59011   12.68495  1.000 63.56621  ? 291 SER   A C    1 
ATOM   2158 O  O    . SER   A 1 291 ? -28.65875 1.55930   13.37746  1.000 59.56944  ? 291 SER   A O    1 
ATOM   2159 C  CB   . SER   A 1 291 ? -28.98030 -1.44748  14.09002  1.000 61.37201  ? 291 SER   A CB   1 
ATOM   2160 O  OG   . SER   A 1 291 ? -29.78287 -2.43230  14.71148  1.000 66.16936  ? 291 SER   A OG   1 
ATOM   2161 N  N    . ILE   A 1 292 ? -28.67758 0.44833   11.41283  1.000 61.53745  ? 292 ILE   A N    1 
ATOM   2162 C  CA   . ILE   A 1 292 ? -27.87217 1.41152   10.67222  1.000 60.19253  ? 292 ILE   A CA   1 
ATOM   2163 C  C    . ILE   A 1 292 ? -28.72247 2.18545   9.63950   1.000 63.73574  ? 292 ILE   A C    1 
ATOM   2164 O  O    . ILE   A 1 292 ? -28.82088 3.41175   9.68989   1.000 59.13111  ? 292 ILE   A O    1 
ATOM   2165 C  CB   . ILE   A 1 292 ? -26.68129 0.69033   9.99876   1.000 53.32259  ? 292 ILE   A CB   1 
ATOM   2166 C  CG1  . ILE   A 1 292 ? -25.70084 0.18442   11.08152  1.000 58.02635  ? 292 ILE   A CG1  1 
ATOM   2167 C  CG2  . ILE   A 1 292 ? -25.98644 1.58075   8.98902   1.000 58.03016  ? 292 ILE   A CG2  1 
ATOM   2168 C  CD1  . ILE   A 1 292 ? -24.59866 -0.68273  10.53410  1.000 55.84598  ? 292 ILE   A CD1  1 
ATOM   2169 N  N    . ILE   A 1 293 ? -29.40959 1.47350   8.75679   1.000 59.53112  ? 293 ILE   A N    1 
ATOM   2170 C  CA   . ILE   A 1 293 ? -30.04388 2.12484   7.60667   1.000 67.02318  ? 293 ILE   A CA   1 
ATOM   2171 C  C    . ILE   A 1 293 ? -31.30473 2.88813   8.03055   1.000 65.40921  ? 293 ILE   A C    1 
ATOM   2172 O  O    . ILE   A 1 293 ? -31.48865 4.06788   7.69427   1.000 65.66073  ? 293 ILE   A O    1 
ATOM   2173 C  CB   . ILE   A 1 293 ? -30.31784 1.06111   6.54090   1.000 64.76424  ? 293 ILE   A CB   1 
ATOM   2174 C  CG1  . ILE   A 1 293 ? -28.94866 0.46951   6.17562   1.000 58.20922  ? 293 ILE   A CG1  1 
ATOM   2175 C  CG2  . ILE   A 1 293 ? -31.03066 1.67685   5.37379   1.000 62.30514  ? 293 ILE   A CG2  1 
ATOM   2176 C  CD1  . ILE   A 1 293 ? -28.99186 -0.85383  5.46075   1.000 52.67004  ? 293 ILE   A CD1  1 
ATOM   2177 N  N    . PHE   A 1 294 ? -32.18182 2.24436   8.79218   1.000 65.20055  ? 294 PHE   A N    1 
ATOM   2178 C  CA   . PHE   A 1 294 ? -33.41129 2.93268   9.17683   1.000 67.92932  ? 294 PHE   A CA   1 
ATOM   2179 C  C    . PHE   A 1 294 ? -33.14230 4.21273   9.95102   1.000 70.95784  ? 294 PHE   A C    1 
ATOM   2180 O  O    . PHE   A 1 294 ? -33.80158 5.22562   9.66272   1.000 69.26402  ? 294 PHE   A O    1 
ATOM   2181 C  CB   . PHE   A 1 294 ? -34.33924 1.99687   9.95705   1.000 67.48271  ? 294 PHE   A CB   1 
ATOM   2182 C  CG   . PHE   A 1 294 ? -35.68558 2.60809   10.26204  1.000 78.62572  ? 294 PHE   A CG   1 
ATOM   2183 C  CD1  . PHE   A 1 294 ? -36.67182 2.67801   9.27994   1.000 74.60893  ? 294 PHE   A CD1  1 
ATOM   2184 C  CD2  . PHE   A 1 294 ? -35.96603 3.10580   11.52486  1.000 79.05460  ? 294 PHE   A CD2  1 
ATOM   2185 C  CE1  . PHE   A 1 294 ? -37.91030 3.24758   9.55352   1.000 82.45873  ? 294 PHE   A CE1  1 
ATOM   2186 C  CE2  . PHE   A 1 294 ? -37.19691 3.66734   11.81044  1.000 80.13881  ? 294 PHE   A CE2  1 
ATOM   2187 C  CZ   . PHE   A 1 294 ? -38.17410 3.74218   10.82126  1.000 87.46540  ? 294 PHE   A CZ   1 
ATOM   2188 N  N    . PRO   A 1 295 ? -32.25997 4.24378   10.95945  1.000 62.79507  ? 295 PRO   A N    1 
ATOM   2189 C  CA   . PRO   A 1 295 ? -31.98604 5.52857   11.61631  1.000 64.59247  ? 295 PRO   A CA   1 
ATOM   2190 C  C    . PRO   A 1 295 ? -31.26049 6.52381   10.71612  1.000 66.49983  ? 295 PRO   A C    1 
ATOM   2191 O  O    . PRO   A 1 295 ? -31.40507 7.73261   10.93722  1.000 68.08156  ? 295 PRO   A O    1 
ATOM   2192 C  CB   . PRO   A 1 295 ? -31.17586 5.14574   12.86883  1.000 65.31687  ? 295 PRO   A CB   1 
ATOM   2193 C  CG   . PRO   A 1 295 ? -31.23721 3.64661   12.97344  1.000 68.56144  ? 295 PRO   A CG   1 
ATOM   2194 C  CD   . PRO   A 1 295 ? -31.60561 3.10775   11.62207  1.000 62.38791  ? 295 PRO   A CD   1 
ATOM   2195 N  N    . SER   A 1 296 ? -30.49539 6.06061   9.71374   1.000 59.89868  ? 296 SER   A N    1 
ATOM   2196 C  CA   . SER   A 1 296 ? -29.79711 6.96545   8.79835   1.000 60.97569  ? 296 SER   A CA   1 
ATOM   2197 C  C    . SER   A 1 296 ? -30.74241 7.69527   7.85790   1.000 73.31006  ? 296 SER   A C    1 
ATOM   2198 O  O    . SER   A 1 296 ? -30.42741 8.80919   7.41651   1.000 71.66548  ? 296 SER   A O    1 
ATOM   2199 C  CB   . SER   A 1 296 ? -28.77045 6.22245   7.93781   1.000 55.19476  ? 296 SER   A CB   1 
ATOM   2200 O  OG   . SER   A 1 296 ? -27.66936 5.75145   8.67961   1.000 66.71363  ? 296 SER   A OG   1 
ATOM   2201 N  N    . TYR   A 1 297 ? -31.85625 7.06366   7.47994   1.000 72.62074  ? 297 TYR   A N    1 
ATOM   2202 C  CA   . TYR   A 1 297 ? -32.77543 7.65420   6.51264   1.000 68.40040  ? 297 TYR   A CA   1 
ATOM   2203 C  C    . TYR   A 1 297 ? -34.11988 8.05691   7.12069   1.000 75.36446  ? 297 TYR   A C    1 
ATOM   2204 O  O    . TYR   A 1 297 ? -34.99671 8.53233   6.38962   1.000 75.12293  ? 297 TYR   A O    1 
ATOM   2205 C  CB   . TYR   A 1 297 ? -32.96949 6.69182   5.33021   1.000 75.50662  ? 297 TYR   A CB   1 
ATOM   2206 C  CG   . TYR   A 1 297 ? -31.69824 6.45951   4.52226   1.000 69.59840  ? 297 TYR   A CG   1 
ATOM   2207 C  CD1  . TYR   A 1 297 ? -31.30682 7.33981   3.51459   1.000 77.81517  ? 297 TYR   A CD1  1 
ATOM   2208 C  CD2  . TYR   A 1 297 ? -30.89591 5.35096   4.75098   1.000 76.38493  ? 297 TYR   A CD2  1 
ATOM   2209 C  CE1  . TYR   A 1 297 ? -30.13542 7.12581   2.76649   1.000 72.35560  ? 297 TYR   A CE1  1 
ATOM   2210 C  CE2  . TYR   A 1 297 ? -29.72616 5.13093   4.00901   1.000 72.59997  ? 297 TYR   A CE2  1 
ATOM   2211 C  CZ   . TYR   A 1 297 ? -29.35235 6.02012   3.02213   1.000 71.83843  ? 297 TYR   A CZ   1 
ATOM   2212 O  OH   . TYR   A 1 297 ? -28.18367 5.79822   2.30992   1.000 70.10168  ? 297 TYR   A OH   1 
ATOM   2213 N  N    . ASN   A 1 298 ? -34.30120 7.89607   8.43766   1.000 74.84727  ? 298 ASN   A N    1 
ATOM   2214 C  CA   . ASN   A 1 298 ? -35.58459 8.09493   9.13233   1.000 77.12331  ? 298 ASN   A CA   1 
ATOM   2215 C  C    . ASN   A 1 298 ? -36.70056 7.27612   8.51153   1.000 78.93610  ? 298 ASN   A C    1 
ATOM   2216 O  O    . ASN   A 1 298 ? -37.87793 7.51125   8.78630   1.000 79.47582  ? 298 ASN   A O    1 
ATOM   2217 C  CB   . ASN   A 1 298 ? -36.00236 9.56835   9.15447   1.000 74.45900  ? 298 ASN   A CB   1 
ATOM   2218 C  CG   . ASN   A 1 298 ? -35.12517 10.41748  10.06294  1.000 90.53296  ? 298 ASN   A CG   1 
ATOM   2219 O  OD1  . ASN   A 1 298 ? -34.01953 10.01725  10.45303  1.000 82.76743  ? 298 ASN   A OD1  1 
ATOM   2220 N  ND2  . ASN   A 1 298 ? -35.62036 11.60712  10.40581  1.000 101.21716 ? 298 ASN   A ND2  1 
ATOM   2221 N  N    . GLU   A 1 299 ? -36.32000 6.27940   7.72632   1.000 84.91724  ? 299 GLU   A N    1 
ATOM   2222 C  CA   . GLU   A 1 299 ? -37.21421 5.41526   6.97179   1.000 82.98740  ? 299 GLU   A CA   1 
ATOM   2223 C  C    . GLU   A 1 299 ? -36.36744 4.24468   6.51373   1.000 79.28985  ? 299 GLU   A C    1 
ATOM   2224 O  O    . GLU   A 1 299 ? -35.14135 4.26988   6.63499   1.000 85.21456  ? 299 GLU   A O    1 
ATOM   2225 C  CB   . GLU   A 1 299 ? -37.79052 6.14026   5.75163   1.000 88.33806  ? 299 GLU   A CB   1 
ATOM   2226 C  CG   . GLU   A 1 299 ? -36.66906 6.52821   4.75322   1.000 90.57422  ? 299 GLU   A CG   1 
ATOM   2227 C  CD   . GLU   A 1 299 ? -37.16732 7.09550   3.41678   1.000 97.44921  ? 299 GLU   A CD   1 
ATOM   2228 O  OE1  . GLU   A 1 299 ? -38.25678 7.71795   3.37672   1.000 92.04722  ? 299 GLU   A OE1  1 
ATOM   2229 O  OE2  . GLU   A 1 299 ? -36.43321 6.93530   2.41079   1.000 95.10083  ? 299 GLU   A OE2  1 
ATOM   2230 N  N    . PHE   A 1 300 ? -37.01584 3.24272   5.93632   1.000 71.75744  ? 300 PHE   A N    1 
ATOM   2231 C  CA   . PHE   A 1 300 ? -36.29398 2.28959   5.09481   1.000 79.13086  ? 300 PHE   A CA   1 
ATOM   2232 C  C    . PHE   A 1 300 ? -37.07281 2.23060   3.78843   1.000 81.91852  ? 300 PHE   A C    1 
ATOM   2233 O  O    . PHE   A 1 300 ? -38.23453 1.81789   3.78834   1.000 64.95620  ? 300 PHE   A O    1 
ATOM   2234 C  CB   . PHE   A 1 300 ? -36.17264 0.88876   5.72542   1.000 77.17298  ? 300 PHE   A CB   1 
ATOM   2235 C  CG   . PHE   A 1 300 ? -35.16437 -0.01694  5.01556   1.000 77.20717  ? 300 PHE   A CG   1 
ATOM   2236 C  CD1  . PHE   A 1 300 ? -35.43772 -0.55429  3.75888   1.000 70.81622  ? 300 PHE   A CD1  1 
ATOM   2237 C  CD2  . PHE   A 1 300 ? -33.93456 -0.32464  5.61692   1.000 68.33825  ? 300 PHE   A CD2  1 
ATOM   2238 C  CE1  . PHE   A 1 300 ? -34.51665 -1.36288  3.09842   1.000 70.21855  ? 300 PHE   A CE1  1 
ATOM   2239 C  CE2  . PHE   A 1 300 ? -33.00617 -1.14791  4.96567   1.000 62.78852  ? 300 PHE   A CE2  1 
ATOM   2240 C  CZ   . PHE   A 1 300 ? -33.29393 -1.66039  3.70413   1.000 65.86530  ? 300 PHE   A CZ   1 
ATOM   2241 N  N    . ASN   A 1 301 ? -36.46764 2.70182   2.69514   1.000 81.48713  ? 301 ASN   A N    1 
ATOM   2242 C  CA   . ASN   A 1 301 ? -37.09629 2.61104   1.37823   1.000 81.74888  ? 301 ASN   A CA   1 
ATOM   2243 C  C    . ASN   A 1 301 ? -36.59858 1.32809   0.73385   1.000 74.12165  ? 301 ASN   A C    1 
ATOM   2244 O  O    . ASN   A 1 301 ? -35.44356 1.25096   0.29986   1.000 73.18168  ? 301 ASN   A O    1 
ATOM   2245 C  CB   . ASN   A 1 301 ? -36.79328 3.82787   0.50308   1.000 89.46162  ? 301 ASN   A CB   1 
ATOM   2246 C  CG   . ASN   A 1 301 ? -37.58601 3.82849   -0.82382  1.000 91.58802  ? 301 ASN   A CG   1 
ATOM   2247 O  OD1  . ASN   A 1 301 ? -38.79311 3.50762   -0.88191  1.000 89.57868  ? 301 ASN   A OD1  1 
ATOM   2248 N  ND2  . ASN   A 1 301 ? -36.88471 4.17122   -1.90524  1.000 97.89973  ? 301 ASN   A ND2  1 
ATOM   2249 N  N    . LEU   A 1 302 ? -37.49364 0.34260   0.65094   1.000 80.32339  ? 302 LEU   A N    1 
ATOM   2250 C  CA   . LEU   A 1 302 ? -37.23730 -0.98241  0.09754   1.000 79.70949  ? 302 LEU   A CA   1 
ATOM   2251 C  C    . LEU   A 1 302 ? -37.45721 -0.93854  -1.40677  1.000 80.12800  ? 302 LEU   A C    1 
ATOM   2252 O  O    . LEU   A 1 302 ? -38.58584 -0.73170  -1.87414  1.000 80.26537  ? 302 LEU   A O    1 
ATOM   2253 C  CB   . LEU   A 1 302 ? -38.15145 -2.01184  0.76810   1.000 75.25298  ? 302 LEU   A CB   1 
ATOM   2254 C  CG   . LEU   A 1 302 ? -37.94506 -3.49384  0.43663   1.000 78.95227  ? 302 LEU   A CG   1 
ATOM   2255 C  CD1  . LEU   A 1 302 ? -36.58871 -3.94007  0.91920   1.000 72.19071  ? 302 LEU   A CD1  1 
ATOM   2256 C  CD2  . LEU   A 1 302 ? -39.00435 -4.36333  1.11258   1.000 77.35407  ? 302 LEU   A CD2  1 
ATOM   2257 N  N    . VAL   A 1 303 ? -36.38497 -1.04133  -2.17405  1.000 72.19583  ? 303 VAL   A N    1 
ATOM   2258 C  CA   . VAL   A 1 303 ? -36.53361 -1.11633  -3.62587  1.000 77.75366  ? 303 VAL   A CA   1 
ATOM   2259 C  C    . VAL   A 1 303 ? -36.77757 -2.57734  -3.99249  1.000 81.38719  ? 303 VAL   A C    1 
ATOM   2260 O  O    . VAL   A 1 303 ? -36.10002 -3.47094  -3.45710  1.000 72.00451  ? 303 VAL   A O    1 
ATOM   2261 C  CB   . VAL   A 1 303 ? -35.29663 -0.55261  -4.34733  1.000 81.28399  ? 303 VAL   A CB   1 
ATOM   2262 C  CG1  . VAL   A 1 303 ? -35.41507 -0.78082  -5.86087  1.000 82.42337  ? 303 VAL   A CG1  1 
ATOM   2263 C  CG2  . VAL   A 1 303 ? -35.10276 0.93510   -4.01305  1.000 80.82662  ? 303 VAL   A CG2  1 
ATOM   2264 N  N    . ARG   A 1 304 ? -37.80059 -2.81943  -4.83518  1.000 79.72680  ? 304 ARG   A N    1 
ATOM   2265 C  CA   . ARG   A 1 304 ? -38.19938 -4.12413  -5.36902  1.000 83.07629  ? 304 ARG   A CA   1 
ATOM   2266 C  C    . ARG   A 1 304 ? -38.82911 -3.90203  -6.73701  1.000 73.01261  ? 304 ARG   A C    1 
ATOM   2267 O  O    . ARG   A 1 304 ? -39.46383 -2.86342  -6.99115  1.000 64.90431  ? 304 ARG   A O    1 
ATOM   2268 C  CB   . ARG   A 1 304 ? -39.23718 -4.88512  -4.51295  1.000 79.24792  ? 304 ARG   A CB   1 
ATOM   2269 C  CG   . ARG   A 1 304 ? -38.78790 -5.23912  -3.10230  1.000 92.08137  ? 304 ARG   A CG   1 
ATOM   2270 C  CD   . ARG   A 1 304 ? -39.82989 -6.08469  -2.32444  1.000 98.66000  ? 304 ARG   A CD   1 
ATOM   2271 N  NE   . ARG   A 1 304 ? -41.06875 -5.36902  -2.02121  1.000 97.96159  ? 304 ARG   A NE   1 
ATOM   2272 C  CZ   . ARG   A 1 304 ? -41.92808 -5.71945  -1.06991  1.000 95.49917  ? 304 ARG   A CZ   1 
ATOM   2273 N  NH1  . ARG   A 1 304 ? -41.71643 -6.77679  -0.29844  1.000 99.66806  ? 304 ARG   A NH1  1 
ATOM   2274 N  NH2  . ARG   A 1 304 ? -43.02367 -4.98543  -0.88315  1.000 88.92402  ? 304 ARG   A NH2  1 
ATOM   2275 N  N    . LYS   A 1 305 ? -38.69539 -4.91398  -7.59642  1.000 89.16981  ? 305 LYS   A N    1 
ATOM   2276 C  CA   . LYS   A 1 305 ? -39.42117 -4.91828  -8.86536  1.000 85.64761  ? 305 LYS   A CA   1 
ATOM   2277 C  C    . LYS   A 1 305 ? -40.92075 -4.96363  -8.60597  1.000 82.71574  ? 305 LYS   A C    1 
ATOM   2278 O  O    . LYS   A 1 305 ? -41.38647 -5.54776  -7.62908  1.000 86.39548  ? 305 LYS   A O    1 
ATOM   2279 C  CB   . LYS   A 1 305 ? -39.02588 -6.12500  -9.73290  1.000 93.32025  ? 305 LYS   A CB   1 
ATOM   2280 C  CG   . LYS   A 1 305 ? -37.53740 -6.25997  -10.06729 1.000 83.93028  ? 305 LYS   A CG   1 
ATOM   2281 C  CD   . LYS   A 1 305 ? -37.14197 -5.34333  -11.23213 1.000 79.31194  ? 305 LYS   A CD   1 
ATOM   2282 C  CE   . LYS   A 1 305 ? -36.05054 -4.36886  -10.75093 1.000 87.13644  ? 305 LYS   A CE   1 
ATOM   2283 N  NZ   . LYS   A 1 305 ? -36.49850 -3.47294  -9.62968  1.000 61.00764  ? 305 LYS   A NZ   1 
ATOM   2284 N  N    . GLU   A 1 306 ? -41.68437 -4.37187  -9.51092  1.000 78.94758  ? 306 GLU   A N    1 
ATOM   2285 C  CA   . GLU   A 1 306 ? -43.14061 -4.37942  -9.35721  1.000 94.29949  ? 306 GLU   A CA   1 
ATOM   2286 C  C    . GLU   A 1 306 ? -43.69223 -5.80529  -9.21133  1.000 89.65586  ? 306 GLU   A C    1 
ATOM   2287 O  O    . GLU   A 1 306 ? -44.75768 -5.99951  -8.61111  1.000 94.70415  ? 306 GLU   A O    1 
ATOM   2288 C  CB   . GLU   A 1 306 ? -43.79583 -3.61528  -10.51882 1.000 84.61031  ? 306 GLU   A CB   1 
ATOM   2289 C  CG   . GLU   A 1 306 ? -43.61773 -2.10423  -10.30061 1.000 96.23530  ? 306 GLU   A CG   1 
ATOM   2290 C  CD   . GLU   A 1 306 ? -44.59122 -1.23922  -11.06627 1.000 113.51414 ? 306 GLU   A CD   1 
ATOM   2291 O  OE1  . GLU   A 1 306 ? -44.85370 -1.52206  -12.25681 1.000 124.90472 ? 306 GLU   A OE1  1 
ATOM   2292 O  OE2  . GLU   A 1 306 ? -45.08877 -0.25727  -10.46980 1.000 113.41718 ? 306 GLU   A OE2  1 
ATOM   2293 N  N    . LYS   A 1 307 ? -43.00323 -6.80456  -9.78236  1.000 90.22761  ? 307 LYS   A N    1 
ATOM   2294 C  CA   . LYS   A 1 307 ? -43.40713 -8.21457  -9.69751  1.000 87.86128  ? 307 LYS   A CA   1 
ATOM   2295 C  C    . LYS   A 1 307 ? -43.20826 -8.82270  -8.30685  1.000 90.63165  ? 307 LYS   A C    1 
ATOM   2296 O  O    . LYS   A 1 307 ? -43.83107 -9.85085  -8.00293  1.000 87.10847  ? 307 LYS   A O    1 
ATOM   2297 C  CB   . LYS   A 1 307 ? -42.63804 -9.00271  -10.77152 1.000 85.48964  ? 307 LYS   A CB   1 
ATOM   2298 C  CG   . LYS   A 1 307 ? -41.09111 -8.84452  -10.70871 1.000 91.50867  ? 307 LYS   A CG   1 
ATOM   2299 C  CD   . LYS   A 1 307 ? -40.40410 -9.60228  -11.84754 1.000 80.48881  ? 307 LYS   A CD   1 
ATOM   2300 C  CE   . LYS   A 1 307 ? -39.18758 -8.79268  -12.31702 1.000 85.96928  ? 307 LYS   A CE   1 
ATOM   2301 N  NZ   . LYS   A 1 307 ? -39.66839 -7.61109  -13.19142 1.000 66.02284  ? 307 LYS   A NZ   1 
ATOM   2302 N  N    . ASN   A 1 308 ? -42.35036 -8.22159  -7.47480  1.000 87.43443  ? 308 ASN   A N    1 
ATOM   2303 C  CA   . ASN   A 1 308 ? -42.16641 -8.57469  -6.06880  1.000 90.83140  ? 308 ASN   A CA   1 
ATOM   2304 C  C    . ASN   A 1 308 ? -42.87115 -7.61636  -5.10096  1.000 89.13078  ? 308 ASN   A C    1 
ATOM   2305 O  O    . ASN   A 1 308 ? -42.58364 -7.64378  -3.90319  1.000 87.86543  ? 308 ASN   A O    1 
ATOM   2306 C  CB   . ASN   A 1 308 ? -40.67223 -8.62889  -5.71709  1.000 80.08318  ? 308 ASN   A CB   1 
ATOM   2307 C  CG   . ASN   A 1 308 ? -39.95574 -9.81394  -6.33629  1.000 81.78820  ? 308 ASN   A CG   1 
ATOM   2308 O  OD1  . ASN   A 1 308 ? -40.54690 -10.86831 -6.57227  1.000 89.40632  ? 308 ASN   A OD1  1 
ATOM   2309 N  ND2  . ASN   A 1 308 ? -38.67222 -9.64782  -6.59246  1.000 82.54983  ? 308 ASN   A ND2  1 
ATOM   2310 N  N    . GLY   A 1 309 ? -43.75543 -6.74973  -5.58195  1.000 90.35941  ? 309 GLY   A N    1 
ATOM   2311 C  CA   . GLY   A 1 309 ? -44.44898 -5.78774  -4.73975  1.000 84.39400  ? 309 GLY   A CA   1 
ATOM   2312 C  C    . GLY   A 1 309 ? -44.14385 -4.33038  -5.03339  1.000 85.82657  ? 309 GLY   A C    1 
ATOM   2313 O  O    . GLY   A 1 309 ? -44.92327 -3.45878  -4.62318  1.000 84.35585  ? 309 GLY   A O    1 
ATOM   2314 N  N    . GLY   A 1 310 ? -43.08112 -4.03017  -5.78384  1.000 84.07394  ? 310 GLY   A N    1 
ATOM   2315 C  CA   . GLY   A 1 310 ? -42.65582 -2.65542  -5.99581  1.000 81.30157  ? 310 GLY   A CA   1 
ATOM   2316 C  C    . GLY   A 1 310 ? -41.98800 -2.03027  -4.76705  1.000 84.44183  ? 310 GLY   A C    1 
ATOM   2317 O  O    . GLY   A 1 310 ? -42.06007 -2.56660  -3.64826  1.000 82.52570  ? 310 GLY   A O    1 
ATOM   2318 N  N    . ASP   A 1 311 ? -41.31189 -0.90009  -4.97373  1.000 82.14829  ? 311 ASP   A N    1 
ATOM   2319 C  CA   . ASP   A 1 311 ? -40.65403 -0.18635  -3.88148  1.000 68.91522  ? 311 ASP   A CA   1 
ATOM   2320 C  C    . ASP   A 1 311 ? -41.66571 0.13488   -2.77333  1.000 76.61219  ? 311 ASP   A C    1 
ATOM   2321 O  O    . ASP   A 1 311 ? -42.86324 0.28419   -3.01674  1.000 79.94180  ? 311 ASP   A O    1 
ATOM   2322 C  CB   . ASP   A 1 311 ? -40.02750 1.09506   -4.41854  1.000 69.44453  ? 311 ASP   A CB   1 
ATOM   2323 C  CG   . ASP   A 1 311 ? -39.18149 0.86339   -5.66995  1.000 80.04297  ? 311 ASP   A CG   1 
ATOM   2324 O  OD1  . ASP   A 1 311 ? -38.58631 1.84845   -6.16395  1.000 86.06937  ? 311 ASP   A OD1  1 
ATOM   2325 O  OD2  . ASP   A 1 311 ? -39.14571 -0.27472  -6.19644  1.000 84.55728  ? 311 ASP   A OD2  1 
ATOM   2326 N  N    . LYS   A 1 312 ? -41.20003 0.20805   -1.53045  1.000 84.16992  ? 312 LYS   A N    1 
ATOM   2327 C  CA   . LYS   A 1 312 ? -42.10540 0.55088   -0.43836  1.000 80.84508  ? 312 LYS   A CA   1 
ATOM   2328 C  C    . LYS   A 1 312 ? -41.32640 1.15561   0.72127   1.000 84.88160  ? 312 LYS   A C    1 
ATOM   2329 O  O    . LYS   A 1 312 ? -40.23707 0.67844   1.05742   1.000 85.90943  ? 312 LYS   A O    1 
ATOM   2330 C  CB   . LYS   A 1 312 ? -42.89611 -0.67077  0.04007   1.000 73.37435  ? 312 LYS   A CB   1 
ATOM   2331 C  CG   . LYS   A 1 312 ? -43.74745 -0.37756  1.26127   1.000 80.62457  ? 312 LYS   A CG   1 
ATOM   2332 C  CD   . LYS   A 1 312 ? -44.54338 -1.58488  1.69425   1.000 82.94879  ? 312 LYS   A CD   1 
ATOM   2333 C  CE   . LYS   A 1 312 ? -45.25849 -1.31488  3.00564   1.000 85.91810  ? 312 LYS   A CE   1 
ATOM   2334 N  NZ   . LYS   A 1 312 ? -46.02618 -2.51216  3.46397   1.000 90.32906  ? 312 LYS   A NZ   1 
ATOM   2335 N  N    . THR   A 1 313 ? -41.88473 2.18514   1.35357   1.000 78.30980  ? 313 THR   A N    1 
ATOM   2336 C  CA   . THR   A 1 313 ? -41.19219 2.78819   2.49243   1.000 85.44199  ? 313 THR   A CA   1 
ATOM   2337 C  C    . THR   A 1 313 ? -41.80736 2.34352   3.81628   1.000 80.93699  ? 313 THR   A C    1 
ATOM   2338 O  O    . THR   A 1 313 ? -43.03577 2.41387   4.00803   1.000 72.37882  ? 313 THR   A O    1 
ATOM   2339 C  CB   . THR   A 1 313 ? -41.20211 4.30958   2.43661   1.000 87.26933  ? 313 THR   A CB   1 
ATOM   2340 O  OG1  . THR   A 1 313 ? -40.60406 4.73946   1.20605   1.000 91.20519  ? 313 THR   A OG1  1 
ATOM   2341 C  CG2  . THR   A 1 313 ? -40.37089 4.83021   3.61426   1.000 81.67785  ? 313 THR   A CG2  1 
ATOM   2342 N  N    . TYR   A 1 314 ? -40.95095 1.85384   4.70847   1.000 75.75777  ? 314 TYR   A N    1 
ATOM   2343 C  CA   . TYR   A 1 314 ? -41.32697 1.56254   6.08730   1.000 84.87088  ? 314 TYR   A CA   1 
ATOM   2344 C  C    . TYR   A 1 314 ? -40.96555 2.79007   6.91030   1.000 80.02903  ? 314 TYR   A C    1 
ATOM   2345 O  O    . TYR   A 1 314 ? -39.85975 3.31757   6.78267   1.000 79.31395  ? 314 TYR   A O    1 
ATOM   2346 C  CB   . TYR   A 1 314 ? -40.64505 0.28557   6.59493   1.000 70.98067  ? 314 TYR   A CB   1 
ATOM   2347 C  CG   . TYR   A 1 314 ? -41.18321 -0.91351  5.82207   1.000 72.54705  ? 314 TYR   A CG   1 
ATOM   2348 C  CD1  . TYR   A 1 314 ? -40.71661 -1.20241  4.53672   1.000 76.69061  ? 314 TYR   A CD1  1 
ATOM   2349 C  CD2  . TYR   A 1 314 ? -42.22209 -1.69150  6.32909   1.000 86.04975  ? 314 TYR   A CD2  1 
ATOM   2350 C  CE1  . TYR   A 1 314 ? -41.23976 -2.25360  3.79903   1.000 84.96824  ? 314 TYR   A CE1  1 
ATOM   2351 C  CE2  . TYR   A 1 314 ? -42.75802 -2.74362  5.59607   1.000 83.28030  ? 314 TYR   A CE2  1 
ATOM   2352 C  CZ   . TYR   A 1 314 ? -42.25717 -3.02092  4.33666   1.000 82.13458  ? 314 TYR   A CZ   1 
ATOM   2353 O  OH   . TYR   A 1 314 ? -42.75618 -4.06847  3.60793   1.000 87.90214  ? 314 TYR   A OH   1 
ATOM   2354 N  N    . TYR   A 1 315 ? -41.94358 3.31312   7.64547   1.000 81.68653  ? 315 TYR   A N    1 
ATOM   2355 C  CA   . TYR   A 1 315 ? -41.75659 4.50657   8.45311   1.000 83.42433  ? 315 TYR   A CA   1 
ATOM   2356 C  C    . TYR   A 1 315 ? -41.62212 4.20609   9.94325   1.000 89.76518  ? 315 TYR   A C    1 
ATOM   2357 O  O    . TYR   A 1 315 ? -41.24775 5.10315   10.70982  1.000 86.03532  ? 315 TYR   A O    1 
ATOM   2358 C  CB   . TYR   A 1 315 ? -42.91789 5.49012   8.19377   1.000 81.58840  ? 315 TYR   A CB   1 
ATOM   2359 C  CG   . TYR   A 1 315 ? -42.94386 5.99158   6.75305   1.000 83.68740  ? 315 TYR   A CG   1 
ATOM   2360 C  CD1  . TYR   A 1 315 ? -41.89855 6.75848   6.25218   1.000 89.99301  ? 315 TYR   A CD1  1 
ATOM   2361 C  CD2  . TYR   A 1 315 ? -43.98274 5.65149   5.88080   1.000 85.32862  ? 315 TYR   A CD2  1 
ATOM   2362 C  CE1  . TYR   A 1 315 ? -41.90035 7.20611   4.93352   1.000 86.70253  ? 315 TYR   A CE1  1 
ATOM   2363 C  CE2  . TYR   A 1 315 ? -43.99032 6.09592   4.55166   1.000 82.65931  ? 315 TYR   A CE2  1 
ATOM   2364 C  CZ   . TYR   A 1 315 ? -42.94049 6.87120   4.09036   1.000 86.20319  ? 315 TYR   A CZ   1 
ATOM   2365 O  OH   . TYR   A 1 315 ? -42.90526 7.32061   2.79048   1.000 81.12179  ? 315 TYR   A OH   1 
ATOM   2366 N  N    . THR   A 1 316 ? -41.88399 2.96547   10.36002  1.000 94.60141  ? 316 THR   A N    1 
ATOM   2367 C  CA   . THR   A 1 316 ? -41.66012 2.50857   11.72769  1.000 92.91619  ? 316 THR   A CA   1 
ATOM   2368 C  C    . THR   A 1 316 ? -41.01429 1.13612   11.66439  1.000 90.69935  ? 316 THR   A C    1 
ATOM   2369 O  O    . THR   A 1 316 ? -41.22822 0.37467   10.71467  1.000 91.09346  ? 316 THR   A O    1 
ATOM   2370 C  CB   . THR   A 1 316 ? -42.94783 2.41999   12.57553  1.000 97.61496  ? 316 THR   A CB   1 
ATOM   2371 O  OG1  . THR   A 1 316 ? -43.82636 1.42265   12.03463  1.000 99.91253  ? 316 THR   A OG1  1 
ATOM   2372 C  CG2  . THR   A 1 316 ? -43.66860 3.76491   12.61145  1.000 99.48477  ? 316 THR   A CG2  1 
ATOM   2373 N  N    . LEU   A 1 317 ? -40.20757 0.82982   12.68006  1.000 91.27173  ? 317 LEU   A N    1 
ATOM   2374 C  CA   . LEU   A 1 317 ? -39.64802 -0.51243  12.77012  1.000 93.13191  ? 317 LEU   A CA   1 
ATOM   2375 C  C    . LEU   A 1 317 ? -40.75089 -1.55543  12.97285  1.000 94.85094  ? 317 LEU   A C    1 
ATOM   2376 O  O    . LEU   A 1 317 ? -40.62144 -2.69339  12.50612  1.000 92.68346  ? 317 LEU   A O    1 
ATOM   2377 C  CB   . LEU   A 1 317 ? -38.59809 -0.55418  13.89059  1.000 87.20765  ? 317 LEU   A CB   1 
ATOM   2378 C  CG   . LEU   A 1 317 ? -37.35477 0.30750   13.57782  1.000 81.81777  ? 317 LEU   A CG   1 
ATOM   2379 C  CD1  . LEU   A 1 317 ? -36.33553 0.24813   14.67739  1.000 82.01974  ? 317 LEU   A CD1  1 
ATOM   2380 C  CD2  . LEU   A 1 317 ? -36.72905 -0.04191  12.23026  1.000 80.49842  ? 317 LEU   A CD2  1 
ATOM   2381 N  N    . GLN   A 1 318 ? -41.85773 -1.18220  13.62789  1.000 97.09072  ? 318 GLN   A N    1 
ATOM   2382 C  CA   . GLN   A 1 318 ? -42.98165 -2.10824  13.76183  1.000 97.51365  ? 318 GLN   A CA   1 
ATOM   2383 C  C    . GLN   A 1 318 ? -43.51780 -2.49444  12.37787  1.000 100.33353 ? 318 GLN   A C    1 
ATOM   2384 O  O    . GLN   A 1 318 ? -43.78618 -3.67237  12.11151  1.000 98.31684  ? 318 GLN   A O    1 
ATOM   2385 C  CB   . GLN   A 1 318 ? -44.07140 -1.47964  14.64835  1.000 103.89453 ? 318 GLN   A CB   1 
ATOM   2386 C  CG   . GLN   A 1 318 ? -45.17684 -2.42210  15.21082  1.000 104.04520 ? 318 GLN   A CG   1 
ATOM   2387 C  CD   . GLN   A 1 318 ? -46.38262 -2.66516  14.28256  1.000 108.33252 ? 318 GLN   A CD   1 
ATOM   2388 O  OE1  . GLN   A 1 318 ? -46.71733 -1.84025  13.42348  1.000 105.88259 ? 318 GLN   A OE1  1 
ATOM   2389 N  NE2  . GLN   A 1 318 ? -47.06044 -3.79560  14.49077  1.000 104.14189 ? 318 GLN   A NE2  1 
ATOM   2390 N  N    . GLU   A 1 319 ? -43.63125 -1.51525  11.47139  1.000 96.53257  ? 319 GLU   A N    1 
ATOM   2391 C  CA   . GLU   A 1 319 ? -44.08341 -1.76741  10.09875  1.000 96.57958  ? 319 GLU   A CA   1 
ATOM   2392 C  C    . GLU   A 1 319 ? -43.13238 -2.68429  9.32945   1.000 93.82024  ? 319 GLU   A C    1 
ATOM   2393 O  O    . GLU   A 1 319 ? -43.56760 -3.64621  8.67117   1.000 87.18435  ? 319 GLU   A O    1 
ATOM   2394 C  CB   . GLU   A 1 319 ? -44.20400 -0.43149  9.37089   1.000 94.31015  ? 319 GLU   A CB   1 
ATOM   2395 C  CG   . GLU   A 1 319 ? -44.70938 -0.49759  7.95232   1.000 101.12177 ? 319 GLU   A CG   1 
ATOM   2396 C  CD   . GLU   A 1 319 ? -44.82030 0.89172   7.34248   1.000 100.46750 ? 319 GLU   A CD   1 
ATOM   2397 O  OE1  . GLU   A 1 319 ? -44.32460 1.85004   7.99414   1.000 96.82690  ? 319 GLU   A OE1  1 
ATOM   2398 O  OE2  . GLU   A 1 319 ? -45.36756 1.01251   6.21420   1.000 96.87288  ? 319 GLU   A OE2  1 
ATOM   2399 N  N    . LEU   A 1 320 ? -41.82504 -2.38662  9.38435   1.000 93.06492  ? 320 LEU   A N    1 
ATOM   2400 C  CA   . LEU   A 1 320 ? -40.83922 -3.21146  8.68965   1.000 89.81781  ? 320 LEU   A CA   1 
ATOM   2401 C  C    . LEU   A 1 320 ? -40.84313 -4.64652  9.20727   1.000 94.80307  ? 320 LEU   A C    1 
ATOM   2402 O  O    . LEU   A 1 320 ? -40.79844 -5.60959  8.42186   1.000 90.43106  ? 320 LEU   A O    1 
ATOM   2403 C  CB   . LEU   A 1 320 ? -39.45389 -2.60934  8.86097   1.000 86.48388  ? 320 LEU   A CB   1 
ATOM   2404 C  CG   . LEU   A 1 320 ? -38.40241 -3.39815  8.08211   1.000 84.16159  ? 320 LEU   A CG   1 
ATOM   2405 C  CD1  . LEU   A 1 320 ? -38.48882 -3.07162  6.57708   1.000 74.09014  ? 320 LEU   A CD1  1 
ATOM   2406 C  CD2  . LEU   A 1 320 ? -36.98988 -3.23867  8.69425   1.000 80.41611  ? 320 LEU   A CD2  1 
ATOM   2407 N  N    . GLU   A 1 321 ? -40.88488 -4.79690  10.53543  1.000 94.09769  ? 321 GLU   A N    1 
ATOM   2408 C  CA   . GLU   A 1 321 ? -40.88439 -6.11077  11.16428  1.000 99.84451  ? 321 GLU   A CA   1 
ATOM   2409 C  C    . GLU   A 1 321 ? -42.13715 -6.88728  10.79512  1.000 104.31731 ? 321 GLU   A C    1 
ATOM   2410 O  O    . GLU   A 1 321 ? -42.06337 -8.07439  10.45568  1.000 111.62784 ? 321 GLU   A O    1 
ATOM   2411 C  CB   . GLU   A 1 321 ? -40.77458 -5.95753  12.68191  1.000 98.38833  ? 321 GLU   A CB   1 
ATOM   2412 C  CG   . GLU   A 1 321 ? -41.09197 -7.22755  13.46071  1.000 108.04522 ? 321 GLU   A CG   1 
ATOM   2413 C  CD   . GLU   A 1 321 ? -40.95935 -7.04734  14.97143  1.000 118.25493 ? 321 GLU   A CD   1 
ATOM   2414 O  OE1  . GLU   A 1 321 ? -40.06550 -6.29299  15.41799  1.000 113.55406 ? 321 GLU   A OE1  1 
ATOM   2415 O  OE2  . GLU   A 1 321 ? -41.76407 -7.65338  15.71429  1.000 125.43740 ? 321 GLU   A OE2  1 
ATOM   2416 N  N    . HIS   A 1 322 ? -43.30304 -6.23076  10.85627  1.000 106.09880 ? 322 HIS   A N    1 
ATOM   2417 C  CA   . HIS   A 1 322 ? -44.55044 -6.86319  10.43751  1.000 107.43350 ? 322 HIS   A CA   1 
ATOM   2418 C  C    . HIS   A 1 322 ? -44.44968 -7.39866  9.01024   1.000 108.39520 ? 322 HIS   A C    1 
ATOM   2419 O  O    . HIS   A 1 322 ? -44.83076 -8.54346  8.74406   1.000 112.27145 ? 322 HIS   A O    1 
ATOM   2420 C  CB   . HIS   A 1 322 ? -45.71504 -5.87183  10.58318  1.000 109.21328 ? 322 HIS   A CB   1 
ATOM   2421 C  CG   . HIS   A 1 322 ? -46.99053 -6.31923  9.93057   1.000 119.34130 ? 322 HIS   A CG   1 
ATOM   2422 N  ND1  . HIS   A 1 322 ? -47.27580 -6.08218  8.60078   1.000 118.60544 ? 322 HIS   A ND1  1 
ATOM   2423 C  CD2  . HIS   A 1 322 ? -48.06166 -6.98141  10.43021  1.000 122.56116 ? 322 HIS   A CD2  1 
ATOM   2424 C  CE1  . HIS   A 1 322 ? -48.46272 -6.58315  8.30809   1.000 119.44646 ? 322 HIS   A CE1  1 
ATOM   2425 N  NE2  . HIS   A 1 322 ? -48.96097 -7.13436  9.40078   1.000 125.11755 ? 322 HIS   A NE2  1 
ATOM   2426 N  N    . ASP   A 1 323 ? -43.94412 -6.59210  8.06634   1.000 103.98690 ? 323 ASP   A N    1 
ATOM   2427 C  CA   . ASP   A 1 323 ? -43.93253 -7.08642  6.68661   1.000 104.75781 ? 323 ASP   A CA   1 
ATOM   2428 C  C    . ASP   A 1 323 ? -42.92735 -8.20789  6.47211   1.000 108.29018 ? 323 ASP   A C    1 
ATOM   2429 O  O    . ASP   A 1 323 ? -43.20824 -9.15090  5.72144   1.000 112.38900 ? 323 ASP   A O    1 
ATOM   2430 C  CB   . ASP   A 1 323 ? -43.66925 -5.97093  5.68665   1.000 97.38751  ? 323 ASP   A CB   1 
ATOM   2431 C  CG   . ASP   A 1 323 ? -44.91886 -5.30458  5.25263   1.000 98.59518  ? 323 ASP   A CG   1 
ATOM   2432 O  OD1  . ASP   A 1 323 ? -45.96725 -5.58736  5.86619   1.000 104.14069 ? 323 ASP   A OD1  1 
ATOM   2433 O  OD2  . ASP   A 1 323 ? -44.86008 -4.52463  4.28358   1.000 99.09248  ? 323 ASP   A OD2  1 
ATOM   2434 N  N    . TYR   A 1 324 ? -41.74676 -8.13514  7.08829   1.000 102.56752 ? 324 TYR   A N    1 
ATOM   2435 C  CA   . TYR   A 1 324 ? -40.81053 -9.21761  6.78932   1.000 108.73093 ? 324 TYR   A CA   1 
ATOM   2436 C  C    . TYR   A 1 324 ? -41.19929 -10.51573 7.50766   1.000 107.43446 ? 324 TYR   A C    1 
ATOM   2437 O  O    . TYR   A 1 324 ? -41.17362 -11.58742 6.88870   1.000 105.35957 ? 324 TYR   A O    1 
ATOM   2438 C  CB   . TYR   A 1 324 ? -39.35951 -8.78952  7.08146   1.000 110.96845 ? 324 TYR   A CB   1 
ATOM   2439 C  CG   . TYR   A 1 324 ? -38.30616 -9.72246  6.47160   1.000 109.74468 ? 324 TYR   A CG   1 
ATOM   2440 C  CD1  . TYR   A 1 324 ? -38.12291 -9.79317  5.08831   1.000 109.39033 ? 324 TYR   A CD1  1 
ATOM   2441 C  CD2  . TYR   A 1 324 ? -37.46554 -10.48526 7.27255   1.000 102.40134 ? 324 TYR   A CD2  1 
ATOM   2442 C  CE1  . TYR   A 1 324 ? -37.16393 -10.63982 4.52466   1.000 106.88151 ? 324 TYR   A CE1  1 
ATOM   2443 C  CE2  . TYR   A 1 324 ? -36.49658 -11.32432 6.72164   1.000 100.70230 ? 324 TYR   A CE2  1 
ATOM   2444 C  CZ   . TYR   A 1 324 ? -36.34968 -11.40109 5.34954   1.000 103.28421 ? 324 TYR   A CZ   1 
ATOM   2445 O  OH   . TYR   A 1 324 ? -35.38948 -12.24004 4.80983   1.000 94.12926  ? 324 TYR   A OH   1 
ATOM   2446 N  N    . VAL   A 1 325 ? -41.62786 -10.44365 8.77849   1.000 106.32833 ? 325 VAL   A N    1 
ATOM   2447 C  CA   . VAL   A 1 325 ? -41.95304 -11.66257 9.53162   1.000 107.18237 ? 325 VAL   A CA   1 
ATOM   2448 C  C    . VAL   A 1 325 ? -43.11477 -12.41506 8.89064   1.000 106.73723 ? 325 VAL   A C    1 
ATOM   2449 O  O    . VAL   A 1 325 ? -43.21958 -13.64410 9.02634   1.000 99.54415  ? 325 VAL   A O    1 
ATOM   2450 C  CB   . VAL   A 1 325 ? -42.25714 -11.33884 11.01366  1.000 100.24960 ? 325 VAL   A CB   1 
ATOM   2451 C  CG1  . VAL   A 1 325 ? -43.20390 -12.37246 11.59305  1.000 91.01373  ? 325 VAL   A CG1  1 
ATOM   2452 C  CG2  . VAL   A 1 325 ? -40.97290 -11.32216 11.83903  1.000 102.84640 ? 325 VAL   A CG2  1 
ATOM   2453 N  N    . ASN   A 1 326 ? -44.01752 -11.69611 8.21947   1.000 108.67635 ? 326 ASN   A N    1 
ATOM   2454 C  CA   . ASN   A 1 326 ? -45.14122 -12.27334 7.49060   1.000 114.88208 ? 326 ASN   A CA   1 
ATOM   2455 C  C    . ASN   A 1 326 ? -44.80962 -12.57867 6.02973   1.000 111.24266 ? 326 ASN   A C    1 
ATOM   2456 O  O    . ASN   A 1 326 ? -45.72397 -12.87014 5.24789   1.000 114.81082 ? 326 ASN   A O    1 
ATOM   2457 C  CB   . ASN   A 1 326 ? -46.36133 -11.34713 7.57358   1.000 119.83406 ? 326 ASN   A CB   1 
ATOM   2458 C  CG   . ASN   A 1 326 ? -46.96849 -11.30683 8.96660   1.000 120.97339 ? 326 ASN   A CG   1 
ATOM   2459 O  OD1  . ASN   A 1 326 ? -47.58992 -12.26941 9.40890   1.000 125.10132 ? 326 ASN   A OD1  1 
ATOM   2460 N  ND2  . ASN   A 1 326 ? -46.78373 -10.19366 9.66569   1.000 122.86009 ? 326 ASN   A ND2  1 
ATOM   2461 N  N    . GLY   A 1 327 ? -43.54113 -12.46851 5.63797   1.000 99.34505  ? 327 GLY   A N    1 
ATOM   2462 C  CA   . GLY   A 1 327 ? -43.11131 -12.84684 4.31206   1.000 95.92402  ? 327 GLY   A CA   1 
ATOM   2463 C  C    . GLY   A 1 327 ? -43.43362 -11.87474 3.20023   1.000 104.50727 ? 327 GLY   A C    1 
ATOM   2464 O  O    . GLY   A 1 327 ? -43.32631 -12.24793 2.02432   1.000 96.25227  ? 327 GLY   A O    1 
ATOM   2465 N  N    . PHE   A 1 328 ? -43.82896 -10.64322 3.52269   1.000 111.67569 ? 328 PHE   A N    1 
ATOM   2466 C  CA   . PHE   A 1 328 ? -44.08503 -9.65268  2.48106   1.000 115.77485 ? 328 PHE   A CA   1 
ATOM   2467 C  C    . PHE   A 1 328 ? -42.79271 -9.14056  1.84951   1.000 110.31358 ? 328 PHE   A C    1 
ATOM   2468 O  O    . PHE   A 1 328 ? -42.83586 -8.51958  0.78275   1.000 111.82725 ? 328 PHE   A O    1 
ATOM   2469 C  CB   . PHE   A 1 328 ? -44.90395 -8.48928  3.04851   1.000 116.33645 ? 328 PHE   A CB   1 
ATOM   2470 C  CG   . PHE   A 1 328 ? -46.25935 -8.89241  3.58560   1.000 121.05637 ? 328 PHE   A CG   1 
ATOM   2471 C  CD1  . PHE   A 1 328 ? -46.67587 -10.21596 3.56327   1.000 122.10243 ? 328 PHE   A CD1  1 
ATOM   2472 C  CD2  . PHE   A 1 328 ? -47.11614 -7.93766  4.11432   1.000 127.81822 ? 328 PHE   A CD2  1 
ATOM   2473 C  CE1  . PHE   A 1 328 ? -47.91609 -10.57838 4.05610   1.000 127.83005 ? 328 PHE   A CE1  1 
ATOM   2474 C  CE2  . PHE   A 1 328 ? -48.35873 -8.29366  4.60704   1.000 134.32321 ? 328 PHE   A CE2  1 
ATOM   2475 C  CZ   . PHE   A 1 328 ? -48.75956 -9.61677  4.57638   1.000 132.19554 ? 328 PHE   A CZ   1 
ATOM   2476 N  N    . ILE   A 1 329 ? -41.65407 -9.37585  2.49271   1.000 101.98324 ? 329 ILE   A N    1 
ATOM   2477 C  CA   . ILE   A 1 329 ? -40.34982 -8.90959  2.03440   1.000 103.43969 ? 329 ILE   A CA   1 
ATOM   2478 C  C    . ILE   A 1 329 ? -39.49884 -10.13738 1.69478   1.000 96.05909  ? 329 ILE   A C    1 
ATOM   2479 O  O    . ILE   A 1 329 ? -39.28701 -11.00116 2.56241   1.000 91.99372  ? 329 ILE   A O    1 
ATOM   2480 C  CB   . ILE   A 1 329 ? -39.66275 -8.04558  3.10762   1.000 98.92652  ? 329 ILE   A CB   1 
ATOM   2481 C  CG1  . ILE   A 1 329 ? -40.64609 -7.01719  3.69747   1.000 97.17860  ? 329 ILE   A CG1  1 
ATOM   2482 C  CG2  . ILE   A 1 329 ? -38.48031 -7.32015  2.49321   1.000 94.28493  ? 329 ILE   A CG2  1 
ATOM   2483 C  CD1  . ILE   A 1 329 ? -40.07948 -6.07829  4.79800   1.000 87.85759  ? 329 ILE   A CD1  1 
ATOM   2484 N  N    . HIS   A 1 330 ? -39.01742 -10.22546 0.43452   1.000 93.21162  ? 330 HIS   A N    1 
ATOM   2485 C  CA   . HIS   A 1 330 ? -38.12207 -11.33016 0.08038   1.000 81.47965  ? 330 HIS   A CA   1 
ATOM   2486 C  C    . HIS   A 1 330 ? -36.77825 -11.12612 0.77189   1.000 91.16599  ? 330 HIS   A C    1 
ATOM   2487 O  O    . HIS   A 1 330 ? -36.25909 -10.00391 0.78668   1.000 82.49198  ? 330 HIS   A O    1 
ATOM   2488 C  CB   . HIS   A 1 330 ? -37.84672 -11.42855 -1.43724  1.000 72.90823  ? 330 HIS   A CB   1 
ATOM   2489 C  CG   . HIS   A 1 330 ? -38.90134 -12.14481 -2.24346  1.000 76.86145  ? 330 HIS   A CG   1 
ATOM   2490 N  ND1  . HIS   A 1 330 ? -38.81299 -12.27227 -3.61513  1.000 72.58819  ? 330 HIS   A ND1  1 
ATOM   2491 C  CD2  . HIS   A 1 330 ? -40.00715 -12.83579 -1.87686  1.000 77.49649  ? 330 HIS   A CD2  1 
ATOM   2492 C  CE1  . HIS   A 1 330 ? -39.84717 -12.96291 -4.06790  1.000 77.85526  ? 330 HIS   A CE1  1 
ATOM   2493 N  NE2  . HIS   A 1 330 ? -40.58685 -13.31996 -3.03141  1.000 84.79744  ? 330 HIS   A NE2  1 
ATOM   2494 N  N    . PRO   A 1 331 ? -36.16209 -12.19634 1.29512   1.000 93.87326  ? 331 PRO   A N    1 
ATOM   2495 C  CA   . PRO   A 1 331 ? -34.85436 -12.01149 1.95499   1.000 90.66430  ? 331 PRO   A CA   1 
ATOM   2496 C  C    . PRO   A 1 331 ? -33.84587 -11.41168 0.99979   1.000 77.52745  ? 331 PRO   A C    1 
ATOM   2497 O  O    . PRO   A 1 331 ? -33.18536 -10.41191 1.31478   1.000 82.82318  ? 331 PRO   A O    1 
ATOM   2498 C  CB   . PRO   A 1 331 ? -34.47990 -13.43530 2.38679   1.000 97.09760  ? 331 PRO   A CB   1 
ATOM   2499 C  CG   . PRO   A 1 331 ? -35.11111 -14.29743 1.30530   1.000 101.10328 ? 331 PRO   A CG   1 
ATOM   2500 C  CD   . PRO   A 1 331 ? -36.42009 -13.61097 0.95538   1.000 93.52833  ? 331 PRO   A CD   1 
ATOM   2501 N  N    . LEU   A 1 332 ? -33.77733 -11.95770 -0.21010  1.000 80.16539  ? 332 LEU   A N    1 
ATOM   2502 C  CA   . LEU   A 1 332 ? -32.81546 -11.46149 -1.17239  1.000 80.88836  ? 332 LEU   A CA   1 
ATOM   2503 C  C    . LEU   A 1 332 ? -33.08193 -9.98693  -1.50991  1.000 86.45209  ? 332 LEU   A C    1 
ATOM   2504 O  O    . LEU   A 1 332 ? -32.13274 -9.23069  -1.76422  1.000 76.41320  ? 332 LEU   A O    1 
ATOM   2505 C  CB   . LEU   A 1 332 ? -32.83764 -12.37061 -2.39102  1.000 84.20345  ? 332 LEU   A CB   1 
ATOM   2506 C  CG   . LEU   A 1 332 ? -31.94567 -12.03284 -3.56210  1.000 82.83304  ? 332 LEU   A CG   1 
ATOM   2507 C  CD1  . LEU   A 1 332 ? -31.90000 -13.25336 -4.43892  1.000 84.21289  ? 332 LEU   A CD1  1 
ATOM   2508 C  CD2  . LEU   A 1 332 ? -32.53921 -10.87592 -4.30644  1.000 89.22407  ? 332 LEU   A CD2  1 
ATOM   2509 N  N    . ASP   A 1 333 ? -34.35237 -9.53932  -1.50821  1.000 75.34853  ? 333 ASP   A N    1 
ATOM   2510 C  CA   . ASP   A 1 333 ? -34.57958 -8.10285  -1.70149  1.000 79.91010  ? 333 ASP   A CA   1 
ATOM   2511 C  C    . ASP   A 1 333 ? -33.95086 -7.28518  -0.55971  1.000 80.19890  ? 333 ASP   A C    1 
ATOM   2512 O  O    . ASP   A 1 333 ? -33.34531 -6.21681  -0.79580  1.000 72.54126  ? 333 ASP   A O    1 
ATOM   2513 C  CB   . ASP   A 1 333 ? -36.07984 -7.79830  -1.84327  1.000 81.23119  ? 333 ASP   A CB   1 
ATOM   2514 C  CG   . ASP   A 1 333 ? -36.65000 -8.22147  -3.22308  1.000 88.04529  ? 333 ASP   A CG   1 
ATOM   2515 O  OD1  . ASP   A 1 333 ? -35.90938 -8.12167  -4.23236  1.000 90.42290  ? 333 ASP   A OD1  1 
ATOM   2516 O  OD2  . ASP   A 1 333 ? -37.84521 -8.61820  -3.31234  1.000 89.35080  ? 333 ASP   A OD2  1 
ATOM   2517 N  N    . LEU   A 1 334 ? -34.05696 -7.79237  0.68131   1.000 75.06250  ? 334 LEU   A N    1 
ATOM   2518 C  CA   . LEU   A 1 334 ? -33.44922 -7.12193  1.82326   1.000 78.52234  ? 334 LEU   A CA   1 
ATOM   2519 C  C    . LEU   A 1 334 ? -31.93765 -7.06968  1.67054   1.000 74.27719  ? 334 LEU   A C    1 
ATOM   2520 O  O    . LEU   A 1 334 ? -31.32887 -6.04684  1.97902   1.000 72.69188  ? 334 LEU   A O    1 
ATOM   2521 C  CB   . LEU   A 1 334 ? -33.84022 -7.82315  3.12316   1.000 69.01141  ? 334 LEU   A CB   1 
ATOM   2522 C  CG   . LEU   A 1 334 ? -33.53210 -7.03455  4.37188   1.000 78.05868  ? 334 LEU   A CG   1 
ATOM   2523 C  CD1  . LEU   A 1 334 ? -34.32959 -5.75625  4.26717   1.000 70.03706  ? 334 LEU   A CD1  1 
ATOM   2524 C  CD2  . LEU   A 1 334 ? -33.92144 -7.80271  5.62741   1.000 76.70651  ? 334 LEU   A CD2  1 
ATOM   2525 N  N    . LYS   A 1 335 ? -31.31985 -8.15251  1.16248   1.000 79.75149  ? 335 LYS   A N    1 
ATOM   2526 C  CA   . LYS   A 1 335 ? -29.86693 -8.17588  0.93507   1.000 75.82342  ? 335 LYS   A CA   1 
ATOM   2527 C  C    . LYS   A 1 335 ? -29.45239 -7.14307  -0.09839  1.000 72.38888  ? 335 LYS   A C    1 
ATOM   2528 O  O    . LYS   A 1 335 ? -28.46319 -6.42241  0.06441   1.000 64.67385  ? 335 LYS   A O    1 
ATOM   2529 C  CB   . LYS   A 1 335 ? -29.39685 -9.54886  0.43761   1.000 74.54943  ? 335 LYS   A CB   1 
ATOM   2530 C  CG   . LYS   A 1 335 ? -29.19536 -10.62638 1.47886   1.000 74.59878  ? 335 LYS   A CG   1 
ATOM   2531 C  CD   . LYS   A 1 335 ? -28.63120 -11.86458 0.79710   1.000 75.32762  ? 335 LYS   A CD   1 
ATOM   2532 C  CE   . LYS   A 1 335 ? -28.02427 -12.80073 1.80949   1.000 75.78786  ? 335 LYS   A CE   1 
ATOM   2533 N  NZ   . LYS   A 1 335 ? -27.41880 -14.00357 1.17869   1.000 73.39887  ? 335 LYS   A NZ   1 
ATOM   2534 N  N    . ASP   A 1 336 ? -30.16497 -7.11493  -1.20663  1.000 65.87355  ? 336 ASP   A N    1 
ATOM   2535 C  CA   . ASP   A 1 336 ? -29.82260 -6.22133  -2.30695  1.000 63.55679  ? 336 ASP   A CA   1 
ATOM   2536 C  C    . ASP   A 1 336 ? -29.81283 -4.76670  -1.85563  1.000 64.38580  ? 336 ASP   A C    1 
ATOM   2537 O  O    . ASP   A 1 336 ? -28.88667 -4.00111  -2.18340  1.000 65.91485  ? 336 ASP   A O    1 
ATOM   2538 C  CB   . ASP   A 1 336 ? -30.84606 -6.43272  -3.42474  1.000 68.60001  ? 336 ASP   A CB   1 
ATOM   2539 C  CG   . ASP   A 1 336 ? -30.79513 -7.84153  -3.98235  1.000 84.60839  ? 336 ASP   A CG   1 
ATOM   2540 O  OD1  . ASP   A 1 336 ? -29.72550 -8.48147  -3.85439  1.000 85.16962  ? 336 ASP   A OD1  1 
ATOM   2541 O  OD2  . ASP   A 1 336 ? -31.82991 -8.30894  -4.53298  1.000 82.51617  ? 336 ASP   A OD2  1 
ATOM   2542 N  N    . ASN   A 1 337 ? -30.85868 -4.36349  -1.10543  1.000 58.85669  ? 337 ASN   A N    1 
ATOM   2543 C  CA   . ASN   A 1 337 ? -30.91787 -2.98758  -0.61642  1.000 67.37638  ? 337 ASN   A CA   1 
ATOM   2544 C  C    . ASN   A 1 337 ? -29.94288 -2.73804  0.53863   1.000 57.83945  ? 337 ASN   A C    1 
ATOM   2545 O  O    . ASN   A 1 337 ? -29.35504 -1.65785  0.61856   1.000 63.07736  ? 337 ASN   A O    1 
ATOM   2546 C  CB   . ASN   A 1 337 ? -32.31119 -2.61945  -0.13384  1.000 64.40249  ? 337 ASN   A CB   1 
ATOM   2547 C  CG   . ASN   A 1 337 ? -33.26781 -2.34869  -1.26438  1.000 75.84456  ? 337 ASN   A CG   1 
ATOM   2548 O  OD1  . ASN   A 1 337 ? -33.14010 -1.34599  -1.98962  1.000 79.25118  ? 337 ASN   A OD1  1 
ATOM   2549 N  ND2  . ASN   A 1 337 ? -34.24862 -3.24157  -1.41646  1.000 70.41519  ? 337 ASN   A ND2  1 
ATOM   2550 N  N    . VAL   A 1 338 ? -29.83577 -3.67218  1.49281   1.000 63.38839  ? 338 VAL   A N    1 
ATOM   2551 C  CA   . VAL   A 1 338 ? -28.87728 -3.48831  2.57954   1.000 63.20142  ? 338 VAL   A CA   1 
ATOM   2552 C  C    . VAL   A 1 338 ? -27.50330 -3.23748  1.99744   1.000 63.41361  ? 338 VAL   A C    1 
ATOM   2553 O  O    . VAL   A 1 338 ? -26.83278 -2.26744  2.35748   1.000 64.07053  ? 338 VAL   A O    1 
ATOM   2554 C  CB   . VAL   A 1 338 ? -28.87547 -4.69594  3.53307   1.000 59.71798  ? 338 VAL   A CB   1 
ATOM   2555 C  CG1  . VAL   A 1 338 ? -27.58744 -4.64842  4.45254   1.000 54.01080  ? 338 VAL   A CG1  1 
ATOM   2556 C  CG2  . VAL   A 1 338 ? -30.10687 -4.67638  4.41741   1.000 51.37721  ? 338 VAL   A CG2  1 
ATOM   2557 N  N    . ALA   A 1 339 ? -27.08523 -4.07712  1.04906   1.000 58.85386  ? 339 ALA   A N    1 
ATOM   2558 C  CA   . ALA   A 1 339 ? -25.78356 -3.87974  0.43351   1.000 62.96253  ? 339 ALA   A CA   1 
ATOM   2559 C  C    . ALA   A 1 339 ? -25.69056 -2.52335  -0.26418  1.000 68.61253  ? 339 ALA   A C    1 
ATOM   2560 O  O    . ALA   A 1 339 ? -24.72765 -1.78085  -0.04089  1.000 69.48819  ? 339 ALA   A O    1 
ATOM   2561 C  CB   . ALA   A 1 339 ? -25.45780 -5.03436  -0.51484  1.000 56.79861  ? 339 ALA   A CB   1 
ATOM   2562 N  N    . MET   A 1 340 ? -26.65321 -2.15954  -1.13066  1.000 66.43405  ? 340 MET   A N    1 
ATOM   2563 C  CA   . MET   A 1 340 ? -26.40084 -0.86440  -1.76751  1.000 67.72864  ? 340 MET   A CA   1 
ATOM   2564 C  C    . MET   A 1 340 ? -26.45355 0.31343   -0.75943  1.000 66.48393  ? 340 MET   A C    1 
ATOM   2565 O  O    . MET   A 1 340 ? -25.72188 1.29913   -0.92217  1.000 62.78313  ? 340 MET   A O    1 
ATOM   2566 C  CB   . MET   A 1 340 ? -27.25848 -0.66484  -3.03154  1.000 67.07503  ? 340 MET   A CB   1 
ATOM   2567 C  CG   . MET   A 1 340 ? -26.70084 0.51991   -3.78056  1.000 76.93174  ? 340 MET   A CG   1 
ATOM   2568 S  SD   . MET   A 1 340 ? -27.13443 0.81822   -5.49093  1.000 113.19109 ? 340 MET   A SD   1 
ATOM   2569 C  CE   . MET   A 1 340 ? -26.36434 -0.60853  -6.26915  1.000 101.37078 ? 340 MET   A CE   1 
ATOM   2570 N  N    . TYR   A 1 341 ? -27.32971 0.26901   0.25589   1.000 66.21371  ? 341 TYR   A N    1 
ATOM   2571 C  CA   . TYR   A 1 341 ? -27.37713 1.34568   1.25791   1.000 67.09792  ? 341 TYR   A CA   1 
ATOM   2572 C  C    . TYR   A 1 341 ? -26.08355 1.44011   2.07869   1.000 69.22821  ? 341 TYR   A C    1 
ATOM   2573 O  O    . TYR   A 1 341 ? -25.63305 2.54703   2.40410   1.000 66.99134  ? 341 TYR   A O    1 
ATOM   2574 C  CB   . TYR   A 1 341 ? -28.57718 1.18961   2.20505   1.000 57.32970  ? 341 TYR   A CB   1 
ATOM   2575 C  CG   . TYR   A 1 341 ? -29.90370 1.69474   1.61671   1.000 70.61049  ? 341 TYR   A CG   1 
ATOM   2576 C  CD1  . TYR   A 1 341 ? -30.00944 2.94655   1.00018   1.000 71.38530  ? 341 TYR   A CD1  1 
ATOM   2577 C  CD2  . TYR   A 1 341 ? -31.06390 0.92702   1.72620   1.000 66.50804  ? 341 TYR   A CD2  1 
ATOM   2578 C  CE1  . TYR   A 1 341 ? -31.25839 3.39293   0.45983   1.000 74.17519  ? 341 TYR   A CE1  1 
ATOM   2579 C  CE2  . TYR   A 1 341 ? -32.29898 1.36789   1.21439   1.000 69.61486  ? 341 TYR   A CE2  1 
ATOM   2580 C  CZ   . TYR   A 1 341 ? -32.38993 2.59808   0.58673   1.000 70.76202  ? 341 TYR   A CZ   1 
ATOM   2581 O  OH   . TYR   A 1 341 ? -33.62061 3.00553   0.08082   1.000 81.54767  ? 341 TYR   A OH   1 
ATOM   2582 N  N    . ILE   A 1 342 ? -25.52392 0.29367   2.49346   1.000 65.05505  ? 342 ILE   A N    1 
ATOM   2583 C  CA   . ILE   A 1 342 ? -24.23760 0.27930   3.19316   1.000 65.15018  ? 342 ILE   A CA   1 
ATOM   2584 C  C    . ILE   A 1 342 ? -23.17361 0.87005   2.28027   1.000 70.96070  ? 342 ILE   A C    1 
ATOM   2585 O  O    . ILE   A 1 342 ? -22.22955 1.52981   2.73436   1.000 58.11563  ? 342 ILE   A O    1 
ATOM   2586 C  CB   . ILE   A 1 342 ? -23.86250 -1.15796  3.64690   1.000 63.95503  ? 342 ILE   A CB   1 
ATOM   2587 C  CG1  . ILE   A 1 342 ? -24.71258 -1.70119  4.80491   1.000 59.73474  ? 342 ILE   A CG1  1 
ATOM   2588 C  CG2  . ILE   A 1 342 ? -22.45680 -1.21091  4.19590   1.000 60.41618  ? 342 ILE   A CG2  1 
ATOM   2589 C  CD1  . ILE   A 1 342 ? -24.98353 -0.73526  5.94527   1.000 59.74954  ? 342 ILE   A CD1  1 
ATOM   2590 N  N    . ASN   A 1 343 ? -23.28553 0.60732   0.97521   1.000 62.80683  ? 343 ASN   A N    1 
ATOM   2591 C  CA   . ASN   A 1 343 ? -22.31632 1.16591   0.03130   1.000 68.28662  ? 343 ASN   A CA   1 
ATOM   2592 C  C    . ASN   A 1 343 ? -22.42947 2.68345   -0.05948  1.000 64.07485  ? 343 ASN   A C    1 
ATOM   2593 O  O    . ASN   A 1 343 ? -21.42481 3.40043   0.02501   1.000 70.91067  ? 343 ASN   A O    1 
ATOM   2594 C  CB   . ASN   A 1 343 ? -22.53521 0.51789   -1.33176  1.000 74.98007  ? 343 ASN   A CB   1 
ATOM   2595 C  CG   . ASN   A 1 343 ? -21.91539 -0.84292  -1.39491  1.000 76.29015  ? 343 ASN   A CG   1 
ATOM   2596 O  OD1  . ASN   A 1 343 ? -20.76315 -1.01606  -0.98588  1.000 67.96922  ? 343 ASN   A OD1  1 
ATOM   2597 N  ND2  . ASN   A 1 343 ? -22.71814 -1.84535  -1.76326  1.000 64.48701  ? 343 ASN   A ND2  1 
ATOM   2598 N  N    . LYS   A 1 344 ? -23.65330 3.18760   -0.19781  1.000 71.50940  ? 344 LYS   A N    1 
ATOM   2599 C  CA   . LYS   A 1 344 ? -23.87550 4.62725   -0.16136  1.000 69.73860  ? 344 LYS   A CA   1 
ATOM   2600 C  C    . LYS   A 1 344 ? -23.29886 5.23694   1.11541   1.000 68.45864  ? 344 LYS   A C    1 
ATOM   2601 O  O    . LYS   A 1 344 ? -22.61504 6.26497   1.06379   1.000 67.41938  ? 344 LYS   A O    1 
ATOM   2602 C  CB   . LYS   A 1 344 ? -25.36497 4.92790   -0.30841  1.000 67.04886  ? 344 LYS   A CB   1 
ATOM   2603 C  CG   . LYS   A 1 344 ? -25.87196 4.62207   -1.72466  1.000 72.56837  ? 344 LYS   A CG   1 
ATOM   2604 C  CD   . LYS   A 1 344 ? -27.36595 4.62410   -1.83768  1.000 68.55476  ? 344 LYS   A CD   1 
ATOM   2605 C  CE   . LYS   A 1 344 ? -27.76612 4.47431   -3.31292  1.000 81.90026  ? 344 LYS   A CE   1 
ATOM   2606 N  NZ   . LYS   A 1 344 ? -29.18730 4.75233   -3.55279  1.000 85.88427  ? 344 LYS   A NZ   1 
ATOM   2607 N  N    . LEU   A 1 345 ? -23.53651 4.59810   2.26685   1.000 71.67862  ? 345 LEU   A N    1 
ATOM   2608 C  CA   . LEU   A 1 345 ? -23.06732 5.15697   3.53707   1.000 66.84752  ? 345 LEU   A CA   1 
ATOM   2609 C  C    . LEU   A 1 345 ? -21.53581 5.16399   3.65549   1.000 60.37536  ? 345 LEU   A C    1 
ATOM   2610 O  O    . LEU   A 1 345 ? -20.95855 6.11329   4.20834   1.000 60.22601  ? 345 LEU   A O    1 
ATOM   2611 C  CB   . LEU   A 1 345 ? -23.71078 4.38630   4.68503   1.000 66.52369  ? 345 LEU   A CB   1 
ATOM   2612 C  CG   . LEU   A 1 345 ? -25.21067 4.64760   4.78216   1.000 61.91604  ? 345 LEU   A CG   1 
ATOM   2613 C  CD1  . LEU   A 1 345 ? -25.78919 3.88873   5.95877   1.000 67.86308  ? 345 LEU   A CD1  1 
ATOM   2614 C  CD2  . LEU   A 1 345 ? -25.46242 6.11758   4.93952   1.000 61.39823  ? 345 LEU   A CD2  1 
ATOM   2615 N  N    . LEU   A 1 346 ? -20.84989 4.14992   3.11883   1.000 61.28212  ? 346 LEU   A N    1 
ATOM   2616 C  CA   . LEU   A 1 346 ? -19.39264 4.12662   3.17451   1.000 57.78956  ? 346 LEU   A CA   1 
ATOM   2617 C  C    . LEU   A 1 346 ? -18.72934 5.01351   2.13040   1.000 63.92357  ? 346 LEU   A C    1 
ATOM   2618 O  O    . LEU   A 1 346 ? -17.51100 5.23924   2.20944   1.000 64.00687  ? 346 LEU   A O    1 
ATOM   2619 C  CB   . LEU   A 1 346 ? -18.85342 2.69927   2.98133   1.000 62.14654  ? 346 LEU   A CB   1 
ATOM   2620 C  CG   . LEU   A 1 346 ? -18.99088 1.66043   4.09016   1.000 60.22946  ? 346 LEU   A CG   1 
ATOM   2621 C  CD1  . LEU   A 1 346 ? -18.46787 0.34141   3.57861   1.000 51.24222  ? 346 LEU   A CD1  1 
ATOM   2622 C  CD2  . LEU   A 1 346 ? -18.14490 2.13835   5.30014   1.000 55.45730  ? 346 LEU   A CD2  1 
ATOM   2623 N  N    . GLN   A 1 347 ? -19.50774 5.54934   1.18831   1.000 70.15693  ? 347 GLN   A N    1 
ATOM   2624 C  CA   . GLN   A 1 347 ? -18.94600 6.31968   0.08364   1.000 69.02182  ? 347 GLN   A CA   1 
ATOM   2625 C  C    . GLN   A 1 347 ? -18.10288 7.48390   0.57960   1.000 69.06813  ? 347 GLN   A C    1 
ATOM   2626 O  O    . GLN   A 1 347 ? -16.92063 7.56334   0.19869   1.000 68.09004  ? 347 GLN   A O    1 
ATOM   2627 C  CB   . GLN   A 1 347 ? -20.10371 6.73726   -0.83428  1.000 72.17818  ? 347 GLN   A CB   1 
ATOM   2628 C  CG   . GLN   A 1 347 ? -19.75222 7.70708   -1.96337  1.000 78.23910  ? 347 GLN   A CG   1 
ATOM   2629 C  CD   . GLN   A 1 347 ? -20.05996 9.19611   -1.63923  1.000 86.41600  ? 347 GLN   A CD   1 
ATOM   2630 O  OE1  . GLN   A 1 347 ? -21.13882 9.54446   -1.11488  1.000 85.88048  ? 347 GLN   A OE1  1 
ATOM   2631 N  NE2  . GLN   A 1 347 ? -19.09724 10.07813  -1.96519  1.000 87.20947  ? 347 GLN   A NE2  1 
ATOM   2632 N  N    . PRO   A 1 348 ? -18.59835 8.37075   1.45453   1.000 64.00926  ? 348 PRO   A N    1 
ATOM   2633 C  CA   . PRO   A 1 348 ? -17.75389 9.50730   1.87570   1.000 67.54504  ? 348 PRO   A CA   1 
ATOM   2634 C  C    . PRO   A 1 348 ? -16.48463 9.10601   2.62851   1.000 63.09217  ? 348 PRO   A C    1 
ATOM   2635 O  O    . PRO   A 1 348 ? -15.48183 9.82734   2.52559   1.000 67.29703  ? 348 PRO   A O    1 
ATOM   2636 C  CB   . PRO   A 1 348 ? -18.70498 10.35756  2.72857   1.000 63.74867  ? 348 PRO   A CB   1 
ATOM   2637 C  CG   . PRO   A 1 348 ? -19.84058 9.44304   3.06656   1.000 61.80270  ? 348 PRO   A CG   1 
ATOM   2638 C  CD   . PRO   A 1 348 ? -19.98988 8.51461   1.93108   1.000 66.06257  ? 348 PRO   A CD   1 
ATOM   2639 N  N    . VAL   A 1 349 ? -16.45016 7.96025   3.32312   1.000 62.19542  ? 349 VAL   A N    1 
ATOM   2640 C  CA   . VAL   A 1 349 ? -15.17542 7.49092   3.87394   1.000 63.73603  ? 349 VAL   A CA   1 
ATOM   2641 C  C    . VAL   A 1 349 ? -14.25695 7.02268   2.75483   1.000 60.34831  ? 349 VAL   A C    1 
ATOM   2642 O  O    . VAL   A 1 349 ? -13.04082 7.27842   2.76364   1.000 59.94488  ? 349 VAL   A O    1 
ATOM   2643 C  CB   . VAL   A 1 349 ? -15.36453 6.38029   4.92602   1.000 53.31095  ? 349 VAL   A CB   1 
ATOM   2644 C  CG1  . VAL   A 1 349 ? -14.00745 5.83004   5.32659   1.000 54.85847  ? 349 VAL   A CG1  1 
ATOM   2645 C  CG2  . VAL   A 1 349 ? -16.02996 6.92453   6.17017   1.000 55.82460  ? 349 VAL   A CG2  1 
ATOM   2646 N  N    . ARG   A 1 350 ? -14.80156 6.25702   1.82215   1.000 64.16775  ? 350 ARG   A N    1 
ATOM   2647 C  CA   . ARG   A 1 350 ? -14.02403 5.86610   0.65126   1.000 70.08867  ? 350 ARG   A CA   1 
ATOM   2648 C  C    . ARG   A 1 350 ? -13.42876 7.09495   -0.03751  1.000 59.17154  ? 350 ARG   A C    1 
ATOM   2649 O  O    . ARG   A 1 350 ? -12.25194 7.10530   -0.40215  1.000 68.64837  ? 350 ARG   A O    1 
ATOM   2650 C  CB   . ARG   A 1 350 ? -14.90897 5.05605   -0.29454  1.000 65.43835  ? 350 ARG   A CB   1 
ATOM   2651 C  CG   . ARG   A 1 350 ? -15.14385 3.64324   0.22248   1.000 67.23496  ? 350 ARG   A CG   1 
ATOM   2652 C  CD   . ARG   A 1 350 ? -15.65509 2.68868   -0.84347  1.000 72.26409  ? 350 ARG   A CD   1 
ATOM   2653 N  NE   . ARG   A 1 350 ? -16.28105 1.51478   -0.24963  1.000 71.34579  ? 350 ARG   A NE   1 
ATOM   2654 C  CZ   . ARG   A 1 350 ? -17.58850 1.29458   -0.24602  1.000 72.25752  ? 350 ARG   A CZ   1 
ATOM   2655 N  NH1  . ARG   A 1 350 ? -18.43523 2.14642   -0.81072  1.000 77.18259  ? 350 ARG   A NH1  1 
ATOM   2656 N  NH2  . ARG   A 1 350 ? -18.06062 0.19402   0.33669   1.000 68.47444  ? 350 ARG   A NH2  1 
ATOM   2657 N  N    . ASP   A 1 351 ? -14.23862 8.14173   -0.21616  1.000 60.88843  ? 351 ASP   A N    1 
ATOM   2658 C  CA   . ASP   A 1 351 ? -13.79845 9.34998   -0.90402  1.000 62.18284  ? 351 ASP   A CA   1 
ATOM   2659 C  C    . ASP   A 1 351 ? -12.71130 10.05149  -0.12943  1.000 72.06738  ? 351 ASP   A C    1 
ATOM   2660 O  O    . ASP   A 1 351 ? -11.66816 10.39892  -0.69653  1.000 71.71051  ? 351 ASP   A O    1 
ATOM   2661 C  CB   . ASP   A 1 351 ? -14.98664 10.28735  -1.14693  1.000 69.95809  ? 351 ASP   A CB   1 
ATOM   2662 C  CG   . ASP   A 1 351 ? -15.92927 9.74274   -2.18579  1.000 76.37755  ? 351 ASP   A CG   1 
ATOM   2663 O  OD1  . ASP   A 1 351 ? -15.50962 8.79129   -2.88392  1.000 82.38132  ? 351 ASP   A OD1  1 
ATOM   2664 O  OD2  . ASP   A 1 351 ? -17.06572 10.25004  -2.34087  1.000 78.55657  ? 351 ASP   A OD2  1 
ATOM   2665 N  N    . HIS   A 1 352 ? -12.89285 10.19937  1.18522   1.000 67.09602  ? 352 HIS   A N    1 
ATOM   2666 C  CA   . HIS   A 1 352 ? -11.82979 10.78316  1.97476   1.000 60.41046  ? 352 HIS   A CA   1 
ATOM   2667 C  C    . HIS   A 1 352 ? -10.53406 10.01983  1.76959   1.000 63.76991  ? 352 HIS   A C    1 
ATOM   2668 O  O    . HIS   A 1 352 ? -9.45879  10.62279  1.69629   1.000 63.87946  ? 352 HIS   A O    1 
ATOM   2669 C  CB   . HIS   A 1 352 ? -12.19377 10.79313  3.46754   1.000 52.66929  ? 352 HIS   A CB   1 
ATOM   2670 C  CG   . HIS   A 1 352 ? -11.13772 11.41453  4.31829   1.000 56.54506  ? 352 HIS   A CG   1 
ATOM   2671 N  ND1  . HIS   A 1 352 ? -10.88189 12.76621  4.30290   1.000 59.50528  ? 352 HIS   A ND1  1 
ATOM   2672 C  CD2  . HIS   A 1 352 ? -10.22240 10.86721  5.15086   1.000 61.26945  ? 352 HIS   A CD2  1 
ATOM   2673 C  CE1  . HIS   A 1 352 ? -9.87539  13.03179  5.11730   1.000 61.19269  ? 352 HIS   A CE1  1 
ATOM   2674 N  NE2  . HIS   A 1 352 ? -9.45714  11.89614  5.64632   1.000 64.71130  ? 352 HIS   A NE2  1 
ATOM   2675 N  N    . PHE   A 1 353 ? -10.59854 8.68504   1.72891   1.000 62.89833  ? 353 PHE   A N    1 
ATOM   2676 C  CA   . PHE   A 1 353 ? -9.35187  7.92028   1.67109   1.000 61.49728  ? 353 PHE   A CA   1 
ATOM   2677 C  C    . PHE   A 1 353 ? -8.82910  7.74822   0.24452   1.000 66.70817  ? 353 PHE   A C    1 
ATOM   2678 O  O    . PHE   A 1 353 ? -7.71966  7.23893   0.05396   1.000 66.05383  ? 353 PHE   A O    1 
ATOM   2679 C  CB   . PHE   A 1 353 ? -9.52626  6.56391   2.35070   1.000 61.80997  ? 353 PHE   A CB   1 
ATOM   2680 C  CG   . PHE   A 1 353 ? -9.46950  6.65982   3.83711   1.000 59.24447  ? 353 PHE   A CG   1 
ATOM   2681 C  CD1  . PHE   A 1 353 ? -8.24801  6.66481   4.48010   1.000 60.04729  ? 353 PHE   A CD1  1 
ATOM   2682 C  CD2  . PHE   A 1 353 ? -10.62895 6.86127   4.58405   1.000 60.89326  ? 353 PHE   A CD2  1 
ATOM   2683 C  CE1  . PHE   A 1 353 ? -8.16723  6.80583   5.87325   1.000 54.18302  ? 353 PHE   A CE1  1 
ATOM   2684 C  CE2  . PHE   A 1 353 ? -10.53775 7.00564   5.99118   1.000 48.61719  ? 353 PHE   A CE2  1 
ATOM   2685 C  CZ   . PHE   A 1 353 ? -9.31244  6.97723   6.59410   1.000 48.38861  ? 353 PHE   A CZ   1 
ATOM   2686 N  N    . GLN   A 1 354 ? -9.61504  8.11550   -0.75220  1.000 67.79936  ? 354 GLN   A N    1 
ATOM   2687 C  CA   . GLN   A 1 354 ? -9.03404  8.14617   -2.08883  1.000 79.58247  ? 354 GLN   A CA   1 
ATOM   2688 C  C    . GLN   A 1 354 ? -8.39946  9.49984   -2.38437  1.000 79.20910  ? 354 GLN   A C    1 
ATOM   2689 O  O    . GLN   A 1 354 ? -7.24035  9.55573   -2.82087  1.000 73.27256  ? 354 GLN   A O    1 
ATOM   2690 C  CB   . GLN   A 1 354 ? -10.09777 7.79585   -3.12525  1.000 75.24643  ? 354 GLN   A CB   1 
ATOM   2691 C  CG   . GLN   A 1 354 ? -10.43022 6.28786   -3.17200  1.000 88.35632  ? 354 GLN   A CG   1 
ATOM   2692 C  CD   . GLN   A 1 354 ? -11.74060 5.96746   -3.91429  1.000 90.63070  ? 354 GLN   A CD   1 
ATOM   2693 O  OE1  . GLN   A 1 354 ? -12.49643 6.86671   -4.28884  1.000 88.67127  ? 354 GLN   A OE1  1 
ATOM   2694 N  NE2  . GLN   A 1 354 ? -11.98837 4.67989   -4.15910  1.000 94.61217  ? 354 GLN   A NE2  1 
ATOM   2695 N  N    . ASN   A 1 355 ? -9.05984  10.58370  -1.96168  1.000 79.40570  ? 355 ASN   A N    1 
ATOM   2696 C  CA   . ASN   A 1 355 ? -8.74369  11.92930  -2.41998  1.000 76.65028  ? 355 ASN   A CA   1 
ATOM   2697 C  C    . ASN   A 1 355 ? -7.86178  12.69648  -1.45720  1.000 78.67799  ? 355 ASN   A C    1 
ATOM   2698 O  O    . ASN   A 1 355 ? -7.13831  13.59841  -1.88590  1.000 85.76179  ? 355 ASN   A O    1 
ATOM   2699 C  CB   . ASN   A 1 355 ? -10.03027 12.72100  -2.63299  1.000 76.23613  ? 355 ASN   A CB   1 
ATOM   2700 C  CG   . ASN   A 1 355 ? -10.98106 12.00776  -3.54118  1.000 82.04434  ? 355 ASN   A CG   1 
ATOM   2701 O  OD1  . ASN   A 1 355 ? -10.56458 11.18870  -4.36153  1.000 88.97041  ? 355 ASN   A OD1  1 
ATOM   2702 N  ND2  . ASN   A 1 355 ? -12.26542 12.31846  -3.42278  1.000 80.03705  ? 355 ASN   A ND2  1 
ATOM   2703 N  N    . ASN   A 1 356 ? -7.87942  12.36492  -0.17679  1.000 67.55487  ? 356 ASN   A N    1 
ATOM   2704 C  CA   . ASN   A 1 356 ? -6.93238  12.95391  0.74515   1.000 78.25996  ? 356 ASN   A CA   1 
ATOM   2705 C  C    . ASN   A 1 356 ? -5.70151  12.06657  0.71655   1.000 80.02722  ? 356 ASN   A C    1 
ATOM   2706 O  O    . ASN   A 1 356 ? -5.79176  10.86351  0.97663   1.000 81.00773  ? 356 ASN   A O    1 
ATOM   2707 C  CB   . ASN   A 1 356 ? -7.48359  13.06745  2.16453   1.000 67.57880  ? 356 ASN   A CB   1 
ATOM   2708 C  CG   . ASN   A 1 356 ? -6.51991  13.77601  3.09292   1.000 75.76721  ? 356 ASN   A CG   1 
ATOM   2709 O  OD1  . ASN   A 1 356 ? -5.46308  13.23825  3.45224   1.000 69.05283  ? 356 ASN   A OD1  1 
ATOM   2710 N  ND2  . ASN   A 1 356 ? -6.89267  14.98343  3.51534   1.000 77.70592  ? 356 ASN   A ND2  1 
ATOM   2711 N  N    . ILE   A 1 357 ? -4.57353  12.64432  0.33070   1.000 77.94110  ? 357 ILE   A N    1 
ATOM   2712 C  CA   . ILE   A 1 357 ? -3.38750  11.84339  0.08744   1.000 81.97745  ? 357 ILE   A CA   1 
ATOM   2713 C  C    . ILE   A 1 357 ? -2.81242  11.29224  1.39228   1.000 73.83259  ? 357 ILE   A C    1 
ATOM   2714 O  O    . ILE   A 1 357 ? -2.47950  10.09972  1.48508   1.000 77.44235  ? 357 ILE   A O    1 
ATOM   2715 C  CB   . ILE   A 1 357 ? -2.39726  12.69086  -0.73090  1.000 93.80738  ? 357 ILE   A CB   1 
ATOM   2716 C  CG1  . ILE   A 1 357 ? -3.04481  13.05257  -2.08413  1.000 100.69532 ? 357 ILE   A CG1  1 
ATOM   2717 C  CG2  . ILE   A 1 357 ? -1.10390  11.97642  -0.95665  1.000 92.58953  ? 357 ILE   A CG2  1 
ATOM   2718 C  CD1  . ILE   A 1 357 ? -3.97022  11.95333  -2.69317  1.000 84.23336  ? 357 ILE   A CD1  1 
ATOM   2719 N  N    . GLU   A 1 358 ? -2.72686  12.12947  2.43497   1.000 75.47517  ? 358 GLU   A N    1 
ATOM   2720 C  CA   . GLU   A 1 358 ? -2.18901  11.67047  3.71431   1.000 73.75140  ? 358 GLU   A CA   1 
ATOM   2721 C  C    . GLU   A 1 358 ? -3.03816  10.55139  4.28291   1.000 65.17088  ? 358 GLU   A C    1 
ATOM   2722 O  O    . GLU   A 1 358 ? -2.51637  9.59028   4.85558   1.000 64.61380  ? 358 GLU   A O    1 
ATOM   2723 C  CB   . GLU   A 1 358 ? -2.13184  12.82081  4.71646   1.000 73.11300  ? 358 GLU   A CB   1 
ATOM   2724 C  CG   . GLU   A 1 358 ? -1.33985  14.00697  4.22793   1.000 82.14151  ? 358 GLU   A CG   1 
ATOM   2725 C  CD   . GLU   A 1 358 ? -0.24888  14.39371  5.19744   1.000 88.86433  ? 358 GLU   A CD   1 
ATOM   2726 O  OE1  . GLU   A 1 358 ? -0.35156  15.48893  5.79442   1.000 91.87164  ? 358 GLU   A OE1  1 
ATOM   2727 O  OE2  . GLU   A 1 358 ? 0.70090   13.59290  5.37926   1.000 91.42517  ? 358 GLU   A OE2  1 
ATOM   2728 N  N    . ALA   A 1 359 ? -4.35465  10.66819  4.13180   1.000 66.26973  ? 359 ALA   A N    1 
ATOM   2729 C  CA   . ALA   A 1 359 ? -5.25272  9.63022   4.60995   1.000 65.98657  ? 359 ALA   A CA   1 
ATOM   2730 C  C    . ALA   A 1 359 ? -5.07006  8.34403   3.81836   1.000 67.15360  ? 359 ALA   A C    1 
ATOM   2731 O  O    . ALA   A 1 359 ? -5.03554  7.25177   4.40228   1.000 60.66595  ? 359 ALA   A O    1 
ATOM   2732 C  CB   . ALA   A 1 359 ? -6.70240  10.11580  4.52441   1.000 61.59654  ? 359 ALA   A CB   1 
ATOM   2733 N  N    . LYS   A 1 360 ? -4.91866  8.44728   2.48699   1.000 68.75541  ? 360 LYS   A N    1 
ATOM   2734 C  CA   . LYS   A 1 360 ? -4.74323  7.23057   1.70158   1.000 62.82531  ? 360 LYS   A CA   1 
ATOM   2735 C  C    . LYS   A 1 360 ? -3.51909  6.46990   2.17725   1.000 55.93727  ? 360 LYS   A C    1 
ATOM   2736 O  O    . LYS   A 1 360 ? -3.52682  5.24023   2.26090   1.000 66.35291  ? 360 LYS   A O    1 
ATOM   2737 C  CB   . LYS   A 1 360 ? -4.63165  7.54203   0.19926   1.000 68.94078  ? 360 LYS   A CB   1 
ATOM   2738 C  CG   . LYS   A 1 360 ? -4.66622  6.26783   -0.68267  1.000 67.53547  ? 360 LYS   A CG   1 
ATOM   2739 C  CD   . LYS   A 1 360 ? -4.62775  6.50426   -2.23129  1.000 71.30511  ? 360 LYS   A CD   1 
ATOM   2740 C  CE   . LYS   A 1 360 ? -3.26182  7.07817   -2.62765  1.000 75.01250  ? 360 LYS   A CE   1 
ATOM   2741 N  NZ   . LYS   A 1 360 ? -2.93261  7.07780   -4.10251  1.000 76.27951  ? 360 LYS   A NZ   1 
ATOM   2742 N  N    . ASN   A 1 361 ? -2.44040  7.18585   2.47901   1.000 60.72704  ? 361 ASN   A N    1 
ATOM   2743 C  CA   . ASN   A 1 361 ? -1.21131  6.53007   2.91028   1.000 64.04473  ? 361 ASN   A CA   1 
ATOM   2744 C  C    . ASN   A 1 361 ? -1.28367  5.98785   4.33005   1.000 66.17002  ? 361 ASN   A C    1 
ATOM   2745 O  O    . ASN   A 1 361 ? -0.60007  5.00668   4.68011   1.000 64.26671  ? 361 ASN   A O    1 
ATOM   2746 C  CB   . ASN   A 1 361 ? -0.10114  7.52837   2.80873   1.000 67.28878  ? 361 ASN   A CB   1 
ATOM   2747 C  CG   . ASN   A 1 361 ? -0.09503  8.14860   1.48265   1.000 81.63359  ? 361 ASN   A CG   1 
ATOM   2748 O  OD1  . ASN   A 1 361 ? -0.81797  7.67170   0.56942   1.000 75.80980  ? 361 ASN   A OD1  1 
ATOM   2749 N  ND2  . ASN   A 1 361 ? 0.78675   9.13391   1.28244   1.000 79.10395  ? 361 ASN   A ND2  1 
ATOM   2750 N  N    . LEU   A 1 362 ? -2.01405  6.68627   5.18708   1.000 66.78807  ? 362 LEU   A N    1 
ATOM   2751 C  CA   . LEU   A 1 362 ? -2.25105  6.16747   6.52230   1.000 60.37043  ? 362 LEU   A CA   1 
ATOM   2752 C  C    . LEU   A 1 362 ? -2.96956  4.82872   6.44225   1.000 53.20155  ? 362 LEU   A C    1 
ATOM   2753 O  O    . LEU   A 1 362 ? -2.51795  3.83646   7.03116   1.000 59.65572  ? 362 LEU   A O    1 
ATOM   2754 C  CB   . LEU   A 1 362 ? -3.07753  7.17800   7.28936   1.000 57.09281  ? 362 LEU   A CB   1 
ATOM   2755 C  CG   . LEU   A 1 362 ? -3.39643  6.67195   8.66949   1.000 48.48464  ? 362 LEU   A CG   1 
ATOM   2756 C  CD1  . LEU   A 1 362 ? -2.10457  6.37994   9.43681   1.000 54.22907  ? 362 LEU   A CD1  1 
ATOM   2757 C  CD2  . LEU   A 1 362 ? -4.22358  7.79561   9.27410   1.000 50.93273  ? 362 LEU   A CD2  1 
ATOM   2758 N  N    . LEU   A 1 363 ? -4.04903  4.78183   5.65078   1.000 60.44204  ? 363 LEU   A N    1 
ATOM   2759 C  CA   . LEU   A 1 363 ? -4.78359  3.53937   5.42547   1.000 58.87818  ? 363 LEU   A CA   1 
ATOM   2760 C  C    . LEU   A 1 363 ? -3.87396  2.47660   4.82859   1.000 63.08249  ? 363 LEU   A C    1 
ATOM   2761 O  O    . LEU   A 1 363 ? -3.93365  1.30413   5.22813   1.000 62.51318  ? 363 LEU   A O    1 
ATOM   2762 C  CB   . LEU   A 1 363 ? -5.98505  3.79250   4.53429   1.000 58.47817  ? 363 LEU   A CB   1 
ATOM   2763 C  CG   . LEU   A 1 363 ? -6.83808  2.59021   4.10975   1.000 51.52385  ? 363 LEU   A CG   1 
ATOM   2764 C  CD1  . LEU   A 1 363 ? -7.41915  1.89494   5.31269   1.000 59.61378  ? 363 LEU   A CD1  1 
ATOM   2765 C  CD2  . LEU   A 1 363 ? -7.93517  3.00325   3.12534   1.000 67.03276  ? 363 LEU   A CD2  1 
ATOM   2766 N  N    . ASN   A 1 364 ? -3.00258  2.86047   3.88562   1.000 65.14649  ? 364 ASN   A N    1 
ATOM   2767 C  CA   . ASN   A 1 364 ? -2.08540  1.86498   3.34073   1.000 68.59036  ? 364 ASN   A CA   1 
ATOM   2768 C  C    . ASN   A 1 364 ? -1.18552  1.28916   4.40839   1.000 57.80301  ? 364 ASN   A C    1 
ATOM   2769 O  O    . ASN   A 1 364 ? -0.98690  0.07229   4.45987   1.000 61.09565  ? 364 ASN   A O    1 
ATOM   2770 C  CB   . ASN   A 1 364 ? -1.22673  2.42513   2.20932   1.000 66.25678  ? 364 ASN   A CB   1 
ATOM   2771 C  CG   . ASN   A 1 364 ? -1.84495  2.19999   0.90445   1.000 69.27353  ? 364 ASN   A CG   1 
ATOM   2772 O  OD1  . ASN   A 1 364 ? -2.00903  1.04881   0.48824   1.000 77.04996  ? 364 ASN   A OD1  1 
ATOM   2773 N  ND2  . ASN   A 1 364 ? -2.26588  3.27131   0.25181   1.000 78.63694  ? 364 ASN   A ND2  1 
ATOM   2774 N  N    . GLU   A 1 365 ? -0.60182  2.14613   5.25153   1.000 66.14586  ? 365 GLU   A N    1 
ATOM   2775 C  CA   . GLU   A 1 365 ? 0.28910   1.65603   6.29776   1.000 62.70267  ? 365 GLU   A CA   1 
ATOM   2776 C  C    . GLU   A 1 365 ? -0.45244  0.76220   7.27883   1.000 58.99724  ? 365 GLU   A C    1 
ATOM   2777 O  O    . GLU   A 1 365 ? 0.05500   -0.29526  7.65196   1.000 58.02408  ? 365 GLU   A O    1 
ATOM   2778 C  CB   . GLU   A 1 365 ? 0.96982   2.82139   7.02423   1.000 65.60455  ? 365 GLU   A CB   1 
ATOM   2779 C  CG   . GLU   A 1 365 ? 1.99160   3.54541   6.14283   1.000 78.21688  ? 365 GLU   A CG   1 
ATOM   2780 C  CD   . GLU   A 1 365 ? 2.58503   4.79271   6.78783   1.000 90.11189  ? 365 GLU   A CD   1 
ATOM   2781 O  OE1  . GLU   A 1 365 ? 3.03281   5.69128   6.02468   1.000 90.44511  ? 365 GLU   A OE1  1 
ATOM   2782 O  OE2  . GLU   A 1 365 ? 2.61182   4.86830   8.03958   1.000 85.93683  ? 365 GLU   A OE2  1 
ATOM   2783 N  N    . ILE   A 1 366 ? -1.64984  1.17275   7.72159   1.000 57.39890  ? 366 ILE   A N    1 
ATOM   2784 C  CA   . ILE   A 1 366 ? -2.28743  0.40466   8.80021   1.000 63.14795  ? 366 ILE   A CA   1 
ATOM   2785 C  C    . ILE   A 1 366 ? -2.81537  -0.92468  8.28152   1.000 61.17785  ? 366 ILE   A C    1 
ATOM   2786 O  O    . ILE   A 1 366 ? -2.84761  -1.90855  9.03264   1.000 58.60816  ? 366 ILE   A O    1 
ATOM   2787 C  CB   . ILE   A 1 366 ? -3.40045  1.19371   9.53840   1.000 54.19512  ? 366 ILE   A CB   1 
ATOM   2788 C  CG1  . ILE   A 1 366 ? -4.60059  1.45961   8.64385   1.000 57.46518  ? 366 ILE   A CG1  1 
ATOM   2789 C  CG2  . ILE   A 1 366 ? -2.83978  2.44571   10.20568  1.000 51.74118  ? 366 ILE   A CG2  1 
ATOM   2790 C  CD1  . ILE   A 1 366 ? -5.83027  0.64654   8.98165   1.000 57.13006  ? 366 ILE   A CD1  1 
ATOM   2791 N  N    . LYS   A 1 367 ? -3.18119  -1.01557  6.99084   1.000 56.46298  ? 367 LYS   A N    1 
ATOM   2792 C  CA   . LYS   A 1 367 ? -3.59760  -2.31535  6.47098   1.000 59.17529  ? 367 LYS   A CA   1 
ATOM   2793 C  C    . LYS   A 1 367 ? -2.46962  -3.34101  6.46867   1.000 60.06654  ? 367 LYS   A C    1 
ATOM   2794 O  O    . LYS   A 1 367 ? -2.75846  -4.54179  6.47811   1.000 65.12149  ? 367 LYS   A O    1 
ATOM   2795 C  CB   . LYS   A 1 367 ? -4.20902  -2.19183  5.06861   1.000 54.83187  ? 367 LYS   A CB   1 
ATOM   2796 C  CG   . LYS   A 1 367 ? -5.68986  -1.78705  5.11047   1.000 63.42669  ? 367 LYS   A CG   1 
ATOM   2797 C  CD   . LYS   A 1 367 ? -6.34563  -1.75476  3.67326   1.000 55.03739  ? 367 LYS   A CD   1 
ATOM   2798 C  CE   . LYS   A 1 367 ? -5.32260  -1.30370  2.63867   1.000 63.11557  ? 367 LYS   A CE   1 
ATOM   2799 N  NZ   . LYS   A 1 367 ? -5.88424  -0.92766  1.28465   1.000 70.50820  ? 367 LYS   A NZ   1 
ATOM   2800 N  N    . LYS   A 1 368 ? -1.20239  -2.90864  6.45651   1.000 59.51669  ? 368 LYS   A N    1 
ATOM   2801 C  CA   . LYS   A 1 368 ? -0.07949  -3.84274  6.53605   1.000 60.44134  ? 368 LYS   A CA   1 
ATOM   2802 C  C    . LYS   A 1 368 ? 0.13941   -4.43422  7.93233   1.000 66.56376  ? 368 LYS   A C    1 
ATOM   2803 O  O    . LYS   A 1 368 ? 1.03116   -5.28284  8.08640   1.000 61.98574  ? 368 LYS   A O    1 
ATOM   2804 C  CB   . LYS   A 1 368 ? 1.21930   -3.16674  6.09672   1.000 61.64121  ? 368 LYS   A CB   1 
ATOM   2805 C  CG   . LYS   A 1 368 ? 1.23195   -2.67767  4.65127   1.000 63.63877  ? 368 LYS   A CG   1 
ATOM   2806 C  CD   . LYS   A 1 368 ? 2.64325   -2.29076  4.19128   1.000 70.49332  ? 368 LYS   A CD   1 
ATOM   2807 C  CE   . LYS   A 1 368 ? 3.02045   -0.85846  4.58371   1.000 74.24948  ? 368 LYS   A CE   1 
ATOM   2808 N  NZ   . LYS   A 1 368 ? 2.93027   0.05124   3.38679   1.000 68.20873  ? 368 LYS   A NZ   1 
ATOM   2809 N  N    . TYR   A 1 369 ? -0.61343  -4.01540  8.95196   1.000 65.18127  ? 369 TYR   A N    1 
ATOM   2810 C  CA   . TYR   A 1 369 ? -0.35600  -4.49830  10.30872  1.000 65.53450  ? 369 TYR   A CA   1 
ATOM   2811 C  C    . TYR   A 1 369 ? -0.92634  -5.89159  10.54450  1.000 73.14414  ? 369 TYR   A C    1 
ATOM   2812 O  O    . TYR   A 1 369 ? -2.03372  -6.22328  10.10455  1.000 76.55262  ? 369 TYR   A O    1 
ATOM   2813 C  CB   . TYR   A 1 369 ? -0.92107  -3.53042  11.33586  1.000 63.71530  ? 369 TYR   A CB   1 
ATOM   2814 C  CG   . TYR   A 1 369 ? -0.17583  -2.22267  11.41901  1.000 57.66158  ? 369 TYR   A CG   1 
ATOM   2815 C  CD1  . TYR   A 1 369 ? 1.12988   -2.09054  10.92250  1.000 52.80137  ? 369 TYR   A CD1  1 
ATOM   2816 C  CD2  . TYR   A 1 369 ? -0.80680  -1.09991  11.91619  1.000 46.57691  ? 369 TYR   A CD2  1 
ATOM   2817 C  CE1  . TYR   A 1 369 ? 1.78815   -0.87213  10.99146  1.000 57.06167  ? 369 TYR   A CE1  1 
ATOM   2818 C  CE2  . TYR   A 1 369 ? -0.16152  0.10976   12.00407  1.000 43.97789  ? 369 TYR   A CE2  1 
ATOM   2819 C  CZ   . TYR   A 1 369 ? 1.13294   0.22352   11.53781  1.000 53.64203  ? 369 TYR   A CZ   1 
ATOM   2820 O  OH   . TYR   A 1 369 ? 1.73711   1.45664   11.63390  1.000 59.02002  ? 369 TYR   A OH   1 
ATOM   2821 N  N    . LYS   A 1 370 ? -0.14688  -6.70975  11.24353  1.000 74.46793  ? 370 LYS   A N    1 
ATOM   2822 C  CA   . LYS   A 1 370 ? -0.59953  -8.03083  11.65458  1.000 82.42646  ? 370 LYS   A CA   1 
ATOM   2823 C  C    . LYS   A 1 370 ? -1.46492  -7.89889  12.90154  1.000 84.35898  ? 370 LYS   A C    1 
ATOM   2824 O  O    . LYS   A 1 370 ? -1.09438  -7.20896  13.85900  1.000 81.29830  ? 370 LYS   A O    1 
ATOM   2825 C  CB   . LYS   A 1 370 ? 0.60463   -8.94928  11.90049  1.000 88.36862  ? 370 LYS   A CB   1 
ATOM   2826 C  CG   . LYS   A 1 370 ? 1.18104   -9.57051  10.61554  1.000 93.48975  ? 370 LYS   A CG   1 
ATOM   2827 C  CD   . LYS   A 1 370 ? 1.53670   -8.53532  9.54675   1.000 88.69610  ? 370 LYS   A CD   1 
ATOM   2828 C  CE   . LYS   A 1 370 ? 2.18533   -9.19191  8.32767   1.000 95.44481  ? 370 LYS   A CE   1 
ATOM   2829 N  NZ   . LYS   A 1 370 ? 2.55006   -8.20717  7.25836   1.000 97.38787  ? 370 LYS   A NZ   1 
ATOM   2830 N  N    . VAL   A 1 371 ? -2.61150  -8.57057  12.89538  1.000 86.55522  ? 371 VAL   A N    1 
ATOM   2831 C  CA   . VAL   A 1 371 ? -3.59307  -8.42727  13.96509  1.000 83.44466  ? 371 VAL   A CA   1 
ATOM   2832 C  C    . VAL   A 1 371 ? -3.34369  -9.51542  15.00765  1.000 85.21630  ? 371 VAL   A C    1 
ATOM   2833 O  O    . VAL   A 1 371 ? -3.34238  -10.71099 14.68827  1.000 78.70556  ? 371 VAL   A O    1 
ATOM   2834 C  CB   . VAL   A 1 371 ? -5.02635  -8.47709  13.40801  1.000 82.88225  ? 371 VAL   A CB   1 
ATOM   2835 C  CG1  . VAL   A 1 371 ? -6.04264  -8.75004  14.50888  1.000 81.09370  ? 371 VAL   A CG1  1 
ATOM   2836 C  CG2  . VAL   A 1 371 ? -5.34714  -7.17610  12.70419  1.000 74.74619  ? 371 VAL   A CG2  1 
ATOM   2837 N  N    . THR   A 1 372 ? -3.14058  -9.09329  16.25928  1.000 79.89348  ? 372 THR   A N    1 
ATOM   2838 C  CA   . THR   A 1 372 ? -2.79269  -9.98769  17.35895  1.000 79.12022  ? 372 THR   A CA   1 
ATOM   2839 C  C    . THR   A 1 372 ? -3.76220  -9.82690  18.53414  1.000 75.53843  ? 372 THR   A C    1 
ATOM   2840 O  O    . THR   A 1 372 ? -4.89071  -9.36390  18.35241  1.000 81.24514  ? 372 THR   A O    1 
ATOM   2841 C  CB   . THR   A 1 372 ? -1.37177  -9.71762  17.85777  1.000 71.01248  ? 372 THR   A CB   1 
ATOM   2842 O  OG1  . THR   A 1 372 ? -1.32448  -8.39827  18.41544  1.000 65.34279  ? 372 THR   A OG1  1 
ATOM   2843 C  CG2  . THR   A 1 372 ? -0.36731  -9.82457  16.71285  1.000 76.88442  ? 372 THR   A CG2  1 
ATOM   2844 N  N    . LYS   B 1 17  ? 53.95372  -3.96109  40.34844  1.000 106.15587 ? 17  LYS   B N    1 
ATOM   2845 C  CA   . LYS   B 1 17  ? 53.19847  -3.02230  41.18083  1.000 110.33037 ? 17  LYS   B CA   1 
ATOM   2846 C  C    . LYS   B 1 17  ? 52.45433  -3.72596  42.33210  1.000 108.42248 ? 17  LYS   B C    1 
ATOM   2847 O  O    . LYS   B 1 17  ? 52.70763  -3.39371  43.48821  1.000 107.79971 ? 17  LYS   B O    1 
ATOM   2848 C  CB   . LYS   B 1 17  ? 52.21833  -2.18192  40.33691  1.000 106.34693 ? 17  LYS   B CB   1 
ATOM   2849 C  CG   . LYS   B 1 17  ? 50.98085  -2.90723  39.83569  1.000 107.51916 ? 17  LYS   B CG   1 
ATOM   2850 C  CD   . LYS   B 1 17  ? 51.36954  -4.20373  39.18182  1.000 105.75242 ? 17  LYS   B CD   1 
ATOM   2851 C  CE   . LYS   B 1 17  ? 50.18439  -5.00435  38.74852  1.000 99.72275  ? 17  LYS   B CE   1 
ATOM   2852 N  NZ   . LYS   B 1 17  ? 50.70664  -6.23098  38.09956  1.000 93.37319  ? 17  LYS   B NZ   1 
ATOM   2853 N  N    . ALA   B 1 18  ? 51.54935  -4.67410  42.05070  1.000 103.13937 ? 18  ALA   B N    1 
ATOM   2854 C  CA   . ALA   B 1 18  ? 50.79450  -5.42705  43.06557  1.000 99.15952  ? 18  ALA   B CA   1 
ATOM   2855 C  C    . ALA   B 1 18  ? 49.50232  -4.69387  43.42624  1.000 99.85556  ? 18  ALA   B C    1 
ATOM   2856 O  O    . ALA   B 1 18  ? 48.73650  -5.16556  44.30986  1.000 94.11503  ? 18  ALA   B O    1 
ATOM   2857 C  CB   . ALA   B 1 18  ? 51.60408  -5.71043  44.34307  1.000 94.47511  ? 18  ALA   B CB   1 
ATOM   2858 N  N    . GLN   B 1 19  ? 49.25041  -3.52994  42.82285  1.000 101.12614 ? 19  GLN   B N    1 
ATOM   2859 C  CA   . GLN   B 1 19  ? 48.00142  -2.83584  43.09058  1.000 105.19544 ? 19  GLN   B CA   1 
ATOM   2860 C  C    . GLN   B 1 19  ? 46.80876  -3.68329  42.66560  1.000 106.15811 ? 19  GLN   B C    1 
ATOM   2861 O  O    . GLN   B 1 19  ? 45.75484  -3.63103  43.31227  1.000 94.37239  ? 19  GLN   B O    1 
ATOM   2862 C  CB   . GLN   B 1 19  ? 47.94804  -1.50581  42.34580  1.000 108.74906 ? 19  GLN   B CB   1 
ATOM   2863 C  CG   . GLN   B 1 19  ? 48.48316  -1.58543  40.93507  1.000 107.05135 ? 19  GLN   B CG   1 
ATOM   2864 C  CD   . GLN   B 1 19  ? 48.36168  -0.26349  40.20880  1.000 112.62418 ? 19  GLN   B CD   1 
ATOM   2865 O  OE1  . GLN   B 1 19  ? 49.10656  0.02232   39.27227  1.000 117.09991 ? 19  GLN   B OE1  1 
ATOM   2866 N  NE2  . GLN   B 1 19  ? 47.39582  0.54394   40.62524  1.000 111.80002 ? 19  GLN   B NE2  1 
ATOM   2867 N  N    . GLU   B 1 20  ? 46.95095  -4.45691  41.57699  1.000 105.13029 ? 20  GLU   B N    1 
ATOM   2868 C  CA   . GLU   B 1 20  ? 45.86952  -5.34162  41.13962  1.000 96.55297  ? 20  GLU   B CA   1 
ATOM   2869 C  C    . GLU   B 1 20  ? 45.47467  -6.30374  42.25604  1.000 90.80785  ? 20  GLU   B C    1 
ATOM   2870 O  O    . GLU   B 1 20  ? 44.28592  -6.47502  42.56337  1.000 85.78264  ? 20  GLU   B O    1 
ATOM   2871 C  CB   . GLU   B 1 20  ? 46.29217  -6.14190  39.89924  1.000 91.55006  ? 20  GLU   B CB   1 
ATOM   2872 C  CG   . GLU   B 1 20  ? 46.36901  -5.41088  38.57078  1.000 86.12971  ? 20  GLU   B CG   1 
ATOM   2873 C  CD   . GLU   B 1 20  ? 47.29230  -6.14516  37.60580  1.000 99.19961  ? 20  GLU   B CD   1 
ATOM   2874 O  OE1  . GLU   B 1 20  ? 47.63364  -7.30444  37.92387  1.000 106.62347 ? 20  GLU   B OE1  1 
ATOM   2875 O  OE2  . GLU   B 1 20  ? 47.69569  -5.58179  36.55316  1.000 91.45159  ? 20  GLU   B OE2  1 
ATOM   2876 N  N    . GLU   B 1 21  ? 46.47158  -6.96260  42.85404  1.000 85.91081  ? 21  GLU   B N    1 
ATOM   2877 C  CA   . GLU   B 1 21  ? 46.22605  -7.87874  43.96216  1.000 81.88579  ? 21  GLU   B CA   1 
ATOM   2878 C  C    . GLU   B 1 21  ? 45.54997  -7.16353  45.12000  1.000 79.74812  ? 21  GLU   B C    1 
ATOM   2879 O  O    . GLU   B 1 21  ? 44.62235  -7.69868  45.75048  1.000 71.79804  ? 21  GLU   B O    1 
ATOM   2880 C  CB   . GLU   B 1 21  ? 47.55312  -8.49637  44.40878  1.000 79.99914  ? 21  GLU   B CB   1 
ATOM   2881 C  CG   . GLU   B 1 21  ? 47.45317  -9.43453  45.58218  1.000 77.67221  ? 21  GLU   B CG   1 
ATOM   2882 C  CD   . GLU   B 1 21  ? 46.99437  -10.82830 45.18574  1.000 67.60965  ? 21  GLU   B CD   1 
ATOM   2883 O  OE1  . GLU   B 1 21  ? 47.09660  -11.16948 43.97681  1.000 68.21221  ? 21  GLU   B OE1  1 
ATOM   2884 O  OE2  . GLU   B 1 21  ? 46.52604  -11.57503 46.08677  1.000 64.92334  ? 21  GLU   B OE2  1 
ATOM   2885 N  N    . SER   B 1 22  ? 46.01585  -5.95424  45.42963  1.000 84.60766  ? 22  SER   B N    1 
ATOM   2886 C  CA   . SER   B 1 22  ? 45.41764  -5.23662  46.54388  1.000 80.94481  ? 22  SER   B CA   1 
ATOM   2887 C  C    . SER   B 1 22  ? 43.94402  -4.92220  46.27317  1.000 80.34525  ? 22  SER   B C    1 
ATOM   2888 O  O    . SER   B 1 22  ? 43.10968  -5.04776  47.17788  1.000 74.61856  ? 22  SER   B O    1 
ATOM   2889 C  CB   . SER   B 1 22  ? 46.21923  -3.96835  46.83252  1.000 91.90303  ? 22  SER   B CB   1 
ATOM   2890 O  OG   . SER   B 1 22  ? 45.90542  -3.46423  48.11948  1.000 93.13371  ? 22  SER   B OG   1 
ATOM   2891 N  N    . LYS   B 1 23  ? 43.60316  -4.53696  45.02603  1.000 77.81802  ? 23  LYS   B N    1 
ATOM   2892 C  CA   . LYS   B 1 23  ? 42.20566  -4.26832  44.64476  1.000 80.29115  ? 23  LYS   B CA   1 
ATOM   2893 C  C    . LYS   B 1 23  ? 41.33670  -5.52361  44.69230  1.000 69.21075  ? 23  LYS   B C    1 
ATOM   2894 O  O    . LYS   B 1 23  ? 40.17115  -5.46061  45.10047  1.000 66.21413  ? 23  LYS   B O    1 
ATOM   2895 C  CB   . LYS   B 1 23  ? 42.12916  -3.62357  43.25730  1.000 81.93742  ? 23  LYS   B CB   1 
ATOM   2896 C  CG   . LYS   B 1 23  ? 42.63926  -2.19539  43.19211  1.000 86.98992  ? 23  LYS   B CG   1 
ATOM   2897 C  CD   . LYS   B 1 23  ? 42.45647  -1.57780  41.81888  1.000 91.27790  ? 23  LYS   B CD   1 
ATOM   2898 C  CE   . LYS   B 1 23  ? 43.75107  -0.88185  41.37892  1.000 97.53656  ? 23  LYS   B CE   1 
ATOM   2899 N  NZ   . LYS   B 1 23  ? 43.47238  0.43863   40.73868  1.000 94.70536  ? 23  LYS   B NZ   1 
ATOM   2900 N  N    . ILE   B 1 24  ? 41.86001  -6.66359  44.23734  1.000 71.52309  ? 24  ILE   B N    1 
ATOM   2901 C  CA   . ILE   B 1 24  ? 41.10533  -7.91115  44.36775  1.000 65.98575  ? 24  ILE   B CA   1 
ATOM   2902 C  C    . ILE   B 1 24  ? 40.78100  -8.17992  45.82827  1.000 64.15834  ? 24  ILE   B C    1 
ATOM   2903 O  O    . ILE   B 1 24  ? 39.65945  -8.56786  46.17819  1.000 55.76858  ? 24  ILE   B O    1 
ATOM   2904 C  CB   . ILE   B 1 24  ? 41.88264  -9.08861  43.76316  1.000 64.87689  ? 24  ILE   B CB   1 
ATOM   2905 C  CG1  . ILE   B 1 24  ? 42.24489  -8.82136  42.30378  1.000 63.33068  ? 24  ILE   B CG1  1 
ATOM   2906 C  CG2  . ILE   B 1 24  ? 41.07760  -10.36776 43.99783  1.000 56.55625  ? 24  ILE   B CG2  1 
ATOM   2907 C  CD1  . ILE   B 1 24  ? 43.08638  -9.91962  41.70430  1.000 64.42202  ? 24  ILE   B CD1  1 
ATOM   2908 N  N    . GLU   B 1 25  ? 41.77742  -8.02661  46.70415  1.000 61.07066  ? 25  GLU   B N    1 
ATOM   2909 C  CA   . GLU   B 1 25  ? 41.53917  -8.24125  48.12808  1.000 59.56394  ? 25  GLU   B CA   1 
ATOM   2910 C  C    . GLU   B 1 25  ? 40.52347  -7.24060  48.68526  1.000 56.30310  ? 25  GLU   B C    1 
ATOM   2911 O  O    . GLU   B 1 25  ? 39.67626  -7.58307  49.52138  1.000 52.06265  ? 25  GLU   B O    1 
ATOM   2912 C  CB   . GLU   B 1 25  ? 42.87387  -8.16492  48.86343  1.000 58.73502  ? 25  GLU   B CB   1 
ATOM   2913 C  CG   . GLU   B 1 25  ? 43.83333  -9.23781  48.29689  1.000 69.11215  ? 25  GLU   B CG   1 
ATOM   2914 C  CD   . GLU   B 1 25  ? 44.72091  -9.84958  49.35335  1.000 81.87545  ? 25  GLU   B CD   1 
ATOM   2915 O  OE1  . GLU   B 1 25  ? 44.44520  -10.99894 49.77390  1.000 84.48500  ? 25  GLU   B OE1  1 
ATOM   2916 O  OE2  . GLU   B 1 25  ? 45.64536  -9.14902  49.80907  1.000 84.91053  ? 25  GLU   B OE2  1 
ATOM   2917 N  N    . ASP   B 1 26  ? 40.60098  -5.98595  48.25162  1.000 61.92414  ? 26  ASP   B N    1 
ATOM   2918 C  CA   . ASP   B 1 26  ? 39.61434  -5.00919  48.71683  1.000 60.52979  ? 26  ASP   B CA   1 
ATOM   2919 C  C    . ASP   B 1 26  ? 38.20893  -5.45629  48.34201  1.000 58.40352  ? 26  ASP   B C    1 
ATOM   2920 O  O    . ASP   B 1 26  ? 37.27933  -5.41594  49.16226  1.000 53.43397  ? 26  ASP   B O    1 
ATOM   2921 C  CB   . ASP   B 1 26  ? 39.91960  -3.63726  48.11114  1.000 68.88580  ? 26  ASP   B CB   1 
ATOM   2922 C  CG   . ASP   B 1 26  ? 41.25969  -3.06595  48.60638  1.000 78.78574  ? 26  ASP   B CG   1 
ATOM   2923 O  OD1  . ASP   B 1 26  ? 41.89287  -2.28172  47.86096  1.000 83.51751  ? 26  ASP   B OD1  1 
ATOM   2924 O  OD2  . ASP   B 1 26  ? 41.70696  -3.46907  49.71100  1.000 77.79460  ? 26  ASP   B OD2  1 
ATOM   2925 N  N    . VAL   B 1 27  ? 38.03942  -5.90163  47.09827  1.000 56.41373  ? 27  VAL   B N    1 
ATOM   2926 C  CA   . VAL   B 1 27  ? 36.70895  -6.31163  46.65766  1.000 59.34165  ? 27  VAL   B CA   1 
ATOM   2927 C  C    . VAL   B 1 27  ? 36.23041  -7.50115  47.47437  1.000 53.84445  ? 27  VAL   B C    1 
ATOM   2928 O  O    . VAL   B 1 27  ? 35.07513  -7.55249  47.90788  1.000 45.42940  ? 27  VAL   B O    1 
ATOM   2929 C  CB   . VAL   B 1 27  ? 36.73377  -6.63265  45.15605  1.000 55.61259  ? 27  VAL   B CB   1 
ATOM   2930 C  CG1  . VAL   B 1 27  ? 35.36584  -7.15743  44.69769  1.000 52.55201  ? 27  VAL   B CG1  1 
ATOM   2931 C  CG2  . VAL   B 1 27  ? 37.16118  -5.41530  44.38376  1.000 51.80353  ? 27  VAL   B CG2  1 
ATOM   2932 N  N    . ASP   B 1 28  ? 37.11474  -8.48182  47.69142  1.000 53.50869  ? 28  ASP   B N    1 
ATOM   2933 C  CA   . ASP   B 1 28  ? 36.73514  -9.66200  48.46745  1.000 52.68303  ? 28  ASP   B CA   1 
ATOM   2934 C  C    . ASP   B 1 28  ? 36.29016  -9.27662  49.85594  1.000 52.30347  ? 28  ASP   B C    1 
ATOM   2935 O  O    . ASP   B 1 28  ? 35.38511  -9.90206  50.42436  1.000 50.47062  ? 28  ASP   B O    1 
ATOM   2936 C  CB   . ASP   B 1 28  ? 37.90586  -10.65324 48.60362  1.000 60.87777  ? 28  ASP   B CB   1 
ATOM   2937 C  CG   . ASP   B 1 28  ? 38.31150  -11.29716 47.29011  1.000 68.08802  ? 28  ASP   B CG   1 
ATOM   2938 O  OD1  . ASP   B 1 28  ? 37.43019  -11.41244 46.41840  1.000 66.07737  ? 28  ASP   B OD1  1 
ATOM   2939 O  OD2  . ASP   B 1 28  ? 39.50000  -11.74263 47.15806  1.000 69.70698  ? 28  ASP   B OD2  1 
ATOM   2940 N  N    . LYS   B 1 29  ? 36.97149  -8.30383  50.45974  1.000 50.70896  ? 29  LYS   B N    1 
ATOM   2941 C  CA   . LYS   B 1 29  ? 36.58512  -7.90531  51.79891  1.000 48.60265  ? 29  LYS   B CA   1 
ATOM   2942 C  C    . LYS   B 1 29  ? 35.22601  -7.20951  51.77535  1.000 56.05395  ? 29  LYS   B C    1 
ATOM   2943 O  O    . LYS   B 1 29  ? 34.35826  -7.51446  52.58963  1.000 47.65824  ? 29  LYS   B O    1 
ATOM   2944 C  CB   . LYS   B 1 29  ? 37.65622  -7.01963  52.44296  1.000 52.14122  ? 29  LYS   B CB   1 
ATOM   2945 C  CG   . LYS   B 1 29  ? 37.16919  -6.25470  53.66035  1.000 64.62792  ? 29  LYS   B CG   1 
ATOM   2946 C  CD   . LYS   B 1 29  ? 37.93351  -4.94696  53.81769  1.000 73.20626  ? 29  LYS   B CD   1 
ATOM   2947 C  CE   . LYS   B 1 29  ? 37.87992  -4.10423  52.50900  1.000 66.92438  ? 29  LYS   B CE   1 
ATOM   2948 N  NZ   . LYS   B 1 29  ? 37.06620  -2.82204  52.66000  1.000 72.89859  ? 29  LYS   B NZ   1 
ATOM   2949 N  N    . ILE   B 1 30  ? 35.02524  -6.26489  50.84731  1.000 56.07574  ? 30  ILE   B N    1 
ATOM   2950 C  CA   . ILE   B 1 30  ? 33.73063  -5.56880  50.77992  1.000 54.86455  ? 30  ILE   B CA   1 
ATOM   2951 C  C    . ILE   B 1 30  ? 32.59649  -6.56382  50.55342  1.000 51.98055  ? 30  ILE   B C    1 
ATOM   2952 O  O    . ILE   B 1 30  ? 31.51350  -6.42942  51.13112  1.000 53.47153  ? 30  ILE   B O    1 
ATOM   2953 C  CB   . ILE   B 1 30  ? 33.73898  -4.50838  49.66621  1.000 56.14471  ? 30  ILE   B CB   1 
ATOM   2954 C  CG1  . ILE   B 1 30  ? 34.72541  -3.38186  49.99237  1.000 54.92842  ? 30  ILE   B CG1  1 
ATOM   2955 C  CG2  . ILE   B 1 30  ? 32.27403  -4.03402  49.35595  1.000 54.82368  ? 30  ILE   B CG2  1 
ATOM   2956 C  CD1  . ILE   B 1 30  ? 35.00288  -2.47682  48.81843  1.000 55.67890  ? 30  ILE   B CD1  1 
ATOM   2957 N  N    . LEU   B 1 31  ? 32.82565  -7.56172  49.68967  1.000 49.23541  ? 31  LEU   B N    1 
ATOM   2958 C  CA   . LEU   B 1 31  ? 31.84333  -8.61445  49.42697  1.000 51.09462  ? 31  LEU   B CA   1 
ATOM   2959 C  C    . LEU   B 1 31  ? 31.56294  -9.44117  50.68342  1.000 53.88255  ? 31  LEU   B C    1 
ATOM   2960 O  O    . LEU   B 1 31  ? 30.40914  -9.68541  51.03755  1.000 52.21728  ? 31  LEU   B O    1 
ATOM   2961 C  CB   . LEU   B 1 31  ? 32.34613  -9.49321  48.27689  1.000 46.30261  ? 31  LEU   B CB   1 
ATOM   2962 C  CG   . LEU   B 1 31  ? 31.54890  -10.73354 47.90690  1.000 51.61328  ? 31  LEU   B CG   1 
ATOM   2963 C  CD1  . LEU   B 1 31  ? 30.22349  -10.32298 47.21708  1.000 47.64820  ? 31  LEU   B CD1  1 
ATOM   2964 C  CD2  . LEU   B 1 31  ? 32.35482  -11.63666 46.99301  1.000 53.24530  ? 31  LEU   B CD2  1 
ATOM   2965 N  N    . ASN   B 1 32  ? 32.61005  -9.90279  51.37809  1.000 54.47694  ? 32  ASN   B N    1 
ATOM   2966 C  CA   . ASN   B 1 32  ? 32.36186  -10.62440 52.62707  1.000 50.63232  ? 32  ASN   B CA   1 
ATOM   2967 C  C    . ASN   B 1 32  ? 31.64440  -9.77001  53.65932  1.000 52.54277  ? 32  ASN   B C    1 
ATOM   2968 O  O    . ASN   B 1 32  ? 30.83438  -10.28536 54.44005  1.000 58.08459  ? 32  ASN   B O    1 
ATOM   2969 C  CB   . ASN   B 1 32  ? 33.66891  -11.14773 53.21518  1.000 59.74523  ? 32  ASN   B CB   1 
ATOM   2970 C  CG   . ASN   B 1 32  ? 33.95242  -12.53337 52.74912  1.000 76.70707  ? 32  ASN   B CG   1 
ATOM   2971 O  OD1  . ASN   B 1 32  ? 34.62272  -12.74245 51.71937  1.000 81.20355  ? 32  ASN   B OD1  1 
ATOM   2972 N  ND2  . ASN   B 1 32  ? 33.37822  -13.51327 53.45975  1.000 81.20355  ? 32  ASN   B ND2  1 
ATOM   2973 N  N    . ASP   B 1 33  ? 31.91317  -8.46948  53.69813  1.000 53.68051  ? 33  ASP   B N    1 
ATOM   2974 C  CA   . ASP   B 1 33  ? 31.20720  -7.65181  54.67817  1.000 57.04536  ? 33  ASP   B CA   1 
ATOM   2975 C  C    . ASP   B 1 33  ? 29.73627  -7.47022  54.26721  1.000 51.86860  ? 33  ASP   B C    1 
ATOM   2976 O  O    . ASP   B 1 33  ? 28.83223  -7.75151  55.05575  1.000 57.55666  ? 33  ASP   B O    1 
ATOM   2977 C  CB   . ASP   B 1 33  ? 31.91533  -6.30616  54.90172  1.000 52.24123  ? 33  ASP   B CB   1 
ATOM   2978 C  CG   . ASP   B 1 33  ? 33.32835  -6.45685  55.53765  1.000 63.80454  ? 33  ASP   B CG   1 
ATOM   2979 O  OD1  . ASP   B 1 33  ? 34.17928  -5.55644  55.29708  1.000 56.59037  ? 33  ASP   B OD1  1 
ATOM   2980 O  OD2  . ASP   B 1 33  ? 33.58195  -7.46727  56.25781  1.000 62.34584  ? 33  ASP   B OD2  1 
ATOM   2981 N  N    . ILE   B 1 34  ? 29.48353  -7.04695  53.02258  1.000 55.78663  ? 34  ILE   B N    1 
ATOM   2982 C  CA   . ILE   B 1 34  ? 28.09990  -6.89911  52.51964  1.000 48.19515  ? 34  ILE   B CA   1 
ATOM   2983 C  C    . ILE   B 1 34  ? 27.29800  -8.17399  52.74930  1.000 55.34023  ? 34  ILE   B C    1 
ATOM   2984 O  O    . ILE   B 1 34  ? 26.12068  -8.12100  53.11443  1.000 56.60181  ? 34  ILE   B O    1 
ATOM   2985 C  CB   . ILE   B 1 34  ? 28.12183  -6.51752  51.02609  1.000 47.56493  ? 34  ILE   B CB   1 
ATOM   2986 C  CG1  . ILE   B 1 34  ? 28.67095  -5.10310  50.83798  1.000 51.08176  ? 34  ILE   B CG1  1 
ATOM   2987 C  CG2  . ILE   B 1 34  ? 26.74396  -6.76142  50.36390  1.000 45.00471  ? 34  ILE   B CG2  1 
ATOM   2988 C  CD1  . ILE   B 1 34  ? 28.50836  -4.55854  49.48376  1.000 57.47255  ? 34  ILE   B CD1  1 
ATOM   2989 N  N    . LEU   B 1 35  ? 27.89957  -9.34148  52.48642  1.000 55.18128  ? 35  LEU   B N    1 
ATOM   2990 C  CA   . LEU   B 1 35  ? 27.22916  -10.61760 52.72730  1.000 55.88434  ? 35  LEU   B CA   1 
ATOM   2991 C  C    . LEU   B 1 35  ? 27.04364  -10.91134 54.20629  1.000 57.37276  ? 35  LEU   B C    1 
ATOM   2992 O  O    . LEU   B 1 35  ? 26.18896  -11.73577 54.55215  1.000 61.11617  ? 35  LEU   B O    1 
ATOM   2993 C  CB   . LEU   B 1 35  ? 28.00842  -11.77222 52.07447  1.000 53.50055  ? 35  LEU   B CB   1 
ATOM   2994 C  CG   . LEU   B 1 35  ? 27.96911  -11.83831 50.52930  1.000 53.63138  ? 35  LEU   B CG   1 
ATOM   2995 C  CD1  . LEU   B 1 35  ? 29.11977  -12.63722 49.94048  1.000 46.67165  ? 35  LEU   B CD1  1 
ATOM   2996 C  CD2  . LEU   B 1 35  ? 26.63750  -12.41788 50.03453  1.000 52.27861  ? 35  LEU   B CD2  1 
ATOM   2997 N  N    . SER   B 1 36  ? 27.86216  -10.30801 55.08200  1.000 65.40294  ? 36  SER   B N    1 
ATOM   2998 C  CA   . SER   B 1 36  ? 27.80546  -10.61993 56.51459  1.000 57.54553  ? 36  SER   B CA   1 
ATOM   2999 C  C    . SER   B 1 36  ? 26.45629  -10.27713 57.15089  1.000 61.65099  ? 36  SER   B C    1 
ATOM   3000 O  O    . SER   B 1 36  ? 25.91231  -11.06836 57.93033  1.000 57.39907  ? 36  SER   B O    1 
ATOM   3001 C  CB   . SER   B 1 36  ? 28.90141  -9.84487  57.23349  1.000 65.03892  ? 36  SER   B CB   1 
ATOM   3002 O  OG   . SER   B 1 36  ? 28.64770  -8.44437  57.12336  1.000 55.99063  ? 36  SER   B OG   1 
ATOM   3003 N  N    . ILE   B 1 37  ? 25.90815  -9.09129  56.84412  1.000 64.54461  ? 37  ILE   B N    1 
ATOM   3004 C  CA   . ILE   B 1 37  ? 24.67488  -8.62866  57.48666  1.000 73.62344  ? 37  ILE   B CA   1 
ATOM   3005 C  C    . ILE   B 1 37  ? 23.42472  -9.21949  56.85475  1.000 70.33623  ? 37  ILE   B C    1 
ATOM   3006 O  O    . ILE   B 1 37  ? 22.30357  -8.85415  57.24448  1.000 62.69565  ? 37  ILE   B O    1 
ATOM   3007 C  CB   . ILE   B 1 37  ? 24.58575  -7.08157  57.52488  1.000 69.35224  ? 37  ILE   B CB   1 
ATOM   3008 C  CG1  . ILE   B 1 37  ? 24.69293  -6.44096  56.11875  1.000 63.84278  ? 37  ILE   B CG1  1 
ATOM   3009 C  CG2  . ILE   B 1 37  ? 25.59852  -6.49686  58.54763  1.000 56.42466  ? 37  ILE   B CG2  1 
ATOM   3010 C  CD1  . ILE   B 1 37  ? 23.57784  -6.75401  55.11510  1.000 57.39578  ? 37  ILE   B CD1  1 
ATOM   3011 N  N    . SER   B 1 38  ? 23.57753  -10.11519 55.89385  1.000 57.87945  ? 38  SER   B N    1 
ATOM   3012 C  CA   . SER   B 1 38  ? 22.44261  -10.67213 55.17353  1.000 49.94707  ? 38  SER   B CA   1 
ATOM   3013 C  C    . SER   B 1 38  ? 22.11317  -12.08299 55.65348  1.000 50.79815  ? 38  SER   B C    1 
ATOM   3014 O  O    . SER   B 1 38  ? 22.98949  -12.83292 56.09463  1.000 53.11030  ? 38  SER   B O    1 
ATOM   3015 C  CB   . SER   B 1 38  ? 22.74828  -10.67478 53.68321  1.000 49.60710  ? 38  SER   B CB   1 
ATOM   3016 O  OG   . SER   B 1 38  ? 23.59074  -11.77490 53.34978  1.000 56.28658  ? 38  SER   B OG   1 
ATOM   3017 N  N    . SER   B 1 39  ? 20.83312  -12.43177 55.60450  1.000 43.29835  ? 39  SER   B N    1 
ATOM   3018 C  CA   . SER   B 1 39  ? 20.46897  -13.82426 55.80761  1.000 42.67122  ? 39  SER   B CA   1 
ATOM   3019 C  C    . SER   B 1 39  ? 20.44028  -14.58333 54.48982  1.000 50.37756  ? 39  SER   B C    1 
ATOM   3020 O  O    . SER   B 1 39  ? 20.59740  -15.81539 54.46663  1.000 45.21973  ? 39  SER   B O    1 
ATOM   3021 C  CB   . SER   B 1 39  ? 19.12865  -13.91021 56.54346  1.000 44.08488  ? 39  SER   B CB   1 
ATOM   3022 O  OG   . SER   B 1 39  ? 18.04338  -13.78251 55.65316  1.000 48.31848  ? 39  SER   B OG   1 
ATOM   3023 N  N    . GLU   B 1 40  ? 20.29002  -13.87341 53.37959  1.000 44.31091  ? 40  GLU   B N    1 
ATOM   3024 C  CA   . GLU   B 1 40  ? 20.38607  -14.58407 52.11865  1.000 42.15617  ? 40  GLU   B CA   1 
ATOM   3025 C  C    . GLU   B 1 40  ? 20.78737  -13.60751 51.04150  1.000 47.45068  ? 40  GLU   B C    1 
ATOM   3026 O  O    . GLU   B 1 40  ? 20.37465  -12.44313 51.07530  1.000 44.22512  ? 40  GLU   B O    1 
ATOM   3027 C  CB   . GLU   B 1 40  ? 19.05823  -15.26834 51.75586  1.000 45.71679  ? 40  GLU   B CB   1 
ATOM   3028 C  CG   . GLU   B 1 40  ? 19.03101  -15.76399 50.33779  1.000 45.34890  ? 40  GLU   B CG   1 
ATOM   3029 C  CD   . GLU   B 1 40  ? 17.63316  -16.23450 49.90107  1.000 57.48186  ? 40  GLU   B CD   1 
ATOM   3030 O  OE1  . GLU   B 1 40  ? 16.66129  -15.42045 49.91152  1.000 48.99900  ? 40  GLU   B OE1  1 
ATOM   3031 O  OE2  . GLU   B 1 40  ? 17.52868  -17.42865 49.50439  1.000 55.65588  ? 40  GLU   B OE2  1 
ATOM   3032 N  N    . CYS   B 1 41  ? 21.59351  -14.08002 50.09237  1.000 43.52770  ? 41  CYS   B N    1 
ATOM   3033 C  CA   . CYS   B 1 41  ? 21.99065  -13.26562 48.96172  1.000 43.07240  ? 41  CYS   B CA   1 
ATOM   3034 C  C    . CYS   B 1 41  ? 21.70813  -14.02042 47.66795  1.000 43.82686  ? 41  CYS   B C    1 
ATOM   3035 O  O    . CYS   B 1 41  ? 22.17159  -15.14984 47.49955  1.000 47.16415  ? 41  CYS   B O    1 
ATOM   3036 C  CB   . CYS   B 1 41  ? 23.45769  -12.87964 49.06376  1.000 40.99549  ? 41  CYS   B CB   1 
ATOM   3037 S  SG   . CYS   B 1 41  ? 23.95199  -11.87098 47.64515  1.000 48.25202  ? 41  CYS   B SG   1 
ATOM   3038 N  N    . ILE   B 1 42  ? 20.93365  -13.40088 46.75970  1.000 41.00601  ? 42  ILE   B N    1 
ATOM   3039 C  CA   . ILE   B 1 42  ? 20.62625  -13.97717 45.43196  1.000 38.88119  ? 42  ILE   B CA   1 
ATOM   3040 C  C    . ILE   B 1 42  ? 21.19051  -12.98748 44.42094  1.000 43.01004  ? 42  ILE   B C    1 
ATOM   3041 O  O    . ILE   B 1 42  ? 20.57241  -11.93796 44.21625  1.000 40.45023  ? 42  ILE   B O    1 
ATOM   3042 C  CB   . ILE   B 1 42  ? 19.11330  -14.16175 45.21373  1.000 42.71527  ? 42  ILE   B CB   1 
ATOM   3043 C  CG1  . ILE   B 1 42  ? 18.48721  -14.98116 46.35535  1.000 43.72623  ? 42  ILE   B CG1  1 
ATOM   3044 C  CG2  . ILE   B 1 42  ? 18.79993  -14.74544 43.77331  1.000 45.21917  ? 42  ILE   B CG2  1 
ATOM   3045 C  CD1  . ILE   B 1 42  ? 18.89161  -16.43191 46.35296  1.000 52.15042  ? 42  ILE   B CD1  1 
ATOM   3046 N  N    . GLN   B 1 43  ? 22.37304  -13.24353 43.81886  1.000 38.28185  ? 43  GLN   B N    1 
ATOM   3047 C  CA   . GLN   B 1 43  ? 23.36002  -14.29907 44.14266  1.000 44.94102  ? 43  GLN   B CA   1 
ATOM   3048 C  C    . GLN   B 1 43  ? 24.71123  -13.65497 44.47338  1.000 45.26777  ? 43  GLN   B C    1 
ATOM   3049 O  O    . GLN   B 1 43  ? 25.01331  -12.56720 43.97703  1.000 39.50299  ? 43  GLN   B O    1 
ATOM   3050 C  CB   . GLN   B 1 43  ? 23.57010  -15.26793 42.95058  1.000 42.83461  ? 43  GLN   B CB   1 
ATOM   3051 C  CG   . GLN   B 1 43  ? 22.27880  -15.94799 42.48452  1.000 46.84361  ? 43  GLN   B CG   1 
ATOM   3052 C  CD   . GLN   B 1 43  ? 21.88755  -17.05730 43.44122  1.000 48.03106  ? 43  GLN   B CD   1 
ATOM   3053 O  OE1  . GLN   B 1 43  ? 22.50043  -17.21368 44.51551  1.000 54.73184  ? 43  GLN   B OE1  1 
ATOM   3054 N  NE2  . GLN   B 1 43  ? 20.89234  -17.83230 43.07139  1.000 50.64186  ? 43  GLN   B NE2  1 
ATOM   3055 N  N    . PRO   B 1 44  ? 25.53290  -14.33834 45.29523  1.000 47.33665  ? 44  PRO   B N    1 
ATOM   3056 C  CA   . PRO   B 1 44  ? 26.84063  -13.76637 45.66305  1.000 44.65813  ? 44  PRO   B CA   1 
ATOM   3057 C  C    . PRO   B 1 44  ? 27.76306  -13.46186 44.49718  1.000 42.76348  ? 44  PRO   B C    1 
ATOM   3058 O  O    . PRO   B 1 44  ? 28.37687  -12.37717 44.48375  1.000 45.34217  ? 44  PRO   B O    1 
ATOM   3059 C  CB   . PRO   B 1 44  ? 27.45336  -14.85334 46.56746  1.000 50.54139  ? 44  PRO   B CB   1 
ATOM   3060 C  CG   . PRO   B 1 44  ? 26.31626  -15.56942 47.14876  1.000 47.00137  ? 44  PRO   B CG   1 
ATOM   3061 C  CD   . PRO   B 1 44  ? 25.20831  -15.53915 46.08308  1.000 47.05960  ? 44  PRO   B CD   1 
ATOM   3062 N  N    . ASP   B 1 45  ? 27.90694  -14.37243 43.51446  1.000 45.85610  ? 45  ASP   B N    1 
ATOM   3063 C  CA   . ASP   B 1 45  ? 28.75312  -14.03877 42.36197  1.000 51.01364  ? 45  ASP   B CA   1 
ATOM   3064 C  C    . ASP   B 1 45  ? 28.22503  -12.84033 41.58883  1.000 50.07864  ? 45  ASP   B C    1 
ATOM   3065 O  O    . ASP   B 1 45  ? 29.01585  -12.08962 40.98336  1.000 46.38250  ? 45  ASP   B O    1 
ATOM   3066 C  CB   . ASP   B 1 45  ? 28.97554  -15.21584 41.40242  1.000 58.23862  ? 45  ASP   B CB   1 
ATOM   3067 C  CG   . ASP   B 1 45  ? 29.63769  -16.43430 42.08185  1.000 76.48687  ? 45  ASP   B CG   1 
ATOM   3068 O  OD1  . ASP   B 1 45  ? 30.73641  -16.27720 42.71530  1.000 80.44364  ? 45  ASP   B OD1  1 
ATOM   3069 O  OD2  . ASP   B 1 45  ? 29.10194  -17.56080 41.89922  1.000 86.51045  ? 45  ASP   B OD2  1 
ATOM   3070 N  N    . GLU   B 1 46  ? 26.89285  -12.66787 41.54240  1.000 43.43350  ? 46  GLU   B N    1 
ATOM   3071 C  CA   . GLU   B 1 46  ? 26.35403  -11.48103 40.89823  1.000 40.81491  ? 46  GLU   B CA   1 
ATOM   3072 C  C    . GLU   B 1 46  ? 26.71521  -10.21613 41.66370  1.000 38.64087  ? 46  GLU   B C    1 
ATOM   3073 O  O    . GLU   B 1 46  ? 26.97866  -9.17801  41.04459  1.000 43.33463  ? 46  GLU   B O    1 
ATOM   3074 C  CB   . GLU   B 1 46  ? 24.83572  -11.62039 40.75741  1.000 40.64917  ? 46  GLU   B CB   1 
ATOM   3075 C  CG   . GLU   B 1 46  ? 24.44533  -12.82621 39.88001  1.000 43.32080  ? 46  GLU   B CG   1 
ATOM   3076 C  CD   . GLU   B 1 46  ? 22.90326  -12.89239 39.68337  1.000 47.49225  ? 46  GLU   B CD   1 
ATOM   3077 O  OE1  . GLU   B 1 46  ? 22.23237  -11.85349 39.90403  1.000 52.42972  ? 46  GLU   B OE1  1 
ATOM   3078 O  OE2  . GLU   B 1 46  ? 22.38463  -13.97300 39.32763  1.000 48.35075  ? 46  GLU   B OE2  1 
ATOM   3079 N  N    . LEU   B 1 47  ? 26.71926  -10.29131 43.00028  1.000 41.66116  ? 47  LEU   B N    1 
ATOM   3080 C  CA   . LEU   B 1 47  ? 27.08236  -9.15042  43.84239  1.000 42.92890  ? 47  LEU   B CA   1 
ATOM   3081 C  C    . LEU   B 1 47  ? 28.53184  -8.75992  43.62734  1.000 41.24229  ? 47  LEU   B C    1 
ATOM   3082 O  O    . LEU   B 1 47  ? 28.84969  -7.56566  43.50308  1.000 45.42943  ? 47  LEU   B O    1 
ATOM   3083 C  CB   . LEU   B 1 47  ? 26.83815  -9.47512  45.31049  1.000 46.52242  ? 47  LEU   B CB   1 
ATOM   3084 C  CG   . LEU   B 1 47  ? 27.16086  -8.35432  46.30298  1.000 44.96436  ? 47  LEU   B CG   1 
ATOM   3085 C  CD1  . LEU   B 1 47  ? 26.46924  -7.05544  45.90754  1.000 46.32647  ? 47  LEU   B CD1  1 
ATOM   3086 C  CD2  . LEU   B 1 47  ? 26.73842  -8.79761  47.69265  1.000 45.76835  ? 47  LEU   B CD2  1 
ATOM   3087 N  N    . ARG   B 1 48  ? 29.41979  -9.76448  43.54762  1.000 43.75157  ? 48  ARG   B N    1 
ATOM   3088 C  CA   . ARG   B 1 48  ? 30.81204  -9.50703  43.15177  1.000 43.72474  ? 48  ARG   B CA   1 
ATOM   3089 C  C    . ARG   B 1 48  ? 30.91244  -8.75371  41.80954  1.000 48.73737  ? 48  ARG   B C    1 
ATOM   3090 O  O    . ARG   B 1 48  ? 31.65357  -7.75998  41.70037  1.000 49.34711  ? 48  ARG   B O    1 
ATOM   3091 C  CB   . ARG   B 1 48  ? 31.57433  -10.84358 43.10790  1.000 47.94881  ? 48  ARG   B CB   1 
ATOM   3092 C  CG   . ARG   B 1 48  ? 33.06591  -10.67532 42.99717  1.000 56.45430  ? 48  ARG   B CG   1 
ATOM   3093 C  CD   . ARG   B 1 48  ? 33.83749  -12.00354 43.20251  1.000 59.62331  ? 48  ARG   B CD   1 
ATOM   3094 N  NE   . ARG   B 1 48  ? 35.17066  -11.70645 43.71958  1.000 66.77107  ? 48  ARG   B NE   1 
ATOM   3095 C  CZ   . ARG   B 1 48  ? 36.02745  -10.91003 43.09301  1.000 75.55202  ? 48  ARG   B CZ   1 
ATOM   3096 N  NH1  . ARG   B 1 48  ? 35.69561  -10.30743 41.95585  1.000 65.11328  ? 48  ARG   B NH1  1 
ATOM   3097 N  NH2  . ARG   B 1 48  ? 37.23244  -10.68544 43.63385  1.000 71.10195  ? 48  ARG   B NH2  1 
ATOM   3098 N  N    . VAL   B 1 49  ? 30.16752  -9.20211  40.76294  1.000 41.64338  ? 49  VAL   B N    1 
ATOM   3099 C  CA   . VAL   B 1 49  ? 30.19319  -8.48990  39.47614  1.000 46.41261  ? 49  VAL   B CA   1 
ATOM   3100 C  C    . VAL   B 1 49  ? 29.71436  -7.03649  39.63531  1.000 50.63432  ? 49  VAL   B C    1 
ATOM   3101 O  O    . VAL   B 1 49  ? 30.30934  -6.10495  39.07480  1.000 52.05856  ? 49  VAL   B O    1 
ATOM   3102 C  CB   . VAL   B 1 49  ? 29.35321  -9.23287  38.40647  1.000 49.94864  ? 49  VAL   B CB   1 
ATOM   3103 C  CG1  . VAL   B 1 49  ? 29.07303  -8.32324  37.25067  1.000 50.88260  ? 49  VAL   B CG1  1 
ATOM   3104 C  CG2  . VAL   B 1 49  ? 30.11279  -10.46386 37.84086  1.000 47.62932  ? 49  VAL   B CG2  1 
ATOM   3105 N  N    . LYS   B 1 50  ? 28.57849  -6.82581  40.31141  1.000 47.74102  ? 50  LYS   B N    1 
ATOM   3106 C  CA   . LYS   B 1 50  ? 28.10874  -5.45058  40.53796  1.000 46.50609  ? 50  LYS   B CA   1 
ATOM   3107 C  C    . LYS   B 1 50  ? 29.22718  -4.57564  41.10539  1.000 55.88442  ? 50  LYS   B C    1 
ATOM   3108 O  O    . LYS   B 1 50  ? 29.50179  -3.46824  40.60950  1.000 54.32857  ? 50  LYS   B O    1 
ATOM   3109 C  CB   . LYS   B 1 50  ? 26.91523  -5.44670  41.48626  1.000 49.88837  ? 50  LYS   B CB   1 
ATOM   3110 C  CG   . LYS   B 1 50  ? 25.69330  -6.10943  40.85094  1.000 47.28454  ? 50  LYS   B CG   1 
ATOM   3111 C  CD   . LYS   B 1 50  ? 24.59207  -5.14529  40.87438  1.000 42.72299  ? 50  LYS   B CD   1 
ATOM   3112 C  CE   . LYS   B 1 50  ? 23.30127  -5.79544  40.40107  1.000 40.27067  ? 50  LYS   B CE   1 
ATOM   3113 N  NZ   . LYS   B 1 50  ? 22.81371  -4.96373  39.27212  1.000 45.17209  ? 50  LYS   B NZ   1 
ATOM   3114 N  N    . LEU   B 1 51  ? 29.91444  -5.08323  42.11745  1.000 44.51773  ? 51  LEU   B N    1 
ATOM   3115 C  CA   . LEU   B 1 51  ? 31.03632  -4.30671  42.65724  1.000 58.96492  ? 51  LEU   B CA   1 
ATOM   3116 C  C    . LEU   B 1 51  ? 32.11023  -4.03591  41.59334  1.000 56.88654  ? 51  LEU   B C    1 
ATOM   3117 O  O    . LEU   B 1 51  ? 32.59602  -2.90001  41.47051  1.000 54.55389  ? 51  LEU   B O    1 
ATOM   3118 C  CB   . LEU   B 1 51  ? 31.64761  -5.04322  43.84296  1.000 49.65009  ? 51  LEU   B CB   1 
ATOM   3119 C  CG   . LEU   B 1 51  ? 30.74067  -5.13826  45.05396  1.000 49.00301  ? 51  LEU   B CG   1 
ATOM   3120 C  CD1  . LEU   B 1 51  ? 31.16033  -6.13846  46.09363  1.000 47.91052  ? 51  LEU   B CD1  1 
ATOM   3121 C  CD2  . LEU   B 1 51  ? 30.40565  -3.76036  45.70525  1.000 53.88385  ? 51  LEU   B CD2  1 
ATOM   3122 N  N    . LEU   B 1 52  ? 32.38759  -4.99549  40.70913  1.000 53.02038  ? 52  LEU   B N    1 
ATOM   3123 C  CA   . LEU   B 1 52  ? 33.47990  -4.57965  39.81802  1.000 56.12174  ? 52  LEU   B CA   1 
ATOM   3124 C  C    . LEU   B 1 52  ? 33.05283  -3.48272  38.84583  1.000 59.91299  ? 52  LEU   B C    1 
ATOM   3125 O  O    . LEU   B 1 52  ? 33.89985  -2.92136  38.16286  1.000 53.89293  ? 52  LEU   B O    1 
ATOM   3126 C  CB   . LEU   B 1 52  ? 34.08675  -5.76881  39.04084  1.000 59.80451  ? 52  LEU   B CB   1 
ATOM   3127 C  CG   . LEU   B 1 52  ? 34.52282  -7.01060  39.84473  1.000 59.45162  ? 52  LEU   B CG   1 
ATOM   3128 C  CD1  . LEU   B 1 52  ? 34.65361  -8.19522  38.86572  1.000 58.05802  ? 52  LEU   B CD1  1 
ATOM   3129 C  CD2  . LEU   B 1 52  ? 35.80066  -6.79994  40.68336  1.000 62.19181  ? 52  LEU   B CD2  1 
ATOM   3130 N  N    . LEU   B 1 53  ? 31.77911  -3.07799  38.85058  1.000 64.43088  ? 53  LEU   B N    1 
ATOM   3131 C  CA   . LEU   B 1 53  ? 31.27216  -2.04415  37.95806  1.000 62.44054  ? 53  LEU   B CA   1 
ATOM   3132 C  C    . LEU   B 1 53  ? 31.90589  -0.68850  38.22321  1.000 73.56033  ? 53  LEU   B C    1 
ATOM   3133 O  O    . LEU   B 1 53  ? 31.69113  0.23357   37.41714  1.000 67.01240  ? 53  LEU   B O    1 
ATOM   3134 C  CB   . LEU   B 1 53  ? 29.77478  -1.92219  38.16167  1.000 64.46846  ? 53  LEU   B CB   1 
ATOM   3135 C  CG   . LEU   B 1 53  ? 29.12561  -3.21377  37.68611  1.000 60.53306  ? 53  LEU   B CG   1 
ATOM   3136 C  CD1  . LEU   B 1 53  ? 27.56484  -3.16792  37.92629  1.000 56.27374  ? 53  LEU   B CD1  1 
ATOM   3137 C  CD2  . LEU   B 1 53  ? 29.60386  -3.58297  36.26153  1.000 52.19562  ? 53  LEU   B CD2  1 
ATOM   3138 N  N    . LYS   B 1 54  ? 32.62566  -0.56023  39.36616  1.000 82.10084  ? 54  LYS   B N    1 
ATOM   3139 C  CA   . LYS   B 1 54  ? 33.43531  0.61123   39.77139  1.000 74.01068  ? 54  LYS   B CA   1 
ATOM   3140 C  C    . LYS   B 1 54  ? 32.57427  1.85286   39.98966  1.000 77.76718  ? 54  LYS   B C    1 
ATOM   3141 O  O    . LYS   B 1 54  ? 32.90504  2.95201   39.53418  1.000 85.28549  ? 54  LYS   B O    1 
ATOM   3142 C  CB   . LYS   B 1 54  ? 34.58482  0.90835   38.78707  1.000 77.06982  ? 54  LYS   B CB   1 
ATOM   3143 C  CG   . LYS   B 1 54  ? 35.70491  -0.12216  38.76512  1.000 76.18800  ? 54  LYS   B CG   1 
ATOM   3144 C  CD   . LYS   B 1 54  ? 36.73458  0.22629   37.69264  1.000 75.86424  ? 54  LYS   B CD   1 
ATOM   3145 C  CE   . LYS   B 1 54  ? 37.92931  -0.71248  37.75417  1.000 83.00738  ? 54  LYS   B CE   1 
ATOM   3146 N  NZ   . LYS   B 1 54  ? 39.08428  -0.31016  36.86798  1.000 87.08589  ? 54  LYS   B NZ   1 
ATOM   3147 N  N    . ARG   B 1 55  ? 31.49054  1.68616   40.75237  1.000 71.01047  ? 55  ARG   B N    1 
ATOM   3148 C  CA   . ARG   B 1 55  ? 30.54274  2.77803   40.88865  1.000 67.50760  ? 55  ARG   B CA   1 
ATOM   3149 C  C    . ARG   B 1 55  ? 29.72504  2.59128   42.16344  1.000 60.32248  ? 55  ARG   B C    1 
ATOM   3150 O  O    . ARG   B 1 55  ? 29.66538  1.49101   42.71915  1.000 67.65223  ? 55  ARG   B O    1 
ATOM   3151 C  CB   . ARG   B 1 55  ? 29.65619  2.80806   39.63550  1.000 63.38350  ? 55  ARG   B CB   1 
ATOM   3152 C  CG   . ARG   B 1 55  ? 28.74374  1.56636   39.47537  1.000 51.58565  ? 55  ARG   B CG   1 
ATOM   3153 C  CD   . ARG   B 1 55  ? 27.64918  1.88863   38.42083  1.000 66.58405  ? 55  ARG   B CD   1 
ATOM   3154 N  NE   . ARG   B 1 55  ? 26.84183  0.72683   38.06799  1.000 60.71607  ? 55  ARG   B NE   1 
ATOM   3155 C  CZ   . ARG   B 1 55  ? 25.77734  0.37545   38.77155  1.000 58.23511  ? 55  ARG   B CZ   1 
ATOM   3156 N  NH1  . ARG   B 1 55  ? 25.43458  1.05236   39.85243  1.000 47.07644  ? 55  ARG   B NH1  1 
ATOM   3157 N  NH2  . ARG   B 1 55  ? 25.04297  -0.66976  38.37663  1.000 50.66590  ? 55  ARG   B NH2  1 
ATOM   3158 N  N    . LYS   B 1 56  ? 29.14012  3.69128   42.66483  1.000 66.61743  ? 56  LYS   B N    1 
ATOM   3159 C  CA   . LYS   B 1 56  ? 28.22388  3.58301   43.80559  1.000 54.04664  ? 56  LYS   B CA   1 
ATOM   3160 C  C    . LYS   B 1 56  ? 27.10217  2.60690   43.44171  1.000 40.61297  ? 56  LYS   B C    1 
ATOM   3161 O  O    . LYS   B 1 56  ? 26.41584  2.83366   42.45746  1.000 47.54852  ? 56  LYS   B O    1 
ATOM   3162 C  CB   . LYS   B 1 56  ? 27.59570  4.95649   44.11451  1.000 60.72868  ? 56  LYS   B CB   1 
ATOM   3163 C  CG   . LYS   B 1 56  ? 28.55574  6.02628   44.56143  1.000 66.43255  ? 56  LYS   B CG   1 
ATOM   3164 C  CD   . LYS   B 1 56  ? 29.01279  5.57894   45.90402  1.000 68.01439  ? 56  LYS   B CD   1 
ATOM   3165 C  CE   . LYS   B 1 56  ? 29.73495  6.55958   46.77170  1.000 67.27447  ? 56  LYS   B CE   1 
ATOM   3166 N  NZ   . LYS   B 1 56  ? 29.63500  5.94126   48.16428  1.000 67.56023  ? 56  LYS   B NZ   1 
ATOM   3167 N  N    . LEU   B 1 57  ? 26.88405  1.56235   44.24964  1.000 43.21361  ? 57  LEU   B N    1 
ATOM   3168 C  CA   . LEU   B 1 57  ? 25.70364  0.72065   44.06064  1.000 36.13410  ? 57  LEU   B CA   1 
ATOM   3169 C  C    . LEU   B 1 57  ? 24.50727  1.35067   44.75062  1.000 40.34140  ? 57  LEU   B C    1 
ATOM   3170 O  O    . LEU   B 1 57  ? 24.63513  1.95057   45.82606  1.000 35.56626  ? 57  LEU   B O    1 
ATOM   3171 C  CB   . LEU   B 1 57  ? 25.91277  -0.69507  44.60495  1.000 41.32714  ? 57  LEU   B CB   1 
ATOM   3172 C  CG   . LEU   B 1 57  ? 27.11365  -1.45055  44.00668  1.000 45.15826  ? 57  LEU   B CG   1 
ATOM   3173 C  CD1  . LEU   B 1 57  ? 27.22747  -2.82869  44.66458  1.000 45.99647  ? 57  LEU   B CD1  1 
ATOM   3174 C  CD2  . LEU   B 1 57  ? 26.94762  -1.56550  42.44605  1.000 41.71998  ? 57  LEU   B CD2  1 
ATOM   3175 N  N    . ILE   B 1 58  ? 23.34572  1.23537   44.11352  1.000 34.53478  ? 58  ILE   B N    1 
ATOM   3176 C  CA   . ILE   B 1 58  ? 22.12081  1.73328   44.70583  1.000 33.73751  ? 58  ILE   B CA   1 
ATOM   3177 C  C    . ILE   B 1 58  ? 21.42143  0.60313   45.44554  1.000 31.55532  ? 58  ILE   B C    1 
ATOM   3178 O  O    . ILE   B 1 58  ? 20.99469  -0.38394  44.82348  1.000 32.30820  ? 58  ILE   B O    1 
ATOM   3179 C  CB   . ILE   B 1 58  ? 21.21573  2.33204   43.63632  1.000 32.98176  ? 58  ILE   B CB   1 
ATOM   3180 C  CG1  . ILE   B 1 58  ? 21.97952  3.48241   42.96811  1.000 38.37936  ? 58  ILE   B CG1  1 
ATOM   3181 C  CG2  . ILE   B 1 58  ? 19.95453  2.84073   44.36710  1.000 32.37375  ? 58  ILE   B CG2  1 
ATOM   3182 C  CD1  . ILE   B 1 58  ? 21.18355  4.13533   41.77529  1.000 47.61496  ? 58  ILE   B CD1  1 
ATOM   3183 N  N    . CYS   B 1 59  ? 21.22352  0.78383   46.75076  1.000 29.49954  ? 59  CYS   B N    1 
ATOM   3184 C  CA   . CYS   B 1 59  ? 20.47480  -0.14414  47.58515  1.000 26.93487  ? 59  CYS   B CA   1 
ATOM   3185 C  C    . CYS   B 1 59  ? 19.14142  0.48762   47.97344  1.000 28.57406  ? 59  CYS   B C    1 
ATOM   3186 O  O    . CYS   B 1 59  ? 19.04315  1.70152   48.08249  1.000 28.69257  ? 59  CYS   B O    1 
ATOM   3187 C  CB   . CYS   B 1 59  ? 21.18931  -0.42998  48.91099  1.000 28.58234  ? 59  CYS   B CB   1 
ATOM   3188 S  SG   . CYS   B 1 59  ? 22.89176  -0.97711  48.56476  1.000 35.59933  ? 59  CYS   B SG   1 
ATOM   3189 N  N    . TYR   B 1 60  ? 18.16576  -0.33183  48.31182  1.000 29.20968  ? 60  TYR   B N    1 
ATOM   3190 C  CA   . TYR   B 1 60  ? 16.96034  0.29187   48.86096  1.000 27.71103  ? 60  TYR   B CA   1 
ATOM   3191 C  C    . TYR   B 1 60  ? 16.20846  -0.66999  49.72933  1.000 25.97571  ? 60  TYR   B C    1 
ATOM   3192 O  O    . TYR   B 1 60  ? 16.34723  -1.89321  49.62964  1.000 28.66542  ? 60  TYR   B O    1 
ATOM   3193 C  CB   . TYR   B 1 60  ? 16.01369  0.84330   47.74946  1.000 30.59194  ? 60  TYR   B CB   1 
ATOM   3194 C  CG   . TYR   B 1 60  ? 14.76901  0.03948   47.39122  1.000 26.57989  ? 60  TYR   B CG   1 
ATOM   3195 C  CD1  . TYR   B 1 60  ? 14.86334  -1.24626  46.77525  1.000 28.42901  ? 60  TYR   B CD1  1 
ATOM   3196 C  CD2  . TYR   B 1 60  ? 13.49283  0.64600   47.45663  1.000 30.10310  ? 60  TYR   B CD2  1 
ATOM   3197 C  CE1  . TYR   B 1 60  ? 13.73579  -1.92690  46.36001  1.000 30.58231  ? 60  TYR   B CE1  1 
ATOM   3198 C  CE2  . TYR   B 1 60  ? 12.35109  -0.06732  47.01146  1.000 31.17909  ? 60  TYR   B CE2  1 
ATOM   3199 C  CZ   . TYR   B 1 60  ? 12.47429  -1.34353  46.46849  1.000 32.19623  ? 60  TYR   B CZ   1 
ATOM   3200 O  OH   . TYR   B 1 60  ? 11.47690  -2.31106  46.06482  1.000 31.04963  ? 60  TYR   B OH   1 
ATOM   3201 N  N    . ASP   B 1 61  ? 15.35289  -0.06791  50.54326  1.000 24.32503  ? 61  ASP   B N    1 
ATOM   3202 C  CA   . ASP   B 1 61  ? 14.36065  -0.76902  51.33910  1.000 28.14340  ? 61  ASP   B CA   1 
ATOM   3203 C  C    . ASP   B 1 61  ? 13.15782  0.15487   51.32147  1.000 30.29307  ? 61  ASP   B C    1 
ATOM   3204 O  O    . ASP   B 1 61  ? 13.28608  1.36020   51.08333  1.000 29.21122  ? 61  ASP   B O    1 
ATOM   3205 C  CB   . ASP   B 1 61  ? 14.85736  -0.99609  52.79305  1.000 29.80881  ? 61  ASP   B CB   1 
ATOM   3206 C  CG   . ASP   B 1 61  ? 14.06268  -2.04606  53.60002  1.000 33.35757  ? 61  ASP   B CG   1 
ATOM   3207 O  OD1  . ASP   B 1 61  ? 12.94811  -2.48620  53.19497  1.000 31.48488  ? 61  ASP   B OD1  1 
ATOM   3208 O  OD2  . ASP   B 1 61  ? 14.57804  -2.44072  54.73116  1.000 29.71265  ? 61  ASP   B OD2  1 
ATOM   3209 N  N    . GLY   B 1 62  ? 11.98982  -0.39231  51.56728  1.000 28.42221  ? 62  GLY   B N    1 
ATOM   3210 C  CA   . GLY   B 1 62  ? 10.81092  0.45327   51.56933  1.000 28.28406  ? 62  GLY   B CA   1 
ATOM   3211 C  C    . GLY   B 1 62  ? 9.90777   0.10754   52.71470  1.000 27.02807  ? 62  GLY   B C    1 
ATOM   3212 O  O    . GLY   B 1 62  ? 9.90994   -1.02413  53.22850  1.000 27.63880  ? 62  GLY   B O    1 
ATOM   3213 N  N    . PHE   B 1 63  ? 9.04905   1.08897   53.06344  1.000 27.00787  ? 63  PHE   B N    1 
ATOM   3214 C  CA   . PHE   B 1 63  ? 8.32856   1.08559   54.32184  1.000 25.95177  ? 63  PHE   B CA   1 
ATOM   3215 C  C    . PHE   B 1 63  ? 6.93693   1.67063   54.15463  1.000 26.14902  ? 63  PHE   B C    1 
ATOM   3216 O  O    . PHE   B 1 63  ? 6.82490   2.83031   53.75192  1.000 30.69239  ? 63  PHE   B O    1 
ATOM   3217 C  CB   . PHE   B 1 63  ? 9.04065   1.95729   55.34801  1.000 28.19722  ? 63  PHE   B CB   1 
ATOM   3218 C  CG   . PHE   B 1 63  ? 10.50512  1.59908   55.51632  1.000 29.06012  ? 63  PHE   B CG   1 
ATOM   3219 C  CD1  . PHE   B 1 63  ? 11.40147  2.02970   54.58681  1.000 27.10755  ? 63  PHE   B CD1  1 
ATOM   3220 C  CD2  . PHE   B 1 63  ? 10.90962  0.75757   56.58093  1.000 34.21460  ? 63  PHE   B CD2  1 
ATOM   3221 C  CE1  . PHE   B 1 63  ? 12.80835  1.68869   54.70381  1.000 30.01557  ? 63  PHE   B CE1  1 
ATOM   3222 C  CE2  . PHE   B 1 63  ? 12.26743  0.37867   56.69391  1.000 31.00004  ? 63  PHE   B CE2  1 
ATOM   3223 C  CZ   . PHE   B 1 63  ? 13.22538  0.88393   55.75882  1.000 30.04715  ? 63  PHE   B CZ   1 
ATOM   3224 N  N    . GLU   B 1 64  ? 5.91858   0.93088   54.58492  1.000 28.54293  ? 64  GLU   B N    1 
ATOM   3225 C  CA   . GLU   B 1 64  ? 4.56249   1.50424   54.68962  1.000 34.77510  ? 64  GLU   B CA   1 
ATOM   3226 C  C    . GLU   B 1 64  ? 4.46293   2.37008   55.94455  1.000 35.67811  ? 64  GLU   B C    1 
ATOM   3227 O  O    . GLU   B 1 64  ? 4.73305   1.87939   57.05541  1.000 30.93228  ? 64  GLU   B O    1 
ATOM   3228 C  CB   . GLU   B 1 64  ? 3.51514   0.38779   54.79687  1.000 31.04445  ? 64  GLU   B CB   1 
ATOM   3229 C  CG   . GLU   B 1 64  ? 3.32392   -0.42616  53.48887  1.000 33.56452  ? 64  GLU   B CG   1 
ATOM   3230 C  CD   . GLU   B 1 64  ? 2.22914   -1.49845  53.68006  1.000 40.78488  ? 64  GLU   B CD   1 
ATOM   3231 O  OE1  . GLU   B 1 64  ? 1.37414   -1.27765  54.56444  1.000 41.07950  ? 64  GLU   B OE1  1 
ATOM   3232 O  OE2  . GLU   B 1 64  ? 2.24079   -2.55457  52.99888  1.000 38.71571  ? 64  GLU   B OE2  1 
ATOM   3233 N  N    . PRO   B 1 65  ? 4.04251   3.65410   55.83478  1.000 29.14733  ? 65  PRO   B N    1 
ATOM   3234 C  CA   . PRO   B 1 65  ? 3.79885   4.40271   57.07167  1.000 32.45035  ? 65  PRO   B CA   1 
ATOM   3235 C  C    . PRO   B 1 65  ? 2.49085   3.97113   57.69689  1.000 37.54609  ? 65  PRO   B C    1 
ATOM   3236 O  O    . PRO   B 1 65  ? 1.45524   4.53428   57.36792  1.000 38.49045  ? 65  PRO   B O    1 
ATOM   3237 C  CB   . PRO   B 1 65  ? 3.78512   5.86556   56.61734  1.000 32.43370  ? 65  PRO   B CB   1 
ATOM   3238 C  CG   . PRO   B 1 65  ? 4.47986   5.85185   55.25805  1.000 32.42973  ? 65  PRO   B CG   1 
ATOM   3239 C  CD   . PRO   B 1 65  ? 4.03085   4.50990   54.63470  1.000 29.89486  ? 65  PRO   B CD   1 
ATOM   3240 N  N    . SER   B 1 66  ? 2.53159   2.98376   58.58459  1.000 36.56078  ? 66  SER   B N    1 
ATOM   3241 C  CA   . SER   B 1 66  ? 1.34995   2.31599   59.12286  1.000 39.34211  ? 66  SER   B CA   1 
ATOM   3242 C  C    . SER   B 1 66  ? 1.15527   2.52471   60.62199  1.000 42.27866  ? 66  SER   B C    1 
ATOM   3243 O  O    . SER   B 1 66  ? 0.11782   2.09541   61.18291  1.000 41.08001  ? 66  SER   B O    1 
ATOM   3244 C  CB   . SER   B 1 66  ? 1.44815   0.81582   58.82144  1.000 41.32312  ? 66  SER   B CB   1 
ATOM   3245 O  OG   . SER   B 1 66  ? 2.72170   0.34595   59.30339  1.000 49.23204  ? 66  SER   B OG   1 
ATOM   3246 N  N    . GLY   B 1 67  ? 2.10412   3.15987   61.29963  1.000 33.97147  ? 67  GLY   B N    1 
ATOM   3247 C  CA   . GLY   B 1 67  ? 1.96643   3.44040   62.71520  1.000 33.13979  ? 67  GLY   B CA   1 
ATOM   3248 C  C    . GLY   B 1 67  ? 3.35904   3.68271   63.27504  1.000 28.01338  ? 67  GLY   B C    1 
ATOM   3249 O  O    . GLY   B 1 67  ? 4.32079   3.86792   62.51193  1.000 35.23534  ? 67  GLY   B O    1 
ATOM   3250 N  N    . ARG   B 1 68  ? 3.45726   3.64962   64.59653  1.000 34.07878  ? 68  ARG   B N    1 
ATOM   3251 C  CA   . ARG   B 1 68  ? 4.79610   3.92758   65.15680  1.000 37.61152  ? 68  ARG   B CA   1 
ATOM   3252 C  C    . ARG   B 1 68  ? 5.79780   2.89264   64.66624  1.000 36.98541  ? 68  ARG   B C    1 
ATOM   3253 O  O    . ARG   B 1 68  ? 5.45261   1.73958   64.41378  1.000 36.70846  ? 68  ARG   B O    1 
ATOM   3254 C  CB   . ARG   B 1 68  ? 4.72118   3.98302   66.67629  1.000 37.87238  ? 68  ARG   B CB   1 
ATOM   3255 C  CG   . ARG   B 1 68  ? 4.00693   5.22567   67.18858  1.000 46.13105  ? 68  ARG   B CG   1 
ATOM   3256 C  CD   . ARG   B 1 68  ? 3.38381   4.93775   68.53982  1.000 51.15450  ? 68  ARG   B CD   1 
ATOM   3257 N  NE   . ARG   B 1 68  ? 4.42692   4.95218   69.53907  1.000 53.23169  ? 68  ARG   B NE   1 
ATOM   3258 C  CZ   . ARG   B 1 68  ? 4.33606   4.44342   70.75979  1.000 57.74734  ? 68  ARG   B CZ   1 
ATOM   3259 N  NH1  . ARG   B 1 68  ? 3.22003   3.86509   71.19686  1.000 54.00768  ? 68  ARG   B NH1  1 
ATOM   3260 N  NH2  . ARG   B 1 68  ? 5.39003   4.53451   71.57025  1.000 48.07651  ? 68  ARG   B NH2  1 
ATOM   3261 N  N    . MET   B 1 69  ? 7.09346   3.28306   64.59363  1.000 34.84654  ? 69  MET   B N    1 
ATOM   3262 C  CA   . MET   B 1 69  ? 8.06670   2.41944   63.95349  1.000 28.34720  ? 69  MET   B CA   1 
ATOM   3263 C  C    . MET   B 1 69  ? 8.57400   1.31896   64.89828  1.000 31.29923  ? 69  MET   B C    1 
ATOM   3264 O  O    . MET   B 1 69  ? 9.01223   1.60423   66.00228  1.000 33.22606  ? 69  MET   B O    1 
ATOM   3265 C  CB   . MET   B 1 69  ? 9.24789   3.25902   63.45132  1.000 29.47701  ? 69  MET   B CB   1 
ATOM   3266 C  CG   . MET   B 1 69  ? 10.21735  2.39699   62.68489  1.000 31.65095  ? 69  MET   B CG   1 
ATOM   3267 S  SD   . MET   B 1 69  ? 11.70842  3.34918   62.26507  1.000 31.55478  ? 69  MET   B SD   1 
ATOM   3268 C  CE   . MET   B 1 69  ? 11.03196  4.68229   61.24307  1.000 33.70443  ? 69  MET   B CE   1 
ATOM   3269 N  N    . HIS   B 1 70  ? 8.50108   0.06081   64.46057  1.000 31.47392  ? 70  HIS   B N    1 
ATOM   3270 C  CA   . HIS   B 1 70  ? 9.05495   -1.04757  65.23407  1.000 34.06662  ? 70  HIS   B CA   1 
ATOM   3271 C  C    . HIS   B 1 70  ? 10.58206  -0.96416  65.21225  1.000 29.28545  ? 70  HIS   B C    1 
ATOM   3272 O  O    . HIS   B 1 70  ? 11.17393  -0.49496  64.23090  1.000 30.46343  ? 70  HIS   B O    1 
ATOM   3273 C  CB   . HIS   B 1 70  ? 8.60017   -2.39949  64.68006  1.000 34.85946  ? 70  HIS   B CB   1 
ATOM   3274 C  CG   . HIS   B 1 70  ? 7.14051   -2.66398  64.91697  1.000 36.72549  ? 70  HIS   B CG   1 
ATOM   3275 N  ND1  . HIS   B 1 70  ? 6.61710   -3.93117  65.06216  1.000 41.69675  ? 70  HIS   B ND1  1 
ATOM   3276 C  CD2  . HIS   B 1 70  ? 6.09358   -1.81057  65.03600  1.000 39.70001  ? 70  HIS   B CD2  1 
ATOM   3277 C  CE1  . HIS   B 1 70  ? 5.30236   -3.84947  65.26125  1.000 40.33766  ? 70  HIS   B CE1  1 
ATOM   3278 N  NE2  . HIS   B 1 70  ? 4.96596   -2.57080  65.27916  1.000 38.89398  ? 70  HIS   B NE2  1 
ATOM   3279 N  N    . ILE   B 1 71  ? 11.22282  -1.40778  66.30157  1.000 32.26362  ? 71  ILE   B N    1 
ATOM   3280 C  CA   . ILE   B 1 71  ? 12.68587  -1.24890  66.31476  1.000 32.48516  ? 71  ILE   B CA   1 
ATOM   3281 C  C    . ILE   B 1 71  ? 13.36441  -1.98321  65.17531  1.000 32.23823  ? 71  ILE   B C    1 
ATOM   3282 O  O    . ILE   B 1 71  ? 14.48912  -1.60941  64.79421  1.000 30.29350  ? 71  ILE   B O    1 
ATOM   3283 C  CB   . ILE   B 1 71  ? 13.33632  -1.65577  67.66932  1.000 31.61852  ? 71  ILE   B CB   1 
ATOM   3284 C  CG1  . ILE   B 1 71  ? 12.99590  -3.08425  68.04431  1.000 33.09193  ? 71  ILE   B CG1  1 
ATOM   3285 C  CG2  . ILE   B 1 71  ? 12.94836  -0.69033  68.81836  1.000 35.78380  ? 71  ILE   B CG2  1 
ATOM   3286 C  CD1  . ILE   B 1 71  ? 13.68597  -3.37720  69.46091  1.000 34.26582  ? 71  ILE   B CD1  1 
ATOM   3287 N  N    . ALA   B 1 72  ? 12.73310  -3.02339  64.58960  1.000 30.44891  ? 72  ALA   B N    1 
ATOM   3288 C  CA   . ALA   B 1 72  ? 13.36095  -3.66473  63.41793  1.000 31.99495  ? 72  ALA   B CA   1 
ATOM   3289 C  C    . ALA   B 1 72  ? 13.67538  -2.66556  62.30273  1.000 32.70950  ? 72  ALA   B C    1 
ATOM   3290 O  O    . ALA   B 1 72  ? 14.67741  -2.80869  61.59774  1.000 30.65765  ? 72  ALA   B O    1 
ATOM   3291 C  CB   . ALA   B 1 72  ? 12.45752  -4.78411  62.85288  1.000 32.80143  ? 72  ALA   B CB   1 
ATOM   3292 N  N    . GLN   B 1 73  ? 12.82342  -1.65131  62.10439  1.000 29.87144  ? 73  GLN   B N    1 
ATOM   3293 C  CA   . GLN   B 1 73  ? 12.98286  -0.74563  60.98066  1.000 26.98169  ? 73  GLN   B CA   1 
ATOM   3294 C  C    . GLN   B 1 73  ? 13.84718  0.46490   61.29493  1.000 31.68881  ? 73  GLN   B C    1 
ATOM   3295 O  O    . GLN   B 1 73  ? 14.08087  1.27346   60.38047  1.000 29.22506  ? 73  GLN   B O    1 
ATOM   3296 C  CB   . GLN   B 1 73  ? 11.57736  -0.29131  60.45858  1.000 28.23942  ? 73  GLN   B CB   1 
ATOM   3297 C  CG   . GLN   B 1 73  ? 10.77338  -1.51662  60.00509  1.000 31.31808  ? 73  GLN   B CG   1 
ATOM   3298 C  CD   . GLN   B 1 73  ? 9.35442   -1.11860  59.72796  1.000 39.25877  ? 73  GLN   B CD   1 
ATOM   3299 O  OE1  . GLN   B 1 73  ? 8.94883   -0.02258  60.10988  1.000 37.18035  ? 73  GLN   B OE1  1 
ATOM   3300 N  NE2  . GLN   B 1 73  ? 8.56786   -2.02708  59.12722  1.000 35.60699  ? 73  GLN   B NE2  1 
ATOM   3301 N  N    . GLY   B 1 74  ? 14.31253  0.60431   62.56242  1.000 31.54145  ? 74  GLY   B N    1 
ATOM   3302 C  CA   . GLY   B 1 74  ? 15.16098  1.70522   62.98686  1.000 30.81279  ? 74  GLY   B CA   1 
ATOM   3303 C  C    . GLY   B 1 74  ? 16.53054  1.19784   63.44924  1.000 31.62577  ? 74  GLY   B C    1 
ATOM   3304 O  O    . GLY   B 1 74  ? 17.54503  1.32823   62.72888  1.000 28.91526  ? 74  GLY   B O    1 
ATOM   3305 N  N    . LEU   B 1 75  ? 16.53107  0.53082   64.60938  1.000 25.65506  ? 75  LEU   B N    1 
ATOM   3306 C  CA   . LEU   B 1 75  ? 17.81620  0.08213   65.21267  1.000 27.79393  ? 75  LEU   B CA   1 
ATOM   3307 C  C    . LEU   B 1 75  ? 18.46843  -0.99392  64.35927  1.000 33.51170  ? 75  LEU   B C    1 
ATOM   3308 O  O    . LEU   B 1 75  ? 19.67803  -0.94305  64.05530  1.000 31.60970  ? 75  LEU   B O    1 
ATOM   3309 C  CB   . LEU   B 1 75  ? 17.55916  -0.45929  66.60787  1.000 28.25117  ? 75  LEU   B CB   1 
ATOM   3310 C  CG   . LEU   B 1 75  ? 17.13530  0.51855   67.71087  1.000 32.15584  ? 75  LEU   B CG   1 
ATOM   3311 C  CD1  . LEU   B 1 75  ? 17.05541  -0.28900  68.97087  1.000 31.12296  ? 75  LEU   B CD1  1 
ATOM   3312 C  CD2  . LEU   B 1 75  ? 18.17872  1.75510   67.83784  1.000 32.04390  ? 75  LEU   B CD2  1 
ATOM   3313 N  N    . LEU   B 1 76  ? 17.69584  -2.02627  63.98290  1.000 28.00222  ? 76  LEU   B N    1 
ATOM   3314 C  CA   . LEU   B 1 76  ? 18.29136  -3.05332  63.12272  1.000 26.35781  ? 76  LEU   B CA   1 
ATOM   3315 C  C    . LEU   B 1 76  ? 18.64913  -2.48490  61.74950  1.000 31.98671  ? 76  LEU   B C    1 
ATOM   3316 O  O    . LEU   B 1 76  ? 19.76269  -2.69001  61.25217  1.000 30.07279  ? 76  LEU   B O    1 
ATOM   3317 C  CB   . LEU   B 1 76  ? 17.34013  -4.25408  62.96523  1.000 32.44557  ? 76  LEU   B CB   1 
ATOM   3318 C  CG   . LEU   B 1 76  ? 17.80826  -5.29862  61.91755  1.000 31.44426  ? 76  LEU   B CG   1 
ATOM   3319 C  CD1  . LEU   B 1 76  ? 18.97773  -6.17185  62.55131  1.000 35.45163  ? 76  LEU   B CD1  1 
ATOM   3320 C  CD2  . LEU   B 1 76  ? 16.62210  -6.25754  61.53908  1.000 32.82826  ? 76  LEU   B CD2  1 
ATOM   3321 N  N    . LYS   B 1 77  ? 17.71640  -1.75152  61.10242  1.000 30.08080  ? 77  LYS   B N    1 
ATOM   3322 C  CA   . LYS   B 1 77  ? 17.99494  -1.16833  59.78071  1.000 31.04457  ? 77  LYS   B CA   1 
ATOM   3323 C  C    . LYS   B 1 77  ? 19.30505  -0.33688  59.77181  1.000 31.51609  ? 77  LYS   B C    1 
ATOM   3324 O  O    . LYS   B 1 77  ? 20.06887  -0.37617  58.79415  1.000 29.58720  ? 77  LYS   B O    1 
ATOM   3325 C  CB   . LYS   B 1 77  ? 16.80532  -0.28293  59.35068  1.000 31.98327  ? 77  LYS   B CB   1 
ATOM   3326 C  CG   . LYS   B 1 77  ? 16.90258  0.36572   57.90209  1.000 33.93180  ? 77  LYS   B CG   1 
ATOM   3327 C  CD   . LYS   B 1 77  ? 17.06828  -0.57216  56.67163  1.000 38.45213  ? 77  LYS   B CD   1 
ATOM   3328 C  CE   . LYS   B 1 77  ? 16.44989  -1.86171  56.89130  1.000 43.55771  ? 77  LYS   B CE   1 
ATOM   3329 N  NZ   . LYS   B 1 77  ? 17.07383  -2.70790  55.84993  1.000 32.12910  ? 77  LYS   B NZ   1 
ATOM   3330 N  N    . SER   B 1 78  ? 19.54819  0.43761   60.81928  1.000 32.91931  ? 78  SER   B N    1 
ATOM   3331 C  CA   . SER   B 1 78  ? 20.70048  1.36476   60.82248  1.000 33.74682  ? 78  SER   B CA   1 
ATOM   3332 C  C    . SER   B 1 78  ? 22.03254  0.61840   60.75312  1.000 32.00811  ? 78  SER   B C    1 
ATOM   3333 O  O    . SER   B 1 78  ? 23.00276  1.11265   60.14333  1.000 30.73399  ? 78  SER   B O    1 
ATOM   3334 C  CB   . SER   B 1 78  ? 20.66087  2.23934   62.08457  1.000 39.53739  ? 78  SER   B CB   1 
ATOM   3335 O  OG   . SER   B 1 78  ? 21.66824  3.26062   62.03413  1.000 42.71689  ? 78  SER   B OG   1 
ATOM   3336 N  N    . ILE   B 1 79  ? 22.09068  -0.57609  61.33482  1.000 30.03283  ? 79  ILE   B N    1 
ATOM   3337 C  CA   . ILE   B 1 79  ? 23.33044  -1.37008  61.29480  1.000 31.20973  ? 79  ILE   B CA   1 
ATOM   3338 C  C    . ILE   B 1 79  ? 23.67429  -1.77100  59.86426  1.000 35.18950  ? 79  ILE   B C    1 
ATOM   3339 O  O    . ILE   B 1 79  ? 24.80574  -1.56741  59.39026  1.000 31.19710  ? 79  ILE   B O    1 
ATOM   3340 C  CB   . ILE   B 1 79  ? 23.18086  -2.58189  62.23512  1.000 33.65766  ? 79  ILE   B CB   1 
ATOM   3341 C  CG1  . ILE   B 1 79  ? 23.15876  -2.11052  63.68182  1.000 34.99212  ? 79  ILE   B CG1  1 
ATOM   3342 C  CG2  . ILE   B 1 79  ? 24.17643  -3.66621  61.91944  1.000 32.83529  ? 79  ILE   B CG2  1 
ATOM   3343 C  CD1  . ILE   B 1 79  ? 22.42887  -3.06824  64.54361  1.000 32.46620  ? 79  ILE   B CD1  1 
ATOM   3344 N  N    . ILE   B 1 80  ? 22.67354  -2.30880  59.12431  1.000 30.65845  ? 80  ILE   B N    1 
ATOM   3345 C  CA   . ILE   B 1 80  ? 22.89518  -2.75699  57.75861  1.000 30.72987  ? 80  ILE   B CA   1 
ATOM   3346 C  C    . ILE   B 1 80  ? 23.18820  -1.56194  56.86861  1.000 29.02221  ? 80  ILE   B C    1 
ATOM   3347 O  O    . ILE   B 1 80  ? 24.07780  -1.60123  56.00096  1.000 32.27316  ? 80  ILE   B O    1 
ATOM   3348 C  CB   . ILE   B 1 80  ? 21.63932  -3.53054  57.27528  1.000 45.13196  ? 80  ILE   B CB   1 
ATOM   3349 C  CG1  . ILE   B 1 80  ? 21.32352  -4.64284  58.30323  1.000 43.90034  ? 80  ILE   B CG1  1 
ATOM   3350 C  CG2  . ILE   B 1 80  ? 21.91861  -4.08728  55.82989  1.000 44.04063  ? 80  ILE   B CG2  1 
ATOM   3351 C  CD1  . ILE   B 1 80  ? 19.88774  -5.27466  58.36810  1.000 41.20010  ? 80  ILE   B CD1  1 
ATOM   3352 N  N    . VAL   B 1 81  ? 22.41573  -0.48224  57.04456  1.000 27.47551  ? 81  VAL   B N    1 
ATOM   3353 C  CA   . VAL   B 1 81  ? 22.58350  0.65672   56.15959  1.000 27.77499  ? 81  VAL   B CA   1 
ATOM   3354 C  C    . VAL   B 1 81  ? 23.96655  1.25135   56.33767  1.000 28.75828  ? 81  VAL   B C    1 
ATOM   3355 O  O    . VAL   B 1 81  ? 24.64288  1.53854   55.35982  1.000 29.61326  ? 81  VAL   B O    1 
ATOM   3356 C  CB   . VAL   B 1 81  ? 21.48899  1.70936   56.40797  1.000 31.29971  ? 81  VAL   B CB   1 
ATOM   3357 C  CG1  . VAL   B 1 81  ? 21.86483  3.02088   55.71142  1.000 27.55345  ? 81  VAL   B CG1  1 
ATOM   3358 C  CG2  . VAL   B 1 81  ? 20.12744  1.11486   55.93776  1.000 30.18089  ? 81  VAL   B CG2  1 
ATOM   3359 N  N    . ASN   B 1 82  ? 24.41096  1.46619   57.59638  1.000 27.85864  ? 82  ASN   B N    1 
ATOM   3360 C  CA   . ASN   B 1 82  ? 25.75641  2.05559   57.77083  1.000 27.61321  ? 82  ASN   B CA   1 
ATOM   3361 C  C    . ASN   B 1 82  ? 26.84827  1.13194   57.25670  1.000 28.89474  ? 82  ASN   B C    1 
ATOM   3362 O  O    . ASN   B 1 82  ? 27.88588  1.59448   56.75346  1.000 31.49080  ? 82  ASN   B O    1 
ATOM   3363 C  CB   . ASN   B 1 82  ? 25.98713  2.42254   59.25300  1.000 26.93188  ? 82  ASN   B CB   1 
ATOM   3364 C  CG   . ASN   B 1 82  ? 25.35436  3.76220   59.57108  1.000 35.23759  ? 82  ASN   B CG   1 
ATOM   3365 O  OD1  . ASN   B 1 82  ? 25.94100  4.79318   59.24872  1.000 29.86424  ? 82  ASN   B OD1  1 
ATOM   3366 N  ND2  . ASN   B 1 82  ? 24.11532  3.76389   60.14127  1.000 30.66281  ? 82  ASN   B ND2  1 
ATOM   3367 N  N    . LYS   B 1 83  ? 26.67302  -0.17498  57.41739  1.000 31.86455  ? 83  LYS   B N    1 
ATOM   3368 C  CA   . LYS   B 1 83  ? 27.66581  -1.08678  56.83197  1.000 33.59515  ? 83  LYS   B CA   1 
ATOM   3369 C  C    . LYS   B 1 83  ? 27.75948  -0.89205  55.32235  1.000 34.75588  ? 83  LYS   B C    1 
ATOM   3370 O  O    . LYS   B 1 83  ? 28.85422  -0.87293  54.74530  1.000 32.20255  ? 83  LYS   B O    1 
ATOM   3371 C  CB   . LYS   B 1 83  ? 27.32275  -2.54361  57.18238  1.000 37.18286  ? 83  LYS   B CB   1 
ATOM   3372 C  CG   . LYS   B 1 83  ? 28.37809  -3.62409  56.82161  1.000 43.66885  ? 83  LYS   B CG   1 
ATOM   3373 C  CD   . LYS   B 1 83  ? 28.73308  -4.47164  58.09374  1.000 61.53538  ? 83  LYS   B CD   1 
ATOM   3374 C  CE   . LYS   B 1 83  ? 30.23909  -4.83690  58.22152  1.000 62.62315  ? 83  LYS   B CE   1 
ATOM   3375 N  NZ   . LYS   B 1 83  ? 30.64796  -5.07077  59.68635  1.000 66.17159  ? 83  LYS   B NZ   1 
ATOM   3376 N  N    . LEU   B 1 84  ? 26.59593  -0.80490  54.63619  1.000 31.09668  ? 84  LEU   B N    1 
ATOM   3377 C  CA   . LEU   B 1 84  ? 26.62359  -0.73073  53.18934  1.000 31.18325  ? 84  LEU   B CA   1 
ATOM   3378 C  C    . LEU   B 1 84  ? 27.11366  0.62493   52.71360  1.000 32.43962  ? 84  LEU   B C    1 
ATOM   3379 O  O    . LEU   B 1 84  ? 27.96988  0.69732   51.83045  1.000 35.98577  ? 84  LEU   B O    1 
ATOM   3380 C  CB   . LEU   B 1 84  ? 25.21664  -1.02412  52.60682  1.000 33.71814  ? 84  LEU   B CB   1 
ATOM   3381 C  CG   . LEU   B 1 84  ? 24.78519  -2.46533  52.84122  1.000 34.11202  ? 84  LEU   B CG   1 
ATOM   3382 C  CD1  . LEU   B 1 84  ? 23.25217  -2.63243  52.47870  1.000 35.17752  ? 84  LEU   B CD1  1 
ATOM   3383 C  CD2  . LEU   B 1 84  ? 25.62728  -3.38508  52.03695  1.000 40.72477  ? 84  LEU   B CD2  1 
ATOM   3384 N  N    . THR   B 1 85  ? 26.62027  1.71598   53.32394  1.000 32.79492  ? 85  THR   B N    1 
ATOM   3385 C  CA   . THR   B 1 85  ? 27.01602  3.02766   52.82933  1.000 30.88196  ? 85  THR   B CA   1 
ATOM   3386 C  C    . THR   B 1 85  ? 28.48185  3.30672   53.12500  1.000 39.60572  ? 85  THR   B C    1 
ATOM   3387 O  O    . THR   B 1 85  ? 29.13454  4.03096   52.35722  1.000 39.31980  ? 85  THR   B O    1 
ATOM   3388 C  CB   . THR   B 1 85  ? 26.17571  4.14710   53.46099  1.000 33.11728  ? 85  THR   B CB   1 
ATOM   3389 O  OG1  . THR   B 1 85  ? 26.35818  4.16333   54.89875  1.000 38.75746  ? 85  THR   B OG1  1 
ATOM   3390 C  CG2  . THR   B 1 85  ? 24.71742  3.94926   53.13690  1.000 30.30519  ? 85  THR   B CG2  1 
ATOM   3391 N  N    . SER   B 1 86  ? 29.04080  2.69832   54.18112  1.000 36.38527  ? 86  SER   B N    1 
ATOM   3392 C  CA   . SER   B 1 86  ? 30.42798  3.04968   54.48469  1.000 35.77860  ? 86  SER   B CA   1 
ATOM   3393 C  C    . SER   B 1 86  ? 31.36092  2.38742   53.47914  1.000 48.72025  ? 86  SER   B C    1 
ATOM   3394 O  O    . SER   B 1 86  ? 32.48502  2.86028   53.27118  1.000 48.92067  ? 86  SER   B O    1 
ATOM   3395 C  CB   . SER   B 1 86  ? 30.76331  2.61803   55.92360  1.000 40.83143  ? 86  SER   B CB   1 
ATOM   3396 O  OG   . SER   B 1 86  ? 30.79450  1.19658   56.00831  1.000 45.14022  ? 86  SER   B OG   1 
ATOM   3397 N  N    . ASN   B 1 87  ? 30.82850  1.40367   52.74715  1.000 46.86868  ? 87  ASN   B N    1 
ATOM   3398 C  CA   . ASN   B 1 87  ? 31.51496  0.61269   51.74082  1.000 49.57633  ? 87  ASN   B CA   1 
ATOM   3399 C  C    . ASN   B 1 87  ? 31.12837  1.07807   50.35609  1.000 53.18729  ? 87  ASN   B C    1 
ATOM   3400 O  O    . ASN   B 1 87  ? 31.06756  0.27143   49.42479  1.000 56.85541  ? 87  ASN   B O    1 
ATOM   3401 C  CB   . ASN   B 1 87  ? 31.16236  -0.87828  51.92524  1.000 45.89451  ? 87  ASN   B CB   1 
ATOM   3402 C  CG   . ASN   B 1 87  ? 31.99146  -1.55013  53.02566  1.000 57.13457  ? 87  ASN   B CG   1 
ATOM   3403 O  OD1  . ASN   B 1 87  ? 33.19126  -1.65551  52.87367  1.000 59.32457  ? 87  ASN   B OD1  1 
ATOM   3404 N  ND2  . ASN   B 1 87  ? 31.35267  -2.01316  54.12812  1.000 51.20834  ? 87  ASN   B ND2  1 
ATOM   3405 N  N    . GLY   B 1 88  ? 30.79978  2.37101   50.24654  1.000 49.62567  ? 88  GLY   B N    1 
ATOM   3406 C  CA   . GLY   B 1 88  ? 30.61712  3.07333   49.01396  1.000 49.46802  ? 88  GLY   B CA   1 
ATOM   3407 C  C    . GLY   B 1 88  ? 29.22811  3.04185   48.39711  1.000 48.14029  ? 88  GLY   B C    1 
ATOM   3408 O  O    . GLY   B 1 88  ? 29.08394  3.54039   47.28885  1.000 56.04684  ? 88  GLY   B O    1 
ATOM   3409 N  N    . CYS   B 1 89  ? 28.19374  2.58015   49.09274  1.000 44.26068  ? 89  CYS   B N    1 
ATOM   3410 C  CA   . CYS   B 1 89  ? 26.86464  2.47632   48.48181  1.000 40.79515  ? 89  CYS   B CA   1 
ATOM   3411 C  C    . CYS   B 1 89  ? 25.99373  3.66020   48.86414  1.000 42.99051  ? 89  CYS   B C    1 
ATOM   3412 O  O    . CYS   B 1 89  ? 26.22614  4.34641   49.86311  1.000 41.64784  ? 89  CYS   B O    1 
ATOM   3413 C  CB   . CYS   B 1 89  ? 26.11567  1.21216   48.92956  1.000 40.69547  ? 89  CYS   B CB   1 
ATOM   3414 S  SG   . CYS   B 1 89  ? 26.87545  -0.36301  48.53218  1.000 53.37371  ? 89  CYS   B SG   1 
ATOM   3415 N  N    . THR   B 1 90  ? 24.95833  3.88273   48.05963  1.000 35.93035  ? 90  THR   B N    1 
ATOM   3416 C  CA   . THR   B 1 90  ? 23.93276  4.82821   48.43226  1.000 35.35558  ? 90  THR   B CA   1 
ATOM   3417 C  C    . THR   B 1 90  ? 22.67738  4.03087   48.71655  1.000 35.76346  ? 90  THR   B C    1 
ATOM   3418 O  O    . THR   B 1 90  ? 22.49675  2.93664   48.18332  1.000 37.64168  ? 90  THR   B O    1 
ATOM   3419 C  CB   . THR   B 1 90  ? 23.69753  5.88920   47.37209  1.000 39.26771  ? 90  THR   B CB   1 
ATOM   3420 O  OG1  . THR   B 1 90  ? 23.40479  5.23730   46.14025  1.000 49.30204  ? 90  THR   B OG1  1 
ATOM   3421 C  CG2  . THR   B 1 90  ? 24.92572  6.80792   47.25071  1.000 52.58428  ? 90  THR   B CG2  1 
ATOM   3422 N  N    . PHE   B 1 91  ? 21.89928  4.50978   49.68135  1.000 32.29009  ? 91  PHE   B N    1 
ATOM   3423 C  CA   . PHE   B 1 91  ? 20.79497  3.72328   50.18926  1.000 34.03801  ? 91  PHE   B CA   1 
ATOM   3424 C  C    . PHE   B 1 91  ? 19.55683  4.58063   50.10236  1.000 32.02782  ? 91  PHE   B C    1 
ATOM   3425 O  O    . PHE   B 1 91  ? 19.49348  5.63492   50.73851  1.000 37.23395  ? 91  PHE   B O    1 
ATOM   3426 C  CB   . PHE   B 1 91  ? 20.99849  3.29427   51.66205  1.000 31.29531  ? 91  PHE   B CB   1 
ATOM   3427 C  CG   . PHE   B 1 91  ? 20.17595  2.10665   52.03679  1.000 32.16451  ? 91  PHE   B CG   1 
ATOM   3428 C  CD1  . PHE   B 1 91  ? 18.81148  2.23994   52.36578  1.000 34.71417  ? 91  PHE   B CD1  1 
ATOM   3429 C  CD2  . PHE   B 1 91  ? 20.75364  0.85629   52.06687  1.000 33.48771  ? 91  PHE   B CD2  1 
ATOM   3430 C  CE1  . PHE   B 1 91  ? 18.02413  1.09883   52.72220  1.000 36.98527  ? 91  PHE   B CE1  1 
ATOM   3431 C  CE2  . PHE   B 1 91  ? 19.98644  -0.28271  52.37820  1.000 33.41903  ? 91  PHE   B CE2  1 
ATOM   3432 C  CZ   . PHE   B 1 91  ? 18.62558  -0.16970  52.71370  1.000 30.50148  ? 91  PHE   B CZ   1 
ATOM   3433 N  N    . ILE   B 1 92  ? 18.52801  4.07240   49.43230  1.000 29.33507  ? 92  ILE   B N    1 
ATOM   3434 C  CA   . ILE   B 1 92  ? 17.25702  4.76333   49.35673  1.000 27.27317  ? 92  ILE   B CA   1 
ATOM   3435 C  C    . ILE   B 1 92  ? 16.29018  4.15535   50.36546  1.000 28.57070  ? 92  ILE   B C    1 
ATOM   3436 O  O    . ILE   B 1 92  ? 16.11257  2.92452   50.42375  1.000 30.28793  ? 92  ILE   B O    1 
ATOM   3437 C  CB   . ILE   B 1 92  ? 16.67727  4.64755   47.93367  1.000 27.33526  ? 92  ILE   B CB   1 
ATOM   3438 C  CG1  . ILE   B 1 92  ? 17.61516  5.37282   46.94174  1.000 30.68537  ? 92  ILE   B CG1  1 
ATOM   3439 C  CG2  . ILE   B 1 92  ? 15.20411  5.12463   47.96849  1.000 29.13218  ? 92  ILE   B CG2  1 
ATOM   3440 C  CD1  . ILE   B 1 92  ? 17.17933  5.13202   45.44269  1.000 33.98305  ? 92  ILE   B CD1  1 
ATOM   3441 N  N    . PHE   B 1 93  ? 15.66612  5.02393   51.17694  1.000 25.06008  ? 93  PHE   B N    1 
ATOM   3442 C  CA   . PHE   B 1 93  ? 14.50948  4.67740   51.97639  1.000 26.06178  ? 93  PHE   B CA   1 
ATOM   3443 C  C    . PHE   B 1 93  ? 13.26303  5.10630   51.18712  1.000 31.25462  ? 93  PHE   B C    1 
ATOM   3444 O  O    . PHE   B 1 93  ? 13.04646  6.31048   50.96133  1.000 30.81275  ? 93  PHE   B O    1 
ATOM   3445 C  CB   . PHE   B 1 93  ? 14.53382  5.41253   53.29754  1.000 26.28577  ? 93  PHE   B CB   1 
ATOM   3446 C  CG   . PHE   B 1 93  ? 15.45646  4.76000   54.32562  1.000 31.32598  ? 93  PHE   B CG   1 
ATOM   3447 C  CD1  . PHE   B 1 93  ? 16.79770  4.83425   54.16992  1.000 37.00307  ? 93  PHE   B CD1  1 
ATOM   3448 C  CD2  . PHE   B 1 93  ? 14.93487  4.16209   55.46951  1.000 32.47450  ? 93  PHE   B CD2  1 
ATOM   3449 C  CE1  . PHE   B 1 93  ? 17.65803  4.25289   55.16099  1.000 38.42942  ? 93  PHE   B CE1  1 
ATOM   3450 C  CE2  . PHE   B 1 93  ? 15.75127  3.61833   56.45998  1.000 33.23498  ? 93  PHE   B CE2  1 
ATOM   3451 C  CZ   . PHE   B 1 93  ? 17.12165  3.64941   56.29730  1.000 34.38854  ? 93  PHE   B CZ   1 
ATOM   3452 N  N    . TRP   B 1 94  ? 12.47900  4.15587   50.79697  1.000 27.27267  ? 94  TRP   B N    1 
ATOM   3453 C  CA   . TRP   B 1 94  ? 11.28295  4.42620   49.97010  1.000 28.08086  ? 94  TRP   B CA   1 
ATOM   3454 C  C    . TRP   B 1 94  ? 10.07261  4.47170   50.90535  1.000 30.33622  ? 94  TRP   B C    1 
ATOM   3455 O  O    . TRP   B 1 94  ? 9.67100   3.46618   51.50257  1.000 28.70345  ? 94  TRP   B O    1 
ATOM   3456 C  CB   . TRP   B 1 94  ? 11.22052  3.34907   48.92333  1.000 27.10443  ? 94  TRP   B CB   1 
ATOM   3457 C  CG   . TRP   B 1 94  ? 10.06976  3.31550   47.90486  1.000 26.58745  ? 94  TRP   B CG   1 
ATOM   3458 C  CD1  . TRP   B 1 94  ? 9.12529   2.33845   47.81224  1.000 31.51709  ? 94  TRP   B CD1  1 
ATOM   3459 C  CD2  . TRP   B 1 94  ? 9.89969   4.18284   46.77159  1.000 27.49919  ? 94  TRP   B CD2  1 
ATOM   3460 N  NE1  . TRP   B 1 94  ? 8.34062   2.55821   46.65866  1.000 31.76791  ? 94  TRP   B NE1  1 
ATOM   3461 C  CE2  . TRP   B 1 94  ? 8.80602   3.67843   46.01700  1.000 32.84442  ? 94  TRP   B CE2  1 
ATOM   3462 C  CE3  . TRP   B 1 94  ? 10.54470  5.35005   46.33020  1.000 30.52985  ? 94  TRP   B CE3  1 
ATOM   3463 C  CZ2  . TRP   B 1 94  ? 8.34316   4.30183   44.86068  1.000 36.58154  ? 94  TRP   B CZ2  1 
ATOM   3464 C  CZ3  . TRP   B 1 94  ? 10.08263  5.96180   45.14116  1.000 32.74708  ? 94  TRP   B CZ3  1 
ATOM   3465 C  CH2  . TRP   B 1 94  ? 9.01005   5.41836   44.41459  1.000 32.05763  ? 94  TRP   B CH2  1 
ATOM   3466 N  N    . ILE   B 1 95  ? 9.57716   5.67606   51.16068  1.000 28.22713  ? 95  ILE   B N    1 
ATOM   3467 C  CA   . ILE   B 1 95  ? 8.47396   5.84803   52.06009  1.000 26.46482  ? 95  ILE   B CA   1 
ATOM   3468 C  C    . ILE   B 1 95  ? 7.23949   5.52551   51.22971  1.000 32.47688  ? 95  ILE   B C    1 
ATOM   3469 O  O    . ILE   B 1 95  ? 6.89780   6.28949   50.36402  1.000 28.10613  ? 95  ILE   B O    1 
ATOM   3470 C  CB   . ILE   B 1 95  ? 8.46201   7.26358   52.64233  1.000 29.51165  ? 95  ILE   B CB   1 
ATOM   3471 C  CG1  . ILE   B 1 95  ? 9.88168   7.51576   53.29851  1.000 31.55178  ? 95  ILE   B CG1  1 
ATOM   3472 C  CG2  . ILE   B 1 95  ? 7.23272   7.50492   53.57894  1.000 28.66202  ? 95  ILE   B CG2  1 
ATOM   3473 C  CD1  . ILE   B 1 95  ? 10.05189  9.01247   53.67046  1.000 35.43743  ? 95  ILE   B CD1  1 
ATOM   3474 N  N    . ALA   B 1 96  ? 6.66795   4.33945   51.42293  1.000 30.09879  ? 96  ALA   B N    1 
ATOM   3475 C  CA   . ALA   B 1 96  ? 5.69538   3.73544   50.50240  1.000 29.70344  ? 96  ALA   B CA   1 
ATOM   3476 C  C    . ALA   B 1 96  ? 4.28268   4.16763   50.88035  1.000 29.41172  ? 96  ALA   B C    1 
ATOM   3477 O  O    . ALA   B 1 96  ? 3.43885   3.35680   51.32032  1.000 30.04680  ? 96  ALA   B O    1 
ATOM   3478 C  CB   . ALA   B 1 96  ? 5.82530   2.22227   50.56048  1.000 28.80692  ? 96  ALA   B CB   1 
ATOM   3479 N  N    . ASP   B 1 97  ? 4.07403   5.48475   50.75747  1.000 31.59398  ? 97  ASP   B N    1 
ATOM   3480 C  CA   . ASP   B 1 97  ? 2.82444   6.08837   51.23358  1.000 29.44984  ? 97  ASP   B CA   1 
ATOM   3481 C  C    . ASP   B 1 97  ? 1.61065   5.55445   50.47128  1.000 27.85363  ? 97  ASP   B C    1 
ATOM   3482 O  O    . ASP   B 1 97  ? 0.59180   5.15095   51.08981  1.000 31.07326  ? 97  ASP   B O    1 
ATOM   3483 C  CB   . ASP   B 1 97  ? 2.87805   7.63239   51.16025  1.000 29.20701  ? 97  ASP   B CB   1 
ATOM   3484 C  CG   . ASP   B 1 97  ? 3.35255   8.20768   49.81332  1.000 34.33176  ? 97  ASP   B CG   1 
ATOM   3485 O  OD1  . ASP   B 1 97  ? 3.64095   7.53749   48.82261  1.000 30.75267  ? 97  ASP   B OD1  1 
ATOM   3486 O  OD2  . ASP   B 1 97  ? 3.52172   9.44032   49.78260  1.000 36.11256  ? 97  ASP   B OD2  1 
ATOM   3487 N  N    . TRP   B 1 98  ? 1.71668   5.50468   49.14944  1.000 34.61474  ? 98  TRP   B N    1 
ATOM   3488 C  CA   . TRP   B 1 98  ? 0.61910   4.95804   48.35307  1.000 31.33585  ? 98  TRP   B CA   1 
ATOM   3489 C  C    . TRP   B 1 98  ? 0.39256   3.49071   48.62829  1.000 34.57587  ? 98  TRP   B C    1 
ATOM   3490 O  O    . TRP   B 1 98  ? -0.72769  2.99683   48.50546  1.000 31.36353  ? 98  TRP   B O    1 
ATOM   3491 C  CB   . TRP   B 1 98  ? 0.91867   5.16891   46.86629  1.000 36.06603  ? 98  TRP   B CB   1 
ATOM   3492 C  CG   . TRP   B 1 98  ? 0.27668   6.37844   46.33164  1.000 42.25534  ? 98  TRP   B CG   1 
ATOM   3493 C  CD1  . TRP   B 1 98  ? -0.38921  7.34675   47.02584  1.000 46.59785  ? 98  TRP   B CD1  1 
ATOM   3494 C  CD2  . TRP   B 1 98  ? 0.33214   6.80945   44.98548  1.000 39.24503  ? 98  TRP   B CD2  1 
ATOM   3495 N  NE1  . TRP   B 1 98  ? -0.77373  8.36182   46.17390  1.000 51.43529  ? 98  TRP   B NE1  1 
ATOM   3496 C  CE2  . TRP   B 1 98  ? -0.33835  8.05353   44.91100  1.000 48.33792  ? 98  TRP   B CE2  1 
ATOM   3497 C  CE3  . TRP   B 1 98  ? 0.95020   6.30591   43.85170  1.000 34.64383  ? 98  TRP   B CE3  1 
ATOM   3498 C  CZ2  . TRP   B 1 98  ? -0.48728  8.75184   43.69808  1.000 57.11487  ? 98  TRP   B CZ2  1 
ATOM   3499 C  CZ3  . TRP   B 1 98  ? 0.81380   6.99943   42.64016  1.000 47.49138  ? 98  TRP   B CZ3  1 
ATOM   3500 C  CH2  . TRP   B 1 98  ? 0.08995   8.19757   42.57503  1.000 49.37351  ? 98  TRP   B CH2  1 
ATOM   3501 N  N    . PHE   B 1 99  ? 1.45202   2.75816   48.96543  1.000 31.41889  ? 99  PHE   B N    1 
ATOM   3502 C  CA   . PHE   B 1 99  ? 1.29632   1.34190   49.27239  1.000 29.90851  ? 99  PHE   B CA   1 
ATOM   3503 C  C    . PHE   B 1 99  ? 0.55447   1.12699   50.57747  1.000 32.58633  ? 99  PHE   B C    1 
ATOM   3504 O  O    . PHE   B 1 99  ? -0.28267  0.22273   50.67154  1.000 33.84175  ? 99  PHE   B O    1 
ATOM   3505 C  CB   . PHE   B 1 99  ? 2.70637   0.67426   49.31647  1.000 25.86722  ? 99  PHE   B CB   1 
ATOM   3506 C  CG   . PHE   B 1 99  ? 3.34656   0.59144   48.00255  1.000 27.68861  ? 99  PHE   B CG   1 
ATOM   3507 C  CD1  . PHE   B 1 99  ? 4.01657   1.67935   47.45169  1.000 29.81638  ? 99  PHE   B CD1  1 
ATOM   3508 C  CD2  . PHE   B 1 99  ? 3.25744   -0.57244  47.25398  1.000 30.08706  ? 99  PHE   B CD2  1 
ATOM   3509 C  CE1  . PHE   B 1 99  ? 4.63063   1.61676   46.18799  1.000 29.25682  ? 99  PHE   B CE1  1 
ATOM   3510 C  CE2  . PHE   B 1 99  ? 3.86424   -0.66396  45.97787  1.000 26.15105  ? 99  PHE   B CE2  1 
ATOM   3511 C  CZ   . PHE   B 1 99  ? 4.56726   0.43149   45.41681  1.000 24.75830  ? 99  PHE   B CZ   1 
ATOM   3512 N  N    . ALA   B 1 100 ? 0.89206   1.90632   51.62678  1.000 30.03169  ? 100 ALA   B N    1 
ATOM   3513 C  CA   . ALA   B 1 100 ? 0.16101   1.85401   52.87560  1.000 27.04027  ? 100 ALA   B CA   1 
ATOM   3514 C  C    . ALA   B 1 100 ? -1.33389  2.12362   52.61796  1.000 35.42764  ? 100 ALA   B C    1 
ATOM   3515 O  O    . ALA   B 1 100 ? -2.21289  1.44012   53.15292  1.000 32.86125  ? 100 ALA   B O    1 
ATOM   3516 C  CB   . ALA   B 1 100 ? 0.71618   2.91101   53.82665  1.000 29.02848  ? 100 ALA   B CB   1 
ATOM   3517 N  N    . HIS   B 1 101 ? -1.61226  3.11857   51.78214  1.000 30.37885  ? 101 HIS   B N    1 
ATOM   3518 C  CA   . HIS   B 1 101 ? -3.00981  3.42135   51.43743  1.000 37.23330  ? 101 HIS   B CA   1 
ATOM   3519 C  C    . HIS   B 1 101 ? -3.68165  2.22913   50.73081  1.000 34.89659  ? 101 HIS   B C    1 
ATOM   3520 O  O    . HIS   B 1 101 ? -4.79297  1.79808   51.09746  1.000 35.97634  ? 101 HIS   B O    1 
ATOM   3521 C  CB   . HIS   B 1 101 ? -3.04134  4.67000   50.56749  1.000 35.64832  ? 101 HIS   B CB   1 
ATOM   3522 C  CG   . HIS   B 1 101 ? -4.41733  4.98891   50.02972  1.000 40.34245  ? 101 HIS   B CG   1 
ATOM   3523 N  ND1  . HIS   B 1 101 ? -5.35991  5.64927   50.78036  1.000 47.00337  ? 101 HIS   B ND1  1 
ATOM   3524 C  CD2  . HIS   B 1 101 ? -4.99101  4.74253   48.82716  1.000 51.40415  ? 101 HIS   B CD2  1 
ATOM   3525 C  CE1  . HIS   B 1 101 ? -6.46620  5.80153   50.06848  1.000 48.95244  ? 101 HIS   B CE1  1 
ATOM   3526 N  NE2  . HIS   B 1 101 ? -6.26375  5.25954   48.87542  1.000 52.41744  ? 101 HIS   B NE2  1 
ATOM   3527 N  N    . LEU   B 1 102 ? -2.99886  1.66637   49.73649  1.000 37.61064  ? 102 LEU   B N    1 
ATOM   3528 C  CA   . LEU   B 1 102 ? -3.51495  0.50163   49.01576  1.000 34.33248  ? 102 LEU   B CA   1 
ATOM   3529 C  C    . LEU   B 1 102 ? -3.73348  -0.66190  49.95498  1.000 37.41341  ? 102 LEU   B C    1 
ATOM   3530 O  O    . LEU   B 1 102 ? -4.62768  -1.48280  49.73206  1.000 35.77556  ? 102 LEU   B O    1 
ATOM   3531 C  CB   . LEU   B 1 102 ? -2.53105  0.14620   47.89350  1.000 33.40309  ? 102 LEU   B CB   1 
ATOM   3532 C  CG   . LEU   B 1 102 ? -2.77380  -0.88382  46.81888  1.000 34.37065  ? 102 LEU   B CG   1 
ATOM   3533 C  CD1  . LEU   B 1 102 ? -4.12857  -0.56063  46.12204  1.000 31.05135  ? 102 LEU   B CD1  1 
ATOM   3534 C  CD2  . LEU   B 1 102 ? -1.62768  -0.84295  45.80139  1.000 30.64067  ? 102 LEU   B CD2  1 
ATOM   3535 N  N    . ASN   B 1 103 ? -2.92236  -0.76267  51.02639  1.000 36.16617  ? 103 ASN   B N    1 
ATOM   3536 C  CA   . ASN   B 1 103 ? -3.02279  -1.85147  51.98967  1.000 35.04182  ? 103 ASN   B CA   1 
ATOM   3537 C  C    . ASN   B 1 103 ? -3.88601  -1.47955  53.20911  1.000 37.58848  ? 103 ASN   B C    1 
ATOM   3538 O  O    . ASN   B 1 103 ? -3.80769  -2.15015  54.24855  1.000 35.03325  ? 103 ASN   B O    1 
ATOM   3539 C  CB   . ASN   B 1 103 ? -1.57908  -2.27283  52.43510  1.000 30.65263  ? 103 ASN   B CB   1 
ATOM   3540 C  CG   . ASN   B 1 103 ? -1.47698  -3.72849  52.85683  1.000 38.11366  ? 103 ASN   B CG   1 
ATOM   3541 O  OD1  . ASN   B 1 103 ? -2.43696  -4.49665  52.75103  1.000 37.03212  ? 103 ASN   B OD1  1 
ATOM   3542 N  ND2  . ASN   B 1 103 ? -0.26272  -4.13005  53.33038  1.000 36.42200  ? 103 ASN   B ND2  1 
ATOM   3543 N  N    . ASN   B 1 104 ? -4.66227  -0.39557  53.13086  1.000 36.83708  ? 104 ASN   B N    1 
ATOM   3544 C  CA   . ASN   B 1 104 ? -5.68296  -0.08339  54.14503  1.000 39.23975  ? 104 ASN   B CA   1 
ATOM   3545 C  C    . ASN   B 1 104 ? -5.09564  0.28572   55.52160  1.000 46.09412  ? 104 ASN   B C    1 
ATOM   3546 O  O    . ASN   B 1 104 ? -5.74872  0.09752   56.55346  1.000 41.27088  ? 104 ASN   B O    1 
ATOM   3547 C  CB   . ASN   B 1 104 ? -6.62456  -1.25485  54.30944  1.000 38.05127  ? 104 ASN   B CB   1 
ATOM   3548 C  CG   . ASN   B 1 104 ? -7.51991  -1.43751  53.08164  1.000 51.39962  ? 104 ASN   B CG   1 
ATOM   3549 O  OD1  . ASN   B 1 104 ? -8.01913  -0.45783  52.51114  1.000 53.69121  ? 104 ASN   B OD1  1 
ATOM   3550 N  ND2  . ASN   B 1 104 ? -7.67309  -2.68483  52.64307  1.000 53.52021  ? 104 ASN   B ND2  1 
ATOM   3551 N  N    . LYS   B 1 105 ? -3.90717  0.86047   55.53790  1.000 37.11367  ? 105 LYS   B N    1 
ATOM   3552 C  CA   . LYS   B 1 105 ? -3.25529  1.30034   56.76646  1.000 37.98794  ? 105 LYS   B CA   1 
ATOM   3553 C  C    . LYS   B 1 105 ? -3.73561  2.68798   57.16692  1.000 40.45198  ? 105 LYS   B C    1 
ATOM   3554 O  O    . LYS   B 1 105 ? -4.10448  3.49746   56.32180  1.000 40.48776  ? 105 LYS   B O    1 
ATOM   3555 C  CB   . LYS   B 1 105 ? -1.74843  1.32380   56.54748  1.000 35.71568  ? 105 LYS   B CB   1 
ATOM   3556 C  CG   . LYS   B 1 105 ? -1.19410  -0.05464  56.16079  1.000 34.61728  ? 105 LYS   B CG   1 
ATOM   3557 C  CD   . LYS   B 1 105 ? -1.60028  -1.11086  57.20485  1.000 41.29012  ? 105 LYS   B CD   1 
ATOM   3558 C  CE   . LYS   B 1 105 ? -1.17095  -2.52282  56.76918  1.000 45.86220  ? 105 LYS   B CE   1 
ATOM   3559 N  NZ   . LYS   B 1 105 ? 0.32325   -2.68060  56.62891  1.000 41.35326  ? 105 LYS   B NZ   1 
ATOM   3560 N  N    . MET   B 1 106 ? -3.73220  2.97333   58.46459  1.000 42.37885  ? 106 MET   B N    1 
ATOM   3561 C  CA   . MET   B 1 106 ? -4.07741  4.32839   58.91883  1.000 47.21955  ? 106 MET   B CA   1 
ATOM   3562 C  C    . MET   B 1 106 ? -5.43834  4.76777   58.35857  1.000 47.29141  ? 106 MET   B C    1 
ATOM   3563 O  O    . MET   B 1 106 ? -5.60926  5.90874   57.90731  1.000 47.21272  ? 106 MET   B O    1 
ATOM   3564 C  CB   . MET   B 1 106 ? -2.99307  5.35580   58.52077  1.000 43.61111  ? 106 MET   B CB   1 
ATOM   3565 C  CG   . MET   B 1 106 ? -1.55794  5.10844   59.07465  1.000 42.40662  ? 106 MET   B CG   1 
ATOM   3566 S  SD   . MET   B 1 106 ? -1.49989  5.42939   60.85704  1.000 51.78796  ? 106 MET   B SD   1 
ATOM   3567 C  CE   . MET   B 1 106 ? -2.68214  6.71531   61.06889  1.000 50.72354  ? 106 MET   B CE   1 
ATOM   3568 N  N    . SER   B 1 107 ? -6.40772  3.84698   58.32507  1.000 44.47087  ? 107 SER   B N    1 
ATOM   3569 C  CA   . SER   B 1 107 ? -7.75412  4.13507   57.83518  1.000 54.46932  ? 107 SER   B CA   1 
ATOM   3570 C  C    . SER   B 1 107 ? -7.76883  4.57065   56.37364  1.000 56.85553  ? 107 SER   B C    1 
ATOM   3571 O  O    . SER   B 1 107 ? -8.73480  5.19905   55.93640  1.000 54.17009  ? 107 SER   B O    1 
ATOM   3572 C  CB   . SER   B 1 107 ? -8.46235  5.21108   58.68610  1.000 57.73699  ? 107 SER   B CB   1 
ATOM   3573 O  OG   . SER   B 1 107 ? -8.28593  5.01926   60.08159  1.000 60.12172  ? 107 SER   B OG   1 
ATOM   3574 N  N    . GLY   B 1 108 ? -6.71371  4.25467   55.61151  1.000 45.64068  ? 108 GLY   B N    1 
ATOM   3575 C  CA   . GLY   B 1 108 ? -6.51202  4.72022   54.25642  1.000 46.51676  ? 108 GLY   B CA   1 
ATOM   3576 C  C    . GLY   B 1 108 ? -6.23677  6.20129   54.13210  1.000 52.97500  ? 108 GLY   B C    1 
ATOM   3577 O  O    . GLY   B 1 108 ? -6.02966  6.68733   53.01100  1.000 56.98889  ? 108 GLY   B O    1 
ATOM   3578 N  N    . ASP   B 1 109 ? -6.21904  6.92641   55.24893  1.000 43.51920  ? 109 ASP   B N    1 
ATOM   3579 C  CA   . ASP   B 1 109 ? -6.17532  8.38714   55.26408  1.000 43.13421  ? 109 ASP   B CA   1 
ATOM   3580 C  C    . ASP   B 1 109 ? -4.76695  8.87234   54.87067  1.000 37.52204  ? 109 ASP   B C    1 
ATOM   3581 O  O    . ASP   B 1 109 ? -3.80717  8.70440   55.64725  1.000 39.22479  ? 109 ASP   B O    1 
ATOM   3582 C  CB   . ASP   B 1 109 ? -6.55146  8.85092   56.66955  1.000 44.72395  ? 109 ASP   B CB   1 
ATOM   3583 C  CG   . ASP   B 1 109 ? -6.67595  10.34865  56.78515  1.000 51.52153  ? 109 ASP   B CG   1 
ATOM   3584 O  OD1  . ASP   B 1 109 ? -7.38186  10.78417  57.72378  1.000 53.74798  ? 109 ASP   B OD1  1 
ATOM   3585 O  OD2  . ASP   B 1 109 ? -6.09761  11.07825  55.93494  1.000 59.85702  ? 109 ASP   B OD2  1 
ATOM   3586 N  N    . LEU   B 1 110 ? -4.64742  9.52782   53.70641  1.000 38.44403  ? 110 LEU   B N    1 
ATOM   3587 C  CA   . LEU   B 1 110 ? -3.32275  9.93784   53.22078  1.000 47.44519  ? 110 LEU   B CA   1 
ATOM   3588 C  C    . LEU   B 1 110 ? -2.69971  11.03596  54.05546  1.000 45.22604  ? 110 LEU   B C    1 
ATOM   3589 O  O    . LEU   B 1 110 ? -1.45887  11.12061  54.11439  1.000 42.31393  ? 110 LEU   B O    1 
ATOM   3590 C  CB   . LEU   B 1 110 ? -3.34207  10.40981  51.77054  1.000 52.11794  ? 110 LEU   B CB   1 
ATOM   3591 C  CG   . LEU   B 1 110 ? -2.89513  9.38545   50.71910  1.000 56.64059  ? 110 LEU   B CG   1 
ATOM   3592 C  CD1  . LEU   B 1 110 ? -3.87082  8.23926   50.57781  1.000 58.45865  ? 110 LEU   B CD1  1 
ATOM   3593 C  CD2  . LEU   B 1 110 ? -2.61606  10.06089  49.36427  1.000 61.71727  ? 110 LEU   B CD2  1 
ATOM   3594 N  N    . LYS   B 1 111 ? -3.51159  11.88050  54.70660  1.000 40.72419  ? 111 LYS   B N    1 
ATOM   3595 C  CA   . LYS   B 1 111 ? -2.91101  12.87784  55.57930  1.000 44.71747  ? 111 LYS   B CA   1 
ATOM   3596 C  C    . LYS   B 1 111 ? -2.22061  12.20434  56.74985  1.000 41.99393  ? 111 LYS   B C    1 
ATOM   3597 O  O    . LYS   B 1 111 ? -1.12701  12.62479  57.15963  1.000 45.60504  ? 111 LYS   B O    1 
ATOM   3598 C  CB   . LYS   B 1 111 ? -3.94303  13.88885  56.09545  1.000 50.16187  ? 111 LYS   B CB   1 
ATOM   3599 C  CG   . LYS   B 1 111 ? -4.68723  14.61170  54.97367  1.000 62.86886  ? 111 LYS   B CG   1 
ATOM   3600 C  CD   . LYS   B 1 111 ? -5.56839  15.76185  55.51368  1.000 62.99095  ? 111 LYS   B CD   1 
ATOM   3601 C  CE   . LYS   B 1 111 ? -4.71739  17.00939  55.77418  1.000 72.27934  ? 111 LYS   B CE   1 
ATOM   3602 N  NZ   . LYS   B 1 111 ? -3.68152  17.17833  54.69534  1.000 78.02973  ? 111 LYS   B NZ   1 
ATOM   3603 N  N    . LYS   B 1 112 ? -2.86411  11.18268  57.33326  1.000 36.77287  ? 112 LYS   B N    1 
ATOM   3604 C  CA   . LYS   B 1 112 ? -2.24371  10.47652  58.44212  1.000 37.15994  ? 112 LYS   B CA   1 
ATOM   3605 C  C    . LYS   B 1 112 ? -0.98168  9.74222   57.96786  1.000 36.66173  ? 112 LYS   B C    1 
ATOM   3606 O  O    . LYS   B 1 112 ? 0.04764   9.75190   58.66850  1.000 36.76130  ? 112 LYS   B O    1 
ATOM   3607 C  CB   . LYS   B 1 112 ? -3.21989  9.49414   59.08276  1.000 38.55143  ? 112 LYS   B CB   1 
ATOM   3608 C  CG   . LYS   B 1 112 ? -4.50639  10.17640  59.74193  1.000 40.59636  ? 112 LYS   B CG   1 
ATOM   3609 C  CD   . LYS   B 1 112 ? -5.23491  9.14305   60.57544  1.000 44.53389  ? 112 LYS   B CD   1 
ATOM   3610 C  CE   . LYS   B 1 112 ? -6.63078  9.62318   61.09091  1.000 50.78930  ? 112 LYS   B CE   1 
ATOM   3611 N  NZ   . LYS   B 1 112 ? -7.03800  8.60187   62.14370  1.000 62.29814  ? 112 LYS   B NZ   1 
ATOM   3612 N  N    . ILE   B 1 113 ? -1.05526  9.09930   56.78236  1.000 35.35549  ? 113 ILE   B N    1 
ATOM   3613 C  CA   . ILE   B 1 113 ? 0.07651   8.33321   56.25565  1.000 34.25542  ? 113 ILE   B CA   1 
ATOM   3614 C  C    . ILE   B 1 113 ? 1.26428   9.25246   56.03712  1.000 37.72323  ? 113 ILE   B C    1 
ATOM   3615 O  O    . ILE   B 1 113 ? 2.42864   8.88767   56.30924  1.000 33.32012  ? 113 ILE   B O    1 
ATOM   3616 C  CB   . ILE   B 1 113 ? -0.32887  7.60842   54.96263  1.000 31.82723  ? 113 ILE   B CB   1 
ATOM   3617 C  CG1  . ILE   B 1 113 ? -1.26924  6.46182   55.31164  1.000 32.92804  ? 113 ILE   B CG1  1 
ATOM   3618 C  CG2  . ILE   B 1 113 ? 0.90308   7.11750   54.14849  1.000 29.12264  ? 113 ILE   B CG2  1 
ATOM   3619 C  CD1  . ILE   B 1 113 ? -1.96696  5.90859   54.01228  1.000 38.78141  ? 113 ILE   B CD1  1 
ATOM   3620 N  N    . LYS   B 1 114 ? 0.98725   10.46643  55.54410  1.000 36.10903  ? 114 LYS   B N    1 
ATOM   3621 C  CA   . LYS   B 1 114 ? 2.04068   11.45637  55.35616  1.000 39.80349  ? 114 LYS   B CA   1 
ATOM   3622 C  C    . LYS   B 1 114 ? 2.66776   11.88468  56.68281  1.000 36.73396  ? 114 LYS   B C    1 
ATOM   3623 O  O    . LYS   B 1 114 ? 3.91104   11.99018  56.78063  1.000 36.01917  ? 114 LYS   B O    1 
ATOM   3624 C  CB   . LYS   B 1 114 ? 1.47979   12.66663  54.62227  1.000 43.29768  ? 114 LYS   B CB   1 
ATOM   3625 C  CG   . LYS   B 1 114 ? 2.47951   13.77531  54.40647  1.000 47.92676  ? 114 LYS   B CG   1 
ATOM   3626 C  CD   . LYS   B 1 114 ? 1.71908   15.07664  54.12742  1.000 63.84591  ? 114 LYS   B CD   1 
ATOM   3627 C  CE   . LYS   B 1 114 ? 2.46890   15.99142  53.16114  1.000 68.25607  ? 114 LYS   B CE   1 
ATOM   3628 N  NZ   . LYS   B 1 114 ? 2.21578   17.41335  53.56008  1.000 69.33914  ? 114 LYS   B NZ   1 
ATOM   3629 N  N    . LYS   B 1 115 ? 1.83972   12.14087  57.72117  1.000 30.82091  ? 115 LYS   B N    1 
ATOM   3630 C  CA   . LYS   B 1 115 ? 2.42711   12.49281  59.02853  1.000 35.53797  ? 115 LYS   B CA   1 
ATOM   3631 C  C    . LYS   B 1 115 ? 3.29976   11.37679  59.55104  1.000 35.15167  ? 115 LYS   B C    1 
ATOM   3632 O  O    . LYS   B 1 115 ? 4.37524   11.62723  60.12025  1.000 33.87853  ? 115 LYS   B O    1 
ATOM   3633 C  CB   . LYS   B 1 115 ? 1.34901   12.85891  60.05042  1.000 37.67213  ? 115 LYS   B CB   1 
ATOM   3634 C  CG   . LYS   B 1 115 ? 0.97765   14.29960  59.79354  1.000 45.83560  ? 115 LYS   B CG   1 
ATOM   3635 C  CD   . LYS   B 1 115 ? -0.16468  14.74809  60.62842  1.000 56.77791  ? 115 LYS   B CD   1 
ATOM   3636 C  CE   . LYS   B 1 115 ? -0.26704  16.24555  60.49402  1.000 63.02782  ? 115 LYS   B CE   1 
ATOM   3637 N  NZ   . LYS   B 1 115 ? 1.07605   16.79741  60.83329  1.000 69.86828  ? 115 LYS   B NZ   1 
ATOM   3638 N  N    . VAL   B 1 116 ? 2.84778   10.13462  59.39721  1.000 33.60907  ? 116 VAL   B N    1 
ATOM   3639 C  CA   . VAL   B 1 116 ? 3.66028   9.02202   59.88440  1.000 34.30942  ? 116 VAL   B CA   1 
ATOM   3640 C  C    . VAL   B 1 116 ? 4.96855   8.95825   59.11025  1.000 34.31222  ? 116 VAL   B C    1 
ATOM   3641 O  O    . VAL   B 1 116 ? 6.04076   8.73849   59.70143  1.000 30.65347  ? 116 VAL   B O    1 
ATOM   3642 C  CB   . VAL   B 1 116 ? 2.89257   7.68429   59.80197  1.000 31.38353  ? 116 VAL   B CB   1 
ATOM   3643 C  CG1  . VAL   B 1 116 ? 3.85559   6.49802   60.14507  1.000 28.69676  ? 116 VAL   B CG1  1 
ATOM   3644 C  CG2  . VAL   B 1 116 ? 1.70809   7.69327   60.78140  1.000 35.60489  ? 116 VAL   B CG2  1 
ATOM   3645 N  N    . GLY   B 1 117 ? 4.91090   9.14553   57.77976  1.000 31.11921  ? 117 GLY   B N    1 
ATOM   3646 C  CA   . GLY   B 1 117 ? 6.14611   9.16909   56.98929  1.000 32.59636  ? 117 GLY   B CA   1 
ATOM   3647 C  C    . GLY   B 1 117 ? 7.13542   10.23149  57.43794  1.000 33.20734  ? 117 GLY   B C    1 
ATOM   3648 O  O    . GLY   B 1 117 ? 8.36376   9.99572   57.45216  1.000 33.30028  ? 117 GLY   B O    1 
ATOM   3649 N  N    . SER   B 1 118 ? 6.63043   11.43631  57.74095  1.000 30.87645  ? 118 SER   B N    1 
ATOM   3650 C  CA   . SER   B 1 118 ? 7.47770   12.48027  58.31394  1.000 36.68859  ? 118 SER   B CA   1 
ATOM   3651 C  C    . SER   B 1 118 ? 8.10101   12.04099  59.63197  1.000 37.31201  ? 118 SER   B C    1 
ATOM   3652 O  O    . SER   B 1 118 ? 9.28584   12.32651  59.88889  1.000 35.77479  ? 118 SER   B O    1 
ATOM   3653 C  CB   . SER   B 1 118 ? 6.69404   13.77630  58.52529  1.000 33.53865  ? 118 SER   B CB   1 
ATOM   3654 O  OG   . SER   B 1 118 ? 6.16871   14.14806  57.27478  1.000 41.79750  ? 118 SER   B OG   1 
ATOM   3655 N  N    . TYR   B 1 119 ? 7.30376   11.39854  60.50968  1.000 31.87289  ? 119 TYR   B N    1 
ATOM   3656 C  CA   . TYR   B 1 119 ? 7.84414   10.87631  61.77095  1.000 29.52272  ? 119 TYR   B CA   1 
ATOM   3657 C  C    . TYR   B 1 119 ? 8.91231   9.80355   61.53149  1.000 33.20758  ? 119 TYR   B C    1 
ATOM   3658 O  O    . TYR   B 1 119 ? 9.95945   9.78674   62.23159  1.000 33.92562  ? 119 TYR   B O    1 
ATOM   3659 C  CB   . TYR   B 1 119 ? 6.68010   10.35930  62.63538  1.000 30.05518  ? 119 TYR   B CB   1 
ATOM   3660 C  CG   . TYR   B 1 119 ? 6.97750   9.22898   63.55172  1.000 30.27166  ? 119 TYR   B CG   1 
ATOM   3661 C  CD1  . TYR   B 1 119 ? 7.52585   9.41255   64.84273  1.000 29.71867  ? 119 TYR   B CD1  1 
ATOM   3662 C  CD2  . TYR   B 1 119 ? 6.79114   7.92379   63.08822  1.000 32.69949  ? 119 TYR   B CD2  1 
ATOM   3663 C  CE1  . TYR   B 1 119 ? 7.79836   8.30959   65.66906  1.000 32.26188  ? 119 TYR   B CE1  1 
ATOM   3664 C  CE2  . TYR   B 1 119 ? 7.07961   6.83151   63.88122  1.000 33.33830  ? 119 TYR   B CE2  1 
ATOM   3665 C  CZ   . TYR   B 1 119 ? 7.56891   7.01903   65.15613  1.000 36.45688  ? 119 TYR   B CZ   1 
ATOM   3666 O  OH   . TYR   B 1 119 ? 7.82434   5.88551   65.88456  1.000 40.87987  ? 119 TYR   B OH   1 
ATOM   3667 N  N    . PHE   B 1 120 ? 8.70988   8.93679   60.51519  1.000 28.39686  ? 120 PHE   B N    1 
ATOM   3668 C  CA   . PHE   B 1 120 ? 9.75300   7.95407   60.15933  1.000 34.14124  ? 120 PHE   B CA   1 
ATOM   3669 C  C    . PHE   B 1 120 ? 11.06695  8.65325   59.86874  1.000 35.05699  ? 120 PHE   B C    1 
ATOM   3670 O  O    . PHE   B 1 120 ? 12.16456  8.20263   60.29313  1.000 31.64255  ? 120 PHE   B O    1 
ATOM   3671 C  CB   . PHE   B 1 120 ? 9.36846   7.16955   58.90449  1.000 30.42277  ? 120 PHE   B CB   1 
ATOM   3672 C  CG   . PHE   B 1 120 ? 8.44433   5.99205   59.13679  1.000 33.16812  ? 120 PHE   B CG   1 
ATOM   3673 C  CD1  . PHE   B 1 120 ? 7.82382   5.77361   60.38859  1.000 32.19405  ? 120 PHE   B CD1  1 
ATOM   3674 C  CD2  . PHE   B 1 120 ? 8.14205   5.14814   58.04640  1.000 33.54946  ? 120 PHE   B CD2  1 
ATOM   3675 C  CE1  . PHE   B 1 120 ? 6.96197   4.65880   60.61446  1.000 32.57366  ? 120 PHE   B CE1  1 
ATOM   3676 C  CE2  . PHE   B 1 120 ? 7.28056   4.02260   58.25015  1.000 32.60107  ? 120 PHE   B CE2  1 
ATOM   3677 C  CZ   . PHE   B 1 120 ? 6.69903   3.78040   59.51043  1.000 30.84468  ? 120 PHE   B CZ   1 
ATOM   3678 N  N    . ILE   B 1 121 ? 10.98712  9.71046   59.05947  1.000 31.47901  ? 121 ILE   B N    1 
ATOM   3679 C  CA   . ILE   B 1 121 ? 12.22703  10.40751  58.70440  1.000 34.93540  ? 121 ILE   B CA   1 
ATOM   3680 C  C    . ILE   B 1 121 ? 12.89067  11.00002  59.95234  1.000 36.60806  ? 121 ILE   B C    1 
ATOM   3681 O  O    . ILE   B 1 121 ? 14.12691  10.96663  60.08167  1.000 34.70408  ? 121 ILE   B O    1 
ATOM   3682 C  CB   . ILE   B 1 121 ? 11.95606  11.48450  57.63816  1.000 32.52043  ? 121 ILE   B CB   1 
ATOM   3683 C  CG1  . ILE   B 1 121 ? 11.62213  10.85886  56.29568  1.000 33.29419  ? 121 ILE   B CG1  1 
ATOM   3684 C  CG2  . ILE   B 1 121 ? 13.17781  12.42421  57.49704  1.000 33.19454  ? 121 ILE   B CG2  1 
ATOM   3685 C  CD1  . ILE   B 1 121 ? 11.16918  11.95348  55.28064  1.000 33.86919  ? 121 ILE   B CD1  1 
ATOM   3686 N  N    . GLU   B 1 122 ? 12.09691  11.58629  60.88140  1.000 31.41885  ? 122 GLU   B N    1 
ATOM   3687 C  CA   . GLU   B 1 122 ? 12.68955  12.11314  62.12805  1.000 33.71280  ? 122 GLU   B CA   1 
ATOM   3688 C  C    . GLU   B 1 122 ? 13.42845  11.01653  62.89614  1.000 38.71609  ? 122 GLU   B C    1 
ATOM   3689 O  O    . GLU   B 1 122 ? 14.53625  11.22254  63.43660  1.000 35.15778  ? 122 GLU   B O    1 
ATOM   3690 C  CB   . GLU   B 1 122 ? 11.61843  12.69401  63.06262  1.000 40.03404  ? 122 GLU   B CB   1 
ATOM   3691 C  CG   . GLU   B 1 122 ? 10.94587  13.99047  62.57125  1.000 49.73440  ? 122 GLU   B CG   1 
ATOM   3692 C  CD   . GLU   B 1 122 ? 11.88658  15.17564  62.42787  1.000 59.59846  ? 122 GLU   B CD   1 
ATOM   3693 O  OE1  . GLU   B 1 122 ? 12.30062  15.76596  63.46280  1.000 58.50918  ? 122 GLU   B OE1  1 
ATOM   3694 O  OE2  . GLU   B 1 122 ? 12.19664  15.52734  61.26362  1.000 64.62347  ? 122 GLU   B OE2  1 
ATOM   3695 N  N    . VAL   B 1 123 ? 12.79322  9.85606   63.01057  1.000 29.00347  ? 123 VAL   B N    1 
ATOM   3696 C  CA   . VAL   B 1 123 ? 13.41087  8.71077   63.67663  1.000 30.08755  ? 123 VAL   B CA   1 
ATOM   3697 C  C    . VAL   B 1 123 ? 14.72531  8.34353   63.00135  1.000 29.73233  ? 123 VAL   B C    1 
ATOM   3698 O  O    . VAL   B 1 123 ? 15.78724  8.18103   63.65770  1.000 32.16533  ? 123 VAL   B O    1 
ATOM   3699 C  CB   . VAL   B 1 123 ? 12.43604  7.51084   63.67557  1.000 31.62029  ? 123 VAL   B CB   1 
ATOM   3700 C  CG1  . VAL   B 1 123 ? 13.15035  6.27743   64.19400  1.000 31.34458  ? 123 VAL   B CG1  1 
ATOM   3701 C  CG2  . VAL   B 1 123 ? 11.20787  7.78795   64.60167  1.000 29.49277  ? 123 VAL   B CG2  1 
ATOM   3702 N  N    . TRP   B 1 124 ? 14.67495  8.12661   61.68619  1.000 27.39489  ? 124 TRP   B N    1 
ATOM   3703 C  CA   . TRP   B 1 124 ? 15.85981  7.63272   60.98873  1.000 28.78149  ? 124 TRP   B CA   1 
ATOM   3704 C  C    . TRP   B 1 124 ? 16.99492  8.62205   61.09487  1.000 31.54557  ? 124 TRP   B C    1 
ATOM   3705 O  O    . TRP   B 1 124 ? 18.16042  8.21956   61.22463  1.000 31.07079  ? 124 TRP   B O    1 
ATOM   3706 C  CB   . TRP   B 1 124 ? 15.54320  7.37250   59.51066  1.000 29.73242  ? 124 TRP   B CB   1 
ATOM   3707 C  CG   . TRP   B 1 124 ? 14.70564  6.14371   59.31796  1.000 29.41642  ? 124 TRP   B CG   1 
ATOM   3708 C  CD1  . TRP   B 1 124 ? 14.79393  4.97166   59.98755  1.000 32.02611  ? 124 TRP   B CD1  1 
ATOM   3709 C  CD2  . TRP   B 1 124 ? 13.65614  5.98922   58.36880  1.000 29.63895  ? 124 TRP   B CD2  1 
ATOM   3710 N  NE1  . TRP   B 1 124 ? 13.86032  4.06868   59.51748  1.000 30.13575  ? 124 TRP   B NE1  1 
ATOM   3711 C  CE2  . TRP   B 1 124 ? 13.14968  4.67094   58.51177  1.000 28.21185  ? 124 TRP   B CE2  1 
ATOM   3712 C  CE3  . TRP   B 1 124 ? 13.11096  6.82848   57.40112  1.000 32.08281  ? 124 TRP   B CE3  1 
ATOM   3713 C  CZ2  . TRP   B 1 124 ? 12.11597  4.17347   57.70240  1.000 28.85431  ? 124 TRP   B CZ2  1 
ATOM   3714 C  CZ3  . TRP   B 1 124 ? 12.08157  6.34467   56.59034  1.000 28.17446  ? 124 TRP   B CZ3  1 
ATOM   3715 C  CH2  . TRP   B 1 124 ? 11.59591  5.02699   56.75828  1.000 31.04190  ? 124 TRP   B CH2  1 
ATOM   3716 N  N    . LYS   B 1 125 ? 16.69817  9.91930   60.98543  1.000 29.42826  ? 125 LYS   B N    1 
ATOM   3717 C  CA   . LYS   B 1 125 ? 17.81715  10.85196  61.12376  1.000 33.53062  ? 125 LYS   B CA   1 
ATOM   3718 C  C    . LYS   B 1 125 ? 18.37252  10.90546  62.53118  1.000 34.58361  ? 125 LYS   B C    1 
ATOM   3719 O  O    . LYS   B 1 125 ? 19.50907  11.37355  62.71127  1.000 34.99374  ? 125 LYS   B O    1 
ATOM   3720 C  CB   . LYS   B 1 125 ? 17.39264  12.25271  60.68083  1.000 32.30474  ? 125 LYS   B CB   1 
ATOM   3721 C  CG   . LYS   B 1 125 ? 17.00320  12.28966  59.19668  1.000 35.34919  ? 125 LYS   B CG   1 
ATOM   3722 C  CD   . LYS   B 1 125 ? 16.55093  13.68296  58.82269  1.000 42.84366  ? 125 LYS   B CD   1 
ATOM   3723 C  CE   . LYS   B 1 125 ? 17.69149  14.66137  58.74378  1.000 51.09814  ? 125 LYS   B CE   1 
ATOM   3724 N  NZ   . LYS   B 1 125 ? 17.08941  16.04358  58.59073  1.000 64.47738  ? 125 LYS   B NZ   1 
ATOM   3725 N  N    . SER   B 1 126 ? 17.61929  10.49457  63.54698  1.000 30.27263  ? 126 SER   B N    1 
ATOM   3726 C  CA   . SER   B 1 126 ? 18.24325  10.53289  64.87003  1.000 29.67008  ? 126 SER   B CA   1 
ATOM   3727 C  C    . SER   B 1 126 ? 18.75118  9.17958   65.32886  1.000 32.02366  ? 126 SER   B C    1 
ATOM   3728 O  O    . SER   B 1 126 ? 19.38801  9.10908   66.37394  1.000 39.16231  ? 126 SER   B O    1 
ATOM   3729 C  CB   . SER   B 1 126 ? 17.23232  11.10231  65.88000  1.000 37.27202  ? 126 SER   B CB   1 
ATOM   3730 O  OG   . SER   B 1 126 ? 16.13050  10.19072  65.97103  1.000 38.51633  ? 126 SER   B OG   1 
ATOM   3731 N  N    . CYS   B 1 127 ? 18.55970  8.11400   64.55127  1.000 29.66965  ? 127 CYS   B N    1 
ATOM   3732 C  CA   . CYS   B 1 127 ? 18.99434  6.77091   64.94693  1.000 31.09800  ? 127 CYS   B CA   1 
ATOM   3733 C  C    . CYS   B 1 127 ? 20.11717  6.25301   64.05957  1.000 36.52220  ? 127 CYS   B C    1 
ATOM   3734 O  O    . CYS   B 1 127 ? 20.35024  5.03836   63.99256  1.000 37.17379  ? 127 CYS   B O    1 
ATOM   3735 C  CB   . CYS   B 1 127 ? 17.84275  5.76817   65.06252  1.000 33.53468  ? 127 CYS   B CB   1 
ATOM   3736 S  SG   . CYS   B 1 127 ? 17.20393  5.10481   63.48141  1.000 36.99061  ? 127 CYS   B SG   1 
ATOM   3737 N  N    . GLY   B 1 128 ? 20.85086  7.15375   63.42694  1.000 32.27857  ? 128 GLY   B N    1 
ATOM   3738 C  CA   . GLY   B 1 128 ? 22.03103  6.81688   62.66021  1.000 34.27269  ? 128 GLY   B CA   1 
ATOM   3739 C  C    . GLY   B 1 128 ? 21.92643  6.94539   61.15038  1.000 37.92109  ? 128 GLY   B C    1 
ATOM   3740 O  O    . GLY   B 1 128 ? 22.82567  6.46542   60.43975  1.000 36.26635  ? 128 GLY   B O    1 
ATOM   3741 N  N    . MET   B 1 129 ? 20.92242  7.65884   60.63333  1.000 28.41615  ? 129 MET   B N    1 
ATOM   3742 C  CA   . MET   B 1 129 ? 20.81181  7.83850   59.20436  1.000 33.95208  ? 129 MET   B CA   1 
ATOM   3743 C  C    . MET   B 1 129 ? 20.70160  9.29329   58.79219  1.000 38.70061  ? 129 MET   B C    1 
ATOM   3744 O  O    . MET   B 1 129 ? 19.99317  9.59816   57.84568  1.000 35.76872  ? 129 MET   B O    1 
ATOM   3745 C  CB   . MET   B 1 129 ? 19.65452  7.02035   58.61685  1.000 33.79445  ? 129 MET   B CB   1 
ATOM   3746 C  CG   . MET   B 1 129 ? 20.19593  5.66250   58.37487  1.000 36.08851  ? 129 MET   B CG   1 
ATOM   3747 S  SD   . MET   B 1 129 ? 19.91766  4.38338   59.47200  1.000 53.20259  ? 129 MET   B SD   1 
ATOM   3748 C  CE   . MET   B 1 129 ? 18.14034  4.28287   59.83157  1.000 38.49112  ? 129 MET   B CE   1 
ATOM   3749 N  N    . ASN   B 1 130 ? 21.35462  10.20791  59.49912  1.000 27.72598  ? 130 ASN   B N    1 
ATOM   3750 C  CA   . ASN   B 1 130 ? 21.44113  11.57468  59.01677  1.000 30.68289  ? 130 ASN   B CA   1 
ATOM   3751 C  C    . ASN   B 1 130 ? 22.71988  11.66014  58.19098  1.000 36.49456  ? 130 ASN   B C    1 
ATOM   3752 O  O    . ASN   B 1 130 ? 23.79471  11.96046  58.71400  1.000 34.58549  ? 130 ASN   B O    1 
ATOM   3753 C  CB   . ASN   B 1 130 ? 21.44951  12.55372  60.18431  1.000 32.00713  ? 130 ASN   B CB   1 
ATOM   3754 C  CG   . ASN   B 1 130 ? 21.35766  13.97913  59.72064  1.000 38.03310  ? 130 ASN   B CG   1 
ATOM   3755 O  OD1  . ASN   B 1 130 ? 21.19302  14.20960  58.55116  1.000 45.91715  ? 130 ASN   B OD1  1 
ATOM   3756 N  ND2  . ASN   B 1 130 ? 21.42128  14.92770  60.63126  1.000 42.78339  ? 130 ASN   B ND2  1 
ATOM   3757 N  N    . MET   B 1 131 ? 22.62082  11.41893  56.88479  1.000 31.22510  ? 131 MET   B N    1 
ATOM   3758 C  CA   . MET   B 1 131 ? 23.87185  11.28333  56.14978  1.000 35.71703  ? 131 MET   B CA   1 
ATOM   3759 C  C    . MET   B 1 131 ? 23.65867  11.40906  54.65530  1.000 37.11655  ? 131 MET   B C    1 
ATOM   3760 O  O    . MET   B 1 131 ? 22.56533  11.13071  54.12360  1.000 33.93643  ? 131 MET   B O    1 
ATOM   3761 C  CB   . MET   B 1 131 ? 24.59835  9.96781   56.52699  1.000 42.07261  ? 131 MET   B CB   1 
ATOM   3762 C  CG   . MET   B 1 131 ? 23.83508  8.69661   56.29124  1.000 41.74062  ? 131 MET   B CG   1 
ATOM   3763 S  SD   . MET   B 1 131 ? 24.40562  7.26504   57.30641  1.000 40.54330  ? 131 MET   B SD   1 
ATOM   3764 C  CE   . MET   B 1 131 ? 25.90268  6.96293   56.40954  1.000 34.74099  ? 131 MET   B CE   1 
ATOM   3765 N  N    . GLU   B 1 132 ? 24.73916  11.84780  53.99066  1.000 30.69128  ? 132 GLU   B N    1 
ATOM   3766 C  CA   . GLU   B 1 132 ? 24.68288  12.16756  52.55441  1.000 31.76756  ? 132 GLU   B CA   1 
ATOM   3767 C  C    . GLU   B 1 132 ? 24.26689  10.97891  51.69658  1.000 37.17744  ? 132 GLU   B C    1 
ATOM   3768 O  O    . GLU   B 1 132 ? 23.48277  11.13200  50.73443  1.000 34.52902  ? 132 GLU   B O    1 
ATOM   3769 C  CB   . GLU   B 1 132 ? 26.05799  12.67429  52.11602  1.000 34.58116  ? 132 GLU   B CB   1 
ATOM   3770 C  CG   . GLU   B 1 132 ? 26.18095  12.94068  50.60174  1.000 37.74998  ? 132 GLU   B CG   1 
ATOM   3771 C  CD   . GLU   B 1 132 ? 27.56335  13.47530  50.23880  1.000 47.35423  ? 132 GLU   B CD   1 
ATOM   3772 O  OE1  . GLU   B 1 132 ? 28.45340  13.58076  51.14778  1.000 38.24477  ? 132 GLU   B OE1  1 
ATOM   3773 O  OE2  . GLU   B 1 132 ? 27.76520  13.79521  49.03200  1.000 41.00736  ? 132 GLU   B OE2  1 
ATOM   3774 N  N    . ASN   B 1 133 ? 24.69753  9.77828   52.06180  1.000 31.92634  ? 133 ASN   B N    1 
ATOM   3775 C  CA   . ASN   B 1 133 ? 24.48854  8.61192   51.21122  1.000 32.48639  ? 133 ASN   B CA   1 
ATOM   3776 C  C    . ASN   B 1 133 ? 23.18451  7.88964   51.47017  1.000 34.33890  ? 133 ASN   B C    1 
ATOM   3777 O  O    . ASN   B 1 133 ? 23.02146  6.78314   50.95023  1.000 37.07943  ? 133 ASN   B O    1 
ATOM   3778 C  CB   . ASN   B 1 133 ? 25.63903  7.58339   51.40088  1.000 32.70566  ? 133 ASN   B CB   1 
ATOM   3779 C  CG   . ASN   B 1 133 ? 26.96929  8.04169   50.78402  1.000 36.32053  ? 133 ASN   B CG   1 
ATOM   3780 O  OD1  . ASN   B 1 133 ? 27.15077  9.22465   50.46305  1.000 40.21942  ? 133 ASN   B OD1  1 
ATOM   3781 N  ND2  . ASN   B 1 133 ? 27.89326  7.08219   50.56650  1.000 35.35926  ? 133 ASN   B ND2  1 
ATOM   3782 N  N    . VAL   B 1 134 ? 22.24790  8.48388   52.22728  1.000 30.44097  ? 134 VAL   B N    1 
ATOM   3783 C  CA   . VAL   B 1 134 ? 20.91060  7.92375   52.46499  1.000 28.52115  ? 134 VAL   B CA   1 
ATOM   3784 C  C    . VAL   B 1 134 ? 19.93894  8.94476   51.90304  1.000 38.70221  ? 134 VAL   B C    1 
ATOM   3785 O  O    . VAL   B 1 134 ? 20.05509  10.13760  52.19873  1.000 35.28271  ? 134 VAL   B O    1 
ATOM   3786 C  CB   . VAL   B 1 134 ? 20.62205  7.67598   53.95531  1.000 33.26147  ? 134 VAL   B CB   1 
ATOM   3787 C  CG1  . VAL   B 1 134 ? 19.18129  7.26372   54.21739  1.000 34.96376  ? 134 VAL   B CG1  1 
ATOM   3788 C  CG2  . VAL   B 1 134 ? 21.56976  6.59704   54.52244  1.000 34.50914  ? 134 VAL   B CG2  1 
ATOM   3789 N  N    . GLN   B 1 135 ? 18.96978  8.48418   51.13263  1.000 30.44687  ? 135 GLN   B N    1 
ATOM   3790 C  CA   . GLN   B 1 135 ? 17.96256  9.38312   50.59084  1.000 34.53721  ? 135 GLN   B CA   1 
ATOM   3791 C  C    . GLN   B 1 135 ? 16.61652  8.91776   51.08235  1.000 30.94607  ? 135 GLN   B C    1 
ATOM   3792 O  O    . GLN   B 1 135 ? 16.36850  7.71996   51.15963  1.000 31.22466  ? 135 GLN   B O    1 
ATOM   3793 C  CB   . GLN   B 1 135 ? 17.92729  9.35485   49.04705  1.000 34.16986  ? 135 GLN   B CB   1 
ATOM   3794 C  CG   . GLN   B 1 135 ? 19.11475  9.85475   48.36587  1.000 44.26050  ? 135 GLN   B CG   1 
ATOM   3795 C  CD   . GLN   B 1 135 ? 18.84785  9.77952   46.89191  1.000 51.70559  ? 135 GLN   B CD   1 
ATOM   3796 O  OE1  . GLN   B 1 135 ? 19.32118  8.87084   46.20648  1.000 57.22474  ? 135 GLN   B OE1  1 
ATOM   3797 N  NE2  . GLN   B 1 135 ? 17.94311  10.63809  46.42781  1.000 50.47765  ? 135 GLN   B NE2  1 
ATOM   3798 N  N    . PHE   B 1 136 ? 15.74551  9.85876   51.42449  1.000 29.75723  ? 136 PHE   B N    1 
ATOM   3799 C  CA   . PHE   B 1 136 ? 14.40033  9.51445   51.85202  1.000 26.49718  ? 136 PHE   B CA   1 
ATOM   3800 C  C    . PHE   B 1 136 ? 13.52672  9.96109   50.68922  1.000 31.31488  ? 136 PHE   B C    1 
ATOM   3801 O  O    . PHE   B 1 136 ? 13.44039  11.16027  50.40976  1.000 33.23766  ? 136 PHE   B O    1 
ATOM   3802 C  CB   . PHE   B 1 136 ? 14.02445  10.23823  53.14331  1.000 28.41110  ? 136 PHE   B CB   1 
ATOM   3803 C  CG   . PHE   B 1 136 ? 14.97429  9.96512   54.30358  1.000 28.71572  ? 136 PHE   B CG   1 
ATOM   3804 C  CD1  . PHE   B 1 136 ? 15.02621  8.71776   54.88953  1.000 28.64423  ? 136 PHE   B CD1  1 
ATOM   3805 C  CD2  . PHE   B 1 136 ? 15.78088  10.97325  54.80020  1.000 31.93783  ? 136 PHE   B CD2  1 
ATOM   3806 C  CE1  . PHE   B 1 136 ? 15.90542  8.42961   55.96023  1.000 30.03961  ? 136 PHE   B CE1  1 
ATOM   3807 C  CE2  . PHE   B 1 136 ? 16.65021  10.72242  55.88038  1.000 33.38098  ? 136 PHE   B CE2  1 
ATOM   3808 C  CZ   . PHE   B 1 136 ? 16.72046  9.45513   56.43322  1.000 34.71719  ? 136 PHE   B CZ   1 
ATOM   3809 N  N    . LEU   B 1 137 ? 12.96450  9.01276   49.96526  1.000 30.24366  ? 137 LEU   B N    1 
ATOM   3810 C  CA   . LEU   B 1 137 ? 12.14396  9.32618   48.78808  1.000 26.95255  ? 137 LEU   B CA   1 
ATOM   3811 C  C    . LEU   B 1 137 ? 10.71294  8.89535   49.07690  1.000 35.06282  ? 137 LEU   B C    1 
ATOM   3812 O  O    . LEU   B 1 137 ? 10.50868  7.89678   49.76187  1.000 30.64262  ? 137 LEU   B O    1 
ATOM   3813 C  CB   . LEU   B 1 137 ? 12.68666  8.59063   47.56223  1.000 27.82609  ? 137 LEU   B CB   1 
ATOM   3814 C  CG   . LEU   B 1 137 ? 14.09338  8.88408   47.11940  1.000 35.66059  ? 137 LEU   B CG   1 
ATOM   3815 C  CD1  . LEU   B 1 137 ? 14.38352  8.06875   45.85290  1.000 36.86246  ? 137 LEU   B CD1  1 
ATOM   3816 C  CD2  . LEU   B 1 137 ? 14.24354  10.40137  46.86406  1.000 40.29305  ? 137 LEU   B CD2  1 
ATOM   3817 N  N    . TRP   B 1 138 ? 9.72935   9.69912   48.64284  1.000 31.70538  ? 138 TRP   B N    1 
ATOM   3818 C  CA   . TRP   B 1 138 ? 8.30731   9.37776   48.82821  1.000 32.26782  ? 138 TRP   B CA   1 
ATOM   3819 C  C    . TRP   B 1 138 ? 7.73935   8.73824   47.55456  1.000 30.04387  ? 138 TRP   B C    1 
ATOM   3820 O  O    . TRP   B 1 138 ? 7.90307   9.27165   46.46435  1.000 29.67854  ? 138 TRP   B O    1 
ATOM   3821 C  CB   . TRP   B 1 138 ? 7.52202   10.64569  49.18832  1.000 29.00248  ? 138 TRP   B CB   1 
ATOM   3822 C  CG   . TRP   B 1 138 ? 7.90313   11.23800  50.49084  1.000 36.15500  ? 138 TRP   B CG   1 
ATOM   3823 C  CD1  . TRP   B 1 138 ? 9.03868   11.96753  50.77500  1.000 31.94320  ? 138 TRP   B CD1  1 
ATOM   3824 C  CD2  . TRP   B 1 138 ? 7.14761   11.18544  51.68553  1.000 35.13739  ? 138 TRP   B CD2  1 
ATOM   3825 N  NE1  . TRP   B 1 138 ? 8.99994   12.39042  52.08114  1.000 37.80243  ? 138 TRP   B NE1  1 
ATOM   3826 C  CE2  . TRP   B 1 138 ? 7.84894   11.92926  52.66152  1.000 33.09390  ? 138 TRP   B CE2  1 
ATOM   3827 C  CE3  . TRP   B 1 138 ? 5.92795   10.58287  52.03347  1.000 30.77765  ? 138 TRP   B CE3  1 
ATOM   3828 C  CZ2  . TRP   B 1 138 ? 7.37184   12.08223  53.95524  1.000 37.81484  ? 138 TRP   B CZ2  1 
ATOM   3829 C  CZ3  . TRP   B 1 138 ? 5.45422   10.74371  53.30381  1.000 36.82530  ? 138 TRP   B CZ3  1 
ATOM   3830 C  CH2  . TRP   B 1 138 ? 6.16015   11.49773  54.24946  1.000 34.77739  ? 138 TRP   B CH2  1 
ATOM   3831 N  N    . ALA   B 1 139 ? 7.08453   7.58807   47.69246  1.000 28.29380  ? 139 ALA   B N    1 
ATOM   3832 C  CA   . ALA   B 1 139 ? 6.63859   6.88236   46.51274  1.000 29.10438  ? 139 ALA   B CA   1 
ATOM   3833 C  C    . ALA   B 1 139 ? 5.74230   7.78500   45.66285  1.000 33.52323  ? 139 ALA   B C    1 
ATOM   3834 O  O    . ALA   B 1 139 ? 5.99134   7.96913   44.47368  1.000 29.86585  ? 139 ALA   B O    1 
ATOM   3835 C  CB   . ALA   B 1 139 ? 5.91977   5.58751   46.91752  1.000 27.83870  ? 139 ALA   B CB   1 
ATOM   3836 N  N    . SER   B 1 140 ? 4.74496   8.41235   46.28047  1.000 35.63089  ? 140 SER   B N    1 
ATOM   3837 C  CA   . SER   B 1 140 ? 3.79147   9.22136   45.51883  1.000 38.13782  ? 140 SER   B CA   1 
ATOM   3838 C  C    . SER   B 1 140 ? 4.49389   10.35157  44.76222  1.000 37.84443  ? 140 SER   B C    1 
ATOM   3839 O  O    . SER   B 1 140 ? 4.23920   10.55700  43.57041  1.000 35.41626  ? 140 SER   B O    1 
ATOM   3840 C  CB   . SER   B 1 140 ? 2.73837   9.78537   46.48135  1.000 38.29498  ? 140 SER   B CB   1 
ATOM   3841 O  OG   . SER   B 1 140 ? 3.38340   10.55441  47.48634  1.000 41.39643  ? 140 SER   B OG   1 
ATOM   3842 N  N    . GLU   B 1 141 ? 5.39018   11.09620  45.44521  1.000 36.34643  ? 141 GLU   B N    1 
ATOM   3843 C  CA   . GLU   B 1 141 ? 6.12332   12.18633  44.79370  1.000 34.05122  ? 141 GLU   B CA   1 
ATOM   3844 C  C    . GLU   B 1 141 ? 6.93590   11.66549  43.61806  1.000 32.67652  ? 141 GLU   B C    1 
ATOM   3845 O  O    . GLU   B 1 141 ? 6.96754   12.27452  42.53309  1.000 34.62886  ? 141 GLU   B O    1 
ATOM   3846 C  CB   . GLU   B 1 141 ? 7.11597   12.86126  45.77093  1.000 34.69468  ? 141 GLU   B CB   1 
ATOM   3847 C  CG   . GLU   B 1 141 ? 6.46475   13.55976  46.91439  1.000 46.16556  ? 141 GLU   B CG   1 
ATOM   3848 C  CD   . GLU   B 1 141 ? 7.44422   14.29509  47.79983  1.000 55.63528  ? 141 GLU   B CD   1 
ATOM   3849 O  OE1  . GLU   B 1 141 ? 6.94108   14.94124  48.76342  1.000 59.60356  ? 141 GLU   B OE1  1 
ATOM   3850 O  OE2  . GLU   B 1 141 ? 8.67810   14.20952  47.54082  1.000 49.74704  ? 141 GLU   B OE2  1 
ATOM   3851 N  N    . GLU   B 1 142 ? 7.64381   10.54910  43.82132  1.000 33.37492  ? 142 GLU   B N    1 
ATOM   3852 C  CA   . GLU   B 1 142 ? 8.55802   10.10442  42.76298  1.000 31.32534  ? 142 GLU   B CA   1 
ATOM   3853 C  C    . GLU   B 1 142 ? 7.79647   9.52054   41.57923  1.000 35.70130  ? 142 GLU   B C    1 
ATOM   3854 O  O    . GLU   B 1 142 ? 8.16898   9.75341   40.43343  1.000 36.05730  ? 142 GLU   B O    1 
ATOM   3855 C  CB   . GLU   B 1 142 ? 9.60846   9.10002   43.29361  1.000 31.29721  ? 142 GLU   B CB   1 
ATOM   3856 C  CG   . GLU   B 1 142 ? 10.56782  9.70100   44.42633  1.000 31.33951  ? 142 GLU   B CG   1 
ATOM   3857 C  CD   . GLU   B 1 142 ? 11.34115  10.92380  43.93138  1.000 39.65073  ? 142 GLU   B CD   1 
ATOM   3858 O  OE1  . GLU   B 1 142 ? 11.92327  10.85364  42.83291  1.000 37.91941  ? 142 GLU   B OE1  1 
ATOM   3859 O  OE2  . GLU   B 1 142 ? 11.30786  11.99824  44.58546  1.000 40.70122  ? 142 GLU   B OE2  1 
ATOM   3860 N  N    . ILE   B 1 143 ? 6.71582   8.77867   41.84340  1.000 32.23544  ? 143 ILE   B N    1 
ATOM   3861 C  CA   . ILE   B 1 143 ? 5.89765   8.24380   40.77113  1.000 34.97463  ? 143 ILE   B CA   1 
ATOM   3862 C  C    . ILE   B 1 143 ? 5.30078   9.37460   39.97027  1.000 37.10418  ? 143 ILE   B C    1 
ATOM   3863 O  O    . ILE   B 1 143 ? 5.36844   9.37463   38.74166  1.000 35.09513  ? 143 ILE   B O    1 
ATOM   3864 C  CB   . ILE   B 1 143 ? 4.80922   7.33707   41.34777  1.000 35.20552  ? 143 ILE   B CB   1 
ATOM   3865 C  CG1  . ILE   B 1 143 ? 5.46213   6.04421   41.84607  1.000 30.09621  ? 143 ILE   B CG1  1 
ATOM   3866 C  CG2  . ILE   B 1 143 ? 3.63823   7.08104   40.26870  1.000 33.50592  ? 143 ILE   B CG2  1 
ATOM   3867 C  CD1  . ILE   B 1 143 ? 4.49558   5.25964   42.78281  1.000 31.38045  ? 143 ILE   B CD1  1 
ATOM   3868 N  N    . ASN   B 1 144 ? 4.78272   10.39363  40.64434  1.000 37.19857  ? 144 ASN   B N    1 
ATOM   3869 C  CA   . ASN   B 1 144 ? 4.16158   11.50942  39.92817  1.000 37.55936  ? 144 ASN   B CA   1 
ATOM   3870 C  C    . ASN   B 1 144 ? 5.14169   12.43160  39.19916  1.000 39.82285  ? 144 ASN   B C    1 
ATOM   3871 O  O    . ASN   B 1 144 ? 4.68553   13.23563  38.36592  1.000 41.76289  ? 144 ASN   B O    1 
ATOM   3872 C  CB   . ASN   B 1 144 ? 3.31661   12.27920  40.92458  1.000 36.08422  ? 144 ASN   B CB   1 
ATOM   3873 C  CG   . ASN   B 1 144 ? 2.00040   11.56273  41.21125  1.000 40.12883  ? 144 ASN   B CG   1 
ATOM   3874 O  OD1  . ASN   B 1 144 ? 1.31229   11.14613  40.27472  1.000 47.17410  ? 144 ASN   B OD1  1 
ATOM   3875 N  ND2  . ASN   B 1 144 ? 1.64446   11.42305  42.47112  1.000 41.50356  ? 144 ASN   B ND2  1 
ATOM   3876 N  N    . LYS   B 1 145 ? 6.45248   12.36476  39.47767  1.000 38.14973  ? 145 LYS   B N    1 
ATOM   3877 C  CA   . LYS   B 1 145 ? 7.41932   13.02944  38.59121  1.000 37.25013  ? 145 LYS   B CA   1 
ATOM   3878 C  C    . LYS   B 1 145 ? 7.58227   12.34912  37.22371  1.000 39.94176  ? 145 LYS   B C    1 
ATOM   3879 O  O    . LYS   B 1 145 ? 7.96092   13.01526  36.24593  1.000 39.82093  ? 145 LYS   B O    1 
ATOM   3880 C  CB   . LYS   B 1 145 ? 8.81519   13.08203  39.24238  1.000 40.19762  ? 145 LYS   B CB   1 
ATOM   3881 C  CG   . LYS   B 1 145 ? 8.86255   13.97562  40.45643  1.000 45.50056  ? 145 LYS   B CG   1 
ATOM   3882 C  CD   . LYS   B 1 145 ? 10.20058  13.87122  41.17462  1.000 49.92842  ? 145 LYS   B CD   1 
ATOM   3883 C  CE   . LYS   B 1 145 ? 10.10666  14.70815  42.44248  1.000 54.67129  ? 145 LYS   B CE   1 
ATOM   3884 N  NZ   . LYS   B 1 145 ? 11.23874  14.54276  43.35014  1.000 50.65820  ? 145 LYS   B NZ   1 
ATOM   3885 N  N    . LYS   B 1 146 ? 7.39803   11.03335  37.12825  1.000 36.86023  ? 146 LYS   B N    1 
ATOM   3886 C  CA   . LYS   B 1 146 ? 7.63190   10.31395  35.87472  1.000 38.60697  ? 146 LYS   B CA   1 
ATOM   3887 C  C    . LYS   B 1 146 ? 6.54830   9.26692   35.70121  1.000 35.16153  ? 146 LYS   B C    1 
ATOM   3888 O  O    . LYS   B 1 146 ? 6.81117   8.05988   35.65993  1.000 30.75536  ? 146 LYS   B O    1 
ATOM   3889 C  CB   . LYS   B 1 146 ? 9.02901   9.68034   35.87722  1.000 42.79976  ? 146 LYS   B CB   1 
ATOM   3890 C  CG   . LYS   B 1 146 ? 10.13819  10.69733  36.00915  1.000 42.69925  ? 146 LYS   B CG   1 
ATOM   3891 C  CD   . LYS   B 1 146 ? 11.52420  10.11802  35.68232  1.000 49.26628  ? 146 LYS   B CD   1 
ATOM   3892 C  CE   . LYS   B 1 146 ? 12.08420  9.39811   36.86471  1.000 56.78198  ? 146 LYS   B CE   1 
ATOM   3893 N  NZ   . LYS   B 1 146 ? 13.39622  8.76509   36.51757  1.000 60.93428  ? 146 LYS   B NZ   1 
ATOM   3894 N  N    . PRO   B 1 147 ? 5.29376   9.70672   35.65167  1.000 35.61996  ? 147 PRO   B N    1 
ATOM   3895 C  CA   . PRO   B 1 147 ? 4.18569   8.74919   35.75859  1.000 38.39544  ? 147 PRO   B CA   1 
ATOM   3896 C  C    . PRO   B 1 147 ? 3.97365   7.92459   34.49339  1.000 33.76477  ? 147 PRO   B C    1 
ATOM   3897 O  O    . PRO   B 1 147 ? 3.49785   6.78235   34.59476  1.000 33.77129  ? 147 PRO   B O    1 
ATOM   3898 C  CB   . PRO   B 1 147 ? 2.96723   9.64699   36.07279  1.000 37.47589  ? 147 PRO   B CB   1 
ATOM   3899 C  CG   . PRO   B 1 147 ? 3.29812   10.95178  35.38868  1.000 41.35601  ? 147 PRO   B CG   1 
ATOM   3900 C  CD   . PRO   B 1 147 ? 4.84762   11.10660  35.61274  1.000 35.31666  ? 147 PRO   B CD   1 
ATOM   3901 N  N    . ASN   B 1 148 ? 4.33935   8.42368   33.31291  1.000 32.55298  ? 148 ASN   B N    1 
ATOM   3902 C  CA   . ASN   B 1 148 ? 4.24398   7.56903   32.12250  1.000 34.37784  ? 148 ASN   B CA   1 
ATOM   3903 C  C    . ASN   B 1 148 ? 5.22347   6.40603   32.21871  1.000 38.01371  ? 148 ASN   B C    1 
ATOM   3904 O  O    . ASN   B 1 148 ? 4.85714   5.23596   32.04590  1.000 34.57813  ? 148 ASN   B O    1 
ATOM   3905 C  CB   . ASN   B 1 148 ? 4.47089   8.38763   30.84755  1.000 36.98040  ? 148 ASN   B CB   1 
ATOM   3906 C  CG   . ASN   B 1 148 ? 4.25952   7.55344   29.55710  1.000 39.02489  ? 148 ASN   B CG   1 
ATOM   3907 O  OD1  . ASN   B 1 148 ? 3.14651   7.32686   29.15293  1.000 49.20040  ? 148 ASN   B OD1  1 
ATOM   3908 N  ND2  . ASN   B 1 148 ? 5.34791   7.09349   28.93161  1.000 44.99115  ? 148 ASN   B ND2  1 
ATOM   3909 N  N    . GLU   B 1 149 ? 6.47485   6.70054   32.55713  1.000 34.09654  ? 149 GLU   B N    1 
ATOM   3910 C  CA   . GLU   B 1 149 ? 7.43749   5.62717   32.77668  1.000 34.46062  ? 149 GLU   B CA   1 
ATOM   3911 C  C    . GLU   B 1 149 ? 6.97501   4.63360   33.86376  1.000 31.61508  ? 149 GLU   B C    1 
ATOM   3912 O  O    . GLU   B 1 149 ? 7.08742   3.39693   33.68791  1.000 34.45549  ? 149 GLU   B O    1 
ATOM   3913 C  CB   . GLU   B 1 149 ? 8.77044   6.24886   33.18004  1.000 36.74149  ? 149 GLU   B CB   1 
ATOM   3914 C  CG   . GLU   B 1 149 ? 9.75498   5.20447   33.48023  1.000 36.78288  ? 149 GLU   B CG   1 
ATOM   3915 C  CD   . GLU   B 1 149 ? 11.09828  5.82678   33.84820  1.000 52.67580  ? 149 GLU   B CD   1 
ATOM   3916 O  OE1  . GLU   B 1 149 ? 11.36138  6.98361   33.41698  1.000 51.95300  ? 149 GLU   B OE1  1 
ATOM   3917 O  OE2  . GLU   B 1 149 ? 11.89538  5.13448   34.50692  1.000 42.97231  ? 149 GLU   B OE2  1 
ATOM   3918 N  N    . TYR   B 1 150 ? 6.49490   5.15582   35.00753  1.000 31.10437  ? 150 TYR   B N    1 
ATOM   3919 C  CA   . TYR   B 1 150 ? 6.18321   4.27525   36.14580  1.000 29.31038  ? 150 TYR   B CA   1 
ATOM   3920 C  C    . TYR   B 1 150 ? 5.02636   3.36657   35.81708  1.000 31.26535  ? 150 TYR   B C    1 
ATOM   3921 O  O    . TYR   B 1 150 ? 5.12291   2.13072   35.91647  1.000 29.45600  ? 150 TYR   B O    1 
ATOM   3922 C  CB   . TYR   B 1 150 ? 5.83901   5.04048   37.40246  1.000 28.90989  ? 150 TYR   B CB   1 
ATOM   3923 C  CG   . TYR   B 1 150 ? 5.63018   4.11536   38.57688  1.000 31.40851  ? 150 TYR   B CG   1 
ATOM   3924 C  CD1  . TYR   B 1 150 ? 6.71490   3.59121   39.27529  1.000 28.77845  ? 150 TYR   B CD1  1 
ATOM   3925 C  CD2  . TYR   B 1 150 ? 4.36007   3.75985   39.00707  1.000 26.45962  ? 150 TYR   B CD2  1 
ATOM   3926 C  CE1  . TYR   B 1 150 ? 6.51219   2.72504   40.37831  1.000 28.64499  ? 150 TYR   B CE1  1 
ATOM   3927 C  CE2  . TYR   B 1 150 ? 4.17017   2.90959   40.09598  1.000 27.76827  ? 150 TYR   B CE2  1 
ATOM   3928 C  CZ   . TYR   B 1 150 ? 5.25128   2.41882   40.77276  1.000 30.81406  ? 150 TYR   B CZ   1 
ATOM   3929 O  OH   . TYR   B 1 150 ? 5.01469   1.61373   41.78887  1.000 32.49443  ? 150 TYR   B OH   1 
ATOM   3930 N  N    . TRP   B 1 151 ? 3.90109   3.97367   35.43705  1.000 30.75981  ? 151 TRP   B N    1 
ATOM   3931 C  CA   . TRP   B 1 151 ? 2.73630   3.13256   35.20262  1.000 30.92511  ? 151 TRP   B CA   1 
ATOM   3932 C  C    . TRP   B 1 151 ? 2.89428   2.27448   33.94691  1.000 28.72642  ? 151 TRP   B C    1 
ATOM   3933 O  O    . TRP   B 1 151 ? 2.37270   1.13876   33.92352  1.000 32.66044  ? 151 TRP   B O    1 
ATOM   3934 C  CB   . TRP   B 1 151 ? 1.49874   4.04666   35.18895  1.000 28.46102  ? 151 TRP   B CB   1 
ATOM   3935 C  CG   . TRP   B 1 151 ? 1.27766   4.63422   36.53974  1.000 29.01679  ? 151 TRP   B CG   1 
ATOM   3936 C  CD1  . TRP   B 1 151 ? 1.46381   5.93321   36.91428  1.000 28.16308  ? 151 TRP   B CD1  1 
ATOM   3937 C  CD2  . TRP   B 1 151 ? 0.84698   3.93868   37.73310  1.000 29.18773  ? 151 TRP   B CD2  1 
ATOM   3938 N  NE1  . TRP   B 1 151 ? 1.20016   6.08636   38.24638  1.000 29.49442  ? 151 TRP   B NE1  1 
ATOM   3939 C  CE2  . TRP   B 1 151 ? 0.79623   4.88024   38.76620  1.000 26.12539  ? 151 TRP   B CE2  1 
ATOM   3940 C  CE3  . TRP   B 1 151 ? 0.44927   2.62680   38.00020  1.000 31.87654  ? 151 TRP   B CE3  1 
ATOM   3941 C  CZ2  . TRP   B 1 151 ? 0.40986   4.56170   40.04106  1.000 30.19305  ? 151 TRP   B CZ2  1 
ATOM   3942 C  CZ3  . TRP   B 1 151 ? 0.06054   2.29765   39.29347  1.000 30.52993  ? 151 TRP   B CZ3  1 
ATOM   3943 C  CH2  . TRP   B 1 151 ? 0.03666   3.26008   40.30512  1.000 32.77523  ? 151 TRP   B CH2  1 
ATOM   3944 N  N    . SER   B 1 152 ? 3.71142   2.68235   32.94008  1.000 28.46063  ? 152 SER   B N    1 
ATOM   3945 C  CA   . SER   B 1 152 ? 3.95985   1.77098   31.82543  1.000 34.78306  ? 152 SER   B CA   1 
ATOM   3946 C  C    . SER   B 1 152 ? 4.69503   0.51969   32.28033  1.000 36.97052  ? 152 SER   B C    1 
ATOM   3947 O  O    . SER   B 1 152 ? 4.41164   -0.58830  31.78550  1.000 35.03075  ? 152 SER   B O    1 
ATOM   3948 C  CB   . SER   B 1 152 ? 4.73512   2.46294   30.70190  1.000 34.85398  ? 152 SER   B CB   1 
ATOM   3949 O  OG   . SER   B 1 152 ? 3.96054   3.54406   30.19146  1.000 37.80445  ? 152 SER   B OG   1 
ATOM   3950 N  N    . LEU   B 1 153 ? 5.65603   0.66900   33.19648  1.000 33.46345  ? 153 LEU   B N    1 
ATOM   3951 C  CA   . LEU   B 1 153 ? 6.27306   -0.51079  33.81011  1.000 30.62129  ? 153 LEU   B CA   1 
ATOM   3952 C  C    . LEU   B 1 153 ? 5.25026   -1.37502  34.52117  1.000 29.76120  ? 153 LEU   B C    1 
ATOM   3953 O  O    . LEU   B 1 153 ? 5.27043   -2.60403  34.40577  1.000 32.11992  ? 153 LEU   B O    1 
ATOM   3954 C  CB   . LEU   B 1 153 ? 7.32886   -0.11717  34.87306  1.000 32.26405  ? 153 LEU   B CB   1 
ATOM   3955 C  CG   . LEU   B 1 153 ? 8.78192   -0.33283  34.65088  1.000 48.61104  ? 153 LEU   B CG   1 
ATOM   3956 C  CD1  . LEU   B 1 153 ? 9.47254   0.07514   35.97162  1.000 35.91781  ? 153 LEU   B CD1  1 
ATOM   3957 C  CD2  . LEU   B 1 153 ? 8.93563   -1.81034  34.25725  1.000 40.13914  ? 153 LEU   B CD2  1 
ATOM   3958 N  N    . VAL   B 1 154 ? 4.43681   -0.75137  35.36077  1.000 28.61869  ? 154 VAL   B N    1 
ATOM   3959 C  CA   . VAL   B 1 154 ? 3.44252   -1.50599  36.12906  1.000 33.45921  ? 154 VAL   B CA   1 
ATOM   3960 C  C    . VAL   B 1 154 ? 2.57836   -2.33148  35.17129  1.000 34.99687  ? 154 VAL   B C    1 
ATOM   3961 O  O    . VAL   B 1 154 ? 2.37576   -3.53694  35.35986  1.000 32.38117  ? 154 VAL   B O    1 
ATOM   3962 C  CB   . VAL   B 1 154 ? 2.58708   -0.55805  36.98293  1.000 27.04830  ? 154 VAL   B CB   1 
ATOM   3963 C  CG1  . VAL   B 1 154 ? 1.47718   -1.35424  37.66658  1.000 31.37749  ? 154 VAL   B CG1  1 
ATOM   3964 C  CG2  . VAL   B 1 154 ? 3.38175   0.06400   38.17361  1.000 28.48471  ? 154 VAL   B CG2  1 
ATOM   3965 N  N    . LEU   B 1 155 ? 2.07766   -1.68534  34.11379  1.000 34.28788  ? 155 LEU   B N    1 
ATOM   3966 C  CA   . LEU   B 1 155 ? 1.23185   -2.38335  33.13204  1.000 31.43445  ? 155 LEU   B CA   1 
ATOM   3967 C  C    . LEU   B 1 155 ? 2.00576   -3.50890  32.41438  1.000 30.34536  ? 155 LEU   B C    1 
ATOM   3968 O  O    . LEU   B 1 155 ? 1.48425   -4.63236  32.23670  1.000 30.76076  ? 155 LEU   B O    1 
ATOM   3969 C  CB   . LEU   B 1 155 ? 0.69006   -1.35513  32.12587  1.000 34.40084  ? 155 LEU   B CB   1 
ATOM   3970 C  CG   . LEU   B 1 155 ? -0.46058  -0.47729  32.67492  1.000 41.83668  ? 155 LEU   B CG   1 
ATOM   3971 C  CD1  . LEU   B 1 155 ? -1.21273  0.19095   31.57190  1.000 35.12188  ? 155 LEU   B CD1  1 
ATOM   3972 C  CD2  . LEU   B 1 155 ? -1.36812  -1.28961  33.51370  1.000 43.82074  ? 155 LEU   B CD2  1 
ATOM   3973 N  N    . ASP   B 1 156 ? 3.28124   -3.27286  32.06094  1.000 32.31810  ? 156 ASP   B N    1 
ATOM   3974 C  CA   . ASP   B 1 156 ? 4.03784   -4.33056  31.38646  1.000 33.65826  ? 156 ASP   B CA   1 
ATOM   3975 C  C    . ASP   B 1 156 ? 4.29255   -5.53600  32.27577  1.000 31.60611  ? 156 ASP   B C    1 
ATOM   3976 O  O    . ASP   B 1 156 ? 4.26827   -6.69881  31.79791  1.000 35.28897  ? 156 ASP   B O    1 
ATOM   3977 C  CB   . ASP   B 1 156 ? 5.35353   -3.77403  30.81568  1.000 37.49486  ? 156 ASP   B CB   1 
ATOM   3978 C  CG   . ASP   B 1 156 ? 5.10360   -3.00653  29.47035  1.000 57.27225  ? 156 ASP   B CG   1 
ATOM   3979 O  OD1  . ASP   B 1 156 ? 5.97613   -2.18881  29.05864  1.000 55.41255  ? 156 ASP   B OD1  1 
ATOM   3980 O  OD2  . ASP   B 1 156 ? 3.99276   -3.20510  28.84999  1.000 52.62271  ? 156 ASP   B OD2  1 
ATOM   3981 N  N    . ILE   B 1 157 ? 4.60275   -5.28317  33.56400  1.000 32.43726  ? 157 ILE   B N    1 
ATOM   3982 C  CA   . ILE   B 1 157 ? 4.71926   -6.37773  34.51129  1.000 35.30306  ? 157 ILE   B CA   1 
ATOM   3983 C  C    . ILE   B 1 157 ? 3.41788   -7.13487  34.58690  1.000 33.32058  ? 157 ILE   B C    1 
ATOM   3984 O  O    . ILE   B 1 157 ? 3.41748   -8.36666  34.55936  1.000 34.48196  ? 157 ILE   B O    1 
ATOM   3985 C  CB   . ILE   B 1 157 ? 5.16803   -5.85664  35.89776  1.000 31.81784  ? 157 ILE   B CB   1 
ATOM   3986 C  CG1  . ILE   B 1 157 ? 6.59229   -5.34269  35.77320  1.000 32.73885  ? 157 ILE   B CG1  1 
ATOM   3987 C  CG2  . ILE   B 1 157 ? 5.03569   -6.92523  37.01420  1.000 27.56691  ? 157 ILE   B CG2  1 
ATOM   3988 C  CD1  . ILE   B 1 157 ? 6.97629   -4.49295  37.00138  1.000 30.18875  ? 157 ILE   B CD1  1 
ATOM   3989 N  N    . SER   B 1 158 ? 2.27565   -6.41169  34.68174  1.000 31.70010  ? 158 SER   B N    1 
ATOM   3990 C  CA   . SER   B 1 158 ? 0.99213   -7.12030  34.78126  1.000 34.09335  ? 158 SER   B CA   1 
ATOM   3991 C  C    . SER   B 1 158 ? 0.72289   -8.00270  33.54885  1.000 35.26903  ? 158 SER   B C    1 
ATOM   3992 O  O    . SER   B 1 158 ? 0.08819   -9.06882  33.65959  1.000 36.35699  ? 158 SER   B O    1 
ATOM   3993 C  CB   . SER   B 1 158 ? -0.18478  -6.11775  34.94682  1.000 33.52595  ? 158 SER   B CB   1 
ATOM   3994 O  OG   . SER   B 1 158 ? -0.54593  -5.60060  33.65722  1.000 34.44577  ? 158 SER   B OG   1 
ATOM   3995 N  N    . ARG   B 1 159 ? 1.17874   -7.58465  32.36924  1.000 33.82803  ? 159 ARG   B N    1 
ATOM   3996 C  CA   . ARG   B 1 159 ? 1.02662   -8.42751  31.17496  1.000 31.45378  ? 159 ARG   B CA   1 
ATOM   3997 C  C    . ARG   B 1 159 ? 1.89904   -9.67873  31.20264  1.000 40.19941  ? 159 ARG   B C    1 
ATOM   3998 O  O    . ARG   B 1 159 ? 1.61972   -10.63949 30.47884  1.000 34.48974  ? 159 ARG   B O    1 
ATOM   3999 C  CB   . ARG   B 1 159 ? 1.41402   -7.65323  29.93163  1.000 42.14444  ? 159 ARG   B CB   1 
ATOM   4000 C  CG   . ARG   B 1 159 ? 0.50672   -6.47496  29.68620  1.000 33.08557  ? 159 ARG   B CG   1 
ATOM   4001 C  CD   . ARG   B 1 159 ? 1.11261   -5.57436  28.61240  1.000 40.95825  ? 159 ARG   B CD   1 
ATOM   4002 N  NE   . ARG   B 1 159 ? 1.13044   -6.22814  27.31778  1.000 42.67645  ? 159 ARG   B NE   1 
ATOM   4003 C  CZ   . ARG   B 1 159 ? 2.09051   -6.09484  26.41149  1.000 49.80853  ? 159 ARG   B CZ   1 
ATOM   4004 N  NH1  . ARG   B 1 159 ? 3.20956   -5.44093  26.67975  1.000 47.74249  ? 159 ARG   B NH1  1 
ATOM   4005 N  NH2  . ARG   B 1 159 ? 1.92024   -6.62281  25.20281  1.000 44.94110  ? 159 ARG   B NH2  1 
ATOM   4006 N  N    . SER   B 1 160 ? 2.97747   -9.67102  31.98980  1.000 35.88115  ? 160 SER   B N    1 
ATOM   4007 C  CA   . SER   B 1 160 ? 3.94332   -10.77990 31.96402  1.000 40.32937  ? 160 SER   B CA   1 
ATOM   4008 C  C    . SER   B 1 160 ? 3.66976   -11.94049 32.91642  1.000 39.59474  ? 160 SER   B C    1 
ATOM   4009 O  O    . SER   B 1 160 ? 4.27343   -12.99944 32.75741  1.000 41.07116  ? 160 SER   B O    1 
ATOM   4010 C  CB   . SER   B 1 160 ? 5.34256   -10.23056 32.30202  1.000 37.97207  ? 160 SER   B CB   1 
ATOM   4011 O  OG   . SER   B 1 160 ? 5.66653   -9.34023  31.25603  1.000 43.44625  ? 160 SER   B OG   1 
ATOM   4012 N  N    . PHE   B 1 161 ? 2.81122   -11.79220 33.90375  1.000 37.79485  ? 161 PHE   B N    1 
ATOM   4013 C  CA   . PHE   B 1 161 ? 2.65125   -12.81926 34.92908  1.000 41.43796  ? 161 PHE   B CA   1 
ATOM   4014 C  C    . PHE   B 1 161 ? 1.17936   -13.12829 35.11712  1.000 39.29091  ? 161 PHE   B C    1 
ATOM   4015 O  O    . PHE   B 1 161 ? 0.35806   -12.22426 35.03864  1.000 37.37137  ? 161 PHE   B O    1 
ATOM   4016 C  CB   . PHE   B 1 161 ? 3.19749   -12.37005 36.26969  1.000 37.58703  ? 161 PHE   B CB   1 
ATOM   4017 C  CG   . PHE   B 1 161 ? 4.68211   -12.15246 36.25674  1.000 36.82692  ? 161 PHE   B CG   1 
ATOM   4018 C  CD1  . PHE   B 1 161 ? 5.53820   -13.23625 36.19971  1.000 39.31075  ? 161 PHE   B CD1  1 
ATOM   4019 C  CD2  . PHE   B 1 161 ? 5.20237   -10.87056 36.30530  1.000 36.45227  ? 161 PHE   B CD2  1 
ATOM   4020 C  CE1  . PHE   B 1 161 ? 6.92629   -13.03887 36.19588  1.000 38.94805  ? 161 PHE   B CE1  1 
ATOM   4021 C  CE2  . PHE   B 1 161 ? 6.60144   -10.65158 36.29420  1.000 36.94408  ? 161 PHE   B CE2  1 
ATOM   4022 C  CZ   . PHE   B 1 161 ? 7.45206   -11.74501 36.24794  1.000 38.38093  ? 161 PHE   B CZ   1 
ATOM   4023 N  N    . ASN   B 1 162 ? 0.86191   -14.38130 35.43474  1.000 41.36020  ? 162 ASN   B N    1 
ATOM   4024 C  CA   . ASN   B 1 162 ? -0.54625  -14.71575 35.62960  1.000 42.99524  ? 162 ASN   B CA   1 
ATOM   4025 C  C    . ASN   B 1 162 ? -0.95137  -14.45651 37.08083  1.000 42.54097  ? 162 ASN   B C    1 
ATOM   4026 O  O    . ASN   B 1 162 ? -0.10919  -14.19167 37.95151  1.000 39.00519  ? 162 ASN   B O    1 
ATOM   4027 C  CB   . ASN   B 1 162 ? -0.85317  -16.15402 35.18776  1.000 42.66925  ? 162 ASN   B CB   1 
ATOM   4028 C  CG   . ASN   B 1 162 ? -0.21132  -17.21213 36.03897  1.000 51.28672  ? 162 ASN   B CG   1 
ATOM   4029 O  OD1  . ASN   B 1 162 ? -0.02582  -17.05593 37.24710  1.000 46.01224  ? 162 ASN   B OD1  1 
ATOM   4030 N  ND2  . ASN   B 1 162 ? 0.10000   -18.34863 35.40036  1.000 54.48319  ? 162 ASN   B ND2  1 
ATOM   4031 N  N    . ILE   B 1 163 ? -2.27455  -14.44154 37.31420  1.000 41.07309  ? 163 ILE   B N    1 
ATOM   4032 C  CA   . ILE   B 1 163 ? -2.82333  -14.03685 38.61291  1.000 36.32689  ? 163 ILE   B CA   1 
ATOM   4033 C  C    . ILE   B 1 163 ? -2.29839  -14.92735 39.72530  1.000 42.73597  ? 163 ILE   B C    1 
ATOM   4034 O  O    . ILE   B 1 163 ? -1.96188  -14.44197 40.80673  1.000 39.83683  ? 163 ILE   B O    1 
ATOM   4035 C  CB   . ILE   B 1 163 ? -4.36845  -14.04746 38.57992  1.000 38.16444  ? 163 ILE   B CB   1 
ATOM   4036 C  CG1  . ILE   B 1 163 ? -4.85298  -12.84905 37.78002  1.000 37.56101  ? 163 ILE   B CG1  1 
ATOM   4037 C  CG2  . ILE   B 1 163 ? -4.91678  -13.94991 39.99063  1.000 42.51934  ? 163 ILE   B CG2  1 
ATOM   4038 C  CD1  . ILE   B 1 163 ? -6.33687  -13.00726 37.24140  1.000 38.57693  ? 163 ILE   B CD1  1 
ATOM   4039 N  N    . ASN   B 1 164 ? -2.21960  -16.24173 39.49328  1.000 41.60893  ? 164 ASN   B N    1 
ATOM   4040 C  CA   . ASN   B 1 164 ? -1.73572  -17.11392 40.56619  1.000 44.65364  ? 164 ASN   B CA   1 
ATOM   4041 C  C    . ASN   B 1 164 ? -0.30536  -16.77408 40.95552  1.000 46.16734  ? 164 ASN   B C    1 
ATOM   4042 O  O    . ASN   B 1 164 ? 0.04229   -16.76942 42.15541  1.000 45.04082  ? 164 ASN   B O    1 
ATOM   4043 C  CB   . ASN   B 1 164 ? -1.84451  -18.58374 40.15203  1.000 48.00835  ? 164 ASN   B CB   1 
ATOM   4044 C  CG   . ASN   B 1 164 ? -3.27599  -19.08672 40.18881  1.000 59.63629  ? 164 ASN   B CG   1 
ATOM   4045 O  OD1  . ASN   B 1 164 ? -4.09014  -18.62863 41.00007  1.000 66.49226  ? 164 ASN   B OD1  1 
ATOM   4046 N  ND2  . ASN   B 1 164 ? -3.58990  -20.04855 39.32367  1.000 61.31403  ? 164 ASN   B ND2  1 
ATOM   4047 N  N    . ARG   B 1 165 ? 0.54496   -16.47321 39.95953  1.000 42.37845  ? 165 ARG   B N    1 
ATOM   4048 C  CA   . ARG   B 1 165 ? 1.93595   -16.12549 40.27595  1.000 43.24333  ? 165 ARG   B CA   1 
ATOM   4049 C  C    . ARG   B 1 165 ? 1.96726   -14.89789 41.16832  1.000 47.45968  ? 165 ARG   B C    1 
ATOM   4050 O  O    . ARG   B 1 165 ? 2.76572   -14.79694 42.12249  1.000 43.58304  ? 165 ARG   B O    1 
ATOM   4051 C  CB   . ARG   B 1 165 ? 2.74227   -15.85608 38.99403  1.000 39.80587  ? 165 ARG   B CB   1 
ATOM   4052 C  CG   . ARG   B 1 165 ? 4.19579   -15.33543 39.29023  1.000 43.09423  ? 165 ARG   B CG   1 
ATOM   4053 C  CD   . ARG   B 1 165 ? 5.07129   -16.37594 40.01802  1.000 48.94199  ? 165 ARG   B CD   1 
ATOM   4054 N  NE   . ARG   B 1 165 ? 6.35144   -15.77619 40.40801  1.000 45.93984  ? 165 ARG   B NE   1 
ATOM   4055 C  CZ   . ARG   B 1 165 ? 6.53830   -15.17622 41.57667  1.000 58.24362  ? 165 ARG   B CZ   1 
ATOM   4056 N  NH1  . ARG   B 1 165 ? 5.56106   -15.10385 42.47885  1.000 55.08254  ? 165 ARG   B NH1  1 
ATOM   4057 N  NH2  . ARG   B 1 165 ? 7.74060   -14.65626 41.87072  1.000 55.67318  ? 165 ARG   B NH2  1 
ATOM   4058 N  N    . MET   B 1 166 ? 1.06699   -13.96835 40.89484  1.000 39.66224  ? 166 MET   B N    1 
ATOM   4059 C  CA   . MET   B 1 166 ? 1.06350   -12.72740 41.63936  1.000 39.28191  ? 166 MET   B CA   1 
ATOM   4060 C  C    . MET   B 1 166 ? 0.47522   -12.91062 43.03653  1.000 38.30508  ? 166 MET   B C    1 
ATOM   4061 O  O    . MET   B 1 166 ? 0.90625   -12.24420 43.98786  1.000 42.14582  ? 166 MET   B O    1 
ATOM   4062 C  CB   . MET   B 1 166 ? 0.28140   -11.69366 40.81567  1.000 41.04413  ? 166 MET   B CB   1 
ATOM   4063 C  CG   . MET   B 1 166 ? 0.61109   -10.28262 41.27563  1.000 41.39625  ? 166 MET   B CG   1 
ATOM   4064 S  SD   . MET   B 1 166 ? 2.32089   -9.78930  40.87602  1.000 43.77564  ? 166 MET   B SD   1 
ATOM   4065 C  CE   . MET   B 1 166 ? 2.59312   -10.34071 39.19237  1.000 34.78746  ? 166 MET   B CE   1 
ATOM   4066 N  N    . LYS   B 1 167 ? -0.52827  -13.79465 43.17697  1.000 37.19541  ? 167 LYS   B N    1 
ATOM   4067 C  CA   . LYS   B 1 167 ? -1.09550  -14.08475 44.48340  1.000 39.74254  ? 167 LYS   B CA   1 
ATOM   4068 C  C    . LYS   B 1 167 ? -0.03433  -14.67791 45.39990  1.000 41.48728  ? 167 LYS   B C    1 
ATOM   4069 O  O    . LYS   B 1 167 ? -0.11019  -14.53625 46.62197  1.000 44.19155  ? 167 LYS   B O    1 
ATOM   4070 C  CB   . LYS   B 1 167 ? -2.25983  -15.05432 44.35513  1.000 39.63716  ? 167 LYS   B CB   1 
ATOM   4071 C  CG   . LYS   B 1 167 ? -3.43990  -14.44341 43.58131  1.000 39.30189  ? 167 LYS   B CG   1 
ATOM   4072 C  CD   . LYS   B 1 167 ? -4.65491  -15.35863 43.55761  1.000 49.75710  ? 167 LYS   B CD   1 
ATOM   4073 C  CE   . LYS   B 1 167 ? -5.35821  -15.23418 44.90016  1.000 65.01786  ? 167 LYS   B CE   1 
ATOM   4074 N  NZ   . LYS   B 1 167 ? -6.27101  -16.35283 45.21255  1.000 69.41911  ? 167 LYS   B NZ   1 
ATOM   4075 N  N    . ARG   B 1 168 ? 0.93369   -15.38363 44.81980  1.000 40.36916  ? 168 ARG   B N    1 
ATOM   4076 C  CA   . ARG   B 1 168 ? 2.01372   -15.90382 45.63698  1.000 40.45907  ? 168 ARG   B CA   1 
ATOM   4077 C  C    . ARG   B 1 168 ? 2.88245   -14.80505 46.24943  1.000 47.14459  ? 168 ARG   B C    1 
ATOM   4078 O  O    . ARG   B 1 168 ? 3.75696   -15.11951 47.05443  1.000 43.55692  ? 168 ARG   B O    1 
ATOM   4079 C  CB   . ARG   B 1 168 ? 2.88942   -16.84832 44.81330  1.000 40.01985  ? 168 ARG   B CB   1 
ATOM   4080 C  CG   . ARG   B 1 168 ? 2.17520   -18.10211 44.33900  1.000 47.19460  ? 168 ARG   B CG   1 
ATOM   4081 C  CD   . ARG   B 1 168 ? 3.14408   -19.21049 43.96754  1.000 57.91352  ? 168 ARG   B CD   1 
ATOM   4082 N  NE   . ARG   B 1 168 ? 3.48052   -19.20785 42.54603  1.000 59.24794  ? 168 ARG   B NE   1 
ATOM   4083 C  CZ   . ARG   B 1 168 ? 2.70215   -19.63859 41.55292  1.000 63.03155  ? 168 ARG   B CZ   1 
ATOM   4084 N  NH1  . ARG   B 1 168 ? 1.45927   -20.05708 41.76622  1.000 61.07826  ? 168 ARG   B NH1  1 
ATOM   4085 N  NH2  . ARG   B 1 168 ? 3.17359   -19.61021 40.30426  1.000 58.86088  ? 168 ARG   B NH2  1 
ATOM   4086 N  N    . CYS   B 1 169 ? 2.68034   -13.53508 45.90823  1.000 40.58866  ? 169 CYS   B N    1 
ATOM   4087 C  CA   . CYS   B 1 169 ? 3.42567   -12.45332 46.53361  1.000 37.07105  ? 169 CYS   B CA   1 
ATOM   4088 C  C    . CYS   B 1 169 ? 2.69901   -11.86873 47.72954  1.000 38.51802  ? 169 CYS   B C    1 
ATOM   4089 O  O    . CYS   B 1 169 ? 3.12094   -10.84328 48.25718  1.000 36.37417  ? 169 CYS   B O    1 
ATOM   4090 C  CB   . CYS   B 1 169 ? 3.69888   -11.33530 45.52807  1.000 38.46961  ? 169 CYS   B CB   1 
ATOM   4091 S  SG   . CYS   B 1 169 ? 4.79893   -11.75254 44.16420  1.000 40.35160  ? 169 CYS   B SG   1 
ATOM   4092 N  N    . LEU   B 1 170 ? 1.61605   -12.49228 48.16944  1.000 34.82132  ? 170 LEU   B N    1 
ATOM   4093 C  CA   . LEU   B 1 170 ? 0.78169   -11.85976 49.17304  1.000 33.95409  ? 170 LEU   B CA   1 
ATOM   4094 C  C    . LEU   B 1 170 ? 1.57162   -11.56696 50.45285  1.000 38.82021  ? 170 LEU   B C    1 
ATOM   4095 O  O    . LEU   B 1 170 ? 1.29411   -10.57914 51.14781  1.000 34.41855  ? 170 LEU   B O    1 
ATOM   4096 C  CB   . LEU   B 1 170 ? -0.42541  -12.74669 49.46040  1.000 39.68645  ? 170 LEU   B CB   1 
ATOM   4097 C  CG   . LEU   B 1 170 ? -1.47132  -12.15327 50.41722  1.000 52.09518  ? 170 LEU   B CG   1 
ATOM   4098 C  CD1  . LEU   B 1 170 ? -2.02451  -10.83797 49.84962  1.000 49.27224  ? 170 LEU   B CD1  1 
ATOM   4099 C  CD2  . LEU   B 1 170 ? -2.61388  -13.15057 50.65651  1.000 55.98425  ? 170 LEU   B CD2  1 
ATOM   4100 N  N    . LYS   B 1 171 ? 2.61393   -12.36052 50.75191  1.000 36.55722  ? 171 LYS   B N    1 
ATOM   4101 C  CA   . LYS   B 1 171 ? 3.31049   -12.10106 52.01252  1.000 36.25944  ? 171 LYS   B CA   1 
ATOM   4102 C  C    . LYS   B 1 171 ? 3.87856   -10.68151 52.06633  1.000 35.53420  ? 171 LYS   B C    1 
ATOM   4103 O  O    . LYS   B 1 171 ? 4.06758   -10.12619 53.16135  1.000 33.34879  ? 171 LYS   B O    1 
ATOM   4104 C  CB   . LYS   B 1 171 ? 4.43179   -13.11889 52.25053  1.000 36.56884  ? 171 LYS   B CB   1 
ATOM   4105 C  CG   . LYS   B 1 171 ? 4.94047   -12.93643 53.67267  1.000 47.65876  ? 171 LYS   B CG   1 
ATOM   4106 C  CD   . LYS   B 1 171 ? 5.73905   -14.06384 54.26334  1.000 56.25305  ? 171 LYS   B CD   1 
ATOM   4107 C  CE   . LYS   B 1 171 ? 5.67807   -13.87706 55.78355  1.000 61.20569  ? 171 LYS   B CE   1 
ATOM   4108 N  NZ   . LYS   B 1 171 ? 6.58893   -14.65664 56.64983  1.000 74.98201  ? 171 LYS   B NZ   1 
ATOM   4109 N  N    . ILE   B 1 172 ? 4.16643   -10.06902 50.90889  1.000 33.86117  ? 172 ILE   B N    1 
ATOM   4110 C  CA   . ILE   B 1 172 ? 4.75646   -8.73685  50.95990  1.000 30.31529  ? 172 ILE   B CA   1 
ATOM   4111 C  C    . ILE   B 1 172 ? 3.81507   -7.67863  51.52169  1.000 32.11496  ? 172 ILE   B C    1 
ATOM   4112 O  O    . ILE   B 1 172 ? 4.29477   -6.60973  51.89468  1.000 33.06543  ? 172 ILE   B O    1 
ATOM   4113 C  CB   . ILE   B 1 172 ? 5.28837   -8.26906  49.58516  1.000 30.11914  ? 172 ILE   B CB   1 
ATOM   4114 C  CG1  . ILE   B 1 172 ? 4.12410   -7.78315  48.66733  1.000 25.18062  ? 172 ILE   B CG1  1 
ATOM   4115 C  CG2  . ILE   B 1 172 ? 6.09070   -9.37581  48.89063  1.000 32.51482  ? 172 ILE   B CG2  1 
ATOM   4116 C  CD1  . ILE   B 1 172 ? 4.60832   -7.31064  47.25007  1.000 26.02704  ? 172 ILE   B CD1  1 
ATOM   4117 N  N    . MET   B 1 173 ? 2.47769   -7.91256  51.52859  1.000 28.96452  ? 173 MET   B N    1 
ATOM   4118 C  CA   . MET   B 1 173 ? 1.49208   -7.04004  52.14685  1.000 29.14389  ? 173 MET   B CA   1 
ATOM   4119 C  C    . MET   B 1 173 ? 1.16819   -7.45703  53.57230  1.000 33.88431  ? 173 MET   B C    1 
ATOM   4120 O  O    . MET   B 1 173 ? 0.24166   -6.88729  54.17326  1.000 35.74540  ? 173 MET   B O    1 
ATOM   4121 C  CB   . MET   B 1 173 ? 0.18093   -7.04336  51.28741  1.000 28.98724  ? 173 MET   B CB   1 
ATOM   4122 C  CG   . MET   B 1 173 ? 0.53271   -6.78005  49.86592  1.000 28.45695  ? 173 MET   B CG   1 
ATOM   4123 S  SD   . MET   B 1 173 ? -0.98225  -6.92773  48.81933  1.000 35.05267  ? 173 MET   B SD   1 
ATOM   4124 C  CE   . MET   B 1 173 ? -2.12656  -5.60606  49.40917  1.000 38.04316  ? 173 MET   B CE   1 
ATOM   4125 N  N    . GLY   B 1 174 ? 1.87677   -8.45464  54.11636  1.000 34.97824  ? 174 GLY   B N    1 
ATOM   4126 C  CA   . GLY   B 1 174 ? 1.61122   -8.93417  55.47408  1.000 38.62091  ? 174 GLY   B CA   1 
ATOM   4127 C  C    . GLY   B 1 174 ? 0.25921   -9.60182  55.62086  1.000 47.15566  ? 174 GLY   B C    1 
ATOM   4128 O  O    . GLY   B 1 174 ? -0.40034  -9.43453  56.65417  1.000 49.13781  ? 174 GLY   B O    1 
ATOM   4129 N  N    . ARG   B 1 175 ? -0.16556  -10.36149 54.60465  1.000 42.89741  ? 175 ARG   B N    1 
ATOM   4130 C  CA   . ARG   B 1 175 ? -1.50625  -10.93490 54.53678  1.000 54.59561  ? 175 ARG   B CA   1 
ATOM   4131 C  C    . ARG   B 1 175 ? -1.44977  -12.43365 54.26883  1.000 63.52590  ? 175 ARG   B C    1 
ATOM   4132 O  O    . ARG   B 1 175 ? -0.49357  -12.93552 53.65957  1.000 57.32436  ? 175 ARG   B O    1 
ATOM   4133 C  CB   . ARG   B 1 175 ? -2.33079  -10.22445 53.44775  1.000 55.35046  ? 175 ARG   B CB   1 
ATOM   4134 C  CG   . ARG   B 1 175 ? -2.54452  -8.79583  53.85397  1.000 51.85417  ? 175 ARG   B CG   1 
ATOM   4135 C  CD   . ARG   B 1 175 ? -3.33671  -7.96577  52.89553  1.000 58.87145  ? 175 ARG   B CD   1 
ATOM   4136 N  NE   . ARG   B 1 175 ? -3.47427  -6.67520  53.55371  1.000 63.67543  ? 175 ARG   B NE   1 
ATOM   4137 C  CZ   . ARG   B 1 175 ? -4.49849  -6.29960  54.30498  1.000 69.13999  ? 175 ARG   B CZ   1 
ATOM   4138 N  NH1  . ARG   B 1 175 ? -5.61405  -7.02088  54.37494  1.000 69.94068  ? 175 ARG   B NH1  1 
ATOM   4139 N  NH2  . ARG   B 1 175 ? -4.39252  -5.18198  55.02303  1.000 69.43505  ? 175 ARG   B NH2  1 
ATOM   4140 N  N    . SER   B 1 176 ? -2.46321  -13.14537 54.79095  1.000 70.11596  ? 176 SER   B N    1 
ATOM   4141 C  CA   . SER   B 1 176 ? -2.67035  -14.57682 54.58591  1.000 75.71912  ? 176 SER   B CA   1 
ATOM   4142 C  C    . SER   B 1 176 ? -3.71610  -14.81489 53.50737  1.000 83.47786  ? 176 SER   B C    1 
ATOM   4143 O  O    . SER   B 1 176 ? -4.60040  -13.98513 53.28805  1.000 80.83102  ? 176 SER   B O    1 
ATOM   4144 C  CB   . SER   B 1 176 ? -3.11261  -15.26595 55.87678  1.000 84.64785  ? 176 SER   B CB   1 
ATOM   4145 O  OG   . SER   B 1 176 ? -2.16045  -15.08847 56.91377  1.000 82.90234  ? 176 SER   B OG   1 
ATOM   4146 N  N    . GLU   B 1 177 ? -3.62925  -15.96691 52.83970  1.000 103.96802 ? 177 GLU   B N    1 
ATOM   4147 C  CA   . GLU   B 1 177 ? -4.49984  -16.17210 51.68619  1.000 105.16852 ? 177 GLU   B CA   1 
ATOM   4148 C  C    . GLU   B 1 177 ? -5.94205  -16.47157 52.08367  1.000 105.21269 ? 177 GLU   B C    1 
ATOM   4149 O  O    . GLU   B 1 177 ? -6.83819  -16.34123 51.24195  1.000 107.92458 ? 177 GLU   B O    1 
ATOM   4150 C  CB   . GLU   B 1 177 ? -3.96335  -17.29659 50.79361  1.000 107.82611 ? 177 GLU   B CB   1 
ATOM   4151 C  CG   . GLU   B 1 177 ? -3.89798  -16.94617 49.28928  1.000 108.92540 ? 177 GLU   B CG   1 
ATOM   4152 C  CD   . GLU   B 1 177 ? -5.25872  -16.81364 48.60861  1.000 119.78626 ? 177 GLU   B CD   1 
ATOM   4153 O  OE1  . GLU   B 1 177 ? -6.23835  -17.45626 49.04728  1.000 115.77594 ? 177 GLU   B OE1  1 
ATOM   4154 O  OE2  . GLU   B 1 177 ? -5.34092  -16.06430 47.61245  1.000 117.94567 ? 177 GLU   B OE2  1 
ATOM   4155 N  N    . GLY   B 1 178 ? -6.18709  -16.87877 53.33167  1.000 85.32346  ? 178 GLY   B N    1 
ATOM   4156 C  CA   . GLY   B 1 178 ? -7.53517  -17.24119 53.75251  1.000 83.43195  ? 178 GLY   B CA   1 
ATOM   4157 C  C    . GLY   B 1 178 ? -8.52333  -16.08928 53.81107  1.000 77.94044  ? 178 GLY   B C    1 
ATOM   4158 O  O    . GLY   B 1 178 ? -9.72233  -16.33390 53.95739  1.000 80.00109  ? 178 GLY   B O    1 
ATOM   4159 N  N    . GLU   B 1 179 ? -8.05438  -14.85429 53.72033  1.000 75.68897  ? 179 GLU   B N    1 
ATOM   4160 C  CA   . GLU   B 1 179 ? -8.91025  -13.68372 53.78131  1.000 69.81525  ? 179 GLU   B CA   1 
ATOM   4161 C  C    . GLU   B 1 179 ? -9.35362  -13.30231 52.37065  1.000 65.55131  ? 179 GLU   B C    1 
ATOM   4162 O  O    . GLU   B 1 179 ? -8.85681  -13.83446 51.37625  1.000 60.07026  ? 179 GLU   B O    1 
ATOM   4163 C  CB   . GLU   B 1 179 ? -8.15862  -12.52744 54.42639  1.000 66.56777  ? 179 GLU   B CB   1 
ATOM   4164 C  CG   . GLU   B 1 179 ? -6.83269  -12.23319 53.71627  1.000 77.14380  ? 179 GLU   B CG   1 
ATOM   4165 C  CD   . GLU   B 1 179 ? -5.95423  -11.20418 54.44137  1.000 80.99318  ? 179 GLU   B CD   1 
ATOM   4166 O  OE1  . GLU   B 1 179 ? -5.12503  -11.63218 55.29683  1.000 85.04017  ? 179 GLU   B OE1  1 
ATOM   4167 O  OE2  . GLU   B 1 179 ? -6.07671  -9.98267  54.13693  1.000 80.39791  ? 179 GLU   B OE2  1 
ATOM   4168 N  N    . GLU   B 1 180 ? -10.26544 -12.33577 52.28258  1.000 59.41264  ? 180 GLU   B N    1 
ATOM   4169 C  CA   . GLU   B 1 180 ? -10.74920 -11.94113 50.96804  1.000 56.20317  ? 180 GLU   B CA   1 
ATOM   4170 C  C    . GLU   B 1 180 ? -9.64475  -11.33729 50.11762  1.000 51.93115  ? 180 GLU   B C    1 
ATOM   4171 O  O    . GLU   B 1 180 ? -8.86564  -10.49195 50.57728  1.000 46.50853  ? 180 GLU   B O    1 
ATOM   4172 C  CB   . GLU   B 1 180 ? -11.92836 -10.97582 51.06492  1.000 63.35862  ? 180 GLU   B CB   1 
ATOM   4173 C  CG   . GLU   B 1 180 ? -12.57389 -10.81492 49.68785  1.000 50.71252  ? 180 GLU   B CG   1 
ATOM   4174 C  CD   . GLU   B 1 180 ? -13.81461 -9.90904  49.67572  1.000 67.25196  ? 180 GLU   B CD   1 
ATOM   4175 O  OE1  . GLU   B 1 180 ? -14.25698 -9.43568  50.74985  1.000 61.65737  ? 180 GLU   B OE1  1 
ATOM   4176 O  OE2  . GLU   B 1 180 ? -14.35184 -9.68536  48.57095  1.000 64.05540  ? 180 GLU   B OE2  1 
ATOM   4177 N  N    . ASN   B 1 181 ? -9.61776  -11.74390 48.84033  1.000 52.47936  ? 181 ASN   B N    1 
ATOM   4178 C  CA   . ASN   B 1 181 ? -8.52584  -11.36257 47.93442  1.000 48.30585  ? 181 ASN   B CA   1 
ATOM   4179 C  C    . ASN   B 1 181 ? -8.98004  -10.19295 47.06827  1.000 44.94369  ? 181 ASN   B C    1 
ATOM   4180 O  O    . ASN   B 1 181 ? -9.52827  -10.37664 45.97549  1.000 45.34819  ? 181 ASN   B O    1 
ATOM   4181 C  CB   . ASN   B 1 181 ? -8.08374  -12.56190 47.10667  1.000 48.10031  ? 181 ASN   B CB   1 
ATOM   4182 C  CG   . ASN   B 1 181 ? -7.57468  -13.69634 47.97863  1.000 66.13056  ? 181 ASN   B CG   1 
ATOM   4183 O  OD1  . ASN   B 1 181 ? -6.57846  -13.53035 48.68418  1.000 63.38245  ? 181 ASN   B OD1  1 
ATOM   4184 N  ND2  . ASN   B 1 181 ? -8.27112  -14.83195 47.96749  1.000 71.98219  ? 181 ASN   B ND2  1 
ATOM   4185 N  N    . TYR   B 1 182 ? -8.73277  -8.98197  47.56026  1.000 41.63815  ? 182 TYR   B N    1 
ATOM   4186 C  CA   . TYR   B 1 182 ? -9.03375  -7.78176  46.79282  1.000 41.26754  ? 182 TYR   B CA   1 
ATOM   4187 C  C    . TYR   B 1 182 ? -8.05308  -7.61075  45.63380  1.000 39.20959  ? 182 TYR   B C    1 
ATOM   4188 O  O    . TYR   B 1 182 ? -6.91781  -8.12106  45.65156  1.000 35.29132  ? 182 TYR   B O    1 
ATOM   4189 C  CB   . TYR   B 1 182 ? -9.00678  -6.54706  47.69155  1.000 41.22553  ? 182 TYR   B CB   1 
ATOM   4190 C  CG   . TYR   B 1 182 ? -10.18238 -6.56231  48.66412  1.000 44.95847  ? 182 TYR   B CG   1 
ATOM   4191 C  CD1  . TYR   B 1 182 ? -11.46469 -6.22807  48.23795  1.000 49.31486  ? 182 TYR   B CD1  1 
ATOM   4192 C  CD2  . TYR   B 1 182 ? -9.99718  -6.90618  50.01793  1.000 60.15840  ? 182 TYR   B CD2  1 
ATOM   4193 C  CE1  . TYR   B 1 182 ? -12.53725 -6.24739  49.12602  1.000 53.38789  ? 182 TYR   B CE1  1 
ATOM   4194 C  CE2  . TYR   B 1 182 ? -11.07419 -6.93372  50.90541  1.000 57.23887  ? 182 TYR   B CE2  1 
ATOM   4195 C  CZ   . TYR   B 1 182 ? -12.32261 -6.59512  50.45243  1.000 53.54307  ? 182 TYR   B CZ   1 
ATOM   4196 O  OH   . TYR   B 1 182 ? -13.37911 -6.62140  51.33042  1.000 68.62146  ? 182 TYR   B OH   1 
ATOM   4197 N  N    . CYS   B 1 183 ? -8.50580  -6.88999  44.60555  1.000 34.79862  ? 183 CYS   B N    1 
ATOM   4198 C  CA   . CYS   B 1 183 ? -7.64040  -6.64936  43.44607  1.000 33.71358  ? 183 CYS   B CA   1 
ATOM   4199 C  C    . CYS   B 1 183 ? -6.39093  -5.84725  43.79235  1.000 34.68627  ? 183 CYS   B C    1 
ATOM   4200 O  O    . CYS   B 1 183 ? -5.39475  -5.89177  43.04076  1.000 34.59700  ? 183 CYS   B O    1 
ATOM   4201 C  CB   . CYS   B 1 183 ? -8.40391  -5.91961  42.34454  1.000 30.69496  ? 183 CYS   B CB   1 
ATOM   4202 S  SG   . CYS   B 1 183 ? -9.64539  -7.07211  41.59131  1.000 40.53657  ? 183 CYS   B SG   1 
ATOM   4203 N  N    . SER   B 1 184 ? -6.43664  -5.07123  44.86637  1.000 34.12887  ? 184 SER   B N    1 
ATOM   4204 C  CA   . SER   B 1 184 ? -5.23915  -4.38866  45.34507  1.000 33.22341  ? 184 SER   B CA   1 
ATOM   4205 C  C    . SER   B 1 184 ? -4.10338  -5.37375  45.57456  1.000 36.80804  ? 184 SER   B C    1 
ATOM   4206 O  O    . SER   B 1 184 ? -2.93359  -4.99403  45.47697  1.000 33.21661  ? 184 SER   B O    1 
ATOM   4207 C  CB   . SER   B 1 184 ? -5.57988  -3.61532  46.62460  1.000 36.99782  ? 184 SER   B CB   1 
ATOM   4208 O  OG   . SER   B 1 184 ? -6.24240  -4.48748  47.54721  1.000 35.90603  ? 184 SER   B OG   1 
ATOM   4209 N  N    . GLN   B 1 185 ? -4.41693  -6.63703  45.88133  1.000 34.30590  ? 185 GLN   B N    1 
ATOM   4210 C  CA   . GLN   B 1 185 ? -3.37413  -7.62986  46.09345  1.000 40.41481  ? 185 GLN   B CA   1 
ATOM   4211 C  C    . GLN   B 1 185 ? -2.68553  -8.04611  44.80300  1.000 39.81551  ? 185 GLN   B C    1 
ATOM   4212 O  O    . GLN   B 1 185 ? -1.68845  -8.77415  44.84567  1.000 41.98493  ? 185 GLN   B O    1 
ATOM   4213 C  CB   . GLN   B 1 185 ? -3.95823  -8.85083  46.82956  1.000 38.03631  ? 185 GLN   B CB   1 
ATOM   4214 C  CG   . GLN   B 1 185 ? -4.49423  -8.42361  48.21816  1.000 36.46631  ? 185 GLN   B CG   1 
ATOM   4215 C  CD   . GLN   B 1 185 ? -5.24903  -9.51746  48.91323  1.000 39.54469  ? 185 GLN   B CD   1 
ATOM   4216 O  OE1  . GLN   B 1 185 ? -5.21364  -10.69709 48.52099  1.000 45.68992  ? 185 GLN   B OE1  1 
ATOM   4217 N  NE2  . GLN   B 1 185 ? -5.99185  -9.12821  49.91618  1.000 48.47298  ? 185 GLN   B NE2  1 
ATOM   4218 N  N    . ILE   B 1 186 ? -3.20863  -7.61862  43.66289  1.000 35.21363  ? 186 ILE   B N    1 
ATOM   4219 C  CA   . ILE   B 1 186 ? -2.52919  -7.75427  42.40698  1.000 32.10868  ? 186 ILE   B CA   1 
ATOM   4220 C  C    . ILE   B 1 186 ? -1.77804  -6.48625  42.10123  1.000 32.78652  ? 186 ILE   B C    1 
ATOM   4221 O  O    . ILE   B 1 186 ? -0.64070  -6.52586  41.61137  1.000 31.72283  ? 186 ILE   B O    1 
ATOM   4222 C  CB   . ILE   B 1 186 ? -3.56174  -8.08254  41.27949  1.000 35.17442  ? 186 ILE   B CB   1 
ATOM   4223 C  CG1  . ILE   B 1 186 ? -4.28417  -9.39828  41.56184  1.000 38.02132  ? 186 ILE   B CG1  1 
ATOM   4224 C  CG2  . ILE   B 1 186 ? -2.85832  -8.12047  39.92048  1.000 31.79119  ? 186 ILE   B CG2  1 
ATOM   4225 C  CD1  . ILE   B 1 186 ? -3.29224  -10.56472 41.79982  1.000 40.00138  ? 186 ILE   B CD1  1 
ATOM   4226 N  N    . LEU   B 1 187 ? -2.40250  -5.33294  42.34658  1.000 29.88111  ? 187 LEU   B N    1 
ATOM   4227 C  CA   . LEU   B 1 187 ? -1.71381  -4.11534  41.93546  1.000 30.80893  ? 187 LEU   B CA   1 
ATOM   4228 C  C    . LEU   B 1 187 ? -0.44570  -3.91716  42.77532  1.000 29.99662  ? 187 LEU   B C    1 
ATOM   4229 O  O    . LEU   B 1 187 ? 0.61293   -3.53071  42.24891  1.000 29.85091  ? 187 LEU   B O    1 
ATOM   4230 C  CB   . LEU   B 1 187 ? -2.62320  -2.89858  42.10237  1.000 30.88019  ? 187 LEU   B CB   1 
ATOM   4231 C  CG   . LEU   B 1 187 ? -3.48263  -2.58137  40.87866  1.000 44.32824  ? 187 LEU   B CG   1 
ATOM   4232 C  CD1  . LEU   B 1 187 ? -4.47444  -3.69154  40.74197  1.000 35.44445  ? 187 LEU   B CD1  1 
ATOM   4233 C  CD2  . LEU   B 1 187 ? -4.17202  -1.25990  41.11183  1.000 44.48883  ? 187 LEU   B CD2  1 
ATOM   4234 N  N    . TYR   B 1 188 ? -0.57104  -4.10752  44.10005  1.000 31.66064  ? 188 TYR   B N    1 
ATOM   4235 C  CA   . TYR   B 1 188 ? 0.52853   -3.81984  45.03873  1.000 30.02026  ? 188 TYR   B CA   1 
ATOM   4236 C  C    . TYR   B 1 188 ? 1.78332   -4.53951  44.61680  1.000 26.25475  ? 188 TYR   B C    1 
ATOM   4237 O  O    . TYR   B 1 188 ? 2.80849   -3.88803  44.46069  1.000 29.98747  ? 188 TYR   B O    1 
ATOM   4238 C  CB   . TYR   B 1 188 ? 0.09166   -4.20076  46.45233  1.000 31.30141  ? 188 TYR   B CB   1 
ATOM   4239 C  CG   . TYR   B 1 188 ? 0.99746   -3.79236  47.59877  1.000 27.63052  ? 188 TYR   B CG   1 
ATOM   4240 C  CD1  . TYR   B 1 188 ? 2.28473   -4.30567  47.68030  1.000 30.92839  ? 188 TYR   B CD1  1 
ATOM   4241 C  CD2  . TYR   B 1 188 ? 0.51376   -3.00232  48.65540  1.000 29.87619  ? 188 TYR   B CD2  1 
ATOM   4242 C  CE1  . TYR   B 1 188 ? 3.09940   -4.00564  48.78157  1.000 33.12881  ? 188 TYR   B CE1  1 
ATOM   4243 C  CE2  . TYR   B 1 188 ? 1.38679   -2.70249  49.80639  1.000 28.58861  ? 188 TYR   B CE2  1 
ATOM   4244 C  CZ   . TYR   B 1 188 ? 2.64023   -3.21181  49.79174  1.000 33.57837  ? 188 TYR   B CZ   1 
ATOM   4245 O  OH   . TYR   B 1 188 ? 3.44527   -2.94692  50.86974  1.000 30.32100  ? 188 TYR   B OH   1 
ATOM   4246 N  N    . PRO   B 1 189 ? 1.80992   -5.86090  44.44071  1.000 28.17702  ? 189 PRO   B N    1 
ATOM   4247 C  CA   . PRO   B 1 189 ? 3.08894   -6.44308  43.98294  1.000 28.68971  ? 189 PRO   B CA   1 
ATOM   4248 C  C    . PRO   B 1 189 ? 3.50664   -5.95830  42.58490  1.000 32.77791  ? 189 PRO   B C    1 
ATOM   4249 O  O    . PRO   B 1 189 ? 4.71034   -5.75128  42.35366  1.000 30.00451  ? 189 PRO   B O    1 
ATOM   4250 C  CB   . PRO   B 1 189 ? 2.86542   -7.96703  44.03741  1.000 27.19782  ? 189 PRO   B CB   1 
ATOM   4251 C  CG   . PRO   B 1 189 ? 1.23457   -8.13322  44.03023  1.000 27.81502  ? 189 PRO   B CG   1 
ATOM   4252 C  CD   . PRO   B 1 189 ? 0.76210   -6.86193  44.71658  1.000 32.20660  ? 189 PRO   B CD   1 
ATOM   4253 N  N    . CYS   B 1 190 ? 2.56677   -5.72129  41.63132  1.000 30.05272  ? 190 CYS   B N    1 
ATOM   4254 C  CA   . CYS   B 1 190 ? 3.03144   -5.18554  40.35657  1.000 29.95526  ? 190 CYS   B CA   1 
ATOM   4255 C  C    . CYS   B 1 190 ? 3.81157   -3.89965  40.58259  1.000 26.69807  ? 190 CYS   B C    1 
ATOM   4256 O  O    . CYS   B 1 190 ? 4.86481   -3.68234  39.97936  1.000 32.76718  ? 190 CYS   B O    1 
ATOM   4257 C  CB   . CYS   B 1 190 ? 1.83414   -4.93475  39.38320  1.000 27.37773  ? 190 CYS   B CB   1 
ATOM   4258 S  SG   . CYS   B 1 190 ? 1.17276   -6.53893  38.82242  1.000 34.95654  ? 190 CYS   B SG   1 
ATOM   4259 N  N    . MET   B 1 191 ? 3.29842   -3.04912  41.45771  1.000 28.50341  ? 191 MET   B N    1 
ATOM   4260 C  CA   . MET   B 1 191 ? 3.91927   -1.76007  41.73094  1.000 28.88723  ? 191 MET   B CA   1 
ATOM   4261 C  C    . MET   B 1 191 ? 5.20737   -1.95958  42.51923  1.000 30.58336  ? 191 MET   B C    1 
ATOM   4262 O  O    . MET   B 1 191 ? 6.20501   -1.32080  42.21997  1.000 28.13762  ? 191 MET   B O    1 
ATOM   4263 C  CB   . MET   B 1 191 ? 2.97445   -0.86595  42.54275  1.000 28.18148  ? 191 MET   B CB   1 
ATOM   4264 C  CG   . MET   B 1 191 ? 1.77111   -0.27529  41.69197  1.000 26.88045  ? 191 MET   B CG   1 
ATOM   4265 S  SD   . MET   B 1 191 ? 0.53319   0.40750   42.79815  1.000 32.22728  ? 191 MET   B SD   1 
ATOM   4266 C  CE   . MET   B 1 191 ? 1.35185   1.84543   43.56885  1.000 35.14384  ? 191 MET   B CE   1 
ATOM   4267 N  N    . GLN   B 1 192 ? 5.21603   -2.85232  43.49477  1.000 26.85544  ? 192 GLN   B N    1 
ATOM   4268 C  CA   . GLN   B 1 192 ? 6.50622   -3.00370  44.21658  1.000 28.69118  ? 192 GLN   B CA   1 
ATOM   4269 C  C    . GLN   B 1 192 ? 7.55706   -3.51205  43.26078  1.000 34.56239  ? 192 GLN   B C    1 
ATOM   4270 O  O    . GLN   B 1 192 ? 8.70466   -3.04311  43.27970  1.000 32.65625  ? 192 GLN   B O    1 
ATOM   4271 C  CB   . GLN   B 1 192 ? 6.36076   -3.92022  45.42489  1.000 29.21169  ? 192 GLN   B CB   1 
ATOM   4272 C  CG   . GLN   B 1 192 ? 7.77853   -4.14447  46.14614  1.000 24.00442  ? 192 GLN   B CG   1 
ATOM   4273 C  CD   . GLN   B 1 192 ? 7.56965   -4.56357  47.59996  1.000 28.98863  ? 192 GLN   B CD   1 
ATOM   4274 O  OE1  . GLN   B 1 192 ? 6.48719   -4.37134  48.17920  1.000 28.56715  ? 192 GLN   B OE1  1 
ATOM   4275 N  NE2  . GLN   B 1 192 ? 8.64100   -5.07719  48.22676  1.000 30.23121  ? 192 GLN   B NE2  1 
ATOM   4276 N  N    . CYS   B 1 193 ? 7.15923   -4.39941  42.33422  1.000 29.73169  ? 193 CYS   B N    1 
ATOM   4277 C  CA   . CYS   B 1 193 ? 8.13154   -4.87958  41.35441  1.000 33.12822  ? 193 CYS   B CA   1 
ATOM   4278 C  C    . CYS   B 1 193 ? 8.61366   -3.71941  40.47998  1.000 33.36096  ? 193 CYS   B C    1 
ATOM   4279 O  O    . CYS   B 1 193 ? 9.82011   -3.52397  40.27243  1.000 32.81406  ? 193 CYS   B O    1 
ATOM   4280 C  CB   . CYS   B 1 193 ? 7.45847   -5.98012  40.51325  1.000 33.49879  ? 193 CYS   B CB   1 
ATOM   4281 S  SG   . CYS   B 1 193 ? 8.57424   -6.83838  39.38304  1.000 34.45588  ? 193 CYS   B SG   1 
ATOM   4282 N  N    . ALA   B 1 194 ? 7.66875   -2.88551  40.00224  1.000 31.13285  ? 194 ALA   B N    1 
ATOM   4283 C  CA   . ALA   B 1 194 ? 8.06389   -1.75165  39.17397  1.000 29.72275  ? 194 ALA   B CA   1 
ATOM   4284 C  C    . ALA   B 1 194 ? 9.07276   -0.85840  39.91439  1.000 26.63037  ? 194 ALA   B C    1 
ATOM   4285 O  O    . ALA   B 1 194 ? 10.01217  -0.33159  39.27271  1.000 29.25685  ? 194 ALA   B O    1 
ATOM   4286 C  CB   . ALA   B 1 194 ? 6.84076   -0.92553  38.78316  1.000 31.01218  ? 194 ALA   B CB   1 
ATOM   4287 N  N    . ASP   B 1 195 ? 8.88859   -0.68753  41.24773  1.000 32.89657  ? 195 ASP   B N    1 
ATOM   4288 C  CA   . ASP   B 1 195 ? 9.78141   0.21804   42.00437  1.000 29.66959  ? 195 ASP   B CA   1 
ATOM   4289 C  C    . ASP   B 1 195 ? 11.23019  -0.18116  41.82038  1.000 28.81668  ? 195 ASP   B C    1 
ATOM   4290 O  O    . ASP   B 1 195 ? 12.09457  0.68092   41.65989  1.000 29.12260  ? 195 ASP   B O    1 
ATOM   4291 C  CB   . ASP   B 1 195 ? 9.50741   0.22341   43.48910  1.000 29.75398  ? 195 ASP   B CB   1 
ATOM   4292 C  CG   . ASP   B 1 195 ? 8.15071   0.78678   43.84687  1.000 31.60953  ? 195 ASP   B CG   1 
ATOM   4293 O  OD1  . ASP   B 1 195 ? 7.68663   0.44039   44.94399  1.000 31.14622  ? 195 ASP   B OD1  1 
ATOM   4294 O  OD2  . ASP   B 1 195 ? 7.54034   1.50687   43.00005  1.000 34.38882  ? 195 ASP   B OD2  1 
ATOM   4295 N  N    . ILE   B 1 196 ? 11.48862  -1.49118  41.77835  1.000 29.11042  ? 196 ILE   B N    1 
ATOM   4296 C  CA   . ILE   B 1 196 ? 12.87353  -1.97112  41.74358  1.000 31.83337  ? 196 ILE   B CA   1 
ATOM   4297 C  C    . ILE   B 1 196 ? 13.57279  -1.45080  40.50123  1.000 34.64585  ? 196 ILE   B C    1 
ATOM   4298 O  O    . ILE   B 1 196 ? 14.74605  -1.08861  40.53189  1.000 32.82797  ? 196 ILE   B O    1 
ATOM   4299 C  CB   . ILE   B 1 196 ? 12.89261  -3.50729  41.77440  1.000 31.58004  ? 196 ILE   B CB   1 
ATOM   4300 C  CG1  . ILE   B 1 196 ? 12.31355  -3.99649  43.09020  1.000 27.08942  ? 196 ILE   B CG1  1 
ATOM   4301 C  CG2  . ILE   B 1 196 ? 14.30913  -4.06553  41.47642  1.000 32.54524  ? 196 ILE   B CG2  1 
ATOM   4302 C  CD1  . ILE   B 1 196 ? 12.12422  -5.53264  43.13728  1.000 28.33510  ? 196 ILE   B CD1  1 
ATOM   4303 N  N    . PHE   B 1 197 ? 12.86547  -1.43623  39.36375  1.000 29.86213  ? 197 PHE   B N    1 
ATOM   4304 C  CA   . PHE   B 1 197 ? 13.40557  -0.90513  38.12727  1.000 28.95768  ? 197 PHE   B CA   1 
ATOM   4305 C  C    . PHE   B 1 197 ? 13.33753  0.60554   38.08675  1.000 31.15782  ? 197 PHE   B C    1 
ATOM   4306 O  O    . PHE   B 1 197 ? 14.29099  1.25572   37.63980  1.000 32.28717  ? 197 PHE   B O    1 
ATOM   4307 C  CB   . PHE   B 1 197 ? 12.58518  -1.49609  36.94418  1.000 32.48226  ? 197 PHE   B CB   1 
ATOM   4308 C  CG   . PHE   B 1 197 ? 12.72412  -2.97305  36.86942  1.000 32.05952  ? 197 PHE   B CG   1 
ATOM   4309 C  CD1  . PHE   B 1 197 ? 13.89985  -3.52224  36.38191  1.000 38.67272  ? 197 PHE   B CD1  1 
ATOM   4310 C  CD2  . PHE   B 1 197 ? 11.80202  -3.79481  37.45099  1.000 34.76833  ? 197 PHE   B CD2  1 
ATOM   4311 C  CE1  . PHE   B 1 197 ? 14.11174  -4.89319  36.40992  1.000 43.69045  ? 197 PHE   B CE1  1 
ATOM   4312 C  CE2  . PHE   B 1 197 ? 11.98571  -5.16970  37.46840  1.000 34.67657  ? 197 PHE   B CE2  1 
ATOM   4313 C  CZ   . PHE   B 1 197 ? 13.12359  -5.71902  36.94354  1.000 40.41968  ? 197 PHE   B CZ   1 
ATOM   4314 N  N    . PHE   B 1 198 ? 12.20876  1.17839   38.53962  1.000 27.11250  ? 198 PHE   B N    1 
ATOM   4315 C  CA   . PHE   B 1 198 ? 12.02300  2.62734   38.48225  1.000 28.88101  ? 198 PHE   B CA   1 
ATOM   4316 C  C    . PHE   B 1 198 ? 13.11624  3.37590   39.25775  1.000 34.41130  ? 198 PHE   B C    1 
ATOM   4317 O  O    . PHE   B 1 198 ? 13.59605  4.43914   38.83071  1.000 33.05472  ? 198 PHE   B O    1 
ATOM   4318 C  CB   . PHE   B 1 198 ? 10.64688  2.93002   39.08562  1.000 31.30431  ? 198 PHE   B CB   1 
ATOM   4319 C  CG   . PHE   B 1 198 ? 10.21530  4.38226   39.02343  1.000 34.04483  ? 198 PHE   B CG   1 
ATOM   4320 C  CD1  . PHE   B 1 198 ? 9.94493   4.96150   37.79606  1.000 33.51186  ? 198 PHE   B CD1  1 
ATOM   4321 C  CD2  . PHE   B 1 198 ? 9.99941   5.11998   40.17472  1.000 32.79878  ? 198 PHE   B CD2  1 
ATOM   4322 C  CE1  . PHE   B 1 198 ? 9.51889   6.25824   37.68815  1.000 32.44407  ? 198 PHE   B CE1  1 
ATOM   4323 C  CE2  . PHE   B 1 198 ? 9.51580   6.41796   40.08495  1.000 35.41292  ? 198 PHE   B CE2  1 
ATOM   4324 C  CZ   . PHE   B 1 198 ? 9.26285   6.97705   38.81035  1.000 31.16063  ? 198 PHE   B CZ   1 
ATOM   4325 N  N    . LEU   B 1 199 ? 13.50719  2.84339   40.40145  1.000 31.66103  ? 199 LEU   B N    1 
ATOM   4326 C  CA   . LEU   B 1 199 ? 14.59557  3.41443   41.20607  1.000 31.96264  ? 199 LEU   B CA   1 
ATOM   4327 C  C    . LEU   B 1 199 ? 15.99909  2.98616   40.74749  1.000 34.41272  ? 199 LEU   B C    1 
ATOM   4328 O  O    . LEU   B 1 199 ? 17.00045  3.36402   41.39857  1.000 34.69179  ? 199 LEU   B O    1 
ATOM   4329 C  CB   . LEU   B 1 199 ? 14.38425  2.98804   42.65607  1.000 27.75699  ? 199 LEU   B CB   1 
ATOM   4330 C  CG   . LEU   B 1 199 ? 13.13480  3.60670   43.27853  1.000 30.40508  ? 199 LEU   B CG   1 
ATOM   4331 C  CD1  . LEU   B 1 199 ? 12.82806  3.04559   44.62682  1.000 35.09341  ? 199 LEU   B CD1  1 
ATOM   4332 C  CD2  . LEU   B 1 199 ? 13.22940  5.16091   43.28758  1.000 35.03538  ? 199 LEU   B CD2  1 
ATOM   4333 N  N    . ASN   B 1 200 ? 16.10948  2.18228   39.69019  1.000 32.17843  ? 200 ASN   B N    1 
ATOM   4334 C  CA   . ASN   B 1 200 ? 17.42121  1.72036   39.17777  1.000 33.43829  ? 200 ASN   B CA   1 
ATOM   4335 C  C    . ASN   B 1 200 ? 18.26339  1.04386   40.27386  1.000 38.29502  ? 200 ASN   B C    1 
ATOM   4336 O  O    . ASN   B 1 200 ? 19.50907  1.22030   40.36292  1.000 36.53933  ? 200 ASN   B O    1 
ATOM   4337 C  CB   . ASN   B 1 200 ? 18.17958  2.86421   38.52175  1.000 34.71543  ? 200 ASN   B CB   1 
ATOM   4338 C  CG   . ASN   B 1 200 ? 19.34360  2.36041   37.69996  1.000 49.37520  ? 200 ASN   B CG   1 
ATOM   4339 O  OD1  . ASN   B 1 200 ? 19.30023  1.22055   37.21769  1.000 47.96552  ? 200 ASN   B OD1  1 
ATOM   4340 N  ND2  . ASN   B 1 200 ? 20.42128  3.14993   37.61149  1.000 56.24878  ? 200 ASN   B ND2  1 
ATOM   4341 N  N    . VAL   B 1 201 ? 17.59796  0.18965   41.06235  1.000 32.50933  ? 201 VAL   B N    1 
ATOM   4342 C  CA   . VAL   B 1 201 ? 18.23104  -0.46865  42.21576  1.000 32.72682  ? 201 VAL   B CA   1 
ATOM   4343 C  C    . VAL   B 1 201 ? 19.21779  -1.53912  41.76270  1.000 32.72251  ? 201 VAL   B C    1 
ATOM   4344 O  O    . VAL   B 1 201 ? 18.91852  -2.35694  40.88285  1.000 32.90684  ? 201 VAL   B O    1 
ATOM   4345 C  CB   . VAL   B 1 201 ? 17.10689  -1.06090  43.07207  1.000 33.10753  ? 201 VAL   B CB   1 
ATOM   4346 C  CG1  . VAL   B 1 201 ? 17.55758  -2.05496  44.06394  1.000 33.20996  ? 201 VAL   B CG1  1 
ATOM   4347 C  CG2  . VAL   B 1 201 ? 16.33874  0.16056   43.79755  1.000 32.20874  ? 201 VAL   B CG2  1 
ATOM   4348 N  N    . ASP   B 1 202 ? 20.38647  -1.58152  42.41713  1.000 34.33910  ? 202 ASP   B N    1 
ATOM   4349 C  CA   . ASP   B 1 202 ? 21.32584  -2.68561  42.24967  1.000 31.16290  ? 202 ASP   B CA   1 
ATOM   4350 C  C    . ASP   B 1 202 ? 21.07361  -3.79299  43.25387  1.000 29.29152  ? 202 ASP   B C    1 
ATOM   4351 O  O    . ASP   B 1 202 ? 21.23872  -4.97737  42.93158  1.000 33.33045  ? 202 ASP   B O    1 
ATOM   4352 C  CB   . ASP   B 1 202 ? 22.78287  -2.18692  42.41624  1.000 31.19357  ? 202 ASP   B CB   1 
ATOM   4353 C  CG   . ASP   B 1 202 ? 23.17964  -1.24962  41.31332  1.000 33.71684  ? 202 ASP   B CG   1 
ATOM   4354 O  OD1  . ASP   B 1 202 ? 23.10766  -1.68159  40.13877  1.000 37.64871  ? 202 ASP   B OD1  1 
ATOM   4355 O  OD2  . ASP   B 1 202 ? 23.45464  -0.05130  41.56406  1.000 35.81572  ? 202 ASP   B OD2  1 
ATOM   4356 N  N    . ILE   B 1 203 ? 20.71522  -3.41458  44.48169  1.000 28.80480  ? 203 ILE   B N    1 
ATOM   4357 C  CA   . ILE   B 1 203 ? 20.52998  -4.33848  45.58577  1.000 26.20982  ? 203 ILE   B CA   1 
ATOM   4358 C  C    . ILE   B 1 203 ? 19.20042  -4.06727  46.24351  1.000 31.70433  ? 203 ILE   B C    1 
ATOM   4359 O  O    . ILE   B 1 203 ? 18.99455  -2.98486  46.81532  1.000 34.11414  ? 203 ILE   B O    1 
ATOM   4360 C  CB   . ILE   B 1 203 ? 21.66609  -4.19027  46.61593  1.000 29.34635  ? 203 ILE   B CB   1 
ATOM   4361 C  CG1  . ILE   B 1 203 ? 22.99030  -4.46506  45.91200  1.000 31.16435  ? 203 ILE   B CG1  1 
ATOM   4362 C  CG2  . ILE   B 1 203 ? 21.38990  -5.11443  47.79933  1.000 28.50582  ? 203 ILE   B CG2  1 
ATOM   4363 C  CD1  . ILE   B 1 203 ? 24.25395  -4.15756  46.91802  1.000 35.12156  ? 203 ILE   B CD1  1 
ATOM   4364 N  N    . CYS   B 1 204 ? 18.29575  -5.04295  46.18024  1.000 30.63418  ? 204 CYS   B N    1 
ATOM   4365 C  CA   . CYS   B 1 204 ? 17.10227  -4.98428  47.01707  1.000 30.20821  ? 204 CYS   B CA   1 
ATOM   4366 C  C    . CYS   B 1 204 ? 17.48208  -5.47926  48.40151  1.000 29.93757  ? 204 CYS   B C    1 
ATOM   4367 O  O    . CYS   B 1 204 ? 17.78949  -6.65911  48.55226  1.000 32.39086  ? 204 CYS   B O    1 
ATOM   4368 C  CB   . CYS   B 1 204 ? 16.02472  -5.89193  46.44768  1.000 31.83174  ? 204 CYS   B CB   1 
ATOM   4369 S  SG   . CYS   B 1 204 ? 15.62439  -5.38052  44.76091  1.000 33.26187  ? 204 CYS   B SG   1 
ATOM   4370 N  N    . GLN   B 1 205 ? 17.45169  -4.60032  49.39933  1.000 27.19669  ? 205 GLN   B N    1 
ATOM   4371 C  CA   . GLN   B 1 205 ? 17.85833  -4.95061  50.77841  1.000 32.32213  ? 205 GLN   B CA   1 
ATOM   4372 C  C    . GLN   B 1 205 ? 16.63452  -4.76264  51.68293  1.000 31.14422  ? 205 GLN   B C    1 
ATOM   4373 O  O    . GLN   B 1 205 ? 16.49980  -3.74823  52.37537  1.000 31.38131  ? 205 GLN   B O    1 
ATOM   4374 C  CB   . GLN   B 1 205 ? 19.06149  -4.07685  51.18373  1.000 32.90147  ? 205 GLN   B CB   1 
ATOM   4375 C  CG   . GLN   B 1 205 ? 19.91903  -4.67024  52.35299  1.000 31.83844  ? 205 GLN   B CG   1 
ATOM   4376 C  CD   . GLN   B 1 205 ? 19.09150  -4.75314  53.60166  1.000 31.69768  ? 205 GLN   B CD   1 
ATOM   4377 O  OE1  . GLN   B 1 205 ? 18.95755  -3.76469  54.32857  1.000 34.04781  ? 205 GLN   B OE1  1 
ATOM   4378 N  NE2  . GLN   B 1 205 ? 18.44295  -5.91248  53.82372  1.000 29.99907  ? 205 GLN   B NE2  1 
ATOM   4379 N  N    . LEU   B 1 206 ? 15.71004  -5.73572  51.64532  1.000 27.20878  ? 206 LEU   B N    1 
ATOM   4380 C  CA   . LEU   B 1 206 ? 14.48874  -5.75163  52.42603  1.000 31.29514  ? 206 LEU   B CA   1 
ATOM   4381 C  C    . LEU   B 1 206 ? 14.49831  -7.00757  53.27894  1.000 29.32254  ? 206 LEU   B C    1 
ATOM   4382 O  O    . LEU   B 1 206 ? 15.34988  -7.89575  53.10716  1.000 30.82501  ? 206 LEU   B O    1 
ATOM   4383 C  CB   . LEU   B 1 206 ? 13.20983  -5.74014  51.50403  1.000 24.91982  ? 206 LEU   B CB   1 
ATOM   4384 C  CG   . LEU   B 1 206 ? 13.19144  -4.50034  50.58490  1.000 31.99833  ? 206 LEU   B CG   1 
ATOM   4385 C  CD1  . LEU   B 1 206 ? 13.84909  -4.82860  49.27529  1.000 31.32140  ? 206 LEU   B CD1  1 
ATOM   4386 C  CD2  . LEU   B 1 206 ? 11.70832  -3.95409  50.33665  1.000 29.79890  ? 206 LEU   B CD2  1 
ATOM   4387 N  N    . GLY   B 1 207 ? 13.52115  -7.09151  54.17330  1.000 29.61415  ? 207 GLY   B N    1 
ATOM   4388 C  CA   . GLY   B 1 207 ? 13.34574  -8.31236  54.93135  1.000 31.34302  ? 207 GLY   B CA   1 
ATOM   4389 C  C    . GLY   B 1 207 ? 13.05091  -9.49780  54.03542  1.000 34.95049  ? 207 GLY   B C    1 
ATOM   4390 O  O    . GLY   B 1 207 ? 12.57293  -9.38345  52.88761  1.000 36.01477  ? 207 GLY   B O    1 
ATOM   4391 N  N    . ILE   B 1 208 ? 13.35992  -10.68549 54.54954  1.000 31.30954  ? 208 ILE   B N    1 
ATOM   4392 C  CA   . ILE   B 1 208 ? 13.12022  -11.89077 53.75984  1.000 34.85469  ? 208 ILE   B CA   1 
ATOM   4393 C  C    . ILE   B 1 208 ? 11.62362  -12.09493 53.47259  1.000 33.95147  ? 208 ILE   B C    1 
ATOM   4394 O  O    . ILE   B 1 208 ? 11.27481  -12.80103 52.51836  1.000 36.82991  ? 208 ILE   B O    1 
ATOM   4395 C  CB   . ILE   B 1 208 ? 13.78458  -13.11766 54.44848  1.000 43.25826  ? 208 ILE   B CB   1 
ATOM   4396 C  CG1  . ILE   B 1 208 ? 13.76122  -14.33211 53.52514  1.000 47.42553  ? 208 ILE   B CG1  1 
ATOM   4397 C  CG2  . ILE   B 1 208 ? 13.06327  -13.48824 55.69734  1.000 45.89305  ? 208 ILE   B CG2  1 
ATOM   4398 C  CD1  . ILE   B 1 208 ? 14.89408  -14.35800 52.62709  1.000 44.94005  ? 208 ILE   B CD1  1 
ATOM   4399 N  N    . ASP   B 1 209 ? 10.72529  -11.45842 54.24196  1.000 33.57326  ? 209 ASP   B N    1 
ATOM   4400 C  CA   . ASP   B 1 209 ? 9.30151   -11.61049 53.91822  1.000 34.07904  ? 209 ASP   B CA   1 
ATOM   4401 C  C    . ASP   B 1 209 ? 8.92030   -10.91364 52.61621  1.000 37.73802  ? 209 ASP   B C    1 
ATOM   4402 O  O    . ASP   B 1 209 ? 7.78459   -11.10028 52.15117  1.000 37.98290  ? 209 ASP   B O    1 
ATOM   4403 C  CB   . ASP   B 1 209 ? 8.38818   -11.13907 55.04895  1.000 33.38684  ? 209 ASP   B CB   1 
ATOM   4404 C  CG   . ASP   B 1 209 ? 8.44682   -9.66039  55.28541  1.000 35.68027  ? 209 ASP   B CG   1 
ATOM   4405 O  OD1  . ASP   B 1 209 ? 9.38197   -8.98469  54.81991  1.000 35.91059  ? 209 ASP   B OD1  1 
ATOM   4406 O  OD2  . ASP   B 1 209 ? 7.59765   -9.16851  56.04653  1.000 37.55668  ? 209 ASP   B OD2  1 
ATOM   4407 N  N    . GLN   B 1 210 ? 9.82441   -10.13335 52.01397  1.000 33.08989  ? 210 GLN   B N    1 
ATOM   4408 C  CA   . GLN   B 1 210 ? 9.61101   -9.50389  50.69962  1.000 32.93587  ? 210 GLN   B CA   1 
ATOM   4409 C  C    . GLN   B 1 210 ? 10.15495  -10.32877 49.54155  1.000 33.60021  ? 210 GLN   B C    1 
ATOM   4410 O  O    . GLN   B 1 210 ? 10.08035  -9.88793  48.37205  1.000 34.07797  ? 210 GLN   B O    1 
ATOM   4411 C  CB   . GLN   B 1 210 ? 10.26773  -8.10510  50.68586  1.000 30.25390  ? 210 GLN   B CB   1 
ATOM   4412 C  CG   . GLN   B 1 210 ? 9.89423   -7.27981  51.90435  1.000 30.66271  ? 210 GLN   B CG   1 
ATOM   4413 C  CD   . GLN   B 1 210 ? 8.43492   -6.85343  51.89196  1.000 34.77770  ? 210 GLN   B CD   1 
ATOM   4414 O  OE1  . GLN   B 1 210 ? 8.01018   -6.22109  50.93951  1.000 30.36486  ? 210 GLN   B OE1  1 
ATOM   4415 N  NE2  . GLN   B 1 210 ? 7.68328   -7.15720  52.95925  1.000 29.91867  ? 210 GLN   B NE2  1 
ATOM   4416 N  N    . ARG   B 1 211 ? 10.74331  -11.50491 49.83280  1.000 31.43260  ? 211 ARG   B N    1 
ATOM   4417 C  CA   . ARG   B 1 211 ? 11.53067  -12.20858 48.81938  1.000 30.01876  ? 211 ARG   B CA   1 
ATOM   4418 C  C    . ARG   B 1 211 ? 10.72372  -12.49218 47.54968  1.000 34.71063  ? 211 ARG   B C    1 
ATOM   4419 O  O    . ARG   B 1 211 ? 11.24715  -12.37360 46.44711  1.000 36.09753  ? 211 ARG   B O    1 
ATOM   4420 C  CB   . ARG   B 1 211 ? 12.05503  -13.50595 49.41570  1.000 33.27594  ? 211 ARG   B CB   1 
ATOM   4421 C  CG   . ARG   B 1 211 ? 12.99152  -14.29253 48.58749  1.000 37.73744  ? 211 ARG   B CG   1 
ATOM   4422 C  CD   . ARG   B 1 211 ? 13.29607  -15.60556 49.34651  1.000 42.35019  ? 211 ARG   B CD   1 
ATOM   4423 N  NE   . ARG   B 1 211 ? 14.48155  -16.24726 48.79952  1.000 46.69115  ? 211 ARG   B NE   1 
ATOM   4424 C  CZ   . ARG   B 1 211 ? 14.47098  -17.10390 47.78695  1.000 47.91900  ? 211 ARG   B CZ   1 
ATOM   4425 N  NH1  . ARG   B 1 211 ? 13.34716  -17.42023 47.15765  1.000 48.13085  ? 211 ARG   B NH1  1 
ATOM   4426 N  NH2  . ARG   B 1 211 ? 15.61841  -17.63173 47.37583  1.000 51.25794  ? 211 ARG   B NH2  1 
ATOM   4427 N  N    . LYS   B 1 212 ? 9.44602   -12.89271 47.68589  1.000 36.29330  ? 212 LYS   B N    1 
ATOM   4428 C  CA   . LYS   B 1 212 ? 8.67723   -13.29144 46.49721  1.000 35.22825  ? 212 LYS   B CA   1 
ATOM   4429 C  C    . LYS   B 1 212 ? 8.67061   -12.19757 45.43142  1.000 33.54967  ? 212 LYS   B C    1 
ATOM   4430 O  O    . LYS   B 1 212 ? 8.84506   -12.46881 44.21508  1.000 34.54439  ? 212 LYS   B O    1 
ATOM   4431 C  CB   . LYS   B 1 212 ? 7.24116   -13.66902 46.90514  1.000 44.51968  ? 212 LYS   B CB   1 
ATOM   4432 C  CG   . LYS   B 1 212 ? 7.27683   -15.10102 47.43639  1.000 48.90361  ? 212 LYS   B CG   1 
ATOM   4433 C  CD   . LYS   B 1 212 ? 7.61668   -16.06064 46.27605  1.000 54.56152  ? 212 LYS   B CD   1 
ATOM   4434 C  CE   . LYS   B 1 212 ? 8.12739   -17.41716 46.79957  1.000 66.88126  ? 212 LYS   B CE   1 
ATOM   4435 N  NZ   . LYS   B 1 212 ? 9.53219   -17.25763 47.42879  1.000 66.91205  ? 212 LYS   B NZ   1 
ATOM   4436 N  N    . VAL   B 1 213 ? 8.47668   -10.95424 45.84896  1.000 33.81230  ? 213 VAL   B N    1 
ATOM   4437 C  CA   . VAL   B 1 213 ? 8.34995   -9.95184  44.78445  1.000 34.03242  ? 213 VAL   B CA   1 
ATOM   4438 C  C    . VAL   B 1 213 ? 9.72150   -9.60017  44.24860  1.000 35.79206  ? 213 VAL   B C    1 
ATOM   4439 O  O    . VAL   B 1 213 ? 9.87297   -9.23353  43.07238  1.000 29.05034  ? 213 VAL   B O    1 
ATOM   4440 C  CB   . VAL   B 1 213 ? 7.56851   -8.72994  45.27939  1.000 32.55624  ? 213 VAL   B CB   1 
ATOM   4441 C  CG1  . VAL   B 1 213 ? 8.42988   -7.91408  46.26587  1.000 33.11238  ? 213 VAL   B CG1  1 
ATOM   4442 C  CG2  . VAL   B 1 213 ? 7.10336   -7.85245  44.06929  1.000 31.21512  ? 213 VAL   B CG2  1 
ATOM   4443 N  N    . ASN   B 1 214 ? 10.76859  -9.72783  45.08194  1.000 32.29218  ? 214 ASN   B N    1 
ATOM   4444 C  CA   . ASN   B 1 214 ? 12.12212  -9.49967  44.57413  1.000 32.46481  ? 214 ASN   B CA   1 
ATOM   4445 C  C    . ASN   B 1 214 ? 12.50621  -10.57636 43.57006  1.000 29.57565  ? 214 ASN   B C    1 
ATOM   4446 O  O    . ASN   B 1 214 ? 13.21046  -10.30166 42.57522  1.000 30.76101  ? 214 ASN   B O    1 
ATOM   4447 C  CB   . ASN   B 1 214 ? 13.09881  -9.46298  45.76870  1.000 29.80397  ? 214 ASN   B CB   1 
ATOM   4448 C  CG   . ASN   B 1 214 ? 13.01246  -8.18014  46.57167  1.000 33.95436  ? 214 ASN   B CG   1 
ATOM   4449 O  OD1  . ASN   B 1 214 ? 12.95939  -7.08000  46.02569  1.000 34.86085  ? 214 ASN   B OD1  1 
ATOM   4450 N  ND2  . ASN   B 1 214 ? 13.06488  -8.31792  47.90824  1.000 34.94016  ? 214 ASN   B ND2  1 
ATOM   4451 N  N    . MET   B 1 215 ? 12.01973  -11.81489 43.79633  1.000 32.59057  ? 215 MET   B N    1 
ATOM   4452 C  CA   . MET   B 1 215 ? 12.28796  -12.86799 42.84449  1.000 36.10344  ? 215 MET   B CA   1 
ATOM   4453 C  C    . MET   B 1 215 ? 11.47767  -12.61976 41.58488  1.000 33.16497  ? 215 MET   B C    1 
ATOM   4454 O  O    . MET   B 1 215 ? 11.96155  -12.87437 40.48360  1.000 34.38720  ? 215 MET   B O    1 
ATOM   4455 C  CB   . MET   B 1 215 ? 11.96812  -14.24967 43.40963  1.000 40.79100  ? 215 MET   B CB   1 
ATOM   4456 C  CG   . MET   B 1 215 ? 12.80509  -14.63269 44.66062  1.000 39.44756  ? 215 MET   B CG   1 
ATOM   4457 S  SD   . MET   B 1 215 ? 14.58316  -14.78221 44.24329  1.000 54.83175  ? 215 MET   B SD   1 
ATOM   4458 C  CE   . MET   B 1 215 ? 14.64333  -16.10635 43.00869  1.000 54.31884  ? 215 MET   B CE   1 
ATOM   4459 N  N    . LEU   B 1 216 ? 10.27849  -12.04406 41.75118  1.000 34.80263  ? 216 LEU   B N    1 
ATOM   4460 C  CA   . LEU   B 1 216 ? 9.46462   -11.73006 40.57872  1.000 33.48780  ? 216 LEU   B CA   1 
ATOM   4461 C  C    . LEU   B 1 216 ? 10.23102  -10.77397 39.69743  1.000 34.17569  ? 216 LEU   B C    1 
ATOM   4462 O  O    . LEU   B 1 216 ? 10.26662  -10.93483 38.46952  1.000 33.98799  ? 216 LEU   B O    1 
ATOM   4463 C  CB   . LEU   B 1 216 ? 8.14004   -11.10894 41.01087  1.000 33.22210  ? 216 LEU   B CB   1 
ATOM   4464 C  CG   . LEU   B 1 216 ? 7.10176   -10.98790 39.90010  1.000 37.57614  ? 216 LEU   B CG   1 
ATOM   4465 C  CD1  . LEU   B 1 216 ? 6.39699   -12.32865 39.73316  1.000 41.28411  ? 216 LEU   B CD1  1 
ATOM   4466 C  CD2  . LEU   B 1 216 ? 6.13168   -9.87942  40.27000  1.000 42.06758  ? 216 LEU   B CD2  1 
ATOM   4467 N  N    . ALA   B 1 217 ? 10.93242  -9.81370  40.32716  1.000 33.65425  ? 217 ALA   B N    1 
ATOM   4468 C  CA   . ALA   B 1 217 ? 11.62811  -8.83173  39.51824  1.000 34.23279  ? 217 ALA   B CA   1 
ATOM   4469 C  C    . ALA   B 1 217 ? 12.70258  -9.52041  38.72420  1.000 35.67100  ? 217 ALA   B C    1 
ATOM   4470 O  O    . ALA   B 1 217 ? 12.91770  -9.20608  37.54947  1.000 31.97959  ? 217 ALA   B O    1 
ATOM   4471 C  CB   . ALA   B 1 217 ? 12.25697  -7.74266  40.39684  1.000 34.45176  ? 217 ALA   B CB   1 
ATOM   4472 N  N    . ARG   B 1 218 ? 13.43908  -10.43985 39.38171  1.000 34.44657  ? 218 ARG   B N    1 
ATOM   4473 C  CA   . ARG   B 1 218 ? 14.48460  -11.15430 38.65033  1.000 35.31210  ? 218 ARG   B CA   1 
ATOM   4474 C  C    . ARG   B 1 218 ? 13.86948  -11.94142 37.50314  1.000 38.50621  ? 218 ARG   B C    1 
ATOM   4475 O  O    . ARG   B 1 218 ? 14.41666  -11.96695 36.39559  1.000 38.71357  ? 218 ARG   B O    1 
ATOM   4476 C  CB   . ARG   B 1 218 ? 15.27574  -12.05684 39.60458  1.000 35.51269  ? 218 ARG   B CB   1 
ATOM   4477 C  CG   . ARG   B 1 218 ? 16.11534  -11.23560 40.58193  1.000 37.16157  ? 218 ARG   B CG   1 
ATOM   4478 C  CD   . ARG   B 1 218 ? 16.88467  -12.12541 41.57942  1.000 33.30401  ? 218 ARG   B CD   1 
ATOM   4479 N  NE   . ARG   B 1 218 ? 17.70261  -13.12561 40.90069  1.000 35.38915  ? 218 ARG   B NE   1 
ATOM   4480 C  CZ   . ARG   B 1 218 ? 18.94641  -12.92326 40.48267  1.000 39.92100  ? 218 ARG   B CZ   1 
ATOM   4481 N  NH1  . ARG   B 1 218 ? 19.54447  -11.74736 40.63380  1.000 35.14547  ? 218 ARG   B NH1  1 
ATOM   4482 N  NH2  . ARG   B 1 218 ? 19.61209  -13.92625 39.91097  1.000 41.18186  ? 218 ARG   B NH2  1 
ATOM   4483 N  N    . GLU   B 1 219 ? 12.72004  -12.58241 37.74370  1.000 37.19566  ? 219 GLU   B N    1 
ATOM   4484 C  CA   . GLU   B 1 219 ? 12.06873  -13.32337 36.66796  1.000 37.13309  ? 219 GLU   B CA   1 
ATOM   4485 C  C    . GLU   B 1 219 ? 11.67832  -12.37525 35.52514  1.000 39.09575  ? 219 GLU   B C    1 
ATOM   4486 O  O    . GLU   B 1 219 ? 11.79247  -12.71170 34.33295  1.000 38.64936  ? 219 GLU   B O    1 
ATOM   4487 C  CB   . GLU   B 1 219 ? 10.82825  -14.00182 37.22948  1.000 43.05482  ? 219 GLU   B CB   1 
ATOM   4488 C  CG   . GLU   B 1 219 ? 10.82291  -15.47476 37.32358  1.000 55.50208  ? 219 GLU   B CG   1 
ATOM   4489 C  CD   . GLU   B 1 219 ? 9.38566   -15.98405 37.36971  1.000 70.55518  ? 219 GLU   B CD   1 
ATOM   4490 O  OE1  . GLU   B 1 219 ? 8.89264   -16.51376 36.32547  1.000 67.33874  ? 219 GLU   B OE1  1 
ATOM   4491 O  OE2  . GLU   B 1 219 ? 8.74141   -15.78892 38.43730  1.000 66.58492  ? 219 GLU   B OE2  1 
ATOM   4492 N  N    . TYR   B 1 220 ? 11.22214  -11.16653 35.87178  1.000 36.76438  ? 220 TYR   B N    1 
ATOM   4493 C  CA   . TYR   B 1 220 ? 10.82571  -10.24952 34.80688  1.000 35.93648  ? 220 TYR   B CA   1 
ATOM   4494 C  C    . TYR   B 1 220 ? 12.03386  -9.89411  33.95731  1.000 38.15404  ? 220 TYR   B C    1 
ATOM   4495 O  O    . TYR   B 1 220 ? 11.92461  -9.69549  32.74557  1.000 34.58629  ? 220 TYR   B O    1 
ATOM   4496 C  CB   . TYR   B 1 220 ? 10.17381  -9.00136  35.42106  1.000 34.38844  ? 220 TYR   B CB   1 
ATOM   4497 C  CG   . TYR   B 1 220 ? 9.70619   -7.96894  34.44327  1.000 37.04092  ? 220 TYR   B CG   1 
ATOM   4498 C  CD1  . TYR   B 1 220 ? 8.56292   -8.19292  33.65786  1.000 34.13395  ? 220 TYR   B CD1  1 
ATOM   4499 C  CD2  . TYR   B 1 220 ? 10.32676  -6.73131  34.37025  1.000 34.55088  ? 220 TYR   B CD2  1 
ATOM   4500 C  CE1  . TYR   B 1 220 ? 8.10512   -7.22624  32.73988  1.000 39.45197  ? 220 TYR   B CE1  1 
ATOM   4501 C  CE2  . TYR   B 1 220 ? 9.89627   -5.75900  33.47754  1.000 40.52168  ? 220 TYR   B CE2  1 
ATOM   4502 C  CZ   . TYR   B 1 220 ? 8.76753   -5.99781  32.68029  1.000 40.38614  ? 220 TYR   B CZ   1 
ATOM   4503 O  OH   . TYR   B 1 220 ? 8.36691   -5.00738  31.80835  1.000 39.41438  ? 220 TYR   B OH   1 
ATOM   4504 N  N    . CYS   B 1 221 ? 13.21841  -9.78744  34.58280  1.000 34.40811  ? 221 CYS   B N    1 
ATOM   4505 C  CA   . CYS   B 1 221 ? 14.38181  -9.50452  33.75354  1.000 32.69484  ? 221 CYS   B CA   1 
ATOM   4506 C  C    . CYS   B 1 221 ? 14.58046  -10.59750 32.74476  1.000 35.53447  ? 221 CYS   B C    1 
ATOM   4507 O  O    . CYS   B 1 221 ? 14.94061  -10.34528 31.58421  1.000 39.46522  ? 221 CYS   B O    1 
ATOM   4508 C  CB   . CYS   B 1 221 ? 15.64203  -9.37122  34.64210  1.000 33.33928  ? 221 CYS   B CB   1 
ATOM   4509 S  SG   . CYS   B 1 221 ? 15.62040  -7.96927  35.67946  1.000 38.57098  ? 221 CYS   B SG   1 
ATOM   4510 N  N    . ASP   B 1 222 ? 14.43316  -11.84456 33.17890  1.000 35.66508  ? 222 ASP   B N    1 
ATOM   4511 C  CA   . ASP   B 1 222 ? 14.69344  -12.92481 32.24605  1.000 37.54313  ? 222 ASP   B CA   1 
ATOM   4512 C  C    . ASP   B 1 222 ? 13.67242  -12.89112 31.11515  1.000 43.62643  ? 222 ASP   B C    1 
ATOM   4513 O  O    . ASP   B 1 222 ? 14.01389  -13.09217 29.94573  1.000 41.44934  ? 222 ASP   B O    1 
ATOM   4514 C  CB   . ASP   B 1 222 ? 14.65531  -14.23784 32.99542  1.000 42.84881  ? 222 ASP   B CB   1 
ATOM   4515 C  CG   . ASP   B 1 222 ? 15.87827  -14.40735 33.89971  1.000 53.55745  ? 222 ASP   B CG   1 
ATOM   4516 O  OD1  . ASP   B 1 222 ? 16.80495  -13.55691 33.81555  1.000 50.45739  ? 222 ASP   B OD1  1 
ATOM   4517 O  OD2  . ASP   B 1 222 ? 15.87625  -15.33791 34.73692  1.000 50.32932  ? 222 ASP   B OD2  1 
ATOM   4518 N  N    . ILE   B 1 223 ? 12.42103  -12.54557 31.44747  1.000 42.00281  ? 223 ILE   B N    1 
ATOM   4519 C  CA   . ILE   B 1 223 ? 11.36615  -12.54964 30.42620  1.000 38.52526  ? 223 ILE   B CA   1 
ATOM   4520 C  C    . ILE   B 1 223 ? 11.63771  -11.49211 29.36526  1.000 38.03054  ? 223 ILE   B C    1 
ATOM   4521 O  O    . ILE   B 1 223 ? 11.42802  -11.72112 28.16094  1.000 40.09833  ? 223 ILE   B O    1 
ATOM   4522 C  CB   . ILE   B 1 223 ? 10.01537  -12.30832 31.10611  1.000 36.29517  ? 223 ILE   B CB   1 
ATOM   4523 C  CG1  . ILE   B 1 223 ? 9.55456   -13.54483 31.87110  1.000 41.03245  ? 223 ILE   B CG1  1 
ATOM   4524 C  CG2  . ILE   B 1 223 ? 8.97601   -11.84617 30.04791  1.000 40.77410  ? 223 ILE   B CG2  1 
ATOM   4525 C  CD1  . ILE   B 1 223 ? 8.34266   -13.25659 32.83486  1.000 44.54764  ? 223 ILE   B CD1  1 
ATOM   4526 N  N    . LYS   B 1 224 ? 12.05145  -10.30668 29.79895  1.000 36.76820  ? 224 LYS   B N    1 
ATOM   4527 C  CA   . LYS   B 1 224 ? 12.29368  -9.15848  28.94090  1.000 37.65727  ? 224 LYS   B CA   1 
ATOM   4528 C  C    . LYS   B 1 224 ? 13.71974  -9.12574  28.40298  1.000 41.65859  ? 224 LYS   B C    1 
ATOM   4529 O  O    . LYS   B 1 224 ? 14.06886  -8.20071  27.66494  1.000 44.32284  ? 224 LYS   B O    1 
ATOM   4530 C  CB   . LYS   B 1 224 ? 12.04768  -7.87177  29.71881  1.000 37.86928  ? 224 LYS   B CB   1 
ATOM   4531 C  CG   . LYS   B 1 224 ? 10.57671  -7.69922  30.14792  1.000 40.15200  ? 224 LYS   B CG   1 
ATOM   4532 C  CD   . LYS   B 1 224 ? 9.73270   -7.40091  28.88817  1.000 41.57130  ? 224 LYS   B CD   1 
ATOM   4533 C  CE   . LYS   B 1 224 ? 8.21923   -7.30931  29.21528  1.000 47.73265  ? 224 LYS   B CE   1 
ATOM   4534 N  NZ   . LYS   B 1 224 ? 7.51813   -6.48330  28.18367  1.000 50.42908  ? 224 LYS   B NZ   1 
ATOM   4535 N  N    . LYS   B 1 225 ? 14.54797  -10.10279 28.74325  1.000 40.41859  ? 225 LYS   B N    1 
ATOM   4536 C  CA   . LYS   B 1 225 ? 15.96278  -10.10710 28.30450  1.000 46.52851  ? 225 LYS   B CA   1 
ATOM   4537 C  C    . LYS   B 1 225 ? 16.70943  -8.88547  28.82143  1.000 41.28787  ? 225 LYS   B C    1 
ATOM   4538 O  O    . LYS   B 1 225 ? 17.58245  -8.34999  28.13903  1.000 45.74840  ? 225 LYS   B O    1 
ATOM   4539 C  CB   . LYS   B 1 225 ? 16.11731  -10.16190 26.76750  1.000 51.19861  ? 225 LYS   B CB   1 
ATOM   4540 C  CG   . LYS   B 1 225 ? 15.55911  -11.37978 26.06526  1.000 51.55401  ? 225 LYS   B CG   1 
ATOM   4541 C  CD   . LYS   B 1 225 ? 15.62595  -12.61190 26.93106  1.000 53.28744  ? 225 LYS   B CD   1 
ATOM   4542 C  CE   . LYS   B 1 225 ? 14.66589  -13.66221 26.36716  1.000 63.68628  ? 225 LYS   B CE   1 
ATOM   4543 N  NZ   . LYS   B 1 225 ? 14.30811  -14.70620 27.38388  1.000 65.97375  ? 225 LYS   B NZ   1 
ATOM   4544 N  N    . ILE   B 1 226 ? 16.37177  -8.40937  30.00942  1.000 42.02766  ? 226 ILE   B N    1 
ATOM   4545 C  CA   . ILE   B 1 226 ? 17.11006  -7.32780  30.63438  1.000 41.94844  ? 226 ILE   B CA   1 
ATOM   4546 C  C    . ILE   B 1 226 ? 18.27976  -7.97899  31.36942  1.000 43.31645  ? 226 ILE   B C    1 
ATOM   4547 O  O    . ILE   B 1 226 ? 18.05945  -8.83096  32.23508  1.000 42.59237  ? 226 ILE   B O    1 
ATOM   4548 C  CB   . ILE   B 1 226 ? 16.22503  -6.53440  31.60197  1.000 45.68767  ? 226 ILE   B CB   1 
ATOM   4549 C  CG1  . ILE   B 1 226 ? 15.08470  -5.81194  30.86139  1.000 41.75624  ? 226 ILE   B CG1  1 
ATOM   4550 C  CG2  . ILE   B 1 226 ? 17.04875  -5.54174  32.41519  1.000 45.24149  ? 226 ILE   B CG2  1 
ATOM   4551 C  CD1  . ILE   B 1 226 ? 14.06096  -5.21534  31.81909  1.000 47.90806  ? 226 ILE   B CD1  1 
ATOM   4552 N  N    . LYS   B 1 227 ? 19.51454  -7.61039  31.00040  1.000 42.69017  ? 227 LYS   B N    1 
ATOM   4553 C  CA   . LYS   B 1 227 ? 20.69090  -8.26879  31.58501  1.000 42.05477  ? 227 LYS   B CA   1 
ATOM   4554 C  C    . LYS   B 1 227 ? 21.09728  -7.68569  32.93165  1.000 45.97277  ? 227 LYS   B C    1 
ATOM   4555 O  O    . LYS   B 1 227 ? 21.68504  -8.40617  33.74513  1.000 48.78073  ? 227 LYS   B O    1 
ATOM   4556 C  CB   . LYS   B 1 227 ? 21.89755  -8.21130  30.63392  1.000 43.38446  ? 227 LYS   B CB   1 
ATOM   4557 C  CG   . LYS   B 1 227 ? 21.71032  -9.06637  29.37108  1.000 58.82105  ? 227 LYS   B CG   1 
ATOM   4558 C  CD   . LYS   B 1 227 ? 21.45449  -10.53253 29.74697  1.000 60.56132  ? 227 LYS   B CD   1 
ATOM   4559 C  CE   . LYS   B 1 227 ? 21.29458  -11.43813 28.51198  1.000 60.91933  ? 227 LYS   B CE   1 
ATOM   4560 N  NZ   . LYS   B 1 227 ? 20.02756  -11.28048 27.76863  1.000 64.68887  ? 227 LYS   B NZ   1 
ATOM   4561 N  N    . LYS   B 1 228 ? 20.78469  -6.41758  33.19598  1.000 42.28304  ? 228 LYS   B N    1 
ATOM   4562 C  CA   . LYS   B 1 228 ? 21.01186  -5.80260  34.50073  1.000 45.03716  ? 228 LYS   B CA   1 
ATOM   4563 C  C    . LYS   B 1 228 ? 19.94874  -6.29814  35.47437  1.000 51.50679  ? 228 LYS   B C    1 
ATOM   4564 O  O    . LYS   B 1 228 ? 18.79129  -5.87707  35.40827  1.000 50.14387  ? 228 LYS   B O    1 
ATOM   4565 C  CB   . LYS   B 1 228 ? 20.96884  -4.28486  34.40131  1.000 44.21513  ? 228 LYS   B CB   1 
ATOM   4566 C  CG   . LYS   B 1 228 ? 21.36397  -3.66452  35.74183  1.000 45.09909  ? 228 LYS   B CG   1 
ATOM   4567 C  CD   . LYS   B 1 228 ? 21.34364  -2.16576  35.70920  1.000 46.95787  ? 228 LYS   B CD   1 
ATOM   4568 C  CE   . LYS   B 1 228 ? 21.57059  -1.67404  37.10842  1.000 54.62520  ? 228 LYS   B CE   1 
ATOM   4569 N  NZ   . LYS   B 1 228 ? 21.36432  -0.23911  37.24118  1.000 55.31216  ? 228 LYS   B NZ   1 
ATOM   4570 N  N    . LYS   B 1 229 ? 20.31967  -7.21504  36.36204  1.000 38.12181  ? 229 LYS   B N    1 
ATOM   4571 C  CA   . LYS   B 1 229 ? 19.35898  -7.80167  37.28102  1.000 38.59974  ? 229 LYS   B CA   1 
ATOM   4572 C  C    . LYS   B 1 229 ? 19.69681  -7.38792  38.69355  1.000 44.45315  ? 229 LYS   B C    1 
ATOM   4573 O  O    . LYS   B 1 229 ? 20.89261  -7.25385  39.02016  1.000 35.88332  ? 229 LYS   B O    1 
ATOM   4574 C  CB   . LYS   B 1 229 ? 19.37075  -9.33106  37.20099  1.000 41.21108  ? 229 LYS   B CB   1 
ATOM   4575 C  CG   . LYS   B 1 229 ? 18.79554  -9.85251  35.92994  1.000 49.45969  ? 229 LYS   B CG   1 
ATOM   4576 C  CD   . LYS   B 1 229 ? 19.11253  -11.31577 35.68667  1.000 50.85974  ? 229 LYS   B CD   1 
ATOM   4577 C  CE   . LYS   B 1 229 ? 18.39765  -12.23546 36.67871  1.000 50.05223  ? 229 LYS   B CE   1 
ATOM   4578 N  NZ   . LYS   B 1 229 ? 18.42245  -13.62244 36.06895  1.000 49.87158  ? 229 LYS   B NZ   1 
ATOM   4579 N  N    . PRO   B 1 230 ? 18.69389  -7.16602  39.53744  1.000 36.78251  ? 230 PRO   B N    1 
ATOM   4580 C  CA   . PRO   B 1 230 ? 18.96900  -6.76718  40.92033  1.000 35.02599  ? 230 PRO   B CA   1 
ATOM   4581 C  C    . PRO   B 1 230 ? 19.43162  -7.94604  41.77918  1.000 36.13747  ? 230 PRO   B C    1 
ATOM   4582 O  O    . PRO   B 1 230 ? 18.99008  -9.08383  41.60003  1.000 33.78030  ? 230 PRO   B O    1 
ATOM   4583 C  CB   . PRO   B 1 230 ? 17.61457  -6.22413  41.40233  1.000 37.16061  ? 230 PRO   B CB   1 
ATOM   4584 C  CG   . PRO   B 1 230 ? 16.64175  -7.01287  40.64629  1.000 31.70747  ? 230 PRO   B CG   1 
ATOM   4585 C  CD   . PRO   B 1 230 ? 17.22470  -7.16658  39.25145  1.000 30.69075  ? 230 PRO   B CD   1 
ATOM   4586 N  N    . VAL   B 1 231 ? 20.37274  -7.67772  42.69165  1.000 32.45973  ? 231 VAL   B N    1 
ATOM   4587 C  CA   . VAL   B 1 231 ? 20.75513  -8.66314  43.71116  1.000 34.62875  ? 231 VAL   B CA   1 
ATOM   4588 C  C    . VAL   B 1 231 ? 19.79354  -8.55452  44.88112  1.000 33.71834  ? 231 VAL   B C    1 
ATOM   4589 O  O    . VAL   B 1 231 ? 19.50686  -7.44980  45.35512  1.000 32.97690  ? 231 VAL   B O    1 
ATOM   4590 C  CB   . VAL   B 1 231 ? 22.20803  -8.45342  44.17868  1.000 34.72516  ? 231 VAL   B CB   1 
ATOM   4591 C  CG1  . VAL   B 1 231 ? 22.50900  -9.33848  45.38818  1.000 39.62480  ? 231 VAL   B CG1  1 
ATOM   4592 C  CG2  . VAL   B 1 231 ? 23.16790  -8.74974  42.98844  1.000 37.03116  ? 231 VAL   B CG2  1 
ATOM   4593 N  N    . ILE   B 1 232 ? 19.29211  -9.69226  45.36321  1.000 31.42475  ? 232 ILE   B N    1 
ATOM   4594 C  CA   . ILE   B 1 232 ? 18.38988  -9.70102  46.50572  1.000 31.34794  ? 232 ILE   B CA   1 
ATOM   4595 C  C    . ILE   B 1 232 ? 19.25648  -9.95825  47.75296  1.000 37.89358  ? 232 ILE   B C    1 
ATOM   4596 O  O    . ILE   B 1 232 ? 19.71715  -11.06498 47.96378  1.000 35.74635  ? 232 ILE   B O    1 
ATOM   4597 C  CB   . ILE   B 1 232 ? 17.28541  -10.76360 46.37900  1.000 31.44533  ? 232 ILE   B CB   1 
ATOM   4598 C  CG1  . ILE   B 1 232 ? 16.66824  -10.77414 44.95334  1.000 34.47311  ? 232 ILE   B CG1  1 
ATOM   4599 C  CG2  . ILE   B 1 232 ? 16.22704  -10.49454 47.41807  1.000 30.15613  ? 232 ILE   B CG2  1 
ATOM   4600 C  CD1  . ILE   B 1 232 ? 16.41566  -9.38958  44.41995  1.000 37.55322  ? 232 ILE   B CD1  1 
ATOM   4601 N  N    . LEU   B 1 233 ? 19.43277  -8.95530  48.59348  1.000 29.36439  ? 233 LEU   B N    1 
ATOM   4602 C  CA   . LEU   B 1 233 ? 20.24529  -9.09224  49.83363  1.000 30.06214  ? 233 LEU   B CA   1 
ATOM   4603 C  C    . LEU   B 1 233 ? 19.28765  -8.98450  51.01118  1.000 29.82586  ? 233 LEU   B C    1 
ATOM   4604 O  O    . LEU   B 1 233 ? 19.02279  -7.89898  51.53194  1.000 31.16076  ? 233 LEU   B O    1 
ATOM   4605 C  CB   . LEU   B 1 233 ? 21.30515  -8.02012  49.85319  1.000 31.71775  ? 233 LEU   B CB   1 
ATOM   4606 C  CG   . LEU   B 1 233 ? 22.31245  -8.12402  51.02402  1.000 34.27223  ? 233 LEU   B CG   1 
ATOM   4607 C  CD1  . LEU   B 1 233 ? 23.11045  -9.35865  50.67062  1.000 36.86672  ? 233 LEU   B CD1  1 
ATOM   4608 C  CD2  . LEU   B 1 233 ? 23.17472  -6.83900  51.06801  1.000 36.45992  ? 233 LEU   B CD2  1 
ATOM   4609 N  N    . SER   B 1 234 ? 18.67312  -10.10499 51.37701  1.000 28.81397  ? 234 SER   B N    1 
ATOM   4610 C  CA   . SER   B 1 234 ? 17.60555  -10.06130 52.36290  1.000 31.47795  ? 234 SER   B CA   1 
ATOM   4611 C  C    . SER   B 1 234 ? 18.18270  -10.18965 53.76765  1.000 36.45593  ? 234 SER   B C    1 
ATOM   4612 O  O    . SER   B 1 234 ? 19.11535  -10.98395 53.99465  1.000 37.86269  ? 234 SER   B O    1 
ATOM   4613 C  CB   . SER   B 1 234 ? 16.60765  -11.19297 52.17396  1.000 34.33996  ? 234 SER   B CB   1 
ATOM   4614 O  OG   . SER   B 1 234 ? 16.08293  -11.19915 50.84075  1.000 39.34211  ? 234 SER   B OG   1 
ATOM   4615 N  N    . HIS   B 1 235 ? 17.61379  -9.41482  54.69064  1.000 33.99239  ? 235 HIS   B N    1 
ATOM   4616 C  CA   . HIS   B 1 235 ? 17.91687  -9.56947  56.12179  1.000 35.36010  ? 235 HIS   B CA   1 
ATOM   4617 C  C    . HIS   B 1 235 ? 16.85447  -10.41337 56.81744  1.000 40.30870  ? 235 HIS   B C    1 
ATOM   4618 O  O    . HIS   B 1 235 ? 15.69425  -10.53337 56.36696  1.000 31.05606  ? 235 HIS   B O    1 
ATOM   4619 C  CB   . HIS   B 1 235 ? 18.06284  -8.21579  56.82649  1.000 32.12084  ? 235 HIS   B CB   1 
ATOM   4620 C  CG   . HIS   B 1 235 ? 16.78961  -7.40728  56.89768  1.000 31.42251  ? 235 HIS   B CG   1 
ATOM   4621 N  ND1  . HIS   B 1 235 ? 16.53522  -6.35168  56.05305  1.000 31.20498  ? 235 HIS   B ND1  1 
ATOM   4622 C  CD2  . HIS   B 1 235 ? 15.72536  -7.48382  57.73974  1.000 34.72180  ? 235 HIS   B CD2  1 
ATOM   4623 C  CE1  . HIS   B 1 235 ? 15.36442  -5.82007  56.34690  1.000 29.29603  ? 235 HIS   B CE1  1 
ATOM   4624 N  NE2  . HIS   B 1 235 ? 14.84993  -6.48147  57.37379  1.000 31.16827  ? 235 HIS   B NE2  1 
ATOM   4625 N  N    . GLY   B 1 236 ? 17.25796  -10.99053 57.95964  1.000 36.37805  ? 236 GLY   B N    1 
ATOM   4626 C  CA   . GLY   B 1 236 ? 16.36233  -11.88369 58.66697  1.000 38.49394  ? 236 GLY   B CA   1 
ATOM   4627 C  C    . GLY   B 1 236 ? 15.27770  -11.13105 59.40923  1.000 33.10986  ? 236 GLY   B C    1 
ATOM   4628 O  O    . GLY   B 1 236 ? 15.46023  -9.98009  59.81375  1.000 35.57529  ? 236 GLY   B O    1 
ATOM   4629 N  N    . MET   B 1 237 ? 14.14928  -11.80707 59.61199  1.000 33.51761  ? 237 MET   B N    1 
ATOM   4630 C  CA   . MET   B 1 237 ? 13.02830  -11.21196 60.34921  1.000 35.11515  ? 237 MET   B CA   1 
ATOM   4631 C  C    . MET   B 1 237 ? 13.27439  -11.31219 61.86321  1.000 36.77818  ? 237 MET   B C    1 
ATOM   4632 O  O    . MET   B 1 237 ? 13.65167  -12.38089 62.36957  1.000 34.31279  ? 237 MET   B O    1 
ATOM   4633 C  CB   . MET   B 1 237 ? 11.70654  -11.89786 59.99508  1.000 34.24386  ? 237 MET   B CB   1 
ATOM   4634 C  CG   . MET   B 1 237 ? 11.39301  -11.95048 58.46293  1.000 36.87916  ? 237 MET   B CG   1 
ATOM   4635 S  SD   . MET   B 1 237 ? 11.42267  -10.29352 57.75191  1.000 37.68988  ? 237 MET   B SD   1 
ATOM   4636 C  CE   . MET   B 1 237 ? 9.90633   -9.66111  58.33436  1.000 33.08424  ? 237 MET   B CE   1 
ATOM   4637 N  N    . LEU   B 1 238 ? 13.10737  -10.20141 62.57436  1.000 31.74455  ? 238 LEU   B N    1 
ATOM   4638 C  CA   . LEU   B 1 238 ? 13.14330  -10.28076 64.05460  1.000 33.05838  ? 238 LEU   B CA   1 
ATOM   4639 C  C    . LEU   B 1 238 ? 11.82593  -10.90646 64.49776  1.000 32.84818  ? 238 LEU   B C    1 
ATOM   4640 O  O    . LEU   B 1 238 ? 10.76374  -10.49883 64.01021  1.000 32.96189  ? 238 LEU   B O    1 
ATOM   4641 C  CB   . LEU   B 1 238 ? 13.30770  -8.90513  64.72428  1.000 32.07839  ? 238 LEU   B CB   1 
ATOM   4642 C  CG   . LEU   B 1 238 ? 14.60684  -8.19248  64.34539  1.000 34.53347  ? 238 LEU   B CG   1 
ATOM   4643 C  CD1  . LEU   B 1 238 ? 14.66242  -6.85898  65.11733  1.000 32.61161  ? 238 LEU   B CD1  1 
ATOM   4644 C  CD2  . LEU   B 1 238 ? 15.80747  -9.07561  64.65545  1.000 34.83527  ? 238 LEU   B CD2  1 
ATOM   4645 N  N    . PRO   B 1 239 ? 11.82886  -11.92333 65.34469  1.000 33.17543  ? 239 PRO   B N    1 
ATOM   4646 C  CA   . PRO   B 1 239 ? 10.54701  -12.53347 65.72126  1.000 36.87715  ? 239 PRO   B CA   1 
ATOM   4647 C  C    . PRO   B 1 239 ? 9.70788   -11.54751 66.52231  1.000 39.17478  ? 239 PRO   B C    1 
ATOM   4648 O  O    . PRO   B 1 239 ? 10.21172  -10.57488 67.09789  1.000 33.74281  ? 239 PRO   B O    1 
ATOM   4649 C  CB   . PRO   B 1 239 ? 10.95774  -13.76446 66.54457  1.000 37.97305  ? 239 PRO   B CB   1 
ATOM   4650 C  CG   . PRO   B 1 239 ? 12.42926  -13.71029 66.69213  1.000 36.75177  ? 239 PRO   B CG   1 
ATOM   4651 C  CD   . PRO   B 1 239 ? 13.00364  -12.71167 65.78292  1.000 34.80807  ? 239 PRO   B CD   1 
ATOM   4652 N  N    . GLY   B 1 240 ? 8.39799   -11.79343 66.53492  1.000 35.63212  ? 240 GLY   B N    1 
ATOM   4653 C  CA   . GLY   B 1 240 ? 7.51306   -10.93230 67.29839  1.000 34.27223  ? 240 GLY   B CA   1 
ATOM   4654 C  C    . GLY   B 1 240 ? 7.83640   -10.94990 68.78300  1.000 36.76034  ? 240 GLY   B C    1 
ATOM   4655 O  O    . GLY   B 1 240 ? 8.24318   -11.97072 69.36002  1.000 35.98795  ? 240 GLY   B O    1 
ATOM   4656 N  N    . LEU   B 1 241 ? 7.58741   -9.81005  69.42993  1.000 36.11808  ? 241 LEU   B N    1 
ATOM   4657 C  CA   . LEU   B 1 241 ? 7.91147   -9.68859  70.84953  1.000 35.93886  ? 241 LEU   B CA   1 
ATOM   4658 C  C    . LEU   B 1 241 ? 7.13067   -10.68583 71.68275  1.000 40.13544  ? 241 LEU   B C    1 
ATOM   4659 O  O    . LEU   B 1 241 ? 7.66012   -11.22410 72.65908  1.000 38.46400  ? 241 LEU   B O    1 
ATOM   4660 C  CB   . LEU   B 1 241 ? 7.60999   -8.27020  71.33084  1.000 37.30064  ? 241 LEU   B CB   1 
ATOM   4661 C  CG   . LEU   B 1 241 ? 8.07592   -7.86295  72.69931  1.000 40.97775  ? 241 LEU   B CG   1 
ATOM   4662 C  CD1  . LEU   B 1 241 ? 9.63341   -7.87733  72.67192  1.000 38.48850  ? 241 LEU   B CD1  1 
ATOM   4663 C  CD2  . LEU   B 1 241 ? 7.48532   -6.48763  72.99372  1.000 43.87868  ? 241 LEU   B CD2  1 
ATOM   4664 N  N    . LEU   B 1 242 ? 5.85531   -10.93116 71.33273  1.000 41.19052  ? 242 LEU   B N    1 
ATOM   4665 C  CA   . LEU   B 1 242 ? 5.02421   -11.90874 72.03117  1.000 44.69781  ? 242 LEU   B CA   1 
ATOM   4666 C  C    . LEU   B 1 242 ? 4.87416   -13.16541 71.16460  1.000 40.19034  ? 242 LEU   B C    1 
ATOM   4667 O  O    . LEU   B 1 242 ? 4.90282   -13.09995 69.93736  1.000 47.75508  ? 242 LEU   B O    1 
ATOM   4668 C  CB   . LEU   B 1 242 ? 3.64972   -11.30682 72.36846  1.000 47.81288  ? 242 LEU   B CB   1 
ATOM   4669 C  CG   . LEU   B 1 242 ? 3.75355   -10.06266 73.26030  1.000 47.80996  ? 242 LEU   B CG   1 
ATOM   4670 C  CD1  . LEU   B 1 242 ? 2.34571   -9.44467  73.58637  1.000 50.56822  ? 242 LEU   B CD1  1 
ATOM   4671 C  CD2  . LEU   B 1 242 ? 4.47154   -10.48558 74.54247  1.000 47.79914  ? 242 LEU   B CD2  1 
ATOM   4672 N  N    . GLU   B 1 243 ? 4.70497   -14.31298 71.80009  1.000 47.08013  ? 243 GLU   B N    1 
ATOM   4673 C  CA   . GLU   B 1 243 ? 4.72857   -15.53805 70.99950  1.000 56.23939  ? 243 GLU   B CA   1 
ATOM   4674 C  C    . GLU   B 1 243 ? 3.49510   -15.57315 70.09474  1.000 62.15756  ? 243 GLU   B C    1 
ATOM   4675 O  O    . GLU   B 1 243 ? 2.38959   -15.79982 70.60378  1.000 65.36557  ? 243 GLU   B O    1 
ATOM   4676 C  CB   . GLU   B 1 243 ? 4.77114   -16.79056 71.87848  1.000 54.85526  ? 243 GLU   B CB   1 
ATOM   4677 C  CG   . GLU   B 1 243 ? 5.11443   -18.06247 71.07140  1.000 61.92542  ? 243 GLU   B CG   1 
ATOM   4678 C  CD   . GLU   B 1 243 ? 5.09767   -19.36197 71.91377  1.000 72.03599  ? 243 GLU   B CD   1 
ATOM   4679 O  OE1  . GLU   B 1 243 ? 4.71816   -19.32407 73.12026  1.000 65.13787  ? 243 GLU   B OE1  1 
ATOM   4680 O  OE2  . GLU   B 1 243 ? 5.50274   -20.42038 71.36075  1.000 79.98832  ? 243 GLU   B OE2  1 
ATOM   4681 N  N    . GLU   B 1 253 ? 1.05688   -2.19163  70.24557  1.000 64.48397  ? 253 GLU   B N    1 
ATOM   4682 C  CA   . GLU   B 1 253 ? 0.89532   -1.59053  71.58178  1.000 78.08323  ? 253 GLU   B CA   1 
ATOM   4683 C  C    . GLU   B 1 253 ? 1.91297   -2.23006  72.55643  1.000 71.84056  ? 253 GLU   B C    1 
ATOM   4684 O  O    . GLU   B 1 253 ? 3.08816   -1.83694  72.57692  1.000 62.61378  ? 253 GLU   B O    1 
ATOM   4685 C  CB   . GLU   B 1 253 ? -0.55263  -1.74093  72.07833  1.000 83.75047  ? 253 GLU   B CB   1 
ATOM   4686 C  CG   . GLU   B 1 253 ? -1.07578  -3.17516  72.28185  1.000 86.64299  ? 253 GLU   B CG   1 
ATOM   4687 C  CD   . GLU   B 1 253 ? -1.12221  -4.01029  71.01693  1.000 86.45108  ? 253 GLU   B CD   1 
ATOM   4688 O  OE1  . GLU   B 1 253 ? -0.43577  -3.65790  70.02680  1.000 85.10901  ? 253 GLU   B OE1  1 
ATOM   4689 O  OE2  . GLU   B 1 253 ? -1.83925  -5.03610  71.03044  1.000 93.20472  ? 253 GLU   B OE2  1 
ATOM   4690 N  N    . ASN   B 1 254 ? 1.47009   -3.20523  73.35616  1.000 66.73496  ? 254 ASN   B N    1 
ATOM   4691 C  CA   . ASN   B 1 254 ? 2.38538   -4.07246  74.09091  1.000 69.28379  ? 254 ASN   B CA   1 
ATOM   4692 C  C    . ASN   B 1 254 ? 2.97425   -5.16712  73.20455  1.000 62.89211  ? 254 ASN   B C    1 
ATOM   4693 O  O    . ASN   B 1 254 ? 3.72471   -6.01512  73.70093  1.000 57.94703  ? 254 ASN   B O    1 
ATOM   4694 C  CB   . ASN   B 1 254 ? 1.66280   -4.71126  75.27887  1.000 71.78823  ? 254 ASN   B CB   1 
ATOM   4695 C  CG   . ASN   B 1 254 ? 1.37250   -3.71631  76.37668  1.000 81.09233  ? 254 ASN   B CG   1 
ATOM   4696 O  OD1  . ASN   B 1 254 ? 2.28332   -3.33717  77.12231  1.000 79.79857  ? 254 ASN   B OD1  1 
ATOM   4697 N  ND2  . ASN   B 1 254 ? 0.10600   -3.27669  76.48735  1.000 78.07059  ? 254 ASN   B ND2  1 
ATOM   4698 N  N    . SER   B 1 255 ? 2.68219   -5.14500  71.90161  1.000 57.69007  ? 255 SER   B N    1 
ATOM   4699 C  CA   . SER   B 1 255 ? 3.11016   -6.19923  70.99185  1.000 55.61192  ? 255 SER   B CA   1 
ATOM   4700 C  C    . SER   B 1 255 ? 4.45326   -5.90069  70.32139  1.000 52.33490  ? 255 SER   B C    1 
ATOM   4701 O  O    . SER   B 1 255 ? 4.97960   -6.75948  69.59523  1.000 44.77225  ? 255 SER   B O    1 
ATOM   4702 C  CB   . SER   B 1 255 ? 2.02150   -6.44578  69.91727  1.000 60.34523  ? 255 SER   B CB   1 
ATOM   4703 O  OG   . SER   B 1 255 ? 1.94389   -5.36926  68.98273  1.000 69.85636  ? 255 SER   B OG   1 
ATOM   4704 N  N    . ALA   B 1 256 ? 4.99809   -4.69864  70.49920  1.000 45.77714  ? 256 ALA   B N    1 
ATOM   4705 C  CA   . ALA   B 1 256 ? 6.29703   -4.43758  69.89540  1.000 36.30874  ? 256 ALA   B CA   1 
ATOM   4706 C  C    . ALA   B 1 256 ? 6.98106   -3.30168  70.63206  1.000 40.21257  ? 256 ALA   B C    1 
ATOM   4707 O  O    . ALA   B 1 256 ? 6.32695   -2.46797  71.26304  1.000 42.04100  ? 256 ALA   B O    1 
ATOM   4708 C  CB   . ALA   B 1 256 ? 6.17842   -4.12897  68.39476  1.000 38.04924  ? 256 ALA   B CB   1 
ATOM   4709 N  N    . ILE   B 1 257 ? 8.32712   -3.27491  70.54239  1.000 36.60962  ? 257 ILE   B N    1 
ATOM   4710 C  CA   . ILE   B 1 257 ? 9.06078   -2.11220  71.02294  1.000 36.20315  ? 257 ILE   B CA   1 
ATOM   4711 C  C    . ILE   B 1 257 ? 9.05434   -1.10286  69.88714  1.000 34.43641  ? 257 ILE   B C    1 
ATOM   4712 O  O    . ILE   B 1 257 ? 9.46129   -1.43865  68.76072  1.000 34.49464  ? 257 ILE   B O    1 
ATOM   4713 C  CB   . ILE   B 1 257 ? 10.51614  -2.48314  71.41193  1.000 42.15042  ? 257 ILE   B CB   1 
ATOM   4714 C  CG1  . ILE   B 1 257 ? 10.60125  -3.65843  72.40163  1.000 39.74350  ? 257 ILE   B CG1  1 
ATOM   4715 C  CG2  . ILE   B 1 257 ? 11.22234  -1.28470  72.02736  1.000 36.24309  ? 257 ILE   B CG2  1 
ATOM   4716 C  CD1  . ILE   B 1 257 ? 9.86434   -3.47123  73.65996  1.000 42.18566  ? 257 ILE   B CD1  1 
ATOM   4717 N  N    . PHE   B 1 258 ? 8.68352   0.14726   70.19147  1.000 34.22064  ? 258 PHE   B N    1 
ATOM   4718 C  CA   . PHE   B 1 258 ? 8.74003   1.21888   69.21476  1.000 32.99317  ? 258 PHE   B CA   1 
ATOM   4719 C  C    . PHE   B 1 258 ? 9.96123   2.11322   69.42017  1.000 35.79826  ? 258 PHE   B C    1 
ATOM   4720 O  O    . PHE   B 1 258 ? 10.46053  2.26494   70.52812  1.000 34.51671  ? 258 PHE   B O    1 
ATOM   4721 C  CB   . PHE   B 1 258 ? 7.50360   2.08666   69.29444  1.000 39.97122  ? 258 PHE   B CB   1 
ATOM   4722 C  CG   . PHE   B 1 258 ? 6.22382   1.29828   69.11020  1.000 37.63452  ? 258 PHE   B CG   1 
ATOM   4723 C  CD1  . PHE   B 1 258 ? 5.87076   0.85995   67.87291  1.000 39.03331  ? 258 PHE   B CD1  1 
ATOM   4724 C  CD2  . PHE   B 1 258 ? 5.36428   1.07760   70.18707  1.000 50.18811  ? 258 PHE   B CD2  1 
ATOM   4725 C  CE1  . PHE   B 1 258 ? 4.68608   0.13499   67.69012  1.000 42.93962  ? 258 PHE   B CE1  1 
ATOM   4726 C  CE2  . PHE   B 1 258 ? 4.16882   0.38575   70.01179  1.000 52.72761  ? 258 PHE   B CE2  1 
ATOM   4727 C  CZ   . PHE   B 1 258 ? 3.84474   -0.08465  68.77148  1.000 41.86564  ? 258 PHE   B CZ   1 
ATOM   4728 N  N    . MET   B 1 259 ? 10.34785  2.79435   68.34429  1.000 31.95260  ? 259 MET   B N    1 
ATOM   4729 C  CA   . MET   B 1 259 ? 11.59453  3.55432   68.32963  1.000 36.48202  ? 259 MET   B CA   1 
ATOM   4730 C  C    . MET   B 1 259 ? 11.52874  4.76651   69.22709  1.000 38.03784  ? 259 MET   B C    1 
ATOM   4731 O  O    . MET   B 1 259 ? 12.57187  5.23222   69.71010  1.000 40.91878  ? 259 MET   B O    1 
ATOM   4732 C  CB   . MET   B 1 259 ? 11.87402  3.99828   66.91657  1.000 32.03736  ? 259 MET   B CB   1 
ATOM   4733 C  CG   . MET   B 1 259 ? 12.35195  2.92701   65.91107  1.000 32.48865  ? 259 MET   B CG   1 
ATOM   4734 S  SD   . MET   B 1 259 ? 13.92304  2.20873   66.50618  1.000 31.43097  ? 259 MET   B SD   1 
ATOM   4735 C  CE   . MET   B 1 259 ? 15.07191  3.63164   66.33305  1.000 33.15673  ? 259 MET   B CE   1 
ATOM   4736 N  N    . ASP   B 1 260 ? 10.33106  5.25295   69.46720  1.000 37.42319  ? 260 ASP   B N    1 
ATOM   4737 C  CA   . ASP   B 1 260 ? 10.06147  6.37482   70.36429  1.000 47.65284  ? 260 ASP   B CA   1 
ATOM   4738 C  C    . ASP   B 1 260 ? 9.71492   5.96665   71.80702  1.000 43.50891  ? 260 ASP   B C    1 
ATOM   4739 O  O    . ASP   B 1 260 ? 9.40806   6.84320   72.62737  1.000 44.90171  ? 260 ASP   B O    1 
ATOM   4740 C  CB   . ASP   B 1 260 ? 8.89994   7.20133   69.79000  1.000 46.60216  ? 260 ASP   B CB   1 
ATOM   4741 C  CG   . ASP   B 1 260 ? 7.64895   6.34247   69.50052  1.000 45.13356  ? 260 ASP   B CG   1 
ATOM   4742 O  OD1  . ASP   B 1 260 ? 7.54095   5.66028   68.43094  1.000 44.74566  ? 260 ASP   B OD1  1 
ATOM   4743 O  OD2  . ASP   B 1 260 ? 6.80262   6.27382   70.40978  1.000 51.91127  ? 260 ASP   B OD2  1 
ATOM   4744 N  N    . ASP   B 1 261 ? 9.65355   4.66908   72.12606  1.000 40.82075  ? 261 ASP   B N    1 
ATOM   4745 C  CA   . ASP   B 1 261 ? 9.25213   4.24087   73.46655  1.000 41.57173  ? 261 ASP   B CA   1 
ATOM   4746 C  C    . ASP   B 1 261 ? 10.13243  4.83539   74.57356  1.000 40.75065  ? 261 ASP   B C    1 
ATOM   4747 O  O    . ASP   B 1 261 ? 11.34366  4.99400   74.42542  1.000 38.83633  ? 261 ASP   B O    1 
ATOM   4748 C  CB   . ASP   B 1 261 ? 9.26042   2.70712   73.54899  1.000 43.18958  ? 261 ASP   B CB   1 
ATOM   4749 C  CG   . ASP   B 1 261 ? 7.89714   2.10334   73.21076  1.000 43.40643  ? 261 ASP   B CG   1 
ATOM   4750 O  OD1  . ASP   B 1 261 ? 6.90192   2.84505   73.32599  1.000 45.41301  ? 261 ASP   B OD1  1 
ATOM   4751 O  OD2  . ASP   B 1 261 ? 7.80836   0.91224   72.85844  1.000 38.24279  ? 261 ASP   B OD2  1 
ATOM   4752 N  N    . SER   B 1 262 ? 9.51570   5.16517   75.68984  1.000 38.08041  ? 262 SER   B N    1 
ATOM   4753 C  CA   . SER   B 1 262 ? 10.30302  5.63744   76.82998  1.000 42.14281  ? 262 SER   B CA   1 
ATOM   4754 C  C    . SER   B 1 262 ? 11.03926  4.48102   77.51760  1.000 42.75088  ? 262 SER   B C    1 
ATOM   4755 O  O    . SER   B 1 262 ? 10.77475  3.28878   77.28400  1.000 38.95447  ? 262 SER   B O    1 
ATOM   4756 C  CB   . SER   B 1 262 ? 9.38344   6.30489   77.85419  1.000 47.60292  ? 262 SER   B CB   1 
ATOM   4757 O  OG   . SER   B 1 262 ? 8.60536   5.28765   78.46230  1.000 45.52581  ? 262 SER   B OG   1 
ATOM   4758 N  N    . GLU   B 1 263 ? 11.94952  4.83634   78.43940  1.000 40.43566  ? 263 GLU   B N    1 
ATOM   4759 C  CA   . GLU   B 1 263 ? 12.68902  3.78427   79.13181  1.000 42.04056  ? 263 GLU   B CA   1 
ATOM   4760 C  C    . GLU   B 1 263 ? 11.74393  2.86765   79.90502  1.000 41.12908  ? 263 GLU   B C    1 
ATOM   4761 O  O    . GLU   B 1 263 ? 11.90286  1.64367   79.87851  1.000 40.46552  ? 263 GLU   B O    1 
ATOM   4762 C  CB   . GLU   B 1 263 ? 13.74454  4.42083   80.04334  1.000 43.86737  ? 263 GLU   B CB   1 
ATOM   4763 C  CG   . GLU   B 1 263 ? 14.76834  5.19573   79.19961  1.000 45.03422  ? 263 GLU   B CG   1 
ATOM   4764 C  CD   . GLU   B 1 263 ? 16.12040  5.48040   79.91502  1.000 61.67330  ? 263 GLU   B CD   1 
ATOM   4765 O  OE1  . GLU   B 1 263 ? 16.42441  6.67951   80.13576  1.000 62.77933  ? 263 GLU   B OE1  1 
ATOM   4766 O  OE2  . GLU   B 1 263 ? 16.85977  4.52670   80.24346  1.000 57.61918  ? 263 GLU   B OE2  1 
ATOM   4767 N  N    . SER   B 1 264 ? 10.70796  3.42411   80.55104  1.000 42.16636  ? 264 SER   B N    1 
ATOM   4768 C  CA   . SER   B 1 264 ? 9.82015   2.52030   81.29181  1.000 44.27471  ? 264 SER   B CA   1 
ATOM   4769 C  C    . SER   B 1 264 ? 8.97849   1.65031   80.34904  1.000 42.11015  ? 264 SER   B C    1 
ATOM   4770 O  O    . SER   B 1 264 ? 8.70701   0.48194   80.67697  1.000 45.10840  ? 264 SER   B O    1 
ATOM   4771 C  CB   . SER   B 1 264 ? 8.90919   3.30092   82.26496  1.000 50.53623  ? 264 SER   B CB   1 
ATOM   4772 O  OG   . SER   B 1 264 ? 7.90296   3.99195   81.55942  1.000 53.84522  ? 264 SER   B OG   1 
ATOM   4773 N  N    . ASP   B 1 265 ? 8.57674   2.18572   79.18301  1.000 42.63617  ? 265 ASP   B N    1 
ATOM   4774 C  CA   . ASP   B 1 265 ? 7.83536   1.38891   78.19432  1.000 41.32073  ? 265 ASP   B CA   1 
ATOM   4775 C  C    . ASP   B 1 265 ? 8.67460   0.20611   77.70541  1.000 44.81843  ? 265 ASP   B C    1 
ATOM   4776 O  O    . ASP   B 1 265 ? 8.18811   -0.93303  77.61818  1.000 36.68159  ? 265 ASP   B O    1 
ATOM   4777 C  CB   . ASP   B 1 265 ? 7.42469   2.24163   76.98554  1.000 44.03001  ? 265 ASP   B CB   1 
ATOM   4778 C  CG   . ASP   B 1 265 ? 6.21937   3.14591   77.28047  1.000 57.29815  ? 265 ASP   B CG   1 
ATOM   4779 O  OD1  . ASP   B 1 265 ? 6.14629   4.24378   76.68155  1.000 64.21831  ? 265 ASP   B OD1  1 
ATOM   4780 O  OD2  . ASP   B 1 265 ? 5.36933   2.76551   78.11291  1.000 52.47605  ? 265 ASP   B OD2  1 
ATOM   4781 N  N    . VAL   B 1 266 ? 9.93473   0.47415   77.33643  1.000 37.27022  ? 266 VAL   B N    1 
ATOM   4782 C  CA   . VAL   B 1 266 ? 10.84667  -0.60761  76.94843  1.000 38.19381  ? 266 VAL   B CA   1 
ATOM   4783 C  C    . VAL   B 1 266 ? 10.97633  -1.62479  78.08160  1.000 38.93792  ? 266 VAL   B C    1 
ATOM   4784 O  O    . VAL   B 1 266 ? 10.90123  -2.84147  77.86964  1.000 36.51316  ? 266 VAL   B O    1 
ATOM   4785 C  CB   . VAL   B 1 266 ? 12.23597  -0.03696  76.56843  1.000 36.44210  ? 266 VAL   B CB   1 
ATOM   4786 C  CG1  . VAL   B 1 266 ? 13.31174  -1.20333  76.42445  1.000 37.98770  ? 266 VAL   B CG1  1 
ATOM   4787 C  CG2  . VAL   B 1 266 ? 12.16232  0.79809   75.25449  1.000 35.29638  ? 266 VAL   B CG2  1 
ATOM   4788 N  N    . ASN   B 1 267 ? 11.20022  -1.14712  79.30569  1.000 38.29135  ? 267 ASN   B N    1 
ATOM   4789 C  CA   . ASN   B 1 267 ? 11.41917  -2.08470  80.40268  1.000 39.91941  ? 267 ASN   B CA   1 
ATOM   4790 C  C    . ASN   B 1 267 ? 10.21417  -2.99808  80.57612  1.000 39.66148  ? 267 ASN   B C    1 
ATOM   4791 O  O    . ASN   B 1 267 ? 10.35020  -4.22288  80.70928  1.000 38.20825  ? 267 ASN   B O    1 
ATOM   4792 C  CB   . ASN   B 1 267 ? 11.72900  -1.32890  81.69648  1.000 36.75339  ? 267 ASN   B CB   1 
ATOM   4793 C  CG   . ASN   B 1 267 ? 13.11770  -0.73719  81.68064  1.000 42.25967  ? 267 ASN   B CG   1 
ATOM   4794 O  OD1  . ASN   B 1 267 ? 13.94220  -1.12213  80.85832  1.000 38.95811  ? 267 ASN   B OD1  1 
ATOM   4795 N  ND2  . ASN   B 1 267 ? 13.39583  0.18029   82.59429  1.000 44.81287  ? 267 ASN   B ND2  1 
ATOM   4796 N  N    . ARG   B 1 268 ? 9.01784   -2.40758  80.54959  1.000 43.89957  ? 268 ARG   B N    1 
ATOM   4797 C  CA   . ARG   B 1 268 ? 7.78175   -3.15728  80.73479  1.000 42.06087  ? 268 ARG   B CA   1 
ATOM   4798 C  C    . ARG   B 1 268 ? 7.55416   -4.18427  79.61868  1.000 43.32952  ? 268 ARG   B C    1 
ATOM   4799 O  O    . ARG   B 1 268 ? 7.20302   -5.33855  79.89527  1.000 44.04897  ? 268 ARG   B O    1 
ATOM   4800 C  CB   . ARG   B 1 268 ? 6.63493   -2.15657  80.80415  1.000 46.97498  ? 268 ARG   B CB   1 
ATOM   4801 C  CG   . ARG   B 1 268 ? 5.28559   -2.79106  80.74876  1.000 53.70340  ? 268 ARG   B CG   1 
ATOM   4802 C  CD   . ARG   B 1 268 ? 4.16517   -1.73217  80.89592  1.000 52.30209  ? 268 ARG   B CD   1 
ATOM   4803 N  NE   . ARG   B 1 268 ? 4.27120   -0.67828  79.87982  1.000 48.51227  ? 268 ARG   B NE   1 
ATOM   4804 C  CZ   . ARG   B 1 268 ? 3.84398   -0.78382  78.62984  1.000 52.03896  ? 268 ARG   B CZ   1 
ATOM   4805 N  NH1  . ARG   B 1 268 ? 3.37860   -1.92922  78.15375  1.000 64.60495  ? 268 ARG   B NH1  1 
ATOM   4806 N  NH2  . ARG   B 1 268 ? 3.92423   0.27223   77.81668  1.000 52.98575  ? 268 ARG   B NH2  1 
ATOM   4807 N  N    . LYS   B 1 269 ? 7.77636   -3.79218  78.34971  1.000 39.38305  ? 269 LYS   B N    1 
ATOM   4808 C  CA   . LYS   B 1 269 ? 7.51799   -4.70560  77.23088  1.000 38.76728  ? 269 LYS   B CA   1 
ATOM   4809 C  C    . LYS   B 1 269 ? 8.55717   -5.82256  77.16800  1.000 43.08570  ? 269 LYS   B C    1 
ATOM   4810 O  O    . LYS   B 1 269 ? 8.24430   -6.95907  76.76771  1.000 39.35052  ? 269 LYS   B O    1 
ATOM   4811 C  CB   . LYS   B 1 269 ? 7.50036   -3.93822  75.92941  1.000 36.99132  ? 269 LYS   B CB   1 
ATOM   4812 C  CG   . LYS   B 1 269 ? 6.28349   -2.96703  75.85841  1.000 48.01818  ? 269 LYS   B CG   1 
ATOM   4813 C  CD   . LYS   B 1 269 ? 6.45202   -2.07261  74.65062  1.000 43.74440  ? 269 LYS   B CD   1 
ATOM   4814 C  CE   . LYS   B 1 269 ? 5.33172   -1.09029  74.42999  1.000 54.74021  ? 269 LYS   B CE   1 
ATOM   4815 N  NZ   . LYS   B 1 269 ? 5.56212   -0.37421  73.11984  1.000 40.15220  ? 269 LYS   B NZ   1 
ATOM   4816 N  N    . ILE   B 1 270 ? 9.81662   -5.50770  77.48307  1.000 36.54678  ? 270 ILE   B N    1 
ATOM   4817 C  CA   . ILE   B 1 270 ? 10.82093  -6.57573  77.51730  1.000 37.34614  ? 270 ILE   B CA   1 
ATOM   4818 C  C    . ILE   B 1 270 ? 10.49549  -7.55953  78.63464  1.000 40.80436  ? 270 ILE   B C    1 
ATOM   4819 O  O    . ILE   B 1 270 ? 10.55866  -8.77889  78.44518  1.000 40.12642  ? 270 ILE   B O    1 
ATOM   4820 C  CB   . ILE   B 1 270 ? 12.24073  -6.00352  77.71075  1.000 40.44448  ? 270 ILE   B CB   1 
ATOM   4821 C  CG1  . ILE   B 1 270 ? 12.73394  -5.22738  76.48176  1.000 36.10542  ? 270 ILE   B CG1  1 
ATOM   4822 C  CG2  . ILE   B 1 270 ? 13.22172  -7.18563  78.04269  1.000 35.38579  ? 270 ILE   B CG2  1 
ATOM   4823 C  CD1  . ILE   B 1 270 ? 12.74298  -6.03437  75.17356  1.000 38.82338  ? 270 ILE   B CD1  1 
ATOM   4824 N  N    . LYS   B 1 271 ? 10.06890  -7.05190  79.80185  1.000 43.36557  ? 271 LYS   B N    1 
ATOM   4825 C  CA   . LYS   B 1 271 ? 9.81785   -7.95384  80.92822  1.000 50.82391  ? 271 LYS   B CA   1 
ATOM   4826 C  C    . LYS   B 1 271 ? 8.78455   -9.02130  80.57053  1.000 46.72303  ? 271 LYS   B C    1 
ATOM   4827 O  O    . LYS   B 1 271 ? 8.91311   -10.17998 80.99181  1.000 45.00768  ? 271 LYS   B O    1 
ATOM   4828 C  CB   . LYS   B 1 271 ? 9.35700   -7.16550  82.17535  1.000 50.70536  ? 271 LYS   B CB   1 
ATOM   4829 C  CG   . LYS   B 1 271 ? 9.07975   -8.06434  83.42780  1.000 57.14650  ? 271 LYS   B CG   1 
ATOM   4830 C  CD   . LYS   B 1 271 ? 8.31893   -7.35167  84.54622  1.000 64.18264  ? 271 LYS   B CD   1 
ATOM   4831 C  CE   . LYS   B 1 271 ? 7.85327   -8.35425  85.64273  1.000 77.12120  ? 271 LYS   B CE   1 
ATOM   4832 N  NZ   . LYS   B 1 271 ? 6.36685   -8.60787  85.77864  1.000 75.26797  ? 271 LYS   B NZ   1 
ATOM   4833 N  N    . LYS   B 1 272 ? 7.77411   -8.66321  79.78240  1.000 43.00326  ? 272 LYS   B N    1 
ATOM   4834 C  CA   . LYS   B 1 272 ? 6.70006   -9.58958  79.43014  1.000 47.97461  ? 272 LYS   B CA   1 
ATOM   4835 C  C    . LYS   B 1 272 ? 6.92494   -10.34641 78.11698  1.000 44.43414  ? 272 LYS   B C    1 
ATOM   4836 O  O    . LYS   B 1 272 ? 6.05093   -11.12786 77.72673  1.000 43.50743  ? 272 LYS   B O    1 
ATOM   4837 C  CB   . LYS   B 1 272 ? 5.33358   -8.84321  79.32590  1.000 49.35079  ? 272 LYS   B CB   1 
ATOM   4838 C  CG   . LYS   B 1 272 ? 4.80485   -8.29303  80.65693  1.000 68.21439  ? 272 LYS   B CG   1 
ATOM   4839 C  CD   . LYS   B 1 272 ? 3.25329   -8.29882  80.71603  1.000 73.65065  ? 272 LYS   B CD   1 
ATOM   4840 C  CE   . LYS   B 1 272 ? 2.69656   -9.17845  81.86625  1.000 78.28934  ? 272 LYS   B CE   1 
ATOM   4841 N  NZ   . LYS   B 1 272 ? 3.14419   -8.79663  83.25736  1.000 73.09051  ? 272 LYS   B NZ   1 
ATOM   4842 N  N    . ALA   B 1 273 ? 8.04442   -10.12292 77.42021  1.000 37.27683  ? 273 ALA   B N    1 
ATOM   4843 C  CA   . ALA   B 1 273 ? 8.23045   -10.69471 76.09376  1.000 38.50755  ? 273 ALA   B CA   1 
ATOM   4844 C  C    . ALA   B 1 273 ? 8.45815   -12.19994 76.16351  1.000 39.17951  ? 273 ALA   B C    1 
ATOM   4845 O  O    . ALA   B 1 273 ? 8.82464   -12.75981 77.20080  1.000 37.73753  ? 273 ALA   B O    1 
ATOM   4846 C  CB   . ALA   B 1 273 ? 9.44104   -10.05221 75.37423  1.000 34.47902  ? 273 ALA   B CB   1 
ATOM   4847 N  N    . TYR   B 1 274 ? 8.27525   -12.83496 75.01112  1.000 39.32904  ? 274 TYR   B N    1 
ATOM   4848 C  CA   . TYR   B 1 274 ? 8.58332   -14.24955 74.81588  1.000 36.96403  ? 274 TYR   B CA   1 
ATOM   4849 C  C    . TYR   B 1 274 ? 10.09742  -14.43915 74.84090  1.000 33.23902  ? 274 TYR   B C    1 
ATOM   4850 O  O    . TYR   B 1 274 ? 10.81657  -13.66927 74.21527  1.000 33.98712  ? 274 TYR   B O    1 
ATOM   4851 C  CB   . TYR   B 1 274 ? 8.03112   -14.68661 73.45378  1.000 39.69217  ? 274 TYR   B CB   1 
ATOM   4852 C  CG   . TYR   B 1 274 ? 8.14061   -16.15777 73.13455  1.000 37.96968  ? 274 TYR   B CG   1 
ATOM   4853 C  CD1  . TYR   B 1 274 ? 7.68424   -17.12758 74.01850  1.000 39.25406  ? 274 TYR   B CD1  1 
ATOM   4854 C  CD2  . TYR   B 1 274 ? 8.74539   -16.57233 71.95680  1.000 38.76935  ? 274 TYR   B CD2  1 
ATOM   4855 C  CE1  . TYR   B 1 274 ? 7.79600   -18.47476 73.71831  1.000 39.95463  ? 274 TYR   B CE1  1 
ATOM   4856 C  CE2  . TYR   B 1 274 ? 8.88916   -17.93004 71.64496  1.000 38.23623  ? 274 TYR   B CE2  1 
ATOM   4857 C  CZ   . TYR   B 1 274 ? 8.38807   -18.87516 72.51175  1.000 40.61456  ? 274 TYR   B CZ   1 
ATOM   4858 O  OH   . TYR   B 1 274 ? 8.52571   -20.22699 72.20007  1.000 40.99138  ? 274 TYR   B OH   1 
ATOM   4859 N  N    . CYS   B 1 275 ? 10.58434  -15.36069 75.66274  1.000 34.39807  ? 275 CYS   B N    1 
ATOM   4860 C  CA   . CYS   B 1 275 ? 12.02730  -15.64665 75.74635  1.000 32.28025  ? 275 CYS   B CA   1 
ATOM   4861 C  C    . CYS   B 1 275 ? 12.16593  -17.08050 76.23639  1.000 35.88957  ? 275 CYS   B C    1 
ATOM   4862 O  O    . CYS   B 1 275 ? 12.46078  -17.32549 77.40790  1.000 36.33533  ? 275 CYS   B O    1 
ATOM   4863 C  CB   . CYS   B 1 275 ? 12.70678  -14.66911 76.68452  1.000 32.58110  ? 275 CYS   B CB   1 
ATOM   4864 S  SG   . CYS   B 1 275 ? 14.55902  -14.81951 76.67232  1.000 34.90705  ? 275 CYS   B SG   1 
ATOM   4865 N  N    . PRO   B 1 276 ? 11.88064  -18.04974 75.38301  1.000 33.43751  ? 276 PRO   B N    1 
ATOM   4866 C  CA   . PRO   B 1 276 ? 11.86924  -19.44972 75.82587  1.000 35.65194  ? 276 PRO   B CA   1 
ATOM   4867 C  C    . PRO   B 1 276 ? 13.23194  -19.87333 76.34652  1.000 34.62592  ? 276 PRO   B C    1 
ATOM   4868 O  O    . PRO   B 1 276 ? 14.23765  -19.60148 75.67948  1.000 35.54993  ? 276 PRO   B O    1 
ATOM   4869 C  CB   . PRO   B 1 276 ? 11.50456  -20.21208 74.54602  1.000 33.91109  ? 276 PRO   B CB   1 
ATOM   4870 C  CG   . PRO   B 1 276 ? 11.88966  -19.28098 73.41738  1.000 36.58291  ? 276 PRO   B CG   1 
ATOM   4871 C  CD   . PRO   B 1 276 ? 11.56836  -17.92212 73.95257  1.000 33.54633  ? 276 PRO   B CD   1 
ATOM   4872 N  N    . PRO   B 1 277 ? 13.30300  -20.52860 77.51573  1.000 35.65794  ? 277 PRO   B N    1 
ATOM   4873 C  CA   . PRO   B 1 277 ? 14.59951  -21.03399 78.02173  1.000 32.63316  ? 277 PRO   B CA   1 
ATOM   4874 C  C    . PRO   B 1 277 ? 15.21807  -21.97867 77.00384  1.000 35.93380  ? 277 PRO   B C    1 
ATOM   4875 O  O    . PRO   B 1 277 ? 14.52566  -22.77518 76.34320  1.000 34.40613  ? 277 PRO   B O    1 
ATOM   4876 C  CB   . PRO   B 1 277 ? 14.23367  -21.78688 79.29813  1.000 36.66924  ? 277 PRO   B CB   1 
ATOM   4877 C  CG   . PRO   B 1 277 ? 12.79688  -21.32321 79.64866  1.000 42.79178  ? 277 PRO   B CG   1 
ATOM   4878 C  CD   . PRO   B 1 277 ? 12.16929  -20.85978 78.41321  1.000 38.65060  ? 277 PRO   B CD   1 
ATOM   4879 N  N    . ASN   B 1 278 ? 16.51258  -21.80503 76.79976  1.000 31.10512  ? 278 ASN   B N    1 
ATOM   4880 C  CA   . ASN   B 1 278 ? 17.35211  -22.68227 75.99247  1.000 35.61649  ? 278 ASN   B CA   1 
ATOM   4881 C  C    . ASN   B 1 278 ? 17.05489  -22.64513 74.49121  1.000 36.22583  ? 278 ASN   B C    1 
ATOM   4882 O  O    . ASN   B 1 278 ? 17.77419  -23.31077 73.73321  1.000 37.35866  ? 278 ASN   B O    1 
ATOM   4883 C  CB   . ASN   B 1 278 ? 17.22255  -24.14376 76.43269  1.000 34.91376  ? 278 ASN   B CB   1 
ATOM   4884 C  CG   . ASN   B 1 278 ? 17.43922  -24.31870 77.92467  1.000 41.66189  ? 278 ASN   B CG   1 
ATOM   4885 O  OD1  . ASN   B 1 278 ? 16.48920  -24.32415 78.69458  1.000 44.78405  ? 278 ASN   B OD1  1 
ATOM   4886 N  ND2  . ASN   B 1 278 ? 18.67226  -24.43735 78.33364  1.000 37.57965  ? 278 ASN   B ND2  1 
ATOM   4887 N  N    . VAL   B 1 279 ? 16.13819  -21.80799 74.02676  1.000 30.64218  ? 279 VAL   B N    1 
ATOM   4888 C  CA   . VAL   B 1 279 ? 15.66523  -21.81414 72.64260  1.000 31.22241  ? 279 VAL   B CA   1 
ATOM   4889 C  C    . VAL   B 1 279 ? 15.95300  -20.47303 71.98722  1.000 34.85034  ? 279 VAL   B C    1 
ATOM   4890 O  O    . VAL   B 1 279 ? 15.53981  -19.41014 72.48449  1.000 33.29054  ? 279 VAL   B O    1 
ATOM   4891 C  CB   . VAL   B 1 279 ? 14.16666  -22.17703 72.56938  1.000 31.84193  ? 279 VAL   B CB   1 
ATOM   4892 C  CG1  . VAL   B 1 279 ? 13.58769  -22.03966 71.10494  1.000 36.01919  ? 279 VAL   B CG1  1 
ATOM   4893 C  CG2  . VAL   B 1 279 ? 14.00484  -23.63790 73.01530  1.000 35.18611  ? 279 VAL   B CG2  1 
ATOM   4894 N  N    . ILE   B 1 280 ? 16.66435  -20.53460 70.85903  1.000 30.49846  ? 280 ILE   B N    1 
ATOM   4895 C  CA   . ILE   B 1 280 ? 16.94878  -19.34712 70.08661  1.000 31.25370  ? 280 ILE   B CA   1 
ATOM   4896 C  C    . ILE   B 1 280 ? 15.90326  -19.13120 68.99534  1.000 32.97903  ? 280 ILE   B C    1 
ATOM   4897 O  O    . ILE   B 1 280 ? 15.57047  -17.98579 68.66624  1.000 33.13445  ? 280 ILE   B O    1 
ATOM   4898 C  CB   . ILE   B 1 280 ? 18.38385  -19.46692 69.51429  1.000 31.82922  ? 280 ILE   B CB   1 
ATOM   4899 C  CG1  . ILE   B 1 280 ? 19.36224  -19.13200 70.63373  1.000 36.99101  ? 280 ILE   B CG1  1 
ATOM   4900 C  CG2  . ILE   B 1 280 ? 18.54322  -18.57132 68.31754  1.000 33.83113  ? 280 ILE   B CG2  1 
ATOM   4901 C  CD1  . ILE   B 1 280 ? 20.85466  -19.32181 70.24527  1.000 42.04789  ? 280 ILE   B CD1  1 
ATOM   4902 N  N    . GLU   B 1 281 ? 15.38489  -20.20312 68.41792  1.000 33.06574  ? 281 GLU   B N    1 
ATOM   4903 C  CA   . GLU   B 1 281 ? 14.46093  -20.08207 67.28358  1.000 36.68905  ? 281 GLU   B CA   1 
ATOM   4904 C  C    . GLU   B 1 281 ? 13.21778  -19.31943 67.74631  1.000 37.21945  ? 281 GLU   B C    1 
ATOM   4905 O  O    . GLU   B 1 281 ? 12.65672  -19.64714 68.78733  1.000 33.35252  ? 281 GLU   B O    1 
ATOM   4906 C  CB   . GLU   B 1 281 ? 14.08769  -21.50657 66.83015  1.000 40.39846  ? 281 GLU   B CB   1 
ATOM   4907 C  CG   . GLU   B 1 281 ? 13.16057  -21.70569 65.63065  1.000 60.33345  ? 281 GLU   B CG   1 
ATOM   4908 C  CD   . GLU   B 1 281 ? 13.77861  -21.31682 64.29603  1.000 72.71429  ? 281 GLU   B CD   1 
ATOM   4909 O  OE1  . GLU   B 1 281 ? 14.99764  -21.01072 64.26465  1.000 75.72548  ? 281 GLU   B OE1  1 
ATOM   4910 O  OE2  . GLU   B 1 281 ? 13.03853  -21.34273 63.28077  1.000 77.25045  ? 281 GLU   B OE2  1 
ATOM   4911 N  N    . ASN   B 1 282 ? 12.81956  -18.26980 67.01044  1.000 33.84886  ? 282 ASN   B N    1 
ATOM   4912 C  CA   . ASN   B 1 282 ? 11.61144  -17.48273 67.30158  1.000 33.19184  ? 282 ASN   B CA   1 
ATOM   4913 C  C    . ASN   B 1 282 ? 11.70840  -16.67615 68.60472  1.000 33.82195  ? 282 ASN   B C    1 
ATOM   4914 O  O    . ASN   B 1 282 ? 10.67809  -16.19448 69.12475  1.000 32.52240  ? 282 ASN   B O    1 
ATOM   4915 C  CB   . ASN   B 1 282 ? 10.37582  -18.40189 67.38026  1.000 37.40689  ? 282 ASN   B CB   1 
ATOM   4916 C  CG   . ASN   B 1 282 ? 9.12071   -17.68020 67.03368  1.000 48.74316  ? 282 ASN   B CG   1 
ATOM   4917 O  OD1  . ASN   B 1 282 ? 9.13990   -16.82237 66.14898  1.000 51.71522  ? 282 ASN   B OD1  1 
ATOM   4918 N  ND2  . ASN   B 1 282 ? 8.00086   -18.00879 67.72142  1.000 51.91074  ? 282 ASN   B ND2  1 
ATOM   4919 N  N    . ASN   B 1 283 ? 12.90914  -16.56104 69.20271  1.000 30.75790  ? 283 ASN   B N    1 
ATOM   4920 C  CA   . ASN   B 1 283 ? 13.10670  -15.85585 70.47167  1.000 29.77798  ? 283 ASN   B CA   1 
ATOM   4921 C  C    . ASN   B 1 283 ? 13.44415  -14.37393 70.22514  1.000 30.90889  ? 283 ASN   B C    1 
ATOM   4922 O  O    . ASN   B 1 283 ? 14.56011  -14.08688 69.74453  1.000 27.59510  ? 283 ASN   B O    1 
ATOM   4923 C  CB   . ASN   B 1 283 ? 14.21893  -16.54538 71.27102  1.000 30.44749  ? 283 ASN   B CB   1 
ATOM   4924 C  CG   . ASN   B 1 283 ? 14.45168  -15.92786 72.63626  1.000 30.96296  ? 283 ASN   B CG   1 
ATOM   4925 O  OD1  . ASN   B 1 283 ? 14.18148  -14.74397 72.86361  1.000 30.68757  ? 283 ASN   B OD1  1 
ATOM   4926 N  ND2  . ASN   B 1 283 ? 15.02909  -16.73122 73.55317  1.000 30.15043  ? 283 ASN   B ND2  1 
ATOM   4927 N  N    . PRO   B 1 284 ? 12.53587  -13.43876 70.46296  1.000 31.98669  ? 284 PRO   B N    1 
ATOM   4928 C  CA   . PRO   B 1 284 ? 12.84454  -12.02926 70.11298  1.000 30.52970  ? 284 PRO   B CA   1 
ATOM   4929 C  C    . PRO   B 1 284 ? 13.91356  -11.38774 70.96965  1.000 30.91677  ? 284 PRO   B C    1 
ATOM   4930 O  O    . PRO   B 1 284 ? 14.72751  -10.59858 70.45299  1.000 32.75040  ? 284 PRO   B O    1 
ATOM   4931 C  CB   . PRO   B 1 284 ? 11.48612  -11.32402 70.34200  1.000 29.02076  ? 284 PRO   B CB   1 
ATOM   4932 C  CG   . PRO   B 1 284 ? 10.82601  -12.18789 71.40276  1.000 34.46901  ? 284 PRO   B CG   1 
ATOM   4933 C  CD   . PRO   B 1 284 ? 11.20827  -13.58724 71.10100  1.000 32.09128  ? 284 PRO   B CD   1 
ATOM   4934 N  N    . ILE   B 1 285 ? 13.93955  -11.71908 72.26815  1.000 28.87868  ? 285 ILE   B N    1 
ATOM   4935 C  CA   . ILE   B 1 285 ? 14.96499  -11.18066 73.17267  1.000 28.66253  ? 285 ILE   B CA   1 
ATOM   4936 C  C    . ILE   B 1 285 ? 16.34213  -11.58731 72.68684  1.000 28.72004  ? 285 ILE   B C    1 
ATOM   4937 O  O    . ILE   B 1 285 ? 17.28818  -10.77514 72.62677  1.000 29.74705  ? 285 ILE   B O    1 
ATOM   4938 C  CB   . ILE   B 1 285 ? 14.71605  -11.67452 74.61448  1.000 28.19421  ? 285 ILE   B CB   1 
ATOM   4939 C  CG1  . ILE   B 1 285 ? 13.32413  -11.21936 75.09977  1.000 31.16220  ? 285 ILE   B CG1  1 
ATOM   4940 C  CG2  . ILE   B 1 285 ? 15.80565  -11.12125 75.59376  1.000 28.52067  ? 285 ILE   B CG2  1 
ATOM   4941 C  CD1  . ILE   B 1 285 ? 13.02663  -9.69039  74.78382  1.000 33.10501  ? 285 ILE   B CD1  1 
ATOM   4942 N  N    . TYR   B 1 286 ? 16.50715  -12.87900 72.42554  1.000 27.97363  ? 286 TYR   B N    1 
ATOM   4943 C  CA   . TYR   B 1 286 ? 17.80718  -13.31820 71.93392  1.000 30.99555  ? 286 TYR   B CA   1 
ATOM   4944 C  C    . TYR   B 1 286 ? 18.11977  -12.65026 70.58607  1.000 30.84747  ? 286 TYR   B C    1 
ATOM   4945 O  O    . TYR   B 1 286 ? 19.25965  -12.24904 70.32473  1.000 29.54890  ? 286 TYR   B O    1 
ATOM   4946 C  CB   . TYR   B 1 286 ? 17.83530  -14.85028 71.83128  1.000 27.40648  ? 286 TYR   B CB   1 
ATOM   4947 C  CG   . TYR   B 1 286 ? 19.21233  -15.31314 71.44342  1.000 30.35367  ? 286 TYR   B CG   1 
ATOM   4948 C  CD1  . TYR   B 1 286 ? 19.63361  -15.37010 70.08927  1.000 31.51415  ? 286 TYR   B CD1  1 
ATOM   4949 C  CD2  . TYR   B 1 286 ? 20.12069  -15.62076 72.44551  1.000 32.59030  ? 286 TYR   B CD2  1 
ATOM   4950 C  CE1  . TYR   B 1 286 ? 21.00263  -15.75956 69.77919  1.000 36.09694  ? 286 TYR   B CE1  1 
ATOM   4951 C  CE2  . TYR   B 1 286 ? 21.45110  -15.99945 72.14566  1.000 33.33015  ? 286 TYR   B CE2  1 
ATOM   4952 C  CZ   . TYR   B 1 286 ? 21.85146  -16.08175 70.80910  1.000 39.01203  ? 286 TYR   B CZ   1 
ATOM   4953 O  OH   . TYR   B 1 286 ? 23.16797  -16.46356 70.58829  1.000 46.92175  ? 286 TYR   B OH   1 
ATOM   4954 N  N    . ALA   B 1 287 ? 17.11205  -12.49795 69.70902  1.000 27.75082  ? 287 ALA   B N    1 
ATOM   4955 C  CA   . ALA   B 1 287 ? 17.33740  -11.85392 68.41586  1.000 26.24705  ? 287 ALA   B CA   1 
ATOM   4956 C  C    . ALA   B 1 287 ? 17.83341  -10.42181 68.59101  1.000 29.22789  ? 287 ALA   B C    1 
ATOM   4957 O  O    . ALA   B 1 287 ? 18.70149  -9.97202  67.84096  1.000 31.64908  ? 287 ALA   B O    1 
ATOM   4958 C  CB   . ALA   B 1 287 ? 16.02150  -11.85825 67.55425  1.000 28.30696  ? 287 ALA   B CB   1 
ATOM   4959 N  N    . TYR   B 1 288 ? 17.28401  -9.68574  69.56694  1.000 28.94591  ? 288 TYR   B N    1 
ATOM   4960 C  CA   . TYR   B 1 288 ? 17.75857  -8.31922  69.82581  1.000 29.82988  ? 288 TYR   B CA   1 
ATOM   4961 C  C    . TYR   B 1 288 ? 19.22501  -8.35379  70.26871  1.000 28.23281  ? 288 TYR   B C    1 
ATOM   4962 O  O    . TYR   B 1 288 ? 20.03891  -7.50275  69.87006  1.000 28.92716  ? 288 TYR   B O    1 
ATOM   4963 C  CB   . TYR   B 1 288 ? 16.95509  -7.67235  70.95210  1.000 26.57554  ? 288 TYR   B CB   1 
ATOM   4964 C  CG   . TYR   B 1 288 ? 15.48636  -7.44616  70.60042  1.000 29.58030  ? 288 TYR   B CG   1 
ATOM   4965 C  CD1  . TYR   B 1 288 ? 15.04179  -7.57721  69.30086  1.000 28.76712  ? 288 TYR   B CD1  1 
ATOM   4966 C  CD2  . TYR   B 1 288 ? 14.57739  -7.22393  71.61576  1.000 31.62381  ? 288 TYR   B CD2  1 
ATOM   4967 C  CE1  . TYR   B 1 288 ? 13.65841  -7.43714  68.99335  1.000 29.23443  ? 288 TYR   B CE1  1 
ATOM   4968 C  CE2  . TYR   B 1 288 ? 13.20109  -7.05385  71.34553  1.000 30.33214  ? 288 TYR   B CE2  1 
ATOM   4969 C  CZ   . TYR   B 1 288 ? 12.77579  -7.16877  70.02645  1.000 33.34081  ? 288 TYR   B CZ   1 
ATOM   4970 O  OH   . TYR   B 1 288 ? 11.40061  -7.07463  69.81610  1.000 36.96624  ? 288 TYR   B OH   1 
ATOM   4971 N  N    . ALA   B 1 289 ? 19.55523  -9.27687  71.16659  1.000 29.63363  ? 289 ALA   B N    1 
ATOM   4972 C  CA   . ALA   B 1 289 ? 20.96849  -9.38347  71.59415  1.000 29.14387  ? 289 ALA   B CA   1 
ATOM   4973 C  C    . ALA   B 1 289 ? 21.87858  -9.66135  70.39124  1.000 33.87075  ? 289 ALA   B C    1 
ATOM   4974 O  O    . ALA   B 1 289 ? 22.93440  -9.04553  70.21899  1.000 31.42160  ? 289 ALA   B O    1 
ATOM   4975 C  CB   . ALA   B 1 289 ? 21.11281  -10.48396 72.65257  1.000 28.16159  ? 289 ALA   B CB   1 
ATOM   4976 N  N    . LYS   B 1 290 ? 21.49764  -10.62129 69.55491  1.000 29.15420  ? 290 LYS   B N    1 
ATOM   4977 C  CA   . LYS   B 1 290 ? 22.40620  -11.09719 68.52107  1.000 29.25004  ? 290 LYS   B CA   1 
ATOM   4978 C  C    . LYS   B 1 290 ? 22.47705  -10.14633 67.33644  1.000 32.45266  ? 290 LYS   B C    1 
ATOM   4979 O  O    . LYS   B 1 290 ? 23.55655  -9.95632  66.77952  1.000 30.14575  ? 290 LYS   B O    1 
ATOM   4980 C  CB   . LYS   B 1 290 ? 22.00210  -12.49253 68.02773  1.000 32.77391  ? 290 LYS   B CB   1 
ATOM   4981 C  CG   . LYS   B 1 290 ? 22.38006  -12.73499 66.56915  1.000 40.28817  ? 290 LYS   B CG   1 
ATOM   4982 C  CD   . LYS   B 1 290 ? 21.84305  -14.05633 66.05669  1.000 37.53876  ? 290 LYS   B CD   1 
ATOM   4983 C  CE   . LYS   B 1 290 ? 22.84742  -14.78058 65.13239  1.000 45.73620  ? 290 LYS   B CE   1 
ATOM   4984 N  NZ   . LYS   B 1 290 ? 22.21261  -16.02330 64.61722  1.000 57.03267  ? 290 LYS   B NZ   1 
ATOM   4985 N  N    . SER   B 1 291 ? 21.33768  -9.56826  66.91505  1.000 30.01140  ? 291 SER   B N    1 
ATOM   4986 C  CA   . SER   B 1 291 ? 21.27152  -8.82583  65.66923  1.000 26.90150  ? 291 SER   B CA   1 
ATOM   4987 C  C    . SER   B 1 291 ? 21.30401  -7.31639  65.81719  1.000 30.11671  ? 291 SER   B C    1 
ATOM   4988 O  O    . SER   B 1 291 ? 21.51612  -6.63383  64.80533  1.000 31.52607  ? 291 SER   B O    1 
ATOM   4989 C  CB   . SER   B 1 291 ? 19.98616  -9.20019  64.89038  1.000 30.00853  ? 291 SER   B CB   1 
ATOM   4990 O  OG   . SER   B 1 291 ? 20.05698  -10.59694 64.61453  1.000 32.93822  ? 291 SER   B OG   1 
ATOM   4991 N  N    . ILE   B 1 292 ? 20.97076  -6.77600  66.98992  1.000 30.15254  ? 292 ILE   B N    1 
ATOM   4992 C  CA   . ILE   B 1 292 ? 21.01756  -5.33599  67.22635  1.000 28.12625  ? 292 ILE   B CA   1 
ATOM   4993 C  C    . ILE   B 1 292 ? 22.16361  -4.96248  68.16865  1.000 32.62439  ? 292 ILE   B C    1 
ATOM   4994 O  O    . ILE   B 1 292 ? 22.99389  -4.11957  67.83945  1.000 32.70961  ? 292 ILE   B O    1 
ATOM   4995 C  CB   . ILE   B 1 292 ? 19.68134  -4.82115  67.76868  1.000 30.63983  ? 292 ILE   B CB   1 
ATOM   4996 C  CG1  . ILE   B 1 292 ? 18.58777  -4.94061  66.63776  1.000 26.78414  ? 292 ILE   B CG1  1 
ATOM   4997 C  CG2  . ILE   B 1 292 ? 19.88214  -3.39314  68.21202  1.000 30.29691  ? 292 ILE   B CG2  1 
ATOM   4998 C  CD1  . ILE   B 1 292 ? 17.17299  -4.65012  67.19488  1.000 30.11203  ? 292 ILE   B CD1  1 
ATOM   4999 N  N    . ILE   B 1 293 ? 22.22024  -5.58903  69.34003  1.000 27.66222  ? 293 ILE   B N    1 
ATOM   5000 C  CA   . ILE   B 1 293 ? 23.12012  -5.12428  70.40840  1.000 30.00961  ? 293 ILE   B CA   1 
ATOM   5001 C  C    . ILE   B 1 293 ? 24.56118  -5.57237  70.14079  1.000 30.12440  ? 293 ILE   B C    1 
ATOM   5002 O  O    . ILE   B 1 293 ? 25.49241  -4.76221  70.13657  1.000 31.08369  ? 293 ILE   B O    1 
ATOM   5003 C  CB   . ILE   B 1 293 ? 22.59399  -5.62176  71.75878  1.000 30.62875  ? 293 ILE   B CB   1 
ATOM   5004 C  CG1  . ILE   B 1 293 ? 21.22154  -4.99750  72.02502  1.000 25.60011  ? 293 ILE   B CG1  1 
ATOM   5005 C  CG2  . ILE   B 1 293 ? 23.57155  -5.22715  72.94115  1.000 30.83894  ? 293 ILE   B CG2  1 
ATOM   5006 C  CD1  . ILE   B 1 293 ? 20.45667  -5.69568  73.14978  1.000 27.23464  ? 293 ILE   B CD1  1 
ATOM   5007 N  N    . PHE   B 1 294 ? 24.76495  -6.85495  69.85811  1.000 27.44764  ? 294 PHE   B N    1 
ATOM   5008 C  CA   . PHE   B 1 294 ? 26.13430  -7.32058  69.64873  1.000 28.68724  ? 294 PHE   B CA   1 
ATOM   5009 C  C    . PHE   B 1 294 ? 26.86456  -6.59881  68.53628  1.000 32.16763  ? 294 PHE   B C    1 
ATOM   5010 O  O    . PHE   B 1 294 ? 28.04100  -6.24057  68.73078  1.000 35.31253  ? 294 PHE   B O    1 
ATOM   5011 C  CB   . PHE   B 1 294 ? 26.13276  -8.82211  69.37692  1.000 27.39830  ? 294 PHE   B CB   1 
ATOM   5012 C  CG   . PHE   B 1 294 ? 27.51008  -9.38886  69.33378  1.000 34.97806  ? 294 PHE   B CG   1 
ATOM   5013 C  CD1  . PHE   B 1 294 ? 28.17237  -9.71843  70.52142  1.000 32.85711  ? 294 PHE   B CD1  1 
ATOM   5014 C  CD2  . PHE   B 1 294 ? 28.16960  -9.49097  68.11025  1.000 37.08561  ? 294 PHE   B CD2  1 
ATOM   5015 C  CE1  . PHE   B 1 294 ? 29.56554  -10.23304 70.49141  1.000 33.04686  ? 294 PHE   B CE1  1 
ATOM   5016 C  CE2  . PHE   B 1 294 ? 29.45690  -10.01057 68.01476  1.000 32.68458  ? 294 PHE   B CE2  1 
ATOM   5017 C  CZ   . PHE   B 1 294 ? 30.18362  -10.37584 69.22000  1.000 32.98400  ? 294 PHE   B CZ   1 
ATOM   5018 N  N    . PRO   B 1 295 ? 26.29170  -6.41020  67.34563  1.000 33.24613  ? 295 PRO   B N    1 
ATOM   5019 C  CA   . PRO   B 1 295 ? 26.99439  -5.64806  66.31459  1.000 30.90559  ? 295 PRO   B CA   1 
ATOM   5020 C  C    . PRO   B 1 295 ? 27.19824  -4.19649  66.68430  1.000 29.92505  ? 295 PRO   B C    1 
ATOM   5021 O  O    . PRO   B 1 295 ? 28.20209  -3.60040  66.28113  1.000 33.08377  ? 295 PRO   B O    1 
ATOM   5022 C  CB   . PRO   B 1 295 ? 26.05432  -5.72681  65.10018  1.000 34.95679  ? 295 PRO   B CB   1 
ATOM   5023 C  CG   . PRO   B 1 295 ? 24.94158  -6.66403  65.49849  1.000 32.61119  ? 295 PRO   B CG   1 
ATOM   5024 C  CD   . PRO   B 1 295 ? 24.94513  -6.84828  66.94385  1.000 30.89468  ? 295 PRO   B CD   1 
ATOM   5025 N  N    . SER   B 1 296 ? 26.29575  -3.60837  67.45814  1.000 28.09023  ? 296 SER   B N    1 
ATOM   5026 C  CA   . SER   B 1 296 ? 26.45710  -2.20308  67.86666  1.000 31.05348  ? 296 SER   B CA   1 
ATOM   5027 C  C    . SER   B 1 296 ? 27.61621  -2.00017  68.83601  1.000 37.06130  ? 296 SER   B C    1 
ATOM   5028 O  O    . SER   B 1 296 ? 28.30039  -0.97345  68.77634  1.000 34.69791  ? 296 SER   B O    1 
ATOM   5029 C  CB   . SER   B 1 296 ? 25.15981  -1.73165  68.53781  1.000 30.72390  ? 296 SER   B CB   1 
ATOM   5030 O  OG   . SER   B 1 296 ? 24.16330  -1.75293  67.51992  1.000 36.10691  ? 296 SER   B OG   1 
ATOM   5031 N  N    . TYR   B 1 297 ? 27.89068  -2.96682  69.69811  1.000 30.63020  ? 297 TYR   B N    1 
ATOM   5032 C  CA   . TYR   B 1 297 ? 28.94383  -2.78492  70.69426  1.000 31.10308  ? 297 TYR   B CA   1 
ATOM   5033 C  C    . TYR   B 1 297 ? 30.15070  -3.68600  70.46762  1.000 32.83112  ? 297 TYR   B C    1 
ATOM   5034 O  O    . TYR   B 1 297 ? 31.12798  -3.59386  71.24070  1.000 31.82038  ? 297 TYR   B O    1 
ATOM   5035 C  CB   . TYR   B 1 297 ? 28.36735  -3.04883  72.06939  1.000 33.80812  ? 297 TYR   B CB   1 
ATOM   5036 C  CG   . TYR   B 1 297 ? 27.35150  -2.02365  72.48947  1.000 34.18667  ? 297 TYR   B CG   1 
ATOM   5037 C  CD1  . TYR   B 1 297 ? 27.75096  -0.83625  73.07891  1.000 34.33750  ? 297 TYR   B CD1  1 
ATOM   5038 C  CD2  . TYR   B 1 297 ? 25.98107  -2.22872  72.26860  1.000 38.30865  ? 297 TYR   B CD2  1 
ATOM   5039 C  CE1  . TYR   B 1 297 ? 26.82751  0.10412   73.45633  1.000 37.86130  ? 297 TYR   B CE1  1 
ATOM   5040 C  CE2  . TYR   B 1 297 ? 25.06374  -1.28519  72.63560  1.000 36.26080  ? 297 TYR   B CE2  1 
ATOM   5041 C  CZ   . TYR   B 1 297 ? 25.50687  -0.13248  73.26919  1.000 35.32974  ? 297 TYR   B CZ   1 
ATOM   5042 O  OH   . TYR   B 1 297 ? 24.59143  0.81219   73.65199  1.000 39.27117  ? 297 TYR   B OH   1 
ATOM   5043 N  N    . ASN   B 1 298 ? 30.11967  -4.52766  69.44132  1.000 29.29910  ? 298 ASN   B N    1 
ATOM   5044 C  CA   . ASN   B 1 298 ? 31.12558  -5.57039  69.21813  1.000 33.73555  ? 298 ASN   B CA   1 
ATOM   5045 C  C    . ASN   B 1 298 ? 31.33370  -6.43872  70.46397  1.000 36.67679  ? 298 ASN   B C    1 
ATOM   5046 O  O    . ASN   B 1 298 ? 32.39395  -7.07858  70.66461  1.000 32.18843  ? 298 ASN   B O    1 
ATOM   5047 C  CB   . ASN   B 1 298 ? 32.43736  -4.95349  68.71008  1.000 34.53775  ? 298 ASN   B CB   1 
ATOM   5048 C  CG   . ASN   B 1 298 ? 32.25720  -4.40630  67.30053  1.000 43.24500  ? 298 ASN   B CG   1 
ATOM   5049 O  OD1  . ASN   B 1 298 ? 32.14246  -5.18804  66.34792  1.000 50.86475  ? 298 ASN   B OD1  1 
ATOM   5050 N  ND2  . ASN   B 1 298 ? 32.01926  -3.08545  67.19113  1.000 38.48773  ? 298 ASN   B ND2  1 
ATOM   5051 N  N    . GLU   B 1 299 ? 30.32759  -6.47179  71.33017  1.000 30.94276  ? 299 GLU   B N    1 
ATOM   5052 C  CA   . GLU   B 1 299 ? 30.39278  -7.34260  72.49893  1.000 32.78004  ? 299 GLU   B CA   1 
ATOM   5053 C  C    . GLU   B 1 299 ? 28.96982  -7.40494  73.03546  1.000 31.60811  ? 299 GLU   B C    1 
ATOM   5054 O  O    . GLU   B 1 299 ? 28.09011  -6.68243  72.57572  1.000 33.72455  ? 299 GLU   B O    1 
ATOM   5055 C  CB   . GLU   B 1 299 ? 31.36761  -6.83548  73.57120  1.000 33.05666  ? 299 GLU   B CB   1 
ATOM   5056 C  CG   . GLU   B 1 299 ? 30.90516  -5.50348  74.19479  1.000 34.12339  ? 299 GLU   B CG   1 
ATOM   5057 C  CD   . GLU   B 1 299 ? 31.85357  -5.01939  75.29974  1.000 43.53596  ? 299 GLU   B CD   1 
ATOM   5058 O  OE1  . GLU   B 1 299 ? 33.06996  -5.25587  75.19413  1.000 39.18311  ? 299 GLU   B OE1  1 
ATOM   5059 O  OE2  . GLU   B 1 299 ? 31.38970  -4.44970  76.29655  1.000 44.56429  ? 299 GLU   B OE2  1 
ATOM   5060 N  N    . PHE   B 1 300 ? 28.75900  -8.27759  73.99169  1.000 29.55873  ? 300 PHE   B N    1 
ATOM   5061 C  CA   . PHE   B 1 300 ? 27.53716  -8.20546  74.79589  1.000 30.95671  ? 300 PHE   B CA   1 
ATOM   5062 C  C    . PHE   B 1 300 ? 27.91311  -8.37029  76.25570  1.000 30.34058  ? 300 PHE   B C    1 
ATOM   5063 O  O    . PHE   B 1 300 ? 28.42314  -9.42398  76.64972  1.000 31.66776  ? 300 PHE   B O    1 
ATOM   5064 C  CB   . PHE   B 1 300 ? 26.55316  -9.26474  74.34528  1.000 27.27798  ? 300 PHE   B CB   1 
ATOM   5065 C  CG   . PHE   B 1 300 ? 25.20522  -9.12761  75.00960  1.000 30.51294  ? 300 PHE   B CG   1 
ATOM   5066 C  CD1  . PHE   B 1 300 ? 25.03544  -9.53258  76.32857  1.000 32.05179  ? 300 PHE   B CD1  1 
ATOM   5067 C  CD2  . PHE   B 1 300 ? 24.12958  -8.55307  74.30381  1.000 27.46596  ? 300 PHE   B CD2  1 
ATOM   5068 C  CE1  . PHE   B 1 300 ? 23.74907  -9.40534  76.98547  1.000 32.30186  ? 300 PHE   B CE1  1 
ATOM   5069 C  CE2  . PHE   B 1 300 ? 22.85390  -8.40377  74.95456  1.000 32.15286  ? 300 PHE   B CE2  1 
ATOM   5070 C  CZ   . PHE   B 1 300 ? 22.68603  -8.83983  76.29860  1.000 29.83702  ? 300 PHE   B CZ   1 
ATOM   5071 N  N    . ASN   B 1 301 ? 27.70367  -7.33803  77.05646  1.000 27.51759  ? 301 ASN   B N    1 
ATOM   5072 C  CA   . ASN   B 1 301 ? 28.02593  -7.41023  78.48286  1.000 31.59153  ? 301 ASN   B CA   1 
ATOM   5073 C  C    . ASN   B 1 301 ? 26.78935  -7.84564  79.28329  1.000 32.04974  ? 301 ASN   B C    1 
ATOM   5074 O  O    . ASN   B 1 301 ? 25.80276  -7.10911  79.34337  1.000 35.34687  ? 301 ASN   B O    1 
ATOM   5075 C  CB   . ASN   B 1 301 ? 28.50284  -6.05345  78.97730  1.000 34.10816  ? 301 ASN   B CB   1 
ATOM   5076 C  CG   . ASN   B 1 301 ? 29.11011  -6.13113  80.36386  1.000 43.70627  ? 301 ASN   B CG   1 
ATOM   5077 O  OD1  . ASN   B 1 301 ? 29.86417  -7.06391  80.67018  1.000 41.27114  ? 301 ASN   B OD1  1 
ATOM   5078 N  ND2  . ASN   B 1 301 ? 28.79703  -5.16466  81.20279  1.000 37.87427  ? 301 ASN   B ND2  1 
ATOM   5079 N  N    . LEU   B 1 302 ? 26.80931  -9.05648  79.81169  1.000 28.42644  ? 302 LEU   B N    1 
ATOM   5080 C  CA   . LEU   B 1 302 ? 25.70717  -9.59623  80.62063  1.000 33.70346  ? 302 LEU   B CA   1 
ATOM   5081 C  C    . LEU   B 1 302 ? 25.96068  -9.30280  82.09744  1.000 33.24268  ? 302 LEU   B C    1 
ATOM   5082 O  O    . LEU   B 1 302 ? 26.76618  -9.98736  82.74948  1.000 36.34134  ? 302 LEU   B O    1 
ATOM   5083 C  CB   . LEU   B 1 302 ? 25.59395  -11.09485 80.37998  1.000 31.02744  ? 302 LEU   B CB   1 
ATOM   5084 C  CG   . LEU   B 1 302 ? 24.41180  -11.88877 80.92945  1.000 32.82451  ? 302 LEU   B CG   1 
ATOM   5085 C  CD1  . LEU   B 1 302 ? 23.14615  -11.57773 80.12988  1.000 34.87308  ? 302 LEU   B CD1  1 
ATOM   5086 C  CD2  . LEU   B 1 302 ? 24.72314  -13.38215 80.85326  1.000 33.32212  ? 302 LEU   B CD2  1 
ATOM   5087 N  N    . VAL   B 1 303 ? 25.25121  -8.32257  82.66360  1.000 31.53706  ? 303 VAL   B N    1 
ATOM   5088 C  CA   . VAL   B 1 303 ? 25.37634  -8.03391  84.10082  1.000 34.09009  ? 303 VAL   B CA   1 
ATOM   5089 C  C    . VAL   B 1 303 ? 24.44683  -8.95868  84.87073  1.000 36.96419  ? 303 VAL   B C    1 
ATOM   5090 O  O    . VAL   B 1 303 ? 23.28058  -9.08042  84.51250  1.000 33.52933  ? 303 VAL   B O    1 
ATOM   5091 C  CB   . VAL   B 1 303 ? 25.04927  -6.56024  84.38375  1.000 36.76370  ? 303 VAL   B CB   1 
ATOM   5092 C  CG1  . VAL   B 1 303 ? 24.97453  -6.27781  85.89759  1.000 41.04118  ? 303 VAL   B CG1  1 
ATOM   5093 C  CG2  . VAL   B 1 303 ? 26.03610  -5.61864  83.63292  1.000 40.37560  ? 303 VAL   B CG2  1 
ATOM   5094 N  N    . ARG   B 1 304 ? 24.96678  -9.63437  85.90325  1.000 33.90663  ? 304 ARG   B N    1 
ATOM   5095 C  CA   . ARG   B 1 304 ? 24.22289  -10.62356 86.70256  1.000 34.64791  ? 304 ARG   B CA   1 
ATOM   5096 C  C    . ARG   B 1 304 ? 24.79461  -10.68714 88.10463  1.000 38.79102  ? 304 ARG   B C    1 
ATOM   5097 O  O    . ARG   B 1 304 ? 25.99864  -10.50456 88.29402  1.000 32.18760  ? 304 ARG   B O    1 
ATOM   5098 C  CB   . ARG   B 1 304 ? 24.33574  -12.05977 86.18909  1.000 29.70011  ? 304 ARG   B CB   1 
ATOM   5099 C  CG   . ARG   B 1 304 ? 23.78512  -12.31789 84.81114  1.000 40.75057  ? 304 ARG   B CG   1 
ATOM   5100 C  CD   . ARG   B 1 304 ? 23.95612  -13.82016 84.51466  1.000 39.17302  ? 304 ARG   B CD   1 
ATOM   5101 N  NE   . ARG   B 1 304 ? 25.37209  -14.19846 84.32536  1.000 36.71957  ? 304 ARG   B NE   1 
ATOM   5102 C  CZ   . ARG   B 1 304 ? 25.76586  -15.32190 83.73755  1.000 32.90262  ? 304 ARG   B CZ   1 
ATOM   5103 N  NH1  . ARG   B 1 304 ? 24.89545  -16.20920 83.29145  1.000 31.77714  ? 304 ARG   B NH1  1 
ATOM   5104 N  NH2  . ARG   B 1 304 ? 27.08828  -15.58534 83.63001  1.000 34.79746  ? 304 ARG   B NH2  1 
ATOM   5105 N  N    . LYS   B 1 305 ? 23.96529  -11.09468 89.06344  1.000 36.59522  ? 305 LYS   B N    1 
ATOM   5106 C  CA   . LYS   B 1 305 ? 24.50792  -11.41322 90.37916  1.000 36.02152  ? 305 LYS   B CA   1 
ATOM   5107 C  C    . LYS   B 1 305 ? 25.46083  -12.60370 90.31722  1.000 37.16614  ? 305 LYS   B C    1 
ATOM   5108 O  O    . LYS   B 1 305 ? 25.31994  -13.50679 89.49582  1.000 34.69244  ? 305 LYS   B O    1 
ATOM   5109 C  CB   . LYS   B 1 305 ? 23.37810  -11.68214 91.37811  1.000 40.82262  ? 305 LYS   B CB   1 
ATOM   5110 C  CG   . LYS   B 1 305 ? 22.41147  -10.51144 91.46844  1.000 42.91663  ? 305 LYS   B CG   1 
ATOM   5111 C  CD   . LYS   B 1 305 ? 21.47405  -10.70115 92.65546  1.000 55.72030  ? 305 LYS   B CD   1 
ATOM   5112 C  CE   . LYS   B 1 305 ? 20.12484  -11.19571 92.20697  1.000 63.40323  ? 305 LYS   B CE   1 
ATOM   5113 N  NZ   . LYS   B 1 305 ? 19.03194  -10.69460 93.11514  1.000 63.37368  ? 305 LYS   B NZ   1 
ATOM   5114 N  N    . GLU   B 1 306 ? 26.44300  -12.62241 91.23450  1.000 36.69451  ? 306 GLU   B N    1 
ATOM   5115 C  CA   . GLU   B 1 306 ? 27.38783  -13.73193 91.24964  1.000 37.39676  ? 306 GLU   B CA   1 
ATOM   5116 C  C    . GLU   B 1 306 ? 26.68959  -15.06958 91.38536  1.000 39.80880  ? 306 GLU   B C    1 
ATOM   5117 O  O    . GLU   B 1 306 ? 27.12137  -16.06257 90.78231  1.000 37.83572  ? 306 GLU   B O    1 
ATOM   5118 C  CB   . GLU   B 1 306 ? 28.37890  -13.62025 92.44621  1.000 42.26774  ? 306 GLU   B CB   1 
ATOM   5119 C  CG   . GLU   B 1 306 ? 29.49536  -12.68670 92.24528  1.000 48.07775  ? 306 GLU   B CG   1 
ATOM   5120 C  CD   . GLU   B 1 306 ? 30.66538  -13.00056 93.20889  1.000 56.82304  ? 306 GLU   B CD   1 
ATOM   5121 O  OE1  . GLU   B 1 306 ? 31.81314  -13.11225 92.70875  1.000 61.14329  ? 306 GLU   B OE1  1 
ATOM   5122 O  OE2  . GLU   B 1 306 ? 30.42278  -13.22488 94.42227  1.000 54.78639  ? 306 GLU   B OE2  1 
ATOM   5123 N  N    . LYS   B 1 307 ? 25.60684  -15.13283 92.17004  1.000 38.70100  ? 307 LYS   B N    1 
ATOM   5124 C  CA   . LYS   B 1 307 ? 25.00836  -16.44830 92.36931  1.000 42.77395  ? 307 LYS   B CA   1 
ATOM   5125 C  C    . LYS   B 1 307 ? 24.32179  -16.95686 91.10415  1.000 39.21681  ? 307 LYS   B C    1 
ATOM   5126 O  O    . LYS   B 1 307 ? 24.07911  -18.16210 90.98953  1.000 38.28842  ? 307 LYS   B O    1 
ATOM   5127 C  CB   . LYS   B 1 307 ? 23.97150  -16.45336 93.48810  1.000 45.81012  ? 307 LYS   B CB   1 
ATOM   5128 C  CG   . LYS   B 1 307 ? 22.74141  -15.60858 93.15703  1.000 51.75724  ? 307 LYS   B CG   1 
ATOM   5129 C  CD   . LYS   B 1 307 ? 21.62468  -15.86055 94.16660  1.000 52.96652  ? 307 LYS   B CD   1 
ATOM   5130 C  CE   . LYS   B 1 307 ? 20.70565  -14.64206 94.28622  1.000 66.26528  ? 307 LYS   B CE   1 
ATOM   5131 N  NZ   . LYS   B 1 307 ? 21.34198  -13.62633 95.17845  1.000 74.93430  ? 307 LYS   B NZ   1 
ATOM   5132 N  N    . ASN   B 1 308 ? 24.02926  -16.06828 90.15267  1.000 37.56421  ? 308 ASN   B N    1 
ATOM   5133 C  CA   . ASN   B 1 308 ? 23.45429  -16.43499 88.86581  1.000 35.98051  ? 308 ASN   B CA   1 
ATOM   5134 C  C    . ASN   B 1 308 ? 24.51431  -16.57891 87.77399  1.000 41.25232  ? 308 ASN   B C    1 
ATOM   5135 O  O    . ASN   B 1 308 ? 24.17156  -16.66194 86.59078  1.000 37.64281  ? 308 ASN   B O    1 
ATOM   5136 C  CB   . ASN   B 1 308 ? 22.42860  -15.38807 88.46782  1.000 38.26265  ? 308 ASN   B CB   1 
ATOM   5137 C  CG   . ASN   B 1 308 ? 21.23748  -15.41042 89.39528  1.000 44.61016  ? 308 ASN   B CG   1 
ATOM   5138 O  OD1  . ASN   B 1 308 ? 20.92666  -16.44943 89.93986  1.000 42.10995  ? 308 ASN   B OD1  1 
ATOM   5139 N  ND2  . ASN   B 1 308 ? 20.61812  -14.26644 89.62347  1.000 43.68301  ? 308 ASN   B ND2  1 
ATOM   5140 N  N    . GLY   B 1 309 ? 25.79733  -16.59797 88.14511  1.000 40.45229  ? 309 GLY   B N    1 
ATOM   5141 C  CA   . GLY   B 1 309 ? 26.85999  -16.70635 87.18060  1.000 38.20454  ? 309 GLY   B CA   1 
ATOM   5142 C  C    . GLY   B 1 309 ? 27.75845  -15.48420 87.09630  1.000 39.84870  ? 309 GLY   B C    1 
ATOM   5143 O  O    . GLY   B 1 309 ? 28.81321  -15.56107 86.44265  1.000 35.24900  ? 309 GLY   B O    1 
ATOM   5144 N  N    . GLY   B 1 310 ? 27.33017  -14.35141 87.64840  1.000 31.03389  ? 310 GLY   B N    1 
ATOM   5145 C  CA   . GLY   B 1 310 ? 28.08700  -13.11029 87.60805  1.000 34.47023  ? 310 GLY   B CA   1 
ATOM   5146 C  C    . GLY   B 1 310 ? 28.20780  -12.42793 86.25419  1.000 32.58655  ? 310 GLY   B C    1 
ATOM   5147 O  O    . GLY   B 1 310 ? 27.87713  -13.00729 85.22029  1.000 32.56946  ? 310 GLY   B O    1 
ATOM   5148 N  N    . ASP   B 1 311 ? 28.63652  -11.16168 86.25442  1.000 30.06562  ? 311 ASP   B N    1 
ATOM   5149 C  CA   . ASP   B 1 311 ? 28.81354  -10.44411 85.00506  1.000 34.55699  ? 311 ASP   B CA   1 
ATOM   5150 C  C    . ASP   B 1 311 ? 29.69457  -11.24014 84.06056  1.000 31.26628  ? 311 ASP   B C    1 
ATOM   5151 O  O    . ASP   B 1 311 ? 30.65358  -11.90097 84.48067  1.000 31.11750  ? 311 ASP   B O    1 
ATOM   5152 C  CB   . ASP   B 1 311 ? 29.49797  -9.09480  85.23111  1.000 34.95168  ? 311 ASP   B CB   1 
ATOM   5153 C  CG   . ASP   B 1 311 ? 28.72363  -8.17249  86.13365  1.000 44.13345  ? 311 ASP   B CG   1 
ATOM   5154 O  OD1  . ASP   B 1 311 ? 27.60438  -8.55582  86.59914  1.000 37.97721  ? 311 ASP   B OD1  1 
ATOM   5155 O  OD2  . ASP   B 1 311 ? 29.30496  -7.09049  86.44383  1.000 39.13127  ? 311 ASP   B OD2  1 
ATOM   5156 N  N    . LYS   B 1 312 ? 29.40816  -11.13346 82.77245  1.000 30.46217  ? 312 LYS   B N    1 
ATOM   5157 C  CA   . LYS   B 1 312 ? 30.28256  -11.78848 81.80318  1.000 33.61696  ? 312 LYS   B CA   1 
ATOM   5158 C  C    . LYS   B 1 312 ? 30.22395  -11.00168 80.50117  1.000 33.77718  ? 312 LYS   B C    1 
ATOM   5159 O  O    . LYS   B 1 312 ? 29.13855  -10.65068 80.03476  1.000 30.94627  ? 312 LYS   B O    1 
ATOM   5160 C  CB   . LYS   B 1 312 ? 29.88941  -13.27172 81.55333  1.000 32.59154  ? 312 LYS   B CB   1 
ATOM   5161 C  CG   . LYS   B 1 312 ? 30.66926  -13.99163 80.44466  1.000 32.38981  ? 312 LYS   B CG   1 
ATOM   5162 C  CD   . LYS   B 1 312 ? 30.16156  -15.50021 80.25759  1.000 30.60548  ? 312 LYS   B CD   1 
ATOM   5163 C  CE   . LYS   B 1 312 ? 30.84121  -16.19450 79.06052  1.000 32.31170  ? 312 LYS   B CE   1 
ATOM   5164 N  NZ   . LYS   B 1 312 ? 32.37442  -16.38026 79.34110  1.000 32.62712  ? 312 LYS   B NZ   1 
ATOM   5165 N  N    . THR   B 1 313 ? 31.38280  -10.79596 79.88292  1.000 31.10665  ? 313 THR   B N    1 
ATOM   5166 C  CA   . THR   B 1 313 ? 31.45718  -10.10436 78.60445  1.000 29.89281  ? 313 THR   B CA   1 
ATOM   5167 C  C    . THR   B 1 313 ? 31.64753  -11.14901 77.53165  1.000 32.89403  ? 313 THR   B C    1 
ATOM   5168 O  O    . THR   B 1 313 ? 32.63304  -11.90904 77.56831  1.000 32.29287  ? 313 THR   B O    1 
ATOM   5169 C  CB   . THR   B 1 313 ? 32.61903  -9.11029  78.60372  1.000 34.78009  ? 313 THR   B CB   1 
ATOM   5170 O  OG1  . THR   B 1 313 ? 32.43986  -8.20923  79.69587  1.000 33.75147  ? 313 THR   B OG1  1 
ATOM   5171 C  CG2  . THR   B 1 313 ? 32.61474  -8.30055  77.28347  1.000 38.92143  ? 313 THR   B CG2  1 
ATOM   5172 N  N    . TYR   B 1 314 ? 30.71351  -11.17099 76.55690  1.000 28.79520  ? 314 TYR   B N    1 
ATOM   5173 C  CA   . TYR   B 1 314 ? 30.77156  -12.05498 75.40653  1.000 30.69370  ? 314 TYR   B CA   1 
ATOM   5174 C  C    . TYR   B 1 314 ? 31.43505  -11.32974 74.24450  1.000 33.59076  ? 314 TYR   B C    1 
ATOM   5175 O  O    . TYR   B 1 314 ? 30.99762  -10.24096 73.86334  1.000 31.95071  ? 314 TYR   B O    1 
ATOM   5176 C  CB   . TYR   B 1 314 ? 29.35591  -12.49732 74.98299  1.000 30.26856  ? 314 TYR   B CB   1 
ATOM   5177 C  CG   . TYR   B 1 314 ? 28.72960  -13.41287 75.97470  1.000 27.76891  ? 314 TYR   B CG   1 
ATOM   5178 C  CD1  . TYR   B 1 314 ? 28.09321  -12.91755 77.13743  1.000 28.76485  ? 314 TYR   B CD1  1 
ATOM   5179 C  CD2  . TYR   B 1 314 ? 28.83103  -14.79476 75.78593  1.000 26.92445  ? 314 TYR   B CD2  1 
ATOM   5180 C  CE1  . TYR   B 1 314 ? 27.57892  -13.80659 78.07714  1.000 28.22857  ? 314 TYR   B CE1  1 
ATOM   5181 C  CE2  . TYR   B 1 314 ? 28.30730  -15.66319 76.69276  1.000 27.26505  ? 314 TYR   B CE2  1 
ATOM   5182 C  CZ   . TYR   B 1 314 ? 27.68529  -15.17493 77.83431  1.000 28.03072  ? 314 TYR   B CZ   1 
ATOM   5183 O  OH   . TYR   B 1 314 ? 27.22856  -16.09669 78.75071  1.000 29.57211  ? 314 TYR   B OH   1 
ATOM   5184 N  N    . TYR   B 1 315 ? 32.49471  -11.92330 73.69944  1.000 31.91543  ? 315 TYR   B N    1 
ATOM   5185 C  CA   . TYR   B 1 315 ? 33.09162  -11.36574 72.49787  1.000 31.42676  ? 315 TYR   B CA   1 
ATOM   5186 C  C    . TYR   B 1 315 ? 32.69919  -12.10871 71.21836  1.000 35.30133  ? 315 TYR   B C    1 
ATOM   5187 O  O    . TYR   B 1 315 ? 33.10709  -11.66949 70.13736  1.000 33.51781  ? 315 TYR   B O    1 
ATOM   5188 C  CB   . TYR   B 1 315 ? 34.61500  -11.35524 72.61312  1.000 31.94889  ? 315 TYR   B CB   1 
ATOM   5189 C  CG   . TYR   B 1 315 ? 35.03457  -10.46586 73.69739  1.000 34.25685  ? 315 TYR   B CG   1 
ATOM   5190 C  CD1  . TYR   B 1 315 ? 34.74724  -9.11189  73.64255  1.000 36.53111  ? 315 TYR   B CD1  1 
ATOM   5191 C  CD2  . TYR   B 1 315 ? 35.73689  -10.95801 74.79549  1.000 37.54578  ? 315 TYR   B CD2  1 
ATOM   5192 C  CE1  . TYR   B 1 315 ? 35.15388  -8.26252  74.68221  1.000 38.53578  ? 315 TYR   B CE1  1 
ATOM   5193 C  CE2  . TYR   B 1 315 ? 36.14217  -10.12313 75.82691  1.000 36.78569  ? 315 TYR   B CE2  1 
ATOM   5194 C  CZ   . TYR   B 1 315 ? 35.85461  -8.77799  75.76088  1.000 43.63668  ? 315 TYR   B CZ   1 
ATOM   5195 O  OH   . TYR   B 1 315 ? 36.24867  -7.92736  76.77715  1.000 40.01997  ? 315 TYR   B OH   1 
ATOM   5196 N  N    . THR   B 1 316 ? 31.97024  -13.23578 71.29056  1.000 29.50630  ? 316 THR   B N    1 
ATOM   5197 C  CA   . THR   B 1 316 ? 31.53867  -13.90484 70.06533  1.000 27.44734  ? 316 THR   B CA   1 
ATOM   5198 C  C    . THR   B 1 316 ? 30.07123  -14.30533 70.21468  1.000 33.10748  ? 316 THR   B C    1 
ATOM   5199 O  O    . THR   B 1 316 ? 29.61166  -14.66588 71.31508  1.000 32.20976  ? 316 THR   B O    1 
ATOM   5200 C  CB   . THR   B 1 316 ? 32.32419  -15.16798 69.76926  1.000 34.34101  ? 316 THR   B CB   1 
ATOM   5201 O  OG1  . THR   B 1 316 ? 32.07601  -16.11412 70.80673  1.000 33.52565  ? 316 THR   B OG1  1 
ATOM   5202 C  CG2  . THR   B 1 316 ? 33.89369  -14.86031 69.78453  1.000 34.60608  ? 316 THR   B CG2  1 
ATOM   5203 N  N    . LEU   B 1 317 ? 29.36807  -14.26534 69.08314  1.000 28.56870  ? 317 LEU   B N    1 
ATOM   5204 C  CA   . LEU   B 1 317 ? 28.02258  -14.81571 69.04754  1.000 29.64345  ? 317 LEU   B CA   1 
ATOM   5205 C  C    . LEU   B 1 317 ? 28.03802  -16.31258 69.28526  1.000 27.89864  ? 317 LEU   B C    1 
ATOM   5206 O  O    . LEU   B 1 317 ? 27.05979  -16.85495 69.82234  1.000 29.81744  ? 317 LEU   B O    1 
ATOM   5207 C  CB   . LEU   B 1 317 ? 27.39003  -14.48761 67.68626  1.000 31.03565  ? 317 LEU   B CB   1 
ATOM   5208 C  CG   . LEU   B 1 317 ? 27.04922  -12.99698 67.63558  1.000 35.57390  ? 317 LEU   B CG   1 
ATOM   5209 C  CD1  . LEU   B 1 317 ? 26.38122  -12.63674 66.24367  1.000 41.19937  ? 317 LEU   B CD1  1 
ATOM   5210 C  CD2  . LEU   B 1 317 ? 26.07085  -12.71254 68.75926  1.000 35.79844  ? 317 LEU   B CD2  1 
ATOM   5211 N  N    . GLN   B 1 318 ? 29.13069  -16.99216 68.90263  1.000 27.03376  ? 318 GLN   B N    1 
ATOM   5212 C  CA   . GLN   B 1 318 ? 29.21515  -18.43141 69.13377  1.000 27.89515  ? 318 GLN   B CA   1 
ATOM   5213 C  C    . GLN   B 1 318 ? 29.10428  -18.76184 70.63469  1.000 30.05743  ? 318 GLN   B C    1 
ATOM   5214 O  O    . GLN   B 1 318 ? 28.34376  -19.65730 71.04179  1.000 30.84109  ? 318 GLN   B O    1 
ATOM   5215 C  CB   . GLN   B 1 318 ? 30.51948  -18.98242 68.56903  1.000 32.81918  ? 318 GLN   B CB   1 
ATOM   5216 C  CG   . GLN   B 1 318 ? 30.56202  -20.53017 68.62714  1.000 39.02930  ? 318 GLN   B CG   1 
ATOM   5217 C  CD   . GLN   B 1 318 ? 31.05352  -21.07796 69.95702  1.000 45.44537  ? 318 GLN   B CD   1 
ATOM   5218 O  OE1  . GLN   B 1 318 ? 31.85698  -20.43384 70.69420  1.000 42.29987  ? 318 GLN   B OE1  1 
ATOM   5219 N  NE2  . GLN   B 1 318 ? 30.56406  -22.27903 70.30172  1.000 45.59423  ? 318 GLN   B NE2  1 
ATOM   5220 N  N    . GLU   B 1 319 ? 29.83104  -18.03875 71.46404  1.000 30.07641  ? 319 GLU   B N    1 
ATOM   5221 C  CA   . GLU   B 1 319 ? 29.73911  -18.27538 72.90452  1.000 30.32614  ? 319 GLU   B CA   1 
ATOM   5222 C  C    . GLU   B 1 319 ? 28.35691  -17.89160 73.44279  1.000 32.72403  ? 319 GLU   B C    1 
ATOM   5223 O  O    . GLU   B 1 319 ? 27.80176  -18.58352 74.31669  1.000 28.60000  ? 319 GLU   B O    1 
ATOM   5224 C  CB   . GLU   B 1 319 ? 30.82046  -17.49704 73.67684  1.000 28.09740  ? 319 GLU   B CB   1 
ATOM   5225 C  CG   . GLU   B 1 319 ? 30.86498  -18.12520 75.08794  1.000 30.00185  ? 319 GLU   B CG   1 
ATOM   5226 C  CD   . GLU   B 1 319 ? 31.87218  -17.47736 76.01267  1.000 36.94066  ? 319 GLU   B CD   1 
ATOM   5227 O  OE1  . GLU   B 1 319 ? 32.29835  -16.34342 75.69001  1.000 39.49678  ? 319 GLU   B OE1  1 
ATOM   5228 O  OE2  . GLU   B 1 319 ? 32.25419  -18.12708 77.04253  1.000 30.76393  ? 319 GLU   B OE2  1 
ATOM   5229 N  N    . LEU   B 1 320 ? 27.81868  -16.75360 72.99239  1.000 28.55535  ? 320 LEU   B N    1 
ATOM   5230 C  CA   . LEU   B 1 320 ? 26.49754  -16.35097 73.48984  1.000 27.77583  ? 320 LEU   B CA   1 
ATOM   5231 C  C    . LEU   B 1 320 ? 25.46013  -17.42834 73.19161  1.000 29.26291  ? 320 LEU   B C    1 
ATOM   5232 O  O    . LEU   B 1 320 ? 24.60464  -17.73291 74.03196  1.000 31.01895  ? 320 LEU   B O    1 
ATOM   5233 C  CB   . LEU   B 1 320 ? 26.07251  -15.03788 72.86393  1.000 29.77889  ? 320 LEU   B CB   1 
ATOM   5234 C  CG   . LEU   B 1 320 ? 24.75820  -14.46115 73.43908  1.000 31.86129  ? 320 LEU   B CG   1 
ATOM   5235 C  CD1  . LEU   B 1 320 ? 25.01348  -13.95462 74.80931  1.000 30.08888  ? 320 LEU   B CD1  1 
ATOM   5236 C  CD2  . LEU   B 1 320 ? 24.34156  -13.29502 72.58816  1.000 35.52801  ? 320 LEU   B CD2  1 
ATOM   5237 N  N    . GLU   B 1 321 ? 25.51202  -17.99450 71.98624  1.000 29.56296  ? 321 GLU   B N    1 
ATOM   5238 C  CA   . GLU   B 1 321 ? 24.54790  -19.02514 71.58780  1.000 30.77555  ? 321 GLU   B CA   1 
ATOM   5239 C  C    . GLU   B 1 321 ? 24.75995  -20.29780 72.37317  1.000 30.91841  ? 321 GLU   B C    1 
ATOM   5240 O  O    . GLU   B 1 321 ? 23.82085  -20.87970 72.90856  1.000 28.19778  ? 321 GLU   B O    1 
ATOM   5241 C  CB   . GLU   B 1 321 ? 24.65518  -19.30512 70.07812  1.000 34.07754  ? 321 GLU   B CB   1 
ATOM   5242 C  CG   . GLU   B 1 321 ? 23.89651  -20.60565 69.70371  1.000 39.55792  ? 321 GLU   B CG   1 
ATOM   5243 C  CD   . GLU   B 1 321 ? 23.89467  -20.89668 68.19870  1.000 52.15704  ? 321 GLU   B CD   1 
ATOM   5244 O  OE1  . GLU   B 1 321 ? 23.84704  -19.90119 67.43082  1.000 46.01183  ? 321 GLU   B OE1  1 
ATOM   5245 O  OE2  . GLU   B 1 321 ? 23.92640  -22.09925 67.81194  1.000 54.54571  ? 321 GLU   B OE2  1 
ATOM   5246 N  N    . HIS   B 1 322 ? 26.01201  -20.74547 72.48586  1.000 29.62712  ? 322 HIS   B N    1 
ATOM   5247 C  CA   . HIS   B 1 322 ? 26.28764  -21.91024 73.32530  1.000 31.17882  ? 322 HIS   B CA   1 
ATOM   5248 C  C    . HIS   B 1 322 ? 25.73727  -21.70372 74.74327  1.000 33.52978  ? 322 HIS   B C    1 
ATOM   5249 O  O    . HIS   B 1 322 ? 25.08530  -22.58442 75.30568  1.000 30.91656  ? 322 HIS   B O    1 
ATOM   5250 C  CB   . HIS   B 1 322 ? 27.80917  -22.15203 73.40986  1.000 32.52424  ? 322 HIS   B CB   1 
ATOM   5251 C  CG   . HIS   B 1 322 ? 28.20204  -23.09306 74.51275  1.000 34.44994  ? 322 HIS   B CG   1 
ATOM   5252 N  ND1  . HIS   B 1 322 ? 28.40801  -22.67466 75.80708  1.000 34.94975  ? 322 HIS   B ND1  1 
ATOM   5253 C  CD2  . HIS   B 1 322 ? 28.39042  -24.43867 74.51527  1.000 35.39648  ? 322 HIS   B CD2  1 
ATOM   5254 C  CE1  . HIS   B 1 322 ? 28.76499  -23.71308 76.55366  1.000 33.72772  ? 322 HIS   B CE1  1 
ATOM   5255 N  NE2  . HIS   B 1 322 ? 28.73874  -24.79594 75.79176  1.000 35.19079  ? 322 HIS   B NE2  1 
ATOM   5256 N  N    . ASP   B 1 323 ? 26.00097  -20.54253 75.32898  1.000 27.38289  ? 323 ASP   B N    1 
ATOM   5257 C  CA   . ASP   B 1 323 ? 25.62236  -20.32702 76.71996  1.000 31.51045  ? 323 ASP   B CA   1 
ATOM   5258 C  C    . ASP   B 1 323 ? 24.11003  -20.23445 76.87231  1.000 29.98251  ? 323 ASP   B C    1 
ATOM   5259 O  O    . ASP   B 1 323 ? 23.56662  -20.71144 77.87397  1.000 32.64261  ? 323 ASP   B O    1 
ATOM   5260 C  CB   . ASP   B 1 323 ? 26.25604  -19.07382 77.25793  1.000 30.09613  ? 323 ASP   B CB   1 
ATOM   5261 C  CG   . ASP   B 1 323 ? 27.74213  -19.28307 77.62680  1.000 32.80581  ? 323 ASP   B CG   1 
ATOM   5262 O  OD1  . ASP   B 1 323 ? 28.33629  -20.33931 77.25033  1.000 30.68538  ? 323 ASP   B OD1  1 
ATOM   5263 O  OD2  . ASP   B 1 323 ? 28.27252  -18.35428 78.25555  1.000 34.10099  ? 323 ASP   B OD2  1 
ATOM   5264 N  N    . TYR   B 1 324 ? 23.40951  -19.64754 75.89298  1.000 28.50595  ? 324 TYR   B N    1 
ATOM   5265 C  CA   . TYR   B 1 324 ? 21.95509  -19.57602 76.04069  1.000 29.65656  ? 324 TYR   B CA   1 
ATOM   5266 C  C    . TYR   B 1 324 ? 21.33474  -20.95314 75.82627  1.000 31.48681  ? 324 TYR   B C    1 
ATOM   5267 O  O    . TYR   B 1 324 ? 20.48669  -21.41694 76.62227  1.000 29.56356  ? 324 TYR   B O    1 
ATOM   5268 C  CB   . TYR   B 1 324 ? 21.37529  -18.53674 75.08404  1.000 29.62921  ? 324 TYR   B CB   1 
ATOM   5269 C  CG   . TYR   B 1 324 ? 19.95726  -18.26852 75.40446  1.000 31.41863  ? 324 TYR   B CG   1 
ATOM   5270 C  CD1  . TYR   B 1 324 ? 19.60993  -17.47910 76.52494  1.000 28.07874  ? 324 TYR   B CD1  1 
ATOM   5271 C  CD2  . TYR   B 1 324 ? 18.94322  -18.88704 74.66872  1.000 30.51667  ? 324 TYR   B CD2  1 
ATOM   5272 C  CE1  . TYR   B 1 324 ? 18.23416  -17.25973 76.87454  1.000 30.80608  ? 324 TYR   B CE1  1 
ATOM   5273 C  CE2  . TYR   B 1 324 ? 17.56957  -18.70502 75.05287  1.000 32.99135  ? 324 TYR   B CE2  1 
ATOM   5274 C  CZ   . TYR   B 1 324 ? 17.25112  -17.88927 76.12979  1.000 31.88753  ? 324 TYR   B CZ   1 
ATOM   5275 O  OH   . TYR   B 1 324 ? 15.92253  -17.71425 76.45193  1.000 33.90566  ? 324 TYR   B OH   1 
ATOM   5276 N  N    . VAL   B 1 325 ? 21.82632  -21.68494 74.83189  1.000 29.93805  ? 325 VAL   B N    1 
ATOM   5277 C  CA   . VAL   B 1 325 ? 21.20497  -22.97541 74.52789  1.000 33.20368  ? 325 VAL   B CA   1 
ATOM   5278 C  C    . VAL   B 1 325 ? 21.46383  -23.96865 75.64582  1.000 35.77142  ? 325 VAL   B C    1 
ATOM   5279 O  O    . VAL   B 1 325 ? 20.61040  -24.80871 75.95832  1.000 34.32015  ? 325 VAL   B O    1 
ATOM   5280 C  CB   . VAL   B 1 325 ? 21.71781  -23.49770 73.16165  1.000 38.44235  ? 325 VAL   B CB   1 
ATOM   5281 C  CG1  . VAL   B 1 325 ? 21.58883  -25.03175 73.04224  1.000 41.47180  ? 325 VAL   B CG1  1 
ATOM   5282 C  CG2  . VAL   B 1 325 ? 21.02734  -22.77893 72.02442  1.000 36.18918  ? 325 VAL   B CG2  1 
ATOM   5283 N  N    . ASN   B 1 326 ? 22.60399  -23.85962 76.32987  1.000 31.36351  ? 326 ASN   B N    1 
ATOM   5284 C  CA   . ASN   B 1 326 ? 22.87235  -24.77194 77.42454  1.000 31.43721  ? 326 ASN   B CA   1 
ATOM   5285 C  C    . ASN   B 1 326 ? 22.32570  -24.28687 78.75660  1.000 33.35944  ? 326 ASN   B C    1 
ATOM   5286 O  O    . ASN   B 1 326 ? 22.57058  -24.93432 79.78007  1.000 33.84633  ? 326 ASN   B O    1 
ATOM   5287 C  CB   . ASN   B 1 326 ? 24.40923  -25.03356 77.48429  1.000 31.87953  ? 326 ASN   B CB   1 
ATOM   5288 C  CG   . ASN   B 1 326 ? 24.83486  -25.89000 76.28769  1.000 42.97519  ? 326 ASN   B CG   1 
ATOM   5289 O  OD1  . ASN   B 1 326 ? 24.55152  -27.07114 76.24546  1.000 43.20961  ? 326 ASN   B OD1  1 
ATOM   5290 N  ND2  . ASN   B 1 326 ? 25.37230  -25.25399 75.26249  1.000 42.07202  ? 326 ASN   B ND2  1 
ATOM   5291 N  N    . GLY   B 1 327 ? 21.57633  -23.18611 78.76498  1.000 34.59578  ? 327 GLY   B N    1 
ATOM   5292 C  CA   . GLY   B 1 327 ? 20.97890  -22.70535 80.00440  1.000 38.04869  ? 327 GLY   B CA   1 
ATOM   5293 C  C    . GLY   B 1 327 ? 21.91943  -21.96903 80.94625  1.000 39.23209  ? 327 GLY   B C    1 
ATOM   5294 O  O    . GLY   B 1 327 ? 21.56996  -21.78848 82.12986  1.000 33.29364  ? 327 GLY   B O    1 
ATOM   5295 N  N    . PHE   B 1 328 ? 23.11826  -21.55952 80.49344  1.000 31.76511  ? 328 PHE   B N    1 
ATOM   5296 C  CA   . PHE   B 1 328 ? 23.97977  -20.80163 81.39598  1.000 32.79986  ? 328 PHE   B CA   1 
ATOM   5297 C  C    . PHE   B 1 328 ? 23.45474  -19.38299 81.58211  1.000 34.94672  ? 328 PHE   B C    1 
ATOM   5298 O  O    . PHE   B 1 328 ? 23.86996  -18.69259 82.52418  1.000 32.62687  ? 328 PHE   B O    1 
ATOM   5299 C  CB   . PHE   B 1 328 ? 25.45286  -20.66636 80.85501  1.000 34.02559  ? 328 PHE   B CB   1 
ATOM   5300 C  CG   . PHE   B 1 328 ? 26.18218  -21.94885 80.66396  1.000 31.47966  ? 328 PHE   B CG   1 
ATOM   5301 C  CD1  . PHE   B 1 328 ? 25.61076  -23.16730 80.90810  1.000 31.67497  ? 328 PHE   B CD1  1 
ATOM   5302 C  CD2  . PHE   B 1 328 ? 27.55049  -21.91574 80.32010  1.000 31.99862  ? 328 PHE   B CD2  1 
ATOM   5303 C  CE1  . PHE   B 1 328 ? 26.32769  -24.36260 80.74737  1.000 34.49190  ? 328 PHE   B CE1  1 
ATOM   5304 C  CE2  . PHE   B 1 328 ? 28.24245  -23.09937 80.13916  1.000 33.16024  ? 328 PHE   B CE2  1 
ATOM   5305 C  CZ   . PHE   B 1 328 ? 27.64682  -24.31359 80.35170  1.000 35.86380  ? 328 PHE   B CZ   1 
ATOM   5306 N  N    . ILE   B 1 329 ? 22.62250  -18.92032 80.64988  1.000 32.93699  ? 329 ILE   B N    1 
ATOM   5307 C  CA   . ILE   B 1 329 ? 22.03705  -17.58737 80.67299  1.000 28.85971  ? 329 ILE   B CA   1 
ATOM   5308 C  C    . ILE   B 1 329 ? 20.55050  -17.79376 80.86119  1.000 35.16700  ? 329 ILE   B C    1 
ATOM   5309 O  O    . ILE   B 1 329 ? 19.89816  -18.39410 79.99599  1.000 34.76102  ? 329 ILE   B O    1 
ATOM   5310 C  CB   . ILE   B 1 329 ? 22.30025  -16.81749 79.37830  1.000 32.26881  ? 329 ILE   B CB   1 
ATOM   5311 C  CG1  . ILE   B 1 329 ? 23.80397  -16.71493 79.13908  1.000 30.71438  ? 329 ILE   B CG1  1 
ATOM   5312 C  CG2  . ILE   B 1 329 ? 21.61483  -15.43224 79.38538  1.000 30.26490  ? 329 ILE   B CG2  1 
ATOM   5313 C  CD1  . ILE   B 1 329 ? 24.07322  -15.98358 77.80379  1.000 32.05317  ? 329 ILE   B CD1  1 
ATOM   5314 N  N    . HIS   B 1 330 ? 20.04368  -17.31997 81.97508  1.000 34.32769  ? 330 HIS   B N    1 
ATOM   5315 C  CA   . HIS   B 1 330 ? 18.60761  -17.42722 82.23891  1.000 36.06122  ? 330 HIS   B CA   1 
ATOM   5316 C  C    . HIS   B 1 330 ? 17.83604  -16.32300 81.52190  1.000 36.25045  ? 330 HIS   B C    1 
ATOM   5317 O  O    . HIS   B 1 330 ? 18.31954  -15.19228 81.35926  1.000 36.85952  ? 330 HIS   B O    1 
ATOM   5318 C  CB   . HIS   B 1 330 ? 18.32420  -17.33157 83.71415  1.000 39.30466  ? 330 HIS   B CB   1 
ATOM   5319 C  CG   . HIS   B 1 330 ? 18.85448  -18.48342 84.50983  1.000 50.93956  ? 330 HIS   B CG   1 
ATOM   5320 N  ND1  . HIS   B 1 330 ? 19.16286  -19.70966 83.94606  1.000 55.11122  ? 330 HIS   B ND1  1 
ATOM   5321 C  CD2  . HIS   B 1 330 ? 19.19448  -18.56826 85.81361  1.000 52.21373  ? 330 HIS   B CD2  1 
ATOM   5322 C  CE1  . HIS   B 1 330 ? 19.65822  -20.50462 84.87824  1.000 49.24432  ? 330 HIS   B CE1  1 
ATOM   5323 N  NE2  . HIS   B 1 330 ? 19.68380  -19.83867 86.02111  1.000 60.95330  ? 330 HIS   B NE2  1 
ATOM   5324 N  N    . PRO   B 1 331 ? 16.60151  -16.59314 81.14380  1.000 33.49446  ? 331 PRO   B N    1 
ATOM   5325 C  CA   . PRO   B 1 331 ? 15.84209  -15.55209 80.44486  1.000 34.39830  ? 331 PRO   B CA   1 
ATOM   5326 C  C    . PRO   B 1 331 ? 15.78424  -14.22822 81.18930  1.000 32.71137  ? 331 PRO   B C    1 
ATOM   5327 O  O    . PRO   B 1 331 ? 15.88520  -13.17499 80.53483  1.000 32.63812  ? 331 PRO   B O    1 
ATOM   5328 C  CB   . PRO   B 1 331 ? 14.45179  -16.18848 80.28717  1.000 34.93415  ? 331 PRO   B CB   1 
ATOM   5329 C  CG   . PRO   B 1 331 ? 14.76700  -17.64670 80.14712  1.000 37.21818  ? 331 PRO   B CG   1 
ATOM   5330 C  CD   . PRO   B 1 331 ? 15.93263  -17.90794 81.10870  1.000 32.98323  ? 331 PRO   B CD   1 
ATOM   5331 N  N    . LEU   B 1 332 ? 15.58877  -14.22925 82.51103  1.000 33.20748  ? 332 LEU   B N    1 
ATOM   5332 C  CA   . LEU   B 1 332 ? 15.44133  -12.95440 83.21063  1.000 34.64661  ? 332 LEU   B CA   1 
ATOM   5333 C  C    . LEU   B 1 332 ? 16.70319  -12.09988 83.08850  1.000 36.21379  ? 332 LEU   B C    1 
ATOM   5334 O  O    . LEU   B 1 332 ? 16.62362  -10.87481 82.96660  1.000 34.53647  ? 332 LEU   B O    1 
ATOM   5335 C  CB   . LEU   B 1 332 ? 15.12654  -13.20202 84.68616  1.000 38.69817  ? 332 LEU   B CB   1 
ATOM   5336 C  CG   . LEU   B 1 332 ? 15.13064  -11.91816 85.54666  1.000 50.88176  ? 332 LEU   B CG   1 
ATOM   5337 C  CD1  . LEU   B 1 332 ? 14.10833  -10.86077 85.02487  1.000 58.74129  ? 332 LEU   B CD1  1 
ATOM   5338 C  CD2  . LEU   B 1 332 ? 14.95277  -12.18911 87.06596  1.000 63.30578  ? 332 LEU   B CD2  1 
ATOM   5339 N  N    . ASP   B 1 333 ? 17.88049  -12.73077 83.15104  1.000 34.32266  ? 333 ASP   B N    1 
ATOM   5340 C  CA   . ASP   B 1 333 ? 19.15074  -11.99876 83.01251  1.000 36.15134  ? 333 ASP   B CA   1 
ATOM   5341 C  C    . ASP   B 1 333 ? 19.33871  -11.46269 81.60209  1.000 34.47940  ? 333 ASP   B C    1 
ATOM   5342 O  O    . ASP   B 1 333 ? 19.79243  -10.31754 81.40844  1.000 34.26040  ? 333 ASP   B O    1 
ATOM   5343 C  CB   . ASP   B 1 333 ? 20.32803  -12.91504 83.38951  1.000 37.20117  ? 333 ASP   B CB   1 
ATOM   5344 C  CG   . ASP   B 1 333 ? 20.43316  -13.14026 84.92248  1.000 41.26363  ? 333 ASP   B CG   1 
ATOM   5345 O  OD1  . ASP   B 1 333 ? 20.17260  -12.18007 85.68185  1.000 38.78717  ? 333 ASP   B OD1  1 
ATOM   5346 O  OD2  . ASP   B 1 333 ? 20.69580  -14.28579 85.37954  1.000 37.58783  ? 333 ASP   B OD2  1 
ATOM   5347 N  N    . LEU   B 1 334 ? 18.99360  -12.27569 80.59771  1.000 31.83476  ? 334 LEU   B N    1 
ATOM   5348 C  CA   . LEU   B 1 334 ? 19.10229  -11.77798 79.22866  1.000 30.77944  ? 334 LEU   B CA   1 
ATOM   5349 C  C    . LEU   B 1 334 ? 18.12389  -10.62888 79.01617  1.000 34.09907  ? 334 LEU   B C    1 
ATOM   5350 O  O    . LEU   B 1 334 ? 18.46963  -9.60770  78.40462  1.000 29.68108  ? 334 LEU   B O    1 
ATOM   5351 C  CB   . LEU   B 1 334 ? 18.85718  -12.91593 78.23113  1.000 30.18363  ? 334 LEU   B CB   1 
ATOM   5352 C  CG   . LEU   B 1 334 ? 19.05243  -12.55269 76.74805  1.000 33.12286  ? 334 LEU   B CG   1 
ATOM   5353 C  CD1  . LEU   B 1 334 ? 20.53197  -12.17641 76.51753  1.000 32.71572  ? 334 LEU   B CD1  1 
ATOM   5354 C  CD2  . LEU   B 1 334 ? 18.59027  -13.69882 75.80247  1.000 31.70341  ? 334 LEU   B CD2  1 
ATOM   5355 N  N    . LYS   B 1 335 ? 16.91415  -10.75344 79.57996  1.000 29.34080  ? 335 LYS   B N    1 
ATOM   5356 C  CA   . LYS   B 1 335 ? 15.93213  -9.67973  79.43333  1.000 31.62500  ? 335 LYS   B CA   1 
ATOM   5357 C  C    . LYS   B 1 335 ? 16.40592  -8.38926  80.07381  1.000 32.72933  ? 335 LYS   B C    1 
ATOM   5358 O  O    . LYS   B 1 335 ? 16.29999  -7.31510  79.46578  1.000 35.77000  ? 335 LYS   B O    1 
ATOM   5359 C  CB   . LYS   B 1 335 ? 14.58634  -10.10687 80.02891  1.000 31.97577  ? 335 LYS   B CB   1 
ATOM   5360 C  CG   . LYS   B 1 335 ? 13.80624  -10.98348 79.11715  1.000 32.91880  ? 335 LYS   B CG   1 
ATOM   5361 C  CD   . LYS   B 1 335 ? 12.45189  -11.39855 79.84211  1.000 34.27894  ? 335 LYS   B CD   1 
ATOM   5362 C  CE   . LYS   B 1 335 ? 11.41525  -11.96835 78.87674  1.000 37.37198  ? 335 LYS   B CE   1 
ATOM   5363 N  NZ   . LYS   B 1 335 ? 10.23576  -12.31088 79.76933  1.000 40.12983  ? 335 LYS   B NZ   1 
ATOM   5364 N  N    . ASP   B 1 336 ? 16.90307  -8.46073  81.31503  1.000 35.40485  ? 336 ASP   B N    1 
ATOM   5365 C  CA   . ASP   B 1 336 ? 17.33904  -7.23558  81.98525  1.000 37.15593  ? 336 ASP   B CA   1 
ATOM   5366 C  C    . ASP   B 1 336 ? 18.41498  -6.53504  81.17511  1.000 34.62988  ? 336 ASP   B C    1 
ATOM   5367 O  O    . ASP   B 1 336 ? 18.38032  -5.29863  81.01539  1.000 34.82468  ? 336 ASP   B O    1 
ATOM   5368 C  CB   . ASP   B 1 336 ? 17.84058  -7.51818  83.41090  1.000 33.53794  ? 336 ASP   B CB   1 
ATOM   5369 C  CG   . ASP   B 1 336 ? 16.71317  -8.00245  84.34968  1.000 43.40475  ? 336 ASP   B CG   1 
ATOM   5370 O  OD1  . ASP   B 1 336 ? 15.48278  -7.75078  84.08931  1.000 48.54831  ? 336 ASP   B OD1  1 
ATOM   5371 O  OD2  . ASP   B 1 336 ? 17.06245  -8.65401  85.34355  1.000 47.87780  ? 336 ASP   B OD2  1 
ATOM   5372 N  N    . ASN   B 1 337 ? 19.38191  -7.32157  80.64387  1.000 30.91977  ? 337 ASN   B N    1 
ATOM   5373 C  CA   . ASN   B 1 337 ? 20.47225  -6.70802  79.89648  1.000 30.67974  ? 337 ASN   B CA   1 
ATOM   5374 C  C    . ASN   B 1 337 ? 20.01990  -6.16699  78.54638  1.000 33.13748  ? 337 ASN   B C    1 
ATOM   5375 O  O    . ASN   B 1 337 ? 20.43426  -5.06347  78.15289  1.000 31.35092  ? 337 ASN   B O    1 
ATOM   5376 C  CB   . ASN   B 1 337 ? 21.60943  -7.72518  79.76624  1.000 32.74374  ? 337 ASN   B CB   1 
ATOM   5377 C  CG   . ASN   B 1 337 ? 22.40073  -7.82384  81.10107  1.000 34.51143  ? 337 ASN   B CG   1 
ATOM   5378 O  OD1  . ASN   B 1 337 ? 23.20155  -6.95169  81.40614  1.000 33.55724  ? 337 ASN   B OD1  1 
ATOM   5379 N  ND2  . ASN   B 1 337 ? 22.00293  -8.74063  81.95194  1.000 31.78821  ? 337 ASN   B ND2  1 
ATOM   5380 N  N    . VAL   B 1 338 ? 19.15643  -6.90686  77.84110  1.000 30.85237  ? 338 VAL   B N    1 
ATOM   5381 C  CA   . VAL   B 1 338 ? 18.61770  -6.42741  76.56392  1.000 30.30680  ? 338 VAL   B CA   1 
ATOM   5382 C  C    . VAL   B 1 338 ? 17.87081  -5.12059  76.76093  1.000 32.38772  ? 338 VAL   B C    1 
ATOM   5383 O  O    . VAL   B 1 338 ? 18.01580  -4.19527  75.95069  1.000 31.14571  ? 338 VAL   B O    1 
ATOM   5384 C  CB   . VAL   B 1 338 ? 17.75530  -7.51273  75.91272  1.000 30.18897  ? 338 VAL   B CB   1 
ATOM   5385 C  CG1  . VAL   B 1 338 ? 16.91007  -6.92464  74.73747  1.000 28.49057  ? 338 VAL   B CG1  1 
ATOM   5386 C  CG2  . VAL   B 1 338 ? 18.71651  -8.58231  75.37798  1.000 30.08459  ? 338 VAL   B CG2  1 
ATOM   5387 N  N    . ALA   B 1 339 ? 17.04836  -5.02511  77.82552  1.000 32.62555  ? 339 ALA   B N    1 
ATOM   5388 C  CA   . ALA   B 1 339 ? 16.31182  -3.78330  78.08295  1.000 32.66225  ? 339 ALA   B CA   1 
ATOM   5389 C  C    . ALA   B 1 339 ? 17.27416  -2.61764  78.28365  1.000 33.10011  ? 339 ALA   B C    1 
ATOM   5390 O  O    . ALA   B 1 339 ? 17.08253  -1.52448  77.71757  1.000 33.61894  ? 339 ALA   B O    1 
ATOM   5391 C  CB   . ALA   B 1 339 ? 15.35238  -3.95682  79.28562  1.000 34.94616  ? 339 ALA   B CB   1 
ATOM   5392 N  N    . MET   B 1 340 ? 18.33565  -2.83439  79.09747  1.000 34.00394  ? 340 MET   B N    1 
ATOM   5393 C  CA   . MET   B 1 340 ? 19.29241  -1.75737  79.34452  1.000 33.44117  ? 340 MET   B CA   1 
ATOM   5394 C  C    . MET   B 1 340 ? 19.93905  -1.27025  78.04770  1.000 31.58468  ? 340 MET   B C    1 
ATOM   5395 O  O    . MET   B 1 340 ? 20.08172  -0.06082  77.81053  1.000 31.59208  ? 340 MET   B O    1 
ATOM   5396 C  CB   . MET   B 1 340 ? 20.39613  -2.28943  80.30912  1.000 33.31614  ? 340 MET   B CB   1 
ATOM   5397 C  CG   . MET   B 1 340 ? 21.33119  -1.25335  80.80041  1.000 46.53924  ? 340 MET   B CG   1 
ATOM   5398 S  SD   . MET   B 1 340 ? 22.38925  -2.17939  81.97157  1.000 67.67187  ? 340 MET   B SD   1 
ATOM   5399 C  CE   . MET   B 1 340 ? 21.11308  -2.68408  83.08624  1.000 43.90116  ? 340 MET   B CE   1 
ATOM   5400 N  N    . TYR   B 1 341 ? 20.38596  -2.20759  77.21238  1.000 30.62957  ? 341 TYR   B N    1 
ATOM   5401 C  CA   . TYR   B 1 341 ? 20.98497  -1.88266  75.92485  1.000 31.51848  ? 341 TYR   B CA   1 
ATOM   5402 C  C    . TYR   B 1 341 ? 20.00524  -1.21044  74.94811  1.000 31.08431  ? 341 TYR   B C    1 
ATOM   5403 O  O    . TYR   B 1 341 ? 20.35573  -0.25789  74.24510  1.000 27.97458  ? 341 TYR   B O    1 
ATOM   5404 C  CB   . TYR   B 1 341 ? 21.48665  -3.16486  75.31344  1.000 31.82632  ? 341 TYR   B CB   1 
ATOM   5405 C  CG   . TYR   B 1 341 ? 22.88611  -3.57850  75.71766  1.000 34.74682  ? 341 TYR   B CG   1 
ATOM   5406 C  CD1  . TYR   B 1 341 ? 23.97230  -2.73507  75.48048  1.000 39.05622  ? 341 TYR   B CD1  1 
ATOM   5407 C  CD2  . TYR   B 1 341 ? 23.11919  -4.83298  76.26348  1.000 30.55959  ? 341 TYR   B CD2  1 
ATOM   5408 C  CE1  . TYR   B 1 341 ? 25.29918  -3.14718  75.76783  1.000 41.59707  ? 341 TYR   B CE1  1 
ATOM   5409 C  CE2  . TYR   B 1 341 ? 24.46337  -5.27665  76.52974  1.000 37.76240  ? 341 TYR   B CE2  1 
ATOM   5410 C  CZ   . TYR   B 1 341 ? 25.52476  -4.41907  76.28445  1.000 41.15937  ? 341 TYR   B CZ   1 
ATOM   5411 O  OH   . TYR   B 1 341 ? 26.82280  -4.82650  76.54964  1.000 37.96838  ? 341 TYR   B OH   1 
ATOM   5412 N  N    . ILE   B 1 342 ? 18.77974  -1.70182  74.86212  1.000 27.89579  ? 342 ILE   B N    1 
ATOM   5413 C  CA   . ILE   B 1 342 ? 17.84975  -1.03441  73.95685  1.000 28.37415  ? 342 ILE   B CA   1 
ATOM   5414 C  C    . ILE   B 1 342 ? 17.65359  0.42420   74.39104  1.000 31.30159  ? 342 ILE   B C    1 
ATOM   5415 O  O    . ILE   B 1 342 ? 17.63157  1.35077   73.54246  1.000 28.80031  ? 342 ILE   B O    1 
ATOM   5416 C  CB   . ILE   B 1 342 ? 16.52111  -1.82136  73.93068  1.000 31.78768  ? 342 ILE   B CB   1 
ATOM   5417 C  CG1  . ILE   B 1 342 ? 16.67010  -3.16268  73.17577  1.000 30.00302  ? 342 ILE   B CG1  1 
ATOM   5418 C  CG2  . ILE   B 1 342 ? 15.44489  -1.01702  73.18662  1.000 29.78018  ? 342 ILE   B CG2  1 
ATOM   5419 C  CD1  . ILE   B 1 342 ? 17.49577  -3.11489  71.91519  1.000 38.87230  ? 342 ILE   B CD1  1 
ATOM   5420 N  N    . ASN   B 1 343 ? 17.56722  0.65890   75.71244  1.000 32.39645  ? 343 ASN   B N    1 
ATOM   5421 C  CA   . ASN   B 1 343 ? 17.40093  2.04331   76.18910  1.000 32.63627  ? 343 ASN   B CA   1 
ATOM   5422 C  C    . ASN   B 1 343 ? 18.62583  2.90591   75.87477  1.000 32.21799  ? 343 ASN   B C    1 
ATOM   5423 O  O    . ASN   B 1 343 ? 18.48012  4.07132   75.47485  1.000 34.41892  ? 343 ASN   B O    1 
ATOM   5424 C  CB   . ASN   B 1 343 ? 17.05828  2.05184   77.65770  1.000 36.79295  ? 343 ASN   B CB   1 
ATOM   5425 C  CG   . ASN   B 1 343 ? 15.59727  1.65588   77.88454  1.000 43.56353  ? 343 ASN   B CG   1 
ATOM   5426 O  OD1  . ASN   B 1 343 ? 14.73117  2.00714   77.07748  1.000 34.96358  ? 343 ASN   B OD1  1 
ATOM   5427 N  ND2  . ASN   B 1 343 ? 15.32926  0.92327   78.94145  1.000 37.43585  ? 343 ASN   B ND2  1 
ATOM   5428 N  N    . LYS   B 1 344 ? 19.84919  2.35949   76.06082  1.000 32.73419  ? 344 LYS   B N    1 
ATOM   5429 C  CA   . LYS   B 1 344 ? 21.04637  3.08649   75.61372  1.000 35.31878  ? 344 LYS   B CA   1 
ATOM   5430 C  C    . LYS   B 1 344 ? 20.96872  3.41963   74.12390  1.000 36.08808  ? 344 LYS   B C    1 
ATOM   5431 O  O    . LYS   B 1 344 ? 21.21663  4.55944   73.72123  1.000 32.53476  ? 344 LYS   B O    1 
ATOM   5432 C  CB   . LYS   B 1 344 ? 22.31395  2.25959   75.87989  1.000 32.70141  ? 344 LYS   B CB   1 
ATOM   5433 C  CG   . LYS   B 1 344 ? 22.65602  2.11115   77.36642  1.000 38.34379  ? 344 LYS   B CG   1 
ATOM   5434 C  CD   . LYS   B 1 344 ? 23.72951  0.99529   77.54288  1.000 35.62964  ? 344 LYS   B CD   1 
ATOM   5435 C  CE   . LYS   B 1 344 ? 24.17784  0.93456   78.96793  1.000 47.77008  ? 344 LYS   B CE   1 
ATOM   5436 N  NZ   . LYS   B 1 344 ? 25.31285  -0.03016  79.04933  1.000 51.13159  ? 344 LYS   B NZ   1 
ATOM   5437 N  N    . LEU   B 1 345 ? 20.62629  2.42831   73.28598  1.000 28.65442  ? 345 LEU   B N    1 
ATOM   5438 C  CA   . LEU   B 1 345 ? 20.62651  2.64368   71.83651  1.000 32.45200  ? 345 LEU   B CA   1 
ATOM   5439 C  C    . LEU   B 1 345 ? 19.54125  3.61993   71.42515  1.000 34.98659  ? 345 LEU   B C    1 
ATOM   5440 O  O    . LEU   B 1 345 ? 19.71584  4.34263   70.45052  1.000 30.42562  ? 345 LEU   B O    1 
ATOM   5441 C  CB   . LEU   B 1 345 ? 20.44295  1.32580   71.07502  1.000 30.24426  ? 345 LEU   B CB   1 
ATOM   5442 C  CG   . LEU   B 1 345 ? 21.70215  0.43216   71.21426  1.000 32.13442  ? 345 LEU   B CG   1 
ATOM   5443 C  CD1  . LEU   B 1 345 ? 21.42535  -0.87528  70.45107  1.000 32.20028  ? 345 LEU   B CD1  1 
ATOM   5444 C  CD2  . LEU   B 1 345 ? 22.90383  1.14200   70.63023  1.000 36.56774  ? 345 LEU   B CD2  1 
ATOM   5445 N  N    . LEU   B 1 346 ? 18.42631  3.65706   72.13475  1.000 33.88950  ? 346 LEU   B N    1 
ATOM   5446 C  CA   . LEU   B 1 346 ? 17.36008  4.58606   71.74524  1.000 33.45006  ? 346 LEU   B CA   1 
ATOM   5447 C  C    . LEU   B 1 346 ? 17.56449  5.98994   72.28969  1.000 36.78809  ? 346 LEU   B C    1 
ATOM   5448 O  O    . LEU   B 1 346 ? 16.72623  6.86850   72.00643  1.000 36.61728  ? 346 LEU   B O    1 
ATOM   5449 C  CB   . LEU   B 1 346 ? 15.98940  4.06806   72.23678  1.000 31.88267  ? 346 LEU   B CB   1 
ATOM   5450 C  CG   . LEU   B 1 346 ? 15.49720  2.82721   71.50554  1.000 30.25772  ? 346 LEU   B CG   1 
ATOM   5451 C  CD1  . LEU   B 1 346 ? 14.14338  2.41671   72.22966  1.000 35.20502  ? 346 LEU   B CD1  1 
ATOM   5452 C  CD2  . LEU   B 1 346 ? 15.21470  3.11644   69.97150  1.000 35.26292  ? 346 LEU   B CD2  1 
ATOM   5453 N  N    . GLN   B 1 347 ? 18.60318  6.22223   73.10463  1.000 35.40348  ? 347 GLN   B N    1 
ATOM   5454 C  CA   . GLN   B 1 347 ? 18.75038  7.55150   73.70620  1.000 35.37762  ? 347 GLN   B CA   1 
ATOM   5455 C  C    . GLN   B 1 347 ? 18.65514  8.71109   72.71589  1.000 33.83682  ? 347 GLN   B C    1 
ATOM   5456 O  O    . GLN   B 1 347 ? 17.96478  9.70178   73.02867  1.000 33.72984  ? 347 GLN   B O    1 
ATOM   5457 C  CB   . GLN   B 1 347 ? 20.09811  7.64632   74.46652  1.000 38.66487  ? 347 GLN   B CB   1 
ATOM   5458 C  CG   . GLN   B 1 347 ? 20.41598  9.10297   74.92377  1.000 39.01910  ? 347 GLN   B CG   1 
ATOM   5459 C  CD   . GLN   B 1 347 ? 21.32241  9.89182   73.88420  1.000 51.72527  ? 347 GLN   B CD   1 
ATOM   5460 O  OE1  . GLN   B 1 347 ? 22.34983  9.36233   73.37596  1.000 54.90871  ? 347 GLN   B OE1  1 
ATOM   5461 N  NE2  . GLN   B 1 347 ? 20.92137  11.12658  73.55156  1.000 41.98052  ? 347 GLN   B NE2  1 
ATOM   5462 N  N    . PRO   B 1 348 ? 19.37268  8.71836   71.58211  1.000 31.93267  ? 348 PRO   B N    1 
ATOM   5463 C  CA   . PRO   B 1 348 ? 19.31685  9.89922   70.72054  1.000 31.04882  ? 348 PRO   B CA   1 
ATOM   5464 C  C    . PRO   B 1 348 ? 17.91266  10.09842  70.12407  1.000 35.35273  ? 348 PRO   B C    1 
ATOM   5465 O  O    . PRO   B 1 348 ? 17.48340  11.23281  69.92713  1.000 30.06683  ? 348 PRO   B O    1 
ATOM   5466 C  CB   . PRO   B 1 348 ? 20.29191  9.58304   69.58986  1.000 36.34548  ? 348 PRO   B CB   1 
ATOM   5467 C  CG   . PRO   B 1 348 ? 20.39835  8.06040   69.58145  1.000 35.84259  ? 348 PRO   B CG   1 
ATOM   5468 C  CD   . PRO   B 1 348 ? 20.26591  7.67194   71.03050  1.000 37.75634  ? 348 PRO   B CD   1 
ATOM   5469 N  N    . VAL   B 1 349 ? 17.17162  9.01474   69.91168  1.000 29.20711  ? 349 VAL   B N    1 
ATOM   5470 C  CA   . VAL   B 1 349 ? 15.77482  9.14347   69.43055  1.000 30.93683  ? 349 VAL   B CA   1 
ATOM   5471 C  C    . VAL   B 1 349 ? 14.88099  9.71610   70.53633  1.000 33.31946  ? 349 VAL   B C    1 
ATOM   5472 O  O    . VAL   B 1 349 ? 14.12020  10.67805  70.30241  1.000 33.85096  ? 349 VAL   B O    1 
ATOM   5473 C  CB   . VAL   B 1 349 ? 15.26943  7.76201   68.97095  1.000 29.41416  ? 349 VAL   B CB   1 
ATOM   5474 C  CG1  . VAL   B 1 349 ? 13.82486  7.87850   68.42717  1.000 32.76321  ? 349 VAL   B CG1  1 
ATOM   5475 C  CG2  . VAL   B 1 349 ? 16.21367  7.18750   67.93008  1.000 34.09108  ? 349 VAL   B CG2  1 
ATOM   5476 N  N    . ARG   B 1 350 ? 14.95597  9.12981   71.74806  1.000 33.42399  ? 350 ARG   B N    1 
ATOM   5477 C  CA   . ARG   B 1 350 ? 14.21222  9.67094   72.90315  1.000 38.14328  ? 350 ARG   B CA   1 
ATOM   5478 C  C    . ARG   B 1 350 ? 14.48785  11.13766  73.05676  1.000 41.35235  ? 350 ARG   B C    1 
ATOM   5479 O  O    . ARG   B 1 350 ? 13.57369  11.95447  73.18786  1.000 38.18196  ? 350 ARG   B O    1 
ATOM   5480 C  CB   . ARG   B 1 350 ? 14.58895  9.03777   74.25138  1.000 39.94324  ? 350 ARG   B CB   1 
ATOM   5481 C  CG   . ARG   B 1 350 ? 14.01003  7.74985   74.65581  1.000 42.75530  ? 350 ARG   B CG   1 
ATOM   5482 C  CD   . ARG   B 1 350 ? 14.15625  7.59400   76.15423  1.000 40.27428  ? 350 ARG   B CD   1 
ATOM   5483 N  NE   . ARG   B 1 350 ? 15.53660  7.78657   76.64118  1.000 45.47804  ? 350 ARG   B NE   1 
ATOM   5484 C  CZ   . ARG   B 1 350 ? 16.47828  6.86855   76.48063  1.000 45.77117  ? 350 ARG   B CZ   1 
ATOM   5485 N  NH1  . ARG   B 1 350 ? 16.20623  5.72081   75.87758  1.000 44.77616  ? 350 ARG   B NH1  1 
ATOM   5486 N  NH2  . ARG   B 1 350 ? 17.72201  7.11257   76.91068  1.000 39.28051  ? 350 ARG   B NH2  1 
ATOM   5487 N  N    . ASP   B 1 351 ? 15.76720  11.49448  73.05566  1.000 34.92791  ? 351 ASP   B N    1 
ATOM   5488 C  CA   . ASP   B 1 351 ? 16.08197  12.88854  73.29442  1.000 40.26732  ? 351 ASP   B CA   1 
ATOM   5489 C  C    . ASP   B 1 351 ? 15.53432  13.78552  72.19031  1.000 35.23768  ? 351 ASP   B C    1 
ATOM   5490 O  O    . ASP   B 1 351 ? 15.01820  14.87514  72.49011  1.000 42.49759  ? 351 ASP   B O    1 
ATOM   5491 C  CB   . ASP   B 1 351 ? 17.58817  13.02723  73.51818  1.000 39.83651  ? 351 ASP   B CB   1 
ATOM   5492 C  CG   . ASP   B 1 351 ? 18.03845  12.43821  74.89359  1.000 49.14597  ? 351 ASP   B CG   1 
ATOM   5493 O  OD1  . ASP   B 1 351 ? 17.21694  12.22790  75.81348  1.000 51.91258  ? 351 ASP   B OD1  1 
ATOM   5494 O  OD2  . ASP   B 1 351 ? 19.23911  12.18954  75.08649  1.000 49.96963  ? 351 ASP   B OD2  1 
ATOM   5495 N  N    . HIS   B 1 352 ? 15.64456  13.36935  70.90748  1.000 35.52307  ? 352 HIS   B N    1 
ATOM   5496 C  CA   . HIS   B 1 352 ? 15.11656  14.17231  69.80189  1.000 35.73757  ? 352 HIS   B CA   1 
ATOM   5497 C  C    . HIS   B 1 352 ? 13.63044  14.43064  70.00790  1.000 40.31188  ? 352 HIS   B C    1 
ATOM   5498 O  O    . HIS   B 1 352 ? 13.17960  15.57198  69.92331  1.000 39.54586  ? 352 HIS   B O    1 
ATOM   5499 C  CB   . HIS   B 1 352 ? 15.34801  13.49247  68.44861  1.000 39.88023  ? 352 HIS   B CB   1 
ATOM   5500 C  CG   . HIS   B 1 352 ? 14.83618  14.27587  67.27221  1.000 38.62306  ? 352 HIS   B CG   1 
ATOM   5501 N  ND1  . HIS   B 1 352 ? 15.39980  15.47147  66.86767  1.000 39.14935  ? 352 HIS   B ND1  1 
ATOM   5502 C  CD2  . HIS   B 1 352 ? 13.79281  14.05515  66.42785  1.000 44.40079  ? 352 HIS   B CD2  1 
ATOM   5503 C  CE1  . HIS   B 1 352 ? 14.74382  15.94072  65.81861  1.000 42.96815  ? 352 HIS   B CE1  1 
ATOM   5504 N  NE2  . HIS   B 1 352 ? 13.75567  15.10467  65.53278  1.000 44.29726  ? 352 HIS   B NE2  1 
ATOM   5505 N  N    . PHE   B 1 353 ? 12.87922  13.40234  70.39310  1.000 37.85787  ? 353 PHE   B N    1 
ATOM   5506 C  CA   . PHE   B 1 353 ? 11.40926  13.59016  70.46820  1.000 37.66275  ? 353 PHE   B CA   1 
ATOM   5507 C  C    . PHE   B 1 353 ? 10.94843  14.17704  71.79290  1.000 42.06566  ? 353 PHE   B C    1 
ATOM   5508 O  O    . PHE   B 1 353 ? 9.79853   14.65110  71.88563  1.000 46.01300  ? 353 PHE   B O    1 
ATOM   5509 C  CB   . PHE   B 1 353 ? 10.69094  12.26607  70.22244  1.000 37.47264  ? 353 PHE   B CB   1 
ATOM   5510 C  CG   . PHE   B 1 353 ? 10.64224  11.88775  68.78768  1.000 37.39118  ? 353 PHE   B CG   1 
ATOM   5511 C  CD1  . PHE   B 1 353 ? 9.67133   12.43384  67.92593  1.000 32.66521  ? 353 PHE   B CD1  1 
ATOM   5512 C  CD2  . PHE   B 1 353 ? 11.54762  10.97291  68.27054  1.000 37.30457  ? 353 PHE   B CD2  1 
ATOM   5513 C  CE1  . PHE   B 1 353 ? 9.62473   12.13719  66.60487  1.000 32.89705  ? 353 PHE   B CE1  1 
ATOM   5514 C  CE2  . PHE   B 1 353 ? 11.48869  10.64223  66.90453  1.000 39.90877  ? 353 PHE   B CE2  1 
ATOM   5515 C  CZ   . PHE   B 1 353 ? 10.50772  11.23859  66.05860  1.000 39.39385  ? 353 PHE   B CZ   1 
ATOM   5516 N  N    . GLN   B 1 354 ? 11.81251  14.19435  72.80293  1.000 39.45079  ? 354 GLN   B N    1 
ATOM   5517 C  CA   . GLN   B 1 354 ? 11.49681  14.86984  74.06282  1.000 46.46162  ? 354 GLN   B CA   1 
ATOM   5518 C  C    . GLN   B 1 354 ? 11.85129  16.34943  73.99234  1.000 51.30582  ? 354 GLN   B C    1 
ATOM   5519 O  O    . GLN   B 1 354 ? 11.12524  17.19238  74.54451  1.000 49.54531  ? 354 GLN   B O    1 
ATOM   5520 C  CB   . GLN   B 1 354 ? 12.20717  14.19122  75.25407  1.000 47.27717  ? 354 GLN   B CB   1 
ATOM   5521 C  CG   . GLN   B 1 354 ? 11.52339  12.84468  75.58094  1.000 51.39289  ? 354 GLN   B CG   1 
ATOM   5522 C  CD   . GLN   B 1 354 ? 12.28343  11.96485  76.55969  1.000 57.53732  ? 354 GLN   B CD   1 
ATOM   5523 O  OE1  . GLN   B 1 354 ? 13.38575  12.31327  77.02874  1.000 68.57839  ? 354 GLN   B OE1  1 
ATOM   5524 N  NE2  . GLN   B 1 354 ? 11.70173  10.79372  76.87258  1.000 61.11816  ? 354 GLN   B NE2  1 
ATOM   5525 N  N    . ASN   B 1 355 ? 12.94046  16.68178  73.28259  1.000 43.58673  ? 355 ASN   B N    1 
ATOM   5526 C  CA   . ASN   B 1 355 ? 13.56279  18.00388  73.36721  1.000 51.18557  ? 355 ASN   B CA   1 
ATOM   5527 C  C    . ASN   B 1 355 ? 13.34590  18.88816  72.15803  1.000 42.75104  ? 355 ASN   B C    1 
ATOM   5528 O  O    . ASN   B 1 355 ? 13.40866  20.11800  72.29206  1.000 49.64147  ? 355 ASN   B O    1 
ATOM   5529 C  CB   . ASN   B 1 355 ? 15.07475  17.86563  73.62829  1.000 46.10329  ? 355 ASN   B CB   1 
ATOM   5530 C  CG   . ASN   B 1 355 ? 15.36605  17.17264  74.91877  1.000 55.42678  ? 355 ASN   B CG   1 
ATOM   5531 O  OD1  . ASN   B 1 355 ? 14.56630  17.23924  75.84456  1.000 57.25182  ? 355 ASN   B OD1  1 
ATOM   5532 N  ND2  . ASN   B 1 355 ? 16.49343  16.47339  74.98973  1.000 47.51062  ? 355 ASN   B ND2  1 
ATOM   5533 N  N    . ASN   B 1 356 ? 13.07782  18.31706  71.00528  1.000 40.59276  ? 356 ASN   B N    1 
ATOM   5534 C  CA   . ASN   B 1 356 ? 12.73596  19.06623  69.81143  1.000 45.00003  ? 356 ASN   B CA   1 
ATOM   5535 C  C    . ASN   B 1 356 ? 11.21466  19.28324  69.76785  1.000 47.86809  ? 356 ASN   B C    1 
ATOM   5536 O  O    . ASN   B 1 356 ? 10.45144  18.32419  69.62673  1.000 39.88628  ? 356 ASN   B O    1 
ATOM   5537 C  CB   . ASN   B 1 356 ? 13.22327  18.30027  68.58749  1.000 44.28418  ? 356 ASN   B CB   1 
ATOM   5538 C  CG   . ASN   B 1 356 ? 12.94354  19.03123  67.28539  1.000 50.70062  ? 356 ASN   B CG   1 
ATOM   5539 O  OD1  . ASN   B 1 356 ? 11.79624  19.10002  66.81854  1.000 46.23387  ? 356 ASN   B OD1  1 
ATOM   5540 N  ND2  . ASN   B 1 356 ? 14.00290  19.58101  66.67803  1.000 45.02492  ? 356 ASN   B ND2  1 
ATOM   5541 N  N    . ILE   B 1 357 ? 10.78505  20.54572  69.81802  1.000 43.32076  ? 357 ILE   B N    1 
ATOM   5542 C  CA   . ILE   B 1 357 ? 9.36894   20.86212  70.03533  1.000 45.36026  ? 357 ILE   B CA   1 
ATOM   5543 C  C    . ILE   B 1 357 ? 8.51268   20.37307  68.86861  1.000 48.45747  ? 357 ILE   B C    1 
ATOM   5544 O  O    . ILE   B 1 357 ? 7.41271   19.83045  69.06566  1.000 46.43405  ? 357 ILE   B O    1 
ATOM   5545 C  CB   . ILE   B 1 357 ? 9.20005   22.38016  70.26275  1.000 49.56425  ? 357 ILE   B CB   1 
ATOM   5546 C  CG1  . ILE   B 1 357 ? 9.95084   22.86673  71.51411  1.000 49.26169  ? 357 ILE   B CG1  1 
ATOM   5547 C  CG2  . ILE   B 1 357 ? 7.71151   22.81437  70.20391  1.000 51.01540  ? 357 ILE   B CG2  1 
ATOM   5548 C  CD1  . ILE   B 1 357 ? 9.96027   21.88972  72.65979  1.000 59.96803  ? 357 ILE   B CD1  1 
ATOM   5549 N  N    . GLU   B 1 358 ? 8.98413   20.58291  67.63309  1.000 45.63906  ? 358 GLU   B N    1 
ATOM   5550 C  CA   . GLU   B 1 358 ? 8.22478   20.16435  66.45723  1.000 46.30945  ? 358 GLU   B CA   1 
ATOM   5551 C  C    . GLU   B 1 358 ? 8.11683   18.64529  66.39002  1.000 45.95029  ? 358 GLU   B C    1 
ATOM   5552 O  O    . GLU   B 1 358 ? 7.07082   18.09365  66.02511  1.000 41.42346  ? 358 GLU   B O    1 
ATOM   5553 C  CB   . GLU   B 1 358 ? 8.87848   20.72515  65.18312  1.000 53.28720  ? 358 GLU   B CB   1 
ATOM   5554 C  CG   . GLU   B 1 358 ? 9.04311   22.30488  65.14758  1.000 62.55950  ? 358 GLU   B CG   1 
ATOM   5555 C  CD   . GLU   B 1 358 ? 10.04484  22.96707  66.20834  1.000 65.02344  ? 358 GLU   B CD   1 
ATOM   5556 O  OE1  . GLU   B 1 358 ? 11.11261  22.38714  66.60240  1.000 58.71920  ? 358 GLU   B OE1  1 
ATOM   5557 O  OE2  . GLU   B 1 358 ? 9.75164   24.12297  66.64847  1.000 68.19186  ? 358 GLU   B OE2  1 
ATOM   5558 N  N    . ALA   B 1 359 ? 9.20432   17.94266  66.71516  1.000 42.99517  ? 359 ALA   B N    1 
ATOM   5559 C  CA   . ALA   B 1 359 ? 9.15883   16.48922  66.67008  1.000 36.70402  ? 359 ALA   B CA   1 
ATOM   5560 C  C    . ALA   B 1 359 ? 8.24335   15.95430  67.78044  1.000 36.12350  ? 359 ALA   B C    1 
ATOM   5561 O  O    . ALA   B 1 359 ? 7.55013   14.94538  67.58431  1.000 38.82590  ? 359 ALA   B O    1 
ATOM   5562 C  CB   . ALA   B 1 359 ? 10.58737  15.93793  66.79914  1.000 41.76351  ? 359 ALA   B CB   1 
ATOM   5563 N  N    . LYS   B 1 360 ? 8.29908   16.57134  68.97515  1.000 37.27359  ? 360 LYS   B N    1 
ATOM   5564 C  CA   . LYS   B 1 360 ? 7.42753   16.19032  70.08638  1.000 37.53913  ? 360 LYS   B CA   1 
ATOM   5565 C  C    . LYS   B 1 360 ? 5.96602   16.34932  69.67869  1.000 44.57359  ? 360 LYS   B C    1 
ATOM   5566 O  O    . LYS   B 1 360 ? 5.13558   15.45987  69.90588  1.000 41.41209  ? 360 LYS   B O    1 
ATOM   5567 C  CB   . LYS   B 1 360 ? 7.72568   17.04762  71.32293  1.000 40.15419  ? 360 LYS   B CB   1 
ATOM   5568 C  CG   . LYS   B 1 360 ? 6.87668   16.74573  72.59653  1.000 45.03339  ? 360 LYS   B CG   1 
ATOM   5569 C  CD   . LYS   B 1 360 ? 7.34203   17.58955  73.82926  1.000 45.85042  ? 360 LYS   B CD   1 
ATOM   5570 C  CE   . LYS   B 1 360 ? 7.19928   19.10299  73.54667  1.000 48.82861  ? 360 LYS   B CE   1 
ATOM   5571 N  NZ   . LYS   B 1 360 ? 7.46520   19.96970  74.74429  1.000 60.54068  ? 360 LYS   B NZ   1 
ATOM   5572 N  N    . ASN   B 1 361 ? 5.64851   17.46667  69.04594  1.000 41.93246  ? 361 ASN   B N    1 
ATOM   5573 C  CA   . ASN   B 1 361 ? 4.25463   17.68155  68.63806  1.000 45.92277  ? 361 ASN   B CA   1 
ATOM   5574 C  C    . ASN   B 1 361 ? 3.82075   16.68660  67.56793  1.000 44.18227  ? 361 ASN   B C    1 
ATOM   5575 O  O    . ASN   B 1 361 ? 2.66945   16.20649  67.58454  1.000 45.74301  ? 361 ASN   B O    1 
ATOM   5576 C  CB   . ASN   B 1 361 ? 4.05700   19.11610  68.14178  1.000 43.40688  ? 361 ASN   B CB   1 
ATOM   5577 C  CG   . ASN   B 1 361 ? 4.17065   20.14493  69.23250  1.000 47.95258  ? 361 ASN   B CG   1 
ATOM   5578 O  OD1  . ASN   B 1 361 ? 3.94565   19.86116  70.42207  1.000 52.58556  ? 361 ASN   B OD1  1 
ATOM   5579 N  ND2  . ASN   B 1 361 ? 4.48251   21.38563  68.83350  1.000 53.78553  ? 361 ASN   B ND2  1 
ATOM   5580 N  N    . LEU   B 1 362 ? 4.72068   16.33838  66.64102  1.000 38.26309  ? 362 LEU   B N    1 
ATOM   5581 C  CA   . LEU   B 1 362 ? 4.40522   15.34730  65.61130  1.000 39.14100  ? 362 LEU   B CA   1 
ATOM   5582 C  C    . LEU   B 1 362 ? 4.14415   13.96416  66.20128  1.000 38.47572  ? 362 LEU   B C    1 
ATOM   5583 O  O    . LEU   B 1 362 ? 3.20563   13.25802  65.78295  1.000 38.62724  ? 362 LEU   B O    1 
ATOM   5584 C  CB   . LEU   B 1 362 ? 5.53848   15.26784  64.57349  1.000 34.94849  ? 362 LEU   B CB   1 
ATOM   5585 C  CG   . LEU   B 1 362 ? 5.40732   14.23621  63.46656  1.000 34.21462  ? 362 LEU   B CG   1 
ATOM   5586 C  CD1  . LEU   B 1 362 ? 4.11262   14.44566  62.55769  1.000 36.03223  ? 362 LEU   B CD1  1 
ATOM   5587 C  CD2  . LEU   B 1 362 ? 6.67038   14.27835  62.57175  1.000 37.37298  ? 362 LEU   B CD2  1 
ATOM   5588 N  N    . LEU   B 1 363 ? 5.02136   13.51806  67.10260  1.000 36.45176  ? 363 LEU   B N    1 
ATOM   5589 C  CA   . LEU   B 1 363 ? 4.81074   12.24236  67.77419  1.000 37.69068  ? 363 LEU   B CA   1 
ATOM   5590 C  C    . LEU   B 1 363 ? 3.49773   12.26341  68.54257  1.000 40.69895  ? 363 LEU   B C    1 
ATOM   5591 O  O    . LEU   B 1 363 ? 2.74972   11.27521  68.55501  1.000 37.18904  ? 363 LEU   B O    1 
ATOM   5592 C  CB   . LEU   B 1 363 ? 5.96296   11.95114  68.74394  1.000 35.60696  ? 363 LEU   B CB   1 
ATOM   5593 C  CG   . LEU   B 1 363 ? 5.84736   10.69297  69.57436  1.000 35.24504  ? 363 LEU   B CG   1 
ATOM   5594 C  CD1  . LEU   B 1 363 ? 5.75461   9.54708   68.58044  1.000 40.47900  ? 363 LEU   B CD1  1 
ATOM   5595 C  CD2  . LEU   B 1 363 ? 7.08301   10.46066  70.52488  1.000 38.86763  ? 363 LEU   B CD2  1 
ATOM   5596 N  N    . ASN   B 1 364 ? 3.21543   13.37026  69.21882  1.000 36.26579  ? 364 ASN   B N    1 
ATOM   5597 C  CA   . ASN   B 1 364 ? 1.98185   13.40624  70.00415  1.000 44.05436  ? 364 ASN   B CA   1 
ATOM   5598 C  C    . ASN   B 1 364 ? 0.78648   13.21979  69.07626  1.000 41.90469  ? 364 ASN   B C    1 
ATOM   5599 O  O    . ASN   B 1 364 ? -0.16988  12.51837  69.42891  1.000 48.50080  ? 364 ASN   B O    1 
ATOM   5600 C  CB   . ASN   B 1 364 ? 1.88493   14.70220  70.81019  1.000 38.70735  ? 364 ASN   B CB   1 
ATOM   5601 C  CG   . ASN   B 1 364 ? 2.72415   14.64860  72.06381  1.000 55.83553  ? 364 ASN   B CG   1 
ATOM   5602 O  OD1  . ASN   B 1 364 ? 3.23029   13.57108  72.45127  1.000 57.26495  ? 364 ASN   B OD1  1 
ATOM   5603 N  ND2  . ASN   B 1 364 ? 2.89990   15.80480  72.70688  1.000 64.86784  ? 364 ASN   B ND2  1 
ATOM   5604 N  N    . GLU   B 1 365 ? 0.82195   13.83562  67.88622  1.000 38.43236  ? 365 GLU   B N    1 
ATOM   5605 C  CA   . GLU   B 1 365 ? -0.27887  13.65011  66.94023  1.000 44.75257  ? 365 GLU   B CA   1 
ATOM   5606 C  C    . GLU   B 1 365 ? -0.38854  12.20519  66.47403  1.000 50.78156  ? 365 GLU   B C    1 
ATOM   5607 O  O    . GLU   B 1 365 ? -1.49137  11.64609  66.41689  1.000 47.67302  ? 365 GLU   B O    1 
ATOM   5608 C  CB   . GLU   B 1 365 ? -0.12684  14.53859  65.71290  1.000 49.32645  ? 365 GLU   B CB   1 
ATOM   5609 C  CG   . GLU   B 1 365 ? -0.31941  15.99905  65.96872  1.000 60.98490  ? 365 GLU   B CG   1 
ATOM   5610 C  CD   . GLU   B 1 365 ? -0.07232  16.81077  64.71409  1.000 71.59453  ? 365 GLU   B CD   1 
ATOM   5611 O  OE1  . GLU   B 1 365 ? -0.29921  16.28973  63.59135  1.000 74.24840  ? 365 GLU   B OE1  1 
ATOM   5612 O  OE2  . GLU   B 1 365 ? 0.42023   17.95351  64.86768  1.000 80.58021  ? 365 GLU   B OE2  1 
ATOM   5613 N  N    . ILE   B 1 366 ? 0.72747   11.60480  66.04963  1.000 38.81778  ? 366 ILE   B N    1 
ATOM   5614 C  CA   . ILE   B 1 366 ? 0.58640   10.29072  65.44233  1.000 41.48711  ? 366 ILE   B CA   1 
ATOM   5615 C  C    . ILE   B 1 366 ? 0.29512   9.20843   66.47303  1.000 46.15806  ? 366 ILE   B C    1 
ATOM   5616 O  O    . ILE   B 1 366 ? -0.27425  8.16887   66.11198  1.000 50.92873  ? 366 ILE   B O    1 
ATOM   5617 C  CB   . ILE   B 1 366 ? 1.78862   9.91440   64.54499  1.000 37.44663  ? 366 ILE   B CB   1 
ATOM   5618 C  CG1  . ILE   B 1 366 ? 3.04880   9.64375   65.32769  1.000 45.29301  ? 366 ILE   B CG1  1 
ATOM   5619 C  CG2  . ILE   B 1 366 ? 2.03325   11.01125  63.46380  1.000 35.07917  ? 366 ILE   B CG2  1 
ATOM   5620 C  CD1  . ILE   B 1 366 ? 3.41985   8.18010   65.29980  1.000 51.31204  ? 366 ILE   B CD1  1 
ATOM   5621 N  N    . LYS   B 1 367 ? 0.64705   9.42354   67.74164  1.000 42.61240  ? 367 LYS   B N    1 
ATOM   5622 C  CA   . LYS   B 1 367 ? 0.32058   8.46076   68.78438  1.000 51.58850  ? 367 LYS   B CA   1 
ATOM   5623 C  C    . LYS   B 1 367 ? -1.18377  8.31279   68.94266  1.000 53.71385  ? 367 LYS   B C    1 
ATOM   5624 O  O    . LYS   B 1 367 ? -1.66219  7.25778   69.36915  1.000 61.03809  ? 367 LYS   B O    1 
ATOM   5625 C  CB   . LYS   B 1 367 ? 0.90275   8.90060   70.12856  1.000 48.72879  ? 367 LYS   B CB   1 
ATOM   5626 C  CG   . LYS   B 1 367 ? 2.33972   8.53797   70.32921  1.000 54.68472  ? 367 LYS   B CG   1 
ATOM   5627 C  CD   . LYS   B 1 367 ? 2.78767   9.02700   71.68861  1.000 47.97028  ? 367 LYS   B CD   1 
ATOM   5628 C  CE   . LYS   B 1 367 ? 4.06346   8.37987   72.10750  1.000 52.51156  ? 367 LYS   B CE   1 
ATOM   5629 N  NZ   . LYS   B 1 367 ? 4.53708   8.97232   73.41805  1.000 52.32975  ? 367 LYS   B NZ   1 
ATOM   5630 N  N    . LYS   B 1 368 ? -1.93337  9.35457   68.61427  1.000 49.63896  ? 368 LYS   B N    1 
ATOM   5631 C  CA   . LYS   B 1 368 ? -3.38081  9.30270   68.72490  1.000 59.74707  ? 368 LYS   B CA   1 
ATOM   5632 C  C    . LYS   B 1 368 ? -4.05856  8.55097   67.58167  1.000 55.56721  ? 368 LYS   B C    1 
ATOM   5633 O  O    . LYS   B 1 368 ? -5.25858  8.28484   67.67058  1.000 64.40051  ? 368 LYS   B O    1 
ATOM   5634 C  CB   . LYS   B 1 368 ? -3.92267  10.74055  68.83264  1.000 59.33164  ? 368 LYS   B CB   1 
ATOM   5635 C  CG   . LYS   B 1 368 ? -3.37352  11.50410  70.09195  1.000 57.05944  ? 368 LYS   B CG   1 
ATOM   5636 C  CD   . LYS   B 1 368 ? -4.07751  12.86238  70.36479  1.000 66.18783  ? 368 LYS   B CD   1 
ATOM   5637 C  CE   . LYS   B 1 368 ? -3.34045  13.72243  71.41675  1.000 68.35572  ? 368 LYS   B CE   1 
ATOM   5638 N  NZ   . LYS   B 1 368 ? -2.90522  12.99061  72.67025  1.000 68.72617  ? 368 LYS   B NZ   1 
ATOM   5639 N  N    . TYR   B 1 369 ? -3.33942  8.15684   66.53931  1.000 56.09635  ? 369 TYR   B N    1 
ATOM   5640 C  CA   . TYR   B 1 369 ? -3.96591  7.52134   65.38358  1.000 51.92450  ? 369 TYR   B CA   1 
ATOM   5641 C  C    . TYR   B 1 369 ? -4.29654  6.06875   65.68023  1.000 63.14198  ? 369 TYR   B C    1 
ATOM   5642 O  O    . TYR   B 1 369 ? -3.50311  5.34956   66.29583  1.000 62.54442  ? 369 TYR   B O    1 
ATOM   5643 C  CB   . TYR   B 1 369 ? -3.04685  7.54616   64.17735  1.000 50.63520  ? 369 TYR   B CB   1 
ATOM   5644 C  CG   . TYR   B 1 369 ? -2.75686  8.88654   63.58623  1.000 45.81148  ? 369 TYR   B CG   1 
ATOM   5645 C  CD1  . TYR   B 1 369 ? -3.52630  10.00331  63.89201  1.000 46.65002  ? 369 TYR   B CD1  1 
ATOM   5646 C  CD2  . TYR   B 1 369 ? -1.67739  9.02897   62.70993  1.000 42.03186  ? 369 TYR   B CD2  1 
ATOM   5647 C  CE1  . TYR   B 1 369 ? -3.23065  11.24229  63.30704  1.000 46.93087  ? 369 TYR   B CE1  1 
ATOM   5648 C  CE2  . TYR   B 1 369 ? -1.38452  10.22952  62.13103  1.000 43.18334  ? 369 TYR   B CE2  1 
ATOM   5649 C  CZ   . TYR   B 1 369 ? -2.15111  11.33764  62.44025  1.000 44.09970  ? 369 TYR   B CZ   1 
ATOM   5650 O  OH   . TYR   B 1 369 ? -1.79112  12.52690  61.84586  1.000 42.77880  ? 369 TYR   B OH   1 
ATOM   5651 N  N    . LYS   B 1 370 ? -5.45740  5.62187   65.20720  1.000 57.68293  ? 370 LYS   B N    1 
ATOM   5652 C  CA   . LYS   B 1 370 ? -5.82244  4.21510   65.34271  1.000 64.55778  ? 370 LYS   B CA   1 
ATOM   5653 C  C    . LYS   B 1 370 ? -5.12894  3.39717   64.25824  1.000 61.56254  ? 370 LYS   B C    1 
ATOM   5654 O  O    . LYS   B 1 370 ? -5.03894  3.82694   63.10247  1.000 61.53604  ? 370 LYS   B O    1 
ATOM   5655 C  CB   . LYS   B 1 370 ? -7.34097  4.02351   65.22767  1.000 72.75850  ? 370 LYS   B CB   1 
ATOM   5656 C  CG   . LYS   B 1 370 ? -8.13895  4.38780   66.47293  1.000 82.93609  ? 370 LYS   B CG   1 
ATOM   5657 C  CD   . LYS   B 1 370 ? -7.88157  5.83827   66.89512  1.000 85.14068  ? 370 LYS   B CD   1 
ATOM   5658 C  CE   . LYS   B 1 370 ? -8.79255  6.28058   68.05330  1.000 82.92163  ? 370 LYS   B CE   1 
ATOM   5659 N  NZ   . LYS   B 1 370 ? -8.54388  7.72401   68.40943  1.000 80.98851  ? 370 LYS   B NZ   1 
ATOM   5660 N  N    . VAL   B 1 371 ? -4.61934  2.22793   64.63385  1.000 59.98269  ? 371 VAL   B N    1 
ATOM   5661 C  CA   . VAL   B 1 371 ? -3.87203  1.37327   63.71030  1.000 64.80954  ? 371 VAL   B CA   1 
ATOM   5662 C  C    . VAL   B 1 371 ? -4.83462  0.37368   63.07357  1.000 65.40884  ? 371 VAL   B C    1 
ATOM   5663 O  O    . VAL   B 1 371 ? -5.54321  -0.34645  63.78595  1.000 68.25891  ? 371 VAL   B O    1 
ATOM   5664 C  CB   . VAL   B 1 371 ? -2.71883  0.65472   64.42982  1.000 67.28036  ? 371 VAL   B CB   1 
ATOM   5665 C  CG1  . VAL   B 1 371 ? -2.26969  -0.56036  63.62120  1.000 68.20828  ? 371 VAL   B CG1  1 
ATOM   5666 C  CG2  . VAL   B 1 371 ? -1.53602  1.61847   64.63966  1.000 57.68843  ? 371 VAL   B CG2  1 
ATOM   5667 N  N    . THR   B 1 372 ? -4.87260  0.33917   61.73236  1.000 60.99361  ? 372 THR   B N    1 
ATOM   5668 C  CA   . THR   B 1 372 ? -5.80238  -0.50279  60.97021  1.000 70.60277  ? 372 THR   B CA   1 
ATOM   5669 C  C    . THR   B 1 372 ? -5.03687  -1.35293  59.95607  1.000 71.54960  ? 372 THR   B C    1 
ATOM   5670 O  O    . THR   B 1 372 ? -3.82177  -1.20321  59.75500  1.000 49.81150  ? 372 THR   B O    1 
ATOM   5671 C  CB   . THR   B 1 372 ? -6.85779  0.30716   60.18482  1.000 56.17362  ? 372 THR   B CB   1 
ATOM   5672 O  OG1  . THR   B 1 372 ? -6.20414  1.03413   59.12743  1.000 60.51514  ? 372 THR   B OG1  1 
ATOM   5673 C  CG2  . THR   B 1 372 ? -7.64224  1.28313   61.09138  1.000 58.35084  ? 372 THR   B CG2  1 
ATOM   5674 N  N    . LYS   B 1 373 ? -5.80440  -2.20673  59.27514  1.000 86.71744  ? 373 LYS   B N    1 
ATOM   5675 C  CA   . LYS   B 1 373 ? -5.35466  -3.06911  58.18086  1.000 83.14252  ? 373 LYS   B CA   1 
ATOM   5676 C  C    . LYS   B 1 373 ? -6.58408  -3.42592  57.31283  1.000 85.05237  ? 373 LYS   B C    1 
ATOM   5677 O  O    . LYS   B 1 373 ? -7.70454  -3.06525  57.66629  1.000 71.19708  ? 373 LYS   B O    1 
ATOM   5678 C  CB   . LYS   B 1 373 ? -4.68789  -4.32695  58.73170  1.000 83.95046  ? 373 LYS   B CB   1 
ATOM   5679 C  CG   . LYS   B 1 373 ? -5.59640  -5.09910  59.69225  1.000 92.72107  ? 373 LYS   B CG   1 
ATOM   5680 C  CD   . LYS   B 1 373 ? -4.79960  -5.87430  60.73156  1.000 98.59692  ? 373 LYS   B CD   1 
ATOM   5681 C  CE   . LYS   B 1 373 ? -3.93467  -6.94443  60.08384  1.000 101.09302 ? 373 LYS   B CE   1 
ATOM   5682 N  NZ   . LYS   B 1 373 ? -4.74875  -7.93193  59.31998  1.000 107.69266 ? 373 LYS   B NZ   1 
ATOM   5683 O  OXT  . LYS   B 1 373 ? -6.54041  -4.06229  56.25218  1.000 88.00282  ? 373 LYS   B OXT  1 
HETATM 5684 C  C02  . A1AZG C 2 .   ? -17.83684 -2.23649  21.89279  1.000 42.20249  ? 401 A1AZG A C02  1 
HETATM 5685 C  C03  . A1AZG C 2 .   ? -18.26666 -1.79676  20.39306  1.000 36.55889  ? 401 A1AZG A C03  1 
HETATM 5686 C  C05  . A1AZG C 2 .   ? -16.57703 -0.38301  21.09697  1.000 35.37045  ? 401 A1AZG A C05  1 
HETATM 5687 C  C06  . A1AZG C 2 .   ? -17.31501 -0.93652  22.44016  1.000 39.42416  ? 401 A1AZG A C06  1 
HETATM 5688 C  C08  . A1AZG C 2 .   ? -15.13497 -0.71817  21.03050  1.000 36.89053  ? 401 A1AZG A C08  1 
HETATM 5689 C  C12  . A1AZG C 2 .   ? -13.37171 -2.34294  24.05682  1.000 35.90046  ? 401 A1AZG A C12  1 
HETATM 5690 C  C13  . A1AZG C 2 .   ? -13.16407 -1.54483  25.37066  1.000 37.24553  ? 401 A1AZG A C13  1 
HETATM 5691 C  C15  . A1AZG C 2 .   ? -12.16805 -0.25749  25.08441  1.000 38.09126  ? 401 A1AZG A C15  1 
HETATM 5692 C  C16  . A1AZG C 2 .   ? -12.34378 0.68885   26.15985  1.000 36.80929  ? 401 A1AZG A C16  1 
HETATM 5693 C  C17  . A1AZG C 2 .   ? -11.36897 0.95963   27.14783  1.000 31.19949  ? 401 A1AZG A C17  1 
HETATM 5694 C  C18  . A1AZG C 2 .   ? -11.60634 1.83167   28.20030  1.000 30.08995  ? 401 A1AZG A C18  1 
HETATM 5695 C  C19  . A1AZG C 2 .   ? -12.79402 2.50404   28.29867  1.000 31.23295  ? 401 A1AZG A C19  1 
HETATM 5696 C  C20  . A1AZG C 2 .   ? -13.79313 2.26389   27.34206  1.000 33.24663  ? 401 A1AZG A C20  1 
HETATM 5697 C  C21  . A1AZG C 2 .   ? -13.53751 1.35005   26.28278  1.000 35.06934  ? 401 A1AZG A C21  1 
HETATM 5698 C  C27  . A1AZG C 2 .   ? -19.54036 -3.34543  18.82529  1.000 38.60747  ? 401 A1AZG A C27  1 
HETATM 5699 C  C29  . A1AZG C 2 .   ? -21.67365 -3.28569  18.08027  1.000 39.29279  ? 401 A1AZG A C29  1 
HETATM 5700 C  C31  . A1AZG C 2 .   ? -20.30666 -5.09952  17.35149  1.000 39.97715  ? 401 A1AZG A C31  1 
HETATM 5701 C  C33  . A1AZG C 2 .   ? -19.25284 -4.54782  18.13653  1.000 42.45684  ? 401 A1AZG A C33  1 
HETATM 5702 C  C34  . A1AZG C 2 .   ? -17.84610 -4.84952  18.45694  1.000 41.26408  ? 401 A1AZG A C34  1 
HETATM 5703 C  C35  . A1AZG C 2 .   ? -17.01444 -6.03631  17.92655  1.000 53.73806  ? 401 A1AZG A C35  1 
HETATM 5704 C  C36  . A1AZG C 2 .   ? -16.76683 -7.18605  18.91707  1.000 58.01849  ? 401 A1AZG A C36  1 
HETATM 5705 C  C37  . A1AZG C 2 .   ? -15.51702 -5.56038  17.36954  1.000 54.36147  ? 401 A1AZG A C37  1 
HETATM 5706 N  N11  . A1AZG C 2 .   ? -12.96967 -1.83477  22.80914  1.000 38.08209  ? 401 A1AZG A N11  1 
HETATM 5707 N  N14  . A1AZG C 2 .   ? -12.82936 -2.47237  26.44535  1.000 35.10352  ? 401 A1AZG A N14  1 
HETATM 5708 N  N26  . A1AZG C 2 .   ? -18.39930 -2.95931  19.50734  1.000 43.44125  ? 401 A1AZG A N26  1 
HETATM 5709 N  N28  . A1AZG C 2 .   ? -20.73574 -2.69609  18.84812  1.000 41.85336  ? 401 A1AZG A N28  1 
HETATM 5710 N  N30  . A1AZG C 2 .   ? -21.50998 -4.45584  17.36855  1.000 40.83323  ? 401 A1AZG A N30  1 
HETATM 5711 N  N32  . A1AZG C 2 .   ? -20.20698 -6.25441  16.62207  1.000 44.87358  ? 401 A1AZG A N32  1 
HETATM 5712 N  N38  . A1AZG C 2 .   ? -17.38018 -3.86279  19.27976  1.000 40.43935  ? 401 A1AZG A N38  1 
HETATM 5713 O  O01  . A1AZG C 2 .   ? -18.92248 -2.65426  22.68652  1.000 42.62304  ? 401 A1AZG A O01  1 
HETATM 5714 O  O04  . A1AZG C 2 .   ? -17.21261 -0.98663  19.96331  1.000 39.62227  ? 401 A1AZG A O04  1 
HETATM 5715 O  O07  . A1AZG C 2 .   ? -18.40667 -0.10322  22.74104  1.000 38.60714  ? 401 A1AZG A O07  1 
HETATM 5716 O  O09  . A1AZG C 2 .   ? -14.82437 -2.03872  21.05472  1.000 38.30174  ? 401 A1AZG A O09  1 
HETATM 5717 O  O22  . A1AZG C 2 .   ? -13.00196 3.35624   29.27473  1.000 30.04965  ? 401 A1AZG A O22  1 
HETATM 5718 O  O23  . A1AZG C 2 .   ? -13.89881 -3.48858  24.02500  1.000 39.86115  ? 401 A1AZG A O23  1 
HETATM 5719 O  O24  . A1AZG C 2 .   ? -12.44565 -1.64344  20.32371  1.000 36.55908  ? 401 A1AZG A O24  1 
HETATM 5720 O  O25  . A1AZG C 2 .   ? -13.18920 -3.80892  21.19734  1.000 39.07961  ? 401 A1AZG A O25  1 
HETATM 5721 S  S10  . A1AZG C 2 .   ? -13.16138 -2.41005  21.30820  1.000 38.99667  ? 401 A1AZG A S10  1 
HETATM 5722 H  H021 . A1AZG C 2 .   ? -17.09854 -2.85970  21.97900  1.000 50.69720  ? 401 A1AZG A H021 1 
HETATM 5723 H  H031 . A1AZG C 2 .   ? -19.09299 -1.28992  20.35836  1.000 43.92487  ? 401 A1AZG A H031 1 
HETATM 5724 H  H051 . A1AZG C 2 .   ? -16.61690 0.58486   21.14723  1.000 42.49875  ? 401 A1AZG A H051 1 
HETATM 5725 H  H061 . A1AZG C 2 .   ? -16.73691 -1.17334  23.18220  1.000 47.36320  ? 401 A1AZG A H061 1 
HETATM 5726 H  H082 . A1AZG C 2 .   ? -14.80922 -0.31651  20.20986  1.000 44.32285  ? 401 A1AZG A H082 1 
HETATM 5727 H  H081 . A1AZG C 2 .   ? -14.72528 -0.26787  21.78567  1.000 44.32285  ? 401 A1AZG A H081 1 
HETATM 5728 H  H131 . A1AZG C 2 .   ? -13.97239 -1.13595  25.71756  1.000 44.74885  ? 401 A1AZG A H131 1 
HETATM 5729 H  H151 . A1AZG C 2 .   ? -12.36013 0.10936   24.20724  1.000 45.76373  ? 401 A1AZG A H151 1 
HETATM 5730 H  H152 . A1AZG C 2 .   ? -11.25557 -0.57183  24.98714  1.000 45.76373  ? 401 A1AZG A H152 1 
HETATM 5731 H  H171 . A1AZG C 2 .   ? -10.54053 0.54065   27.09262  1.000 37.49360  ? 401 A1AZG A H171 1 
HETATM 5732 H  H181 . A1AZG C 2 .   ? -10.94446 1.95441   28.84198  1.000 36.16216  ? 401 A1AZG A H181 1 
HETATM 5733 H  H201 . A1AZG C 2 .   ? -14.61879 2.68963   27.38615  1.000 39.95017  ? 401 A1AZG A H201 1 
HETATM 5734 H  H211 . A1AZG C 2 .   ? -14.20510 1.19793   25.65343  1.000 42.13742  ? 401 A1AZG A H211 1 
HETATM 5735 H  H291 . A1AZG C 2 .   ? -22.49967 -2.86122  18.03097  1.000 47.20556  ? 401 A1AZG A H291 1 
HETATM 5736 H  H351 . A1AZG C 2 .   ? -17.49833 -6.43550  17.18669  1.000 64.53989  ? 401 A1AZG A H351 1 
HETATM 5737 H  H362 . A1AZG C 2 .   ? -16.00268 -7.03988  19.49639  1.000 69.67640  ? 401 A1AZG A H362 1 
HETATM 5738 H  H363 . A1AZG C 2 .   ? -16.59875 -8.03864  18.48609  1.000 69.67640  ? 401 A1AZG A H363 1 
HETATM 5739 H  H361 . A1AZG C 2 .   ? -17.51212 -7.34763  19.51651  1.000 69.67640  ? 401 A1AZG A H361 1 
HETATM 5740 H  H373 . A1AZG C 2 .   ? -15.04320 -4.94372  17.94931  1.000 65.28798  ? 401 A1AZG A H373 1 
HETATM 5741 H  H372 . A1AZG C 2 .   ? -15.52607 -5.10590  16.51265  1.000 65.28798  ? 401 A1AZG A H372 1 
HETATM 5742 H  H371 . A1AZG C 2 .   ? -14.88249 -6.28211  17.23775  1.000 65.28798  ? 401 A1AZG A H371 1 
HETATM 5743 H  H111 . A1AZG C 2 .   ? -12.55740 -1.09052  22.93458  1.000 45.75272  ? 401 A1AZG A H111 1 
HETATM 5744 H  H142 . A1AZG C 2 .   ? -12.72941 -2.07722  27.21913  1.000 42.17844  ? 401 A1AZG A H142 1 
HETATM 5745 H  H141 . A1AZG C 2 .   ? -13.41226 -3.12826  26.57683  1.000 42.17844  ? 401 A1AZG A H141 1 
HETATM 5746 H  H321 . A1AZG C 2 .   ? -20.88730 -6.76057  16.41484  1.000 53.90251  ? 401 A1AZG A H321 1 
HETATM 5747 H  H322 . A1AZG C 2 .   ? -19.50310 -6.61075  16.30797  1.000 53.90251  ? 401 A1AZG A H322 1 
HETATM 5748 H  H011 . A1AZG C 2 .   ? -19.24694 -3.39122  22.42237  1.000 51.20186  ? 401 A1AZG A H011 1 
HETATM 5749 H  H071 . A1AZG C 2 .   ? -19.13281 -0.36471  22.40110  1.000 46.38278  ? 401 A1AZG A H071 1 
HETATM 5750 H  H221 . A1AZG C 2 .   ? -12.99794 4.16856   29.04411  1.000 36.11379  ? 401 A1AZG A H221 1 
HETATM 5751 C  C1   . MLI   D 3 .   ? -28.52398 12.48581  39.04771  1.000 56.22978  ? 402 MLI   A C1   1 
HETATM 5752 C  C2   . MLI   D 3 .   ? -27.12861 12.01126  38.61475  1.000 58.15095  ? 402 MLI   A C2   1 
HETATM 5753 C  C3   . MLI   D 3 .   ? -29.03226 11.77775  40.34164  1.000 65.79598  ? 402 MLI   A C3   1 
HETATM 5754 O  O6   . MLI   D 3 .   ? -26.48198 12.79056  37.86473  1.000 53.70054  ? 402 MLI   A O6   1 
HETATM 5755 O  O7   . MLI   D 3 .   ? -26.73510 10.88949  39.02961  1.000 54.34847  ? 402 MLI   A O7   1 
HETATM 5756 O  O8   . MLI   D 3 .   ? -28.49045 10.67412  40.64745  1.000 65.05808  ? 402 MLI   A O8   1 
HETATM 5757 O  O9   . MLI   D 3 .   ? -29.94656 12.34811  40.99256  1.000 58.12336  ? 402 MLI   A O9   1 
HETATM 5758 H  H11  . MLI   D 3 .   ? -29.16778 12.32601  38.33997  1.000 67.52995  ? 402 MLI   A H11  1 
HETATM 5759 H  H12  . MLI   D 3 .   ? -28.51930 13.44282  39.20585  1.000 67.52995  ? 402 MLI   A H12  1 
HETATM 5760 CL CL   . CL    E 4 .   ? -3.57237  14.71763  38.81289  1.000 58.32424  ? 403 CL    A CL   1 
HETATM 5761 NA NA   . NA    F 5 .   ? -13.91423 -5.50076  22.79270  1.000 40.57598  ? 404 NA    A NA   1 
HETATM 5762 C  C02  . A1AZG G 2 .   ? 10.30639  -5.56423  55.97352  1.000 31.60983  ? 401 A1AZG B C02  1 
HETATM 5763 C  C03  . A1AZG G 2 .   ? 11.06863  -4.89314  57.19318  1.000 28.78060  ? 401 A1AZG B C03  1 
HETATM 5764 C  C05  . A1AZG G 2 .   ? 10.49262  -3.22544  55.73563  1.000 30.39186  ? 401 A1AZG B C05  1 
HETATM 5765 C  C06  . A1AZG G 2 .   ? 10.59707  -4.58138  54.91012  1.000 31.61282  ? 401 A1AZG B C06  1 
HETATM 5766 C  C08  . A1AZG G 2 .   ? 9.16652   -2.55458  55.72505  1.000 29.37396  ? 401 A1AZG B C08  1 
HETATM 5767 C  C12  . A1AZG G 2 .   ? 6.50390   -3.72916  53.27356  1.000 31.37176  ? 401 A1AZG B C12  1 
HETATM 5768 C  C13  . A1AZG G 2 .   ? 6.69567   -3.40098  51.83312  1.000 32.98703  ? 401 A1AZG B C13  1 
HETATM 5769 C  C15  . A1AZG G 2 .   ? 6.69099   -1.84182  51.55363  1.000 27.99780  ? 401 A1AZG B C15  1 
HETATM 5770 C  C16  . A1AZG G 2 .   ? 7.28963   -1.57413  50.22174  1.000 29.21981  ? 401 A1AZG B C16  1 
HETATM 5771 C  C17  . A1AZG G 2 .   ? 6.56784   -1.07329  49.12973  1.000 28.41972  ? 401 A1AZG B C17  1 
HETATM 5772 C  C18  . A1AZG G 2 .   ? 7.16314   -0.86893  47.89640  1.000 25.39780  ? 401 A1AZG B C18  1 
HETATM 5773 C  C19  . A1AZG G 2 .   ? 8.52197   -1.13060  47.69413  1.000 29.63491  ? 401 A1AZG B C19  1 
HETATM 5774 C  C20  . A1AZG G 2 .   ? 9.24817   -1.64740  48.73292  1.000 28.62648  ? 401 A1AZG B C20  1 
HETATM 5775 C  C21  . A1AZG G 2 .   ? 8.62671   -1.86748  49.95361  1.000 24.69741  ? 401 A1AZG B C21  1 
HETATM 5776 C  C27  . A1AZG G 2 .   ? 11.21161  -6.26990  59.31450  1.000 31.85210  ? 401 A1AZG B C27  1 
HETATM 5777 C  C29  . A1AZG G 2 .   ? 12.90901  -7.43699  60.22781  1.000 32.67071  ? 401 A1AZG B C29  1 
HETATM 5778 C  C31  . A1AZG G 2 .   ? 10.78880  -7.46397  61.31665  1.000 34.36903  ? 401 A1AZG B C31  1 
HETATM 5779 C  C33  . A1AZG G 2 .   ? 10.31367  -6.61732  60.32170  1.000 31.46700  ? 401 A1AZG B C33  1 
HETATM 5780 C  C34  . A1AZG G 2 .   ? 9.01517   -6.00028  59.94110  1.000 31.63979  ? 401 A1AZG B C34  1 
HETATM 5781 C  C35  . A1AZG G 2 .   ? 7.67947   -6.00934  60.68752  1.000 37.48930  ? 401 A1AZG B C35  1 
HETATM 5782 C  C36  . A1AZG G 2 .   ? 6.50033   -5.50450  59.87517  1.000 39.34210  ? 401 A1AZG B C36  1 
HETATM 5783 C  C37  . A1AZG G 2 .   ? 7.88815   -5.05454  62.01980  1.000 44.13125  ? 401 A1AZG B C37  1 
HETATM 5784 N  N11  . A1AZG G 2 .   ? 6.58040   -2.72834  54.18773  1.000 32.58341  ? 401 A1AZG B N11  1 
HETATM 5785 N  N14  . A1AZG G 2 .   ? 5.83784   -4.07201  51.07385  1.000 30.18033  ? 401 A1AZG B N14  1 
HETATM 5786 N  N26  . A1AZG G 2 .   ? 10.53024  -5.48469  58.38432  1.000 30.37251  ? 401 A1AZG B N26  1 
HETATM 5787 N  N28  . A1AZG G 2 .   ? 12.51611  -6.63984  59.22819  1.000 29.83780  ? 401 A1AZG B N28  1 
HETATM 5788 N  N30  . A1AZG G 2 .   ? 12.11899  -7.88693  61.26160  1.000 33.26227  ? 401 A1AZG B N30  1 
HETATM 5789 N  N32  . A1AZG G 2 .   ? 9.98756   -7.88849  62.30067  1.000 35.35682  ? 401 A1AZG B N32  1 
HETATM 5790 N  N38  . A1AZG G 2 .   ? 9.21023   -5.31732  58.76501  1.000 34.86743  ? 401 A1AZG B N38  1 
HETATM 5791 O  O01  . A1AZG G 2 .   ? 10.78680  -6.82964  55.54442  1.000 33.52764  ? 401 A1AZG B O01  1 
HETATM 5792 O  O04  . A1AZG G 2 .   ? 10.75771  -3.54852  57.10913  1.000 29.83616  ? 401 A1AZG B O04  1 
HETATM 5793 O  O07  . A1AZG G 2 .   ? 11.93000  -4.66032  54.38350  1.000 32.29891  ? 401 A1AZG B O07  1 
HETATM 5794 O  O09  . A1AZG G 2 .   ? 8.15807   -3.29370  56.12941  1.000 32.30600  ? 401 A1AZG B O09  1 
HETATM 5795 O  O22  . A1AZG G 2 .   ? 9.10088   -0.93363  46.49702  1.000 28.70444  ? 401 A1AZG B O22  1 
HETATM 5796 O  O23  . A1AZG G 2 .   ? 6.23051   -4.88212  53.68481  1.000 33.07895  ? 401 A1AZG B O23  1 
HETATM 5797 O  O24  . A1AZG G 2 .   ? 6.50666   -1.39200  56.32162  1.000 32.24233  ? 401 A1AZG B O24  1 
HETATM 5798 O  O25  . A1AZG G 2 .   ? 5.68595   -3.61668  56.38644  1.000 31.77933  ? 401 A1AZG B O25  1 
HETATM 5799 S  S10  . A1AZG G 2 .   ? 6.57984   -2.70583  55.80031  1.000 33.82925  ? 401 A1AZG B S10  1 
HETATM 5800 H  H021 . A1AZG G 2 .   ? 9.34142   -5.61746  56.05654  1.000 37.98601  ? 401 A1AZG B H021 1 
HETATM 5801 H  H031 . A1AZG G 2 .   ? 12.03715  -4.94613  57.18517  1.000 34.59093  ? 401 A1AZG B H031 1 
HETATM 5802 H  H051 . A1AZG G 2 .   ? 11.08620  -2.61083  55.27649  1.000 36.52444  ? 401 A1AZG B H051 1 
HETATM 5803 H  H061 . A1AZG G 2 .   ? 9.88847   -4.79731  54.28389  1.000 37.98959  ? 401 A1AZG B H061 1 
HETATM 5804 H  H082 . A1AZG G 2 .   ? 9.25741   -1.77397  56.29363  1.000 35.30297  ? 401 A1AZG B H082 1 
HETATM 5805 H  H081 . A1AZG G 2 .   ? 9.02167   -2.26332  54.81122  1.000 35.30297  ? 401 A1AZG B H081 1 
HETATM 5806 H  H131 . A1AZG G 2 .   ? 7.57397   -3.71779  51.57021  1.000 39.63865  ? 401 A1AZG B H131 1 
HETATM 5807 H  H151 . A1AZG G 2 .   ? 7.15124   -1.39168  52.27919  1.000 33.65157  ? 401 A1AZG B H151 1 
HETATM 5808 H  H152 . A1AZG G 2 .   ? 5.78358   -1.51025  51.64064  1.000 33.65157  ? 401 A1AZG B H152 1 
HETATM 5809 H  H171 . A1AZG G 2 .   ? 5.66577   -0.87222  49.23337  1.000 34.15788  ? 401 A1AZG B H171 1 
HETATM 5810 H  H181 . A1AZG G 2 .   ? 6.64146   -0.55138  47.19504  1.000 30.53158  ? 401 A1AZG B H181 1 
HETATM 5811 H  H201 . A1AZG G 2 .   ? 10.14987  -1.85436  48.63802  1.000 34.40598  ? 401 A1AZG B H201 1 
HETATM 5812 H  H211 . A1AZG G 2 .   ? 9.13839   -2.23548  50.63746  1.000 29.69111  ? 401 A1AZG B H211 1 
HETATM 5813 H  H291 . A1AZG G 2 .   ? 13.79858  -7.70799  60.21678  1.000 39.25906  ? 401 A1AZG B H291 1 
HETATM 5814 H  H351 . A1AZG G 2 .   ? 7.38483   -6.89295  60.95830  1.000 45.04137  ? 401 A1AZG B H351 1 
HETATM 5815 H  H362 . A1AZG G 2 .   ? 5.67900   -5.43610  60.38666  1.000 47.26473  ? 401 A1AZG B H362 1 
HETATM 5816 H  H363 . A1AZG G 2 .   ? 6.28125   -6.07031  59.11836  1.000 47.26473  ? 401 A1AZG B H363 1 
HETATM 5817 H  H361 . A1AZG G 2 .   ? 6.63922   -4.62110  59.49938  1.000 47.26473  ? 401 A1AZG B H361 1 
HETATM 5818 H  H373 . A1AZG G 2 .   ? 8.56924   -5.36106  62.63872  1.000 53.01171  ? 401 A1AZG B H373 1 
HETATM 5819 H  H372 . A1AZG G 2 .   ? 7.10113   -4.95557  62.57809  1.000 53.01171  ? 401 A1AZG B H372 1 
HETATM 5820 H  H371 . A1AZG G 2 .   ? 8.14867   -4.13979  61.82936  1.000 53.01171  ? 401 A1AZG B H371 1 
HETATM 5821 H  H111 . A1AZG G 2 .   ? 6.63869   -1.98672  53.75623  1.000 39.15431  ? 401 A1AZG B H111 1 
HETATM 5822 H  H142 . A1AZG G 2 .   ? 5.34289   -4.68368  51.52152  1.000 36.27060  ? 401 A1AZG B H142 1 
HETATM 5823 H  H141 . A1AZG G 2 .   ? 6.19024   -4.48161  50.38653  1.000 36.27060  ? 401 A1AZG B H141 1 
HETATM 5824 H  H321 . A1AZG G 2 .   ? 9.90831   -8.71382  62.53537  1.000 42.48240  ? 401 A1AZG B H321 1 
HETATM 5825 H  H322 . A1AZG G 2 .   ? 9.45121   -7.41269  62.78291  1.000 42.48240  ? 401 A1AZG B H322 1 
HETATM 5826 H  H011 . A1AZG G 2 .   ? 10.23508  -7.47615  55.73647  1.000 40.28738  ? 401 A1AZG B H011 1 
HETATM 5827 H  H071 . A1AZG G 2 .   ? 12.47559  -5.12282  54.86510  1.000 38.81291  ? 401 A1AZG B H071 1 
HETATM 5828 H  H221 . A1AZG G 2 .   ? 9.38641   -0.14825  46.35065  1.000 34.49954  ? 401 A1AZG B H221 1 
HETATM 5829 C  C1   . MLI   H 3 .   ? 25.69262  -6.75692  36.10816  1.000 58.19182  ? 402 MLI   B C1   1 
HETATM 5830 C  C2   . MLI   H 3 .   ? 24.39989  -6.16480  36.66730  1.000 55.62621  ? 402 MLI   B C2   1 
HETATM 5831 C  C3   . MLI   H 3 .   ? 25.64614  -8.03011  35.21971  1.000 69.88618  ? 402 MLI   B C3   1 
HETATM 5832 O  O6   . MLI   H 3 .   ? 23.32768  -6.85176  36.67236  1.000 51.62750  ? 402 MLI   B O6   1 
HETATM 5833 O  O7   . MLI   H 3 .   ? 24.52657  -4.98825  37.11466  1.000 57.51275  ? 402 MLI   B O7   1 
HETATM 5834 O  O8   . MLI   H 3 .   ? 26.59960  -8.25006  34.40162  1.000 58.35471  ? 402 MLI   B O8   1 
HETATM 5835 O  O9   . MLI   H 3 .   ? 24.63514  -8.75355  35.42027  1.000 70.44620  ? 402 MLI   B O9   1 
HETATM 5836 H  H11  . MLI   H 3 .   ? 26.28185  -6.96578  36.84984  1.000 69.88439  ? 402 MLI   B H11  1 
HETATM 5837 H  H12  . MLI   H 3 .   ? 26.14110  -6.07621  35.58241  1.000 69.88439  ? 402 MLI   B H12  1 
HETATM 5838 CL CL   . CL    I 4 .   ? 7.40332   9.84257   32.43286  1.000 49.23259  ? 403 CL    B CL   1 
HETATM 5839 NA NA   . NA    J 5 .   ? 27.27067  -8.65305  89.03900  1.000 37.93603  ? 404 NA    B NA   1 
HETATM 5840 NA NA   . NA    K 5 .   ? 20.61848  12.12708  53.33627  1.000 48.75415  ? 405 NA    B NA   1 
HETATM 5841 NA NA   . NA    L 5 .   ? 5.05300   -5.79724  55.50746  1.000 34.33746  ? 406 NA    B NA   1 
HETATM 5842 O  O    . HOH   M 6 .   ? -42.84803 19.98854  24.02550  1.000 69.12809  ? 501 HOH   A O    1 
HETATM 5843 O  O    . HOH   M 6 .   ? -22.55800 -9.35087  24.16108  1.000 57.24426  ? 502 HOH   A O    1 
HETATM 5844 O  O    . HOH   M 6 .   ? -25.45460 18.50729  22.42067  1.000 50.33867  ? 503 HOH   A O    1 
HETATM 5845 O  O    . HOH   M 6 .   ? -47.90028 24.17759  26.81987  1.000 71.24171  ? 504 HOH   A O    1 
HETATM 5846 O  O    . HOH   M 6 .   ? -34.50743 0.45722   23.01139  1.000 61.34008  ? 505 HOH   A O    1 
HETATM 5847 O  O    . HOH   M 6 .   ? -10.66366 17.82784  23.52885  1.000 62.48254  ? 506 HOH   A O    1 
HETATM 5848 O  O    . HOH   M 6 .   ? -2.84834  -8.66338  28.25033  1.000 46.68967  ? 507 HOH   A O    1 
HETATM 5849 O  O    . HOH   M 6 .   ? -11.87304 14.34276  36.39823  1.000 52.41281  ? 508 HOH   A O    1 
HETATM 5850 O  O    . HOH   M 6 .   ? -21.43410 -7.90462  11.22102  1.000 55.52317  ? 509 HOH   A O    1 
HETATM 5851 O  O    . HOH   M 6 .   ? -7.54712  8.10606   46.90308  1.000 63.45659  ? 510 HOH   A O    1 
HETATM 5852 O  O    . HOH   M 6 .   ? -11.03524 -2.58034  18.46953  1.000 39.41490  ? 511 HOH   A O    1 
HETATM 5853 O  O    . HOH   M 6 .   ? 1.56533   9.93844   3.54461   1.000 70.14987  ? 512 HOH   A O    1 
HETATM 5854 O  O    . HOH   M 6 .   ? -27.01497 -1.44022  29.49195  1.000 50.33004  ? 513 HOH   A O    1 
HETATM 5855 O  O    . HOH   M 6 .   ? -21.87118 17.80905  17.96121  1.000 51.44669  ? 514 HOH   A O    1 
HETATM 5856 O  O    . HOH   M 6 .   ? -10.16076 -6.88132  9.09399   1.000 67.19937  ? 515 HOH   A O    1 
HETATM 5857 O  O    . HOH   M 6 .   ? -6.18291  11.12223  12.43658  1.000 53.48581  ? 516 HOH   A O    1 
HETATM 5858 O  O    . HOH   M 6 .   ? 3.19433   5.62524   15.61023  1.000 57.21927  ? 517 HOH   A O    1 
HETATM 5859 O  O    . HOH   M 6 .   ? -22.61497 -1.69418  28.24230  1.000 43.52544  ? 518 HOH   A O    1 
HETATM 5860 O  O    . HOH   M 6 .   ? -11.51910 12.23086  7.67334   1.000 56.50169  ? 519 HOH   A O    1 
HETATM 5861 O  O    . HOH   M 6 .   ? -12.66940 7.18309   44.12497  1.000 56.14866  ? 520 HOH   A O    1 
HETATM 5862 O  O    . HOH   M 6 .   ? -21.66001 18.81526  30.98055  1.000 52.03737  ? 521 HOH   A O    1 
HETATM 5863 O  O    . HOH   M 6 .   ? -27.95132 8.47855   43.33440  1.000 54.15489  ? 522 HOH   A O    1 
HETATM 5864 O  O    . HOH   M 6 .   ? -24.91059 5.80797   45.17525  1.000 53.49965  ? 523 HOH   A O    1 
HETATM 5865 O  O    . HOH   M 6 .   ? -0.45052  14.04592  28.23724  1.000 41.84768  ? 524 HOH   A O    1 
HETATM 5866 O  O    . HOH   M 6 .   ? -11.29598 -0.14253  8.53303   1.000 52.37505  ? 525 HOH   A O    1 
HETATM 5867 O  O    . HOH   M 6 .   ? -16.01132 -5.18449  21.91562  1.000 44.84083  ? 526 HOH   A O    1 
HETATM 5868 O  O    . HOH   M 6 .   ? -18.21743 15.32676  26.57355  1.000 46.98183  ? 527 HOH   A O    1 
HETATM 5869 O  O    . HOH   M 6 .   ? -22.73651 14.33016  16.47068  1.000 41.66109  ? 528 HOH   A O    1 
HETATM 5870 O  O    . HOH   M 6 .   ? -17.80964 12.94373  11.11143  1.000 48.45974  ? 529 HOH   A O    1 
HETATM 5871 O  O    . HOH   M 6 .   ? -9.86923  14.38250  29.86185  1.000 48.52370  ? 530 HOH   A O    1 
HETATM 5872 O  O    . HOH   M 6 .   ? -33.10007 19.96479  31.61151  1.000 70.05134  ? 531 HOH   A O    1 
HETATM 5873 O  O    . HOH   M 6 .   ? -50.42669 21.17632  32.24968  1.000 62.07365  ? 532 HOH   A O    1 
HETATM 5874 O  O    . HOH   M 6 .   ? -29.37746 17.44046  31.23408  1.000 56.03240  ? 533 HOH   A O    1 
HETATM 5875 O  O    . HOH   M 6 .   ? -6.25341  13.40431  24.02104  1.000 39.01192  ? 534 HOH   A O    1 
HETATM 5876 O  O    . HOH   M 6 .   ? -18.93915 9.47858   35.93729  1.000 39.40719  ? 535 HOH   A O    1 
HETATM 5877 O  O    . HOH   M 6 .   ? -34.39593 4.15350   3.54844   1.000 74.54212  ? 536 HOH   A O    1 
HETATM 5878 O  O    . HOH   M 6 .   ? 2.60049   13.72045  33.44892  1.000 63.18161  ? 537 HOH   A O    1 
HETATM 5879 O  O    . HOH   M 6 .   ? -27.95058 7.94459   37.64370  1.000 45.60325  ? 538 HOH   A O    1 
HETATM 5880 O  O    . HOH   M 6 .   ? -20.92299 14.91254  34.01556  1.000 43.83997  ? 539 HOH   A O    1 
HETATM 5881 O  O    . HOH   M 6 .   ? -14.96271 15.01014  30.47790  1.000 45.12032  ? 540 HOH   A O    1 
HETATM 5882 O  O    . HOH   M 6 .   ? -19.03809 1.27408   19.36288  1.000 40.52580  ? 541 HOH   A O    1 
HETATM 5883 O  O    . HOH   M 6 .   ? -26.63153 0.42026   40.99162  1.000 66.85067  ? 542 HOH   A O    1 
HETATM 5884 O  O    . HOH   M 6 .   ? -45.86814 27.34657  38.89432  1.000 64.56906  ? 543 HOH   A O    1 
HETATM 5885 O  O    . HOH   M 6 .   ? -15.31550 -6.77143  24.09366  1.000 43.43152  ? 544 HOH   A O    1 
HETATM 5886 O  O    . HOH   M 6 .   ? -16.88863 -5.51157  46.57146  1.000 52.15521  ? 545 HOH   A O    1 
HETATM 5887 O  O    . HOH   M 6 .   ? -11.04024 2.45600   47.74166  1.000 47.84816  ? 546 HOH   A O    1 
HETATM 5888 O  O    . HOH   M 6 .   ? -21.61536 20.55118  14.85553  1.000 56.81956  ? 547 HOH   A O    1 
HETATM 5889 O  O    . HOH   M 6 .   ? -4.37038  -6.76523  17.05236  1.000 63.69416  ? 548 HOH   A O    1 
HETATM 5890 O  O    . HOH   M 6 .   ? -11.06820 -9.87065  33.81493  1.000 48.44027  ? 549 HOH   A O    1 
HETATM 5891 O  O    . HOH   M 6 .   ? 2.03372   -9.93708  26.64162  1.000 48.27138  ? 550 HOH   A O    1 
HETATM 5892 O  O    . HOH   M 6 .   ? 0.58245   7.56505   33.85452  1.000 37.16828  ? 551 HOH   A O    1 
HETATM 5893 O  O    . HOH   M 6 .   ? -26.15727 16.63253  16.40491  1.000 50.89880  ? 552 HOH   A O    1 
HETATM 5894 O  O    . HOH   M 6 .   ? -8.70292  10.37757  42.11133  1.000 39.21598  ? 553 HOH   A O    1 
HETATM 5895 O  O    . HOH   M 6 .   ? -26.63343 -0.89877  38.96381  1.000 56.32919  ? 554 HOH   A O    1 
HETATM 5896 O  O    . HOH   M 6 .   ? -44.11651 12.62625  31.74395  1.000 72.48621  ? 555 HOH   A O    1 
HETATM 5897 O  O    . HOH   M 6 .   ? -20.86603 8.81599   37.95227  1.000 51.35476  ? 556 HOH   A O    1 
HETATM 5898 O  O    . HOH   M 6 .   ? -10.58668 -7.65607  22.00549  1.000 46.50424  ? 557 HOH   A O    1 
HETATM 5899 O  O    . HOH   M 6 .   ? -22.98400 1.15247   27.69276  1.000 46.40965  ? 558 HOH   A O    1 
HETATM 5900 O  O    . HOH   M 6 .   ? -16.98723 1.67747   30.28104  1.000 35.84092  ? 559 HOH   A O    1 
HETATM 5901 O  O    . HOH   M 6 .   ? -8.89964  -3.62829  49.99386  1.000 49.54005  ? 560 HOH   A O    1 
HETATM 5902 O  O    . HOH   M 6 .   ? -17.04811 -11.66083 31.36076  1.000 49.36301  ? 561 HOH   A O    1 
HETATM 5903 O  O    . HOH   M 6 .   ? -19.47542 -7.37139  30.05007  1.000 44.74938  ? 562 HOH   A O    1 
HETATM 5904 O  O    . HOH   M 6 .   ? -40.14994 14.01234  32.07318  1.000 69.82830  ? 563 HOH   A O    1 
HETATM 5905 O  O    . HOH   M 6 .   ? -4.55460  15.01360  20.94585  1.000 59.95161  ? 564 HOH   A O    1 
HETATM 5906 O  O    . HOH   M 6 .   ? -22.55761 10.17537  36.33530  1.000 41.28009  ? 565 HOH   A O    1 
HETATM 5907 O  O    . HOH   M 6 .   ? -6.87611  14.65283  31.73808  1.000 47.53443  ? 566 HOH   A O    1 
HETATM 5908 O  O    . HOH   M 6 .   ? -16.05119 19.66521  20.37240  1.000 59.49345  ? 567 HOH   A O    1 
HETATM 5909 O  O    . HOH   M 6 .   ? -33.73109 -1.07810  29.27508  1.000 54.76948  ? 568 HOH   A O    1 
HETATM 5910 O  O    . HOH   M 6 .   ? -33.46388 0.41543   26.31398  1.000 61.45109  ? 569 HOH   A O    1 
HETATM 5911 O  O    . HOH   M 6 .   ? -17.07554 16.09731  23.68407  1.000 48.26252  ? 570 HOH   A O    1 
HETATM 5912 O  O    . HOH   M 6 .   ? -23.73625 22.27810  30.30886  1.000 62.74544  ? 571 HOH   A O    1 
HETATM 5913 O  O    . HOH   M 6 .   ? -28.75995 9.99958   13.88563  1.000 56.18040  ? 572 HOH   A O    1 
HETATM 5914 O  O    . HOH   M 6 .   ? -32.56627 20.02979  37.86124  1.000 67.01677  ? 573 HOH   A O    1 
HETATM 5915 O  O    . HOH   M 6 .   ? -31.65112 19.33509  17.90778  1.000 64.20819  ? 574 HOH   A O    1 
HETATM 5916 O  O    . HOH   M 6 .   ? -9.94130  8.11331   44.08180  1.000 48.32579  ? 575 HOH   A O    1 
HETATM 5917 O  O    . HOH   M 6 .   ? -20.02462 18.91491  28.05898  1.000 55.67316  ? 576 HOH   A O    1 
HETATM 5918 O  O    . HOH   M 6 .   ? -29.21354 17.82560  28.28777  1.000 54.78653  ? 577 HOH   A O    1 
HETATM 5919 O  O    . HOH   M 6 .   ? -12.64694 -3.76087  17.63225  1.000 48.23715  ? 578 HOH   A O    1 
HETATM 5920 O  O    . HOH   M 6 .   ? -11.87136 -5.60018  23.91810  1.000 39.79539  ? 579 HOH   A O    1 
HETATM 5921 O  O    . HOH   M 6 .   ? -25.10161 5.48074   48.05605  1.000 61.20395  ? 580 HOH   A O    1 
HETATM 5922 O  O    . HOH   M 6 .   ? -18.42189 -8.55266  16.14328  1.000 56.75043  ? 581 HOH   A O    1 
HETATM 5923 O  O    . HOH   M 6 .   ? -11.23662 16.48887  19.80251  1.000 50.36997  ? 582 HOH   A O    1 
HETATM 5924 O  O    . HOH   M 6 .   ? -29.73762 10.02476  37.62320  1.000 47.37355  ? 583 HOH   A O    1 
HETATM 5925 O  O    . HOH   M 6 .   ? -0.11873  9.12244   13.49292  1.000 61.75521  ? 584 HOH   A O    1 
HETATM 5926 O  O    . HOH   M 6 .   ? -24.17513 19.32789  17.83036  1.000 62.22269  ? 585 HOH   A O    1 
HETATM 5927 O  O    . HOH   M 6 .   ? -23.39258 -7.49812  33.21715  1.000 53.28844  ? 586 HOH   A O    1 
HETATM 5928 O  O    . HOH   M 6 .   ? -16.10389 -7.83862  45.08223  1.000 46.08524  ? 587 HOH   A O    1 
HETATM 5929 O  O    . HOH   M 6 .   ? -31.44693 17.28361  26.58951  1.000 52.50670  ? 588 HOH   A O    1 
HETATM 5930 O  O    . HOH   M 6 .   ? -13.91457 0.54393   49.26634  1.000 46.83288  ? 589 HOH   A O    1 
HETATM 5931 O  O    . HOH   M 6 .   ? -3.95491  -18.71780 34.43545  1.000 55.88532  ? 590 HOH   A O    1 
HETATM 5932 O  O    . HOH   M 6 .   ? -19.48961 10.36799  40.43810  1.000 53.49332  ? 591 HOH   A O    1 
HETATM 5933 O  O    . HOH   M 6 .   ? -18.43601 11.30464  37.80995  1.000 52.14849  ? 592 HOH   A O    1 
HETATM 5934 O  O    . HOH   M 6 .   ? -25.28582 15.51218  38.23872  1.000 59.19068  ? 593 HOH   A O    1 
HETATM 5935 O  O    . HOH   M 6 .   ? -10.54304 -4.62643  19.77755  1.000 50.15151  ? 594 HOH   A O    1 
HETATM 5936 O  O    . HOH   M 6 .   ? -24.27582 -2.70474  39.61272  1.000 53.87915  ? 595 HOH   A O    1 
HETATM 5937 O  O    . HOH   M 6 .   ? -26.62923 -7.64653  21.78787  1.000 52.78415  ? 596 HOH   A O    1 
HETATM 5938 O  O    . HOH   M 6 .   ? -34.59812 -2.22171  24.37656  1.000 62.67653  ? 597 HOH   A O    1 
HETATM 5939 O  O    . HOH   M 6 .   ? -33.47255 17.55600  18.41620  1.000 60.26946  ? 598 HOH   A O    1 
HETATM 5940 O  O    . HOH   M 6 .   ? -28.96296 19.65592  21.60135  1.000 56.97871  ? 599 HOH   A O    1 
HETATM 5941 O  O    . HOH   M 6 .   ? -21.38214 1.77826   18.21099  1.000 44.84184  ? 600 HOH   A O    1 
HETATM 5942 O  O    . HOH   M 6 .   ? -5.49610  5.79017   45.77480  1.000 48.38043  ? 601 HOH   A O    1 
HETATM 5943 O  O    . HOH   M 6 .   ? 1.47721   11.32475  27.34537  1.000 46.84890  ? 602 HOH   A O    1 
HETATM 5944 O  O    . HOH   M 6 .   ? 5.67073   -0.87034  22.14056  1.000 57.04270  ? 603 HOH   A O    1 
HETATM 5945 O  O    . HOH   M 6 .   ? -16.67394 -12.69276 43.77357  1.000 57.98396  ? 604 HOH   A O    1 
HETATM 5946 O  O    . HOH   M 6 .   ? -14.32498 13.17496  38.63463  1.000 58.51496  ? 605 HOH   A O    1 
HETATM 5947 O  O    . HOH   M 6 .   ? -34.15835 -1.74964  21.37194  1.000 69.32633  ? 606 HOH   A O    1 
HETATM 5948 O  O    . HOH   M 6 .   ? -4.29329  -10.17756 21.29861  1.000 62.36767  ? 607 HOH   A O    1 
HETATM 5949 O  O    . HOH   M 6 .   ? -25.74941 19.04256  37.59019  1.000 63.82959  ? 608 HOH   A O    1 
HETATM 5950 O  O    . HOH   M 6 .   ? -6.25000  -17.12290 37.55141  1.000 55.99737  ? 609 HOH   A O    1 
HETATM 5951 O  O    . HOH   M 6 .   ? -11.55202 -13.53629 44.98003  1.000 44.52187  ? 610 HOH   A O    1 
HETATM 5952 O  O    . HOH   M 6 .   ? -0.68731  6.21474   20.77221  1.000 56.09303  ? 611 HOH   A O    1 
HETATM 5953 O  O    . HOH   M 6 .   ? -31.37050 9.40409   39.65355  1.000 55.46930  ? 612 HOH   A O    1 
HETATM 5954 O  O    . HOH   M 6 .   ? -39.29522 9.00064   21.08879  1.000 63.73062  ? 613 HOH   A O    1 
HETATM 5955 O  O    . HOH   M 6 .   ? -13.05521 -7.16631  21.26321  1.000 46.08577  ? 614 HOH   A O    1 
HETATM 5956 O  O    . HOH   M 6 .   ? -16.35983 16.40570  28.35448  1.000 54.32176  ? 615 HOH   A O    1 
HETATM 5957 O  O    . HOH   M 6 .   ? -20.57370 17.61295  33.51037  1.000 55.10323  ? 616 HOH   A O    1 
HETATM 5958 O  O    . HOH   M 6 .   ? -17.67533 18.90500  23.37913  1.000 49.46737  ? 617 HOH   A O    1 
HETATM 5959 O  O    . HOH   M 6 .   ? -44.04166 27.71588  40.40107  1.000 66.90156  ? 618 HOH   A O    1 
HETATM 5960 O  O    . HOH   M 6 .   ? -35.14371 1.04584   28.75907  1.000 61.14285  ? 619 HOH   A O    1 
HETATM 5961 O  O    . HOH   M 6 .   ? -24.87079 -9.61146  23.05841  1.000 64.61122  ? 620 HOH   A O    1 
HETATM 5962 O  O    . HOH   M 6 .   ? -27.57400 6.35750   44.91994  1.000 58.85985  ? 621 HOH   A O    1 
HETATM 5963 O  O    . HOH   M 6 .   ? -24.96720 27.43122  18.27468  1.000 69.15945  ? 622 HOH   A O    1 
HETATM 5964 O  O    . HOH   M 6 .   ? -12.22630 15.13132  29.80040  1.000 55.19741  ? 623 HOH   A O    1 
HETATM 5965 O  O    . HOH   N 6 .   ? 25.62669  -13.49525 55.44559  1.000 56.82068  ? 501 HOH   B O    1 
HETATM 5966 O  O    . HOH   N 6 .   ? 30.59711  -12.34167 54.85616  1.000 59.78818  ? 502 HOH   B O    1 
HETATM 5967 O  O    . HOH   N 6 .   ? 18.94924  -9.65342  86.13937  1.000 49.58866  ? 503 HOH   B O    1 
HETATM 5968 O  O    . HOH   N 6 .   ? -8.99630  -15.98397 50.31152  1.000 73.32511  ? 504 HOH   B O    1 
HETATM 5969 O  O    . HOH   N 6 .   ? 34.98814  -0.28961  52.00676  1.000 59.42513  ? 505 HOH   B O    1 
HETATM 5970 O  O    . HOH   N 6 .   ? 17.37359  -12.73353 49.47184  1.000 42.52742  ? 506 HOH   B O    1 
HETATM 5971 O  O    . HOH   N 6 .   ? 23.42360  -17.51076 67.34882  1.000 45.03433  ? 507 HOH   B O    1 
HETATM 5972 O  O    . HOH   N 6 .   ? 16.92196  -14.76933 37.65458  1.000 52.25503  ? 508 HOH   B O    1 
HETATM 5973 O  O    . HOH   N 6 .   ? 5.15349   -0.16041  58.37681  1.000 51.32185  ? 509 HOH   B O    1 
HETATM 5974 O  O    . HOH   N 6 .   ? 23.74831  -16.03138 39.42730  1.000 51.18783  ? 510 HOH   B O    1 
HETATM 5975 O  O    . HOH   N 6 .   ? 7.38707   -0.41904  62.04281  1.000 42.22905  ? 511 HOH   B O    1 
HETATM 5976 O  O    . HOH   N 6 .   ? 11.21791  -17.05041 79.58813  1.000 43.30397  ? 512 HOH   B O    1 
HETATM 5977 O  O    . HOH   N 6 .   ? 21.72040  9.52285   63.32770  1.000 39.11142  ? 513 HOH   B O    1 
HETATM 5978 O  O    . HOH   N 6 .   ? -3.78579  12.64888  66.76217  1.000 54.60128  ? 514 HOH   B O    1 
HETATM 5979 O  O    . HOH   N 6 .   ? 7.84748   -13.27148 58.35324  1.000 62.18342  ? 515 HOH   B O    1 
HETATM 5980 O  O    . HOH   N 6 .   ? 9.67510   -5.32266  69.19318  1.000 38.56148  ? 516 HOH   B O    1 
HETATM 5981 O  O    . HOH   N 6 .   ? 22.84363  -10.64584 33.43284  1.000 56.23719  ? 517 HOH   B O    1 
HETATM 5982 O  O    . HOH   N 6 .   ? 21.92675  1.10173   39.58470  1.000 44.45450  ? 518 HOH   B O    1 
HETATM 5983 O  O    . HOH   N 6 .   ? 5.93711   14.59024  42.32260  1.000 43.54668  ? 519 HOH   B O    1 
HETATM 5984 O  O    . HOH   N 6 .   ? -6.04062  5.47323   61.43661  1.000 49.69036  ? 520 HOH   B O    1 
HETATM 5985 O  O    . HOH   N 6 .   ? 52.03791  -8.01228  39.35246  1.000 75.49740  ? 521 HOH   B O    1 
HETATM 5986 O  O    . HOH   N 6 .   ? 13.83302  -10.04697 50.41785  1.000 35.25377  ? 522 HOH   B O    1 
HETATM 5987 O  O    . HOH   N 6 .   ? 23.49259  0.52258   66.54937  1.000 45.37309  ? 523 HOH   B O    1 
HETATM 5988 O  O    . HOH   N 6 .   ? 29.79880  0.89435   45.21177  1.000 56.82088  ? 524 HOH   B O    1 
HETATM 5989 O  O    . HOH   N 6 .   ? 2.28547   14.05719  37.91240  1.000 56.30694  ? 525 HOH   B O    1 
HETATM 5990 O  O    . HOH   N 6 .   ? 16.42309  -0.93934  81.53293  1.000 46.20056  ? 526 HOH   B O    1 
HETATM 5991 O  O    . HOH   N 6 .   ? 10.61530  -8.04958  67.44920  1.000 37.65709  ? 527 HOH   B O    1 
HETATM 5992 O  O    . HOH   N 6 .   ? 6.89221   7.97946   73.04287  1.000 53.63094  ? 528 HOH   B O    1 
HETATM 5993 O  O    . HOH   N 6 .   ? 31.01312  -20.26023 77.83745  1.000 32.37109  ? 529 HOH   B O    1 
HETATM 5994 O  O    . HOH   N 6 .   ? 22.29827  -18.24361 85.70495  1.000 44.18225  ? 530 HOH   B O    1 
HETATM 5995 O  O    . HOH   N 6 .   ? 4.44421   -14.55531 74.38419  1.000 51.30753  ? 531 HOH   B O    1 
HETATM 5996 O  O    . HOH   N 6 .   ? 16.15666  -15.51542 68.04428  1.000 36.17312  ? 532 HOH   B O    1 
HETATM 5997 O  O    . HOH   N 6 .   ? -6.15864  -3.58749  50.03285  1.000 47.46283  ? 533 HOH   B O    1 
HETATM 5998 O  O    . HOH   N 6 .   ? 31.05766  -14.24456 86.06604  1.000 31.55345  ? 534 HOH   B O    1 
HETATM 5999 O  O    . HOH   N 6 .   ? 31.73683  -0.51093  47.00221  1.000 54.54067  ? 535 HOH   B O    1 
HETATM 6000 O  O    . HOH   N 6 .   ? 33.68608  -18.55746 70.38728  1.000 37.34042  ? 536 HOH   B O    1 
HETATM 6001 O  O    . HOH   N 6 .   ? 12.71570  6.33670   72.10599  1.000 41.87142  ? 537 HOH   B O    1 
HETATM 6002 O  O    . HOH   N 6 .   ? 15.78686  -7.88348  49.76873  1.000 37.77194  ? 538 HOH   B O    1 
HETATM 6003 O  O    . HOH   N 6 .   ? 13.21603  8.67188   42.08497  1.000 44.96292  ? 539 HOH   B O    1 
HETATM 6004 O  O    . HOH   N 6 .   ? 18.24007  -12.39876 29.37141  1.000 56.95428  ? 540 HOH   B O    1 
HETATM 6005 O  O    . HOH   N 6 .   ? -2.48172  1.03812   60.22951  1.000 45.41816  ? 541 HOH   B O    1 
HETATM 6006 O  O    . HOH   N 6 .   ? 18.45427  -12.69873 64.85939  1.000 38.10195  ? 542 HOH   B O    1 
HETATM 6007 O  O    . HOH   N 6 .   ? 28.89856  -3.18141  76.32678  1.000 43.44163  ? 543 HOH   B O    1 
HETATM 6008 O  O    . HOH   N 6 .   ? -0.66773  15.15831  56.49683  1.000 50.05200  ? 544 HOH   B O    1 
HETATM 6009 O  O    . HOH   N 6 .   ? 19.98295  11.29934  55.80114  1.000 40.69090  ? 545 HOH   B O    1 
HETATM 6010 O  O    . HOH   N 6 .   ? 6.84470   -7.44439  67.81577  1.000 45.34552  ? 546 HOH   B O    1 
HETATM 6011 O  O    . HOH   N 6 .   ? 34.41009  3.72261   54.91216  1.000 48.58241  ? 547 HOH   B O    1 
HETATM 6012 O  O    . HOH   N 6 .   ? 28.60381  4.74989   59.00999  1.000 43.82690  ? 548 HOH   B O    1 
HETATM 6013 O  O    . HOH   N 6 .   ? 31.27164  3.85397   45.78361  1.000 59.88482  ? 549 HOH   B O    1 
HETATM 6014 O  O    . HOH   N 6 .   ? 30.42896  -0.92729  41.86183  1.000 49.09055  ? 550 HOH   B O    1 
HETATM 6015 O  O    . HOH   N 6 .   ? 19.24848  13.23415  69.69471  1.000 44.41052  ? 551 HOH   B O    1 
HETATM 6016 O  O    . HOH   N 6 .   ? 16.90541  -2.23292  39.11651  1.000 36.90139  ? 552 HOH   B O    1 
HETATM 6017 O  O    . HOH   N 6 .   ? 5.13704   19.12159  64.47481  1.000 47.84964  ? 553 HOH   B O    1 
HETATM 6018 O  O    . HOH   N 6 .   ? 30.33651  14.42519  48.58848  1.000 43.82295  ? 554 HOH   B O    1 
HETATM 6019 O  O    . HOH   N 6 .   ? 12.37833  2.49989   34.69352  1.000 50.06261  ? 555 HOH   B O    1 
HETATM 6020 O  O    . HOH   N 6 .   ? 33.95983  -9.19290  69.52506  1.000 46.03890  ? 556 HOH   B O    1 
HETATM 6021 O  O    . HOH   N 6 .   ? 12.01172  -23.67447 76.00487  1.000 41.41260  ? 557 HOH   B O    1 
HETATM 6022 O  O    . HOH   N 6 .   ? 7.10839   -6.58341  56.61427  1.000 37.80370  ? 558 HOH   B O    1 
HETATM 6023 O  O    . HOH   N 6 .   ? 24.82874  -10.06832 64.40881  1.000 43.70823  ? 559 HOH   B O    1 
HETATM 6024 O  O    . HOH   N 6 .   ? 0.90820   -5.30473  56.46002  1.000 44.84955  ? 560 HOH   B O    1 
HETATM 6025 O  O    . HOH   N 6 .   ? 8.14563   -10.67639 63.39969  1.000 46.19391  ? 561 HOH   B O    1 
HETATM 6026 O  O    . HOH   N 6 .   ? 21.22508  -12.01640 88.26354  1.000 35.98620  ? 562 HOH   B O    1 
HETATM 6027 O  O    . HOH   N 6 .   ? 13.92781  4.30195   75.57964  1.000 40.03648  ? 563 HOH   B O    1 
HETATM 6028 O  O    . HOH   N 6 .   ? 35.18850  -5.09773  76.86430  1.000 42.72411  ? 564 HOH   B O    1 
HETATM 6029 O  O    . HOH   N 6 .   ? 13.93922  -17.22738 64.78010  1.000 45.94311  ? 565 HOH   B O    1 
HETATM 6030 O  O    . HOH   N 6 .   ? 0.46945   8.80440   39.20508  1.000 36.01741  ? 566 HOH   B O    1 
HETATM 6031 O  O    . HOH   N 6 .   ? 21.78144  -16.32530 83.96495  1.000 37.17026  ? 567 HOH   B O    1 
HETATM 6032 O  O    . HOH   N 6 .   ? 26.76376  -0.96536  61.16545  1.000 32.71170  ? 568 HOH   B O    1 
HETATM 6033 O  O    . HOH   N 6 .   ? 9.63311   -2.76533  30.95623  1.000 51.83966  ? 569 HOH   B O    1 
HETATM 6034 O  O    . HOH   N 6 .   ? 24.61588  -4.80178  80.13417  1.000 42.28129  ? 570 HOH   B O    1 
HETATM 6035 O  O    . HOH   N 6 .   ? 11.79211  18.70624  64.13055  1.000 55.42652  ? 571 HOH   B O    1 
HETATM 6036 O  O    . HOH   N 6 .   ? 4.91475   -6.70671  28.93728  1.000 45.06001  ? 572 HOH   B O    1 
HETATM 6037 O  O    . HOH   N 6 .   ? 9.29683   -14.34635 56.42992  1.000 51.18253  ? 573 HOH   B O    1 
HETATM 6038 O  O    . HOH   N 6 .   ? 18.29039  -11.75965 32.38227  1.000 49.31696  ? 574 HOH   B O    1 
HETATM 6039 O  O    . HOH   N 6 .   ? 10.93732  -21.77827 68.95800  1.000 45.30574  ? 575 HOH   B O    1 
HETATM 6040 O  O    . HOH   N 6 .   ? 30.03487  -4.53653  64.46487  1.000 45.92339  ? 576 HOH   B O    1 
HETATM 6041 O  O    . HOH   N 6 .   ? 5.91910   -10.35772 57.86637  1.000 51.06759  ? 577 HOH   B O    1 
HETATM 6042 O  O    . HOH   N 6 .   ? 9.52098   16.47752  76.65624  1.000 56.54681  ? 578 HOH   B O    1 
HETATM 6043 O  O    . HOH   N 6 .   ? 19.28761  4.58246   78.95963  1.000 47.85528  ? 579 HOH   B O    1 
HETATM 6044 O  O    . HOH   N 6 .   ? 29.27837  -17.60408 84.66536  1.000 40.50609  ? 580 HOH   B O    1 
HETATM 6045 O  O    . HOH   N 6 .   ? 21.35121  0.79945   65.37083  1.000 41.29800  ? 581 HOH   B O    1 
HETATM 6046 O  O    . HOH   N 6 .   ? 8.12228   6.66748   80.95292  1.000 60.71413  ? 582 HOH   B O    1 
HETATM 6047 O  O    . HOH   N 6 .   ? 32.00977  -1.56816  72.88222  1.000 46.01128  ? 583 HOH   B O    1 
HETATM 6048 O  O    . HOH   N 6 .   ? 8.01936   13.19649  73.40035  1.000 50.68912  ? 584 HOH   B O    1 
HETATM 6049 O  O    . HOH   N 6 .   ? 20.12470  -3.99494  39.02084  1.000 35.91735  ? 585 HOH   B O    1 
HETATM 6050 O  O    . HOH   N 6 .   ? 8.46826   -20.70299 69.48165  1.000 47.44409  ? 586 HOH   B O    1 
HETATM 6051 O  O    . HOH   N 6 .   ? 10.53796  12.18651  47.27779  1.000 33.45950  ? 587 HOH   B O    1 
HETATM 6052 O  O    . HOH   N 6 .   ? 5.05155   -15.49396 33.65213  1.000 50.69568  ? 588 HOH   B O    1 
HETATM 6053 O  O    . HOH   N 6 .   ? 15.17203  -3.91149  59.11350  1.000 42.95730  ? 589 HOH   B O    1 
HETATM 6054 O  O    . HOH   N 6 .   ? 20.00740  2.87129   65.67602  1.000 44.69444  ? 590 HOH   B O    1 
HETATM 6055 O  O    . HOH   N 6 .   ? 5.89254   -10.62339 28.81445  1.000 48.23456  ? 591 HOH   B O    1 
HETATM 6056 O  O    . HOH   N 6 .   ? 0.49323   17.50180  68.70154  1.000 52.12816  ? 592 HOH   B O    1 
HETATM 6057 O  O    . HOH   N 6 .   ? -0.72842  -10.99085 46.20024  1.000 45.80918  ? 593 HOH   B O    1 
HETATM 6058 O  O    . HOH   N 6 .   ? 10.87283  10.14038  39.96706  1.000 43.40934  ? 594 HOH   B O    1 
HETATM 6059 O  O    . HOH   N 6 .   ? 22.42188  -7.04554  62.21651  1.000 35.02859  ? 595 HOH   B O    1 
HETATM 6060 O  O    . HOH   N 6 .   ? 8.45927   2.08368   31.66219  1.000 40.13921  ? 596 HOH   B O    1 
HETATM 6061 O  O    . HOH   N 6 .   ? 12.68207  -5.17256  81.88776  1.000 53.56048  ? 597 HOH   B O    1 
HETATM 6062 O  O    . HOH   N 6 .   ? 21.93651  -11.04745 62.61412  1.000 43.10141  ? 598 HOH   B O    1 
HETATM 6063 O  O    . HOH   N 6 .   ? 17.71218  -9.83887  61.44100  1.000 42.95149  ? 599 HOH   B O    1 
HETATM 6064 O  O    . HOH   N 6 .   ? 19.63263  -16.84793 65.26165  1.000 46.21587  ? 600 HOH   B O    1 
HETATM 6065 O  O    . HOH   N 6 .   ? 33.30616  -12.44187 67.46817  1.000 42.83236  ? 601 HOH   B O    1 
HETATM 6066 O  O    . HOH   N 6 .   ? 7.98007   -6.31362  65.58257  1.000 42.68531  ? 602 HOH   B O    1 
HETATM 6067 O  O    . HOH   N 6 .   ? 22.13803  8.60389   66.49699  1.000 37.30243  ? 603 HOH   B O    1 
HETATM 6068 O  O    . HOH   N 6 .   ? 12.27344  21.17143  74.62358  1.000 52.04322  ? 604 HOH   B O    1 
HETATM 6069 O  O    . HOH   N 6 .   ? 23.43576  1.88109   63.71534  1.000 41.53911  ? 605 HOH   B O    1 
HETATM 6070 O  O    . HOH   N 6 .   ? 7.71980   -12.93275 50.03162  1.000 35.82689  ? 606 HOH   B O    1 
HETATM 6071 O  O    . HOH   N 6 .   ? 27.89321  -22.45051 69.46064  1.000 42.13871  ? 607 HOH   B O    1 
HETATM 6072 O  O    . HOH   N 6 .   ? 22.83966  -9.27723  38.85158  1.000 41.76155  ? 608 HOH   B O    1 
HETATM 6073 O  O    . HOH   N 6 .   ? 33.94769  -14.06943 78.99362  1.000 37.37024  ? 609 HOH   B O    1 
HETATM 6074 O  O    . HOH   N 6 .   ? 27.07372  -17.53959 81.59334  1.000 42.54082  ? 610 HOH   B O    1 
HETATM 6075 O  O    . HOH   N 6 .   ? 13.50568  -2.97114  57.40533  1.000 31.90136  ? 611 HOH   B O    1 
HETATM 6076 O  O    . HOH   N 6 .   ? 4.95982   1.08218   60.85965  1.000 57.47953  ? 612 HOH   B O    1 
HETATM 6077 O  O    . HOH   N 6 .   ? 17.64205  6.04402   42.01511  1.000 46.78713  ? 613 HOH   B O    1 
HETATM 6078 O  O    . HOH   N 6 .   ? 11.07684  -5.03831  46.67891  1.000 30.90840  ? 614 HOH   B O    1 
HETATM 6079 O  O    . HOH   N 6 .   ? 17.09850  -3.47300  82.74899  1.000 40.23186  ? 615 HOH   B O    1 
HETATM 6080 O  O    . HOH   N 6 .   ? 23.39908  5.50713   72.19600  1.000 44.32065  ? 616 HOH   B O    1 
HETATM 6081 O  O    . HOH   N 6 .   ? 10.26922  14.76366  58.84790  1.000 40.55664  ? 617 HOH   B O    1 
HETATM 6082 O  O    . HOH   N 6 .   ? 1.44513   2.70446   66.34408  1.000 48.16012  ? 618 HOH   B O    1 
HETATM 6083 O  O    . HOH   N 6 .   ? 23.55920  -20.16514 89.06046  1.000 60.02256  ? 619 HOH   B O    1 
HETATM 6084 O  O    . HOH   N 6 .   ? 12.64824  22.72946  68.95440  1.000 49.08763  ? 620 HOH   B O    1 
HETATM 6085 O  O    . HOH   N 6 .   ? 8.15828   -14.75345 68.84052  1.000 41.62840  ? 621 HOH   B O    1 
HETATM 6086 O  O    . HOH   N 6 .   ? 16.35652  -15.59358 40.51578  1.000 49.70534  ? 622 HOH   B O    1 
HETATM 6087 O  O    . HOH   N 6 .   ? 2.88548   -15.52105 49.72718  1.000 48.33512  ? 623 HOH   B O    1 
HETATM 6088 O  O    . HOH   N 6 .   ? 14.04042  7.87034   33.74279  1.000 55.54807  ? 624 HOH   B O    1 
HETATM 6089 O  O    . HOH   N 6 .   ? 7.54939   -22.01119 74.18367  1.000 53.95168  ? 625 HOH   B O    1 
HETATM 6090 O  O    . HOH   N 6 .   ? -11.63517 -13.48072 47.84550  1.000 56.62190  ? 626 HOH   B O    1 
HETATM 6091 O  O    . HOH   N 6 .   ? 15.82930  13.74255  63.68584  1.000 44.78873  ? 627 HOH   B O    1 
HETATM 6092 O  O    . HOH   N 6 .   ? 28.60714  -6.54345  89.15101  1.000 46.41906  ? 628 HOH   B O    1 
HETATM 6093 O  O    . HOH   N 6 .   ? 4.11159   -9.46480  69.29564  1.000 46.66805  ? 629 HOH   B O    1 
HETATM 6094 O  O    . HOH   N 6 .   ? 18.45445  -20.33370 78.46919  1.000 39.50132  ? 630 HOH   B O    1 
HETATM 6095 O  O    . HOH   N 6 .   ? 25.73212  -8.95956  38.47973  1.000 50.66388  ? 631 HOH   B O    1 
HETATM 6096 O  O    . HOH   N 6 .   ? 17.20099  17.01890  68.46418  1.000 48.30840  ? 632 HOH   B O    1 
HETATM 6097 O  O    . HOH   N 6 .   ? 33.89990  -13.98977 75.39516  1.000 46.38223  ? 633 HOH   B O    1 
HETATM 6098 O  O    . HOH   N 6 .   ? 4.01353   15.89124  58.00166  1.000 50.93415  ? 634 HOH   B O    1 
HETATM 6099 O  O    . HOH   N 6 .   ? 10.19137  9.35006   32.29402  1.000 45.27402  ? 635 HOH   B O    1 
HETATM 6100 O  O    . HOH   N 6 .   ? 7.42719   -7.93960  63.59384  1.000 46.49719  ? 636 HOH   B O    1 
HETATM 6101 O  O    . HOH   N 6 .   ? 21.28301  12.94086  51.08903  1.000 52.78086  ? 637 HOH   B O    1 
HETATM 6102 O  O    . HOH   N 6 .   ? 16.43017  -14.59679 29.57516  1.000 65.99046  ? 638 HOH   B O    1 
HETATM 6103 O  O    . HOH   N 6 .   ? 22.83892  -10.71526 36.51040  1.000 62.40816  ? 639 HOH   B O    1 
HETATM 6104 O  O    . HOH   N 6 .   ? 19.92557  1.96476   79.85203  1.000 39.68497  ? 640 HOH   B O    1 
HETATM 6105 O  O    . HOH   N 6 .   ? -1.56456  -7.30626  58.20713  1.000 67.30424  ? 641 HOH   B O    1 
HETATM 6106 O  O    . HOH   N 6 .   ? 12.84453  21.56197  64.45129  1.000 55.38965  ? 642 HOH   B O    1 
HETATM 6107 O  O    . HOH   N 6 .   ? 6.13737   6.05998   79.74553  1.000 59.59647  ? 643 HOH   B O    1 
HETATM 6108 O  O    . HOH   N 6 .   ? 26.76626  -17.30583 43.57809  1.000 54.85339  ? 644 HOH   B O    1 
HETATM 6109 O  O    . HOH   N 6 .   ? -7.14203  10.00663  52.31646  1.000 50.17864  ? 645 HOH   B O    1 
HETATM 6110 O  O    . HOH   N 6 .   ? 11.00916  -14.76611 81.11654  1.000 45.61030  ? 646 HOH   B O    1 
HETATM 6111 O  O    . HOH   N 6 .   ? 13.20483  -7.60115  82.29008  1.000 54.91308  ? 647 HOH   B O    1 
HETATM 6112 O  O    . HOH   N 6 .   ? -11.22010 -10.90859 54.63120  1.000 60.92342  ? 648 HOH   B O    1 
HETATM 6113 O  O    . HOH   N 6 .   ? 5.27888   -7.95851  54.76798  1.000 34.29105  ? 649 HOH   B O    1 
HETATM 6114 O  O    . HOH   N 6 .   ? -1.23742  15.88479  53.78393  1.000 59.57099  ? 650 HOH   B O    1 
HETATM 6115 O  O    . HOH   N 6 .   ? 5.47938   -13.83769 30.23679  1.000 47.85851  ? 651 HOH   B O    1 
HETATM 6116 O  O    . HOH   N 6 .   ? 10.39647  15.60776  49.46786  1.000 58.10733  ? 652 HOH   B O    1 
HETATM 6117 O  O    . HOH   N 6 .   ? 23.05576  -16.59198 50.52408  1.000 58.46009  ? 653 HOH   B O    1 
HETATM 6118 O  O    . HOH   N 6 .   ? 22.42633  9.66084   48.41999  1.000 46.28005  ? 654 HOH   B O    1 
HETATM 6119 O  O    . HOH   N 6 .   ? 17.57540  14.32999  77.83839  1.000 69.92522  ? 655 HOH   B O    1 
HETATM 6120 O  O    . HOH   N 6 .   ? 3.19278   -5.15322  54.20072  1.000 33.45556  ? 656 HOH   B O    1 
HETATM 6121 O  O    . HOH   N 6 .   ? 16.73904  12.63268  51.34440  1.000 42.55981  ? 657 HOH   B O    1 
HETATM 6122 O  O    . HOH   N 6 .   ? 8.40973   -0.28890  83.51666  1.000 50.41436  ? 658 HOH   B O    1 
HETATM 6123 O  O    . HOH   N 6 .   ? 23.81567  -2.57414  78.86296  1.000 45.00961  ? 659 HOH   B O    1 
HETATM 6124 O  O    . HOH   N 6 .   ? 5.62907   -2.33351  59.29616  1.000 47.59696  ? 660 HOH   B O    1 
HETATM 6125 O  O    . HOH   N 6 .   ? 13.86949  -14.68974 58.96732  1.000 44.63652  ? 661 HOH   B O    1 
HETATM 6126 O  O    . HOH   N 6 .   ? 32.77999  -3.30498  56.64014  1.000 47.49863  ? 662 HOH   B O    1 
HETATM 6127 O  O    . HOH   N 6 .   ? 25.20370  -2.34100  35.92463  1.000 56.97294  ? 663 HOH   B O    1 
HETATM 6128 O  O    . HOH   N 6 .   ? 16.61400  -22.86721 69.00820  1.000 50.90048  ? 664 HOH   B O    1 
HETATM 6129 O  O    . HOH   N 6 .   ? 30.82281  -13.39446 66.62826  1.000 31.36876  ? 665 HOH   B O    1 
HETATM 6130 O  O    . HOH   N 6 .   ? 23.92444  -14.74687 53.32655  1.000 54.82916  ? 666 HOH   B O    1 
HETATM 6131 O  O    . HOH   N 6 .   ? 16.67046  18.68936  67.70252  1.000 56.92266  ? 667 HOH   B O    1 
HETATM 6132 O  O    . HOH   N 6 .   ? 25.25205  -13.05141 94.30733  1.000 47.78054  ? 668 HOH   B O    1 
HETATM 6133 O  O    . HOH   N 6 .   ? 49.51841  -10.90610 42.20626  1.000 65.63854  ? 669 HOH   B O    1 
HETATM 6134 O  O    . HOH   N 6 .   ? 20.20827  -10.72971 58.52851  1.000 46.77626  ? 670 HOH   B O    1 
HETATM 6135 O  O    . HOH   N 6 .   ? 8.92995   -17.07522 77.52753  1.000 40.35367  ? 671 HOH   B O    1 
HETATM 6136 O  O    . HOH   N 6 .   ? 30.79317  -15.96212 66.59296  1.000 31.82195  ? 672 HOH   B O    1 
HETATM 6137 O  O    . HOH   N 6 .   ? 14.77694  1.14158   34.64931  1.000 54.70301  ? 673 HOH   B O    1 
HETATM 6138 O  O    . HOH   N 6 .   ? 17.84437  -4.33341  37.84209  1.000 42.23536  ? 674 HOH   B O    1 
HETATM 6139 O  O    . HOH   N 6 .   ? 14.66956  -16.69235 84.04722  1.000 38.80669  ? 675 HOH   B O    1 
HETATM 6140 O  O    . HOH   N 6 .   ? 3.13375   -16.41840 35.51522  1.000 43.35646  ? 676 HOH   B O    1 
HETATM 6141 O  O    . HOH   N 6 .   ? 17.50280  -1.18989  36.64818  1.000 46.44063  ? 677 HOH   B O    1 
HETATM 6142 O  O    . HOH   N 6 .   ? -3.42221  -12.49119 46.80299  1.000 49.57827  ? 678 HOH   B O    1 
HETATM 6143 O  O    . HOH   N 6 .   ? 22.65273  -25.04938 82.84435  1.000 50.27126  ? 679 HOH   B O    1 
HETATM 6144 O  O    . HOH   N 6 .   ? 7.93543   -0.49484  30.72185  1.000 46.49347  ? 680 HOH   B O    1 
HETATM 6145 O  O    . HOH   N 6 .   ? 19.14918  -16.96260 40.22941  1.000 58.71193  ? 681 HOH   B O    1 
HETATM 6146 O  O    . HOH   N 6 .   ? -5.51151  -5.91715  51.33726  1.000 56.53678  ? 682 HOH   B O    1 
HETATM 6147 O  O    . HOH   N 6 .   ? 25.99919  -10.56866 93.52967  1.000 47.58773  ? 683 HOH   B O    1 
HETATM 6148 O  O    . HOH   N 6 .   ? 10.72549  6.45934   81.28001  1.000 45.42137  ? 684 HOH   B O    1 
HETATM 6149 O  O    . HOH   N 6 .   ? 19.68637  7.03008   43.69876  1.000 46.87667  ? 685 HOH   B O    1 
HETATM 6150 O  O    . HOH   N 6 .   ? 28.12979  0.09785   35.28165  1.000 57.03973  ? 686 HOH   B O    1 
HETATM 6151 O  O    . HOH   N 6 .   ? 25.10910  -7.69552  89.39831  1.000 38.93891  ? 687 HOH   B O    1 
HETATM 6152 O  O    . HOH   N 6 .   ? 11.15471  1.22340   84.54900  1.000 48.97966  ? 688 HOH   B O    1 
HETATM 6153 O  O    . HOH   N 6 .   ? 11.82205  13.83068  52.07817  1.000 64.39514  ? 689 HOH   B O    1 
HETATM 6154 O  O    . HOH   N 6 .   ? 2.38624   -0.24553  29.36981  1.000 46.99413  ? 690 HOH   B O    1 
HETATM 6155 O  O    . HOH   N 6 .   ? 8.28533   8.01619   29.70504  1.000 50.03007  ? 691 HOH   B O    1 
HETATM 6156 O  O    . HOH   N 6 .   ? 20.65908  6.27840   77.78655  1.000 47.38095  ? 692 HOH   B O    1 
HETATM 6157 O  O    . HOH   N 6 .   ? 29.60955  -27.05721 77.85245  1.000 36.48964  ? 693 HOH   B O    1 
HETATM 6158 O  O    . HOH   N 6 .   ? 26.20018  -11.01280 37.03765  1.000 48.39048  ? 694 HOH   B O    1 
HETATM 6159 O  O    . HOH   N 6 .   ? -3.67224  -17.62891 36.96555  1.000 43.96514  ? 695 HOH   B O    1 
HETATM 6160 O  O    . HOH   N 6 .   ? 10.69768  -5.19258  65.86886  1.000 25.06029  ? 696 HOH   B O    1 
HETATM 6161 O  O    . HOH   N 6 .   ? -5.66868  6.08110   70.02694  0.50  59.33142  ? 697 HOH   B O    1 
HETATM 6162 O  O    . HOH   N 6 .   ? 21.51057  14.20748  54.04774  1.000 48.44255  ? 698 HOH   B O    1 
HETATM 6163 O  O    . HOH   N 6 .   ? 17.29502  -3.09042  34.63467  1.000 46.79909  ? 699 HOH   B O    1 
HETATM 6164 O  O    . HOH   N 6 .   ? 26.10971  3.38811   75.05144  1.000 52.17428  ? 700 HOH   B O    1 
HETATM 6165 O  O    . HOH   N 6 .   ? 17.62711  1.33173   81.27752  1.000 47.61418  ? 701 HOH   B O    1 
HETATM 6166 O  O    . HOH   N 6 .   ? 12.73322  7.77538   39.60163  1.000 46.96283  ? 702 HOH   B O    1 
HETATM 6167 O  O    . HOH   N 6 .   ? 3.61400   -6.03266  57.32917  1.000 40.39817  ? 703 HOH   B O    1 
HETATM 6168 O  O    . HOH   N 6 .   ? 12.36050  8.03909   79.24153  1.000 41.23476  ? 704 HOH   B O    1 
HETATM 6169 O  O    . HOH   N 6 .   ? 29.24718  6.30553   40.59461  1.000 62.64228  ? 705 HOH   B O    1 
HETATM 6170 O  O    . HOH   N 6 .   ? 4.19529   -8.58767  27.54095  1.000 47.12708  ? 706 HOH   B O    1 
HETATM 6171 O  O    . HOH   N 6 .   ? 8.60951   -2.93531  83.89718  1.000 61.50288  ? 707 HOH   B O    1 
HETATM 6172 O  O    . HOH   N 6 .   ? 17.70591  -11.83272 62.43769  1.000 53.89297  ? 708 HOH   B O    1 
HETATM 6173 O  O    . HOH   N 6 .   ? 31.41031  -22.40994 74.09504  1.000 59.94858  ? 709 HOH   B O    1 
HETATM 6174 O  O    . HOH   N 6 .   ? 18.59272  13.08087  53.48958  1.000 48.00345  ? 710 HOH   B O    1 
HETATM 6175 O  O    . HOH   N 6 .   ? 2.94663   14.27867  44.14482  1.000 52.03126  ? 711 HOH   B O    1 
HETATM 6176 O  O    . HOH   N 6 .   ? 4.93974   -2.14679  61.71708  1.000 47.50516  ? 712 HOH   B O    1 
HETATM 6177 O  O    . HOH   N 6 .   ? 34.00645  0.88738   47.45549  1.000 54.21992  ? 713 HOH   B O    1 
HETATM 6178 O  O    . HOH   N 6 .   ? 28.88145  -17.42839 65.33481  1.000 47.53517  ? 714 HOH   B O    1 
HETATM 6179 O  O    . HOH   N 6 .   ? 1.77909   16.58173  57.08357  1.000 56.94723  ? 715 HOH   B O    1 
HETATM 6180 O  O    . HOH   N 6 .   ? 35.28301  1.00517   54.79159  1.000 63.66061  ? 716 HOH   B O    1 
HETATM 6181 O  O    . HOH   N 6 .   ? 31.86396  -22.63599 77.11823  1.000 38.45678  ? 717 HOH   B O    1 
HETATM 6182 O  O    . HOH   N 6 .   ? 22.46125  5.97225   66.89196  1.000 43.01576  ? 718 HOH   B O    1 
HETATM 6183 O  O    . HOH   N 6 .   ? 36.34758  -10.51323 68.69883  1.000 46.19536  ? 719 HOH   B O    1 
HETATM 6184 O  O    . HOH   N 6 .   ? 23.78224  4.30753   65.28464  1.000 45.23766  ? 720 HOH   B O    1 
HETATM 6185 O  O    . HOH   N 6 .   ? 17.43603  -21.45851 81.10934  1.000 46.23546  ? 721 HOH   B O    1 
HETATM 6186 O  O    . HOH   N 6 .   ? 22.53656  -7.59154  88.70539  1.000 46.47644  ? 722 HOH   B O    1 
HETATM 6187 O  O    . HOH   N 6 .   ? 4.19855   -18.36277 36.81649  1.000 59.39525  ? 723 HOH   B O    1 
HETATM 6188 O  O    . HOH   N 6 .   ? 3.82729   -4.52812  62.10210  1.000 45.54268  ? 724 HOH   B O    1 
HETATM 6189 O  O    . HOH   N 6 .   ? 20.08461  -9.09739  60.45707  1.000 52.45764  ? 725 HOH   B O    1 
HETATM 6190 O  O    . HOH   N 6 .   ? 26.40983  -24.31113 70.86486  1.000 45.25866  ? 726 HOH   B O    1 
HETATM 6191 O  O    . HOH   N 6 .   ? 21.13294  -12.75112 59.56940  1.000 56.68671  ? 727 HOH   B O    1 
HETATM 6192 O  O    . HOH   N 6 .   ? 27.24784  -5.96302  61.68911  1.000 45.68323  ? 728 HOH   B O    1 
HETATM 6193 O  O    . HOH   N 6 .   ? 18.46631  -14.81364 66.66335  1.000 41.89222  ? 729 HOH   B O    1 
HETATM 6194 O  O    . HOH   N 6 .   ? 25.32636  -15.59380 51.08827  1.000 53.36269  ? 730 HOH   B O    1 
HETATM 6195 O  O    . HOH   N 6 .   ? 15.47661  -21.18951 82.64492  1.000 53.35503  ? 731 HOH   B O    1 
HETATM 6196 O  O    . HOH   N 6 .   ? 29.40363  -7.23796  63.88058  1.000 55.36551  ? 732 HOH   B O    1 
HETATM 6197 O  O    . HOH   N 6 .   ? 8.39684   10.79863  73.74915  1.000 55.47300  ? 733 HOH   B O    1 
HETATM 6198 O  O    . HOH   N 6 .   ? 8.48950   -19.77287 77.24811  1.000 44.32497  ? 734 HOH   B O    1 
HETATM 6199 O  O    . HOH   N 6 .   ? 20.75404  -12.54189 32.53379  1.000 56.72858  ? 735 HOH   B O    1 
HETATM 6200 O  O    . HOH   N 6 .   ? 11.00486  1.49928   32.41365  1.000 46.73044  ? 736 HOH   B O    1 
HETATM 6201 O  O    . HOH   N 6 .   ? 18.81062  13.40893  49.58837  1.000 56.61925  ? 737 HOH   B O    1 
HETATM 6202 O  O    . HOH   N 6 .   ? 33.66719  3.27796   47.14730  1.000 53.08756  ? 738 HOH   B O    1 
HETATM 6203 O  O    . HOH   N 6 .   ? 19.84019  -9.42900  89.01677  1.000 56.06600  ? 739 HOH   B O    1 
HETATM 6204 O  O    . HOH   N 6 .   ? 8.49953   4.08363   29.28520  1.000 53.48695  ? 740 HOH   B O    1 
HETATM 6205 O  O    . HOH   N 6 .   ? 15.55181  -15.46527 65.03214  1.000 46.27916  ? 741 HOH   B O    1 
HETATM 6206 O  O    . HOH   N 6 .   ? 24.92085  -7.78437  62.28461  1.000 43.70560  ? 742 HOH   B O    1 
HETATM 6207 O  O    . HOH   N 6 .   ? 24.62004  -12.39274 63.26057  1.000 52.54415  ? 743 HOH   B O    1 
HETATM 6208 O  O    . HOH   N 6 .   ? 3.88738   -8.61744  58.38006  1.000 50.87259  ? 744 HOH   B O    1 
HETATM 6209 O  O    . HOH   N 6 .   ? 28.04676  -9.28514  64.48121  1.000 43.28822  ? 745 HOH   B O    1 
HETATM 6210 O  O    . HOH   N 6 .   ? 9.52207   -22.59231 75.96284  1.000 55.29230  ? 746 HOH   B O    1 
HETATM 6211 O  O    . HOH   N 6 .   ? 38.61245  -9.78918  73.20945  1.000 53.26482  ? 747 HOH   B O    1 
HETATM 6212 O  O    . HOH   N 6 .   ? 33.71458  -16.11705 66.38223  1.000 41.48645  ? 748 HOH   B O    1 
HETATM 6213 O  O    . HOH   N 6 .   ? 10.46420  20.76247  62.21202  1.000 66.25026  ? 749 HOH   B O    1 
HETATM 6214 O  O    . HOH   N 6 .   ? 10.86717  -18.94159 81.57678  1.000 60.49500  ? 750 HOH   B O    1 
HETATM 6215 O  O    . HOH   N 6 .   ? 11.40340  -15.36293 58.01877  1.000 53.70836  ? 751 HOH   B O    1 
HETATM 6216 O  O    . HOH   N 6 .   ? 15.76510  8.10118   42.08406  1.000 52.14934  ? 752 HOH   B O    1 
HETATM 6217 O  O    . HOH   N 6 .   ? 25.81371  -4.72422  88.93493  1.000 53.18058  ? 753 HOH   B O    1 
HETATM 6218 O  O    . HOH   N 6 .   ? 13.95766  14.39411  53.99944  1.000 56.50895  ? 754 HOH   B O    1 
HETATM 6219 O  O    . HOH   N 6 .   ? 29.78095  -11.66867 64.89341  1.000 46.47137  ? 755 HOH   B O    1 
HETATM 6220 O  O    . HOH   N 6 .   ? 12.54212  -1.76064  32.98722  1.000 58.61500  ? 756 HOH   B O    1 
HETATM 6221 O  O    . HOH   N 6 .   ? 7.77141   12.05018  29.88721  1.000 60.23047  ? 757 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   . LYS   A 17  ? 0.76010 1.37021 0.84967 0.37098  -0.03693 0.07225  17  LYS   A N   
2    C  CA  . LYS   A 17  ? 0.79062 1.44227 0.90476 0.36084  -0.03132 0.08617  17  LYS   A CA  
3    C  C   . LYS   A 17  ? 0.78472 1.44003 0.92138 0.34033  -0.03687 0.09419  17  LYS   A C   
4    O  O   . LYS   A 17  ? 0.62932 1.29653 0.78271 0.32271  -0.03377 0.10252  17  LYS   A O   
5    C  CB  . LYS   A 17  ? 0.70499 1.38172 0.81657 0.37729  -0.02928 0.08790  17  LYS   A CB  
6    C  CG  . LYS   A 17  ? 0.81992 1.48920 0.93091 0.38341  -0.03825 0.08505  17  LYS   A CG  
7    C  CD  . LYS   A 17  ? 0.84456 1.46773 0.93568 0.38871  -0.04784 0.07214  17  LYS   A CD  
8    C  CE  . LYS   A 17  ? 0.80807 1.42419 0.89927 0.39333  -0.05700 0.07041  17  LYS   A CE  
9    N  NZ  . LYS   A 17  ? 0.74746 1.31833 0.81774 0.39842  -0.06648 0.05870  17  LYS   A NZ  
10   N  N   . ALA   A 18  ? 0.71233 1.35617 0.84893 0.34183  -0.04571 0.09175  18  ALA   A N   
11   C  CA  . ALA   A 18  ? 0.67087 1.31602 0.82665 0.32208  -0.05143 0.09876  18  ALA   A CA  
12   C  C   . ALA   A 18  ? 0.76173 1.37821 0.91327 0.31016  -0.05419 0.09459  18  ALA   A C   
13   O  O   . ALA   A 18  ? 0.70306 1.32291 0.87064 0.29159  -0.05679 0.10108  18  ALA   A O   
14   C  CB  . ALA   A 18  ? 0.67567 1.31387 0.83130 0.32613  -0.06084 0.09712  18  ALA   A CB  
15   N  N   . GLN   A 19  ? 0.71908 1.30828 0.84886 0.32071  -0.05362 0.08404  19  GLN   A N   
16   C  CA  . GLN   A 19  ? 0.73289 1.29502 0.85642 0.31150  -0.05545 0.07960  19  GLN   A CA  
17   C  C   . GLN   A 19  ? 0.69469 1.27322 0.83093 0.29871  -0.04733 0.08616  19  GLN   A C   
18   O  O   . GLN   A 19  ? 0.64259 1.21169 0.78601 0.28326  -0.04934 0.08801  19  GLN   A O   
19   C  CB  . GLN   A 19  ? 0.87462 1.40364 0.97068 0.32762  -0.05777 0.06686  19  GLN   A CB  
20   C  CG  . GLN   A 19  ? 0.96260 1.50329 1.04679 0.34677  -0.05194 0.06336  19  GLN   A CG  
21   C  CD  . GLN   A 19  ? 1.10117 1.60709 1.15659 0.36365  -0.05617 0.05022  19  GLN   A CD  
22   O  OE1 . GLN   A 19  ? 1.14029 1.61843 1.18433 0.36077  -0.05809 0.04440  19  GLN   A OE1 
23   N  NE2 . GLN   A 19  ? 1.10207 1.60908 1.14528 0.38140  -0.05826 0.04560  19  GLN   A NE2 
24   N  N   . GLU   A 20  ? 0.64800 1.25100 0.78628 0.30504  -0.03841 0.08989  20  GLU   A N   
25   C  CA  . GLU   A 20  ? 0.63752 1.25778 0.78798 0.29280  -0.03076 0.09729  20  GLU   A CA  
26   C  C   . GLU   A 20  ? 0.55278 1.19154 0.72851 0.27185  -0.03283 0.10894  20  GLU   A C   
27   O  O   . GLU   A 20  ? 0.57288 1.20549 0.75653 0.25626  -0.03292 0.11150  20  GLU   A O   
28   C  CB  . GLU   A 20  ? 0.63120 1.27728 0.77875 0.30430  -0.02172 0.10052  20  GLU   A CB  
29   C  CG  . GLU   A 20  ? 0.62524 1.25145 0.74758 0.32155  -0.01892 0.08930  20  GLU   A CG  
30   C  CD  . GLU   A 20  ? 0.65502 1.30284 0.76805 0.33937  -0.01288 0.08960  20  GLU   A CD  
31   O  OE1 . GLU   A 20  ? 0.70162 1.33430 0.79358 0.35304  -0.01067 0.08078  20  GLU   A OE1 
32   O  OE2 . GLU   A 20  ? 0.70876 1.38938 0.83520 0.33927  -0.01023 0.09906  20  GLU   A OE2 
33   N  N   . GLU   A 21  ? 0.62153 1.28213 0.80968 0.27125  -0.03527 0.11591  21  GLU   A N   
34   C  CA  . GLU   A 21  ? 0.61945 1.29583 0.83085 0.25145  -0.03902 0.12685  21  GLU   A CA  
35   C  C   . GLU   A 21  ? 0.57102 1.22071 0.78269 0.23944  -0.04785 0.12298  21  GLU   A C   
36   O  O   . GLU   A 21  ? 0.47809 1.12877 0.70227 0.22157  -0.04916 0.12841  21  GLU   A O   
37   C  CB  . GLU   A 21  ? 0.49088 1.19128 0.71308 0.25468  -0.04154 0.13354  21  GLU   A CB  
38   C  CG  . GLU   A 21  ? 0.62760 1.34259 0.87316 0.23465  -0.04742 0.14465  21  GLU   A CG  
39   C  CD  . GLU   A 21  ? 0.57723 1.32105 0.84053 0.22156  -0.04166 0.15773  21  GLU   A CD  
40   O  OE1 . GLU   A 21  ? 0.46507 1.22524 0.72388 0.23024  -0.03230 0.15986  21  GLU   A OE1 
41   O  OE2 . GLU   A 21  ? 0.49673 1.24645 0.77765 0.20261  -0.04723 0.16618  21  GLU   A OE2 
42   N  N   . SER   A 22  ? 0.57316 1.19773 0.76944 0.24944  -0.05418 0.11346  22  SER   A N   
43   C  CA  . SER   A 22  ? 0.60011 1.19943 0.79409 0.23950  -0.06308 0.10988  22  SER   A CA  
44   C  C   . SER   A 22  ? 0.58761 1.16900 0.77615 0.23177  -0.06074 0.10626  22  SER   A C   
45   O  O   . SER   A 22  ? 0.65033 1.22419 0.84621 0.21624  -0.06558 0.10850  22  SER   A O   
46   C  CB  . SER   A 22  ? 0.75640 1.33237 0.93255 0.25343  -0.07009 0.10087  22  SER   A CB  
47   O  OG  . SER   A 22  ? 0.81537 1.37257 0.99091 0.24382  -0.07991 0.09966  22  SER   A OG  
48   N  N   . LYS   A 23  ? 0.60573 1.18018 0.78108 0.24236  -0.05367 0.10060  23  LYS   A N   
49   C  CA  . LYS   A 23  ? 0.54050 1.10024 0.71195 0.23494  -0.05088 0.09775  23  LYS   A CA  
50   C  C   . LYS   A 23  ? 0.58440 1.16478 0.77655 0.21655  -0.04757 0.10790  23  LYS   A C   
51   O  O   . LYS   A 23  ? 0.50540 1.07479 0.70169 0.20287  -0.05037 0.10822  23  LYS   A O   
52   C  CB  . LYS   A 23  ? 0.67707 1.22894 0.83173 0.24978  -0.04368 0.09080  23  LYS   A CB  
53   C  CG  . LYS   A 23  ? 0.73897 1.26269 0.86924 0.26757  -0.04761 0.07923  23  LYS   A CG  
54   C  CD  . LYS   A 23  ? 0.84879 1.36554 0.96334 0.28026  -0.04065 0.07297  23  LYS   A CD  
55   C  CE  . LYS   A 23  ? 0.83057 1.31411 0.92927 0.28056  -0.04302 0.06443  23  LYS   A CE  
56   N  NZ  . LYS   A 23  ? 0.87909 1.36729 0.98718 0.26715  -0.03756 0.06791  23  LYS   A NZ  
57   N  N   . ILE   A 24  ? 0.44268 1.05277 0.64725 0.21596  -0.04203 0.11654  24  ILE   A N   
58   C  CA  . ILE   A 24  ? 0.45693 1.08626 0.68117 0.19786  -0.04009 0.12740  24  ILE   A CA  
59   C  C   . ILE   A 24  ? 0.46787 1.09458 0.70577 0.18090  -0.04983 0.13209  24  ILE   A C   
60   O  O   . ILE   A 24  ? 0.49298 1.11492 0.73908 0.16486  -0.05202 0.13513  24  ILE   A O   
61   C  CB  . ILE   A 24  ? 0.44794 1.11032 0.68220 0.20098  -0.03382 0.13689  24  ILE   A CB  
62   C  CG1 . ILE   A 24  ? 0.57478 1.23910 0.79289 0.21905  -0.02479 0.13158  24  ILE   A CG1 
63   C  CG2 . ILE   A 24  ? 0.52596 1.20514 0.77948 0.18132  -0.03306 0.14861  24  ILE   A CG2 
64   C  CD1 . ILE   A 24  ? 0.45754 1.15706 0.68285 0.22466  -0.01794 0.14114  24  ILE   A CD1 
65   N  N   . GLU   A 25  ? 0.43245 1.06242 0.67263 0.18425  -0.05622 0.13282  25  GLU   A N   
66   C  CA  . GLU   A 25  ? 0.44910 1.07655 0.70106 0.16884  -0.06630 0.13718  25  GLU   A CA  
67   C  C   . GLU   A 25  ? 0.49308 1.09160 0.73567 0.16234  -0.07196 0.12999  25  GLU   A C   
68   O  O   . GLU   A 25  ? 0.53793 1.13326 0.79017 0.14539  -0.07770 0.13389  25  GLU   A O   
69   C  CB  . GLU   A 25  ? 0.48720 1.11921 0.73946 0.17620  -0.07236 0.13730  25  GLU   A CB  
70   C  CG  . GLU   A 25  ? 0.54079 1.20239 0.80116 0.18437  -0.06700 0.14408  25  GLU   A CG  
71   C  CD  . GLU   A 25  ? 0.71797 1.39197 0.99026 0.18036  -0.07492 0.14999  25  GLU   A CD  
72   O  OE1 . GLU   A 25  ? 0.69128 1.39122 0.98170 0.17088  -0.07460 0.16133  25  GLU   A OE1 
73   O  OE2 . GLU   A 25  ? 0.73033 1.38796 0.99252 0.18805  -0.08139 0.14324  25  GLU   A OE2 
74   N  N   . ASP   A 26  ? 0.47034 1.04684 0.69304 0.17582  -0.07095 0.11951  26  ASP   A N   
75   C  CA  . ASP   A 26  ? 0.49848 1.04823 0.71043 0.17087  -0.07593 0.11292  26  ASP   A CA  
76   C  C   . ASP   A 26  ? 0.47511 1.02351 0.69249 0.15844  -0.07176 0.11464  26  ASP   A C   
77   O  O   . ASP   A 26  ? 0.53045 1.05910 0.74680 0.14172  -0.07604 0.11321  26  ASP   A O   
78   C  CB  . ASP   A 26  ? 0.57728 1.10117 0.76516 0.18711  -0.07498 0.10170  26  ASP   A CB  
79   C  CG  . ASP   A 26  ? 0.72055 1.24134 0.90108 0.19951  -0.08142 0.09931  26  ASP   A CG  
80   O  OD1 . ASP   A 26  ? 0.72514 1.25500 0.91602 0.19263  -0.08806 0.10442  26  ASP   A OD1 
81   O  OD2 . ASP   A 26  ? 0.75222 1.25819 0.91509 0.21571  -0.08017 0.09175  26  ASP   A OD2 
82   N  N   . VAL   A 27  ? 0.41275 0.97210 0.63089 0.16376  -0.06206 0.11565  27  VAL   A N   
83   C  CA  . VAL   A 27  ? 0.37956 0.93775 0.60267 0.15264  -0.05813 0.11734  27  VAL   A CA  
84   C  C   . VAL   A 27  ? 0.43268 1.00411 0.67551 0.13302  -0.06285 0.12719  27  VAL   A C   
85   O  O   . VAL   A 27  ? 0.35706 0.91503 0.60128 0.11909  -0.06554 0.12655  27  VAL   A O   
86   C  CB  . VAL   A 27  ? 0.43512 1.00330 0.65509 0.16129  -0.04694 0.11741  27  VAL   A CB  
87   C  CG1 . VAL   A 27  ? 0.37489 0.94319 0.60201 0.14794  -0.04363 0.12045  27  VAL   A CG1 
88   C  CG2 . VAL   A 27  ? 0.48789 1.03790 0.68665 0.17944  -0.04365 0.10675  27  VAL   A CG2 
89   N  N   . ASP   A 28  ? 0.40832 1.00177 0.66422 0.13074  -0.06375 0.13569  28  ASP   A N   
90   C  CA  . ASP   A 28  ? 0.50657 1.11107 0.78083 0.11173  -0.06953 0.14561  28  ASP   A CA  
91   C  C   . ASP   A 28  ? 0.47648 1.06313 0.75077 0.10051  -0.08155 0.14332  28  ASP   A C   
92   O  O   . ASP   A 28  ? 0.44721 1.02815 0.72882 0.08442  -0.08664 0.14639  28  ASP   A O   
93   C  CB  . ASP   A 28  ? 0.44551 1.07649 0.73270 0.11232  -0.06919 0.15518  28  ASP   A CB  
94   C  CG  . ASP   A 28  ? 0.54558 1.19748 0.83382 0.12087  -0.05770 0.15952  28  ASP   A CG  
95   O  OD1 . ASP   A 28  ? 0.49599 1.14503 0.78108 0.11935  -0.05120 0.15874  28  ASP   A OD1 
96   O  OD2 . ASP   A 28  ? 0.73117 1.40320 1.02328 0.12900  -0.05552 0.16409  28  ASP   A OD2 
97   N  N   . LYS   A 29  ? 0.44508 1.02118 0.70941 0.10926  -0.08662 0.13755  29  LYS   A N   
98   C  CA  . LYS   A 29  ? 0.48246 1.03277 0.73955 0.09889  -0.09666 0.13283  29  LYS   A CA  
99   C  C   . LYS   A 29  ? 0.50608 1.01981 0.74542 0.09167  -0.09397 0.12257  29  LYS   A C   
100  O  O   . LYS   A 29  ? 0.43758 0.93524 0.67695 0.07676  -0.10021 0.12174  29  LYS   A O   
101  C  CB  . LYS   A 29  ? 0.49585 1.03623 0.74087 0.11037  -0.10047 0.12730  29  LYS   A CB  
102  C  CG  . LYS   A 29  ? 0.59539 1.09494 0.81872 0.10621  -0.10526 0.11625  29  LYS   A CG  
103  C  CD  . LYS   A 29  ? 0.63671 1.12787 0.84610 0.12167  -0.10663 0.11077  29  LYS   A CD  
104  C  CE  . LYS   A 29  ? 0.76509 1.21887 0.95392 0.11728  -0.11274 0.10167  29  LYS   A CE  
105  N  NZ  . LYS   A 29  ? 0.85338 1.27276 1.02166 0.11392  -0.10832 0.09177  29  LYS   A NZ  
106  N  N   . ILE   A 30  ? 0.42021 0.91994 0.64359 0.10266  -0.08537 0.11448  30  ILE   A N   
107  C  CA  . ILE   A 30  ? 0.48023 0.94755 0.68740 0.09649  -0.08225 0.10529  30  ILE   A CA  
108  C  C   . ILE   A 30  ? 0.48741 0.96166 0.70661 0.08339  -0.08077 0.11026  30  ILE   A C   
109  O  O   . ILE   A 30  ? 0.46563 0.91611 0.67765 0.07199  -0.08328 0.10541  30  ILE   A O   
110  C  CB  . ILE   A 30  ? 0.46302 0.91699 0.65274 0.11083  -0.07399 0.09713  30  ILE   A CB  
111  C  CG1 . ILE   A 30  ? 0.53141 0.96984 0.70554 0.12186  -0.07730 0.09093  30  ILE   A CG1 
112  C  CG2 . ILE   A 30  ? 0.47925 0.90669 0.65630 0.10415  -0.06940 0.08978  30  ILE   A CG2 
113  C  CD1 . ILE   A 30  ? 0.55182 0.97815 0.70934 0.13709  -0.07089 0.08380  30  ILE   A CD1 
114  N  N   . LEU   A 31  ? 0.40719 0.91412 0.64407 0.08543  -0.07664 0.12001  31  LEU   A N   
115  C  CA  . LEU   A 31  ? 0.46825 0.98385 0.71785 0.07277  -0.07591 0.12629  31  LEU   A CA  
116  C  C   . LEU   A 31  ? 0.45037 0.96278 0.71035 0.05564  -0.08735 0.13121  31  LEU   A C   
117  O  O   . LEU   A 31  ? 0.46196 0.95233 0.71675 0.04404  -0.09033 0.12725  31  LEU   A O   
118  C  CB  . LEU   A 31  ? 0.35613 0.91193 0.62392 0.07880  -0.06990 0.13769  31  LEU   A CB  
119  C  CG  . LEU   A 31  ? 0.35260 0.92230 0.63641 0.06506  -0.07006 0.14698  31  LEU   A CG  
120  C  CD1 . LEU   A 31  ? 0.38452 0.93063 0.65507 0.06334  -0.06351 0.13884  31  LEU   A CD1 
121  C  CD2 . LEU   A 31  ? 0.43845 1.03310 0.73055 0.06900  -0.06258 0.15558  31  LEU   A CD2 
122  N  N   . ASN   A 32  ? 0.47139 1.00362 0.74467 0.05441  -0.09475 0.13911  32  ASN   A N   
123  C  CA  . ASN   A 32  ? 0.40571 0.93278 0.68785 0.03812  -0.10725 0.14352  32  ASN   A CA  
124  C  C   . ASN   A 32  ? 0.51416 1.00057 0.77549 0.03352  -0.11266 0.13099  32  ASN   A C   
125  O  O   . ASN   A 32  ? 0.49967 0.97109 0.76161 0.01997  -0.12076 0.13058  32  ASN   A O   
126  C  CB  . ASN   A 32  ? 0.53482 1.09111 0.83493 0.03817  -0.11455 0.15444  32  ASN   A CB  
127  C  CG  . ASN   A 32  ? 0.59217 1.17103 0.90962 0.03038  -0.11168 0.16631  32  ASN   A CG  
128  O  OD1 . ASN   A 32  ? 0.61649 1.20246 0.93551 0.03132  -0.10252 0.16838  32  ASN   A OD1 
129  N  ND2 . ASN   A 32  ? 0.60027 1.18876 0.92953 0.02201  -0.11970 0.17424  32  ASN   A ND2 
130  N  N   . ASP   A 33  ? 0.45072 0.91869 0.69282 0.04489  -0.10849 0.12082  33  ASP   A N   
131  C  CA  . ASP   A 33  ? 0.56250 0.99458 0.78444 0.04130  -0.11263 0.10972  33  ASP   A CA  
132  C  C   . ASP   A 33  ? 0.53101 0.94121 0.74287 0.03527  -0.10836 0.10307  33  ASP   A C   
133  O  O   . ASP   A 33  ? 0.50893 0.89982 0.71565 0.02479  -0.11517 0.09948  33  ASP   A O   
134  C  CB  . ASP   A 33  ? 0.63175 1.05190 0.83655 0.05497  -0.10878 0.10212  33  ASP   A CB  
135  C  CG  . ASP   A 33  ? 0.77002 1.17025 0.96332 0.05226  -0.11768 0.09716  33  ASP   A CG  
136  O  OD1 . ASP   A 33  ? 0.74728 1.14182 0.94489 0.04027  -0.12689 0.09873  33  ASP   A OD1 
137  O  OD2 . ASP   A 33  ? 0.81481 1.20441 0.99410 0.06231  -0.11602 0.09176  33  ASP   A OD2 
138  N  N   . ILE   A 34  ? 0.44319 0.85577 0.65132 0.04260  -0.09747 0.10096  34  ILE   A N   
139  C  CA  . ILE   A 34  ? 0.45079 0.84505 0.65066 0.03739  -0.09304 0.09528  34  ILE   A CA  
140  C  C   . ILE   A 34  ? 0.53016 0.93057 0.74436 0.02329  -0.09920 0.10172  34  ILE   A C   
141  O  O   . ILE   A 34  ? 0.49530 0.87355 0.70138 0.01505  -0.10268 0.09613  34  ILE   A O   
142  C  CB  . ILE   A 34  ? 0.46995 0.87027 0.66629 0.04783  -0.08108 0.09373  34  ILE   A CB  
143  C  CG1 . ILE   A 34  ? 0.43245 0.81773 0.61048 0.06037  -0.07720 0.08559  34  ILE   A CG1 
144  C  CG2 . ILE   A 34  ? 0.45638 0.84496 0.64971 0.04130  -0.07699 0.09071  34  ILE   A CG2 
145  C  CD1 . ILE   A 34  ? 0.46737 0.85168 0.63769 0.07098  -0.06709 0.08209  34  ILE   A CD1 
146  N  N   . LEU   A 35  ? 0.48266 0.91341 0.71830 0.02029  -0.10146 0.11397  35  LEU   A N   
147  C  CA  . LEU   A 35  ? 0.49486 0.93176 0.74496 0.00606  -0.10829 0.12153  35  LEU   A CA  
148  C  C   . LEU   A 35  ? 0.48263 0.90285 0.73141 -0.00523 -0.12249 0.12029  35  LEU   A C   
149  O  O   . LEU   A 35  ? 0.53941 0.94982 0.79137 -0.01683 -0.12916 0.12142  35  LEU   A O   
150  C  CB  . LEU   A 35  ? 0.52038 0.99675 0.79466 0.00531  -0.10740 0.13660  35  LEU   A CB  
151  C  CG  . LEU   A 35  ? 0.41672 0.91032 0.69344 0.01450  -0.09403 0.13880  35  LEU   A CG  
152  C  CD1 . LEU   A 35  ? 0.37463 0.91064 0.67185 0.01945  -0.09149 0.15251  35  LEU   A CD1 
153  C  CD2 . LEU   A 35  ? 0.42825 0.91309 0.70570 0.00570  -0.09202 0.13889  35  LEU   A CD2 
154  N  N   . SER   A 36  ? 0.42973 0.84483 0.67260 -0.00168 -0.12786 0.11749  36  SER   A N   
155  C  CA  . SER   A 36  ? 0.51796 0.91837 0.75947 -0.01174 -0.14221 0.11662  36  SER   A CA  
156  C  C   . SER   A 36  ? 0.56048 0.92678 0.78399 -0.01674 -0.14484 0.10544  36  SER   A C   
157  O  O   . SER   A 36  ? 0.60681 0.96193 0.83218 -0.02748 -0.15697 0.10610  36  SER   A O   
158  C  CB  . SER   A 36  ? 0.55911 0.95908 0.79515 -0.00545 -0.14637 0.11467  36  SER   A CB  
159  O  OG  . SER   A 36  ? 0.64604 1.02581 0.86024 0.00501  -0.13846 0.10308  36  SER   A OG  
160  N  N   . ILE   A 37  ? 0.59922 0.94827 0.80464 -0.00880 -0.13445 0.09506  37  ILE   A N   
161  C  CA  . ILE   A 37  ? 0.56637 0.88552 0.75478 -0.01262 -0.13669 0.08468  37  ILE   A CA  
162  C  C   . ILE   A 37  ? 0.58267 0.89970 0.77658 -0.01956 -0.13541 0.08605  37  ILE   A C   
163  O  O   . ILE   A 37  ? 0.54796 0.84154 0.72891 -0.02260 -0.13770 0.07778  37  ILE   A O   
164  C  CB  . ILE   A 37  ? 0.51226 0.81329 0.67886 -0.00263 -0.12753 0.07363  37  ILE   A CB  
165  C  CG1 . ILE   A 37  ? 0.58110 0.89200 0.74788 0.00606  -0.11351 0.07386  37  ILE   A CG1 
166  C  CG2 . ILE   A 37  ? 0.59101 0.88664 0.74864 0.00184  -0.13260 0.07102  37  ILE   A CG2 
167  C  CD1 . ILE   A 37  ? 0.47627 0.78813 0.64771 0.00240  -0.10778 0.07454  37  ILE   A CD1 
168  N  N   . SER   A 38  ? 0.54341 0.88500 0.75622 -0.02210 -0.13245 0.09664  38  SER   A N   
169  C  CA  . SER   A 38  ? 0.43021 0.77274 0.64969 -0.02847 -0.13064 0.09949  38  SER   A CA  
170  C  C   . SER   A 38  ? 0.51889 0.86920 0.75540 -0.04209 -0.14422 0.10962  38  SER   A C   
171  O  O   . SER   A 38  ? 0.51322 0.88285 0.76473 -0.04582 -0.15135 0.11951  38  SER   A O   
172  C  CB  . SER   A 38  ? 0.46130 0.82670 0.68950 -0.02170 -0.11744 0.10499  38  SER   A CB  
173  O  OG  . SER   A 38  ? 0.54592 0.94345 0.79622 -0.02456 -0.12033 0.11913  38  SER   A OG  
174  N  N   . SER   A 39  ? 0.44307 0.77851 0.67759 -0.04968 -0.14820 0.10763  39  SER   A N   
175  C  CA  . SER   A 39  ? 0.49720 0.83930 0.74827 -0.06330 -0.16074 0.11821  39  SER   A CA  
176  C  C   . SER   A 39  ? 0.44681 0.81400 0.71504 -0.06597 -0.15357 0.12952  39  SER   A C   
177  O  O   . SER   A 39  ? 0.46291 0.84550 0.74979 -0.07722 -0.16276 0.14250  39  SER   A O   
178  C  CB  . SER   A 39  ? 0.45726 0.76704 0.69557 -0.06995 -0.17149 0.10964  39  SER   A CB  
179  O  OG  . SER   A 39  ? 0.55058 0.85126 0.78232 -0.06809 -0.16279 0.10463  39  SER   A OG  
180  N  N   . GLU   A 40  ? 0.43596 0.80731 0.69800 -0.05628 -0.13800 0.12528  40  GLU   A N   
181  C  CA  . GLU   A 40  ? 0.44865 0.84652 0.72668 -0.05750 -0.13074 0.13647  40  GLU   A CA  
182  C  C   . GLU   A 40  ? 0.44537 0.85206 0.71564 -0.04267 -0.11377 0.13153  40  GLU   A C   
183  O  O   . GLU   A 40  ? 0.44573 0.82993 0.69674 -0.03507 -0.10768 0.11844  40  GLU   A O   
184  C  CB  . GLU   A 40  ? 0.50760 0.89317 0.78649 -0.06659 -0.13393 0.13713  40  GLU   A CB  
185  C  CG  . GLU   A 40  ? 0.48325 0.89605 0.77735 -0.06756 -0.12557 0.14868  40  GLU   A CG  
186  C  CD  . GLU   A 40  ? 0.61120 1.00871 0.90233 -0.07407 -0.12625 0.14701  40  GLU   A CD  
187  O  OE1 . GLU   A 40  ? 0.50270 0.91011 0.80936 -0.08643 -0.13488 0.15916  40  GLU   A OE1 
188  O  OE2 . GLU   A 40  ? 0.53351 0.90884 0.80700 -0.06736 -0.11891 0.13402  40  GLU   A OE2 
189  N  N   . CYS   A 41  ? 0.37791 0.81749 0.66283 -0.03838 -0.10665 0.14225  41  CYS   A N   
190  C  CA  . CYS   A 41  ? 0.36462 0.81261 0.64199 -0.02364 -0.09159 0.13790  41  CYS   A CA  
191  C  C   . CYS   A 41  ? 0.40705 0.87826 0.69641 -0.02387 -0.08414 0.14725  41  CYS   A C   
192  O  O   . CYS   A 41  ? 0.37407 0.87460 0.68362 -0.02984 -0.08745 0.16191  41  CYS   A O   
193  C  CB  . CYS   A 41  ? 0.40648 0.87248 0.68587 -0.01290 -0.08868 0.13971  41  CYS   A CB  
194  S  SG  . CYS   A 41  ? 0.39934 0.87170 0.66677 0.00654  -0.07172 0.13321  41  CYS   A SG  
195  N  N   . ILE   A 42  ? 0.35028 0.80936 0.62738 -0.01752 -0.07432 0.13935  42  ILE   A N   
196  C  CA  . ILE   A 42  ? 0.33644 0.81514 0.62126 -0.01545 -0.06580 0.14629  42  ILE   A CA  
197  C  C   . ILE   A 42  ? 0.37842 0.86008 0.65104 0.00180  -0.05269 0.13912  42  ILE   A C   
198  O  O   . ILE   A 42  ? 0.33734 0.79367 0.59243 0.00665  -0.04764 0.12702  42  ILE   A O   
199  C  CB  . ILE   A 42  ? 0.37015 0.82930 0.65130 -0.02476 -0.06771 0.14355  42  ILE   A CB  
200  C  CG1 . ILE   A 42  ? 0.38551 0.83809 0.67696 -0.04137 -0.08277 0.14987  42  ILE   A CG1 
201  C  CG2 . ILE   A 42  ? 0.40242 0.87929 0.68857 -0.02122 -0.05773 0.14922  42  ILE   A CG2 
202  C  CD1 . ILE   A 42  ? 0.50724 0.92823 0.78773 -0.04838 -0.08711 0.14139  42  ILE   A CD1 
203  N  N   . GLN   A 43  ? 0.34431 0.85647 0.62551 0.01161  -0.04746 0.14644  43  GLN   A N   
204  C  CA  . GLN   A 43  ? 0.35842 0.90249 0.65953 0.00777  -0.05261 0.16059  43  GLN   A CA  
205  C  C   . GLN   A 43  ? 0.40959 0.96118 0.70704 0.01974  -0.05171 0.15785  43  GLN   A C   
206  O  O   . GLN   A 43  ? 0.38297 0.92737 0.66617 0.03421  -0.04407 0.14864  43  GLN   A O   
207  C  CB  . GLN   A 43  ? 0.39355 0.95689 0.69894 0.00924  -0.04409 0.16994  43  GLN   A CB  
208  C  CG  . GLN   A 43  ? 0.38909 0.94619 0.69786 -0.00206 -0.04472 0.17377  43  GLN   A CG  
209  C  CD  . GLN   A 43  ? 0.44936 1.00443 0.77062 -0.02044 -0.05691 0.18340  43  GLN   A CD  
210  O  OE1 . GLN   A 43  ? 0.49103 1.04693 0.81797 -0.02530 -0.06556 0.18607  43  GLN   A OE1 
211  N  NE2 . GLN   A 43  ? 0.44059 0.99274 0.76569 -0.03047 -0.05807 0.18912  43  GLN   A NE2 
212  N  N   . PRO   A 44  ? 0.39650 0.95734 0.70333 0.01382  -0.05911 0.16498  44  PRO   A N   
213  C  CA  . PRO   A 44  ? 0.42831 0.99568 0.73163 0.02524  -0.05890 0.16223  44  PRO   A CA  
214  C  C   . PRO   A 44  ? 0.40962 0.99220 0.70612 0.04279  -0.04666 0.16127  44  PRO   A C   
215  O  O   . PRO   A 44  ? 0.40713 0.98630 0.69374 0.05656  -0.04439 0.15376  44  PRO   A O   
216  C  CB  . PRO   A 44  ? 0.42405 1.00225 0.74092 0.01416  -0.06813 0.17253  44  PRO   A CB  
217  C  CG  . PRO   A 44  ? 0.46473 1.03127 0.78897 -0.00432 -0.07733 0.17687  44  PRO   A CG  
218  C  CD  . PRO   A 44  ? 0.41246 0.97492 0.73238 -0.00373 -0.06930 0.17500  44  PRO   A CD  
219  N  N   . ASP   A 45  ? 0.41140 1.01060 0.71224 0.04270  -0.03967 0.16921  45  ASP   A N   
220  C  CA  . ASP   A 45  ? 0.38065 0.99433 0.67352 0.05950  -0.02850 0.16851  45  ASP   A CA  
221  C  C   . ASP   A 45  ? 0.40900 1.00617 0.68531 0.07272  -0.02206 0.15582  45  ASP   A C   
222  O  O   . ASP   A 45  ? 0.34477 0.94236 0.60974 0.08940  -0.01735 0.14945  45  ASP   A O   
223  C  CB  . ASP   A 45  ? 0.51525 1.14584 0.81457 0.05413  -0.02341 0.17921  45  ASP   A CB  
224  C  CG  . ASP   A 45  ? 0.67552 1.31531 0.99146 0.03615  -0.03194 0.19189  45  ASP   A CG  
225  O  OD1 . ASP   A 45  ? 0.63938 1.29234 0.96280 0.03547  -0.03610 0.19765  45  ASP   A OD1 
226  O  OD2 . ASP   A 45  ? 0.71183 1.34249 1.03259 0.02250  -0.03569 0.19509  45  ASP   A OD2 
227  N  N   . GLU   A 46  ? 0.33496 0.91593 0.60939 0.06513  -0.02278 0.15189  46  GLU   A N   
228  C  CA  . GLU   A 46  ? 0.30882 0.87254 0.56843 0.07552  -0.01766 0.14024  46  GLU   A CA  
229  C  C   . GLU   A 46  ? 0.36967 0.91164 0.61720 0.08117  -0.02200 0.12961  46  GLU   A C   
230  O  O   . GLU   A 46  ? 0.31572 0.84206 0.54558 0.09449  -0.01719 0.11956  46  GLU   A O   
231  C  CB  . GLU   A 46  ? 0.34721 0.89828 0.60871 0.06385  -0.01842 0.13927  46  GLU   A CB  
232  C  CG  . GLU   A 46  ? 0.37610 0.94041 0.64565 0.05585  -0.01492 0.14920  46  GLU   A CG  
233  C  CD  . GLU   A 46  ? 0.46794 1.01828 0.73721 0.04662  -0.01484 0.14702  46  GLU   A CD  
234  O  OE1 . GLU   A 46  ? 0.44235 0.96440 0.69627 0.04941  -0.01358 0.13453  46  GLU   A OE1 
235  O  OE2 . GLU   A 46  ? 0.32005 0.87785 0.59807 0.03568  -0.01566 0.15614  46  GLU   A OE2 
236  N  N   . LEU   A 47  ? 0.30857 0.84056 0.56044 0.06964  -0.03137 0.13029  47  LEU   A N   
237  C  CA  . LEU   A 47  ? 0.35950 0.86539 0.59599 0.07344  -0.03532 0.11991  47  LEU   A CA  
238  C  C   . LEU   A 47  ? 0.38945 0.91201 0.62487 0.08931  -0.03373 0.12064  47  LEU   A C   
239  O  O   . LEU   A 47  ? 0.34963 0.85259 0.56712 0.10046  -0.03178 0.11062  47  LEU   A O   
240  C  CB  . LEU   A 47  ? 0.37724 0.87039 0.61850 0.05810  -0.04609 0.12086  47  LEU   A CB  
241  C  CG  . LEU   A 47  ? 0.39777 0.86439 0.62308 0.06091  -0.05064 0.11081  47  LEU   A CG  
242  C  CD1 . LEU   A 47  ? 0.42592 0.86232 0.62941 0.06669  -0.04532 0.09826  47  LEU   A CD1 
243  C  CD2 . LEU   A 47  ? 0.45835 0.91358 0.68784 0.04657  -0.06188 0.11182  47  LEU   A CD2 
244  N  N   . ARG   A 48  ? 0.36386 0.92333 0.61829 0.09097  -0.03464 0.13286  48  ARG   A N   
245  C  CA  . ARG   A 48  ? 0.31563 0.88707 0.56540 0.10671  -0.03167 0.13239  48  ARG   A CA  
246  C  C   . ARG   A 48  ? 0.35273 0.91782 0.58600 0.12404  -0.02286 0.12443  48  ARG   A C   
247  O  O   . ARG   A 48  ? 0.39650 0.95175 0.61674 0.13827  -0.02331 0.11676  48  ARG   A O   
248  C  CB  . ARG   A 48  ? 0.41900 1.01686 0.68198 0.10307  -0.03024 0.14415  48  ARG   A CB  
249  C  CG  . ARG   A 48  ? 0.45041 1.06001 0.70916 0.11775  -0.02860 0.14379  48  ARG   A CG  
250  C  CD  . ARG   A 48  ? 0.45802 1.09519 0.73199 0.11172  -0.02868 0.15670  48  ARG   A CD  
251  N  NE  . ARG   A 48  ? 0.68159 1.32304 0.96342 0.10818  -0.03713 0.15960  48  ARG   A NE  
252  C  CZ  . ARG   A 48  ? 0.73265 1.38366 1.03071 0.09213  -0.04418 0.16945  48  ARG   A CZ  
253  N  NH1 . ARG   A 48  ? 0.66142 1.31915 0.96973 0.07813  -0.04398 0.17797  48  ARG   A NH1 
254  N  NH2 . ARG   A 48  ? 0.62591 1.27852 0.92938 0.09003  -0.05232 0.17085  48  ARG   A NH2 
255  N  N   . VAL   A 49  ? 0.33952 0.90783 0.57205 0.12282  -0.01573 0.12592  49  VAL   A N   
256  C  CA  . VAL   A 49  ? 0.44791 1.00840 0.66374 0.13875  -0.00802 0.11813  49  VAL   A CA  
257  C  C   . VAL   A 49  ? 0.39400 0.92347 0.59355 0.14367  -0.01036 0.10573  49  VAL   A C   
258  O  O   . VAL   A 49  ? 0.41046 0.92899 0.59412 0.15947  -0.00901 0.09794  49  VAL   A O   
259  C  CB  . VAL   A 49  ? 0.32268 0.89020 0.54013 0.13491  -0.00083 0.12205  49  VAL   A CB  
260  C  CG1 . VAL   A 49  ? 0.28354 0.83485 0.48196 0.14928  0.00518  0.11169  49  VAL   A CG1 
261  C  CG2 . VAL   A 49  ? 0.41835 1.01380 0.64393 0.13551  0.00304  0.13296  49  VAL   A CG2 
262  N  N   . LYS   A 50  ? 0.35971 0.86308 0.55625 0.12753  -0.01376 0.10200  50  LYS   A N   
263  C  CA  . LYS   A 50  ? 0.44174 0.90542 0.61724 0.12766  -0.01577 0.08947  50  LYS   A CA  
264  C  C   . LYS   A 50  ? 0.43310 0.88835 0.59989 0.13633  -0.02079 0.08533  50  LYS   A C   
265  O  O   . LYS   A 50  ? 0.43082 0.86260 0.57881 0.14570  -0.02072 0.07621  50  LYS   A O   
266  C  CB  . LYS   A 50  ? 0.38632 0.82794 0.56202 0.10912  -0.01993 0.08731  50  LYS   A CB  
267  C  CG  . LYS   A 50  ? 0.41158 0.85419 0.59295 0.09968  -0.01619 0.08965  50  LYS   A CG  
268  C  CD  . LYS   A 50  ? 0.41147 0.82970 0.57588 0.10360  -0.01150 0.08034  50  LYS   A CD  
269  C  CE  . LYS   A 50  ? 0.42913 0.84381 0.59812 0.09249  -0.00891 0.08167  50  LYS   A CE  
270  N  NZ  . LYS   A 50  ? 0.39651 0.78942 0.54860 0.09855  -0.00414 0.07271  50  LYS   A NZ  
271  N  N   . LEU   A 51  ? 0.32597 0.79806 0.50599 0.13202  -0.02623 0.09210  51  LEU   A N   
272  C  CA  . LEU   A 51  ? 0.44386 0.90854 0.61672 0.13911  -0.03178 0.08884  51  LEU   A CA  
273  C  C   . LEU   A 51  ? 0.55526 1.03108 0.72101 0.16032  -0.02879 0.08702  51  LEU   A C   
274  O  O   . LEU   A 51  ? 0.47548 0.93865 0.63023 0.16876  -0.03320 0.08210  51  LEU   A O   
275  C  CB  . LEU   A 51  ? 0.34774 0.83015 0.53765 0.12966  -0.03864 0.09722  51  LEU   A CB  
276  C  CG  . LEU   A 51  ? 0.49296 0.95470 0.68352 0.11068  -0.04422 0.09581  51  LEU   A CG  
277  C  CD1 . LEU   A 51  ? 0.45698 0.93784 0.66657 0.09941  -0.05172 0.10539  51  LEU   A CD1 
278  C  CD2 . LEU   A 51  ? 0.39331 0.81826 0.56279 0.11078  -0.04754 0.08481  51  LEU   A CD2 
279  N  N   . LEU   A 52  ? 0.43660 0.94043 0.61063 0.16933  -0.02230 0.09240  52  LEU   A N   
280  C  CA  . LEU   A 52  ? 0.43817 0.95152 0.60305 0.19164  -0.01937 0.08945  52  LEU   A CA  
281  C  C   . LEU   A 52  ? 0.57065 1.05316 0.71225 0.20089  -0.01686 0.07803  52  LEU   A C   
282  O  O   . LEU   A 52  ? 0.56475 1.04895 0.69514 0.22010  -0.01581 0.07386  52  LEU   A O   
283  C  CB  . LEU   A 52  ? 0.44597 0.98716 0.61934 0.19327  -0.01215 0.09740  52  LEU   A CB  
284  C  CG  . LEU   A 52  ? 0.43600 1.00152 0.62911 0.18188  -0.01486 0.10859  52  LEU   A CG  
285  C  CD1 . LEU   A 52  ? 0.48725 1.07917 0.69127 0.17723  -0.00819 0.11867  52  LEU   A CD1 
286  C  CD2 . LEU   A 52  ? 0.41276 0.98104 0.60072 0.19392  -0.01825 0.10667  52  LEU   A CD2 
287  N  N   . LEU   A 53  ? 0.41753 0.87140 0.55104 0.18814  -0.01660 0.07278  53  LEU   A N   
288  C  CA  . LEU   A 53  ? 0.60227 1.02877 0.71552 0.19546  -0.01448 0.06321  53  LEU   A CA  
289  C  C   . LEU   A 53  ? 0.64786 1.04469 0.74056 0.20487  -0.02043 0.05423  53  LEU   A C   
290  O  O   . LEU   A 53  ? 0.78312 1.16133 0.85894 0.21509  -0.01979 0.04710  53  LEU   A O   
291  C  CB  . LEU   A 53  ? 0.49478 0.89985 0.60562 0.17902  -0.01275 0.06051  53  LEU   A CB  
292  C  CG  . LEU   A 53  ? 0.54080 0.96264 0.66321 0.17226  -0.00617 0.06571  53  LEU   A CG  
293  C  CD1 . LEU   A 53  ? 0.56305 1.02500 0.70691 0.17194  -0.00403 0.07719  53  LEU   A CD1 
294  C  CD2 . LEU   A 53  ? 0.43555 0.83756 0.55900 0.15311  -0.00675 0.06415  53  LEU   A CD2 
295  N  N   . LYS   A 54  ? 0.63121 1.02215 0.72424 0.20165  -0.02685 0.05456  54  LYS   A N   
296  C  CA  . LYS   A 54  ? 0.73723 1.10160 0.81106 0.21125  -0.03327 0.04714  54  LYS   A CA  
297  C  C   . LYS   A 54  ? 0.73194 1.05746 0.78822 0.20350  -0.03505 0.03952  54  LYS   A C   
298  O  O   . LYS   A 54  ? 0.78709 1.09055 0.82515 0.21411  -0.03771 0.03286  54  LYS   A O   
299  C  CB  . LYS   A 54  ? 0.86303 1.23764 0.92891 0.23463  -0.03285 0.04478  54  LYS   A CB  
300  C  CG  . LYS   A 54  ? 0.76729 1.18257 0.85011 0.24419  -0.03153 0.05272  54  LYS   A CG  
301  C  CD  . LYS   A 54  ? 0.85276 1.27862 0.92624 0.26742  -0.02952 0.04978  54  LYS   A CD  
302  C  CE  . LYS   A 54  ? 0.94147 1.39730 1.02644 0.26997  -0.02670 0.05655  54  LYS   A CE  
303  N  NZ  . LYS   A 54  ? 0.96309 1.41948 1.03266 0.28864  -0.02458 0.05175  54  LYS   A NZ  
304  N  N   . ARG   A 55  ? 0.69440 1.01235 0.75652 0.18494  -0.03399 0.04089  55  ARG   A N   
305  C  CA  . ARG   A 55  ? 0.61237 0.89826 0.66159 0.17440  -0.03523 0.03543  55  ARG   A CA  
306  C  C   . ARG   A 55  ? 0.55384 0.84211 0.61421 0.15621  -0.03559 0.03893  55  ARG   A C   
307  O  O   . ARG   A 55  ? 0.55818 0.87174 0.63617 0.15138  -0.03360 0.04527  55  ARG   A O   
308  C  CB  . ARG   A 55  ? 0.66385 0.94215 0.70755 0.17518  -0.02987 0.03224  55  ARG   A CB  
309  C  CG  . ARG   A 55  ? 0.59803 0.89916 0.65889 0.16677  -0.02305 0.03752  55  ARG   A CG  
310  C  CD  . ARG   A 55  ? 0.63053 0.91680 0.68459 0.16247  -0.01896 0.03372  55  ARG   A CD  
311  N  NE  . ARG   A 55  ? 0.60171 0.90893 0.67034 0.15672  -0.01260 0.03856  55  ARG   A NE  
312  C  CZ  . ARG   A 55  ? 0.61649 0.92723 0.69641 0.14091  -0.01171 0.04187  55  ARG   A CZ  
313  N  NH1 . ARG   A 55  ? 0.49116 0.78867 0.57013 0.13007  -0.01627 0.04090  55  ARG   A NH1 
314  N  NH2 . ARG   A 55  ? 0.52121 0.84836 0.61269 0.13625  -0.00662 0.04615  55  ARG   A NH2 
315  N  N   . LYS   A 56  ? 0.54881 0.81092 0.59856 0.14624  -0.03855 0.03509  56  LYS   A N   
316  C  CA  . LYS   A 56  ? 0.47648 0.73773 0.53379 0.12995  -0.03915 0.03701  56  LYS   A CA  
317  C  C   . LYS   A 56  ? 0.44293 0.71626 0.51206 0.12199  -0.03331 0.03934  56  LYS   A C   
318  O  O   . LYS   A 56  ? 0.48362 0.75184 0.54822 0.12464  -0.02874 0.03687  56  LYS   A O   
319  C  CB  . LYS   A 56  ? 0.51859 0.75051 0.56060 0.12240  -0.04210 0.03223  56  LYS   A CB  
320  C  CG  . LYS   A 56  ? 0.59735 0.81567 0.62765 0.12760  -0.04873 0.03078  56  LYS   A CG  
321  C  CD  . LYS   A 56  ? 0.57140 0.80058 0.61003 0.12334  -0.05312 0.03434  56  LYS   A CD  
322  C  CE  . LYS   A 56  ? 0.66282 0.87196 0.68674 0.12473  -0.05973 0.03229  56  LYS   A CE  
323  N  NZ  . LYS   A 56  ? 0.76013 0.97343 0.78898 0.11679  -0.06407 0.03468  56  LYS   A NZ  
324  N  N   . LEU   A 57  ? 0.38438 0.67358 0.46858 0.11254  -0.03423 0.04437  57  LEU   A N   
325  C  CA  . LEU   A 57  ? 0.35498 0.65113 0.44929 0.10250  -0.03052 0.04652  57  LEU   A CA  
326  C  C   . LEU   A 57  ? 0.39744 0.67050 0.48330 0.09082  -0.03176 0.04174  57  LEU   A C   
327  O  O   . LEU   A 57  ? 0.43170 0.69411 0.51251 0.08605  -0.03682 0.04023  57  LEU   A O   
328  C  CB  . LEU   A 57  ? 0.41492 0.73633 0.52858 0.09682  -0.03283 0.05446  57  LEU   A CB  
329  C  CG  . LEU   A 57  ? 0.40639 0.75369 0.52871 0.10915  -0.03174 0.05996  57  LEU   A CG  
330  C  CD1 . LEU   A 57  ? 0.39784 0.77123 0.54011 0.10271  -0.03509 0.06909  57  LEU   A CD1 
331  C  CD2 . LEU   A 57  ? 0.36469 0.72128 0.48699 0.11750  -0.02438 0.06020  57  LEU   A CD2 
332  N  N   . ILE   A 58  ? 0.38838 0.65549 0.47318 0.08642  -0.02717 0.03969  58  ILE   A N   
333  C  CA  . ILE   A 58  ? 0.38547 0.63419 0.46359 0.07608  -0.02754 0.03549  58  ILE   A CA  
334  C  C   . ILE   A 58  ? 0.39598 0.65443 0.48711 0.06537  -0.02976 0.03882  58  ILE   A C   
335  O  O   . ILE   A 58  ? 0.38121 0.65513 0.48467 0.06358  -0.02741 0.04312  58  ILE   A O   
336  C  CB  . ILE   A 58  ? 0.42893 0.66603 0.49930 0.07694  -0.02211 0.03156  58  ILE   A CB  
337  C  CG1 . ILE   A 58  ? 0.44856 0.67223 0.50447 0.08681  -0.02209 0.02813  58  ILE   A CG1 
338  C  CG2 . ILE   A 58  ? 0.43305 0.65558 0.49913 0.06592  -0.02213 0.02800  58  ILE   A CG2 
339  C  CD1 . ILE   A 58  ? 0.56788 0.77883 0.61520 0.08831  -0.01788 0.02440  58  ILE   A CD1 
340  N  N   . CYS   A 59  ? 0.41217 0.66120 0.50002 0.05836  -0.03499 0.03708  59  CYS   A N   
341  C  CA  . CYS   A 59  ? 0.30770 0.56052 0.40469 0.04816  -0.03904 0.03889  59  CYS   A CA  
342  C  C   . CYS   A 59  ? 0.32736 0.56099 0.41392 0.04183  -0.03863 0.03271  59  CYS   A C   
343  O  O   . CYS   A 59  ? 0.36891 0.58740 0.44136 0.04405  -0.03732 0.02805  59  CYS   A O   
344  C  CB  . CYS   A 59  ? 0.33522 0.59311 0.43632 0.04599  -0.04675 0.04158  59  CYS   A CB  
345  S  SG  . CYS   A 59  ? 0.46103 0.74263 0.57304 0.05551  -0.04705 0.04871  59  CYS   A SG  
346  N  N   . TYR   A 60  ? 0.33246 0.56680 0.42566 0.03380  -0.04081 0.03301  60  TYR   A N   
347  C  CA  . TYR   A 60  ? 0.30696 0.52349 0.38889 0.02919  -0.04104 0.02652  60  TYR   A CA  
348  C  C   . TYR   A 60  ? 0.33799 0.55374 0.42581 0.02104  -0.04765 0.02656  60  TYR   A C   
349  O  O   . TYR   A 60  ? 0.33445 0.56267 0.43627 0.01736  -0.05110 0.03211  60  TYR   A O   
350  C  CB  . TYR   A 60  ? 0.31831 0.52763 0.39464 0.03052  -0.03361 0.02318  60  TYR   A CB  
351  C  CG  . TYR   A 60  ? 0.38249 0.59398 0.46630 0.02528  -0.03246 0.02339  60  TYR   A CG  
352  C  CD1 . TYR   A 60  ? 0.34915 0.57656 0.44802 0.02374  -0.03303 0.02967  60  TYR   A CD1 
353  C  CD2 . TYR   A 60  ? 0.35944 0.55792 0.43519 0.02222  -0.03048 0.01779  60  TYR   A CD2 
354  C  CE1 . TYR   A 60  ? 0.31497 0.54352 0.42040 0.01853  -0.03245 0.03042  60  TYR   A CE1 
355  C  CE2 . TYR   A 60  ? 0.30523 0.50474 0.38720 0.01809  -0.02980 0.01782  60  TYR   A CE2 
356  C  CZ  . TYR   A 60  ? 0.29603 0.50927 0.39239 0.01590  -0.03104 0.02396  60  TYR   A CZ  
357  O  OH  . TYR   A 60  ? 0.34618 0.55942 0.44837 0.01124  -0.03105 0.02443  60  TYR   A OH  
358  N  N   . ASP   A 61  ? 0.33216 0.53294 0.40857 0.01844  -0.04966 0.02045  61  ASP   A N   
359  C  CA  . ASP   A 61  ? 0.35112 0.54585 0.42861 0.01210  -0.05584 0.01807  61  ASP   A CA  
360  C  C   . ASP   A 61  ? 0.35814 0.53947 0.42277 0.01286  -0.05117 0.01109  61  ASP   A C   
361  O  O   . ASP   A 61  ? 0.31860 0.49516 0.37308 0.01699  -0.04577 0.00887  61  ASP   A O   
362  C  CB  . ASP   A 61  ? 0.31985 0.51079 0.39426 0.01005  -0.06528 0.01733  61  ASP   A CB  
363  C  CG  . ASP   A 61  ? 0.41341 0.59945 0.49166 0.00349  -0.07469 0.01632  61  ASP   A CG  
364  O  OD1 . ASP   A 61  ? 0.37898 0.56187 0.45987 0.00059  -0.07388 0.01500  61  ASP   A OD1 
365  O  OD2 . ASP   A 61  ? 0.42008 0.60478 0.49865 0.00123  -0.08408 0.01708  61  ASP   A OD2 
366  N  N   . GLY   A 62  ? 0.37128 0.54672 0.43625 0.00891  -0.05394 0.00804  62  GLY   A N   
367  C  CA  . GLY   A 62  ? 0.35752 0.52240 0.41129 0.01008  -0.04947 0.00158  62  GLY   A CA  
368  C  C   . GLY   A 62  ? 0.41935 0.57417 0.46665 0.00791  -0.05695 -0.00386 62  GLY   A C   
369  O  O   . GLY   A 62  ? 0.36589 0.52066 0.41996 0.00398  -0.06589 -0.00228 62  GLY   A O   
370  N  N   . PHE   A 63  ? 0.34212 0.48859 0.37598 0.01073  -0.05374 -0.01011 63  PHE   A N   
371  C  CA  . PHE   A 63  ? 0.39653 0.53334 0.41998 0.01139  -0.06070 -0.01635 63  PHE   A CA  
372  C  C   . PHE   A 63  ? 0.42958 0.56092 0.44446 0.01385  -0.05602 -0.02225 63  PHE   A C   
373  O  O   . PHE   A 63  ? 0.39478 0.52827 0.40346 0.01648  -0.04757 -0.02260 63  PHE   A O   
374  C  CB  . PHE   A 63  ? 0.39899 0.53383 0.41120 0.01435  -0.06251 -0.01767 63  PHE   A CB  
375  C  CG  . PHE   A 63  ? 0.35364 0.49459 0.37357 0.01279  -0.06667 -0.01186 63  PHE   A CG  
376  C  CD1 . PHE   A 63  ? 0.37089 0.52018 0.39651 0.01390  -0.06027 -0.00642 63  PHE   A CD1 
377  C  CD2 . PHE   A 63  ? 0.42110 0.55914 0.44212 0.01075  -0.07765 -0.01200 63  PHE   A CD2 
378  C  CE1 . PHE   A 63  ? 0.39793 0.55418 0.43068 0.01361  -0.06408 -0.00117 63  PHE   A CE1 
379  C  CE2 . PHE   A 63  ? 0.44868 0.59433 0.47816 0.00928  -0.08159 -0.00596 63  PHE   A CE2 
380  C  CZ  . PHE   A 63  ? 0.41114 0.56661 0.44652 0.01110  -0.07428 -0.00063 63  PHE   A CZ  
381  N  N   . GLU   A 64  ? 0.40904 0.53317 0.42324 0.01308  -0.06228 -0.02662 64  GLU   A N   
382  C  CA  . GLU   A 64  ? 0.41437 0.53314 0.41851 0.01691  -0.05923 -0.03335 64  GLU   A CA  
383  C  C   . GLU   A 64  ? 0.46670 0.58172 0.45445 0.02217  -0.06082 -0.03869 64  GLU   A C   
384  O  O   . GLU   A 64  ? 0.41521 0.52378 0.39826 0.02276  -0.07054 -0.04134 64  GLU   A O   
385  C  CB  . GLU   A 64  ? 0.39184 0.50239 0.39896 0.01541  -0.06707 -0.03682 64  GLU   A CB  
386  C  CG  . GLU   A 64  ? 0.43851 0.55269 0.46039 0.01053  -0.06502 -0.03200 64  GLU   A CG  
387  C  CD  . GLU   A 64  ? 0.46220 0.56613 0.48490 0.00919  -0.07371 -0.03579 64  GLU   A CD  
388  O  OE1 . GLU   A 64  ? 0.47088 0.56499 0.48050 0.01428  -0.07809 -0.04396 64  GLU   A OE1 
389  O  OE2 . GLU   A 64  ? 0.46473 0.57023 0.50043 0.00346  -0.07688 -0.03054 64  GLU   A OE2 
390  N  N   . PRO   A 65  ? 0.46857 0.58771 0.44690 0.02601  -0.05210 -0.04012 65  PRO   A N   
391  C  CA  . PRO   A 65  ? 0.49011 0.60724 0.45223 0.03144  -0.05394 -0.04497 65  PRO   A CA  
392  C  C   . PRO   A 65  ? 0.49682 0.60664 0.45047 0.03629  -0.05910 -0.05329 65  PRO   A C   
393  O  O   . PRO   A 65  ? 0.55010 0.66300 0.49963 0.03965  -0.05296 -0.05613 65  PRO   A O   
394  C  CB  . PRO   A 65  ? 0.49904 0.62473 0.45577 0.03285  -0.04304 -0.04212 65  PRO   A CB  
395  C  CG  . PRO   A 65  ? 0.48133 0.61139 0.45165 0.02774  -0.03742 -0.03516 65  PRO   A CG  
396  C  CD  . PRO   A 65  ? 0.40610 0.53263 0.38780 0.02517  -0.04110 -0.03617 65  PRO   A CD  
397  N  N   . SER   A 66  ? 0.52548 0.62524 0.47661 0.03686  -0.07104 -0.05721 66  SER   A N   
398  C  CA  . SER   A 66  ? 0.57415 0.66364 0.51891 0.04109  -0.07841 -0.06516 66  SER   A CA  
399  C  C   . SER   A 66  ? 0.72241 0.80416 0.64907 0.04894  -0.08633 -0.07319 66  SER   A C   
400  O  O   . SER   A 66  ? 0.80687 0.87897 0.72583 0.05420  -0.09302 -0.08084 66  SER   A O   
401  C  CB  . SER   A 66  ? 0.60451 0.68531 0.56212 0.03463  -0.08852 -0.06318 66  SER   A CB  
402  O  OG  . SER   A 66  ? 0.69343 0.77229 0.65527 0.03022  -0.09660 -0.05916 66  SER   A OG  
403  N  N   . GLY   A 67  ? 0.57800 0.66286 0.49700 0.05042  -0.08648 -0.07195 67  GLY   A N   
404  C  CA  . GLY   A 67  ? 0.73840 0.81536 0.64016 0.05769  -0.09528 -0.07915 67  GLY   A CA  
405  C  C   . GLY   A 67  ? 0.67078 0.74979 0.57175 0.05485  -0.09779 -0.07456 67  GLY   A C   
406  O  O   . GLY   A 67  ? 0.68899 0.77877 0.59630 0.05090  -0.08886 -0.06724 67  GLY   A O   
407  N  N   . ARG   A 68  ? 0.69429 0.76210 0.58592 0.05763  -0.11047 -0.07934 68  ARG   A N   
408  C  CA  . ARG   A 68  ? 0.69838 0.76745 0.58942 0.05494  -0.11405 -0.07513 68  ARG   A CA  
409  C  C   . ARG   A 68  ? 0.65097 0.72319 0.56292 0.04438  -0.11527 -0.06591 68  ARG   A C   
410  O  O   . ARG   A 68  ? 0.67189 0.74173 0.59773 0.03892  -0.11777 -0.06370 68  ARG   A O   
411  C  CB  . ARG   A 68  ? 0.69946 0.75466 0.57591 0.06014  -0.12875 -0.08248 68  ARG   A CB  
412  C  CG  . ARG   A 68  ? 0.75839 0.81387 0.61131 0.07238  -0.12670 -0.09088 68  ARG   A CG  
413  C  CD  . ARG   A 68  ? 0.93401 0.97819 0.77122 0.07746  -0.14000 -0.09636 68  ARG   A CD  
414  N  NE  . ARG   A 68  ? 0.95646 0.98105 0.79104 0.07819  -0.15728 -0.10298 68  ARG   A NE  
415  C  CZ  . ARG   A 68  ? 0.95230 0.96414 0.77739 0.07989  -0.17177 -0.10661 68  ARG   A CZ  
416  N  NH1 . ARG   A 68  ? 0.91216 0.92918 0.72983 0.08114  -0.17087 -0.10433 68  ARG   A NH1 
417  N  NH2 . ARG   A 68  ? 1.02604 1.01850 0.84849 0.08024  -0.18840 -0.11257 68  ARG   A NH2 
418  N  N   . MET   A 69  ? 0.66675 0.74565 0.58074 0.04195  -0.11304 -0.06010 69  MET   A N   
419  C  CA  . MET   A 69  ? 0.58019 0.66460 0.51294 0.03365  -0.11357 -0.05128 69  MET   A CA  
420  C  C   . MET   A 69  ? 0.61575 0.69158 0.55243 0.03005  -0.12901 -0.05104 69  MET   A C   
421  O  O   . MET   A 69  ? 0.66446 0.73519 0.58968 0.03314  -0.13603 -0.05377 69  MET   A O   
422  C  CB  . MET   A 69  ? 0.58963 0.68480 0.52317 0.03315  -0.10452 -0.04499 69  MET   A CB  
423  C  CG  . MET   A 69  ? 0.51355 0.61582 0.46661 0.02620  -0.10439 -0.03627 69  MET   A CG  
424  S  SD  . MET   A 69  ? 0.52430 0.63648 0.47866 0.02618  -0.09654 -0.02917 69  MET   A SD  
425  C  CE  . MET   A 69  ? 0.49628 0.61316 0.44652 0.02843  -0.08208 -0.02955 69  MET   A CE  
426  N  N   . HIS   A 70  ? 0.59198 0.66725 0.54545 0.02300  -0.13436 -0.04681 70  HIS   A N   
427  C  CA  . HIS   A 70  ? 0.65899 0.72822 0.61963 0.01760  -0.14937 -0.04434 70  HIS   A CA  
428  C  C   . HIS   A 70  ? 0.55989 0.63857 0.52620 0.01529  -0.14898 -0.03755 70  HIS   A C   
429  O  O   . HIS   A 70  ? 0.54330 0.63479 0.51651 0.01490  -0.13737 -0.03196 70  HIS   A O   
430  C  CB  . HIS   A 70  ? 0.59054 0.66116 0.57013 0.00958  -0.15298 -0.03900 70  HIS   A CB  
431  C  CG  . HIS   A 70  ? 0.61716 0.67972 0.60420 0.00295  -0.17049 -0.03643 70  HIS   A CG  
432  N  ND1 . HIS   A 70  ? 0.61669 0.68629 0.61341 -0.00198 -0.17639 -0.02926 70  HIS   A ND1 
433  C  CD2 . HIS   A 70  ? 0.62719 0.67527 0.61408 -0.00005 -0.18407 -0.03940 70  HIS   A CD2 
434  C  CE1 . HIS   A 70  ? 0.55886 0.61923 0.56110 -0.00814 -0.19287 -0.02768 70  HIS   A CE1 
435  N  NE2 . HIS   A 70  ? 0.60866 0.65486 0.60475 -0.00729 -0.19835 -0.03375 70  HIS   A NE2 
436  N  N   . ILE   A 71  ? 0.54281 0.61447 0.50597 0.01401  -0.16250 -0.03806 71  ILE   A N   
437  C  CA  . ILE   A 71  ? 0.52153 0.60245 0.48996 0.01232  -0.16243 -0.03172 71  ILE   A CA  
438  C  C   . ILE   A 71  ? 0.47235 0.56904 0.46396 0.00566  -0.15744 -0.02117 71  ILE   A C   
439  O  O   . ILE   A 71  ? 0.49786 0.60604 0.49404 0.00650  -0.15025 -0.01592 71  ILE   A O   
440  C  CB  . ILE   A 71  ? 0.51879 0.58932 0.48174 0.01116  -0.17936 -0.03359 71  ILE   A CB  
441  C  CG1 . ILE   A 71  ? 0.55213 0.63140 0.51743 0.01090  -0.17936 -0.02816 71  ILE   A CG1 
442  C  CG2 . ILE   A 71  ? 0.57859 0.64549 0.55695 0.00259  -0.19264 -0.02948 71  ILE   A CG2 
443  C  CD1 . ILE   A 71  ? 0.65187 0.71974 0.60950 0.01039  -0.19642 -0.03080 71  ILE   A CD1 
444  N  N   . ALA   A 72  ? 0.49502 0.59286 0.50069 -0.00029 -0.16067 -0.01792 72  ALA   A N   
445  C  CA  . ALA   A 72  ? 0.56629 0.68141 0.59333 -0.00554 -0.15465 -0.00776 72  ALA   A CA  
446  C  C   . ALA   A 72  ? 0.53642 0.66130 0.56280 -0.00097 -0.13762 -0.00686 72  ALA   A C   
447  O  O   . ALA   A 72  ? 0.47870 0.61798 0.51651 -0.00153 -0.13159 0.00032  72  ALA   A O   
448  C  CB  . ALA   A 72  ? 0.49601 0.61090 0.53711 -0.01275 -0.16037 -0.00417 72  ALA   A CB  
449  N  N   . GLN   A 73  ? 0.49369 0.61111 0.50662 0.00394  -0.13022 -0.01394 73  GLN   A N   
450  C  CA  . GLN   A 73  ? 0.45545 0.58066 0.46809 0.00723  -0.11540 -0.01276 73  GLN   A CA  
451  C  C   . GLN   A 73  ? 0.50709 0.63399 0.50836 0.01234  -0.10963 -0.01328 73  GLN   A C   
452  O  O   . GLN   A 73  ? 0.43971 0.57296 0.44163 0.01447  -0.09870 -0.01092 73  GLN   A O   
453  C  CB  . GLN   A 73  ? 0.41972 0.53764 0.42422 0.00961  -0.11012 -0.01919 73  GLN   A CB  
454  C  CG  . GLN   A 73  ? 0.47658 0.59249 0.49261 0.00439  -0.11559 -0.01798 73  GLN   A CG  
455  C  CD  . GLN   A 73  ? 0.60304 0.70871 0.60898 0.00739  -0.11407 -0.02573 73  GLN   A CD  
456  O  OE1 . GLN   A 73  ? 0.63201 0.73167 0.62112 0.01365  -0.11135 -0.03264 73  GLN   A OE1 
457  N  NE2 . GLN   A 73  ? 0.48997 0.59446 0.50594 0.00324  -0.11599 -0.02434 73  GLN   A NE2 
458  N  N   . GLY   A 74  ? 0.55443 0.67537 0.54553 0.01404  -0.11749 -0.01578 74  GLY   A N   
459  C  CA  . GLY   A 74  ? 0.52215 0.64433 0.50229 0.01829  -0.11344 -0.01550 74  GLY   A CA  
460  C  C   . GLY   A 74  ? 0.54353 0.67117 0.53115 0.01660  -0.12019 -0.00995 74  GLY   A C   
461  O  O   . GLY   A 74  ? 0.62024 0.75771 0.61631 0.01693  -0.11468 -0.00401 74  GLY   A O   
462  N  N   . LEU   A 75  ? 0.52984 0.65131 0.51480 0.01512  -0.13268 -0.01173 75  LEU   A N   
463  C  CA  . LEU   A 75  ? 0.55283 0.68004 0.54411 0.01383  -0.13933 -0.00640 75  LEU   A CA  
464  C  C   . LEU   A 75  ? 0.56166 0.70314 0.57578 0.00908  -0.13963 0.00223  75  LEU   A C   
465  O  O   . LEU   A 75  ? 0.56338 0.71565 0.58462 0.01045  -0.13691 0.00803  75  LEU   A O   
466  C  CB  . LEU   A 75  ? 0.58605 0.70291 0.56993 0.01275  -0.15404 -0.01005 75  LEU   A CB  
467  C  CG  . LEU   A 75  ? 0.68247 0.78762 0.64261 0.01884  -0.15517 -0.01775 75  LEU   A CG  
468  C  CD1 . LEU   A 75  ? 0.65325 0.74846 0.60770 0.01781  -0.17128 -0.02071 75  LEU   A CD1 
469  C  CD2 . LEU   A 75  ? 0.67492 0.78572 0.62807 0.02290  -0.14657 -0.01507 75  LEU   A CD2 
470  N  N   . LEU   A 76  ? 0.52841 0.67054 0.55400 0.00369  -0.14399 0.00349  76  LEU   A N   
471  C  CA  . LEU   A 76  ? 0.52084 0.67894 0.56863 -0.00116 -0.14450 0.01269  76  LEU   A CA  
472  C  C   . LEU   A 76  ? 0.49465 0.66433 0.54818 0.00237  -0.13028 0.01603  76  LEU   A C   
473  O  O   . LEU   A 76  ? 0.49335 0.67831 0.55937 0.00312  -0.12774 0.02319  76  LEU   A O   
474  C  CB  . LEU   A 76  ? 0.48099 0.63638 0.53879 -0.00837 -0.15281 0.01393  76  LEU   A CB  
475  C  CG  . LEU   A 76  ? 0.42179 0.59712 0.50307 -0.01325 -0.15082 0.02463  76  LEU   A CG  
476  C  CD1 . LEU   A 76  ? 0.50544 0.69383 0.59942 -0.01625 -0.15943 0.03281  76  LEU   A CD1 
477  C  CD2 . LEU   A 76  ? 0.56019 0.73383 0.65107 -0.02014 -0.15520 0.02654  76  LEU   A CD2 
478  N  N   . LYS   A 77  ? 0.49383 0.65664 0.53807 0.00512  -0.12126 0.01088  77  LYS   A N   
479  C  CA  . LYS   A 77  ? 0.50026 0.67167 0.54815 0.00868  -0.10881 0.01351  77  LYS   A CA  
480  C  C   . LYS   A 77  ? 0.51521 0.69056 0.55844 0.01394  -0.10566 0.01560  77  LYS   A C   
481  O  O   . LYS   A 77  ? 0.46929 0.65655 0.52195 0.01649  -0.10059 0.02090  77  LYS   A O   
482  C  CB  . LYS   A 77  ? 0.40285 0.56464 0.43956 0.01056  -0.10087 0.00725  77  LYS   A CB  
483  C  CG  . LYS   A 77  ? 0.49132 0.65875 0.53014 0.01371  -0.08879 0.00898  77  LYS   A CG  
484  C  CD  . LYS   A 77  ? 0.55100 0.73227 0.60784 0.01191  -0.08600 0.01541  77  LYS   A CD  
485  C  CE  . LYS   A 77  ? 0.47817 0.66348 0.54767 0.00542  -0.09446 0.01840  77  LYS   A CE  
486  N  NZ  . LYS   A 77  ? 0.39688 0.59871 0.48303 0.00466  -0.09046 0.02586  77  LYS   A NZ  
487  N  N   . SER   A 78  ? 0.51780 0.68312 0.54573 0.01625  -0.10892 0.01149  78  SER   A N   
488  C  CA  . SER   A 78  ? 0.53241 0.70009 0.55517 0.02108  -0.10625 0.01376  78  SER   A CA  
489  C  C   . SER   A 78  ? 0.49817 0.67865 0.53492 0.02086  -0.11221 0.02044  78  SER   A C   
490  O  O   . SER   A 78  ? 0.49931 0.68744 0.53931 0.02548  -0.10792 0.02425  78  SER   A O   
491  C  CB  . SER   A 78  ? 0.64178 0.79713 0.64502 0.02332  -0.10861 0.00883  78  SER   A CB  
492  O  OG  . SER   A 78  ? 0.65282 0.80468 0.65440 0.02115  -0.11987 0.00758  78  SER   A OG  
493  N  N   . ILE   A 79  ? 0.52863 0.71224 0.57443 0.01575  -0.12237 0.02233  79  ILE   A N   
494  C  CA  . ILE   A 79  ? 0.54828 0.74739 0.60966 0.01512  -0.12778 0.02995  79  ILE   A CA  
495  C  C   . ILE   A 79  ? 0.53093 0.74727 0.60837 0.01664  -0.12014 0.03612  79  ILE   A C   
496  O  O   . ILE   A 79  ? 0.47574 0.70477 0.55980 0.02167  -0.11775 0.04098  79  ILE   A O   
497  C  CB  . ILE   A 79  ? 0.59907 0.79883 0.66884 0.00789  -0.14103 0.03195  79  ILE   A CB  
498  C  CG1 . ILE   A 79  ? 0.65647 0.84045 0.71007 0.00789  -0.14998 0.02614  79  ILE   A CG1 
499  C  CG2 . ILE   A 79  ? 0.54595 0.76620 0.63565 0.00626  -0.14557 0.04157  79  ILE   A CG2 
500  C  CD1 . ILE   A 79  ? 0.62384 0.80123 0.68086 0.00083  -0.16238 0.02515  79  ILE   A CD1 
501  N  N   . ILE   A 80  ? 0.45206 0.66927 0.53545 0.01297  -0.11655 0.03590  80  ILE   A N   
502  C  CA  . ILE   A 80  ? 0.45665 0.69067 0.55479 0.01435  -0.10939 0.04176  80  ILE   A CA  
503  C  C   . ILE   A 80  ? 0.48495 0.71841 0.57519 0.02299  -0.09860 0.04000  80  ILE   A C   
504  O  O   . ILE   A 80  ? 0.38512 0.63372 0.48437 0.02829  -0.09460 0.04508  80  ILE   A O   
505  C  CB  . ILE   A 80  ? 0.45374 0.68605 0.55760 0.00838  -0.10820 0.04129  80  ILE   A CB  
506  C  CG1 . ILE   A 80  ? 0.46204 0.69362 0.57413 -0.00056 -0.12080 0.04374  80  ILE   A CG1 
507  C  CG2 . ILE   A 80  ? 0.46285 0.71112 0.57870 0.01095  -0.09903 0.04643  80  ILE   A CG2 
508  C  CD1 . ILE   A 80  ? 0.48257 0.70489 0.59456 -0.00629 -0.12221 0.04093  80  ILE   A CD1 
509  N  N   . VAL   A 81  ? 0.39838 0.61476 0.47171 0.02470  -0.09396 0.03301  81  VAL   A N   
510  C  CA  . VAL   A 81  ? 0.41662 0.63034 0.48219 0.03173  -0.08505 0.03171  81  VAL   A CA  
511  C  C   . VAL   A 81  ? 0.39719 0.61420 0.45993 0.03808  -0.08705 0.03408  81  VAL   A C   
512  O  O   . VAL   A 81  ? 0.42905 0.65181 0.49324 0.04496  -0.08204 0.03610  81  VAL   A O   
513  C  CB  . VAL   A 81  ? 0.41962 0.61562 0.46825 0.03126  -0.08054 0.02496  81  VAL   A CB  
514  C  CG1 . VAL   A 81  ? 0.43760 0.62890 0.47695 0.03784  -0.07411 0.02453  81  VAL   A CG1 
515  C  CG2 . VAL   A 81  ? 0.46373 0.65881 0.51653 0.02722  -0.07660 0.02308  81  VAL   A CG2 
516  N  N   . ASN   A 82  ? 0.41430 0.62600 0.47117 0.03662  -0.09479 0.03328  82  ASN   A N   
517  C  CA  . ASN   A 82  ? 0.43391 0.64819 0.48791 0.04263  -0.09747 0.03561  82  ASN   A CA  
518  C  C   . ASN   A 82  ? 0.45420 0.68986 0.52602 0.04618  -0.09862 0.04250  82  ASN   A C   
519  O  O   . ASN   A 82  ? 0.49820 0.73873 0.56928 0.05454  -0.09596 0.04429  82  ASN   A O   
520  C  CB  . ASN   A 82  ? 0.48054 0.68638 0.52606 0.03976  -0.10626 0.03381  82  ASN   A CB  
521  C  CG  . ASN   A 82  ? 0.56044 0.74808 0.58585 0.04008  -0.10416 0.02833  82  ASN   A CG  
522  O  OD1 . ASN   A 82  ? 0.59879 0.78013 0.61617 0.04338  -0.09690 0.02698  82  ASN   A OD1 
523  N  ND2 . ASN   A 82  ? 0.57432 0.75361 0.59087 0.03679  -0.11089 0.02547  82  ASN   A ND2 
524  N  N   . LYS   A 83  ? 0.46952 0.71851 0.55735 0.04020  -0.10268 0.04671  83  LYS   A N   
525  C  CA  . LYS   A 83  ? 0.44164 0.71503 0.54839 0.04294  -0.10252 0.05455  83  LYS   A CA  
526  C  C   . LYS   A 83  ? 0.47761 0.75830 0.58619 0.05057  -0.09231 0.05521  83  LYS   A C   
527  O  O   . LYS   A 83  ? 0.47053 0.76407 0.58330 0.05967  -0.09022 0.05850  83  LYS   A O   
528  C  CB  . LYS   A 83  ? 0.53671 0.82066 0.65925 0.03315  -0.10800 0.05922  83  LYS   A CB  
529  C  CG  . LYS   A 83  ? 0.58326 0.89498 0.72713 0.03333  -0.11103 0.06925  83  LYS   A CG  
530  C  CD  . LYS   A 83  ? 0.60875 0.92362 0.75315 0.03460  -0.11989 0.07141  83  LYS   A CD  
531  C  CE  . LYS   A 83  ? 0.73618 1.07054 0.90084 0.02673  -0.12944 0.08057  83  LYS   A CE  
532  N  NZ  . LYS   A 83  ? 0.75362 1.07313 0.91626 0.01499  -0.13909 0.07839  83  LYS   A NZ  
533  N  N   . LEU   A 84  ? 0.40936 0.68106 0.51350 0.04788  -0.08615 0.05154  84  LEU   A N   
534  C  CA  . LEU   A 84  ? 0.40402 0.68293 0.51054 0.05455  -0.07730 0.05231  84  LEU   A CA  
535  C  C   . LEU   A 84  ? 0.45758 0.72521 0.54925 0.06461  -0.07355 0.04839  84  LEU   A C   
536  O  O   . LEU   A 84  ? 0.41367 0.69213 0.50855 0.07412  -0.06980 0.05056  84  LEU   A O   
537  C  CB  . LEU   A 84  ? 0.38184 0.65340 0.48745 0.04864  -0.07243 0.04947  84  LEU   A CB  
538  C  CG  . LEU   A 84  ? 0.44014 0.72330 0.56141 0.03929  -0.07601 0.05417  84  LEU   A CG  
539  C  CD1 . LEU   A 84  ? 0.45332 0.72356 0.56961 0.03365  -0.07232 0.04959  84  LEU   A CD1 
540  C  CD2 . LEU   A 84  ? 0.49087 0.80136 0.63076 0.04204  -0.07364 0.06292  84  LEU   A CD2 
541  N  N   . THR   A 85  ? 0.44150 0.68733 0.51629 0.06291  -0.07482 0.04281  85  THR   A N   
542  C  CA  . THR   A 85  ? 0.44931 0.68188 0.50933 0.07076  -0.07234 0.03971  85  THR   A CA  
543  C  C   . THR   A 85  ? 0.49125 0.72926 0.55087 0.07871  -0.07719 0.04223  85  THR   A C   
544  O  O   . THR   A 85  ? 0.50821 0.73956 0.55887 0.08767  -0.07581 0.04095  85  THR   A O   
545  C  CB  . THR   A 85  ? 0.46297 0.67296 0.50589 0.06585  -0.07219 0.03451  85  THR   A CB  
546  O  OG1 . THR   A 85  ? 0.48544 0.69106 0.52470 0.06089  -0.07889 0.03410  85  THR   A OG1 
547  C  CG2 . THR   A 85  ? 0.40504 0.60986 0.44772 0.05952  -0.06661 0.03159  85  THR   A CG2 
548  N  N   . SER   A 86  ? 0.44181 0.68999 0.50987 0.07570  -0.08373 0.04555  86  SER   A N   
549  C  CA  . SER   A 86  ? 0.51246 0.76941 0.58260 0.08416  -0.08804 0.04857  86  SER   A CA  
550  C  C   . SER   A 86  ? 0.55789 0.84057 0.64452 0.09138  -0.08546 0.05398  86  SER   A C   
551  O  O   . SER   A 86  ? 0.48649 0.78034 0.57656 0.10014  -0.08855 0.05688  86  SER   A O   
552  C  CB  . SER   A 86  ? 0.50954 0.76599 0.58054 0.07858  -0.09672 0.04991  86  SER   A CB  
553  O  OG  . SER   A 86  ? 0.57979 0.85072 0.66659 0.07034  -0.09980 0.05373  86  SER   A OG  
554  N  N   . ASN   A 87  ? 0.46005 0.75465 0.55812 0.08746  -0.08060 0.05616  87  ASN   A N   
555  C  CA  . ASN   A 87  ? 0.51722 0.83866 0.63086 0.09445  -0.07710 0.06206  87  ASN   A CA  
556  C  C   . ASN   A 87  ? 0.53245 0.85268 0.64179 0.10157  -0.06853 0.05962  87  ASN   A C   
557  O  O   . ASN   A 87  ? 0.49104 0.83068 0.61337 0.10183  -0.06403 0.06398  87  ASN   A O   
558  C  CB  . ASN   A 87  ? 0.41497 0.75690 0.54844 0.08450  -0.07983 0.06907  87  ASN   A CB  
559  C  CG  . ASN   A 87  ? 0.56709 0.91960 0.70900 0.08202  -0.08874 0.07379  87  ASN   A CG  
560  O  OD1 . ASN   A 87  ? 0.52457 0.89388 0.67237 0.09135  -0.08994 0.07773  87  ASN   A OD1 
561  N  ND2 . ASN   A 87  ? 0.51575 0.85770 0.65720 0.07022  -0.09554 0.07298  87  ASN   A ND2 
562  N  N   . GLY   A 88  ? 0.48599 0.78323 0.57697 0.10685  -0.06657 0.05307  88  GLY   A N   
563  C  CA  . GLY   A 88  ? 0.48744 0.78321 0.57340 0.11552  -0.05994 0.05072  88  GLY   A CA  
564  C  C   . GLY   A 88  ? 0.46009 0.74547 0.54333 0.10790  -0.05442 0.04779  88  GLY   A C   
565  O  O   . GLY   A 88  ? 0.51090 0.80117 0.59451 0.11408  -0.04872 0.04731  88  GLY   A O   
566  N  N   . CYS   A 89  ? 0.43988 0.71323 0.52124 0.09523  -0.05603 0.04605  89  CYS   A N   
567  C  CA  . CYS   A 89  ? 0.39615 0.66053 0.47576 0.08752  -0.05135 0.04334  89  CYS   A CA  
568  C  C   . CYS   A 89  ? 0.49300 0.73055 0.55484 0.08396  -0.05165 0.03728  89  CYS   A C   
569  O  O   . CYS   A 89  ? 0.46435 0.69083 0.51706 0.08358  -0.05646 0.03593  89  CYS   A O   
570  C  CB  . CYS   A 89  ? 0.47510 0.74890 0.56780 0.07570  -0.05314 0.04645  89  CYS   A CB  
571  S  SG  . CYS   A 89  ? 0.50599 0.81428 0.62276 0.07617  -0.05373 0.05612  89  CYS   A SG  
572  N  N   . THR   A 90  ? 0.38456 0.61319 0.44219 0.08096  -0.04648 0.03431  90  THR   A N   
573  C  CA  . THR   A 90  ? 0.46374 0.67097 0.50775 0.07503  -0.04593 0.02970  90  THR   A CA  
574  C  C   . THR   A 90  ? 0.45464 0.66388 0.50518 0.06497  -0.04405 0.02902  90  THR   A C   
575  O  O   . THR   A 90  ? 0.44977 0.67324 0.51307 0.06380  -0.04171 0.03165  90  THR   A O   
576  C  CB  . THR   A 90  ? 0.46633 0.66017 0.49899 0.08037  -0.04230 0.02678  90  THR   A CB  
577  O  OG1 . THR   A 90  ? 0.48077 0.68376 0.52113 0.08198  -0.03682 0.02717  90  THR   A OG1 
578  C  CG2 . THR   A 90  ? 0.52255 0.71327 0.54821 0.09167  -0.04546 0.02716  90  THR   A CG2 
579  N  N   . PHE   A 91  ? 0.42396 0.61991 0.46583 0.05799  -0.04568 0.02586  91  PHE   A N   
580  C  CA  . PHE   A 91  ? 0.38082 0.57839 0.42818 0.04942  -0.04618 0.02483  91  PHE   A CA  
581  C  C   . PHE   A 91  ? 0.41431 0.59740 0.45085 0.04555  -0.04244 0.02031  91  PHE   A C   
582  O  O   . PHE   A 91  ? 0.43314 0.60403 0.45665 0.04604  -0.04275 0.01842  91  PHE   A O   
583  C  CB  . PHE   A 91  ? 0.40600 0.60525 0.45511 0.04500  -0.05361 0.02551  91  PHE   A CB  
584  C  CG  . PHE   A 91  ? 0.42326 0.62679 0.48118 0.03754  -0.05586 0.02541  91  PHE   A CG  
585  C  CD1 . PHE   A 91  ? 0.40544 0.59710 0.45535 0.03256  -0.05513 0.02051  91  PHE   A CD1 
586  C  CD2 . PHE   A 91  ? 0.45546 0.67538 0.52982 0.03588  -0.05846 0.03061  91  PHE   A CD2 
587  C  CE1 . PHE   A 91  ? 0.37430 0.56791 0.43151 0.02642  -0.05800 0.01992  91  PHE   A CE1 
588  C  CE2 . PHE   A 91  ? 0.46355 0.68571 0.54594 0.02843  -0.06164 0.03110  91  PHE   A CE2 
589  C  CZ  . PHE   A 91  ? 0.35484 0.56260 0.42815 0.02402  -0.06156 0.02530  91  PHE   A CZ  
590  N  N   . ILE   A 92  ? 0.35740 0.54288 0.39968 0.04189  -0.03898 0.01928  92  ILE   A N   
591  C  CA  . ILE   A 92  ? 0.35297 0.52732 0.38693 0.03814  -0.03532 0.01517  92  ILE   A CA  
592  C  C   . ILE   A 92  ? 0.38984 0.56317 0.42525 0.03179  -0.03855 0.01276  92  ILE   A C   
593  O  O   . ILE   A 92  ? 0.41072 0.59222 0.45760 0.02893  -0.04056 0.01426  92  ILE   A O   
594  C  CB  . ILE   A 92  ? 0.37109 0.54725 0.40901 0.03956  -0.02923 0.01511  92  ILE   A CB  
595  C  CG1 . ILE   A 92  ? 0.38888 0.56206 0.42153 0.04683  -0.02723 0.01629  92  ILE   A CG1 
596  C  CG2 . ILE   A 92  ? 0.31742 0.48463 0.34942 0.03465  -0.02602 0.01107  92  ILE   A CG2 
597  C  CD1 . ILE   A 92  ? 0.39296 0.56993 0.43015 0.05031  -0.02201 0.01667  92  ILE   A CD1 
598  N  N   . PHE   A 93  ? 0.32959 0.49282 0.35295 0.02975  -0.03917 0.00915  93  PHE   A N   
599  C  CA  . PHE   A 93  ? 0.36429 0.52429 0.38596 0.02539  -0.04129 0.00531  93  PHE   A CA  
600  C  C   . PHE   A 93  ? 0.35480 0.51105 0.37408 0.02439  -0.03491 0.00274  93  PHE   A C   
601  O  O   . PHE   A 93  ? 0.39622 0.54685 0.40612 0.02551  -0.03078 0.00205  93  PHE   A O   
602  C  CB  . PHE   A 93  ? 0.35464 0.50758 0.36354 0.02504  -0.04488 0.00259  93  PHE   A CB  
603  C  CG  . PHE   A 93  ? 0.38966 0.54506 0.40044 0.02506  -0.05262 0.00403  93  PHE   A CG  
604  C  CD1 . PHE   A 93  ? 0.41533 0.57361 0.42663 0.02820  -0.05401 0.00787  93  PHE   A CD1 
605  C  CD2 . PHE   A 93  ? 0.38743 0.54123 0.39865 0.02227  -0.05935 0.00132  93  PHE   A CD2 
606  C  CE1 . PHE   A 93  ? 0.39230 0.55353 0.40575 0.02818  -0.06161 0.00945  93  PHE   A CE1 
607  C  CE2 . PHE   A 93  ? 0.41478 0.57017 0.42749 0.02189  -0.06742 0.00275  93  PHE   A CE2 
608  C  CZ  . PHE   A 93  ? 0.45598 0.61589 0.47036 0.02466  -0.06820 0.00705  93  PHE   A CZ  
609  N  N   . TRP   A 94  ? 0.34727 0.50661 0.37513 0.02188  -0.03464 0.00188  94  TRP   A N   
610  C  CA  . TRP   A 94  ? 0.36590 0.52244 0.39279 0.02104  -0.02893 -0.00047 94  TRP   A CA  
611  C  C   . TRP   A 94  ? 0.40202 0.55278 0.42219 0.01899  -0.03092 -0.00575 94  TRP   A C   
612  O  O   . TRP   A 94  ? 0.38429 0.53498 0.40900 0.01677  -0.03655 -0.00728 94  TRP   A O   
613  C  CB  . TRP   A 94  ? 0.36328 0.52724 0.40345 0.02021  -0.02768 0.00231  94  TRP   A CB  
614  C  CG  . TRP   A 94  ? 0.36590 0.52875 0.40813 0.01937  -0.02250 0.00089  94  TRP   A CG  
615  C  CD1 . TRP   A 94  ? 0.32583 0.48967 0.37471 0.01615  -0.02383 -0.00014 94  TRP   A CD1 
616  C  CD2 . TRP   A 94  ? 0.31013 0.47039 0.34827 0.02174  -0.01597 0.00087  94  TRP   A CD2 
617  N  NE1 . TRP   A 94  ? 0.31961 0.48279 0.36940 0.01664  -0.01776 -0.00074 94  TRP   A NE1 
618  C  CE2 . TRP   A 94  ? 0.35891 0.52014 0.40243 0.02008  -0.01304 -0.00006 94  TRP   A CE2 
619  C  CE3 . TRP   A 94  ? 0.35362 0.51036 0.38460 0.02506  -0.01335 0.00209  94  TRP   A CE3 
620  C  CZ2 . TRP   A 94  ? 0.36710 0.52591 0.40843 0.02161  -0.00726 -0.00033 94  TRP   A CZ2 
621  C  CZ3 . TRP   A 94  ? 0.41907 0.57253 0.44795 0.02637  -0.00822 0.00199  94  TRP   A CZ3 
622  C  CH2 . TRP   A 94  ? 0.37323 0.52812 0.40734 0.02470  -0.00517 0.00072  94  TRP   A CH2 
623  N  N   . ILE   A 95  ? 0.37797 0.52402 0.38666 0.02003  -0.02722 -0.00822 95  ILE   A N   
624  C  CA  . ILE   A 95  ? 0.37504 0.51731 0.37574 0.01991  -0.02822 -0.01347 95  ILE   A CA  
625  C  C   . ILE   A 95  ? 0.41070 0.55303 0.41652 0.01888  -0.02476 -0.01553 95  ILE   A C   
626  O  O   . ILE   A 95  ? 0.38611 0.52903 0.39088 0.01906  -0.01838 -0.01458 95  ILE   A O   
627  C  CB  . ILE   A 95  ? 0.43736 0.57802 0.42488 0.02142  -0.02478 -0.01395 95  ILE   A CB  
628  C  CG1 . ILE   A 95  ? 0.48388 0.62420 0.46716 0.02222  -0.02707 -0.01027 95  ILE   A CG1 
629  C  CG2 . ILE   A 95  ? 0.42182 0.56090 0.40020 0.02296  -0.02605 -0.01959 95  ILE   A CG2 
630  C  CD1 . ILE   A 95  ? 0.50759 0.64781 0.49274 0.02249  -0.03435 -0.01073 95  ILE   A CD1 
631  N  N   . ALA   A 96  ? 0.37128 0.51224 0.38265 0.01748  -0.02978 -0.01797 96  ALA   A N   
632  C  CA  . ALA   A 96  ? 0.40694 0.54818 0.42595 0.01594  -0.02781 -0.01865 96  ALA   A CA  
633  C  C   . ALA   A 96  ? 0.38171 0.51872 0.39222 0.01780  -0.02635 -0.02469 96  ALA   A C   
634  O  O   . ALA   A 96  ? 0.37096 0.50354 0.38153 0.01782  -0.03133 -0.02878 96  ALA   A O   
635  C  CB  . ALA   A 96  ? 0.36382 0.50596 0.39394 0.01277  -0.03487 -0.01678 96  ALA   A CB  
636  N  N   . ASP   A 97  ? 0.39202 0.53062 0.39424 0.01970  -0.02016 -0.02495 97  ASP   A N   
637  C  CA  . ASP   A 97  ? 0.40950 0.54732 0.40241 0.02251  -0.01827 -0.03008 97  ASP   A CA  
638  C  C   . ASP   A 97  ? 0.37917 0.51609 0.37766 0.02217  -0.01640 -0.03243 97  ASP   A C   
639  O  O   . ASP   A 97  ? 0.40969 0.54309 0.40435 0.02464  -0.01986 -0.03807 97  ASP   A O   
640  C  CB  . ASP   A 97  ? 0.39585 0.53805 0.38035 0.02343  -0.01195 -0.02778 97  ASP   A CB  
641  C  CG  . ASP   A 97  ? 0.46192 0.60607 0.45216 0.02072  -0.00604 -0.02221 97  ASP   A CG  
642  O  OD1 . ASP   A 97  ? 0.42241 0.56567 0.42241 0.01910  -0.00581 -0.02025 97  ASP   A OD1 
643  O  OD2 . ASP   A 97  ? 0.43865 0.58530 0.42292 0.02032  -0.00184 -0.01951 97  ASP   A OD2 
644  N  N   . TRP   A 98  ? 0.41065 0.54988 0.41761 0.01969  -0.01163 -0.02846 98  TRP   A N   
645  C  CA  . TRP   A 98  ? 0.38275 0.52098 0.39535 0.01913  -0.01014 -0.03028 98  TRP   A CA  
646  C  C   . TRP   A 98  ? 0.43378 0.56743 0.45260 0.01776  -0.01766 -0.03200 98  TRP   A C   
647  O  O   . TRP   A 98  ? 0.35637 0.48659 0.37589 0.01842  -0.01921 -0.03564 98  TRP   A O   
648  C  CB  . TRP   A 98  ? 0.45053 0.59164 0.47031 0.01708  -0.00439 -0.02559 98  TRP   A CB  
649  C  CG  . TRP   A 98  ? 0.62512 0.76836 0.63993 0.01787  0.00193  -0.02578 98  TRP   A CG  
650  C  CD1 . TRP   A 98  ? 0.64591 0.79142 0.65137 0.02003  0.00366  -0.02851 98  TRP   A CD1 
651  C  CD2 . TRP   A 98  ? 0.52828 0.67259 0.54688 0.01650  0.00710  -0.02256 98  TRP   A CD2 
652  N  NE1 . TRP   A 98  ? 0.61950 0.76839 0.62412 0.01914  0.00957  -0.02636 98  TRP   A NE1 
653  C  CE2 . TRP   A 98  ? 0.61967 0.76653 0.63186 0.01687  0.01130  -0.02298 98  TRP   A CE2 
654  C  CE3 . TRP   A 98  ? 0.48047 0.62442 0.50662 0.01538  0.00832  -0.01910 98  TRP   A CE3 
655  C  CZ2 . TRP   A 98  ? 0.61128 0.75865 0.62506 0.01526  0.01579  -0.02011 98  TRP   A CZ2 
656  C  CZ3 . TRP   A 98  ? 0.56651 0.71009 0.59277 0.01490  0.01303  -0.01709 98  TRP   A CZ3 
657  C  CH2 . TRP   A 98  ? 0.50476 0.64922 0.52519 0.01442  0.01619  -0.01765 98  TRP   A CH2 
658  N  N   . PHE   A 99  ? 0.38653 0.52015 0.41039 0.01552  -0.02302 -0.02886 99  PHE   A N   
659  C  CA  . PHE   A 99  ? 0.36458 0.49408 0.39517 0.01283  -0.03160 -0.02903 99  PHE   A CA  
660  C  C   . PHE   A 99  ? 0.34819 0.46910 0.36924 0.01554  -0.03921 -0.03596 99  PHE   A C   
661  O  O   . PHE   A 99  ? 0.40300 0.51723 0.42612 0.01470  -0.04540 -0.03864 99  PHE   A O   
662  C  CB  . PHE   A 99  ? 0.35351 0.48753 0.39254 0.00957  -0.03543 -0.02288 99  PHE   A CB  
663  C  CG  . PHE   A 99  ? 0.33142 0.47408 0.38012 0.00815  -0.02918 -0.01641 99  PHE   A CG  
664  C  CD1 . PHE   A 99  ? 0.27933 0.42570 0.32411 0.01072  -0.02226 -0.01474 99  PHE   A CD1 
665  C  CD2 . PHE   A 99  ? 0.33297 0.47944 0.39356 0.00466  -0.03064 -0.01214 99  PHE   A CD2 
666  C  CE1 . PHE   A 99  ? 0.30855 0.46151 0.36037 0.01095  -0.01703 -0.00969 99  PHE   A CE1 
667  C  CE2 . PHE   A 99  ? 0.27472 0.43024 0.34327 0.00466  -0.02478 -0.00642 99  PHE   A CE2 
668  C  CZ  . PHE   A 99  ? 0.32079 0.47908 0.38446 0.00844  -0.01796 -0.00571 99  PHE   A CZ  
669  N  N   . ALA   A 100 ? 0.37824 0.49859 0.38818 0.01909  -0.03981 -0.03880 100 ALA   A N   
670  C  CA  . ALA   A 100 ? 0.37376 0.48644 0.37182 0.02370  -0.04633 -0.04632 100 ALA   A CA  
671  C  C   . ALA   A 100 ? 0.45035 0.56115 0.44369 0.02771  -0.04335 -0.05180 100 ALA   A C   
672  O  O   . ALA   A 100 ? 0.43984 0.54165 0.42852 0.03057  -0.05095 -0.05780 100 ALA   A O   
673  C  CB  . ALA   A 100 ? 0.39562 0.51126 0.38152 0.02774  -0.04419 -0.04785 100 ALA   A CB  
674  N  N   . HIS   A 101 ? 0.39348 0.51236 0.38727 0.02834  -0.03290 -0.04987 101 HIS   A N   
675  C  CA  . HIS   A 101 ? 0.40500 0.52435 0.39543 0.03213  -0.02926 -0.05435 101 HIS   A CA  
676  C  C   . HIS   A 101 ? 0.39223 0.50523 0.39183 0.02936  -0.03342 -0.05468 101 HIS   A C   
677  O  O   . HIS   A 101 ? 0.43613 0.54276 0.43130 0.03325  -0.03770 -0.06076 101 HIS   A O   
678  C  CB  . HIS   A 101 ? 0.41460 0.54413 0.40557 0.03170  -0.01813 -0.05060 101 HIS   A CB  
679  C  CG  . HIS   A 101 ? 0.51271 0.64484 0.50323 0.03440  -0.01364 -0.05356 101 HIS   A CG  
680  N  ND1 . HIS   A 101 ? 0.56710 0.70289 0.54705 0.04115  -0.01228 -0.05905 101 HIS   A ND1 
681  C  CD2 . HIS   A 101 ? 0.63507 0.76760 0.63432 0.03172  -0.01027 -0.05166 101 HIS   A CD2 
682  C  CE1 . HIS   A 101 ? 0.59541 0.73425 0.57829 0.04230  -0.00814 -0.06019 101 HIS   A CE1 
683  N  NE2 . HIS   A 101 ? 0.63752 0.77346 0.63190 0.03644  -0.00721 -0.05596 101 HIS   A NE2 
684  N  N   . LEU   A 102 ? 0.40268 0.51776 0.41475 0.02312  -0.03227 -0.04798 102 LEU   A N   
685  C  CA  . LEU   A 102 ? 0.36724 0.47777 0.38873 0.01964  -0.03603 -0.04676 102 LEU   A CA  
686  C  C   . LEU   A 102 ? 0.44117 0.54045 0.46130 0.01913  -0.04875 -0.05001 102 LEU   A C   
687  O  O   . LEU   A 102 ? 0.43498 0.52706 0.45789 0.01831  -0.05387 -0.05180 102 LEU   A O   
688  C  CB  . LEU   A 102 ? 0.47903 0.59625 0.51336 0.01372  -0.03257 -0.03821 102 LEU   A CB  
689  C  CG  . LEU   A 102 ? 0.39513 0.51263 0.44051 0.00967  -0.03266 -0.03440 102 LEU   A CG  
690  C  CD1 . LEU   A 102 ? 0.32579 0.44304 0.36809 0.01276  -0.02633 -0.03810 102 LEU   A CD1 
691  C  CD2 . LEU   A 102 ? 0.28511 0.41213 0.34042 0.00609  -0.02792 -0.02625 102 LEU   A CD2 
692  N  N   . ASN   A 103 ? 0.39417 0.49082 0.41013 0.01916  -0.05501 -0.05036 103 ASN   A N   
693  C  CA  . ASN   A 103 ? 0.43092 0.51578 0.44567 0.01779  -0.06876 -0.05265 103 ASN   A CA  
694  C  C   . ASN   A 103 ? 0.49042 0.56545 0.48877 0.02608  -0.07450 -0.06280 103 ASN   A C   
695  O  O   . ASN   A 103 ? 0.47825 0.54198 0.47145 0.02660  -0.08679 -0.06608 103 ASN   A O   
696  C  CB  . ASN   A 103 ? 0.38854 0.47688 0.40922 0.01277  -0.07287 -0.04652 103 ASN   A CB  
697  C  CG  . ASN   A 103 ? 0.49280 0.57160 0.51913 0.00741  -0.08715 -0.04464 103 ASN   A CG  
698  O  OD1 . ASN   A 103 ? 0.43686 0.50528 0.46332 0.00668  -0.09451 -0.04731 103 ASN   A OD1 
699  N  ND2 . ASN   A 103 ? 0.42686 0.50857 0.45776 0.00340  -0.09224 -0.03974 103 ASN   A ND2 
700  N  N   . ASN   A 104 ? 0.42601 0.50599 0.41568 0.03299  -0.06597 -0.06765 104 ASN   A N   
701  C  CA  . ASN   A 104 ? 0.45688 0.53011 0.43097 0.04256  -0.07009 -0.07751 104 ASN   A CA  
702  C  C   . ASN   A 104 ? 0.53493 0.60593 0.49647 0.04717  -0.07486 -0.08120 104 ASN   A C   
703  O  O   . ASN   A 104 ? 0.56800 0.62910 0.51628 0.05483  -0.08318 -0.08967 104 ASN   A O   
704  C  CB  . ASN   A 104 ? 0.49698 0.55474 0.47032 0.04365  -0.08170 -0.08247 104 ASN   A CB  
705  C  CG  . ASN   A 104 ? 0.68305 0.74325 0.66565 0.04128  -0.07632 -0.08035 104 ASN   A CG  
706  O  OD1 . ASN   A 104 ? 0.64448 0.71649 0.62754 0.04362  -0.06428 -0.07966 104 ASN   A OD1 
707  N  ND2 . ASN   A 104 ? 0.60422 0.65275 0.59384 0.03647  -0.08608 -0.07909 104 ASN   A ND2 
708  N  N   . LYS   A 105 ? 0.50922 0.58925 0.47336 0.04368  -0.06960 -0.07543 105 LYS   A N   
709  C  CA  . LYS   A 105 ? 0.59010 0.66870 0.54231 0.04784  -0.07368 -0.07837 105 LYS   A CA  
710  C  C   . LYS   A 105 ? 0.60913 0.69721 0.54762 0.05663  -0.06511 -0.08264 105 LYS   A C   
711  O  O   . LYS   A 105 ? 0.54815 0.64776 0.48997 0.05641  -0.05381 -0.07969 105 LYS   A O   
712  C  CB  . LYS   A 105 ? 0.54955 0.63411 0.50974 0.04090  -0.07199 -0.07026 105 LYS   A CB  
713  C  CG  . LYS   A 105 ? 0.47002 0.54976 0.44484 0.03215  -0.07951 -0.06440 105 LYS   A CG  
714  C  CD  . LYS   A 105 ? 0.58649 0.64985 0.55687 0.03295  -0.09519 -0.06979 105 LYS   A CD  
715  C  CE  . LYS   A 105 ? 0.65755 0.71762 0.64431 0.02282  -0.10339 -0.06233 105 LYS   A CE  
716  N  NZ  . LYS   A 105 ? 0.65562 0.72387 0.64927 0.01787  -0.10290 -0.05514 105 LYS   A NZ  
717  N  N   . MET   A 106 ? 0.62401 0.70802 0.54688 0.06430  -0.07078 -0.08908 106 MET   A N   
718  C  CA  . MET   A 106 ? 0.65509 0.75128 0.56467 0.07262  -0.06234 -0.09176 106 MET   A CA  
719  C  C   . MET   A 106 ? 0.69484 0.79765 0.60322 0.07796  -0.05552 -0.09501 106 MET   A C   
720  O  O   . MET   A 106 ? 0.66921 0.78770 0.57767 0.07865  -0.04386 -0.09132 106 MET   A O   
721  C  CB  . MET   A 106 ? 0.61410 0.72440 0.52794 0.06735  -0.05184 -0.08295 106 MET   A CB  
722  C  CG  . MET   A 106 ? 0.62847 0.73608 0.54408 0.06218  -0.05602 -0.07832 106 MET   A CG  
723  S  SD  . MET   A 106 ? 0.73952 0.84435 0.63494 0.07093  -0.06262 -0.08447 106 MET   A SD  
724  C  CE  . MET   A 106 ? 0.89805 0.98308 0.78771 0.07591  -0.07843 -0.09454 106 MET   A CE  
725  N  N   . SER   A 107 ? 0.60488 0.69572 0.51347 0.08079  -0.06316 -0.10102 107 SER   A N   
726  C  CA  . SER   A 107 ? 0.75418 0.85022 0.66173 0.08647  -0.05793 -0.10469 107 SER   A CA  
727  C  C   . SER   A 107 ? 0.78644 0.89363 0.70956 0.07813  -0.04655 -0.09627 107 SER   A C   
728  O  O   . SER   A 107 ? 0.79530 0.91321 0.71795 0.08198  -0.03851 -0.09690 107 SER   A O   
729  C  CB  . SER   A 107 ? 0.89176 0.99990 0.78269 0.09891  -0.05282 -0.11026 107 SER   A CB  
730  O  OG  . SER   A 107 ? 0.87633 0.97679 0.75102 0.10693  -0.06179 -0.11705 107 SER   A OG  
731  N  N   . GLY   A 108 ? 0.63702 0.74270 0.57357 0.06724  -0.04581 -0.08824 108 GLY   A N   
732  C  CA  . GLY   A 108 ? 0.64209 0.75784 0.59139 0.05998  -0.03544 -0.08020 108 GLY   A CA  
733  C  C   . GLY   A 108 ? 0.68036 0.81201 0.62635 0.06036  -0.02448 -0.07563 108 GLY   A C   
734  O  O   . GLY   A 108 ? 0.64121 0.77964 0.59694 0.05402  -0.01690 -0.06863 108 GLY   A O   
735  N  N   . ASP   A 109 ? 0.48960 0.62673 0.42189 0.06717  -0.02428 -0.07874 109 ASP   A N   
736  C  CA  . ASP   A 109 ? 0.57202 0.72605 0.49950 0.06866  -0.01424 -0.07459 109 ASP   A CA  
737  C  C   . ASP   A 109 ? 0.56766 0.72516 0.50129 0.06003  -0.01025 -0.06540 109 ASP   A C   
738  O  O   . ASP   A 109 ? 0.55890 0.71236 0.48823 0.05922  -0.01456 -0.06460 109 ASP   A O   
739  C  CB  . ASP   A 109 ? 0.59649 0.75531 0.50672 0.07934  -0.01623 -0.08087 109 ASP   A CB  
740  C  CG  . ASP   A 109 ? 0.68331 0.86219 0.58783 0.08137  -0.00613 -0.07598 109 ASP   A CG  
741  O  OD1 . ASP   A 109 ? 0.75553 0.94187 0.66831 0.07301  0.00071  -0.06683 109 ASP   A OD1 
742  O  OD2 . ASP   A 109 ? 0.82490 1.01236 0.71589 0.09173  -0.00559 -0.08110 109 ASP   A OD2 
743  N  N   . LEU   A 110 ? 0.54362 0.70842 0.48630 0.05413  -0.00242 -0.05858 110 LEU   A N   
744  C  CA  . LEU   A 110 ? 0.60489 0.76999 0.55380 0.04630  0.00011  -0.05034 110 LEU   A CA  
745  C  C   . LEU   A 110 ? 0.55515 0.72840 0.49429 0.04715  0.00247  -0.04668 110 LEU   A C   
746  O  O   . LEU   A 110 ? 0.48435 0.65429 0.42486 0.04273  0.00104  -0.04194 110 LEU   A O   
747  C  CB  . LEU   A 110 ? 0.69378 0.86280 0.65299 0.04075  0.00665  -0.04481 110 LEU   A CB  
748  C  CG  . LEU   A 110 ? 0.68356 0.84266 0.65449 0.03716  0.00367  -0.04544 110 LEU   A CG  
749  C  CD1 . LEU   A 110 ? 0.76676 0.92949 0.74426 0.03609  0.00879  -0.04482 110 LEU   A CD1 
750  C  CD2 . LEU   A 110 ? 0.75939 0.91295 0.73754 0.03128  0.00191  -0.03998 110 LEU   A CD2 
751  N  N   . LYS   A 111 ? 0.54282 0.72744 0.47179 0.05327  0.00585  -0.04864 111 LYS   A N   
752  C  CA  . LYS   A 111 ? 0.52021 0.71383 0.43876 0.05459  0.00779  -0.04498 111 LYS   A CA  
753  C  C   . LYS   A 111 ? 0.48451 0.66884 0.39500 0.05785  -0.00014 -0.04928 111 LYS   A C   
754  O  O   . LYS   A 111 ? 0.50626 0.69090 0.41363 0.05477  -0.00070 -0.04437 111 LYS   A O   
755  C  CB  . LYS   A 111 ? 0.57874 0.78894 0.48784 0.06182  0.01303  -0.04647 111 LYS   A CB  
756  C  CG  . LYS   A 111 ? 0.76085 0.98224 0.67791 0.05904  0.02050  -0.04222 111 LYS   A CG  
757  C  CD  . LYS   A 111 ? 0.81875 1.05190 0.73795 0.05153  0.02668  -0.03076 111 LYS   A CD  
758  C  CE  . LYS   A 111 ? 0.91305 1.16399 0.82012 0.05630  0.03022  -0.02798 111 LYS   A CE  
759  N  NZ  . LYS   A 111 ? 1.00123 1.25469 0.90686 0.04864  0.03122  -0.01782 111 LYS   A NZ  
760  N  N   . LYS   A 112 ? 0.50093 0.67672 0.40688 0.06444  -0.00702 -0.05849 112 LYS   A N   
761  C  CA  . LYS   A 112 ? 0.51353 0.67899 0.41178 0.06735  -0.01608 -0.06288 112 LYS   A CA  
762  C  C   . LYS   A 112 ? 0.48577 0.64054 0.39549 0.05882  -0.02043 -0.05855 112 LYS   A C   
763  O  O   . LYS   A 112 ? 0.49321 0.64458 0.39914 0.05766  -0.02457 -0.05687 112 LYS   A O   
764  C  CB  . LYS   A 112 ? 0.51332 0.66933 0.40495 0.07560  -0.02405 -0.07354 112 LYS   A CB  
765  C  CG  . LYS   A 112 ? 0.57807 0.74465 0.45703 0.08640  -0.02067 -0.07918 112 LYS   A CG  
766  C  CD  . LYS   A 112 ? 0.68749 0.84093 0.55829 0.09530  -0.03077 -0.09048 112 LYS   A CD  
767  C  CE  . LYS   A 112 ? 0.79460 0.95941 0.65359 0.10757  -0.02697 -0.09675 112 LYS   A CE  
768  N  NZ  . LYS   A 112 ? 0.75997 0.91016 0.60779 0.11803  -0.03820 -0.10870 112 LYS   A NZ  
769  N  N   . ILE   A 113 ? 0.46229 0.61255 0.38590 0.05343  -0.01966 -0.05675 113 ILE   A N   
770  C  CA  . ILE   A 113 ? 0.48007 0.62274 0.41537 0.04624  -0.02326 -0.05236 113 ILE   A CA  
771  C  C   . ILE   A 113 ? 0.47043 0.61864 0.40692 0.04167  -0.01854 -0.04430 113 ILE   A C   
772  O  O   . ILE   A 113 ? 0.47607 0.61994 0.41410 0.03923  -0.02300 -0.04184 113 ILE   A O   
773  C  CB  . ILE   A 113 ? 0.47197 0.61129 0.42081 0.04226  -0.02216 -0.05159 113 ILE   A CB  
774  C  CG1 . ILE   A 113 ? 0.44486 0.57499 0.39283 0.04581  -0.02995 -0.05911 113 ILE   A CG1 
775  C  CG2 . ILE   A 113 ? 0.44421 0.58131 0.40555 0.03517  -0.02238 -0.04492 113 ILE   A CG2 
776  C  CD1 . ILE   A 113 ? 0.47438 0.60312 0.43418 0.04274  -0.02742 -0.05849 113 ILE   A CD1 
777  N  N   . LYS   A 114 ? 0.46328 0.62102 0.39845 0.04055  -0.01021 -0.03986 114 LYS   A N   
778  C  CA  . LYS   A 114 ? 0.49582 0.65718 0.43017 0.03637  -0.00704 -0.03211 114 LYS   A CA  
779  C  C   . LYS   A 114 ? 0.55205 0.71491 0.47412 0.03932  -0.01021 -0.03223 114 LYS   A C   
780  O  O   . LYS   A 114 ? 0.47283 0.63279 0.39522 0.03619  -0.01223 -0.02756 114 LYS   A O   
781  C  CB  . LYS   A 114 ? 0.60937 0.78015 0.54436 0.03389  0.00116  -0.02681 114 LYS   A CB  
782  C  CG  . LYS   A 114 ? 0.67172 0.84452 0.60500 0.02903  0.00326  -0.01821 114 LYS   A CG  
783  C  CD  . LYS   A 114 ? 0.78895 0.97219 0.72075 0.02622  0.01002  -0.01220 114 LYS   A CD  
784  C  CE  . LYS   A 114 ? 0.80994 1.00702 0.73123 0.03101  0.01332  -0.01343 114 LYS   A CE  
785  N  NZ  . LYS   A 114 ? 0.84476 1.05274 0.76933 0.03114  0.01942  -0.01265 114 LYS   A NZ  
786  N  N   . LYS   A 115 ? 0.49905 0.66687 0.40932 0.04608  -0.01066 -0.03750 115 LYS   A N   
787  C  CA  . LYS   A 115 ? 0.49319 0.66246 0.39052 0.04969  -0.01396 -0.03804 115 LYS   A CA  
788  C  C   . LYS   A 115 ? 0.48636 0.64323 0.38523 0.04931  -0.02342 -0.04097 115 LYS   A C   
789  O  O   . LYS   A 115 ? 0.48767 0.64319 0.38272 0.04778  -0.02602 -0.03743 115 LYS   A O   
790  C  CB  . LYS   A 115 ? 0.56119 0.73801 0.44480 0.05880  -0.01326 -0.04436 115 LYS   A CB  
791  C  CG  . LYS   A 115 ? 0.66941 0.86362 0.54836 0.05923  -0.00382 -0.03876 115 LYS   A CG  
792  C  CD  . LYS   A 115 ? 0.79295 0.99338 0.66064 0.05941  -0.00363 -0.03365 115 LYS   A CD  
793  C  CE  . LYS   A 115 ? 0.85630 1.07473 0.72029 0.05746  0.00490  -0.02508 115 LYS   A CE  
794  N  NZ  . LYS   A 115 ? 0.95931 1.18074 0.81437 0.05546  0.00388  -0.01861 115 LYS   A NZ  
795  N  N   . VAL   A 116 ? 0.46815 0.61617 0.37259 0.05048  -0.02922 -0.04701 116 VAL   A N   
796  C  CA  . VAL   A 116 ? 0.52914 0.66630 0.43648 0.04926  -0.03911 -0.04903 116 VAL   A CA  
797  C  C   . VAL   A 116 ? 0.50735 0.64357 0.42687 0.04205  -0.03847 -0.04147 116 VAL   A C   
798  O  O   . VAL   A 116 ? 0.46431 0.59690 0.38315 0.04093  -0.04414 -0.03985 116 VAL   A O   
799  C  CB  . VAL   A 116 ? 0.51718 0.64500 0.42912 0.05071  -0.04607 -0.05570 116 VAL   A CB  
800  C  CG1 . VAL   A 116 ? 0.52124 0.63923 0.44009 0.04690  -0.05649 -0.05522 116 VAL   A CG1 
801  C  CG2 . VAL   A 116 ? 0.47865 0.60538 0.37529 0.05995  -0.04884 -0.06441 116 VAL   A CG2 
802  N  N   . GLY   A 117 ? 0.46225 0.60161 0.39282 0.03773  -0.03206 -0.03702 117 GLY   A N   
803  C  CA  . GLY   A 117 ? 0.45983 0.59876 0.40017 0.03263  -0.03124 -0.03023 117 GLY   A CA  
804  C  C   . GLY   A 117 ? 0.45745 0.59912 0.39000 0.03224  -0.02982 -0.02525 117 GLY   A C   
805  O  O   . GLY   A 117 ? 0.48770 0.62668 0.42367 0.03047  -0.03355 -0.02191 117 GLY   A O   
806  N  N   . SER   A 118 ? 0.43179 0.57978 0.35411 0.03375  -0.02442 -0.02395 118 SER   A N   
807  C  CA  . SER   A 118 ? 0.46277 0.61332 0.37607 0.03318  -0.02396 -0.01881 118 SER   A CA  
808  C  C   . SER   A 118 ? 0.45595 0.60258 0.36172 0.03621  -0.03155 -0.02178 118 SER   A C   
809  O  O   . SER   A 118 ? 0.52152 0.66619 0.42533 0.03467  -0.03417 -0.01743 118 SER   A O   
810  C  CB  . SER   A 118 ? 0.52326 0.68368 0.42636 0.03442  -0.01751 -0.01670 118 SER   A CB  
811  O  OG  . SER   A 118 ? 0.59663 0.75990 0.50811 0.03088  -0.01138 -0.01366 118 SER   A OG  
812  N  N   . TYR   A 119 ? 0.44358 0.58843 0.34347 0.04107  -0.03572 -0.02934 119 TYR   A N   
813  C  CA  . TYR   A 119 ? 0.44703 0.58665 0.33896 0.04416  -0.04427 -0.03274 119 TYR   A CA  
814  C  C   . TYR   A 119 ? 0.49949 0.63198 0.40335 0.04029  -0.05119 -0.03106 119 TYR   A C   
815  O  O   . TYR   A 119 ? 0.50320 0.63345 0.40370 0.04010  -0.05618 -0.02899 119 TYR   A O   
816  C  CB  . TYR   A 119 ? 0.48941 0.62644 0.37236 0.05070  -0.04847 -0.04184 119 TYR   A CB  
817  C  CG  . TYR   A 119 ? 0.49701 0.62453 0.37548 0.05303  -0.05989 -0.04661 119 TYR   A CG  
818  C  CD1 . TYR   A 119 ? 0.53971 0.66771 0.40438 0.05647  -0.06312 -0.04673 119 TYR   A CD1 
819  C  CD2 . TYR   A 119 ? 0.52357 0.64157 0.41068 0.05176  -0.06817 -0.05083 119 TYR   A CD2 
820  C  CE1 . TYR   A 119 ? 0.59192 0.71064 0.45193 0.05850  -0.07430 -0.05099 119 TYR   A CE1 
821  C  CE2 . TYR   A 119 ? 0.54224 0.65062 0.42498 0.05315  -0.08045 -0.05461 119 TYR   A CE2 
822  C  CZ  . TYR   A 119 ? 0.58116 0.68993 0.45015 0.05679  -0.08311 -0.05501 119 TYR   A CZ  
823  O  OH  . TYR   A 119 ? 0.63307 0.73219 0.49687 0.05833  -0.09535 -0.05878 119 TYR   A OH  
824  N  N   . PHE   A 120 ? 0.50078 0.63107 0.41890 0.03722  -0.05140 -0.03126 120 PHE   A N   
825  C  CA  . PHE   A 120 ? 0.51015 0.63728 0.44094 0.03355  -0.05716 -0.02837 120 PHE   A CA  
826  C  C   . PHE   A 120 ? 0.46815 0.59819 0.40098 0.03153  -0.05458 -0.02126 120 PHE   A C   
827  O  O   . PHE   A 120 ? 0.50274 0.63125 0.43804 0.03091  -0.06062 -0.01917 120 PHE   A O   
828  C  CB  . PHE   A 120 ? 0.46268 0.58989 0.40862 0.03039  -0.05588 -0.02803 120 PHE   A CB  
829  C  CG  . PHE   A 120 ? 0.44031 0.56178 0.38731 0.03124  -0.06241 -0.03423 120 PHE   A CG  
830  C  CD1 . PHE   A 120 ? 0.48624 0.60238 0.41956 0.03597  -0.06783 -0.04099 120 PHE   A CD1 
831  C  CD2 . PHE   A 120 ? 0.49986 0.62086 0.46111 0.02757  -0.06355 -0.03310 120 PHE   A CD2 
832  C  CE1 . PHE   A 120 ? 0.49227 0.60074 0.42548 0.03723  -0.07512 -0.04703 120 PHE   A CE1 
833  C  CE2 . PHE   A 120 ? 0.49650 0.61060 0.45866 0.02773  -0.07066 -0.03824 120 PHE   A CE2 
834  C  CZ  . PHE   A 120 ? 0.50972 0.61653 0.45777 0.03256  -0.07701 -0.04537 120 PHE   A CZ  
835  N  N   . ILE   A 121 ? 0.46843 0.60211 0.40071 0.03044  -0.04635 -0.01730 121 ILE   A N   
836  C  CA  . ILE   A 121 ? 0.49252 0.62660 0.42576 0.02892  -0.04498 -0.01076 121 ILE   A CA  
837  C  C   . ILE   A 121 ? 0.52544 0.65842 0.44621 0.03059  -0.04879 -0.00967 121 ILE   A C   
838  O  O   . ILE   A 121 ? 0.50032 0.63153 0.42271 0.03024  -0.05249 -0.00600 121 ILE   A O   
839  C  CB  . ILE   A 121 ? 0.46646 0.60258 0.39978 0.02709  -0.03686 -0.00682 121 ILE   A CB  
840  C  CG1 . ILE   A 121 ? 0.49844 0.63485 0.44540 0.02561  -0.03410 -0.00691 121 ILE   A CG1 
841  C  CG2 . ILE   A 121 ? 0.54758 0.68170 0.47710 0.02604  -0.03672 -0.00035 121 ILE   A CG2 
842  C  CD1 . ILE   A 121 ? 0.47642 0.61381 0.42304 0.02377  -0.02673 -0.00384 121 ILE   A CD1 
843  N  N   . GLU   A 122 ? 0.51754 0.65242 0.42509 0.03303  -0.04766 -0.01262 122 GLU   A N   
844  C  CA  . GLU   A 122 ? 0.54596 0.68047 0.44033 0.03512  -0.05137 -0.01178 122 GLU   A CA  
845  C  C   . GLU   A 122 ? 0.53993 0.66933 0.43640 0.03633  -0.06107 -0.01458 122 GLU   A C   
846  O  O   . GLU   A 122 ? 0.54997 0.67767 0.44328 0.03623  -0.06510 -0.01120 122 GLU   A O   
847  C  CB  . GLU   A 122 ? 0.53447 0.67375 0.41471 0.03891  -0.04855 -0.01546 122 GLU   A CB  
848  C  CG  . GLU   A 122 ? 0.71610 0.86296 0.59207 0.03716  -0.03975 -0.01030 122 GLU   A CG  
849  C  CD  . GLU   A 122 ? 0.89400 1.04120 0.76422 0.03435  -0.03953 -0.00212 122 GLU   A CD  
850  O  OE1 . GLU   A 122 ? 1.06469 1.20990 0.94210 0.02992  -0.03695 0.00390  122 GLU   A OE1 
851  O  OE2 . GLU   A 122 ? 0.91277 1.06165 0.77023 0.03689  -0.04235 -0.00178 122 GLU   A OE2 
852  N  N   . VAL   A 123 ? 0.51391 0.64045 0.41549 0.03723  -0.06569 -0.02047 123 VAL   A N   
853  C  CA  . VAL   A 123 ? 0.53352 0.65514 0.43890 0.03719  -0.07612 -0.02249 123 VAL   A CA  
854  C  C   . VAL   A 123 ? 0.55750 0.68080 0.47648 0.03383  -0.07756 -0.01630 123 VAL   A C   
855  O  O   . VAL   A 123 ? 0.54566 0.66784 0.46314 0.03411  -0.08340 -0.01408 123 VAL   A O   
856  C  CB  . VAL   A 123 ? 0.50555 0.62293 0.41637 0.03728  -0.08138 -0.02856 123 VAL   A CB  
857  C  CG1 . VAL   A 123 ? 0.53376 0.64656 0.45084 0.03554  -0.09306 -0.02877 123 VAL   A CG1 
858  C  CG2 . VAL   A 123 ? 0.51228 0.62731 0.40842 0.04241  -0.08120 -0.03567 123 VAL   A CG2 
859  N  N   . TRP   A 124 ? 0.52432 0.65093 0.45642 0.03134  -0.07228 -0.01350 124 TRP   A N   
860  C  CA  . TRP   A 124 ? 0.52601 0.65582 0.47147 0.02963  -0.07366 -0.00815 124 TRP   A CA  
861  C  C   . TRP   A 124 ? 0.54339 0.67298 0.48257 0.03094  -0.07278 -0.00340 124 TRP   A C   
862  O  O   . TRP   A 124 ? 0.53172 0.66284 0.47679 0.03131  -0.07765 -0.00022 124 TRP   A O   
863  C  CB  . TRP   A 124 ? 0.43383 0.56753 0.39186 0.02796  -0.06719 -0.00618 124 TRP   A CB  
864  C  CG  . TRP   A 124 ? 0.48600 0.62068 0.45434 0.02587  -0.06976 -0.00894 124 TRP   A CG  
865  C  CD1 . TRP   A 124 ? 0.44385 0.57815 0.41856 0.02416  -0.07872 -0.00991 124 TRP   A CD1 
866  C  CD2 . TRP   A 124 ? 0.42471 0.56037 0.39841 0.02468  -0.06396 -0.01047 124 TRP   A CD2 
867  N  NE1 . TRP   A 124 ? 0.46796 0.60250 0.45158 0.02168  -0.07919 -0.01161 124 TRP   A NE1 
868  C  CE2 . TRP   A 124 ? 0.46986 0.60533 0.45288 0.02226  -0.06997 -0.01223 124 TRP   A CE2 
869  C  CE3 . TRP   A 124 ? 0.45097 0.58727 0.42239 0.02506  -0.05505 -0.01019 124 TRP   A CE3 
870  C  CZ2 . TRP   A 124 ? 0.44281 0.57864 0.43274 0.02055  -0.06699 -0.01379 124 TRP   A CZ2 
871  C  CZ3 . TRP   A 124 ? 0.44830 0.58558 0.42712 0.02361  -0.05167 -0.01202 124 TRP   A CZ3 
872  C  CH2 . TRP   A 124 ? 0.40476 0.54160 0.39214 0.02161  -0.05749 -0.01399 124 TRP   A CH2 
873  N  N   . LYS   A 125 ? 0.47111 0.59929 0.39886 0.03148  -0.06688 -0.00219 125 LYS   A N   
874  C  CA  . LYS   A 125 ? 0.51532 0.64157 0.43570 0.03218  -0.06722 0.00280  125 LYS   A CA  
875  C  C   . LYS   A 125 ? 0.57481 0.69893 0.48531 0.03381  -0.07436 0.00202  125 LYS   A C   
876  O  O   . LYS   A 125 ? 0.55756 0.67974 0.46413 0.03450  -0.07676 0.00631  125 LYS   A O   
877  C  CB  . LYS   A 125 ? 0.57472 0.70035 0.48569 0.03107  -0.06017 0.00555  125 LYS   A CB  
878  C  CG  . LYS   A 125 ? 0.55278 0.67907 0.47291 0.02952  -0.05417 0.00704  125 LYS   A CG  
879  C  CD  . LYS   A 125 ? 0.69785 0.82291 0.60988 0.02743  -0.04860 0.01123  125 LYS   A CD  
880  C  CE  . LYS   A 125 ? 0.75297 0.88200 0.65273 0.02711  -0.04620 0.00980  125 LYS   A CE  
881  N  NZ  . LYS   A 125 ? 0.98389 1.11427 0.87766 0.02390  -0.04061 0.01529  125 LYS   A NZ  
882  N  N   . SER   A 126 ? 0.52707 0.65040 0.43211 0.03492  -0.07841 -0.00346 126 SER   A N   
883  C  CA  . SER   A 126 ? 0.57173 0.69229 0.46832 0.03675  -0.08662 -0.00427 126 SER   A CA  
884  C  C   . SER   A 126 ? 0.64414 0.76424 0.55232 0.03605  -0.09562 -0.00579 126 SER   A C   
885  O  O   . SER   A 126 ? 0.66251 0.77946 0.56428 0.03734  -0.10392 -0.00775 126 SER   A O   
886  C  CB  . SER   A 126 ? 0.64180 0.76102 0.52091 0.03959  -0.08692 -0.00888 126 SER   A CB  
887  O  OG  . SER   A 126 ? 0.77934 0.89774 0.66039 0.04051  -0.08760 -0.01541 126 SER   A OG  
888  N  N   . CYS   A 127 ? 0.63426 0.75816 0.55947 0.03383  -0.09464 -0.00427 127 CYS   A N   
889  C  CA  . CYS   A 127 ? 0.69022 0.81567 0.62753 0.03206  -0.10334 -0.00477 127 CYS   A CA  
890  C  C   . CYS   A 127 ? 0.70029 0.83073 0.64720 0.03211  -0.10747 0.00090  127 CYS   A C   
891  O  O   . CYS   A 127 ? 0.67873 0.81304 0.63767 0.03004  -0.11488 0.00206  127 CYS   A O   
892  C  CB  . CYS   A 127 ? 0.59151 0.72054 0.54325 0.02927  -0.10074 -0.00541 127 CYS   A CB  
893  S  SG  . CYS   A 127 ? 0.66127 0.78337 0.60739 0.02863  -0.10479 -0.01321 127 CYS   A SG  
894  N  N   . GLY   A 128 ? 0.64543 0.77593 0.58718 0.03442  -0.10391 0.00475  128 GLY   A N   
895  C  CA  . GLY   A 128 ? 0.71545 0.85043 0.66492 0.03578  -0.10872 0.00950  128 GLY   A CA  
896  C  C   . GLY   A 128 ? 0.70520 0.84843 0.67005 0.03678  -0.10442 0.01383  128 GLY   A C   
897  O  O   . GLY   A 128 ? 0.62346 0.77435 0.59949 0.03793  -0.10922 0.01746  128 GLY   A O   
898  N  N   . MET   A 129 ? 0.63173 0.77463 0.59763 0.03684  -0.09574 0.01363  129 MET   A N   
899  C  CA  . MET   A 129 ? 0.58924 0.73988 0.56858 0.03879  -0.09168 0.01710  129 MET   A CA  
900  C  C   . MET   A 129 ? 0.61765 0.76402 0.59006 0.04319  -0.08857 0.01997  129 MET   A C   
901  O  O   . MET   A 129 ? 0.63186 0.76886 0.59008 0.04280  -0.08608 0.01933  129 MET   A O   
902  C  CB  . MET   A 129 ? 0.58496 0.73719 0.57012 0.03656  -0.08485 0.01517  129 MET   A CB  
903  C  CG  . MET   A 129 ? 0.54079 0.69868 0.53740 0.03257  -0.08818 0.01379  129 MET   A CG  
904  S  SD  . MET   A 129 ? 0.55234 0.71129 0.55481 0.03043  -0.07997 0.01186  129 MET   A SD  
905  C  CE  . MET   A 129 ? 0.60840 0.75556 0.59215 0.03079  -0.07359 0.00766  129 MET   A CE  
906  N  N   . ASN   A 130 ? 0.58652 0.74023 0.56902 0.04756  -0.08914 0.02346  130 ASN   A N   
907  C  CA  . ASN   A 130 ? 0.61469 0.76345 0.59196 0.05283  -0.08641 0.02563  130 ASN   A CA  
908  C  C   . ASN   A 130 ? 0.65868 0.80444 0.63589 0.05206  -0.07863 0.02431  130 ASN   A C   
909  O  O   . ASN   A 130 ? 0.59977 0.75424 0.58900 0.05142  -0.07541 0.02381  130 ASN   A O   
910  C  CB  . ASN   A 130 ? 0.62165 0.78069 0.60993 0.05935  -0.08923 0.02900  130 ASN   A CB  
911  C  CG  . ASN   A 130 ? 0.80212 0.96505 0.79149 0.06009  -0.09730 0.03073  130 ASN   A CG  
912  O  OD1 . ASN   A 130 ? 0.84982 1.00291 0.82638 0.05829  -0.10090 0.02994  130 ASN   A OD1 
913  N  ND2 . ASN   A 130 ? 0.75236 0.93083 0.75724 0.06246  -0.10035 0.03358  130 ASN   A ND2 
914  N  N   . MET   A 131 ? 0.65578 0.78958 0.61942 0.05079  -0.07595 0.02397  131 MET   A N   
915  C  CA  . MET   A 131 ? 0.60944 0.73953 0.57187 0.04884  -0.06911 0.02271  131 MET   A CA  
916  C  C   . MET   A 131 ? 0.60521 0.73121 0.56777 0.05410  -0.06727 0.02450  131 MET   A C   
917  O  O   . MET   A 131 ? 0.54198 0.66447 0.50386 0.05276  -0.06216 0.02361  131 MET   A O   
918  C  CB  . MET   A 131 ? 0.67288 0.79400 0.62121 0.04393  -0.06721 0.02215  131 MET   A CB  
919  C  CG  . MET   A 131 ? 0.65722 0.78091 0.60187 0.04039  -0.06952 0.01963  131 MET   A CG  
920  S  SD  . MET   A 131 ? 0.79565 0.92805 0.75274 0.03773  -0.06749 0.01518  131 MET   A SD  
921  C  CE  . MET   A 131 ? 0.68560 0.81463 0.63926 0.03517  -0.05901 0.01383  131 MET   A CE  
922  N  N   . GLU   A 132 ? 0.59115 0.71655 0.55358 0.06067  -0.07175 0.02670  132 GLU   A N   
923  C  CA  . GLU   A 132 ? 0.65481 0.77250 0.61356 0.06617  -0.07073 0.02750  132 GLU   A CA  
924  C  C   . GLU   A 132 ? 0.57357 0.69950 0.54324 0.06845  -0.06512 0.02591  132 GLU   A C   
925  O  O   . GLU   A 132 ? 0.68360 0.80131 0.64880 0.07042  -0.06268 0.02542  132 GLU   A O   
926  C  CB  . GLU   A 132 ? 0.74920 0.86399 0.70513 0.07477  -0.07672 0.02943  132 GLU   A CB  
927  C  CG  . GLU   A 132 ? 0.89008 0.99210 0.83861 0.07941  -0.07605 0.02932  132 GLU   A CG  
928  C  CD  . GLU   A 132 ? 1.12451 1.21950 1.06744 0.08946  -0.08230 0.03036  132 GLU   A CD  
929  O  OE1 . GLU   A 132 ? 1.11804 1.22046 1.06439 0.09327  -0.08651 0.03143  132 GLU   A OE1 
930  O  OE2 . GLU   A 132 ? 1.17280 1.25439 1.10765 0.09375  -0.08364 0.02997  132 GLU   A OE2 
931  N  N   . ASN   A 133 ? 0.55025 0.69217 0.53409 0.06828  -0.06379 0.02560  133 ASN   A N   
932  C  CA  . ASN   A 133 ? 0.50647 0.65871 0.50172 0.07040  -0.05870 0.02506  133 ASN   A CA  
933  C  C   . ASN   A 133 ? 0.52386 0.68108 0.52560 0.06233  -0.05477 0.02337  133 ASN   A C   
934  O  O   . ASN   A 133 ? 0.46775 0.63782 0.48229 0.06256  -0.05231 0.02401  133 ASN   A O   
935  C  CB  . ASN   A 133 ? 0.54452 0.71330 0.55211 0.07752  -0.06054 0.02749  133 ASN   A CB  
936  C  CG  . ASN   A 133 ? 0.49591 0.65955 0.49665 0.08760  -0.06393 0.02830  133 ASN   A CG  
937  O  OD1 . ASN   A 133 ? 0.68831 0.85536 0.68926 0.09106  -0.06926 0.03008  133 ASN   A OD1 
938  N  ND2 . ASN   A 133 ? 0.53807 0.69212 0.53178 0.09268  -0.06172 0.02679  133 ASN   A ND2 
939  N  N   . VAL   A 134 ? 0.48250 0.63062 0.47553 0.05552  -0.05460 0.02154  134 VAL   A N   
940  C  CA  . VAL   A 134 ? 0.44015 0.59079 0.43693 0.04887  -0.05143 0.01909  134 VAL   A CA  
941  C  C   . VAL   A 134 ? 0.47437 0.61457 0.46196 0.04603  -0.04655 0.01738  134 VAL   A C   
942  O  O   . VAL   A 134 ? 0.48855 0.61822 0.46436 0.04618  -0.04735 0.01841  134 VAL   A O   
943  C  CB  . VAL   A 134 ? 0.44993 0.60126 0.44472 0.04429  -0.05604 0.01795  134 VAL   A CB  
944  C  CG1 . VAL   A 134 ? 0.45548 0.60718 0.45182 0.03864  -0.05389 0.01462  134 VAL   A CG1 
945  C  CG2 . VAL   A 134 ? 0.47797 0.64008 0.48296 0.04630  -0.06185 0.02036  134 VAL   A CG2 
946  N  N   . GLN   A 135 ? 0.46264 0.60624 0.45626 0.04336  -0.04191 0.01550  135 GLN   A N   
947  C  CA  . GLN   A 135 ? 0.47199 0.60810 0.45884 0.04002  -0.03726 0.01392  135 GLN   A CA  
948  C  C   . GLN   A 135 ? 0.46327 0.60285 0.45285 0.03493  -0.03549 0.01078  135 GLN   A C   
949  O  O   . GLN   A 135 ? 0.44853 0.59598 0.44839 0.03423  -0.03668 0.00999  135 GLN   A O   
950  C  CB  . GLN   A 135 ? 0.51758 0.65315 0.50831 0.04273  -0.03312 0.01411  135 GLN   A CB  
951  C  CG  . GLN   A 135 ? 0.55220 0.68284 0.53945 0.04915  -0.03487 0.01615  135 GLN   A CG  
952  C  CD  . GLN   A 135 ? 0.64603 0.77634 0.63669 0.05176  -0.03067 0.01538  135 GLN   A CD  
953  O  OE1 . GLN   A 135 ? 0.54786 0.68805 0.54808 0.05641  -0.02944 0.01567  135 GLN   A OE1 
954  N  NE2 . GLN   A 135 ? 0.60050 0.72092 0.58389 0.04843  -0.02839 0.01479  135 GLN   A NE2 
955  N  N   . PHE   A 136 ? 0.45987 0.59389 0.44037 0.03155  -0.03289 0.00937  136 PHE   A N   
956  C  CA  . PHE   A 136 ? 0.46066 0.59691 0.44195 0.02811  -0.03055 0.00572  136 PHE   A CA  
957  C  C   . PHE   A 136 ? 0.46147 0.59586 0.44367 0.02703  -0.02467 0.00546  136 PHE   A C   
958  O  O   . PHE   A 136 ? 0.49579 0.62473 0.46997 0.02608  -0.02267 0.00741  136 PHE   A O   
959  C  CB  . PHE   A 136 ? 0.45491 0.58875 0.42452 0.02631  -0.03196 0.00435  136 PHE   A CB  
960  C  CG  . PHE   A 136 ? 0.47592 0.61032 0.44312 0.02745  -0.03819 0.00447  136 PHE   A CG  
961  C  CD1 . PHE   A 136 ? 0.46583 0.60407 0.43995 0.02721  -0.04248 0.00184  136 PHE   A CD1 
962  C  CD2 . PHE   A 136 ? 0.53845 0.66890 0.49639 0.02838  -0.04065 0.00757  136 PHE   A CD2 
963  C  CE1 . PHE   A 136 ? 0.43015 0.56869 0.40244 0.02797  -0.04926 0.00196  136 PHE   A CE1 
964  C  CE2 . PHE   A 136 ? 0.53123 0.66222 0.48677 0.02958  -0.04693 0.00756  136 PHE   A CE2 
965  C  CZ  . PHE   A 136 ? 0.48952 0.62479 0.45263 0.02943  -0.05120 0.00462  136 PHE   A CZ  
966  N  N   . LEU   A 137 ? 0.42160 0.56041 0.41383 0.02682  -0.02252 0.00378  137 LEU   A N   
967  C  CA  . LEU   A 137 ? 0.41681 0.55415 0.41081 0.02609  -0.01731 0.00339  137 LEU   A CA  
968  C  C   . LEU   A 137 ? 0.44535 0.58501 0.44101 0.02328  -0.01540 -0.00044 137 LEU   A C   
969  O  O   . LEU   A 137 ? 0.42961 0.57303 0.43152 0.02275  -0.01817 -0.00243 137 LEU   A O   
970  C  CB  . LEU   A 137 ? 0.39529 0.53596 0.39892 0.02924  -0.01617 0.00492  137 LEU   A CB  
971  C  CG  . LEU   A 137 ? 0.47454 0.61290 0.47604 0.03405  -0.01836 0.00803  137 LEU   A CG  
972  C  CD1 . LEU   A 137 ? 0.46127 0.60470 0.47116 0.03864  -0.01664 0.00914  137 LEU   A CD1 
973  C  CD2 . LEU   A 137 ? 0.45693 0.58449 0.44645 0.03378  -0.01846 0.00951  137 LEU   A CD2 
974  N  N   . TRP   A 138 ? 0.42124 0.55859 0.41169 0.02153  -0.01129 -0.00118 138 TRP   A N   
975  C  CA  . TRP   A 138 ? 0.45493 0.59458 0.44662 0.02000  -0.00907 -0.00510 138 TRP   A CA  
976  C  C   . TRP   A 138 ? 0.39419 0.53484 0.39489 0.01978  -0.00596 -0.00548 138 TRP   A C   
977  O  O   . TRP   A 138 ? 0.41219 0.55042 0.41305 0.02009  -0.00313 -0.00310 138 TRP   A O   
978  C  CB  . TRP   A 138 ? 0.43714 0.57658 0.41916 0.01855  -0.00586 -0.00514 138 TRP   A CB  
979  C  CG  . TRP   A 138 ? 0.43628 0.57640 0.40856 0.01896  -0.00841 -0.00496 138 TRP   A CG  
980  C  CD1 . TRP   A 138 ? 0.49895 0.63647 0.46517 0.01888  -0.01066 -0.00096 138 TRP   A CD1 
981  C  CD2 . TRP   A 138 ? 0.42673 0.57014 0.39289 0.02014  -0.00918 -0.00908 138 TRP   A CD2 
982  N  NE1 . TRP   A 138 ? 0.46842 0.60818 0.42565 0.01948  -0.01251 -0.00199 138 TRP   A NE1 
983  C  CE2 . TRP   A 138 ? 0.48479 0.62835 0.44138 0.02071  -0.01156 -0.00719 138 TRP   A CE2 
984  C  CE3 . TRP   A 138 ? 0.41810 0.56363 0.38530 0.02154  -0.00880 -0.01450 138 TRP   A CE3 
985  C  CZ2 . TRP   A 138 ? 0.53285 0.67954 0.48033 0.02304  -0.01305 -0.01069 138 TRP   A CZ2 
986  C  CZ3 . TRP   A 138 ? 0.41328 0.56100 0.37104 0.02434  -0.01072 -0.01840 138 TRP   A CZ3 
987  C  CH2 . TRP   A 138 ? 0.47042 0.61912 0.41838 0.02525  -0.01260 -0.01656 138 TRP   A CH2 
988  N  N   . ALA   A 139 ? 0.39173 0.53500 0.39919 0.01922  -0.00719 -0.00844 139 ALA   A N   
989  C  CA  . ALA   A 139 ? 0.38464 0.52949 0.40092 0.01884  -0.00461 -0.00830 139 ALA   A CA  
990  C  C   . ALA   A 139 ? 0.45920 0.60189 0.47208 0.01813  0.00063  -0.00880 139 ALA   A C   
991  O  O   . ALA   A 139 ? 0.34959 0.49115 0.36514 0.01876  0.00327  -0.00666 139 ALA   A O   
992  C  CB  . ALA   A 139 ? 0.34792 0.49449 0.37059 0.01746  -0.00774 -0.01113 139 ALA   A CB  
993  N  N   . SER   A 140 ? 0.44571 0.58838 0.45240 0.01726  0.00192  -0.01156 140 SER   A N   
994  C  CA  . SER   A 140 ? 0.42040 0.56287 0.42537 0.01614  0.00668  -0.01138 140 SER   A CA  
995  C  C   . SER   A 140 ? 0.47428 0.61331 0.47544 0.01537  0.00820  -0.00674 140 SER   A C   
996  O  O   . SER   A 140 ? 0.49323 0.62999 0.49668 0.01475  0.01063  -0.00547 140 SER   A O   
997  C  CB  . SER   A 140 ? 0.45204 0.59770 0.45031 0.01618  0.00788  -0.01434 140 SER   A CB  
998  O  OG  . SER   A 140 ? 0.46699 0.61366 0.45680 0.01648  0.00641  -0.01298 140 SER   A OG  
999  N  N   . GLU   A 141 ? 0.45561 0.59305 0.45011 0.01535  0.00601  -0.00419 141 GLU   A N   
1000 C  CA  . GLU   A 141 ? 0.44875 0.58069 0.43846 0.01435  0.00584  0.00044  141 GLU   A CA  
1001 C  C   . GLU   A 141 ? 0.45792 0.58515 0.45235 0.01704  0.00489  0.00150  141 GLU   A C   
1002 O  O   . GLU   A 141 ? 0.47528 0.59684 0.46808 0.01669  0.00551  0.00348  141 GLU   A O   
1003 C  CB  . GLU   A 141 ? 0.50386 0.63429 0.48586 0.01417  0.00267  0.00311  141 GLU   A CB  
1004 C  CG  . GLU   A 141 ? 0.60910 0.74480 0.58418 0.01214  0.00375  0.00321  141 GLU   A CG  
1005 C  CD  . GLU   A 141 ? 0.58362 0.71741 0.55060 0.01186  0.00035  0.00662  141 GLU   A CD  
1006 O  OE1 . GLU   A 141 ? 0.89206 1.03122 0.85192 0.01036  0.00137  0.00777  141 GLU   A OE1 
1007 O  OE2 . GLU   A 141 ? 0.66728 0.79513 0.63453 0.01356  -0.00324 0.00833  141 GLU   A OE2 
1008 N  N   . GLU   A 142 ? 0.43907 0.56895 0.43895 0.02010  0.00288  0.00049  142 GLU   A N   
1009 C  CA  . GLU   A 142 ? 0.42533 0.55330 0.42900 0.02415  0.00214  0.00187  142 GLU   A CA  
1010 C  C   . GLU   A 142 ? 0.38966 0.51919 0.39962 0.02463  0.00541  0.00054  142 GLU   A C   
1011 O  O   . GLU   A 142 ? 0.44624 0.57129 0.45517 0.02745  0.00583  0.00159  142 GLU   A O   
1012 C  CB  . GLU   A 142 ? 0.42580 0.55951 0.43476 0.02709  -0.00076 0.00220  142 GLU   A CB  
1013 C  CG  . GLU   A 142 ? 0.42348 0.55495 0.42572 0.02707  -0.00444 0.00356  142 GLU   A CG  
1014 C  CD  . GLU   A 142 ? 0.54855 0.67097 0.54229 0.02890  -0.00619 0.00634  142 GLU   A CD  
1015 O  OE1 . GLU   A 142 ? 0.53556 0.65528 0.53055 0.03349  -0.00655 0.00710  142 GLU   A OE1 
1016 O  OE2 . GLU   A 142 ? 0.52719 0.64497 0.51245 0.02594  -0.00755 0.00791  142 GLU   A OE2 
1017 N  N   . ILE   A 143 ? 0.39355 0.52839 0.40908 0.02227  0.00719  -0.00198 143 ILE   A N   
1018 C  CA  . ILE   A 143 ? 0.39127 0.52743 0.41250 0.02232  0.01010  -0.00303 143 ILE   A CA  
1019 C  C   . ILE   A 143 ? 0.44293 0.57278 0.45874 0.02088  0.01225  -0.00269 143 ILE   A C   
1020 O  O   . ILE   A 143 ? 0.36863 0.49560 0.38560 0.02289  0.01339  -0.00220 143 ILE   A O   
1021 C  CB  . ILE   A 143 ? 0.38098 0.52219 0.40809 0.01985  0.01041  -0.00584 143 ILE   A CB  
1022 C  CG1 . ILE   A 143 ? 0.34964 0.49679 0.38409 0.02061  0.00716  -0.00499 143 ILE   A CG1 
1023 C  CG2 . ILE   A 143 ? 0.40868 0.54993 0.43999 0.01920  0.01353  -0.00696 143 ILE   A CG2 
1024 C  CD1 . ILE   A 143 ? 0.38989 0.53855 0.42711 0.01785  0.00500  -0.00791 143 ILE   A CD1 
1025 N  N   . ASN   A 144 ? 0.44211 0.57040 0.45179 0.01746  0.01247  -0.00246 144 ASN   A N   
1026 C  CA  . ASN   A 144 ? 0.49179 0.61553 0.49758 0.01493  0.01395  -0.00100 144 ASN   A CA  
1027 C  C   . ASN   A 144 ? 0.49539 0.60957 0.49492 0.01596  0.01100  0.00242  144 ASN   A C   
1028 O  O   . ASN   A 144 ? 0.56256 0.67107 0.55973 0.01417  0.01096  0.00385  144 ASN   A O   
1029 C  CB  . ASN   A 144 ? 0.43393 0.56183 0.43583 0.01093  0.01534  -0.00072 144 ASN   A CB  
1030 C  CG  . ASN   A 144 ? 0.45300 0.58787 0.45976 0.01077  0.01802  -0.00479 144 ASN   A CG  
1031 O  OD1 . ASN   A 144 ? 0.53553 0.67023 0.54775 0.01130  0.01966  -0.00649 144 ASN   A OD1 
1032 N  ND2 . ASN   A 144 ? 0.52054 0.66095 0.52457 0.01066  0.01797  -0.00664 144 ASN   A ND2 
1033 N  N   . LYS   A 145 ? 0.51367 0.62508 0.51030 0.01903  0.00776  0.00367  145 LYS   A N   
1034 C  CA  . LYS   A 145 ? 0.49096 0.59154 0.48142 0.02194  0.00392  0.00595  145 LYS   A CA  
1035 C  C   . LYS   A 145 ? 0.54502 0.64322 0.53847 0.02749  0.00445  0.00421  145 LYS   A C   
1036 O  O   . LYS   A 145 ? 0.52271 0.61002 0.51000 0.02968  0.00137  0.00518  145 LYS   A O   
1037 C  CB  . LYS   A 145 ? 0.52269 0.62142 0.50931 0.02512  0.00007  0.00733  145 LYS   A CB  
1038 C  CG  . LYS   A 145 ? 0.56694 0.66572 0.54778 0.02033  -0.00160 0.00995  145 LYS   A CG  
1039 C  CD  . LYS   A 145 ? 0.59692 0.69464 0.57483 0.02391  -0.00546 0.01088  145 LYS   A CD  
1040 C  CE  . LYS   A 145 ? 0.62064 0.71983 0.59276 0.01923  -0.00669 0.01339  145 LYS   A CE  
1041 N  NZ  . LYS   A 145 ? 0.73172 0.83059 0.70173 0.02281  -0.01049 0.01391  145 LYS   A NZ  
1042 N  N   . LYS   A 146 ? 0.45371 0.56155 0.45581 0.03004  0.00759  0.00200  146 LYS   A N   
1043 C  CA  . LYS   A 146 ? 0.48334 0.59213 0.48862 0.03599  0.00865  0.00100  146 LYS   A CA  
1044 C  C   . LYS   A 146 ? 0.39489 0.51283 0.40939 0.03391  0.01292  -0.00061 146 LYS   A C   
1045 O  O   . LYS   A 146 ? 0.37293 0.50007 0.39478 0.03678  0.01428  -0.00050 146 LYS   A O   
1046 C  CB  . LYS   A 146 ? 0.48373 0.59648 0.48988 0.04314  0.00678  0.00177  146 LYS   A CB  
1047 C  CG  . LYS   A 146 ? 0.45442 0.55637 0.45064 0.04605  0.00179  0.00302  146 LYS   A CG  
1048 C  CD  . LYS   A 146 ? 0.57095 0.67638 0.56711 0.05559  -0.00009 0.00326  146 LYS   A CD  
1049 C  CE  . LYS   A 146 ? 0.72827 0.84503 0.73067 0.05524  -0.00024 0.00457  146 LYS   A CE  
1050 N  NZ  . LYS   A 146 ? 0.74937 0.87380 0.75396 0.06481  -0.00146 0.00546  146 LYS   A NZ  
1051 N  N   . PRO   A 147 ? 0.40146 0.51745 0.41596 0.02880  0.01476  -0.00160 147 PRO   A N   
1052 C  CA  . PRO   A 147 ? 0.41277 0.53665 0.43553 0.02645  0.01797  -0.00338 147 PRO   A CA  
1053 C  C   . PRO   A 147 ? 0.36950 0.49533 0.39643 0.03008  0.01982  -0.00363 147 PRO   A C   
1054 O  O   . PRO   A 147 ? 0.38913 0.52276 0.42400 0.02924  0.02159  -0.00403 147 PRO   A O   
1055 C  CB  . PRO   A 147 ? 0.51533 0.63671 0.53558 0.02095  0.01915  -0.00425 147 PRO   A CB  
1056 C  CG  . PRO   A 147 ? 0.50266 0.61384 0.51457 0.02066  0.01686  -0.00210 147 PRO   A CG  
1057 C  CD  . PRO   A 147 ? 0.42448 0.53213 0.43192 0.02448  0.01348  -0.00053 147 PRO   A CD  
1058 N  N   . ASN   A 148 ? 0.36835 0.48680 0.38960 0.03424  0.01891  -0.00327 148 ASN   A N   
1059 C  CA  . ASN   A 148 ? 0.43072 0.55255 0.45514 0.03896  0.02079  -0.00345 148 ASN   A CA  
1060 C  C   . ASN   A 148 ? 0.43360 0.56656 0.46361 0.04399  0.02129  -0.00161 148 ASN   A C   
1061 O  O   . ASN   A 148 ? 0.40973 0.55308 0.44820 0.04390  0.02366  -0.00045 148 ASN   A O   
1062 C  CB  . ASN   A 148 ? 0.45803 0.56818 0.47332 0.04348  0.01873  -0.00407 148 ASN   A CB  
1063 C  CG  . ASN   A 148 ? 0.52416 0.63787 0.54152 0.04864  0.02102  -0.00462 148 ASN   A CG  
1064 O  OD1 . ASN   A 148 ? 0.49046 0.60507 0.51133 0.04513  0.02318  -0.00540 148 ASN   A OD1 
1065 N  ND2 . ASN   A 148 ? 0.49614 0.61328 0.51141 0.05737  0.02068  -0.00404 148 ASN   A ND2 
1066 N  N   . GLU   A 149 ? 0.40124 0.53286 0.42699 0.04819  0.01870  -0.00068 149 GLU   A N   
1067 C  CA  . GLU   A 149 ? 0.43286 0.57733 0.46494 0.05267  0.01902  0.00174  149 GLU   A CA  
1068 C  C   . GLU   A 149 ? 0.43073 0.58600 0.47363 0.04620  0.01984  0.00316  149 GLU   A C   
1069 O  O   . GLU   A 149 ? 0.41929 0.58717 0.47133 0.04689  0.02132  0.00588  149 GLU   A O   
1070 C  CB  . GLU   A 149 ? 0.42878 0.56921 0.45451 0.05696  0.01541  0.00221  149 GLU   A CB  
1071 C  CG  . GLU   A 149 ? 0.43812 0.59341 0.47065 0.06238  0.01550  0.00514  149 GLU   A CG  
1072 C  CD  . GLU   A 149 ? 0.63600 0.78697 0.66211 0.06692  0.01150  0.00538  149 GLU   A CD  
1073 O  OE1 . GLU   A 149 ? 0.62050 0.75587 0.63516 0.06870  0.00845  0.00342  149 GLU   A OE1 
1074 O  OE2 . GLU   A 149 ? 0.64988 0.81265 0.68249 0.06821  0.01075  0.00793  149 GLU   A OE2 
1075 N  N   . TYR   A 150 ? 0.34431 0.49472 0.38584 0.03989  0.01830  0.00165  150 TYR   A N   
1076 C  CA  . TYR   A 150 ? 0.35649 0.51468 0.40617 0.03488  0.01727  0.00236  150 TYR   A CA  
1077 C  C   . TYR   A 150 ? 0.36006 0.52233 0.41698 0.03138  0.01905  0.00223  150 TYR   A C   
1078 O  O   . TYR   A 150 ? 0.31482 0.48715 0.38096 0.03031  0.01842  0.00515  150 TYR   A O   
1079 C  CB  . TYR   A 150 ? 0.35285 0.50470 0.39754 0.03028  0.01516  0.00010  150 TYR   A CB  
1080 C  CG  . TYR   A 150 ? 0.38831 0.54604 0.43946 0.02627  0.01266  0.00011  150 TYR   A CG  
1081 C  CD1 . TYR   A 150 ? 0.34181 0.50599 0.39672 0.02730  0.00955  0.00263  150 TYR   A CD1 
1082 C  CD2 . TYR   A 150 ? 0.31397 0.47048 0.36741 0.02188  0.01253  -0.00235 150 TYR   A CD2 
1083 C  CE1 . TYR   A 150 ? 0.37470 0.54256 0.43504 0.02317  0.00584  0.00266  150 TYR   A CE1 
1084 C  CE2 . TYR   A 150 ? 0.30757 0.46698 0.36567 0.01856  0.00858  -0.00284 150 TYR   A CE2 
1085 C  CZ  . TYR   A 150 ? 0.38797 0.55257 0.44939 0.01891  0.00497  -0.00022 150 TYR   A CZ  
1086 O  OH  . TYR   A 150 ? 0.35017 0.51596 0.41561 0.01530  -0.00026 -0.00067 150 TYR   A OH  
1087 N  N   . TRP   A 151 ? 0.34987 0.50463 0.40307 0.02917  0.02082  -0.00061 151 TRP   A N   
1088 C  CA  . TRP   A 151 ? 0.32882 0.48664 0.38863 0.02582  0.02178  -0.00097 151 TRP   A CA  
1089 C  C   . TRP   A 151 ? 0.31610 0.48102 0.38104 0.02906  0.02390  0.00212  151 TRP   A C   
1090 O  O   . TRP   A 151 ? 0.33914 0.51010 0.41204 0.02610  0.02361  0.00393  151 TRP   A O   
1091 C  CB  . TRP   A 151 ? 0.29989 0.44921 0.35473 0.02286  0.02301  -0.00482 151 TRP   A CB  
1092 C  CG  . TRP   A 151 ? 0.28176 0.42828 0.33296 0.01977  0.02098  -0.00722 151 TRP   A CG  
1093 C  CD1 . TRP   A 151 ? 0.27881 0.42021 0.32200 0.01960  0.02095  -0.00806 151 TRP   A CD1 
1094 C  CD2 . TRP   A 151 ? 0.27692 0.42591 0.33178 0.01685  0.01802  -0.00870 151 TRP   A CD2 
1095 N  NE1 . TRP   A 151 ? 0.32626 0.46834 0.36773 0.01731  0.01914  -0.00996 151 TRP   A NE1 
1096 C  CE2 . TRP   A 151 ? 0.28564 0.43143 0.33363 0.01605  0.01706  -0.01096 151 TRP   A CE2 
1097 C  CE3 . TRP   A 151 ? 0.33289 0.48575 0.39569 0.01474  0.01538  -0.00807 151 TRP   A CE3 
1098 C  CZ2 . TRP   A 151 ? 0.39884 0.54482 0.44636 0.01445  0.01373  -0.01362 151 TRP   A CZ2 
1099 C  CZ3 . TRP   A 151 ? 0.27853 0.42975 0.34114 0.01235  0.01083  -0.01067 151 TRP   A CZ3 
1100 C  CH2 . TRP   A 151 ? 0.35241 0.50005 0.40689 0.01288  0.01029  -0.01391 151 TRP   A CH2 
1101 N  N   . SER   A 152 ? 0.34067 0.50538 0.40092 0.03551  0.02546  0.00309  152 SER   A N   
1102 C  CA  . SER   A 152 ? 0.36021 0.53451 0.42494 0.03996  0.02770  0.00642  152 SER   A CA  
1103 C  C   . SER   A 152 ? 0.35018 0.53974 0.42493 0.03967  0.02671  0.01161  152 SER   A C   
1104 O  O   . SER   A 152 ? 0.33735 0.53750 0.42005 0.03885  0.02795  0.01560  152 SER   A O   
1105 C  CB  . SER   A 152 ? 0.42577 0.59586 0.48150 0.04858  0.02871  0.00558  152 SER   A CB  
1106 O  OG  . SER   A 152 ? 0.41924 0.57513 0.46676 0.04755  0.02873  0.00168  152 SER   A OG  
1107 N  N   . LEU   A 153 ? 0.37352 0.56492 0.44820 0.04005  0.02414  0.01226  153 LEU   A N   
1108 C  CA  . LEU   A 153 ? 0.33369 0.53979 0.41897 0.03833  0.02213  0.01765  153 LEU   A CA  
1109 C  C   . LEU   A 153 ? 0.30444 0.51170 0.39807 0.02947  0.01946  0.01883  153 LEU   A C   
1110 O  O   . LEU   A 153 ? 0.31602 0.53564 0.41988 0.02705  0.01885  0.02454  153 LEU   A O   
1111 C  CB  . LEU   A 153 ? 0.37494 0.57992 0.45766 0.03934  0.01902  0.01720  153 LEU   A CB  
1112 C  CG  . LEU   A 153 ? 0.47113 0.68384 0.55208 0.04784  0.01958  0.01955  153 LEU   A CG  
1113 C  CD1 . LEU   A 153 ? 0.41190 0.62049 0.49032 0.04634  0.01559  0.01846  153 LEU   A CD1 
1114 C  CD2 . LEU   A 153 ? 0.43073 0.66414 0.52305 0.05007  0.02084  0.02652  153 LEU   A CD2 
1115 N  N   . VAL   A 154 ? 0.28643 0.48097 0.37535 0.02485  0.01733  0.01370  154 VAL   A N   
1116 C  CA  . VAL   A 154 ? 0.28878 0.48138 0.38334 0.01763  0.01353  0.01343  154 VAL   A CA  
1117 C  C   . VAL   A 154 ? 0.32828 0.52473 0.42869 0.01581  0.01508  0.01603  154 VAL   A C   
1118 O  O   . VAL   A 154 ? 0.34180 0.54471 0.45153 0.01088  0.01154  0.02053  154 VAL   A O   
1119 C  CB  . VAL   A 154 ? 0.27493 0.45363 0.36115 0.01543  0.01228  0.00657  154 VAL   A CB  
1120 C  CG1 . VAL   A 154 ? 0.31561 0.49093 0.40617 0.00979  0.00805  0.00537  154 VAL   A CG1 
1121 C  CG2 . VAL   A 154 ? 0.28444 0.46013 0.36534 0.01612  0.00978  0.00477  154 VAL   A CG2 
1122 N  N   . LEU   A 155 ? 0.30537 0.49679 0.40003 0.01918  0.01964  0.01337  155 LEU   A N   
1123 C  CA  . LEU   A 155 ? 0.31104 0.50574 0.41025 0.01794  0.02130  0.01573  155 LEU   A CA  
1124 C  C   . LEU   A 155 ? 0.33937 0.55095 0.44683 0.02000  0.02272  0.02367  155 LEU   A C   
1125 O  O   . LEU   A 155 ? 0.35602 0.57432 0.47180 0.01562  0.02128  0.02852  155 LEU   A O   
1126 C  CB  . LEU   A 155 ? 0.33743 0.52311 0.42819 0.02149  0.02543  0.01123  155 LEU   A CB  
1127 C  CG  . LEU   A 155 ? 0.36203 0.53492 0.44838 0.01769  0.02417  0.00518  155 LEU   A CG  
1128 C  CD1 . LEU   A 155 ? 0.40356 0.57055 0.48535 0.01645  0.02190  0.00154  155 LEU   A CD1 
1129 C  CD2 . LEU   A 155 ? 0.34206 0.50820 0.42142 0.02096  0.02801  0.00220  155 LEU   A CD2 
1130 N  N   . ASP   A 156 ? 0.28108 0.50063 0.38648 0.02683  0.02520  0.02560  156 ASP   A N   
1131 C  CA  . ASP   A 156 ? 0.31714 0.55601 0.43062 0.02978  0.02702  0.03362  156 ASP   A CA  
1132 C  C   . ASP   A 156 ? 0.32524 0.57604 0.45161 0.02251  0.02214  0.04069  156 ASP   A C   
1133 O  O   . ASP   A 156 ? 0.34059 0.60520 0.47680 0.01939  0.02189  0.04842  156 ASP   A O   
1134 C  CB  . ASP   A 156 ? 0.35548 0.60020 0.46285 0.04032  0.03032  0.03345  156 ASP   A CB  
1135 C  CG  . ASP   A 156 ? 0.60454 0.84134 0.70092 0.04807  0.03459  0.02909  156 ASP   A CG  
1136 O  OD1 . ASP   A 156 ? 0.56997 0.80328 0.65723 0.05680  0.03569  0.02618  156 ASP   A OD1 
1137 O  OD2 . ASP   A 156 ? 0.50424 0.73676 0.60051 0.04538  0.03598  0.02835  156 ASP   A OD2 
1138 N  N   . ILE   A 157 ? 0.30885 0.55383 0.43512 0.01911  0.01755  0.03848  157 ILE   A N   
1139 C  CA  . ILE   A 157 ? 0.32067 0.57274 0.45801 0.01116  0.01105  0.04420  157 ILE   A CA  
1140 C  C   . ILE   A 157 ? 0.30000 0.54604 0.44196 0.00304  0.00713  0.04520  157 ILE   A C   
1141 O  O   . ILE   A 157 ? 0.28539 0.54260 0.43879 -0.00303 0.00320  0.05357  157 ILE   A O   
1142 C  CB  . ILE   A 157 ? 0.31057 0.55373 0.44415 0.00961  0.00639  0.03989  157 ILE   A CB  
1143 C  CG1 . ILE   A 157 ? 0.34535 0.59789 0.47693 0.01723  0.00923  0.04124  157 ILE   A CG1 
1144 C  CG2 . ILE   A 157 ? 0.32425 0.56843 0.46709 0.00031  -0.00223 0.04390  157 ILE   A CG2 
1145 C  CD1 . ILE   A 157 ? 0.36204 0.60365 0.48641 0.01766  0.00618  0.03577  157 ILE   A CD1 
1146 N  N   . SER   A 158 ? 0.28466 0.51319 0.41804 0.00259  0.00750  0.03718  158 SER   A N   
1147 C  CA  . SER   A 158 ? 0.32838 0.55001 0.46548 -0.00435 0.00295  0.03758  158 SER   A CA  
1148 C  C   . SER   A 158 ? 0.32764 0.56098 0.47173 -0.00521 0.00568  0.04495  158 SER   A C   
1149 O  O   . SER   A 158 ? 0.33263 0.56623 0.48414 -0.01251 0.00022  0.04967  158 SER   A O   
1150 C  CB  . SER   A 158 ? 0.31107 0.51383 0.43764 -0.00341 0.00341  0.02757  158 SER   A CB  
1151 O  OG  . SER   A 158 ? 0.33400 0.53522 0.45511 0.00153  0.01034  0.02514  158 SER   A OG  
1152 N  N   . ARG   A 159 ? 0.27792 0.51980 0.41876 0.00237  0.01343  0.04586  159 ARG   A N   
1153 C  CA  . ARG   A 159 ? 0.30605 0.56114 0.45243 0.00292  0.01674  0.05312  159 ARG   A CA  
1154 C  C   . ARG   A 159 ? 0.33974 0.61687 0.49913 -0.00031 0.01483  0.06500  159 ARG   A C   
1155 O  O   . ARG   A 159 ? 0.33679 0.62577 0.50309 -0.00279 0.01565  0.07290  159 ARG   A O   
1156 C  CB  . ARG   A 159 ? 0.38856 0.64720 0.52657 0.01339  0.02492  0.05061  159 ARG   A CB  
1157 C  CG  . ARG   A 159 ? 0.40584 0.64541 0.53207 0.01629  0.02718  0.04083  159 ARG   A CG  
1158 C  CD  . ARG   A 159 ? 0.43203 0.67240 0.54863 0.02685  0.03322  0.03776  159 ARG   A CD  
1159 N  NE  . ARG   A 159 ? 0.46731 0.72061 0.58539 0.03140  0.03737  0.04311  159 ARG   A NE  
1160 C  CZ  . ARG   A 159 ? 0.49164 0.75593 0.60572 0.04134  0.04162  0.04482  159 ARG   A CZ  
1161 N  NH1 . ARG   A 159 ? 0.49791 0.76303 0.60793 0.04713  0.04176  0.04267  159 ARG   A NH1 
1162 N  NH2 . ARG   A 159 ? 0.56516 0.83946 0.67840 0.04631  0.04551  0.04853  159 ARG   A NH2 
1163 N  N   . SER   A 160 ? 0.33466 0.61871 0.49745 -0.00003 0.01261  0.06689  160 SER   A N   
1164 C  CA  . SER   A 160 ? 0.31042 0.61918 0.48611 -0.00184 0.01157  0.07889  160 SER   A CA  
1165 C  C   . SER   A 160 ? 0.35674 0.66800 0.54495 -0.01443 0.00178  0.08663  160 SER   A C   
1166 O  O   . SER   A 160 ? 0.35544 0.68929 0.55652 -0.01790 0.00026  0.09877  160 SER   A O   
1167 C  CB  . SER   A 160 ? 0.39243 0.70834 0.56578 0.00534  0.01364  0.07742  160 SER   A CB  
1168 O  OG  . SER   A 160 ? 0.44087 0.75407 0.60247 0.01710  0.02135  0.07109  160 SER   A OG  
1169 N  N   . PHE   A 161 ? 0.32203 0.61158 0.50687 -0.02109 -0.00561 0.08038  161 PHE   A N   
1170 C  CA  . PHE   A 161 ? 0.29120 0.57950 0.48593 -0.03231 -0.01694 0.08641  161 PHE   A CA  
1171 C  C   . PHE   A 161 ? 0.34879 0.61792 0.54148 -0.03931 -0.02371 0.08332  161 PHE   A C   
1172 O  O   . PHE   A 161 ? 0.36498 0.61618 0.54615 -0.03518 -0.02101 0.07261  161 PHE   A O   
1173 C  CB  . PHE   A 161 ? 0.36221 0.64185 0.55396 -0.03270 -0.02234 0.08121  161 PHE   A CB  
1174 C  CG  . PHE   A 161 ? 0.31070 0.60840 0.50549 -0.02680 -0.01788 0.08482  161 PHE   A CG  
1175 C  CD1 . PHE   A 161 ? 0.38696 0.70817 0.59651 -0.03124 -0.02078 0.09784  161 PHE   A CD1 
1176 C  CD2 . PHE   A 161 ? 0.29105 0.58322 0.47417 -0.01664 -0.01091 0.07586  161 PHE   A CD2 
1177 C  CE1 . PHE   A 161 ? 0.38816 0.72690 0.60057 -0.02493 -0.01681 0.10101  161 PHE   A CE1 
1178 C  CE2 . PHE   A 161 ? 0.36847 0.67631 0.55363 -0.01033 -0.00735 0.07889  161 PHE   A CE2 
1179 C  CZ  . PHE   A 161 ? 0.36566 0.69710 0.56545 -0.01401 -0.01014 0.09116  161 PHE   A CZ  
1180 N  N   . ASN   A 162 ? 0.32516 0.59747 0.52892 -0.05002 -0.03344 0.09276  162 ASN   A N   
1181 C  CA  . ASN   A 162 ? 0.41068 0.66280 0.61138 -0.05586 -0.04089 0.08929  162 ASN   A CA  
1182 C  C   . ASN   A 162 ? 0.41454 0.64363 0.60845 -0.05837 -0.05101 0.08022  162 ASN   A C   
1183 O  O   . ASN   A 162 ? 0.40423 0.63420 0.59762 -0.05744 -0.05336 0.07844  162 ASN   A O   
1184 C  CB  . ASN   A 162 ? 0.43977 0.70248 0.65370 -0.06626 -0.04747 0.10332  162 ASN   A CB  
1185 C  CG  . ASN   A 162 ? 0.39611 0.66886 0.62309 -0.07613 -0.05817 0.11448  162 ASN   A CG  
1186 O  OD1 . ASN   A 162 ? 0.46968 0.73110 0.69404 -0.07760 -0.06539 0.10953  162 ASN   A OD1 
1187 N  ND2 . ASN   A 162 ? 0.49247 0.78784 0.73390 -0.08319 -0.05937 0.13045  162 ASN   A ND2 
1188 N  N   . ILE   A 163 ? 0.38913 0.59702 0.57651 -0.06036 -0.05684 0.07366  163 ILE   A N   
1189 C  CA  . ILE   A 163 ? 0.40929 0.59403 0.58707 -0.06006 -0.06558 0.06294  163 ILE   A CA  
1190 C  C   . ILE   A 163 ? 0.47287 0.65628 0.65789 -0.06848 -0.07908 0.06893  163 ILE   A C   
1191 O  O   . ILE   A 163 ? 0.42868 0.60255 0.60722 -0.06625 -0.08334 0.06199  163 ILE   A O   
1192 C  CB  . ILE   A 163 ? 0.41553 0.58000 0.58603 -0.06021 -0.07006 0.05608  163 ILE   A CB  
1193 C  CG1 . ILE   A 163 ? 0.35153 0.51467 0.51248 -0.05070 -0.05725 0.04737  163 ILE   A CG1 
1194 C  CG2 . ILE   A 163 ? 0.45172 0.59320 0.61354 -0.06064 -0.08204 0.04693  163 ILE   A CG2 
1195 C  CD1 . ILE   A 163 ? 0.35945 0.50829 0.51577 -0.05063 -0.05939 0.04304  163 ILE   A CD1 
1196 N  N   . ASN   A 164 ? 0.45797 0.65088 0.65644 -0.07866 -0.08665 0.08236  164 ASN   A N   
1197 C  CA  . ASN   A 164 ? 0.44175 0.63261 0.64777 -0.08788 -0.10111 0.08892  164 ASN   A CA  
1198 C  C   . ASN   A 164 ? 0.48011 0.68744 0.69023 -0.08544 -0.09708 0.09151  164 ASN   A C   
1199 O  O   . ASN   A 164 ? 0.51695 0.71479 0.72500 -0.08763 -0.10665 0.08866  164 ASN   A O   
1200 C  CB  . ASN   A 164 ? 0.46852 0.66932 0.68964 -0.10025 -0.10969 0.10489  164 ASN   A CB  
1201 C  CG  . ASN   A 164 ? 0.62177 0.80021 0.83796 -0.10419 -0.11877 0.10186  164 ASN   A CG  
1202 O  OD1 . ASN   A 164 ? 0.63824 0.79061 0.84067 -0.09965 -0.12426 0.08823  164 ASN   A OD1 
1203 N  ND2 . ASN   A 164 ? 0.73763 0.92636 0.96457 -0.11223 -0.12079 0.11464  164 ASN   A ND2 
1204 N  N   . ARG   A 165 ? 0.44815 0.67953 0.66322 -0.08016 -0.08343 0.09650  165 ARG   A N   
1205 C  CA  . ARG   A 165 ? 0.52807 0.77545 0.74644 -0.07647 -0.07908 0.09859  165 ARG   A CA  
1206 C  C   . ARG   A 165 ? 0.49552 0.72559 0.69885 -0.06838 -0.07738 0.08389  165 ARG   A C   
1207 O  O   . ARG   A 165 ? 0.43999 0.67058 0.64389 -0.06901 -0.08231 0.08355  165 ARG   A O   
1208 C  CB  . ARG   A 165 ? 0.42520 0.69896 0.64855 -0.06975 -0.06455 0.10453  165 ARG   A CB  
1209 C  CG  . ARG   A 165 ? 0.47383 0.76210 0.69858 -0.06405 -0.05990 0.10503  165 ARG   A CG  
1210 C  CD  . ARG   A 165 ? 0.50220 0.80107 0.74060 -0.07380 -0.07155 0.11596  165 ARG   A CD  
1211 N  NE  . ARG   A 165 ? 0.42224 0.73526 0.66136 -0.06714 -0.06640 0.11583  165 ARG   A NE  
1212 C  CZ  . ARG   A 165 ? 0.67192 1.01278 0.91868 -0.06172 -0.05684 0.12380  165 ARG   A CZ  
1213 N  NH1 . ARG   A 165 ? 0.58479 0.94286 0.83866 -0.06204 -0.05095 0.13243  165 ARG   A NH1 
1214 N  NH2 . ARG   A 165 ? 0.57615 0.92812 0.82285 -0.05518 -0.05334 0.12308  165 ARG   A NH2 
1215 N  N   . MET   A 166 ? 0.43270 0.64782 0.62269 -0.06112 -0.07088 0.07220  166 MET   A N   
1216 C  CA  . MET   A 166 ? 0.45331 0.65420 0.62899 -0.05340 -0.06829 0.05915  166 MET   A CA  
1217 C  C   . MET   A 166 ? 0.45542 0.63433 0.62464 -0.05709 -0.08202 0.05278  166 MET   A C   
1218 O  O   . MET   A 166 ? 0.46522 0.63762 0.62684 -0.05348 -0.08376 0.04630  166 MET   A O   
1219 C  CB  . MET   A 166 ? 0.41175 0.60610 0.57652 -0.04511 -0.05709 0.05018  166 MET   A CB  
1220 C  CG  . MET   A 166 ? 0.42756 0.61664 0.58020 -0.03650 -0.05038 0.04030  166 MET   A CG  
1221 S  SD  . MET   A 166 ? 0.46486 0.67570 0.62239 -0.03172 -0.04174 0.04612  166 MET   A SD  
1222 C  CE  . MET   A 166 ? 0.34565 0.57699 0.51393 -0.03178 -0.03406 0.05653  166 MET   A CE  
1223 N  N   . LYS   A 167 ? 0.45324 0.61990 0.62450 -0.06377 -0.09245 0.05444  167 LYS   A N   
1224 C  CA  . LYS   A 167 ? 0.41629 0.56101 0.58085 -0.06677 -0.10738 0.04858  167 LYS   A CA  
1225 C  C   . LYS   A 167 ? 0.48888 0.63908 0.66114 -0.07307 -0.11727 0.05545  167 LYS   A C   
1226 O  O   . LYS   A 167 ? 0.47589 0.61018 0.63939 -0.07203 -0.12664 0.04825  167 LYS   A O   
1227 C  CB  . LYS   A 167 ? 0.46229 0.59295 0.62847 -0.07315 -0.11797 0.05046  167 LYS   A CB  
1228 C  CG  . LYS   A 167 ? 0.52175 0.64139 0.67724 -0.06592 -0.11076 0.04071  167 LYS   A CG  
1229 C  CD  . LYS   A 167 ? 0.57454 0.67955 0.73129 -0.07175 -0.12160 0.04255  167 LYS   A CD  
1230 C  CE  . LYS   A 167 ? 0.64108 0.71954 0.78753 -0.07189 -0.13771 0.03416  167 LYS   A CE  
1231 N  NZ  . LYS   A 167 ? 0.78534 0.85329 0.93762 -0.08071 -0.15038 0.04082  167 LYS   A NZ  
1232 N  N   . ARG   A 168 ? 0.46878 0.64227 0.65734 -0.07933 -0.11561 0.06958  168 ARG   A N   
1233 C  CA  . ARG   A 168 ? 0.45093 0.63194 0.64755 -0.08496 -0.12442 0.07642  168 ARG   A CA  
1234 C  C   . ARG   A 168 ? 0.50554 0.68997 0.69446 -0.07645 -0.11752 0.06935  168 ARG   A C   
1235 O  O   . ARG   A 168 ? 0.45379 0.64255 0.64778 -0.08028 -0.12525 0.07359  168 ARG   A O   
1236 C  CB  . ARG   A 168 ? 0.44521 0.65345 0.66222 -0.09367 -0.12448 0.09435  168 ARG   A CB  
1237 C  CG  . ARG   A 168 ? 0.53968 0.74162 0.76497 -0.10512 -0.13645 0.10305  168 ARG   A CG  
1238 C  CD  . ARG   A 168 ? 0.57590 0.80234 0.82219 -0.11690 -0.14233 0.12234  168 ARG   A CD  
1239 N  NE  . ARG   A 168 ? 0.76988 1.01812 1.02377 -0.11536 -0.12939 0.13023  168 ARG   A NE  
1240 C  CZ  . ARG   A 168 ? 0.71736 0.99148 0.97534 -0.10779 -0.11408 0.13345  168 ARG   A CZ  
1241 N  NH1 . ARG   A 168 ? 0.73455 1.01886 0.99258 -0.10257 -0.11038 0.13176  168 ARG   A NH1 
1242 N  NH2 . ARG   A 168 ? 0.64182 0.92994 0.90209 -0.10426 -0.10243 0.13725  168 ARG   A NH2 
1243 N  N   . CYS   A 169 ? 0.44297 0.62519 0.62006 -0.06573 -0.10429 0.05935  169 CYS   A N   
1244 C  CA  . CYS   A 169 ? 0.45261 0.63465 0.62060 -0.05806 -0.09912 0.05218  169 CYS   A CA  
1245 C  C   . CYS   A 169 ? 0.38665 0.54436 0.53831 -0.05433 -0.10590 0.03928  169 CYS   A C   
1246 O  O   . CYS   A 169 ? 0.41259 0.56884 0.55472 -0.04746 -0.10090 0.03256  169 CYS   A O   
1247 C  CB  . CYS   A 169 ? 0.44799 0.63947 0.61073 -0.04854 -0.08226 0.04839  169 CYS   A CB  
1248 S  SG  . CYS   A 169 ? 0.45157 0.67309 0.62974 -0.04876 -0.07306 0.06144  169 CYS   A SG  
1249 N  N   . LEU   A 170 ? 0.42317 0.56203 0.57086 -0.05823 -0.11751 0.03586  170 LEU   A N   
1250 C  CA  . LEU   A 170 ? 0.41535 0.53109 0.54542 -0.05242 -0.12310 0.02232  170 LEU   A CA  
1251 C  C   . LEU   A 170 ? 0.44382 0.55503 0.56789 -0.05100 -0.12999 0.01903  170 LEU   A C   
1252 O  O   . LEU   A 170 ? 0.41883 0.51853 0.52706 -0.04293 -0.12844 0.00777  170 LEU   A O   
1253 C  CB  . LEU   A 170 ? 0.46715 0.56361 0.59515 -0.05709 -0.13689 0.02051  170 LEU   A CB  
1254 C  CG  . LEU   A 170 ? 0.65515 0.72806 0.76382 -0.04919 -0.14242 0.00578  170 LEU   A CG  
1255 C  CD1 . LEU   A 170 ? 0.59480 0.66967 0.69323 -0.03898 -0.12689 -0.00301 170 LEU   A CD1 
1256 C  CD2 . LEU   A 170 ? 0.74554 0.79775 0.85221 -0.05387 -0.15899 0.00450  170 LEU   A CD2 
1257 N  N   . LYS   A 171 ? 0.44837 0.56998 0.58492 -0.05849 -0.13723 0.02911  171 LYS   A N   
1258 C  CA  . LYS   A 171 ? 0.41947 0.53611 0.55034 -0.05743 -0.14477 0.02612  171 LYS   A CA  
1259 C  C   . LYS   A 171 ? 0.45876 0.58148 0.57965 -0.04751 -0.13152 0.01948  171 LYS   A C   
1260 O  O   . LYS   A 171 ? 0.43300 0.54575 0.54199 -0.04326 -0.13592 0.01225  171 LYS   A O   
1261 C  CB  . LYS   A 171 ? 0.43909 0.57028 0.58719 -0.06715 -0.15301 0.03949  171 LYS   A CB  
1262 C  CG  . LYS   A 171 ? 0.61946 0.74501 0.76184 -0.06630 -0.16153 0.03653  171 LYS   A CG  
1263 C  CD  . LYS   A 171 ? 0.58585 0.72023 0.74446 -0.07769 -0.17547 0.04923  171 LYS   A CD  
1264 C  CE  . LYS   A 171 ? 0.67227 0.79000 0.81959 -0.07649 -0.18866 0.04243  171 LYS   A CE  
1265 N  NZ  . LYS   A 171 ? 0.72343 0.85567 0.88482 -0.08394 -0.19686 0.05347  171 LYS   A NZ  
1266 N  N   . ILE   A 172 ? 0.39599 0.53446 0.52099 -0.04378 -0.11603 0.02211  172 ILE   A N   
1267 C  CA  . ILE   A 172 ? 0.40639 0.54985 0.52240 -0.03534 -0.10481 0.01700  172 ILE   A CA  
1268 C  C   . ILE   A 172 ? 0.46534 0.59223 0.56268 -0.02774 -0.10234 0.00417  172 ILE   A C   
1269 O  O   . ILE   A 172 ? 0.39760 0.52479 0.48492 -0.02146 -0.09649 -0.00079 172 ILE   A O   
1270 C  CB  . ILE   A 172 ? 0.29248 0.45412 0.41539 -0.03235 -0.09006 0.02206  172 ILE   A CB  
1271 C  CG1 . ILE   A 172 ? 0.35525 0.51157 0.47290 -0.02901 -0.08173 0.01720  172 ILE   A CG1 
1272 C  CG2 . ILE   A 172 ? 0.34392 0.52480 0.48568 -0.03894 -0.09146 0.03525  172 ILE   A CG2 
1273 C  CD1 . ILE   A 172 ? 0.33706 0.50811 0.45918 -0.02540 -0.06839 0.02096  172 ILE   A CD1 
1274 N  N   . MET   A 173 ? 0.42153 0.53498 0.51403 -0.02792 -0.10661 -0.00084 173 MET   A N   
1275 C  CA  . MET   A 173 ? 0.39881 0.49764 0.47367 -0.02012 -0.10543 -0.01298 173 MET   A CA  
1276 C  C   . MET   A 173 ? 0.48650 0.56783 0.55087 -0.01932 -0.12014 -0.01950 173 MET   A C   
1277 O  O   . MET   A 173 ? 0.45936 0.52865 0.50830 -0.01201 -0.12074 -0.02981 173 MET   A O   
1278 C  CB  . MET   A 173 ? 0.40081 0.49485 0.47452 -0.01870 -0.10124 -0.01604 173 MET   A CB  
1279 C  CG  . MET   A 173 ? 0.39411 0.50350 0.47667 -0.01900 -0.08771 -0.01034 173 MET   A CG  
1280 S  SD  . MET   A 173 ? 0.40454 0.50775 0.48690 -0.01838 -0.08468 -0.01313 173 MET   A SD  
1281 C  CE  . MET   A 173 ? 0.45523 0.54717 0.51758 -0.00784 -0.08069 -0.02690 173 MET   A CE  
1282 N  N   . GLY   A 174 ? 0.44513 0.52537 0.51718 -0.02623 -0.13232 -0.01362 174 GLY   A N   
1283 C  CA  . GLY   A 174 ? 0.52029 0.58230 0.58209 -0.02575 -0.14813 -0.01960 174 GLY   A CA  
1284 C  C   . GLY   A 174 ? 0.62292 0.66560 0.67823 -0.02542 -0.15863 -0.02550 174 GLY   A C   
1285 O  O   . GLY   A 174 ? 0.71577 0.74107 0.75469 -0.01899 -0.16706 -0.03582 174 GLY   A O   
1286 N  N   . ARG   A 175 ? 0.59578 0.64089 0.66273 -0.03150 -0.15861 -0.01936 175 ARG   A N   
1287 C  CA  . ARG   A 175 ? 0.77253 0.79931 0.83340 -0.03075 -0.16764 -0.02481 175 ARG   A CA  
1288 C  C   . ARG   A 175 ? 0.81328 0.83638 0.88877 -0.04314 -0.18155 -0.01441 175 ARG   A C   
1289 O  O   . ARG   A 175 ? 0.66697 0.70823 0.76011 -0.05177 -0.17810 -0.00173 175 ARG   A O   
1290 C  CB  . ARG   A 175 ? 0.71694 0.74849 0.77590 -0.02543 -0.15378 -0.02824 175 ARG   A CB  
1291 C  CG  . ARG   A 175 ? 0.65192 0.68567 0.69578 -0.01366 -0.14181 -0.03839 175 ARG   A CG  
1292 C  CD  . ARG   A 175 ? 0.75115 0.78980 0.79391 -0.00906 -0.12905 -0.04122 175 ARG   A CD  
1293 N  NE  . ARG   A 175 ? 0.78873 0.82921 0.81672 0.00163  -0.11963 -0.05041 175 ARG   A NE  
1294 C  CZ  . ARG   A 175 ? 0.87072 0.89837 0.88279 0.01057  -0.12400 -0.06142 175 ARG   A CZ  
1295 N  NH1 . ARG   A 175 ? 0.83700 0.84699 0.84499 0.01096  -0.13730 -0.06573 175 ARG   A NH1 
1296 N  NH2 . ARG   A 175 ? 0.84254 0.87546 0.84210 0.01962  -0.11532 -0.06799 175 ARG   A NH2 
1297 N  N   . SER   A 176 ? 0.93224 0.93194 0.99973 -0.04353 -0.19766 -0.01973 176 SER   A N   
1298 C  CA  . SER   A 176 ? 1.05770 1.04878 1.13657 -0.05552 -0.21403 -0.01065 176 SER   A CA  
1299 C  C   . SER   A 176 ? 1.02171 1.01147 1.10520 -0.05720 -0.21045 -0.00872 176 SER   A C   
1300 O  O   . SER   A 176 ? 1.08505 1.07118 1.15759 -0.04727 -0.20090 -0.01840 176 SER   A O   
1301 C  CB  . SER   A 176 ? 1.13555 1.09834 1.20122 -0.05473 -0.23610 -0.01805 176 SER   A CB  
1302 O  OG  . SER   A 176 ? 1.08504 1.04907 1.14558 -0.05270 -0.23923 -0.02017 176 SER   A OG  
1303 N  N   . GLU   A 177 ? 1.09769 1.09134 1.19778 -0.07005 -0.21835 0.00448  177 GLU   A N   
1304 C  CA  . GLU   A 177 ? 1.35894 1.35590 1.46550 -0.07236 -0.21259 0.00836  177 GLU   A CA  
1305 C  C   . GLU   A 177 ? 1.40242 1.37146 1.49536 -0.06800 -0.22450 -0.00157 177 GLU   A C   
1306 O  O   . GLU   A 177 ? 1.36126 1.33119 1.45409 -0.06528 -0.21680 -0.00306 177 GLU   A O   
1307 C  CB  . GLU   A 177 ? 1.34440 1.35709 1.47319 -0.08733 -0.21622 0.02670  177 GLU   A CB  
1308 C  CG  . GLU   A 177 ? 1.35306 1.38879 1.49255 -0.08742 -0.19768 0.03348  177 GLU   A CG  
1309 C  CD  . GLU   A 177 ? 1.38929 1.41170 1.52204 -0.08382 -0.19678 0.02771  177 GLU   A CD  
1310 O  OE1 . GLU   A 177 ? 1.50451 1.50258 1.63103 -0.08634 -0.21390 0.02448  177 GLU   A OE1 
1311 O  OE2 . GLU   A 177 ? 1.28010 1.31522 1.41326 -0.07825 -0.17990 0.02621  177 GLU   A OE2 
1312 N  N   . GLY   A 178 ? 1.25069 1.19459 1.33089 -0.06598 -0.24294 -0.00925 178 GLY   A N   
1313 C  CA  . GLY   A 178 ? 1.19715 1.11311 1.26387 -0.06123 -0.25620 -0.01867 178 GLY   A CA  
1314 C  C   . GLY   A 178 ? 1.11644 1.02892 1.16704 -0.04544 -0.24380 -0.03336 178 GLY   A C   
1315 O  O   . GLY   A 178 ? 1.12145 1.01340 1.16191 -0.04061 -0.25290 -0.04083 178 GLY   A O   
1316 N  N   . GLU   A 179 ? 1.04986 0.98170 1.09799 -0.03748 -0.22417 -0.03723 179 GLU   A N   
1317 C  CA  . GLU   A 179 ? 0.98017 0.91104 1.01346 -0.02287 -0.21249 -0.05032 179 GLU   A CA  
1318 C  C   . GLU   A 179 ? 0.88690 0.83279 0.92946 -0.02363 -0.19689 -0.04606 179 GLU   A C   
1319 O  O   . GLU   A 179 ? 0.78285 0.74207 0.84278 -0.03455 -0.19312 -0.03315 179 GLU   A O   
1320 C  CB  . GLU   A 179 ? 0.97018 0.91318 0.99481 -0.01402 -0.20040 -0.05655 179 GLU   A CB  
1321 C  CG  . GLU   A 179 ? 1.00655 0.97645 1.04667 -0.02077 -0.18540 -0.04548 179 GLU   A CG  
1322 C  CD  . GLU   A 179 ? 1.00702 0.98632 1.03821 -0.01312 -0.17616 -0.05087 179 GLU   A CD  
1323 O  OE1 . GLU   A 179 ? 1.00053 0.96939 1.02331 -0.01161 -0.18736 -0.05469 179 GLU   A OE1 
1324 O  OE2 . GLU   A 179 ? 0.90566 0.90235 0.93810 -0.00889 -0.15819 -0.05091 179 GLU   A OE2 
1325 N  N   . GLU   A 180 ? 0.80748 0.75216 0.83777 -0.01131 -0.18773 -0.05708 180 GLU   A N   
1326 C  CA  . GLU   A 180 ? 0.74202 0.69977 0.77893 -0.01055 -0.17302 -0.05468 180 GLU   A CA  
1327 C  C   . GLU   A 180 ? 0.65286 0.63706 0.70189 -0.01469 -0.15549 -0.04606 180 GLU   A C   
1328 O  O   . GLU   A 180 ? 0.60352 0.59651 0.64864 -0.01113 -0.14917 -0.04813 180 GLU   A O   
1329 C  CB  . GLU   A 180 ? 0.76482 0.71839 0.78607 0.00398  -0.16648 -0.06814 180 GLU   A CB  
1330 C  CG  . GLU   A 180 ? 0.81954 0.77857 0.84611 0.00452  -0.15756 -0.06679 180 GLU   A CG  
1331 C  CD  . GLU   A 180 ? 0.88200 0.84198 0.89504 0.01869  -0.14904 -0.07883 180 GLU   A CD  
1332 O  OE1 . GLU   A 180 ? 0.86662 0.83014 0.88264 0.02026  -0.14247 -0.07891 180 GLU   A OE1 
1333 O  OE2 . GLU   A 180 ? 0.97153 0.92902 0.97076 0.02842  -0.14954 -0.08801 180 GLU   A OE2 
1334 N  N   . ASN   A 181 ? 0.62520 0.62156 0.68813 -0.02168 -0.14810 -0.03652 181 ASN   A N   
1335 C  CA  . ASN   A 181 ? 0.55640 0.57674 0.63103 -0.02559 -0.13316 -0.02769 181 ASN   A CA  
1336 C  C   . ASN   A 181 ? 0.52499 0.55582 0.59575 -0.01778 -0.11622 -0.03245 181 ASN   A C   
1337 O  O   . ASN   A 181 ? 0.50158 0.53630 0.57813 -0.01950 -0.11107 -0.02920 181 ASN   A O   
1338 C  CB  . ASN   A 181 ? 0.57440 0.60366 0.66653 -0.03770 -0.13560 -0.01346 181 ASN   A CB  
1339 C  CG  . ASN   A 181 ? 0.72217 0.74194 0.81977 -0.04705 -0.15351 -0.00704 181 ASN   A CG  
1340 O  OD1 . ASN   A 181 ? 0.76182 0.78462 0.85946 -0.04822 -0.15662 -0.00602 181 ASN   A OD1 
1341 N  ND2 . ASN   A 181 ? 0.78282 0.79079 0.88514 -0.05414 -0.16593 -0.00225 181 ASN   A ND2 
1342 N  N   . TYR   A 182 ? 0.49730 0.53257 0.55809 -0.00949 -0.10817 -0.03978 182 TYR   A N   
1343 C  CA  . TYR   A 182 ? 0.46915 0.51570 0.52730 -0.00336 -0.09253 -0.04283 182 TYR   A CA  
1344 C  C   . TYR   A 182 ? 0.48780 0.55278 0.55836 -0.00871 -0.08103 -0.03293 182 TYR   A C   
1345 O  O   . TYR   A 182 ? 0.43802 0.51022 0.51703 -0.01482 -0.08293 -0.02513 182 TYR   A O   
1346 C  CB  . TYR   A 182 ? 0.46392 0.51150 0.50862 0.00594  -0.08766 -0.05177 182 TYR   A CB  
1347 C  CG  . TYR   A 182 ? 0.58118 0.61265 0.61179 0.01422  -0.09668 -0.06289 182 TYR   A CG  
1348 C  CD1 . TYR   A 182 ? 0.63568 0.66512 0.66138 0.02060  -0.09273 -0.06873 182 TYR   A CD1 
1349 C  CD2 . TYR   A 182 ? 0.71526 0.73347 0.73698 0.01638  -0.10964 -0.06777 182 TYR   A CD2 
1350 C  CE1 . TYR   A 182 ? 0.69366 0.70937 0.70587 0.02976  -0.10091 -0.07931 182 TYR   A CE1 
1351 C  CE2 . TYR   A 182 ? 0.75975 0.76252 0.76681 0.02569  -0.11846 -0.07881 182 TYR   A CE2 
1352 C  CZ  . TYR   A 182 ? 0.70547 0.70761 0.70784 0.03274  -0.11377 -0.08458 182 TYR   A CZ  
1353 O  OH  . TYR   A 182 ? 0.84164 0.82971 0.82900 0.04351  -0.12222 -0.09588 182 TYR   A OH  
1354 N  N   . CYS   A 183 ? 0.35136 0.42397 0.42289 -0.00598 -0.06960 -0.03323 183 CYS   A N   
1355 C  CA  . CYS   A 183 ? 0.37919 0.46796 0.46039 -0.00934 -0.05878 -0.02497 183 CYS   A CA  
1356 C  C   . CYS   A 183 ? 0.35191 0.45036 0.43135 -0.00756 -0.05255 -0.02406 183 CYS   A C   
1357 O  O   . CYS   A 183 ? 0.35561 0.46650 0.44315 -0.01046 -0.04658 -0.01660 183 CYS   A O   
1358 C  CB  . CYS   A 183 ? 0.35257 0.44547 0.43249 -0.00561 -0.04846 -0.02705 183 CYS   A CB  
1359 S  SG  . CYS   A 183 ? 0.41154 0.49561 0.49614 -0.00883 -0.05464 -0.02562 183 CYS   A SG  
1360 N  N   . SER   A 184 ? 0.39691 0.49027 0.46512 -0.00200 -0.05356 -0.03165 184 SER   A N   
1361 C  CA  . SER   A 184 ? 0.34762 0.44828 0.41325 -0.00062 -0.04948 -0.03079 184 SER   A CA  
1362 C  C   . SER   A 184 ? 0.41316 0.51745 0.48783 -0.00699 -0.05596 -0.02322 184 SER   A C   
1363 O  O   . SER   A 184 ? 0.39301 0.50775 0.47081 -0.00744 -0.05073 -0.01885 184 SER   A O   
1364 C  CB  . SER   A 184 ? 0.38436 0.47800 0.43594 0.00606  -0.05180 -0.03989 184 SER   A CB  
1365 O  OG  . SER   A 184 ? 0.43059 0.51009 0.47743 0.00656  -0.06475 -0.04461 184 SER   A OG  
1366 N  N   . GLN   A 185 ? 0.39390 0.49026 0.47358 -0.01222 -0.06761 -0.02082 185 GLN   A N   
1367 C  CA  . GLN   A 185 ? 0.39217 0.49370 0.48232 -0.01949 -0.07469 -0.01210 185 GLN   A CA  
1368 C  C   . GLN   A 185 ? 0.40690 0.52491 0.51101 -0.02424 -0.06799 -0.00132 185 GLN   A C   
1369 O  O   . GLN   A 185 ? 0.40432 0.53148 0.51843 -0.02971 -0.07186 0.00715  185 GLN   A O   
1370 C  CB  . GLN   A 185 ? 0.38067 0.46809 0.47210 -0.02461 -0.09059 -0.01184 185 GLN   A CB  
1371 C  CG  . GLN   A 185 ? 0.45500 0.52605 0.53127 -0.01853 -0.09819 -0.02291 185 GLN   A CG  
1372 C  CD  . GLN   A 185 ? 0.57847 0.63158 0.65345 -0.02230 -0.11522 -0.02424 185 GLN   A CD  
1373 O  OE1 . GLN   A 185 ? 0.54742 0.60117 0.63455 -0.03143 -0.12251 -0.01513 185 GLN   A OE1 
1374 N  NE2 . GLN   A 185 ? 0.66968 0.70666 0.72946 -0.01511 -0.12232 -0.03531 185 GLN   A NE2 
1375 N  N   . ILE   A 186 ? 0.38500 0.50754 0.48976 -0.02186 -0.05849 -0.00140 186 ILE   A N   
1376 C  CA  . ILE   A 186 ? 0.33929 0.47797 0.45380 -0.02338 -0.04991 0.00699  186 ILE   A CA  
1377 C  C   . ILE   A 186 ? 0.36256 0.50917 0.47195 -0.01713 -0.03866 0.00480  186 ILE   A C   
1378 O  O   . ILE   A 186 ? 0.33944 0.49940 0.45515 -0.01730 -0.03448 0.01126  186 ILE   A O   
1379 C  CB  . ILE   A 186 ? 0.41238 0.55029 0.53007 -0.02448 -0.04712 0.00848  186 ILE   A CB  
1380 C  CG1 . ILE   A 186 ? 0.34997 0.47891 0.47285 -0.03130 -0.05922 0.01156  186 ILE   A CG1 
1381 C  CG2 . ILE   A 186 ? 0.37718 0.53206 0.50202 -0.02363 -0.03658 0.01571  186 ILE   A CG2 
1382 C  CD1 . ILE   A 186 ? 0.40354 0.54016 0.53860 -0.03985 -0.06825 0.02232  186 ILE   A CD1 
1383 N  N   . LEU   A 187 ? 0.32041 0.45947 0.41834 -0.01139 -0.03394 -0.00386 187 LEU   A N   
1384 C  CA  . LEU   A 187 ? 0.31814 0.46344 0.41114 -0.00643 -0.02430 -0.00507 187 LEU   A CA  
1385 C  C   . LEU   A 187 ? 0.33163 0.48087 0.42369 -0.00600 -0.02626 -0.00360 187 LEU   A C   
1386 O  O   . LEU   A 187 ? 0.29936 0.45776 0.39304 -0.00391 -0.02050 -0.00000 187 LEU   A O   
1387 C  CB  . LEU   A 187 ? 0.32405 0.46151 0.40561 -0.00158 -0.02028 -0.01348 187 LEU   A CB  
1388 C  CG  . LEU   A 187 ? 0.45986 0.59652 0.53977 0.00049  -0.01371 -0.01555 187 LEU   A CG  
1389 C  CD1 . LEU   A 187 ? 0.57592 0.72079 0.65685 0.00234  -0.00548 -0.01190 187 LEU   A CD1 
1390 C  CD2 . LEU   A 187 ? 0.42033 0.55491 0.50756 -0.00315 -0.01756 -0.01293 187 LEU   A CD2 
1391 N  N   . TYR   A 188 ? 0.35252 0.49386 0.44047 -0.00701 -0.03452 -0.00709 188 TYR   A N   
1392 C  CA  . TYR   A 188 ? 0.31712 0.46080 0.40295 -0.00648 -0.03732 -0.00641 188 TYR   A CA  
1393 C  C   . TYR   A 188 ? 0.28836 0.44537 0.38599 -0.00960 -0.03754 0.00288  188 TYR   A C   
1394 O  O   . TYR   A 188 ? 0.29326 0.45759 0.38969 -0.00636 -0.03225 0.00455  188 TYR   A O   
1395 C  CB  . TYR   A 188 ? 0.29288 0.42497 0.37334 -0.00764 -0.04819 -0.01115 188 TYR   A CB  
1396 C  CG  . TYR   A 188 ? 0.32308 0.45447 0.39807 -0.00621 -0.05184 -0.01257 188 TYR   A CG  
1397 C  CD1 . TYR   A 188 ? 0.32208 0.46272 0.40596 -0.00959 -0.05464 -0.00528 188 TYR   A CD1 
1398 C  CD2 . TYR   A 188 ? 0.36967 0.49213 0.43055 -0.00122 -0.05292 -0.02093 188 TYR   A CD2 
1399 C  CE1 . TYR   A 188 ? 0.35119 0.49063 0.43003 -0.00838 -0.05871 -0.00656 188 TYR   A CE1 
1400 C  CE2 . TYR   A 188 ? 0.35511 0.47661 0.41025 0.00010  -0.05695 -0.02208 188 TYR   A CE2 
1401 C  CZ  . TYR   A 188 ? 0.39112 0.52037 0.45548 -0.00377 -0.06008 -0.01494 188 TYR   A CZ  
1402 O  OH  . TYR   A 188 ? 0.39352 0.52155 0.45244 -0.00258 -0.06453 -0.01596 188 TYR   A OH  
1403 N  N   . PRO   A 189 ? 0.32087 0.48223 0.43000 -0.01567 -0.04386 0.00958  189 PRO   A N   
1404 C  CA  . PRO   A 189 ? 0.33146 0.50956 0.45242 -0.01782 -0.04292 0.01931  189 PRO   A CA  
1405 C  C   . PRO   A 189 ? 0.34580 0.53562 0.46881 -0.01321 -0.03164 0.02232  189 PRO   A C   
1406 O  O   . PRO   A 189 ? 0.32543 0.52700 0.45159 -0.01043 -0.02843 0.02651  189 PRO   A O   
1407 C  CB  . PRO   A 189 ? 0.32787 0.50853 0.46088 -0.02621 -0.05240 0.02666  189 PRO   A CB  
1408 C  CG  . PRO   A 189 ? 0.33125 0.49603 0.45872 -0.02757 -0.05618 0.02074  189 PRO   A CG  
1409 C  CD  . PRO   A 189 ? 0.33376 0.48544 0.44553 -0.02091 -0.05343 0.00924  189 PRO   A CD  
1410 N  N   . CYS   A 190 ? 0.29622 0.48262 0.41656 -0.01147 -0.02589 0.01987  190 CYS   A N   
1411 C  CA  . CYS   A 190 ? 0.30587 0.50162 0.42622 -0.00621 -0.01612 0.02198  190 CYS   A CA  
1412 C  C   . CYS   A 190 ? 0.27107 0.46452 0.38205 -0.00024 -0.01180 0.01771  190 CYS   A C   
1413 O  O   . CYS   A 190 ? 0.30707 0.51014 0.41916 0.00431  -0.00705 0.02101  190 CYS   A O   
1414 C  CB  . CYS   A 190 ? 0.29209 0.48237 0.40927 -0.00501 -0.01113 0.01900  190 CYS   A CB  
1415 S  SG  . CYS   A 190 ? 0.35948 0.55416 0.48839 -0.01196 -0.01571 0.02583  190 CYS   A SG  
1416 N  N   . MET   A 191 ? 0.26703 0.44758 0.36788 0.00033  -0.01357 0.01032  191 MET   A N   
1417 C  CA  . MET   A 191 ? 0.29473 0.47198 0.38579 0.00516  -0.00978 0.00662  191 MET   A CA  
1418 C  C   . MET   A 191 ? 0.30298 0.48640 0.39635 0.00557  -0.01335 0.00991  191 MET   A C   
1419 O  O   . MET   A 191 ? 0.26922 0.45625 0.35935 0.01016  -0.00958 0.01089  191 MET   A O   
1420 C  CB  . MET   A 191 ? 0.26417 0.42882 0.34408 0.00564  -0.01043 -0.00114 191 MET   A CB  
1421 C  CG  . MET   A 191 ? 0.30784 0.46779 0.38441 0.00664  -0.00546 -0.00443 191 MET   A CG  
1422 S  SD  . MET   A 191 ? 0.34164 0.49050 0.40747 0.00722  -0.00730 -0.01273 191 MET   A SD  
1423 C  CE  . MET   A 191 ? 0.30952 0.45817 0.36549 0.01048  -0.00399 -0.01395 191 MET   A CE  
1424 N  N   . GLN   A 192 ? 0.29134 0.47488 0.38966 0.00098  -0.02140 0.01147  192 GLN   A N   
1425 C  CA  . GLN   A 192 ? 0.30290 0.49306 0.40401 0.00127  -0.02506 0.01494  192 GLN   A CA  
1426 C  C   . GLN   A 192 ? 0.35165 0.55848 0.46285 0.00326  -0.02155 0.02281  192 GLN   A C   
1427 O  O   . GLN   A 192 ? 0.35094 0.56404 0.46116 0.00760  -0.01998 0.02461  192 GLN   A O   
1428 C  CB  . GLN   A 192 ? 0.28209 0.46858 0.38687 -0.00455 -0.03567 0.01547  192 GLN   A CB  
1429 C  CG  . GLN   A 192 ? 0.32203 0.51671 0.43129 -0.00494 -0.04046 0.01998  192 GLN   A CG  
1430 C  CD  . GLN   A 192 ? 0.35303 0.53851 0.46015 -0.00933 -0.05158 0.01761  192 GLN   A CD  
1431 O  OE1 . GLN   A 192 ? 0.31519 0.48666 0.41414 -0.01014 -0.05515 0.01098  192 GLN   A OE1 
1432 N  NE2 . GLN   A 192 ? 0.31874 0.51198 0.43244 -0.01137 -0.05730 0.02270  192 GLN   A NE2 
1433 N  N   . CYS   A 193 ? 0.33169 0.54633 0.45191 0.00101  -0.02001 0.02754  193 CYS   A N   
1434 C  CA  . CYS   A 193 ? 0.27727 0.51014 0.40646 0.00416  -0.01596 0.03521  193 CYS   A CA  
1435 C  C   . CYS   A 193 ? 0.36331 0.59488 0.48329 0.01303  -0.00787 0.03185  193 CYS   A C   
1436 O  O   . CYS   A 193 ? 0.31587 0.55687 0.43643 0.01877  -0.00601 0.03458  193 CYS   A O   
1437 C  CB  . CYS   A 193 ? 0.27220 0.51321 0.41151 -0.00014 -0.01579 0.04095  193 CYS   A CB  
1438 S  SG  . CYS   A 193 ? 0.32773 0.59616 0.48001 0.00335  -0.01138 0.05228  193 CYS   A SG  
1439 N  N   . ALA   A 194 ? 0.30607 0.52431 0.41644 0.01433  -0.00408 0.02543  194 ALA   A N   
1440 C  CA  . ALA   A 194 ? 0.33653 0.55083 0.43751 0.02174  0.00207  0.02233  194 ALA   A CA  
1441 C  C   . ALA   A 194 ? 0.34049 0.55096 0.43423 0.02541  0.00073  0.02037  194 ALA   A C   
1442 O  O   . ALA   A 194 ? 0.30689 0.52010 0.39670 0.03251  0.00368  0.02105  194 ALA   A O   
1443 C  CB  . ALA   A 194 ? 0.31274 0.51277 0.40499 0.02096  0.00506  0.01610  194 ALA   A CB  
1444 N  N   . ASP   A 195 ? 0.32811 0.53136 0.41895 0.02120  -0.00425 0.01768  195 ASP   A N   
1445 C  CA  . ASP   A 195 ? 0.34996 0.54877 0.43309 0.02418  -0.00582 0.01592  195 ASP   A CA  
1446 C  C   . ASP   A 195 ? 0.33772 0.54950 0.42640 0.02909  -0.00631 0.02119  195 ASP   A C   
1447 O  O   . ASP   A 195 ? 0.29238 0.50139 0.37376 0.03517  -0.00489 0.02023  195 ASP   A O   
1448 C  CB  . ASP   A 195 ? 0.29455 0.48727 0.37563 0.01919  -0.01188 0.01346  195 ASP   A CB  
1449 C  CG  . ASP   A 195 ? 0.33776 0.51784 0.41083 0.01632  -0.01138 0.00733  195 ASP   A CG  
1450 O  OD1 . ASP   A 195 ? 0.40270 0.57785 0.47076 0.01800  -0.00608 0.00494  195 ASP   A OD1 
1451 O  OD2 . ASP   A 195 ? 0.37962 0.55504 0.45120 0.01282  -0.01678 0.00487  195 ASP   A OD2 
1452 N  N   . ILE   A 196 ? 0.35944 0.58597 0.46124 0.02664  -0.00856 0.02724  196 ILE   A N   
1453 C  CA  . ILE   A 196 ? 0.29483 0.53745 0.40391 0.03110  -0.00940 0.03319  196 ILE   A CA  
1454 C  C   . ILE   A 196 ? 0.37586 0.62229 0.48022 0.04103  -0.00346 0.03321  196 ILE   A C   
1455 O  O   . ILE   A 196 ? 0.39651 0.64722 0.49829 0.04791  -0.00382 0.03412  196 ILE   A O   
1456 C  CB  . ILE   A 196 ? 0.33012 0.58976 0.45533 0.02562  -0.01242 0.04098  196 ILE   A CB  
1457 C  CG1 . ILE   A 196 ? 0.30941 0.56251 0.43777 0.01632  -0.02065 0.04056  196 ILE   A CG1 
1458 C  CG2 . ILE   A 196 ? 0.38045 0.66197 0.51533 0.03081  -0.01234 0.04863  196 ILE   A CG2 
1459 C  CD1 . ILE   A 196 ? 0.26109 0.52652 0.40429 0.00899  -0.02499 0.04808  196 ILE   A CD1 
1460 N  N   . PHE   A 197 ? 0.30985 0.55385 0.41221 0.04249  0.00143  0.03187  197 PHE   A N   
1461 C  CA  . PHE   A 197 ? 0.30649 0.55205 0.40278 0.05253  0.00627  0.03116  197 PHE   A CA  
1462 C  C   . PHE   A 197 ? 0.36244 0.58777 0.44319 0.05565  0.00664  0.02440  197 PHE   A C   
1463 O  O   . PHE   A 197 ? 0.37854 0.60133 0.45168 0.06444  0.00711  0.02330  197 PHE   A O   
1464 C  CB  . PHE   A 197 ? 0.36370 0.61573 0.46456 0.05256  0.01071  0.03309  197 PHE   A CB  
1465 C  CG  . PHE   A 197 ? 0.39146 0.66478 0.50803 0.04895  0.01000  0.04131  197 PHE   A CG  
1466 C  CD1 . PHE   A 197 ? 0.40775 0.70177 0.53117 0.05587  0.01115  0.04750  197 PHE   A CD1 
1467 C  CD2 . PHE   A 197 ? 0.35982 0.63270 0.48437 0.03845  0.00712  0.04330  197 PHE   A CD2 
1468 C  CE1 . PHE   A 197 ? 0.42477 0.74059 0.56379 0.05157  0.01005  0.05657  197 PHE   A CE1 
1469 C  CE2 . PHE   A 197 ? 0.40025 0.69230 0.53974 0.03385  0.00508  0.05209  197 PHE   A CE2 
1470 C  CZ  . PHE   A 197 ? 0.42278 0.73713 0.57003 0.03990  0.00671  0.05922  197 PHE   A CZ  
1471 N  N   . PHE   A 198 ? 0.35323 0.56434 0.42904 0.04859  0.00590  0.02020  198 PHE   A N   
1472 C  CA  . PHE   A 198 ? 0.43432 0.62765 0.49641 0.04988  0.00616  0.01511  198 PHE   A CA  
1473 C  C   . PHE   A 198 ? 0.42604 0.61507 0.48171 0.05303  0.00254  0.01484  198 PHE   A C   
1474 O  O   . PHE   A 198 ? 0.41241 0.59057 0.45734 0.05780  0.00211  0.01282  198 PHE   A O   
1475 C  CB  . PHE   A 198 ? 0.31249 0.49601 0.37248 0.04151  0.00601  0.01167  198 PHE   A CB  
1476 C  CG  . PHE   A 198 ? 0.37827 0.54642 0.42607 0.04119  0.00666  0.00779  198 PHE   A CG  
1477 C  CD1 . PHE   A 198 ? 0.40518 0.56683 0.44753 0.04465  0.00944  0.00653  198 PHE   A CD1 
1478 C  CD2 . PHE   A 198 ? 0.40949 0.57024 0.45154 0.03674  0.00433  0.00574  198 PHE   A CD2 
1479 C  CE1 . PHE   A 198 ? 0.38578 0.53373 0.41779 0.04324  0.00922  0.00411  198 PHE   A CE1 
1480 C  CE2 . PHE   A 198 ? 0.43732 0.58611 0.46902 0.03543  0.00505  0.00353  198 PHE   A CE2 
1481 C  CZ  . PHE   A 198 ? 0.40898 0.55134 0.43622 0.03815  0.00726  0.00308  198 PHE   A CZ  
1482 N  N   . LEU   A 199 ? 0.35247 0.54843 0.41401 0.04991  -0.00097 0.01692  199 LEU   A N   
1483 C  CA  . LEU   A 199 ? 0.38347 0.57646 0.43968 0.05274  -0.00480 0.01707  199 LEU   A CA  
1484 C  C   . LEU   A 199 ? 0.41066 0.61617 0.47095 0.06160  -0.00534 0.02070  199 LEU   A C   
1485 O  O   . LEU   A 199 ? 0.40732 0.61102 0.46339 0.06515  -0.00880 0.02101  199 LEU   A O   
1486 C  CB  . LEU   A 199 ? 0.36628 0.56069 0.42626 0.04571  -0.00905 0.01738  199 LEU   A CB  
1487 C  CG  . LEU   A 199 ? 0.42468 0.60675 0.47817 0.03899  -0.00888 0.01311  199 LEU   A CG  
1488 C  CD1 . LEU   A 199 ? 0.40209 0.58571 0.45906 0.03304  -0.01371 0.01281  199 LEU   A CD1 
1489 C  CD2 . LEU   A 199 ? 0.42651 0.59430 0.46590 0.04057  -0.00846 0.01038  199 LEU   A CD2 
1490 N  N   . ASN   A 200 ? 0.37914 0.59792 0.44705 0.06580  -0.00195 0.02355  200 ASN   A N   
1491 C  CA  . ASN   A 200 ? 0.38102 0.61517 0.45315 0.07570  -0.00170 0.02729  200 ASN   A CA  
1492 C  C   . ASN   A 200 ? 0.40884 0.65572 0.48996 0.07378  -0.00594 0.03154  200 ASN   A C   
1493 O  O   . ASN   A 200 ? 0.41562 0.66664 0.49447 0.08149  -0.00803 0.03251  200 ASN   A O   
1494 C  CB  . ASN   A 200 ? 0.41268 0.63491 0.47089 0.08617  -0.00225 0.02378  200 ASN   A CB  
1495 C  CG  . ASN   A 200 ? 0.60511 0.84321 0.66599 0.09886  -0.00084 0.02650  200 ASN   A CG  
1496 O  OD1 . ASN   A 200 ? 0.62113 0.87957 0.69369 0.09997  0.00255  0.03110  200 ASN   A OD1 
1497 N  ND2 . ASN   A 200 ? 0.65290 0.88218 0.70252 0.10896  -0.00367 0.02393  200 ASN   A ND2 
1498 N  N   . VAL   A 201 ? 0.33989 0.59271 0.43125 0.06368  -0.00790 0.03414  201 VAL   A N   
1499 C  CA  . VAL   A 201 ? 0.33609 0.59887 0.43598 0.06001  -0.01332 0.03812  201 VAL   A CA  
1500 C  C   . VAL   A 201 ? 0.37308 0.66149 0.48598 0.06563  -0.01259 0.04560  201 VAL   A C   
1501 O  O   . VAL   A 201 ? 0.35762 0.65932 0.47801 0.06702  -0.00842 0.04931  201 VAL   A O   
1502 C  CB  . VAL   A 201 ? 0.36359 0.62327 0.46963 0.04787  -0.01664 0.03840  201 VAL   A CB  
1503 C  CG1 . VAL   A 201 ? 0.44942 0.71918 0.56517 0.04317  -0.02315 0.04296  201 VAL   A CG1 
1504 C  CG2 . VAL   A 201 ? 0.37861 0.61518 0.47107 0.04375  -0.01684 0.03091  201 VAL   A CG2 
1505 N  N   . ASP   A 202 ? 0.33939 0.63595 0.45486 0.06929  -0.01648 0.04819  202 ASP   A N   
1506 C  CA  . ASP   A 202 ? 0.33843 0.66261 0.46880 0.07283  -0.01710 0.05659  202 ASP   A CA  
1507 C  C   . ASP   A 202 ? 0.32190 0.65639 0.46675 0.06102  -0.02282 0.06261  202 ASP   A C   
1508 O  O   . ASP   A 202 ? 0.33287 0.69106 0.49341 0.05908  -0.02254 0.07121  202 ASP   A O   
1509 C  CB  . ASP   A 202 ? 0.28064 0.60909 0.40649 0.08381  -0.01894 0.05643  202 ASP   A CB  
1510 C  CG  . ASP   A 202 ? 0.41183 0.73406 0.52517 0.09726  -0.01434 0.05196  202 ASP   A CG  
1511 O  OD1 . ASP   A 202 ? 0.40032 0.73729 0.51827 0.10321  -0.00914 0.05475  202 ASP   A OD1 
1512 O  OD2 . ASP   A 202 ? 0.39303 0.69427 0.49120 0.10128  -0.01625 0.04567  202 ASP   A OD2 
1513 N  N   . ILE   A 203 ? 0.25681 0.57417 0.39630 0.05329  -0.02855 0.05862  203 ILE   A N   
1514 C  CA  . ILE   A 203 ? 0.33680 0.65940 0.48727 0.04257  -0.03612 0.06308  203 ILE   A CA  
1515 C  C   . ILE   A 203 ? 0.34454 0.64481 0.48720 0.03346  -0.03886 0.05685  203 ILE   A C   
1516 O  O   . ILE   A 203 ? 0.36054 0.64102 0.48853 0.03464  -0.03928 0.04938  203 ILE   A O   
1517 C  CB  . ILE   A 203 ? 0.31075 0.63727 0.46219 0.04434  -0.04235 0.06469  203 ILE   A CB  
1518 C  CG1 . ILE   A 203 ? 0.33821 0.68941 0.49818 0.05452  -0.03992 0.07115  203 ILE   A CG1 
1519 C  CG2 . ILE   A 203 ? 0.31325 0.64110 0.47405 0.03265  -0.05152 0.06833  203 ILE   A CG2 
1520 C  CD1 . ILE   A 203 ? 0.40559 0.75818 0.56370 0.05851  -0.04559 0.07141  203 ILE   A CD1 
1521 N  N   . CYS   A 204 ? 0.35606 0.65993 0.50809 0.02483  -0.04083 0.06018  204 CYS   A N   
1522 C  CA  . CYS   A 204 ? 0.37652 0.66133 0.52298 0.01608  -0.04575 0.05499  204 CYS   A CA  
1523 C  C   . CYS   A 204 ? 0.34877 0.63306 0.49939 0.00995  -0.05617 0.05701  204 CYS   A C   
1524 O  O   . CYS   A 204 ? 0.32344 0.62385 0.48947 0.00452  -0.06171 0.06558  204 CYS   A O   
1525 C  CB  . CYS   A 204 ? 0.28691 0.57455 0.44154 0.00945  -0.04539 0.05793  204 CYS   A CB  
1526 S  SG  . CYS   A 204 ? 0.33507 0.62509 0.48559 0.01693  -0.03336 0.05626  204 CYS   A SG  
1527 N  N   . GLN   A 205 ? 0.33720 0.60390 0.47436 0.01060  -0.05926 0.04983  205 GLN   A N   
1528 C  CA  . GLN   A 205 ? 0.31969 0.58431 0.45849 0.00600  -0.06951 0.05086  205 GLN   A CA  
1529 C  C   . GLN   A 205 ? 0.38406 0.62733 0.51262 0.00025  -0.07499 0.04356  205 GLN   A C   
1530 O  O   . GLN   A 205 ? 0.37689 0.60472 0.49015 0.00312  -0.07470 0.03609  205 GLN   A O   
1531 C  CB  . GLN   A 205 ? 0.33141 0.59579 0.46280 0.01306  -0.06889 0.04926  205 GLN   A CB  
1532 C  CG  . GLN   A 205 ? 0.34483 0.61553 0.48274 0.00974  -0.07906 0.05346  205 GLN   A CG  
1533 C  CD  . GLN   A 205 ? 0.36388 0.61679 0.49457 0.00262  -0.08812 0.04844  205 GLN   A CD  
1534 O  OE1 . GLN   A 205 ? 0.33482 0.57122 0.44949 0.00524  -0.08850 0.04097  205 GLN   A OE1 
1535 N  NE2 . GLN   A 205 ? 0.30723 0.56265 0.44854 -0.00606 -0.09567 0.05240  205 GLN   A NE2 
1536 N  N   . LEU   A 206 ? 0.30488 0.54788 0.44153 -0.00733 -0.07989 0.04597  206 LEU   A N   
1537 C  CA  . LEU   A 206 ? 0.39202 0.61568 0.52001 -0.01208 -0.08610 0.03932  206 LEU   A CA  
1538 C  C   . LEU   A 206 ? 0.38754 0.61224 0.52563 -0.02093 -0.09958 0.04430  206 LEU   A C   
1539 O  O   . LEU   A 206 ? 0.38510 0.62767 0.53893 -0.02455 -0.10336 0.05410  206 LEU   A O   
1540 C  CB  . LEU   A 206 ? 0.29493 0.51309 0.42106 -0.01249 -0.07972 0.03643  206 LEU   A CB  
1541 C  CG  . LEU   A 206 ? 0.39480 0.61154 0.51159 -0.00453 -0.06715 0.03213  206 LEU   A CG  
1542 C  CD1 . LEU   A 206 ? 0.35586 0.59089 0.48378 -0.00156 -0.05923 0.03913  206 LEU   A CD1 
1543 C  CD2 . LEU   A 206 ? 0.35243 0.55289 0.45786 -0.00433 -0.06374 0.02398  206 LEU   A CD2 
1544 N  N   . GLY   A 207 ? 0.35727 0.56296 0.48635 -0.02439 -0.10757 0.03782  207 GLY   A N   
1545 C  CA  . GLY   A 207 ? 0.38196 0.58491 0.51941 -0.03329 -0.12215 0.04210  207 GLY   A CA  
1546 C  C   . GLY   A 207 ? 0.44293 0.65840 0.59797 -0.04070 -0.12363 0.05176  207 GLY   A C   
1547 O  O   . GLY   A 207 ? 0.36972 0.58857 0.52610 -0.03897 -0.11447 0.05179  207 GLY   A O   
1548 N  N   . ILE   A 208 ? 0.35762 0.57938 0.52611 -0.04975 -0.13633 0.06043  208 ILE   A N   
1549 C  CA  . ILE   A 208 ? 0.37702 0.61184 0.56308 -0.05816 -0.13904 0.07131  208 ILE   A CA  
1550 C  C   . ILE   A 208 ? 0.43440 0.65174 0.61409 -0.06064 -0.14042 0.06601  208 ILE   A C   
1551 O  O   . ILE   A 208 ? 0.36738 0.59536 0.55844 -0.06491 -0.13747 0.07334  208 ILE   A O   
1552 C  CB  . ILE   A 208 ? 0.45717 0.70058 0.65879 -0.06891 -0.15435 0.08229  208 ILE   A CB  
1553 C  CG1 . ILE   A 208 ? 0.46418 0.72797 0.68617 -0.07725 -0.15466 0.09621  208 ILE   A CG1 
1554 C  CG2 . ILE   A 208 ? 0.50760 0.72475 0.70026 -0.07478 -0.17112 0.07647  208 ILE   A CG2 
1555 C  CD1 . ILE   A 208 ? 0.57882 0.87541 0.81513 -0.07344 -0.14373 0.10640  208 ILE   A CD1 
1556 N  N   . ASP   A 209 ? 0.48607 0.67789 0.64718 -0.05700 -0.14392 0.05330  209 ASP   A N   
1557 C  CA  . ASP   A 209 ? 0.47610 0.65298 0.63129 -0.05794 -0.14420 0.04814  209 ASP   A CA  
1558 C  C   . ASP   A 209 ? 0.40106 0.58536 0.55428 -0.05153 -0.12748 0.04608  209 ASP   A C   
1559 O  O   . ASP   A 209 ? 0.39226 0.56809 0.54368 -0.05290 -0.12691 0.04378  209 ASP   A O   
1560 C  CB  . ASP   A 209 ? 0.48635 0.63531 0.62174 -0.05443 -0.15232 0.03488  209 ASP   A CB  
1561 C  CG  . ASP   A 209 ? 0.48813 0.63144 0.60574 -0.04318 -0.14180 0.02393  209 ASP   A CG  
1562 O  OD1 . ASP   A 209 ? 0.45606 0.61405 0.57573 -0.03871 -0.13111 0.02633  209 ASP   A OD1 
1563 O  OD2 . ASP   A 209 ? 0.46712 0.59070 0.56797 -0.03865 -0.14521 0.01294  209 ASP   A OD2 
1564 N  N   . GLN   A 210 ? 0.34937 0.54850 0.50304 -0.04479 -0.11491 0.04714  210 GLN   A N   
1565 C  CA  . GLN   A 210 ? 0.36100 0.56713 0.51342 -0.03907 -0.10021 0.04601  210 GLN   A CA  
1566 C  C   . GLN   A 210 ? 0.36712 0.59704 0.53768 -0.04241 -0.09575 0.05841  210 GLN   A C   
1567 O  O   . GLN   A 210 ? 0.36815 0.60528 0.53864 -0.03770 -0.08426 0.05847  210 GLN   A O   
1568 C  CB  . GLN   A 210 ? 0.32237 0.52898 0.46323 -0.02922 -0.08964 0.03976  210 GLN   A CB  
1569 C  CG  . GLN   A 210 ? 0.35211 0.53949 0.47556 -0.02567 -0.09367 0.02915  210 GLN   A CG  
1570 C  CD  . GLN   A 210 ? 0.38070 0.55039 0.49232 -0.02426 -0.09312 0.02015  210 GLN   A CD  
1571 O  OE1 . GLN   A 210 ? 0.40060 0.57110 0.50902 -0.02045 -0.08281 0.01768  210 GLN   A OE1 
1572 N  NE2 . GLN   A 210 ? 0.41864 0.57251 0.52410 -0.02717 -0.10495 0.01545  210 GLN   A NE2 
1573 N  N   . ARG   A 211 ? 0.35396 0.59663 0.53999 -0.05060 -0.10517 0.06931  211 ARG   A N   
1574 C  CA  . ARG   A 211 ? 0.37529 0.64580 0.57888 -0.05245 -0.10016 0.08222  211 ARG   A CA  
1575 C  C   . ARG   A 211 ? 0.42058 0.69598 0.62773 -0.05271 -0.09254 0.08479  211 ARG   A C   
1576 O  O   . ARG   A 211 ? 0.37906 0.67390 0.59162 -0.04729 -0.08151 0.08956  211 ARG   A O   
1577 C  CB  . ARG   A 211 ? 0.31669 0.59787 0.53648 -0.06343 -0.11379 0.09396  211 ARG   A CB  
1578 C  CG  . ARG   A 211 ? 0.50051 0.81465 0.74013 -0.06581 -0.10985 0.10909  211 ARG   A CG  
1579 C  CD  . ARG   A 211 ? 0.49745 0.81929 0.75306 -0.07894 -0.12526 0.12108  211 ARG   A CD  
1580 N  NE  . ARG   A 211 ? 0.53198 0.88899 0.80689 -0.08035 -0.12228 0.13602  211 ARG   A NE  
1581 C  CZ  . ARG   A 211 ? 0.50011 0.88043 0.78962 -0.08399 -0.11798 0.14823  211 ARG   A CZ  
1582 N  NH1 . ARG   A 211 ? 0.44443 0.81616 0.73153 -0.08666 -0.11564 0.14733  211 ARG   A NH1 
1583 N  NH2 . ARG   A 211 ? 0.56875 0.98314 0.87591 -0.08478 -0.11611 0.16216  211 ARG   A NH2 
1584 N  N   . LYS   A 212 ? 0.33337 0.59077 0.53654 -0.05812 -0.09853 0.08126  212 LYS   A N   
1585 C  CA  . LYS   A 212 ? 0.38112 0.64355 0.58907 -0.05974 -0.09304 0.08503  212 LYS   A CA  
1586 C  C   . LYS   A 212 ? 0.40969 0.67535 0.60876 -0.04862 -0.07710 0.07884  212 LYS   A C   
1587 O  O   . LYS   A 212 ? 0.35099 0.63536 0.55790 -0.04645 -0.06865 0.08574  212 LYS   A O   
1588 C  CB  . LYS   A 212 ? 0.41610 0.65452 0.61806 -0.06578 -0.10274 0.07991  212 LYS   A CB  
1589 C  CG  . LYS   A 212 ? 0.42002 0.65903 0.63512 -0.07894 -0.11904 0.09034  212 LYS   A CG  
1590 C  CD  . LYS   A 212 ? 0.59030 0.85466 0.82326 -0.08460 -0.11517 0.10534  212 LYS   A CD  
1591 C  CE  . LYS   A 212 ? 0.71206 0.98135 0.96072 -0.09904 -0.13071 0.11877  212 LYS   A CE  
1592 N  NZ  . LYS   A 212 ? 0.68401 0.92595 0.92532 -0.10455 -0.14110 0.11352  212 LYS   A NZ  
1593 N  N   . VAL   A 213 ? 0.32228 0.57079 0.50479 -0.04124 -0.07310 0.06633  213 VAL   A N   
1594 C  CA  . VAL   A 213 ? 0.29847 0.54838 0.47287 -0.03203 -0.05953 0.06118  213 VAL   A CA  
1595 C  C   . VAL   A 213 ? 0.34594 0.61521 0.52411 -0.02514 -0.05207 0.06557  213 VAL   A C   
1596 O  O   . VAL   A 213 ? 0.29944 0.57779 0.47670 -0.01855 -0.04197 0.06618  213 VAL   A O   
1597 C  CB  . VAL   A 213 ? 0.29398 0.52142 0.45037 -0.02690 -0.05732 0.04782  213 VAL   A CB  
1598 C  CG1 . VAL   A 213 ? 0.33891 0.56346 0.48776 -0.02252 -0.05806 0.04365  213 VAL   A CG1 
1599 C  CG2 . VAL   A 213 ? 0.29860 0.52406 0.44762 -0.02023 -0.04549 0.04311  213 VAL   A CG2 
1600 N  N   . ASN   A 214 ? 0.33692 0.61254 0.51897 -0.02598 -0.05753 0.06858  214 ASN   A N   
1601 C  CA  . ASN   A 214 ? 0.36135 0.65744 0.54848 -0.01913 -0.05135 0.07376  214 ASN   A CA  
1602 C  C   . ASN   A 214 ? 0.32332 0.64562 0.52686 -0.02100 -0.04866 0.08625  214 ASN   A C   
1603 O  O   . ASN   A 214 ? 0.29796 0.63542 0.50208 -0.01227 -0.03922 0.08838  214 ASN   A O   
1604 C  CB  . ASN   A 214 ? 0.37935 0.67775 0.56829 -0.02011 -0.05853 0.07506  214 ASN   A CB  
1605 C  CG  . ASN   A 214 ? 0.33990 0.61772 0.51178 -0.01526 -0.05834 0.06363  214 ASN   A CG  
1606 O  OD1 . ASN   A 214 ? 0.36522 0.63559 0.52550 -0.00768 -0.04974 0.05682  214 ASN   A OD1 
1607 N  ND2 . ASN   A 214 ? 0.38123 0.65100 0.55163 -0.01953 -0.06824 0.06226  214 ASN   A ND2 
1608 N  N   . MET   A 215 ? 0.28289 0.60999 0.49882 -0.03204 -0.05704 0.09452  215 MET   A N   
1609 C  CA  . MET   A 215 ? 0.36217 0.71571 0.59375 -0.03439 -0.05403 0.10746  215 MET   A CA  
1610 C  C   . MET   A 215 ? 0.35640 0.70810 0.58223 -0.02936 -0.04409 0.10446  215 MET   A C   
1611 O  O   . MET   A 215 ? 0.31545 0.68945 0.54739 -0.02383 -0.03593 0.11117  215 MET   A O   
1612 C  CB  . MET   A 215 ? 0.31023 0.66834 0.55655 -0.04872 -0.06654 0.11807  215 MET   A CB  
1613 C  CG  . MET   A 215 ? 0.33971 0.70337 0.59465 -0.05490 -0.07773 0.12358  215 MET   A CG  
1614 S  SD  . MET   A 215 ? 0.51960 0.92260 0.78987 -0.04950 -0.07235 0.13617  215 MET   A SD  
1615 C  CE  . MET   A 215 ? 0.45772 0.85415 0.71132 -0.03314 -0.06215 0.12358  215 MET   A CE  
1616 N  N   . LEU   A 216 ? 0.32846 0.65403 0.54148 -0.03001 -0.04441 0.09384  216 LEU   A N   
1617 C  CA  . LEU   A 216 ? 0.33898 0.66056 0.54595 -0.02575 -0.03587 0.09034  216 LEU   A CA  
1618 C  C   . LEU   A 216 ? 0.31526 0.64469 0.51472 -0.01271 -0.02426 0.08672  216 LEU   A C   
1619 O  O   . LEU   A 216 ? 0.36443 0.70670 0.56599 -0.00803 -0.01674 0.09044  216 LEU   A O   
1620 C  CB  . LEU   A 216 ? 0.29573 0.58810 0.48958 -0.02770 -0.03860 0.07876  216 LEU   A CB  
1621 C  CG  . LEU   A 216 ? 0.32132 0.60735 0.50996 -0.02549 -0.03190 0.07543  216 LEU   A CG  
1622 C  CD1 . LEU   A 216 ? 0.43722 0.72831 0.63741 -0.03531 -0.03795 0.08429  216 LEU   A CD1 
1623 C  CD2 . LEU   A 216 ? 0.40379 0.66340 0.57658 -0.02302 -0.03131 0.06203  216 LEU   A CD2 
1624 N  N   . ALA   A 217 ? 0.31529 0.63718 0.50565 -0.00653 -0.02347 0.07988  217 ALA   A N   
1625 C  CA  . ALA   A 217 ? 0.27392 0.59959 0.45553 0.00595  -0.01422 0.07584  217 ALA   A CA  
1626 C  C   . ALA   A 217 ? 0.29181 0.64724 0.48479 0.01113  -0.01029 0.08624  217 ALA   A C   
1627 O  O   . ALA   A 217 ? 0.30377 0.66737 0.49278 0.02066  -0.00212 0.08594  217 ALA   A O   
1628 C  CB  . ALA   A 217 ? 0.36487 0.67754 0.53580 0.01026  -0.01588 0.06818  217 ALA   A CB  
1629 N  N   . ARG   A 218 ? 0.28691 0.65925 0.49376 0.00542  -0.01643 0.09555  218 ARG   A N   
1630 C  CA  . ARG   A 218 ? 0.32089 0.72537 0.53982 0.01057  -0.01254 0.10653  218 ARG   A CA  
1631 C  C   . ARG   A 218 ? 0.36371 0.78252 0.58943 0.00933  -0.00779 0.11367  218 ARG   A C   
1632 O  O   . ARG   A 218 ? 0.33374 0.76994 0.55872 0.01995  0.00051  0.11619  218 ARG   A O   
1633 C  CB  . ARG   A 218 ? 0.25458 0.67580 0.48889 0.00293  -0.02088 0.11651  218 ARG   A CB  
1634 C  CG  . ARG   A 218 ? 0.27340 0.68626 0.50092 0.00755  -0.02384 0.11042  218 ARG   A CG  
1635 C  CD  . ARG   A 218 ? 0.28028 0.70868 0.52244 0.00030  -0.03289 0.11973  218 ARG   A CD  
1636 N  NE  . ARG   A 218 ? 0.30868 0.77381 0.56783 0.00214  -0.03048 0.13370  218 ARG   A NE  
1637 C  CZ  . ARG   A 218 ? 0.34233 0.82802 0.60285 0.01419  -0.02505 0.13605  218 ARG   A CZ  
1638 N  NH1 . ARG   A 218 ? 0.28747 0.75938 0.53315 0.02538  -0.02185 0.12549  218 ARG   A NH1 
1639 N  NH2 . ARG   A 218 ? 0.29805 0.81990 0.57537 0.01518  -0.02318 0.14987  218 ARG   A NH2 
1640 N  N   . GLU   A 219 ? 0.32204 0.73229 0.55296 -0.00289 -0.01334 0.11638  219 GLU   A N   
1641 C  CA  . GLU   A 219 ? 0.29603 0.71862 0.53303 -0.00489 -0.00942 0.12346  219 GLU   A CA  
1642 C  C   . GLU   A 219 ? 0.36308 0.77472 0.58503 0.00603  0.00026  0.11404  219 GLU   A C   
1643 O  O   . GLU   A 219 ? 0.36308 0.79238 0.58703 0.01218  0.00737  0.11910  219 GLU   A O   
1644 C  CB  . GLU   A 219 ? 0.39523 0.80577 0.63858 -0.01992 -0.01857 0.12679  219 GLU   A CB  
1645 C  CG  . GLU   A 219 ? 0.54199 0.96245 0.79012 -0.02225 -0.01463 0.13356  219 GLU   A CG  
1646 C  CD  . GLU   A 219 ? 0.59937 1.01773 0.85923 -0.03802 -0.02520 0.14236  219 GLU   A CD  
1647 O  OE1 . GLU   A 219 ? 0.77633 1.19344 1.04404 -0.04683 -0.03557 0.14639  219 GLU   A OE1 
1648 O  OE2 . GLU   A 219 ? 0.74025 1.15697 1.00087 -0.04155 -0.02390 0.14512  219 GLU   A OE2 
1649 N  N   . TYR   A 220 ? 0.32202 0.70538 0.52850 0.00893  0.00045  0.10062  220 TYR   A N   
1650 C  CA  . TYR   A 220 ? 0.32587 0.69760 0.51843 0.01807  0.00835  0.09214  220 TYR   A CA  
1651 C  C   . TYR   A 220 ? 0.36990 0.75771 0.55832 0.03262  0.01591  0.09266  220 TYR   A C   
1652 O  O   . TYR   A 220 ? 0.35597 0.74889 0.53969 0.04000  0.02253  0.09237  220 TYR   A O   
1653 C  CB  . TYR   A 220 ? 0.30163 0.64256 0.47963 0.01776  0.00656  0.07906  220 TYR   A CB  
1654 C  CG  . TYR   A 220 ? 0.33779 0.66489 0.50138 0.02613  0.01339  0.07031  220 TYR   A CG  
1655 C  CD1 . TYR   A 220 ? 0.40502 0.72569 0.56684 0.02356  0.01574  0.06926  220 TYR   A CD1 
1656 C  CD2 . TYR   A 220 ? 0.39256 0.71080 0.54373 0.03597  0.01643  0.06293  220 TYR   A CD2 
1657 C  CE1 . TYR   A 220 ? 0.38832 0.69580 0.53722 0.03060  0.02105  0.06144  220 TYR   A CE1 
1658 C  CE2 . TYR   A 220 ? 0.42136 0.72518 0.55913 0.04273  0.02129  0.05525  220 TYR   A CE2 
1659 C  CZ  . TYR   A 220 ? 0.42019 0.71908 0.55724 0.03982  0.02355  0.05459  220 TYR   A CZ  
1660 O  OH  . TYR   A 220 ? 0.38870 0.67361 0.51312 0.04592  0.02758  0.04750  220 TYR   A OH  
1661 N  N   . CYS   A 221 ? 0.28239 0.67938 0.47265 0.03738  0.01445  0.09385  221 CYS   A N   
1662 C  CA  . CYS   A 221 ? 0.35331 0.76694 0.53990 0.05228  0.02064  0.09470  221 CYS   A CA  
1663 C  C   . CYS   A 221 ? 0.36008 0.80508 0.55821 0.05493  0.02519  0.10636  221 CYS   A C   
1664 O  O   . CYS   A 221 ? 0.37652 0.82972 0.56748 0.06749  0.03217  0.10507  221 CYS   A O   
1665 C  CB  . CYS   A 221 ? 0.32409 0.74597 0.51379 0.05572  0.01723  0.09604  221 CYS   A CB  
1666 S  SG  . CYS   A 221 ? 0.37159 0.76001 0.54614 0.05536  0.01258  0.08300  221 CYS   A SG  
1667 N  N   . ASP   A 222 ? 0.32123 0.78442 0.53701 0.04323  0.02075  0.11829  222 ASP   A N   
1668 C  CA  . ASP   A 222 ? 0.34232 0.83867 0.57054 0.04470  0.02488  0.13133  222 ASP   A CA  
1669 C  C   . ASP   A 222 ? 0.37223 0.86226 0.59389 0.04595  0.03007  0.12939  222 ASP   A C   
1670 O  O   . ASP   A 222 ? 0.36252 0.86391 0.57800 0.05517  0.03649  0.13205  222 ASP   A O   
1671 C  CB  . ASP   A 222 ? 0.33604 0.84526 0.58185 0.02903  0.01723  0.14414  222 ASP   A CB  
1672 C  CG  . ASP   A 222 ? 0.44198 0.96227 0.69404 0.02915  0.01295  0.14828  222 ASP   A CG  
1673 O  OD1 . ASP   A 222 ? 0.40078 0.92277 0.64467 0.04250  0.01663  0.14214  222 ASP   A OD1 
1674 O  OD2 . ASP   A 222 ? 0.44681 0.97284 0.71167 0.01562  0.00513  0.15768  222 ASP   A OD2 
1675 N  N   . ILE   A 223 ? 0.32597 0.78744 0.54172 0.03678  0.02644  0.12231  223 ILE   A N   
1676 C  CA  . ILE   A 223 ? 0.37231 0.82554 0.58210 0.03672  0.03037  0.12017  223 ILE   A CA  
1677 C  C   . ILE   A 223 ? 0.47113 0.91739 0.66396 0.05303  0.03812  0.11064  223 ILE   A C   
1678 O  O   . ILE   A 223 ? 0.43351 0.88993 0.62353 0.05935  0.04394  0.11299  223 ILE   A O   
1679 C  CB  . ILE   A 223 ? 0.33123 0.75392 0.53745 0.02443  0.02415  0.11336  223 ILE   A CB  
1680 C  CG1 . ILE   A 223 ? 0.35236 0.78159 0.57481 0.00823  0.01562  0.12394  223 ILE   A CG1 
1681 C  CG2 . ILE   A 223 ? 0.37163 0.77733 0.56609 0.02749  0.02856  0.10597  223 ILE   A CG2 
1682 C  CD1 . ILE   A 223 ? 0.40501 0.80122 0.62137 -0.00152 0.00830  0.11480  223 ILE   A CD1 
1683 N  N   . LYS   A 224 ? 0.41795 0.84632 0.59879 0.05999  0.03757  0.10007  224 LYS   A N   
1684 C  CA  . LYS   A 224 ? 0.34872 0.76400 0.51189 0.07411  0.04248  0.08991  224 LYS   A CA  
1685 C  C   . LYS   A 224 ? 0.39435 0.83062 0.55489 0.09012  0.04669  0.09203  224 LYS   A C   
1686 O  O   . LYS   A 224 ? 0.43034 0.85425 0.57498 0.10301  0.04928  0.08321  224 LYS   A O   
1687 C  CB  . LYS   A 224 ? 0.34967 0.73281 0.50084 0.07209  0.03869  0.07789  224 LYS   A CB  
1688 C  CG  . LYS   A 224 ? 0.47969 0.84022 0.62953 0.05975  0.03562  0.07352  224 LYS   A CG  
1689 C  CD  . LYS   A 224 ? 0.51917 0.86985 0.65895 0.06444  0.04022  0.06887  224 LYS   A CD  
1690 C  CE  . LYS   A 224 ? 0.54694 0.87858 0.68637 0.05325  0.03761  0.06535  224 LYS   A CE  
1691 N  NZ  . LYS   A 224 ? 0.56724 0.88017 0.69266 0.05847  0.04061  0.05676  224 LYS   A NZ  
1692 N  N   . LYS   A 225 ? 0.36293 0.82952 0.53822 0.08978  0.04650  0.10321  225 LYS   A N   
1693 C  CA  . LYS   A 225 ? 0.44830 0.93083 0.61816 0.10454  0.04946  0.10463  225 LYS   A CA  
1694 C  C   . LYS   A 225 ? 0.48501 0.95522 0.64639 0.11398  0.04748  0.09529  225 LYS   A C   
1695 O  O   . LYS   A 225 ? 0.49988 0.97076 0.64877 0.12975  0.04985  0.09084  225 LYS   A O   
1696 C  CB  . LYS   A 225 ? 0.55159 1.03490 0.70715 0.11653  0.05521  0.10276  225 LYS   A CB  
1697 C  CG  . LYS   A 225 ? 0.55080 1.04790 0.71334 0.10828  0.05696  0.11314  225 LYS   A CG  
1698 C  CD  . LYS   A 225 ? 0.61066 1.12794 0.79064 0.09598  0.05330  0.12632  225 LYS   A CD  
1699 C  CE  . LYS   A 225 ? 0.72069 1.24491 0.91085 0.08223  0.05240  0.13631  225 LYS   A CE  
1700 N  NZ  . LYS   A 225 ? 0.67304 1.21121 0.88089 0.06779  0.04649  0.14826  225 LYS   A NZ  
1701 N  N   . ILE   A 226 ? 0.45033 0.89872 0.61216 0.10250  0.04137  0.09092  226 ILE   A N   
1702 C  CA  . ILE   A 226 ? 0.40971 0.84076 0.56138 0.10791  0.03794  0.08267  226 ILE   A CA  
1703 C  C   . ILE   A 226 ? 0.44224 0.89743 0.60718 0.10798  0.03542  0.09086  226 ILE   A C   
1704 O  O   . ILE   A 226 ? 0.40319 0.86653 0.58303 0.09415  0.03126  0.09819  226 ILE   A O   
1705 C  CB  . ILE   A 226 ? 0.43123 0.82957 0.57679 0.09599  0.03288  0.07463  226 ILE   A CB  
1706 C  CG1 . ILE   A 226 ? 0.44274 0.81854 0.57618 0.09549  0.03525  0.06707  226 ILE   A CG1 
1707 C  CG2 . ILE   A 226 ? 0.42843 0.81169 0.56467 0.10080  0.02899  0.06786  226 ILE   A CG2 
1708 C  CD1 . ILE   A 226 ? 0.40975 0.75956 0.54087 0.08201  0.03081  0.06150  226 ILE   A CD1 
1709 N  N   . LYS   A 227 ? 0.45627 0.92197 0.61540 0.12373  0.03716  0.08947  227 LYS   A N   
1710 C  CA  . LYS   A 227 ? 0.41997 0.91186 0.59149 0.12632  0.03536  0.09746  227 LYS   A CA  
1711 C  C   . LYS   A 227 ? 0.42554 0.89884 0.59479 0.12085  0.02846  0.09261  227 LYS   A C   
1712 O  O   . LYS   A 227 ? 0.42286 0.91420 0.60545 0.11673  0.02498  0.10000  227 LYS   A O   
1713 C  CB  . LYS   A 227 ? 0.46543 0.96563 0.62424 0.14413  0.03921  0.09613  227 LYS   A CB  
1714 C  CG  . LYS   A 227 ? 0.54984 1.06138 0.70474 0.14692  0.04488  0.10107  227 LYS   A CG  
1715 C  CD  . LYS   A 227 ? 0.60160 1.13491 0.77410 0.13222  0.04449  0.11495  227 LYS   A CD  
1716 C  CE  . LYS   A 227 ? 0.54752 1.09316 0.71635 0.13435  0.04984  0.12101  227 LYS   A CE  
1717 N  NZ  . LYS   A 227 ? 0.66629 1.19634 0.83186 0.12914  0.05148  0.11695  227 LYS   A NZ  
1718 N  N   . LYS   A 228 ? 0.40665 0.84549 0.55915 0.12121  0.02627  0.08087  228 LYS   A N   
1719 C  CA  . LYS   A 228 ? 0.49758 0.91731 0.64671 0.11515  0.01985  0.07625  228 LYS   A CA  
1720 C  C   . LYS   A 228 ? 0.46890 0.88144 0.62804 0.09622  0.01567  0.07904  228 LYS   A C   
1721 O  O   . LYS   A 228 ? 0.49015 0.88140 0.64290 0.08890  0.01580  0.07373  228 LYS   A O   
1722 C  CB  . LYS   A 228 ? 0.44591 0.83307 0.57403 0.12147  0.01888  0.06410  228 LYS   A CB  
1723 C  CG  . LYS   A 228 ? 0.46866 0.83955 0.59296 0.11688  0.01247  0.06039  228 LYS   A CG  
1724 C  CD  . LYS   A 228 ? 0.46947 0.80955 0.57417 0.12164  0.01056  0.05014  228 LYS   A CD  
1725 C  CE  . LYS   A 228 ? 0.52330 0.84954 0.62591 0.11477  0.00430  0.04797  228 LYS   A CE  
1726 N  NZ  . LYS   A 228 ? 0.64425 0.94021 0.72833 0.11703  0.00219  0.03922  228 LYS   A NZ  
1727 N  N   . LYS   A 229 ? 0.37392 0.80439 0.54874 0.08854  0.01140  0.08751  229 LYS   A N   
1728 C  CA  . LYS   A 229 ? 0.39085 0.81571 0.57563 0.07113  0.00595  0.09091  229 LYS   A CA  
1729 C  C   . LYS   A 229 ? 0.32760 0.73963 0.51121 0.06547  -0.00154 0.08799  229 LYS   A C   
1730 O  O   . LYS   A 229 ? 0.32598 0.74896 0.51128 0.07234  -0.00312 0.08984  229 LYS   A O   
1731 C  CB  . LYS   A 229 ? 0.32160 0.77748 0.52727 0.06377  0.00514  0.10487  229 LYS   A CB  
1732 C  CG  . LYS   A 229 ? 0.42910 0.89765 0.63791 0.06538  0.01151  0.10934  229 LYS   A CG  
1733 C  CD  . LYS   A 229 ? 0.43400 0.93842 0.66369 0.06023  0.01111  0.12491  229 LYS   A CD  
1734 C  CE  . LYS   A 229 ? 0.47235 0.97292 0.71486 0.04138  0.00238  0.13110  229 LYS   A CE  
1735 N  NZ  . LYS   A 229 ? 0.50134 1.03051 0.76037 0.03479  0.00258  0.14617  229 LYS   A NZ  
1736 N  N   . PRO   A 230 ? 0.34738 0.73710 0.52775 0.05376  -0.00632 0.08346  230 PRO   A N   
1737 C  CA  . PRO   A 230 ? 0.31901 0.69509 0.49649 0.04852  -0.01362 0.08006  230 PRO   A CA  
1738 C  C   . PRO   A 230 ? 0.30232 0.69739 0.49718 0.04005  -0.02070 0.09000  230 PRO   A C   
1739 O  O   . PRO   A 230 ? 0.31896 0.72749 0.52740 0.03149  -0.02251 0.09825  230 PRO   A O   
1740 C  CB  . PRO   A 230 ? 0.32729 0.67553 0.49533 0.03981  -0.01557 0.07219  230 PRO   A CB  
1741 C  CG  . PRO   A 230 ? 0.36499 0.71982 0.54030 0.03478  -0.01292 0.07628  230 PRO   A CG  
1742 C  CD  . PRO   A 230 ? 0.33550 0.71023 0.51270 0.04623  -0.00501 0.08025  230 PRO   A CD  
1743 N  N   . VAL   A 231 ? 0.26650 0.66208 0.46082 0.04205  -0.02544 0.08962  231 VAL   A N   
1744 C  CA  . VAL   A 231 ? 0.33061 0.73932 0.53972 0.03286  -0.03406 0.09785  231 VAL   A CA  
1745 C  C   . VAL   A 231 ? 0.32596 0.70966 0.53002 0.02102  -0.04197 0.09255  231 VAL   A C   
1746 O  O   . VAL   A 231 ? 0.32030 0.67922 0.50809 0.02324  -0.04170 0.08212  231 VAL   A O   
1747 C  CB  . VAL   A 231 ? 0.30969 0.72957 0.51975 0.04091  -0.03596 0.09937  231 VAL   A CB  
1748 C  CG1 . VAL   A 231 ? 0.35971 0.78890 0.58328 0.03068  -0.04639 0.10668  231 VAL   A CG1 
1749 C  CG2 . VAL   A 231 ? 0.42556 0.87268 0.64141 0.05330  -0.02845 0.10512  231 VAL   A CG2 
1750 N  N   . ILE   A 232 ? 0.31824 0.70798 0.53546 0.00867  -0.04936 0.09977  232 ILE   A N   
1751 C  CA  . ILE   A 232 ? 0.38454 0.75079 0.59684 -0.00185 -0.05861 0.09481  232 ILE   A CA  
1752 C  C   . ILE   A 232 ? 0.41424 0.78468 0.63224 -0.00562 -0.06839 0.09825  232 ILE   A C   
1753 O  O   . ILE   A 232 ? 0.38044 0.77138 0.61586 -0.01229 -0.07444 0.10959  232 ILE   A O   
1754 C  CB  . ILE   A 232 ? 0.35616 0.72178 0.57760 -0.01339 -0.06318 0.09983  232 ILE   A CB  
1755 C  CG1 . ILE   A 232 ? 0.30327 0.67373 0.52441 -0.01012 -0.05346 0.10040  232 ILE   A CG1 
1756 C  CG2 . ILE   A 232 ? 0.34408 0.68186 0.55602 -0.02093 -0.07201 0.09199  232 ILE   A CG2 
1757 C  CD1 . ILE   A 232 ? 0.40873 0.76294 0.61186 0.00042  -0.04352 0.08893  232 ILE   A CD1 
1758 N  N   . LEU   A 233 ? 0.28881 0.63999 0.49243 -0.00218 -0.07060 0.08912  233 LEU   A N   
1759 C  CA  . LEU   A 233 ? 0.30987 0.66238 0.51641 -0.00489 -0.08010 0.09109  233 LEU   A CA  
1760 C  C   . LEU   A 233 ? 0.34176 0.66798 0.53879 -0.01305 -0.08931 0.08404  233 LEU   A C   
1761 O  O   . LEU   A 233 ? 0.31934 0.62452 0.49892 -0.00883 -0.08781 0.07365  233 LEU   A O   
1762 C  CB  . LEU   A 233 ? 0.32048 0.67185 0.51682 0.00649  -0.07540 0.08628  233 LEU   A CB  
1763 C  CG  . LEU   A 233 ? 0.32102 0.67664 0.52013 0.00610  -0.08375 0.08862  233 LEU   A CG  
1764 C  CD1 . LEU   A 233 ? 0.40756 0.79544 0.62878 0.00375  -0.08698 0.10222  233 LEU   A CD1 
1765 C  CD2 . LEU   A 233 ? 0.35225 0.69897 0.53619 0.01773  -0.07846 0.08133  233 LEU   A CD2 
1766 N  N   . SER   A 234 ? 0.35577 0.68248 0.56323 -0.02436 -0.09858 0.08954  234 SER   A N   
1767 C  CA  . SER   A 234 ? 0.38834 0.68833 0.58513 -0.03084 -0.10744 0.08183  234 SER   A CA  
1768 C  C   . SER   A 234 ? 0.46964 0.76307 0.66493 -0.03436 -0.11973 0.08136  234 SER   A C   
1769 O  O   . SER   A 234 ? 0.41188 0.72384 0.62226 -0.03840 -0.12624 0.09133  234 SER   A O   
1770 C  CB  . SER   A 234 ? 0.38352 0.68229 0.58976 -0.04112 -0.11335 0.08682  234 SER   A CB  
1771 O  OG  . SER   A 234 ? 0.37511 0.68038 0.58306 -0.03823 -0.10248 0.08772  234 SER   A OG  
1772 N  N   . HIS   A 235 ? 0.37757 0.64567 0.55439 -0.03242 -0.12282 0.06996  235 HIS   A N   
1773 C  CA  . HIS   A 235 ? 0.43723 0.69604 0.61069 -0.03604 -0.13578 0.06860  235 HIS   A CA  
1774 C  C   . HIS   A 235 ? 0.42387 0.66747 0.59811 -0.04592 -0.14915 0.06804  235 HIS   A C   
1775 O  O   . HIS   A 235 ? 0.44765 0.68269 0.61981 -0.04808 -0.14714 0.06551  235 HIS   A O   
1776 C  CB  . HIS   A 235 ? 0.41937 0.66115 0.57200 -0.02782 -0.13280 0.05746  235 HIS   A CB  
1777 C  CG  . HIS   A 235 ? 0.42170 0.64082 0.55630 -0.02522 -0.12933 0.04614  235 HIS   A CG  
1778 N  ND1 . HIS   A 235 ? 0.39824 0.61517 0.52371 -0.01797 -0.11585 0.04106  235 HIS   A ND1 
1779 C  CD2 . HIS   A 235 ? 0.40378 0.60206 0.52748 -0.02827 -0.13796 0.03896  235 HIS   A CD2 
1780 C  CE1 . HIS   A 235 ? 0.44146 0.63937 0.55276 -0.01728 -0.11569 0.03206  235 HIS   A CE1 
1781 N  NE2 . HIS   A 235 ? 0.41422 0.60058 0.52366 -0.02276 -0.12875 0.03022  235 HIS   A NE2 
1782 N  N   . GLY   A 236 ? 0.40665 0.64724 0.58471 -0.05211 -0.16379 0.07109  236 GLY   A N   
1783 C  CA  . GLY   A 236 ? 0.47379 0.69809 0.65215 -0.06156 -0.17900 0.07080  236 GLY   A CA  
1784 C  C   . GLY   A 236 ? 0.48007 0.67419 0.63503 -0.05714 -0.18166 0.05610  236 GLY   A C   
1785 O  O   . GLY   A 236 ? 0.44448 0.62981 0.58302 -0.04848 -0.17622 0.04703  236 GLY   A O   
1786 N  N   . MET   A 237 ? 0.51883 0.69710 0.67196 -0.06304 -0.19100 0.05403  237 MET   A N   
1787 C  CA  . MET   A 237 ? 0.52948 0.67979 0.66030 -0.05809 -0.19497 0.04004  237 MET   A CA  
1788 C  C   . MET   A 237 ? 0.53655 0.67245 0.65797 -0.05880 -0.21015 0.03597  237 MET   A C   
1789 O  O   . MET   A 237 ? 0.57413 0.71120 0.70699 -0.06808 -0.22535 0.04366  237 MET   A O   
1790 C  CB  . MET   A 237 ? 0.51098 0.64754 0.64160 -0.06296 -0.20103 0.03843  237 MET   A CB  
1791 C  CG  . MET   A 237 ? 0.53299 0.68288 0.67289 -0.06287 -0.18718 0.04269  237 MET   A CG  
1792 S  SD  . MET   A 237 ? 0.51096 0.66460 0.63749 -0.04973 -0.16526 0.03389  237 MET   A SD  
1793 C  CE  . MET   A 237 ? 0.48958 0.61376 0.59271 -0.04408 -0.16879 0.01849  237 MET   A CE  
1794 N  N   . LEU   A 238 ? 0.52710 0.65008 0.62786 -0.04932 -0.20651 0.02454  238 LEU   A N   
1795 C  CA  . LEU   A 238 ? 0.57705 0.68494 0.66610 -0.04866 -0.22072 0.01946  238 LEU   A CA  
1796 C  C   . LEU   A 238 ? 0.62409 0.70725 0.70436 -0.05199 -0.23692 0.01349  238 LEU   A C   
1797 O  O   . LEU   A 238 ? 0.62636 0.69729 0.69534 -0.04728 -0.23252 0.00533  238 LEU   A O   
1798 C  CB  . LEU   A 238 ? 0.54155 0.64415 0.61031 -0.03712 -0.21119 0.00946  238 LEU   A CB  
1799 C  CG  . LEU   A 238 ? 0.62788 0.72105 0.68539 -0.03502 -0.22245 0.00572  238 LEU   A CG  
1800 C  CD1 . LEU   A 238 ? 0.61733 0.73013 0.69157 -0.03957 -0.22399 0.01674  238 LEU   A CD1 
1801 C  CD2 . LEU   A 238 ? 0.69048 0.77506 0.72447 -0.02330 -0.21312 -0.00547 238 LEU   A CD2 
1802 N  N   . PRO   A 239 ? 0.69570 0.77096 0.78138 -0.06018 -0.25630 0.01771  239 PRO   A N   
1803 C  CA  . PRO   A 239 ? 0.73234 0.78213 0.80986 -0.06367 -0.27358 0.01246  239 PRO   A CA  
1804 C  C   . PRO   A 239 ? 0.74678 0.77130 0.79533 -0.05212 -0.27716 -0.00411 239 PRO   A C   
1805 O  O   . PRO   A 239 ? 0.69374 0.71924 0.72901 -0.04352 -0.27087 -0.01021 239 PRO   A O   
1806 C  CB  . PRO   A 239 ? 0.71557 0.76480 0.80643 -0.07549 -0.29381 0.02216  239 PRO   A CB  
1807 C  CG  . PRO   A 239 ? 0.76359 0.83632 0.86568 -0.07597 -0.28730 0.03009  239 PRO   A CG  
1808 C  CD  . PRO   A 239 ? 0.64719 0.73872 0.74990 -0.06777 -0.26347 0.02937  239 PRO   A CD  
1809 N  N   . GLY   A 240 ? 0.81115 0.81362 0.84955 -0.05136 -0.28693 -0.01126 240 GLY   A N   
1810 C  CA  . GLY   A 240 ? 0.77518 0.75246 0.78594 -0.04035 -0.29417 -0.02676 240 GLY   A CA  
1811 C  C   . GLY   A 240 ? 0.89912 0.86167 0.90173 -0.04182 -0.31389 -0.02880 240 GLY   A C   
1812 O  O   . GLY   A 240 ? 0.85716 0.81994 0.87502 -0.05375 -0.32909 -0.01899 240 GLY   A O   
1813 N  N   . LEU   A 241 ? 0.86997 0.81969 0.84762 -0.02938 -0.31403 -0.04160 241 LEU   A N   
1814 C  CA  . LEU   A 241 ? 0.94922 0.88472 0.91560 -0.02852 -0.33132 -0.04512 241 LEU   A CA  
1815 C  C   . LEU   A 241 ? 0.99331 0.90215 0.95664 -0.03468 -0.35771 -0.04680 241 LEU   A C   
1816 O  O   . LEU   A 241 ? 1.06514 0.96528 1.02884 -0.03994 -0.37537 -0.04425 241 LEU   A O   
1817 C  CB  . LEU   A 241 ? 0.99395 0.92196 0.93242 -0.01262 -0.32461 -0.05891 241 LEU   A CB  
1818 C  CG  . LEU   A 241 ? 0.84493 0.79933 0.78924 -0.00958 -0.30215 -0.05427 241 LEU   A CG  
1819 C  CD1 . LEU   A 241 ? 0.87439 0.82401 0.79248 0.00480  -0.29533 -0.06582 241 LEU   A CD1 
1820 C  CD2 . LEU   A 241 ? 0.88714 0.85689 0.85132 -0.01991 -0.30613 -0.04161 241 LEU   A CD2 
1821 N  N   . LEU   A 242 ? 1.11287 1.00752 1.07296 -0.03433 -0.36184 -0.05089 242 LEU   A N   
1822 C  CA  . LEU   A 242 ? 1.18983 1.05595 1.14481 -0.03866 -0.38410 -0.05287 242 LEU   A CA  
1823 C  C   . LEU   A 242 ? 1.26183 1.13570 1.24541 -0.05630 -0.38885 -0.03601 242 LEU   A C   
1824 O  O   . LEU   A 242 ? 1.21260 1.11180 1.21731 -0.06381 -0.37846 -0.02585 242 LEU   A O   
1825 C  CB  . LEU   A 242 ? 1.17000 1.01336 1.10237 -0.02619 -0.38500 -0.06752 242 LEU   A CB  
1826 C  CG  . LEU   A 242 ? 1.12096 0.95783 1.02382 -0.00777 -0.37971 -0.08372 242 LEU   A CG  
1827 C  CD1 . LEU   A 242 ? 1.19484 1.01222 1.07612 0.00569  -0.37940 -0.09771 242 LEU   A CD1 
1828 C  CD2 . LEU   A 242 ? 1.19918 1.02313 1.09078 -0.00527 -0.39013 -0.08602 242 LEU   A CD2 
1829 N  N   . GLU   A 243 ? 1.28415 1.13638 1.26800 -0.06263 -0.40480 -0.03245 243 GLU   A N   
1830 C  CA  . GLU   A 243 ? 1.25621 1.11547 1.26621 -0.07987 -0.41069 -0.01501 243 GLU   A CA  
1831 C  C   . GLU   A 243 ? 1.32827 1.19214 1.34913 -0.08450 -0.40516 -0.01069 243 GLU   A C   
1832 O  O   . GLU   A 243 ? 1.31594 1.15887 1.32031 -0.07621 -0.40742 -0.02173 243 GLU   A O   
1833 C  CB  . GLU   A 243 ? 1.25856 1.08816 1.26212 -0.08392 -0.43036 -0.01393 243 GLU   A CB  
1834 C  CG  . GLU   A 243 ? 1.25513 1.09205 1.28477 -0.10225 -0.43812 0.00551  243 GLU   A CG  
1835 C  CD  . GLU   A 243 ? 1.30879 1.11360 1.33030 -0.10581 -0.45908 0.00635  243 GLU   A CD  
1836 O  OE1 . GLU   A 243 ? 1.32658 1.10214 1.32184 -0.09334 -0.46777 -0.00877 243 GLU   A OE1 
1837 O  OE2 . GLU   A 243 ? 1.22984 1.03908 1.27101 -0.12072 -0.46694 0.02256  243 GLU   A OE2 
1838 N  N   . GLY   A 244 ? 1.30946 1.20219 1.35789 -0.09689 -0.39712 0.00540  244 GLY   A N   
1839 C  CA  . GLY   A 244 ? 1.25541 1.15628 1.31681 -0.10257 -0.39097 0.01171  244 GLY   A CA  
1840 C  C   . GLY   A 244 ? 1.31516 1.23564 1.37661 -0.09525 -0.37396 0.00639  244 GLY   A C   
1841 O  O   . GLY   A 244 ? 1.39310 1.31712 1.46203 -0.09820 -0.36910 0.00931  244 GLY   A O   
1842 N  N   . GLN   A 245 ? 1.27117 1.20417 1.32445 -0.08581 -0.36421 -0.00068 245 GLN   A N   
1843 C  CA  . GLN   A 245 ? 1.18021 1.12866 1.22918 -0.07511 -0.33819 -0.00605 245 GLN   A CA  
1844 C  C   . GLN   A 245 ? 1.11717 1.10181 1.18803 -0.07949 -0.31904 0.00670  245 GLN   A C   
1845 O  O   . GLN   A 245 ? 1.07380 1.07392 1.16424 -0.09055 -0.32511 0.02015  245 GLN   A O   
1846 C  CB  . GLN   A 245 ? 1.14458 1.08117 1.16580 -0.05827 -0.33188 -0.02289 245 GLN   A CB  
1847 C  CG  . GLN   A 245 ? 1.20929 1.11068 1.20637 -0.05196 -0.35295 -0.03618 245 GLN   A CG  
1848 C  CD  . GLN   A 245 ? 1.20230 1.09377 1.17105 -0.03338 -0.34343 -0.05349 245 GLN   A CD  
1849 O  OE1 . GLN   A 245 ? 1.05888 0.96824 1.02414 -0.02607 -0.32488 -0.05526 245 GLN   A OE1 
1850 N  NE2 . GLN   A 245 ? 1.27856 1.14179 1.22685 -0.02551 -0.35653 -0.06594 245 GLN   A NE2 
1851 N  N   . GLU   A 253 ? 1.22845 1.16418 1.09859 0.04900  -0.24215 -0.10716 253 GLU   A N   
1852 C  CA  . GLU   A 253 ? 1.25572 1.18071 1.09950 0.06201  -0.24860 -0.11839 253 GLU   A CA  
1853 C  C   . GLU   A 253 ? 1.21023 1.12920 1.05314 0.05749  -0.26157 -0.11559 253 GLU   A C   
1854 O  O   . GLU   A 253 ? 1.07883 1.01396 0.92770 0.05442  -0.25227 -0.10894 253 GLU   A O   
1855 C  CB  . GLU   A 253 ? 1.38447 1.28597 1.20953 0.07218  -0.26223 -0.13122 253 GLU   A CB  
1856 C  CG  . GLU   A 253 ? 1.41696 1.29454 1.24864 0.06380  -0.28503 -0.13060 253 GLU   A CG  
1857 C  CD  . GLU   A 253 ? 1.37701 1.26143 1.23476 0.05011  -0.28135 -0.11982 253 GLU   A CD  
1858 O  OE1 . GLU   A 253 ? 1.35471 1.26294 1.22895 0.04453  -0.26269 -0.11082 253 GLU   A OE1 
1859 O  OE2 . GLU   A 253 ? 1.36937 1.23460 1.23019 0.04530  -0.29772 -0.12043 253 GLU   A OE2 
1860 N  N   . ASN   A 254 ? 1.28556 1.18034 1.12070 0.05712  -0.28396 -0.12064 254 ASN   A N   
1861 C  CA  . ASN   A 254 ? 1.21587 1.10369 1.05452 0.04989  -0.29899 -0.11626 254 ASN   A CA  
1862 C  C   . ASN   A 254 ? 1.13115 1.02720 1.00007 0.03175  -0.30250 -0.10137 254 ASN   A C   
1863 O  O   . ASN   A 254 ? 1.10337 0.99506 0.97916 0.02373  -0.31608 -0.09589 254 ASN   A O   
1864 C  CB  . ASN   A 254 ? 1.32646 1.18385 1.14332 0.05702  -0.32294 -0.12776 254 ASN   A CB  
1865 C  CG  . ASN   A 254 ? 1.37659 1.22952 1.16254 0.07541  -0.32032 -0.14114 254 ASN   A CG  
1866 O  OD1 . ASN   A 254 ? 1.32616 1.19948 1.10773 0.08199  -0.30045 -0.14107 254 ASN   A OD1 
1867 N  ND2 . ASN   A 254 ? 1.40919 1.23561 1.17357 0.08365  -0.34080 -0.15211 254 ASN   A ND2 
1868 N  N   . SER   A 255 ? 1.16553 1.07510 1.05290 0.02530  -0.29027 -0.09420 255 SER   A N   
1869 C  CA  . SER   A 255 ? 1.06279 0.98260 0.97829 0.00913  -0.29294 -0.07976 255 SER   A CA  
1870 C  C   . SER   A 255 ? 0.93955 0.88694 0.87089 0.00446  -0.27605 -0.06927 255 SER   A C   
1871 O  O   . SER   A 255 ? 0.90154 0.85996 0.85514 -0.00776 -0.27897 -0.05699 255 SER   A O   
1872 C  CB  . SER   A 255 ? 0.96744 0.88627 0.89514 0.00391  -0.29093 -0.07673 255 SER   A CB  
1873 O  OG  . SER   A 255 ? 1.03080 0.96727 0.96104 0.00866  -0.26855 -0.07671 255 SER   A OG  
1874 N  N   . ALA   A 256 ? 0.86767 0.82620 0.78754 0.01400  -0.25996 -0.07348 256 ALA   A N   
1875 C  CA  . ALA   A 256 ? 0.75285 0.73492 0.68635 0.01010  -0.24552 -0.06394 256 ALA   A CA  
1876 C  C   . ALA   A 256 ? 0.70816 0.69424 0.62270 0.02083  -0.23642 -0.07007 256 ALA   A C   
1877 O  O   . ALA   A 256 ? 0.81160 0.78750 0.70426 0.03188  -0.23611 -0.08104 256 ALA   A O   
1878 C  CB  . ALA   A 256 ? 0.74773 0.74723 0.69834 0.00603  -0.22875 -0.05698 256 ALA   A CB  
1879 N  N   . ILE   A 257 ? 0.68634 0.68748 0.60914 0.01767  -0.23011 -0.06255 257 ILE   A N   
1880 C  CA  . ILE   A 257 ? 0.65917 0.66808 0.56769 0.02604  -0.21866 -0.06547 257 ILE   A CA  
1881 C  C   . ILE   A 257 ? 0.67335 0.69755 0.58616 0.02819  -0.19820 -0.06325 257 ILE   A C   
1882 O  O   . ILE   A 257 ? 0.68642 0.72233 0.61913 0.02097  -0.19120 -0.05498 257 ILE   A O   
1883 C  CB  . ILE   A 257 ? 0.60030 0.61845 0.51638 0.02170  -0.22061 -0.05793 257 ILE   A CB  
1884 C  CG1 . ILE   A 257 ? 0.67840 0.68191 0.59269 0.01804  -0.24206 -0.05893 257 ILE   A CG1 
1885 C  CG2 . ILE   A 257 ? 0.64349 0.66873 0.54398 0.03004  -0.20913 -0.06047 257 ILE   A CG2 
1886 C  CD1 . ILE   A 257 ? 0.72388 0.70750 0.61186 0.02790  -0.25196 -0.07158 257 ILE   A CD1 
1887 N  N   . PHE   A 258 ? 0.62435 0.64880 0.51829 0.03820  -0.18917 -0.07038 258 PHE   A N   
1888 C  CA  . PHE   A 258 ? 0.70566 0.74460 0.60078 0.04070  -0.17035 -0.06815 258 PHE   A CA  
1889 C  C   . PHE   A 258 ? 0.68174 0.73067 0.56927 0.04375  -0.16219 -0.06527 258 PHE   A C   
1890 O  O   . PHE   A 258 ? 0.69202 0.73551 0.56838 0.04658  -0.17035 -0.06750 258 PHE   A O   
1891 C  CB  . PHE   A 258 ? 0.73992 0.77377 0.62125 0.04890  -0.16611 -0.07701 258 PHE   A CB  
1892 C  CG  . PHE   A 258 ? 0.73766 0.76153 0.62722 0.04562  -0.17351 -0.07919 258 PHE   A CG  
1893 C  CD1 . PHE   A 258 ? 0.74697 0.77984 0.65430 0.03943  -0.16441 -0.07317 258 PHE   A CD1 
1894 C  CD2 . PHE   A 258 ? 0.78228 0.78683 0.66240 0.04799  -0.19094 -0.08651 258 PHE   A CD2 
1895 C  CE1 . PHE   A 258 ? 0.74972 0.77381 0.66523 0.03568  -0.17132 -0.07416 258 PHE   A CE1 
1896 C  CE2 . PHE   A 258 ? 0.83402 0.82808 0.72201 0.04411  -0.19901 -0.08768 258 PHE   A CE2 
1897 C  CZ  . PHE   A 258 ? 0.83752 0.84205 0.74371 0.03765  -0.18878 -0.08113 258 PHE   A CZ  
1898 N  N   . MET   A 259 ? 0.63516 0.69802 0.52881 0.04285  -0.14664 -0.05996 259 MET   A N   
1899 C  CA  . MET   A 259 ? 0.58725 0.65997 0.47742 0.04371  -0.13874 -0.05495 259 MET   A CA  
1900 C  C   . MET   A 259 ? 0.63916 0.71073 0.50590 0.05263  -0.13635 -0.06067 259 MET   A C   
1901 O  O   . MET   A 259 ? 0.70909 0.78572 0.56994 0.05352  -0.13369 -0.05710 259 MET   A O   
1902 C  CB  . MET   A 259 ? 0.66084 0.74656 0.56321 0.04031  -0.12401 -0.04786 259 MET   A CB  
1903 C  CG  . MET   A 259 ? 0.58545 0.67608 0.51024 0.03248  -0.12494 -0.04063 259 MET   A CG  
1904 S  SD  . MET   A 259 ? 0.57877 0.66984 0.51221 0.02808  -0.13663 -0.03512 259 MET   A SD  
1905 C  CE  . MET   A 259 ? 0.50751 0.60621 0.43316 0.03115  -0.12811 -0.03091 259 MET   A CE  
1906 N  N   . ASP   A 260 ? 0.73631 0.80255 0.58947 0.05965  -0.13685 -0.06903 260 ASP   A N   
1907 C  CA  . ASP   A 260 ? 0.87130 0.93859 0.70158 0.06915  -0.13482 -0.07432 260 ASP   A CA  
1908 C  C   . ASP   A 260 ? 0.89608 0.94921 0.71080 0.07494  -0.15013 -0.08229 260 ASP   A C   
1909 O  O   . ASP   A 260 ? 1.06698 1.12133 0.86171 0.08328  -0.14962 -0.08632 260 ASP   A O   
1910 C  CB  . ASP   A 260 ? 0.79551 0.86848 0.61813 0.07537  -0.12502 -0.07867 260 ASP   A CB  
1911 C  CG  . ASP   A 260 ? 0.88955 0.95140 0.71387 0.07733  -0.13226 -0.08603 260 ASP   A CG  
1912 O  OD1 . ASP   A 260 ? 0.92591 0.98339 0.76834 0.06918  -0.13620 -0.08265 260 ASP   A OD1 
1913 O  OD2 . ASP   A 260 ? 1.01926 1.07788 0.82723 0.08719  -0.13334 -0.09467 260 ASP   A OD2 
1914 N  N   . ASP   A 261 ? 0.84563 0.88589 0.66898 0.07038  -0.16416 -0.08382 261 ASP   A N   
1915 C  CA  . ASP   A 261 ? 0.94850 0.97254 0.75676 0.07554  -0.18084 -0.09172 261 ASP   A CA  
1916 C  C   . ASP   A 261 ? 0.99260 1.01910 0.78853 0.07849  -0.18263 -0.09033 261 ASP   A C   
1917 O  O   . ASP   A 261 ? 1.07730 1.11363 0.88417 0.07216  -0.17728 -0.08140 261 ASP   A O   
1918 C  CB  . ASP   A 261 ? 0.76892 0.78084 0.59301 0.06672  -0.19591 -0.08994 261 ASP   A CB  
1919 C  CG  . ASP   A 261 ? 0.85341 0.85407 0.67966 0.06730  -0.20171 -0.09571 261 ASP   A CG  
1920 O  OD1 . ASP   A 261 ? 0.94979 0.94765 0.76025 0.07721  -0.19807 -0.10413 261 ASP   A OD1 
1921 O  OD2 . ASP   A 261 ? 0.81721 0.81229 0.66115 0.05785  -0.21046 -0.09142 261 ASP   A OD2 
1922 N  N   . SER   A 262 ? 1.10400 1.12107 0.87616 0.08886  -0.19070 -0.09944 262 SER   A N   
1923 C  CA  . SER   A 262 ? 1.13372 1.15105 0.89138 0.09270  -0.19440 -0.09927 262 SER   A CA  
1924 C  C   . SER   A 262 ? 1.13234 1.13670 0.89615 0.08671  -0.21183 -0.09816 262 SER   A C   
1925 O  O   . SER   A 262 ? 1.11169 1.10567 0.88874 0.08034  -0.22264 -0.09833 262 SER   A O   
1926 C  CB  . SER   A 262 ? 1.12379 1.13741 0.85236 0.10731  -0.19589 -0.10962 262 SER   A CB  
1927 O  OG  . SER   A 262 ? 1.14819 1.14178 0.86730 0.11245  -0.21232 -0.11994 262 SER   A OG  
1928 N  N   . GLU   A 263 ? 1.07824 1.08357 0.83221 0.08852  -0.21519 -0.09647 263 GLU   A N   
1929 C  CA  . GLU   A 263 ? 1.05504 1.04907 0.81459 0.08296  -0.23210 -0.09509 263 GLU   A CA  
1930 C  C   . GLU   A 263 ? 1.04919 1.02159 0.79808 0.08701  -0.25059 -0.10527 263 GLU   A C   
1931 O  O   . GLU   A 263 ? 1.00363 0.96588 0.76625 0.07863  -0.26486 -0.10301 263 GLU   A O   
1932 C  CB  . GLU   A 263 ? 1.11896 1.11588 0.86654 0.08569  -0.23387 -0.09287 263 GLU   A CB  
1933 C  CG  . GLU   A 263 ? 1.10474 1.11999 0.86432 0.08021  -0.21928 -0.08169 263 GLU   A CG  
1934 C  CD  . GLU   A 263 ? 1.20299 1.21826 0.96169 0.07780  -0.22639 -0.07686 263 GLU   A CD  
1935 O  OE1 . GLU   A 263 ? 1.12049 1.14674 0.89709 0.07029  -0.22020 -0.06701 263 GLU   A OE1 
1936 O  OE2 . GLU   A 263 ? 1.09073 1.09489 0.83084 0.08381  -0.23845 -0.08300 263 GLU   A OE2 
1937 N  N   . SER   A 264 ? 1.09869 1.06386 0.82281 0.10005  -0.25135 -0.11628 264 SER   A N   
1938 C  CA  . SER   A 264 ? 1.18401 1.12598 0.89592 0.10520  -0.27018 -0.12700 264 SER   A CA  
1939 C  C   . SER   A 264 ? 1.08382 1.02032 0.81135 0.09975  -0.27157 -0.12732 264 SER   A C   
1940 O  O   . SER   A 264 ? 1.05226 0.96942 0.78198 0.09655  -0.28974 -0.13093 264 SER   A O   
1941 C  CB  . SER   A 264 ? 1.18582 1.12137 0.86457 0.12278  -0.27163 -0.13955 264 SER   A CB  
1942 O  OG  . SER   A 264 ? 1.19302 1.13801 0.86672 0.13017  -0.25761 -0.14323 264 SER   A OG  
1943 N  N   . ASP   A 265 ? 1.13290 1.08526 0.87081 0.09844  -0.25358 -0.12344 265 ASP   A N   
1944 C  CA  . ASP   A 265 ? 0.99539 0.94410 0.75061 0.09184  -0.25418 -0.12214 265 ASP   A CA  
1945 C  C   . ASP   A 265 ? 0.89663 0.84292 0.67741 0.07653  -0.26369 -0.11259 265 ASP   A C   
1946 O  O   . ASP   A 265 ? 0.94631 0.87742 0.73393 0.07162  -0.27809 -0.11416 265 ASP   A O   
1947 C  CB  . ASP   A 265 ? 1.04560 1.01428 0.81087 0.09102  -0.23240 -0.11728 265 ASP   A CB  
1948 C  CG  . ASP   A 265 ? 1.09804 1.06847 0.84299 0.10486  -0.22446 -0.12674 265 ASP   A CG  
1949 O  OD1 . ASP   A 265 ? 1.11186 1.06485 0.83964 0.11409  -0.23705 -0.13789 265 ASP   A OD1 
1950 O  OD2 . ASP   A 265 ? 1.09779 1.08732 0.84521 0.10617  -0.20586 -0.12257 265 ASP   A OD2 
1951 N  N   . VAL   A 266 ? 0.86858 0.83062 0.66389 0.06895  -0.25585 -0.10206 266 VAL   A N   
1952 C  CA  . VAL   A 266 ? 0.90207 0.86629 0.72228 0.05521  -0.26358 -0.09193 266 VAL   A CA  
1953 C  C   . VAL   A 266 ? 0.95348 0.89812 0.76779 0.05343  -0.28700 -0.09534 266 VAL   A C   
1954 O  O   . VAL   A 266 ? 0.86212 0.79880 0.69198 0.04381  -0.30007 -0.09148 266 VAL   A O   
1955 C  CB  . VAL   A 266 ? 0.78922 0.77369 0.62209 0.05034  -0.25105 -0.08142 266 VAL   A CB  
1956 C  CG1 . VAL   A 266 ? 0.84497 0.83229 0.69987 0.03848  -0.26118 -0.07179 266 VAL   A CG1 
1957 C  CG2 . VAL   A 266 ? 0.78078 0.78260 0.62490 0.04912  -0.23031 -0.07653 266 VAL   A CG2 
1958 N  N   . ASN   A 267 ? 0.95172 0.88866 0.74352 0.06227  -0.29306 -0.10196 267 ASN   A N   
1959 C  CA  . ASN   A 267 ? 0.87135 0.78840 0.65529 0.06131  -0.31624 -0.10575 267 ASN   A CA  
1960 C  C   . ASN   A 267 ? 0.93263 0.82617 0.70910 0.06323  -0.33259 -0.11438 267 ASN   A C   
1961 O  O   . ASN   A 267 ? 0.90559 0.78789 0.69569 0.05290  -0.34956 -0.11039 267 ASN   A O   
1962 C  CB  . ASN   A 267 ? 0.80994 0.72452 0.56866 0.07222  -0.31722 -0.11186 267 ASN   A CB  
1963 C  CG  . ASN   A 267 ? 1.00990 0.94273 0.78035 0.06639  -0.30891 -0.10123 267 ASN   A CG  
1964 O  OD1 . ASN   A 267 ? 0.97616 0.91982 0.77307 0.05420  -0.30756 -0.09017 267 ASN   A OD1 
1965 N  ND2 . ASN   A 267 ? 1.04545 0.98151 0.79605 0.07533  -0.30439 -0.10441 267 ASN   A ND2 
1966 N  N   . ARG   A 268 ? 0.97631 0.86421 0.73417 0.07530  -0.32673 -0.12482 268 ARG   A N   
1967 C  CA  . ARG   A 268 ? 1.01891 0.88382 0.76867 0.07843  -0.34170 -0.13365 268 ARG   A CA  
1968 C  C   . ARG   A 268 ? 1.05386 0.92001 0.83146 0.06418  -0.34373 -0.12490 268 ARG   A C   
1969 O  O   . ARG   A 268 ? 1.02858 0.87454 0.81008 0.05887  -0.36111 -0.12565 268 ARG   A O   
1970 C  CB  . ARG   A 268 ? 0.98966 0.85310 0.71580 0.09497  -0.33195 -0.14565 268 ARG   A CB  
1971 C  CG  . ARG   A 268 ? 1.11926 0.96399 0.84404 0.09752  -0.33878 -0.15201 268 ARG   A CG  
1972 C  CD  . ARG   A 268 ? 1.25238 1.09701 0.95341 0.11559  -0.32841 -0.16372 268 ARG   A CD  
1973 N  NE  . ARG   A 268 ? 1.31058 1.18138 1.01176 0.11929  -0.30777 -0.16201 268 ARG   A NE  
1974 C  CZ  . ARG   A 268 ? 1.31920 1.19980 1.03350 0.11661  -0.29533 -0.15927 268 ARG   A CZ  
1975 N  NH1 . ARG   A 268 ? 1.33893 1.20547 1.06444 0.11032  -0.30548 -0.15945 268 ARG   A NH1 
1976 N  NH2 . ARG   A 268 ? 1.30307 1.20764 1.01859 0.12031  -0.27279 -0.15612 268 ARG   A NH2 
1977 N  N   . LYS   A 269 ? 0.92811 0.81759 0.72617 0.05789  -0.32370 -0.11562 269 LYS   A N   
1978 C  CA  . LYS   A 269 ? 0.91204 0.80349 0.73520 0.04525  -0.32535 -0.10742 269 LYS   A CA  
1979 C  C   . LYS   A 269 ? 0.95548 0.84939 0.80170 0.02978  -0.33754 -0.09535 269 LYS   A C   
1980 O  O   . LYS   A 269 ? 0.95734 0.84200 0.81754 0.01984  -0.35057 -0.09096 269 LYS   A O   
1981 C  CB  . LYS   A 269 ? 0.90392 0.81898 0.74176 0.04343  -0.30121 -0.10120 269 LYS   A CB  
1982 C  CG  . LYS   A 269 ? 0.87459 0.78791 0.69573 0.05573  -0.29057 -0.11113 269 LYS   A CG  
1983 C  CD  . LYS   A 269 ? 0.94700 0.88498 0.78237 0.05350  -0.26648 -0.10407 269 LYS   A CD  
1984 C  CE  . LYS   A 269 ? 0.91021 0.84883 0.73092 0.06495  -0.25552 -0.11280 269 LYS   A CE  
1985 N  NZ  . LYS   A 269 ? 0.84954 0.81086 0.68517 0.06149  -0.23369 -0.10526 269 LYS   A NZ  
1986 N  N   . ILE   A 270 ? 0.90324 0.81136 0.75511 0.02709  -0.33300 -0.08882 270 ILE   A N   
1987 C  CA  . ILE   A 270 ? 0.93297 0.84654 0.80744 0.01304  -0.34395 -0.07681 270 ILE   A CA  
1988 C  C   . ILE   A 270 ? 0.93701 0.82472 0.80184 0.01099  -0.37127 -0.08128 270 ILE   A C   
1989 O  O   . ILE   A 270 ? 0.96483 0.84926 0.84905 -0.00196 -0.38357 -0.07231 270 ILE   A O   
1990 C  CB  . ILE   A 270 ? 0.98735 0.92199 0.86841 0.01234  -0.33241 -0.06963 270 ILE   A CB  
1991 C  CG1 . ILE   A 270 ? 0.84156 0.80010 0.73380 0.01309  -0.30727 -0.06428 270 ILE   A CG1 
1992 C  CG2 . ILE   A 270 ? 0.95303 0.89421 0.85695 -0.00117 -0.34484 -0.05747 270 ILE   A CG2 
1993 C  CD1 . ILE   A 270 ? 0.88793 0.85327 0.80089 0.00487  -0.30276 -0.05793 270 ILE   A CD1 
1994 N  N   . LYS   A 271 ? 0.97318 0.84352 0.80945 0.02384  -0.37643 -0.09373 271 LYS   A N   
1995 C  CA  . LYS   A 271 ? 1.12185 0.96799 0.95008 0.02346  -0.39259 -0.09661 271 LYS   A CA  
1996 C  C   . LYS   A 271 ? 1.11553 0.94236 0.95054 0.01779  -0.40330 -0.09636 271 LYS   A C   
1997 O  O   . LYS   A 271 ? 1.09662 0.91010 0.94091 0.00870  -0.41784 -0.09075 271 LYS   A O   
1998 C  CB  . LYS   A 271 ? 1.14299 0.97523 0.93833 0.04080  -0.39162 -0.11072 271 LYS   A CB  
1999 C  CG  . LYS   A 271 ? 1.21383 1.02042 0.99600 0.04373  -0.40784 -0.11552 271 LYS   A CG  
2000 C  CD  . LYS   A 271 ? 1.31763 1.10870 1.06671 0.06321  -0.40559 -0.13119 271 LYS   A CD  
2001 C  CE  . LYS   A 271 ? 1.46083 1.22357 1.19618 0.06724  -0.42297 -0.13671 271 LYS   A CE  
2002 N  NZ  . LYS   A 271 ? 1.48032 1.23309 1.18382 0.08694  -0.41978 -0.15055 271 LYS   A NZ  
2003 N  N   . LYS   A 272 ? 1.10658 0.93188 0.93744 0.02273  -0.39644 -0.10173 272 LYS   A N   
2004 C  CA  . LYS   A 272 ? 1.10009 0.90648 0.93582 0.01847  -0.40586 -0.10194 272 LYS   A CA  
2005 C  C   . LYS   A 272 ? 0.99243 0.81450 0.85923 0.00196  -0.40418 -0.08781 272 LYS   A C   
2006 O  O   . LYS   A 272 ? 1.02279 0.83114 0.89672 -0.00375 -0.41187 -0.08559 272 LYS   A O   
2007 C  CB  . LYS   A 272 ? 1.06960 0.86478 0.88274 0.03407  -0.39982 -0.11599 272 LYS   A CB  
2008 C  CG  . LYS   A 272 ? 1.24452 1.03617 1.06832 0.02954  -0.39924 -0.11434 272 LYS   A CG  
2009 C  CD  . LYS   A 272 ? 1.29717 1.05963 1.12213 0.02496  -0.41721 -0.11380 272 LYS   A CD  
2010 C  CE  . LYS   A 272 ? 1.29247 1.05476 1.13056 0.01894  -0.41536 -0.11024 272 LYS   A CE  
2011 N  NZ  . LYS   A 272 ? 1.39871 1.13011 1.23252 0.01834  -0.43145 -0.11223 272 LYS   A NZ  
2012 N  N   . ALA   A 273 ? 1.01214 0.86253 0.89779 -0.00564 -0.39471 -0.07761 273 ALA   A N   
2013 C  CA  . ALA   A 273 ? 0.95423 0.82234 0.86918 -0.01980 -0.39125 -0.06415 273 ALA   A CA  
2014 C  C   . ALA   A 273 ? 1.04188 0.90327 0.97625 -0.03477 -0.40532 -0.05207 273 ALA   A C   
2015 O  O   . ALA   A 273 ? 1.09788 0.94523 1.02627 -0.03561 -0.41720 -0.05237 273 ALA   A O   
2016 C  CB  . ALA   A 273 ? 0.97173 0.87251 0.90226 -0.02262 -0.37555 -0.05567 273 ALA   A CB  
2017 N  N   . TYR   A 274 ? 1.07936 0.95138 1.03712 -0.04667 -0.40376 -0.04090 274 TYR   A N   
2018 C  CA  . TYR   A 274 ? 1.09426 0.96598 1.07382 -0.06223 -0.41469 -0.02661 274 TYR   A CA  
2019 C  C   . TYR   A 274 ? 1.05782 0.95604 1.05618 -0.06979 -0.41110 -0.01464 274 TYR   A C   
2020 O  O   . TYR   A 274 ? 1.06547 0.99253 1.07770 -0.07099 -0.39739 -0.00867 274 TYR   A O   
2021 C  CB  . TYR   A 274 ? 1.06609 0.94421 1.06490 -0.07226 -0.41238 -0.01735 274 TYR   A CB  
2022 C  CG  . TYR   A 274 ? 1.12409 0.99681 1.14142 -0.08748 -0.42521 -0.00331 274 TYR   A CG  
2023 C  CD1 . TYR   A 274 ? 1.16566 1.00819 1.17042 -0.08748 -0.44286 -0.00679 274 TYR   A CD1 
2024 C  CD2 . TYR   A 274 ? 1.11959 1.01632 1.16580 -0.10125 -0.41993 0.01346  274 TYR   A CD2 
2025 C  CE1 . TYR   A 274 ? 1.14585 0.98182 1.16658 -0.10156 -0.45560 0.00655  274 TYR   A CE1 
2026 C  CE2 . TYR   A 274 ? 1.10741 0.99961 1.16959 -0.11507 -0.43147 0.02704  274 TYR   A CE2 
2027 C  CZ  . TYR   A 274 ? 1.17260 1.03381 1.22199 -0.11556 -0.44975 0.02370  274 TYR   A CZ  
2028 O  OH  . TYR   A 274 ? 1.17659 1.03195 1.24121 -0.12963 -0.46231 0.03786  274 TYR   A OH  
2029 N  N   . CYS   A 275 ? 1.10800 0.99629 1.10758 -0.07487 -0.42388 -0.01058 275 CYS   A N   
2030 C  CA  . CYS   A 275 ? 1.12275 1.03409 1.13847 -0.08108 -0.42205 0.00005  275 CYS   A CA  
2031 C  C   . CYS   A 275 ? 1.17744 1.07846 1.20465 -0.09309 -0.43783 0.01015  275 CYS   A C   
2032 O  O   . CYS   A 275 ? 1.27538 1.16064 1.29091 -0.09073 -0.44879 0.00621  275 CYS   A O   
2033 C  CB  . CYS   A 275 ? 1.05994 0.97016 1.05514 -0.06852 -0.41878 -0.01070 275 CYS   A CB  
2034 S  SG  . CYS   A 275 ? 1.06850 1.00997 1.08136 -0.07293 -0.41318 0.00060  275 CYS   A SG  
2035 N  N   . PRO   A 276 ? 1.15752 1.06687 1.20742 -0.10629 -0.43962 0.02384  276 PRO   A N   
2036 C  CA  . PRO   A 276 ? 1.22737 1.12424 1.28729 -0.11830 -0.45572 0.03413  276 PRO   A CA  
2037 C  C   . PRO   A 276 ? 1.29024 1.20192 1.36011 -0.12266 -0.45865 0.04186  276 PRO   A C   
2038 O  O   . PRO   A 276 ? 1.22914 1.17482 1.31719 -0.12530 -0.44637 0.05075  276 PRO   A O   
2039 C  CB  . PRO   A 276 ? 1.13489 1.04820 1.21996 -0.13112 -0.45167 0.04928  276 PRO   A CB  
2040 C  CG  . PRO   A 276 ? 1.05052 0.99477 1.14453 -0.12682 -0.43142 0.04973  276 PRO   A CG  
2041 C  CD  . PRO   A 276 ? 1.04912 0.97938 1.11581 -0.11063 -0.42694 0.03082  276 PRO   A CD  
2042 N  N   . PRO   A 277 ? 1.47993 1.36674 1.53819 -0.12295 -0.47498 0.03874  277 PRO   A N   
2043 C  CA  . PRO   A 277 ? 1.57592 1.47618 1.64365 -0.12730 -0.47863 0.04617  277 PRO   A CA  
2044 C  C   . PRO   A 277 ? 1.59733 1.52753 1.69826 -0.14273 -0.47593 0.06699  277 PRO   A C   
2045 O  O   . PRO   A 277 ? 1.65027 1.57549 1.76352 -0.15365 -0.48243 0.07713  277 PRO   A O   
2046 C  CB  . PRO   A 277 ? 1.46826 1.33138 1.51792 -0.12633 -0.49896 0.03987  277 PRO   A CB  
2047 C  CG  . PRO   A 277 ? 1.53014 1.36117 1.55441 -0.11590 -0.50295 0.02448  277 PRO   A CG  
2048 C  CD  . PRO   A 277 ? 1.44520 1.29001 1.47967 -0.11775 -0.49067 0.02733  277 PRO   A CD  
2049 N  N   . ASN   A 278 ? 1.23597 1.19817 1.35097 -0.14294 -0.46589 0.07367  278 ASN   A N   
2050 C  CA  . ASN   A 278 ? 1.16099 1.15444 1.30648 -0.15562 -0.46299 0.09317  278 ASN   A CA  
2051 C  C   . ASN   A 278 ? 1.08606 1.10219 1.25150 -0.16202 -0.45120 0.10391  278 ASN   A C   
2052 O  O   . ASN   A 278 ? 1.04974 1.09091 1.24032 -0.17301 -0.44897 0.12113  278 ASN   A O   
2053 C  CB  . ASN   A 278 ? 1.07337 1.05015 1.22387 -0.16684 -0.48207 0.10190  278 ASN   A CB  
2054 C  CG  . ASN   A 278 ? 1.10639 1.06209 1.23757 -0.16024 -0.49361 0.09164  278 ASN   A CG  
2055 O  OD1 . ASN   A 278 ? 1.16617 1.14109 1.30673 -0.16132 -0.49209 0.09720  278 ASN   A OD1 
2056 N  ND2 . ASN   A 278 ? 0.98207 0.89907 1.08602 -0.15262 -0.50465 0.07665  278 ASN   A ND2 
2057 N  N   . VAL   A 279 ? 1.02360 1.03194 1.17814 -0.15522 -0.44357 0.09443  279 VAL   A N   
2058 C  CA  . VAL   A 279 ? 0.97883 1.00538 1.14950 -0.16031 -0.43274 0.10304  279 VAL   A CA  
2059 C  C   . VAL   A 279 ? 1.16425 1.21028 1.33180 -0.14921 -0.41428 0.09560  279 VAL   A C   
2060 O  O   . VAL   A 279 ? 1.07716 1.10533 1.22152 -0.13748 -0.41328 0.07942  279 VAL   A O   
2061 C  CB  . VAL   A 279 ? 0.96798 0.96376 1.12895 -0.16370 -0.44270 0.09957  279 VAL   A CB  
2062 C  CG1 . VAL   A 279 ? 1.01130 1.02783 1.19066 -0.17005 -0.43135 0.11024  279 VAL   A CG1 
2063 C  CG2 . VAL   A 279 ? 1.06705 1.03641 1.22568 -0.17263 -0.46368 0.10444  279 VAL   A CG2 
2064 N  N   . ILE   A 280 ? 1.25808 1.34052 1.44813 -0.15235 -0.39978 0.10757  280 ILE   A N   
2065 C  CA  . ILE   A 280 ? 1.26674 1.36848 1.45535 -0.14217 -0.38244 0.10200  280 ILE   A CA  
2066 C  C   . ILE   A 280 ? 1.29476 1.39402 1.48309 -0.14193 -0.37524 0.10003  280 ILE   A C   
2067 O  O   . ILE   A 280 ? 1.28057 1.37542 1.45507 -0.13181 -0.36739 0.08833  280 ILE   A O   
2068 C  CB  . ILE   A 280 ? 1.27009 1.41303 1.48129 -0.14288 -0.36953 0.11463  280 ILE   A CB  
2069 C  CG1 . ILE   A 280 ? 1.28414 1.43031 1.48922 -0.13689 -0.37208 0.11088  280 ILE   A CG1 
2070 C  CG2 . ILE   A 280 ? 1.26878 1.43445 1.48616 -0.13666 -0.35117 0.11469  280 ILE   A CG2 
2071 C  CD1 . ILE   A 280 ? 1.29205 1.47693 1.51839 -0.13672 -0.36100 0.12297  280 ILE   A CD1 
2072 N  N   . GLU   A 281 ? 1.30759 1.41024 1.51095 -0.15295 -0.37760 0.11181  281 GLU   A N   
2073 C  CA  . GLU   A 281 ? 1.37618 1.48196 1.58228 -0.15292 -0.36877 0.11179  281 GLU   A CA  
2074 C  C   . GLU   A 281 ? 1.44725 1.51769 1.62821 -0.14600 -0.37517 0.09496  281 GLU   A C   
2075 O  O   . GLU   A 281 ? 1.38120 1.41963 1.54745 -0.14716 -0.39095 0.08872  281 GLU   A O   
2076 C  CB  . GLU   A 281 ? 1.42328 1.53883 1.64937 -0.16629 -0.37073 0.12850  281 GLU   A CB  
2077 C  CG  . GLU   A 281 ? 1.51496 1.63245 1.74237 -0.16563 -0.36174 0.12769  281 GLU   A CG  
2078 C  CD  . GLU   A 281 ? 1.52402 1.67018 1.75651 -0.15646 -0.34213 0.12557  281 GLU   A CD  
2079 O  OE1 . GLU   A 281 ? 1.50354 1.66963 1.74024 -0.15123 -0.33553 0.12640  281 GLU   A OE1 
2080 O  OE2 . GLU   A 281 ? 1.53147 1.67884 1.76288 -0.15403 -0.33386 0.12276  281 GLU   A OE2 
2081 N  N   . ASN   A 282 ? 1.41798 1.49476 1.59358 -0.13789 -0.36264 0.08750  282 ASN   A N   
2082 C  CA  . ASN   A 282 ? 1.34653 1.39607 1.49956 -0.12963 -0.36475 0.07163  282 ASN   A CA  
2083 C  C   . ASN   A 282 ? 1.27050 1.29692 1.39711 -0.11833 -0.37129 0.05522  282 ASN   A C   
2084 O  O   . ASN   A 282 ? 1.24728 1.24855 1.35198 -0.11008 -0.37447 0.04089  282 ASN   A O   
2085 C  CB  . ASN   A 282 ? 1.42631 1.45076 1.57667 -0.13671 -0.37621 0.07278  282 ASN   A CB  
2086 C  CG  . ASN   A 282 ? 1.45551 1.49960 1.62624 -0.14495 -0.36750 0.08550  282 ASN   A CG  
2087 O  OD1 . ASN   A 282 ? 1.42164 1.46886 1.60739 -0.15685 -0.37355 0.09940  282 ASN   A OD1 
2088 N  ND2 . ASN   A 282 ? 1.44334 1.50060 1.61412 -0.13858 -0.35337 0.08118  282 ASN   A ND2 
2089 N  N   . ASN   A 283 ? 1.22497 1.26067 1.35249 -0.11674 -0.37237 0.05682  283 ASN   A N   
2090 C  CA  . ASN   A 283 ? 1.15406 1.17023 1.25703 -0.10625 -0.37823 0.04273  283 ASN   A CA  
2091 C  C   . ASN   A 283 ? 1.04612 1.07617 1.14115 -0.09495 -0.36379 0.03515  283 ASN   A C   
2092 O  O   . ASN   A 283 ? 1.06369 1.11791 1.16821 -0.09326 -0.35439 0.04074  283 ASN   A O   
2093 C  CB  . ASN   A 283 ? 1.06275 1.08492 1.17229 -0.11045 -0.38542 0.04944  283 ASN   A CB  
2094 C  CG  . ASN   A 283 ? 1.07769 1.07824 1.16119 -0.10005 -0.39266 0.03547  283 ASN   A CG  
2095 O  OD1 . ASN   A 283 ? 1.02114 1.01169 1.08341 -0.08803 -0.38782 0.02181  283 ASN   A OD1 
2096 N  ND2 . ASN   A 283 ? 1.03883 1.03388 1.12408 -0.10448 -0.40368 0.03947  283 ASN   A ND2 
2097 N  N   . PRO   A 284 ? 1.04853 1.06187 1.12357 -0.08521 -0.35838 0.02180  284 PRO   A N   
2098 C  CA  . PRO   A 284 ? 0.96032 0.98700 1.02772 -0.07328 -0.33301 0.01599  284 PRO   A CA  
2099 C  C   . PRO   A 284 ? 0.90634 0.93725 0.96177 -0.06442 -0.32714 0.01113  284 PRO   A C   
2100 O  O   . PRO   A 284 ? 0.93722 0.98595 0.99358 -0.05783 -0.30728 0.01146  284 PRO   A O   
2101 C  CB  . PRO   A 284 ? 0.90213 0.90602 0.94833 -0.06473 -0.33067 0.00221  284 PRO   A CB  
2102 C  CG  . PRO   A 284 ? 0.92389 0.89733 0.95617 -0.06651 -0.35563 -0.00447 284 PRO   A CG  
2103 C  CD  . PRO   A 284 ? 1.03476 1.01446 1.09005 -0.08229 -0.37149 0.01035  284 PRO   A CD  
2104 N  N   . ILE   A 285 ? 0.96572 0.97945 1.00890 -0.06389 -0.34453 0.00645  285 ILE   A N   
2105 C  CA  . ILE   A 285 ? 0.94706 0.96678 0.98165 -0.05721 -0.34056 0.00410  285 ILE   A CA  
2106 C  C   . ILE   A 285 ? 0.96194 1.01342 1.02209 -0.06338 -0.33199 0.01869  285 ILE   A C   
2107 O  O   . ILE   A 285 ? 0.82944 0.89634 0.88800 -0.05613 -0.31547 0.01856  285 ILE   A O   
2108 C  CB  . ILE   A 285 ? 0.97820 0.97452 0.99828 -0.05759 -0.36358 -0.00155 285 ILE   A CB  
2109 C  CG1 . ILE   A 285 ? 0.98522 0.95017 0.97815 -0.04925 -0.37165 -0.01703 285 ILE   A CG1 
2110 C  CG2 . ILE   A 285 ? 0.90426 0.90706 0.91624 -0.05147 -0.36065 -0.00306 285 ILE   A CG2 
2111 C  CD1 . ILE   A 285 ? 0.89256 0.85789 0.86713 -0.03543 -0.35130 -0.02783 285 ILE   A CD1 
2112 N  N   . TYR   A 286 ? 0.98074 1.04274 1.06472 -0.07669 -0.34368 0.03187  286 TYR   A N   
2113 C  CA  . TYR   A 286 ? 0.97537 1.07026 1.08483 -0.08196 -0.33551 0.04637  286 TYR   A CA  
2114 C  C   . TYR   A 286 ? 0.89082 1.00573 1.00812 -0.07743 -0.31214 0.04880  286 TYR   A C   
2115 O  O   . TYR   A 286 ? 0.91039 1.04904 1.03749 -0.07402 -0.29897 0.05460  286 TYR   A O   
2116 C  CB  . TYR   A 286 ? 1.06763 1.17127 1.20135 -0.09734 -0.35121 0.06084  286 TYR   A CB  
2117 C  CG  . TYR   A 286 ? 1.13256 1.27284 1.29304 -0.10190 -0.34207 0.07633  286 TYR   A CG  
2118 C  CD1 . TYR   A 286 ? 1.08703 1.25257 1.26639 -0.10436 -0.32902 0.08550  286 TYR   A CD1 
2119 C  CD2 . TYR   A 286 ? 1.12278 1.27301 1.28886 -0.10259 -0.34590 0.08142  286 TYR   A CD2 
2120 C  CE1 . TYR   A 286 ? 1.11543 1.31531 1.31757 -0.10641 -0.31956 0.09893  286 TYR   A CE1 
2121 C  CE2 . TYR   A 286 ? 1.13896 1.32340 1.32850 -0.10507 -0.33699 0.09492  286 TYR   A CE2 
2122 C  CZ  . TYR   A 286 ? 1.10494 1.31422 1.31197 -0.10646 -0.32358 0.10344  286 TYR   A CZ  
2123 O  OH  . TYR   A 286 ? 1.10464 1.34828 1.33330 -0.10706 -0.31400 0.11614  286 TYR   A OH  
2124 N  N   . ALA   A 287 ? 0.93222 1.03767 1.04534 -0.07708 -0.30736 0.04451  287 ALA   A N   
2125 C  CA  . ALA   A 287 ? 0.77705 0.89919 0.89526 -0.07203 -0.28548 0.04564  287 ALA   A CA  
2126 C  C   . ALA   A 287 ? 0.75115 0.87419 0.85230 -0.05880 -0.26944 0.03675  287 ALA   A C   
2127 O  O   . ALA   A 287 ? 0.71767 0.86191 0.82755 -0.05503 -0.25335 0.04151  287 ALA   A O   
2128 C  CB  . ALA   A 287 ? 0.89089 0.99881 1.00407 -0.07307 -0.28452 0.04076  287 ALA   A CB  
2129 N  N   . TYR   A 288 ? 0.69900 0.79909 0.77518 -0.05138 -0.27405 0.02404  288 TYR   A N   
2130 C  CA  . TYR   A 288 ? 0.73324 0.83426 0.79301 -0.03993 -0.26051 0.01686  288 TYR   A CA  
2131 C  C   . TYR   A 288 ? 0.74301 0.86089 0.81163 -0.03987 -0.26014 0.02408  288 TYR   A C   
2132 O  O   . TYR   A 288 ? 0.70415 0.83751 0.77535 -0.03438 -0.24491 0.02636  288 TYR   A O   
2133 C  CB  . TYR   A 288 ? 0.67269 0.74752 0.70381 -0.03200 -0.26643 0.00261  288 TYR   A CB  
2134 C  CG  . TYR   A 288 ? 0.67565 0.73566 0.69318 -0.02737 -0.26144 -0.00692 288 TYR   A CG  
2135 C  CD1 . TYR   A 288 ? 0.75904 0.80458 0.75066 -0.01650 -0.25726 -0.01933 288 TYR   A CD1 
2136 C  CD2 . TYR   A 288 ? 0.73762 0.80050 0.76838 -0.03328 -0.25986 -0.00293 288 TYR   A CD2 
2137 C  CE1 . TYR   A 288 ? 0.77472 0.80920 0.75421 -0.01131 -0.25214 -0.02782 288 TYR   A CE1 
2138 C  CE2 . TYR   A 288 ? 0.75804 0.80778 0.77617 -0.02835 -0.25518 -0.01183 288 TYR   A CE2 
2139 C  CZ  . TYR   A 288 ? 0.70355 0.73969 0.69641 -0.01719 -0.25124 -0.02426 288 TYR   A CZ  
2140 O  OH  . TYR   A 288 ? 0.76460 0.78997 0.74548 -0.01159 -0.24631 -0.03280 288 TYR   A OH  
2141 N  N   . ALA   A 289 ? 0.74919 0.86445 0.82347 -0.04619 -0.27757 0.02831  289 ALA   A N   
2142 C  CA  . ALA   A 289 ? 0.65812 0.79036 0.74180 -0.04611 -0.27801 0.03558  289 ALA   A CA  
2143 C  C   . ALA   A 289 ? 0.64451 0.80671 0.75124 -0.04760 -0.26452 0.04704  289 ALA   A C   
2144 O  O   . ALA   A 289 ? 0.73498 0.90925 0.84018 -0.04012 -0.25167 0.04745  289 ALA   A O   
2145 C  CB  . ALA   A 289 ? 0.74891 0.87628 0.83990 -0.05496 -0.30003 0.04055  289 ALA   A CB  
2146 N  N   . LYS   A 290 ? 0.71098 0.88432 0.83732 -0.05625 -0.26645 0.05572  290 LYS   A N   
2147 C  CA  . LYS   A 290 ? 0.78438 0.98843 0.93365 -0.05769 -0.25555 0.06766  290 LYS   A CA  
2148 C  C   . LYS   A 290 ? 0.77474 0.98500 0.91865 -0.04861 -0.23439 0.06372  290 LYS   A C   
2149 O  O   . LYS   A 290 ? 0.68977 0.92282 0.84501 -0.04460 -0.22351 0.07025  290 LYS   A O   
2150 C  CB  . LYS   A 290 ? 0.76931 0.98441 0.94108 -0.07029 -0.26462 0.07916  290 LYS   A CB  
2151 C  CG  . LYS   A 290 ? 0.77425 1.01404 0.96256 -0.06976 -0.24918 0.08716  290 LYS   A CG  
2152 C  CD  . LYS   A 290 ? 0.91899 1.16815 1.12728 -0.08219 -0.25675 0.09809  290 LYS   A CD  
2153 C  CE  . LYS   A 290 ? 0.94719 1.23398 1.18094 -0.08388 -0.24760 0.11291  290 LYS   A CE  
2154 N  NZ  . LYS   A 290 ? 0.86799 1.16474 1.12051 -0.09611 -0.25366 0.12416  290 LYS   A NZ  
2155 N  N   . SER   A 291 ? 0.71338 0.90489 0.84118 -0.04519 -0.22865 0.05371  291 SER   A N   
2156 C  CA  . SER   A 291 ? 0.75840 0.95773 0.88492 -0.03867 -0.20996 0.05203  291 SER   A CA  
2157 C  C   . SER   A 291 ? 0.70691 0.89620 0.81211 -0.02765 -0.19890 0.04219  291 SER   A C   
2158 O  O   . SER   A 291 ? 0.65251 0.85216 0.75869 -0.02173 -0.18416 0.04292  291 SER   A O   
2159 C  CB  . SER   A 291 ? 0.67202 0.86183 0.79801 -0.04238 -0.20866 0.04932  291 SER   A CB  
2160 O  OG  . SER   A 291 ? 0.72283 0.92231 0.86900 -0.05343 -0.21910 0.05966  291 SER   A OG  
2161 N  N   . ILE   A 292 ? 0.69411 0.86388 0.78016 -0.02489 -0.20624 0.03360  292 ILE   A N   
2162 C  CA  . ILE   A 292 ? 0.68722 0.84750 0.75232 -0.01542 -0.19744 0.02520  292 ILE   A CA  
2163 C  C   . ILE   A 292 ? 0.73240 0.89558 0.79369 -0.01247 -0.20242 0.02675  292 ILE   A C   
2164 O  O   . ILE   A 292 ? 0.67133 0.84377 0.73162 -0.00663 -0.19279 0.02856  292 ILE   A O   
2165 C  CB  . ILE   A 292 ? 0.61523 0.75197 0.65882 -0.01289 -0.20042 0.01367  292 ILE   A CB  
2166 C  CG1 . ILE   A 292 ? 0.67449 0.80961 0.72063 -0.01388 -0.19238 0.01174  292 ILE   A CG1 
2167 C  CG2 . ILE   A 292 ? 0.68517 0.81304 0.70667 -0.00409 -0.19428 0.00614  292 ILE   A CG2 
2168 C  CD1 . ILE   A 292 ? 0.66027 0.77402 0.68760 -0.01132 -0.19650 0.00096  292 ILE   A CD1 
2169 N  N   . ILE   A 293 ? 0.68209 0.83754 0.74228 -0.01676 -0.21841 0.02669  293 ILE   A N   
2170 C  CA  . ILE   A 293 ? 0.78013 0.93409 0.83236 -0.01332 -0.22406 0.02621  293 ILE   A CA  
2171 C  C   . ILE   A 293 ? 0.74514 0.92269 0.81742 -0.01445 -0.22283 0.03717  293 ILE   A C   
2172 O  O   . ILE   A 293 ? 0.74810 0.93121 0.81550 -0.00785 -0.21643 0.03759  293 ILE   A O   
2173 C  CB  . ILE   A 293 ? 0.76033 0.89678 0.80364 -0.01718 -0.24243 0.02192  293 ILE   A CB  
2174 C  CG1 . ILE   A 293 ? 0.69188 0.80661 0.71320 -0.01302 -0.24102 0.01011  293 ILE   A CG1 
2175 C  CG2 . ILE   A 293 ? 0.73208 0.86735 0.76789 -0.01411 -0.24919 0.02188  293 ILE   A CG2 
2176 C  CD1 . ILE   A 293 ? 0.63127 0.72613 0.64383 -0.01654 -0.25907 0.00467  293 ILE   A CD1 
2177 N  N   . PHE   A 294 ? 0.72987 0.92247 0.82498 -0.02249 -0.22892 0.04661  294 PHE   A N   
2178 C  CA  . PHE   A 294 ? 0.74955 0.96730 0.86415 -0.02269 -0.22796 0.05738  294 PHE   A CA  
2179 C  C   . PHE   A 294 ? 0.78295 1.01418 0.89894 -0.01410 -0.21054 0.05861  294 PHE   A C   
2180 O  O   . PHE   A 294 ? 0.75750 0.99911 0.87511 -0.00854 -0.20851 0.06160  294 PHE   A O   
2181 C  CB  . PHE   A 294 ? 0.72974 0.96450 0.86980 -0.03321 -0.23653 0.06867  294 PHE   A CB  
2182 C  CG  . PHE   A 294 ? 0.85443 1.11764 1.01535 -0.03336 -0.23701 0.08046  294 PHE   A CG  
2183 C  CD1 . PHE   A 294 ? 0.80217 1.06734 0.96529 -0.03510 -0.24957 0.08347  294 PHE   A CD1 
2184 C  CD2 . PHE   A 294 ? 0.84575 1.13434 1.02363 -0.03103 -0.22516 0.08840  294 PHE   A CD2 
2185 C  CE1 . PHE   A 294 ? 0.88577 1.17880 1.06848 -0.03450 -0.24995 0.09445  294 PHE   A CE1 
2186 C  CE2 . PHE   A 294 ? 0.84388 1.16052 1.04051 -0.02968 -0.22530 0.09908  294 PHE   A CE2 
2187 C  CZ  . PHE   A 294 ? 0.93478 1.25421 1.13430 -0.03144 -0.23762 0.10227  294 PHE   A CZ  
2188 N  N   . PRO   A 295 ? 0.67937 0.91126 0.79529 -0.01243 -0.19852 0.05679  295 PRO   A N   
2189 C  CA  . PRO   A 295 ? 0.69928 0.94096 0.81398 -0.00354 -0.18335 0.05713  295 PRO   A CA  
2190 C  C   . PRO   A 295 ? 0.73651 0.96198 0.82820 0.00452  -0.17832 0.04879  295 PRO   A C   
2191 O  O   . PRO   A 295 ? 0.75433 0.98746 0.84500 0.01193  -0.17028 0.05033  295 PRO   A O   
2192 C  CB  . PRO   A 295 ? 0.70608 0.95005 0.82561 -0.00494 -0.17374 0.05691  295 PRO   A CB  
2193 C  CG  . PRO   A 295 ? 0.74603 0.98556 0.87343 -0.01528 -0.18434 0.05860  295 PRO   A CG  
2194 C  CD  . PRO   A 295 ? 0.67541 0.90066 0.79438 -0.01882 -0.19940 0.05549  295 PRO   A CD  
2195 N  N   . SER   A 296 ? 0.66642 0.87014 0.73931 0.00364  -0.18323 0.04038  296 SER   A N   
2196 C  CA  . SER   A 296 ? 0.69201 0.88188 0.74291 0.01057  -0.17883 0.03359  296 SER   A CA  
2197 C  C   . SER   A 296 ? 0.84799 1.04082 0.89664 0.01358  -0.18532 0.03613  296 SER   A C   
2198 O  O   . SER   A 296 ? 0.83302 1.02119 0.86875 0.02014  -0.17957 0.03396  296 SER   A O   
2199 C  CB  . SER   A 296 ? 0.63249 0.80095 0.66370 0.00969  -0.18262 0.02431  296 SER   A CB  
2200 O  OG  . SER   A 296 ? 0.78090 0.94430 0.80962 0.00894  -0.17496 0.02045  296 SER   A OG  
2201 N  N   . TYR   A 297 ? 0.83339 1.03247 0.89340 0.00848  -0.19817 0.04071  297 TYR   A N   
2202 C  CA  . TYR   A 297 ? 0.77996 0.98121 0.83773 0.01094  -0.20584 0.04293  297 TYR   A CA  
2203 C  C   . TYR   A 297 ? 0.85236 1.07824 0.93291 0.01094  -0.20736 0.05325  297 TYR   A C   
2204 O  O   . TYR   A 297 ? 0.84762 1.07778 0.92892 0.01298  -0.21426 0.05601  297 TYR   A O   
2205 C  CB  . TYR   A 297 ? 0.87778 1.06441 0.92671 0.00614  -0.22110 0.03908  297 TYR   A CB  
2206 C  CG  . TYR   A 297 ? 0.81925 0.98273 0.84244 0.00891  -0.21972 0.02839  297 TYR   A CG  
2207 C  CD1 . TYR   A 297 ? 0.93337 1.08695 0.93630 0.01548  -0.21723 0.02387  297 TYR   A CD1 
2208 C  CD2 . TYR   A 297 ? 0.91031 1.06272 0.92925 0.00528  -0.22122 0.02319  297 TYR   A CD2 
2209 C  CE1 . TYR   A 297 ? 0.87805 1.01359 0.85754 0.01849  -0.21543 0.01489  297 TYR   A CE1 
2210 C  CE2 . TYR   A 297 ? 0.87660 1.01007 0.87180 0.00914  -0.21966 0.01336  297 TYR   A CE2 
2211 C  CZ  . TYR   A 297 ? 0.87579 1.00211 0.85163 0.01577  -0.21642 0.00951  297 TYR   A CZ  
2212 O  OH  . TYR   A 297 ? 0.86662 0.97745 0.81947 0.01997  -0.21417 0.00065  297 TYR   A OH  
2213 N  N   . ASN   A 298 ? 0.83390 1.07721 0.93274 0.00935  -0.20090 0.05916  298 ASN   A N   
2214 C  CA  . ASN   A 298 ? 0.84565 1.11639 0.96830 0.00914  -0.20226 0.06993  298 ASN   A CA  
2215 C  C   . ASN   A 298 ? 0.86233 1.13971 0.99718 0.00120  -0.21826 0.07580  298 ASN   A C   
2216 O  O   . ASN   A 298 ? 0.85522 1.15589 1.00860 0.00129  -0.22142 0.08510  298 ASN   A O   
2217 C  CB  . ASN   A 298 ? 0.80938 1.08958 0.93014 0.01989  -0.19549 0.07155  298 ASN   A CB  
2218 C  CG  . ASN   A 298 ? 1.01564 1.29443 1.12978 0.02750  -0.18038 0.06838  298 ASN   A CG  
2219 O  OD1 . ASN   A 298 ? 0.92387 1.19065 1.03027 0.02524  -0.17430 0.06329  298 ASN   A OD1 
2220 N  ND2 . ASN   A 298 ? 1.14615 1.43672 1.26292 0.03701  -0.17494 0.07125  298 ASN   A ND2 
2221 N  N   . GLU   A 299 ? 0.94803 1.20556 1.07288 -0.00554 -0.22870 0.07061  299 GLU   A N   
2222 C  CA  . GLU   A 299 ? 0.92146 1.17830 1.05338 -0.01369 -0.24623 0.07436  299 GLU   A CA  
2223 C  C   . GLU   A 299 ? 0.88754 1.11928 1.00583 -0.01959 -0.25394 0.06648  299 GLU   A C   
2224 O  O   . GLU   A 299 ? 0.97296 1.18946 1.07534 -0.01590 -0.24500 0.05802  299 GLU   A O   
2225 C  CB  . GLU   A 299 ? 0.99402 1.24639 1.11604 -0.00888 -0.25286 0.07277  299 GLU   A CB  
2226 C  CG  . GLU   A 299 ? 1.04157 1.26648 1.13336 -0.00274 -0.24979 0.06046  299 GLU   A CG  
2227 C  CD  . GLU   A 299 ? 1.13539 1.35254 1.21470 0.00110  -0.25810 0.05834  299 GLU   A CD  
2228 O  OE1 . GLU   A 299 ? 1.05706 1.29139 1.14892 0.00305  -0.26084 0.06557  299 GLU   A OE1 
2229 O  OE2 . GLU   A 299 ? 1.12097 1.31529 1.17713 0.00289  -0.26145 0.04932  299 GLU   A OE2 
2230 N  N   . PHE   A 300 ? 0.79209 1.01880 0.91556 -0.02816 -0.27129 0.06900  300 PHE   A N   
2231 C  CA  . PHE   A 300 ? 0.90150 1.09948 1.00564 -0.03085 -0.28162 0.05924  300 PHE   A CA  
2232 C  C   . PHE   A 300 ? 0.94166 1.13163 1.03925 -0.03181 -0.29734 0.05858  300 PHE   A C   
2233 O  O   . PHE   A 300 ? 0.71635 0.91908 0.83261 -0.03948 -0.30978 0.06797  300 PHE   A O   
2234 C  CB  . PHE   A 300 ? 0.87474 1.06834 0.98914 -0.04115 -0.29006 0.06166  300 PHE   A CB  
2235 C  CG  . PHE   A 300 ? 0.89339 1.05559 0.98454 -0.04091 -0.29771 0.04944  300 PHE   A CG  
2236 C  CD1 . PHE   A 300 ? 0.82333 0.96638 0.90098 -0.04218 -0.31491 0.04435  300 PHE   A CD1 
2237 C  CD2 . PHE   A 300 ? 0.78738 0.93957 0.86959 -0.03852 -0.28781 0.04278  300 PHE   A CD2 
2238 C  CE1 . PHE   A 300 ? 0.83285 0.94755 0.88759 -0.04001 -0.32200 0.03246  300 PHE   A CE1 
2239 C  CE2 . PHE   A 300 ? 0.73350 0.85826 0.79392 -0.03678 -0.29469 0.03126  300 PHE   A CE2 
2240 C  CZ  . PHE   A 300 ? 0.78346 0.88951 0.82962 -0.03697 -0.31165 0.02587  300 PHE   A CZ  
2241 N  N   . ASN   A 301 ? 0.95108 1.12207 1.02299 -0.02400 -0.29650 0.04845  301 ASN   A N   
2242 C  CA  . ASN   A 301 ? 0.96121 1.12156 1.02331 -0.02413 -0.31175 0.04642  301 ASN   A CA  
2243 C  C   . ASN   A 301 ? 0.87838 1.01259 0.92532 -0.02790 -0.32599 0.03818  301 ASN   A C   
2244 O  O   . ASN   A 301 ? 0.88082 0.99574 0.90401 -0.02150 -0.32109 0.02704  301 ASN   A O   
2245 C  CB  . ASN   A 301 ? 1.06732 1.22224 1.10958 -0.01356 -0.30416 0.04083  301 ASN   A CB  
2246 C  CG  . ASN   A 301 ? 1.09973 1.24657 1.13363 -0.01351 -0.31990 0.04004  301 ASN   A CG  
2247 O  OD1 . ASN   A 301 ? 1.06459 1.22260 1.11639 -0.02021 -0.33274 0.04833  301 ASN   A OD1 
2248 N  ND2 . ASN   A 301 ? 1.19517 1.32306 1.20151 -0.00603 -0.31916 0.03034  301 ASN   A ND2 
2249 N  N   . LEU   A 302 ? 0.95246 1.08650 1.01296 -0.03797 -0.34430 0.04397  302 LEU   A N   
2250 C  CA  . LEU   A 302 ? 0.95697 1.06576 1.00587 -0.04276 -0.36182 0.03749  302 LEU   A CA  
2251 C  C   . LEU   A 302 ? 0.97543 1.06593 1.00313 -0.03833 -0.37490 0.03035  302 LEU   A C   
2252 O  O   . LEU   A 302 ? 0.97106 1.07008 1.00858 -0.04169 -0.38318 0.03690  302 LEU   A O   
2253 C  CB  . LEU   A 302 ? 0.88909 1.00658 0.96360 -0.05643 -0.37434 0.04840  302 LEU   A CB  
2254 C  CG  . LEU   A 302 ? 0.94815 1.03838 1.01329 -0.06202 -0.38687 0.04258  302 LEU   A CG  
2255 C  CD1 . LEU   A 302 ? 0.87162 0.94757 0.92373 -0.05854 -0.38231 0.03381  302 LEU   A CD1 
2256 C  CD2 . LEU   A 302 ? 0.91563 1.01631 1.00716 -0.07547 -0.39306 0.05518  302 LEU   A CD2 
2257 N  N   . VAL   A 303 ? 0.89256 0.95981 0.89075 -0.02956 -0.37313 0.01694  303 VAL   A N   
2258 C  CA  . VAL   A 303 ? 0.97681 1.02506 0.95242 -0.02475 -0.38650 0.00936  303 VAL   A CA  
2259 C  C   . VAL   A 303 ? 1.03091 1.05787 1.00356 -0.03086 -0.40062 0.00596  303 VAL   A C   
2260 O  O   . VAL   A 303 ? 0.91647 0.93222 0.88715 -0.03287 -0.40136 0.00205  303 VAL   A O   
2261 C  CB  . VAL   A 303 ? 1.03635 1.07117 0.98091 -0.01153 -0.37445 -0.00301 303 VAL   A CB  
2262 C  CG1 . VAL   A 303 ? 1.06614 1.08014 0.98544 -0.00615 -0.38957 -0.01142 303 VAL   A CG1 
2263 C  CG2 . VAL   A 303 ? 1.02282 1.07728 0.97095 -0.00573 -0.35328 0.00105  303 VAL   A CG2 
2264 N  N   . ARG   A 304 ? 1.01110 1.03296 0.98519 -0.03429 -0.41191 0.00839  304 ARG   A N   
2265 C  CA  . ARG   A 304 ? 1.06224 1.06190 1.03239 -0.03980 -0.42715 0.00575  304 ARG   A CA  
2266 C  C   . ARG   A 304 ? 0.94260 0.93238 0.89916 -0.03611 -0.43601 0.00261  304 ARG   A C   
2267 O  O   . ARG   A 304 ? 0.83193 0.83913 0.79500 -0.03463 -0.43229 0.00817  304 ARG   A O   
2268 C  CB  . ARG   A 304 ? 1.00002 1.01048 1.00056 -0.05433 -0.43371 0.01871  304 ARG   A CB  
2269 C  CG  . ARG   A 304 ? 1.15346 1.17457 1.17064 -0.05993 -0.42622 0.02377  304 ARG   A CG  
2270 C  CD  . ARG   A 304 ? 1.22416 1.25477 1.26970 -0.07462 -0.43327 0.03718  304 ARG   A CD  
2271 N  NE  . ARG   A 304 ? 1.19686 1.25758 1.26766 -0.08015 -0.43029 0.05088  304 ARG   A NE  
2272 C  CZ  . ARG   A 304 ? 1.14953 1.23017 1.24883 -0.09146 -0.43022 0.06492  304 ARG   A CZ  
2273 N  NH1 . ARG   A 304 ? 1.20215 1.27550 1.30929 -0.09960 -0.43339 0.06807  304 ARG   A NH1 
2274 N  NH2 . ARG   A 304 ? 1.04990 1.15892 1.16988 -0.09418 -0.42662 0.07628  304 ARG   A NH2 
2275 N  N   . LYS   A 305 ? 1.16276 1.12418 1.10110 -0.03463 -0.44839 -0.00595 305 LYS   A N   
2276 C  CA  . LYS   A 305 ? 1.12550 1.07564 1.05307 -0.03286 -0.45930 -0.00809 305 LYS   A CA  
2277 C  C   . LYS   A 305 ? 1.07346 1.03976 1.02960 -0.04512 -0.46671 0.00592  305 LYS   A C   
2278 O  O   . LYS   A 305 ? 1.10902 1.08458 1.08903 -0.05608 -0.46870 0.01538  305 LYS   A O   
2279 C  CB  . LYS   A 305 ? 1.24198 1.15757 1.14620 -0.02922 -0.47228 -0.01944 305 LYS   A CB  
2280 C  CG  . LYS   A 305 ? 1.13878 1.03702 1.01317 -0.01604 -0.46592 -0.03408 305 LYS   A CG  
2281 C  CD  . LYS   A 305 ? 1.08950 0.98572 0.93827 -0.00321 -0.46067 -0.04205 305 LYS   A CD  
2282 C  CE  . LYS   A 305 ? 1.18614 1.09706 1.02759 0.00476  -0.44279 -0.04477 305 LYS   A CE  
2283 N  NZ  . LYS   A 305 ? 0.83615 0.77652 0.70535 -0.00266 -0.43329 -0.03229 305 LYS   A NZ  
2284 N  N   . GLU   A 306 ? 1.02555 0.99534 0.97876 -0.04316 -0.47092 0.00747  306 GLU   A N   
2285 C  CA  . GLU   A 306 ? 1.20578 1.19190 1.18527 -0.05394 -0.47804 0.02062  306 GLU   A CA  
2286 C  C   . GLU   A 306 ? 1.14892 1.11945 1.13815 -0.06522 -0.49301 0.02440  306 GLU   A C   
2287 O  O   . GLU   A 306 ? 1.19787 1.18579 1.21467 -0.07673 -0.49660 0.03773  306 GLU   A O   
2288 C  CB  . GLU   A 306 ? 1.08565 1.07303 1.05613 -0.04894 -0.48189 0.01974  306 GLU   A CB  
2289 C  CG  . GLU   A 306 ? 1.22412 1.23568 1.19670 -0.04162 -0.46678 0.02218  306 GLU   A CG  
2290 C  CD  . GLU   A 306 ? 1.43831 1.46101 1.41370 -0.03981 -0.46944 0.02667  306 GLU   A CD  
2291 O  OE1 . GLU   A 306 ? 1.59450 1.59823 1.55308 -0.03740 -0.48026 0.02098  306 GLU   A OE1 
2292 O  OE2 . GLU   A 306 ? 1.42155 1.47207 1.41571 -0.04013 -0.46061 0.03580  306 GLU   A OE2 
2293 N  N   . LYS   A 307 ? 1.17471 1.11242 1.14111 -0.06164 -0.50216 0.01315  307 LYS   A N   
2294 C  CA  . LYS   A 307 ? 1.14967 1.06709 1.12157 -0.07130 -0.51771 0.01565  307 LYS   A CA  
2295 C  C   . LYS   A 307 ? 1.17529 1.10104 1.16725 -0.08045 -0.51387 0.02315  307 LYS   A C   
2296 O  O   . LYS   A 307 ? 1.12911 1.04634 1.13427 -0.09178 -0.52584 0.03053  307 LYS   A O   
2297 C  CB  . LYS   A 307 ? 1.14353 1.02263 1.08206 -0.06186 -0.52781 0.00002  307 LYS   A CB  
2298 C  CG  . LYS   A 307 ? 1.23069 1.10065 1.14558 -0.04889 -0.51636 -0.01329 307 LYS   A CG  
2299 C  CD  . LYS   A 307 ? 1.11420 0.94827 0.99573 -0.03796 -0.52616 -0.02863 307 LYS   A CD  
2300 C  CE  . LYS   A 307 ? 1.19207 1.02691 1.04746 -0.02199 -0.51232 -0.04081 307 LYS   A CE  
2301 N  NZ  . LYS   A 307 ? 0.93690 0.78503 0.78664 -0.01711 -0.50838 -0.03984 307 LYS   A NZ  
2302 N  N   . ASN   A 308 ? 1.12901 1.07024 1.12286 -0.07588 -0.49793 0.02172  308 ASN   A N   
2303 C  CA  . ASN   A 308 ? 1.16059 1.11538 1.17520 -0.08391 -0.49144 0.02978  308 ASN   A CA  
2304 C  C   . ASN   A 308 ? 1.11580 1.11072 1.16005 -0.08949 -0.47926 0.04399  308 ASN   A C   
2305 O  O   . ASN   A 308 ? 1.08939 1.09981 1.14928 -0.09359 -0.47010 0.04990  308 ASN   A O   
2306 C  CB  . ASN   A 308 ? 1.03399 0.97812 1.03068 -0.07477 -0.48205 0.01838  308 ASN   A CB  
2307 C  CG  . ASN   A 308 ? 1.07651 0.98262 1.04845 -0.07033 -0.49370 0.00601  308 ASN   A CG  
2308 O  OD1 . ASN   A 308 ? 1.17821 1.06588 1.15294 -0.07781 -0.50920 0.00881  308 ASN   A OD1 
2309 N  ND2 . ASN   A 308 ? 1.09829 0.99252 1.04570 -0.05765 -0.48639 -0.00747 308 ASN   A ND2 
2310 N  N   . GLY   A 309 ? 1.12311 1.13542 1.17472 -0.08871 -0.47849 0.04925  309 GLY   A N   
2311 C  CA  . GLY   A 309 ? 1.02597 1.07644 1.10418 -0.09180 -0.46695 0.06199  309 GLY   A CA  
2312 C  C   . GLY   A 309 ? 1.04185 1.10732 1.11185 -0.08013 -0.45466 0.05807  309 GLY   A C   
2313 O  O   . GLY   A 309 ? 1.00671 1.10185 1.09658 -0.08110 -0.44766 0.06812  309 GLY   A O   
2314 N  N   . GLY   A 310 ? 1.03602 1.08172 1.07669 -0.06870 -0.45232 0.04412  310 GLY   A N   
2315 C  CA  . GLY   A 310 ? 0.99994 1.05792 1.03122 -0.05777 -0.44028 0.04073  310 GLY   A CA  
2316 C  C   . GLY   A 310 ? 1.02956 1.10747 1.07137 -0.05562 -0.42457 0.04391  310 GLY   A C   
2317 O  O   . GLY   A 310 ? 0.99517 1.08376 1.05668 -0.06350 -0.42190 0.05107  310 GLY   A O   
2318 N  N   . ASP   A 311 ? 1.00377 1.08582 1.03167 -0.04492 -0.41430 0.03878  311 ASP   A N   
2319 C  CA  . ASP   A 311 ? 0.82759 0.92729 0.86358 -0.04177 -0.39967 0.04147  311 ASP   A CA  
2320 C  C   . ASP   A 311 ? 0.90273 1.03526 0.97292 -0.04882 -0.39433 0.05657  311 ASP   A C   
2321 O  O   . ASP   A 311 ? 0.93570 1.08132 1.02040 -0.05266 -0.39928 0.06453  311 ASP   A O   
2322 C  CB  . ASP   A 311 ? 0.84076 0.94035 0.85746 -0.02970 -0.39136 0.03562  311 ASP   A CB  
2323 C  CG  . ASP   A 311 ? 0.99634 1.06656 0.97837 -0.02174 -0.39616 0.02152  311 ASP   A CG  
2324 O  OD1 . ASP   A 311 ? 1.07946 1.14774 1.04305 -0.01195 -0.38933 0.01653  311 ASP   A OD1 
2325 O  OD2 . ASP   A 311 ? 1.06364 1.11289 1.03626 -0.02475 -0.40678 0.01578  311 ASP   A OD2 
2326 N  N   . LYS   A 312 ? 0.98927 1.13614 1.07267 -0.05027 -0.38395 0.06074  312 LYS   A N   
2327 C  CA  . LYS   A 312 ? 0.92574 1.10565 1.04035 -0.05526 -0.37701 0.07484  312 LYS   A CA  
2328 C  C   . LYS   A 312 ? 0.96972 1.16474 1.09065 -0.05121 -0.36227 0.07662  312 LYS   A C   
2329 O  O   . LYS   A 312 ? 0.99136 1.17154 1.10127 -0.05067 -0.35861 0.06963  312 LYS   A O   
2330 C  CB  . LYS   A 312 ? 0.82336 1.00676 0.95777 -0.06819 -0.38481 0.08312  312 LYS   A CB  
2331 C  CG  . LYS   A 312 ? 0.89289 1.11186 1.05862 -0.07277 -0.37596 0.09769  312 LYS   A CG  
2332 C  CD  . LYS   A 312 ? 0.91520 1.13711 1.09937 -0.08612 -0.38401 0.10684  312 LYS   A CD  
2333 C  CE  . LYS   A 312 ? 0.93095 1.18907 1.14448 -0.08975 -0.37322 0.12104  312 LYS   A CE  
2334 N  NZ  . LYS   A 312 ? 0.97988 1.24107 1.21114 -0.10360 -0.38100 0.13129  312 LYS   A NZ  
2335 N  N   . THR   A 313 ? 0.87117 1.09505 1.00919 -0.04756 -0.35211 0.08545  313 THR   A N   
2336 C  CA  . THR   A 313 ? 0.95626 1.19213 1.09801 -0.04191 -0.33136 0.08548  313 THR   A CA  
2337 C  C   . THR   A 313 ? 0.87986 1.14336 1.05202 -0.05008 -0.32954 0.09862  313 THR   A C   
2338 O  O   . THR   A 313 ? 0.75675 1.04332 0.94999 -0.05383 -0.33274 0.10949  313 THR   A O   
2339 C  CB  . THR   A 313 ? 0.97770 1.22419 1.11394 -0.02977 -0.31684 0.08441  313 THR   A CB  
2340 O  OG1 . THR   A 313 ? 1.04524 1.26707 1.15307 -0.02270 -0.31821 0.07322  313 THR   A OG1 
2341 C  CG2 . THR   A 313 ? 0.90375 1.15820 1.04143 -0.02429 -0.29697 0.08329  313 THR   A CG2 
2342 N  N   . TYR   A 314 ? 0.81558 1.07502 0.98785 -0.05205 -0.32131 0.09649  314 TYR   A N   
2343 C  CA  . TYR   A 314 ? 0.91342 1.19941 1.11187 -0.05797 -0.31567 0.10820  314 TYR   A CA  
2344 C  C   . TYR   A 314 ? 0.84654 1.14873 1.04547 -0.04653 -0.29408 0.10771  314 TYR   A C   
2345 O  O   . TYR   A 314 ? 0.85050 1.13495 1.02811 -0.03807 -0.28282 0.09660  314 TYR   A O   
2346 C  CB  . TYR   A 314 ? 0.74234 1.01386 0.94075 -0.06705 -0.32056 0.10660  314 TYR   A CB  
2347 C  CG  . TYR   A 314 ? 0.76940 1.02164 0.96542 -0.07684 -0.33742 0.10603  314 TYR   A CG  
2348 C  CD1 . TYR   A 314 ? 0.84065 1.06153 1.01172 -0.07448 -0.34875 0.09415  314 TYR   A CD1 
2349 C  CD2 . TYR   A 314 ? 0.92884 1.19432 1.14634 -0.08757 -0.34138 0.11756  314 TYR   A CD2 
2350 C  CE1 . TYR   A 314 ? 0.95289 1.15507 1.12045 -0.08221 -0.36373 0.09325  314 TYR   A CE1 
2351 C  CE2 . TYR   A 314 ? 0.90089 1.14763 1.11575 -0.09646 -0.35697 0.11765  314 TYR   A CE2 
2352 C  CZ  . TYR   A 314 ? 0.90542 1.12006 1.09526 -0.09352 -0.36819 0.10521  314 TYR   A CZ  
2353 O  OH  . TYR   A 314 ? 0.98656 1.18086 1.17246 -0.10149 -0.38391 0.10480  314 TYR   A OH  
2354 N  N   . TYR   A 315 ? 0.84864 1.18438 1.07070 -0.04544 -0.28934 0.11968  315 TYR   A N   
2355 C  CA  . TYR   A 315 ? 0.86462 1.21708 1.08804 -0.03368 -0.27060 0.11987  315 TYR   A CA  
2356 C  C   . TYR   A 315 ? 0.93243 1.30518 1.17306 -0.03615 -0.26051 0.12705  315 TYR   A C   
2357 O  O   . TYR   A 315 ? 0.88271 1.26487 1.12137 -0.02607 -0.24452 0.12541  315 TYR   A O   
2358 C  CB  . TYR   A 315 ? 0.83008 1.20592 1.06399 -0.02697 -0.27111 0.12672  315 TYR   A CB  
2359 C  CG  . TYR   A 315 ? 0.87024 1.22517 1.08433 -0.02244 -0.27864 0.11870  315 TYR   A CG  
2360 C  CD1 . TYR   A 315 ? 0.96711 1.29780 1.15442 -0.01301 -0.26983 0.10614  315 TYR   A CD1 
2361 C  CD2 . TYR   A 315 ? 0.88704 1.24612 1.10894 -0.02834 -0.29524 0.12411  315 TYR   A CD2 
2362 C  CE1 . TYR   A 315 ? 0.93781 1.25007 1.10642 -0.00906 -0.27656 0.09945  315 TYR   A CE1 
2363 C  CE2 . TYR   A 315 ? 0.86622 1.20558 1.06888 -0.02400 -0.30233 0.11664  315 TYR   A CE2 
2364 C  CZ  . TYR   A 315 ? 0.92775 1.24400 1.10358 -0.01424 -0.29261 0.10437  315 TYR   A CZ  
2365 O  OH  . TYR   A 315 ? 0.87627 1.17370 1.03229 -0.00991 -0.29901 0.09748  315 TYR   A OH  
2366 N  N   . THR   A 316 ? 0.98674 1.36478 1.24290 -0.04929 -0.27009 0.13479  316 THR   A N   
2367 C  CA  . THR   A 316 ? 0.95512 1.34924 1.22603 -0.05323 -0.26191 0.14148  316 THR   A CA  
2368 C  C   . THR   A 316 ? 0.93675 1.30688 1.20253 -0.06502 -0.27164 0.13825  316 THR   A C   
2369 O  O   . THR   A 316 ? 0.95102 1.30033 1.20979 -0.07217 -0.28606 0.13520  316 THR   A O   
2370 C  CB  . THR   A 316 ? 0.99601 1.42173 1.29119 -0.05602 -0.25682 0.15479  316 THR   A CB  
2371 O  OG1 . THR   A 316 ? 1.02448 1.44470 1.32704 -0.06808 -0.27021 0.16001  316 THR   A OG1 
2372 C  CG2 . THR   A 316 ? 1.01032 1.45953 1.31012 -0.04316 -0.24825 0.15748  316 THR   A CG2 
2373 N  N   . LEU   A 317 ? 0.94388 1.31364 1.21039 -0.06572 -0.26219 0.13740  317 LEU   A N   
2374 C  CA  . LEU   A 317 ? 0.97479 1.32470 1.23909 -0.07701 -0.27202 0.13586  317 LEU   A CA  
2375 C  C   . LEU   A 317 ? 0.98899 1.34519 1.26972 -0.08936 -0.27980 0.14647  317 LEU   A C   
2376 O  O   . LEU   A 317 ? 0.97152 1.30371 1.24631 -0.09881 -0.29292 0.14400  317 LEU   A O   
2377 C  CB  . LEU   A 317 ? 0.90156 1.24959 1.16235 -0.07399 -0.25729 0.13235  317 LEU   A CB  
2378 C  CG  . LEU   A 317 ? 0.84964 1.17543 1.08363 -0.06095 -0.24376 0.11649  317 LEU   A CG  
2379 C  CD1 . LEU   A 317 ? 0.85375 1.17775 1.08488 -0.05845 -0.23016 0.11336  317 LEU   A CD1 
2380 C  CD2 . LEU   A 317 ? 0.85263 1.14344 1.06250 -0.06067 -0.25396 0.10368  317 LEU   A CD2 
2381 N  N   . GLN   A 318 ? 1.00042 1.38788 1.30070 -0.08904 -0.27244 0.15837  318 GLN   A N   
2382 C  CA  . GLN   A 318 ? 0.99799 1.39311 1.31398 -0.10109 -0.28022 0.16994  318 GLN   A CA  
2383 C  C   . GLN   A 318 ? 1.04273 1.41827 1.35122 -0.10591 -0.29695 0.16681  318 GLN   A C   
2384 O  O   . GLN   A 318 ? 1.02213 1.38163 1.33183 -0.11779 -0.30972 0.16979  318 GLN   A O   
2385 C  CB  . GLN   A 318 ? 1.05908 1.49300 1.39544 -0.09770 -0.26843 0.18266  318 GLN   A CB  
2386 C  CG  . GLN   A 318 ? 1.04945 1.49864 1.40515 -0.11045 -0.27244 0.19796  318 GLN   A CG  
2387 C  CD  . GLN   A 318 ? 1.10130 1.55164 1.46321 -0.11664 -0.28506 0.20365  318 GLN   A CD  
2388 O  OE1 . GLN   A 318 ? 1.07155 1.52318 1.42833 -0.10887 -0.28683 0.19880  318 GLN   A OE1 
2389 N  NE2 . GLN   A 318 ? 1.04438 1.49483 1.41771 -0.13083 -0.29391 0.21484  318 GLN   A NE2 
2390 N  N   . GLU   A 319 ? 0.99801 1.37262 1.29716 -0.09644 -0.29749 0.16047  319 GLU   A N   
2391 C  CA  . GLU   A 319 ? 1.00820 1.36356 1.29782 -0.09933 -0.31274 0.15627  319 GLU   A CA  
2392 C  C   . GLU   A 319 ? 0.99326 1.30940 1.26208 -0.10368 -0.32532 0.14484  319 GLU   A C   
2393 O  O   . GLU   A 319 ? 0.91596 1.21415 1.18250 -0.11270 -0.33995 0.14550  319 GLU   A O   
2394 C  CB  . GLU   A 319 ? 0.98018 1.34166 1.26152 -0.08673 -0.30904 0.15091  319 GLU   A CB  
2395 C  CG  . GLU   A 319 ? 1.07556 1.42004 1.34657 -0.08780 -0.32318 0.14655  319 GLU   A CG  
2396 C  CD  . GLU   A 319 ? 1.06729 1.41946 1.33056 -0.07489 -0.31841 0.14228  319 GLU   A CD  
2397 O  OE1 . GLU   A 319 ? 1.01656 1.38266 1.27976 -0.06507 -0.30481 0.14132  319 GLU   A OE1 
2398 O  OE2 . GLU   A 319 ? 1.02721 1.37003 1.28349 -0.07447 -0.32857 0.13979  319 GLU   A OE2 
2399 N  N   . LEU   A 320 ? 0.99391 1.29578 1.24636 -0.09666 -0.32001 0.13406  320 LEU   A N   
2400 C  CA  . LEU   A 320 ? 0.97232 1.23732 1.20302 -0.09867 -0.33075 0.12202  320 LEU   A CA  
2401 C  C   . LEU   A 320 ? 1.03722 1.29054 1.27432 -0.11094 -0.33828 0.12638  320 LEU   A C   
2402 O  O   . LEU   A 320 ? 0.99516 1.22023 1.22058 -0.11635 -0.35306 0.12130  320 LEU   A O   
2403 C  CB  . LEU   A 320 ? 0.93819 1.19485 1.15295 -0.08914 -0.32186 0.11157  320 LEU   A CB  
2404 C  CG  . LEU   A 320 ? 0.92973 1.14849 1.11953 -0.08906 -0.33238 0.09783  320 LEU   A CG  
2405 C  CD1 . LEU   A 320 ? 0.81527 1.01504 0.98478 -0.08334 -0.34187 0.08865  320 LEU   A CD1 
2406 C  CD2 . LEU   A 320 ? 0.88962 1.09919 1.06664 -0.08235 -0.31891 0.08890  320 LEU   A CD2 
2407 N  N   . GLU   A 321 ? 1.01557 1.28957 1.27015 -0.11484 -0.32828 0.13581  321 GLU   A N   
2408 C  CA  . GLU   A 321 ? 1.08904 1.35390 1.35070 -0.12662 -0.33434 0.14159  321 GLU   A CA  
2409 C  C   . GLU   A 321 ? 1.14205 1.40671 1.41483 -0.13776 -0.34709 0.15172  321 GLU   A C   
2410 O  O   . GLU   A 321 ? 1.24551 1.48392 1.51191 -0.14630 -0.36104 0.15048  321 GLU   A O   
2411 C  CB  . GLU   A 321 ? 1.05618 1.34733 1.33480 -0.12757 -0.31949 0.15081  321 GLU   A CB  
2412 C  CG  . GLU   A 321 ? 1.17507 1.46432 1.46583 -0.14086 -0.32475 0.16128  321 GLU   A CG  
2413 C  CD  . GLU   A 321 ? 1.29055 1.60611 1.59649 -0.14097 -0.30932 0.17022  321 GLU   A CD  
2414 O  OE1 . GLU   A 321 ? 1.23096 1.55227 1.53130 -0.13139 -0.29697 0.16349  321 GLU   A OE1 
2415 O  OE2 . GLU   A 321 ? 1.37076 1.70148 1.69381 -0.15057 -0.30960 0.18447  321 GLU   A OE2 
2416 N  N   . HIS   A 322 ? 1.14958 1.44296 1.43874 -0.13748 -0.34284 0.16197  322 HIS   A N   
2417 C  CA  . HIS   A 322 ? 1.16223 1.45739 1.46237 -0.14777 -0.35501 0.17215  322 HIS   A CA  
2418 C  C   . HIS   A 322 ? 1.19255 1.45248 1.47349 -0.14913 -0.37257 0.16198  322 HIS   A C   
2419 O  O   . HIS   A 322 ? 1.24749 1.48923 1.52908 -0.16002 -0.38694 0.16608  322 HIS   A O   
2420 C  CB  . HIS   A 322 ? 1.16692 1.49828 1.48441 -0.14405 -0.34683 0.18208  322 HIS   A CB  
2421 C  CG  . HIS   A 322 ? 1.29149 1.62473 1.61821 -0.15277 -0.35965 0.19094  322 HIS   A CG  
2422 N  ND1 . HIS   A 322 ? 1.29121 1.60904 1.60621 -0.14978 -0.37024 0.18368  322 HIS   A ND1 
2423 C  CD2 . HIS   A 322 ? 1.32041 1.66955 1.66681 -0.16452 -0.36366 0.20707  322 HIS   A CD2 
2424 C  CE1 . HIS   A 322 ? 1.29571 1.61948 1.62323 -0.15936 -0.38043 0.19457  322 HIS   A CE1 
2425 N  NE2 . HIS   A 322 ? 1.35471 1.69764 1.70155 -0.16862 -0.37678 0.20917  322 HIS   A NE2 
2426 N  N   . ASP   A 323 ? 1.14646 1.39541 1.40916 -0.13792 -0.37208 0.14892  323 ASP   A N   
2427 C  CA  . ASP   A 323 ? 1.17329 1.38999 1.41704 -0.13844 -0.38849 0.13959  323 ASP   A CA  
2428 C  C   . ASP   A 323 ? 1.23656 1.41621 1.46177 -0.14104 -0.39825 0.12969  323 ASP   A C   
2429 O  O   . ASP   A 323 ? 1.29967 1.45374 1.51686 -0.14709 -0.41443 0.12796  323 ASP   A O   
2430 C  CB  . ASP   A 323 ? 1.08645 1.30002 1.31382 -0.12580 -0.38598 0.12863  323 ASP   A CB  
2431 C  CG  . ASP   A 323 ? 1.09064 1.32534 1.33020 -0.12551 -0.38693 0.13641  323 ASP   A CG  
2432 O  OD1 . ASP   A 323 ? 1.14588 1.40258 1.40840 -0.13421 -0.38691 0.15086  323 ASP   A OD1 
2433 O  OD2 . ASP   A 323 ? 1.10348 1.33244 1.32914 -0.11664 -0.38805 0.12834  323 ASP   A OD2 
2434 N  N   . TYR   A 324 ? 1.16831 1.34323 1.38556 -0.13595 -0.38930 0.12270  324 TYR   A N   
2435 C  CA  . TYR   A 324 ? 1.26501 1.40326 1.46301 -0.13717 -0.39953 0.11231  324 TYR   A CA  
2436 C  C   . TYR   A 324 ? 1.24612 1.37860 1.45730 -0.15083 -0.40764 0.12303  324 TYR   A C   
2437 O  O   . TYR   A 324 ? 1.23404 1.33544 1.43370 -0.15549 -0.42355 0.11919  324 TYR   A O   
2438 C  CB  . TYR   A 324 ? 1.30086 1.43216 1.48328 -0.12691 -0.38909 0.10008  324 TYR   A CB  
2439 C  CG  . TYR   A 324 ? 1.30729 1.39865 1.46386 -0.12391 -0.39956 0.08562  324 TYR   A CG  
2440 C  CD1 . TYR   A 324 ? 1.31945 1.38468 1.45221 -0.11723 -0.40989 0.07334  324 TYR   A CD1 
2441 C  CD2 . TYR   A 324 ? 1.21855 1.29889 1.37334 -0.12633 -0.39837 0.08368  324 TYR   A CD2 
2442 C  CE1 . TYR   A 324 ? 1.30784 1.33738 1.41579 -0.11262 -0.41876 0.05963  324 TYR   A CE1 
2443 C  CE2 . TYR   A 324 ? 1.21713 1.26144 1.34766 -0.12201 -0.40758 0.06995  324 TYR   A CE2 
2444 C  CZ  . TYR   A 324 ? 1.26603 1.28530 1.37300 -0.11474 -0.41754 0.05784  324 TYR   A CZ  
2445 O  OH  . TYR   A 324 ? 1.17001 1.15442 1.25205 -0.10881 -0.42600 0.04391  324 TYR   A OH  
2446 N  N   . VAL   A 325 ? 1.21446 1.37621 1.44932 -0.15723 -0.39759 0.13717  325 VAL   A N   
2447 C  CA  . VAL   A 325 ? 1.22287 1.37976 1.46981 -0.17043 -0.40470 0.14850  325 VAL   A CA  
2448 C  C   . VAL   A 325 ? 1.21825 1.36609 1.47119 -0.18096 -0.42135 0.15728  325 VAL   A C   
2449 O  O   . VAL   A 325 ? 1.13383 1.26130 1.38709 -0.19106 -0.43406 0.16223  325 VAL   A O   
2450 C  CB  . VAL   A 325 ? 1.11489 1.30835 1.38578 -0.17436 -0.38937 0.16281  325 VAL   A CB  
2451 C  CG1 . VAL   A 325 ? 0.99032 1.18870 1.27908 -0.18955 -0.39765 0.18004  325 VAL   A CG1 
2452 C  CG2 . VAL   A 325 ? 1.15136 1.34088 1.41546 -0.16928 -0.37905 0.15577  325 VAL   A CG2 
2453 N  N   . ASN   A 326 ? 1.23601 1.39890 1.49429 -0.17898 -0.42187 0.16011  326 ASN   A N   
2454 C  CA  . ASN   A 326 ? 1.31552 1.47068 1.57880 -0.18797 -0.43767 0.16771  326 ASN   A CA  
2455 C  C   . ASN   A 326 ? 1.29041 1.40809 1.52822 -0.18291 -0.45257 0.15278  326 ASN   A C   
2456 O  O   . ASN   A 326 ? 1.33729 1.44814 1.57686 -0.18821 -0.46543 0.15704  326 ASN   A O   
2457 C  CB  . ASN   A 326 ? 1.35880 1.55189 1.64246 -0.18848 -0.43035 0.17949  326 ASN   A CB  
2458 C  CG  . ASN   A 326 ? 1.35246 1.58149 1.66248 -0.19563 -0.41909 0.19724  326 ASN   A CG  
2459 O  OD1 . ASN   A 326 ? 1.40069 1.62944 1.72315 -0.20873 -0.42737 0.21074  326 ASN   A OD1 
2460 N  ND2 . ASN   A 326 ? 1.36362 1.62320 1.68130 -0.18664 -0.40034 0.19755  326 ASN   A ND2 
2461 N  N   . GLY   A 327 ? 1.15530 1.25009 1.36927 -0.17211 -0.45056 0.13555  327 GLY   A N   
2462 C  CA  . GLY   A 327 ? 1.13318 1.19100 1.32049 -0.16608 -0.46405 0.12067  327 GLY   A CA  
2463 C  C   . GLY   A 327 ? 1.24364 1.30558 1.42159 -0.15728 -0.46357 0.11386  327 GLY   A C   
2464 O  O   . GLY   A 327 ? 1.15573 1.18825 1.31317 -0.15354 -0.47646 0.10368  327 GLY   A O   
2465 N  N   . PHE   A 328 ? 1.31831 1.41506 1.50980 -0.15322 -0.44940 0.11909  328 PHE   A N   
2466 C  CA  . PHE   A 328 ? 1.37223 1.47275 1.55393 -0.14409 -0.44849 0.11256  328 PHE   A CA  
2467 C  C   . PHE   A 328 ? 1.31869 1.40048 1.47224 -0.12985 -0.44378 0.09444  328 PHE   A C   
2468 O  O   . PHE   A 328 ? 1.34495 1.42033 1.48364 -0.12178 -0.44598 0.08658  328 PHE   A O   
2469 C  CB  . PHE   A 328 ? 1.35765 1.50053 1.56208 -0.14318 -0.43507 0.12388  328 PHE   A CB  
2470 C  CG  . PHE   A 328 ? 1.40106 1.56575 1.63278 -0.15604 -0.43895 0.14213  328 PHE   A CG  
2471 C  CD1 . PHE   A 328 ? 1.41933 1.56530 1.65470 -0.16856 -0.45410 0.14850  328 PHE   A CD1 
2472 C  CD2 . PHE   A 328 ? 1.46651 1.67040 1.71961 -0.15506 -0.42755 0.15321  328 PHE   A CD2 
2473 C  CE1 . PHE   A 328 ? 1.47670 1.64339 1.73687 -0.18079 -0.45773 0.16634  328 PHE   A CE1 
2474 C  CE2 . PHE   A 328 ? 1.53346 1.75914 1.81107 -0.16624 -0.43047 0.17026  328 PHE   A CE2 
2475 C  CZ  . PHE   A 328 ? 1.51134 1.71879 1.79270 -0.17962 -0.44558 0.17726  328 PHE   A CZ  
2476 N  N   . ILE   A 329 ? 1.21841 1.29217 1.36431 -0.12662 -0.43714 0.08819  329 ILE   A N   
2477 C  CA  . ILE   A 329 ? 1.25067 1.30888 1.37068 -0.11331 -0.43134 0.07194  329 ILE   A CA  
2478 C  C   . ILE   A 329 ? 1.17676 1.19715 1.27590 -0.11261 -0.44240 0.06106  329 ILE   A C   
2479 O  O   . ILE   A 329 ? 1.12388 1.13981 1.23165 -0.11991 -0.44400 0.06562  329 ILE   A O   
2480 C  CB  . ILE   A 329 ? 1.18276 1.26506 1.31094 -0.10860 -0.41307 0.07337  329 ILE   A CB  
2481 C  CG1 . ILE   A 329 ? 1.13909 1.26069 1.29257 -0.11062 -0.40257 0.08688  329 ILE   A CG1 
2482 C  CG2 . ILE   A 329 ? 1.13669 1.20696 1.23875 -0.09447 -0.40680 0.05810  329 ILE   A CG2 
2483 C  CD1 . ILE   A 329 ? 1.00919 1.15669 1.17231 -0.10540 -0.38425 0.08952  329 ILE   A CD1 
2484 N  N   . HIS   A 330 ? 1.15911 1.15225 1.23026 -0.10321 -0.45000 0.04680  330 HIS   A N   
2485 C  CA  . HIS   A 330 ? 1.02992 0.98715 1.07878 -0.09964 -0.45945 0.03493  330 HIS   A CA  
2486 C  C   . HIS   A 330 ? 1.15524 1.11317 1.19547 -0.09222 -0.44698 0.02711  330 HIS   A C   
2487 O  O   . HIS   A 330 ? 1.04185 1.01538 1.07709 -0.08359 -0.43377 0.02303  330 HIS   A O   
2488 C  CB  . HIS   A 330 ? 0.94066 0.86990 0.95962 -0.08911 -0.46890 0.02066  330 HIS   A CB  
2489 C  CG  . HIS   A 330 ? 0.99576 0.90899 1.01563 -0.09581 -0.48655 0.02450  330 HIS   A CG  
2490 N  ND1 . HIS   A 330 ? 0.95816 0.84695 0.95291 -0.08711 -0.49613 0.01306  330 HIS   A ND1 
2491 C  CD2 . HIS   A 330 ? 0.99559 0.91191 1.03702 -0.11008 -0.49687 0.03827  330 HIS   A CD2 
2492 C  CE1 . HIS   A 330 ? 1.02643 0.90396 1.02775 -0.09577 -0.51186 0.01950  330 HIS   A CE1 
2493 N  NE2 . HIS   A 330 ? 1.09947 0.99331 1.12914 -0.11006 -0.51277 0.03505  330 HIS   A NE2 
2494 N  N   . PRO   A 331 ? 1.19691 1.13627 1.23358 -0.09480 -0.45159 0.02444  331 PRO   A N   
2495 C  CA  . PRO   A 331 ? 1.15885 1.09890 1.18708 -0.08746 -0.43979 0.01669  331 PRO   A CA  
2496 C  C   . PRO   A 331 ? 1.00630 0.93451 1.00488 -0.07132 -0.43495 0.00027  331 PRO   A C   
2497 O  O   . PRO   A 331 ? 1.06853 1.01353 1.06484 -0.06443 -0.42060 -0.00251 331 PRO   A O   
2498 C  CB  . PRO   A 331 ? 1.24944 1.16476 1.27507 -0.09233 -0.44982 0.01542  331 PRO   A CB  
2499 C  CG  . PRO   A 331 ? 1.31304 1.20080 1.32763 -0.09398 -0.46846 0.01294  331 PRO   A CG  
2500 C  CD  . PRO   A 331 ? 1.20466 1.11345 1.23554 -0.10046 -0.46955 0.02379  331 PRO   A CD  
2501 N  N   . LEU   A 332 ? 1.05662 0.95702 1.03228 -0.06496 -0.44678 -0.00994 332 LEU   A N   
2502 C  CA  . LEU   A 332 ? 1.07948 0.96860 1.02532 -0.04897 -0.44205 -0.02536 332 LEU   A CA  
2503 C  C   . LEU   A 332 ? 1.14123 1.05467 1.08888 -0.04474 -0.43123 -0.02300 332 LEU   A C   
2504 O  O   . LEU   A 332 ? 1.01886 0.93529 0.94920 -0.03310 -0.42043 -0.03188 332 LEU   A O   
2505 C  CB  . LEU   A 332 ? 1.14017 0.99617 1.06301 -0.04332 -0.45741 -0.03528 332 LEU   A CB  
2506 C  CG  . LEU   A 332 ? 1.13848 0.98043 1.02837 -0.02620 -0.45448 -0.05119 332 LEU   A CG  
2507 C  CD1 . LEU   A 332 ? 1.17402 0.98108 1.04461 -0.02172 -0.47078 -0.06000 332 LEU   A CD1 
2508 C  CD2 . LEU   A 332 ? 1.21441 1.07237 1.10332 -0.02380 -0.45027 -0.04880 332 LEU   A CD2 
2509 N  N   . ASP   A 333 ? 0.98776 0.91919 0.95595 -0.05365 -0.43372 -0.01075 333 ASP   A N   
2510 C  CA  . ASP   A 333 ? 1.03655 0.99187 1.00780 -0.04930 -0.42291 -0.00781 333 ASP   A CA  
2511 C  C   . ASP   A 333 ? 1.02865 1.00740 1.01114 -0.04816 -0.40666 -0.00417 333 ASP   A C   
2512 O  O   . ASP   A 333 ? 0.93282 0.91985 0.90356 -0.03853 -0.39611 -0.00908 333 ASP   A O   
2513 C  CB  . ASP   A 333 ? 1.04069 1.01242 1.03330 -0.05862 -0.42836 0.00503  333 ASP   A CB  
2514 C  CG  . ASP   A 333 ? 1.13935 1.08957 1.11640 -0.05670 -0.44279 -0.00007 333 ASP   A CG  
2515 O  OD1 . ASP   A 333 ? 1.18526 1.11691 1.13349 -0.04468 -0.44351 -0.01343 333 ASP   A OD1 
2516 O  OD2 . ASP   A 333 ? 1.14949 1.10248 1.14295 -0.06683 -0.45298 0.00957  333 ASP   A OD2 
2517 N  N   . LEU   A 334 ? 0.95303 0.94164 0.95736 -0.05776 -0.40472 0.00454  334 LEU   A N   
2518 C  CA  . LEU   A 334 ? 0.98617 0.99569 1.00164 -0.05694 -0.39004 0.00808  334 LEU   A CA  
2519 C  C   . LEU   A 334 ? 0.94591 0.94038 0.93590 -0.04511 -0.38387 -0.00625 334 LEU   A C   
2520 O  O   . LEU   A 334 ? 0.92181 0.93058 0.90957 -0.03784 -0.36301 -0.00744 334 LEU   A O   
2521 C  CB  . LEU   A 334 ? 0.85320 0.87388 0.89504 -0.06937 -0.38999 0.01979  334 LEU   A CB  
2522 C  CG  . LEU   A 334 ? 0.95287 1.00096 1.01205 -0.07011 -0.37471 0.02689  334 LEU   A CG  
2523 C  CD1 . LEU   A 334 ? 0.83862 0.91290 0.90957 -0.06843 -0.36621 0.03470  334 LEU   A CD1 
2524 C  CD2 . LEU   A 334 ? 0.92394 0.98273 1.00783 -0.08219 -0.37454 0.03860  334 LEU   A CD2 
2525 N  N   . LYS   A 335 ? 1.03149 0.99710 1.00161 -0.04131 -0.39255 -0.01711 335 LYS   A N   
2526 C  CA  . LYS   A 335 ? 0.99512 0.94656 0.93926 -0.02864 -0.38657 -0.03148 335 LYS   A CA  
2527 C  C   . LYS   A 335 ? 0.95835 0.91125 0.88084 -0.01595 -0.37699 -0.03922 335 LYS   A C   
2528 O  O   . LYS   A 335 ? 0.86116 0.82171 0.77444 -0.00713 -0.35730 -0.04373 335 LYS   A O   
2529 C  CB  . LYS   A 335 ? 0.99561 0.91537 0.92155 -0.02539 -0.39805 -0.04171 335 LYS   A CB  
2530 C  CG  . LYS   A 335 ? 0.99450 0.90707 0.93284 -0.03324 -0.40183 -0.03844 335 LYS   A CG  
2531 C  CD  . LYS   A 335 ? 1.02268 0.90143 0.93800 -0.02657 -0.41321 -0.05054 335 LYS   A CD  
2532 C  CE  . LYS   A 335 ? 1.02951 0.89953 0.95055 -0.03016 -0.41413 -0.05064 335 LYS   A CE  
2533 N  NZ  . LYS   A 335 ? 1.01812 0.85453 0.91617 -0.02213 -0.42517 -0.06275 335 LYS   A NZ  
2534 N  N   . ASP   A 336 ? 0.88156 0.82615 0.79518 -0.01486 -0.38875 -0.04060 336 ASP   A N   
2535 C  CA  . ASP   A 336 ? 0.86010 0.80385 0.75092 -0.00305 -0.38335 -0.04799 336 ASP   A CA  
2536 C  C   . ASP   A 336 ? 0.85762 0.82861 0.76014 -0.00181 -0.36062 -0.04048 336 ASP   A C   
2537 O  O   . ASP   A 336 ? 0.88160 0.85547 0.76739 0.00859  -0.34494 -0.04648 336 ASP   A O   
2538 C  CB  . ASP   A 336 ? 0.92868 0.86245 0.81535 -0.00480 -0.39626 -0.04720 336 ASP   A CB  
2539 C  CG  . ASP   A 336 ? 1.14524 1.05011 1.01938 -0.00420 -0.41015 -0.05466 336 ASP   A CG  
2540 O  OD1 . ASP   A 336 ? 1.16217 1.05261 1.02128 0.00265  -0.40844 -0.06424 336 ASP   A OD1 
2541 O  OD2 . ASP   A 336 ? 1.11975 1.01621 0.99928 -0.01030 -0.42301 -0.05075 336 ASP   A OD2 
2542 N  N   . ASN   A 337 ? 0.77113 0.76275 0.70240 -0.01225 -0.35924 -0.02687 337 ASN   A N   
2543 C  CA  . ASN   A 337 ? 0.86698 0.88339 0.80962 -0.01057 -0.33909 -0.01977 337 ASN   A CA  
2544 C  C   . ASN   A 337 ? 0.74093 0.76712 0.68958 -0.00902 -0.32001 -0.01947 337 ASN   A C   
2545 O  O   . ASN   A 337 ? 0.80568 0.84210 0.74888 -0.00235 -0.30227 -0.02019 337 ASN   A O   
2546 C  CB  . ASN   A 337 ? 0.81297 0.85015 0.78387 -0.02041 -0.34285 -0.00569 337 ASN   A CB  
2547 C  CG  . ASN   A 337 ? 0.96040 0.99485 0.92649 -0.02024 -0.35578 -0.00450 337 ASN   A CG  
2548 O  OD1 . ASN   A 337 ? 1.00713 1.04413 0.95993 -0.01218 -0.34798 -0.00733 337 ASN   A OD1 
2549 N  ND2 . ASN   A 337 ? 0.88964 0.91887 0.86694 -0.02975 -0.37638 0.00037  337 ASN   A ND2 
2550 N  N   . VAL   A 338 ? 0.80750 0.83181 0.76916 -0.01601 -0.32377 -0.01707 338 VAL   A N   
2551 C  CA  . VAL   A 338 ? 0.80090 0.83324 0.76723 -0.01431 -0.30643 -0.01730 338 VAL   A CA  
2552 C  C   . VAL   A 338 ? 0.81648 0.83728 0.75567 -0.00213 -0.29635 -0.02958 338 VAL   A C   
2553 O  O   . VAL   A 338 ? 0.82136 0.85403 0.75900 0.00286  -0.27774 -0.02924 338 VAL   A O   
2554 C  CB  . VAL   A 338 ? 0.75382 0.78129 0.73390 -0.02299 -0.31454 -0.01446 338 VAL   A CB  
2555 C  CG1 . VAL   A 338 ? 0.68182 0.71126 0.65908 -0.01865 -0.29762 -0.01853 338 VAL   A CG1 
2556 C  CG2 . VAL   A 338 ? 0.63098 0.67901 0.64212 -0.03507 -0.31786 0.00059  338 VAL   A CG2 
2557 N  N   . ALA   A 339 ? 0.77377 0.77179 0.69062 0.00322  -0.30904 -0.04033 339 ALA   A N   
2558 C  CA  . ALA   A 339 ? 0.83752 0.82683 0.72794 0.01567  -0.29978 -0.05172 339 ALA   A CA  
2559 C  C   . ALA   A 339 ? 0.90869 0.90894 0.78934 0.02225  -0.28763 -0.05099 339 ALA   A C   
2560 O  O   . ALA   A 339 ? 0.91909 0.92775 0.79339 0.02802  -0.27017 -0.05251 339 ALA   A O   
2561 C  CB  . ALA   A 339 ? 0.77589 0.73914 0.64305 0.02158  -0.31706 -0.06360 339 ALA   A CB  
2562 N  N   . MET   A 340 ? 0.88176 0.88181 0.76061 0.02136  -0.29693 -0.04836 340 MET   A N   
2563 C  CA  . MET   A 340 ? 0.89884 0.90810 0.76644 0.02820  -0.28451 -0.04800 340 MET   A CA  
2564 C  C   . MET   A 340 ? 0.86939 0.90066 0.75603 0.02485  -0.26665 -0.03831 340 MET   A C   
2565 O  O   . MET   A 340 ? 0.82367 0.86145 0.70035 0.03086  -0.25213 -0.03904 340 MET   A O   
2566 C  CB  . MET   A 340 ? 0.89613 0.89911 0.75331 0.02993  -0.29736 -0.04862 340 MET   A CB  
2567 C  CG  . MET   A 340 ? 1.02478 1.03360 0.86467 0.03847  -0.28470 -0.05018 340 MET   A CG  
2568 S  SD  . MET   A 340 ? 1.49518 1.49419 1.31137 0.04523  -0.29566 -0.05451 340 MET   A SD  
2569 C  CE  . MET   A 340 ? 1.36244 1.33727 1.15191 0.05340  -0.30873 -0.06904 340 MET   A CE  
2570 N  N   . TYR   A 341 ? 0.85305 0.89633 0.76644 0.01563  -0.26794 -0.02881 341 TYR   A N   
2571 C  CA  . TYR   A 341 ? 0.85199 0.91526 0.78216 0.01387  -0.25172 -0.02047 341 TYR   A CA  
2572 C  C   . TYR   A 341 ? 0.87930 0.94449 0.80657 0.01691  -0.23624 -0.02360 341 TYR   A C   
2573 O  O   . TYR   A 341 ? 0.84757 0.92306 0.77474 0.02009  -0.22125 -0.02100 341 TYR   A O   
2574 C  CB  . TYR   A 341 ? 0.71383 0.79147 0.67297 0.00432  -0.25645 -0.00963 341 TYR   A CB  
2575 C  CG  . TYR   A 341 ? 0.87686 0.96216 0.84385 0.00202  -0.26528 -0.00308 341 TYR   A CG  
2576 C  CD1 . TYR   A 341 ? 0.88771 0.97832 0.84629 0.00799  -0.25838 -0.00219 341 TYR   A CD1 
2577 C  CD2 . TYR   A 341 ? 0.81828 0.90640 0.80233 -0.00664 -0.28083 0.00312  341 TYR   A CD2 
2578 C  CE1 . TYR   A 341 ? 0.91814 1.01591 0.88426 0.00622  -0.26714 0.00382  341 TYR   A CE1 
2579 C  CE2 . TYR   A 341 ? 0.85183 0.94868 0.84453 -0.00892 -0.28924 0.00969  341 TYR   A CE2 
2580 C  CZ  . TYR   A 341 ? 0.86783 0.96942 0.85138 -0.00205 -0.28217 0.00965  341 TYR   A CZ  
2581 O  OH  . TYR   A 341 ? 0.99870 1.10883 0.99091 -0.00396 -0.29107 0.01601  341 TYR   A OH  
2582 N  N   . ILE   A 342 ? 0.83001 0.88544 0.75635 0.01540  -0.24040 -0.02847 342 ILE   A N   
2583 C  CA  . ILE   A 342 ? 0.83245 0.88846 0.75450 0.01878  -0.22691 -0.03232 342 ILE   A CA  
2584 C  C   . ILE   A 342 ? 0.91583 0.96726 0.81309 0.02861  -0.21854 -0.03950 342 ILE   A C   
2585 O  O   . ILE   A 342 ? 0.75162 0.81022 0.64629 0.03176  -0.20329 -0.03944 342 ILE   A O   
2586 C  CB  . ILE   A 342 ? 0.82103 0.86477 0.74420 0.01614  -0.23549 -0.03714 342 ILE   A CB  
2587 C  CG1 . ILE   A 342 ? 0.75614 0.80763 0.70588 0.00543  -0.24063 -0.02829 342 ILE   A CG1 
2588 C  CG2 . ILE   A 342 ? 0.77897 0.82202 0.69455 0.02107  -0.22244 -0.04243 342 ILE   A CG2 
2589 C  CD1 . ILE   A 342 ? 0.74235 0.81549 0.71238 0.00198  -0.22625 -0.01848 342 ILE   A CD1 
2590 N  N   . ASN   A 343 ? 0.82282 0.86247 0.70108 0.03356  -0.22889 -0.04556 343 ASN   A N   
2591 C  CA  . ASN   A 343 ? 0.90102 0.93847 0.75509 0.04311  -0.22124 -0.05146 343 ASN   A CA  
2592 C  C   . ASN   A 343 ? 0.84251 0.89348 0.69856 0.04354  -0.20939 -0.04439 343 ASN   A C   
2593 O  O   . ASN   A 343 ? 0.92967 0.98676 0.77785 0.04754  -0.19551 -0.04451 343 ASN   A O   
2594 C  CB  . ASN   A 343 ? 0.99780 1.01988 0.83122 0.04857  -0.23621 -0.05921 343 ASN   A CB  
2595 C  CG  . ASN   A 343 ? 1.02319 1.02978 0.84570 0.05238  -0.24483 -0.06897 343 ASN   A CG  
2596 O  OD1 . ASN   A 343 ? 0.91933 0.92722 0.73597 0.05684  -0.23489 -0.07320 343 ASN   A OD1 
2597 N  ND2 . ASN   A 343 ? 0.87863 0.87058 0.70100 0.04968  -0.26403 -0.07182 343 ASN   A ND2 
2598 N  N   . LYS   A 344 ? 0.93136 0.98715 0.79851 0.03922  -0.21527 -0.03772 344 LYS   A N   
2599 C  CA  . LYS   A 344 ? 0.90372 0.97134 0.77469 0.03941  -0.20536 -0.03054 344 LYS   A CA  
2600 C  C   . LYS   A 344 ? 0.87947 0.95822 0.76342 0.03738  -0.19020 -0.02593 344 LYS   A C   
2601 O  O   . LYS   A 344 ? 0.86717 0.95076 0.74370 0.04052  -0.17859 -0.02415 344 LYS   A O   
2602 C  CB  . LYS   A 344 ? 0.86361 0.93580 0.74814 0.03496  -0.21494 -0.02392 344 LYS   A CB  
2603 C  CG  . LYS   A 344 ? 0.94251 1.00375 0.81101 0.03790  -0.22883 -0.02808 344 LYS   A CG  
2604 C  CD  . LYS   A 344 ? 0.88546 0.95038 0.76893 0.03262  -0.24096 -0.02203 344 LYS   A CD  
2605 C  CE  . LYS   A 344 ? 1.06450 1.11797 0.92937 0.03639  -0.25382 -0.02640 344 LYS   A CE  
2606 N  NZ  . LYS   A 344 ? 1.10883 1.16768 0.98670 0.03210  -0.26422 -0.01971 344 LYS   A NZ  
2607 N  N   . LEU   A 345 ? 0.91277 0.99519 0.81550 0.03197  -0.19068 -0.02374 345 LEU   A N   
2608 C  CA  . LEU   A 345 ? 0.84384 0.93673 0.75932 0.03022  -0.17707 -0.01934 345 LEU   A CA  
2609 C  C   . LEU   A 345 ? 0.76727 0.85721 0.66951 0.03444  -0.16605 -0.02459 345 LEU   A C   
2610 O  O   . LEU   A 345 ? 0.76238 0.85957 0.66637 0.03522  -0.15358 -0.02117 345 LEU   A O   
2611 C  CB  . LEU   A 345 ? 0.83053 0.92866 0.76841 0.02352  -0.18102 -0.01550 345 LEU   A CB  
2612 C  CG  . LEU   A 345 ? 0.76349 0.87081 0.71822 0.01921  -0.18864 -0.00769 345 LEU   A CG  
2613 C  CD1 . LEU   A 345 ? 0.82858 0.94393 0.80597 0.01222  -0.19168 -0.00256 345 LEU   A CD1 
2614 C  CD2 . LEU   A 345 ? 0.75241 0.87037 0.71007 0.02202  -0.17931 -0.00201 345 LEU   A CD2 
2615 N  N   . LEU   A 346 ? 0.78692 0.86635 0.67518 0.03769  -0.17087 -0.03284 346 LEU   A N   
2616 C  CA  . LEU   A 346 ? 0.74713 0.82584 0.62276 0.04246  -0.16061 -0.03769 346 LEU   A CA  
2617 C  C   . LEU   A 346 ? 0.83092 0.91114 0.68674 0.04842  -0.15454 -0.03852 346 LEU   A C   
2618 O  O   . LEU   A 346 ? 0.83380 0.91743 0.68074 0.05182  -0.14421 -0.04029 346 LEU   A O   
2619 C  CB  . LEU   A 346 ? 0.80909 0.87641 0.67579 0.04537  -0.16808 -0.04675 346 LEU   A CB  
2620 C  CG  . LEU   A 346 ? 0.78049 0.84492 0.66304 0.04019  -0.17211 -0.04715 346 LEU   A CG  
2621 C  CD1 . LEU   A 346 ? 0.67627 0.72616 0.54454 0.04491  -0.18173 -0.05714 346 LEU   A CD1 
2622 C  CD2 . LEU   A 346 ? 0.71348 0.78789 0.60576 0.03871  -0.15694 -0.04391 346 LEU   A CD2 
2623 N  N   . GLN   A 347 ? 0.91235 0.99133 0.76197 0.04930  -0.16063 -0.03637 347 GLN   A N   
2624 C  CA  . GLN   A 347 ? 0.90429 0.98435 0.73387 0.05474  -0.15647 -0.03670 347 GLN   A CA  
2625 C  C   . GLN   A 347 ? 0.90132 0.99104 0.73191 0.05404  -0.14171 -0.03094 347 GLN   A C   
2626 O  O   . GLN   A 347 ? 0.89289 0.98516 0.70907 0.05827  -0.13445 -0.03328 347 GLN   A O   
2627 C  CB  . GLN   A 347 ? 0.94625 1.02346 0.77273 0.05452  -0.16622 -0.03412 347 GLN   A CB  
2628 C  CG  . GLN   A 347 ? 1.02866 1.10777 0.83630 0.05897  -0.16267 -0.03228 347 GLN   A CG  
2629 C  CD  . GLN   A 347 ? 1.12701 1.21373 0.94267 0.05559  -0.15551 -0.02270 347 GLN   A CD  
2630 O  OE1 . GLN   A 347 ? 1.11412 1.20273 0.94622 0.05151  -0.15922 -0.01787 347 GLN   A OE1 
2631 N  NE2 . GLN   A 347 ? 1.13953 1.23092 0.94311 0.05759  -0.14572 -0.01968 347 GLN   A NE2 
2632 N  N   . PRO   A 348 ? 0.82990 0.92547 0.67669 0.04918  -0.13704 -0.02346 348 PRO   A N   
2633 C  CA  . PRO   A 348 ? 0.87278 0.97502 0.71860 0.04854  -0.12454 -0.01811 348 PRO   A CA  
2634 C  C   . PRO   A 348 ? 0.81512 0.92049 0.66161 0.04878  -0.11527 -0.02069 348 PRO   A C   
2635 O  O   . PRO   A 348 ? 0.86953 0.97966 0.70779 0.04960  -0.10625 -0.01791 348 PRO   A O   
2636 C  CB  . PRO   A 348 ? 0.81766 0.92340 0.68110 0.04445  -0.12399 -0.01105 348 PRO   A CB  
2637 C  CG  . PRO   A 348 ? 0.78885 0.89313 0.66624 0.04222  -0.13369 -0.01272 348 PRO   A CG  
2638 C  CD  . PRO   A 348 ? 0.84962 0.94642 0.71404 0.04492  -0.14372 -0.01897 348 PRO   A CD  
2639 N  N   . VAL   A 349 ? 0.80167 0.90458 0.65689 0.04798  -0.11772 -0.02559 349 VAL   A N   
2640 C  CA  . VAL   A 349 ? 0.82106 0.92639 0.67423 0.04936  -0.10973 -0.02900 349 VAL   A CA  
2641 C  C   . VAL   A 349 ? 0.78563 0.88989 0.61745 0.05614  -0.10981 -0.03506 349 VAL   A C   
2642 O  O   . VAL   A 349 ? 0.78085 0.89169 0.60509 0.05840  -0.10041 -0.03482 349 VAL   A O   
2643 C  CB  . VAL   A 349 ? 0.68519 0.78754 0.55284 0.04678  -0.11277 -0.03241 349 VAL   A CB  
2644 C  CG1 . VAL   A 349 ? 0.70584 0.80980 0.56873 0.04941  -0.10553 -0.03689 349 VAL   A CG1 
2645 C  CG2 . VAL   A 349 ? 0.70856 0.81572 0.59680 0.04101  -0.10965 -0.02575 349 VAL   A CG2 
2646 N  N   . ARG   A 350 ? 0.83985 0.93635 0.66188 0.05989  -0.12078 -0.04078 350 ARG   A N   
2647 C  CA  . ARG   A 350 ? 0.92258 1.01842 0.72205 0.06803  -0.12160 -0.04683 350 ARG   A CA  
2648 C  C   . ARG   A 350 ? 0.78500 0.89047 0.57278 0.06937  -0.11296 -0.04070 350 ARG   A C   
2649 O  O   . ARG   A 350 ? 0.90673 1.01970 0.68190 0.07416  -0.10562 -0.04202 350 ARG   A O   
2650 C  CB  . ARG   A 350 ? 0.87050 0.95496 0.66090 0.07152  -0.13631 -0.05297 350 ARG   A CB  
2651 C  CG  . ARG   A 350 ? 0.89462 0.96859 0.69141 0.07150  -0.14553 -0.06018 350 ARG   A CG  
2652 C  CD  . ARG   A 350 ? 0.96758 1.02843 0.74970 0.07703  -0.16060 -0.06825 350 ARG   A CD  
2653 N  NE  . ARG   A 350 ? 0.95611 1.00528 0.74943 0.07348  -0.17232 -0.07209 350 ARG   A NE  
2654 C  CZ  . ARG   A 350 ? 0.96625 1.00881 0.77040 0.06752  -0.18440 -0.06951 350 ARG   A CZ  
2655 N  NH1 . ARG   A 350 ? 1.02721 1.07316 0.83221 0.06526  -0.18648 -0.06394 350 ARG   A NH1 
2656 N  NH2 . ARG   A 350 ? 0.91808 0.95085 0.73279 0.06346  -0.19507 -0.07199 350 ARG   A NH2 
2657 N  N   . ASP   A 351 ? 0.80513 0.91111 0.59725 0.06512  -0.11411 -0.03342 351 ASP   A N   
2658 C  CA  . ASP   A 351 ? 0.82272 0.93602 0.60392 0.06533  -0.10782 -0.02653 351 ASP   A CA  
2659 C  C   . ASP   A 351 ? 0.94311 1.06575 0.72937 0.06209  -0.09528 -0.02081 351 ASP   A C   
2660 O  O   . ASP   A 351 ? 0.94001 1.07145 0.71321 0.06467  -0.08849 -0.01857 351 ASP   A O   
2661 C  CB  . ASP   A 351 ? 0.92070 1.03049 0.70690 0.06143  -0.11310 -0.02021 351 ASP   A CB  
2662 C  CG  . ASP   A 351 ? 1.00757 1.10962 0.78482 0.06502  -0.12541 -0.02486 351 ASP   A CG  
2663 O  OD1 . ASP   A 351 ? 1.08921 1.18868 0.85223 0.07135  -0.12909 -0.03263 351 ASP   A OD1 
2664 O  OD2 . ASP   A 351 ? 1.03437 1.13275 0.81768 0.06226  -0.13189 -0.02111 351 ASP   A OD2 
2665 N  N   . HIS   A 352 ? 0.87419 0.99594 0.67921 0.05665  -0.09222 -0.01840 352 HIS   A N   
2666 C  CA  . HIS   A 352 ? 0.78543 0.91469 0.59520 0.05360  -0.08129 -0.01363 352 HIS   A CA  
2667 C  C   . HIS   A 352 ? 0.82897 0.96515 0.62885 0.05846  -0.07583 -0.01857 352 HIS   A C   
2668 O  O   . HIS   A 352 ? 0.82888 0.97492 0.62333 0.05782  -0.06723 -0.01361 352 HIS   A O   
2669 C  CB  . HIS   A 352 ? 0.68139 0.80801 0.51179 0.04858  -0.07957 -0.01238 352 HIS   A CB  
2670 C  CG  . HIS   A 352 ? 0.72681 0.85958 0.56206 0.04530  -0.06939 -0.00761 352 HIS   A CG  
2671 N  ND1 . HIS   A 352 ? 0.76409 0.89921 0.59763 0.04163  -0.06521 0.00110  352 HIS   A ND1 
2672 C  CD2 . HIS   A 352 ? 0.78358 0.92014 0.62424 0.04512  -0.06329 -0.01019 352 HIS   A CD2 
2673 C  CE1 . HIS   A 352 ? 0.78229 0.92218 0.62058 0.03888  -0.05729 0.00386  352 HIS   A CE1 
2674 N  NE2 . HIS   A 352 ? 0.82480 0.96628 0.66766 0.04107  -0.05558 -0.00294 352 HIS   A NE2 
2675 N  N   . PHE   A 353 ? 0.82015 0.95151 0.61819 0.06332  -0.08107 -0.02803 353 PHE   A N   
2676 C  CA  . PHE   A 353 ? 0.80307 0.94090 0.59265 0.06903  -0.07589 -0.03341 353 PHE   A CA  
2677 C  C   . PHE   A 353 ? 0.87470 1.01824 0.64167 0.07739  -0.07653 -0.03632 353 PHE   A C   
2678 O  O   . PHE   A 353 ? 0.86667 1.01872 0.62436 0.08358  -0.07135 -0.04005 353 PHE   A O   
2679 C  CB  . PHE   A 353 ? 0.80738 0.93669 0.60443 0.07099  -0.08128 -0.04229 353 PHE   A CB  
2680 C  CG  . PHE   A 353 ? 0.76829 0.89762 0.58511 0.06434  -0.07651 -0.03930 353 PHE   A CG  
2681 C  CD1 . PHE   A 353 ? 0.77492 0.91270 0.59391 0.06451  -0.06688 -0.03857 353 PHE   A CD1 
2682 C  CD2 . PHE   A 353 ? 0.78593 0.90865 0.61910 0.05800  -0.08109 -0.03624 353 PHE   A CD2 
2683 C  CE1 . PHE   A 353 ? 0.69485 0.83251 0.53135 0.05853  -0.06238 -0.03565 353 PHE   A CE1 
2684 C  CE2 . PHE   A 353 ? 0.62420 0.74828 0.47476 0.05258  -0.07595 -0.03315 353 PHE   A CE2 
2685 C  CZ  . PHE   A 353 ? 0.61885 0.74950 0.47019 0.05294  -0.06692 -0.03314 353 PHE   A CZ  
2686 N  N   . GLN   A 354 ? 0.89294 1.03255 0.65058 0.07849  -0.08301 -0.03502 354 GLN   A N   
2687 C  CA  . GLN   A 354 ? 1.04689 1.19451 0.78237 0.08626  -0.08200 -0.03604 354 GLN   A CA  
2688 C  C   . GLN   A 354 ? 1.03885 1.20006 0.77068 0.08207  -0.07270 -0.02434 354 GLN   A C   
2689 O  O   . GLN   A 354 ? 0.96247 1.13833 0.68322 0.08633  -0.06501 -0.02258 354 GLN   A O   
2690 C  CB  . GLN   A 354 ? 0.99926 1.13606 0.72371 0.09046  -0.09413 -0.04087 354 GLN   A CB  
2691 C  CG  . GLN   A 354 ? 1.17064 1.29494 0.89155 0.09707  -0.10447 -0.05346 354 GLN   A CG  
2692 C  CD  . GLN   A 354 ? 1.20575 1.31603 0.92177 0.09814  -0.11873 -0.05726 354 GLN   A CD  
2693 O  OE1 . GLN   A 354 ? 1.18055 1.29038 0.89817 0.09360  -0.12071 -0.05056 354 GLN   A OE1 
2694 N  NE2 . GLN   A 354 ? 1.26247 1.36069 0.97168 0.10442  -0.12946 -0.06804 354 GLN   A NE2 
2695 N  N   . ASN   A 355 ? 1.03884 1.19609 0.78212 0.07323  -0.07284 -0.01576 355 ASN   A N   
2696 C  CA  . ASN   A 355 ? 1.00289 1.16844 0.74103 0.06868  -0.06784 -0.00425 355 ASN   A CA  
2697 C  C   . ASN   A 355 ? 1.02228 1.19564 0.77148 0.06155  -0.05830 0.00401  355 ASN   A C   
2698 O  O   . ASN   A 355 ? 1.11066 1.29485 0.85305 0.05867  -0.05269 0.01342  355 ASN   A O   
2699 C  CB  . ASN   A 355 ? 1.00001 1.15475 0.74187 0.06418  -0.07532 0.00013  355 ASN   A CB  
2700 C  CG  . ASN   A 355 ? 1.07959 1.22577 0.81194 0.07019  -0.08585 -0.00741 355 ASN   A CG  
2701 O  OD1 . ASN   A 355 ? 1.17131 1.32091 0.88825 0.07838  -0.08726 -0.01411 355 ASN   A OD1 
2702 N  ND2 . ASN   A 355 ? 1.05500 1.19023 0.79582 0.06676  -0.09380 -0.00641 355 ASN   A ND2 
2703 N  N   . ASN   A 356 ? 0.87754 1.04594 0.64329 0.05836  -0.05671 0.00128  356 ASN   A N   
2704 C  CA  . ASN   A 356 ? 1.00761 1.18326 0.78265 0.05253  -0.04801 0.00790  356 ASN   A CA  
2705 C  C   . ASN   A 356 ? 1.02769 1.21574 0.79723 0.05818  -0.04162 0.00315  356 ASN   A C   
2706 O  O   . ASN   A 356 ? 1.04105 1.22475 0.81212 0.06379  -0.04423 -0.00713 356 ASN   A O   
2707 C  CB  . ASN   A 356 ? 0.86922 1.03464 0.66383 0.04702  -0.04889 0.00752  356 ASN   A CB  
2708 C  CG  . ASN   A 356 ? 0.96816 1.13948 0.77116 0.04087  -0.04090 0.01469  356 ASN   A CG  
2709 O  OD1 . ASN   A 356 ? 0.87981 1.06022 0.68366 0.04235  -0.03464 0.01269  356 ASN   A OD1 
2710 N  ND2 . ASN   A 356 ? 0.99267 1.15796 0.80184 0.03425  -0.04183 0.02284  356 ASN   A ND2 
2711 N  N   . ILE   A 357 ? 0.99838 1.20226 0.76077 0.05705  -0.03401 0.01091  357 ILE   A N   
2712 C  CA  . ILE   A 357 ? 1.04700 1.26611 0.80166 0.06410  -0.02781 0.00693  357 ILE   A CA  
2713 C  C   . ILE   A 357 ? 0.93913 1.15803 0.70814 0.06264  -0.02349 0.00320  357 ILE   A C   
2714 O  O   . ILE   A 357 ? 0.98531 1.20531 0.75183 0.07050  -0.02359 -0.00675 357 ILE   A O   
2715 C  CB  . ILE   A 357 ? 1.19387 1.43271 0.93768 0.06261  -0.02097 0.01814  357 ILE   A CB  
2716 C  CG1 . ILE   A 357 ? 1.28667 1.52472 1.01457 0.06557  -0.02617 0.02025  357 ILE   A CG1 
2717 C  CG2 . ILE   A 357 ? 1.17430 1.43275 0.91094 0.07010  -0.01349 0.01555  357 ILE   A CG2 
2718 C  CD1 . ILE   A 357 ? 1.08527 1.31127 0.80395 0.07546  -0.03496 0.00694  357 ILE   A CD1 
2719 N  N   . GLU   A 358 ? 0.95609 1.17190 0.73972 0.05301  -0.02060 0.01061  358 GLU   A N   
2720 C  CA  . GLU   A 358 ? 0.92987 1.14522 0.72713 0.05122  -0.01658 0.00762  358 GLU   A CA  
2721 C  C   . GLU   A 358 ? 0.82379 1.02454 0.62787 0.05512  -0.02276 -0.00391 358 GLU   A C   
2722 O  O   . GLU   A 358 ? 0.81496 1.01720 0.62288 0.05896  -0.02081 -0.01075 358 GLU   A O   
2723 C  CB  . GLU   A 358 ? 0.91868 1.13005 0.72923 0.04058  -0.01426 0.01713  358 GLU   A CB  
2724 C  CG  . GLU   A 358 ? 1.03075 1.25436 0.83590 0.03469  -0.00983 0.03007  358 GLU   A CG  
2725 C  CD  . GLU   A 358 ? 1.11002 1.34126 0.92515 0.02852  -0.00336 0.03623  358 GLU   A CD  
2726 O  OE1 . GLU   A 358 ? 1.14810 1.37212 0.97049 0.01974  -0.00449 0.04460  358 GLU   A OE1 
2727 O  OE2 . GLU   A 358 ? 1.13823 1.38185 0.95367 0.03286  0.00218  0.03236  358 GLU   A OE2 
2728 N  N   . ALA   A 359 ? 0.84166 1.02864 0.64765 0.05387  -0.03070 -0.00554 359 ALA   A N   
2729 C  CA  . ALA   A 359 ? 0.84005 1.01402 0.65312 0.05642  -0.03771 -0.01493 359 ALA   A CA  
2730 C  C   . ALA   A 359 ? 0.85896 1.03336 0.65922 0.06634  -0.04160 -0.02520 359 ALA   A C   
2731 O  O   . ALA   A 359 ? 0.77700 0.94581 0.58223 0.06940  -0.04403 -0.03322 359 ALA   A O   
2732 C  CB  . ALA   A 359 ? 0.78689 0.94879 0.60471 0.05287  -0.04547 -0.01307 359 ALA   A CB  
2733 N  N   . LYS   A 360 ? 0.88301 1.06365 0.66573 0.07195  -0.04264 -0.02514 360 LYS   A N   
2734 C  CA  . LYS   A 360 ? 0.81295 0.99287 0.58125 0.08295  -0.04720 -0.03575 360 LYS   A CA  
2735 C  C   . LYS   A 360 ? 0.72277 0.91173 0.49086 0.08816  -0.04099 -0.04037 360 LYS   A C   
2736 O  O   . LYS   A 360 ? 0.85821 1.03966 0.62324 0.09519  -0.04626 -0.05091 360 LYS   A O   
2737 C  CB  . LYS   A 360 ? 0.89451 1.08243 0.64249 0.08906  -0.04795 -0.03431 360 LYS   A CB  
2738 C  CG  . LYS   A 360 ? 0.88388 1.06733 0.61482 0.10180  -0.05521 -0.04665 360 LYS   A CG  
2739 C  CD  . LYS   A 360 ? 0.93657 1.12748 0.64522 0.10939  -0.05679 -0.04621 360 LYS   A CD  
2740 C  CE  . LYS   A 360 ? 0.97815 1.19356 0.67843 0.11194  -0.04463 -0.03889 360 LYS   A CE  
2741 N  NZ  . LYS   A 360 ? 0.99809 1.22549 0.67469 0.12212  -0.04445 -0.03949 360 LYS   A NZ  
2742 N  N   . ASN   A 361 ? 0.77712 0.98203 0.54820 0.08482  -0.03046 -0.03235 361 ASN   A N   
2743 C  CA  . ASN   A 361 ? 0.81539 1.03142 0.58659 0.08992  -0.02396 -0.03588 361 ASN   A CA  
2744 C  C   . ASN   A 361 ? 0.83992 1.04590 0.62834 0.08580  -0.02453 -0.03959 361 ASN   A C   
2745 O  O   . ASN   A 361 ? 0.81540 1.02336 0.60309 0.09220  -0.02346 -0.04691 361 ASN   A O   
2746 C  CB  . ASN   A 361 ? 0.84971 1.08656 0.62039 0.08610  -0.01328 -0.02463 361 ASN   A CB  
2747 C  CG  . ASN   A 361 ? 1.03319 1.28021 0.78830 0.08859  -0.01275 -0.01924 361 ASN   A CG  
2748 O  OD1 . ASN   A 361 ? 0.96634 1.20541 0.70868 0.09555  -0.02020 -0.02592 361 ASN   A OD1 
2749 N  ND2 . ASN   A 361 ? 0.99515 1.26089 0.74955 0.08376  -0.00440 -0.00726 361 ASN   A ND2 
2750 N  N   . LEU   A 362 ? 0.84570 1.04251 0.64943 0.07544  -0.02547 -0.03388 362 LEU   A N   
2751 C  CA  . LEU   A 362 ? 0.76241 0.94918 0.58221 0.07158  -0.02680 -0.03717 362 LEU   A CA  
2752 C  C   . LEU   A 362 ? 0.67712 0.84963 0.49466 0.07739  -0.03683 -0.04834 362 LEU   A C   
2753 O  O   . LEU   A 362 ? 0.75878 0.92860 0.57927 0.08102  -0.03743 -0.05503 362 LEU   A O   
2754 C  CB  . LEU   A 362 ? 0.71856 0.89813 0.55257 0.06120  -0.02718 -0.02944 362 LEU   A CB  
2755 C  CG  . LEU   A 362 ? 0.60712 0.77763 0.45744 0.05745  -0.02846 -0.03220 362 LEU   A CG  
2756 C  CD1 . LEU   A 362 ? 0.67553 0.85488 0.53005 0.05814  -0.02077 -0.03267 362 LEU   A CD1 
2757 C  CD2 . LEU   A 362 ? 0.63612 0.80139 0.49770 0.04900  -0.02868 -0.02432 362 LEU   A CD2 
2758 N  N   . LEU   A 363 ? 0.77403 0.93720 0.58529 0.07846  -0.04547 -0.05026 363 LEU   A N   
2759 C  CA  . LEU   A 363 ? 0.76029 0.90887 0.56795 0.08346  -0.05695 -0.06022 363 LEU   A CA  
2760 C  C   . LEU   A 363 ? 0.81784 0.96920 0.60981 0.09539  -0.05798 -0.06973 363 LEU   A C   
2761 O  O   . LEU   A 363 ? 0.81381 0.95431 0.60710 0.09904  -0.06461 -0.07813 363 LEU   A O   
2762 C  CB  . LEU   A 363 ? 0.75988 0.90024 0.56179 0.08281  -0.06572 -0.05971 363 LEU   A CB  
2763 C  CG  . LEU   A 363 ? 0.67892 0.80331 0.47544 0.08738  -0.07963 -0.06912 363 LEU   A CG  
2764 C  CD1 . LEU   A 363 ? 0.77913 0.89263 0.59330 0.08153  -0.08480 -0.07075 363 LEU   A CD1 
2765 C  CD2 . LEU   A 363 ? 0.87945 0.99817 0.66931 0.08668  -0.08747 -0.06745 363 LEU   A CD2 
2766 N  N   . ASN   A 364 ? 0.84406 1.01042 0.62079 0.10200  -0.05168 -0.06832 364 ASN   A N   
2767 C  CA  . ASN   A 364 ? 0.89128 1.06244 0.65240 0.11511  -0.05201 -0.07762 364 ASN   A CA  
2768 C  C   . ASN   A 364 ? 0.75049 0.92490 0.52086 0.11589  -0.04704 -0.08028 364 ASN   A C   
2769 O  O   . ASN   A 364 ? 0.79705 0.96279 0.56151 0.12433  -0.05327 -0.09076 364 ASN   A O   
2770 C  CB  . ASN   A 364 ? 0.86072 1.05186 0.60488 0.12223  -0.04454 -0.07424 364 ASN   A CB  
2771 C  CG  . ASN   A 364 ? 0.90697 1.09231 0.63280 0.12978  -0.05282 -0.07910 364 ASN   A CG  
2772 O  OD1 . ASN   A 364 ? 1.01327 1.18703 0.72725 0.14002  -0.06221 -0.09082 364 ASN   A OD1 
2773 N  ND2 . ASN   A 364 ? 1.02470 1.21558 0.74757 0.12478  -0.05092 -0.07052 364 ASN   A ND2 
2774 N  N   . GLU   A 365 ? 0.84771 1.03386 0.63167 0.10755  -0.03650 -0.07104 365 GLU   A N   
2775 C  CA  . GLU   A 365 ? 0.79972 0.98976 0.59293 0.10790  -0.03145 -0.07297 365 GLU   A CA  
2776 C  C   . GLU   A 365 ? 0.75548 0.92563 0.56052 0.10455  -0.03997 -0.07882 365 GLU   A C   
2777 O  O   . GLU   A 365 ? 0.74504 0.91100 0.54861 0.11088  -0.04243 -0.08676 365 GLU   A O   
2778 C  CB  . GLU   A 365 ? 0.82738 1.03213 0.63317 0.09849  -0.01981 -0.06127 365 GLU   A CB  
2779 C  CG  . GLU   A 365 ? 0.98312 1.21091 0.77785 0.10204  -0.01085 -0.05486 365 GLU   A CG  
2780 C  CD  . GLU   A 365 ? 1.12548 1.36599 0.93237 0.09116  -0.00128 -0.04196 365 GLU   A CD  
2781 O  OE1 . GLU   A 365 ? 1.12675 1.38304 0.92671 0.08984  0.00408  -0.03334 365 GLU   A OE1 
2782 O  OE2 . GLU   A 365 ? 1.06935 1.30384 0.89202 0.08399  0.00028  -0.04022 365 GLU   A OE2 
2783 N  N   . ILE   A 366 ? 0.73511 0.89366 0.55213 0.09471  -0.04468 -0.07451 366 ILE   A N   
2784 C  CA  . ILE   A 366 ? 0.80838 0.95174 0.63922 0.09004  -0.05133 -0.07774 366 ILE   A CA  
2785 C  C   . ILE   A 366 ? 0.79203 0.91926 0.61319 0.09724  -0.06476 -0.08845 366 ILE   A C   
2786 O  O   . ILE   A 366 ? 0.76097 0.87750 0.58837 0.09730  -0.07028 -0.09353 366 ILE   A O   
2787 C  CB  . ILE   A 366 ? 0.69113 0.82917 0.53887 0.07800  -0.05209 -0.06960 366 ILE   A CB  
2788 C  CG1 . ILE   A 366 ? 0.73663 0.86750 0.57929 0.07692  -0.06018 -0.06876 366 ILE   A CG1 
2789 C  CG2 . ILE   A 366 ? 0.65269 0.80333 0.50990 0.07116  -0.04029 -0.05983 366 ILE   A CG2 
2790 C  CD1 . ILE   A 366 ? 0.73502 0.84985 0.58582 0.07355  -0.07233 -0.07196 366 ILE   A CD1 
2791 N  N   . LYS   A 367 ? 0.73871 0.86312 0.54350 0.10377  -0.07095 -0.09224 367 LYS   A N   
2792 C  CA  . LYS   A 367 ? 0.78247 0.88984 0.57608 0.11150  -0.08501 -0.10316 367 LYS   A CA  
2793 C  C   . LYS   A 367 ? 0.79727 0.90496 0.58003 0.12324  -0.08514 -0.11270 367 LYS   A C   
2794 O  O   . LYS   A 367 ? 0.86877 0.95885 0.64670 0.12792  -0.09758 -0.12168 367 LYS   A O   
2795 C  CB  . LYS   A 367 ? 0.73426 0.83794 0.51116 0.11682  -0.09216 -0.10569 367 LYS   A CB  
2796 C  CG  . LYS   A 367 ? 0.84290 0.93655 0.63048 0.10647  -0.09972 -0.10027 367 LYS   A CG  
2797 C  CD  . LYS   A 367 ? 0.74434 0.83243 0.51441 0.11212  -0.10854 -0.10352 367 LYS   A CD  
2798 C  CE  . LYS   A 367 ? 0.84790 0.95169 0.59851 0.12247  -0.10001 -0.10461 367 LYS   A CE  
2799 N  NZ  . LYS   A 367 ? 0.94715 1.05015 0.68170 0.12667  -0.10513 -0.10492 367 LYS   A NZ  
2800 N  N   . LYS   A 368 ? 0.78513 0.91223 0.56400 0.12812  -0.07241 -0.11072 368 LYS   A N   
2801 C  CA  . LYS   A 368 ? 0.79893 0.92877 0.56880 0.13981  -0.07157 -0.11934 368 LYS   A CA  
2802 C  C   . LYS   A 368 ? 0.87357 0.99608 0.65947 0.13465  -0.07187 -0.12013 368 LYS   A C   
2803 O  O   . LYS   A 368 ? 0.81770 0.94047 0.59701 0.14431  -0.07230 -0.12771 368 LYS   A O   
2804 C  CB  . LYS   A 368 ? 0.80793 0.96409 0.57007 0.14621  -0.05746 -0.11564 368 LYS   A CB  
2805 C  CG  . LYS   A 368 ? 0.83593 1.00260 0.57946 0.15361  -0.05626 -0.11517 368 LYS   A CG  
2806 C  CD  . LYS   A 368 ? 0.91664 1.11093 0.65086 0.16227  -0.04346 -0.11258 368 LYS   A CD  
2807 C  CE  . LYS   A 368 ? 0.95309 1.16707 0.70098 0.14999  -0.03003 -0.09763 368 LYS   A CE  
2808 N  NZ  . LYS   A 368 ? 0.87606 1.10353 0.61203 0.15096  -0.02642 -0.09116 368 LYS   A NZ  
2809 N  N   . TYR   A 369 ? 0.85123 0.96812 0.65725 0.12060  -0.07150 -0.11259 369 TYR   A N   
2810 C  CA  . TYR   A 369 ? 0.85225 0.96434 0.67342 0.11552  -0.07061 -0.11230 369 TYR   A CA  
2811 C  C   . TYR   A 369 ? 0.95669 1.04582 0.77663 0.11768  -0.08597 -0.12086 369 TYR   A C   
2812 O  O   . TYR   A 369 ? 1.00554 1.07983 0.82328 0.11532  -0.09792 -0.12251 369 TYR   A O   
2813 C  CB  . TYR   A 369 ? 0.82101 0.93677 0.66311 0.10082  -0.06434 -0.10107 369 TYR   A CB  
2814 C  CG  . TYR   A 369 ? 0.73632 0.87260 0.58195 0.09757  -0.04970 -0.09230 369 TYR   A CG  
2815 C  CD1 . TYR   A 369 ? 0.67286 0.82565 0.50771 0.10616  -0.04133 -0.09370 369 TYR   A CD1 
2816 C  CD2 . TYR   A 369 ? 0.59048 0.72992 0.44931 0.08629  -0.04509 -0.08230 369 TYR   A CD2 
2817 C  CE1 . TYR   A 369 ? 0.71925 0.89070 0.55813 0.10166  -0.02909 -0.08427 369 TYR   A CE1 
2818 C  CE2 . TYR   A 369 ? 0.55126 0.70672 0.41298 0.08258  -0.03354 -0.07394 369 TYR   A CE2 
2819 C  CZ  . TYR   A 369 ? 0.67160 0.84284 0.52371 0.08952  -0.02583 -0.07450 369 TYR   A CZ  
2820 O  OH  . TYR   A 369 ? 0.73325 0.92003 0.58920 0.08422  -0.01550 -0.06480 369 TYR   A OH  
2821 N  N   . LYS   A 370 ? 0.97398 1.06006 0.79540 0.12192  -0.08624 -0.12590 370 LYS   A N   
2822 C  CA  . LYS   A 370 ? 1.08206 1.14561 0.90415 0.12257  -0.10095 -0.13284 370 LYS   A CA  
2823 C  C   . LYS   A 370 ? 1.10100 1.15847 0.94579 0.10718  -0.10229 -0.12444 370 LYS   A C   
2824 O  O   . LYS   A 370 ? 1.05334 1.12319 0.91244 0.10022  -0.09063 -0.11703 370 LYS   A O   
2825 C  CB  . LYS   A 370 ? 1.16034 1.22301 0.97426 0.13395  -0.10097 -0.14158 370 LYS   A CB  
2826 C  CG  . LYS   A 370 ? 1.23434 1.29511 1.02273 0.15176  -0.10643 -0.15319 370 LYS   A CG  
2827 C  CD  . LYS   A 370 ? 1.17015 1.25199 0.94791 0.15684  -0.09575 -0.15011 370 LYS   A CD  
2828 C  CE  . LYS   A 370 ? 1.26418 1.34646 1.01583 0.17612  -0.10039 -0.16181 370 LYS   A CE  
2829 N  NZ  . LYS   A 370 ? 1.28499 1.38961 1.02569 0.18122  -0.08991 -0.15801 370 LYS   A NZ  
2830 N  N   . VAL   A 371 ? 1.13397 1.17290 0.98183 0.10207  -0.11690 -0.12534 371 VAL   A N   
2831 C  CA  . VAL   A 371 ? 1.08864 1.12403 0.95785 0.08755  -0.11883 -0.11633 371 VAL   A CA  
2832 C  C   . VAL   A 371 ? 1.11257 1.13624 0.98902 0.08578  -0.12512 -0.11881 371 VAL   A C   
2833 O  O   . VAL   A 371 ? 1.03961 1.04509 0.90575 0.09169  -0.13916 -0.12726 371 VAL   A O   
2834 C  CB  . VAL   A 371 ? 1.08445 1.10942 0.95528 0.08153  -0.13087 -0.11381 371 VAL   A CB  
2835 C  CG1 . VAL   A 371 ? 1.05687 1.07587 0.94845 0.06816  -0.13675 -0.10596 371 VAL   A CG1 
2836 C  CG2 . VAL   A 371 ? 0.97726 1.01633 0.84642 0.08020  -0.12220 -0.10832 371 VAL   A CG2 
2837 N  N   . THR   A 372 ? 1.03632 1.06943 0.92984 0.07778  -0.11541 -0.11142 372 THR   A N   
2838 C  CA  . THR   A 372 ? 1.02664 1.05152 0.92805 0.07563  -0.11898 -0.11249 372 THR   A CA  
2839 C  C   . THR   A 372 ? 0.97390 0.99921 0.89701 0.06124  -0.11954 -0.10193 372 THR   A C   
2840 O  O   . THR   A 372 ? 1.04329 1.07009 0.97357 0.05387  -0.12227 -0.09559 372 THR   A O   
2841 C  CB  . THR   A 372 ? 0.92006 0.95778 0.82031 0.08147  -0.10570 -0.11428 372 THR   A CB  
2842 O  OG1 . THR   A 372 ? 0.83807 0.89410 0.75056 0.07431  -0.09086 -0.10475 372 THR   A OG1 
2843 C  CG2 . THR   A 372 ? 0.99997 1.04185 0.87944 0.09635  -0.10367 -0.12368 372 THR   A CG2 
2844 N  N   . LYS   B 17  ? 1.00145 1.80861 1.22338 0.09118  0.07649  0.08602  17  LYS   B N   
2845 C  CA  . LYS   B 17  ? 1.05969 1.84273 1.28963 0.07287  0.07249  0.09015  17  LYS   B CA  
2846 C  C   . LYS   B 17  ? 1.04654 1.79711 1.27591 0.07635  0.06919  0.07563  17  LYS   B C   
2847 O  O   . LYS   B 17  ? 1.03746 1.78007 1.27837 0.06632  0.06469  0.07912  17  LYS   B O   
2848 C  CB  . LYS   B 17  ? 1.01380 1.78926 1.23764 0.06462  0.07399  0.09442  17  LYS   B CB  
2849 C  CG  . LYS   B 17  ? 1.04091 1.79447 1.24986 0.07627  0.07626  0.07898  17  LYS   B CG  
2850 C  CD  . LYS   B 17  ? 1.01846 1.78353 1.21612 0.09797  0.07927  0.06807  17  LYS   B CD  
2851 C  CE  . LYS   B 17  ? 0.95492 1.69651 1.13758 0.10986  0.08006  0.05231  17  LYS   B CE  
2852 N  NZ  . LYS   B 17  ? 0.87407 1.62826 1.04543 0.13096  0.08162  0.04278  17  LYS   B NZ  
2853 N  N   . ALA   B 18  ? 0.99029 1.72203 1.20650 0.09000  0.07065  0.05998  18  ALA   B N   
2854 C  CA  . ALA   B 18  ? 0.95064 1.65197 1.16500 0.09452  0.06733  0.04604  18  ALA   B CA  
2855 C  C   . ALA   B 18  ? 0.96811 1.64306 1.18288 0.08181  0.06556  0.04573  18  ALA   B C   
2856 O  O   . ALA   B 18  ? 0.90444 1.55326 1.11824 0.08335  0.06257  0.03549  18  ALA   B O   
2857 C  CB  . ALA   B 18  ? 0.88733 1.58908 1.11322 0.09306  0.06326  0.04632  18  ALA   B CB  
2858 N  N   . GLN   B 19  ? 0.98156 1.66271 1.19806 0.06894  0.06681  0.05718  19  GLN   B N   
2859 C  CA  . GLN   B 19  ? 1.04152 1.69819 1.25723 0.05780  0.06514  0.05667  19  GLN   B CA  
2860 C  C   . GLN   B 19  ? 1.06520 1.70141 1.26692 0.06995  0.06711  0.04158  19  GLN   B C   
2861 O  O   . GLN   B 19  ? 0.92470 1.53539 1.12563 0.06576  0.06489  0.03553  19  GLN   B O   
2862 C  CB  . GLN   B 19  ? 1.08220 1.74963 1.30014 0.04361  0.06593  0.07121  19  GLN   B CB  
2863 C  CG  . GLN   B 19  ? 1.05422 1.74793 1.26532 0.05130  0.07079  0.07576  19  GLN   B CG  
2864 C  CD  . GLN   B 19  ? 1.12113 1.82396 1.33412 0.03694  0.07093  0.09035  19  GLN   B CD  
2865 O  OE1 . GLN   B 19  ? 1.16906 1.89869 1.38151 0.03776  0.07340  0.09995  19  GLN   B OE1 
2866 N  NE2 . GLN   B 19  ? 1.11758 1.79808 1.33223 0.02404  0.06793  0.09214  19  GLN   B NE2 
2867 N  N   . GLU   B 20  ? 1.05234 1.69952 1.24261 0.08499  0.07071  0.03564  20  GLU   B N   
2868 C  CA  . GLU   B 20  ? 0.95508 1.58225 1.13125 0.09728  0.07139  0.02101  20  GLU   B CA  
2869 C  C   . GLU   B 20  ? 0.89036 1.49377 1.06616 0.10388  0.06747  0.00821  20  GLU   B C   
2870 O  O   . GLU   B 20  ? 0.83672 1.41473 1.00790 0.10324  0.06592  0.00021  20  GLU   B O   
2871 C  CB  . GLU   B 20  ? 0.89028 1.53404 1.05417 0.11397  0.07431  0.01622  20  GLU   B CB  
2872 C  CG  . GLU   B 20  ? 0.81640 1.48012 0.97602 0.11122  0.07827  0.02558  20  GLU   B CG  
2873 C  CD  . GLU   B 20  ? 0.97624 1.66504 1.12785 0.12716  0.08052  0.02401  20  GLU   B CD  
2874 O  OE1 . GLU   B 20  ? 1.07313 1.75802 1.22005 0.14135  0.07860  0.01320  20  GLU   B OE1 
2875 O  OE2 . GLU   B 20  ? 0.87079 1.58342 1.02054 0.12592  0.08375  0.03360  20  GLU   B OE2 
2876 N  N   . GLU   B 21  ? 0.82393 1.43597 1.00432 0.11067  0.06565  0.00632  21  GLU   B N   
2877 C  CA  . GLU   B 21  ? 0.77984 1.37087 0.96058 0.11686  0.06126  -0.00484 21  GLU   B CA  
2878 C  C   . GLU   B 21  ? 0.75574 1.32829 0.94603 0.10211  0.05830  -0.00196 21  GLU   B C   
2879 O  O   . GLU   B 21  ? 0.66464 1.21215 0.85121 0.10499  0.05540  -0.01200 21  GLU   B O   
2880 C  CB  . GLU   B 21  ? 0.74881 1.35599 0.93480 0.12444  0.05982  -0.00457 21  GLU   B CB  
2881 C  CG  . GLU   B 21  ? 0.72554 1.31304 0.91260 0.13082  0.05471  -0.01501 21  GLU   B CG  
2882 C  CD  . GLU   B 21  ? 0.60848 1.18037 0.78001 0.14921  0.05263  -0.03065 21  GLU   B CD  
2883 O  OE1 . GLU   B 21  ? 0.61634 1.19868 0.77673 0.15928  0.05517  -0.03311 21  GLU   B OE1 
2884 O  OE2 . GLU   B 21  ? 0.58267 1.13134 0.75278 0.15345  0.04769  -0.04026 21  GLU   B OE2 
2885 N  N   . SER   B 22  ? 0.80927 1.39381 1.01163 0.08625  0.05822  0.01194  22  SER   B N   
2886 C  CA  . SER   B 22  ? 0.76577 1.33320 0.97656 0.07236  0.05445  0.01493  22  SER   B CA  
2887 C  C   . SER   B 22  ? 0.76751 1.31431 0.97094 0.06864  0.05532  0.01072  22  SER   B C   
2888 O  O   . SER   B 22  ? 0.70195 1.22714 0.90607 0.06627  0.05221  0.00472  22  SER   B O   
2889 C  CB  . SER   B 22  ? 0.89493 1.47822 1.11875 0.05583  0.05283  0.03112  22  SER   B CB  
2890 O  OG  . SER   B 22  ? 0.91285 1.48052 1.14528 0.04447  0.04740  0.03306  22  SER   B OG  
2891 N  N   . LYS   B 23  ? 0.73560 1.28946 0.93167 0.06862  0.05942  0.01370  23  LYS   B N   
2892 C  CA  . LYS   B 23  ? 0.77560 1.31117 0.96393 0.06602  0.06053  0.00958  23  LYS   B CA  
2893 C  C   . LYS   B 23  ? 0.64571 1.16077 0.82321 0.08008  0.05976  -0.00646 23  LYS   B C   
2894 O  O   . LYS   B 23  ? 0.61560 1.10953 0.79070 0.07689  0.05838  -0.01156 23  LYS   B O   
2895 C  CB  . LYS   B 23  ? 0.79378 1.34301 0.97646 0.06369  0.06471  0.01653  23  LYS   B CB  
2896 C  CG  . LYS   B 23  ? 0.84982 1.41326 1.04214 0.04686  0.06427  0.03308  23  LYS   B CG  
2897 C  CD  . LYS   B 23  ? 0.90230 1.47759 1.08825 0.04475  0.06798  0.03967  23  LYS   B CD  
2898 C  CE  . LYS   B 23  ? 0.96972 1.57331 1.16291 0.03834  0.06848  0.05432  23  LYS   B CE  
2899 N  NZ  . LYS   B 23  ? 0.93199 1.54010 1.12628 0.02433  0.06842  0.06700  23  LYS   B NZ  
2900 N  N   . ILE   B 24  ? 0.67558 1.19621 0.84576 0.09575  0.06006  -0.01439 24  ILE   B N   
2901 C  CA  . ILE   B 24  ? 0.61610 1.11505 0.77601 0.10888  0.05736  -0.02948 24  ILE   B CA  
2902 C  C   . ILE   B 24  ? 0.59691 1.07738 0.76343 0.10582  0.05274  -0.03393 24  ILE   B C   
2903 O  O   . ILE   B 24  ? 0.49990 0.95749 0.66157 0.10747  0.05041  -0.04226 24  ILE   B O   
2904 C  CB  . ILE   B 24  ? 0.60194 1.10984 0.75325 0.12611  0.05682  -0.03675 24  ILE   B CB  
2905 C  CG1 . ILE   B 24  ? 0.57781 1.10632 0.72215 0.12989  0.06126  -0.03211 24  ILE   B CG1 
2906 C  CG2 . ILE   B 24  ? 0.50874 0.99065 0.64949 0.13852  0.05205  -0.05205 24  ILE   B CG2 
2907 C  CD1 . ILE   B 24  ? 0.59078 1.13060 0.72636 0.14714  0.06048  -0.03864 24  ILE   B CD1 
2908 N  N   . GLU   B 25  ? 0.55075 1.04136 0.72830 0.10190  0.05094  -0.02856 25  GLU   B N   
2909 C  CA  . GLU   B 25  ? 0.53533 1.00886 0.71897 0.09861  0.04600  -0.03207 25  GLU   B CA  
2910 C  C   . GLU   B 25  ? 0.50361 0.95042 0.68524 0.08180  0.04388  -0.02709 25  GLU   B C   
2911 O  O   . GLU   B 25  ? 0.46292 0.87725 0.63798 0.07963  0.03936  -0.03295 25  GLU   B O   
2912 C  CB  . GLU   B 25  ? 0.51530 1.00575 0.71061 0.09668  0.04420  -0.02594 25  GLU   B CB  
2913 C  CG  . GLU   B 25  ? 0.64465 1.14716 0.83414 0.11233  0.04464  -0.03113 25  GLU   B CG  
2914 C  CD  . GLU   B 25  ? 0.80351 1.30751 0.99987 0.11661  0.04032  -0.03315 25  GLU   B CD  
2915 O  OE1 . GLU   B 25  ? 0.84446 1.33122 1.03436 0.12807  0.03623  -0.04481 25  GLU   B OE1 
2916 O  OE2 . GLU   B 25  ? 0.83237 1.35312 1.04073 0.10766  0.04019  -0.02280 25  GLU   B OE2 
2917 N  N   . ASP   B 26  ? 0.56843 1.02887 0.75554 0.06990  0.04672  -0.01585 26  ASP   B N   
2918 C  CA  . ASP   B 26  ? 0.56045 0.99515 0.74426 0.05540  0.04425  -0.01173 26  ASP   B CA  
2919 C  C   . ASP   B 26  ? 0.54655 0.95558 0.71694 0.05951  0.04445  -0.02072 26  ASP   B C   
2920 O  O   . ASP   B 26  ? 0.49556 0.87424 0.66045 0.05429  0.04065  -0.02382 26  ASP   B O   
2921 C  CB  . ASP   B 26  ? 0.65751 1.11169 0.84814 0.04321  0.04669  0.00160  26  ASP   B CB  
2922 C  CG  . ASP   B 26  ? 0.77031 1.24775 0.97544 0.03600  0.04490  0.01244  26  ASP   B CG  
2923 O  OD1 . ASP   B 26  ? 0.81817 1.32392 1.03120 0.03018  0.04774  0.02360  26  ASP   B OD1 
2924 O  OD2 . ASP   B 26  ? 0.75940 1.22824 0.96821 0.03666  0.04049  0.00995  26  ASP   B OD2 
2925 N  N   . VAL   B 27  ? 0.51893 0.94076 0.68378 0.06929  0.04868  -0.02480 27  VAL   B N   
2926 C  CA  . VAL   B 27  ? 0.56789 0.96646 0.72036 0.07279  0.04826  -0.03277 27  VAL   B CA  
2927 C  C   . VAL   B 27  ? 0.50908 0.88139 0.65538 0.07990  0.04305  -0.04349 27  VAL   B C   
2928 O  O   . VAL   B 27  ? 0.41403 0.75831 0.55376 0.07553  0.04015  -0.04670 27  VAL   B O   
2929 C  CB  . VAL   B 27  ? 0.51584 0.93424 0.66294 0.08329  0.05307  -0.03559 27  VAL   B CB  
2930 C  CG1 . VAL   B 27  ? 0.48975 0.88312 0.62387 0.08746  0.05148  -0.04442 27  VAL   B CG1 
2931 C  CG2 . VAL   B 27  ? 0.45691 0.90114 0.61025 0.07488  0.05803  -0.02358 27  VAL   B CG2 
2932 N  N   . ASP   B 28  ? 0.50093 0.88278 0.64938 0.09107  0.04151  -0.04870 28  ASP   B N   
2933 C  CA  . ASP   B 28  ? 0.50072 0.85768 0.64331 0.09786  0.03558  -0.05836 28  ASP   B CA  
2934 C  C   . ASP   B 28  ? 0.50305 0.83636 0.64789 0.08614  0.03165  -0.05525 28  ASP   B C   
2935 O  O   . ASP   B 28  ? 0.49113 0.79738 0.62914 0.08652  0.02730  -0.06091 28  ASP   B O   
2936 C  CB  . ASP   B 28  ? 0.59849 0.97043 0.74416 0.11106  0.03391  -0.06333 28  ASP   B CB  
2937 C  CG  . ASP   B 28  ? 0.68449 1.07739 0.82516 0.12666  0.03676  -0.06904 28  ASP   B CG  
2938 O  OD1 . ASP   B 28  ? 0.66491 1.04959 0.79615 0.12943  0.03755  -0.07305 28  ASP   B OD1 
2939 O  OD2 . ASP   B 28  ? 0.69531 1.11237 0.84086 0.13713  0.03774  -0.07006 28  ASP   B OD2 
2940 N  N   . LYS   B 29  ? 0.47624 0.81991 0.63056 0.07617  0.03244  -0.04615 29  LYS   B N   
2941 C  CA  . LYS   B 29  ? 0.45673 0.77806 0.61189 0.06609  0.02837  -0.04354 29  LYS   B CA  
2942 C  C   . LYS   B 29  ? 0.56017 0.86097 0.70865 0.05734  0.02870  -0.04196 29  LYS   B C   
2943 O  O   . LYS   B 29  ? 0.46399 0.73976 0.60705 0.05531  0.02532  -0.04523 29  LYS   B O   
2944 C  CB  . LYS   B 29  ? 0.49304 0.82897 0.65912 0.05770  0.02779  -0.03440 29  LYS   B CB  
2945 C  CG  . LYS   B 29  ? 0.65886 0.97244 0.82427 0.04587  0.02387  -0.03036 29  LYS   B CG  
2946 C  CD  . LYS   B 29  ? 0.75980 1.08765 0.93405 0.03465  0.02350  -0.01935 29  LYS   B CD  
2947 C  CE  . LYS   B 29  ? 0.67356 1.01986 0.84940 0.03084  0.02824  -0.01316 29  LYS   B CE  
2948 N  NZ  . LYS   B 29  ? 0.75572 1.08620 0.92789 0.01840  0.02670  -0.00724 29  LYS   B NZ  
2949 N  N   . ILE   B 30  ? 0.55653 0.86868 0.70541 0.05222  0.03271  -0.03646 30  ILE   B N   
2950 C  CA  . ILE   B 30  ? 0.54958 0.84301 0.69201 0.04461  0.03290  -0.03500 30  ILE   B CA  
2951 C  C   . ILE   B 30  ? 0.52240 0.79717 0.65545 0.05144  0.03174  -0.04380 30  ILE   B C   
2952 O  O   . ILE   B 30  ? 0.55029 0.80297 0.67842 0.04665  0.02972  -0.04451 30  ILE   B O   
2953 C  CB  . ILE   B 30  ? 0.55986 0.86969 0.70370 0.03939  0.03710  -0.02811 30  ILE   B CB  
2954 C  CG1 . ILE   B 30  ? 0.53637 0.86106 0.68961 0.02967  0.03658  -0.01760 30  ILE   B CG1 
2955 C  CG2 . ILE   B 30  ? 0.55232 0.84295 0.68778 0.03486  0.03747  -0.02883 30  ILE   B CG2 
2956 C  CD1 . ILE   B 30  ? 0.53766 0.88400 0.69389 0.02527  0.04045  -0.00970 30  ILE   B CD1 
2957 N  N   . LEU   B 31  ? 0.48552 0.76946 0.61574 0.06291  0.03256  -0.05032 31  LEU   B N   
2958 C  CA  . LEU   B 31  ? 0.51805 0.78400 0.63932 0.06981  0.02978  -0.05881 31  LEU   B CA  
2959 C  C   . LEU   B 31  ? 0.56107 0.80529 0.68093 0.07032  0.02409  -0.06266 31  LEU   B C   
2960 O  O   . LEU   B 31  ? 0.54881 0.77181 0.66340 0.06735  0.02142  -0.06440 31  LEU   B O   
2961 C  CB  . LEU   B 31  ? 0.45346 0.73446 0.57137 0.08320  0.03068  -0.06525 31  LEU   B CB  
2962 C  CG  . LEU   B 31  ? 0.52985 0.79322 0.63800 0.09227  0.02601  -0.07490 31  LEU   B CG  
2963 C  CD1 . LEU   B 31  ? 0.48542 0.73771 0.58729 0.08745  0.02699  -0.07441 31  LEU   B CD1 
2964 C  CD2 . LEU   B 31  ? 0.54644 0.82547 0.65118 0.10748  0.02572  -0.08188 31  LEU   B CD2 
2965 N  N   . ASN   B 32  ? 0.56498 0.81512 0.68978 0.07407  0.02198  -0.06351 32  ASN   B N   
2966 C  CA  . ASN   B 32  ? 0.52361 0.75316 0.64703 0.07368  0.01643  -0.06616 32  ASN   B CA  
2967 C  C   . ASN   B 32  ? 0.55269 0.76722 0.67647 0.06191  0.01615  -0.06037 32  ASN   B C   
2968 O  O   . ASN   B 32  ? 0.63105 0.82520 0.75070 0.06040  0.01243  -0.06213 32  ASN   B O   
2969 C  CB  . ASN   B 32  ? 0.63379 0.87339 0.76287 0.07929  0.01426  -0.06739 32  ASN   B CB  
2970 C  CG  . ASN   B 32  ? 0.85030 1.08929 0.97493 0.09288  0.01057  -0.07626 32  ASN   B CG  
2971 O  OD1 . ASN   B 32  ? 0.90059 1.15932 1.02546 0.10201  0.01302  -0.07902 32  ASN   B OD1 
2972 N  ND2 . ASN   B 32  ? 0.91674 1.13239 1.03624 0.09479  0.00413  -0.08083 32  ASN   B ND2 
2973 N  N   . ASP   B 33  ? 0.56248 0.78650 0.69063 0.05369  0.01948  -0.05321 33  ASP   B N   
2974 C  CA  . ASP   B 33  ? 0.61082 0.81921 0.73744 0.04414  0.01849  -0.04865 33  ASP   B CA  
2975 C  C   . ASP   B 33  ? 0.55196 0.74707 0.67174 0.04157  0.01960  -0.04928 33  ASP   B C   
2976 O  O   . ASP   B 33  ? 0.63134 0.80854 0.74701 0.03965  0.01722  -0.05005 33  ASP   B O   
2977 C  CB  . ASP   B 33  ? 0.54451 0.76367 0.67675 0.03606  0.01983  -0.04095 33  ASP   B CB  
2978 C  CG  . ASP   B 33  ? 0.68451 0.91538 0.82439 0.03722  0.01771  -0.03932 33  ASP   B CG  
2979 O  OD1 . ASP   B 33  ? 0.58544 0.83284 0.73190 0.03236  0.01884  -0.03301 33  ASP   B OD1 
2980 O  OD2 . ASP   B 33  ? 0.66846 0.89234 0.80806 0.04260  0.01448  -0.04380 33  ASP   B OD2 
2981 N  N   . ILE   B 34  ? 0.59869 0.80362 0.71733 0.04185  0.02317  -0.04869 34  ILE   B N   
2982 C  CA  . ILE   B 34  ? 0.50830 0.70209 0.62081 0.03993  0.02407  -0.04941 34  ILE   B CA  
2983 C  C   . ILE   B 34  ? 0.60553 0.78374 0.71341 0.04472  0.02029  -0.05517 34  ILE   B C   
2984 O  O   . ILE   B 34  ? 0.62751 0.79136 0.73175 0.04100  0.01927  -0.05424 34  ILE   B O   
2985 C  CB  . ILE   B 34  ? 0.49567 0.70418 0.60740 0.04169  0.02794  -0.04909 34  ILE   B CB  
2986 C  CG1 . ILE   B 34  ? 0.53457 0.75579 0.65052 0.03434  0.03089  -0.04142 34  ILE   B CG1 
2987 C  CG2 . ILE   B 34  ? 0.46921 0.66649 0.57428 0.04240  0.02786  -0.05186 34  ILE   B CG2 
2988 C  CD1 . ILE   B 34  ? 0.61185 0.84545 0.72639 0.03411  0.03461  -0.03948 34  ILE   B CD1 
2989 N  N   . LEU   B 35  ? 0.60254 0.78377 0.71033 0.05326  0.01766  -0.06091 35  LEU   B N   
2990 C  CA  . LEU   B 35  ? 0.61839 0.78325 0.72171 0.05748  0.01223  -0.06603 35  LEU   B CA  
2991 C  C   . LEU   B 35  ? 0.64168 0.79235 0.74587 0.05369  0.00869  -0.06409 35  LEU   B C   
2992 O  O   . LEU   B 35  ? 0.69537 0.83067 0.79610 0.05375  0.00428  -0.06561 35  LEU   B O   
2993 C  CB  . LEU   B 35  ? 0.58680 0.75736 0.68862 0.06871  0.00916  -0.07320 35  LEU   B CB  
2994 C  CG  . LEU   B 35  ? 0.58614 0.76750 0.68411 0.07507  0.01124  -0.07694 35  LEU   B CG  
2995 C  CD1 . LEU   B 35  ? 0.49387 0.68818 0.59125 0.08725  0.00996  -0.08303 35  LEU   B CD1 
2996 C  CD2 . LEU   B 35  ? 0.57684 0.74164 0.66787 0.07531  0.00735  -0.08008 35  LEU   B CD2 
2997 N  N   . SER   B 36  ? 0.74018 0.89600 0.84883 0.05048  0.00989  -0.06048 36  SER   B N   
2998 C  CA  . SER   B 36  ? 0.64480 0.78811 0.75356 0.04788  0.00640  -0.05889 36  SER   B CA  
2999 C  C   . SER   B 36  ? 0.70269 0.83205 0.80772 0.04146  0.00644  -0.05513 36  SER   B C   
3000 O  O   . SER   B 36  ? 0.65380 0.77038 0.75672 0.04124  0.00252  -0.05518 36  SER   B O   
3001 C  CB  . SER   B 36  ? 0.73514 0.88718 0.84886 0.04511  0.00765  -0.05536 36  SER   B CB  
3002 O  OG  . SER   B 36  ? 0.61908 0.77516 0.73314 0.03820  0.01149  -0.05017 36  SER   B OG  
3003 N  N   . ILE   B 37  ? 0.73861 0.87102 0.84277 0.03635  0.01065  -0.05137 37  ILE   B N   
3004 C  CA  . ILE   B 37  ? 0.85837 0.98005 0.95893 0.03126  0.01122  -0.04757 37  ILE   B CA  
3005 C  C   . ILE   B 37  ? 0.81978 0.93519 0.91748 0.03168  0.01037  -0.04865 37  ILE   B C   
3006 O  O   . ILE   B 37  ? 0.72592 0.83504 0.82119 0.02790  0.01127  -0.04513 37  ILE   B O   
3007 C  CB  . ILE   B 37  ? 0.80326 0.92874 0.90308 0.02623  0.01490  -0.04324 37  ILE   B CB  
3008 C  CG1 . ILE   B 37  ? 0.72943 0.86607 0.83023 0.02603  0.01824  -0.04343 37  ILE   B CG1 
3009 C  CG2 . ILE   B 37  ? 0.63858 0.76512 0.74018 0.02428  0.01378  -0.04098 37  ILE   B CG2 
3010 C  CD1 . ILE   B 37  ? 0.64939 0.78402 0.74736 0.02712  0.01924  -0.04507 37  ILE   B CD1 
3011 N  N   . SER   B 38  ? 0.66143 0.77865 0.75907 0.03656  0.00825  -0.05337 38  SER   B N   
3012 C  CA  . SER   B 38  ? 0.56399 0.67496 0.65881 0.03681  0.00633  -0.05458 38  SER   B CA  
3013 C  C   . SER   B 38  ? 0.57928 0.67778 0.67304 0.03857  -0.00061 -0.05626 38  SER   B C   
3014 O  O   . SER   B 38  ? 0.60899 0.70540 0.70356 0.04245  -0.00424 -0.05904 38  SER   B O   
3015 C  CB  . SER   B 38  ? 0.55700 0.67703 0.65081 0.04134  0.00770  -0.05885 38  SER   B CB  
3016 O  OG  . SER   B 38  ? 0.64154 0.76221 0.73488 0.04890  0.00354  -0.06479 38  SER   B OG  
3017 N  N   . SER   B 39  ? 0.48759 0.57776 0.57979 0.03525  -0.00301 -0.05387 39  SER   B N   
3018 C  CA  . SER   B 39  ? 0.48413 0.56197 0.57521 0.03631  -0.01108 -0.05510 39  SER   B CA  
3019 C  C   . SER   B 39  ? 0.58364 0.65884 0.67164 0.04166  -0.01563 -0.06131 39  SER   B C   
3020 O  O   . SER   B 39  ? 0.52250 0.58724 0.60840 0.04534  -0.02376 -0.06489 39  SER   B O   
3021 C  CB  . SER   B 39  ? 0.50412 0.57504 0.59586 0.02939  -0.01245 -0.04805 39  SER   B CB  
3022 O  OG  . SER   B 39  ? 0.55799 0.62891 0.64898 0.02718  -0.01245 -0.04701 39  SER   B OG  
3023 N  N   . GLU   B 40  ? 0.50433 0.58815 0.59113 0.04279  -0.01115 -0.06297 40  GLU   B N   
3024 C  CA  . GLU   B 40  ? 0.47907 0.56106 0.56160 0.04937  -0.01547 -0.06966 40  GLU   B CA  
3025 C  C   . GLU   B 40  ? 0.54141 0.63835 0.62315 0.05204  -0.00842 -0.07154 40  GLU   B C   
3026 O  O   . GLU   B 40  ? 0.49756 0.60143 0.58136 0.04649  -0.00199 -0.06663 40  GLU   B O   
3027 C  CB  . GLU   B 40  ? 0.52913 0.59853 0.60937 0.04618  -0.02212 -0.06851 40  GLU   B CB  
3028 C  CG  . GLU   B 40  ? 0.52696 0.59461 0.60148 0.05280  -0.02613 -0.07540 40  GLU   B CG  
3029 C  CD  . GLU   B 40  ? 0.68499 0.74127 0.75778 0.04828  -0.03252 -0.07333 40  GLU   B CD  
3030 O  OE1 . GLU   B 40  ? 0.57510 0.63578 0.65086 0.04126  -0.02789 -0.06730 40  GLU   B OE1 
3031 O  OE2 . GLU   B 40  ? 0.66795 0.71066 0.73606 0.05224  -0.04291 -0.07797 40  GLU   B OE2 
3032 N  N   . CYS   B 41  ? 0.49118 0.59327 0.56941 0.06096  -0.00995 -0.07844 41  CYS   B N   
3033 C  CA  . CYS   B 41  ? 0.48061 0.59834 0.55761 0.06405  -0.00370 -0.07989 41  CYS   B CA  
3034 C  C   . CYS   B 41  ? 0.49377 0.60790 0.56355 0.07149  -0.00853 -0.08660 41  CYS   B C   
3035 O  O   . CYS   B 41  ? 0.53966 0.64714 0.60522 0.07978  -0.01534 -0.09315 41  CYS   B O   
3036 C  CB  . CYS   B 41  ? 0.44789 0.58167 0.52809 0.06839  0.00098  -0.08074 41  CYS   B CB  
3037 S  SG  . CYS   B 41  ? 0.53287 0.68840 0.61209 0.07132  0.00862  -0.08074 41  CYS   B SG  
3038 N  N   . ILE   B 42  ? 0.45769 0.57512 0.52523 0.06900  -0.00570 -0.08525 42  ILE   B N   
3039 C  CA  . ILE   B 42  ? 0.43429 0.54906 0.49396 0.07610  -0.00997 -0.09155 42  ILE   B CA  
3040 C  C   . ILE   B 42  ? 0.48019 0.61511 0.53888 0.07900  -0.00165 -0.09137 42  ILE   B C   
3041 O  O   . ILE   B 42  ? 0.44544 0.58524 0.50625 0.07183  0.00364  -0.08586 42  ILE   B O   
3042 C  CB  . ILE   B 42  ? 0.48817 0.58880 0.54601 0.07002  -0.01486 -0.08942 42  ILE   B CB  
3043 C  CG1 . ILE   B 42  ? 0.50575 0.58910 0.56654 0.06453  -0.02226 -0.08662 42  ILE   B CG1 
3044 C  CG2 . ILE   B 42  ? 0.52427 0.62104 0.57281 0.07772  -0.02023 -0.09645 42  ILE   B CG2 
3045 C  CD1 . ILE   B 42  ? 0.61871 0.68843 0.67434 0.07213  -0.03287 -0.09349 42  ILE   B CD1 
3046 N  N   . GLN   B 43  ? 0.41685 0.56499 0.47270 0.08926  -0.00017 -0.09651 43  GLN   B N   
3047 C  CA  . GLN   B 43  ? 0.50228 0.64882 0.55646 0.09884  -0.00499 -0.10270 43  GLN   B CA  
3048 C  C   . GLN   B 43  ? 0.49715 0.66502 0.55780 0.10031  0.00249  -0.09989 43  GLN   B C   
3049 O  O   . GLN   B 43  ? 0.41713 0.60313 0.48067 0.09742  0.01044  -0.09524 43  GLN   B O   
3050 C  CB  . GLN   B 43  ? 0.47973 0.62472 0.52307 0.11265  -0.01076 -0.11249 43  GLN   B CB  
3051 C  CG  . GLN   B 43  ? 0.54007 0.66358 0.57620 0.11168  -0.01969 -0.11565 43  GLN   B CG  
3052 C  CD  . GLN   B 43  ? 0.56285 0.66307 0.59904 0.10977  -0.03025 -0.11708 43  GLN   B CD  
3053 O  OE1 . GLN   B 43  ? 0.64589 0.74590 0.68777 0.10822  -0.02991 -0.11513 43  GLN   B OE1 
3054 N  NE2 . GLN   B 43  ? 0.60451 0.68515 0.63450 0.10951  -0.04016 -0.11995 43  GLN   B NE2 
3055 N  N   . PRO   B 44  ? 0.52326 0.68900 0.58632 0.10456  -0.00072 -0.10228 44  PRO   B N   
3056 C  CA  . PRO   B 44  ? 0.48006 0.66650 0.55025 0.10558  0.00560  -0.09913 44  PRO   B CA  
3057 C  C   . PRO   B 44  ? 0.44819 0.65991 0.51672 0.11451  0.01112  -0.10092 44  PRO   B C   
3058 O  O   . PRO   B 44  ? 0.47184 0.70359 0.54737 0.10938  0.01878  -0.09396 44  PRO   B O   
3059 C  CB  . PRO   B 44  ? 0.55761 0.73444 0.62829 0.11126  -0.00097 -0.10352 44  PRO   B CB  
3060 C  CG  . PRO   B 44  ? 0.52275 0.67283 0.59026 0.10654  -0.00898 -0.10440 44  PRO   B CG  
3061 C  CD  . PRO   B 44  ? 0.52795 0.67137 0.58873 0.10598  -0.01044 -0.10604 44  PRO   B CD  
3062 N  N   . ASP   B 45  ? 0.49034 0.70249 0.54950 0.12794  0.00711  -0.10967 45  ASP   B N   
3063 C  CA  . ASP   B 45  ? 0.54737 0.78652 0.60439 0.13708  0.01321  -0.11073 45  ASP   B CA  
3064 C  C   . ASP   B 45  ? 0.53162 0.78166 0.58947 0.12905  0.02024  -0.10408 45  ASP   B C   
3065 O  O   . ASP   B 45  ? 0.47479 0.75158 0.53595 0.13036  0.02774  -0.09961 45  ASP   B O   
3066 C  CB  . ASP   B 45  ? 0.64350 0.88104 0.68827 0.15467  0.00738  -0.12208 45  ASP   B CB  
3067 C  CG  . ASP   B 45  ? 0.87846 1.10629 0.92139 0.16473  -0.00030 -0.12934 45  ASP   B CG  
3068 O  OD1 . ASP   B 45  ? 0.92054 1.16424 0.97172 0.16594  0.00332  -0.12654 45  ASP   B OD1 
3069 O  OD2 . ASP   B 45  ? 1.01645 1.22143 1.04912 0.17221  -0.01055 -0.13799 45  ASP   B OD2 
3070 N  N   . GLU   B 46  ? 0.45495 0.68562 0.50971 0.12103  0.01758  -0.10302 46  GLU   B N   
3071 C  CA  . GLU   B 46  ? 0.41854 0.65792 0.47432 0.11280  0.02379  -0.09635 46  GLU   B CA  
3072 C  C   . GLU   B 46  ? 0.38384 0.63368 0.45066 0.10040  0.03020  -0.08586 46  GLU   B C   
3073 O  O   . GLU   B 46  ? 0.43645 0.70444 0.50563 0.09652  0.03660  -0.07960 46  GLU   B O   
3074 C  CB  . GLU   B 46  ? 0.42586 0.64213 0.47650 0.10733  0.01893  -0.09754 46  GLU   B CB  
3075 C  CG  . GLU   B 46  ? 0.46753 0.67225 0.50621 0.11920  0.01122  -0.10775 46  GLU   B CG  
3076 C  CD  . GLU   B 46  ? 0.52875 0.71228 0.56347 0.11247  0.00613  -0.10763 46  GLU   B CD  
3077 O  OE1 . GLU   B 46  ? 0.58931 0.77336 0.62942 0.10077  0.01073  -0.09987 46  GLU   B OE1 
3078 O  OE2 . GLU   B 46  ? 0.54810 0.71460 0.57442 0.11896  -0.00298 -0.11506 46  GLU   B OE2 
3079 N  N   . LEU   B 47  ? 0.42409 0.66184 0.49700 0.09410  0.02783  -0.08371 47  LEU   B N   
3080 C  CA  . LEU   B 47  ? 0.43477 0.67932 0.51701 0.08299  0.03227  -0.07457 47  LEU   B CA  
3081 C  C   . LEU   B 47  ? 0.40247 0.67394 0.49061 0.08610  0.03711  -0.07114 47  LEU   B C   
3082 O  O   . LEU   B 47  ? 0.44901 0.73455 0.54255 0.07812  0.04205  -0.06266 47  LEU   B O   
3083 C  CB  . LEU   B 47  ? 0.48521 0.71128 0.57114 0.07781  0.02806  -0.07415 47  LEU   B CB  
3084 C  CG  . LEU   B 47  ? 0.46174 0.69100 0.55570 0.06702  0.03114  -0.06567 47  LEU   B CG  
3085 C  CD1 . LEU   B 47  ? 0.47856 0.70918 0.57245 0.05790  0.03491  -0.05906 47  LEU   B CD1 
3086 C  CD2 . LEU   B 47  ? 0.47813 0.68744 0.57342 0.06327  0.02660  -0.06616 47  LEU   B CD2 
3087 N  N   . ARG   B 48  ? 0.43197 0.71133 0.51906 0.09789  0.03519  -0.07735 48  ARG   B N   
3088 C  CA  . ARG   B 48  ? 0.41984 0.72920 0.51231 0.10304  0.04006  -0.07436 48  ARG   B CA  
3089 C  C   . ARG   B 48  ? 0.47662 0.80803 0.56715 0.10372  0.04616  -0.07020 48  ARG   B C   
3090 O  O   . ARG   B 48  ? 0.47434 0.82788 0.57275 0.09751  0.05140  -0.06094 48  ARG   B O   
3091 C  CB  . ARG   B 48  ? 0.47332 0.78618 0.56234 0.11846  0.03636  -0.08356 48  ARG   B CB  
3092 C  CG  . ARG   B 48  ? 0.56823 0.91208 0.66469 0.12386  0.04083  -0.08016 48  ARG   B CG  
3093 C  CD  . ARG   B 48  ? 0.60896 0.95385 0.70260 0.13923  0.03628  -0.08944 48  ARG   B CD  
3094 N  NE  . ARG   B 48  ? 0.68780 1.05652 0.79268 0.13913  0.03949  -0.08385 48  ARG   B NE  
3095 C  CZ  . ARG   B 48  ? 0.78572 1.18755 0.89736 0.13836  0.04657  -0.07604 48  ARG   B CZ  
3096 N  NH1 . ARG   B 48  ? 0.65158 1.06379 0.75864 0.13672  0.05102  -0.07245 48  ARG   B NH1 
3097 N  NH2 . ARG   B 48  ? 0.71985 1.14016 0.84154 0.13666  0.04804  -0.06997 48  ARG   B NH2 
3098 N  N   . VAL   B 49  ? 0.39225 0.71788 0.47213 0.11078  0.04502  -0.07637 49  VAL   B N   
3099 C  CA  . VAL   B 49  ? 0.44690 0.79266 0.52390 0.11144  0.05070  -0.07230 49  VAL   B CA  
3100 C  C   . VAL   B 49  ? 0.49861 0.84387 0.58139 0.09510  0.05413  -0.06125 49  VAL   B C   
3101 O  O   . VAL   B 49  ? 0.50728 0.87620 0.59451 0.09101  0.05961  -0.05269 49  VAL   B O   
3102 C  CB  . VAL   B 49  ? 0.49964 0.83504 0.56314 0.12136  0.04763  -0.08136 49  VAL   B CB  
3103 C  CG1 . VAL   B 49  ? 0.50758 0.85764 0.56809 0.11834  0.05300  -0.07588 49  VAL   B CG1 
3104 C  CG2 . VAL   B 49  ? 0.46949 0.81468 0.52553 0.14028  0.04539  -0.09142 49  VAL   B CG2 
3105 N  N   . LYS   B 50  ? 0.47114 0.78977 0.55303 0.08612  0.05057  -0.06118 50  LYS   B N   
3106 C  CA  . LYS   B 50  ? 0.45494 0.77087 0.54121 0.07181  0.05284  -0.05152 50  LYS   B CA  
3107 C  C   . LYS   B 50  ? 0.56438 0.89766 0.66132 0.06439  0.05565  -0.04207 50  LYS   B C   
3108 O  O   . LYS   B 50  ? 0.53852 0.88692 0.63879 0.05715  0.05918  -0.03297 50  LYS   B O   
3109 C  CB  . LYS   B 50  ? 0.50794 0.79451 0.59308 0.06465  0.04841  -0.05295 50  LYS   B CB  
3110 C  CG  . LYS   B 50  ? 0.48350 0.75384 0.55926 0.06924  0.04527  -0.05994 50  LYS   B CG  
3111 C  CD  . LYS   B 50  ? 0.42976 0.68870 0.50482 0.05917  0.04568  -0.05488 50  LYS   B CD  
3112 C  CE  . LYS   B 50  ? 0.40706 0.64874 0.47431 0.06226  0.04177  -0.06096 50  LYS   B CE  
3113 N  NZ  . LYS   B 50  ? 0.46809 0.71692 0.53133 0.05982  0.04483  -0.05747 50  LYS   B NZ  
3114 N  N   . LEU   B 51  ? 0.41916 0.75078 0.52153 0.06604  0.05347  -0.04378 51  LEU   B N   
3115 C  CA  . LEU   B 51  ? 0.59295 0.94160 0.70585 0.05913  0.05524  -0.03476 51  LEU   B CA  
3116 C  C   . LEU   B 51  ? 0.55393 0.93715 0.67035 0.06320  0.06049  -0.02950 51  LEU   B C   
3117 O  O   . LEU   B 51  ? 0.51708 0.91544 0.64028 0.05335  0.06272  -0.01843 51  LEU   B O   
3118 C  CB  . LEU   B 51  ? 0.47545 0.81801 0.59302 0.06210  0.05185  -0.03841 51  LEU   B CB  
3119 C  CG  . LEU   B 51  ? 0.47798 0.79011 0.59380 0.05626  0.04708  -0.04091 51  LEU   B CG  
3120 C  CD1 . LEU   B 51  ? 0.46646 0.76974 0.58417 0.06144  0.04318  -0.04645 51  LEU   B CD1 
3121 C  CD2 . LEU   B 51  ? 0.54143 0.84510 0.66081 0.04194  0.04659  -0.03197 51  LEU   B CD2 
3122 N  N   . LEU   B 52  ? 0.50261 0.89853 0.61339 0.07743  0.06224  -0.03672 52  LEU   B N   
3123 C  CA  . LEU   B 52  ? 0.52814 0.96054 0.64369 0.08010  0.06789  -0.02954 52  LEU   B CA  
3124 C  C   . LEU   B 52  ? 0.57379 1.01515 0.68748 0.07221  0.07144  -0.02118 52  LEU   B C   
3125 O  O   . LEU   B 52  ? 0.48775 0.95498 0.60495 0.07039  0.07502  -0.01221 52  LEU   B O   
3126 C  CB  . LEU   B 52  ? 0.57256 1.01862 0.68112 0.09790  0.06875  -0.03795 52  LEU   B CB  
3127 C  CG  . LEU   B 52  ? 0.57088 1.00855 0.67946 0.10849  0.06460  -0.04760 52  LEU   B CG  
3128 C  CD1 . LEU   B 52  ? 0.55797 0.99524 0.65273 0.12556  0.06268  -0.05760 52  LEU   B CD1 
3129 C  CD2 . LEU   B 52  ? 0.59685 1.04903 0.71713 0.10449  0.06466  -0.04071 52  LEU   B CD2 
3130 N  N   . LEU   B 53  ? 0.64151 1.05752 0.74905 0.06540  0.06913  -0.02235 53  LEU   B N   
3131 C  CA  . LEU   B 53  ? 0.61550 1.03659 0.72037 0.05793  0.07164  -0.01494 53  LEU   B CA  
3132 C  C   . LEU   B 53  ? 0.74851 1.18287 0.86358 0.04349  0.07248  -0.00047 53  LEU   B C   
3133 O  O   . LEU   B 53  ? 0.66314 1.10609 0.77694 0.03690  0.07448  0.00753  53  LEU   B O   
3134 C  CB  . LEU   B 53  ? 0.65444 1.04319 0.75188 0.05343  0.06797  -0.01948 53  LEU   B CB  
3135 C  CG  . LEU   B 53  ? 0.61187 0.98924 0.69887 0.06686  0.06635  -0.03244 53  LEU   B CG  
3136 C  CD1 . LEU   B 53  ? 0.57060 0.91633 0.65121 0.06213  0.06225  -0.03656 53  LEU   B CD1 
3137 C  CD2 . LEU   B 53  ? 0.49986 0.90252 0.58082 0.07846  0.07061  -0.03430 53  LEU   B CD2 
3138 N  N   . LYS   B 54  ? 0.85378 1.28741 0.97827 0.03813  0.06997  0.00293  54  LYS   B N   
3139 C  CA  . LYS   B 54  ? 0.74339 1.18988 0.87879 0.02465  0.06905  0.01667  54  LYS   B CA  
3140 C  C   . LYS   B 54  ? 0.79860 1.22421 0.93199 0.01065  0.06539  0.02313  54  LYS   B C   
3141 O  O   . LYS   B 54  ? 0.88808 1.32686 1.02552 0.00058  0.06550  0.03515  54  LYS   B O   
3142 C  CB  . LYS   B 54  ? 0.76645 1.25353 0.90832 0.02572  0.07422  0.02646  54  LYS   B CB  
3143 C  CG  . LYS   B 54  ? 0.75057 1.25138 0.89284 0.03764  0.07506  0.02217  54  LYS   B CG  
3144 C  CD  . LYS   B 54  ? 0.73794 1.26487 0.87969 0.03807  0.07745  0.03183  54  LYS   B CD  
3145 C  CE  . LYS   B 54  ? 0.82293 1.36510 0.96588 0.04926  0.07795  0.02868  54  LYS   B CE  
3146 N  NZ  . LYS   B 54  ? 0.86445 1.43545 1.00897 0.04872  0.08001  0.03978  54  LYS   B NZ  
3147 N  N   . ARG   B 55  ? 0.72593 1.11888 0.85326 0.00994  0.06155  0.01559  55  ARG   B N   
3148 C  CA  . ARG   B 55  ? 0.68976 1.06205 0.81316 -0.00060 0.05818  0.01994  55  ARG   B CA  
3149 C  C   . ARG   B 55  ? 0.61039 0.95094 0.73065 -0.00173 0.05348  0.01320  55  ARG   B C   
3150 O  O   . ARG   B 55  ? 0.70596 1.03921 0.82530 0.00645  0.05338  0.00417  55  ARG   B O   
3151 C  CB  . ARG   B 55  ? 0.64031 1.01308 0.75490 0.00299  0.06121  0.01785  55  ARG   B CB  
3152 C  CG  . ARG   B 55  ? 0.49852 0.85697 0.60453 0.01500  0.06206  0.00428  55  ARG   B CG  
3153 C  CD  . ARG   B 55  ? 0.69352 1.04576 0.79061 0.01522  0.06316  0.00345  55  ARG   B CD  
3154 N  NE  . ARG   B 55  ? 0.62546 0.96701 0.71446 0.02627  0.06334  -0.00832 55  ARG   B NE  
3155 C  CZ  . ARG   B 55  ? 0.60403 0.91919 0.68944 0.02630  0.05974  -0.01478 55  ARG   B CZ  
3156 N  NH1 . ARG   B 55  ? 0.46732 0.76565 0.55572 0.01762  0.05652  -0.01148 55  ARG   B NH1 
3157 N  NH2 . ARG   B 55  ? 0.51359 0.81950 0.59198 0.03535  0.05892  -0.02440 55  ARG   B NH2 
3158 N  N   . LYS   B 56  ? 0.69685 1.01898 0.81533 -0.01179 0.04912  0.01811  56  LYS   B N   
3159 C  CA  . LYS   B 56  ? 0.54883 0.84185 0.66285 -0.01199 0.04519  0.01196  56  LYS   B CA  
3160 C  C   . LYS   B 56  ? 0.38482 0.66697 0.49131 -0.00283 0.04746  0.00175  56  LYS   B C   
3161 O  O   . LYS   B 56  ? 0.47411 0.75711 0.57540 -0.00216 0.04930  0.00185  56  LYS   B O   
3162 C  CB  . LYS   B 56  ? 0.64040 0.91607 0.75095 -0.02203 0.04042  0.01807  56  LYS   B CB  
3163 C  CG  . LYS   B 56  ? 0.70899 0.98947 0.82567 -0.03251 0.03574  0.02847  56  LYS   B CG  
3164 C  CD  . LYS   B 56  ? 0.73073 1.00268 0.85083 -0.03132 0.03279  0.02501  56  LYS   B CD  
3165 C  CE  . LYS   B 56  ? 0.72168 0.98852 0.84592 -0.04113 0.02585  0.03285  56  LYS   B CE  
3166 N  NZ  . LYS   B 56  ? 0.73126 0.98139 0.85433 -0.03697 0.02343  0.02558  56  LYS   B NZ  
3167 N  N   . LEU   B 57  ? 0.42171 0.69267 0.52754 0.00342  0.04655  -0.00641 57  LEU   B N   
3168 C  CA  . LEU   B 57  ? 0.33898 0.59597 0.43798 0.01002  0.04687  -0.01488 57  LEU   B CA  
3169 C  C   . LEU   B 57  ? 0.40136 0.63543 0.49600 0.00501  0.04392  -0.01457 57  LEU   B C   
3170 O  O   . LEU   B 57  ? 0.34363 0.56780 0.43993 -0.00026 0.04087  -0.01155 57  LEU   B O   
3171 C  CB  . LEU   B 57  ? 0.40553 0.65942 0.50530 0.01845  0.04619  -0.02307 57  LEU   B CB  
3172 C  CG  . LEU   B 57  ? 0.44542 0.72166 0.54872 0.02589  0.04870  -0.02484 57  LEU   B CG  
3173 C  CD1 . LEU   B 57  ? 0.45872 0.72722 0.56172 0.03414  0.04646  -0.03330 57  LEU   B CD1 
3174 C  CD2 . LEU   B 57  ? 0.39881 0.68908 0.49728 0.03113  0.05220  -0.02591 57  LEU   B CD2 
3175 N  N   . ILE   B 58  ? 0.33240 0.55869 0.42108 0.00717  0.04457  -0.01764 58  ILE   B N   
3176 C  CA  . ILE   B 58  ? 0.33024 0.53692 0.41471 0.00408  0.04222  -0.01778 58  ILE   B CA  
3177 C  C   . ILE   B 58  ? 0.30714 0.50133 0.39049 0.00918  0.04095  -0.02463 58  ILE   B C   
3178 O  O   . ILE   B 58  ? 0.31707 0.51211 0.39839 0.01489  0.04154  -0.02993 58  ILE   B O   
3179 C  CB  . ILE   B 58  ? 0.32267 0.52849 0.40200 0.00279  0.04318  -0.01616 58  ILE   B CB  
3180 C  CG1 . ILE   B 58  ? 0.38640 0.60468 0.46716 -0.00335 0.04374  -0.00802 58  ILE   B CG1 
3181 C  CG2 . ILE   B 58  ? 0.32275 0.50920 0.39811 0.00059  0.04064  -0.01637 58  ILE   B CG2 
3182 C  CD1 . ILE   B 58  ? 0.50489 0.72401 0.58025 -0.00486 0.04465  -0.00559 58  ILE   B CD1 
3183 N  N   . CYS   B 59  ? 0.28509 0.46679 0.36897 0.00692  0.03858  -0.02412 59  CYS   B N   
3184 C  CA  . CYS   B 59  ? 0.25693 0.42660 0.33988 0.01030  0.03709  -0.02872 59  CYS   B CA  
3185 C  C   . CYS   B 59  ? 0.28346 0.44011 0.36212 0.00814  0.03614  -0.02726 59  CYS   B C   
3186 O  O   . CYS   B 59  ? 0.28676 0.44024 0.36319 0.00407  0.03550  -0.02302 59  CYS   B O   
3187 C  CB  . CYS   B 59  ? 0.27800 0.44384 0.36416 0.01007  0.03524  -0.02891 59  CYS   B CB  
3188 S  SG  . CYS   B 59  ? 0.35907 0.54235 0.45119 0.01255  0.03621  -0.02956 59  CYS   B SG  
3189 N  N   . TYR   B 60  ? 0.29443 0.44332 0.37209 0.01091  0.03536  -0.03034 60  TYR   B N   
3190 C  CA  . TYR   B 60  ? 0.27992 0.41877 0.35420 0.00949  0.03474  -0.02830 60  TYR   B CA  
3191 C  C   . TYR   B 60  ? 0.25994 0.39193 0.33508 0.01169  0.03352  -0.03011 60  TYR   B C   
3192 O  O   . TYR   B 60  ? 0.29281 0.42589 0.37045 0.01408  0.03247  -0.03332 60  TYR   B O   
3193 C  CB  . TYR   B 60  ? 0.31719 0.45694 0.38822 0.00892  0.03568  -0.02727 60  TYR   B CB  
3194 C  CG  . TYR   B 60  ? 0.26744 0.40438 0.33809 0.01123  0.03524  -0.02946 60  TYR   B CG  
3195 C  CD1 . TYR   B 60  ? 0.28925 0.42926 0.36166 0.01413  0.03429  -0.03356 60  TYR   B CD1 
3196 C  CD2 . TYR   B 60  ? 0.31462 0.44653 0.38263 0.01068  0.03515  -0.02727 60  TYR   B CD2 
3197 C  CE1 . TYR   B 60  ? 0.31777 0.45445 0.38977 0.01528  0.03255  -0.03495 60  TYR   B CE1 
3198 C  CE2 . TYR   B 60  ? 0.32829 0.45941 0.39695 0.01198  0.03429  -0.02836 60  TYR   B CE2 
3199 C  CZ  . TYR   B 60  ? 0.33985 0.47282 0.41064 0.01370  0.03266  -0.03195 60  TYR   B CZ  
3200 O  OH  . TYR   B 60  ? 0.32569 0.45642 0.39763 0.01451  0.02990  -0.03327 60  TYR   B OH  
3201 N  N   . ASP   B 61  ? 0.24226 0.36725 0.31473 0.01110  0.03326  -0.02768 61  ASP   B N   
3202 C  CA  . ASP   B 61  ? 0.29197 0.41234 0.36501 0.01260  0.03255  -0.02745 61  ASP   B CA  
3203 C  C   . ASP   B 61  ? 0.32127 0.43918 0.39054 0.01276  0.03337  -0.02474 61  ASP   B C   
3204 O  O   . ASP   B 61  ? 0.30934 0.42582 0.37474 0.01193  0.03362  -0.02338 61  ASP   B O   
3205 C  CB  . ASP   B 61  ? 0.31435 0.43048 0.38776 0.01314  0.03156  -0.02692 61  ASP   B CB  
3206 C  CG  . ASP   B 61  ? 0.35946 0.47315 0.43482 0.01426  0.03056  -0.02615 61  ASP   B CG  
3207 O  OD1 . ASP   B 61  ? 0.33497 0.44978 0.41154 0.01419  0.03036  -0.02507 61  ASP   B OD1 
3208 O  OD2 . ASP   B 61  ? 0.31409 0.42488 0.38998 0.01479  0.02951  -0.02592 61  ASP   B OD2 
3209 N  N   . GLY   B 62  ? 0.29727 0.41493 0.36772 0.01379  0.03326  -0.02354 62  GLY   B N   
3210 C  CA  . GLY   B 62  ? 0.29675 0.41394 0.36398 0.01497  0.03418  -0.02091 62  GLY   B CA  
3211 C  C   . GLY   B 62  ? 0.28057 0.39794 0.34843 0.01688  0.03444  -0.01811 62  GLY   B C   
3212 O  O   . GLY   B 62  ? 0.28657 0.40494 0.35863 0.01612  0.03346  -0.01762 62  GLY   B O   
3213 N  N   . PHE   B 63  ? 0.28190 0.39899 0.34529 0.01972  0.03550  -0.01587 63  PHE   B N   
3214 C  CA  . PHE   B 63  ? 0.26851 0.38713 0.33041 0.02312  0.03639  -0.01290 63  PHE   B CA  
3215 C  C   . PHE   B 63  ? 0.26994 0.39345 0.33016 0.02632  0.03767  -0.01010 63  PHE   B C   
3216 O  O   . PHE   B 63  ? 0.33060 0.45051 0.38506 0.02855  0.03750  -0.01116 63  PHE   B O   
3217 C  CB  . PHE   B 63  ? 0.30158 0.41334 0.35645 0.02607  0.03591  -0.01394 63  PHE   B CB  
3218 C  CG  . PHE   B 63  ? 0.31351 0.42084 0.36981 0.02307  0.03441  -0.01649 63  PHE   B CG  
3219 C  CD1 . PHE   B 63  ? 0.28947 0.39467 0.34583 0.02009  0.03341  -0.01863 63  PHE   B CD1 
3220 C  CD2 . PHE   B 63  ? 0.37820 0.48534 0.43646 0.02325  0.03407  -0.01604 63  PHE   B CD2 
3221 C  CE1 . PHE   B 63  ? 0.32599 0.42977 0.38470 0.01752  0.03216  -0.02050 63  PHE   B CE1 
3222 C  CE2 . PHE   B 63  ? 0.33786 0.44189 0.39810 0.02081  0.03250  -0.01845 63  PHE   B CE2 
3223 C  CZ  . PHE   B 63  ? 0.32606 0.42896 0.38664 0.01816  0.03164  -0.02069 63  PHE   B CZ  
3224 N  N   . GLU   B 64  ? 0.29596 0.42770 0.36084 0.02679  0.03856  -0.00602 64  GLU   B N   
3225 C  CA  . GLU   B 64  ? 0.37285 0.51206 0.43638 0.03108  0.04020  -0.00249 64  GLU   B CA  
3226 C  C   . GLU   B 64  ? 0.38738 0.52548 0.44274 0.03823  0.04159  -0.00200 64  GLU   B C   
3227 O  O   . GLU   B 64  ? 0.32690 0.46623 0.38216 0.03920  0.04216  -0.00052 64  GLU   B O   
3228 C  CB  . GLU   B 64  ? 0.31886 0.46954 0.39115 0.02860  0.04036  0.00314  64  GLU   B CB  
3229 C  CG  . GLU   B 64  ? 0.34824 0.49954 0.42752 0.02253  0.03774  0.00279  64  GLU   B CG  
3230 C  CD  . GLU   B 64  ? 0.43320 0.59512 0.52132 0.01928  0.03642  0.00949  64  GLU   B CD  
3231 O  OE1 . GLU   B 64  ? 0.43334 0.60547 0.52202 0.02267  0.03880  0.01491  64  GLU   B OE1 
3232 O  OE2 . GLU   B 64  ? 0.40556 0.56581 0.49964 0.01362  0.03257  0.00965  64  GLU   B OE2 
3233 N  N   . PRO   B 65  ? 0.30822 0.44353 0.35571 0.04405  0.04164  -0.00327 65  PRO   B N   
3234 C  CA  . PRO   B 65  ? 0.35328 0.48785 0.39183 0.05255  0.04233  -0.00305 65  PRO   B CA  
3235 C  C   . PRO   B 65  ? 0.41128 0.56200 0.45331 0.05687  0.04550  0.00266  65  PRO   B C   
3236 O  O   . PRO   B 65  ? 0.42136 0.57893 0.46217 0.06160  0.04649  0.00424  65  PRO   B O   
3237 C  CB  . PRO   B 65  ? 0.35963 0.48434 0.38837 0.05725  0.04000  -0.00654 65  PRO   B CB  
3238 C  CG  . PRO   B 65  ? 0.36037 0.47881 0.39300 0.04934  0.03811  -0.00872 65  PRO   B CG  
3239 C  CD  . PRO   B 65  ? 0.32045 0.45025 0.36517 0.04331  0.04012  -0.00578 65  PRO   B CD  
3240 N  N   . SER   B 66  ? 0.39493 0.55266 0.44155 0.05520  0.04691  0.00631  66  SER   B N   
3241 C  CA  . SER   B 66  ? 0.42201 0.59794 0.47488 0.05668  0.04976  0.01376  66  SER   B CA  
3242 C  C   . SER   B 66  ? 0.45944 0.64154 0.50541 0.06490  0.05212  0.01609  66  SER   B C   
3243 O  O   . SER   B 66  ? 0.43676 0.63697 0.48712 0.06740  0.05508  0.02332  66  SER   B O   
3244 C  CB  . SER   B 66  ? 0.44150 0.62187 0.50672 0.04651  0.04855  0.01775  66  SER   B CB  
3245 O  OG  . SER   B 66  ? 0.54588 0.71518 0.60953 0.04327  0.04686  0.01452  66  SER   B OG  
3246 N  N   . GLY   B 67  ? 0.36225 0.53093 0.39758 0.06921  0.05068  0.01076  67  GLY   B N   
3247 C  CA  . GLY   B 67  ? 0.35326 0.52611 0.37978 0.07826  0.05238  0.01197  67  GLY   B CA  
3248 C  C   . GLY   B 67  ? 0.29689 0.45191 0.31558 0.07787  0.04915  0.00620  67  GLY   B C   
3249 O  O   . GLY   B 67  ? 0.39286 0.53364 0.41227 0.07188  0.04585  0.00138  67  GLY   B O   
3250 N  N   . ARG   B 68  ? 0.37528 0.53259 0.38697 0.08408  0.05008  0.00729  68  ARG   B N   
3251 C  CA  . ARG   B 68  ? 0.42848 0.56819 0.43240 0.08379  0.04624  0.00174  68  ARG   B CA  
3252 C  C   . ARG   B 68  ? 0.41868 0.55320 0.43339 0.07170  0.04468  0.00163  68  ARG   B C   
3253 O  O   . ARG   B 68  ? 0.40779 0.55294 0.43403 0.06511  0.04656  0.00671  68  ARG   B O   
3254 C  CB  . ARG   B 68  ? 0.43380 0.57715 0.42803 0.09266  0.04733  0.00302  68  ARG   B CB  
3255 C  CG  . ARG   B 68  ? 0.54328 0.68675 0.52274 0.10698  0.04730  0.00050  68  ARG   B CG  
3256 C  CD  . ARG   B 68  ? 0.60376 0.76225 0.57763 0.11611  0.05111  0.00511  68  ARG   B CD  
3257 N  NE  . ARG   B 68  ? 0.63730 0.78297 0.60229 0.11774  0.04792  0.00167  68  ARG   B NE  
3258 C  CZ  . ARG   B 68  ? 0.69263 0.84765 0.65386 0.12224  0.05032  0.00547  68  ARG   B CZ  
3259 N  NH1 . ARG   B 68  ? 0.63564 0.81493 0.60147 0.12563  0.05630  0.01378  68  ARG   B NH1 
3260 N  NH2 . ARG   B 68  ? 0.57787 0.71829 0.53053 0.12326  0.04637  0.00137  68  ARG   B NH2 
3261 N  N   . MET   B 69  ? 0.39850 0.51639 0.40912 0.06902  0.04053  -0.00401 69  MET   B N   
3262 C  CA  . MET   B 69  ? 0.31429 0.42797 0.33480 0.05875  0.03901  -0.00489 69  MET   B CA  
3263 C  C   . MET   B 69  ? 0.34973 0.46579 0.37371 0.05616  0.03914  -0.00243 69  MET   B C   
3264 O  O   . MET   B 69  ? 0.37861 0.48958 0.39424 0.06090  0.03792  -0.00358 69  MET   B O   
3265 C  CB  . MET   B 69  ? 0.33523 0.43329 0.35148 0.05643  0.03465  -0.01068 69  MET   B CB  
3266 C  CG  . MET   B 69  ? 0.35982 0.45640 0.38638 0.04708  0.03367  -0.01159 69  MET   B CG  
3267 S  SD  . MET   B 69  ? 0.36486 0.44667 0.38741 0.04390  0.02864  -0.01657 69  MET   B SD  
3268 C  CE  . MET   B 69  ? 0.39501 0.47331 0.41230 0.04605  0.02774  -0.01763 69  MET   B CE  
3269 N  N   . HIS   B 70  ? 0.34584 0.46859 0.38143 0.04885  0.03986  0.00091  70  HIS   B N   
3270 C  CA  . HIS   B 70  ? 0.37727 0.50044 0.41666 0.04547  0.03890  0.00318  70  HIS   B CA  
3271 C  C   . HIS   B 70  ? 0.32161 0.43148 0.35962 0.04275  0.03531  -0.00250 70  HIS   B C   
3272 O  O   . HIS   B 70  ? 0.33821 0.44176 0.37751 0.04004  0.03377  -0.00676 70  HIS   B O   
3273 C  CB  . HIS   B 70  ? 0.38061 0.51173 0.43216 0.03822  0.03886  0.00788  70  HIS   B CB  
3274 C  CG  . HIS   B 70  ? 0.39813 0.54461 0.45266 0.03968  0.04183  0.01550  70  HIS   B CG  
3275 N  ND1 . HIS   B 70  ? 0.45520 0.61035 0.51873 0.03402  0.04108  0.02257  70  HIS   B ND1 
3276 C  CD2 . HIS   B 70  ? 0.43434 0.58984 0.48425 0.04623  0.04512  0.01763  70  HIS   B CD2 
3277 C  CE1 . HIS   B 70  ? 0.43227 0.60280 0.49758 0.03630  0.04411  0.02955  70  HIS   B CE1 
3278 N  NE2 . HIS   B 70  ? 0.41640 0.58807 0.47332 0.04441  0.04700  0.02644  70  HIS   B NE2 
3279 N  N   . ILE   B 71  ? 0.36117 0.46797 0.39673 0.04344  0.03392  -0.00201 71  ILE   B N   
3280 C  CA  . ILE   B 71  ? 0.36817 0.46347 0.40264 0.04119  0.03026  -0.00710 71  ILE   B CA  
3281 C  C   . ILE   B 71  ? 0.36196 0.45636 0.40659 0.03415  0.02887  -0.00914 71  ILE   B C   
3282 O  O   . ILE   B 71  ? 0.33953 0.42717 0.38432 0.03224  0.02648  -0.01332 71  ILE   B O   
3283 C  CB  . ILE   B 71  ? 0.35978 0.45145 0.39013 0.04298  0.02845  -0.00644 71  ILE   B CB  
3284 C  CG1 . ILE   B 71  ? 0.37355 0.47267 0.41112 0.03961  0.02918  -0.00121 71  ILE   B CG1 
3285 C  CG2 . ILE   B 71  ? 0.41764 0.50730 0.43468 0.05164  0.02879  -0.00636 71  ILE   B CG2 
3286 C  CD1 . ILE   B 71  ? 0.39173 0.48649 0.42372 0.04196  0.02716  -0.00058 71  ILE   B CD1 
3287 N  N   . ALA   B 72  ? 0.33418 0.43553 0.38720 0.03037  0.02979  -0.00615 72  ALA   B N   
3288 C  CA  . ALA   B 72  ? 0.35170 0.45144 0.41253 0.02531  0.02799  -0.00915 72  ALA   B CA  
3289 C  C   . ALA   B 72  ? 0.36183 0.45943 0.42155 0.02502  0.02846  -0.01312 72  ALA   B C   
3290 O  O   . ALA   B 72  ? 0.33547 0.43074 0.39864 0.02247  0.02689  -0.01666 72  ALA   B O   
3291 C  CB  . ALA   B 72  ? 0.35737 0.46319 0.42574 0.02180  0.02776  -0.00553 72  ALA   B CB  
3292 N  N   . GLN   B 73  ? 0.32694 0.42618 0.38186 0.02786  0.03049  -0.01224 73  GLN   B N   
3293 C  CA  . GLN   B 73  ? 0.29127 0.38863 0.34529 0.02697  0.03055  -0.01500 73  GLN   B CA  
3294 C  C   . GLN   B 73  ? 0.35602 0.44510 0.40291 0.02850  0.02842  -0.01758 73  GLN   B C   
3295 O  O   . GLN   B 73  ? 0.32577 0.41282 0.37183 0.02694  0.02775  -0.01910 73  GLN   B O   
3296 C  CB  . GLN   B 73  ? 0.30574 0.40859 0.35864 0.02898  0.03299  -0.01266 73  GLN   B CB  
3297 C  CG  . GLN   B 73  ? 0.33936 0.45008 0.40050 0.02594  0.03380  -0.00959 73  GLN   B CG  
3298 C  CD  . GLN   B 73  ? 0.43773 0.55561 0.49832 0.02816  0.03607  -0.00623 73  GLN   B CD  
3299 O  OE1 . GLN   B 73  ? 0.41407 0.53130 0.46732 0.03330  0.03733  -0.00620 73  GLN   B OE1 
3300 N  NE2 . GLN   B 73  ? 0.38677 0.51134 0.45479 0.02474  0.03593  -0.00321 73  GLN   B NE2 
3301 N  N   . GLY   B 74  ? 0.35768 0.44159 0.39917 0.03121  0.02669  -0.01767 74  GLY   B N   
3302 C  CA  . GLY   B 74  ? 0.35409 0.42834 0.38831 0.03237  0.02306  -0.01986 74  GLY   B CA  
3303 C  C   . GLY   B 74  ? 0.36425 0.43558 0.40181 0.02935  0.02030  -0.02117 74  GLY   B C   
3304 O  O   . GLY   B 74  ? 0.32839 0.39959 0.37068 0.02489  0.01854  -0.02252 74  GLY   B O   
3305 N  N   . LEU   B 75  ? 0.28929 0.36027 0.32522 0.03176  0.02019  -0.02019 75  LEU   B N   
3306 C  CA  . LEU   B 75  ? 0.31681 0.38430 0.35494 0.02974  0.01706  -0.02143 75  LEU   B CA  
3307 C  C   . LEU   B 75  ? 0.38342 0.45716 0.43271 0.02505  0.01767  -0.02222 75  LEU   B C   
3308 O  O   . LEU   B 75  ? 0.35813 0.43153 0.41137 0.02216  0.01533  -0.02394 75  LEU   B O   
3309 C  CB  . LEU   B 75  ? 0.32453 0.39079 0.35810 0.03357  0.01698  -0.01979 75  LEU   B CB  
3310 C  CG  . LEU   B 75  ? 0.38056 0.44013 0.40109 0.04008  0.01558  -0.01977 75  LEU   B CG  
3311 C  CD1 . LEU   B 75  ? 0.36781 0.42880 0.38593 0.04285  0.01591  -0.01765 75  LEU   B CD1 
3312 C  CD2 . LEU   B 75  ? 0.38532 0.43283 0.39937 0.03975  0.00965  -0.02294 75  LEU   B CD2 
3313 N  N   . LEU   B 76  ? 0.30989 0.38974 0.36433 0.02456  0.02025  -0.02081 76  LEU   B N   
3314 C  CA  . LEU   B 76  ? 0.28467 0.36877 0.34803 0.02145  0.01985  -0.02248 76  LEU   B CA  
3315 C  C   . LEU   B 76  ? 0.35380 0.44137 0.42018 0.01924  0.02060  -0.02449 76  LEU   B C   
3316 O  O   . LEU   B 76  ? 0.32710 0.41739 0.39815 0.01759  0.01935  -0.02657 76  LEU   B O   
3317 C  CB  . LEU   B 76  ? 0.35921 0.44694 0.42664 0.02102  0.02082  -0.02040 76  LEU   B CB  
3318 C  CG  . LEU   B 76  ? 0.34318 0.43350 0.41806 0.01902  0.01943  -0.02302 76  LEU   B CG  
3319 C  CD1 . LEU   B 76  ? 0.39401 0.48152 0.47147 0.01936  0.01606  -0.02480 76  LEU   B CD1 
3320 C  CD2 . LEU   B 76  ? 0.35901 0.45133 0.43698 0.01784  0.01927  -0.02052 76  LEU   B CD2 
3321 N  N   . LYS   B 77  ? 0.33016 0.41888 0.39390 0.01947  0.02270  -0.02353 77  LYS   B N   
3322 C  CA  . LYS   B 77  ? 0.34045 0.43271 0.40639 0.01719  0.02341  -0.02475 77  LYS   B CA  
3323 C  C   . LYS   B 77  ? 0.34698 0.43786 0.41263 0.01501  0.02096  -0.02532 77  LYS   B C   
3324 O  O   . LYS   B 77  ? 0.31870 0.41603 0.38944 0.01259  0.02118  -0.02611 77  LYS   B O   
3325 C  CB  . LYS   B 77  ? 0.35412 0.44570 0.41540 0.01823  0.02521  -0.02325 77  LYS   B CB  
3326 C  CG  . LYS   B 77  ? 0.37707 0.47230 0.43988 0.01572  0.02600  -0.02380 77  LYS   B CG  
3327 C  CD  . LYS   B 77  ? 0.42943 0.53245 0.49912 0.01418  0.02738  -0.02549 77  LYS   B CD  
3328 C  CE  . LYS   B 77  ? 0.49272 0.59674 0.56553 0.01545  0.02759  -0.02581 77  LYS   B CE  
3329 N  NZ  . LYS   B 77  ? 0.34454 0.45375 0.42247 0.01490  0.02720  -0.02870 77  LYS   B NZ  
3330 N  N   . SER   B 78  ? 0.36936 0.45254 0.42888 0.01592  0.01830  -0.02453 78  SER   B N   
3331 C  CA  . SER   B 78  ? 0.38086 0.46153 0.43983 0.01283  0.01461  -0.02403 78  SER   B CA  
3332 C  C   . SER   B 78  ? 0.35394 0.44129 0.42093 0.01063  0.01360  -0.02478 78  SER   B C   
3333 O  O   . SER   B 78  ? 0.33476 0.42723 0.40576 0.00686  0.01208  -0.02359 78  SER   B O   
3334 C  CB  . SER   B 78  ? 0.46132 0.53012 0.51080 0.01504  0.01061  -0.02359 78  SER   B CB  
3335 O  OG  . SER   B 78  ? 0.50340 0.56788 0.55177 0.01115  0.00555  -0.02241 78  SER   B OG  
3336 N  N   . ILE   B 79  ? 0.32769 0.41606 0.39736 0.01296  0.01422  -0.02624 79  ILE   B N   
3337 C  CA  . ILE   B 79  ? 0.33804 0.43278 0.41501 0.01222  0.01300  -0.02749 79  ILE   B CA  
3338 C  C   . ILE   B 79  ? 0.38227 0.48865 0.46612 0.01138  0.01543  -0.02860 79  ILE   B C   
3339 O  O   . ILE   B 79  ? 0.32716 0.44200 0.41619 0.00942  0.01463  -0.02804 79  ILE   B O   
3340 C  CB  . ILE   B 79  ? 0.37009 0.46150 0.44725 0.01526  0.01246  -0.02873 79  ILE   B CB  
3341 C  CG1 . ILE   B 79  ? 0.39252 0.47432 0.46270 0.01635  0.00973  -0.02749 79  ILE   B CG1 
3342 C  CG2 . ILE   B 79  ? 0.35483 0.45322 0.43955 0.01603  0.01165  -0.03096 79  ILE   B CG2 
3343 C  CD1 . ILE   B 79  ? 0.36246 0.44074 0.43037 0.01924  0.01034  -0.02710 79  ILE   B CD1 
3344 N  N   . ILE   B 80  ? 0.32442 0.43229 0.40818 0.01301  0.01827  -0.02982 80  ILE   B N   
3345 C  CA  . ILE   B 80  ? 0.32039 0.43831 0.40890 0.01349  0.02028  -0.03157 80  ILE   B CA  
3346 C  C   . ILE   B 80  ? 0.29674 0.42060 0.38537 0.01010  0.02133  -0.02916 80  ILE   B C   
3347 O  O   . ILE   B 80  ? 0.33239 0.46791 0.42593 0.00956  0.02217  -0.02915 80  ILE   B O   
3348 C  CB  . ILE   B 80  ? 0.50400 0.61957 0.59123 0.01556  0.02180  -0.03308 80  ILE   B CB  
3349 C  CG1 . ILE   B 80  ? 0.49074 0.59951 0.57777 0.01758  0.01973  -0.03379 80  ILE   B CG1 
3350 C  CG2 . ILE   B 80  ? 0.48584 0.61086 0.57664 0.01726  0.02309  -0.03588 80  ILE   B CG2 
3351 C  CD1 . ILE   B 80  ? 0.45874 0.56270 0.54397 0.01803  0.01992  -0.03278 80  ILE   B CD1 
3352 N  N   . VAL   B 81  ? 0.28151 0.39804 0.36440 0.00814  0.02110  -0.02678 81  VAL   B N   
3353 C  CA  . VAL   B 81  ? 0.28416 0.40464 0.36652 0.00447  0.02126  -0.02397 81  VAL   B CA  
3354 C  C   . VAL   B 81  ? 0.29381 0.41909 0.37978 0.00057  0.01836  -0.02113 81  VAL   B C   
3355 O  O   . VAL   B 81  ? 0.29923 0.43621 0.38973 -0.00214 0.01925  -0.01890 81  VAL   B O   
3356 C  CB  . VAL   B 81  ? 0.33503 0.44471 0.40951 0.00398  0.02044  -0.02233 81  VAL   B CB  
3357 C  CG1 . VAL   B 81  ? 0.28759 0.39846 0.36085 -0.00075 0.01857  -0.01864 81  VAL   B CG1 
3358 C  CG2 . VAL   B 81  ? 0.32147 0.43083 0.39444 0.00716  0.02376  -0.02417 81  VAL   B CG2 
3359 N  N   . ASN   B 82  ? 0.28579 0.40289 0.36983 0.00005  0.01455  -0.02058 82  ASN   B N   
3360 C  CA  . ASN   B 82  ? 0.27967 0.40157 0.36794 -0.00455 0.01077  -0.01713 82  ASN   B CA  
3361 C  C   . ASN   B 82  ? 0.28719 0.42567 0.38501 -0.00365 0.01275  -0.01778 82  ASN   B C   
3362 O  O   . ASN   B 82  ? 0.31409 0.46452 0.41789 -0.00779 0.01167  -0.01378 82  ASN   B O   
3363 C  CB  . ASN   B 82  ? 0.27711 0.38568 0.36050 -0.00471 0.00555  -0.01695 82  ASN   B CB  
3364 C  CG  . ASN   B 82  ? 0.39016 0.48454 0.46417 -0.00655 0.00160  -0.01500 82  ASN   B CG  
3365 O  OD1 . ASN   B 82  ? 0.32202 0.41621 0.39648 -0.01217 -0.00263 -0.01083 82  ASN   B OD1 
3366 N  ND2 . ASN   B 82  ? 0.33887 0.42197 0.40421 -0.00164 0.00269  -0.01763 82  ASN   B ND2 
3367 N  N   . LYS   B 83  ? 0.32384 0.46365 0.42322 0.00186  0.01502  -0.02238 83  LYS   B N   
3368 C  CA  . LYS   B 83  ? 0.33792 0.49337 0.44517 0.00453  0.01665  -0.02393 83  LYS   B CA  
3369 C  C   . LYS   B 83  ? 0.34678 0.51684 0.45695 0.00411  0.02022  -0.02267 83  LYS   B C   
3370 O  O   . LYS   B 83  ? 0.30662 0.49346 0.42348 0.00348  0.02093  -0.02043 83  LYS   B O   
3371 C  CB  . LYS   B 83  ? 0.38484 0.53626 0.49168 0.01093  0.01732  -0.02946 83  LYS   B CB  
3372 C  CG  . LYS   B 83  ? 0.46044 0.62491 0.57387 0.01575  0.01761  -0.03240 83  LYS   B CG  
3373 C  CD  . LYS   B 83  ? 0.68932 0.84570 0.80305 0.01847  0.01421  -0.03472 83  LYS   B CD  
3374 C  CE  . LYS   B 83  ? 0.69624 0.86570 0.81745 0.02040  0.01261  -0.03472 83  LYS   B CE  
3375 N  NZ  . LYS   B 83  ? 0.74455 0.90428 0.86538 0.02003  0.00837  -0.03462 83  LYS   B NZ  
3376 N  N   . LEU   B 84  ? 0.30363 0.46899 0.40891 0.00500  0.02269  -0.02398 84  LEU   B N   
3377 C  CA  . LEU   B 84  ? 0.29969 0.47845 0.40668 0.00551  0.02609  -0.02336 84  LEU   B CA  
3378 C  C   . LEU   B 84  ? 0.31268 0.49859 0.42128 -0.00149 0.02539  -0.01644 84  LEU   B C   
3379 O  O   . LEU   B 84  ? 0.34972 0.55386 0.46371 -0.00219 0.02725  -0.01363 84  LEU   B O   
3380 C  CB  . LEU   B 84  ? 0.33629 0.50728 0.43756 0.00813  0.02819  -0.02654 84  LEU   B CB  
3381 C  CG  . LEU   B 84  ? 0.34323 0.50910 0.44378 0.01440  0.02804  -0.03255 84  LEU   B CG  
3382 C  CD1 . LEU   B 84  ? 0.36176 0.51787 0.45696 0.01531  0.02889  -0.03428 84  LEU   B CD1 
3383 C  CD2 . LEU   B 84  ? 0.42110 0.60079 0.52546 0.01982  0.02918  -0.03589 84  LEU   B CD2 
3384 N  N   . THR   B 85  ? 0.32345 0.49543 0.42718 -0.00654 0.02212  -0.01325 85  THR   B N   
3385 C  CA  . THR   B 85  ? 0.29756 0.47380 0.40201 -0.01382 0.02001  -0.00624 85  THR   B CA  
3386 C  C   . THR   B 85  ? 0.40166 0.58936 0.51382 -0.01836 0.01703  -0.00116 85  THR   B C   
3387 O  O   . THR   B 85  ? 0.39219 0.59305 0.50874 -0.02404 0.01655  0.00554  85  THR   B O   
3388 C  CB  . THR   B 85  ? 0.33525 0.49168 0.43138 -0.01724 0.01571  -0.00456 85  THR   B CB  
3389 O  OG1 . THR   B 85  ? 0.41181 0.55529 0.50551 -0.01682 0.01137  -0.00589 85  THR   B OG1 
3390 C  CG2 . THR   B 85  ? 0.30480 0.45239 0.39427 -0.01299 0.01870  -0.00858 85  THR   B CG2 
3391 N  N   . SER   B 86  ? 0.36104 0.54580 0.47563 -0.01612 0.01502  -0.00363 86  SER   B N   
3392 C  CA  . SER   B 86  ? 0.34704 0.54291 0.46948 -0.02111 0.01145  0.00193  86  SER   B CA  
3393 C  C   . SER   B 86  ? 0.49901 0.72147 0.63067 -0.01857 0.01605  0.00318  86  SER   B C   
3394 O  O   . SER   B 86  ? 0.49348 0.73212 0.63316 -0.02386 0.01432  0.01018  86  SER   B O   
3395 C  CB  . SER   B 86  ? 0.41488 0.59970 0.53683 -0.01924 0.00758  -0.00103 86  SER   B CB  
3396 O  OG  . SER   B 86  ? 0.46709 0.65687 0.59116 -0.01108 0.01141  -0.00750 86  SER   B OG  
3397 N  N   . ASN   B 87  ? 0.47448 0.70194 0.60438 -0.01075 0.02157  -0.00287 87  ASN   B N   
3398 C  CA  . ASN   B 87  ? 0.49904 0.74987 0.63476 -0.00511 0.02627  -0.00397 87  ASN   B CA  
3399 C  C   . ASN   B 87  ? 0.54185 0.80315 0.67587 -0.00624 0.03005  -0.00113 87  ASN   B C   
3400 O  O   . ASN   B 87  ? 0.58455 0.85763 0.71807 0.00121  0.03453  -0.00530 87  ASN   B O   
3401 C  CB  . ASN   B 87  ? 0.45495 0.70079 0.58804 0.00532  0.02816  -0.01358 87  ASN   B CB  
3402 C  CG  . ASN   B 87  ? 0.59613 0.84115 0.73358 0.00791  0.02522  -0.01566 87  ASN   B CG  
3403 O  OD1 . ASN   B 87  ? 0.61483 0.87901 0.76022 0.00857  0.02546  -0.01277 87  ASN   B OD1 
3404 N  ND2 . ASN   B 87  ? 0.52969 0.75384 0.66215 0.00955  0.02250  -0.02023 87  ASN   B ND2 
3405 N  N   . GLY   B 88  ? 0.49968 0.75441 0.63146 -0.01506 0.02753  0.00547  88  GLY   B N   
3406 C  CA  . GLY   B 88  ? 0.49435 0.75977 0.62544 -0.01860 0.02988  0.01071  88  GLY   B CA  
3407 C  C   . GLY   B 88  ? 0.48463 0.73771 0.60677 -0.01558 0.03227  0.00617  88  GLY   B C   
3408 O  O   . GLY   B 88  ? 0.58175 0.84478 0.70300 -0.01772 0.03453  0.01017  88  GLY   B O   
3409 N  N   . CYS   B 89  ? 0.44458 0.67681 0.56031 -0.01163 0.03141  -0.00083 89  CYS   B N   
3410 C  CA  . CYS   B 89  ? 0.40641 0.62889 0.51473 -0.00863 0.03357  -0.00481 89  CYS   B CA  
3411 C  C   . CYS   B 89  ? 0.44226 0.64665 0.54453 -0.01459 0.02999  -0.00165 89  CYS   B C   
3412 O  O   . CYS   B 89  ? 0.42900 0.62265 0.53078 -0.01919 0.02522  0.00120  89  CYS   B O   
3413 C  CB  . CYS   B 89  ? 0.40985 0.62147 0.51492 -0.00072 0.03455  -0.01370 89  CYS   B CB  
3414 S  SG  . CYS   B 89  ? 0.56414 0.79059 0.67323 0.00875  0.03722  -0.01992 89  CYS   B SG  
3415 N  N   . THR   B 90  ? 0.35601 0.55634 0.45285 -0.01367 0.03182  -0.00262 90  THR   B N   
3416 C  CA  . THR   B 90  ? 0.35716 0.53912 0.44707 -0.01675 0.02867  -0.00142 90  THR   B CA  
3417 C  C   . THR   B 90  ? 0.36773 0.53814 0.45298 -0.01037 0.03044  -0.00846 90  THR   B C   
3418 O  O   . THR   B 90  ? 0.38881 0.56600 0.47540 -0.00499 0.03382  -0.01312 90  THR   B O   
3419 C  CB  . THR   B 90  ? 0.40642 0.59178 0.49380 -0.02175 0.02826  0.00431  90  THR   B CB  
3420 O  OG1 . THR   B 90  ? 0.52937 0.72706 0.61683 -0.01750 0.03336  0.00190  90  THR   B OG1 
3421 C  CG2 . THR   B 90  ? 0.57007 0.76544 0.66245 -0.02999 0.02496  0.01321  90  THR   B CG2 
3422 N  N   . PHE   B 91  ? 0.33123 0.48443 0.41121 -0.01062 0.02747  -0.00914 91  PHE   B N   
3423 C  CA  . PHE   B 91  ? 0.35747 0.50142 0.43440 -0.00516 0.02881  -0.01450 91  PHE   B CA  
3424 C  C   . PHE   B 91  ? 0.33798 0.47090 0.40803 -0.00540 0.02776  -0.01355 91  PHE   B C   
3425 O  O   . PHE   B 91  ? 0.40893 0.53137 0.47442 -0.00773 0.02388  -0.01095 91  PHE   B O   
3426 C  CB  . PHE   B 91  ? 0.32550 0.46098 0.40259 -0.00335 0.02676  -0.01654 91  PHE   B CB  
3427 C  CG  . PHE   B 91  ? 0.33774 0.46974 0.41463 0.00188  0.02866  -0.02125 91  PHE   B CG  
3428 C  CD1 . PHE   B 91  ? 0.37487 0.49740 0.44671 0.00395  0.02885  -0.02197 91  PHE   B CD1 
3429 C  CD2 . PHE   B 91  ? 0.35069 0.48920 0.43249 0.00475  0.02971  -0.02446 91  PHE   B CD2 
3430 C  CE1 . PHE   B 91  ? 0.40400 0.52457 0.47671 0.00767  0.03004  -0.02489 91  PHE   B CE1 
3431 C  CE2 . PHE   B 91  ? 0.35130 0.48550 0.43298 0.00870  0.03019  -0.02807 91  PHE   B CE2 
3432 C  CZ  . PHE   B 91  ? 0.31856 0.44418 0.39618 0.00951  0.03029  -0.02777 91  PHE   B CZ  
3433 N  N   . ILE   B 92  ? 0.30398 0.43789 0.37273 -0.00220 0.03049  -0.01615 92  ILE   B N   
3434 C  CA  . ILE   B 92  ? 0.28285 0.40774 0.34567 -0.00136 0.02981  -0.01558 92  ILE   B CA  
3435 C  C   . ILE   B 92  ? 0.30233 0.41965 0.36358 0.00306  0.03015  -0.01846 92  ILE   B C   
3436 O  O   . ILE   B 92  ? 0.32157 0.44265 0.38658 0.00559  0.03198  -0.02138 92  ILE   B O   
3437 C  CB  . ILE   B 92  ? 0.28138 0.41321 0.34402 -0.00104 0.03224  -0.01580 92  ILE   B CB  
3438 C  CG1 . ILE   B 92  ? 0.32049 0.46129 0.38412 -0.00570 0.03202  -0.01160 92  ILE   B CG1 
3439 C  CG2 . ILE   B 92  ? 0.30883 0.43186 0.36620 0.00106  0.03173  -0.01592 92  ILE   B CG2 
3440 C  CD1 . ILE   B 92  ? 0.35944 0.50924 0.42252 -0.00472 0.03480  -0.01209 92  ILE   B CD1 
3441 N  N   . PHE   B 93  ? 0.26342 0.37010 0.31865 0.00427  0.02787  -0.01733 93  PHE   B N   
3442 C  CA  . PHE   B 93  ? 0.27852 0.38041 0.33130 0.00889  0.02870  -0.01873 93  PHE   B CA  
3443 C  C   . PHE   B 93  ? 0.34524 0.44715 0.39515 0.01039  0.02966  -0.01807 93  PHE   B C   
3444 O  O   . PHE   B 93  ? 0.34352 0.43954 0.38768 0.01003  0.02738  -0.01634 93  PHE   B O   
3445 C  CB  . PHE   B 93  ? 0.28688 0.37838 0.33347 0.01102  0.02568  -0.01822 93  PHE   B CB  
3446 C  CG  . PHE   B 93  ? 0.34996 0.44102 0.39926 0.01087  0.02496  -0.01923 93  PHE   B CG  
3447 C  CD1 . PHE   B 93  ? 0.41989 0.51341 0.47264 0.00670  0.02326  -0.01852 93  PHE   B CD1 
3448 C  CD2 . PHE   B 93  ? 0.36570 0.45443 0.41375 0.01499  0.02575  -0.02020 93  PHE   B CD2 
3449 C  CE1 . PHE   B 93  ? 0.43734 0.53025 0.49255 0.00683  0.02216  -0.01947 93  PHE   B CE1 
3450 C  CE2 . PHE   B 93  ? 0.37528 0.46259 0.42491 0.01503  0.02464  -0.02097 93  PHE   B CE2 
3451 C  CZ  . PHE   B 93  ? 0.38813 0.47707 0.44140 0.01104  0.02274  -0.02092 93  PHE   B CZ  
3452 N  N   . TRP   B 94  ? 0.29168 0.39922 0.34533 0.01191  0.03210  -0.01922 94  TRP   B N   
3453 C  CA  . TRP   B 94  ? 0.30190 0.41101 0.35404 0.01311  0.03291  -0.01850 94  TRP   B CA  
3454 C  C   . TRP   B 94  ? 0.33200 0.43878 0.38187 0.01760  0.03328  -0.01761 94  TRP   B C   
3455 O  O   . TRP   B 94  ? 0.30881 0.41910 0.36269 0.01883  0.03446  -0.01759 94  TRP   B O   
3456 C  CB  . TRP   B 94  ? 0.28516 0.40200 0.34269 0.01182  0.03439  -0.02009 94  TRP   B CB  
3457 C  CG  . TRP   B 94  ? 0.27764 0.39747 0.33509 0.01244  0.03486  -0.01974 94  TRP   B CG  
3458 C  CD1 . TRP   B 94  ? 0.33779 0.46071 0.39900 0.01350  0.03498  -0.02010 94  TRP   B CD1 
3459 C  CD2 . TRP   B 94  ? 0.29012 0.41056 0.34417 0.01124  0.03461  -0.01875 94  TRP   B CD2 
3460 N  NE1 . TRP   B 94  ? 0.34045 0.46582 0.40076 0.01331  0.03478  -0.01976 94  TRP   B NE1 
3461 C  CE2 . TRP   B 94  ? 0.35611 0.48004 0.41179 0.01221  0.03483  -0.01910 94  TRP   B CE2 
3462 C  CE3 . TRP   B 94  ? 0.33070 0.44880 0.38049 0.00894  0.03357  -0.01694 94  TRP   B CE3 
3463 C  CZ2 . TRP   B 94  ? 0.40401 0.52913 0.45679 0.01164  0.03452  -0.01828 94  TRP   B CZ2 
3464 C  CZ3 . TRP   B 94  ? 0.35926 0.47877 0.40622 0.00798  0.03325  -0.01564 94  TRP   B CZ3 
3465 C  CH2 . TRP   B 94  ? 0.34889 0.47197 0.39718 0.00964  0.03398  -0.01665 94  TRP   B CH2 
3466 N  N   . ILE   B 95  ? 0.30965 0.41035 0.35251 0.02039  0.03177  -0.01652 95  ILE   B N   
3467 C  CA  . ILE   B 95  ? 0.28857 0.38877 0.32820 0.02612  0.03233  -0.01562 95  ILE   B CA  
3468 C  C   . ILE   B 95  ? 0.36105 0.46879 0.40413 0.02684  0.03408  -0.01437 95  ILE   B C   
3469 O  O   . ILE   B 95  ? 0.30726 0.41332 0.34733 0.02681  0.03310  -0.01411 95  ILE   B O   
3470 C  CB  . ILE   B 95  ? 0.33407 0.42373 0.36350 0.03020  0.02910  -0.01574 95  ILE   B CB  
3471 C  CG1 . ILE   B 95  ? 0.36332 0.44506 0.39045 0.02753  0.02618  -0.01671 95  ILE   B CG1 
3472 C  CG2 . ILE   B 95  ? 0.32446 0.41541 0.34916 0.03840  0.03001  -0.01509 95  ILE   B CG2 
3473 C  CD1 . ILE   B 95  ? 0.42077 0.48877 0.43692 0.03014  0.02071  -0.01689 95  ILE   B CD1 
3474 N  N   . ALA   B 96  ? 0.32600 0.44172 0.37589 0.02650  0.03594  -0.01327 96  ALA   B N   
3475 C  CA  . ALA   B 96  ? 0.31670 0.43991 0.37199 0.02511  0.03657  -0.01195 96  ALA   B CA  
3476 C  C   . ALA   B 96  ? 0.31170 0.44010 0.36571 0.03010  0.03750  -0.00891 96  ALA   B C   
3477 O  O   . ALA   B 96  ? 0.31497 0.45203 0.37465 0.03055  0.03855  -0.00574 96  ALA   B O   
3478 C  CB  . ALA   B 96  ? 0.30119 0.42901 0.36433 0.02171  0.03651  -0.01175 96  ALA   B CB  
3479 N  N   . ASP   B 97  ? 0.34366 0.46682 0.38994 0.03400  0.03663  -0.00952 97  ASP   B N   
3480 C  CA  . ASP   B 97  ? 0.31606 0.44376 0.35915 0.04093  0.03737  -0.00730 97  ASP   B CA  
3481 C  C   . ASP   B 97  ? 0.28977 0.42862 0.33992 0.03994  0.03827  -0.00434 97  ASP   B C   
3482 O  O   . ASP   B 97  ? 0.32551 0.47543 0.37970 0.04304  0.03999  -0.00051 97  ASP   B O   
3483 C  CB  . ASP   B 97  ? 0.32008 0.43740 0.35225 0.04578  0.03482  -0.00918 97  ASP   B CB  
3484 C  CG  . ASP   B 97  ? 0.38783 0.49844 0.41818 0.04106  0.03245  -0.01050 97  ASP   B CG  
3485 O  OD1 . ASP   B 97  ? 0.33930 0.45350 0.37566 0.03496  0.03307  -0.01056 97  ASP   B OD1 
3486 O  OD2 . ASP   B 97  ? 0.41682 0.51710 0.43819 0.04384  0.02922  -0.01152 97  ASP   B OD2 
3487 N  N   . TRP   B 98  ? 0.37534 0.51252 0.42735 0.03544  0.03695  -0.00552 98  TRP   B N   
3488 C  CA  . TRP   B 98  ? 0.32850 0.47500 0.38712 0.03386  0.03677  -0.00294 98  TRP   B CA  
3489 C  C   . TRP   B 98  ? 0.36377 0.51805 0.43191 0.02968  0.03685  -0.00039 98  TRP   B C   
3490 O  O   . TRP   B 98  ? 0.31760 0.48195 0.39212 0.02922  0.03649  0.00371  98  TRP   B O   
3491 C  CB  . TRP   B 98  ? 0.39035 0.53228 0.44771 0.03000  0.03494  -0.00526 98  TRP   B CB  
3492 C  CG  . TRP   B 98  ? 0.47135 0.61129 0.52287 0.03387  0.03403  -0.00496 98  TRP   B CG  
3493 C  CD1 . TRP   B 98  ? 0.52815 0.66805 0.57431 0.04105  0.03423  -0.00386 98  TRP   B CD1 
3494 C  CD2 . TRP   B 98  ? 0.43521 0.57170 0.48422 0.03142  0.03228  -0.00613 98  TRP   B CD2 
3495 N  NE1 . TRP   B 98  ? 0.59269 0.72829 0.63333 0.04308  0.03221  -0.00435 98  TRP   B NE1 
3496 C  CE2 . TRP   B 98  ? 0.55347 0.68715 0.59601 0.03673  0.03112  -0.00539 98  TRP   B CE2 
3497 C  CE3 . TRP   B 98  ? 0.37687 0.51207 0.42736 0.02595  0.03142  -0.00792 98  TRP   B CE3 
3498 C  CZ2 . TRP   B 98  ? 0.66725 0.79708 0.70578 0.03567  0.02899  -0.00571 98  TRP   B CZ2 
3499 C  CZ3 . TRP   B 98  ? 0.54186 0.67449 0.58811 0.02517  0.02984  -0.00821 98  TRP   B CZ3 
3500 C  CH2 . TRP   B 98  ? 0.56847 0.69833 0.60918 0.02950  0.02860  -0.00684 98  TRP   B CH2 
3501 N  N   . PHE   B 99  ? 0.32489 0.47450 0.39439 0.02621  0.03657  -0.00241 99  PHE   B N   
3502 C  CA  . PHE   B 99  ? 0.30133 0.45599 0.37907 0.02213  0.03541  0.00002  99  PHE   B CA  
3503 C  C   . PHE   B 99  ? 0.33122 0.49496 0.41195 0.02483  0.03718  0.00535  99  PHE   B C   
3504 O  O   . PHE   B 99  ? 0.34143 0.51422 0.43018 0.02189  0.03590  0.01040  99  PHE   B O   
3505 C  CB  . PHE   B 99  ? 0.25295 0.39956 0.33033 0.01884  0.03439  -0.00406 99  PHE   B CB  
3506 C  CG  . PHE   B 99  ? 0.27818 0.41977 0.35409 0.01624  0.03270  -0.00833 99  PHE   B CG  
3507 C  CD1 . PHE   B 99  ? 0.30897 0.44562 0.37829 0.01749  0.03380  -0.01121 99  PHE   B CD1 
3508 C  CD2 . PHE   B 99  ? 0.30690 0.44876 0.38751 0.01265  0.02937  -0.00922 99  PHE   B CD2 
3509 C  CE1 . PHE   B 99  ? 0.30316 0.43757 0.37090 0.01533  0.03273  -0.01447 99  PHE   B CE1 
3510 C  CE2 . PHE   B 99  ? 0.25918 0.39731 0.33713 0.01157  0.02789  -0.01366 99  PHE   B CE2 
3511 C  CZ  . PHE   B 99  ? 0.24445 0.38012 0.31613 0.01296  0.03012  -0.01612 99  PHE   B CZ  
3512 N  N   . ALA   B 100 ? 0.30176 0.46333 0.37597 0.03025  0.03963  0.00467  100 ALA   B N   
3513 C  CA  . ALA   B 100 ? 0.26017 0.43185 0.33538 0.03460  0.04191  0.00967  100 ALA   B CA  
3514 C  C   . ALA   B 100 ? 0.36072 0.54589 0.43948 0.03759  0.04282  0.01467  100 ALA   B C   
3515 O  O   . ALA   B 100 ? 0.32112 0.52024 0.40721 0.03685  0.04359  0.02140  100 ALA   B O   
3516 C  CB  . ALA   B 100 ? 0.29107 0.45610 0.35579 0.04167  0.04355  0.00673  100 ALA   B CB  
3517 N  N   . HIS   B 101 ? 0.29955 0.48123 0.37348 0.04068  0.04243  0.01196  101 HIS   B N   
3518 C  CA  . HIS   B 101 ? 0.38097 0.57543 0.45830 0.04391  0.04297  0.01631  101 HIS   B CA  
3519 C  C   . HIS   B 101 ? 0.34441 0.54773 0.43378 0.03598  0.04056  0.02105  101 HIS   B C   
3520 O  O   . HIS   B 101 ? 0.35008 0.56966 0.44720 0.03611  0.04115  0.02831  101 HIS   B O   
3521 C  CB  . HIS   B 101 ? 0.36631 0.55250 0.43567 0.04789  0.04198  0.01196  101 HIS   B CB  
3522 C  CG  . HIS   B 101 ? 0.42058 0.61879 0.49346 0.05102  0.04193  0.01574  101 HIS   B CG  
3523 N  ND1 . HIS   B 101 ? 0.50202 0.71150 0.57239 0.06041  0.04425  0.01875  101 HIS   B ND1 
3524 C  CD2 . HIS   B 101 ? 0.55790 0.75897 0.63625 0.04660  0.03964  0.01686  101 HIS   B CD2 
3525 C  CE1 . HIS   B 101 ? 0.52174 0.74148 0.59675 0.06148  0.04358  0.02191  101 HIS   B CE1 
3526 N  NE2 . HIS   B 101 ? 0.56582 0.78005 0.64575 0.05277  0.04059  0.02085  101 HIS   B NE2 
3527 N  N   . LEU   B 102 ? 0.38170 0.57478 0.47255 0.02915  0.03733  0.01730  102 LEU   B N   
3528 C  CA  . LEU   B 102 ? 0.33550 0.53299 0.43599 0.02170  0.03332  0.02061  102 LEU   B CA  
3529 C  C   . LEU   B 102 ? 0.36918 0.57455 0.47781 0.01763  0.03237  0.02678  102 LEU   B C   
3530 O  O   . LEU   B 102 ? 0.34223 0.55685 0.46023 0.01258  0.02905  0.03304  102 LEU   B O   
3531 C  CB  . LEU   B 102 ? 0.32934 0.51273 0.42710 0.01712  0.03009  0.01404  102 LEU   B CB  
3532 C  CG  . LEU   B 102 ? 0.34037 0.52185 0.44371 0.01067  0.02455  0.01408  102 LEU   B CG  
3533 C  CD1 . LEU   B 102 ? 0.29382 0.48485 0.40114 0.01094  0.02311  0.01821  102 LEU   B CD1 
3534 C  CD2 . LEU   B 102 ? 0.29975 0.46797 0.39649 0.00976  0.02319  0.00620  102 LEU   B CD2 
3535 N  N   . ASN   B 103 ? 0.35572 0.55739 0.46104 0.01922  0.03460  0.02571  103 ASN   B N   
3536 C  CA  . ASN   B 103 ? 0.33706 0.54520 0.44918 0.01527  0.03359  0.03176  103 ASN   B CA  
3537 C  C   . ASN   B 103 ? 0.36319 0.58836 0.47664 0.02074  0.03802  0.03904  103 ASN   B C   
3538 O  O   . ASN   B 103 ? 0.32795 0.55861 0.44454 0.01913  0.03852  0.04391  103 ASN   B O   
3539 C  CB  . ASN   B 103 ? 0.28757 0.48182 0.39527 0.01381  0.03305  0.02634  103 ASN   B CB  
3540 C  CG  . ASN   B 103 ? 0.37949 0.57395 0.49470 0.00677  0.02879  0.03074  103 ASN   B CG  
3541 O  OD1 . ASN   B 103 ? 0.35977 0.56343 0.48385 0.00167  0.02534  0.03809  103 ASN   B OD1 
3542 N  ND2 . ASN   B 103 ? 0.36289 0.54640 0.47458 0.00612  0.02822  0.02643  103 ASN   B ND2 
3543 N  N   . ASN   B 104 ? 0.35195 0.58560 0.46209 0.02807  0.04125  0.03964  104 ASN   B N   
3544 C  CA  . ASN   B 104 ? 0.37511 0.62868 0.48714 0.03441  0.04532  0.04717  104 ASN   B CA  
3545 C  C   . ASN   B 104 ? 0.46492 0.71767 0.56878 0.04132  0.04931  0.04594  104 ASN   B C   
3546 O  O   . ASN   B 104 ? 0.39716 0.66712 0.50383 0.04467  0.05227  0.05338  104 ASN   B O   
3547 C  CB  . ASN   B 104 ? 0.34973 0.62043 0.47561 0.02692  0.04305  0.05817  104 ASN   B CB  
3548 C  CG  . ASN   B 104 ? 0.51447 0.79020 0.64828 0.02205  0.03913  0.06084  104 ASN   B CG  
3549 O  OD1 . ASN   B 104 ? 0.54389 0.82210 0.67402 0.02810  0.04078  0.05828  104 ASN   B OD1 
3550 N  ND2 . ASN   B 104 ? 0.53823 0.81330 0.68200 0.01118  0.03301  0.06545  104 ASN   B ND2 
3551 N  N   . LYS   B 105 ? 0.36084 0.59492 0.45439 0.04385  0.04927  0.03707  105 LYS   B N   
3552 C  CA  . LYS   B 105 ? 0.37632 0.60640 0.46065 0.05053  0.05194  0.03471  105 LYS   B CA  
3553 C  C   . LYS   B 105 ? 0.41002 0.64325 0.48373 0.06319  0.05482  0.03245  105 LYS   B C   
3554 O  O   . LYS   B 105 ? 0.41247 0.64267 0.48321 0.06624  0.05400  0.02944  105 LYS   B O   
3555 C  CB  . LYS   B 105 ? 0.35663 0.56525 0.43515 0.04711  0.04963  0.02653  105 LYS   B CB  
3556 C  CG  . LYS   B 105 ? 0.34123 0.54537 0.42870 0.03624  0.04625  0.02759  105 LYS   B CG  
3557 C  CD  . LYS   B 105 ? 0.41922 0.63588 0.51374 0.03341  0.04670  0.03592  105 LYS   B CD  
3558 C  CE  . LYS   B 105 ? 0.47616 0.68706 0.57933 0.02275  0.04172  0.03727  105 LYS   B CE  
3559 N  NZ  . LYS   B 105 ? 0.42687 0.61935 0.52502 0.02088  0.03977  0.02912  105 LYS   B NZ  
3560 N  N   . MET   B 106 ? 0.43488 0.67347 0.50185 0.07127  0.05768  0.03366  106 MET   B N   
3561 C  CA  . MET   B 106 ? 0.50053 0.73895 0.55465 0.08504  0.05932  0.03007  106 MET   B CA  
3562 C  C   . MET   B 106 ? 0.49489 0.74931 0.55266 0.09006  0.06068  0.03391  106 MET   B C   
3563 O  O   . MET   B 106 ? 0.49940 0.74613 0.54833 0.09757  0.05945  0.02865  106 MET   B O   
3564 C  CB  . MET   B 106 ? 0.46739 0.68041 0.50922 0.08714  0.05582  0.01992  106 MET   B CB  
3565 C  CG  . MET   B 106 ? 0.45920 0.65567 0.49639 0.08317  0.05399  0.01549  106 MET   B CG  
3566 S  SD  . MET   B 106 ? 0.58049 0.78081 0.60641 0.09476  0.05619  0.01587  106 MET   B SD  
3567 C  CE  . MET   B 106 ? 0.56771 0.77643 0.58312 0.11064  0.05748  0.01517  106 MET   B CE  
3568 N  N   . SER   B 107 ? 0.44734 0.72364 0.51871 0.08517  0.06242  0.04352  107 SER   B N   
3569 C  CA  . SER   B 107 ? 0.56584 0.86081 0.64293 0.08911  0.06370  0.04866  107 SER   B CA  
3570 C  C   . SER   B 107 ? 0.59992 0.88262 0.67771 0.08526  0.06006  0.04373  107 SER   B C   
3571 O  O   . SER   B 107 ? 0.56246 0.85523 0.64052 0.09143  0.06058  0.04510  107 SER   B O   
3572 C  CB  . SER   B 107 ? 0.60675 0.91375 0.67324 0.10612  0.06738  0.04847  107 SER   B CB  
3573 O  OG  . SER   B 107 ? 0.63588 0.95094 0.69753 0.11201  0.07070  0.05108  107 SER   B OG  
3574 N  N   . GLY   B 108 ? 0.46475 0.72683 0.54256 0.07574  0.05645  0.03814  108 GLY   B N   
3575 C  CA  . GLY   B 108 ? 0.48095 0.72928 0.55719 0.07237  0.05307  0.03270  108 GLY   B CA  
3576 C  C   . GLY   B 108 ? 0.57224 0.80663 0.63393 0.08215  0.05226  0.02518  108 GLY   B C   
3577 O  O   . GLY   B 108 ? 0.62783 0.85030 0.68718 0.07949  0.04931  0.02096  108 GLY   B O   
3578 N  N   . ASP   B 109 ? 0.45587 0.69063 0.50703 0.09341  0.05411  0.02351  109 ASP   B N   
3579 C  CA  . ASP   B 109 ? 0.46007 0.68250 0.49633 0.10468  0.05217  0.01710  109 ASP   B CA  
3580 C  C   . ASP   B 109 ? 0.40083 0.59632 0.42852 0.09994  0.04794  0.00946  109 ASP   B C   
3581 O  O   . ASP   B 109 ? 0.42690 0.61326 0.45020 0.09884  0.04771  0.00714  109 ASP   B O   
3582 C  CB  . ASP   B 109 ? 0.48027 0.71154 0.50750 0.11842  0.05485  0.01770  109 ASP   B CB  
3583 C  CG  . ASP   B 109 ? 0.57590 0.79510 0.58659 0.13217  0.05185  0.01122  109 ASP   B CG  
3584 O  OD1 . ASP   B 109 ? 0.60236 0.83369 0.60613 0.14599  0.05412  0.01224  109 ASP   B OD1 
3585 O  OD2 . ASP   B 109 ? 0.69053 0.88881 0.69495 0.12948  0.04692  0.00549  109 ASP   B OD2 
3586 N  N   . LEU   B 110 ? 0.41739 0.60096 0.44235 0.09750  0.04442  0.00604  110 LEU   B N   
3587 C  CA  . LEU   B 110 ? 0.54098 0.70201 0.55971 0.09146  0.04042  0.00047  110 LEU   B CA  
3588 C  C   . LEU   B 110 ? 0.52347 0.66818 0.52673 0.09987  0.03714  -0.00458 110 LEU   B C   
3589 O  O   . LEU   B 110 ? 0.49298 0.62216 0.49259 0.09432  0.03445  -0.00775 110 LEU   B O   
3590 C  CB  . LEU   B 110 ? 0.60271 0.75582 0.62171 0.08672  0.03730  -0.00108 110 LEU   B CB  
3591 C  CG  . LEU   B 110 ? 0.65582 0.81032 0.68594 0.07376  0.03771  0.00021  110 LEU   B CG  
3592 C  CD1 . LEU   B 110 ? 0.66794 0.84194 0.71128 0.07048  0.04064  0.00584  110 LEU   B CD1 
3593 C  CD2 . LEU   B 110 ? 0.72504 0.86817 0.75176 0.06983  0.03415  -0.00225 110 LEU   B CD2 
3594 N  N   . LYS   B 111 ? 0.46861 0.61636 0.46236 0.11347  0.03670  -0.00544 111 LYS   B N   
3595 C  CA  . LYS   B 111 ? 0.53034 0.66073 0.50799 0.12216  0.03235  -0.01071 111 LYS   B CA  
3596 C  C   . LYS   B 111 ? 0.49532 0.62712 0.47314 0.12118  0.03459  -0.01043 111 LYS   B C   
3597 O  O   . LYS   B 111 ? 0.55008 0.66340 0.51931 0.12004  0.03028  -0.01455 111 LYS   B O   
3598 C  CB  . LYS   B 111 ? 0.60228 0.73556 0.56807 0.13900  0.03101  -0.01244 111 LYS   B CB  
3599 C  CG  . LYS   B 111 ? 0.76407 0.89572 0.72894 0.14116  0.02828  -0.01279 111 LYS   B CG  
3600 C  CD  . LYS   B 111 ? 0.77089 0.90133 0.72115 0.15955  0.02540  -0.01594 111 LYS   B CD  
3601 C  CE  . LYS   B 111 ? 0.90486 1.00499 0.83644 0.16465  0.01612  -0.02298 111 LYS   B CE  
3602 N  NZ  . LYS   B 111 ? 0.98320 1.06431 0.91726 0.14985  0.01123  -0.02370 111 LYS   B NZ  
3603 N  N   . LYS   B 112 ? 0.41870 0.57246 0.40604 0.12162  0.04079  -0.00505 112 LYS   B N   
3604 C  CA  . LYS   B 112 ? 0.42270 0.57863 0.41058 0.12032  0.04294  -0.00410 112 LYS   B CA  
3605 C  C   . LYS   B 112 ? 0.41744 0.56275 0.41279 0.10576  0.04167  -0.00490 112 LYS   B C   
3606 O  O   . LYS   B 112 ? 0.42445 0.55801 0.41430 0.10471  0.03969  -0.00772 112 LYS   B O   
3607 C  CB  . LYS   B 112 ? 0.42813 0.61087 0.42578 0.12237  0.04941  0.00329  112 LYS   B CB  
3608 C  CG  . LYS   B 112 ? 0.45128 0.64973 0.44147 0.13895  0.05177  0.00490  112 LYS   B CG  
3609 C  CD  . LYS   B 112 ? 0.48890 0.71451 0.48867 0.13978  0.05815  0.01336  112 LYS   B CD  
3610 C  CE  . LYS   B 112 ? 0.56170 0.81012 0.55794 0.15514  0.06181  0.01704  112 LYS   B CE  
3611 N  NZ  . LYS   B 112 ? 0.69663 0.96983 0.70058 0.15512  0.06770  0.02573  112 LYS   B NZ  
3612 N  N   . ILE   B 113 ? 0.39537 0.54514 0.40284 0.09518  0.04252  -0.00256 113 ILE   B N   
3613 C  CA  . ILE   B 113 ? 0.38157 0.52371 0.39627 0.08262  0.04160  -0.00339 113 ILE   B CA  
3614 C  C   . ILE   B 113 ? 0.43588 0.55642 0.44101 0.08110  0.03646  -0.00890 113 ILE   B C   
3615 O  O   . ILE   B 113 ? 0.38253 0.49504 0.38844 0.07525  0.03529  -0.01046 113 ILE   B O   
3616 C  CB  . ILE   B 113 ? 0.34408 0.49421 0.37100 0.07381  0.04262  -0.00063 113 ILE   B CB  
3617 C  CG1 . ILE   B 113 ? 0.34751 0.51794 0.38566 0.07243  0.04648  0.00590  113 ILE   B CG1 
3618 C  CG2 . ILE   B 113 ? 0.31188 0.45150 0.34315 0.06282  0.04068  -0.00312 113 ILE   B CG2 
3619 C  CD1 . ILE   B 113 ? 0.41538 0.59391 0.46422 0.06562  0.04625  0.00881  113 ILE   B CD1 
3620 N  N   . LYS   B 114 ? 0.42158 0.53263 0.41778 0.08612  0.03275  -0.01140 114 LYS   B N   
3621 C  CA  . LYS   B 114 ? 0.47856 0.56865 0.46514 0.08445  0.02656  -0.01547 114 LYS   B CA  
3622 C  C   . LYS   B 114 ? 0.44688 0.52618 0.42266 0.09051  0.02359  -0.01832 114 LYS   B C   
3623 O  O   . LYS   B 114 ? 0.44265 0.50924 0.41667 0.08437  0.01998  -0.02005 114 LYS   B O   
3624 C  CB  . LYS   B 114 ? 0.52826 0.61005 0.50680 0.08921  0.02232  -0.01694 114 LYS   B CB  
3625 C  CG  . LYS   B 114 ? 0.59776 0.65725 0.56599 0.08702  0.01455  -0.01996 114 LYS   B CG  
3626 C  CD  . LYS   B 114 ? 0.80652 0.85631 0.76302 0.09600  0.00926  -0.02179 114 LYS   B CD  
3627 C  CE  . LYS   B 114 ? 0.86982 0.90189 0.82172 0.08891  0.00204  -0.02213 114 LYS   B CE  
3628 N  NZ  . LYS   B 114 ? 0.89550 0.90871 0.83036 0.09915  -0.00666 -0.02543 114 LYS   B NZ  
3629 N  N   . LYS   B 115 ? 0.37264 0.45754 0.34087 0.10289  0.02483  -0.01868 115 LYS   B N   
3630 C  CA  . LYS   B 115 ? 0.43961 0.51420 0.39647 0.10945  0.02180  -0.02173 115 LYS   B CA  
3631 C  C   . LYS   B 115 ? 0.43054 0.50936 0.39571 0.10143  0.02472  -0.02011 115 LYS   B C   
3632 O  O   . LYS   B 115 ? 0.42115 0.48581 0.38026 0.09981  0.02037  -0.02282 115 LYS   B O   
3633 C  CB  . LYS   B 115 ? 0.46708 0.55002 0.41426 0.12524  0.02348  -0.02221 115 LYS   B CB  
3634 C  CG  . LYS   B 115 ? 0.58035 0.64821 0.51299 0.13484  0.01670  -0.02650 115 LYS   B CG  
3635 C  CD  . LYS   B 115 ? 0.71928 0.79635 0.64167 0.15211  0.01818  -0.02749 115 LYS   B CD  
3636 C  CE  . LYS   B 115 ? 0.81136 0.86710 0.71630 0.16207  0.00905  -0.03321 115 LYS   B CE  
3637 N  NZ  . LYS   B 115 ? 0.91006 0.93937 0.80525 0.15777  0.00033  -0.03738 115 LYS   B NZ  
3638 N  N   . VAL   B 116 ? 0.40016 0.49783 0.37900 0.09641  0.03129  -0.01551 116 VAL   B N   
3639 C  CA  . VAL   B 116 ? 0.40536 0.50632 0.39192 0.08903  0.03344  -0.01397 116 VAL   B CA  
3640 C  C   . VAL   B 116 ? 0.40814 0.49679 0.39877 0.07794  0.03008  -0.01601 116 VAL   B C   
3641 O  O   . VAL   B 116 ? 0.36471 0.44579 0.35419 0.07478  0.02814  -0.01744 116 VAL   B O   
3642 C  CB  . VAL   B 116 ? 0.35668 0.47868 0.35706 0.08509  0.03966  -0.00815 116 VAL   B CB  
3643 C  CG1 . VAL   B 116 ? 0.31982 0.44222 0.32830 0.07631  0.04056  -0.00697 116 VAL   B CG1 
3644 C  CG2 . VAL   B 116 ? 0.40625 0.54353 0.40305 0.09602  0.04335  -0.00476 116 VAL   B CG2 
3645 N  N   . GLY   B 117 ? 0.36640 0.45412 0.36187 0.07214  0.02940  -0.01583 117 GLY   B N   
3646 C  CA  . GLY   B 117 ? 0.38709 0.46546 0.38596 0.06237  0.02647  -0.01716 117 GLY   B CA  
3647 C  C   . GLY   B 117 ? 0.40448 0.46469 0.39255 0.06332  0.01983  -0.02010 117 GLY   B C   
3648 O  O   . GLY   B 117 ? 0.40641 0.46135 0.39750 0.05628  0.01788  -0.02051 117 GLY   B O   
3649 N  N   . SER   B 118 ? 0.38260 0.43261 0.35796 0.07186  0.01545  -0.02205 118 SER   B N   
3650 C  CA  . SER   B 118 ? 0.46674 0.49720 0.43006 0.07370  0.00741  -0.02484 118 SER   B CA  
3651 C  C   . SER   B 118 ? 0.47621 0.50463 0.43685 0.07590  0.00717  -0.02606 118 SER   B C   
3652 O  O   . SER   B 118 ? 0.46159 0.47787 0.41982 0.07095  0.00176  -0.02702 118 SER   B O   
3653 C  CB  . SER   B 118 ? 0.43563 0.45461 0.38408 0.08466  0.00204  -0.02738 118 SER   B CB  
3654 O  OG  . SER   B 118 ? 0.53863 0.55939 0.49009 0.08191  0.00206  -0.02597 118 SER   B OG  
3655 N  N   . TYR   B 119 ? 0.40332 0.44380 0.36391 0.08344  0.01252  -0.02551 119 TYR   B N   
3656 C  CA  . TYR   B 119 ? 0.37439 0.41460 0.33274 0.08552  0.01289  -0.02612 119 TYR   B CA  
3657 C  C   . TYR   B 119 ? 0.41529 0.45993 0.38651 0.07380  0.01498  -0.02436 119 TYR   B C   
3658 O  O   . TYR   B 119 ? 0.42824 0.46407 0.39671 0.07174  0.01135  -0.02575 119 TYR   B O   
3659 C  CB  . TYR   B 119 ? 0.37647 0.43210 0.33339 0.09532  0.01888  -0.02440 119 TYR   B CB  
3660 C  CG  . TYR   B 119 ? 0.37427 0.43930 0.33661 0.09369  0.02288  -0.02221 119 TYR   B CG  
3661 C  CD1 . TYR   B 119 ? 0.37350 0.43016 0.32552 0.09934  0.01982  -0.02448 119 TYR   B CD1 
3662 C  CD2 . TYR   B 119 ? 0.39455 0.47545 0.37243 0.08563  0.02884  -0.01781 119 TYR   B CD2 
3663 C  CE1 . TYR   B 119 ? 0.40083 0.46667 0.35831 0.09731  0.02354  -0.02188 119 TYR   B CE1 
3664 C  CE2 . TYR   B 119 ? 0.39827 0.48688 0.38156 0.08326  0.03174  -0.01528 119 TYR   B CE2 
3665 C  CZ  . TYR   B 119 ? 0.44331 0.52509 0.41680 0.08893  0.02946  -0.01708 119 TYR   B CZ  
3666 O  OH  . TYR   B 119 ? 0.49460 0.58458 0.47406 0.08600  0.03234  -0.01398 119 TYR   B OH  
3667 N  N   . PHE   B 120 ? 0.34567 0.40292 0.33037 0.06636  0.01996  -0.02164 120 PHE   B N   
3668 C  CA  . PHE   B 120 ? 0.41347 0.47423 0.40950 0.05628  0.02126  -0.02070 120 PHE   B CA  
3669 C  C   . PHE   B 120 ? 0.43028 0.47779 0.42394 0.05053  0.01521  -0.02228 120 PHE   B C   
3670 O  O   . PHE   B 120 ? 0.38661 0.43207 0.38359 0.04607  0.01384  -0.02256 120 PHE   B O   
3671 C  CB  . PHE   B 120 ? 0.35841 0.43103 0.36649 0.05004  0.02556  -0.01860 120 PHE   B CB  
3672 C  CG  . PHE   B 120 ? 0.38571 0.47321 0.40132 0.05115  0.03101  -0.01568 120 PHE   B CG  
3673 C  CD1 . PHE   B 120 ? 0.37310 0.46555 0.38458 0.05817  0.03287  -0.01414 120 PHE   B CD1 
3674 C  CD2 . PHE   B 120 ? 0.38388 0.48062 0.41023 0.04520  0.03367  -0.01400 120 PHE   B CD2 
3675 C  CE1 . PHE   B 120 ? 0.37020 0.47777 0.38967 0.05791  0.03736  -0.00979 120 PHE   B CE1 
3676 C  CE2 . PHE   B 120 ? 0.36510 0.47465 0.39895 0.04500  0.03725  -0.01043 120 PHE   B CE2 
3677 C  CZ  . PHE   B 120 ? 0.34183 0.45719 0.37294 0.05064  0.03905  -0.00780 120 PHE   B CZ  
3678 N  N   . ILE   B 121 ? 0.38906 0.42877 0.37822 0.04966  0.01141  -0.02257 121 ILE   B N   
3679 C  CA  . ILE   B 121 ? 0.43696 0.46550 0.42492 0.04278  0.00509  -0.02247 121 ILE   B CA  
3680 C  C   . ILE   B 121 ? 0.46632 0.48050 0.44412 0.04619  -0.00152 -0.02439 121 ILE   B C   
3681 O  O   . ILE   B 121 ? 0.44258 0.45256 0.42346 0.03960  -0.00514 -0.02369 121 ILE   B O   
3682 C  CB  . ILE   B 121 ? 0.40983 0.43181 0.39398 0.04104  0.00136  -0.02155 121 ILE   B CB  
3683 C  CG1 . ILE   B 121 ? 0.41145 0.44716 0.40641 0.03574  0.00708  -0.01953 121 ILE   B CG1 
3684 C  CG2 . ILE   B 121 ? 0.42413 0.43240 0.40472 0.03445  -0.00714 -0.02034 121 ILE   B CG2 
3685 C  CD1 . ILE   B 121 ? 0.42248 0.45189 0.41250 0.03515  0.00356  -0.01843 121 ILE   B CD1 
3686 N  N   . GLU   B 122 ? 0.40741 0.41397 0.37239 0.05701  -0.00370 -0.02687 122 GLU   B N   
3687 C  CA  . GLU   B 122 ? 0.44512 0.43706 0.39875 0.06149  -0.01055 -0.02936 122 GLU   B CA  
3688 C  C   . GLU   B 122 ? 0.50383 0.50283 0.46437 0.05854  -0.00740 -0.02892 122 GLU   B C   
3689 O  O   . GLU   B 122 ? 0.46278 0.45191 0.42114 0.05508  -0.01331 -0.02947 122 GLU   B O   
3690 C  CB  . GLU   B 122 ? 0.53206 0.51841 0.47065 0.07576  -0.01181 -0.03251 122 GLU   B CB  
3691 C  CG  . GLU   B 122 ? 0.66270 0.63691 0.59008 0.08141  -0.01758 -0.03418 122 GLU   B CG  
3692 C  CD  . GLU   B 122 ? 0.79798 0.74953 0.71696 0.07702  -0.02970 -0.03501 122 GLU   B CD  
3693 O  OE1 . GLU   B 122 ? 0.79398 0.72913 0.69997 0.08247  -0.03774 -0.03810 122 GLU   B OE1 
3694 O  OE2 . GLU   B 122 ? 0.86008 0.81016 0.78516 0.06794  -0.03171 -0.03215 122 GLU   B OE2 
3695 N  N   . VAL   B 123 ? 0.37268 0.38818 0.34113 0.06007  0.00113  -0.02765 123 VAL   B N   
3696 C  CA  . VAL   B 123 ? 0.38165 0.40432 0.35721 0.05718  0.00418  -0.02686 123 VAL   B CA  
3697 C  C   . VAL   B 123 ? 0.37333 0.39673 0.35964 0.04609  0.00268  -0.02572 123 VAL   B C   
3698 O  O   . VAL   B 123 ? 0.40571 0.42413 0.39229 0.04339  -0.00082 -0.02618 123 VAL   B O   
3699 C  CB  . VAL   B 123 ? 0.39247 0.43285 0.37611 0.05896  0.01277  -0.02453 123 VAL   B CB  
3700 C  CG1 . VAL   B 123 ? 0.38414 0.43074 0.37607 0.05457  0.01501  -0.02338 123 VAL   B CG1 
3701 C  CG2 . VAL   B 123 ? 0.36805 0.41126 0.34128 0.07082  0.01472  -0.02466 123 VAL   B CG2 
3702 N  N   . TRP   B 124 ? 0.33792 0.36933 0.33363 0.03992  0.00565  -0.02405 124 TRP   B N   
3703 C  CA  . TRP   B 124 ? 0.35020 0.38656 0.35682 0.03062  0.00558  -0.02275 124 TRP   B CA  
3704 C  C   . TRP   B 124 ? 0.39051 0.41492 0.39315 0.02630  -0.00241 -0.02229 124 TRP   B C   
3705 O  O   . TRP   B 124 ? 0.38157 0.40835 0.39063 0.02086  -0.00390 -0.02142 124 TRP   B O   
3706 C  CB  . TRP   B 124 ? 0.35604 0.40255 0.37111 0.02608  0.00966  -0.02127 124 TRP   B CB  
3707 C  CG  . TRP   B 124 ? 0.34554 0.40462 0.36754 0.02781  0.01650  -0.02116 124 TRP   B CG  
3708 C  CD1 . TRP   B 124 ? 0.37503 0.43999 0.40182 0.02853  0.01925  -0.02130 124 TRP   B CD1 
3709 C  CD2 . TRP   B 124 ? 0.34498 0.41133 0.36984 0.02839  0.02030  -0.02038 124 TRP   B CD2 
3710 N  NE1 . TRP   B 124 ? 0.34576 0.42083 0.37843 0.02904  0.02405  -0.02031 124 TRP   B NE1 
3711 C  CE2 . TRP   B 124 ? 0.32124 0.39765 0.35303 0.02898  0.02485  -0.01984 124 TRP   B CE2 
3712 C  CE3 . TRP   B 124 ? 0.37730 0.44214 0.39956 0.02811  0.01964  -0.01981 124 TRP   B CE3 
3713 C  CZ2 . TRP   B 124 ? 0.32495 0.40996 0.36142 0.02899  0.02841  -0.01870 124 TRP   B CZ2 
3714 C  CZ3 . TRP   B 124 ? 0.32325 0.39725 0.35000 0.02869  0.02386  -0.01904 124 TRP   B CZ3 
3715 C  CH2 . TRP   B 124 ? 0.35388 0.43781 0.38776 0.02904  0.02803  -0.01849 124 TRP   B CH2 
3716 N  N   . LYS   B 125 ? 0.37130 0.38298 0.36386 0.02820  -0.00829 -0.02242 125 LYS   B N   
3717 C  CA  . LYS   B 125 ? 0.42863 0.42774 0.41764 0.02288  -0.01748 -0.02108 125 LYS   B CA  
3718 C  C   . LYS   B 125 ? 0.44776 0.43652 0.42974 0.02625  -0.02266 -0.02309 125 LYS   B C   
3719 O  O   . LYS   B 125 ? 0.45535 0.43656 0.43769 0.02021  -0.03001 -0.02139 125 LYS   B O   
3720 C  CB  . LYS   B 125 ? 0.42111 0.40629 0.40003 0.02378  -0.02434 -0.02057 125 LYS   B CB  
3721 C  CG  . LYS   B 125 ? 0.45403 0.44900 0.44008 0.01908  -0.02020 -0.01788 125 LYS   B CG  
3722 C  CD  . LYS   B 125 ? 0.55764 0.53740 0.53283 0.02038  -0.02771 -0.01729 125 LYS   B CD  
3723 C  CE  . LYS   B 125 ? 0.66718 0.63419 0.64013 0.01214  -0.03844 -0.01370 125 LYS   B CE  
3724 N  NZ  . LYS   B 125 ? 0.84757 0.79547 0.80680 0.01548  -0.04736 -0.01401 125 LYS   B NZ  
3725 N  N   . SER   B 126 ? 0.39558 0.38386 0.37079 0.03555  -0.01966 -0.02614 126 SER   B N   
3726 C  CA  . SER   B 126 ? 0.39357 0.37204 0.36171 0.03855  -0.02490 -0.02798 126 SER   B CA  
3727 C  C   . SER   B 126 ? 0.41592 0.40678 0.39405 0.03650  -0.01931 -0.02752 126 SER   B C   
3728 O  O   . SER   B 126 ? 0.51004 0.49409 0.48386 0.03793  -0.02346 -0.02866 126 SER   B O   
3729 C  CB  . SER   B 126 ? 0.49898 0.46689 0.45029 0.05127  -0.02699 -0.03166 126 SER   B CB  
3730 O  OG  . SER   B 126 ? 0.50856 0.49173 0.46315 0.05711  -0.01704 -0.03166 126 SER   B OG  
3731 N  N   . CYS   B 127 ? 0.37623 0.38381 0.36727 0.03293  -0.01106 -0.02594 127 CYS   B N   
3732 C  CA  . CYS   B 127 ? 0.38777 0.40595 0.38787 0.03139  -0.00649 -0.02565 127 CYS   B CA  
3733 C  C   . CYS   B 127 ? 0.44890 0.47618 0.46260 0.02234  -0.00582 -0.02379 127 CYS   B C   
3734 O  O   . CYS   B 127 ? 0.45049 0.48858 0.47336 0.02099  -0.00119 -0.02372 127 CYS   B O   
3735 C  CB  . CYS   B 127 ? 0.41416 0.44334 0.41667 0.03622  0.00143  -0.02552 127 CYS   B CB  
3736 S  SG  . CYS   B 127 ? 0.44906 0.49283 0.46358 0.03192  0.00834  -0.02387 127 CYS   B SG  
3737 N  N   . GLY   B 128 ? 0.39621 0.41934 0.41089 0.01644  -0.01099 -0.02201 128 GLY   B N   
3738 C  CA  . GLY   B 128 ? 0.41405 0.44726 0.44090 0.00833  -0.01101 -0.01951 128 GLY   B CA  
3739 C  C   . GLY   B 128 ? 0.45457 0.49782 0.48844 0.00364  -0.00772 -0.01725 128 GLY   B C   
3740 O  O   . GLY   B 128 ? 0.42589 0.48157 0.47049 -0.00167 -0.00600 -0.01531 128 GLY   B O   
3741 N  N   . MET   B 129 ? 0.33788 0.37630 0.36550 0.00570  -0.00736 -0.01725 129 MET   B N   
3742 C  CA  . MET   B 129 ? 0.40316 0.45042 0.43644 0.00130  -0.00467 -0.01491 129 MET   B CA  
3743 C  C   . MET   B 129 ? 0.46938 0.50561 0.49545 -0.00148 -0.01108 -0.01233 129 MET   B C   
3744 O  O   . MET   B 129 ? 0.43161 0.47034 0.45711 -0.00159 -0.00876 -0.01154 129 MET   B O   
3745 C  CB  . MET   B 129 ? 0.39745 0.45344 0.43315 0.00547  0.00311  -0.01690 129 MET   B CB  
3746 C  CG  . MET   B 129 ? 0.41847 0.48798 0.46475 0.00424  0.00793  -0.01773 129 MET   B CG  
3747 S  SD  . MET   B 129 ? 0.63457 0.70507 0.68182 0.00937  0.01082  -0.02059 129 MET   B SD  
3748 C  CE  . MET   B 129 ? 0.45168 0.51885 0.49196 0.01622  0.01423  -0.02170 129 MET   B CE  
3749 N  N   . ASN   B 130 ? 0.33697 0.35965 0.35683 -0.00363 -0.01998 -0.01100 130 ASN   B N   
3750 C  CA  . ASN   B 130 ? 0.38008 0.39163 0.39410 -0.00804 -0.02780 -0.00756 130 ASN   B CA  
3751 C  C   . ASN   B 130 ? 0.44606 0.46911 0.47146 -0.01889 -0.02956 -0.00136 130 ASN   B C   
3752 O  O   . ASN   B 130 ? 0.42246 0.44194 0.44970 -0.02404 -0.03628 0.00145  130 ASN   B O   
3753 C  CB  . ASN   B 130 ? 0.40891 0.39807 0.40915 -0.00459 -0.03806 -0.00924 130 ASN   B CB  
3754 C  CG  . ASN   B 130 ? 0.49294 0.46711 0.48503 -0.00801 -0.04741 -0.00625 130 ASN   B CG  
3755 O  OD1 . ASN   B 130 ? 0.58882 0.57024 0.58558 -0.01264 -0.04525 -0.00281 130 ASN   B OD1 
3756 N  ND2 . ASN   B 130 ? 0.56476 0.51712 0.54370 -0.00521 -0.05828 -0.00773 130 ASN   B ND2 
3757 N  N   . MET   B 131 ? 0.37181 0.40971 0.40489 -0.02237 -0.02379 0.00126  131 MET   B N   
3758 C  CA  . MET   B 131 ? 0.41939 0.47330 0.46440 -0.03127 -0.02368 0.00718  131 MET   B CA  
3759 C  C   . MET   B 131 ? 0.43129 0.49799 0.48098 -0.03495 -0.01937 0.01084  131 MET   B C   
3760 O  O   . MET   B 131 ? 0.39163 0.45942 0.43838 -0.02978 -0.01373 0.00747  131 MET   B O   
3761 C  CB  . MET   B 131 ? 0.49175 0.56030 0.54652 -0.02969 -0.01808 0.00498  131 MET   B CB  
3762 C  CG  . MET   B 131 ? 0.48346 0.56155 0.54095 -0.02254 -0.00836 -0.00054 131 MET   B CG  
3763 S  SD  . MET   B 131 ? 0.46432 0.54858 0.52756 -0.01814 -0.00504 -0.00486 131 MET   B SD  
3764 C  CE  . MET   B 131 ? 0.37906 0.48503 0.45591 -0.02491 -0.00388 0.00016  131 MET   B CE  
3765 N  N   . GLU   B 132 ? 0.34389 0.42116 0.40107 -0.04425 -0.02244 0.01845  132 GLU   B N   
3766 C  CA  . GLU   B 132 ? 0.35216 0.44179 0.41308 -0.04901 -0.01973 0.02365  132 GLU   B CA  
3767 C  C   . GLU   B 132 ? 0.41275 0.52053 0.47930 -0.04365 -0.00849 0.01970  132 GLU   B C   
3768 O  O   . GLU   B 132 ? 0.37932 0.48934 0.44328 -0.04254 -0.00523 0.01971  132 GLU   B O   
3769 C  CB  . GLU   B 132 ? 0.38067 0.48281 0.45045 -0.05992 -0.02434 0.03341  132 GLU   B CB  
3770 C  CG  . GLU   B 132 ? 0.41337 0.53276 0.48820 -0.06538 -0.02098 0.04019  132 GLU   B CG  
3771 C  CD  . GLU   B 132 ? 0.52698 0.66095 0.61132 -0.07679 -0.02585 0.05143  132 GLU   B CD  
3772 O  OE1 . GLU   B 132 ? 0.41138 0.54249 0.49926 -0.08057 -0.03186 0.05369  132 GLU   B OE1 
3773 O  OE2 . GLU   B 132 ? 0.44007 0.58945 0.52857 -0.08223 -0.02383 0.05863  132 GLU   B OE2 
3774 N  N   . ASN   B 133 ? 0.34044 0.45912 0.41350 -0.03959 -0.00322 0.01570  133 ASN   B N   
3775 C  CA  . ASN   B 133 ? 0.34005 0.47577 0.41851 -0.03479 0.00586  0.01217  133 ASN   B CA  
3776 C  C   . ASN   B 133 ? 0.36818 0.49538 0.44116 -0.02638 0.01014  0.00448  133 ASN   B C   
3777 O  O   . ASN   B 133 ? 0.39779 0.53628 0.47478 -0.02194 0.01633  0.00071  133 ASN   B O   
3778 C  CB  . ASN   B 133 ? 0.33402 0.48635 0.42229 -0.03390 0.00885  0.01154  133 ASN   B CB  
3779 C  CG  . ASN   B 133 ? 0.37099 0.54121 0.46781 -0.04169 0.00712  0.02005  133 ASN   B CG  
3780 O  OD1 . ASN   B 133 ? 0.42187 0.58897 0.51731 -0.04945 0.00180  0.02737  133 ASN   B OD1 
3781 N  ND2 . ASN   B 133 ? 0.34915 0.53936 0.45498 -0.03943 0.01146  0.01954  133 ASN   B ND2 
3782 N  N   . VAL   B 134 ? 0.32820 0.43644 0.39198 -0.02383 0.00660  0.00234  134 VAL   B N   
3783 C  CA  . VAL   B 134 ? 0.30769 0.40943 0.36655 -0.01639 0.01040  -0.00344 134 VAL   B CA  
3784 C  C   . VAL   B 134 ? 0.44205 0.53499 0.49347 -0.01662 0.00843  -0.00192 134 VAL   B C   
3785 O  O   . VAL   B 134 ? 0.40484 0.48552 0.45022 -0.01970 0.00162  0.00119  134 VAL   B O   
3786 C  CB  . VAL   B 134 ? 0.37335 0.46283 0.42761 -0.01159 0.00847  -0.00720 134 VAL   B CB  
3787 C  CG1 . VAL   B 134 ? 0.39833 0.48255 0.44758 -0.00462 0.01189  -0.01135 134 VAL   B CG1 
3788 C  CG2 . VAL   B 134 ? 0.38396 0.48167 0.44556 -0.01113 0.01018  -0.00882 134 VAL   B CG2 
3789 N  N   . GLN   B 135 ? 0.33592 0.43371 0.38721 -0.01314 0.01342  -0.00423 135 GLN   B N   
3790 C  CA  . GLN   B 135 ? 0.39264 0.48263 0.43698 -0.01250 0.01181  -0.00317 135 GLN   B CA  
3791 C  C   . GLN   B 135 ? 0.35025 0.43493 0.39062 -0.00498 0.01460  -0.00786 135 GLN   B C   
3792 O  O   . GLN   B 135 ? 0.34960 0.44197 0.39482 -0.00188 0.01942  -0.01100 135 GLN   B O   
3793 C  CB  . GLN   B 135 ? 0.38276 0.48503 0.43052 -0.01551 0.01506  -0.00070 135 GLN   B CB  
3794 C  CG  . GLN   B 135 ? 0.50620 0.61736 0.55814 -0.02298 0.01310  0.00532  135 GLN   B CG  
3795 C  CD  . GLN   B 135 ? 0.59607 0.71900 0.64951 -0.02411 0.01692  0.00709  135 GLN   B CD  
3796 O  OE1 . GLN   B 135 ? 0.65852 0.79766 0.71810 -0.02333 0.02199  0.00618  135 GLN   B OE1 
3797 N  NE2 . GLN   B 135 ? 0.58573 0.69971 0.63248 -0.02426 0.01460  0.00847  135 GLN   B NE2 
3798 N  N   . PHE   B 136 ? 0.34244 0.41427 0.37393 -0.00187 0.01105  -0.00799 136 PHE   B N   
3799 C  CA  . PHE   B 136 ? 0.30313 0.37252 0.33112 0.00553  0.01384  -0.01137 136 PHE   B CA  
3800 C  C   . PHE   B 136 ? 0.36416 0.43532 0.39033 0.00560  0.01476  -0.01024 136 PHE   B C   
3801 O  O   . PHE   B 136 ? 0.39384 0.45566 0.41338 0.00433  0.00979  -0.00802 136 PHE   B O   
3802 C  CB  . PHE   B 136 ? 0.33539 0.39035 0.35375 0.01097  0.00931  -0.01281 136 PHE   B CB  
3803 C  CG  . PHE   B 136 ? 0.34033 0.39163 0.35910 0.01051  0.00712  -0.01362 136 PHE   B CG  
3804 C  CD1 . PHE   B 136 ? 0.33482 0.39413 0.35940 0.01255  0.01180  -0.01567 136 PHE   B CD1 
3805 C  CD2 . PHE   B 136 ? 0.38724 0.42606 0.40019 0.00785  -0.00050 -0.01207 136 PHE   B CD2 
3806 C  CE1 . PHE   B 136 ? 0.35344 0.40954 0.37839 0.01227  0.00972  -0.01640 136 PHE   B CE1 
3807 C  CE2 . PHE   B 136 ? 0.40665 0.44184 0.41983 0.00746  -0.00302 -0.01284 136 PHE   B CE2 
3808 C  CZ  . PHE   B 136 ? 0.41848 0.46284 0.43777 0.00976  0.00245  -0.01506 136 PHE   B CZ  
3809 N  N   . LEU   B 137 ? 0.34499 0.42727 0.37686 0.00653  0.02013  -0.01151 137 LEU   B N   
3810 C  CA  . LEU   B 137 ? 0.30276 0.38785 0.33347 0.00648  0.02113  -0.01054 137 LEU   B CA  
3811 C  C   . LEU   B 137 ? 0.40541 0.49150 0.43532 0.01282  0.02369  -0.01268 137 LEU   B C   
3812 O  O   . LEU   B 137 ? 0.34661 0.43708 0.38059 0.01525  0.02645  -0.01446 137 LEU   B O   
3813 C  CB  . LEU   B 137 ? 0.30722 0.40521 0.34484 0.00228  0.02454  -0.01000 137 LEU   B CB  
3814 C  CG  . LEU   B 137 ? 0.40406 0.50663 0.44426 -0.00392 0.02319  -0.00689 137 LEU   B CG  
3815 C  CD1 . LEU   B 137 ? 0.41260 0.52975 0.45826 -0.00540 0.02738  -0.00720 137 LEU   B CD1 
3816 C  CD2 . LEU   B 137 ? 0.46795 0.56127 0.50173 -0.00774 0.01759  -0.00233 137 LEU   B CD2 
3817 N  N   . TRP   B 138 ? 0.36605 0.44802 0.39059 0.01551  0.02221  -0.01192 138 TRP   B N   
3818 C  CA  . TRP   B 138 ? 0.37207 0.45740 0.39656 0.02150  0.02454  -0.01296 138 TRP   B CA  
3819 C  C   . TRP   B 138 ? 0.33881 0.43391 0.36880 0.01946  0.02739  -0.01267 138 TRP   B C   
3820 O  O   . TRP   B 138 ? 0.33485 0.42959 0.36321 0.01629  0.02616  -0.01138 138 TRP   B O   
3821 C  CB  . TRP   B 138 ? 0.33734 0.41254 0.35209 0.02722  0.02077  -0.01270 138 TRP   B CB  
3822 C  CG  . TRP   B 138 ? 0.43389 0.49834 0.44149 0.03102  0.01724  -0.01377 138 TRP   B CG  
3823 C  CD1 . TRP   B 138 ? 0.38573 0.43919 0.38877 0.02740  0.01206  -0.01321 138 TRP   B CD1 
3824 C  CD2 . TRP   B 138 ? 0.42257 0.48634 0.42615 0.03937  0.01801  -0.01531 138 TRP   B CD2 
3825 N  NE1 . TRP   B 138 ? 0.46568 0.50957 0.46107 0.03349  0.00895  -0.01507 138 TRP   B NE1 
3826 C  CE2 . TRP   B 138 ? 0.40392 0.45443 0.39906 0.04143  0.01291  -0.01651 138 TRP   B CE2 
3827 C  CE3 . TRP   B 138 ? 0.36299 0.43711 0.36931 0.04536  0.02230  -0.01522 138 TRP   B CE3 
3828 C  CZ2 . TRP   B 138 ? 0.46719 0.51421 0.45540 0.05030  0.01234  -0.01841 138 TRP   B CZ2 
3829 C  CZ3 . TRP   B 138 ? 0.44196 0.51475 0.44248 0.05366  0.02228  -0.01617 138 TRP   B CZ3 
3830 C  CH2 . TRP   B 138 ? 0.42381 0.48292 0.41465 0.05671  0.01749  -0.01815 138 TRP   B CH2 
3831 N  N   . ALA   B 139 ? 0.31180 0.41524 0.34800 0.02099  0.03053  -0.01352 139 ALA   B N   
3832 C  CA  . ALA   B 139 ? 0.31785 0.42907 0.35891 0.01885  0.03205  -0.01367 139 ALA   B CA  
3833 C  C   . ALA   B 139 ? 0.37573 0.48549 0.41251 0.02030  0.03067  -0.01232 139 ALA   B C   
3834 O  O   . ALA   B 139 ? 0.32917 0.44027 0.36533 0.01708  0.03020  -0.01199 139 ALA   B O   
3835 C  CB  . ALA   B 139 ? 0.29715 0.41554 0.34505 0.02010  0.03391  -0.01396 139 ALA   B CB  
3836 N  N   . SER   B 140 ? 0.40453 0.51171 0.43757 0.02574  0.02988  -0.01146 140 SER   B N   
3837 C  CA  . SER   B 140 ? 0.43792 0.54406 0.46708 0.02810  0.02832  -0.01032 140 SER   B CA  
3838 C  C   . SER   B 140 ? 0.43936 0.53675 0.46180 0.02502  0.02499  -0.00954 140 SER   B C   
3839 O  O   . SER   B 140 ? 0.40813 0.50741 0.43012 0.02281  0.02441  -0.00858 140 SER   B O   
3840 C  CB  . SER   B 140 ? 0.44162 0.54661 0.46680 0.03603  0.02782  -0.00981 140 SER   B CB  
3841 O  OG  . SER   B 140 ? 0.48680 0.58140 0.50468 0.03875  0.02549  -0.01080 140 SER   B OG  
3842 N  N   . GLU   B 141 ? 0.42543 0.51306 0.44251 0.02442  0.02218  -0.00941 141 GLU   B N   
3843 C  CA  . GLU   B 141 ? 0.40117 0.48023 0.41239 0.02015  0.01790  -0.00729 141 GLU   B CA  
3844 C  C   . GLU   B 141 ? 0.37928 0.46667 0.39560 0.01298  0.01996  -0.00592 141 GLU   B C   
3845 O  O   . GLU   B 141 ? 0.40514 0.49194 0.41865 0.00986  0.01818  -0.00347 141 GLU   B O   
3846 C  CB  . GLU   B 141 ? 0.41469 0.48259 0.42095 0.01917  0.01384  -0.00694 141 GLU   B CB  
3847 C  CG  . GLU   B 141 ? 0.56611 0.62355 0.56442 0.02718  0.01057  -0.00868 141 GLU   B CG  
3848 C  CD  . GLU   B 141 ? 0.69263 0.73666 0.68460 0.02614  0.00497  -0.00854 141 GLU   B CD  
3849 O  OE1 . GLU   B 141 ? 0.74922 0.78291 0.73253 0.03394  0.00136  -0.01061 141 GLU   B OE1 
3850 O  OE2 . GLU   B 141 ? 0.61669 0.66130 0.61217 0.01817  0.00402  -0.00637 141 GLU   B OE2 
3851 N  N   . GLU   B 142 ? 0.38316 0.47858 0.40636 0.01076  0.02348  -0.00740 142 GLU   B N   
3852 C  CA  . GLU   B 142 ? 0.35314 0.45710 0.37998 0.00532  0.02525  -0.00641 142 GLU   B CA  
3853 C  C   . GLU   B 142 ? 0.40529 0.51712 0.43407 0.00603  0.02739  -0.00737 142 GLU   B C   
3854 O  O   . GLU   B 142 ? 0.40882 0.52496 0.43624 0.00280  0.02739  -0.00552 142 GLU   B O   
3855 C  CB  . GLU   B 142 ? 0.34878 0.45874 0.38163 0.00373  0.02776  -0.00813 142 GLU   B CB  
3856 C  CG  . GLU   B 142 ? 0.35244 0.45480 0.38352 0.00203  0.02498  -0.00678 142 GLU   B CG  
3857 C  CD  . GLU   B 142 ? 0.46052 0.55858 0.48744 -0.00342 0.02089  -0.00201 142 GLU   B CD  
3858 O  OE1 . GLU   B 142 ? 0.43476 0.54210 0.46390 -0.00767 0.02225  0.00048  142 GLU   B OE1 
3859 O  OE2 . GLU   B 142 ? 0.48020 0.56537 0.50090 -0.00328 0.01570  -0.00037 142 GLU   B OE2 
3860 N  N   . ILE   B 143 ? 0.35963 0.47375 0.39142 0.01008  0.02879  -0.00974 143 ILE   B N   
3861 C  CA  . ILE   B 143 ? 0.39179 0.51188 0.42520 0.01070  0.02954  -0.01057 143 ILE   B CA  
3862 C  C   . ILE   B 143 ? 0.42202 0.53826 0.44951 0.01078  0.02719  -0.00809 143 ILE   B C   
3863 O  O   . ILE   B 143 ? 0.39568 0.51600 0.42178 0.00868  0.02720  -0.00745 143 ILE   B O   
3864 C  CB  . ILE   B 143 ? 0.39209 0.51505 0.43052 0.01414  0.03035  -0.01214 143 ILE   B CB  
3865 C  CG1 . ILE   B 143 ? 0.32416 0.45098 0.36837 0.01316  0.03194  -0.01453 143 ILE   B CG1 
3866 C  CG2 . ILE   B 143 ? 0.36888 0.49605 0.40815 0.01499  0.02946  -0.01205 143 ILE   B CG2 
3867 C  CD1 . ILE   B 143 ? 0.33804 0.46683 0.38745 0.01566  0.03214  -0.01444 143 ILE   B CD1 
3868 N  N   . ASN   B 144 ? 0.42755 0.53537 0.45045 0.01363  0.02471  -0.00672 144 ASN   B N   
3869 C  CA  . ASN   B 144 ? 0.43601 0.53851 0.45256 0.01439  0.02154  -0.00448 144 ASN   B CA  
3870 C  C   . ASN   B 144 ? 0.46781 0.56606 0.47922 0.00895  0.01893  -0.00106 144 ASN   B C   
3871 O  O   . ASN   B 144 ? 0.49521 0.59002 0.50157 0.00854  0.01618  0.00124  144 ASN   B O   
3872 C  CB  . ASN   B 144 ? 0.42142 0.51588 0.43374 0.02056  0.01910  -0.00464 144 ASN   B CB  
3873 C  CG  . ASN   B 144 ? 0.46842 0.57057 0.48571 0.02580  0.02135  -0.00601 144 ASN   B CG  
3874 O  OD1 . ASN   B 144 ? 0.55449 0.66319 0.57471 0.02521  0.02198  -0.00578 144 ASN   B OD1 
3875 N  ND2 . ASN   B 144 ? 0.48551 0.58767 0.50376 0.03069  0.02225  -0.00688 144 ASN   B ND2 
3876 N  N   . LYS   B 145 ? 0.44590 0.54493 0.45868 0.00449  0.01935  0.00007  145 LYS   B N   
3877 C  CA  . LYS   B 145 ? 0.43506 0.53516 0.44512 -0.00193 0.01758  0.00466  145 LYS   B CA  
3878 C  C   . LYS   B 145 ? 0.46404 0.57714 0.47642 -0.00402 0.02104  0.00489  145 LYS   B C   
3879 O  O   . LYS   B 145 ? 0.46304 0.57815 0.47183 -0.00823 0.01954  0.00939  145 LYS   B O   
3880 C  CB  . LYS   B 145 ? 0.47161 0.57188 0.48384 -0.00639 0.01715  0.00655  145 LYS   B CB  
3881 C  CG  . LYS   B 145 ? 0.54523 0.63066 0.55292 -0.00526 0.01204  0.00710  145 LYS   B CG  
3882 C  CD  . LYS   B 145 ? 0.60000 0.68618 0.61088 -0.00955 0.01149  0.00855  145 LYS   B CD  
3883 C  CE  . LYS   B 145 ? 0.66760 0.73713 0.67253 -0.00703 0.00567  0.00801  145 LYS   B CE  
3884 N  NZ  . LYS   B 145 ? 0.61611 0.68474 0.62393 -0.00999 0.00466  0.00848  145 LYS   B NZ  
3885 N  N   . LYS   B 146 ? 0.42031 0.54219 0.43801 -0.00129 0.02509  0.00044  146 LYS   B N   
3886 C  CA  . LYS   B 146 ? 0.43836 0.57167 0.45686 -0.00197 0.02771  -0.00039 146 LYS   B CA  
3887 C  C   . LYS   B 146 ? 0.39318 0.52848 0.41432 0.00260  0.02870  -0.00523 146 LYS   B C   
3888 O  O   . LYS   B 146 ? 0.33403 0.47547 0.35906 0.00416  0.03074  -0.00906 146 LYS   B O   
3889 C  CB  . LYS   B 146 ? 0.48701 0.63011 0.50908 -0.00413 0.03062  -0.00054 146 LYS   B CB  
3890 C  CG  . LYS   B 146 ? 0.48621 0.62922 0.50696 -0.00985 0.02908  0.00555  146 LYS   B CG  
3891 C  CD  . LYS   B 146 ? 0.56333 0.72077 0.58780 -0.01193 0.03239  0.00660  146 LYS   B CD  
3892 C  CE  . LYS   B 146 ? 0.65687 0.81372 0.68687 -0.01048 0.03359  0.00323  146 LYS   B CE  
3893 N  NZ  . LYS   B 146 ? 0.70306 0.87529 0.73688 -0.01123 0.03687  0.00376  146 LYS   B NZ  
3894 N  N   . PRO   B 147 ? 0.40150 0.53118 0.42072 0.00491  0.02651  -0.00495 147 PRO   B N   
3895 C  CA  . PRO   B 147 ? 0.43469 0.56610 0.45807 0.00855  0.02664  -0.00841 147 PRO   B CA  
3896 C  C   . PRO   B 147 ? 0.37398 0.51197 0.39696 0.00891  0.02669  -0.01067 147 PRO   B C   
3897 O  O   . PRO   B 147 ? 0.37188 0.51203 0.39925 0.01072  0.02636  -0.01400 147 PRO   B O   
3898 C  CB  . PRO   B 147 ? 0.42589 0.55090 0.44713 0.01120  0.02415  -0.00653 147 PRO   B CB  
3899 C  CG  . PRO   B 147 ? 0.47906 0.59933 0.49295 0.00882  0.02195  -0.00276 147 PRO   B CG  
3900 C  CD  . PRO   B 147 ? 0.40242 0.52357 0.41588 0.00443  0.02315  -0.00114 147 PRO   B CD  
3901 N  N   . ASN   B 148 ? 0.35948 0.50048 0.37690 0.00723  0.02653  -0.00883 148 ASN   B N   
3902 C  CA  . ASN   B 148 ? 0.38110 0.52837 0.39673 0.00865  0.02643  -0.01176 148 ASN   B CA  
3903 C  C   . ASN   B 148 ? 0.42440 0.57750 0.44245 0.00980  0.02846  -0.01572 148 ASN   B C   
3904 O  O   . ASN   B 148 ? 0.38011 0.53374 0.39997 0.01249  0.02703  -0.02029 148 ASN   B O   
3905 C  CB  . ASN   B 148 ? 0.41539 0.56594 0.42375 0.00701  0.02615  -0.00842 148 ASN   B CB  
3906 C  CG  . ASN   B 148 ? 0.44055 0.59701 0.44521 0.00967  0.02552  -0.01188 148 ASN   B CG  
3907 O  OD1 . ASN   B 148 ? 0.57060 0.72398 0.57482 0.01141  0.02264  -0.01342 148 ASN   B OD1 
3908 N  ND2 . ASN   B 148 ? 0.51408 0.67953 0.51585 0.01049  0.02794  -0.01312 148 ASN   B ND2 
3909 N  N   . GLU   B 149 ? 0.37344 0.53034 0.39173 0.00781  0.03106  -0.01389 149 GLU   B N   
3910 C  CA  . GLU   B 149 ? 0.37524 0.53792 0.39619 0.00967  0.03295  -0.01770 149 GLU   B CA  
3911 C  C   . GLU   B 149 ? 0.33908 0.49600 0.36615 0.01149  0.03169  -0.02158 149 GLU   B C   
3912 O  O   . GLU   B 149 ? 0.37423 0.53265 0.40228 0.01457  0.03067  -0.02651 149 GLU   B O   
3913 C  CB  . GLU   B 149 ? 0.40216 0.56986 0.42399 0.00650  0.03557  -0.01388 149 GLU   B CB  
3914 C  CG  . GLU   B 149 ? 0.39950 0.57363 0.42445 0.00895  0.03749  -0.01764 149 GLU   B CG  
3915 C  CD  . GLU   B 149 ? 0.59789 0.77888 0.62467 0.00537  0.03984  -0.01309 149 GLU   B CD  
3916 O  OE1 . GLU   B 149 ? 0.58882 0.77226 0.61290 0.00095  0.03984  -0.00677 149 GLU   B OE1 
3917 O  OE2 . GLU   B 149 ? 0.47254 0.65677 0.50345 0.00678  0.04113  -0.01549 149 GLU   B OE2 
3918 N  N   . TYR   B 150 ? 0.33366 0.48389 0.36427 0.00993  0.03132  -0.01925 150 TYR   B N   
3919 C  CA  . TYR   B 150 ? 0.31014 0.45674 0.34677 0.01111  0.03065  -0.02158 150 TYR   B CA  
3920 C  C   . TYR   B 150 ? 0.33476 0.47981 0.37338 0.01281  0.02751  -0.02396 150 TYR   B C   
3921 O  O   . TYR   B 150 ? 0.31103 0.45587 0.35230 0.01414  0.02576  -0.02759 150 TYR   B O   
3922 C  CB  . TYR   B 150 ? 0.30620 0.44723 0.34502 0.01020  0.03097  -0.01853 150 TYR   B CB  
3923 C  CG  . TYR   B 150 ? 0.33646 0.47569 0.38123 0.01127  0.03075  -0.02017 150 TYR   B CG  
3924 C  CD1 . TYR   B 150 ? 0.30213 0.44208 0.34924 0.01097  0.03209  -0.02176 150 TYR   B CD1 
3925 C  CD2 . TYR   B 150 ? 0.27298 0.41092 0.32144 0.01236  0.02909  -0.01943 150 TYR   B CD2 
3926 C  CE1 . TYR   B 150 ? 0.29938 0.43732 0.35168 0.01170  0.03155  -0.02277 150 TYR   B CE1 
3927 C  CE2 . TYR   B 150 ? 0.28782 0.42530 0.34194 0.01268  0.02877  -0.01970 150 TYR   B CE2 
3928 C  CZ  . TYR   B 150 ? 0.32615 0.46293 0.38172 0.01231  0.02994  -0.02143 150 TYR   B CZ  
3929 O  OH  . TYR   B 150 ? 0.34597 0.48208 0.40660 0.01241  0.02928  -0.02118 150 TYR   B OH  
3930 N  N   . TRP   B 151 ? 0.32929 0.47270 0.36674 0.01265  0.02596  -0.02163 151 TRP   B N   
3931 C  CA  . TRP   B 151 ? 0.33058 0.47319 0.37124 0.01342  0.02228  -0.02282 151 TRP   B CA  
3932 C  C   . TRP   B 151 ? 0.30363 0.44744 0.34040 0.01483  0.01953  -0.02697 151 TRP   B C   
3933 O  O   . TRP   B 151 ? 0.35321 0.49474 0.39301 0.01527  0.01533  -0.02937 151 TRP   B O   
3934 C  CB  . TRP   B 151 ? 0.29952 0.44141 0.34046 0.01343  0.02139  -0.01897 151 TRP   B CB  
3935 C  CG  . TRP   B 151 ? 0.30592 0.44641 0.35018 0.01386  0.02330  -0.01604 151 TRP   B CG  
3936 C  CD1 . TRP   B 151 ? 0.29739 0.43495 0.33773 0.01448  0.02493  -0.01356 151 TRP   B CD1 
3937 C  CD2 . TRP   B 151 ? 0.30538 0.44694 0.35669 0.01414  0.02321  -0.01521 151 TRP   B CD2 
3938 N  NE1 . TRP   B 151 ? 0.31355 0.44999 0.35711 0.01610  0.02596  -0.01211 151 TRP   B NE1 
3939 C  CE2 . TRP   B 151 ? 0.26732 0.40739 0.31793 0.01585  0.02543  -0.01271 151 TRP   B CE2 
3940 C  CE3 . TRP   B 151 ? 0.33672 0.48004 0.39440 0.01305  0.02075  -0.01589 151 TRP   B CE3 
3941 C  CZ2 . TRP   B 151 ? 0.31651 0.45847 0.37222 0.01708  0.02629  -0.01101 151 TRP   B CZ2 
3942 C  CZ3 . TRP   B 151 ? 0.31693 0.46230 0.38076 0.01310  0.02142  -0.01327 151 TRP   B CZ3 
3943 C  CH2 . TRP   B 151 ? 0.34564 0.49126 0.40841 0.01542  0.02466  -0.01087 151 TRP   B CH2 
3944 N  N   . SER   B 152 ? 0.30138 0.44883 0.33117 0.01581  0.02131  -0.02799 152 SER   B N   
3945 C  CA  . SER   B 152 ? 0.38259 0.53161 0.40739 0.01885  0.01873  -0.03284 152 SER   B CA  
3946 C  C   . SER   B 152 ? 0.41001 0.55793 0.43677 0.02112  0.01759  -0.03755 152 SER   B C   
3947 O  O   . SER   B 152 ? 0.38728 0.53152 0.41221 0.02374  0.01249  -0.04215 152 SER   B O   
3948 C  CB  . SER   B 152 ? 0.38391 0.53970 0.40068 0.02000  0.02156  -0.03225 152 SER   B CB  
3949 O  OG  . SER   B 152 ? 0.42234 0.57746 0.43659 0.01798  0.02131  -0.02803 152 SER   B OG  
3950 N  N   . LEU   B 153 ? 0.36385 0.51393 0.39368 0.02036  0.02139  -0.03667 153 LEU   B N   
3951 C  CA  . LEU   B 153 ? 0.32763 0.47564 0.36020 0.02243  0.01990  -0.04079 153 LEU   B CA  
3952 C  C   . LEU   B 153 ? 0.31736 0.45755 0.35588 0.02086  0.01488  -0.04096 153 LEU   B C   
3953 O  O   . LEU   B 153 ? 0.34893 0.48438 0.38710 0.02303  0.00984  -0.04533 153 LEU   B O   
3954 C  CB  . LEU   B 153 ? 0.34621 0.49724 0.38244 0.02103  0.02451  -0.03881 153 LEU   B CB  
3955 C  CG  . LEU   B 153 ? 0.55163 0.71001 0.58536 0.02393  0.02732  -0.04121 153 LEU   B CG  
3956 C  CD1 . LEU   B 153 ? 0.38891 0.54754 0.42826 0.02104  0.03042  -0.03823 153 LEU   B CD1 
3957 C  CD2 . LEU   B 153 ? 0.44607 0.60167 0.47736 0.02934  0.02285  -0.04817 153 LEU   B CD2 
3958 N  N   . VAL   B 154 ? 0.30139 0.44052 0.34547 0.01728  0.01601  -0.03589 154 VAL   B N   
3959 C  CA  . VAL   B 154 ? 0.36181 0.49666 0.41282 0.01513  0.01185  -0.03422 154 VAL   B CA  
3960 C  C   . VAL   B 154 ? 0.38300 0.51411 0.43261 0.01542  0.00486  -0.03634 154 VAL   B C   
3961 O  O   . VAL   B 154 ? 0.35087 0.47646 0.40300 0.01497  -0.00109 -0.03823 154 VAL   B O   
3962 C  CB  . VAL   B 154 ? 0.27825 0.41536 0.33410 0.01269  0.01457  -0.02818 154 VAL   B CB  
3963 C  CG1 . VAL   B 154 ? 0.33081 0.46698 0.39441 0.01031  0.01039  -0.02517 154 VAL   B CG1 
3964 C  CG2 . VAL   B 154 ? 0.29564 0.43373 0.35292 0.01252  0.01968  -0.02642 154 VAL   B CG2 
3965 N  N   . LEU   B 155 ? 0.37488 0.50799 0.41991 0.01602  0.00467  -0.03593 155 LEU   B N   
3966 C  CA  . LEU   B 155 ? 0.34080 0.46989 0.38368 0.01634  -0.00258 -0.03795 155 LEU   B CA  
3967 C  C   . LEU   B 155 ? 0.33103 0.45491 0.36704 0.02061  -0.00723 -0.04527 155 LEU   B C   
3968 O  O   . LEU   B 155 ? 0.33866 0.45482 0.37529 0.02033  -0.01564 -0.04754 155 LEU   B O   
3969 C  CB  . LEU   B 155 ? 0.37875 0.51140 0.41692 0.01673  -0.00120 -0.03624 155 LEU   B CB  
3970 C  CG  . LEU   B 155 ? 0.46965 0.60565 0.51431 0.01357  0.00028  -0.02964 155 LEU   B CG  
3971 C  CD1 . LEU   B 155 ? 0.38558 0.52295 0.42594 0.01403  -0.00125 -0.02857 155 LEU   B CD1 
3972 C  CD2 . LEU   B 155 ? 0.49197 0.62695 0.54607 0.01044  -0.00410 -0.02661 155 LEU   B CD2 
3973 N  N   . ASP   B 156 ? 0.35681 0.48481 0.38631 0.02484  -0.00250 -0.04885 156 ASP   B N   
3974 C  CA  . ASP   B 156 ? 0.37749 0.50186 0.39951 0.03077  -0.00670 -0.05631 156 ASP   B CA  
3975 C  C   . ASP   B 156 ? 0.35269 0.46935 0.37885 0.03090  -0.01147 -0.05880 156 ASP   B C   
3976 O  O   . ASP   B 156 ? 0.40391 0.51165 0.42525 0.03452  -0.01979 -0.06449 156 ASP   B O   
3977 C  CB  . ASP   B 156 ? 0.42521 0.55931 0.44012 0.03559  0.00008  -0.05855 156 ASP   B CB  
3978 C  CG  . ASP   B 156 ? 0.67654 0.81610 0.68344 0.03730  0.00143  -0.05810 156 ASP   B CG  
3979 O  OD1 . ASP   B 156 ? 0.65079 0.80089 0.65374 0.03878  0.00802  -0.05657 156 ASP   B OD1 
3980 O  OD2 . ASP   B 156 ? 0.62026 0.75380 0.62536 0.03648  -0.00450 -0.05845 156 ASP   B OD2 
3981 N  N   . ILE   B 157 ? 0.35981 0.47884 0.39382 0.02750  -0.00689 -0.05491 157 ILE   B N   
3982 C  CA  . ILE   B 157 ? 0.39698 0.50857 0.43580 0.02654  -0.01160 -0.05591 157 ILE   B CA  
3983 C  C   . ILE   B 157 ? 0.37321 0.47633 0.41649 0.02220  -0.02058 -0.05357 157 ILE   B C   
3984 O  O   . ILE   B 157 ? 0.39180 0.48469 0.43367 0.02330  -0.02931 -0.05718 157 ILE   B O   
3985 C  CB  . ILE   B 157 ? 0.34882 0.46507 0.39504 0.02335  -0.00492 -0.05135 157 ILE   B CB  
3986 C  CG1 . ILE   B 157 ? 0.35946 0.48312 0.40134 0.02752  0.00190  -0.05404 157 ILE   B CG1 
3987 C  CG2 . ILE   B 157 ? 0.29535 0.40417 0.34790 0.02083  -0.00996 -0.05040 157 ILE   B CG2 
3988 C  CD1 . ILE   B 157 ? 0.32350 0.45201 0.37153 0.02398  0.00870  -0.04894 157 ILE   B CD1 
3989 N  N   . SER   B 158 ? 0.34944 0.45676 0.39826 0.01718  -0.01928 -0.04712 158 SER   B N   
3990 C  CA  . SER   B 158 ? 0.37959 0.48144 0.43436 0.01216  -0.02796 -0.04339 158 SER   B CA  
3991 C  C   . SER   B 158 ? 0.40029 0.49226 0.44751 0.01475  -0.03822 -0.04903 158 SER   B C   
3992 O  O   . SER   B 158 ? 0.41616 0.49878 0.46646 0.01143  -0.04861 -0.04817 158 SER   B O   
3993 C  CB  . SER   B 158 ? 0.36733 0.47781 0.42869 0.00776  -0.02446 -0.03577 158 SER   B CB  
3994 O  OG  . SER   B 158 ? 0.38085 0.49227 0.43567 0.00992  -0.02529 -0.03784 158 SER   B OG  
3995 N  N   . ARG   B 159 ? 0.38495 0.47849 0.42187 0.02053  -0.03624 -0.05443 159 ARG   B N   
3996 C  CA  . ARG   B 159 ? 0.36138 0.44491 0.38881 0.02470  -0.04614 -0.06097 159 ARG   B CA  
3997 C  C   . ARG   B 159 ? 0.47785 0.55046 0.49908 0.03012  -0.05285 -0.06847 159 ARG   B C   
3998 O  O   . ARG   B 159 ? 0.41199 0.47212 0.42634 0.03284  -0.06424 -0.07359 159 ARG   B O   
3999 C  CB  . ARG   B 159 ? 0.49826 0.58793 0.51511 0.03059  -0.04144 -0.06487 159 ARG   B CB  
4000 C  CG  . ARG   B 159 ? 0.37950 0.47737 0.40024 0.02622  -0.03688 -0.05848 159 ARG   B CG  
4001 C  CD  . ARG   B 159 ? 0.48002 0.58560 0.49061 0.03155  -0.03050 -0.06118 159 ARG   B CD  
4002 N  NE  . ARG   B 159 ? 0.50791 0.60706 0.50654 0.03763  -0.03783 -0.06819 159 ARG   B NE  
4003 C  CZ  . ARG   B 159 ? 0.60058 0.70444 0.58748 0.04542  -0.03456 -0.07369 159 ARG   B CZ  
4004 N  NH1 . ARG   B 159 ? 0.57085 0.68589 0.55726 0.04752  -0.02459 -0.07286 159 ARG   B NH1 
4005 N  NH2 . ARG   B 159 ? 0.54477 0.64276 0.52003 0.05132  -0.04173 -0.07977 159 ARG   B NH2 
4006 N  N   . SER   B 160 ? 0.42143 0.49784 0.44406 0.03240  -0.04660 -0.06964 160 SER   B N   
4007 C  CA  . SER   B 160 ? 0.48313 0.55045 0.49875 0.03933  -0.05215 -0.07754 160 SER   B CA  
4008 C  C   . SER   B 160 ? 0.47608 0.53057 0.49777 0.03508  -0.06152 -0.07611 160 SER   B C   
4009 O  O   . SER   B 160 ? 0.50097 0.54403 0.51551 0.04106  -0.06937 -0.08321 160 SER   B O   
4010 C  CB  . SER   B 160 ? 0.44998 0.52875 0.46404 0.04438  -0.04113 -0.07954 160 SER   B CB  
4011 O  OG  . SER   B 160 ? 0.51817 0.60765 0.52494 0.04883  -0.03457 -0.08121 160 SER   B OG  
4012 N  N   . PHE   B 161 ? 0.44856 0.50484 0.48264 0.02550  -0.06124 -0.06707 161 PHE   B N   
4013 C  CA  . PHE   B 161 ? 0.49576 0.54227 0.53643 0.02073  -0.06889 -0.06418 161 PHE   B CA  
4014 C  C   . PHE   B 161 ? 0.46683 0.50973 0.51631 0.01109  -0.07710 -0.05600 161 PHE   B C   
4015 O  O   . PHE   B 161 ? 0.43700 0.49078 0.49216 0.00681  -0.07172 -0.04990 161 PHE   B O   
4016 C  CB  . PHE   B 161 ? 0.44124 0.49678 0.49012 0.01808  -0.05927 -0.05941 161 PHE   B CB  
4017 C  CG  . PHE   B 161 ? 0.43239 0.49215 0.47471 0.02634  -0.05199 -0.06616 161 PHE   B CG  
4018 C  CD1 . PHE   B 161 ? 0.46968 0.51860 0.50535 0.03268  -0.05882 -0.07358 161 PHE   B CD1 
4019 C  CD2 . PHE   B 161 ? 0.42251 0.49703 0.46548 0.02768  -0.03913 -0.06466 161 PHE   B CD2 
4020 C  CE1 . PHE   B 161 ? 0.46466 0.52002 0.49517 0.04067  -0.05186 -0.07929 161 PHE   B CE1 
4021 C  CE2 . PHE   B 161 ? 0.42839 0.50882 0.46649 0.03450  -0.03260 -0.06972 161 PHE   B CE2 
4022 C  CZ  . PHE   B 161 ? 0.45132 0.52329 0.48370 0.04105  -0.03861 -0.07687 161 PHE   B CZ  
4023 N  N   . ASN   B 162 ? 0.49725 0.52571 0.54853 0.00742  -0.09017 -0.05511 162 ASN   B N   
4024 C  CA  . ASN   B 162 ? 0.51531 0.54198 0.57633 -0.00287 -0.09873 -0.04583 162 ASN   B CA  
4025 C  C   . ASN   B 162 ? 0.50100 0.53904 0.57633 -0.01117 -0.09275 -0.03464 162 ASN   B C   
4026 O  O   . ASN   B 162 ? 0.45404 0.49734 0.53064 -0.00892 -0.08410 -0.03501 162 ASN   B O   
4027 C  CB  . ASN   B 162 ? 0.51989 0.52511 0.57624 -0.00430 -0.11756 -0.04874 162 ASN   B CB  
4028 C  CG  . ASN   B 162 ? 0.63309 0.62602 0.68955 -0.00463 -0.12433 -0.04976 162 ASN   B CG  
4029 O  OD1 . ASN   B 162 ? 0.56052 0.56169 0.62604 -0.00885 -0.11756 -0.04339 162 ASN   B OD1 
4030 N  ND2 . ASN   B 162 ? 0.68435 0.65592 0.72984 0.00019  -0.13908 -0.05797 162 ASN   B ND2 
4031 N  N   . ILE   B 163 ? 0.47684 0.52078 0.56297 -0.02040 -0.09670 -0.02429 163 ILE   B N   
4032 C  CA  . ILE   B 163 ? 0.40720 0.46622 0.50684 -0.02744 -0.08977 -0.01274 163 ILE   B CA  
4033 C  C   . ILE   B 163 ? 0.48952 0.54186 0.59239 -0.03020 -0.09342 -0.01040 163 ILE   B C   
4034 O  O   . ILE   B 163 ? 0.44758 0.51066 0.55537 -0.03038 -0.08341 -0.00651 163 ILE   B O   
4035 C  CB  . ILE   B 163 ? 0.42401 0.49122 0.53484 -0.03665 -0.09532 -0.00163 163 ILE   B CB  
4036 C  CG1 . ILE   B 163 ? 0.41305 0.49179 0.52231 -0.03340 -0.08756 -0.00257 163 ILE   B CG1 
4037 C  CG2 . ILE   B 163 ? 0.46971 0.55166 0.59417 -0.04373 -0.09066 0.01080  163 ILE   B CG2 
4038 C  CD1 . ILE   B 163 ? 0.42195 0.50473 0.53907 -0.04082 -0.09647 0.00535  163 ILE   B CD1 
4039 N  N   . ASN   B 164 ? 0.48265 0.51615 0.58215 -0.03216 -0.10849 -0.01278 164 ASN   B N   
4040 C  CA  . ASN   B 164 ? 0.52267 0.54883 0.62514 -0.03511 -0.11285 -0.01007 164 ASN   B CA  
4041 C  C   . ASN   B 164 ? 0.54408 0.57062 0.63945 -0.02603 -0.10266 -0.01844 164 ASN   B C   
4042 O  O   . ASN   B 164 ? 0.52612 0.55820 0.62702 -0.02817 -0.09738 -0.01374 164 ASN   B O   
4043 C  CB  . ASN   B 164 ? 0.57441 0.57713 0.67256 -0.03793 -0.13245 -0.01225 164 ASN   B CB  
4044 C  CG  . ASN   B 164 ? 0.71788 0.72111 0.82691 -0.05035 -0.14400 -0.00005 164 ASN   B CG  
4045 O  OD1 . ASN   B 164 ? 0.79402 0.81594 0.91644 -0.05824 -0.13780 0.01250  164 ASN   B OD1 
4046 N  ND2 . ASN   B 164 ? 0.74778 0.73087 0.85100 -0.05193 -0.16146 -0.00338 164 ASN   B ND2 
4047 N  N   . ARG   B 165 ? 0.50165 0.52364 0.58490 -0.01583 -0.09971 -0.03039 165 ARG   B N   
4048 C  CA  . ARG   B 165 ? 0.51378 0.53822 0.59105 -0.00738 -0.09010 -0.03774 165 ARG   B CA  
4049 C  C   . ARG   B 165 ? 0.55826 0.60203 0.64296 -0.00910 -0.07460 -0.03165 165 ARG   B C   
4050 O  O   . ARG   B 165 ? 0.50765 0.55455 0.59376 -0.00760 -0.06848 -0.03152 165 ARG   B O   
4051 C  CB  . ARG   B 165 ? 0.47568 0.49702 0.53975 0.00354  -0.08816 -0.04984 165 ARG   B CB  
4052 C  CG  . ARG   B 165 ? 0.51655 0.54492 0.57592 0.01187  -0.07680 -0.05613 165 ARG   B CG  
4053 C  CD  . ARG   B 165 ? 0.59500 0.61201 0.65257 0.01443  -0.08265 -0.05943 165 ARG   B CD  
4054 N  NE  . ARG   B 165 ? 0.55442 0.58112 0.60997 0.02090  -0.07117 -0.06347 165 ARG   B NE  
4055 C  CZ  . ARG   B 165 ? 0.70414 0.74112 0.76773 0.01683  -0.06207 -0.05724 165 ARG   B CZ  
4056 N  NH1 . ARG   B 165 ? 0.65972 0.69986 0.73331 0.00738  -0.06229 -0.04699 165 ARG   B NH1 
4057 N  NH2 . ARG   B 165 ? 0.66966 0.71453 0.73114 0.02255  -0.05292 -0.06107 165 ARG   B NH2 
4058 N  N   . MET   B 166 ? 0.45391 0.50999 0.54308 -0.01209 -0.06900 -0.02649 166 MET   B N   
4059 C  CA  . MET   B 166 ? 0.44182 0.51468 0.53603 -0.01232 -0.05520 -0.02172 166 MET   B CA  
4060 C  C   . MET   B 166 ? 0.42350 0.50329 0.52863 -0.01950 -0.05442 -0.01097 166 MET   B C   
4061 O  O   . MET   B 166 ? 0.46847 0.55723 0.57565 -0.01813 -0.04472 -0.00888 166 MET   B O   
4062 C  CB  . MET   B 166 ? 0.46094 0.54344 0.55512 -0.01208 -0.05054 -0.02034 166 MET   B CB  
4063 C  CG  . MET   B 166 ? 0.46073 0.55684 0.55529 -0.00910 -0.03661 -0.01923 166 MET   B CG  
4064 S  SD  . MET   B 166 ? 0.49521 0.58905 0.57902 -0.00020 -0.02939 -0.02976 166 MET   B SD  
4065 C  CE  . MET   B 166 ? 0.38823 0.47211 0.46143 0.00505  -0.03687 -0.03908 166 MET   B CE  
4066 N  N   . LYS   B 167 ? 0.40826 0.48463 0.52036 -0.02734 -0.06490 -0.00350 167 LYS   B N   
4067 C  CA  . LYS   B 167 ? 0.43438 0.51865 0.55701 -0.03454 -0.06494 0.00780  167 LYS   B CA  
4068 C  C   . LYS   B 167 ? 0.45975 0.53636 0.58022 -0.03295 -0.06512 0.00547  167 LYS   B C   
4069 O  O   . LYS   B 167 ? 0.48888 0.57475 0.61545 -0.03577 -0.06003 0.01274  167 LYS   B O   
4070 C  CB  . LYS   B 167 ? 0.43162 0.51243 0.56199 -0.04401 -0.07807 0.01651  167 LYS   B CB  
4071 C  CG  . LYS   B 167 ? 0.42251 0.51371 0.55708 -0.04645 -0.07776 0.02068  167 LYS   B CG  
4072 C  CD  . LYS   B 167 ? 0.55189 0.64246 0.69620 -0.05715 -0.09083 0.03135  167 LYS   B CD  
4073 C  CE  . LYS   B 167 ? 0.73455 0.84416 0.89167 -0.06371 -0.08595 0.04547  167 LYS   B CE  
4074 N  NZ  . LYS   B 167 ? 0.78715 0.89575 0.95472 -0.07553 -0.09935 0.05760  167 LYS   B NZ  
4075 N  N   . ARG   B 168 ? 0.45415 0.51407 0.56562 -0.02797 -0.07151 -0.00457 168 ARG   B N   
4076 C  CA  . ARG   B 168 ? 0.45850 0.51133 0.56743 -0.02537 -0.07150 -0.00762 168 ARG   B CA  
4077 C  C   . ARG   B 168 ? 0.53996 0.60415 0.64718 -0.01970 -0.05692 -0.01028 168 ARG   B C   
4078 O  O   . ARG   B 168 ? 0.49607 0.55670 0.60220 -0.01783 -0.05575 -0.01185 168 ARG   B O   
4079 C  CB  . ARG   B 168 ? 0.46279 0.49627 0.56151 -0.01939 -0.08135 -0.01869 168 ARG   B CB  
4080 C  CG  . ARG   B 168 ? 0.55901 0.57633 0.65784 -0.02479 -0.09854 -0.01673 168 ARG   B CG  
4081 C  CD  . ARG   B 168 ? 0.70520 0.70143 0.79382 -0.01844 -0.10946 -0.02681 168 ARG   B CD  
4082 N  NE  . ARG   B 168 ? 0.72856 0.71687 0.80572 -0.00970 -0.11271 -0.03826 168 ARG   B NE  
4083 C  CZ  . ARG   B 168 ? 0.78078 0.75934 0.85479 -0.01148 -0.12376 -0.03930 168 ARG   B CZ  
4084 N  NH1 . ARG   B 168 ? 0.75372 0.73040 0.83657 -0.02276 -0.13275 -0.02872 168 ARG   B NH1 
4085 N  NH2 . ARG   B 168 ? 0.73422 0.70623 0.79600 -0.00166 -0.12564 -0.05077 168 ARG   B NH2 
4086 N  N   . CYS   B 169 ? 0.45292 0.52962 0.55964 -0.01706 -0.04670 -0.01068 169 CYS   B N   
4087 C  CA  . CYS   B 169 ? 0.40570 0.49196 0.51088 -0.01266 -0.03435 -0.01219 169 CYS   B CA  
4088 C  C   . CYS   B 169 ? 0.41710 0.51659 0.52982 -0.01669 -0.02807 -0.00221 169 CYS   B C   
4089 O  O   . CYS   B 169 ? 0.38785 0.49524 0.49897 -0.01315 -0.01836 -0.00276 169 CYS   B O   
4090 C  CB  . CYS   B 169 ? 0.42367 0.51503 0.52298 -0.00721 -0.02728 -0.01814 169 CYS   B CB  
4091 S  SG  . CYS   B 169 ? 0.45459 0.53530 0.54328 0.00018  -0.03118 -0.03049 169 CYS   B SG  
4092 N  N   . LEU   B 170 ? 0.36665 0.46916 0.48724 -0.02378 -0.03382 0.00718  170 LEU   B N   
4093 C  CA  . LEU   B 170 ? 0.34802 0.46661 0.47547 -0.02646 -0.02728 0.01707  170 LEU   B CA  
4094 C  C   . LEU   B 170 ? 0.40909 0.53069 0.53521 -0.02372 -0.02045 0.01753  170 LEU   B C   
4095 O  O   . LEU   B 170 ? 0.34892 0.48302 0.47581 -0.02139 -0.01171 0.02119  170 LEU   B O   
4096 C  CB  . LEU   B 170 ? 0.41612 0.53865 0.55313 -0.03526 -0.03556 0.02819  170 LEU   B CB  
4097 C  CG  . LEU   B 170 ? 0.56379 0.70678 0.70881 -0.03777 -0.02912 0.03981  170 LEU   B CG  
4098 C  CD1 . LEU   B 170 ? 0.52471 0.67909 0.66832 -0.03306 -0.02114 0.03841  170 LEU   B CD1 
4099 C  CD2 . LEU   B 170 ? 0.60777 0.75592 0.76345 -0.04769 -0.03839 0.05211  170 LEU   B CD2 
4100 N  N   . LYS   B 171 ? 0.38549 0.49507 0.50845 -0.02288 -0.02446 0.01298  171 LYS   B N   
4101 C  CA  . LYS   B 171 ? 0.38101 0.49366 0.50302 -0.02071 -0.01853 0.01407  171 LYS   B CA  
4102 C  C   . LYS   B 171 ? 0.37157 0.49041 0.48816 -0.01404 -0.00776 0.00912  171 LYS   B C   
4103 O  O   . LYS   B 171 ? 0.34192 0.46712 0.45805 -0.01220 -0.00165 0.01194  171 LYS   B O   
4104 C  CB  . LYS   B 171 ? 0.39067 0.48914 0.50963 -0.01997 -0.02453 0.00902  171 LYS   B CB  
4105 C  CG  . LYS   B 171 ? 0.52962 0.63232 0.64888 -0.01908 -0.01937 0.01226  171 LYS   B CG  
4106 C  CD  . LYS   B 171 ? 0.64256 0.73364 0.76116 -0.02017 -0.02606 0.01118  171 LYS   B CD  
4107 C  CE  . LYS   B 171 ? 0.70169 0.80116 0.82269 -0.02154 -0.02130 0.01873  171 LYS   B CE  
4108 N  NZ  . LYS   B 171 ? 0.87958 0.97026 0.99913 -0.02145 -0.02493 0.01797  171 LYS   B NZ  
4109 N  N   . ILE   B 172 ? 0.35270 0.46930 0.46457 -0.01040 -0.00589 0.00202  172 ILE   B N   
4110 C  CA  . ILE   B 172 ? 0.30803 0.42907 0.41475 -0.00508 0.00294  -0.00192 172 ILE   B CA  
4111 C  C   . ILE   B 172 ? 0.32625 0.45945 0.43453 -0.00439 0.00920  0.00425  172 ILE   B C   
4112 O  O   . ILE   B 172 ? 0.33910 0.47450 0.44274 -0.00013 0.01550  0.00206  172 ILE   B O   
4113 C  CB  . ILE   B 172 ? 0.30861 0.42590 0.40988 -0.00170 0.00365  -0.00984 172 ILE   B CB  
4114 C  CG1 . ILE   B 172 ? 0.24387 0.36652 0.34636 -0.00290 0.00352  -0.00751 172 ILE   B CG1 
4115 C  CG2 . ILE   B 172 ? 0.34336 0.44983 0.44223 -0.00084 -0.00315 -0.01632 172 ILE   B CG2 
4116 C  CD1 . ILE   B 172 ? 0.25762 0.37723 0.35406 0.00040  0.00416  -0.01480 172 ILE   B CD1 
4117 N  N   . MET   B 173 ? 0.28161 0.42290 0.39601 -0.00808 0.00708  0.01183  173 MET   B N   
4118 C  CA  . MET   B 173 ? 0.27864 0.43367 0.39503 -0.00649 0.01261  0.01843  173 MET   B CA  
4119 C  C   . MET   B 173 ? 0.33474 0.49750 0.45521 -0.00807 0.01351  0.02643  173 MET   B C   
4120 O  O   . MET   B 173 ? 0.35296 0.52960 0.47560 -0.00631 0.01772  0.03306  173 MET   B O   
4121 C  CB  . MET   B 173 ? 0.27247 0.43487 0.39405 -0.00936 0.00992  0.02287  173 MET   B CB  
4122 C  CG  . MET   B 173 ? 0.27008 0.42406 0.38709 -0.00806 0.00822  0.01508  173 MET   B CG  
4123 S  SD  . MET   B 173 ? 0.34923 0.51021 0.47240 -0.01200 0.00348  0.02013  173 MET   B SD  
4124 C  CE  . MET   B 173 ? 0.38031 0.55971 0.50545 -0.00787 0.01135  0.02690  173 MET   B CE  
4125 N  N   . GLY   B 174 ? 0.35089 0.50586 0.47226 -0.01092 0.00946  0.02629  174 GLY   B N   
4126 C  CA  . GLY   B 174 ? 0.39342 0.55553 0.51846 -0.01298 0.00980  0.03450  174 GLY   B CA  
4127 C  C   . GLY   B 174 ? 0.49439 0.66837 0.62894 -0.01938 0.00590  0.04594  174 GLY   B C   
4128 O  O   . GLY   B 174 ? 0.51359 0.70223 0.65120 -0.01906 0.00967  0.05464  174 GLY   B O   
4129 N  N   . ARG   B 175 ? 0.44074 0.60926 0.57990 -0.02510 -0.00198 0.04645  175 ARG   B N   
4130 C  CA  . ARG   B 175 ? 0.58182 0.76166 0.73090 -0.03218 -0.00686 0.05763  175 ARG   B CA  
4131 C  C   . ARG   B 175 ? 0.69752 0.86500 0.85117 -0.04075 -0.01909 0.06023  175 ARG   B C   
4132 O  O   . ARG   B 175 ? 0.62700 0.77592 0.77515 -0.03983 -0.02428 0.05091  175 ARG   B O   
4133 C  CB  . ARG   B 175 ? 0.58893 0.77496 0.73917 -0.03082 -0.00560 0.05653  175 ARG   B CB  
4134 C  CG  . ARG   B 175 ? 0.54182 0.74052 0.68788 -0.02256 0.00519  0.05572  175 ARG   B CG  
4135 C  CD  . ARG   B 175 ? 0.62837 0.83372 0.77476 -0.02008 0.00717  0.05468  175 ARG   B CD  
4136 N  NE  . ARG   B 175 ? 0.68726 0.90346 0.82866 -0.01148 0.01666  0.05438  175 ARG   B NE  
4137 C  CZ  . ARG   B 175 ? 0.74837 0.98450 0.89413 -0.00922 0.02088  0.06337  175 ARG   B CZ  
4138 N  NH1 . ARG   B 175 ? 0.74997 1.00049 0.90696 -0.01581 0.01700  0.07462  175 ARG   B NH1 
4139 N  NH2 . ARG   B 175 ? 0.75254 0.99466 0.89101 0.00011  0.02870  0.06130  175 ARG   B NH2 
4140 N  N   . SER   B 176 ? 0.77405 0.95249 0.93756 -0.04877 -0.02395 0.07346  176 SER   B N   
4141 C  CA  . SER   B 176 ? 0.84668 1.01446 1.01585 -0.05857 -0.03742 0.07874  176 SER   B CA  
4142 C  C   . SER   B 176 ? 0.94225 1.11194 1.11759 -0.06422 -0.04472 0.08243  176 SER   B C   
4143 O  O   . SER   B 176 ? 0.90182 1.08847 1.08092 -0.06257 -0.03878 0.08628  176 SER   B O   
4144 C  CB  . SER   B 176 ? 0.95356 1.13230 1.13037 -0.06543 -0.03947 0.09272  176 SER   B CB  
4145 O  OG  . SER   B 176 ? 0.93418 1.11077 1.10496 -0.06031 -0.03334 0.08959  176 SER   B OG  
4146 N  N   . GLU   B 177 ? 1.20757 1.35919 1.38355 -0.07060 -0.05846 0.08124  177 GLU   B N   
4147 C  CA  . GLU   B 177 ? 1.22204 1.37193 1.40196 -0.07517 -0.06644 0.08264  177 GLU   B CA  
4148 C  C   . GLU   B 177 ? 1.21136 1.38095 1.40529 -0.08519 -0.07022 0.09992  177 GLU   B C   
4149 O  O   . GLU   B 177 ? 1.24236 1.41722 1.44106 -0.08826 -0.07396 0.10270  177 GLU   B O   
4150 C  CB  . GLU   B 177 ? 1.26651 1.38929 1.44110 -0.07781 -0.08117 0.07509  177 GLU   B CB  
4151 C  CG  . GLU   B 177 ? 1.28615 1.39875 1.45377 -0.07284 -0.08329 0.06380  177 GLU   B CG  
4152 C  CD  . GLU   B 177 ? 1.41740 1.54073 1.59320 -0.07881 -0.08751 0.07160  177 GLU   B CD  
4153 O  OE1 . GLU   B 177 ? 1.36001 1.49178 1.54717 -0.08929 -0.09500 0.08561  177 GLU   B OE1 
4154 O  OE2 . GLU   B 177 ? 1.39554 1.51930 1.56657 -0.07324 -0.08365 0.06409  177 GLU   B OE2 
4155 N  N   . GLY   B 178 ? 0.95317 1.13473 1.15401 -0.09046 -0.06954 0.11210  178 GLY   B N   
4156 C  CA  . GLY   B 178 ? 0.91736 1.12010 1.13257 -0.10075 -0.07351 0.13023  178 GLY   B CA  
4157 C  C   . GLY   B 178 ? 0.83639 1.06776 1.05724 -0.09658 -0.06201 0.13592  178 GLY   B C   
4158 O  O   . GLY   B 178 ? 0.85167 1.10276 1.08525 -0.10470 -0.06544 0.15078  178 GLY   B O   
4159 N  N   . GLU   B 179 ? 0.80985 1.04426 1.02173 -0.08423 -0.04912 0.12506  179 GLU   B N   
4160 C  CA  . GLU   B 179 ? 0.72610 0.98540 0.94116 -0.07824 -0.03831 0.12874  179 GLU   B CA  
4161 C  C   . GLU   B 179 ? 0.67399 0.92818 0.88849 -0.07736 -0.04153 0.12269  179 GLU   B C   
4162 O  O   . GLU   B 179 ? 0.61401 0.84484 0.82355 -0.07960 -0.05057 0.11391  179 GLU   B O   
4163 C  CB  . GLU   B 179 ? 0.68741 0.95000 0.89186 -0.06533 -0.02423 0.12003  179 GLU   B CB  
4164 C  CG  . GLU   B 179 ? 0.83458 1.07093 1.02561 -0.05869 -0.02360 0.10231  179 GLU   B CG  
4165 C  CD  . GLU   B 179 ? 0.88665 1.12342 1.06729 -0.04752 -0.01166 0.09433  179 GLU   B CD  
4166 O  OE1 . GLU   B 179 ? 0.94145 1.17101 1.11868 -0.04746 -0.01140 0.09342  179 GLU   B OE1 
4167 O  OE2 . GLU   B 179 ? 0.87878 1.12165 1.05432 -0.03903 -0.00354 0.08890  179 GLU   B OE2 
4168 N  N   . GLU   B 180 ? 0.58759 0.86374 0.80608 -0.07287 -0.03390 0.12677  180 GLU   B N   
4169 C  CA  . GLU   B 180 ? 0.54822 0.82081 0.76644 -0.07207 -0.03690 0.12182  180 GLU   B CA  
4170 C  C   . GLU   B 180 ? 0.50655 0.75652 0.71007 -0.06344 -0.03394 0.10392  180 GLU   B C   
4171 O  O   . GLU   B 180 ? 0.44145 0.68991 0.63575 -0.05401 -0.02380 0.09619  180 GLU   B O   
4172 C  CB  . GLU   B 180 ? 0.62711 0.92813 0.85210 -0.06788 -0.02911 0.12945  180 GLU   B CB  
4173 C  CG  . GLU   B 180 ? 0.46738 0.76496 0.69451 -0.06981 -0.03503 0.12688  180 GLU   B CG  
4174 C  CD  . GLU   B 180 ? 0.66492 0.99077 0.89958 -0.06579 -0.02864 0.13466  180 GLU   B CD  
4175 O  OE1 . GLU   B 180 ? 0.58462 0.93474 0.82334 -0.06126 -0.01976 0.14283  180 GLU   B OE1 
4176 O  OE2 . GLU   B 180 ? 0.62463 0.94850 0.86068 -0.06662 -0.03286 0.13243  180 GLU   B OE2 
4177 N  N   . ASN   B 181 ? 0.51981 0.75306 0.72111 -0.06668 -0.04320 0.09783  181 ASN   B N   
4178 C  CA  . ASN   B 181 ? 0.47873 0.69034 0.66633 -0.05957 -0.04196 0.08159  181 ASN   B CA  
4179 C  C   . ASN   B 181 ? 0.43494 0.65332 0.61940 -0.05318 -0.03617 0.07709  181 ASN   B C   
4180 O  O   . ASN   B 181 ? 0.44096 0.65512 0.62694 -0.05631 -0.04334 0.07634  181 ASN   B O   
4181 C  CB  . ASN   B 181 ? 0.48505 0.67283 0.66971 -0.06536 -0.05576 0.07655  181 ASN   B CB  
4182 C  CG  . ASN   B 181 ? 0.71564 0.89468 0.90234 -0.07107 -0.06209 0.08047  181 ASN   B CG  
4183 O  OD1 . ASN   B 181 ? 0.68445 0.85891 0.86489 -0.06592 -0.05567 0.07530  181 ASN   B OD1 
4184 N  ND2 . ASN   B 181 ? 0.78750 0.96435 0.98315 -0.08208 -0.07516 0.09028  181 ASN   B ND2 
4185 N  N   . TYR   B 182 ? 0.39174 0.61932 0.57100 -0.04401 -0.02390 0.07389  182 TYR   B N   
4186 C  CA  . TYR   B 182 ? 0.38722 0.61901 0.56174 -0.03703 -0.01829 0.06882  182 TYR   B CA  
4187 C  C   . TYR   B 182 ? 0.37223 0.58253 0.53503 -0.03365 -0.02009 0.05529  182 TYR   B C   
4188 O  O   . TYR   B 182 ? 0.33019 0.52426 0.48646 -0.03340 -0.02195 0.04817  182 TYR   B O   
4189 C  CB  . TYR   B 182 ? 0.38340 0.62865 0.55434 -0.02781 -0.00609 0.06901  182 TYR   B CB  
4190 C  CG  . TYR   B 182 ? 0.41828 0.68939 0.60056 -0.02927 -0.00357 0.08276  182 TYR   B CG  
4191 C  CD1 . TYR   B 182 ? 0.46501 0.75349 0.65524 -0.02981 -0.00432 0.08987  182 TYR   B CD1 
4192 C  CD2 . TYR   B 182 ? 0.60707 0.88665 0.79203 -0.02971 -0.00026 0.08896  182 TYR   B CD2 
4193 C  CE1 . TYR   B 182 ? 0.50402 0.81929 0.70518 -0.03061 -0.00161 0.10316  182 TYR   B CE1 
4194 C  CE2 . TYR   B 182 ? 0.55789 0.86379 0.75314 -0.03063 0.00246  0.10233  182 TYR   B CE2 
4195 C  CZ  . TYR   B 182 ? 0.50227 0.82648 0.70564 -0.03085 0.00200  0.10933  182 TYR   B CZ  
4196 O  OH  . TYR   B 182 ? 0.68005 1.03318 0.89407 -0.03121 0.00511  0.12317  182 TYR   B OH  
4197 N  N   . CYS   B 183 ? 0.31687 0.52830 0.47702 -0.03073 -0.01955 0.05210  183 CYS   B N   
4198 C  CA  . CYS   B 183 ? 0.31275 0.50661 0.46160 -0.02717 -0.02069 0.04018  183 CYS   B CA  
4199 C  C   . CYS   B 183 ? 0.33076 0.51796 0.46920 -0.01980 -0.01198 0.03186  183 CYS   B C   
4200 O  O   . CYS   B 183 ? 0.33745 0.51015 0.46693 -0.01759 -0.01303 0.02253  183 CYS   B O   
4201 C  CB  . CYS   B 183 ? 0.27355 0.47141 0.42132 -0.02520 -0.02111 0.03922  183 CYS   B CB  
4202 S  SG  . CYS   B 183 ? 0.39416 0.59358 0.55246 -0.03506 -0.03479 0.04676  183 CYS   B SG  
4203 N  N   . SER   B 184 ? 0.31987 0.51799 0.45889 -0.01555 -0.00370 0.03512  184 SER   B N   
4204 C  CA  . SER   B 184 ? 0.31377 0.50493 0.44365 -0.00962 0.00323  0.02827  184 SER   B CA  
4205 C  C   . SER   B 184 ? 0.36434 0.54232 0.49188 -0.01223 -0.00012 0.02393  184 SER   B C   
4206 O  O   . SER   B 184 ? 0.32474 0.49332 0.44401 -0.00836 0.00322  0.01625  184 SER   B O   
4207 C  CB  . SER   B 184 ? 0.35663 0.56123 0.48789 -0.00497 0.01073  0.03347  184 SER   B CB  
4208 O  OG  . SER   B 184 ? 0.33574 0.55155 0.47697 -0.00976 0.00851  0.04303  184 SER   B OG  
4209 N  N   . GLN   B 185 ? 0.33046 0.50772 0.46528 -0.01885 -0.00723 0.02911  185 GLN   B N   
4210 C  CA  . GLN   B 185 ? 0.41321 0.57691 0.54546 -0.02082 -0.01153 0.02487  185 GLN   B CA  
4211 C  C   . GLN   B 185 ? 0.41319 0.56133 0.53829 -0.01998 -0.01713 0.01549  185 GLN   B C   
4212 O  O   . GLN   B 185 ? 0.44596 0.58222 0.56705 -0.01957 -0.02035 0.01013  185 GLN   B O   
4213 C  CB  . GLN   B 185 ? 0.37891 0.54555 0.52075 -0.02848 -0.01859 0.03402  185 GLN   B CB  
4214 C  CG  . GLN   B 185 ? 0.35123 0.53531 0.49901 -0.02802 -0.01173 0.04329  185 GLN   B CG  
4215 C  CD  . GLN   B 185 ? 0.38424 0.57548 0.54280 -0.03639 -0.01825 0.05474  185 GLN   B CD  
4216 O  OE1 . GLN   B 185 ? 0.46499 0.64486 0.62616 -0.04309 -0.02886 0.05547  185 GLN   B OE1 
4217 N  NE2 . GLN   B 185 ? 0.48883 0.69940 0.65353 -0.03597 -0.01263 0.06426  185 GLN   B NE2 
4218 N  N   . ILE   B 186 ? 0.35545 0.50401 0.47850 -0.01910 -0.01854 0.01346  186 ILE   B N   
4219 C  CA  . ILE   B 186 ? 0.32312 0.45941 0.43746 -0.01631 -0.02187 0.00413  186 ILE   B CA  
4220 C  C   . ILE   B 186 ? 0.33389 0.47170 0.44015 -0.00980 -0.01276 -0.00170 186 ILE   B C   
4221 O  O   . ILE   B 186 ? 0.32577 0.45533 0.42422 -0.00618 -0.01196 -0.00952 186 ILE   B O   
4222 C  CB  . ILE   B 186 ? 0.36170 0.49682 0.47794 -0.01954 -0.02991 0.00561  186 ILE   B CB  
4223 C  CG1 . ILE   B 186 ? 0.39597 0.52813 0.52054 -0.02730 -0.04087 0.01219  186 ILE   B CG1 
4224 C  CG2 . ILE   B 186 ? 0.32635 0.44982 0.43175 -0.01520 -0.03265 -0.00451 186 ILE   B CG2 
4225 C  CD1 . ILE   B 186 ? 0.42741 0.54425 0.54821 -0.02776 -0.04730 0.00737  186 ILE   B CD1 
4226 N  N   . LEU   B 187 ? 0.29298 0.44160 0.40077 -0.00802 -0.00630 0.00225  187 LEU   B N   
4227 C  CA  . LEU   B 187 ? 0.30771 0.45565 0.40723 -0.00265 0.00056  -0.00292 187 LEU   B CA  
4228 C  C   . LEU   B 187 ? 0.29977 0.44435 0.39562 -0.00008 0.00562  -0.00613 187 LEU   B C   
4229 O  O   . LEU   B 187 ? 0.30202 0.44150 0.39068 0.00284  0.00802  -0.01222 187 LEU   B O   
4230 C  CB  . LEU   B 187 ? 0.30473 0.46298 0.40559 -0.00050 0.00546  0.00165  187 LEU   B CB  
4231 C  CG  . LEU   B 187 ? 0.47473 0.63469 0.57485 -0.00074 0.00244  0.00180  187 LEU   B CG  
4232 C  CD1 . LEU   B 187 ? 0.35858 0.52101 0.46714 -0.00622 -0.00535 0.00671  187 LEU   B CD1 
4233 C  CD2 . LEU   B 187 ? 0.47392 0.64278 0.57367 0.00300  0.00779  0.00518  187 LEU   B CD2 
4234 N  N   . TYR   B 188 ? 0.31769 0.46668 0.41859 -0.00112 0.00748  -0.00133 188 TYR   B N   
4235 C  CA  . TYR   B 188 ? 0.29880 0.44534 0.39650 0.00138  0.01227  -0.00356 188 TYR   B CA  
4236 C  C   . TYR   B 188 ? 0.25570 0.39248 0.34938 0.00167  0.00974  -0.01031 188 TYR   B C   
4237 O  O   . TYR   B 188 ? 0.30568 0.44015 0.39356 0.00474  0.01376  -0.01481 188 TYR   B O   
4238 C  CB  . TYR   B 188 ? 0.31090 0.46355 0.41486 -0.00023 0.01304  0.00301  188 TYR   B CB  
4239 C  CG  . TYR   B 188 ? 0.26582 0.41735 0.36666 0.00267  0.01802  0.00194  188 TYR   B CG  
4240 C  CD1 . TYR   B 188 ? 0.31151 0.45426 0.40937 0.00273  0.01708  -0.00333 188 TYR   B CD1 
4241 C  CD2 . TYR   B 188 ? 0.29146 0.45118 0.39252 0.00567  0.02291  0.00650  188 TYR   B CD2 
4242 C  CE1 . TYR   B 188 ? 0.34048 0.48214 0.43612 0.00486  0.02082  -0.00385 188 TYR   B CE1 
4243 C  CE2 . TYR   B 188 ? 0.27717 0.43447 0.37460 0.00844  0.02652  0.00536  188 TYR   B CE2 
4244 C  CZ  . TYR   B 188 ? 0.34415 0.49231 0.43936 0.00741  0.02519  0.00034  188 TYR   B CZ  
4245 O  OH  . TYR   B 188 ? 0.30467 0.45056 0.39683 0.00967  0.02799  -0.00048 188 TYR   B OH  
4246 N  N   . PRO   B 189 ? 0.28118 0.41204 0.37739 -0.00108 0.00277  -0.01120 189 PRO   B N   
4247 C  CA  . PRO   B 189 ? 0.29239 0.41450 0.38319 0.00134  0.00076  -0.01874 189 PRO   B CA  
4248 C  C   . PRO   B 189 ? 0.34702 0.46779 0.43060 0.00477  0.00157  -0.02474 189 PRO   B C   
4249 O  O   . PRO   B 189 ? 0.31405 0.43352 0.39247 0.00829  0.00451  -0.02989 189 PRO   B O   
4250 C  CB  . PRO   B 189 ? 0.27497 0.38933 0.36909 -0.00185 -0.00856 -0.01836 189 PRO   B CB  
4251 C  CG  . PRO   B 189 ? 0.27850 0.39827 0.38007 -0.00729 -0.01269 -0.01021 189 PRO   B CG  
4252 C  CD  . PRO   B 189 ? 0.32935 0.46120 0.43316 -0.00626 -0.00395 -0.00513 189 PRO   B CD  
4253 N  N   . CYS   B 190 ? 0.31212 0.43454 0.39520 0.00393  -0.00070 -0.02373 190 CYS   B N   
4254 C  CA  . CYS   B 190 ? 0.31354 0.43564 0.38899 0.00744  0.00077  -0.02897 190 CYS   B CA  
4255 C  C   . CYS   B 190 ? 0.27170 0.39890 0.34380 0.00967  0.00905  -0.02916 190 CYS   B C   
4256 O  O   . CYS   B 190 ? 0.35042 0.47776 0.41683 0.01264  0.01122  -0.03366 190 CYS   B O   
4257 C  CB  . CYS   B 190 ? 0.28035 0.40415 0.35573 0.00610  -0.00232 -0.02706 190 CYS   B CB  
4258 S  SG  . CYS   B 190 ? 0.37878 0.49354 0.45587 0.00358  -0.01446 -0.02835 190 CYS   B SG  
4259 N  N   . MET   B 191 ? 0.29197 0.42366 0.36737 0.00844  0.01315  -0.02397 191 MET   B N   
4260 C  CA  . MET   B 191 ? 0.29717 0.43147 0.36894 0.01013  0.01937  -0.02359 191 MET   B CA  
4261 C  C   . MET   B 191 ? 0.31941 0.45187 0.39075 0.01096  0.02153  -0.02573 191 MET   B C   
4262 O  O   . MET   B 191 ? 0.28954 0.42290 0.35666 0.01222  0.02455  -0.02778 191 MET   B O   
4263 C  CB  . MET   B 191 ? 0.28612 0.42429 0.36035 0.00999  0.02201  -0.01811 191 MET   B CB  
4264 C  CG  . MET   B 191 ? 0.26870 0.41018 0.34245 0.01009  0.02096  -0.01580 191 MET   B CG  
4265 S  SD  . MET   B 191 ? 0.33281 0.48090 0.41078 0.01134  0.02313  -0.00930 191 MET   B SD  
4266 C  CE  . MET   B 191 ? 0.37303 0.51809 0.44419 0.01497  0.02821  -0.00998 191 MET   B CE  
4267 N  N   . GLN   B 192 ? 0.27135 0.40179 0.34725 0.00989  0.01962  -0.02476 192 GLN   B N   
4268 C  CA  . GLN   B 192 ? 0.29541 0.42411 0.37061 0.01099  0.02156  -0.02704 192 GLN   B CA  
4269 C  C   . GLN   B 192 ? 0.37137 0.49900 0.44284 0.01325  0.02025  -0.03284 192 GLN   B C   
4270 O  O   . GLN   B 192 ? 0.34723 0.47727 0.41629 0.01468  0.02354  -0.03461 192 GLN   B O   
4271 C  CB  . GLN   B 192 ? 0.30109 0.42745 0.38137 0.00952  0.01937  -0.02485 192 GLN   B CB  
4272 C  CG  . GLN   B 192 ? 0.23617 0.36030 0.31558 0.01096  0.02085  -0.02770 192 GLN   B CG  
4273 C  CD  . GLN   B 192 ? 0.29831 0.42131 0.38182 0.00954  0.02050  -0.02392 192 GLN   B CD  
4274 O  OE1 . GLN   B 192 ? 0.29101 0.41706 0.37735 0.00807  0.02094  -0.01866 192 GLN   B OE1 
4275 N  NE2 . GLN   B 192 ? 0.31501 0.43499 0.39865 0.01042  0.02007  -0.02625 192 GLN   B NE2 
4276 N  N   . CYS   B 193 ? 0.31146 0.43633 0.38189 0.01396  0.01522  -0.03567 193 CYS   B N   
4277 C  CA  . CYS   B 193 ? 0.35621 0.48099 0.42152 0.01794  0.01392  -0.04182 193 CYS   B CA  
4278 C  C   . CYS   B 193 ? 0.35837 0.49029 0.41890 0.01925  0.01895  -0.04203 193 CYS   B C   
4279 O  O   . CYS   B 193 ? 0.35061 0.48747 0.40870 0.02165  0.02189  -0.04425 193 CYS   B O   
4280 C  CB  . CYS   B 193 ? 0.36351 0.48216 0.42713 0.01893  0.00639  -0.04490 193 CYS   B CB  
4281 S  SG  . CYS   B 193 ? 0.37879 0.49589 0.43448 0.02614  0.00316  -0.05370 193 CYS   B SG  
4282 N  N   . ALA   B 194 ? 0.32995 0.46338 0.38957 0.01733  0.01992  -0.03884 194 ALA   B N   
4283 C  CA  . ALA   B 194 ? 0.31170 0.45103 0.36661 0.01778  0.02392  -0.03807 194 ALA   B CA  
4284 C  C   . ALA   B 194 ? 0.27115 0.41393 0.32676 0.01657  0.02865  -0.03567 194 ALA   B C   
4285 O  O   . ALA   B 194 ? 0.30339 0.45253 0.35571 0.01726  0.03129  -0.03589 194 ALA   B O   
4286 C  CB  . ALA   B 194 ? 0.32833 0.46738 0.38262 0.01576  0.02384  -0.03440 194 ALA   B CB  
4287 N  N   . ASP   B 195 ? 0.35034 0.48955 0.41003 0.01471  0.02932  -0.03294 195 ASP   B N   
4288 C  CA  . ASP   B 195 ? 0.30904 0.44953 0.36873 0.01338  0.03257  -0.03061 195 ASP   B CA  
4289 C  C   . ASP   B 195 ? 0.29657 0.44218 0.35615 0.01477  0.03368  -0.03328 195 ASP   B C   
4290 O  O   . ASP   B 195 ? 0.29927 0.44977 0.35748 0.01335  0.03608  -0.03117 195 ASP   B O   
4291 C  CB  . ASP   B 195 ? 0.31056 0.44635 0.37361 0.01254  0.03258  -0.02849 195 ASP   B CB  
4292 C  CG  . ASP   B 195 ? 0.33484 0.46814 0.39804 0.01212  0.03231  -0.02507 195 ASP   B CG  
4293 O  OD1 . ASP   B 195 ? 0.32858 0.45993 0.39490 0.01232  0.03191  -0.02350 195 ASP   B OD1 
4294 O  OD2 . ASP   B 195 ? 0.37070 0.50499 0.43093 0.01197  0.03240  -0.02385 195 ASP   B OD2 
4295 N  N   . ILE   B 196 ? 0.30008 0.44498 0.36100 0.01764  0.03134  -0.03763 196 ILE   B N   
4296 C  CA  . ILE   B 196 ? 0.33262 0.48309 0.39381 0.02028  0.03225  -0.04054 196 ILE   B CA  
4297 C  C   . ILE   B 196 ? 0.36605 0.52699 0.42335 0.02171  0.03479  -0.04066 196 ILE   B C   
4298 O  O   . ILE   B 196 ? 0.33988 0.50933 0.39810 0.02165  0.03744  -0.03941 196 ILE   B O   
4299 C  CB  . ILE   B 196 ? 0.33071 0.47675 0.39243 0.02423  0.02797  -0.04586 196 ILE   B CB  
4300 C  CG1 . ILE   B 196 ? 0.27524 0.41257 0.34146 0.02188  0.02559  -0.04424 196 ILE   B CG1 
4301 C  CG2 . ILE   B 196 ? 0.34085 0.49418 0.40154 0.02910  0.02865  -0.04996 196 ILE   B CG2 
4302 C  CD1 . ILE   B 196 ? 0.29322 0.42343 0.35996 0.02450  0.01955  -0.04843 196 ILE   B CD1 
4303 N  N   . PHE   B 197 ? 0.30666 0.46827 0.35970 0.02298  0.03382  -0.04172 197 PHE   B N   
4304 C  CA  . PHE   B 197 ? 0.29310 0.46547 0.34169 0.02434  0.03634  -0.04108 197 PHE   B CA  
4305 C  C   . PHE   B 197 ? 0.32025 0.49506 0.36854 0.01883  0.03900  -0.03441 197 PHE   B C   
4306 O  O   . PHE   B 197 ? 0.33127 0.51669 0.37881 0.01760  0.04179  -0.03123 197 PHE   B O   
4307 C  CB  . PHE   B 197 ? 0.34021 0.51062 0.38334 0.02806  0.03339  -0.04501 197 PHE   B CB  
4308 C  CG  . PHE   B 197 ? 0.33664 0.50303 0.37844 0.03395  0.02921  -0.05191 197 PHE   B CG  
4309 C  CD1 . PHE   B 197 ? 0.41832 0.59390 0.45717 0.04021  0.03023  -0.05596 197 PHE   B CD1 
4310 C  CD2 . PHE   B 197 ? 0.37428 0.52832 0.41844 0.03315  0.02407  -0.05369 197 PHE   B CD2 
4311 C  CE1 . PHE   B 197 ? 0.48436 0.65448 0.52120 0.04658  0.02544  -0.06288 197 PHE   B CE1 
4312 C  CE2 . PHE   B 197 ? 0.37558 0.52365 0.41832 0.03806  0.01878  -0.05971 197 PHE   B CE2 
4313 C  CZ  . PHE   B 197 ? 0.44748 0.60231 0.48597 0.04515  0.01913  -0.06480 197 PHE   B CZ  
4314 N  N   . PHE   B 198 ? 0.27199 0.43742 0.32074 0.01562  0.03769  -0.03184 198 PHE   B N   
4315 C  CA  . PHE   B 198 ? 0.29516 0.46000 0.34219 0.01118  0.03879  -0.02606 198 PHE   B CA  
4316 C  C   . PHE   B 198 ? 0.36367 0.53075 0.41305 0.00769  0.04016  -0.02213 198 PHE   B C   
4317 O  O   . PHE   B 198 ? 0.34568 0.51707 0.39319 0.00403  0.04085  -0.01716 198 PHE   B O   
4318 C  CB  . PHE   B 198 ? 0.32922 0.48350 0.37670 0.01020  0.03682  -0.02500 198 PHE   B CB  
4319 C  CG  . PHE   B 198 ? 0.36616 0.51690 0.41049 0.00710  0.03664  -0.02002 198 PHE   B CG  
4320 C  CD1 . PHE   B 198 ? 0.35980 0.51386 0.39963 0.00638  0.03657  -0.01824 198 PHE   B CD1 
4321 C  CD2 . PHE   B 198 ? 0.35275 0.49582 0.39763 0.00571  0.03584  -0.01753 198 PHE   B CD2 
4322 C  CE1 . PHE   B 198 ? 0.34899 0.49843 0.38531 0.00380  0.03542  -0.01379 198 PHE   B CE1 
4323 C  CE2 . PHE   B 198 ? 0.38905 0.52678 0.42970 0.00406  0.03441  -0.01373 198 PHE   B CE2 
4324 C  CZ  . PHE   B 198 ? 0.33559 0.47624 0.37213 0.00290  0.03403  -0.01179 198 PHE   B CZ  
4325 N  N   . LEU   B 199 ? 0.32860 0.49233 0.38205 0.00828  0.03983  -0.02379 199 LEU   B N   
4326 C  CA  . LEU   B 199 ? 0.33101 0.49641 0.38702 0.00517  0.04032  -0.02056 199 LEU   B CA  
4327 C  C   . LEU   B 199 ? 0.35663 0.53589 0.41501 0.00615  0.04234  -0.02085 199 LEU   B C   
4328 O  O   . LEU   B 199 ? 0.35803 0.54043 0.41967 0.00332  0.04244  -0.01787 199 LEU   B O   
4329 C  CB  . LEU   B 199 ? 0.27985 0.43602 0.33877 0.00592  0.03902  -0.02229 199 LEU   B CB  
4330 C  CG  . LEU   B 199 ? 0.31785 0.46291 0.37449 0.00535  0.03747  -0.02082 199 LEU   B CG  
4331 C  CD1 . LEU   B 199 ? 0.37865 0.51699 0.43775 0.00695  0.03666  -0.02236 199 LEU   B CD1 
4332 C  CD2 . LEU   B 199 ? 0.37910 0.52023 0.43186 0.00159  0.03621  -0.01577 199 LEU   B CD2 
4333 N  N   . ASN   B 200 ? 0.32602 0.51393 0.38269 0.01070  0.04359  -0.02447 200 ASN   B N   
4334 C  CA  . ASN   B 200 ? 0.33622 0.53984 0.39444 0.01358  0.04588  -0.02515 200 ASN   B CA  
4335 C  C   . ASN   B 200 ? 0.39600 0.59959 0.45945 0.01509  0.04549  -0.02732 200 ASN   B C   
4336 O  O   . ASN   B 200 ? 0.36846 0.58431 0.43556 0.01422  0.04715  -0.02452 200 ASN   B O   
4337 C  CB  . ASN   B 200 ? 0.34820 0.56447 0.40636 0.00878  0.04793  -0.01773 200 ASN   B CB  
4338 C  CG  . ASN   B 200 ? 0.52687 0.76334 0.58582 0.01305  0.05103  -0.01808 200 ASN   B CG  
4339 O  OD1 . ASN   B 200 ? 0.50888 0.74837 0.56522 0.02102  0.05137  -0.02501 200 ASN   B OD1 
4340 N  ND2 . ASN   B 200 ? 0.60805 0.85846 0.67069 0.00822  0.05269  -0.01064 200 ASN   B ND2 
4341 N  N   . VAL   B 201 ? 0.32666 0.51778 0.39076 0.01750  0.04307  -0.03205 201 VAL   B N   
4342 C  CA  . VAL   B 201 ? 0.32889 0.51717 0.39741 0.01870  0.04202  -0.03407 201 VAL   B CA  
4343 C  C   . VAL   B 201 ? 0.32500 0.52410 0.39420 0.02540  0.04254  -0.03878 201 VAL   B C   
4344 O  O   . VAL   B 201 ? 0.32829 0.52861 0.39341 0.03127  0.04160  -0.04385 201 VAL   B O   
4345 C  CB  . VAL   B 201 ? 0.33890 0.51164 0.40740 0.01901  0.03909  -0.03672 201 VAL   B CB  
4346 C  CG1 . VAL   B 201 ? 0.34044 0.50916 0.41223 0.02146  0.03725  -0.03990 201 VAL   B CG1 
4347 C  CG2 . VAL   B 201 ? 0.33064 0.49449 0.39866 0.01330  0.03897  -0.03154 201 VAL   B CG2 
4348 N  N   . ASP   B 202 ? 0.34157 0.54766 0.41550 0.02525  0.04332  -0.03754 202 ASP   B N   
4349 C  CA  . ASP   B 202 ? 0.29802 0.51304 0.37299 0.03272  0.04322  -0.04258 202 ASP   B CA  
4350 C  C   . ASP   B 202 ? 0.27853 0.47990 0.35451 0.03564  0.03934  -0.04771 202 ASP   B C   
4351 O  O   . ASP   B 202 ? 0.33059 0.53158 0.40423 0.04322  0.03702  -0.05415 202 ASP   B O   
4352 C  CB  . ASP   B 202 ? 0.29091 0.52288 0.37142 0.03118  0.04588  -0.03798 202 ASP   B CB  
4353 C  CG  . ASP   B 202 ? 0.31747 0.56622 0.39739 0.02868  0.04942  -0.03221 202 ASP   B CG  
4354 O  OD1 . ASP   B 202 ? 0.36589 0.62353 0.44106 0.03489  0.05094  -0.03537 202 ASP   B OD1 
4355 O  OD2 . ASP   B 202 ? 0.34202 0.59369 0.42513 0.02038  0.05005  -0.02433 202 ASP   B OD2 
4356 N  N   . ILE   B 203 ? 0.27516 0.46528 0.35401 0.03005  0.03813  -0.04477 203 ILE   B N   
4357 C  CA  . ILE   B 203 ? 0.24575 0.42394 0.32616 0.03148  0.03466  -0.04785 203 ILE   B CA  
4358 C  C   . ILE   B 203 ? 0.32049 0.48429 0.39983 0.02693  0.03315  -0.04574 203 ILE   B C   
4359 O  O   . ILE   B 203 ? 0.35158 0.51299 0.43161 0.02160  0.03458  -0.04083 203 ILE   B O   
4360 C  CB  . ILE   B 203 ? 0.28249 0.46457 0.36796 0.03011  0.03499  -0.04585 203 ILE   B CB  
4361 C  CG1 . ILE   B 203 ? 0.29902 0.49869 0.38639 0.03518  0.03683  -0.04734 203 ILE   B CG1 
4362 C  CG2 . ILE   B 203 ? 0.27592 0.44477 0.36240 0.03118  0.03125  -0.04845 203 ILE   B CG2 
4363 C  CD1 . ILE   B 203 ? 0.34475 0.55111 0.43860 0.03279  0.03712  -0.04400 203 ILE   B CD1 
4364 N  N   . CYS   B 204 ? 0.31070 0.46508 0.38818 0.02922  0.02969  -0.04918 204 CYS   B N   
4365 C  CA  . CYS   B 204 ? 0.30899 0.45184 0.38694 0.02532  0.02806  -0.04654 204 CYS   B CA  
4366 C  C   . CYS   B 204 ? 0.30645 0.44359 0.38746 0.02485  0.02629  -0.04615 204 CYS   B C   
4367 O  O   . CYS   B 204 ? 0.33846 0.47218 0.42006 0.02836  0.02271  -0.04991 204 CYS   B O   
4368 C  CB  . CYS   B 204 ? 0.33254 0.46849 0.40843 0.02693  0.02414  -0.04916 204 CYS   B CB  
4369 S  SG  . CYS   B 204 ? 0.34998 0.49251 0.42131 0.02827  0.02576  -0.05023 204 CYS   B SG  
4370 N  N   . GLN   B 205 ? 0.27206 0.40718 0.35411 0.02103  0.02811  -0.04186 205 GLN   B N   
4371 C  CA  . GLN   B 205 ? 0.33793 0.46802 0.42214 0.02060  0.02665  -0.04109 205 GLN   B CA  
4372 C  C   . GLN   B 205 ? 0.32594 0.44812 0.40929 0.01796  0.02621  -0.03745 205 GLN   B C   
4373 O  O   . GLN   B 205 ? 0.32991 0.45071 0.41173 0.01593  0.02802  -0.03412 205 GLN   B O   
4374 C  CB  . GLN   B 205 ? 0.34294 0.47871 0.42845 0.01924  0.02861  -0.03934 205 GLN   B CB  
4375 C  CG  . GLN   B 205 ? 0.32948 0.46267 0.41757 0.02030  0.02659  -0.04013 205 GLN   B CG  
4376 C  CD  . GLN   B 205 ? 0.33150 0.45456 0.41831 0.01865  0.02528  -0.03777 205 GLN   B CD  
4377 O  OE1 . GLN   B 205 ? 0.36286 0.48315 0.44765 0.01628  0.02630  -0.03452 205 GLN   B OE1 
4378 N  NE2 . GLN   B 205 ? 0.31171 0.42909 0.39903 0.01999  0.02254  -0.03900 205 GLN   B NE2 
4379 N  N   . LEU   B 206 ? 0.27748 0.39484 0.36148 0.01826  0.02332  -0.03781 206 LEU   B N   
4380 C  CA  . LEU   B 206 ? 0.33060 0.44359 0.41489 0.01599  0.02282  -0.03355 206 LEU   B CA  
4381 C  C   . LEU   B 206 ? 0.30665 0.41413 0.39334 0.01599  0.01871  -0.03328 206 LEU   B C   
4382 O  O   . LEU   B 206 ? 0.32605 0.43158 0.41358 0.01823  0.01564  -0.03725 206 LEU   B O   
4383 C  CB  . LEU   B 206 ? 0.24972 0.36344 0.33367 0.01489  0.02234  -0.03237 206 LEU   B CB  
4384 C  CG  . LEU   B 206 ? 0.33871 0.45732 0.41977 0.01489  0.02595  -0.03250 206 LEU   B CG  
4385 C  CD1 . LEU   B 206 ? 0.32927 0.45142 0.40939 0.01698  0.02527  -0.03703 206 LEU   B CD1 
4386 C  CD2 . LEU   B 206 ? 0.31089 0.43010 0.39123 0.01340  0.02683  -0.02883 206 LEU   B CD2 
4387 N  N   . GLY   B 207 ? 0.31067 0.41626 0.39827 0.01379  0.01840  -0.02830 207 GLY   B N   
4388 C  CA  . GLY   B 207 ? 0.33339 0.43397 0.42353 0.01263  0.01386  -0.02650 207 GLY   B CA  
4389 C  C   . GLY   B 207 ? 0.38006 0.47616 0.47174 0.01232  0.00793  -0.02882 207 GLY   B C   
4390 O  O   . GLY   B 207 ? 0.39332 0.49081 0.48427 0.01249  0.00752  -0.03053 207 GLY   B O   
4391 N  N   . ILE   B 208 ? 0.33575 0.42504 0.42884 0.01213  0.00230  -0.02915 208 ILE   B N   
4392 C  CA  . ILE   B 208 ? 0.38301 0.46496 0.47635 0.01225  -0.00534 -0.03178 208 ILE   B CA  
4393 C  C   . ILE   B 208 ? 0.37077 0.45263 0.46660 0.00744  -0.00807 -0.02625 208 ILE   B C   
4394 O  O   . ILE   B 208 ? 0.40931 0.48559 0.50447 0.00743  -0.01415 -0.02874 208 ILE   B O   
4395 C  CB  . ILE   B 208 ? 0.49234 0.56519 0.58609 0.01312  -0.01198 -0.03305 208 ILE   B CB  
4396 C  CG1 . ILE   B 208 ? 0.54906 0.61188 0.64101 0.01503  -0.02115 -0.03773 208 ILE   B CG1 
4397 C  CG2 . ILE   B 208 ? 0.52521 0.59633 0.62218 0.00787  -0.01381 -0.02489 208 ILE   B CG2 
4398 C  CD1 . ILE   B 208 ? 0.51869 0.58225 0.60659 0.02240  -0.02080 -0.04663 208 ILE   B CD1 
4399 N  N   . ASP   B 209 ? 0.36288 0.45149 0.46126 0.00390  -0.00390 -0.01885 209 ASP   B N   
4400 C  CA  . ASP   B 209 ? 0.36725 0.45857 0.46903 -0.00055 -0.00621 -0.01299 209 ASP   B CA  
4401 C  C   . ASP   B 209 ? 0.41304 0.50788 0.51296 0.00092  -0.00395 -0.01622 209 ASP   B C   
4402 O  O   . ASP   B 209 ? 0.41463 0.51117 0.51738 -0.00251 -0.00682 -0.01225 209 ASP   B O   
4403 C  CB  . ASP   B 209 ? 0.35444 0.45469 0.45942 -0.00360 -0.00216 -0.00391 209 ASP   B CB  
4404 C  CG  . ASP   B 209 ? 0.38180 0.49028 0.48360 -0.00014 0.00672  -0.00436 209 ASP   B CG  
4405 O  OD1 . ASP   B 209 ? 0.38662 0.49353 0.48429 0.00364  0.00989  -0.01085 209 ASP   B OD1 
4406 O  OD2 . ASP   B 209 ? 0.40236 0.51912 0.50550 -0.00094 0.01024  0.00226  209 ASP   B OD2 
4407 N  N   . GLN   B 210 ? 0.35502 0.45160 0.45064 0.00547  0.00070  -0.02259 210 GLN   B N   
4408 C  CA  . GLN   B 210 ? 0.35294 0.45254 0.44594 0.00714  0.00257  -0.02596 210 GLN   B CA  
4409 C  C   . GLN   B 210 ? 0.36453 0.45772 0.45440 0.01022  -0.00297 -0.03304 210 GLN   B C   
4410 O  O   . GLN   B 210 ? 0.37077 0.46652 0.45752 0.01226  -0.00173 -0.03637 210 GLN   B O   
4411 C  CB  . GLN   B 210 ? 0.31785 0.42394 0.40772 0.00983  0.01047  -0.02767 210 GLN   B CB  
4412 C  CG  . GLN   B 210 ? 0.32130 0.43167 0.41207 0.00862  0.01513  -0.02211 210 GLN   B CG  
4413 C  CD  . GLN   B 210 ? 0.37103 0.48662 0.46374 0.00646  0.01627  -0.01636 210 GLN   B CD  
4414 O  OE1 . GLN   B 210 ? 0.31476 0.43304 0.40592 0.00698  0.01772  -0.01738 210 GLN   B OE1 
4415 N  NE2 . GLN   B 210 ? 0.30744 0.42583 0.40351 0.00434  0.01586  -0.00993 210 GLN   B NE2 
4416 N  N   . ARG   B 211 ? 0.33998 0.42469 0.42963 0.01145  -0.00929 -0.03575 211 ARG   B N   
4417 C  CA  . ARG   B 211 ? 0.32558 0.40462 0.41037 0.01701  -0.01400 -0.04400 211 ARG   B CA  
4418 C  C   . ARG   B 211 ? 0.38699 0.46266 0.46919 0.01712  -0.01888 -0.04597 211 ARG   B C   
4419 O  O   . ARG   B 211 ? 0.40585 0.48301 0.48268 0.02259  -0.01836 -0.05242 211 ARG   B O   
4420 C  CB  . ARG   B 211 ? 0.37041 0.43876 0.45516 0.01818  -0.02175 -0.04589 211 ARG   B CB  
4421 C  CG  . ARG   B 211 ? 0.43092 0.49308 0.50985 0.02571  -0.02697 -0.05492 211 ARG   B CG  
4422 C  CD  . ARG   B 211 ? 0.49355 0.54284 0.57272 0.02591  -0.03608 -0.05546 211 ARG   B CD  
4423 N  NE  . ARG   B 211 ? 0.55190 0.59704 0.62512 0.03519  -0.03970 -0.06478 211 ARG   B NE  
4424 C  CZ  . ARG   B 211 ? 0.57284 0.60827 0.63959 0.04068  -0.04830 -0.07146 211 ARG   B CZ  
4425 N  NH1 . ARG   B 211 ? 0.57839 0.60637 0.64399 0.03700  -0.05466 -0.06984 211 ARG   B NH1 
4426 N  NH2 . ARG   B 211 ? 0.61767 0.65133 0.67856 0.05067  -0.05078 -0.08010 211 ARG   B NH2 
4427 N  N   . LYS   B 212 ? 0.40703 0.47892 0.49302 0.01112  -0.02400 -0.04006 212 LYS   B N   
4428 C  CA  . LYS   B 212 ? 0.39606 0.46289 0.47955 0.01088  -0.03050 -0.04196 212 LYS   B CA  
4429 C  C   . LYS   B 212 ? 0.37308 0.44878 0.45288 0.01397  -0.02374 -0.04488 212 LYS   B C   
4430 O  O   . LYS   B 212 ? 0.38894 0.46109 0.46250 0.01859  -0.02732 -0.05126 212 LYS   B O   
4431 C  CB  . LYS   B 212 ? 0.51208 0.57727 0.60219 0.00258  -0.03582 -0.03302 212 LYS   B CB  
4432 C  CG  . LYS   B 212 ? 0.57168 0.62345 0.66299 0.00004  -0.04700 -0.03191 212 LYS   B CG  
4433 C  CD  . LYS   B 212 ? 0.65068 0.68819 0.73421 0.00515  -0.05745 -0.04074 212 LYS   B CD  
4434 C  CE  . LYS   B 212 ? 0.81244 0.83443 0.89431 0.00573  -0.06828 -0.04262 212 LYS   B CE  
4435 N  NZ  . LYS   B 212 ? 0.81264 0.83752 0.89219 0.01209  -0.06197 -0.04750 212 LYS   B NZ  
4436 N  N   . VAL   B 213 ? 0.37180 0.45848 0.45444 0.01195  -0.01451 -0.04040 213 VAL   B N   
4437 C  CA  . VAL   B 213 ? 0.37346 0.46712 0.45250 0.01402  -0.00953 -0.04232 213 VAL   B CA  
4438 C  C   . VAL   B 213 ? 0.39628 0.49383 0.46982 0.02032  -0.00522 -0.04888 213 VAL   B C   
4439 O  O   . VAL   B 213 ? 0.31141 0.41246 0.37991 0.02369  -0.00393 -0.05259 213 VAL   B O   
4440 C  CB  . VAL   B 213 ? 0.35051 0.45310 0.43339 0.01024  -0.00262 -0.03549 213 VAL   B CB  
4441 C  CG1 . VAL   B 213 ? 0.35569 0.46339 0.43904 0.01122  0.00471  -0.03443 213 VAL   B CG1 
4442 C  CG2 . VAL   B 213 ? 0.33304 0.44053 0.41246 0.01128  0.00001  -0.03649 213 VAL   B CG2 
4443 N  N   . ASN   B 214 ? 0.35143 0.44958 0.42594 0.02209  -0.00308 -0.05004 214 ASN   B N   
4444 C  CA  . ASN   B 214 ? 0.35309 0.45696 0.42346 0.02808  0.00045  -0.05563 214 ASN   B CA  
4445 C  C   . ASN   B 214 ? 0.32033 0.41870 0.38471 0.03461  -0.00618 -0.06319 214 ASN   B C   
4446 O  O   . ASN   B 214 ? 0.33466 0.44023 0.39388 0.04030  -0.00351 -0.06778 214 ASN   B O   
4447 C  CB  . ASN   B 214 ? 0.31779 0.42331 0.39131 0.02818  0.00327  -0.05471 214 ASN   B CB  
4448 C  CG  . ASN   B 214 ? 0.36714 0.47910 0.44387 0.02390  0.01038  -0.04887 214 ASN   B CG  
4449 O  OD1 . ASN   B 214 ? 0.37682 0.49569 0.45204 0.02324  0.01527  -0.04750 214 ASN   B OD1 
4450 N  ND2 . ASN   B 214 ? 0.37941 0.48838 0.45977 0.02140  0.01041  -0.04553 214 ASN   B ND2 
4451 N  N   . MET   B 215 ? 0.36280 0.44828 0.42721 0.03406  -0.01552 -0.06431 215 MET   B N   
4452 C  CA  . MET   B 215 ? 0.41246 0.48971 0.46960 0.04097  -0.02362 -0.07208 215 MET   B CA  
4453 C  C   . MET   B 215 ? 0.37668 0.45412 0.42932 0.04140  -0.02527 -0.07332 215 MET   B C   
4454 O  O   . MET   B 215 ? 0.39465 0.47272 0.43919 0.04920  -0.02711 -0.08035 215 MET   B O   
4455 C  CB  . MET   B 215 ? 0.47705 0.53805 0.53477 0.03971  -0.03490 -0.07260 215 MET   B CB  
4456 C  CG  . MET   B 215 ? 0.45937 0.51869 0.52076 0.03984  -0.03443 -0.07176 215 MET   B CG  
4457 S  SD  . MET   B 215 ? 0.65401 0.72003 0.70932 0.05185  -0.03149 -0.08106 215 MET   B SD  
4458 C  CE  . MET   B 215 ? 0.65583 0.70812 0.69992 0.06174  -0.04383 -0.09126 215 MET   B CE  
4459 N  N   . LEU   B 216 ? 0.39535 0.47399 0.45300 0.03366  -0.02393 -0.06637 216 LEU   B N   
4460 C  CA  . LEU   B 216 ? 0.37972 0.45906 0.43360 0.03361  -0.02535 -0.06699 216 LEU   B CA  
4461 C  C   . LEU   B 216 ? 0.38601 0.47781 0.43470 0.03888  -0.01715 -0.07016 216 LEU   B C   
4462 O  O   . LEU   B 216 ? 0.38629 0.47788 0.42722 0.04430  -0.01967 -0.07539 216 LEU   B O   
4463 C  CB  . LEU   B 216 ? 0.37309 0.45495 0.43424 0.02491  -0.02368 -0.05832 216 LEU   B CB  
4464 C  CG  . LEU   B 216 ? 0.42962 0.51001 0.48809 0.02378  -0.02746 -0.05818 216 LEU   B CG  
4465 C  CD1 . LEU   B 216 ? 0.48161 0.54736 0.53964 0.02193  -0.04063 -0.05905 216 LEU   B CD1 
4466 C  CD2 . LEU   B 216 ? 0.48133 0.57068 0.54636 0.01748  -0.02127 -0.05006 216 LEU   B CD2 
4467 N  N   . ALA   B 217 ? 0.37454 0.47721 0.42695 0.03759  -0.00790 -0.06698 217 ALA   B N   
4468 C  CA  . ALA   B 217 ? 0.37889 0.49437 0.42743 0.04093  -0.00048 -0.06810 217 ALA   B CA  
4469 C  C   . ALA   B 217 ? 0.39872 0.51668 0.43993 0.05042  -0.00237 -0.07595 217 ALA   B C   
4470 O  O   . ALA   B 217 ? 0.35168 0.47699 0.38642 0.05509  -0.00046 -0.07875 217 ALA   B O   
4471 C  CB  . ALA   B 217 ? 0.37674 0.50169 0.43057 0.03736  0.00800  -0.06301 217 ALA   B CB  
4472 N  N   . ARG   B 218 ? 0.38465 0.49767 0.42650 0.05405  -0.00585 -0.07945 218 ARG   B N   
4473 C  CA  . ARG   B 218 ? 0.39718 0.51309 0.43143 0.06486  -0.00804 -0.08757 218 ARG   B CA  
4474 C  C   . ARG   B 218 ? 0.44395 0.55015 0.46896 0.07033  -0.01647 -0.09371 218 ARG   B C   
4475 O  O   . ARG   B 218 ? 0.44689 0.56063 0.46342 0.07908  -0.01550 -0.09917 218 ARG   B O   
4476 C  CB  . ARG   B 218 ? 0.40089 0.51112 0.43731 0.06794  -0.01157 -0.09034 218 ARG   B CB  
4477 C  CG  . ARG   B 218 ? 0.41532 0.53726 0.45939 0.06425  -0.00303 -0.08528 218 ARG   B CG  
4478 C  CD  . ARG   B 218 ? 0.36760 0.48374 0.41406 0.06710  -0.00669 -0.08774 218 ARG   B CD  
4479 N  NE  . ARG   B 218 ? 0.39682 0.51222 0.43559 0.07896  -0.01164 -0.09664 218 ARG   B NE  
4480 C  CZ  . ARG   B 218 ? 0.44952 0.58094 0.48636 0.08682  -0.00650 -0.09969 218 ARG   B CZ  
4481 N  NH1 . ARG   B 218 ? 0.38128 0.53035 0.42374 0.08295  0.00327  -0.09399 218 ARG   B NH1 
4482 N  NH2 . ARG   B 218 ? 0.46859 0.59854 0.49759 0.09902  -0.01183 -0.10836 218 ARG   B NH2 
4483 N  N   . GLU   B 219 ? 0.43230 0.52233 0.45863 0.06527  -0.02515 -0.09249 219 GLU   B N   
4484 C  CA  . GLU   B 219 ? 0.43822 0.51702 0.45565 0.06961  -0.03469 -0.09799 219 GLU   B CA  
4485 C  C   . GLU   B 219 ? 0.46103 0.55007 0.47436 0.06990  -0.02945 -0.09704 219 GLU   B C   
4486 O  O   . GLU   B 219 ? 0.45924 0.54742 0.46184 0.07825  -0.03314 -0.10371 219 GLU   B O   
4487 C  CB  . GLU   B 219 ? 0.51726 0.57918 0.53945 0.06136  -0.04445 -0.09412 219 GLU   B CB  
4488 C  CG  . GLU   B 219 ? 0.68283 0.72576 0.70024 0.06512  -0.05804 -0.09959 219 GLU   B CG  
4489 C  CD  . GLU   B 219 ? 0.87724 0.90570 0.89783 0.05646  -0.06851 -0.09502 219 GLU   B CD  
4490 O  OE1 . GLU   B 219 ? 0.84281 0.86090 0.85485 0.06010  -0.07787 -0.09996 219 GLU   B OE1 
4491 O  OE2 . GLU   B 219 ? 0.82305 0.85211 0.85476 0.04604  -0.06701 -0.08599 219 GLU   B OE2 
4492 N  N   . TYR   B 220 ? 0.42581 0.52431 0.44675 0.06139  -0.02114 -0.08889 220 TYR   B N   
4493 C  CA  . TYR   B 220 ? 0.41374 0.52095 0.43073 0.06124  -0.01677 -0.08749 220 TYR   B CA  
4494 C  C   . TYR   B 220 ? 0.43928 0.56138 0.44902 0.07005  -0.01057 -0.09159 220 TYR   B C   
4495 O  O   . TYR   B 220 ? 0.39535 0.52197 0.39680 0.07475  -0.01053 -0.09432 220 TYR   B O   
4496 C  CB  . TYR   B 220 ? 0.38898 0.50261 0.41501 0.05124  -0.00959 -0.07817 220 TYR   B CB  
4497 C  CG  . TYR   B 220 ? 0.42099 0.54260 0.44380 0.05001  -0.00534 -0.07566 220 TYR   B CG  
4498 C  CD1 . TYR   B 220 ? 0.38786 0.50189 0.40719 0.04901  -0.01163 -0.07635 220 TYR   B CD1 
4499 C  CD2 . TYR   B 220 ? 0.38434 0.52016 0.40828 0.04869  0.00420  -0.07162 220 TYR   B CD2 
4500 C  CE1 . TYR   B 220 ? 0.45396 0.57503 0.47001 0.04795  -0.00798 -0.07392 220 TYR   B CE1 
4501 C  CE2 . TYR   B 220 ? 0.45886 0.60122 0.47955 0.04717  0.00755  -0.06874 220 TYR   B CE2 
4502 C  CZ  . TYR   B 220 ? 0.46090 0.59592 0.47767 0.04694  0.00174  -0.06997 220 TYR   B CZ  
4503 O  OH  . TYR   B 220 ? 0.44756 0.58908 0.46093 0.04555  0.00507  -0.06696 220 TYR   B OH  
4504 N  N   . CYS   B 221 ? 0.38762 0.51910 0.40063 0.07237  -0.00507 -0.09145 221 CYS   B N   
4505 C  CA  . CYS   B 221 ? 0.36233 0.51073 0.36919 0.08090  0.00067  -0.09448 221 CYS   B CA  
4506 C  C   . CYS   B 221 ? 0.40412 0.54740 0.39863 0.09312  -0.00664 -0.10432 221 CYS   B C   
4507 O  O   . CYS   B 221 ? 0.45286 0.60783 0.43881 0.10033  -0.00383 -0.10701 221 CYS   B O   
4508 C  CB  . CYS   B 221 ? 0.36489 0.52390 0.37795 0.08170  0.00632  -0.09288 221 CYS   B CB  
4509 S  SG  . CYS   B 221 ? 0.42476 0.59112 0.44964 0.06928  0.01477  -0.08211 221 CYS   B SG  
4510 N  N   . ASP   B 222 ? 0.41216 0.53821 0.40474 0.09644  -0.01645 -0.10995 222 ASP   B N   
4511 C  CA  . ASP   B 222 ? 0.44274 0.56181 0.42192 0.10955  -0.02476 -0.12036 222 ASP   B CA  
4512 C  C   . ASP   B 222 ? 0.52487 0.63698 0.49576 0.11003  -0.02982 -0.12222 222 ASP   B C   
4513 O  O   . ASP   B 222 ? 0.49969 0.61703 0.45817 0.12109  -0.03095 -0.12874 222 ASP   B O   
4514 C  CB  . ASP   B 222 ? 0.51675 0.61571 0.49561 0.11169  -0.03586 -0.12526 222 ASP   B CB  
4515 C  CG  . ASP   B 222 ? 0.64796 0.75503 0.63195 0.11496  -0.03148 -0.12563 222 ASP   B CG  
4516 O  OD1 . ASP   B 222 ? 0.60031 0.72958 0.58725 0.11663  -0.02031 -0.12272 222 ASP   B OD1 
4517 O  OD2 . ASP   B 222 ? 0.61159 0.70310 0.59760 0.11460  -0.03937 -0.12772 222 ASP   B OD2 
4518 N  N   . ILE   B 223 ? 0.50518 0.60770 0.48303 0.09818  -0.03211 -0.11590 223 ILE   B N   
4519 C  CA  . ILE   B 223 ? 0.46602 0.56081 0.43695 0.09778  -0.03798 -0.11724 223 ILE   B CA  
4520 C  C   . ILE   B 223 ? 0.45526 0.56877 0.42096 0.10080  -0.02878 -0.11576 223 ILE   B C   
4521 O  O   . ILE   B 223 ? 0.48601 0.59792 0.43963 0.10827  -0.03298 -0.12124 223 ILE   B O   
4522 C  CB  . ILE   B 223 ? 0.43767 0.52216 0.41923 0.08408  -0.04108 -0.10938 223 ILE   B CB  
4523 C  CG1 . ILE   B 223 ? 0.50360 0.56757 0.48788 0.08147  -0.05328 -0.11097 223 ILE   B CG1 
4524 C  CG2 . ILE   B 223 ? 0.49628 0.57969 0.47326 0.08191  -0.04318 -0.10815 223 ILE   B CG2 
4525 C  CD1 . ILE   B 223 ? 0.54533 0.60411 0.54316 0.06708  -0.05431 -0.10098 223 ILE   B CD1 
4526 N  N   . LYS   B 224 ? 0.43073 0.56117 0.40512 0.09451  -0.01696 -0.10790 224 LYS   B N   
4527 C  CA  . LYS   B 224 ? 0.43686 0.58552 0.40842 0.09469  -0.00796 -0.10401 224 LYS   B CA  
4528 C  C   . LYS   B 224 ? 0.48323 0.65108 0.44852 0.10531  -0.00168 -0.10724 224 LYS   B C   
4529 O  O   . LYS   B 224 ? 0.51192 0.69742 0.47473 0.10574  0.00598  -0.10327 224 LYS   B O   
4530 C  CB  . LYS   B 224 ? 0.43300 0.58903 0.41682 0.08229  0.00036  -0.09340 224 LYS   B CB  
4531 C  CG  . LYS   B 224 ? 0.46458 0.60638 0.45463 0.07233  -0.00422 -0.08900 224 LYS   B CG  
4532 C  CD  . LYS   B 224 ? 0.48555 0.62628 0.46769 0.07335  -0.00683 -0.08966 224 LYS   B CD  
4533 C  CE  . LYS   B 224 ? 0.56578 0.69373 0.55411 0.06433  -0.01220 -0.08542 224 LYS   B CE  
4534 N  NZ  . LYS   B 224 ? 0.60002 0.73223 0.58383 0.06283  -0.01084 -0.08282 224 LYS   B NZ  
4535 N  N   . LYS   B 225 ? 0.46904 0.63485 0.43182 0.11391  -0.00488 -0.11380 225 LYS   B N   
4536 C  CA  . LYS   B 225 ? 0.54103 0.72793 0.49891 0.12486  0.00145  -0.11653 225 LYS   B CA  
4537 C  C   . LYS   B 225 ? 0.46394 0.67188 0.43293 0.11701  0.01334  -0.10649 225 LYS   B C   
4538 O  O   . LYS   B 225 ? 0.51382 0.74455 0.47986 0.12186  0.02075  -0.10428 225 LYS   B O   
4539 C  CB  . LYS   B 225 ? 0.60178 0.79885 0.54468 0.13647  0.00150  -0.12164 225 LYS   B CB  
4540 C  CG  . LYS   B 225 ? 0.61755 0.79503 0.54624 0.14698  -0.01102 -0.13285 225 LYS   B CG  
4541 C  CD  . LYS   B 225 ? 0.64580 0.80345 0.57543 0.15010  -0.02072 -0.13938 225 LYS   B CD  
4542 C  CE  . LYS   B 225 ? 0.79004 0.92176 0.70798 0.15500  -0.03560 -0.14794 225 LYS   B CE  
4543 N  NZ  . LYS   B 225 ? 0.82569 0.93299 0.74803 0.15167  -0.04670 -0.15073 225 LYS   B NZ  
4544 N  N   . ILE   B 226 ? 0.47143 0.67251 0.45292 0.10481  0.01491  -0.09983 226 ILE   B N   
4545 C  CA  . ILE   B 226 ? 0.46155 0.67903 0.45327 0.09735  0.02423  -0.09087 226 ILE   B CA  
4546 C  C   . ILE   B 226 ? 0.47580 0.69898 0.47105 0.10305  0.02487  -0.09389 226 ILE   B C   
4547 O  O   . ILE   B 226 ? 0.47132 0.67785 0.46915 0.10300  0.01872  -0.09782 226 ILE   B O   
4548 C  CB  . ILE   B 226 ? 0.50912 0.71575 0.51106 0.08323  0.02494  -0.08322 226 ILE   B CB  
4549 C  CG1 . ILE   B 226 ? 0.46173 0.66427 0.46054 0.07796  0.02456  -0.07982 226 ILE   B CG1 
4550 C  CG2 . ILE   B 226 ? 0.49583 0.71545 0.50768 0.07605  0.03248  -0.07499 226 ILE   B CG2 
4551 C  CD1 . ILE   B 226 ? 0.54090 0.73089 0.54849 0.06626  0.02380  -0.07381 226 ILE   B CD1 
4552 N  N   . LYS   B 227 ? 0.45976 0.70714 0.45514 0.10808  0.03191  -0.09172 227 LYS   B N   
4553 C  CA  . LYS   B 227 ? 0.44812 0.70343 0.44635 0.11517  0.03248  -0.09502 227 LYS   B CA  
4554 C  C   . LYS   B 227 ? 0.49281 0.74930 0.50465 0.10453  0.03602  -0.08764 227 LYS   B C   
4555 O  O   . LYS   B 227 ? 0.52842 0.78137 0.54365 0.10808  0.03367  -0.09111 227 LYS   B O   
4556 C  CB  . LYS   B 227 ? 0.45727 0.74083 0.45032 0.12627  0.03837  -0.09570 227 LYS   B CB  
4557 C  CG  . LYS   B 227 ? 0.65850 0.94078 0.63565 0.14110  0.03379  -0.10564 227 LYS   B CG  
4558 C  CD  . LYS   B 227 ? 0.69048 0.94914 0.66143 0.14998  0.02303  -0.11721 227 LYS   B CD  
4559 C  CE  . LYS   B 227 ? 0.70223 0.95680 0.65563 0.16594  0.01667  -0.12821 227 LYS   B CE  
4560 N  NZ  . LYS   B 227 ? 0.75729 0.99709 0.70351 0.16218  0.01208  -0.12903 227 LYS   B NZ  
4561 N  N   . LYS   B 228 ? 0.44260 0.70249 0.46147 0.09205  0.04076  -0.07793 228 LYS   B N   
4562 C  CA  . LYS   B 228 ? 0.47452 0.73184 0.50485 0.08163  0.04284  -0.07120 228 LYS   B CA  
4563 C  C   . LYS   B 228 ? 0.56434 0.79580 0.59688 0.07677  0.03660  -0.07372 228 LYS   B C   
4564 O  O   . LYS   B 228 ? 0.55124 0.77091 0.58309 0.07036  0.03497  -0.07146 228 LYS   B O   
4565 C  CB  . LYS   B 228 ? 0.45925 0.72632 0.49440 0.07077  0.04839  -0.06054 228 LYS   B CB  
4566 C  CG  . LYS   B 228 ? 0.46768 0.73252 0.51336 0.06145  0.04976  -0.05423 228 LYS   B CG  
4567 C  CD  . LYS   B 228 ? 0.48769 0.75914 0.53736 0.05074  0.05346  -0.04389 228 LYS   B CD  
4568 C  CE  . LYS   B 228 ? 0.58447 0.84844 0.64260 0.04256  0.05288  -0.03936 228 LYS   B CE  
4569 N  NZ  . LYS   B 228 ? 0.59236 0.85606 0.65319 0.03196  0.05420  -0.03019 228 LYS   B NZ  
4570 N  N   . LYS   B 229 ? 0.39661 0.62005 0.43179 0.08003  0.03291  -0.07805 229 LYS   B N   
4571 C  CA  . LYS   B 229 ? 0.40961 0.61018 0.44682 0.07578  0.02665  -0.07986 229 LYS   B CA  
4572 C  C   . LYS   B 229 ? 0.48118 0.67983 0.52801 0.06821  0.02867  -0.07456 229 LYS   B C   
4573 O  O   . LYS   B 229 ? 0.36691 0.57878 0.41771 0.07014  0.03213  -0.07324 229 LYS   B O   
4574 C  CB  . LYS   B 229 ? 0.44870 0.63728 0.47986 0.08555  0.01860  -0.08938 229 LYS   B CB  
4575 C  CG  . LYS   B 229 ? 0.55821 0.74242 0.57861 0.09272  0.01412  -0.09547 229 LYS   B CG  
4576 C  CD  . LYS   B 229 ? 0.58177 0.75658 0.59408 0.10488  0.00581  -0.10571 229 LYS   B CD  
4577 C  CE  . LYS   B 229 ? 0.57868 0.72947 0.59360 0.10091  -0.00331 -0.10742 229 LYS   B CE  
4578 N  NZ  . LYS   B 229 ? 0.58448 0.72227 0.58814 0.11295  -0.01383 -0.11796 229 LYS   B NZ  
4579 N  N   . PRO   B 230 ? 0.38773 0.57154 0.43831 0.06002  0.02660  -0.07124 230 PRO   B N   
4580 C  CA  . PRO   B 230 ? 0.36380 0.54488 0.42215 0.05354  0.02817  -0.06652 230 PRO   B CA  
4581 C  C   . PRO   B 230 ? 0.37996 0.55318 0.43992 0.05774  0.02356  -0.07107 230 PRO   B C   
4582 O  O   . PRO   B 230 ? 0.35535 0.51700 0.41115 0.06250  0.01709  -0.07682 230 PRO   B O   
4583 C  CB  . PRO   B 230 ? 0.39441 0.56309 0.45444 0.04536  0.02721  -0.06213 230 PRO   B CB  
4584 C  CG  . PRO   B 230 ? 0.33024 0.48958 0.38492 0.04847  0.02198  -0.06654 230 PRO   B CG  
4585 C  CD  . PRO   B 230 ? 0.31588 0.48642 0.36381 0.05622  0.02303  -0.07089 230 PRO   B CD  
4586 N  N   . VAL   B 231 ? 0.32948 0.50863 0.39521 0.05600  0.02614  -0.06840 231 VAL   B N   
4587 C  CA  . VAL   B 231 ? 0.35908 0.52953 0.42713 0.05845  0.02183  -0.07146 231 VAL   B CA  
4588 C  C   . VAL   B 231 ? 0.35138 0.50691 0.42285 0.05052  0.01975  -0.06745 231 VAL   B C   
4589 O  O   . VAL   B 231 ? 0.34040 0.49757 0.41500 0.04339  0.02367  -0.06134 231 VAL   B O   
4590 C  CB  . VAL   B 231 ? 0.35412 0.53832 0.42695 0.06042  0.02518  -0.07028 231 VAL   B CB  
4591 C  CG1 . VAL   B 231 ? 0.41877 0.59241 0.49438 0.06155  0.02070  -0.07242 231 VAL   B CG1 
4592 C  CG2 . VAL   B 231 ? 0.37877 0.58026 0.44798 0.07019  0.02704  -0.07455 231 VAL   B CG2 
4593 N  N   . ILE   B 232 ? 0.32747 0.46857 0.39795 0.05196  0.01315  -0.07055 232 ILE   B N   
4594 C  CA  . ILE   B 232 ? 0.32934 0.45848 0.40325 0.04493  0.01116  -0.06607 232 ILE   B CA  
4595 C  C   . ILE   B 232 ? 0.41121 0.53939 0.48917 0.04482  0.01087  -0.06531 232 ILE   B C   
4596 O  O   . ILE   B 232 ? 0.38620 0.50879 0.46321 0.04972  0.00574  -0.06969 232 ILE   B O   
4597 C  CB  . ILE   B 232 ? 0.33625 0.45079 0.40774 0.04480  0.00351  -0.06794 232 ILE   B CB  
4598 C  CG1 . ILE   B 232 ? 0.37615 0.49142 0.44225 0.04736  0.00213  -0.07086 232 ILE   B CG1 
4599 C  CG2 . ILE   B 232 ? 0.32087 0.42838 0.39655 0.03675  0.00335  -0.06128 232 ILE   B CG2 
4600 C  CD1 . ILE   B 232 ? 0.41145 0.53746 0.47794 0.04375  0.00941  -0.06675 232 ILE   B CD1 
4601 N  N   . LEU   B 233 ? 0.30064 0.43270 0.38238 0.03944  0.01547  -0.05992 233 LEU   B N   
4602 C  CA  . LEU   B 233 ? 0.30862 0.43966 0.39394 0.03887  0.01515  -0.05877 233 LEU   B CA  
4603 C  C   . LEU   B 233 ? 0.30865 0.42928 0.39531 0.03298  0.01407  -0.05397 233 LEU   B C   
4604 O  O   . LEU   B 233 ? 0.32469 0.44709 0.41219 0.02841  0.01788  -0.04924 233 LEU   B O   
4605 C  CB  . LEU   B 233 ? 0.32435 0.46850 0.41228 0.03781  0.02040  -0.05635 233 LEU   B CB  
4606 C  CG  . LEU   B 233 ? 0.35524 0.49999 0.44695 0.03771  0.01978  -0.05548 233 LEU   B CG  
4607 C  CD1 . LEU   B 233 ? 0.38754 0.53438 0.47885 0.04571  0.01627  -0.06166 233 LEU   B CD1 
4608 C  CD2 . LEU   B 233 ? 0.37794 0.53472 0.47265 0.03428  0.02425  -0.05123 233 LEU   B CD2 
4609 N  N   . SER   B 234 ? 0.29962 0.40932 0.38586 0.03324  0.00837  -0.05484 234 SER   B N   
4610 C  CA  . SER   B 234 ? 0.33534 0.43774 0.42294 0.02774  0.00751  -0.04932 234 SER   B CA  
4611 C  C   . SER   B 234 ? 0.39864 0.49829 0.48823 0.02677  0.00712  -0.04720 234 SER   B C   
4612 O  O   . SER   B 234 ? 0.41695 0.51462 0.50704 0.03045  0.00383  -0.05074 234 SER   B O   
4613 C  CB  . SER   B 234 ? 0.37503 0.46761 0.46212 0.02685  0.00084  -0.04931 234 SER   B CB  
4614 O  OG  . SER   B 234 ? 0.43885 0.53255 0.52342 0.02826  -0.00005 -0.05193 234 SER   B OG  
4615 N  N   . HIS   B 235 ? 0.36735 0.46684 0.45737 0.02260  0.01018  -0.04172 235 HIS   B N   
4616 C  CA  . HIS   B 235 ? 0.38566 0.48137 0.47649 0.02147  0.00937  -0.03898 235 HIS   B CA  
4617 C  C   . HIS   B 235 ? 0.45042 0.53912 0.54201 0.01862  0.00553  -0.03470 235 HIS   B C   
4618 O  O   . HIS   B 235 ? 0.33328 0.42145 0.42526 0.01624  0.00472  -0.03211 235 HIS   B O   
4619 C  CB  . HIS   B 235 ? 0.34384 0.44331 0.43330 0.01977  0.01431  -0.03581 235 HIS   B CB  
4620 C  CG  . HIS   B 235 ? 0.33540 0.43562 0.42290 0.01726  0.01722  -0.03144 235 HIS   B CG  
4621 N  ND1 . HIS   B 235 ? 0.33167 0.43643 0.41754 0.01686  0.02061  -0.03157 235 HIS   B ND1 
4622 C  CD2 . HIS   B 235 ? 0.37810 0.47622 0.46495 0.01552  0.01723  -0.02649 235 HIS   B CD2 
4623 C  CE1 . HIS   B 235 ? 0.30815 0.41273 0.39224 0.01553  0.02234  -0.02760 235 HIS   B CE1 
4624 N  NE2 . HIS   B 235 ? 0.33259 0.43426 0.41740 0.01490  0.02068  -0.02432 235 HIS   B NE2 
4625 N  N   . GLY   B 236 ? 0.40198 0.48608 0.49414 0.01845  0.00292  -0.03315 236 GLY   B N   
4626 C  CA  . GLY   B 236 ? 0.43032 0.50862 0.52366 0.01519  -0.00138 -0.02804 236 GLY   B CA  
4627 C  C   . GLY   B 236 ? 0.36073 0.44366 0.45363 0.01198  0.00283  -0.02098 236 GLY   B C   
4628 O  O   . GLY   B 236 ? 0.39125 0.47879 0.48166 0.01310  0.00819  -0.02049 236 GLY   B O   
4629 N  N   . MET   B 237 ? 0.36555 0.44730 0.46066 0.00820  -0.00029 -0.01521 237 MET   B N   
4630 C  CA  . MET   B 237 ? 0.38346 0.47218 0.47857 0.00590  0.00365  -0.00765 237 MET   B CA  
4631 C  C   . MET   B 237 ? 0.40511 0.49369 0.49860 0.00598  0.00416  -0.00342 237 MET   B C   
4632 O  O   . MET   B 237 ? 0.37551 0.45780 0.47042 0.00452  -0.00124 -0.00233 237 MET   B O   
4633 C  CB  . MET   B 237 ? 0.37053 0.46081 0.46978 0.00124  0.00005  -0.00169 237 MET   B CB  
4634 C  CG  . MET   B 237 ? 0.40396 0.49294 0.50433 0.00105  -0.00186 -0.00588 237 MET   B CG  
4635 S  SD  . MET   B 237 ? 0.41281 0.50949 0.50974 0.00470  0.00650  -0.00971 237 MET   B SD  
4636 C  CE  . MET   B 237 ? 0.35063 0.45751 0.44890 0.00263  0.01049  -0.00087 237 MET   B CE  
4637 N  N   . LEU   B 238 ? 0.34071 0.43514 0.43030 0.00825  0.01000  -0.00150 238 LEU   B N   
4638 C  CA  . LEU   B 238 ? 0.35791 0.45330 0.44486 0.00882  0.01059  0.00332  238 LEU   B CA  
4639 C  C   . LEU   B 238 ? 0.35198 0.45387 0.44223 0.00498  0.00954  0.01277  238 LEU   B C   
4640 O  O   . LEU   B 238 ? 0.35028 0.45993 0.44219 0.00416  0.01210  0.01598  238 LEU   B O   
4641 C  CB  . LEU   B 238 ? 0.34665 0.44537 0.42681 0.01342  0.01617  0.00234  238 LEU   B CB  
4642 C  CG  . LEU   B 238 ? 0.38043 0.47373 0.45796 0.01603  0.01663  -0.00545 238 LEU   B CG  
4643 C  CD1 . LEU   B 238 ? 0.35834 0.45258 0.42817 0.02012  0.02029  -0.00560 238 LEU   B CD1 
4644 C  CD2 . LEU   B 238 ? 0.38586 0.47244 0.46528 0.01561  0.01224  -0.00843 238 LEU   B CD2 
4645 N  N   . PRO   B 239 ? 0.35628 0.45598 0.44825 0.00206  0.00536  0.01804  239 PRO   B N   
4646 C  CA  . PRO   B 239 ? 0.39901 0.50685 0.49530 -0.00280 0.00394  0.02868  239 PRO   B CA  
4647 C  C   . PRO   B 239 ? 0.42469 0.54641 0.51737 0.00054  0.01123  0.03434  239 PRO   B C   
4648 O  O   . PRO   B 239 ? 0.35818 0.48020 0.44369 0.00655  0.01588  0.03050  239 PRO   B O   
4649 C  CB  . PRO   B 239 ? 0.41465 0.51574 0.51241 -0.00637 -0.00252 0.03279  239 PRO   B CB  
4650 C  CG  . PRO   B 239 ? 0.40412 0.49449 0.49779 -0.00228 -0.00361 0.02396  239 PRO   B CG  
4651 C  CD  . PRO   B 239 ? 0.38064 0.46992 0.47199 0.00220  0.00040  0.01469  239 PRO   B CD  
4652 N  N   . GLY   B 240 ? 0.37426 0.50783 0.47177 -0.00304 0.01168  0.04361  240 GLY   B N   
4653 C  CA  . GLY   B 240 ? 0.35298 0.50214 0.44708 0.00123  0.01858  0.04956  240 GLY   B CA  
4654 C  C   . GLY   B 240 ? 0.38548 0.53748 0.47377 0.00434  0.02033  0.05335  240 GLY   B C   
4655 O  O   . GLY   B 240 ? 0.37673 0.52361 0.46703 0.00006  0.01545  0.05699  240 GLY   B O   
4656 N  N   . LEU   B 241 ? 0.37726 0.53752 0.45755 0.01230  0.02692  0.05284  241 LEU   B N   
4657 C  CA  . LEU   B 241 ? 0.37674 0.53942 0.44935 0.01690  0.02882  0.05541  241 LEU   B CA  
4658 C  C   . LEU   B 241 ? 0.42402 0.59949 0.50146 0.01201  0.02765  0.06860  241 LEU   B C   
4659 O  O   . LEU   B 241 ? 0.40487 0.57717 0.47942 0.01144  0.02561  0.07132  241 LEU   B O   
4660 C  CB  . LEU   B 241 ? 0.39522 0.56474 0.45730 0.02733  0.03534  0.05263  241 LEU   B CB  
4661 C  CG  . LEU   B 241 ? 0.44566 0.61471 0.49659 0.03448  0.03714  0.05223  241 LEU   B CG  
4662 C  CD1 . LEU   B 241 ? 0.42190 0.57088 0.46961 0.03384  0.03280  0.04262  241 LEU   B CD1 
4663 C  CD2 . LEU   B 241 ? 0.48326 0.66006 0.52386 0.04533  0.04273  0.05004  241 LEU   B CD2 
4664 N  N   . LEU   B 242 ? 0.42968 0.62064 0.51473 0.00816  0.02871  0.07773  242 LEU   B N   
4665 C  CA  . LEU   B 242 ? 0.46713 0.67253 0.55866 0.00183  0.02700  0.09228  242 LEU   B CA  
4666 C  C   . LEU   B 242 ? 0.40858 0.60657 0.51190 -0.01010 0.01833  0.09622  242 LEU   B C   
4667 O  O   . LEU   B 242 ? 0.50588 0.69551 0.61308 -0.01219 0.01591  0.08982  242 LEU   B O   
4668 C  CB  . LEU   B 242 ? 0.49786 0.72886 0.58995 0.00602  0.03392  0.10150  242 LEU   B CB  
4669 C  CG  . LEU   B 242 ? 0.50027 0.73759 0.57870 0.01945  0.04156  0.09713  242 LEU   B CG  
4670 C  CD1 . LEU   B 242 ? 0.52615 0.79084 0.60438 0.02562  0.04867  0.10597  242 LEU   B CD1 
4671 C  CD2 . LEU   B 242 ? 0.50362 0.73717 0.57536 0.02077  0.04049  0.09931  242 LEU   B CD2 
4672 N  N   . GLU   B 243 ? 0.49337 0.69374 0.60172 -0.01782 0.01296  0.10690  243 GLU   B N   
4673 C  CA  . GLU   B 243 ? 0.61039 0.79848 0.72797 -0.02863 0.00258  0.10910  243 GLU   B CA  
4674 C  C   . GLU   B 243 ? 0.67830 0.87819 0.80521 -0.03385 0.00180  0.11544  243 GLU   B C   
4675 O  O   . GLU   B 243 ? 0.71007 0.93061 0.84292 -0.03799 0.00313  0.12971  243 GLU   B O   
4676 C  CB  . GLU   B 243 ? 0.59218 0.77893 0.71314 -0.03667 -0.00454 0.12022  243 GLU   B CB  
4677 C  CG  . GLU   B 243 ? 0.68628 0.85292 0.81368 -0.04616 -0.01737 0.11917  243 GLU   B CG  
4678 C  CD  . GLU   B 243 ? 0.81418 0.97776 0.94510 -0.05520 -0.02624 0.13126  243 GLU   B CD  
4679 O  OE1 . GLU   B 243 ? 0.72179 0.90175 0.85141 -0.05520 -0.02195 0.14225  243 GLU   B OE1 
4680 O  OE2 . GLU   B 243 ? 0.92040 1.06429 1.05450 -0.06174 -0.03797 0.12938  243 GLU   B OE2 
4681 N  N   . GLU   B 253 ? 0.71969 0.97091 0.75950 0.07610  0.06520  0.05911  253 GLU   B N   
4682 C  CA  . GLU   B 253 ? 0.89379 1.15309 0.91992 0.08904  0.06871  0.05982  253 GLU   B CA  
4683 C  C   . GLU   B 253 ? 0.81913 1.06896 0.84152 0.08621  0.06646  0.05976  253 GLU   B C   
4684 O  O   . GLU   B 253 ? 0.71228 0.93974 0.72702 0.08688  0.06277  0.05007  253 GLU   B O   
4685 C  CB  . GLU   B 253 ? 0.95390 1.24447 0.98376 0.09408  0.07435  0.07165  253 GLU   B CB  
4686 C  CG  . GLU   B 253 ? 0.97930 1.28811 1.02462 0.08225  0.07456  0.08579  253 GLU   B CG  
4687 C  CD  . GLU   B 253 ? 0.97336 1.27655 1.03483 0.06730  0.07014  0.08788  253 GLU   B CD  
4688 O  OE1 . GLU   B 253 ? 0.96369 1.24564 1.02443 0.06458  0.06669  0.07751  253 GLU   B OE1 
4689 O  OE2 . GLU   B 253 ? 1.04887 1.36905 1.12344 0.05823  0.06961  0.10033  253 GLU   B OE2 
4690 N  N   . ASN   B 254 ? 0.74679 1.01397 0.77486 0.08269  0.06829  0.07110  254 ASN   B N   
4691 C  CA  . ASN   B 254 ? 0.78200 1.04036 0.81011 0.07683  0.06524  0.07260  254 ASN   B CA  
4692 C  C   . ASN   B 254 ? 0.70060 0.94650 0.74251 0.06160  0.05969  0.07284  254 ASN   B C   
4693 O  O   . ASN   B 254 ? 0.64004 0.87806 0.68362 0.05569  0.05630  0.07439  254 ASN   B O   
4694 C  CB  . ASN   B 254 ? 0.80558 1.08773 0.83432 0.07852  0.06887  0.08563  254 ASN   B CB  
4695 C  CG  . ASN   B 254 ? 0.92595 1.21746 0.93773 0.09524  0.07364  0.08394  254 ASN   B CG  
4696 O  OD1 . ASN   B 254 ? 0.91892 1.19545 0.91762 0.10135  0.07187  0.07677  254 ASN   B OD1 
4697 N  ND2 . ASN   B 254 ? 0.87952 1.19595 0.89085 0.10344  0.07930  0.09030  254 ASN   B ND2 
4698 N  N   . SER   B 255 ? 0.63277 0.87572 0.68347 0.05604  0.05826  0.07068  255 SER   B N   
4699 C  CA  . SER   B 255 ? 0.60586 0.83826 0.66888 0.04289  0.05268  0.07092  255 SER   B CA  
4700 C  C   . SER   B 255 ? 0.57391 0.78118 0.63340 0.04155  0.04878  0.05812  255 SER   B C   
4701 O  O   . SER   B 255 ? 0.47882 0.67568 0.54664 0.03232  0.04389  0.05669  255 SER   B O   
4702 C  CB  . SER   B 255 ? 0.65804 0.90197 0.73284 0.03718  0.05262  0.07633  255 SER   B CB  
4703 O  OG  . SER   B 255 ? 0.78171 1.01971 0.85280 0.04228  0.05411  0.06775  255 SER   B OG  
4704 N  N   . ALA   B 256 ? 0.49806 0.69578 0.54547 0.05062  0.05031  0.04907  256 ALA   B N   
4705 C  CA  . ALA   B 256 ? 0.38599 0.56233 0.43125 0.04840  0.04644  0.03854  256 ALA   B CA  
4706 C  C   . ALA   B 256 ? 0.44358 0.61007 0.47425 0.05797  0.04684  0.03134  256 ALA   B C   
4707 O  O   . ALA   B 256 ? 0.46728 0.64162 0.48847 0.06775  0.05013  0.03222  256 ALA   B O   
4708 C  CB  . ALA   B 256 ? 0.40772 0.57926 0.45872 0.04476  0.04550  0.03396  256 ALA   B CB  
4709 N  N   . ILE   B 257 ? 0.40444 0.55347 0.43310 0.05540  0.04283  0.02412  257 ILE   B N   
4710 C  CA  . ILE   B 257 ? 0.40775 0.54448 0.42333 0.06298  0.04147  0.01664  257 ILE   B CA  
4711 C  C   . ILE   B 257 ? 0.38802 0.51788 0.40253 0.06382  0.04090  0.01064  257 ILE   B C   
4712 O  O   . ILE   B 257 ? 0.38730 0.51252 0.41082 0.05622  0.03926  0.00843  257 ILE   B O   
4713 C  CB  . ILE   B 257 ? 0.48809 0.61053 0.50290 0.05935  0.03699  0.01237  257 ILE   B CB  
4714 C  CG1 . ILE   B 257 ? 0.45489 0.58277 0.47242 0.05674  0.03669  0.01860  257 ILE   B CG1 
4715 C  CG2 . ILE   B 257 ? 0.42212 0.53191 0.42304 0.06686  0.03450  0.00570  257 ILE   B CG2 
4716 C  CD1 . ILE   B 257 ? 0.48523 0.62395 0.49368 0.06471  0.03982  0.02389  257 ILE   B CD1 
4717 N  N   . PHE   B 258 ? 0.38999 0.51781 0.39242 0.07345  0.04153  0.00756  258 PHE   B N   
4718 C  CA  . PHE   B 258 ? 0.37833 0.49740 0.37787 0.07466  0.03991  0.00191  258 PHE   B CA  
4719 C  C   . PHE   B 258 ? 0.42339 0.52326 0.41352 0.07632  0.03448  -0.00541 258 PHE   B C   
4720 O  O   . PHE   B 258 ? 0.41214 0.50608 0.39326 0.08094  0.03236  -0.00677 258 PHE   B O   
4721 C  CB  . PHE   B 258 ? 0.46631 0.59402 0.45839 0.08439  0.04281  0.00306  258 PHE   B CB  
4722 C  CG  . PHE   B 258 ? 0.42641 0.57531 0.42822 0.08285  0.04795  0.01134  258 PHE   B CG  
4723 C  CD1 . PHE   B 258 ? 0.43867 0.59180 0.45262 0.07487  0.04854  0.01308  258 PHE   B CD1 
4724 C  CD2 . PHE   B 258 ? 0.58131 0.74632 0.57928 0.08993  0.05181  0.01761  258 PHE   B CD2 
4725 C  CE1 . PHE   B 258 ? 0.47860 0.65083 0.50208 0.07258  0.05213  0.02130  258 PHE   B CE1 
4726 C  CE2 . PHE   B 258 ? 0.60306 0.78934 0.61101 0.08773  0.05608  0.02654  258 PHE   B CE2 
4727 C  CZ  . PHE   B 258 ? 0.46024 0.64933 0.48113 0.07867  0.05581  0.02837  258 PHE   B CZ  
4728 N  N   . MET   B 259 ? 0.37726 0.46802 0.36877 0.07294  0.03192  -0.00961 259 MET   B N   
4729 C  CA  . MET   B 259 ? 0.44229 0.51575 0.42810 0.07150  0.02593  -0.01518 259 MET   B CA  
4730 C  C   . MET   B 259 ? 0.47125 0.53406 0.43996 0.08187  0.02212  -0.01868 259 MET   B C   
4731 O  O   . MET   B 259 ? 0.51467 0.56323 0.47683 0.08169  0.01628  -0.02226 259 MET   B O   
4732 C  CB  . MET   B 259 ? 0.38551 0.45458 0.37717 0.06531  0.02447  -0.01728 259 MET   B CB  
4733 C  CG  . MET   B 259 ? 0.38420 0.45917 0.39105 0.05502  0.02616  -0.01590 259 MET   B CG  
4734 S  SD  . MET   B 259 ? 0.37168 0.44034 0.38221 0.04979  0.02276  -0.01733 259 MET   B SD  
4735 C  CE  . MET   B 259 ? 0.40143 0.45394 0.40443 0.04896  0.01589  -0.02180 259 MET   B CE  
4736 N  N   . ASP   B 260 ? 0.46366 0.53331 0.42494 0.09118  0.02482  -0.01766 260 ASP   B N   
4737 C  CA  . ASP   B 260 ? 0.60227 0.66301 0.54531 0.10380  0.02131  -0.02130 260 ASP   B CA  
4738 C  C   . ASP   B 260 ? 0.54982 0.61849 0.48483 0.11249  0.02379  -0.01912 260 ASP   B C   
4739 O  O   . ASP   B 260 ? 0.57502 0.63771 0.49333 0.12494  0.02117  -0.02236 260 ASP   B O   
4740 C  CB  . ASP   B 260 ? 0.58919 0.65402 0.52746 0.11105  0.02282  -0.02178 260 ASP   B CB  
4741 C  CG  . ASP   B 260 ? 0.55904 0.64778 0.50805 0.11086  0.03124  -0.01516 260 ASP   B CG  
4742 O  OD1 . ASP   B 260 ? 0.54664 0.64284 0.51065 0.10074  0.03401  -0.01215 260 ASP   B OD1 
4743 O  OD2 . ASP   B 260 ? 0.64295 0.74396 0.58548 0.12075  0.03486  -0.01243 260 ASP   B OD2 
4744 N  N   . ASP   B 261 ? 0.50755 0.59027 0.45318 0.10712  0.02867  -0.01340 261 ASP   B N   
4745 C  CA  . ASP   B 261 ? 0.51606 0.60881 0.45467 0.11487  0.03154  -0.00991 261 ASP   B CA  
4746 C  C   . ASP   B 261 ? 0.51641 0.59257 0.43936 0.12147  0.02536  -0.01522 261 ASP   B C   
4747 O  O   . ASP   B 261 ? 0.49747 0.55703 0.42110 0.11510  0.01933  -0.01933 261 ASP   B O   
4748 C  CB  . ASP   B 261 ? 0.52687 0.63372 0.48042 0.10543  0.03584  -0.00263 261 ASP   B CB  
4749 C  CG  . ASP   B 261 ? 0.51895 0.64855 0.48175 0.10508  0.04266  0.00521  261 ASP   B CG  
4750 O  OD1 . ASP   B 261 ? 0.54426 0.68199 0.49924 0.11524  0.04517  0.00554  261 ASP   B OD1 
4751 O  OD2 . ASP   B 261 ? 0.44554 0.58470 0.42282 0.09518  0.04487  0.01112  261 ASP   B OD2 
4752 N  N   . SER   B 262 ? 0.48556 0.56711 0.39421 0.13461  0.02666  -0.01489 262 SER   B N   
4753 C  CA  . SER   B 262 ? 0.54745 0.61360 0.44019 0.14156  0.02051  -0.01976 262 SER   B CA  
4754 C  C   . SER   B 262 ? 0.55179 0.62126 0.45128 0.13444  0.02132  -0.01594 262 SER   B C   
4755 O  O   . SER   B 262 ? 0.49339 0.57872 0.40798 0.12611  0.02699  -0.00889 262 SER   B O   
4756 C  CB  . SER   B 262 ? 0.62094 0.69305 0.49471 0.15954  0.02183  -0.02080 262 SER   B CB  
4757 O  OG  . SER   B 262 ? 0.58446 0.68158 0.46373 0.16108  0.03022  -0.01224 262 SER   B OG  
4758 N  N   . GLU   B 263 ? 0.53189 0.58547 0.41902 0.13831  0.01478  -0.02053 263 GLU   B N   
4759 C  CA  . GLU   B 263 ? 0.54975 0.60529 0.44231 0.13217  0.01487  -0.01724 263 GLU   B CA  
4760 C  C   . GLU   B 263 ? 0.53017 0.60865 0.42390 0.13629  0.02273  -0.00897 263 GLU   B C   
4761 O  O   . GLU   B 263 ? 0.51397 0.60218 0.42136 0.12668  0.02580  -0.00273 263 GLU   B O   
4762 C  CB  . GLU   B 263 ? 0.58486 0.61954 0.46237 0.13688  0.00599  -0.02363 263 GLU   B CB  
4763 C  CG  . GLU   B 263 ? 0.60576 0.61963 0.48571 0.12962  -0.00227 -0.02974 263 GLU   B CG  
4764 C  CD  . GLU   B 263 ? 0.82560 0.81972 0.69799 0.12818  -0.01187 -0.03423 263 GLU   B CD  
4765 O  OE1 . GLU   B 263 ? 0.85090 0.82606 0.70837 0.13439  -0.02052 -0.04038 263 GLU   B OE1 
4766 O  OE2 . GLU   B 263 ? 0.77042 0.76733 0.65151 0.12096  -0.01150 -0.03156 263 GLU   B OE2 
4767 N  N   . SER   B 264 ? 0.54451 0.63311 0.42450 0.15050  0.02598  -0.00818 264 SER   B N   
4768 C  CA  . SER   B 264 ? 0.56216 0.67563 0.44446 0.15356  0.03369  0.00135  264 SER   B CA  
4769 C  C   . SER   B 264 ? 0.52137 0.65501 0.42362 0.14374  0.04052  0.00986  264 SER   B C   
4770 O  O   . SER   B 264 ? 0.55067 0.70035 0.46289 0.13756  0.04465  0.01905  264 SER   B O   
4771 C  CB  . SER   B 264 ? 0.64504 0.76775 0.50736 0.17249  0.03604  0.00069  264 SER   B CB  
4772 O  OG  . SER   B 264 ? 0.68443 0.81522 0.54622 0.17865  0.03908  -0.00006 264 SER   B OG  
4773 N  N   . ASP   B 265 ? 0.52660 0.65872 0.43466 0.14174  0.04092  0.00724  265 ASP   B N   
4774 C  CA  . ASP   B 265 ? 0.49809 0.64688 0.42502 0.13182  0.04612  0.01457  265 ASP   B CA  
4775 C  C   . ASP   B 265 ? 0.53852 0.68243 0.48195 0.11579  0.04426  0.01714  265 ASP   B C   
4776 O  O   . ASP   B 265 ? 0.42594 0.58552 0.38227 0.10817  0.04782  0.02612  265 ASP   B O   
4777 C  CB  . ASP   B 265 ? 0.53314 0.67752 0.46228 0.13231  0.04568  0.01002  265 ASP   B CB  
4778 C  CG  . ASP   B 265 ? 0.70111 0.85767 0.61829 0.14756  0.04919  0.01014  265 ASP   B CG  
4779 O  OD1 . ASP   B 265 ? 0.79501 0.93981 0.70518 0.15283  0.04608  0.00312  265 ASP   B OD1 
4780 O  OD2 . ASP   B 265 ? 0.63374 0.81181 0.54830 0.15448  0.05473  0.01744  265 ASP   B OD2 
4781 N  N   . VAL   B 266 ? 0.45017 0.57241 0.39352 0.11055  0.03806  0.00947  266 VAL   B N   
4782 C  CA  . VAL   B 266 ? 0.45903 0.57596 0.41620 0.09736  0.03576  0.01079  266 VAL   B CA  
4783 C  C   . VAL   B 266 ? 0.46607 0.59026 0.42314 0.09643  0.03656  0.01714  266 VAL   B C   
4784 O  O   . VAL   B 266 ? 0.42834 0.56042 0.39858 0.08707  0.03766  0.02367  266 VAL   B O   
4785 C  CB  . VAL   B 266 ? 0.44498 0.53953 0.40012 0.09390  0.02893  0.00186  266 VAL   B CB  
4786 C  CG1 . VAL   B 266 ? 0.46205 0.55186 0.42945 0.08256  0.02624  0.00290  266 VAL   B CG1 
4787 C  CG2 . VAL   B 266 ? 0.43146 0.51973 0.38990 0.09180  0.02793  -0.00290 266 VAL   B CG2 
4788 N  N   . ASN   B 267 ? 0.46439 0.58468 0.40583 0.10616  0.03515  0.01524  267 ASN   B N   
4789 C  CA  . ASN   B 267 ? 0.48343 0.60941 0.42392 0.10516  0.03541  0.02116  267 ASN   B CA  
4790 C  C   . ASN   B 267 ? 0.46928 0.61983 0.41785 0.10311  0.04172  0.03313  267 ASN   B C   
4791 O  O   . ASN   B 267 ? 0.44563 0.60137 0.40474 0.09392  0.04141  0.04016  267 ASN   B O   
4792 C  CB  . ASN   B 267 ? 0.45240 0.57126 0.37280 0.11762  0.03304  0.01709  267 ASN   B CB  
4793 C  CG  . ASN   B 267 ? 0.53228 0.62630 0.44710 0.11642  0.02505  0.00732  267 ASN   B CG  
4794 O  OD1 . ASN   B 267 ? 0.48935 0.57428 0.41660 0.10556  0.02198  0.00506  267 ASN   B OD1 
4795 N  ND2 . ASN   B 267 ? 0.57440 0.65785 0.47044 0.12768  0.02120  0.00175  267 ASN   B ND2 
4796 N  N   . ARG   B 268 ? 0.51930 0.68530 0.46338 0.11146  0.04689  0.03593  268 ARG   B N   
4797 C  CA  . ARG   B 268 ? 0.48462 0.67708 0.43642 0.11008  0.05301  0.04841  268 ARG   B CA  
4798 C  C   . ARG   B 268 ? 0.49228 0.68933 0.46471 0.09514  0.05283  0.05409  268 ARG   B C   
4799 O  O   . ARG   B 268 ? 0.49396 0.70370 0.47600 0.08749  0.05370  0.06473  268 ARG   B O   
4800 C  CB  . ARG   B 268 ? 0.54508 0.75210 0.48765 0.12316  0.05809  0.04859  268 ARG   B CB  
4801 C  CG  . ARG   B 268 ? 0.61709 0.85347 0.56993 0.12119  0.06449  0.06156  268 ARG   B CG  
4802 C  CD  . ARG   B 268 ? 0.59749 0.84987 0.53988 0.13643  0.06971  0.06126  268 ARG   B CD  
4803 N  NE  . ARG   B 268 ? 0.55556 0.79240 0.49528 0.13947  0.06731  0.05054  268 ARG   B NE  
4804 C  CZ  . ARG   B 268 ? 0.59483 0.83407 0.54835 0.13138  0.06787  0.05150  268 ARG   B CZ  
4805 N  NH1 . ARG   B 268 ? 0.74322 0.99661 0.71486 0.11862  0.06964  0.06173  268 ARG   B NH1 
4806 N  NH2 . ARG   B 268 ? 0.61299 0.83848 0.56175 0.13564  0.06566  0.04197  268 ARG   B NH2 
4807 N  N   . LYS   B 269 ? 0.44388 0.62972 0.42278 0.09071  0.05089  0.04723  269 LYS   B N   
4808 C  CA  . LYS   B 269 ? 0.42893 0.61828 0.42577 0.07788  0.05021  0.05166  269 LYS   B CA  
4809 C  C   . LYS   B 269 ? 0.48503 0.66187 0.49016 0.06698  0.04490  0.05167  269 LYS   B C   
4810 O  O   . LYS   B 269 ? 0.43132 0.61428 0.44954 0.05690  0.04365  0.05904  269 LYS   B O   
4811 C  CB  . LYS   B 269 ? 0.40825 0.58925 0.40801 0.07728  0.04966  0.04406  269 LYS   B CB  
4812 C  CG  . LYS   B 269 ? 0.54508 0.74057 0.53882 0.08741  0.05474  0.04533  269 LYS   B CG  
4813 C  CD  . LYS   B 269 ? 0.49494 0.67815 0.48900 0.08752  0.05312  0.03654  269 LYS   B CD  
4814 C  CE  . LYS   B 269 ? 0.63229 0.82686 0.62073 0.09730  0.05706  0.03658  269 LYS   B CE  
4815 N  NZ  . LYS   B 269 ? 0.45115 0.63249 0.44195 0.09481  0.05465  0.02886  269 LYS   B NZ  
4816 N  N   . ILE   B 270 ? 0.41079 0.56910 0.40873 0.06872  0.04084  0.04317  270 ILE   B N   
4817 C  CA  . ILE   B 270 ? 0.42210 0.56968 0.42720 0.05981  0.03576  0.04317  270 ILE   B CA  
4818 C  C   . ILE   B 270 ? 0.46221 0.62072 0.46745 0.05817  0.03614  0.05363  270 ILE   B C   
4819 O  O   . ILE   B 270 ? 0.44985 0.60883 0.46594 0.04851  0.03308  0.05946  270 ILE   B O   
4820 C  CB  . ILE   B 270 ? 0.47049 0.59815 0.46807 0.06237  0.03130  0.03274  270 ILE   B CB  
4821 C  CG1 . ILE   B 270 ? 0.41838 0.53480 0.41867 0.06100  0.02974  0.02367  270 ILE   B CG1 
4822 C  CG2 . ILE   B 270 ? 0.40717 0.52664 0.41069 0.05504  0.02632  0.03403  270 ILE   B CG2 
4823 C  CD1 . ILE   B 270 ? 0.44775 0.56408 0.46328 0.05106  0.02858  0.02424  270 ILE   B CD1 
4824 N  N   . LYS   B 271 ? 0.49561 0.66376 0.48833 0.06785  0.03963  0.05674  271 LYS   B N   
4825 C  CA  . LYS   B 271 ? 0.58662 0.76595 0.57851 0.06649  0.04007  0.06728  271 LYS   B CA  
4826 C  C   . LYS   B 271 ? 0.52415 0.72086 0.53025 0.05709  0.04134  0.08016  271 LYS   B C   
4827 O  O   . LYS   B 271 ? 0.49989 0.69812 0.51208 0.04920  0.03807  0.08826  271 LYS   B O   
4828 C  CB  . LYS   B 271 ? 0.58694 0.77742 0.56222 0.08000  0.04456  0.06901  271 LYS   B CB  
4829 C  CG  . LYS   B 271 ? 0.66456 0.86900 0.63775 0.07925  0.04557  0.08098  271 LYS   B CG  
4830 C  CD  . LYS   B 271 ? 0.75289 0.97505 0.71071 0.09335  0.05148  0.08479  271 LYS   B CD  
4831 C  CE  . LYS   B 271 ? 0.91014 1.15139 0.86872 0.09083  0.05334  0.09955  271 LYS   B CE  
4832 N  NZ  . LYS   B 271 ? 0.87410 1.14746 0.83827 0.09142  0.06009  0.11392  271 LYS   B NZ  
4833 N  N   . LYS   B 272 ? 0.47108 0.68004 0.48280 0.05729  0.04512  0.08245  272 LYS   B N   
4834 C  CA  . LYS   B 272 ? 0.52356 0.75032 0.54894 0.04831  0.04585  0.09540  272 LYS   B CA  
4835 C  C   . LYS   B 272 ? 0.47775 0.69288 0.51766 0.03612  0.04029  0.09358  272 LYS   B C   
4836 O  O   . LYS   B 272 ? 0.45803 0.68541 0.50964 0.02775  0.03933  0.10395  272 LYS   B O   
4837 C  CB  . LYS   B 272 ? 0.53357 0.78363 0.55790 0.05541  0.05302  0.10053  272 LYS   B CB  
4838 C  CG  . LYS   B 272 ? 0.77083 1.03917 0.78183 0.06787  0.05900  0.10562  272 LYS   B CG  
4839 C  CD  . LYS   B 272 ? 0.82718 1.12747 0.84374 0.06980  0.06526  0.11856  272 LYS   B CD  
4840 C  CE  . LYS   B 272 ? 0.87769 1.20092 0.89602 0.06727  0.06724  0.13493  272 LYS   B CE  
4841 N  NZ  . LYS   B 272 ? 0.81734 1.14153 0.81823 0.07892  0.06957  0.13335  272 LYS   B NZ  
4842 N  N   . ALA   B 273 ? 0.39474 0.58760 0.43401 0.03519  0.03634  0.08109  273 ALA   B N   
4843 C  CA  . ALA   B 273 ? 0.40976 0.59250 0.46085 0.02605  0.03168  0.07797  273 ALA   B CA  
4844 C  C   . ALA   B 273 ? 0.41686 0.59469 0.47709 0.01522  0.02471  0.08492  273 ALA   B C   
4845 O  O   . ALA   B 273 ? 0.39997 0.57705 0.45683 0.01453  0.02270  0.08963  273 ALA   B O   
4846 C  CB  . ALA   B 273 ? 0.36673 0.52900 0.41432 0.02858  0.02955  0.06329  273 ALA   B CB  
4847 N  N   . TYR   B 274 ? 0.41687 0.58959 0.48787 0.00710  0.02024  0.08485  274 TYR   B N   
4848 C  CA  . TYR   B 274 ? 0.38745 0.55031 0.46670 -0.00296 0.01153  0.08900  274 TYR   B CA  
4849 C  C   . TYR   B 274 ? 0.34865 0.49048 0.42380 -0.00138 0.00698  0.07822  274 TYR   B C   
4850 O  O   . TYR   B 274 ? 0.36229 0.49489 0.43418 0.00346  0.00860  0.06647  274 TYR   B O   
4851 C  CB  . TYR   B 274 ? 0.41920 0.58007 0.50885 -0.00996 0.00765  0.08922  274 TYR   B CB  
4852 C  CG  . TYR   B 274 ? 0.39816 0.54843 0.49609 -0.02032 -0.00275 0.09405  274 TYR   B CG  
4853 C  CD1 . TYR   B 274 ? 0.41114 0.56794 0.51240 -0.02706 -0.00692 0.10756  274 TYR   B CD1 
4854 C  CD2 . TYR   B 274 ? 0.41289 0.54583 0.51435 -0.02285 -0.00904 0.08490  274 TYR   B CD2 
4855 C  CE1 . TYR   B 274 ? 0.42189 0.56629 0.52991 -0.03668 -0.01808 0.11188  274 TYR   B CE1 
4856 C  CE2 . TYR   B 274 ? 0.40837 0.52874 0.51570 -0.03110 -0.01999 0.08808  274 TYR   B CE2 
4857 C  CZ  . TYR   B 274 ? 0.43575 0.56098 0.54644 -0.03832 -0.02498 0.10161  274 TYR   B CZ  
4858 O  OH  . TYR   B 274 ? 0.44380 0.55412 0.55957 -0.04668 -0.03743 0.10484  274 TYR   B OH  
4859 N  N   . CYS   B 275 ? 0.36544 0.50144 0.44009 -0.00475 0.00178  0.08274  275 CYS   B N   
4860 C  CA  . CYS   B 275 ? 0.34595 0.46311 0.41745 -0.00323 -0.00315 0.07333  275 CYS   B CA  
4861 C  C   . CYS   B 275 ? 0.39245 0.50316 0.46803 -0.01075 -0.01170 0.08124  275 CYS   B C   
4862 O  O   . CYS   B 275 ? 0.39954 0.51107 0.46997 -0.00973 -0.01228 0.08587  275 CYS   B O   
4863 C  CB  . CYS   B 275 ? 0.35354 0.47054 0.41385 0.00570  0.00182  0.06799  275 CYS   B CB  
4864 S  SG  . CYS   B 275 ? 0.39109 0.48674 0.44848 0.00814  -0.00374 0.05547  275 CYS   B SG  
4865 N  N   . PRO   B 276 ? 0.36070 0.46487 0.44491 -0.01845 -0.01904 0.08365  276 PRO   B N   
4866 C  CA  . PRO   B 276 ? 0.38980 0.48694 0.47787 -0.02648 -0.02871 0.09255  276 PRO   B CA  
4867 C  C   . PRO   B 276 ? 0.38390 0.46468 0.46705 -0.02358 -0.03373 0.08579  276 PRO   B C   
4868 O  O   . PRO   B 276 ? 0.40006 0.46884 0.48183 -0.01873 -0.03451 0.07276  276 PRO   B O   
4869 C  CB  . PRO   B 276 ? 0.36782 0.45627 0.46438 -0.03321 -0.03652 0.09193  276 PRO   B CB  
4870 C  CG  . PRO   B 276 ? 0.40301 0.48838 0.49860 -0.02684 -0.03159 0.07835  276 PRO   B CG  
4871 C  CD  . PRO   B 276 ? 0.36105 0.46244 0.45112 -0.02007 -0.01987 0.07817  276 PRO   B CD  
4872 N  N   . PRO   B 277 ? 0.39772 0.47874 0.47838 -0.02634 -0.03716 0.09469  277 PRO   B N   
4873 C  CA  . PRO   B 277 ? 0.36626 0.43100 0.44264 -0.02388 -0.04306 0.08873  277 PRO   B CA  
4874 C  C   . PRO   B 277 ? 0.41287 0.45822 0.49422 -0.02659 -0.05351 0.08169  277 PRO   B C   
4875 O  O   . PRO   B 277 ? 0.39253 0.43443 0.48031 -0.03383 -0.06034 0.08704  277 PRO   B O   
4876 C  CB  . PRO   B 277 ? 0.41636 0.48583 0.49107 -0.02900 -0.04648 0.10278  277 PRO   B CB  
4877 C  CG  . PRO   B 277 ? 0.48543 0.57880 0.56167 -0.03152 -0.03888 0.11547  277 PRO   B CG  
4878 C  CD  . PRO   B 277 ? 0.42956 0.52733 0.51166 -0.03205 -0.03593 0.11153  277 PRO   B CD  
4879 N  N   . ASN   B 278 ? 0.35674 0.39023 0.43489 -0.02003 -0.05461 0.06907  278 ASN   B N   
4880 C  CA  . ASN   B 278 ? 0.41915 0.43425 0.49986 -0.01965 -0.06440 0.06077  278 ASN   B CA  
4881 C  C   . ASN   B 278 ? 0.42614 0.43855 0.51173 -0.01987 -0.06545 0.05438  278 ASN   B C   
4882 O  O   . ASN   B 278 ? 0.44502 0.44284 0.53160 -0.01776 -0.07320 0.04617  278 ASN   B O   
4883 C  CB  . ASN   B 278 ? 0.41373 0.41681 0.49602 -0.02667 -0.07684 0.06944  278 ASN   B CB  
4884 C  CG  . ASN   B 278 ? 0.49998 0.50557 0.57741 -0.02741 -0.07682 0.07735  278 ASN   B CG  
4885 O  OD1 . ASN   B 278 ? 0.53535 0.55343 0.61281 -0.03272 -0.07417 0.09048  278 ASN   B OD1 
4886 N  ND2 . ASN   B 278 ? 0.45309 0.44843 0.52634 -0.02179 -0.07947 0.06976  278 ASN   B ND2 
4887 N  N   . VAL   B 279 ? 0.35020 0.37623 0.43784 -0.02070 -0.05754 0.05641  279 VAL   B N   
4888 C  CA  . VAL   B 279 ? 0.35652 0.38103 0.44876 -0.02199 -0.05886 0.05230  279 VAL   B CA  
4889 C  C   . VAL   B 279 ? 0.40031 0.43292 0.49093 -0.01513 -0.04866 0.04259  279 VAL   B C   
4890 O  O   . VAL   B 279 ? 0.37681 0.42314 0.46494 -0.01313 -0.03917 0.04524  279 VAL   B O   
4891 C  CB  . VAL   B 279 ? 0.35977 0.39279 0.45729 -0.03086 -0.06062 0.06524  279 VAL   B CB  
4892 C  CG1 . VAL   B 279 ? 0.41130 0.44402 0.51325 -0.03197 -0.06127 0.06091  279 VAL   B CG1 
4893 C  CG2 . VAL   B 279 ? 0.40534 0.42655 0.50502 -0.03868 -0.07354 0.07433  279 VAL   B CG2 
4894 N  N   . ILE   B 280 ? 0.34779 0.37173 0.43928 -0.01117 -0.05120 0.03147  280 ILE   B N   
4895 C  CA  . ILE   B 280 ? 0.35529 0.38623 0.44597 -0.00571 -0.04281 0.02286  280 ILE   B CA  
4896 C  C   . ILE   B 280 ? 0.37417 0.41032 0.46856 -0.00862 -0.04129 0.02405  280 ILE   B C   
4897 O  O   . ILE   B 280 ? 0.37282 0.41958 0.46656 -0.00639 -0.03269 0.02229  280 ILE   B O   
4898 C  CB  . ILE   B 280 ? 0.36598 0.38783 0.45555 0.00080  -0.04552 0.01075  280 ILE   B CB  
4899 C  CG1 . ILE   B 280 ? 0.43254 0.45462 0.51834 0.00442  -0.04331 0.00943  280 ILE   B CG1 
4900 C  CG2 . ILE   B 280 ? 0.38919 0.41664 0.47960 0.00464  -0.03975 0.00271  280 ILE   B CG2 
4901 C  CD1 . ILE   B 280 ? 0.49895 0.51413 0.58455 0.01080  -0.04640 -0.00117 280 ILE   B CD1 
4902 N  N   . GLU   B 281 ? 0.37687 0.40473 0.47474 -0.01350 -0.05028 0.02691  281 GLU   B N   
4903 C  CA  . GLU   B 281 ? 0.42053 0.45160 0.52189 -0.01617 -0.05026 0.02723  281 GLU   B CA  
4904 C  C   . GLU   B 281 ? 0.42090 0.46896 0.52431 -0.02000 -0.04249 0.03718  281 GLU   B C   
4905 O  O   . GLU   B 281 ? 0.36980 0.42327 0.47418 -0.02462 -0.04323 0.04797  281 GLU   B O   
4906 C  CB  . GLU   B 281 ? 0.47128 0.48835 0.57533 -0.02174 -0.06361 0.03036  281 GLU   B CB  
4907 C  CG  . GLU   B 281 ? 0.72297 0.73897 0.83046 -0.02538 -0.06742 0.03091  281 GLU   B CG  
4908 C  CD  . GLU   B 281 ? 0.88193 0.89395 0.98693 -0.01814 -0.06587 0.01768  281 GLU   B CD  
4909 O  OE1 . GLU   B 281 ? 0.92207 0.93179 1.02336 -0.01050 -0.06283 0.00821  281 GLU   B OE1 
4910 O  OE2 . GLU   B 281 ? 0.93875 0.95072 1.04570 -0.02027 -0.06802 0.01736  281 GLU   B OE2 
4911 N  N   . ASN   B 282 ? 0.37500 0.43248 0.47863 -0.01740 -0.03482 0.03369  282 ASN   B N   
4912 C  CA  . ASN   B 282 ? 0.36056 0.43477 0.46581 -0.01947 -0.02742 0.04196  282 ASN   B CA  
4913 C  C   . ASN   B 282 ? 0.36672 0.45118 0.46718 -0.01585 -0.01952 0.04547  282 ASN   B C   
4914 O  O   . ASN   B 282 ? 0.34512 0.44446 0.44611 -0.01692 -0.01415 0.05403  282 ASN   B O   
4915 C  CB  . ASN   B 282 ? 0.41063 0.48838 0.52228 -0.02850 -0.03372 0.05441  282 ASN   B CB  
4916 C  CG  . ASN   B 282 ? 0.54766 0.64156 0.66279 -0.03016 -0.02767 0.06016  282 ASN   B CG  
4917 O  OD1 . ASN   B 282 ? 0.58504 0.68102 0.69888 -0.02583 -0.02264 0.05261  282 ASN   B OD1 
4918 N  ND2 . ASN   B 282 ? 0.58192 0.68870 0.70176 -0.03643 -0.02810 0.07420  282 ASN   B ND2 
4919 N  N   . ASN   B 283 ? 0.33197 0.40928 0.42741 -0.01123 -0.01920 0.03949  283 ASN   B N   
4920 C  CA  . ASN   B 283 ? 0.31922 0.40354 0.40867 -0.00728 -0.01320 0.04196  283 ASN   B CA  
4921 C  C   . ASN   B 283 ? 0.33381 0.42246 0.41813 -0.00030 -0.00505 0.03414  283 ASN   B C   
4922 O  O   . ASN   B 283 ? 0.29513 0.37541 0.37795 0.00313  -0.00564 0.02440  283 ASN   B O   
4923 C  CB  . ASN   B 283 ? 0.33223 0.40563 0.41901 -0.00648 -0.01837 0.04011  283 ASN   B CB  
4924 C  CG  . ASN   B 283 ? 0.33919 0.41831 0.41895 -0.00247 -0.01345 0.04280  283 ASN   B CG  
4925 O  OD1 . ASN   B 283 ? 0.33434 0.42235 0.40930 0.00229  -0.00589 0.04166  283 ASN   B OD1 
4926 N  ND2 . ASN   B 283 ? 0.33170 0.40408 0.40980 -0.00369 -0.01856 0.04566  283 ASN   B ND2 
4927 N  N   . PRO   B 284 ? 0.34408 0.44540 0.42587 0.00194  0.00181  0.03807  284 PRO   B N   
4928 C  CA  . PRO   B 284 ? 0.32694 0.42963 0.40342 0.00826  0.00789  0.03033  284 PRO   B CA  
4929 C  C   . PRO   B 284 ? 0.33622 0.43357 0.40490 0.01371  0.00924  0.02524  284 PRO   B C   
4930 O  O   . PRO   B 284 ? 0.36203 0.45393 0.42841 0.01687  0.01034  0.01682  284 PRO   B O   
4931 C  CB  . PRO   B 284 ? 0.30332 0.42109 0.37826 0.00994  0.01386  0.03712  284 PRO   B CB  
4932 C  CG  . PRO   B 284 ? 0.36916 0.49489 0.44561 0.00653  0.01239  0.04857  284 PRO   B CG  
4933 C  CD  . PRO   B 284 ? 0.34011 0.45582 0.42339 -0.00066 0.00412  0.05006  284 PRO   B CD  
4934 N  N   . ILE   B 285 ? 0.31121 0.41021 0.37584 0.01449  0.00868  0.03070  285 ILE   B N   
4935 C  CA  . ILE   B 285 ? 0.31314 0.40609 0.36981 0.01955  0.00889  0.02618  285 ILE   B CA  
4936 C  C   . ILE   B 285 ? 0.31691 0.39753 0.37679 0.01844  0.00395  0.01832  285 ILE   B C   
4937 O  O   . ILE   B 285 ? 0.33280 0.40838 0.38907 0.02203  0.00455  0.01112  285 ILE   B O   
4938 C  CB  . ILE   B 285 ? 0.30734 0.40441 0.35950 0.02003  0.00840  0.03422  285 ILE   B CB  
4939 C  CG1 . ILE   B 285 ? 0.34074 0.45369 0.38959 0.02235  0.01411  0.04253  285 ILE   B CG1 
4940 C  CG2 . ILE   B 285 ? 0.31700 0.40664 0.36001 0.02555  0.00781  0.02923  285 ILE   B CG2 
4941 C  CD1 . ILE   B 285 ? 0.36642 0.48295 0.40847 0.02959  0.01983  0.03696  285 ILE   B CD1 
4942 N  N   . TYR   B 286 ? 0.30695 0.38264 0.37328 0.01369  -0.00172 0.02012  286 TYR   B N   
4943 C  CA  . TYR   B 286 ? 0.34769 0.41308 0.41692 0.01400  -0.00645 0.01241  286 TYR   B CA  
4944 C  C   . TYR   B 286 ? 0.34482 0.41038 0.41686 0.01530  -0.00434 0.00474  286 TYR   B C   
4945 O  O   . TYR   B 286 ? 0.32969 0.39158 0.40146 0.01792  -0.00480 -0.00222 286 TYR   B O   
4946 C  CB  . TYR   B 286 ? 0.30269 0.36138 0.37726 0.00956  -0.01395 0.01537  286 TYR   B CB  
4947 C  CG  . TYR   B 286 ? 0.34259 0.39163 0.41907 0.01172  -0.01887 0.00718  286 TYR   B CG  
4948 C  CD1 . TYR   B 286 ? 0.35662 0.40344 0.43733 0.01283  -0.02002 -0.00019 286 TYR   B CD1 
4949 C  CD2 . TYR   B 286 ? 0.37369 0.41733 0.44727 0.01351  -0.02195 0.00673  286 TYR   B CD2 
4950 C  CE1 . TYR   B 286 ? 0.41622 0.45682 0.49848 0.01632  -0.02406 -0.00785 286 TYR   B CE1 
4951 C  CE2 . TYR   B 286 ? 0.38473 0.42135 0.46032 0.01640  -0.02627 -0.00077 286 TYR   B CE2 
4952 C  CZ  . TYR   B 286 ? 0.45541 0.49135 0.53552 0.01793  -0.02714 -0.00778 286 TYR   B CZ  
4953 O  OH  . TYR   B 286 ? 0.55641 0.58800 0.63840 0.02177  -0.03106 -0.01460 286 TYR   B OH  
4954 N  N   . ALA   B 287 ? 0.30282 0.37378 0.37781 0.01331  -0.00203 0.00650  287 ALA   B N   
4955 C  CA  . ALA   B 287 ? 0.28279 0.35458 0.35990 0.01444  0.00009  -0.00007 287 ALA   B CA  
4956 C  C   . ALA   B 287 ? 0.32172 0.39536 0.39345 0.01836  0.00465  -0.00399 287 ALA   B C   
4957 O  O   . ALA   B 287 ? 0.35243 0.42452 0.42557 0.01951  0.00472  -0.01022 287 ALA   B O   
4958 C  CB  . ALA   B 287 ? 0.30580 0.38356 0.38618 0.01165  0.00187  0.00344  287 ALA   B CB  
4959 N  N   . TYR   B 288 ? 0.31917 0.39631 0.38433 0.02062  0.00797  -0.00013 288 TYR   B N   
4960 C  CA  . TYR   B 288 ? 0.33299 0.40895 0.39146 0.02461  0.01050  -0.00394 288 TYR   B CA  
4961 C  C   . TYR   B 288 ? 0.31532 0.38433 0.37306 0.02552  0.00693  -0.00835 288 TYR   B C   
4962 O  O   . TYR   B 288 ? 0.32507 0.39196 0.38207 0.02643  0.00683  -0.01317 288 TYR   B O   
4963 C  CB  . TYR   B 288 ? 0.29346 0.37309 0.34320 0.02847  0.01348  0.00059  288 TYR   B CB  
4964 C  CG  . TYR   B 288 ? 0.32828 0.41731 0.37832 0.02869  0.01759  0.00534  288 TYR   B CG  
4965 C  CD1 . TYR   B 288 ? 0.31480 0.40656 0.37166 0.02548  0.01828  0.00438  288 TYR   B CD1 
4966 C  CD2 . TYR   B 288 ? 0.35388 0.45003 0.39765 0.03230  0.02042  0.01122  288 TYR   B CD2 
4967 C  CE1 . TYR   B 288 ? 0.31714 0.41845 0.37519 0.02534  0.02161  0.00940  288 TYR   B CE1 
4968 C  CE2 . TYR   B 288 ? 0.33340 0.44083 0.37825 0.03288  0.02431  0.01645  288 TYR   B CE2 
4969 C  CZ  . TYR   B 288 ? 0.36828 0.47776 0.42075 0.02899  0.02463  0.01546  288 TYR   B CZ  
4970 O  OH  . TYR   B 288 ? 0.40954 0.53111 0.46390 0.02921  0.02803  0.02141  288 TYR   B OH  
4971 N  N   . ALA   B 289 ? 0.33410 0.40002 0.39183 0.02511  0.00370  -0.00596 289 ALA   B N   
4972 C  CA  . ALA   B 289 ? 0.32990 0.38979 0.38765 0.02608  -0.00013 -0.01001 289 ALA   B CA  
4973 C  C   . ALA   B 289 ? 0.38720 0.44696 0.45278 0.02479  -0.00195 -0.01561 289 ALA   B C   
4974 O  O   . ALA   B 289 ? 0.35615 0.41536 0.42237 0.02569  -0.00277 -0.01976 289 ALA   B O   
4975 C  CB  . ALA   B 289 ? 0.31885 0.37525 0.37591 0.02563  -0.00382 -0.00623 289 ALA   B CB  
4976 N  N   . LYS   B 290 ? 0.32517 0.38593 0.39663 0.02286  -0.00311 -0.01548 290 LYS   B N   
4977 C  CA  . LYS   B 290 ? 0.32427 0.38509 0.40201 0.02327  -0.00549 -0.02100 290 LYS   B CA  
4978 C  C   . LYS   B 290 ? 0.36232 0.42890 0.44183 0.02334  -0.00182 -0.02440 290 LYS   B C   
4979 O  O   . LYS   B 290 ? 0.33105 0.40041 0.41394 0.02453  -0.00248 -0.02870 290 LYS   B O   
4980 C  CB  . LYS   B 290 ? 0.36860 0.42622 0.45044 0.02205  -0.00951 -0.02040 290 LYS   B CB  
4981 C  CG  . LYS   B 290 ? 0.46145 0.52132 0.54799 0.02339  -0.01016 -0.02607 290 LYS   B CG  
4982 C  CD  . LYS   B 290 ? 0.42771 0.48204 0.51655 0.02251  -0.01534 -0.02572 290 LYS   B CD  
4983 C  CE  . LYS   B 290 ? 0.53108 0.58380 0.62289 0.02681  -0.01947 -0.03295 290 LYS   B CE  
4984 N  NZ  . LYS   B 290 ? 0.67666 0.72128 0.76904 0.02615  -0.02586 -0.03284 290 LYS   B NZ  
4985 N  N   . SER   B 291 ? 0.33105 0.40059 0.40866 0.02210  0.00196  -0.02203 291 SER   B N   
4986 C  CA  . SER   B 291 ? 0.28939 0.36390 0.36885 0.02179  0.00493  -0.02477 291 SER   B CA  
4987 C  C   . SER   B 291 ? 0.33123 0.40706 0.40601 0.02205  0.00792  -0.02459 291 SER   B C   
4988 O  O   . SER   B 291 ? 0.34718 0.42696 0.42371 0.02138  0.00965  -0.02675 291 SER   B O   
4989 C  CB  . SER   B 291 ? 0.32759 0.40408 0.40852 0.02020  0.00626  -0.02272 291 SER   B CB  
4990 O  OG  . SER   B 291 ? 0.36447 0.43765 0.44938 0.01981  0.00179  -0.02351 291 SER   B OG  
4991 N  N   . ILE   B 292 ? 0.33506 0.40745 0.40315 0.02325  0.00828  -0.02179 292 ILE   B N   
4992 C  CA  . ILE   B 292 ? 0.31207 0.38273 0.37386 0.02433  0.00943  -0.02211 292 ILE   B CA  
4993 C  C   . ILE   B 292 ? 0.37177 0.43730 0.43051 0.02516  0.00589  -0.02336 292 ILE   B C   
4994 O  O   . ILE   B 292 ? 0.37288 0.43787 0.43207 0.02395  0.00439  -0.02529 292 ILE   B O   
4995 C  CB  . ILE   B 292 ? 0.34637 0.41693 0.40088 0.02667  0.01219  -0.01864 292 ILE   B CB  
4996 C  CG1 . ILE   B 292 ? 0.29429 0.37082 0.35256 0.02529  0.01546  -0.01747 292 ILE   B CG1 
4997 C  CG2 . ILE   B 292 ? 0.34657 0.41203 0.39255 0.02910  0.01145  -0.01983 292 ILE   B CG2 
4998 C  CD1 . ILE   B 292 ? 0.33727 0.41687 0.38998 0.02792  0.01842  -0.01305 292 ILE   B CD1 
4999 N  N   . ILE   B 293 ? 0.31109 0.37305 0.36690 0.02675  0.00404  -0.02167 293 ILE   B N   
5000 C  CA  . ILE   B 293 ? 0.34454 0.40044 0.39525 0.02815  0.00039  -0.02247 293 ILE   B CA  
5001 C  C   . ILE   B 293 ? 0.34301 0.40018 0.40140 0.02620  -0.00304 -0.02515 293 ILE   B C   
5002 O  O   . ILE   B 293 ? 0.35554 0.41150 0.41399 0.02509  -0.00564 -0.02662 293 ILE   B O   
5003 C  CB  . ILE   B 293 ? 0.35570 0.40834 0.39971 0.03100  -0.00004 -0.01926 293 ILE   B CB  
5004 C  CG1 . ILE   B 293 ? 0.29418 0.34829 0.33022 0.03405  0.00369  -0.01644 293 ILE   B CG1 
5005 C  CG2 . ILE   B 293 ? 0.36288 0.40815 0.40071 0.03290  -0.00462 -0.02040 293 ILE   B CG2 
5006 C  CD1 . ILE   B 293 ? 0.31588 0.37171 0.34720 0.03650  0.00470  -0.01156 293 ILE   B CD1 
5007 N  N   . PHE   B 294 ? 0.30588 0.36593 0.37107 0.02582  -0.00362 -0.02563 294 PHE   B N   
5008 C  CA  . PHE   B 294 ? 0.31844 0.38099 0.39055 0.02549  -0.00686 -0.02840 294 PHE   B CA  
5009 C  C   . PHE   B 294 ? 0.35823 0.42806 0.43593 0.02370  -0.00607 -0.03050 294 PHE   B C   
5010 O  O   . PHE   B 294 ? 0.39644 0.46830 0.47697 0.02289  -0.00901 -0.03124 294 PHE   B O   
5011 C  CB  . PHE   B 294 ? 0.30003 0.36348 0.37750 0.02647  -0.00818 -0.02924 294 PHE   B CB  
5012 C  CG  . PHE   B 294 ? 0.39318 0.45916 0.47667 0.02783  -0.01186 -0.03223 294 PHE   B CG  
5013 C  CD1 . PHE   B 294 ? 0.36867 0.42953 0.45022 0.02892  -0.01589 -0.03161 294 PHE   B CD1 
5014 C  CD2 . PHE   B 294 ? 0.41452 0.48932 0.50525 0.02851  -0.01113 -0.03551 294 PHE   B CD2 
5015 C  CE1 . PHE   B 294 ? 0.36770 0.43229 0.45564 0.03075  -0.01969 -0.03448 294 PHE   B CE1 
5016 C  CE2 . PHE   B 294 ? 0.35509 0.43496 0.45181 0.03086  -0.01418 -0.03824 294 PHE   B CE2 
5017 C  CZ  . PHE   B 294 ? 0.36090 0.43571 0.45664 0.03194  -0.01861 -0.03775 294 PHE   B CZ  
5018 N  N   . PRO   B 295 ? 0.36931 0.44444 0.44946 0.02276  -0.00254 -0.03102 295 PRO   B N   
5019 C  CA  . PRO   B 295 ? 0.33534 0.41858 0.42035 0.02072  -0.00170 -0.03197 295 PRO   B CA  
5020 C  C   . PRO   B 295 ? 0.32570 0.40532 0.40599 0.01815  -0.00316 -0.03005 295 PRO   B C   
5021 O  O   . PRO   B 295 ? 0.36221 0.44768 0.44714 0.01549  -0.00491 -0.02958 295 PRO   B O   
5022 C  CB  . PRO   B 295 ? 0.38487 0.47232 0.47102 0.02056  0.00238  -0.03246 295 PRO   B CB  
5023 C  CG  . PRO   B 295 ? 0.35802 0.43981 0.44124 0.02223  0.00296  -0.03177 295 PRO   B CG  
5024 C  CD  . PRO   B 295 ? 0.34039 0.41467 0.41879 0.02316  0.00050  -0.02997 295 PRO   B CD  
5025 N  N   . SER   B 296 ? 0.30867 0.37900 0.37963 0.01910  -0.00313 -0.02866 296 SER   B N   
5026 C  CA  . SER   B 296 ? 0.35061 0.41432 0.41496 0.01763  -0.00609 -0.02750 296 SER   B CA  
5027 C  C   . SER   B 296 ? 0.42836 0.48773 0.49207 0.01685  -0.01188 -0.02735 296 SER   B C   
5028 O  O   . SER   B 296 ? 0.39918 0.45668 0.46251 0.01356  -0.01592 -0.02625 296 SER   B O   
5029 C  CB  . SER   B 296 ? 0.35310 0.40810 0.40617 0.02102  -0.00479 -0.02675 296 SER   B CB  
5030 O  OG  . SER   B 296 ? 0.41906 0.47907 0.47377 0.02091  -0.00001 -0.02647 296 SER   B OG  
5031 N  N   . TYR   B 297 ? 0.34738 0.40505 0.41138 0.01926  -0.01310 -0.02800 297 TYR   B N   
5032 C  CA  . TYR   B 297 ? 0.35540 0.40827 0.41810 0.01883  -0.01898 -0.02788 297 TYR   B CA  
5033 C  C   . TYR   B 297 ? 0.37052 0.43261 0.44430 0.01792  -0.02043 -0.02864 297 TYR   B C   
5034 O  O   . TYR   B 297 ? 0.35832 0.41805 0.43266 0.01725  -0.02561 -0.02832 297 TYR   B O   
5035 C  CB  . TYR   B 297 ? 0.39654 0.43916 0.44886 0.02303  -0.02019 -0.02775 297 TYR   B CB  
5036 C  CG  . TYR   B 297 ? 0.40847 0.44218 0.44829 0.02552  -0.01990 -0.02728 297 TYR   B CG  
5037 C  CD1 . TYR   B 297 ? 0.41646 0.44017 0.44804 0.02545  -0.02578 -0.02760 297 TYR   B CD1 
5038 C  CD2 . TYR   B 297 ? 0.46139 0.49671 0.49745 0.02828  -0.01435 -0.02651 297 TYR   B CD2 
5039 C  CE1 . TYR   B 297 ? 0.46836 0.48304 0.48715 0.02927  -0.02620 -0.02796 297 TYR   B CE1 
5040 C  CE2 . TYR   B 297 ? 0.44149 0.47020 0.46606 0.03181  -0.01399 -0.02629 297 TYR   B CE2 
5041 C  CZ  . TYR   B 297 ? 0.43644 0.45425 0.45167 0.03295  -0.02003 -0.02743 297 TYR   B CZ  
5042 O  OH  . TYR   B 297 ? 0.49325 0.50340 0.49548 0.03803  -0.02038 -0.02799 297 TYR   B OH  
5043 N  N   . ASN   B 298 ? 0.31966 0.39194 0.40163 0.01850  -0.01655 -0.02986 298 ASN   B N   
5044 C  CA  . ASN   B 298 ? 0.36984 0.45087 0.46109 0.01995  -0.01767 -0.03146 298 ASN   B CA  
5045 C  C   . ASN   B 298 ? 0.41064 0.48403 0.49888 0.02285  -0.02109 -0.03204 298 ASN   B C   
5046 O  O   . ASN   B 298 ? 0.35022 0.42822 0.44458 0.02416  -0.02416 -0.03311 298 ASN   B O   
5047 C  CB  . ASN   B 298 ? 0.37348 0.46567 0.47313 0.01671  -0.01996 -0.03025 298 ASN   B CB  
5048 C  CG  . ASN   B 298 ? 0.47880 0.58144 0.58287 0.01433  -0.01595 -0.02941 298 ASN   B CG  
5049 O  OD1 . ASN   B 298 ? 0.57067 0.68229 0.67967 0.01706  -0.01224 -0.03153 298 ASN   B OD1 
5050 N  ND2 . ASN   B 298 ? 0.42114 0.51996 0.52126 0.00985  -0.01693 -0.02661 298 ASN   B ND2 
5051 N  N   . GLU   B 299 ? 0.34481 0.40739 0.42348 0.02421  -0.02064 -0.03098 299 GLU   B N   
5052 C  CA  . GLU   B 299 ? 0.37159 0.42723 0.44667 0.02678  -0.02355 -0.03068 299 GLU   B CA  
5053 C  C   . GLU   B 299 ? 0.36220 0.41076 0.42800 0.02812  -0.02077 -0.02851 299 GLU   B C   
5054 O  O   . GLU   B 299 ? 0.39008 0.43895 0.45235 0.02745  -0.01723 -0.02774 299 GLU   B O   
5055 C  CB  . GLU   B 299 ? 0.37767 0.42842 0.44991 0.02642  -0.02913 -0.03025 299 GLU   B CB  
5056 C  CG  . GLU   B 299 ? 0.39773 0.43966 0.45914 0.02568  -0.03033 -0.02892 299 GLU   B CG  
5057 C  CD  . GLU   B 299 ? 0.52062 0.55561 0.57794 0.02547  -0.03720 -0.02874 299 GLU   B CD  
5058 O  OE1 . GLU   B 299 ? 0.46064 0.50145 0.52670 0.02374  -0.04075 -0.02911 299 GLU   B OE1 
5059 O  OE2 . GLU   B 299 ? 0.54130 0.56550 0.58644 0.02762  -0.03931 -0.02824 299 GLU   B OE2 
5060 N  N   . PHE   B 300 ? 0.33916 0.38253 0.40141 0.03004  -0.02247 -0.02704 300 PHE   B N   
5061 C  CA  . PHE   B 300 ? 0.36181 0.40010 0.41430 0.03152  -0.02036 -0.02365 300 PHE   B CA  
5062 C  C   . PHE   B 300 ? 0.35873 0.39001 0.40406 0.03364  -0.02436 -0.02223 300 PHE   B C   
5063 O  O   . PHE   B 300 ? 0.37485 0.40484 0.42355 0.03391  -0.02744 -0.02189 300 PHE   B O   
5064 C  CB  . PHE   B 300 ? 0.31329 0.35428 0.36887 0.03097  -0.01765 -0.02143 300 PHE   B CB  
5065 C  CG  . PHE   B 300 ? 0.35740 0.39735 0.40460 0.03204  -0.01455 -0.01676 300 PHE   B CG  
5066 C  CD1 . PHE   B 300 ? 0.38048 0.41651 0.42084 0.03382  -0.01635 -0.01315 300 PHE   B CD1 
5067 C  CD2 . PHE   B 300 ? 0.31769 0.36202 0.36387 0.03165  -0.00975 -0.01571 300 PHE   B CD2 
5068 C  CE1 . PHE   B 300 ? 0.38553 0.42381 0.41799 0.03549  -0.01287 -0.00783 300 PHE   B CE1 
5069 C  CE2 . PHE   B 300 ? 0.37898 0.42504 0.41764 0.03346  -0.00653 -0.01081 300 PHE   B CE2 
5070 C  CZ  . PHE   B 300 ? 0.35261 0.39648 0.38458 0.03550  -0.00795 -0.00673 300 PHE   B CZ  
5071 N  N   . ASN   B 301 ? 0.32826 0.35423 0.36305 0.03567  -0.02500 -0.02172 301 ASN   B N   
5072 C  CA  . ASN   B 301 ? 0.38512 0.40400 0.41121 0.03845  -0.02897 -0.02057 301 ASN   B CA  
5073 C  C   . ASN   B 301 ? 0.39378 0.41266 0.41131 0.04133  -0.02578 -0.01594 301 ASN   B C   
5074 O  O   . ASN   B 301 ? 0.43776 0.45766 0.44760 0.04383  -0.02215 -0.01472 301 ASN   B O   
5075 C  CB  . ASN   B 301 ? 0.42215 0.43402 0.43979 0.03993  -0.03268 -0.02277 301 ASN   B CB  
5076 C  CG  . ASN   B 301 ? 0.54907 0.55300 0.55856 0.04266  -0.03819 -0.02255 301 ASN   B CG  
5077 O  OD1 . ASN   B 301 ? 0.51615 0.52059 0.53137 0.04162  -0.04109 -0.02226 301 ASN   B OD1 
5078 N  ND2 . ASN   B 301 ? 0.48252 0.47855 0.47798 0.04679  -0.04016 -0.02302 301 ASN   B ND2 
5079 N  N   . LEU   B 302 ? 0.34719 0.36615 0.36674 0.04088  -0.02714 -0.01290 302 LEU   B N   
5080 C  CA  . LEU   B 302 ? 0.41563 0.43660 0.42835 0.04257  -0.02462 -0.00680 302 LEU   B CA  
5081 C  C   . LEU   B 302 ? 0.41586 0.43109 0.41613 0.04694  -0.02755 -0.00561 302 LEU   B C   
5082 O  O   . LEU   B 302 ? 0.45634 0.46709 0.45737 0.04654  -0.03229 -0.00532 302 LEU   B O   
5083 C  CB  . LEU   B 302 ? 0.37818 0.40114 0.39959 0.03895  -0.02579 -0.00335 302 LEU   B CB  
5084 C  CG  . LEU   B 302 ? 0.40049 0.42770 0.41899 0.03811  -0.02367 0.00477  302 LEU   B CG  
5085 C  CD1 . LEU   B 302 ? 0.42305 0.45855 0.44342 0.03696  -0.01779 0.00730  302 LEU   B CD1 
5086 C  CD2 . LEU   B 302 ? 0.40520 0.42940 0.43149 0.03428  -0.02839 0.00726  302 LEU   B CD2 
5087 N  N   . VAL   B 303 ? 0.39841 0.41358 0.38627 0.05192  -0.02507 -0.00498 303 VAL   B N   
5088 C  CA  . VAL   B 303 ? 0.43721 0.44710 0.41096 0.05747  -0.02777 -0.00394 303 VAL   B CA  
5089 C  C   . VAL   B 303 ? 0.47244 0.48951 0.44251 0.05852  -0.02468 0.00403  303 VAL   B C   
5090 O  O   . VAL   B 303 ? 0.42531 0.45199 0.39666 0.05825  -0.01904 0.00852  303 VAL   B O   
5091 C  CB  . VAL   B 303 ? 0.47694 0.48264 0.43727 0.06379  -0.02744 -0.00739 303 VAL   B CB  
5092 C  CG1 . VAL   B 303 ? 0.53840 0.53936 0.48162 0.07130  -0.02979 -0.00625 303 VAL   B CG1 
5093 C  CG2 . VAL   B 303 ? 0.52393 0.52180 0.48836 0.06132  -0.03189 -0.01412 303 VAL   B CG2 
5094 N  N   . ARG   B 304 ? 0.43628 0.44949 0.40253 0.05913  -0.02869 0.00650  304 ARG   B N   
5095 C  CA  . ARG   B 304 ? 0.44436 0.46434 0.40777 0.05894  -0.02691 0.01537  304 ARG   B CA  
5096 C  C   . ARG   B 304 ? 0.50276 0.51662 0.45450 0.06326  -0.03127 0.01624  304 ARG   B C   
5097 O  O   . ARG   B 304 ? 0.42259 0.42606 0.37433 0.06337  -0.03729 0.01056  304 ARG   B O   
5098 C  CB  . ARG   B 304 ? 0.37665 0.39798 0.35384 0.05137  -0.02883 0.01943  304 ARG   B CB  
5099 C  CG  . ARG   B 304 ? 0.51071 0.53743 0.50020 0.04637  -0.02571 0.01941  304 ARG   B CG  
5100 C  CD  . ARG   B 304 ? 0.48775 0.51267 0.48798 0.04000  -0.02979 0.02334  304 ARG   B CD  
5101 N  NE  . ARG   B 304 ? 0.45809 0.47309 0.46399 0.03914  -0.03621 0.01693  304 ARG   B NE  
5102 C  CZ  . ARG   B 304 ? 0.40765 0.41886 0.42363 0.03506  -0.04063 0.01672  304 ARG   B CZ  
5103 N  NH1 . ARG   B 304 ? 0.39058 0.40481 0.41199 0.03057  -0.04045 0.02257  304 ARG   B NH1 
5104 N  NH2 . ARG   B 304 ? 0.43261 0.43655 0.45298 0.03585  -0.04618 0.01063  304 ARG   B NH2 
5105 N  N   . LYS   B 305 ? 0.47524 0.49670 0.41850 0.06598  -0.02859 0.02431  305 LYS   B N   
5106 C  CA  . LYS   B 305 ? 0.47304 0.48933 0.40629 0.06914  -0.03301 0.02637  305 LYS   B CA  
5107 C  C   . LYS   B 305 ? 0.48627 0.49560 0.43028 0.06250  -0.03923 0.02711  305 LYS   B C   
5108 O  O   . LYS   B 305 ? 0.44965 0.46140 0.40710 0.05568  -0.03925 0.02974  305 LYS   B O   
5109 C  CB  . LYS   B 305 ? 0.53328 0.56189 0.45591 0.07313  -0.02834 0.03626  305 LYS   B CB  
5110 C  CG  . LYS   B 305 ? 0.56095 0.59767 0.47201 0.08152  -0.02216 0.03523  305 LYS   B CG  
5111 C  CD  . LYS   B 305 ? 0.72297 0.77302 0.62112 0.08759  -0.01798 0.04462  305 LYS   B CD  
5112 C  CE  . LYS   B 305 ? 0.81134 0.88044 0.71725 0.08398  -0.01077 0.05461  305 LYS   B CE  
5113 N  NZ  . LYS   B 305 ? 0.81056 0.89603 0.70132 0.09399  -0.00440 0.06073  305 LYS   B NZ  
5114 N  N   . GLU   B 306 ? 0.48575 0.48561 0.42286 0.06513  -0.04532 0.02465  306 GLU   B N   
5115 C  CA  . GLU   B 306 ? 0.49385 0.48686 0.44020 0.06004  -0.05178 0.02503  306 GLU   B CA  
5116 C  C   . GLU   B 306 ? 0.52077 0.51968 0.47210 0.05492  -0.05121 0.03517  306 GLU   B C   
5117 O  O   . GLU   B 306 ? 0.49307 0.48789 0.45662 0.04919  -0.05528 0.03532  306 GLU   B O   
5118 C  CB  . GLU   B 306 ? 0.56216 0.54555 0.49828 0.06415  -0.05833 0.02283  306 GLU   B CB  
5119 C  CG  . GLU   B 306 ? 0.63882 0.61306 0.57485 0.06621  -0.06285 0.01316  306 GLU   B CG  
5120 C  CD  . GLU   B 306 ? 0.75425 0.71866 0.68610 0.06759  -0.07111 0.01161  306 GLU   B CD  
5121 O  OE1 . GLU   B 306 ? 0.80721 0.76633 0.74962 0.06470  -0.07638 0.00623  306 GLU   B OE1 
5122 O  OE2 . GLU   B 306 ? 0.73306 0.69652 0.65204 0.07137  -0.07220 0.01639  306 GLU   B OE2 
5123 N  N   . LYS   B 307 ? 0.50661 0.51538 0.44848 0.05701  -0.04676 0.04411  307 LYS   B N   
5124 C  CA  . LYS   B 307 ? 0.55472 0.56873 0.50176 0.05080  -0.04768 0.05525  307 LYS   B CA  
5125 C  C   . LYS   B 307 ? 0.50320 0.52239 0.46446 0.04384  -0.04543 0.05765  307 LYS   B C   
5126 O  O   . LYS   B 307 ? 0.48907 0.50787 0.45785 0.03702  -0.04903 0.06505  307 LYS   B O   
5127 C  CB  . LYS   B 307 ? 0.59303 0.61974 0.52781 0.05396  -0.04317 0.06609  307 LYS   B CB  
5128 C  CG  . LYS   B 307 ? 0.66451 0.70606 0.59597 0.05748  -0.03418 0.06817  307 LYS   B CG  
5129 C  CD  . LYS   B 307 ? 0.67733 0.73563 0.59953 0.05960  -0.02944 0.08123  307 LYS   B CD  
5130 C  CE  . LYS   B 307 ? 0.84497 0.91637 0.75645 0.06881  -0.02107 0.08014  307 LYS   B CE  
5131 N  NZ  . LYS   B 307 ? 0.96337 1.02664 0.85716 0.07995  -0.02247 0.07189  307 LYS   B NZ  
5132 N  N   . ASN   B 308 ? 0.47999 0.50268 0.44460 0.04536  -0.04051 0.05151  308 ASN   B N   
5133 C  CA  . ASN   B 308 ? 0.45431 0.48089 0.43190 0.03944  -0.03864 0.05223  308 ASN   B CA  
5134 C  C   . ASN   B 308 ? 0.52102 0.53677 0.50961 0.03720  -0.04313 0.04228  308 ASN   B C   
5135 O  O   . ASN   B 308 ? 0.47138 0.48931 0.46956 0.03382  -0.04145 0.04034  308 ASN   B O   
5136 C  CB  . ASN   B 308 ? 0.48042 0.51863 0.45475 0.04278  -0.03035 0.05213  308 ASN   B CB  
5137 C  CG  . ASN   B 308 ? 0.55884 0.61168 0.52446 0.04486  -0.02534 0.06337  308 ASN   B CG  
5138 O  OD1 . ASN   B 308 ? 0.52549 0.58180 0.49269 0.04017  -0.02777 0.07342  308 ASN   B OD1 
5139 N  ND2 . ASN   B 308 ? 0.54749 0.60896 0.50330 0.05234  -0.01891 0.06189  308 ASN   B ND2 
5140 N  N   . GLY   B 309 ? 0.51480 0.52011 0.50209 0.03943  -0.04879 0.03612  309 GLY   B N   
5141 C  CA  . GLY   B 309 ? 0.48539 0.48333 0.48288 0.03835  -0.05273 0.02718  309 GLY   B CA  
5142 C  C   . GLY   B 309 ? 0.50810 0.50322 0.50274 0.04289  -0.05235 0.01794  309 GLY   B C   
5143 O  O   . GLY   B 309 ? 0.44855 0.43921 0.45154 0.04237  -0.05607 0.01112  309 GLY   B O   
5144 N  N   . GLY   B 310 ? 0.39914 0.39738 0.38263 0.04733  -0.04823 0.01772  310 GLY   B N   
5145 C  CA  . GLY   B 310 ? 0.44540 0.43942 0.42489 0.05109  -0.04906 0.00977  310 GLY   B CA  
5146 C  C   . GLY   B 310 ? 0.41780 0.41418 0.40616 0.04935  -0.04651 0.00375  310 GLY   B C   
5147 O  O   . GLY   B 310 ? 0.41261 0.41324 0.41164 0.04542  -0.04451 0.00433  310 GLY   B O   
5148 N  N   . ASP   B 311 ? 0.38867 0.38186 0.37182 0.05226  -0.04702 -0.00172 311 ASP   B N   
5149 C  CA  . ASP   B 311 ? 0.44212 0.43763 0.43326 0.05019  -0.04512 -0.00675 311 ASP   B CA  
5150 C  C   . ASP   B 311 ? 0.39486 0.39179 0.40132 0.04594  -0.04769 -0.00943 311 ASP   B C   
5151 O  O   . ASP   B 311 ? 0.39319 0.38629 0.40284 0.04572  -0.05315 -0.01022 311 ASP   B O   
5152 C  CB  . ASP   B 311 ? 0.45143 0.44064 0.43594 0.05268  -0.04845 -0.01196 311 ASP   B CB  
5153 C  CG  . ASP   B 311 ? 0.57452 0.56045 0.54191 0.05873  -0.04707 -0.01104 311 ASP   B CG  
5154 O  OD1 . ASP   B 311 ? 0.49689 0.48825 0.45783 0.06135  -0.04230 -0.00576 311 ASP   B OD1 
5155 O  OD2 . ASP   B 311 ? 0.51634 0.49412 0.47635 0.06113  -0.05168 -0.01536 311 ASP   B OD2 
5156 N  N   . LYS   B 312 ? 0.37978 0.38248 0.39516 0.04336  -0.04400 -0.01125 312 LYS   B N   
5157 C  CA  . LYS   B 312 ? 0.41440 0.41961 0.44328 0.04085  -0.04629 -0.01464 312 LYS   B CA  
5158 C  C   . LYS   B 312 ? 0.41230 0.42352 0.44755 0.03916  -0.04257 -0.01807 312 LYS   B C   
5159 O  O   . LYS   B 312 ? 0.37612 0.39052 0.40918 0.03867  -0.03738 -0.01645 312 LYS   B O   
5160 C  CB  . LYS   B 312 ? 0.39935 0.40502 0.43397 0.03928  -0.04693 -0.01161 312 LYS   B CB  
5161 C  CG  . LYS   B 312 ? 0.39178 0.39996 0.43892 0.03846  -0.04926 -0.01591 312 LYS   B CG  
5162 C  CD  . LYS   B 312 ? 0.36906 0.37416 0.41965 0.03725  -0.05167 -0.01285 312 LYS   B CD  
5163 C  CE  . LYS   B 312 ? 0.38648 0.39352 0.44770 0.03820  -0.05416 -0.01815 312 LYS   B CE  
5164 N  NZ  . LYS   B 312 ? 0.38933 0.39578 0.45457 0.04142  -0.05960 -0.02255 312 LYS   B NZ  
5165 N  N   . THR   B 313 ? 0.37465 0.38878 0.41848 0.03820  -0.04522 -0.02221 313 THR   B N   
5166 C  CA  . THR   B 313 ? 0.35461 0.37582 0.40536 0.03621  -0.04207 -0.02486 313 THR   B CA  
5167 C  C   . THR   B 313 ? 0.38684 0.41435 0.44864 0.03584  -0.04127 -0.02658 313 THR   B C   
5168 O  O   . THR   B 313 ? 0.37680 0.40542 0.44477 0.03715  -0.04544 -0.02844 313 THR   B O   
5169 C  CB  . THR   B 313 ? 0.41537 0.43767 0.46845 0.03506  -0.04577 -0.02722 313 THR   B CB  
5170 O  OG1 . THR   B 313 ? 0.40938 0.42282 0.45020 0.03624  -0.04815 -0.02616 313 THR   B OG1 
5171 C  CG2 . THR   B 313 ? 0.46300 0.49328 0.52256 0.03233  -0.04238 -0.02869 313 THR   B CG2 
5172 N  N   . TYR   B 314 ? 0.33294 0.36440 0.39675 0.03472  -0.03636 -0.02631 314 TYR   B N   
5173 C  CA  . TYR   B 314 ? 0.35231 0.38892 0.42500 0.03498  -0.03572 -0.02856 314 TYR   B CA  
5174 C  C   . TYR   B 314 ? 0.38328 0.42966 0.46336 0.03433  -0.03372 -0.03194 314 TYR   B C   
5175 O  O   . TYR   B 314 ? 0.36246 0.41119 0.44033 0.03225  -0.03015 -0.03131 314 TYR   B O   
5176 C  CB  . TYR   B 314 ? 0.34801 0.38344 0.41862 0.03376  -0.03219 -0.02591 314 TYR   B CB  
5177 C  CG  . TYR   B 314 ? 0.32045 0.34869 0.38595 0.03362  -0.03459 -0.02136 314 TYR   B CG  
5178 C  CD1 . TYR   B 314 ? 0.33732 0.36235 0.39326 0.03350  -0.03327 -0.01680 314 TYR   B CD1 
5179 C  CD2 . TYR   B 314 ? 0.30964 0.33412 0.37924 0.03406  -0.03896 -0.02145 314 TYR   B CD2 
5180 C  CE1 . TYR   B 314 ? 0.33354 0.35386 0.38516 0.03310  -0.03555 -0.01151 314 TYR   B CE1 
5181 C  CE2 . TYR   B 314 ? 0.31761 0.33533 0.38301 0.03299  -0.04212 -0.01626 314 TYR   B CE2 
5182 C  CZ  . TYR   B 314 ? 0.33049 0.34716 0.38740 0.03214  -0.04007 -0.01084 314 TYR   B CZ  
5183 O  OH  . TYR   B 314 ? 0.35297 0.36449 0.40614 0.03080  -0.04339 -0.00470 314 TYR   B OH  
5184 N  N   . TYR   B 315 ? 0.35715 0.40980 0.44569 0.03645  -0.03622 -0.03519 315 TYR   B N   
5185 C  CA  . TYR   B 315 ? 0.34429 0.40921 0.44058 0.03611  -0.03381 -0.03755 315 TYR   B CA  
5186 C  C   . TYR   B 315 ? 0.39020 0.46020 0.49089 0.03836  -0.03137 -0.04027 315 TYR   B C   
5187 O  O   . TYR   B 315 ? 0.36183 0.44334 0.46835 0.03852  -0.02869 -0.04198 315 TYR   B O   
5188 C  CB  . TYR   B 315 ? 0.34582 0.41874 0.44935 0.03757  -0.03760 -0.03906 315 TYR   B CB  
5189 C  CG  . TYR   B 315 ? 0.37797 0.44619 0.47744 0.03475  -0.04057 -0.03656 315 TYR   B CG  
5190 C  CD1 . TYR   B 315 ? 0.40810 0.47586 0.50406 0.03058  -0.03886 -0.03448 315 TYR   B CD1 
5191 C  CD2 . TYR   B 315 ? 0.42176 0.48472 0.52008 0.03650  -0.04602 -0.03641 315 TYR   B CD2 
5192 C  CE1 . TYR   B 315 ? 0.43748 0.49853 0.52818 0.02843  -0.04315 -0.03261 315 TYR   B CE1 
5193 C  CE2 . TYR   B 315 ? 0.41557 0.47301 0.50912 0.03418  -0.04969 -0.03438 315 TYR   B CE2 
5194 C  CZ  . TYR   B 315 ? 0.50411 0.56024 0.59364 0.03026  -0.04850 -0.03266 315 TYR   B CZ  
5195 O  OH  . TYR   B 315 ? 0.46288 0.51140 0.54629 0.02840  -0.05346 -0.03113 315 TYR   B OH  
5196 N  N   . THR   B 316 ? 0.32039 0.38231 0.41841 0.04008  -0.03294 -0.04047 316 THR   B N   
5197 C  CA  . THR   B 316 ? 0.29247 0.35708 0.39333 0.04227  -0.03178 -0.04333 316 THR   B CA  
5198 C  C   . THR   B 316 ? 0.36924 0.42422 0.46447 0.03963  -0.03110 -0.04014 316 THR   B C   
5199 O  O   . THR   B 316 ? 0.36253 0.40847 0.45283 0.03801  -0.03346 -0.03631 316 THR   B O   
5200 C  CB  . THR   B 316 ? 0.37850 0.44307 0.48323 0.04826  -0.03693 -0.04772 316 THR   B CB  
5201 O  OG1 . THR   B 316 ? 0.37396 0.42541 0.47445 0.04843  -0.04236 -0.04583 316 THR   B OG1 
5202 C  CG2 . THR   B 316 ? 0.37567 0.45216 0.48704 0.05145  -0.03808 -0.05010 316 THR   B CG2 
5203 N  N   . LEU   B 317 ? 0.31031 0.36851 0.40666 0.03922  -0.02807 -0.04130 317 LEU   B N   
5204 C  CA  . LEU   B 317 ? 0.32765 0.37821 0.42046 0.03677  -0.02840 -0.03823 317 LEU   B CA  
5205 C  C   . LEU   B 317 ? 0.30891 0.34962 0.40150 0.03881  -0.03562 -0.03878 317 LEU   B C   
5206 O  O   . LEU   B 317 ? 0.33700 0.36962 0.42631 0.03544  -0.03778 -0.03380 317 LEU   B O   
5207 C  CB  . LEU   B 317 ? 0.34282 0.39905 0.43734 0.03632  -0.02449 -0.04001 317 LEU   B CB  
5208 C  CG  . LEU   B 317 ? 0.39864 0.46138 0.49163 0.03311  -0.01808 -0.03775 317 LEU   B CG  
5209 C  CD1 . LEU   B 317 ? 0.46748 0.53595 0.56196 0.03250  -0.01416 -0.03923 317 LEU   B CD1 
5210 C  CD2 . LEU   B 317 ? 0.40549 0.46217 0.49252 0.02982  -0.01705 -0.03191 317 LEU   B CD2 
5211 N  N   . GLN   B 318 ? 0.29653 0.33815 0.39248 0.04441  -0.03986 -0.04432 318 GLN   B N   
5212 C  CA  . GLN   B 318 ? 0.31168 0.34174 0.40646 0.04715  -0.04820 -0.04544 318 GLN   B CA  
5213 C  C   . GLN   B 318 ? 0.34324 0.36435 0.43446 0.04405  -0.05170 -0.03981 318 GLN   B C   
5214 O  O   . GLN   B 318 ? 0.35778 0.36793 0.44612 0.04132  -0.05676 -0.03569 318 GLN   B O   
5215 C  CB  . GLN   B 318 ? 0.37156 0.40555 0.46986 0.05528  -0.05192 -0.05278 318 GLN   B CB  
5216 C  CG  . GLN   B 318 ? 0.45577 0.47549 0.55168 0.05939  -0.06195 -0.05513 318 GLN   B CG  
5217 C  CD  . GLN   B 318 ? 0.54043 0.55158 0.63471 0.05920  -0.06756 -0.05245 318 GLN   B CD  
5218 O  OE1 . GLN   B 318 ? 0.49767 0.51576 0.59378 0.05926  -0.06491 -0.05165 318 GLN   B OE1 
5219 N  NE2 . GLN   B 318 ? 0.54888 0.54402 0.63947 0.05846  -0.07620 -0.05051 318 GLN   B NE2 
5220 N  N   . GLU   B 319 ? 0.34197 0.36768 0.43312 0.04402  -0.04949 -0.03898 319 GLU   B N   
5221 C  CA  . GLU   B 319 ? 0.34919 0.36716 0.43590 0.04160  -0.05243 -0.03370 319 GLU   B CA  
5222 C  C   . GLU   B 319 ? 0.38187 0.39790 0.46359 0.03572  -0.04876 -0.02628 319 GLU   B C   
5223 O  O   . GLU   B 319 ? 0.33345 0.34172 0.41150 0.03309  -0.05243 -0.02049 319 GLU   B O   
5224 C  CB  . GLU   B 319 ? 0.31920 0.34219 0.40618 0.04300  -0.05131 -0.03465 319 GLU   B CB  
5225 C  CG  . GLU   B 319 ? 0.34827 0.36131 0.43036 0.04214  -0.05651 -0.03029 319 GLU   B CG  
5226 C  CD  . GLU   B 319 ? 0.43566 0.45113 0.51679 0.04334  -0.05693 -0.03072 319 GLU   B CD  
5227 O  OE1 . GLU   B 319 ? 0.46434 0.48872 0.54763 0.04316  -0.05259 -0.03276 319 GLU   B OE1 
5228 O  OE2 . GLU   B 319 ? 0.36091 0.36882 0.43916 0.04422  -0.06240 -0.02881 319 GLU   B OE2 
5229 N  N   . LEU   B 320 ? 0.32653 0.35055 0.40789 0.03384  -0.04158 -0.02582 320 LEU   B N   
5230 C  CA  . LEU   B 320 ? 0.31821 0.34240 0.39474 0.02956  -0.03774 -0.01895 320 LEU   B CA  
5231 C  C   . LEU   B 320 ? 0.33854 0.35744 0.41588 0.02645  -0.04116 -0.01478 320 LEU   B C   
5232 O  O   . LEU   B 320 ? 0.36269 0.37934 0.43655 0.02292  -0.04180 -0.00716 320 LEU   B O   
5233 C  CB  . LEU   B 320 ? 0.34087 0.37354 0.41706 0.02886  -0.03044 -0.01999 320 LEU   B CB  
5234 C  CG  . LEU   B 320 ? 0.36846 0.40319 0.43894 0.02608  -0.02591 -0.01336 320 LEU   B CG  
5235 C  CD1 . LEU   B 320 ? 0.34884 0.38195 0.41245 0.02727  -0.02568 -0.01073 320 LEU   B CD1 
5236 C  CD2 . LEU   B 320 ? 0.41250 0.45421 0.48320 0.02597  -0.01986 -0.01536 320 LEU   B CD2 
5237 N  N   . GLU   B 321 ? 0.34137 0.35881 0.42307 0.02772  -0.04370 -0.01931 321 GLU   B N   
5238 C  CA  . GLU   B 321 ? 0.35870 0.36942 0.44121 0.02441  -0.04856 -0.01572 321 GLU   B CA  
5239 C  C   . GLU   B 321 ? 0.36486 0.36387 0.44603 0.02365  -0.05762 -0.01258 321 GLU   B C   
5240 O  O   . GLU   B 321 ? 0.33229 0.32702 0.41208 0.01826  -0.06070 -0.00432 321 GLU   B O   
5241 C  CB  . GLU   B 321 ? 0.39940 0.40997 0.48542 0.02722  -0.05005 -0.02256 321 GLU   B CB  
5242 C  CG  . GLU   B 321 ? 0.47250 0.47178 0.55874 0.02450  -0.05858 -0.01996 321 GLU   B CG  
5243 C  CD  . GLU   B 321 ? 0.63194 0.62986 0.71993 0.02791  -0.06072 -0.02696 321 GLU   B CD  
5244 O  OE1 . GLU   B 321 ? 0.55007 0.55872 0.63945 0.02916  -0.05307 -0.03013 321 GLU   B OE1 
5245 O  OE2 . GLU   B 321 ? 0.66659 0.65212 0.75378 0.02947  -0.07047 -0.02913 321 GLU   B OE2 
5246 N  N   . HIS   B 322 ? 0.34986 0.34423 0.43161 0.02891  -0.06232 -0.01848 322 HIS   B N   
5247 C  CA  . HIS   B 322 ? 0.37420 0.35648 0.45397 0.02855  -0.07144 -0.01553 322 HIS   B CA  
5248 C  C   . HIS   B 322 ? 0.40505 0.38818 0.48075 0.02351  -0.06960 -0.00588 322 HIS   B C   
5249 O  O   . HIS   B 322 ? 0.37500 0.35058 0.44911 0.01879  -0.07541 0.00176  322 HIS   B O   
5250 C  CB  . HIS   B 322 ? 0.39155 0.37187 0.47236 0.03585  -0.07509 -0.02323 322 HIS   B CB  
5251 C  CG  . HIS   B 322 ? 0.42062 0.38973 0.49859 0.03574  -0.08330 -0.01986 322 HIS   B CG  
5252 N  ND1 . HIS   B 322 ? 0.42733 0.39843 0.50217 0.03396  -0.08113 -0.01504 322 HIS   B ND1 
5253 C  CD2 . HIS   B 322 ? 0.43773 0.39247 0.51471 0.03724  -0.09436 -0.02044 322 HIS   B CD2 
5254 C  CE1 . HIS   B 322 ? 0.41644 0.37599 0.48907 0.03431  -0.08998 -0.01276 322 HIS   B CE1 
5255 N  NE2 . HIS   B 322 ? 0.43803 0.38708 0.51198 0.03605  -0.09831 -0.01577 322 HIS   B NE2 
5256 N  N   . ASP   B 323 ? 0.32487 0.31717 0.39839 0.02460  -0.06207 -0.00590 323 ASP   B N   
5257 C  CA  . ASP   B 323 ? 0.37864 0.37196 0.44666 0.02184  -0.06051 0.00208  323 ASP   B CA  
5258 C  C   . ASP   B 323 ? 0.35809 0.35649 0.42462 0.01607  -0.05701 0.01138  323 ASP   B C   
5259 O  O   . ASP   B 323 ? 0.39334 0.39040 0.45652 0.01248  -0.05920 0.02035  323 ASP   B O   
5260 C  CB  . ASP   B 323 ? 0.35946 0.35979 0.42427 0.02514  -0.05439 -0.00095 323 ASP   B CB  
5261 C  CG  . ASP   B 323 ? 0.39501 0.39086 0.46060 0.02972  -0.05907 -0.00676 323 ASP   B CG  
5262 O  OD1 . ASP   B 323 ? 0.36941 0.35793 0.43857 0.03171  -0.06623 -0.01012 323 ASP   B OD1 
5263 O  OD2 . ASP   B 323 ? 0.41120 0.41092 0.47356 0.03158  -0.05588 -0.00802 323 ASP   B OD2 
5264 N  N   . TYR   B 324 ? 0.33617 0.34152 0.40540 0.01509  -0.05171 0.01002  324 TYR   B N   
5265 C  CA  . TYR   B 324 ? 0.34874 0.36070 0.41737 0.00981  -0.04850 0.01938  324 TYR   B CA  
5266 C  C   . TYR   B 324 ? 0.37342 0.37741 0.44552 0.00411  -0.05708 0.02553  324 TYR   B C   
5267 O  O   . TYR   B 324 ? 0.34878 0.35484 0.41966 -0.00126 -0.05872 0.03659  324 TYR   B O   
5268 C  CB  . TYR   B 324 ? 0.34467 0.36609 0.41502 0.01051  -0.04083 0.01634  324 TYR   B CB  
5269 C  CG  . TYR   B 324 ? 0.36453 0.39553 0.43370 0.00649  -0.03636 0.02591  324 TYR   B CG  
5270 C  CD1 . TYR   B 324 ? 0.32163 0.36108 0.38416 0.00823  -0.03049 0.03089  324 TYR   B CD1 
5271 C  CD2 . TYR   B 324 ? 0.35111 0.38297 0.42541 0.00118  -0.03884 0.03072  324 TYR   B CD2 
5272 C  CE1 . TYR   B 324 ? 0.35260 0.40391 0.41398 0.00546  -0.02594 0.04066  324 TYR   B CE1 
5273 C  CE2 . TYR   B 324 ? 0.37861 0.42204 0.45287 -0.00300 -0.03487 0.04139  324 TYR   B CE2 
5274 C  CZ  . TYR   B 324 ? 0.36322 0.41714 0.43123 -0.00041 -0.02807 0.04607  324 TYR   B CZ  
5275 O  OH  . TYR   B 324 ? 0.38413 0.45177 0.45236 -0.00335 -0.02383 0.05639  324 TYR   B OH  
5276 N  N   . VAL   B 325 ? 0.35585 0.34996 0.43169 0.00545  -0.06377 0.01881  325 VAL   B N   
5277 C  CA  . VAL   B 325 ? 0.39975 0.38369 0.47814 -0.00001 -0.07358 0.02411  325 VAL   B CA  
5278 C  C   . VAL   B 325 ? 0.43632 0.41064 0.51219 -0.00260 -0.08185 0.03060  325 VAL   B C   
5279 O  O   . VAL   B 325 ? 0.41893 0.38926 0.49582 -0.00996 -0.08814 0.04093  325 VAL   B O   
5280 C  CB  . VAL   B 325 ? 0.46839 0.44276 0.54948 0.00388  -0.07946 0.01396  325 VAL   B CB  
5281 C  CG1 . VAL   B 325 ? 0.51245 0.46947 0.59382 0.00068  -0.09357 0.01670  325 VAL   B CG1 
5282 C  CG2 . VAL   B 325 ? 0.43604 0.41907 0.51991 0.00350  -0.07318 0.01136  325 VAL   B CG2 
5283 N  N   . ASN   B 326 ? 0.38257 0.35387 0.45523 0.00267  -0.08210 0.02589  326 ASN   B N   
5284 C  CA  . ASN   B 326 ? 0.38757 0.34961 0.45729 0.00042  -0.08997 0.03214  326 ASN   B CA  
5285 C  C   . ASN   B 326 ? 0.40986 0.38230 0.47534 -0.00286 -0.08414 0.04256  326 ASN   B C   
5286 O  O   . ASN   B 326 ? 0.41912 0.38556 0.48133 -0.00458 -0.08966 0.04839  326 ASN   B O   
5287 C  CB  . ASN   B 326 ? 0.39664 0.34951 0.46512 0.00819  -0.09458 0.02185  326 ASN   B CB  
5288 C  CG  . ASN   B 326 ? 0.54028 0.48091 0.61167 0.01163  -0.10327 0.01352  326 ASN   B CG  
5289 O  OD1 . ASN   B 326 ? 0.54798 0.47473 0.61906 0.00832  -0.11434 0.01726  326 ASN   B OD1 
5290 N  ND2 . ASN   B 326 ? 0.52610 0.47251 0.59993 0.01784  -0.09826 0.00307  326 ASN   B ND2 
5291 N  N   . GLY   B 327 ? 0.42066 0.40840 0.48542 -0.00320 -0.07352 0.04509  327 GLY   B N   
5292 C  CA  . GLY   B 327 ? 0.46240 0.46139 0.52189 -0.00483 -0.06774 0.05481  327 GLY   B CA  
5293 C  C   . GLY   B 327 ? 0.47922 0.47959 0.53183 0.00162  -0.06384 0.05028  327 GLY   B C   
5294 O  O   . GLY   B 327 ? 0.40388 0.41077 0.45036 0.00112  -0.06118 0.05832  327 GLY   B O   
5295 N  N   . PHE   B 328 ? 0.38624 0.38122 0.43947 0.00770  -0.06389 0.03819  328 PHE   B N   
5296 C  CA  . PHE   B 328 ? 0.40100 0.39732 0.44792 0.01310  -0.06089 0.03447  328 PHE   B CA  
5297 C  C   . PHE   B 328 ? 0.42569 0.43443 0.46770 0.01578  -0.05077 0.03437  328 PHE   B C   
5298 O  O   . PHE   B 328 ? 0.39825 0.40869 0.43274 0.01979  -0.04830 0.03360  328 PHE   B O   
5299 C  CB  . PHE   B 328 ? 0.41778 0.40729 0.46775 0.01860  -0.06373 0.02224  328 PHE   B CB  
5300 C  CG  . PHE   B 328 ? 0.38852 0.36542 0.44215 0.01873  -0.07387 0.01989  328 PHE   B CG  
5301 C  CD1 . PHE   B 328 ? 0.39350 0.36252 0.44749 0.01367  -0.08131 0.02770  328 PHE   B CD1 
5302 C  CD2 . PHE   B 328 ? 0.39551 0.36843 0.45186 0.02451  -0.07670 0.00988  328 PHE   B CD2 
5303 C  CE1 . PHE   B 328 ? 0.43317 0.38810 0.48927 0.01473  -0.09209 0.02484  328 PHE   B CE1 
5304 C  CE2 . PHE   B 328 ? 0.41320 0.37459 0.47216 0.02624  -0.08636 0.00699  328 PHE   B CE2 
5305 C  CZ  . PHE   B 328 ? 0.45106 0.40228 0.50932 0.02176  -0.09434 0.01390  328 PHE   B CZ  
5306 N  N   . ILE   B 329 ? 0.39659 0.41262 0.44225 0.01431  -0.04572 0.03411  329 ILE   B N   
5307 C  CA  . ILE   B 329 ? 0.34282 0.36978 0.38394 0.01725  -0.03676 0.03360  329 ILE   B CA  
5308 C  C   . ILE   B 329 ? 0.41928 0.45665 0.46026 0.01311  -0.03356 0.04463  329 ILE   B C   
5309 O  O   . ILE   B 329 ? 0.41147 0.44948 0.45981 0.00808  -0.03540 0.04739  329 ILE   B O   
5310 C  CB  . ILE   B 329 ? 0.38407 0.41211 0.42989 0.01915  -0.03344 0.02441  329 ILE   B CB  
5311 C  CG1 . ILE   B 329 ? 0.36633 0.38662 0.41405 0.02260  -0.03701 0.01477  329 ILE   B CG1 
5312 C  CG2 . ILE   B 329 ? 0.35718 0.39508 0.39766 0.02219  -0.02509 0.02419  329 ILE   B CG2 
5313 C  CD1 . ILE   B 329 ? 0.38057 0.40379 0.43351 0.02395  -0.03372 0.00677  329 ILE   B CD1 
5314 N  N   . HIS   B 330 ? 0.40862 0.45446 0.44122 0.01548  -0.02929 0.05095  330 HIS   B N   
5315 C  CA  . HIS   B 330 ? 0.42598 0.48579 0.45840 0.01234  -0.02526 0.06248  330 HIS   B CA  
5316 C  C   . HIS   B 330 ? 0.42490 0.49510 0.45735 0.01521  -0.01744 0.05983  330 HIS   B C   
5317 O  O   . HIS   B 330 ? 0.43483 0.50333 0.46234 0.02143  -0.01374 0.05089  330 HIS   B O   
5318 C  CB  . HIS   B 330 ? 0.46780 0.53521 0.49039 0.01507  -0.02311 0.07060  330 HIS   B CB  
5319 C  CG  . HIS   B 330 ? 0.61802 0.67715 0.64031 0.01133  -0.03075 0.07595  330 HIS   B CG  
5320 N  ND1 . HIS   B 330 ? 0.67167 0.71949 0.70282 0.00450  -0.03938 0.07686  330 HIS   B ND1 
5321 C  CD2 . HIS   B 330 ? 0.63720 0.69621 0.65047 0.01417  -0.03175 0.07986  330 HIS   B CD2 
5322 C  CE1 . HIS   B 330 ? 0.60070 0.64168 0.62868 0.00298  -0.04546 0.08145  330 HIS   B CE1 
5323 N  NE2 . HIS   B 330 ? 0.75014 0.79826 0.76755 0.00848  -0.04072 0.08361  330 HIS   B NE2 
5324 N  N   . PRO   B 331 ? 0.38454 0.46594 0.42216 0.01069  -0.01522 0.06821  331 PRO   B N   
5325 C  CA  . PRO   B 331 ? 0.39262 0.48403 0.43033 0.01376  -0.00804 0.06572  331 PRO   B CA  
5326 C  C   . PRO   B 331 ? 0.37303 0.47111 0.39875 0.02315  -0.00124 0.06278  331 PRO   B C   
5327 O  O   . PRO   B 331 ? 0.37312 0.47001 0.39697 0.02760  0.00229  0.05450  331 PRO   B O   
5328 C  CB  . PRO   B 331 ? 0.39260 0.49769 0.43705 0.00718  -0.00728 0.07838  331 PRO   B CB  
5329 C  CG  . PRO   B 331 ? 0.42264 0.51694 0.47455 -0.00131 -0.01678 0.08256  331 PRO   B CG  
5330 C  CD  . PRO   B 331 ? 0.37493 0.45807 0.42021 0.00165  -0.02071 0.07938  331 PRO   B CD  
5331 N  N   . LEU   B 332 ? 0.38003 0.48484 0.39686 0.02662  0.00026  0.06939  332 LEU   B N   
5332 C  CA  . LEU   B 332 ? 0.40069 0.51136 0.40436 0.03690  0.00609  0.06625  332 LEU   B CA  
5333 C  C   . LEU   B 332 ? 0.42774 0.52258 0.42564 0.04210  0.00390  0.05295  332 LEU   B C   
5334 O  O   . LEU   B 332 ? 0.40886 0.50396 0.39941 0.04907  0.00744  0.04675  332 LEU   B O   
5335 C  CB  . LEU   B 332 ? 0.45209 0.57205 0.44622 0.04030  0.00733  0.07537  332 LEU   B CB  
5336 C  CG  . LEU   B 332 ? 0.61091 0.73389 0.58847 0.05275  0.01183  0.07077  332 LEU   B CG  
5337 C  CD1 . LEU   B 332 ? 0.70728 0.84237 0.68225 0.05876  0.01877  0.06951  332 LEU   B CD1 
5338 C  CD2 . LEU   B 332 ? 0.76916 0.90063 0.73554 0.05723  0.01266  0.07909  332 LEU   B CD2 
5339 N  N   . ASP   B 333 ? 0.40734 0.48842 0.40835 0.03884  -0.00255 0.04892  333 ASP   B N   
5340 C  CA  . ASP   B 333 ? 0.43619 0.50367 0.43373 0.04251  -0.00539 0.03743  333 ASP   B CA  
5341 C  C   . ASP   B 333 ? 0.41358 0.47776 0.41872 0.04083  -0.00450 0.02976  333 ASP   B C   
5342 O  O   . ASP   B 333 ? 0.41412 0.47355 0.41407 0.04539  -0.00369 0.02216  333 ASP   B O   
5343 C  CB  . ASP   B 333 ? 0.45232 0.50830 0.45286 0.03933  -0.01254 0.03595  333 ASP   B CB  
5344 C  CG  . ASP   B 333 ? 0.50721 0.56365 0.49696 0.04278  -0.01396 0.04131  333 ASP   B CG  
5345 O  OD1 . ASP   B 333 ? 0.47884 0.53889 0.45601 0.05028  -0.01060 0.04064  333 ASP   B OD1 
5346 O  OD2 . ASP   B 333 ? 0.46060 0.51401 0.45356 0.03841  -0.01863 0.04664  333 ASP   B OD2 
5347 N  N   . LEU   B 334 ? 0.37549 0.44160 0.39248 0.03420  -0.00531 0.03188  334 LEU   B N   
5348 C  CA  . LEU   B 334 ? 0.36049 0.42486 0.38412 0.03294  -0.00406 0.02508  334 LEU   B CA  
5349 C  C   . LEU   B 334 ? 0.40136 0.47451 0.41974 0.03720  0.00233  0.02531  334 LEU   B C   
5350 O  O   . LEU   B 334 ? 0.34720 0.41662 0.36392 0.03986  0.00350  0.01804  334 LEU   B O   
5351 C  CB  . LEU   B 334 ? 0.34899 0.41309 0.38476 0.02585  -0.00685 0.02729  334 LEU   B CB  
5352 C  CG  . LEU   B 334 ? 0.38451 0.44672 0.42729 0.02459  -0.00609 0.02013  334 LEU   B CG  
5353 C  CD1 . LEU   B 334 ? 0.38232 0.43539 0.42534 0.02678  -0.00900 0.01083  334 LEU   B CD1 
5354 C  CD2 . LEU   B 334 ? 0.36323 0.42524 0.41611 0.01840  -0.00926 0.02292  334 LEU   B CD2 
5355 N  N   . LYS   B 335 ? 0.33805 0.42351 0.35326 0.03828  0.00621  0.03407  335 LYS   B N   
5356 C  CA  . LYS   B 335 ? 0.36564 0.46069 0.37528 0.04368  0.01225  0.03444  335 LYS   B CA  
5357 C  C   . LYS   B 335 ? 0.38615 0.47527 0.38215 0.05263  0.01287  0.02781  335 LYS   B C   
5358 O  O   . LYS   B 335 ? 0.42632 0.51342 0.41936 0.05616  0.01466  0.02208  335 LYS   B O   
5359 C  CB  . LYS   B 335 ? 0.36461 0.47675 0.37357 0.04380  0.01630  0.04608  335 LYS   B CB  
5360 C  CG  . LYS   B 335 ? 0.36979 0.48907 0.39190 0.03543  0.01612  0.05229  335 LYS   B CG  
5361 C  CD  . LYS   B 335 ? 0.38042 0.51965 0.40237 0.03499  0.01997  0.06594  335 LYS   B CD  
5362 C  CE  . LYS   B 335 ? 0.41216 0.56128 0.44652 0.02747  0.02042  0.07269  335 LYS   B CE  
5363 N  NZ  . LYS   B 335 ? 0.44028 0.61053 0.47394 0.02738  0.02402  0.08687  335 LYS   B NZ  
5364 N  N   . ASP   B 336 ? 0.42434 0.50978 0.41110 0.05650  0.01071  0.02868  336 ASP   B N   
5365 C  CA  . ASP   B 336 ? 0.45383 0.53184 0.42609 0.06543  0.00992  0.02227  336 ASP   B CA  
5366 C  C   . ASP   B 336 ? 0.42565 0.48965 0.40048 0.06381  0.00594  0.01244  336 ASP   B C   
5367 O  O   . ASP   B 336 ? 0.43234 0.49172 0.39912 0.06926  0.00609  0.00702  336 ASP   B O   
5368 C  CB  . ASP   B 336 ? 0.41250 0.48707 0.37472 0.06926  0.00707  0.02429  336 ASP   B CB  
5369 C  CG  . ASP   B 336 ? 0.53377 0.62468 0.49074 0.07248  0.01164  0.03488  336 ASP   B CG  
5370 O  OD1 . ASP   B 336 ? 0.59393 0.69957 0.55111 0.07492  0.01750  0.03969  336 ASP   B OD1 
5371 O  OD2 . ASP   B 336 ? 0.59194 0.68215 0.54505 0.07239  0.00929  0.03900  336 ASP   B OD2 
5372 N  N   . ASN   B 337 ? 0.37708 0.43463 0.36310 0.05645  0.00193  0.01041  337 ASN   B N   
5373 C  CA  . ASN   B 337 ? 0.37632 0.42351 0.36586 0.05457  -0.00172 0.00227  337 ASN   B CA  
5374 C  C   . ASN   B 337 ? 0.40427 0.45467 0.40013 0.05244  0.00129  -0.00019 337 ASN   B C   
5375 O  O   . ASN   B 337 ? 0.38494 0.42898 0.37727 0.05419  -0.00016 -0.00576 337 ASN   B O   
5376 C  CB  . ASN   B 337 ? 0.40102 0.44293 0.40016 0.04887  -0.00648 0.00108  337 ASN   B CB  
5377 C  CG  . ASN   B 337 ? 0.42861 0.46337 0.41930 0.05199  -0.01102 0.00089  337 ASN   B CG  
5378 O  OD1 . ASN   B 337 ? 0.42142 0.44772 0.40588 0.05475  -0.01463 -0.00429 337 ASN   B OD1 
5379 N  ND2 . ASN   B 337 ? 0.39348 0.43216 0.38217 0.05204  -0.01076 0.00731  337 ASN   B ND2 
5380 N  N   . VAL   B 338 ? 0.36928 0.42897 0.37401 0.04844  0.00480  0.00430  338 VAL   B N   
5381 C  CA  . VAL   B 338 ? 0.35928 0.42273 0.36951 0.04668  0.00781  0.00242  338 VAL   B CA  
5382 C  C   . VAL   B 338 ? 0.38874 0.45384 0.38801 0.05361  0.01079  0.00134  338 VAL   B C   
5383 O  O   . VAL   B 338 ? 0.37441 0.43550 0.37349 0.05391  0.01061  -0.00347 338 VAL   B O   
5384 C  CB  . VAL   B 338 ? 0.35129 0.42387 0.37189 0.04138  0.01005  0.00809  338 VAL   B CB  
5385 C  CG1 . VAL   B 338 ? 0.32670 0.40499 0.35082 0.04084  0.01388  0.00724  338 VAL   B CG1 
5386 C  CG2 . VAL   B 338 ? 0.34842 0.41537 0.37928 0.03544  0.00558  0.00601  338 VAL   B CG2 
5387 N  N   . ALA   B 339 ? 0.39284 0.46432 0.38246 0.05973  0.01335  0.00599  339 ALA   B N   
5388 C  CA  . ALA   B 339 ? 0.39685 0.46989 0.37427 0.06840  0.01579  0.00441  339 ALA   B CA  
5389 C  C   . ALA   B 339 ? 0.41085 0.46834 0.37847 0.07235  0.01057  -0.00352 339 ALA   B C   
5390 O  O   . ALA   B 339 ? 0.42038 0.47339 0.38360 0.07526  0.01018  -0.00767 339 ALA   B O   
5391 C  CB  . ALA   B 339 ? 0.42511 0.50954 0.39315 0.07548  0.01941  0.01100  339 ALA   B CB  
5392 N  N   . MET   B 340 ? 0.42652 0.47489 0.39059 0.07211  0.00562  -0.00538 340 MET   B N   
5393 C  CA  . MET   B 340 ? 0.42748 0.46052 0.38261 0.07493  -0.00072 -0.01214 340 MET   B CA  
5394 C  C   . MET   B 340 ? 0.40277 0.43019 0.36711 0.06843  -0.00305 -0.01637 340 MET   B C   
5395 O  O   . MET   B 340 ? 0.40829 0.42663 0.36544 0.07106  -0.00640 -0.02061 340 MET   B O   
5396 C  CB  . MET   B 340 ? 0.42894 0.45470 0.38222 0.07380  -0.00585 -0.01263 340 MET   B CB  
5397 C  CG  . MET   B 340 ? 0.60510 0.61526 0.54791 0.07697  -0.01336 -0.01846 340 MET   B CG  
5398 S  SD  . MET   B 340 ? 0.87436 0.88019 0.81666 0.07559  -0.01797 -0.01725 340 MET   B SD  
5399 C  CE  . MET   B 340 ? 0.57314 0.59011 0.50479 0.08363  -0.01212 -0.01109 340 MET   B CE  
5400 N  N   . TYR   B 341 ? 0.38392 0.41622 0.36364 0.06008  -0.00202 -0.01518 341 TYR   B N   
5401 C  CA  . TYR   B 341 ? 0.39258 0.42298 0.38200 0.05398  -0.00330 -0.01830 341 TYR   B CA  
5402 C  C   . TYR   B 341 ? 0.38557 0.42026 0.37523 0.05478  0.00059  -0.01840 341 TYR   B C   
5403 O  O   . TYR   B 341 ? 0.34822 0.37719 0.33750 0.05331  -0.00187 -0.02160 341 TYR   B O   
5404 C  CB  . TYR   B 341 ? 0.38956 0.42603 0.39366 0.04712  -0.00241 -0.01690 341 TYR   B CB  
5405 C  CG  . TYR   B 341 ? 0.42715 0.45816 0.43490 0.04440  -0.00771 -0.01880 341 TYR   B CG  
5406 C  CD1 . TYR   B 341 ? 0.48391 0.50812 0.49193 0.04245  -0.01264 -0.02249 341 TYR   B CD1 
5407 C  CD2 . TYR   B 341 ? 0.37196 0.40530 0.38387 0.04322  -0.00819 -0.01633 341 TYR   B CD2 
5408 C  CE1 . TYR   B 341 ? 0.51521 0.53678 0.52851 0.03959  -0.01750 -0.02377 341 TYR   B CE1 
5409 C  CE2 . TYR   B 341 ? 0.46298 0.49219 0.47963 0.04084  -0.01323 -0.01834 341 TYR   B CE2 
5410 C  CZ  . TYR   B 341 ? 0.50738 0.53164 0.52485 0.03930  -0.01750 -0.02203 341 TYR   B CZ  
5411 O  OH  . TYR   B 341 ? 0.46586 0.48811 0.48865 0.03717  -0.02238 -0.02346 341 TYR   B OH  
5412 N  N   . ILE   B 342 ? 0.34124 0.38649 0.33219 0.05654  0.00628  -0.01432 342 ILE   B N   
5413 C  CA  . ILE   B 342 ? 0.34589 0.39530 0.33690 0.05770  0.00964  -0.01447 342 ILE   B CA  
5414 C  C   . ILE   B 342 ? 0.39098 0.43128 0.36705 0.06533  0.00694  -0.01789 342 ILE   B C   
5415 O  O   . ILE   B 342 ? 0.36110 0.39668 0.33649 0.06463  0.00557  -0.02069 342 ILE   B O   
5416 C  CB  . ILE   B 342 ? 0.38315 0.44670 0.37794 0.05850  0.01570  -0.00854 342 ILE   B CB  
5417 C  CG1 . ILE   B 342 ? 0.35349 0.42317 0.36333 0.05016  0.01674  -0.00590 342 ILE   B CG1 
5418 C  CG2 . ILE   B 342 ? 0.35679 0.42518 0.34954 0.06154  0.01909  -0.00854 342 ILE   B CG2 
5419 C  CD1 . ILE   B 342 ? 0.46415 0.52981 0.48301 0.04420  0.01484  -0.01016 342 ILE   B CD1 
5420 N  N   . ASN   B 343 ? 0.41045 0.44690 0.37357 0.07291  0.00525  -0.01793 343 ASN   B N   
5421 C  CA  . ASN   B 343 ? 0.42264 0.44806 0.36933 0.08161  0.00126  -0.02205 343 ASN   B CA  
5422 C  C   . ASN   B 343 ? 0.42330 0.43234 0.36850 0.07765  -0.00694 -0.02699 343 ASN   B C   
5423 O  O   . ASN   B 343 ? 0.45659 0.45658 0.39459 0.08026  -0.01050 -0.03010 343 ASN   B O   
5424 C  CB  . ASN   B 343 ? 0.48008 0.50547 0.41242 0.09140  0.00107  -0.02125 343 ASN   B CB  
5425 C  CG  . ASN   B 343 ? 0.56046 0.60334 0.49141 0.09738  0.00900  -0.01592 343 ASN   B CG  
5426 O  OD1 . ASN   B 343 ? 0.44843 0.49793 0.38210 0.09832  0.01261  -0.01524 343 ASN   B OD1 
5427 N  ND2 . ASN   B 343 ? 0.48118 0.53255 0.40867 0.10087  0.01158  -0.01152 343 ASN   B ND2 
5428 N  N   . LYS   B 344 ? 0.42882 0.43406 0.38087 0.07120  -0.01065 -0.02728 344 LYS   B N   
5429 C  CA  . LYS   B 344 ? 0.46479 0.45819 0.41897 0.06547  -0.01815 -0.03036 344 LYS   B CA  
5430 C  C   . LYS   B 344 ? 0.46990 0.46712 0.43417 0.05912  -0.01639 -0.03015 344 LYS   B C   
5431 O  O   . LYS   B 344 ? 0.42991 0.41692 0.38935 0.05836  -0.02181 -0.03220 344 LYS   B O   
5432 C  CB  . LYS   B 344 ? 0.42844 0.42215 0.39191 0.05903  -0.02093 -0.02976 344 LYS   B CB  
5433 C  CG  . LYS   B 344 ? 0.50593 0.49253 0.45843 0.06451  -0.02491 -0.03045 344 LYS   B CG  
5434 C  CD  . LYS   B 344 ? 0.46630 0.45697 0.43049 0.05819  -0.02585 -0.02902 344 LYS   B CD  
5435 C  CE  . LYS   B 344 ? 0.62646 0.60885 0.57973 0.06300  -0.03078 -0.02982 344 LYS   B CE  
5436 N  NZ  . LYS   B 344 ? 0.66417 0.64948 0.62912 0.05673  -0.03275 -0.02882 344 LYS   B NZ  
5437 N  N   . LEU   B 345 ? 0.36658 0.37777 0.34439 0.05443  -0.00951 -0.02749 345 LEU   B N   
5438 C  CA  . LEU   B 345 ? 0.40989 0.42563 0.39751 0.04837  -0.00773 -0.02731 345 LEU   B CA  
5439 C  C   . LEU   B 345 ? 0.44539 0.45893 0.42501 0.05307  -0.00649 -0.02794 345 LEU   B C   
5440 O  O   . LEU   B 345 ? 0.38772 0.39843 0.36988 0.04921  -0.00838 -0.02861 345 LEU   B O   
5441 C  CB  . LEU   B 345 ? 0.37245 0.40221 0.37448 0.04357  -0.00148 -0.02495 345 LEU   B CB  
5442 C  CG  . LEU   B 345 ? 0.39279 0.42417 0.40401 0.03851  -0.00371 -0.02506 345 LEU   B CG  
5443 C  CD1 . LEU   B 345 ? 0.38564 0.42872 0.40910 0.03513  0.00140  -0.02339 345 LEU   B CD1 
5444 C  CD2 . LEU   B 345 ? 0.44896 0.47619 0.46425 0.03318  -0.00879 -0.02654 345 LEU   B CD2 
5445 N  N   . LEU   B 346 ? 0.43389 0.44973 0.40402 0.06154  -0.00337 -0.02736 346 LEU   B N   
5446 C  CA  . LEU   B 346 ? 0.43131 0.44598 0.39366 0.06721  -0.00222 -0.02816 346 LEU   B CA  
5447 C  C   . LEU   B 346 ? 0.48484 0.48200 0.43094 0.07340  -0.01028 -0.03210 346 LEU   B C   
5448 O  O   . LEU   B 346 ? 0.48655 0.48037 0.42437 0.07923  -0.01065 -0.03346 346 LEU   B O   
5449 C  CB  . LEU   B 346 ? 0.40829 0.43558 0.36753 0.07457  0.00476  -0.02525 346 LEU   B CB  
5450 C  CG  . LEU   B 346 ? 0.37719 0.42071 0.35175 0.06844  0.01174  -0.02086 346 LEU   B CG  
5451 C  CD1 . LEU   B 346 ? 0.43698 0.49348 0.40716 0.07600  0.01753  -0.01663 346 LEU   B CD1 
5452 C  CD2 . LEU   B 346 ? 0.43678 0.48327 0.41978 0.06317  0.01339  -0.02114 346 LEU   B CD2 
5453 N  N   . GLN   B 347 ? 0.47320 0.45837 0.41360 0.07302  -0.01741 -0.03407 347 GLN   B N   
5454 C  CA  . GLN   B 347 ? 0.48501 0.45113 0.40805 0.07963  -0.02664 -0.03806 347 GLN   B CA  
5455 C  C   . GLN   B 347 ? 0.46938 0.42605 0.39021 0.07744  -0.03138 -0.03934 347 GLN   B C   
5456 O  O   . GLN   B 347 ? 0.47677 0.42283 0.38198 0.08697  -0.03528 -0.04237 347 GLN   B O   
5457 C  CB  . GLN   B 347 ? 0.53166 0.48535 0.45208 0.07620  -0.03524 -0.03946 347 GLN   B CB  
5458 C  CG  . GLN   B 347 ? 0.54965 0.48011 0.45279 0.08090  -0.04750 -0.04356 347 GLN   B CG  
5459 C  CD  . GLN   B 347 ? 0.71121 0.63252 0.62159 0.06972  -0.05520 -0.04249 347 GLN   B CD  
5460 O  OE1 . GLN   B 347 ? 0.74407 0.67224 0.66996 0.05848  -0.05507 -0.03942 347 GLN   B OE1 
5461 N  NE2 . GLN   B 347 ? 0.59616 0.50337 0.49554 0.07304  -0.06176 -0.04452 347 GLN   B NE2 
5462 N  N   . PRO   B 348 ? 0.44010 0.39886 0.37433 0.06597  -0.03234 -0.03725 348 PRO   B N   
5463 C  CA  . PRO   B 348 ? 0.43351 0.38195 0.36425 0.06369  -0.03800 -0.03777 348 PRO   B CA  
5464 C  C   . PRO   B 348 ? 0.48660 0.44193 0.41471 0.06985  -0.03178 -0.03795 348 PRO   B C   
5465 O  O   . PRO   B 348 ? 0.42750 0.37040 0.34450 0.07437  -0.03736 -0.03998 348 PRO   B O   
5466 C  CB  . PRO   B 348 ? 0.49228 0.44827 0.44041 0.05014  -0.03752 -0.03419 348 PRO   B CB  
5467 C  CG  . PRO   B 348 ? 0.47519 0.44961 0.43705 0.04732  -0.02826 -0.03235 348 PRO   B CG  
5468 C  CD  . PRO   B 348 ? 0.50374 0.47471 0.45612 0.05527  -0.02863 -0.03422 348 PRO   B CD  
5469 N  N   . VAL   B 349 ? 0.39942 0.37354 0.33677 0.07060  -0.02116 -0.03578 349 VAL   B N   
5470 C  CA  . VAL   B 349 ? 0.41918 0.40173 0.35455 0.07679  -0.01517 -0.03538 349 VAL   B CA  
5471 C  C   . VAL   B 349 ? 0.45723 0.43425 0.37451 0.09138  -0.01653 -0.03824 349 VAL   B C   
5472 O  O   . VAL   B 349 ? 0.46948 0.44009 0.37660 0.09857  -0.01893 -0.04035 349 VAL   B O   
5473 C  CB  . VAL   B 349 ? 0.38774 0.39158 0.33829 0.07282  -0.00469 -0.03158 349 VAL   B CB  
5474 C  CG1 . VAL   B 349 ? 0.42699 0.44089 0.37698 0.07826  0.00112  -0.03039 349 VAL   B CG1 
5475 C  CG2 . VAL   B 349 ? 0.44004 0.44876 0.40651 0.06032  -0.00392 -0.02972 349 VAL   B CG2 
5476 N  N   . ARG   B 350 ? 0.45915 0.43912 0.37168 0.09660  -0.01510 -0.03835 350 ARG   B N   
5477 C  CA  . ARG   B 350 ? 0.52669 0.50213 0.42045 0.11170  -0.01665 -0.04124 350 ARG   B CA  
5478 C  C   . ARG   B 350 ? 0.58089 0.53252 0.45779 0.11737  -0.02815 -0.04657 350 ARG   B C   
5479 O  O   . ARG   B 350 ? 0.54672 0.49398 0.41004 0.12902  -0.02964 -0.04941 350 ARG   B O   
5480 C  CB  . ARG   B 350 ? 0.55079 0.52760 0.43927 0.11577  -0.01644 -0.04114 350 ARG   B CB  
5481 C  CG  . ARG   B 350 ? 0.57645 0.57472 0.47334 0.11618  -0.00651 -0.03616 350 ARG   B CG  
5482 C  CD  . ARG   B 350 ? 0.55017 0.54594 0.43413 0.12500  -0.00819 -0.03716 350 ARG   B CD  
5483 N  NE  . ARG   B 350 ? 0.62311 0.60123 0.50362 0.12047  -0.01709 -0.04027 350 ARG   B NE  
5484 C  CZ  . ARG   B 350 ? 0.62095 0.60240 0.51574 0.10902  -0.01638 -0.03770 350 ARG   B CZ  
5485 N  NH1 . ARG   B 350 ? 0.59678 0.59597 0.50854 0.10153  -0.00808 -0.03267 350 ARG   B NH1 
5486 N  NH2 . ARG   B 350 ? 0.54477 0.51104 0.43667 0.10517  -0.02487 -0.04028 350 ARG   B NH2 
5487 N  N   . ASP   B 351 ? 0.50471 0.44033 0.38207 0.10930  -0.03721 -0.04779 351 ASP   B N   
5488 C  CA  . ASP   B 351 ? 0.58640 0.49678 0.44679 0.11408  -0.05021 -0.05244 351 ASP   B CA  
5489 C  C   . ASP   B 351 ? 0.52484 0.42979 0.38424 0.11350  -0.05255 -0.05277 351 ASP   B C   
5490 O  O   . ASP   B 351 ? 0.62812 0.51723 0.46937 0.12456  -0.05992 -0.05723 351 ASP   B O   
5491 C  CB  . ASP   B 351 ? 0.58484 0.48096 0.44780 0.10406  -0.05984 -0.05233 351 ASP   B CB  
5492 C  CG  . ASP   B 351 ? 0.70501 0.60048 0.56183 0.10882  -0.06049 -0.05370 351 ASP   B CG  
5493 O  OD1 . ASP   B 351 ? 0.74213 0.64282 0.58750 0.12181  -0.05624 -0.05567 351 ASP   B OD1 
5494 O  OD2 . ASP   B 351 ? 0.71499 0.60541 0.57822 0.09976  -0.06545 -0.05250 351 ASP   B OD2 
5495 N  N   . HIS   B 352 ? 0.51840 0.43530 0.39601 0.10139  -0.04706 -0.04840 352 HIS   B N   
5496 C  CA  . HIS   B 352 ? 0.52254 0.43540 0.39993 0.10022  -0.04887 -0.04814 352 HIS   B CA  
5497 C  C   . HIS   B 352 ? 0.58208 0.50074 0.44885 0.11492  -0.04413 -0.05051 352 HIS   B C   
5498 O  O   . HIS   B 352 ? 0.58223 0.48558 0.43475 0.12271  -0.05152 -0.05394 352 HIS   B O   
5499 C  CB  . HIS   B 352 ? 0.56265 0.49146 0.46116 0.08648  -0.04173 -0.04302 352 HIS   B CB  
5500 C  CG  . HIS   B 352 ? 0.54774 0.47323 0.44653 0.08455  -0.04338 -0.04222 352 HIS   B CG  
5501 N  ND1 . HIS   B 352 ? 0.56343 0.46870 0.45536 0.08040  -0.05518 -0.04253 352 HIS   B ND1 
5502 C  CD2 . HIS   B 352 ? 0.61439 0.55361 0.51904 0.08616  -0.03545 -0.04078 352 HIS   B CD2 
5503 C  CE1 . HIS   B 352 ? 0.61078 0.51755 0.50426 0.07956  -0.05409 -0.04135 352 HIS   B CE1 
5504 N  NE2 . HIS   B 352 ? 0.61826 0.54554 0.51929 0.08334  -0.04208 -0.04057 352 HIS   B NE2 
5505 N  N   . PHE   B 353 ? 0.54198 0.48210 0.41435 0.11965  -0.03281 -0.04861 353 PHE   B N   
5506 C  CA  . PHE   B 353 ? 0.53845 0.48899 0.40357 0.13282  -0.02718 -0.04942 353 PHE   B CA  
5507 C  C   . PHE   B 353 ? 0.60426 0.54644 0.44761 0.15032  -0.03127 -0.05430 353 PHE   B C   
5508 O  O   . PHE   B 353 ? 0.65597 0.60288 0.48943 0.16352  -0.02923 -0.05608 353 PHE   B O   
5509 C  CB  . PHE   B 353 ? 0.52121 0.50010 0.40248 0.12983  -0.01371 -0.04397 353 PHE   B CB  
5510 C  CG  . PHE   B 353 ? 0.51133 0.49943 0.40994 0.11772  -0.00935 -0.04029 353 PHE   B CG  
5511 C  CD1 . PHE   B 353 ? 0.45050 0.44204 0.34858 0.12116  -0.00784 -0.04016 353 PHE   B CD1 
5512 C  CD2 . PHE   B 353 ? 0.50283 0.49667 0.41790 0.10361  -0.00683 -0.03712 353 PHE   B CD2 
5513 C  CE1 . PHE   B 353 ? 0.44615 0.44514 0.35865 0.11066  -0.00444 -0.03709 353 PHE   B CE1 
5514 C  CE2 . PHE   B 353 ? 0.52814 0.53042 0.45779 0.09359  -0.00306 -0.03422 353 PHE   B CE2 
5515 C  CZ  . PHE   B 353 ? 0.52132 0.52599 0.44948 0.09699  -0.00187 -0.03415 353 PHE   B CZ  
5516 N  N   . GLN   B 354 ? 0.57805 0.50794 0.41296 0.15155  -0.03739 -0.05674 354 GLN   B N   
5517 C  CA  . GLN   B 354 ? 0.67854 0.59677 0.49002 0.16890  -0.04326 -0.06238 354 GLN   B CA  
5518 C  C   . GLN   B 354 ? 0.75611 0.64336 0.54992 0.17344  -0.05858 -0.06849 354 GLN   B C   
5519 O  O   . GLN   B 354 ? 0.74379 0.62157 0.51713 0.19049  -0.06335 -0.07393 354 GLN   B O   
5520 C  CB  . GLN   B 354 ? 0.68950 0.60838 0.49844 0.16921  -0.04326 -0.06232 354 GLN   B CB  
5521 C  CG  . GLN   B 354 ? 0.72755 0.67688 0.54827 0.16989  -0.02879 -0.05652 354 GLN   B CG  
5522 C  CD  . GLN   B 354 ? 0.80355 0.75616 0.62644 0.16666  -0.02759 -0.05483 354 GLN   B CD  
5523 O  OE1 . GLN   B 354 ? 0.95222 0.88497 0.76848 0.16368  -0.03732 -0.05815 354 GLN   B OE1 
5524 N  NE2 . GLN   B 354 ? 0.83720 0.81508 0.66992 0.16662  -0.01614 -0.04903 354 GLN   B NE2 
5525 N  N   . ASN   B 355 ? 0.66093 0.53276 0.46241 0.15848  -0.06676 -0.06727 355 ASN   B N   
5526 C  CA  . ASN   B 355 ? 0.77326 0.61285 0.55871 0.15972  -0.08379 -0.07188 355 ASN   B CA  
5527 C  C   . ASN   B 355 ? 0.66938 0.49877 0.45619 0.15492  -0.08923 -0.07122 355 ASN   B C   
5528 O  O   . ASN   B 355 ? 0.77160 0.57415 0.54039 0.16121  -0.10340 -0.07583 355 ASN   B O   
5529 C  CB  . ASN   B 355 ? 0.71116 0.53841 0.50214 0.14639  -0.09186 -0.07028 355 ASN   B CB  
5530 C  CG  . ASN   B 355 ? 0.82934 0.66125 0.61538 0.15214  -0.08940 -0.07178 355 ASN   B CG  
5531 O  OD1 . ASN   B 355 ? 0.85707 0.69100 0.62724 0.16896  -0.08730 -0.07591 355 ASN   B OD1 
5532 N  ND2 . ASN   B 355 ? 0.72338 0.55876 0.52304 0.13877  -0.08918 -0.06816 355 ASN   B ND2 
5533 N  N   . ASN   B 356 ? 0.62913 0.47777 0.43544 0.14457  -0.07928 -0.06578 356 ASN   B N   
5534 C  CA  . ASN   B 356 ? 0.68637 0.52881 0.49462 0.14060  -0.08267 -0.06460 356 ASN   B CA  
5535 C  C   . ASN   B 356 ? 0.72226 0.57442 0.52209 0.15640  -0.07654 -0.06730 356 ASN   B C   
5536 O  O   . ASN   B 356 ? 0.60832 0.48747 0.41971 0.15790  -0.06249 -0.06434 356 ASN   B O   
5537 C  CB  . ASN   B 356 ? 0.66336 0.52285 0.49639 0.12216  -0.07484 -0.05751 356 ASN   B CB  
5538 C  CG  . ASN   B 356 ? 0.74536 0.59961 0.58142 0.11661  -0.07806 -0.05542 356 ASN   B CG  
5539 O  OD1 . ASN   B 356 ? 0.68587 0.54973 0.52108 0.12400  -0.07207 -0.05600 356 ASN   B OD1 
5540 N  ND2 . ASN   B 356 ? 0.67687 0.51684 0.51702 0.10309  -0.08774 -0.05227 356 ASN   B ND2 
5541 N  N   . ILE   B 357 ? 0.67843 0.50865 0.45891 0.16749  -0.08772 -0.07243 357 ILE   B N   
5542 C  CA  . ILE   B 357 ? 0.70581 0.54347 0.47421 0.18624  -0.08357 -0.07626 357 ILE   B CA  
5543 C  C   . ILE   B 357 ? 0.73140 0.59287 0.51690 0.18124  -0.07164 -0.07128 357 ILE   B C   
5544 O  O   . ILE   B 357 ? 0.69719 0.58207 0.48502 0.19122  -0.06034 -0.07060 357 ILE   B O   
5545 C  CB  . ILE   B 357 ? 0.77819 0.58367 0.52136 0.19892  -0.10019 -0.08333 357 ILE   B CB  
5546 C  CG1 . ILE   B 357 ? 0.78906 0.56989 0.51277 0.20607  -0.11294 -0.08908 357 ILE   B CG1 
5547 C  CG2 . ILE   B 357 ? 0.79752 0.61114 0.52969 0.21776  -0.09635 -0.08697 357 ILE   B CG2 
5548 C  CD1 . ILE   B 357 ? 0.91856 0.71717 0.64278 0.21222  -0.10357 -0.08945 357 ILE   B CD1 
5549 N  N   . GLU   B 358 ? 0.69346 0.54979 0.49082 0.16589  -0.07441 -0.06732 358 GLU   B N   
5550 C  CA  . GLU   B 358 ? 0.69001 0.56674 0.50280 0.16065  -0.06433 -0.06285 358 GLU   B CA  
5551 C  C   . GLU   B 358 ? 0.66840 0.57590 0.50160 0.15328  -0.04887 -0.05763 358 GLU   B C   
5552 O  O   . GLU   B 358 ? 0.60092 0.53073 0.44225 0.15691  -0.03836 -0.05527 358 GLU   B O   
5553 C  CB  . GLU   B 358 ? 0.78026 0.64411 0.60030 0.14543  -0.07134 -0.05947 358 GLU   B CB  
5554 C  CG  . GLU   B 358 ? 0.91574 0.74562 0.71562 0.15059  -0.08910 -0.06360 358 GLU   B CG  
5555 C  CD  . GLU   B 358 ? 0.96176 0.76342 0.74541 0.15263  -0.10392 -0.06762 358 GLU   B CD  
5556 O  OE1 . GLU   B 358 ? 0.87866 0.68189 0.67051 0.14222  -0.10369 -0.06520 358 GLU   B OE1 
5557 O  OE2 . GLU   B 358 ? 1.01780 0.79395 0.77923 0.16539  -0.11709 -0.07355 358 GLU   B OE2 
5558 N  N   . ALA   B 359 ? 0.62763 0.53630 0.46968 0.14245  -0.04804 -0.05547 359 ALA   B N   
5559 C  CA  . ALA   B 359 ? 0.53299 0.46814 0.39345 0.13545  -0.03491 -0.05075 359 ALA   B CA  
5560 C  C   . ALA   B 359 ? 0.52237 0.47329 0.37687 0.14965  -0.02745 -0.05175 359 ALA   B C   
5561 O  O   . ALA   B 359 ? 0.54392 0.51982 0.41147 0.14825  -0.01601 -0.04741 359 ALA   B O   
5562 C  CB  . ALA   B 359 ? 0.59533 0.52636 0.46514 0.12174  -0.03703 -0.04870 359 ALA   B CB  
5563 N  N   . LYS   B 360 ? 0.54809 0.48497 0.38316 0.16272  -0.03425 -0.05693 360 LYS   B N   
5564 C  CA  . LYS   B 360 ? 0.54910 0.50120 0.37602 0.17795  -0.02773 -0.05779 360 LYS   B CA  
5565 C  C   . LYS   B 360 ? 0.63276 0.60162 0.45922 0.18840  -0.02122 -0.05682 360 LYS   B C   
5566 O  O   . LYS   B 360 ? 0.58083 0.57670 0.41594 0.19156  -0.00997 -0.05229 360 LYS   B O   
5567 C  CB  . LYS   B 360 ? 0.59743 0.52801 0.40024 0.19193  -0.03810 -0.06469 360 LYS   B CB  
5568 C  CG  . LYS   B 360 ? 0.65792 0.60401 0.44913 0.20986  -0.03198 -0.06594 360 LYS   B CG  
5569 C  CD  . LYS   B 360 ? 0.68488 0.60656 0.45067 0.22345  -0.04368 -0.07362 360 LYS   B CD  
5570 C  CE  . LYS   B 360 ? 0.73846 0.63188 0.48492 0.23301  -0.05739 -0.08076 360 LYS   B CE  
5571 N  NZ  . LYS   B 360 ? 0.90404 0.77308 0.62315 0.24908  -0.06965 -0.08904 360 LYS   B NZ  
5572 N  N   . ASN   B 361 ? 0.60754 0.56096 0.42474 0.19306  -0.02866 -0.06036 361 ASN   B N   
5573 C  CA  . ASN   B 361 ? 0.65311 0.62220 0.46954 0.20373  -0.02311 -0.05967 361 ASN   B CA  
5574 C  C   . ASN   B 361 ? 0.61492 0.60862 0.45519 0.19084  -0.01209 -0.05227 361 ASN   B C   
5575 O  O   . ASN   B 361 ? 0.62445 0.64324 0.47034 0.19755  -0.00281 -0.04874 361 ASN   B O   
5576 C  CB  . ASN   B 361 ? 0.63448 0.57934 0.43544 0.21113  -0.03467 -0.06522 361 ASN   B CB  
5577 C  CG  . ASN   B 361 ? 0.70864 0.63019 0.48315 0.22812  -0.04600 -0.07326 361 ASN   B CG  
5578 O  OD1 . ASN   B 361 ? 0.76769 0.69748 0.53284 0.24037  -0.04289 -0.07511 361 ASN   B OD1 
5579 N  ND2 . ASN   B 361 ? 0.79705 0.68855 0.55800 0.22974  -0.06004 -0.07810 361 ASN   B ND2 
5580 N  N   . LEU   B 362 ? 0.53708 0.52513 0.39162 0.17255  -0.01310 -0.04952 362 LEU   B N   
5581 C  CA  . LEU   B 362 ? 0.53392 0.54317 0.41009 0.16021  -0.00368 -0.04317 362 LEU   B CA  
5582 C  C   . LEU   B 362 ? 0.51315 0.54739 0.40136 0.15807  0.00687  -0.03804 362 LEU   B C   
5583 O  O   . LEU   B 362 ? 0.50339 0.56067 0.40360 0.15706  0.01536  -0.03298 362 LEU   B O   
5584 C  CB  . LEU   B 362 ? 0.48101 0.47877 0.36810 0.14236  -0.00741 -0.04177 362 LEU   B CB  
5585 C  CG  . LEU   B 362 ? 0.45855 0.47484 0.36662 0.12923  0.00087  -0.03618 362 LEU   B CG  
5586 C  CD1 . LEU   B 362 ? 0.47636 0.50474 0.38796 0.13329  0.00475  -0.03441 362 LEU   B CD1 
5587 C  CD2 . LEU   B 362 ? 0.50007 0.50407 0.41587 0.11368  -0.00370 -0.03545 362 LEU   B CD2 
5588 N  N   . LEU   B 363 ? 0.48968 0.51920 0.37612 0.15565  0.00578  -0.03859 363 LEU   B N   
5589 C  CA  . LEU   B 363 ? 0.49492 0.54612 0.39103 0.15405  0.01458  -0.03352 363 LEU   B CA  
5590 C  C   . LEU   B 363 ? 0.52915 0.59914 0.41809 0.16980  0.02015  -0.03187 363 LEU   B C   
5591 O  O   . LEU   B 363 ? 0.47209 0.56741 0.37351 0.16776  0.02904  -0.02511 363 LEU   B O   
5592 C  CB  . LEU   B 363 ? 0.47363 0.51391 0.36535 0.15137  0.01105  -0.03528 363 LEU   B CB  
5593 C  CG  . LEU   B 363 ? 0.46003 0.51967 0.35944 0.15019  0.01869  -0.03018 363 LEU   B CG  
5594 C  CD1 . LEU   B 363 ? 0.51380 0.58915 0.43507 0.13581  0.02521  -0.02405 363 LEU   B CD1 
5595 C  CD2 . LEU   B 363 ? 0.51196 0.55855 0.40628 0.14744  0.01419  -0.03241 363 LEU   B CD2 
5596 N  N   . ASN   B 364 ? 0.48370 0.54199 0.35224 0.18587  0.01455  -0.03768 364 ASN   B N   
5597 C  CA  . ASN   B 364 ? 0.57818 0.65673 0.43895 0.20263  0.02023  -0.03610 364 ASN   B CA  
5598 C  C   . ASN   B 364 ? 0.53991 0.63964 0.41263 0.20223  0.02680  -0.03113 364 ASN   B C   
5599 O  O   . ASN   B 364 ? 0.61162 0.73967 0.49152 0.20643  0.03556  -0.02458 364 ASN   B O   
5600 C  CB  . ASN   B 364 ? 0.52515 0.58552 0.36003 0.22165  0.01197  -0.04441 364 ASN   B CB  
5601 C  CG  . ASN   B 364 ? 0.75001 0.79884 0.57264 0.22578  0.00800  -0.04765 364 ASN   B CG  
5602 O  OD1 . ASN   B 364 ? 0.76104 0.81995 0.59483 0.21598  0.01301  -0.04284 364 ASN   B OD1 
5603 N  ND2 . ASN   B 364 ? 0.87983 0.90602 0.67883 0.24034  -0.00192 -0.05602 364 ASN   B ND2 
5604 N  N   . GLU   B 365 ? 0.49927 0.58639 0.37460 0.19677  0.02238  -0.03346 365 GLU   B N   
5605 C  CA  . GLU   B 365 ? 0.56901 0.67527 0.45611 0.19556  0.02803  -0.02880 365 GLU   B CA  
5606 C  C   . GLU   B 365 ? 0.63044 0.75851 0.54052 0.18037  0.03637  -0.02021 365 GLU   B C   
5607 O  O   . GLU   B 365 ? 0.57915 0.73360 0.49861 0.18276  0.04365  -0.01369 365 GLU   B O   
5608 C  CB  . GLU   B 365 ? 0.63367 0.72112 0.51939 0.19123  0.02132  -0.03264 365 GLU   B CB  
5609 C  CG  . GLU   B 365 ? 0.79528 0.86271 0.65916 0.20688  0.01244  -0.04028 365 GLU   B CG  
5610 C  CD  . GLU   B 365 ? 0.93620 0.98414 0.79992 0.20011  0.00520  -0.04288 365 GLU   B CD  
5611 O  OE1 . GLU   B 365 ? 0.96066 1.01941 0.84103 0.18821  0.00967  -0.03817 365 GLU   B OE1 
5612 O  OE2 . GLU   B 365 ? 1.06489 1.08538 0.91141 0.20600  -0.00575 -0.04944 365 GLU   B OE2 
5613 N  N   . ILE   B 366 ? 0.47930 0.59656 0.39903 0.16447  0.03471  -0.01991 366 ILE   B N   
5614 C  CA  . ILE   B 366 ? 0.50027 0.63528 0.44077 0.15057  0.04106  -0.01264 366 ILE   B CA  
5615 C  C   . ILE   B 366 ? 0.55071 0.70630 0.49679 0.15134  0.04740  -0.00627 366 ILE   B C   
5616 O  O   . ILE   B 366 ? 0.59918 0.77470 0.56118 0.14351  0.05288  0.00124  366 ILE   B O   
5617 C  CB  . ILE   B 366 ? 0.45103 0.57085 0.40092 0.13408  0.03777  -0.01407 366 ILE   B CB  
5618 C  CG1 . ILE   B 366 ? 0.55594 0.66284 0.50215 0.13013  0.03477  -0.01645 366 ILE   B CG1 
5619 C  CG2 . ILE   B 366 ? 0.42890 0.53024 0.37372 0.13262  0.03153  -0.01897 366 ILE   B CG2 
5620 C  CD1 . ILE   B 366 ? 0.62301 0.74146 0.58515 0.11802  0.03927  -0.01114 366 ILE   B CD1 
5621 N  N   . LYS   B 367 ? 0.51162 0.66272 0.44474 0.16042  0.04620  -0.00866 367 LYS   B N   
5622 C  CA  . LYS   B 367 ? 0.61715 0.78879 0.55418 0.16216  0.05219  -0.00196 367 LYS   B CA  
5623 C  C   . LYS   B 367 ? 0.63310 0.83399 0.57380 0.17090  0.05897  0.00504  367 LYS   B C   
5624 O  O   . LYS   B 367 ? 0.71458 0.93843 0.66616 0.16702  0.06486  0.01406  367 LYS   B O   
5625 C  CB  . LYS   B 367 ? 0.59041 0.75125 0.50981 0.17284  0.04915  -0.00659 367 LYS   B CB  
5626 C  CG  . LYS   B 367 ? 0.67202 0.81351 0.59224 0.16245  0.04462  -0.00964 367 LYS   B CG  
5627 C  CD  . LYS   B 367 ? 0.59649 0.72803 0.49813 0.17435  0.04120  -0.01414 367 LYS   B CD  
5628 C  CE  . LYS   B 367 ? 0.65686 0.77663 0.56171 0.16420  0.03847  -0.01472 367 LYS   B CE  
5629 N  NZ  . LYS   B 367 ? 0.66537 0.77261 0.55031 0.17635  0.03379  -0.01997 367 LYS   B NZ  
5630 N  N   . LYS   B 368 ? 0.58442 0.78528 0.51636 0.18256  0.05777  0.00155  368 LYS   B N   
5631 C  CA  . LYS   B 368 ? 0.70149 0.93165 0.63698 0.19194  0.06408  0.00815  368 LYS   B CA  
5632 C  C   . LYS   B 368 ? 0.63609 0.88272 0.59249 0.17931  0.06764  0.01572  368 LYS   B C   
5633 O  O   . LYS   B 368 ? 0.73633 1.01103 0.69957 0.18420  0.07322  0.02346  368 LYS   B O   
5634 C  CB  . LYS   B 368 ? 0.70483 0.92785 0.62165 0.21090  0.06070  0.00080  368 LYS   B CB  
5635 C  CG  . LYS   B 368 ? 0.68902 0.89636 0.58262 0.22603  0.05633  -0.00684 368 LYS   B CG  
5636 C  CD  . LYS   B 368 ? 0.81282 1.01599 0.68603 0.24805  0.05288  -0.01377 368 LYS   B CD  
5637 C  CE  . LYS   B 368 ? 0.85676 1.03504 0.70541 0.26083  0.04505  -0.02318 368 LYS   B CE  
5638 N  NZ  . LYS   B 368 ? 0.85976 1.04550 0.70602 0.26072  0.04791  -0.01983 368 LYS   B NZ  
5639 N  N   . TYR   B 369 ? 0.64430 0.87591 0.61120 0.16339  0.06452  0.01428  369 TYR   B N   
5640 C  CA  . TYR   B 369 ? 0.58133 0.82550 0.56607 0.15224  0.06659  0.02025  369 TYR   B CA  
5641 C  C   . TYR   B 369 ? 0.71054 0.97691 0.71166 0.14216  0.07128  0.03111  369 TYR   B C   
5642 O  O   . TYR   B 369 ? 0.70417 0.96557 0.70666 0.13593  0.07101  0.03219  369 TYR   B O   
5643 C  CB  . TYR   B 369 ? 0.57113 0.79224 0.56054 0.13931  0.06157  0.01497  369 TYR   B CB  
5644 C  CG  . TYR   B 369 ? 0.52146 0.72087 0.49830 0.14526  0.05604  0.00610  369 TYR   B CG  
5645 C  CD1 . TYR   B 369 ? 0.53583 0.73727 0.49939 0.16156  0.05531  0.00308  369 TYR   B CD1 
5646 C  CD2 . TYR   B 369 ? 0.48074 0.65749 0.45880 0.13451  0.05104  0.00102  369 TYR   B CD2 
5647 C  CE1 . TYR   B 369 ? 0.55093 0.72969 0.50254 0.16619  0.04873  -0.00487 369 TYR   B CE1 
5648 C  CE2 . TYR   B 369 ? 0.50549 0.66238 0.47290 0.13825  0.04529  -0.00578 369 TYR   B CE2 
5649 C  CZ  . TYR   B 369 ? 0.52169 0.67824 0.47565 0.15374  0.04367  -0.00876 369 TYR   B CZ  
5650 O  OH  . TYR   B 369 ? 0.51617 0.65008 0.45915 0.15638  0.03650  -0.01532 369 TYR   B OH  
5651 N  N   . LYS   B 370 ? 0.62919 0.91932 0.64317 0.13980  0.07474  0.03954  370 LYS   B N   
5652 C  CA  . LYS   B 370 ? 0.70395 1.01404 0.73492 0.12817  0.07755  0.05093  370 LYS   B CA  
5653 C  C   . LYS   B 370 ? 0.66700 0.96205 0.71004 0.11067  0.07344  0.04998  370 LYS   B C   
5654 O  O   . LYS   B 370 ? 0.67040 0.95312 0.71457 0.10739  0.07050  0.04479  370 LYS   B O   
5655 C  CB  . LYS   B 370 ? 0.79370 1.13585 0.83494 0.13131  0.08187  0.06137  370 LYS   B CB  
5656 C  CG  . LYS   B 370 ? 0.91711 1.28360 0.95049 0.14702  0.08732  0.06637  370 LYS   B CG  
5657 C  CD  . LYS   B 370 ? 0.95807 1.30784 0.96904 0.16459  0.08558  0.05474  370 LYS   B CD  
5658 C  CE  . LYS   B 370 ? 0.92910 1.29329 0.92825 0.17800  0.08643  0.05857  370 LYS   B CE  
5659 N  NZ  . LYS   B 370 ? 0.91847 1.26384 0.89488 0.19539  0.08304  0.04667  370 LYS   B NZ  
5660 N  N   . VAL   B 371 ? 0.64412 0.93973 0.69521 0.10012  0.07291  0.05478  371 VAL   B N   
5661 C  CA  . VAL   B 371 ? 0.70696 0.98756 0.76794 0.08490  0.06853  0.05323  371 VAL   B CA  
5662 C  C   . VAL   B 371 ? 0.70283 1.00142 0.78100 0.07486  0.06821  0.06342  371 VAL   B C   
5663 O  O   . VAL   B 371 ? 0.72919 1.04947 0.81487 0.07328  0.07052  0.07431  371 VAL   B O   
5664 C  CB  . VAL   B 371 ? 0.74281 1.01134 0.80220 0.07938  0.06681  0.05193  371 VAL   B CB  
5665 C  CG1 . VAL   B 371 ? 0.75266 1.01389 0.82505 0.06402  0.06267  0.05381  371 VAL   B CG1 
5666 C  CG2 . VAL   B 371 ? 0.63437 0.87882 0.67871 0.08552  0.06476  0.04032  371 VAL   B CG2 
5667 N  N   . THR   B 372 ? 0.64777 0.93772 0.73199 0.06793  0.06486  0.06042  372 THR   B N   
5668 C  CA  . THR   B 372 ? 0.75960 1.06375 0.85923 0.05852  0.06307  0.06902  372 THR   B CA  
5669 C  C   . THR   B 372 ? 0.77558 1.06131 0.88167 0.04554  0.05714  0.06545  372 THR   B C   
5670 O  O   . THR   B 372 ? 0.50984 0.77381 0.60896 0.04446  0.05520  0.05629  372 THR   B O   
5671 C  CB  . THR   B 372 ? 0.57299 0.88754 0.67381 0.06406  0.06429  0.06938  372 THR   B CB  
5672 O  OG1 . THR   B 372 ? 0.63769 0.92986 0.73174 0.06430  0.06154  0.05845  372 THR   B OG1 
5673 C  CG2 . THR   B 372 ? 0.59733 0.92978 0.68996 0.07952  0.06992  0.07144  372 THR   B CG2 
5674 N  N   . LYS   B 373 ? 0.96000 1.25552 1.07934 0.03630  0.05390  0.07288  373 LYS   B N   
5675 C  CA  . LYS   B 373 ? 0.91747 1.19816 1.04341 0.02481  0.04736  0.07036  373 LYS   B CA  
5676 C  C   . LYS   B 373 ? 0.93315 1.22765 1.07081 0.01926  0.04448  0.07774  373 LYS   B C   
5677 O  O   . LYS   B 373 ? 0.74898 1.06568 0.89050 0.02385  0.04798  0.08544  373 LYS   B O   
5678 C  CB  . LYS   B 373 ? 0.92834 1.20279 1.05860 0.01630  0.04359  0.07354  373 LYS   B CB  
5679 C  CG  . LYS   B 373 ? 1.02877 1.32583 1.16838 0.01281  0.04414  0.08768  373 LYS   B CG  
5680 C  CD  . LYS   B 373 ? 1.10551 1.39704 1.24368 0.00969  0.04309  0.08967  373 LYS   B CD  
5681 C  CE  . LYS   B 373 ? 1.14301 1.41355 1.28451 -0.00060 0.03511  0.08570  373 LYS   B CE  
5682 N  NZ  . LYS   B 373 ? 1.22075 1.49614 1.37494 -0.01146 0.02794  0.09363  373 LYS   B NZ  
5683 O  OXT . LYS   B 373 ? 0.97169 1.25687 1.11515 0.01068  0.03844  0.07652  373 LYS   B OXT 
5684 C  C02 . A1AZG C .   ? 0.45680 0.60660 0.54010 -0.01774 -0.11213 0.00873  401 A1AZG A C02 
5685 C  C03 . A1AZG C .   ? 0.39090 0.53496 0.46322 -0.01464 -0.11794 0.00511  401 A1AZG A C03 
5686 C  C05 . A1AZG C .   ? 0.37876 0.52543 0.43973 -0.00537 -0.09586 -0.00024 401 A1AZG A C05 
5687 C  C06 . A1AZG C .   ? 0.41944 0.57807 0.50042 -0.01180 -0.09711 0.00872  401 A1AZG A C06 
5688 C  C08 . A1AZG C .   ? 0.40601 0.54137 0.45429 -0.00186 -0.09181 -0.00848 401 A1AZG A C08 
5689 C  C12 . A1AZG C .   ? 0.38891 0.52315 0.45199 -0.00682 -0.08288 -0.00808 401 A1AZG A C12 
5690 C  C13 . A1AZG C .   ? 0.39917 0.54551 0.47048 -0.00617 -0.07094 -0.00319 401 A1AZG A C13 
5691 C  C15 . A1AZG C .   ? 0.41418 0.56003 0.47308 0.00066  -0.05966 -0.00775 401 A1AZG A C15 
5692 C  C16 . A1AZG C .   ? 0.39174 0.54868 0.45817 0.00162  -0.05078 -0.00233 401 A1AZG A C16 
5693 C  C17 . A1AZG C .   ? 0.32070 0.47816 0.38658 0.00333  -0.04224 -0.00336 401 A1AZG A C17 
5694 C  C18 . A1AZG C .   ? 0.30137 0.46836 0.37355 0.00493  -0.03501 0.00152  401 A1AZG A C18 
5695 C  C19 . A1AZG C .   ? 0.31016 0.48746 0.38909 0.00579  -0.03531 0.00738  401 A1AZG A C19 
5696 C  C20 . A1AZG C .   ? 0.33453 0.51324 0.41545 0.00388  -0.04320 0.00908  401 A1AZG A C20 
5697 C  C21 . A1AZG C .   ? 0.36338 0.53119 0.43790 0.00142  -0.05103 0.00417  401 A1AZG A C21 
5698 C  C27 . A1AZG C .   ? 0.42257 0.55077 0.49356 -0.02206 -0.14569 0.00457  401 A1AZG A C27 
5699 C  C29 . A1AZG C .   ? 0.42247 0.56212 0.50835 -0.02933 -0.16068 0.01539  401 A1AZG A C29 
5700 C  C31 . A1AZG C .   ? 0.45040 0.55428 0.51428 -0.02825 -0.17481 0.00056  401 A1AZG A C31 
5701 C  C33 . A1AZG C .   ? 0.48103 0.58985 0.54228 -0.02333 -0.15907 -0.00200 401 A1AZG A C33 
5702 C  C34 . A1AZG C .   ? 0.47282 0.57191 0.52312 -0.01842 -0.15246 -0.01006 401 A1AZG A C34 
5703 C  C35 . A1AZG C .   ? 0.64293 0.72038 0.67850 -0.01576 -0.16223 -0.02006 401 A1AZG A C35 
5704 C  C36 . A1AZG C .   ? 0.69640 0.76776 0.74027 -0.02128 -0.16772 -0.01834 401 A1AZG A C36 
5705 C  C37 . A1AZG C .   ? 0.65990 0.73109 0.67450 -0.00444 -0.15148 -0.03136 401 A1AZG A C37 
5706 N  N11 . A1AZG C .   ? 0.42367 0.55154 0.47174 -0.00151 -0.08246 -0.01436 401 A1AZG A N11 
5707 N  N14 . A1AZG C .   ? 0.36980 0.51525 0.44872 -0.00986 -0.07174 -0.00161 401 A1AZG A N14 
5708 N  N26 . A1AZG C .   ? 0.48522 0.61400 0.55136 -0.01748 -0.13274 0.00085  401 A1AZG A N26 
5709 N  N28 . A1AZG C .   ? 0.45446 0.59819 0.53759 -0.02452 -0.14605 0.01310  401 A1AZG A N28 
5710 N  N30 . A1AZG C .   ? 0.45134 0.57160 0.52854 -0.03180 -0.17512 0.00978  401 A1AZG A N30 
5711 N  N32 . A1AZG C .   ? 0.52240 0.60605 0.57654 -0.02952 -0.19041 -0.00546 401 A1AZG A N32 
5712 N  N38 . A1AZG C .   ? 0.45668 0.56886 0.51098 -0.01556 -0.13655 -0.00766 401 A1AZG A N38 
5713 O  O01 . A1AZG C .   ? 0.45145 0.61435 0.55368 -0.02489 -0.11672 0.01911  401 A1AZG A O01 
5714 O  O04 . A1AZG C .   ? 0.43655 0.57545 0.49346 -0.00724 -0.10847 -0.00197 401 A1AZG A O04 
5715 O  O07 . A1AZG C .   ? 0.40002 0.57492 0.49196 -0.01185 -0.09453 0.01669  401 A1AZG A O07 
5716 O  O09 . A1AZG C .   ? 0.42767 0.55260 0.47502 -0.00447 -0.10002 -0.01200 401 A1AZG A O09 
5717 O  O22 . A1AZG C .   ? 0.29095 0.47676 0.37403 0.00899  -0.02878 0.01117  401 A1AZG A O22 
5718 O  O23 . A1AZG C .   ? 0.43901 0.56794 0.50760 -0.01203 -0.09420 -0.00658 401 A1AZG A O23 
5719 O  O24 . A1AZG C .   ? 0.41851 0.53176 0.43881 0.00673  -0.08848 -0.02598 401 A1AZG A O24 
5720 O  O25 . A1AZG C .   ? 0.44834 0.55248 0.48403 -0.00264 -0.10557 -0.02326 401 A1AZG A O25 
5721 S  S10 . A1AZG C .   ? 0.44328 0.55911 0.47931 0.00011  -0.09375 -0.02029 401 A1AZG A S10 
5751 C  C1  . MLI   D .   ? 0.48887 0.98301 0.66460 0.13991  0.01039  0.09415  402 MLI   A C1  
5752 C  C2  . MLI   D .   ? 0.52769 0.98721 0.69457 0.12640  0.00836  0.08671  402 MLI   A C2  
5753 C  C3  . MLI   D .   ? 0.59616 1.12017 0.78362 0.14002  0.01652  0.10416  402 MLI   A C3  
5754 O  O6  . MLI   D .   ? 0.48625 0.91670 0.63742 0.12837  0.00531  0.07705  402 MLI   A O6  
5755 O  O7  . MLI   D .   ? 0.47529 0.93852 0.65118 0.11453  0.00960  0.09116  402 MLI   A O7  
5756 O  O8  . MLI   D .   ? 0.58382 1.10819 0.77990 0.12673  0.01709  0.10821  402 MLI   A O8  
5757 O  O9  . MLI   D .   ? 0.49622 1.03362 0.67858 0.15113  0.02013  0.10648  402 MLI   A O9  
5760 CL CL  . CL    E .   ? 0.70426 0.80516 0.70663 0.04806  0.00984  -0.00129 403 CL    A CL  
5761 NA NA  . NA    F .   ? 0.46006 0.56330 0.51835 -0.01472 -0.11698 -0.01456 404 NA    A NA  
5762 C  C02 . A1AZG G .   ? 0.33334 0.44804 0.41965 0.01144  0.02476  -0.01268 401 A1AZG B C02 
5763 C  C03 . A1AZG G .   ? 0.29961 0.41237 0.38155 0.01398  0.02700  -0.01282 401 A1AZG B C03 
5764 C  C05 . A1AZG G .   ? 0.32032 0.43624 0.39819 0.01542  0.03050  -0.01471 401 A1AZG B C05 
5765 C  C06 . A1AZG G .   ? 0.33419 0.44940 0.41756 0.01267  0.02690  -0.01645 401 A1AZG B C06 
5766 C  C08 . A1AZG G .   ? 0.30628 0.42713 0.38267 0.01691  0.03258  -0.01095 401 A1AZG B C08 
5767 C  C12 . A1AZG G .   ? 0.32421 0.45604 0.41173 0.01111  0.02881  -0.00610 401 A1AZG B C12 
5768 C  C13 . A1AZG G .   ? 0.34588 0.47565 0.43183 0.01081  0.02824  -0.01041 401 A1AZG B C13 
5769 C  C15 . A1AZG G .   ? 0.28451 0.41481 0.36446 0.01388  0.03190  -0.01148 401 A1AZG B C15 
5770 C  C16 . A1AZG G .   ? 0.30148 0.42938 0.37936 0.01317  0.03139  -0.01584 401 A1AZG B C16 
5771 C  C17 . A1AZG G .   ? 0.29094 0.42113 0.36774 0.01313  0.03143  -0.01569 401 A1AZG B C17 
5772 C  C18 . A1AZG G .   ? 0.25387 0.38288 0.32825 0.01261  0.03108  -0.01932 401 A1AZG B C18 
5773 C  C19 . A1AZG G .   ? 0.30850 0.43562 0.38187 0.01245  0.03103  -0.02306 401 A1AZG B C19 
5774 C  C20 . A1AZG G .   ? 0.29588 0.42088 0.37092 0.01258  0.03081  -0.02350 401 A1AZG B C20 
5775 C  C21 . A1AZG G .   ? 0.24558 0.37019 0.32262 0.01274  0.03080  -0.02005 401 A1AZG B C21 
5776 C  C27 . A1AZG G .   ? 0.33848 0.44935 0.42240 0.01307  0.02415  -0.00721 401 A1AZG B C27 
5777 C  C29 . A1AZG G .   ? 0.35149 0.45347 0.43638 0.01276  0.01956  -0.01045 401 A1AZG B C29 
5778 C  C31 . A1AZG G .   ? 0.36918 0.48193 0.45476 0.01157  0.02199  0.00152  401 A1AZG B C31 
5779 C  C33 . A1AZG G .   ? 0.33170 0.44744 0.41646 0.01258  0.02450  -0.00042 401 A1AZG B C33 
5780 C  C34 . A1AZG G .   ? 0.33106 0.45503 0.41608 0.01322  0.02732  0.00329  401 A1AZG B C34 
5781 C  C35 . A1AZG G .   ? 0.40105 0.53601 0.48736 0.01368  0.02936  0.01157  401 A1AZG B C35 
5782 C  C36 . A1AZG G .   ? 0.42120 0.56415 0.50947 0.01390  0.03118  0.01390  401 A1AZG B C36 
5783 C  C37 . A1AZG G .   ? 0.48751 0.62397 0.56531 0.02009  0.03327  0.01201  401 A1AZG B C37 
5784 N  N11 . A1AZG G .   ? 0.34081 0.47369 0.42352 0.01482  0.03238  -0.00511 401 A1AZG B N11 
5785 N  N14 . A1AZG G .   ? 0.30828 0.44015 0.39829 0.00831  0.02513  -0.00882 401 A1AZG B N14 
5786 N  N26 . A1AZG G .   ? 0.31876 0.43334 0.40192 0.01360  0.02641  -0.00764 401 A1AZG B N26 
5787 N  N28 . A1AZG G .   ? 0.31488 0.41986 0.39896 0.01324  0.02199  -0.01211 401 A1AZG B N28 
5788 N  N30 . A1AZG G .   ? 0.35787 0.46261 0.44334 0.01168  0.01922  -0.00392 401 A1AZG B N30 
5789 N  N32 . A1AZG G .   ? 0.37940 0.49795 0.46606 0.01060  0.02213  0.00895  401 A1AZG B N32 
5790 N  N38 . A1AZG G .   ? 0.37305 0.49494 0.45681 0.01388  0.02817  -0.00165 401 A1AZG B N38 
5791 O  O01 . A1AZG G .   ? 0.35796 0.46826 0.44768 0.00970  0.02003  -0.01519 401 A1AZG B O01 
5792 O  O04 . A1AZG G .   ? 0.31403 0.42845 0.39115 0.01636  0.03024  -0.01271 401 A1AZG B O04 
5793 O  O07 . A1AZG G .   ? 0.34401 0.45644 0.42676 0.01319  0.02616  -0.02170 401 A1AZG B O07 
5794 O  O09 . A1AZG G .   ? 0.34030 0.46642 0.42076 0.01584  0.03200  -0.00611 401 A1AZG B O09 
5795 O  O22 . A1AZG G .   ? 0.29702 0.42565 0.36797 0.01246  0.03118  -0.02589 401 A1AZG B O22 
5796 O  O23 . A1AZG G .   ? 0.34396 0.47638 0.43650 0.00819  0.02562  -0.00301 401 A1AZG B O23 
5797 O  O24 . A1AZG G .   ? 0.33895 0.47352 0.41259 0.02252  0.03698  -0.00208 401 A1AZG B O24 
5798 O  O25 . A1AZG G .   ? 0.32630 0.46830 0.41287 0.01522  0.03302  0.00472  401 A1AZG B O25 
5799 S  S10 . A1AZG G .   ? 0.35654 0.49133 0.43749 0.01727  0.03402  -0.00161 401 A1AZG B S10 
5829 C  C1  . MLI   H .   ? 0.61685 0.92847 0.66570 0.09747  0.05122  -0.07041 402 MLI   B C1  
5830 C  C2  . MLI   H .   ? 0.59148 0.88008 0.64198 0.08514  0.04875  -0.06706 402 MLI   B C2  
5831 C  C3  . MLI   H .   ? 0.76963 1.07920 0.80653 0.11351  0.04723  -0.08193 402 MLI   B C3  
5832 O  O6  . MLI   H .   ? 0.55001 0.81690 0.59470 0.08687  0.04304  -0.07332 402 MLI   B O6  
5833 O  O7  . MLI   H .   ? 0.61123 0.90487 0.66913 0.07388  0.05225  -0.05763 402 MLI   B O7  
5834 O  O8  . MLI   H .   ? 0.61685 0.95019 0.65017 0.12451  0.05076  -0.08362 402 MLI   B O8  
5835 O  O9  . MLI   H .   ? 0.78706 1.07095 0.81862 0.11430  0.04018  -0.08848 402 MLI   B O9  
5838 CL CL  . CL    I .   ? 0.56911 0.72166 0.57985 -0.00189 0.02974  0.00039  403 CL    B CL  
5839 NA NA  . NA    J .   ? 0.50633 0.49311 0.44195 0.07117  -0.04493 -0.00052 404 NA    B NA  
5840 NA NA  . NA    K .   ? 0.58847 0.64192 0.62204 -0.02468 -0.01396 0.00572  405 NA    B NA  
5841 NA NA  . NA    L .   ? 0.35447 0.49683 0.45337 0.00580  0.02494  0.00875  406 NA    B NA  
5842 O  O   . HOH   M .   ? 0.61610 1.18296 0.82749 0.19388  -0.08688 0.11477  501 HOH   A O   
5843 O  O   . HOH   M .   ? 0.61762 0.77161 0.78579 -0.08201 -0.19393 0.05911  502 HOH   A O   
5844 O  O   . HOH   M .   ? 0.54806 0.77286 0.59172 0.09866  -0.06424 0.03736  503 HOH   A O   
5845 O  O   . HOH   M .   ? 0.62274 1.26554 0.81858 0.27482  -0.06686 0.11364  504 HOH   A O   
5846 O  O   . HOH   M .   ? 0.54180 0.96222 0.82662 -0.04912 -0.15752 0.14142  505 HOH   A O   
5847 O  O   . HOH   M .   ? 0.76688 0.87300 0.73417 0.03840  -0.02786 0.01622  506 HOH   A O   
5848 O  O   . HOH   M .   ? 0.55994 0.63047 0.58359 0.01682  -0.07248 -0.05667 507 HOH   A O   
5849 O  O   . HOH   M .   ? 0.59757 0.76526 0.62862 0.07414  0.00499  0.01035  508 HOH   A O   
5850 O  O   . HOH   M .   ? 0.69853 0.71686 0.69424 -0.01956 -0.24878 -0.03080 509 HOH   A O   
5851 O  O   . HOH   M .   ? 0.71375 0.91926 0.77806 0.06627  0.03671  0.01556  510 HOH   A O   
5852 O  O   . HOH   M .   ? 0.47110 0.56498 0.46151 0.01675  -0.09549 -0.04187 511 HOH   A O   
5853 O  O   . HOH   M .   ? 0.87156 1.13703 0.65678 0.06732  0.00375  0.00261  512 HOH   A O   
5854 O  O   . HOH   M .   ? 0.43647 0.79533 0.68051 -0.04389 -0.10098 0.11302  513 HOH   A O   
5855 O  O   . HOH   M .   ? 0.59794 0.76009 0.59671 0.06581  -0.07127 0.02773  514 HOH   A O   
5856 O  O   . HOH   M .   ? 0.89632 0.90561 0.75134 0.07037  -0.16642 -0.10419 515 HOH   A O   
5857 O  O   . HOH   M .   ? 0.66094 0.80946 0.56182 0.02831  -0.02676 -0.00334 516 HOH   A O   
5858 O  O   . HOH   M .   ? 0.68710 0.89355 0.59343 0.04683  0.01181  -0.02809 517 HOH   A O   
5859 O  O   . HOH   M .   ? 0.40001 0.66919 0.58457 -0.03547 -0.09482 0.07085  518 HOH   A O   
5860 O  O   . HOH   M .   ? 0.71427 0.84395 0.58858 0.03565  -0.06166 -0.00112 519 HOH   A O   
5861 O  O   . HOH   M .   ? 0.58901 0.85479 0.68959 0.06311  0.03033  0.03618  520 HOH   A O   
5862 O  O   . HOH   M .   ? 0.57161 0.79610 0.60947 0.12382  -0.02701 0.02680  521 HOH   A O   
5863 O  O   . HOH   M .   ? 0.43696 0.97820 0.64248 0.10960  0.02716  0.12261  522 HOH   A O   
5864 O  O   . HOH   M .   ? 0.43541 0.95119 0.64615 0.08175  0.03105  0.12342  523 HOH   A O   
5865 O  O   . HOH   M .   ? 0.49626 0.61481 0.47895 0.00845  0.00712  0.00895  524 HOH   A O   
5866 O  O   . HOH   M .   ? 0.67806 0.75683 0.55512 0.05486  -0.11501 -0.06622 525 HOH   A O   
5867 O  O   . HOH   M .   ? 0.50749 0.61976 0.57650 -0.02104 -0.12870 -0.00520 526 HOH   A O   
5868 O  O   . HOH   M .   ? 0.52153 0.70729 0.55628 0.06695  -0.03104 0.02216  527 HOH   A O   
5869 O  O   . HOH   M .   ? 0.46142 0.64186 0.47965 0.04915  -0.08038 0.02671  528 HOH   A O   
5870 O  O   . HOH   M .   ? 0.58884 0.71997 0.53245 0.03467  -0.08178 0.00834  529 HOH   A O   
5871 O  O   . HOH   M .   ? 0.56665 0.70093 0.57609 0.04374  -0.00708 0.00774  530 HOH   A O   
5872 O  O   . HOH   M .   ? 0.69867 1.14086 0.82210 0.20262  -0.03459 0.06932  531 HOH   A O   
5873 O  O   . HOH   M .   ? 0.44379 1.23110 0.68362 0.26780  -0.02348 0.15582  532 HOH   A O   
5874 O  O   . HOH   M .   ? 0.54374 0.92452 0.66072 0.15186  -0.03011 0.06195  533 HOH   A O   
5875 O  O   . HOH   M .   ? 0.45908 0.58544 0.43776 0.02055  -0.00852 0.00578  534 HOH   A O   
5876 O  O   . HOH   M .   ? 0.36383 0.65413 0.47934 0.06406  0.00023  0.04523  535 HOH   A O   
5877 O  O   . HOH   M .   ? 0.87105 1.03889 0.92232 -0.00945 -0.26243 0.03872  536 HOH   A O   
5878 O  O   . HOH   M .   ? 0.76520 0.87307 0.76234 0.00610  0.01371  0.00604  537 HOH   A O   
5879 O  O   . HOH   M .   ? 0.34168 0.83145 0.55959 0.07664  -0.00432 0.11241  538 HOH   A O   
5880 O  O   . HOH   M .   ? 0.43922 0.71023 0.51627 0.10543  -0.00857 0.03574  539 HOH   A O   
5881 O  O   . HOH   M .   ? 0.50394 0.67597 0.53446 0.06693  -0.01380 0.01589  540 HOH   A O   
5882 O  O   . HOH   M .   ? 0.43835 0.59914 0.50231 -0.00358 -0.10382 0.00808  541 HOH   A O   
5883 O  O   . HOH   M .   ? 0.58037 1.09807 0.86157 0.00103  -0.01667 0.15694  542 HOH   A O   
5884 O  O   . HOH   M .   ? 0.57449 1.23806 0.64078 0.38602  0.00017  0.07848  543 HOH   A O   
5885 O  O   . HOH   M .   ? 0.48518 0.59513 0.56989 -0.02934 -0.12979 -0.00022 544 HOH   A O   
5886 O  O   . HOH   M .   ? 0.46015 0.82898 0.69253 -0.03681 -0.01281 0.12554  545 HOH   A O   
5887 O  O   . HOH   M .   ? 0.46829 0.75247 0.59725 0.03762  0.03425  0.05189  546 HOH   A O   
5888 O  O   . HOH   M .   ? 0.69143 0.81770 0.64975 0.06771  -0.08473 0.03045  547 HOH   A O   
5889 O  O   . HOH   M .   ? 0.81402 0.87192 0.73415 0.05947  -0.09802 -0.09110 548 HOH   A O   
5890 O  O   . HOH   M .   ? 0.52763 0.65428 0.65860 -0.04526 -0.09635 0.02085  549 HOH   A O   
5891 O  O   . HOH   M .   ? 0.59709 0.66097 0.57603 0.05276  -0.06546 -0.08944 550 HOH   A O   
5892 O  O   . HOH   M .   ? 0.41613 0.55326 0.44284 0.01406  0.02099  -0.01100 551 HOH   A O   
5893 O  O   . HOH   M .   ? 0.56614 0.77036 0.59741 0.06887  -0.09089 0.03727  552 HOH   A O   
5894 O  O   . HOH   M .   ? 0.41753 0.60220 0.47030 0.06384  0.02468  0.01029  553 HOH   A O   
5895 O  O   . HOH   M .   ? 0.45616 0.94243 0.74167 -0.02064 -0.03742 0.15475  554 HOH   A O   
5896 O  O   . HOH   M .   ? 0.58024 1.29228 0.88163 0.12834  -0.03839 0.17910  555 HOH   A O   
5897 O  O   . HOH   M .   ? 0.48894 0.83237 0.62994 0.07121  0.00568  0.06178  556 HOH   A O   
5898 O  O   . HOH   M .   ? 0.56154 0.62386 0.58155 0.00073  -0.12371 -0.04231 557 HOH   A O   
5899 O  O   . HOH   M .   ? 0.43701 0.71770 0.60864 -0.01563 -0.07882 0.06549  558 HOH   A O   
5900 O  O   . HOH   M .   ? 0.33531 0.56369 0.46279 -0.00226 -0.04426 0.03553  559 HOH   A O   
5901 O  O   . HOH   M .   ? 0.48435 0.75602 0.64193 -0.00295 0.01952  0.06785  560 HOH   A O   
5902 O  O   . HOH   M .   ? 0.51908 0.66378 0.69271 -0.08163 -0.15203 0.05799  561 HOH   A O   
5903 O  O   . HOH   M .   ? 0.43752 0.64289 0.61986 -0.06488 -0.12309 0.06503  562 HOH   A O   
5904 O  O   . HOH   M .   ? 0.58710 1.22326 0.84280 0.14559  -0.03259 0.14476  563 HOH   A O   
5905 O  O   . HOH   M .   ? 0.73400 0.85858 0.68530 0.01305  -0.01015 0.01434  564 HOH   A O   
5906 O  O   . HOH   M .   ? 0.35878 0.71077 0.49891 0.08095  -0.00100 0.06287  565 HOH   A O   
5907 O  O   . HOH   M .   ? 0.56183 0.68008 0.56418 0.03863  -0.00042 0.00502  566 HOH   A O   
5908 O  O   . HOH   M .   ? 0.72819 0.84056 0.69173 0.05694  -0.05149 0.02234  567 HOH   A O   
5909 O  O   . HOH   M .   ? 0.41895 0.91399 0.74805 -0.05583 -0.12159 0.17413  568 HOH   A O   
5910 O  O   . HOH   M .   ? 0.52943 0.97967 0.82576 -0.04328 -0.13004 0.14921  569 HOH   A O   
5911 O  O   . HOH   M .   ? 0.55561 0.71267 0.56547 0.05776  -0.03832 0.01899  570 HOH   A O   
5912 O  O   . HOH   M .   ? 0.71963 0.93177 0.73265 0.15957  -0.04191 0.02360  571 HOH   A O   
5913 O  O   . HOH   M .   ? 0.60782 0.84062 0.68616 0.02884  -0.12888 0.04442  572 HOH   A O   
5914 O  O   . HOH   M .   ? 0.65031 1.13652 0.75950 0.23988  -0.00186 0.06831  573 HOH   A O   
5915 O  O   . HOH   M .   ? 0.69851 0.97320 0.76792 0.11130  -0.10089 0.05468  574 HOH   A O   
5916 O  O   . HOH   M .   ? 0.51214 0.73466 0.58936 0.06205  0.03059  0.02142  575 HOH   A O   
5917 O  O   . HOH   M .   ? 0.63716 0.82091 0.65726 0.10133  -0.03522 0.02303  576 HOH   A O   
5918 O  O   . HOH   M .   ? 0.54452 0.88819 0.64893 0.13793  -0.04436 0.05692  577 HOH   A O   
5919 O  O   . HOH   M .   ? 0.58581 0.66786 0.57912 0.01168  -0.11728 -0.04128 578 HOH   A O   
5920 O  O   . HOH   M .   ? 0.45363 0.55334 0.50507 -0.00885 -0.10298 -0.02162 579 HOH   A O   
5921 O  O   . HOH   M .   ? 0.53013 1.06475 0.73059 0.09005  0.04264  0.13252  580 HOH   A O   
5922 O  O   . HOH   M .   ? 0.69679 0.73624 0.72323 -0.02397 -0.20794 -0.02471 581 HOH   A O   
5923 O  O   . HOH   M .   ? 0.61298 0.72927 0.57158 0.03129  -0.03343 0.01572  582 HOH   A O   
5924 O  O   . HOH   M .   ? 0.35418 0.87609 0.56971 0.10565  -0.00100 0.11402  583 HOH   A O   
5925 O  O   . HOH   M .   ? 0.75398 0.94307 0.64937 0.03336  0.00071  -0.00888 584 HOH   A O   
5926 O  O   . HOH   M .   ? 0.72920 0.90230 0.73267 0.08140  -0.08004 0.03269  585 HOH   A O   
5927 O  O   . HOH   M .   ? 0.48910 0.79347 0.74215 -0.08569 -0.12043 0.12040  586 HOH   A O   
5928 O  O   . HOH   M .   ? 0.39743 0.72249 0.63111 -0.05876 -0.03733 0.12105  587 HOH   A O   
5929 O  O   . HOH   M .   ? 0.49747 0.87282 0.62473 0.13313  -0.05580 0.06801  588 HOH   A O   
5930 O  O   . HOH   M .   ? 0.42165 0.77106 0.58672 0.02945  0.03381  0.08352  589 HOH   A O   
5931 O  O   . HOH   M .   ? 0.69557 0.66531 0.76251 -0.02811 -0.16604 -0.03388 590 HOH   A O   
5932 O  O   . HOH   M .   ? 0.52752 0.85962 0.64536 0.09275  0.01808  0.05276  591 HOH   A O   
5933 O  O   . HOH   M .   ? 0.53211 0.81853 0.63076 0.08491  0.00883  0.04021  592 HOH   A O   
5934 O  O   . HOH   M .   ? 0.58526 0.96960 0.69411 0.15508  0.00596  0.05700  593 HOH   A O   
5935 O  O   . HOH   M .   ? 0.60839 0.68967 0.60746 0.01280  -0.10458 -0.04491 594 HOH   A O   
5936 O  O   . HOH   M .   ? 0.44529 0.88376 0.71811 -0.03575 -0.04187 0.14500  595 HOH   A O   
5937 O  O   . HOH   M .   ? 0.53806 0.73571 0.73179 -0.08830 -0.21082 0.07978  596 HOH   A O   
5938 O  O   . HOH   M .   ? 0.54640 0.97559 0.85944 -0.07686 -0.17251 0.16044  597 HOH   A O   
5939 O  O   . HOH   M .   ? 0.61931 0.94326 0.72739 0.10485  -0.10373 0.06672  598 HOH   A O   
5940 O  O   . HOH   M .   ? 0.61483 0.87594 0.67416 0.11892  -0.07684 0.04644  599 HOH   A O   
5941 O  O   . HOH   M .   ? 0.48528 0.65871 0.55979 -0.00599 -0.11718 0.01710  600 HOH   A O   
5942 O  O   . HOH   M .   ? 0.52470 0.71467 0.59887 0.04328  0.03386  0.01201  601 HOH   A O   
5943 O  O   . HOH   M .   ? 0.55046 0.69180 0.53779 0.00648  0.01575  0.00184  602 HOH   A O   
5944 O  O   . HOH   M .   ? 0.68065 0.85614 0.63057 0.05897  0.00601  -0.06274 603 HOH   A O   
5945 O  O   . HOH   M .   ? 0.55550 0.83622 0.81141 -0.10475 -0.09238 0.13930  604 HOH   A O   
5946 O  O   . HOH   M .   ? 0.65032 0.86716 0.70582 0.08731  0.01188  0.01969  605 HOH   A O   
5947 O  O   . HOH   M .   ? 0.66104 1.03523 0.93781 -0.07139 -0.18831 0.13642  606 HOH   A O   
5948 O  O   . HOH   M .   ? 0.79467 0.82200 0.75301 0.04228  -0.11701 -0.08752 607 HOH   A O   
5949 O  O   . HOH   M .   ? 0.66904 1.01792 0.73828 0.19113  -0.00387 0.04133  608 HOH   A O   
5950 O  O   . HOH   M .   ? 0.66005 0.69093 0.77666 -0.05559 -0.14202 0.00727  609 HOH   A O   
5951 O  O   . HOH   M .   ? 0.42570 0.63003 0.63590 -0.08683 -0.08275 0.09851  610 HOH   A O   
5952 O  O   . HOH   M .   ? 0.67109 0.82962 0.63057 0.02584  0.00139  -0.02336 611 HOH   A O   
5953 O  O   . HOH   M .   ? 0.43648 1.00581 0.66528 0.10881  0.00851  0.13216  612 HOH   A O   
5954 O  O   . HOH   M .   ? 0.54393 1.05699 0.82056 0.03715  -0.13082 0.14101  613 HOH   A O   
5955 O  O   . HOH   M .   ? 0.54853 0.61985 0.58267 -0.00920 -0.13537 -0.03016 614 HOH   A O   
5956 O  O   . HOH   M .   ? 0.62549 0.79194 0.64654 0.07171  -0.02391 0.01780  615 HOH   A O   
5957 O  O   . HOH   M .   ? 0.60354 0.84019 0.64994 0.12264  -0.01472 0.02665  616 HOH   A O   
5958 O  O   . HOH   M .   ? 0.58322 0.72213 0.57419 0.07101  -0.04530 0.02090  617 HOH   A O   
5959 O  O   . HOH   M .   ? 0.62614 1.25301 0.66280 0.39366  0.00291  0.06525  618 HOH   A O   
5960 O  O   . HOH   M .   ? 0.49014 1.01433 0.81868 -0.03423 -0.11166 0.17391  619 HOH   A O   
5961 O  O   . HOH   M .   ? 0.70040 0.86737 0.88715 -0.09487 -0.21650 0.07406  620 HOH   A O   
5962 O  O   . HOH   M .   ? 0.48841 1.04105 0.70694 0.08927  0.02993  0.13691  621 HOH   A O   
5963 O  O   . HOH   M .   ? 0.86541 0.96071 0.80162 0.13277  -0.10625 0.03220  622 HOH   A O   
5964 O  O   . HOH   M .   ? 0.64617 0.79087 0.66021 0.05473  -0.01194 0.01098  623 HOH   A O   
5965 O  O   . HOH   N .   ? 0.64960 0.76243 0.74689 0.05632  -0.00557 -0.06869 501 HOH   B O   
5966 O  O   . HOH   N .   ? 0.66092 0.83586 0.77490 0.07072  0.00397  -0.07127 502 HOH   B O   
5967 O  O   . HOH   N .   ? 0.61966 0.69045 0.57403 0.06722  -0.00081 0.03596  503 HOH   B O   
5968 O  O   . HOH   N .   ? 0.79047 0.99074 1.00481 -0.09639 -0.07810 0.11680  504 HOH   B O   
5969 O  O   . HOH   N .   ? 0.59853 0.90093 0.75842 -0.00147 0.02586  0.00250  505 HOH   B O   
5970 O  O   . HOH   N .   ? 0.48241 0.57242 0.56102 0.04025  -0.00790 -0.06436 506 HOH   B O   
5971 O  O   . HOH   N .   ? 0.53066 0.55994 0.62050 0.02662  -0.03646 -0.02803 507 HOH   B O   
5972 O  O   . HOH   N .   ? 0.62483 0.72508 0.63554 0.10026  -0.02844 -0.11534 508 HOH   B O   
5973 O  O   . HOH   N .   ? 0.58022 0.72526 0.64451 0.03387  0.04183  0.00435  509 HOH   B O   
5974 O  O   . HOH   N .   ? 0.58974 0.74878 0.60638 0.14118  -0.01439 -0.12996 510 HOH   B O   
5975 O  O   . HOH   N .   ? 0.47403 0.60602 0.52446 0.04047  0.04094  0.00267  511 HOH   B O   
5976 O  O   . HOH   N .   ? 0.48081 0.62212 0.54242 -0.00690 -0.00398 0.10566  512 HOH   B O   
5977 O  O   . HOH   N .   ? 0.49428 0.49421 0.49756 0.01040  -0.02685 -0.01920 513 HOH   B O   
5978 O  O   . HOH   N .   ? 0.66088 0.84482 0.56890 0.21098  0.04846  -0.01202 514 HOH   B O   
5979 O  O   . HOH   N .   ? 0.71669 0.81598 0.83002 -0.01354 -0.01081 0.01562  515 HOH   B O   
5980 O  O   . HOH   N .   ? 0.42693 0.56258 0.47565 0.03709  0.03546  0.02238  516 HOH   B O   
5981 O  O   . HOH   N .   ? 0.62724 0.87930 0.63022 0.13374  0.02529  -0.10855 517 HOH   B O   
5982 O  O   . HOH   N .   ? 0.45499 0.70629 0.52779 0.01705  0.05188  -0.02041 518 HOH   B O   
5983 O  O   . HOH   N .   ? 0.53011 0.59620 0.52826 0.01393  0.00863  -0.00044 519 HOH   B O   
5984 O  O   . HOH   N .   ? 0.52340 0.80176 0.56285 0.11617  0.06840  0.03813  520 HOH   B O   
5985 O  O   . HOH   N .   ? 0.64591 1.40294 0.81971 0.15090  0.07775  0.02961  521 HOH   B O   
5986 O  O   . HOH   N .   ? 0.38573 0.48234 0.47142 0.02035  0.00366  -0.04368 522 HOH   B O   
5987 O  O   . HOH   N .   ? 0.54098 0.59550 0.58749 0.01908  -0.00070 -0.02560 523 HOH   B O   
5988 O  O   . HOH   N .   ? 0.57704 0.88155 0.70035 0.00536  0.04653  -0.00191 524 HOH   B O   
5989 O  O   . HOH   N .   ? 0.68299 0.77256 0.68386 0.01752  0.01257  0.00083  525 HOH   B O   
5990 O  O   . HOH   N .   ? 0.59347 0.64682 0.51512 0.10115  0.00905  -0.00472 526 HOH   B O   
5991 O  O   . HOH   N .   ? 0.41200 0.53572 0.48308 0.01895  0.02523  0.02179  527 HOH   B O   
5992 O  O   . HOH   N .   ? 0.68474 0.76784 0.58515 0.15062  0.02737  -0.02138 528 HOH   B O   
5993 O  O   . HOH   N .   ? 0.38983 0.37811 0.46202 0.04105  -0.07188 -0.02053 529 HOH   B O   
5994 O  O   . HOH   N .   ? 0.54653 0.57453 0.55767 0.02210  -0.04122 0.05554  530 HOH   B O   
5995 O  O   . HOH   N .   ? 0.54200 0.76491 0.64254 -0.01426 0.01820  0.12372  531 HOH   B O   
5996 O  O   . HOH   N .   ? 0.40858 0.46829 0.49754 0.00277  -0.01724 0.01101  532 HOH   B O   
5997 O  O   . HOH   N .   ? 0.47685 0.71053 0.61598 -0.00043 0.02091  0.04921  533 HOH   B O   
5998 O  O   . HOH   N .   ? 0.40195 0.38715 0.40979 0.04579  -0.06144 -0.00288 534 HOH   B O   
5999 O  O   . HOH   N .   ? 0.54074 0.85502 0.67653 0.01231  0.04355  -0.00617 535 HOH   B O   
6000 O  O   . HOH   N .   ? 0.42224 0.46896 0.52757 0.06229  -0.05534 -0.05539 536 HOH   B O   
6001 O  O   . HOH   N .   ? 0.54210 0.57437 0.47445 0.10011  0.00923  -0.02706 537 HOH   B O   
6002 O  O   . HOH   N .   ? 0.41239 0.52731 0.49546 0.02424  0.01584  -0.04672 538 HOH   B O   
6003 O  O   . HOH   N .   ? 0.51166 0.64415 0.55258 -0.00794 0.03035  -0.00320 539 HOH   B O   
6004 O  O   . HOH   N .   ? 0.67475 0.86083 0.62843 0.14820  -0.00539 -0.13225 540 HOH   B O   
6005 O  O   . HOH   N .   ? 0.47158 0.70991 0.54419 0.06165  0.05780  0.03924  541 HOH   B O   
6006 O  O   . HOH   N .   ? 0.43117 0.49740 0.51912 0.01516  -0.00539 -0.01598 542 HOH   B O   
6007 O  O   . HOH   N .   ? 0.53661 0.55190 0.56207 0.03247  -0.03249 -0.02734 543 HOH   B O   
6008 O  O   . HOH   N .   ? 0.62792 0.70178 0.57205 0.12824  0.01571  -0.02316 544 HOH   B O   
6009 O  O   . HOH   N .   ? 0.49463 0.53221 0.51923 -0.01127 -0.01378 -0.00423 545 HOH   B O   
6010 O  O   . HOH   N .   ? 0.49456 0.65919 0.56917 0.02206  0.03494  0.04222  546 HOH   B O   
6011 O  O   . HOH   N .   ? 0.48499 0.72560 0.63533 -0.03509 0.00264  0.02002  547 HOH   B O   
6012 O  O   . HOH   N .   ? 0.48556 0.60225 0.57741 -0.02145 -0.00720 -0.00383 548 HOH   B O   
6013 O  O   . HOH   N .   ? 0.60780 0.92380 0.74375 -0.02145 0.03897  0.02373  549 HOH   B O   
6014 O  O   . HOH   N .   ? 0.46390 0.82034 0.58098 0.03058  0.05866  -0.01053 550 HOH   B O   
6015 O  O   . HOH   N .   ? 0.62439 0.53126 0.53175 0.06411  -0.06064 -0.04059 551 HOH   B O   
6016 O  O   . HOH   N .   ? 0.38475 0.57734 0.43999 0.03233  0.03972  -0.04590 552 HOH   B O   
6017 O  O   . HOH   N .   ? 0.68123 0.61711 0.51973 0.16713  -0.03708 -0.05542 553 HOH   B O   
6018 O  O   . HOH   N .   ? 0.45720 0.64132 0.56655 -0.10187 -0.03084 0.07998  554 HOH   B O   
6019 O  O   . HOH   N .   ? 0.56019 0.74806 0.59390 0.01710  0.04094  -0.02800 555 HOH   B O   
6020 O  O   . HOH   N .   ? 0.51354 0.61072 0.62501 0.03127  -0.02529 -0.03845 556 HOH   B O   
6021 O  O   . HOH   N .   ? 0.47124 0.53046 0.57179 -0.05137 -0.06568 0.11195  557 HOH   B O   
6022 O  O   . HOH   N .   ? 0.40377 0.53314 0.49946 0.00624  0.02284  0.00337  558 HOH   B O   
6023 O  O   . HOH   N .   ? 0.49563 0.57707 0.58801 0.02711  -0.00181 -0.03698 559 HOH   B O   
6024 O  O   . HOH   N .   ? 0.46955 0.65390 0.58064 0.00603  0.03005  0.03297  560 HOH   B O   
6025 O  O   . HOH   N .   ? 0.50880 0.63706 0.60929 -0.00174 0.01302  0.02937  561 HOH   B O   
6026 O  O   . HOH   N .   ? 0.45423 0.50540 0.40769 0.06027  -0.01600 0.04146  562 HOH   B O   
6027 O  O   . HOH   N .   ? 0.52008 0.55732 0.44380 0.10515  0.00941  -0.02285 563 HOH   B O   
6028 O  O   . HOH   N .   ? 0.50709 0.54212 0.57411 0.02263  -0.05397 -0.02859 564 HOH   B O   
6029 O  O   . HOH   N .   ? 0.53063 0.58328 0.63172 -0.00757 -0.03031 0.01281  565 HOH   B O   
6030 O  O   . HOH   N .   ? 0.40272 0.52932 0.43646 0.02211  0.02502  -0.00754 566 HOH   B O   
6031 O  O   . HOH   N .   ? 0.45350 0.49058 0.46822 0.02652  -0.03028 0.04369  567 HOH   B O   
6032 O  O   . HOH   N .   ? 0.34708 0.45795 0.43786 0.00620  0.00695  -0.02543 568 HOH   B O   
6033 O  O   . HOH   N .   ? 0.59759 0.76484 0.60724 0.04431  0.01957  -0.05928 569 HOH   B O   
6034 O  O   . HOH   N .   ? 0.53580 0.54927 0.52143 0.05332  -0.02031 -0.01614 570 HOH   B O   
6035 O  O   . HOH   N .   ? 0.78532 0.66989 0.65075 0.10078  -0.06298 -0.04619 571 HOH   B O   
6036 O  O   . HOH   N .   ? 0.53446 0.64628 0.53133 0.04868  -0.02214 -0.07576 572 HOH   B O   
6037 O  O   . HOH   N .   ? 0.58635 0.66344 0.69492 -0.00928 -0.02128 -0.00086 573 HOH   B O   
6038 O  O   . HOH   N .   ? 0.57070 0.74818 0.55494 0.12341  -0.00018 -0.11793 574 HOH   B O   
6039 O  O   . HOH   N .   ? 0.51948 0.56792 0.63401 -0.04260 -0.06114 0.06960  575 HOH   B O   
6040 O  O   . HOH   N .   ? 0.50972 0.62184 0.61332 0.01574  -0.00340 -0.03159 576 HOH   B O   
6041 O  O   . HOH   N .   ? 0.56662 0.69485 0.67887 -0.00851 0.00670  0.02036  577 HOH   B O   
6042 O  O   . HOH   N .   ? 0.82919 0.73724 0.58209 0.22212  -0.04980 -0.07593 578 HOH   B O   
6043 O  O   . HOH   N .   ? 0.64654 0.62349 0.54825 0.09883  -0.02267 -0.03499 579 HOH   B O   
6044 O  O   . HOH   N .   ? 0.50913 0.49583 0.53409 0.03648  -0.06254 0.00872  580 HOH   B O   
6045 O  O   . HOH   N .   ? 0.48903 0.54773 0.53238 0.02174  0.00659  -0.02486 581 HOH   B O   
6046 O  O   . HOH   N .   ? 0.79336 0.88566 0.62785 0.19581  0.02626  -0.01932 582 HOH   B O   
6047 O  O   . HOH   N .   ? 0.54881 0.58947 0.60994 0.01396  -0.03828 -0.02621 583 HOH   B O   
6048 O  O   . HOH   N .   ? 0.70040 0.69237 0.53318 0.18224  -0.00998 -0.05071 584 HOH   B O   
6049 O  O   . HOH   N .   ? 0.36196 0.58290 0.41984 0.04812  0.04195  -0.05406 585 HOH   B O   
6050 O  O   . HOH   N .   ? 0.53049 0.61897 0.65320 -0.04982 -0.04820 0.09083  586 HOH   B O   
6051 O  O   . HOH   N .   ? 0.39700 0.46380 0.41051 0.00768  0.01241  -0.00580 587 HOH   B O   
6052 O  O   . HOH   N .   ? 0.63414 0.64777 0.64430 0.04559  -0.08925 -0.09117 588 HOH   B O   
6053 O  O   . HOH   N .   ? 0.48588 0.58600 0.56030 0.01751  0.02578  -0.02132 589 HOH   B O   
6054 O  O   . HOH   N .   ? 0.54255 0.58774 0.56790 0.02733  0.00433  -0.02472 590 HOH   B O   
6055 O  O   . HOH   N .   ? 0.59154 0.66884 0.57231 0.06583  -0.04864 -0.09730 591 HOH   B O   
6056 O  O   . HOH   N .   ? 0.71101 0.74248 0.52714 0.23783  -0.00246 -0.05465 592 HOH   B O   
6057 O  O   . HOH   N .   ? 0.49848 0.61893 0.62312 -0.02553 -0.03141 0.01197  593 HOH   B O   
6058 O  O   . HOH   N .   ? 0.49817 0.62372 0.52747 -0.00687 0.02761  0.00003  594 HOH   B O   
6059 O  O   . HOH   N .   ? 0.38429 0.47561 0.47103 0.02123  0.01053  -0.03307 595 HOH   B O   
6060 O  O   . HOH   N .   ? 0.44458 0.61754 0.46299 0.02231  0.03132  -0.03384 596 HOH   B O   
6061 O  O   . HOH   N .   ? 0.65018 0.77912 0.60575 0.08743  0.03127  0.03536  597 HOH   B O   
6062 O  O   . HOH   N .   ? 0.48940 0.56740 0.58086 0.02451  -0.00054 -0.03495 598 HOH   B O   
6063 O  O   . HOH   N .   ? 0.48688 0.57025 0.57483 0.01683  0.00759  -0.02408 599 HOH   B O   
6064 O  O   . HOH   N .   ? 0.54202 0.57990 0.63407 0.01527  -0.02977 -0.01832 600 HOH   B O   
6065 O  O   . HOH   N .   ? 0.47021 0.57075 0.58647 0.04500  -0.02447 -0.04862 601 HOH   B O   
6066 O  O   . HOH   N .   ? 0.46794 0.61254 0.54137 0.02247  0.03347  0.02484  602 HOH   B O   
6067 O  O   . HOH   N .   ? 0.48027 0.46672 0.47033 0.02241  -0.03086 -0.02516 603 HOH   B O   
6068 O  O   . HOH   N .   ? 0.82593 0.60596 0.54552 0.20230  -0.11383 -0.09065 604 HOH   B O   
6069 O  O   . HOH   N .   ? 0.48620 0.55149 0.54061 0.01131  0.00186  -0.02374 605 HOH   B O   
6070 O  O   . HOH   N .   ? 0.39456 0.47268 0.49402 -0.00212 -0.02333 -0.02099 606 HOH   B O   
6071 O  O   . HOH   N .   ? 0.50926 0.49533 0.59650 0.04691  -0.07531 -0.04216 607 HOH   B O   
6072 O  O   . HOH   N .   ? 0.43908 0.66246 0.48521 0.09176  0.02804  -0.08627 608 HOH   B O   
6073 O  O   . HOH   N .   ? 0.44357 0.46288 0.51345 0.04167  -0.05678 -0.02848 609 HOH   B O   
6074 O  O   . HOH   N .   ? 0.52525 0.52559 0.56551 0.02974  -0.05183 0.00867  610 HOH   B O   
6075 O  O   . HOH   N .   ? 0.34421 0.45012 0.41778 0.01700  0.02900  -0.02001 611 HOH   B O   
6076 O  O   . HOH   N .   ? 0.66306 0.80984 0.71106 0.04825  0.04500  0.00586  612 HOH   B O   
6077 O  O   . HOH   N .   ? 0.51377 0.68980 0.57413 -0.00926 0.03847  -0.00477 613 HOH   B O   
6078 O  O   . HOH   N .   ? 0.32505 0.44702 0.40232 0.01581  0.02151  -0.03678 614 HOH   B O   
6079 O  O   . HOH   N .   ? 0.51047 0.57378 0.44437 0.09099  0.00940  0.00645  615 HOH   B O   
6080 O  O   . HOH   N .   ? 0.57650 0.55605 0.55144 0.04102  -0.03253 -0.03162 616 HOH   B O   
6081 O  O   . HOH   N .   ? 0.53854 0.52037 0.48205 0.06516  -0.01585 -0.02780 617 HOH   B O   
6082 O  O   . HOH   N .   ? 0.53893 0.73704 0.55389 0.09402  0.05883  0.02232  618 HOH   B O   
6083 O  O   . HOH   N .   ? 0.75752 0.77093 0.75214 0.02168  -0.05620 0.07042  619 HOH   B O   
6084 O  O   . HOH   N .   ? 0.77561 0.54572 0.54378 0.14893  -0.12164 -0.07226 620 HOH   B O   
6085 O  O   . HOH   N .   ? 0.44778 0.58104 0.55287 -0.01696 -0.00172 0.06634  621 HOH   B O   
6086 O  O   . HOH   N .   ? 0.59505 0.67087 0.62265 0.08393  -0.03593 -0.10612 622 HOH   B O   
6087 O  O   . HOH   N .   ? 0.54705 0.62068 0.66879 -0.03010 -0.05403 0.00880  623 HOH   B O   
6088 O  O   . HOH   N .   ? 0.62615 0.82896 0.65546 -0.00703 0.04295  0.00364  624 HOH   B O   
6089 O  O   . HOH   N .   ? 0.60201 0.72406 0.72385 -0.06268 -0.04777 0.13556  625 HOH   B O   
6090 O  O   . HOH   N .   ? 0.56325 0.80184 0.78628 -0.08868 -0.06823 0.11752  626 HOH   B O   
6091 O  O   . HOH   N .   ? 0.60496 0.55380 0.54300 0.05242  -0.03604 -0.03104 627 HOH   B O   
6092 O  O   . HOH   N .   ? 0.62380 0.59156 0.54835 0.07553  -0.05479 -0.01266 628 HOH   B O   
6093 O  O   . HOH   N .   ? 0.49180 0.69862 0.58275 0.01166  0.03514  0.07498  629 HOH   B O   
6094 O  O   . HOH   N .   ? 0.46776 0.50168 0.53144 -0.00557 -0.04543 0.05744  630 HOH   B O   
6095 O  O   . HOH   N .   ? 0.53317 0.80610 0.58573 0.10337  0.03829  -0.08354 631 HOH   B O   
6096 O  O   . HOH   N .   ? 0.70249 0.56230 0.57071 0.08033  -0.08200 -0.04667 632 HOH   B O   
6097 O  O   . HOH   N .   ? 0.54370 0.58566 0.63295 0.04223  -0.04815 -0.03614 633 HOH   B O   
6098 O  O   . HOH   N .   ? 0.66526 0.67807 0.59194 0.10900  -0.00298 -0.03080 634 HOH   B O   
6099 O  O   . HOH   N .   ? 0.51053 0.68463 0.52505 -0.00591 0.03533  0.00362  635 HOH   B O   
6100 O  O   . HOH   N .   ? 0.51143 0.65414 0.60112 0.01011  0.02642  0.02668  636 HOH   B O   
6101 O  O   . HOH   N .   ? 0.63122 0.70180 0.67241 -0.03745 -0.01428 0.01671  637 HOH   B O   
6102 O  O   . HOH   N .   ? 0.81207 0.94071 0.75456 0.15015  -0.03318 -0.14528 638 HOH   B O   
6103 O  O   . HOH   N .   ? 0.70624 0.93383 0.73115 0.11515  0.02221  -0.10150 639 HOH   B O   
6104 O  O   . HOH   N .   ? 0.53060 0.52698 0.45026 0.09032  -0.01561 -0.02701 640 HOH   B O   
6105 O  O   . HOH   N .   ? 0.73467 0.95544 0.86714 -0.00520 0.02626  0.06203  641 HOH   B O   
6106 O  O   . HOH   N .   ? 0.81714 0.63794 0.64947 0.10200  -0.09830 -0.05031 642 HOH   B O   
6107 O  O   . HOH   N .   ? 0.75853 0.89122 0.61464 0.19301  0.04025  -0.00757 643 HOH   B O   
6108 O  O   . HOH   N .   ? 0.62839 0.78717 0.66861 0.14267  -0.01763 -0.12768 644 HOH   B O   
6109 O  O   . HOH   N .   ? 0.55459 0.76373 0.58825 0.10443  0.04508  0.01222  645 HOH   B O   
6110 O  O   . HOH   N .   ? 0.51081 0.67209 0.55008 0.01371  0.01201  0.10132  646 HOH   B O   
6111 O  O   . HOH   N .   ? 0.66050 0.79255 0.63340 0.07101  0.02740  0.04748  647 HOH   B O   
6112 O  O   . HOH   N .   ? 0.58708 0.91698 0.81076 -0.06071 -0.01129 0.14294  648 HOH   B O   
6113 O  O   . HOH   N .   ? 0.35464 0.48725 0.46101 -0.00199 0.01414  0.00837  649 HOH   B O   
6114 O  O   . HOH   N .   ? 0.74784 0.81670 0.69888 0.11789  0.01190  -0.02112 650 HOH   B O   
6115 O  O   . HOH   N .   ? 0.60032 0.63442 0.58366 0.06449  -0.07800 -0.10404 651 HOH   B O   
6116 O  O   . HOH   N .   ? 0.73595 0.75277 0.71909 0.01645  -0.00934 -0.00584 652 HOH   B O   
6117 O  O   . HOH   N .   ? 0.68727 0.77366 0.76029 0.07666  -0.02515 -0.09032 653 HOH   B O   
6118 O  O   . HOH   N .   ? 0.51710 0.65518 0.58615 -0.03534 0.01084  0.01524  654 HOH   B O   
6119 O  O   . HOH   N .   ? 1.00249 0.85426 0.80009 0.14442  -0.08163 -0.06806 655 HOH   B O   
6120 O  O   . HOH   N .   ? 0.33819 0.49209 0.44088 0.00517  0.02562  0.01294  656 HOH   B O   
6121 O  O   . HOH   N .   ? 0.51649 0.56475 0.53585 -0.01114 -0.00508 0.00017  657 HOH   B O   
6122 O  O   . HOH   N .   ? 0.61746 0.78880 0.50926 0.15233  0.04880  0.02971  658 HOH   B O   
6123 O  O   . HOH   N .   ? 0.57373 0.58384 0.55259 0.05577  -0.01839 -0.02083 659 HOH   B O   
6124 O  O   . HOH   N .   ? 0.52885 0.67646 0.60315 0.02640  0.03929  0.00918  660 HOH   B O   
6125 O  O   . HOH   N .   ? 0.51125 0.57438 0.61036 0.00442  -0.01839 -0.01549 661 HOH   B O   
6126 O  O   . HOH   N .   ? 0.48388 0.69881 0.62204 0.01396  0.01490  -0.02421 662 HOH   B O   
6127 O  O   . HOH   N .   ? 0.59050 0.92010 0.65411 0.05879  0.06240  -0.03684 663 HOH   B O   
6128 O  O   . HOH   N .   ? 0.61435 0.60914 0.71050 -0.01542 -0.07406 0.02642  664 HOH   B O   
6129 O  O   . HOH   N .   ? 0.33329 0.41775 0.44083 0.04425  -0.02252 -0.04912 665 HOH   B O   
6130 O  O   . HOH   N .   ? 0.63194 0.73161 0.71970 0.06166  -0.01253 -0.07580 666 HOH   B O   
6131 O  O   . HOH   N .   ? 0.82418 0.66053 0.67809 0.08318  -0.09435 -0.04794 667 HOH   B O   
6132 O  O   . HOH   N .   ? 0.63331 0.64444 0.53770 0.07630  -0.04294 0.04138  668 HOH   B O   
6133 O  O   . HOH   N .   ? 0.56123 1.21129 0.72144 0.16960  0.06281  -0.01780 669 HOH   B O   
6134 O  O   . HOH   N .   ? 0.53192 0.62050 0.62486 0.02492  0.00376  -0.04059 670 HOH   B O   
6135 O  O   . HOH   N .   ? 0.43012 0.59231 0.51082 -0.01699 -0.00190 0.11501  671 HOH   B O   
6136 O  O   . HOH   N .   ? 0.34464 0.41399 0.45046 0.05248  -0.03298 -0.05452 672 HOH   B O   
6137 O  O   . HOH   N .   ? 0.61133 0.81984 0.64729 0.02478  0.04464  -0.03292 673 HOH   B O   
6138 O  O   . HOH   N .   ? 0.45178 0.65338 0.49959 0.04880  0.03666  -0.05850 674 HOH   B O   
6139 O  O   . HOH   N .   ? 0.44504 0.56202 0.46742 0.01338  -0.00685 0.09666  675 HOH   B O   
6140 O  O   . HOH   N .   ? 0.53769 0.53876 0.57090 0.02281  -0.10270 -0.07303 676 HOH   B O   
6141 O  O   . HOH   N .   ? 0.49973 0.71803 0.54678 0.03482  0.04525  -0.04214 677 HOH   B O   
6142 O  O   . HOH   N .   ? 0.53434 0.66809 0.68132 -0.04387 -0.04732 0.03619  678 HOH   B O   
6143 O  O   . HOH   N .   ? 0.62956 0.60158 0.67893 -0.00688 -0.08913 0.06587  679 HOH   B O   
6144 O  O   . HOH   N .   ? 0.52933 0.69527 0.54194 0.03269  0.02260  -0.04721 680 HOH   B O   
6145 O  O   . HOH   N .   ? 0.70980 0.79484 0.72615 0.11062  -0.03877 -0.12256 681 HOH   B O   
6146 O  O   . HOH   N .   ? 0.59007 0.81926 0.73881 -0.01280 0.01336  0.05714  682 HOH   B O   
6147 O  O   . HOH   N .   ? 0.63834 0.63520 0.53457 0.08506  -0.04451 0.02197  683 HOH   B O   
6148 O  O   . HOH   N .   ? 0.61266 0.66521 0.44793 0.17954  0.01213  -0.02673 684 HOH   B O   
6149 O  O   . HOH   N .   ? 0.51281 0.68845 0.57984 -0.01808 0.03361  0.00304  685 HOH   B O   
6150 O  O   . HOH   N .   ? 0.56199 0.96060 0.64466 0.04361  0.07338  -0.00719 686 HOH   B O   
6151 O  O   . HOH   N .   ? 0.52089 0.52006 0.43855 0.08117  -0.03460 0.00406  687 HOH   B O   
6152 O  O   . HOH   N .   ? 0.62919 0.74089 0.49092 0.16040  0.03007  0.00648  688 HOH   B O   
6153 O  O   . HOH   N .   ? 0.81098 0.83386 0.80188 0.01869  -0.00449 -0.01074 689 HOH   B O   
6154 O  O   . HOH   N .   ? 0.54307 0.68448 0.55801 0.02481  0.00442  -0.04235 690 HOH   B O   
6155 O  O   . HOH   N .   ? 0.57230 0.75190 0.57671 0.00391  0.03465  -0.00504 691 HOH   B O   
6156 O  O   . HOH   N .   ? 0.64873 0.60018 0.55134 0.08947  -0.03689 -0.04054 692 HOH   B O   
6157 O  O   . HOH   N .   ? 0.46654 0.38648 0.53343 0.03611  -0.12013 -0.00855 693 HOH   B O   
6158 O  O   . HOH   N .   ? 0.50982 0.78470 0.54411 0.13129  0.03117  -0.10167 694 HOH   B O   
6159 O  O   . HOH   N .   ? 0.52583 0.52953 0.61511 -0.03559 -0.14037 -0.01818 695 HOH   B O   
6160 O  O   . HOH   N .   ? 0.25697 0.37687 0.31834 0.02755  0.03128  0.00910  696 HOH   B O   
6161 O  O   . HOH   N .   ? 0.65201 0.97525 0.62707 0.00000  0.08485  0.00000  697 HOH   B O   
6162 O  O   . HOH   N .   ? 0.59685 0.62377 0.61998 -0.03320 -0.03255 0.01256  698 HOH   B O   
6163 O  O   . HOH   N .   ? 0.50750 0.73008 0.54057 0.05213  0.04146  -0.05573 699 HOH   B O   
6164 O  O   . HOH   N .   ? 0.67484 0.65244 0.65510 0.03927  -0.04087 -0.03169 700 HOH   B O   
6165 O  O   . HOH   N .   ? 0.62791 0.64862 0.53260 0.10690  -0.00345 -0.01922 701 HOH   B O   
6166 O  O   . HOH   N .   ? 0.53119 0.68163 0.57155 -0.00582 0.03503  -0.00499 702 HOH   B O   
6167 O  O   . HOH   N .   ? 0.42394 0.58369 0.52731 0.00580  0.02754  0.02239  703 HOH   B O   
6168 O  O   . HOH   N .   ? 0.57263 0.57992 0.41419 0.16323  -0.00449 -0.03881 704 HOH   B O   
6169 O  O   . HOH   N .   ? 0.63917 0.98370 0.75725 -0.03076 0.04872  0.04183  705 HOH   B O   
6170 O  O   . HOH   N .   ? 0.57270 0.66295 0.55497 0.05687  -0.04179 -0.08724 706 HOH   B O   
6171 O  O   . HOH   N .   ? 0.74313 0.93306 0.66064 0.12984  0.05130  0.04847  707 HOH   B O   
6172 O  O   . HOH   N .   ? 0.62787 0.70168 0.71814 0.01533  -0.00086 -0.02106 708 HOH   B O   
6173 O  O   . HOH   N .   ? 0.73652 0.71988 0.82137 0.05225  -0.08191 -0.03778 709 HOH   B O   
6174 O  O   . HOH   N .   ? 0.59167 0.62384 0.60841 -0.01491 -0.01642 0.00117  710 HOH   B O   
6175 O  O   . HOH   N .   ? 0.63753 0.70584 0.63358 0.03558  0.01144  -0.00679 711 HOH   B O   
6176 O  O   . HOH   N .   ? 0.52582 0.68568 0.59348 0.03475  0.04337  0.01707  712 HOH   B O   
6177 O  O   . HOH   N .   ? 0.51974 0.86657 0.67380 -0.00160 0.04075  0.01208  713 HOH   B O   
6178 O  O   . HOH   N .   ? 0.55081 0.60420 0.65111 0.05289  -0.03774 -0.05625 714 HOH   B O   
6179 O  O   . HOH   N .   ? 0.73816 0.76381 0.66176 0.12268  -0.00037 -0.03032 715 HOH   B O   
6180 O  O   . HOH   N .   ? 0.66442 0.93077 0.82363 -0.01618 0.01172  0.00811  716 HOH   B O   
6181 O  O   . HOH   N .   ? 0.47079 0.44292 0.54747 0.04773  -0.08756 -0.02677 717 HOH   B O   
6182 O  O   . HOH   N .   ? 0.53853 0.54966 0.54622 0.02251  -0.01835 -0.02542 718 HOH   B O   
6183 O  O   . HOH   N .   ? 0.50119 0.62370 0.63033 0.03964  -0.02885 -0.04301 719 HOH   B O   
6184 O  O   . HOH   N .   ? 0.54855 0.58690 0.58337 0.01183  -0.01112 -0.02272 720 HOH   B O   
6185 O  O   . HOH   N .   ? 0.55187 0.59630 0.60857 -0.01340 -0.04894 0.08401  721 HOH   B O   
6186 O  O   . HOH   N .   ? 0.60798 0.63234 0.52557 0.08428  -0.01990 0.01311  722 HOH   B O   
6187 O  O   . HOH   N .   ? 0.74930 0.72657 0.78088 0.02488  -0.11692 -0.07694 723 HOH   B O   
6188 O  O   . HOH   N .   ? 0.48956 0.66626 0.57459 0.02367  0.04048  0.03140  724 HOH   B O   
6189 O  O   . HOH   N .   ? 0.60486 0.69384 0.69445 0.02115  0.00894  -0.03348 725 HOH   B O   
6190 O  O   . HOH   N .   ? 0.55951 0.51867 0.64144 0.03594  -0.09069 -0.02789 726 HOH   B O   
6191 O  O   . HOH   N .   ? 0.66097 0.73775 0.75512 0.02841  -0.00606 -0.04313 727 HOH   B O   
6192 O  O   . HOH   N .   ? 0.50615 0.62207 0.60753 0.02127  0.00704  -0.03692 728 HOH   B O   
6193 O  O   . HOH   N .   ? 0.48316 0.53709 0.57146 0.01177  -0.01614 -0.00805 729 HOH   B O   
6194 O  O   . HOH   N .   ? 0.61046 0.72564 0.69143 0.08156  -0.01446 -0.08973 730 HOH   B O   
6195 O  O   . HOH   N .   ? 0.63292 0.70916 0.68517 -0.01744 -0.03993 0.10788  731 HOH   B O   
6196 O  O   . HOH   N .   ? 0.62821 0.74088 0.73454 0.02509  -0.00151 -0.03848 732 HOH   B O   
6197 O  O   . HOH   N .   ? 0.74114 0.76509 0.60150 0.16577  0.00425  -0.03977 733 HOH   B O   
6198 O  O   . HOH   N .   ? 0.47875 0.62911 0.57628 -0.03935 -0.02172 0.13305  734 HOH   B O   
6199 O  O   . HOH   N .   ? 0.65679 0.85997 0.63866 0.14297  0.00428  -0.12516 735 HOH   B O   
6200 O  O   . HOH   N .   ? 0.52194 0.70960 0.54401 0.02514  0.03693  -0.03536 736 HOH   B O   
6201 O  O   . HOH   N .   ? 0.68554 0.74996 0.71577 -0.02967 -0.00926 0.01319  737 HOH   B O   
6202 O  O   . HOH   N .   ? 0.50762 0.84790 0.66157 -0.02221 0.03583  0.02844  738 HOH   B O   
6203 O  O   . HOH   N .   ? 0.71419 0.77690 0.63917 0.08049  -0.00618 0.03707  739 HOH   B O   
6204 O  O   . HOH   N .   ? 0.61349 0.80007 0.61870 0.01980  0.03430  -0.02533 740 HOH   B O   
6205 O  O   . HOH   N .   ? 0.53487 0.59372 0.62980 0.00240  -0.01858 0.00165  741 HOH   B O   
6206 O  O   . HOH   N .   ? 0.48942 0.58739 0.58380 0.02432  0.00627  -0.03788 742 HOH   B O   
6207 O  O   . HOH   N .   ? 0.60798 0.68450 0.70396 0.03165  -0.00829 -0.04216 743 HOH   B O   
6208 O  O   . HOH   N .   ? 0.55492 0.70991 0.66810 -0.00472 0.01761  0.03084  744 HOH   B O   
6209 O  O   . HOH   N .   ? 0.48226 0.57904 0.58346 0.02972  -0.00393 -0.04103 745 HOH   B O   
6210 O  O   . HOH   N .   ? 0.63001 0.73212 0.73872 -0.05675 -0.05164 0.13056  746 HOH   B O   
6211 O  O   . HOH   N .   ? 0.59988 0.70027 0.72367 0.03397  -0.04797 -0.03644 747 HOH   B O   
6212 O  O   . HOH   N .   ? 0.45594 0.54768 0.57268 0.06374  -0.03561 -0.06147 748 HOH   B O   
6213 O  O   . HOH   N .   ? 0.93333 0.79765 0.78623 0.10472  -0.07388 -0.04611 749 HOH   B O   
6214 O  O   . HOH   N .   ? 0.69570 0.84512 0.75772 -0.01771 -0.01222 0.13051  750 HOH   B O   
6215 O  O   . HOH   N .   ? 0.62398 0.68785 0.72884 -0.00511 -0.02528 -0.00548 751 HOH   B O   
6216 O  O   . HOH   N .   ? 0.59345 0.74492 0.64306 -0.01314 0.03259  -0.00014 752 HOH   B O   
6217 O  O   . HOH   N .   ? 0.71400 0.69131 0.61531 0.08948  -0.04231 -0.01204 753 HOH   B O   
6218 O  O   . HOH   N .   ? 0.71943 0.72300 0.70465 0.01419  -0.01595 -0.01040 754 HOH   B O   
6219 O  O   . HOH   N .   ? 0.52042 0.61718 0.62810 0.03914  -0.01260 -0.04750 755 HOH   B O   
6220 O  O   . HOH   N .   ? 0.67210 0.86031 0.69470 0.04017  0.03282  -0.05167 756 HOH   B O   
6221 O  O   . HOH   N .   ? 0.71084 0.87018 0.70746 -0.01010 0.02676  0.01416  757 HOH   B O   
# 
